data_8YRE
# 
_entry.id   8YRE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YRE         pdb_00008yre 10.2210/pdb8yre/pdb 
WWPDB D_1300046223 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YRE 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              liulin@ahu.edu.cn 
_pdbx_contact_author.name_first         Lin 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9803-6540 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhang, C.' 1 ? 
'Liu, L.'   2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural insight into the regulation of GDP-mannose pyrophosphorylase activity of Arabidopsis KJC2-VTC1 complex' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhang, C.' 1 ? 
primary 'Liu, L.'   2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'ADP-glucose pyrophosphorylase family protein' 44988.461 3  ?        ? ? ? 
2 polymer     man 'Mannose-1-phosphate guanylyltransferase 1'    39625.184 3  2.7.7.13 ? ? ? 
3 non-polymer syn 'SULFATE ION'                                  96.063    12 ?        ? ? ? 
4 water       nat water                                          18.015    2  ?        ? ? ? 
# 
_entity_name_com.entity_id   2 
_entity_name_com.name        
;GDP-mannose pyrophosphorylase 1,Protein CYTOKINESIS DEFECTIVE 1,Protein EMBRYO DEFECTIVE 101,Protein HYPERSENSITIVE TO AMMONIUM ION 1,Protein SENSITIVE TO OZONE 1,Protein VITAMIN C DEFECTIVE 1
;
# 
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 
;MSEEKVVAVIMVGGPTKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELK
IPVRYLKEDKPHGSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIA
DPDTKELLHYTEKPETFVSDLINCGVYVFTSDIFNAIEEVYSQIRDTSSNYQSATRSVPADFVRLDQDILSPLAGKKQLY
TYENKDFWEQIKTPGKSLKCSALYLSQFRETSPHILASGDGTNRKPTIIGDVYIHPSVKLHPTAKIGPNVSISANVRVGP
GVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRVQASGDYNDRLGITILGEAVTVEDEVAVIGSIVLQNKTLNVSV
QDDIIL
;
;MSEEKVVAVIMVGGPTKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELK
IPVRYLKEDKPHGSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIA
DPDTKELLHYTEKPETFVSDLINCGVYVFTSDIFNAIEEVYSQIRDTSSNYQSATRSVPADFVRLDQDILSPLAGKKQLY
TYENKDFWEQIKTPGKSLKCSALYLSQFRETSPHILASGDGTNRKPTIIGDVYIHPSVKLHPTAKIGPNVSISANVRVGP
GVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRVQASGDYNDRLGITILGEAVTVEDEVAVIGSIVLQNKTLNVSV
QDDIIL
;
A,B,C ? 
2 'polypeptide(L)' no no 
;MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQE
TEPLGTAGPLALARDKLLDGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEESTGRVEKF
VEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYLDSLRKK
SPAKLTSGPHIVGNVLVDETATIGEGCLIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWAR
IENMTILGEDVHVSDEIYSNGGVVLPHKEIKSNILKPEIVM
;
;MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQE
TEPLGTAGPLALARDKLLDGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEESTGRVEKF
VEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYLDSLRKK
SPAKLTSGPHIVGNVLVDETATIGEGCLIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWAR
IENMTILGEDVHVSDEIYSNGGVVLPHKEIKSNILKPEIVM
;
D,E,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'SULFATE ION' SO4 
4 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   GLU n 
1 4   GLU n 
1 5   LYS n 
1 6   VAL n 
1 7   VAL n 
1 8   ALA n 
1 9   VAL n 
1 10  ILE n 
1 11  MET n 
1 12  VAL n 
1 13  GLY n 
1 14  GLY n 
1 15  PRO n 
1 16  THR n 
1 17  LYS n 
1 18  GLY n 
1 19  THR n 
1 20  ARG n 
1 21  PHE n 
1 22  ARG n 
1 23  PRO n 
1 24  LEU n 
1 25  SER n 
1 26  PHE n 
1 27  ASN n 
1 28  THR n 
1 29  PRO n 
1 30  LYS n 
1 31  PRO n 
1 32  LEU n 
1 33  ILE n 
1 34  PRO n 
1 35  LEU n 
1 36  ALA n 
1 37  GLY n 
1 38  GLN n 
1 39  PRO n 
1 40  MET n 
1 41  ILE n 
1 42  HIS n 
1 43  HIS n 
1 44  PRO n 
1 45  ILE n 
1 46  SER n 
1 47  ALA n 
1 48  CYS n 
1 49  LYS n 
1 50  LYS n 
1 51  ILE n 
1 52  SER n 
1 53  ASN n 
1 54  LEU n 
1 55  ALA n 
1 56  GLN n 
1 57  ILE n 
1 58  PHE n 
1 59  LEU n 
1 60  ILE n 
1 61  GLY n 
1 62  PHE n 
1 63  TYR n 
1 64  GLU n 
1 65  GLU n 
1 66  ARG n 
1 67  GLU n 
1 68  PHE n 
1 69  ALA n 
1 70  LEU n 
1 71  TYR n 
1 72  VAL n 
1 73  SER n 
1 74  SER n 
1 75  ILE n 
1 76  SER n 
1 77  ASN n 
1 78  GLU n 
1 79  LEU n 
1 80  LYS n 
1 81  ILE n 
1 82  PRO n 
1 83  VAL n 
1 84  ARG n 
1 85  TYR n 
1 86  LEU n 
1 87  LYS n 
1 88  GLU n 
1 89  ASP n 
1 90  LYS n 
1 91  PRO n 
1 92  HIS n 
1 93  GLY n 
1 94  SER n 
1 95  ALA n 
1 96  GLY n 
1 97  ALA n 
1 98  LEU n 
1 99  TYR n 
1 100 TYR n 
1 101 PHE n 
1 102 ARG n 
1 103 ASP n 
1 104 ARG n 
1 105 ILE n 
1 106 MET n 
1 107 GLU n 
1 108 GLU n 
1 109 LYS n 
1 110 PRO n 
1 111 SER n 
1 112 HIS n 
1 113 VAL n 
1 114 PHE n 
1 115 LEU n 
1 116 LEU n 
1 117 ASN n 
1 118 CYS n 
1 119 ASP n 
1 120 VAL n 
1 121 CYS n 
1 122 CYS n 
1 123 SER n 
1 124 PHE n 
1 125 PRO n 
1 126 LEU n 
1 127 GLN n 
1 128 GLY n 
1 129 ILE n 
1 130 LEU n 
1 131 ASP n 
1 132 ALA n 
1 133 HIS n 
1 134 ARG n 
1 135 ARG n 
1 136 TYR n 
1 137 GLY n 
1 138 GLY n 
1 139 ILE n 
1 140 GLY n 
1 141 THR n 
1 142 MET n 
1 143 LEU n 
1 144 VAL n 
1 145 ILE n 
1 146 LYS n 
1 147 VAL n 
1 148 SER n 
1 149 ALA n 
1 150 GLU n 
1 151 ALA n 
1 152 ALA n 
1 153 SER n 
1 154 GLN n 
1 155 PHE n 
1 156 GLY n 
1 157 GLU n 
1 158 LEU n 
1 159 ILE n 
1 160 ALA n 
1 161 ASP n 
1 162 PRO n 
1 163 ASP n 
1 164 THR n 
1 165 LYS n 
1 166 GLU n 
1 167 LEU n 
1 168 LEU n 
1 169 HIS n 
1 170 TYR n 
1 171 THR n 
1 172 GLU n 
1 173 LYS n 
1 174 PRO n 
1 175 GLU n 
1 176 THR n 
1 177 PHE n 
1 178 VAL n 
1 179 SER n 
1 180 ASP n 
1 181 LEU n 
1 182 ILE n 
1 183 ASN n 
1 184 CYS n 
1 185 GLY n 
1 186 VAL n 
1 187 TYR n 
1 188 VAL n 
1 189 PHE n 
1 190 THR n 
1 191 SER n 
1 192 ASP n 
1 193 ILE n 
1 194 PHE n 
1 195 ASN n 
1 196 ALA n 
1 197 ILE n 
1 198 GLU n 
1 199 GLU n 
1 200 VAL n 
1 201 TYR n 
1 202 SER n 
1 203 GLN n 
1 204 ILE n 
1 205 ARG n 
1 206 ASP n 
1 207 THR n 
1 208 SER n 
1 209 SER n 
1 210 ASN n 
1 211 TYR n 
1 212 GLN n 
1 213 SER n 
1 214 ALA n 
1 215 THR n 
1 216 ARG n 
1 217 SER n 
1 218 VAL n 
1 219 PRO n 
1 220 ALA n 
1 221 ASP n 
1 222 PHE n 
1 223 VAL n 
1 224 ARG n 
1 225 LEU n 
1 226 ASP n 
1 227 GLN n 
1 228 ASP n 
1 229 ILE n 
1 230 LEU n 
1 231 SER n 
1 232 PRO n 
1 233 LEU n 
1 234 ALA n 
1 235 GLY n 
1 236 LYS n 
1 237 LYS n 
1 238 GLN n 
1 239 LEU n 
1 240 TYR n 
1 241 THR n 
1 242 TYR n 
1 243 GLU n 
1 244 ASN n 
1 245 LYS n 
1 246 ASP n 
1 247 PHE n 
1 248 TRP n 
1 249 GLU n 
1 250 GLN n 
1 251 ILE n 
1 252 LYS n 
1 253 THR n 
1 254 PRO n 
1 255 GLY n 
1 256 LYS n 
1 257 SER n 
1 258 LEU n 
1 259 LYS n 
1 260 CYS n 
1 261 SER n 
1 262 ALA n 
1 263 LEU n 
1 264 TYR n 
1 265 LEU n 
1 266 SER n 
1 267 GLN n 
1 268 PHE n 
1 269 ARG n 
1 270 GLU n 
1 271 THR n 
1 272 SER n 
1 273 PRO n 
1 274 HIS n 
1 275 ILE n 
1 276 LEU n 
1 277 ALA n 
1 278 SER n 
1 279 GLY n 
1 280 ASP n 
1 281 GLY n 
1 282 THR n 
1 283 ASN n 
1 284 ARG n 
1 285 LYS n 
1 286 PRO n 
1 287 THR n 
1 288 ILE n 
1 289 ILE n 
1 290 GLY n 
1 291 ASP n 
1 292 VAL n 
1 293 TYR n 
1 294 ILE n 
1 295 HIS n 
1 296 PRO n 
1 297 SER n 
1 298 VAL n 
1 299 LYS n 
1 300 LEU n 
1 301 HIS n 
1 302 PRO n 
1 303 THR n 
1 304 ALA n 
1 305 LYS n 
1 306 ILE n 
1 307 GLY n 
1 308 PRO n 
1 309 ASN n 
1 310 VAL n 
1 311 SER n 
1 312 ILE n 
1 313 SER n 
1 314 ALA n 
1 315 ASN n 
1 316 VAL n 
1 317 ARG n 
1 318 VAL n 
1 319 GLY n 
1 320 PRO n 
1 321 GLY n 
1 322 VAL n 
1 323 ARG n 
1 324 LEU n 
1 325 ILE n 
1 326 SER n 
1 327 CYS n 
1 328 ILE n 
1 329 ILE n 
1 330 LEU n 
1 331 ASP n 
1 332 ASP n 
1 333 VAL n 
1 334 GLU n 
1 335 ILE n 
1 336 LYS n 
1 337 GLU n 
1 338 ASN n 
1 339 ALA n 
1 340 VAL n 
1 341 VAL n 
1 342 ILE n 
1 343 ASN n 
1 344 SER n 
1 345 ILE n 
1 346 ILE n 
1 347 GLY n 
1 348 TRP n 
1 349 LYS n 
1 350 SER n 
1 351 SER n 
1 352 ILE n 
1 353 GLY n 
1 354 ARG n 
1 355 TRP n 
1 356 SER n 
1 357 ARG n 
1 358 VAL n 
1 359 GLN n 
1 360 ALA n 
1 361 SER n 
1 362 GLY n 
1 363 ASP n 
1 364 TYR n 
1 365 ASN n 
1 366 ASP n 
1 367 ARG n 
1 368 LEU n 
1 369 GLY n 
1 370 ILE n 
1 371 THR n 
1 372 ILE n 
1 373 LEU n 
1 374 GLY n 
1 375 GLU n 
1 376 ALA n 
1 377 VAL n 
1 378 THR n 
1 379 VAL n 
1 380 GLU n 
1 381 ASP n 
1 382 GLU n 
1 383 VAL n 
1 384 ALA n 
1 385 VAL n 
1 386 ILE n 
1 387 GLY n 
1 388 SER n 
1 389 ILE n 
1 390 VAL n 
1 391 LEU n 
1 392 GLN n 
1 393 ASN n 
1 394 LYS n 
1 395 THR n 
1 396 LEU n 
1 397 ASN n 
1 398 VAL n 
1 399 SER n 
1 400 VAL n 
1 401 GLN n 
1 402 ASP n 
1 403 ASP n 
1 404 ILE n 
1 405 ILE n 
1 406 LEU n 
2 1   MET n 
2 2   LYS n 
2 3   ALA n 
2 4   LEU n 
2 5   ILE n 
2 6   LEU n 
2 7   VAL n 
2 8   GLY n 
2 9   GLY n 
2 10  PHE n 
2 11  GLY n 
2 12  THR n 
2 13  ARG n 
2 14  LEU n 
2 15  ARG n 
2 16  PRO n 
2 17  LEU n 
2 18  THR n 
2 19  LEU n 
2 20  SER n 
2 21  PHE n 
2 22  PRO n 
2 23  LYS n 
2 24  PRO n 
2 25  LEU n 
2 26  VAL n 
2 27  ASP n 
2 28  PHE n 
2 29  ALA n 
2 30  ASN n 
2 31  LYS n 
2 32  PRO n 
2 33  MET n 
2 34  ILE n 
2 35  LEU n 
2 36  HIS n 
2 37  GLN n 
2 38  ILE n 
2 39  GLU n 
2 40  ALA n 
2 41  LEU n 
2 42  LYS n 
2 43  ALA n 
2 44  VAL n 
2 45  GLY n 
2 46  VAL n 
2 47  ASP n 
2 48  GLU n 
2 49  VAL n 
2 50  VAL n 
2 51  LEU n 
2 52  ALA n 
2 53  ILE n 
2 54  ASN n 
2 55  TYR n 
2 56  GLN n 
2 57  PRO n 
2 58  GLU n 
2 59  VAL n 
2 60  MET n 
2 61  LEU n 
2 62  ASN n 
2 63  PHE n 
2 64  LEU n 
2 65  LYS n 
2 66  ASP n 
2 67  PHE n 
2 68  GLU n 
2 69  THR n 
2 70  LYS n 
2 71  LEU n 
2 72  GLU n 
2 73  ILE n 
2 74  LYS n 
2 75  ILE n 
2 76  THR n 
2 77  CYS n 
2 78  SER n 
2 79  GLN n 
2 80  GLU n 
2 81  THR n 
2 82  GLU n 
2 83  PRO n 
2 84  LEU n 
2 85  GLY n 
2 86  THR n 
2 87  ALA n 
2 88  GLY n 
2 89  PRO n 
2 90  LEU n 
2 91  ALA n 
2 92  LEU n 
2 93  ALA n 
2 94  ARG n 
2 95  ASP n 
2 96  LYS n 
2 97  LEU n 
2 98  LEU n 
2 99  ASP n 
2 100 GLY n 
2 101 SER n 
2 102 GLY n 
2 103 GLU n 
2 104 PRO n 
2 105 PHE n 
2 106 PHE n 
2 107 VAL n 
2 108 LEU n 
2 109 ASN n 
2 110 SER n 
2 111 ASP n 
2 112 VAL n 
2 113 ILE n 
2 114 SER n 
2 115 GLU n 
2 116 TYR n 
2 117 PRO n 
2 118 LEU n 
2 119 LYS n 
2 120 GLU n 
2 121 MET n 
2 122 LEU n 
2 123 GLU n 
2 124 PHE n 
2 125 HIS n 
2 126 LYS n 
2 127 SER n 
2 128 HIS n 
2 129 GLY n 
2 130 GLY n 
2 131 GLU n 
2 132 ALA n 
2 133 SER n 
2 134 ILE n 
2 135 MET n 
2 136 VAL n 
2 137 THR n 
2 138 LYS n 
2 139 VAL n 
2 140 ASP n 
2 141 GLU n 
2 142 PRO n 
2 143 SER n 
2 144 LYS n 
2 145 TYR n 
2 146 GLY n 
2 147 VAL n 
2 148 VAL n 
2 149 VAL n 
2 150 MET n 
2 151 GLU n 
2 152 GLU n 
2 153 SER n 
2 154 THR n 
2 155 GLY n 
2 156 ARG n 
2 157 VAL n 
2 158 GLU n 
2 159 LYS n 
2 160 PHE n 
2 161 VAL n 
2 162 GLU n 
2 163 LYS n 
2 164 PRO n 
2 165 LYS n 
2 166 LEU n 
2 167 TYR n 
2 168 VAL n 
2 169 GLY n 
2 170 ASN n 
2 171 LYS n 
2 172 ILE n 
2 173 ASN n 
2 174 ALA n 
2 175 GLY n 
2 176 ILE n 
2 177 TYR n 
2 178 LEU n 
2 179 LEU n 
2 180 ASN n 
2 181 PRO n 
2 182 SER n 
2 183 VAL n 
2 184 LEU n 
2 185 ASP n 
2 186 LYS n 
2 187 ILE n 
2 188 GLU n 
2 189 LEU n 
2 190 ARG n 
2 191 PRO n 
2 192 THR n 
2 193 SER n 
2 194 ILE n 
2 195 GLU n 
2 196 LYS n 
2 197 GLU n 
2 198 THR n 
2 199 PHE n 
2 200 PRO n 
2 201 LYS n 
2 202 ILE n 
2 203 ALA n 
2 204 ALA n 
2 205 ALA n 
2 206 GLN n 
2 207 GLY n 
2 208 LEU n 
2 209 TYR n 
2 210 ALA n 
2 211 MET n 
2 212 VAL n 
2 213 LEU n 
2 214 PRO n 
2 215 GLY n 
2 216 PHE n 
2 217 TRP n 
2 218 MET n 
2 219 ASP n 
2 220 ILE n 
2 221 GLY n 
2 222 GLN n 
2 223 PRO n 
2 224 ARG n 
2 225 ASP n 
2 226 TYR n 
2 227 ILE n 
2 228 THR n 
2 229 GLY n 
2 230 LEU n 
2 231 ARG n 
2 232 LEU n 
2 233 TYR n 
2 234 LEU n 
2 235 ASP n 
2 236 SER n 
2 237 LEU n 
2 238 ARG n 
2 239 LYS n 
2 240 LYS n 
2 241 SER n 
2 242 PRO n 
2 243 ALA n 
2 244 LYS n 
2 245 LEU n 
2 246 THR n 
2 247 SER n 
2 248 GLY n 
2 249 PRO n 
2 250 HIS n 
2 251 ILE n 
2 252 VAL n 
2 253 GLY n 
2 254 ASN n 
2 255 VAL n 
2 256 LEU n 
2 257 VAL n 
2 258 ASP n 
2 259 GLU n 
2 260 THR n 
2 261 ALA n 
2 262 THR n 
2 263 ILE n 
2 264 GLY n 
2 265 GLU n 
2 266 GLY n 
2 267 CYS n 
2 268 LEU n 
2 269 ILE n 
2 270 GLY n 
2 271 PRO n 
2 272 ASP n 
2 273 VAL n 
2 274 ALA n 
2 275 ILE n 
2 276 GLY n 
2 277 PRO n 
2 278 GLY n 
2 279 CYS n 
2 280 ILE n 
2 281 VAL n 
2 282 GLU n 
2 283 SER n 
2 284 GLY n 
2 285 VAL n 
2 286 ARG n 
2 287 LEU n 
2 288 SER n 
2 289 ARG n 
2 290 CYS n 
2 291 THR n 
2 292 VAL n 
2 293 MET n 
2 294 ARG n 
2 295 GLY n 
2 296 VAL n 
2 297 ARG n 
2 298 ILE n 
2 299 LYS n 
2 300 LYS n 
2 301 HIS n 
2 302 ALA n 
2 303 CYS n 
2 304 ILE n 
2 305 SER n 
2 306 SER n 
2 307 SER n 
2 308 ILE n 
2 309 ILE n 
2 310 GLY n 
2 311 TRP n 
2 312 HIS n 
2 313 SER n 
2 314 THR n 
2 315 VAL n 
2 316 GLY n 
2 317 GLN n 
2 318 TRP n 
2 319 ALA n 
2 320 ARG n 
2 321 ILE n 
2 322 GLU n 
2 323 ASN n 
2 324 MET n 
2 325 THR n 
2 326 ILE n 
2 327 LEU n 
2 328 GLY n 
2 329 GLU n 
2 330 ASP n 
2 331 VAL n 
2 332 HIS n 
2 333 VAL n 
2 334 SER n 
2 335 ASP n 
2 336 GLU n 
2 337 ILE n 
2 338 TYR n 
2 339 SER n 
2 340 ASN n 
2 341 GLY n 
2 342 GLY n 
2 343 VAL n 
2 344 VAL n 
2 345 LEU n 
2 346 PRO n 
2 347 HIS n 
2 348 LYS n 
2 349 GLU n 
2 350 ILE n 
2 351 LYS n 
2 352 SER n 
2 353 ASN n 
2 354 ILE n 
2 355 LEU n 
2 356 LYS n 
2 357 PRO n 
2 358 GLU n 
2 359 ILE n 
2 360 VAL n 
2 361 MET n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 406 'thale cress' ? 'KJC2, At2g04650, F28I8.31, F28I8_31'                     ? ? ? ? ? ? 
'Arabidopsis thaliana' 3702 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 361 'thale cress' ? 'CYT1, EMB101, GMP1, HSN1, SOZ1, VTC1, At2g39770, T5I7.7' ? ? ? ? ? ? 
'Arabidopsis thaliana' 3702 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
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 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  MET 11  11  11  MET MET A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  THR 16  16  16  THR THR A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  THR 28  28  28  THR THR A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  PRO 31  31  31  PRO PRO A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  MET 40  40  40  MET MET A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  HIS 42  42  42  HIS HIS A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  CYS 48  48  48  CYS CYS A . n 
A 1 49  LYS 49  49  49  LYS LYS A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLN 56  56  56  GLN GLN A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  PHE 58  58  58  PHE PHE A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  ILE 81  81  81  ILE ILE A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  LYS 87  87  87  LYS LYS 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  LYS 90  90  90  LYS LYS A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  TYR 99  99  99  TYR TYR A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 PHE 101 101 101 PHE PHE A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 HIS 112 112 112 HIS HIS A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 CYS 118 118 118 CYS CYS A . n 
A 1 119 ASP 119 119 119 ASP ASP A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 CYS 121 121 121 CYS CYS A . n 
A 1 122 CYS 122 122 122 CYS CYS A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 PHE 124 124 124 PHE PHE A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 HIS 133 133 133 HIS HIS A . n 
A 1 134 ARG 134 134 134 ARG ARG A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 TYR 136 136 136 TYR TYR A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ILE 139 139 139 ILE ILE 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 LEU 143 143 143 LEU LEU A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 PHE 155 155 155 PHE PHE A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 PRO 162 162 162 PRO PRO A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 HIS 169 169 169 HIS HIS A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 THR 171 171 171 THR THR A . n 
A 1 172 GLU 172 172 172 GLU GLU A . n 
A 1 173 LYS 173 173 173 LYS LYS A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 GLU 175 175 175 GLU GLU A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 ASP 180 180 180 ASP ASP A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 CYS 184 184 184 CYS CYS A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 TYR 187 187 187 TYR TYR A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 SER 191 191 191 SER SER A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 ILE 193 193 193 ILE ILE A . n 
A 1 194 PHE 194 194 194 PHE PHE A . n 
A 1 195 ASN 195 195 195 ASN ASN A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 GLU 198 198 198 GLU GLU A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 TYR 201 201 201 TYR TYR A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 GLN 203 203 203 GLN GLN A . n 
A 1 204 ILE 204 204 204 ILE ILE A . n 
A 1 205 ARG 205 205 205 ARG ARG A . n 
A 1 206 ASP 206 206 ?   ?   ?   A . n 
A 1 207 THR 207 207 ?   ?   ?   A . n 
A 1 208 SER 208 208 ?   ?   ?   A . n 
A 1 209 SER 209 209 ?   ?   ?   A . n 
A 1 210 ASN 210 210 ?   ?   ?   A . n 
A 1 211 TYR 211 211 ?   ?   ?   A . n 
A 1 212 GLN 212 212 ?   ?   ?   A . n 
A 1 213 SER 213 213 ?   ?   ?   A . n 
A 1 214 ALA 214 214 ?   ?   ?   A . n 
A 1 215 THR 215 215 ?   ?   ?   A . n 
A 1 216 ARG 216 216 ?   ?   ?   A . n 
A 1 217 SER 217 217 ?   ?   ?   A . n 
A 1 218 VAL 218 218 ?   ?   ?   A . n 
A 1 219 PRO 219 219 ?   ?   ?   A . n 
A 1 220 ALA 220 220 ?   ?   ?   A . n 
A 1 221 ASP 221 221 ?   ?   ?   A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 ARG 224 224 224 ARG ARG A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 GLN 238 238 238 GLN GLN A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 THR 241 241 241 THR THR A . n 
A 1 242 TYR 242 242 242 TYR TYR A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 ASP 246 246 246 ASP ASP A . n 
A 1 247 PHE 247 247 247 PHE PHE A . n 
A 1 248 TRP 248 248 248 TRP TRP A . n 
A 1 249 GLU 249 249 249 GLU GLU A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 PRO 254 254 254 PRO PRO A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 LEU 258 258 258 LEU LEU A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 CYS 260 260 260 CYS CYS A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 TYR 264 264 264 TYR TYR A . n 
A 1 265 LEU 265 265 265 LEU LEU A . n 
A 1 266 SER 266 266 266 SER SER A . n 
A 1 267 GLN 267 267 267 GLN GLN A . n 
A 1 268 PHE 268 268 268 PHE PHE A . n 
A 1 269 ARG 269 269 269 ARG ARG A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 SER 272 272 272 SER SER A . n 
A 1 273 PRO 273 273 273 PRO PRO A . n 
A 1 274 HIS 274 274 274 HIS HIS A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 GLY 279 279 279 GLY GLY A . n 
A 1 280 ASP 280 280 280 ASP ASP A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 THR 282 282 282 THR THR A . n 
A 1 283 ASN 283 283 283 ASN ASN A . n 
A 1 284 ARG 284 284 284 ARG ARG A . n 
A 1 285 LYS 285 285 285 LYS LYS A . n 
A 1 286 PRO 286 286 286 PRO PRO A . n 
A 1 287 THR 287 287 287 THR THR A . n 
A 1 288 ILE 288 288 288 ILE ILE A . n 
A 1 289 ILE 289 289 289 ILE ILE A . n 
A 1 290 GLY 290 290 290 GLY GLY A . n 
A 1 291 ASP 291 291 291 ASP ASP A . n 
A 1 292 VAL 292 292 292 VAL VAL A . n 
A 1 293 TYR 293 293 293 TYR TYR A . n 
A 1 294 ILE 294 294 294 ILE ILE A . n 
A 1 295 HIS 295 295 295 HIS HIS A . n 
A 1 296 PRO 296 296 296 PRO PRO A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 LYS 299 299 299 LYS LYS A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 HIS 301 301 301 HIS HIS A . n 
A 1 302 PRO 302 302 302 PRO PRO A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 LYS 305 305 305 LYS LYS A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 PRO 308 308 308 PRO PRO A . n 
A 1 309 ASN 309 309 309 ASN ASN A . n 
A 1 310 VAL 310 310 310 VAL VAL A . n 
A 1 311 SER 311 311 311 SER SER A . n 
A 1 312 ILE 312 312 312 ILE ILE A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 ALA 314 314 314 ALA ALA A . n 
A 1 315 ASN 315 315 315 ASN ASN A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 ARG 317 317 317 ARG ARG A . n 
A 1 318 VAL 318 318 318 VAL VAL A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 PRO 320 320 320 PRO PRO A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 ARG 323 323 323 ARG ARG A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 ILE 325 325 325 ILE ILE A . n 
A 1 326 SER 326 326 326 SER SER A . n 
A 1 327 CYS 327 327 327 CYS CYS A . n 
A 1 328 ILE 328 328 328 ILE ILE A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 ASP 331 331 331 ASP ASP A . n 
A 1 332 ASP 332 332 332 ASP ASP A . n 
A 1 333 VAL 333 333 333 VAL VAL A . n 
A 1 334 GLU 334 334 334 GLU GLU A . n 
A 1 335 ILE 335 335 335 ILE ILE A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 ASN 338 338 338 ASN ASN A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 VAL 340 340 340 VAL VAL A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 ASN 343 343 343 ASN ASN A . n 
A 1 344 SER 344 344 344 SER SER A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 ILE 346 346 346 ILE ILE A . n 
A 1 347 GLY 347 347 347 GLY GLY A . n 
A 1 348 TRP 348 348 348 TRP TRP A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 SER 350 350 350 SER SER A . n 
A 1 351 SER 351 351 351 SER SER A . n 
A 1 352 ILE 352 352 352 ILE ILE A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 ARG 354 354 354 ARG ARG A . n 
A 1 355 TRP 355 355 355 TRP TRP A . n 
A 1 356 SER 356 356 356 SER SER A . n 
A 1 357 ARG 357 357 357 ARG ARG A . n 
A 1 358 VAL 358 358 358 VAL VAL A . n 
A 1 359 GLN 359 359 359 GLN GLN A . n 
A 1 360 ALA 360 360 360 ALA ALA A . n 
A 1 361 SER 361 361 361 SER SER A . n 
A 1 362 GLY 362 362 362 GLY GLY A . n 
A 1 363 ASP 363 363 363 ASP ASP A . n 
A 1 364 TYR 364 364 364 TYR TYR A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 ASP 366 366 366 ASP ASP A . n 
A 1 367 ARG 367 367 367 ARG ARG A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 GLY 369 369 369 GLY GLY A . n 
A 1 370 ILE 370 370 370 ILE ILE A . n 
A 1 371 THR 371 371 371 THR THR A . n 
A 1 372 ILE 372 372 372 ILE ILE A . n 
A 1 373 LEU 373 373 373 LEU LEU A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 GLU 375 375 375 GLU GLU A . n 
A 1 376 ALA 376 376 376 ALA ALA A . n 
A 1 377 VAL 377 377 377 VAL VAL A . n 
A 1 378 THR 378 378 378 THR THR A . n 
A 1 379 VAL 379 379 379 VAL VAL A . n 
A 1 380 GLU 380 380 380 GLU GLU A . n 
A 1 381 ASP 381 381 381 ASP ASP A . n 
A 1 382 GLU 382 382 382 GLU GLU A . n 
A 1 383 VAL 383 383 383 VAL VAL A . n 
A 1 384 ALA 384 384 384 ALA ALA A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 ILE 386 386 386 ILE ILE A . n 
A 1 387 GLY 387 387 387 GLY GLY A . n 
A 1 388 SER 388 388 388 SER SER A . n 
A 1 389 ILE 389 389 389 ILE ILE A . n 
A 1 390 VAL 390 390 390 VAL VAL A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 GLN 392 392 392 GLN GLN A . n 
A 1 393 ASN 393 393 393 ASN ASN A . n 
A 1 394 LYS 394 394 394 LYS LYS A . n 
A 1 395 THR 395 395 395 THR THR A . n 
A 1 396 LEU 396 396 396 LEU LEU A . n 
A 1 397 ASN 397 397 397 ASN ASN A . n 
A 1 398 VAL 398 398 398 VAL VAL A . n 
A 1 399 SER 399 399 399 SER SER A . n 
A 1 400 VAL 400 400 400 VAL VAL A . n 
A 1 401 GLN 401 401 401 GLN GLN A . n 
A 1 402 ASP 402 402 402 ASP ASP A . n 
A 1 403 ASP 403 403 403 ASP ASP A . n 
A 1 404 ILE 404 404 404 ILE ILE A . n 
A 1 405 ILE 405 405 405 ILE ILE A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   GLU 3   3   ?   ?   ?   B . n 
B 1 4   GLU 4   4   4   GLU GLU B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   VAL 6   6   6   VAL VAL B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   ALA 8   8   8   ALA ALA B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  ILE 10  10  10  ILE ILE B . n 
B 1 11  MET 11  11  11  MET MET B . n 
B 1 12  VAL 12  12  12  VAL VAL B . n 
B 1 13  GLY 13  13  13  GLY GLY B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  THR 16  16  16  THR THR B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  GLY 18  18  18  GLY GLY B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  ARG 20  20  20  ARG ARG B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  PRO 23  23  23  PRO PRO B . n 
B 1 24  LEU 24  24  24  LEU LEU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  ASN 27  27  27  ASN ASN B . n 
B 1 28  THR 28  28  28  THR THR B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  PRO 31  31  31  PRO PRO B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  PRO 34  34  34  PRO PRO B . n 
B 1 35  LEU 35  35  35  LEU LEU B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  MET 40  40  40  MET MET B . n 
B 1 41  ILE 41  41  41  ILE ILE B . n 
B 1 42  HIS 42  42  42  HIS HIS B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  PRO 44  44  44  PRO PRO B . n 
B 1 45  ILE 45  45  45  ILE ILE B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  ALA 47  47  47  ALA ALA B . n 
B 1 48  CYS 48  48  48  CYS CYS B . n 
B 1 49  LYS 49  49  49  LYS LYS B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  ILE 51  51  51  ILE ILE B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLN 56  56  56  GLN GLN B . n 
B 1 57  ILE 57  57  57  ILE ILE B . n 
B 1 58  PHE 58  58  58  PHE PHE B . n 
B 1 59  LEU 59  59  59  LEU LEU B . n 
B 1 60  ILE 60  60  60  ILE ILE B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PHE 62  62  62  PHE PHE B . n 
B 1 63  TYR 63  63  63  TYR TYR B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  PHE 68  68  68  PHE PHE B . n 
B 1 69  ALA 69  69  69  ALA ALA B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  TYR 71  71  71  TYR TYR B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  ILE 75  75  75  ILE ILE B . n 
B 1 76  SER 76  76  76  SER SER B . n 
B 1 77  ASN 77  77  77  ASN ASN B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  ILE 81  81  81  ILE ILE B . n 
B 1 82  PRO 82  82  82  PRO PRO B . n 
B 1 83  VAL 83  83  83  VAL VAL B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  GLU 88  88  88  GLU GLU B . n 
B 1 89  ASP 89  89  89  ASP ASP B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  PRO 91  91  91  PRO PRO B . n 
B 1 92  HIS 92  92  92  HIS HIS B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  SER 94  94  94  SER SER B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  GLY 96  96  96  GLY GLY B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  TYR 99  99  99  TYR TYR B . n 
B 1 100 TYR 100 100 100 TYR TYR B . n 
B 1 101 PHE 101 101 101 PHE PHE B . n 
B 1 102 ARG 102 102 102 ARG ARG B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 ILE 105 105 105 ILE ILE B . n 
B 1 106 MET 106 106 106 MET MET B . n 
B 1 107 GLU 107 107 107 GLU GLU B . n 
B 1 108 GLU 108 108 108 GLU GLU B . n 
B 1 109 LYS 109 109 109 LYS LYS B . n 
B 1 110 PRO 110 110 110 PRO PRO B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 HIS 112 112 112 HIS HIS B . n 
B 1 113 VAL 113 113 113 VAL VAL B . n 
B 1 114 PHE 114 114 114 PHE PHE B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 CYS 118 118 118 CYS CYS B . n 
B 1 119 ASP 119 119 119 ASP ASP B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 CYS 121 121 121 CYS CYS B . n 
B 1 122 CYS 122 122 122 CYS CYS B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 PHE 124 124 124 PHE PHE B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 GLY 128 128 128 GLY GLY B . n 
B 1 129 ILE 129 129 129 ILE ILE B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 ASP 131 131 131 ASP ASP B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 HIS 133 133 133 HIS HIS B . n 
B 1 134 ARG 134 134 134 ARG ARG B . n 
B 1 135 ARG 135 135 135 ARG ARG B . n 
B 1 136 TYR 136 136 136 TYR TYR B . n 
B 1 137 GLY 137 137 137 GLY GLY B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 THR 141 141 141 THR THR B . n 
B 1 142 MET 142 142 142 MET MET B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ILE 145 145 145 ILE ILE B . n 
B 1 146 LYS 146 146 146 LYS LYS B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 SER 148 148 148 SER SER B . n 
B 1 149 ALA 149 149 149 ALA ALA B . n 
B 1 150 GLU 150 150 150 GLU GLU B . n 
B 1 151 ALA 151 151 151 ALA ALA B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 SER 153 153 153 SER SER B . n 
B 1 154 GLN 154 154 154 GLN GLN B . n 
B 1 155 PHE 155 155 155 PHE PHE B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 GLU 157 157 157 GLU GLU B . n 
B 1 158 LEU 158 158 158 LEU LEU B . n 
B 1 159 ILE 159 159 159 ILE ILE B . n 
B 1 160 ALA 160 160 160 ALA ALA B . n 
B 1 161 ASP 161 161 161 ASP ASP B . n 
B 1 162 PRO 162 162 162 PRO PRO B . n 
B 1 163 ASP 163 163 163 ASP ASP B . n 
B 1 164 THR 164 164 164 THR THR B . n 
B 1 165 LYS 165 165 165 LYS LYS B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 LEU 168 168 168 LEU LEU B . n 
B 1 169 HIS 169 169 169 HIS HIS B . n 
B 1 170 TYR 170 170 170 TYR TYR B . n 
B 1 171 THR 171 171 171 THR THR B . n 
B 1 172 GLU 172 172 172 GLU GLU B . n 
B 1 173 LYS 173 173 173 LYS LYS B . n 
B 1 174 PRO 174 174 174 PRO PRO B . n 
B 1 175 GLU 175 175 175 GLU GLU B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 SER 179 179 179 SER SER B . n 
B 1 180 ASP 180 180 180 ASP ASP B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 ILE 182 182 182 ILE ILE B . n 
B 1 183 ASN 183 183 183 ASN ASN B . n 
B 1 184 CYS 184 184 184 CYS CYS B . n 
B 1 185 GLY 185 185 185 GLY GLY B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 TYR 187 187 187 TYR TYR B . n 
B 1 188 VAL 188 188 188 VAL VAL B . n 
B 1 189 PHE 189 189 189 PHE PHE B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 SER 191 191 191 SER SER B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 ILE 193 193 193 ILE ILE B . n 
B 1 194 PHE 194 194 194 PHE PHE B . n 
B 1 195 ASN 195 195 195 ASN ASN B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 ILE 197 197 197 ILE ILE B . n 
B 1 198 GLU 198 198 198 GLU GLU B . n 
B 1 199 GLU 199 199 199 GLU GLU B . n 
B 1 200 VAL 200 200 200 VAL VAL B . n 
B 1 201 TYR 201 201 201 TYR TYR B . n 
B 1 202 SER 202 202 202 SER SER B . n 
B 1 203 GLN 203 203 203 GLN GLN B . n 
B 1 204 ILE 204 204 204 ILE ILE B . n 
B 1 205 ARG 205 205 205 ARG ARG B . n 
B 1 206 ASP 206 206 ?   ?   ?   B . n 
B 1 207 THR 207 207 ?   ?   ?   B . n 
B 1 208 SER 208 208 ?   ?   ?   B . n 
B 1 209 SER 209 209 ?   ?   ?   B . n 
B 1 210 ASN 210 210 ?   ?   ?   B . n 
B 1 211 TYR 211 211 ?   ?   ?   B . n 
B 1 212 GLN 212 212 ?   ?   ?   B . n 
B 1 213 SER 213 213 ?   ?   ?   B . n 
B 1 214 ALA 214 214 ?   ?   ?   B . n 
B 1 215 THR 215 215 ?   ?   ?   B . n 
B 1 216 ARG 216 216 ?   ?   ?   B . n 
B 1 217 SER 217 217 ?   ?   ?   B . n 
B 1 218 VAL 218 218 ?   ?   ?   B . n 
B 1 219 PRO 219 219 ?   ?   ?   B . n 
B 1 220 ALA 220 220 ?   ?   ?   B . n 
B 1 221 ASP 221 221 ?   ?   ?   B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 VAL 223 223 223 VAL VAL B . n 
B 1 224 ARG 224 224 224 ARG ARG B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 ASP 226 226 226 ASP ASP B . n 
B 1 227 GLN 227 227 227 GLN GLN B . n 
B 1 228 ASP 228 228 228 ASP ASP B . n 
B 1 229 ILE 229 229 229 ILE ILE B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 SER 231 231 231 SER SER B . n 
B 1 232 PRO 232 232 232 PRO PRO B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 GLY 235 235 235 GLY GLY B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 LYS 237 237 237 LYS LYS B . n 
B 1 238 GLN 238 238 238 GLN GLN B . n 
B 1 239 LEU 239 239 239 LEU LEU B . n 
B 1 240 TYR 240 240 240 TYR TYR B . n 
B 1 241 THR 241 241 241 THR THR B . n 
B 1 242 TYR 242 242 242 TYR TYR B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 LYS 245 245 245 LYS LYS B . n 
B 1 246 ASP 246 246 246 ASP ASP B . n 
B 1 247 PHE 247 247 247 PHE PHE B . n 
B 1 248 TRP 248 248 248 TRP TRP B . n 
B 1 249 GLU 249 249 249 GLU GLU B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 ILE 251 251 251 ILE ILE B . n 
B 1 252 LYS 252 252 252 LYS LYS B . n 
B 1 253 THR 253 253 253 THR THR B . n 
B 1 254 PRO 254 254 254 PRO PRO B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 LYS 256 256 256 LYS LYS B . n 
B 1 257 SER 257 257 257 SER SER B . n 
B 1 258 LEU 258 258 258 LEU LEU B . n 
B 1 259 LYS 259 259 259 LYS LYS B . n 
B 1 260 CYS 260 260 260 CYS CYS B . n 
B 1 261 SER 261 261 261 SER SER B . n 
B 1 262 ALA 262 262 262 ALA ALA B . n 
B 1 263 LEU 263 263 263 LEU LEU B . n 
B 1 264 TYR 264 264 264 TYR TYR B . n 
B 1 265 LEU 265 265 265 LEU LEU B . n 
B 1 266 SER 266 266 266 SER SER B . n 
B 1 267 GLN 267 267 267 GLN GLN B . n 
B 1 268 PHE 268 268 268 PHE PHE B . n 
B 1 269 ARG 269 269 269 ARG ARG B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 THR 271 271 271 THR THR B . n 
B 1 272 SER 272 272 272 SER SER B . n 
B 1 273 PRO 273 273 273 PRO PRO B . n 
B 1 274 HIS 274 274 274 HIS HIS B . n 
B 1 275 ILE 275 275 275 ILE ILE B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 ALA 277 277 277 ALA ALA B . n 
B 1 278 SER 278 278 278 SER SER B . n 
B 1 279 GLY 279 279 279 GLY GLY B . n 
B 1 280 ASP 280 280 280 ASP ASP B . n 
B 1 281 GLY 281 281 281 GLY GLY B . n 
B 1 282 THR 282 282 282 THR THR B . n 
B 1 283 ASN 283 283 283 ASN ASN B . n 
B 1 284 ARG 284 284 284 ARG ARG B . n 
B 1 285 LYS 285 285 285 LYS LYS B . n 
B 1 286 PRO 286 286 286 PRO PRO B . n 
B 1 287 THR 287 287 287 THR THR B . n 
B 1 288 ILE 288 288 288 ILE ILE B . n 
B 1 289 ILE 289 289 289 ILE ILE B . n 
B 1 290 GLY 290 290 290 GLY GLY B . n 
B 1 291 ASP 291 291 291 ASP ASP B . n 
B 1 292 VAL 292 292 292 VAL VAL B . n 
B 1 293 TYR 293 293 293 TYR TYR B . n 
B 1 294 ILE 294 294 294 ILE ILE B . n 
B 1 295 HIS 295 295 295 HIS HIS B . n 
B 1 296 PRO 296 296 296 PRO PRO B . n 
B 1 297 SER 297 297 297 SER SER B . n 
B 1 298 VAL 298 298 298 VAL VAL B . n 
B 1 299 LYS 299 299 299 LYS LYS B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 HIS 301 301 301 HIS HIS B . n 
B 1 302 PRO 302 302 302 PRO PRO B . n 
B 1 303 THR 303 303 303 THR THR B . n 
B 1 304 ALA 304 304 304 ALA ALA B . n 
B 1 305 LYS 305 305 305 LYS LYS B . n 
B 1 306 ILE 306 306 306 ILE ILE B . n 
B 1 307 GLY 307 307 307 GLY GLY B . n 
B 1 308 PRO 308 308 308 PRO PRO B . n 
B 1 309 ASN 309 309 309 ASN ASN B . n 
B 1 310 VAL 310 310 310 VAL VAL B . n 
B 1 311 SER 311 311 311 SER SER B . n 
B 1 312 ILE 312 312 312 ILE ILE B . n 
B 1 313 SER 313 313 313 SER SER B . n 
B 1 314 ALA 314 314 314 ALA ALA B . n 
B 1 315 ASN 315 315 315 ASN ASN B . n 
B 1 316 VAL 316 316 316 VAL VAL B . n 
B 1 317 ARG 317 317 317 ARG ARG B . n 
B 1 318 VAL 318 318 318 VAL VAL B . n 
B 1 319 GLY 319 319 319 GLY GLY B . n 
B 1 320 PRO 320 320 320 PRO PRO B . n 
B 1 321 GLY 321 321 321 GLY GLY B . n 
B 1 322 VAL 322 322 322 VAL VAL B . n 
B 1 323 ARG 323 323 323 ARG ARG B . n 
B 1 324 LEU 324 324 324 LEU LEU B . n 
B 1 325 ILE 325 325 325 ILE ILE B . n 
B 1 326 SER 326 326 326 SER SER B . n 
B 1 327 CYS 327 327 327 CYS CYS B . n 
B 1 328 ILE 328 328 328 ILE ILE B . n 
B 1 329 ILE 329 329 329 ILE ILE B . n 
B 1 330 LEU 330 330 330 LEU LEU B . n 
B 1 331 ASP 331 331 331 ASP ASP B . n 
B 1 332 ASP 332 332 332 ASP ASP B . n 
B 1 333 VAL 333 333 333 VAL VAL B . n 
B 1 334 GLU 334 334 334 GLU GLU B . n 
B 1 335 ILE 335 335 335 ILE ILE B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 GLU 337 337 337 GLU GLU B . n 
B 1 338 ASN 338 338 338 ASN ASN B . n 
B 1 339 ALA 339 339 339 ALA ALA B . n 
B 1 340 VAL 340 340 340 VAL VAL B . n 
B 1 341 VAL 341 341 341 VAL VAL B . n 
B 1 342 ILE 342 342 342 ILE ILE B . n 
B 1 343 ASN 343 343 343 ASN ASN B . n 
B 1 344 SER 344 344 344 SER SER B . n 
B 1 345 ILE 345 345 345 ILE ILE B . n 
B 1 346 ILE 346 346 346 ILE ILE B . n 
B 1 347 GLY 347 347 347 GLY GLY B . n 
B 1 348 TRP 348 348 348 TRP TRP B . n 
B 1 349 LYS 349 349 349 LYS LYS B . n 
B 1 350 SER 350 350 350 SER SER B . n 
B 1 351 SER 351 351 351 SER SER B . n 
B 1 352 ILE 352 352 352 ILE ILE B . n 
B 1 353 GLY 353 353 353 GLY GLY B . n 
B 1 354 ARG 354 354 354 ARG ARG B . n 
B 1 355 TRP 355 355 355 TRP TRP B . n 
B 1 356 SER 356 356 356 SER SER B . n 
B 1 357 ARG 357 357 357 ARG ARG B . n 
B 1 358 VAL 358 358 358 VAL VAL B . n 
B 1 359 GLN 359 359 359 GLN GLN B . n 
B 1 360 ALA 360 360 360 ALA ALA B . n 
B 1 361 SER 361 361 361 SER SER B . n 
B 1 362 GLY 362 362 362 GLY GLY B . n 
B 1 363 ASP 363 363 363 ASP ASP B . n 
B 1 364 TYR 364 364 364 TYR TYR B . n 
B 1 365 ASN 365 365 365 ASN ASN B . n 
B 1 366 ASP 366 366 366 ASP ASP B . n 
B 1 367 ARG 367 367 367 ARG ARG B . n 
B 1 368 LEU 368 368 368 LEU LEU B . n 
B 1 369 GLY 369 369 369 GLY GLY B . n 
B 1 370 ILE 370 370 370 ILE ILE B . n 
B 1 371 THR 371 371 371 THR THR B . n 
B 1 372 ILE 372 372 372 ILE ILE B . n 
B 1 373 LEU 373 373 373 LEU LEU B . n 
B 1 374 GLY 374 374 374 GLY GLY B . n 
B 1 375 GLU 375 375 375 GLU GLU B . n 
B 1 376 ALA 376 376 376 ALA ALA B . n 
B 1 377 VAL 377 377 377 VAL VAL B . n 
B 1 378 THR 378 378 378 THR THR B . n 
B 1 379 VAL 379 379 379 VAL VAL B . n 
B 1 380 GLU 380 380 380 GLU GLU B . n 
B 1 381 ASP 381 381 381 ASP ASP B . n 
B 1 382 GLU 382 382 382 GLU GLU B . n 
B 1 383 VAL 383 383 383 VAL VAL B . n 
B 1 384 ALA 384 384 384 ALA ALA B . n 
B 1 385 VAL 385 385 385 VAL VAL B . n 
B 1 386 ILE 386 386 386 ILE ILE B . n 
B 1 387 GLY 387 387 387 GLY GLY B . n 
B 1 388 SER 388 388 388 SER SER B . n 
B 1 389 ILE 389 389 389 ILE ILE B . n 
B 1 390 VAL 390 390 390 VAL VAL B . n 
B 1 391 LEU 391 391 391 LEU LEU B . n 
B 1 392 GLN 392 392 392 GLN GLN B . n 
B 1 393 ASN 393 393 393 ASN ASN B . n 
B 1 394 LYS 394 394 394 LYS LYS B . n 
B 1 395 THR 395 395 395 THR THR B . n 
B 1 396 LEU 396 396 396 LEU LEU B . n 
B 1 397 ASN 397 397 397 ASN ASN B . n 
B 1 398 VAL 398 398 398 VAL VAL B . n 
B 1 399 SER 399 399 399 SER SER B . n 
B 1 400 VAL 400 400 400 VAL VAL B . n 
B 1 401 GLN 401 401 401 GLN GLN B . n 
B 1 402 ASP 402 402 402 ASP ASP B . n 
B 1 403 ASP 403 403 403 ASP ASP B . n 
B 1 404 ILE 404 404 404 ILE ILE B . n 
B 1 405 ILE 405 405 405 ILE ILE B . n 
B 1 406 LEU 406 406 406 LEU LEU B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   GLU 3   3   ?   ?   ?   C . n 
C 1 4   GLU 4   4   4   GLU GLU C . n 
C 1 5   LYS 5   5   5   LYS LYS C . n 
C 1 6   VAL 6   6   6   VAL VAL C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   ALA 8   8   8   ALA ALA C . n 
C 1 9   VAL 9   9   9   VAL VAL C . n 
C 1 10  ILE 10  10  10  ILE ILE C . n 
C 1 11  MET 11  11  11  MET MET C . n 
C 1 12  VAL 12  12  12  VAL VAL C . n 
C 1 13  GLY 13  13  13  GLY GLY C . n 
C 1 14  GLY 14  14  14  GLY GLY C . n 
C 1 15  PRO 15  15  15  PRO PRO C . n 
C 1 16  THR 16  16  16  THR THR C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  GLY 18  18  18  GLY GLY C . n 
C 1 19  THR 19  19  19  THR THR C . n 
C 1 20  ARG 20  20  20  ARG ARG C . n 
C 1 21  PHE 21  21  21  PHE PHE C . n 
C 1 22  ARG 22  22  22  ARG ARG C . n 
C 1 23  PRO 23  23  23  PRO PRO C . n 
C 1 24  LEU 24  24  24  LEU LEU C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  PHE 26  26  26  PHE PHE C . n 
C 1 27  ASN 27  27  27  ASN ASN C . n 
C 1 28  THR 28  28  28  THR THR C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  LYS 30  30  30  LYS LYS C . n 
C 1 31  PRO 31  31  31  PRO PRO C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  ILE 33  33  33  ILE ILE C . n 
C 1 34  PRO 34  34  34  PRO PRO C . n 
C 1 35  LEU 35  35  35  LEU LEU C . n 
C 1 36  ALA 36  36  36  ALA ALA C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  PRO 39  39  39  PRO PRO C . n 
C 1 40  MET 40  40  40  MET MET C . n 
C 1 41  ILE 41  41  41  ILE ILE C . n 
C 1 42  HIS 42  42  42  HIS HIS C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  PRO 44  44  44  PRO PRO C . n 
C 1 45  ILE 45  45  45  ILE ILE C . n 
C 1 46  SER 46  46  46  SER SER C . n 
C 1 47  ALA 47  47  47  ALA ALA C . n 
C 1 48  CYS 48  48  48  CYS CYS C . n 
C 1 49  LYS 49  49  49  LYS LYS C . n 
C 1 50  LYS 50  50  50  LYS LYS C . n 
C 1 51  ILE 51  51  51  ILE ILE C . n 
C 1 52  SER 52  52  52  SER SER C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  LEU 54  54  54  LEU LEU C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  GLN 56  56  56  GLN GLN C . n 
C 1 57  ILE 57  57  57  ILE ILE C . n 
C 1 58  PHE 58  58  58  PHE PHE C . n 
C 1 59  LEU 59  59  59  LEU LEU C . n 
C 1 60  ILE 60  60  60  ILE ILE C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  PHE 62  62  62  PHE PHE C . n 
C 1 63  TYR 63  63  63  TYR TYR C . n 
C 1 64  GLU 64  64  64  GLU GLU C . n 
C 1 65  GLU 65  65  65  GLU GLU C . n 
C 1 66  ARG 66  66  66  ARG ARG C . n 
C 1 67  GLU 67  67  67  GLU GLU C . n 
C 1 68  PHE 68  68  68  PHE PHE C . n 
C 1 69  ALA 69  69  69  ALA ALA C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  TYR 71  71  71  TYR TYR C . n 
C 1 72  VAL 72  72  72  VAL VAL C . n 
C 1 73  SER 73  73  73  SER SER C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ILE 75  75  75  ILE ILE C . n 
C 1 76  SER 76  76  76  SER SER C . n 
C 1 77  ASN 77  77  77  ASN ASN C . n 
C 1 78  GLU 78  78  78  GLU GLU C . n 
C 1 79  LEU 79  79  79  LEU LEU C . n 
C 1 80  LYS 80  80  80  LYS LYS C . n 
C 1 81  ILE 81  81  81  ILE ILE C . n 
C 1 82  PRO 82  82  82  PRO PRO C . n 
C 1 83  VAL 83  83  83  VAL VAL C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  TYR 85  85  85  TYR TYR C . n 
C 1 86  LEU 86  86  86  LEU LEU C . n 
C 1 87  LYS 87  87  87  LYS LYS C . n 
C 1 88  GLU 88  88  88  GLU GLU C . n 
C 1 89  ASP 89  89  89  ASP ASP C . n 
C 1 90  LYS 90  90  90  LYS LYS C . n 
C 1 91  PRO 91  91  91  PRO PRO C . n 
C 1 92  HIS 92  92  92  HIS HIS C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  SER 94  94  94  SER SER C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  GLY 96  96  96  GLY GLY C . n 
C 1 97  ALA 97  97  97  ALA ALA C . n 
C 1 98  LEU 98  98  98  LEU LEU C . n 
C 1 99  TYR 99  99  99  TYR TYR C . n 
C 1 100 TYR 100 100 100 TYR TYR C . n 
C 1 101 PHE 101 101 101 PHE PHE C . n 
C 1 102 ARG 102 102 102 ARG ARG C . n 
C 1 103 ASP 103 103 103 ASP ASP C . n 
C 1 104 ARG 104 104 104 ARG ARG C . n 
C 1 105 ILE 105 105 105 ILE ILE C . n 
C 1 106 MET 106 106 106 MET MET C . n 
C 1 107 GLU 107 107 107 GLU GLU C . n 
C 1 108 GLU 108 108 108 GLU GLU C . n 
C 1 109 LYS 109 109 109 LYS LYS C . n 
C 1 110 PRO 110 110 110 PRO PRO C . n 
C 1 111 SER 111 111 111 SER SER C . n 
C 1 112 HIS 112 112 112 HIS HIS C . n 
C 1 113 VAL 113 113 113 VAL VAL C . n 
C 1 114 PHE 114 114 114 PHE PHE C . n 
C 1 115 LEU 115 115 115 LEU LEU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 ASN 117 117 117 ASN ASN C . n 
C 1 118 CYS 118 118 118 CYS CYS C . n 
C 1 119 ASP 119 119 119 ASP ASP C . n 
C 1 120 VAL 120 120 120 VAL VAL C . n 
C 1 121 CYS 121 121 121 CYS CYS C . n 
C 1 122 CYS 122 122 122 CYS CYS C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 PHE 124 124 124 PHE PHE C . n 
C 1 125 PRO 125 125 125 PRO PRO C . n 
C 1 126 LEU 126 126 126 LEU LEU C . n 
C 1 127 GLN 127 127 127 GLN GLN C . n 
C 1 128 GLY 128 128 128 GLY GLY C . n 
C 1 129 ILE 129 129 129 ILE ILE C . n 
C 1 130 LEU 130 130 130 LEU LEU C . n 
C 1 131 ASP 131 131 131 ASP ASP C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 HIS 133 133 133 HIS HIS C . n 
C 1 134 ARG 134 134 134 ARG ARG C . n 
C 1 135 ARG 135 135 135 ARG ARG C . n 
C 1 136 TYR 136 136 136 TYR TYR C . n 
C 1 137 GLY 137 137 137 GLY GLY C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 ILE 139 139 139 ILE ILE C . n 
C 1 140 GLY 140 140 140 GLY GLY C . n 
C 1 141 THR 141 141 141 THR THR C . n 
C 1 142 MET 142 142 ?   ?   ?   C . n 
C 1 143 LEU 143 143 ?   ?   ?   C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 ILE 145 145 145 ILE ILE C . n 
C 1 146 LYS 146 146 146 LYS LYS C . n 
C 1 147 VAL 147 147 147 VAL VAL C . n 
C 1 148 SER 148 148 148 SER SER C . n 
C 1 149 ALA 149 149 149 ALA ALA C . n 
C 1 150 GLU 150 150 150 GLU GLU C . n 
C 1 151 ALA 151 151 151 ALA ALA C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 SER 153 153 153 SER SER C . n 
C 1 154 GLN 154 154 154 GLN GLN C . n 
C 1 155 PHE 155 155 155 PHE PHE C . n 
C 1 156 GLY 156 156 156 GLY GLY C . n 
C 1 157 GLU 157 157 157 GLU GLU C . n 
C 1 158 LEU 158 158 158 LEU LEU C . n 
C 1 159 ILE 159 159 159 ILE ILE C . n 
C 1 160 ALA 160 160 160 ALA ALA C . n 
C 1 161 ASP 161 161 161 ASP ASP C . n 
C 1 162 PRO 162 162 162 PRO PRO C . n 
C 1 163 ASP 163 163 163 ASP ASP C . n 
C 1 164 THR 164 164 164 THR THR C . n 
C 1 165 LYS 165 165 165 LYS LYS C . n 
C 1 166 GLU 166 166 166 GLU GLU C . n 
C 1 167 LEU 167 167 167 LEU LEU C . n 
C 1 168 LEU 168 168 168 LEU LEU C . n 
C 1 169 HIS 169 169 169 HIS HIS C . n 
C 1 170 TYR 170 170 170 TYR TYR C . n 
C 1 171 THR 171 171 171 THR THR C . n 
C 1 172 GLU 172 172 172 GLU GLU C . n 
C 1 173 LYS 173 173 173 LYS LYS C . n 
C 1 174 PRO 174 174 174 PRO PRO C . n 
C 1 175 GLU 175 175 175 GLU GLU C . n 
C 1 176 THR 176 176 176 THR THR C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 VAL 178 178 178 VAL VAL C . n 
C 1 179 SER 179 179 179 SER SER C . n 
C 1 180 ASP 180 180 180 ASP ASP C . n 
C 1 181 LEU 181 181 181 LEU LEU C . n 
C 1 182 ILE 182 182 182 ILE ILE C . n 
C 1 183 ASN 183 183 183 ASN ASN C . n 
C 1 184 CYS 184 184 184 CYS CYS C . n 
C 1 185 GLY 185 185 185 GLY GLY C . n 
C 1 186 VAL 186 186 ?   ?   ?   C . n 
C 1 187 TYR 187 187 ?   ?   ?   C . n 
C 1 188 VAL 188 188 188 VAL VAL C . n 
C 1 189 PHE 189 189 189 PHE PHE C . n 
C 1 190 THR 190 190 190 THR THR C . n 
C 1 191 SER 191 191 191 SER SER C . n 
C 1 192 ASP 192 192 192 ASP ASP C . n 
C 1 193 ILE 193 193 193 ILE ILE C . n 
C 1 194 PHE 194 194 194 PHE PHE C . n 
C 1 195 ASN 195 195 195 ASN ASN C . n 
C 1 196 ALA 196 196 196 ALA ALA C . n 
C 1 197 ILE 197 197 197 ILE ILE C . n 
C 1 198 GLU 198 198 198 GLU GLU C . n 
C 1 199 GLU 199 199 199 GLU GLU C . n 
C 1 200 VAL 200 200 200 VAL VAL C . n 
C 1 201 TYR 201 201 201 TYR TYR C . n 
C 1 202 SER 202 202 202 SER SER C . n 
C 1 203 GLN 203 203 203 GLN GLN C . n 
C 1 204 ILE 204 204 204 ILE ILE C . n 
C 1 205 ARG 205 205 205 ARG ARG C . n 
C 1 206 ASP 206 206 ?   ?   ?   C . n 
C 1 207 THR 207 207 ?   ?   ?   C . n 
C 1 208 SER 208 208 ?   ?   ?   C . n 
C 1 209 SER 209 209 ?   ?   ?   C . n 
C 1 210 ASN 210 210 ?   ?   ?   C . n 
C 1 211 TYR 211 211 ?   ?   ?   C . n 
C 1 212 GLN 212 212 ?   ?   ?   C . n 
C 1 213 SER 213 213 ?   ?   ?   C . n 
C 1 214 ALA 214 214 ?   ?   ?   C . n 
C 1 215 THR 215 215 ?   ?   ?   C . n 
C 1 216 ARG 216 216 ?   ?   ?   C . n 
C 1 217 SER 217 217 ?   ?   ?   C . n 
C 1 218 VAL 218 218 ?   ?   ?   C . n 
C 1 219 PRO 219 219 ?   ?   ?   C . n 
C 1 220 ALA 220 220 ?   ?   ?   C . n 
C 1 221 ASP 221 221 ?   ?   ?   C . n 
C 1 222 PHE 222 222 222 PHE PHE C . n 
C 1 223 VAL 223 223 223 VAL VAL C . n 
C 1 224 ARG 224 224 224 ARG ARG C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 ASP 226 226 226 ASP ASP C . n 
C 1 227 GLN 227 227 227 GLN GLN C . n 
C 1 228 ASP 228 228 228 ASP ASP C . n 
C 1 229 ILE 229 229 229 ILE ILE C . n 
C 1 230 LEU 230 230 230 LEU LEU C . n 
C 1 231 SER 231 231 231 SER SER C . n 
C 1 232 PRO 232 232 232 PRO PRO C . n 
C 1 233 LEU 233 233 233 LEU LEU C . n 
C 1 234 ALA 234 234 234 ALA ALA C . n 
C 1 235 GLY 235 235 235 GLY GLY C . n 
C 1 236 LYS 236 236 236 LYS LYS C . n 
C 1 237 LYS 237 237 237 LYS LYS C . n 
C 1 238 GLN 238 238 238 GLN GLN C . n 
C 1 239 LEU 239 239 239 LEU LEU C . n 
C 1 240 TYR 240 240 240 TYR TYR C . n 
C 1 241 THR 241 241 241 THR THR C . n 
C 1 242 TYR 242 242 ?   ?   ?   C . n 
C 1 243 GLU 243 243 ?   ?   ?   C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 LYS 245 245 245 LYS LYS C . n 
C 1 246 ASP 246 246 246 ASP ASP C . n 
C 1 247 PHE 247 247 247 PHE PHE C . n 
C 1 248 TRP 248 248 248 TRP TRP C . n 
C 1 249 GLU 249 249 249 GLU GLU C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 ILE 251 251 251 ILE ILE C . n 
C 1 252 LYS 252 252 252 LYS LYS C . n 
C 1 253 THR 253 253 253 THR THR C . n 
C 1 254 PRO 254 254 254 PRO PRO C . n 
C 1 255 GLY 255 255 255 GLY GLY C . n 
C 1 256 LYS 256 256 256 LYS LYS C . n 
C 1 257 SER 257 257 257 SER SER C . n 
C 1 258 LEU 258 258 258 LEU LEU C . n 
C 1 259 LYS 259 259 259 LYS LYS C . n 
C 1 260 CYS 260 260 260 CYS CYS C . n 
C 1 261 SER 261 261 261 SER SER C . n 
C 1 262 ALA 262 262 262 ALA ALA C . n 
C 1 263 LEU 263 263 263 LEU LEU C . n 
C 1 264 TYR 264 264 264 TYR TYR C . n 
C 1 265 LEU 265 265 265 LEU LEU C . n 
C 1 266 SER 266 266 266 SER SER C . n 
C 1 267 GLN 267 267 267 GLN GLN C . n 
C 1 268 PHE 268 268 268 PHE PHE C . n 
C 1 269 ARG 269 269 269 ARG ARG C . n 
C 1 270 GLU 270 270 270 GLU GLU C . n 
C 1 271 THR 271 271 271 THR THR C . n 
C 1 272 SER 272 272 272 SER SER C . n 
C 1 273 PRO 273 273 273 PRO PRO C . n 
C 1 274 HIS 274 274 274 HIS HIS C . n 
C 1 275 ILE 275 275 275 ILE ILE C . n 
C 1 276 LEU 276 276 276 LEU LEU C . n 
C 1 277 ALA 277 277 277 ALA ALA C . n 
C 1 278 SER 278 278 278 SER SER C . n 
C 1 279 GLY 279 279 279 GLY GLY C . n 
C 1 280 ASP 280 280 280 ASP ASP C . n 
C 1 281 GLY 281 281 281 GLY GLY C . n 
C 1 282 THR 282 282 282 THR THR C . n 
C 1 283 ASN 283 283 283 ASN ASN C . n 
C 1 284 ARG 284 284 284 ARG ARG C . n 
C 1 285 LYS 285 285 285 LYS LYS C . n 
C 1 286 PRO 286 286 286 PRO PRO C . n 
C 1 287 THR 287 287 287 THR THR C . n 
C 1 288 ILE 288 288 288 ILE ILE C . n 
C 1 289 ILE 289 289 289 ILE ILE C . n 
C 1 290 GLY 290 290 290 GLY GLY C . n 
C 1 291 ASP 291 291 291 ASP ASP C . n 
C 1 292 VAL 292 292 292 VAL VAL C . n 
C 1 293 TYR 293 293 293 TYR TYR C . n 
C 1 294 ILE 294 294 294 ILE ILE C . n 
C 1 295 HIS 295 295 295 HIS HIS C . n 
C 1 296 PRO 296 296 296 PRO PRO C . n 
C 1 297 SER 297 297 297 SER SER C . n 
C 1 298 VAL 298 298 298 VAL VAL C . n 
C 1 299 LYS 299 299 299 LYS LYS C . n 
C 1 300 LEU 300 300 300 LEU LEU C . n 
C 1 301 HIS 301 301 301 HIS HIS C . n 
C 1 302 PRO 302 302 302 PRO PRO C . n 
C 1 303 THR 303 303 303 THR THR C . n 
C 1 304 ALA 304 304 304 ALA ALA C . n 
C 1 305 LYS 305 305 305 LYS LYS C . n 
C 1 306 ILE 306 306 306 ILE ILE C . n 
C 1 307 GLY 307 307 307 GLY GLY C . n 
C 1 308 PRO 308 308 308 PRO PRO C . n 
C 1 309 ASN 309 309 309 ASN ASN C . n 
C 1 310 VAL 310 310 310 VAL VAL C . n 
C 1 311 SER 311 311 311 SER SER C . n 
C 1 312 ILE 312 312 312 ILE ILE C . n 
C 1 313 SER 313 313 313 SER SER C . n 
C 1 314 ALA 314 314 314 ALA ALA C . n 
C 1 315 ASN 315 315 315 ASN ASN C . n 
C 1 316 VAL 316 316 316 VAL VAL C . n 
C 1 317 ARG 317 317 317 ARG ARG C . n 
C 1 318 VAL 318 318 318 VAL VAL C . n 
C 1 319 GLY 319 319 319 GLY GLY C . n 
C 1 320 PRO 320 320 320 PRO PRO C . n 
C 1 321 GLY 321 321 321 GLY GLY C . n 
C 1 322 VAL 322 322 322 VAL VAL C . n 
C 1 323 ARG 323 323 323 ARG ARG C . n 
C 1 324 LEU 324 324 324 LEU LEU C . n 
C 1 325 ILE 325 325 325 ILE ILE C . n 
C 1 326 SER 326 326 326 SER SER C . n 
C 1 327 CYS 327 327 327 CYS CYS C . n 
C 1 328 ILE 328 328 328 ILE ILE C . n 
C 1 329 ILE 329 329 329 ILE ILE C . n 
C 1 330 LEU 330 330 330 LEU LEU C . n 
C 1 331 ASP 331 331 331 ASP ASP C . n 
C 1 332 ASP 332 332 332 ASP ASP C . n 
C 1 333 VAL 333 333 333 VAL VAL C . n 
C 1 334 GLU 334 334 334 GLU GLU C . n 
C 1 335 ILE 335 335 335 ILE ILE C . n 
C 1 336 LYS 336 336 336 LYS LYS C . n 
C 1 337 GLU 337 337 337 GLU GLU C . n 
C 1 338 ASN 338 338 338 ASN ASN C . n 
C 1 339 ALA 339 339 339 ALA ALA C . n 
C 1 340 VAL 340 340 340 VAL VAL C . n 
C 1 341 VAL 341 341 341 VAL VAL C . n 
C 1 342 ILE 342 342 342 ILE ILE C . n 
C 1 343 ASN 343 343 343 ASN ASN C . n 
C 1 344 SER 344 344 344 SER SER C . n 
C 1 345 ILE 345 345 345 ILE ILE C . n 
C 1 346 ILE 346 346 346 ILE ILE C . n 
C 1 347 GLY 347 347 347 GLY GLY C . n 
C 1 348 TRP 348 348 348 TRP TRP C . n 
C 1 349 LYS 349 349 349 LYS LYS C . n 
C 1 350 SER 350 350 350 SER SER C . n 
C 1 351 SER 351 351 351 SER SER C . n 
C 1 352 ILE 352 352 352 ILE ILE C . n 
C 1 353 GLY 353 353 353 GLY GLY C . n 
C 1 354 ARG 354 354 354 ARG ARG C . n 
C 1 355 TRP 355 355 355 TRP TRP C . n 
C 1 356 SER 356 356 356 SER SER C . n 
C 1 357 ARG 357 357 357 ARG ARG C . n 
C 1 358 VAL 358 358 358 VAL VAL C . n 
C 1 359 GLN 359 359 359 GLN GLN C . n 
C 1 360 ALA 360 360 360 ALA ALA C . n 
C 1 361 SER 361 361 361 SER SER C . n 
C 1 362 GLY 362 362 362 GLY GLY C . n 
C 1 363 ASP 363 363 363 ASP ASP C . n 
C 1 364 TYR 364 364 364 TYR TYR C . n 
C 1 365 ASN 365 365 365 ASN ASN C . n 
C 1 366 ASP 366 366 366 ASP ASP C . n 
C 1 367 ARG 367 367 367 ARG ARG C . n 
C 1 368 LEU 368 368 368 LEU LEU C . n 
C 1 369 GLY 369 369 369 GLY GLY C . n 
C 1 370 ILE 370 370 370 ILE ILE C . n 
C 1 371 THR 371 371 371 THR THR C . n 
C 1 372 ILE 372 372 372 ILE ILE C . n 
C 1 373 LEU 373 373 373 LEU LEU C . n 
C 1 374 GLY 374 374 374 GLY GLY C . n 
C 1 375 GLU 375 375 375 GLU GLU C . n 
C 1 376 ALA 376 376 376 ALA ALA C . n 
C 1 377 VAL 377 377 377 VAL VAL C . n 
C 1 378 THR 378 378 378 THR THR C . n 
C 1 379 VAL 379 379 379 VAL VAL C . n 
C 1 380 GLU 380 380 380 GLU GLU C . n 
C 1 381 ASP 381 381 381 ASP ASP C . n 
C 1 382 GLU 382 382 382 GLU GLU C . n 
C 1 383 VAL 383 383 383 VAL VAL C . n 
C 1 384 ALA 384 384 384 ALA ALA C . n 
C 1 385 VAL 385 385 385 VAL VAL C . n 
C 1 386 ILE 386 386 386 ILE ILE C . n 
C 1 387 GLY 387 387 387 GLY GLY C . n 
C 1 388 SER 388 388 388 SER SER C . n 
C 1 389 ILE 389 389 389 ILE ILE C . n 
C 1 390 VAL 390 390 390 VAL VAL C . n 
C 1 391 LEU 391 391 391 LEU LEU C . n 
C 1 392 GLN 392 392 392 GLN GLN C . n 
C 1 393 ASN 393 393 393 ASN ASN C . n 
C 1 394 LYS 394 394 394 LYS LYS C . n 
C 1 395 THR 395 395 395 THR THR C . n 
C 1 396 LEU 396 396 396 LEU LEU C . n 
C 1 397 ASN 397 397 397 ASN ASN C . n 
C 1 398 VAL 398 398 398 VAL VAL C . n 
C 1 399 SER 399 399 399 SER SER C . n 
C 1 400 VAL 400 400 400 VAL VAL C . n 
C 1 401 GLN 401 401 401 GLN GLN C . n 
C 1 402 ASP 402 402 402 ASP ASP C . n 
C 1 403 ASP 403 403 403 ASP ASP C . n 
C 1 404 ILE 404 404 404 ILE ILE C . n 
C 1 405 ILE 405 405 405 ILE ILE C . n 
C 1 406 LEU 406 406 406 LEU LEU C . n 
D 2 1   MET 1   1   1   MET MET D . n 
D 2 2   LYS 2   2   2   LYS LYS D . n 
D 2 3   ALA 3   3   3   ALA ALA D . n 
D 2 4   LEU 4   4   4   LEU LEU D . n 
D 2 5   ILE 5   5   5   ILE ILE D . n 
D 2 6   LEU 6   6   6   LEU LEU D . n 
D 2 7   VAL 7   7   7   VAL VAL D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   GLY 9   9   9   GLY GLY D . n 
D 2 10  PHE 10  10  10  PHE PHE D . n 
D 2 11  GLY 11  11  11  GLY GLY D . n 
D 2 12  THR 12  12  12  THR THR D . n 
D 2 13  ARG 13  13  13  ARG ARG D . n 
D 2 14  LEU 14  14  14  LEU LEU D . n 
D 2 15  ARG 15  15  15  ARG ARG D . n 
D 2 16  PRO 16  16  16  PRO PRO D . n 
D 2 17  LEU 17  17  17  LEU LEU D . n 
D 2 18  THR 18  18  18  THR THR D . n 
D 2 19  LEU 19  19  19  LEU LEU D . n 
D 2 20  SER 20  20  20  SER SER D . n 
D 2 21  PHE 21  21  21  PHE PHE D . n 
D 2 22  PRO 22  22  22  PRO PRO D . n 
D 2 23  LYS 23  23  23  LYS LYS D . n 
D 2 24  PRO 24  24  24  PRO PRO D . n 
D 2 25  LEU 25  25  25  LEU LEU D . n 
D 2 26  VAL 26  26  26  VAL VAL D . n 
D 2 27  ASP 27  27  27  ASP ASP D . n 
D 2 28  PHE 28  28  28  PHE PHE D . n 
D 2 29  ALA 29  29  29  ALA ALA D . n 
D 2 30  ASN 30  30  30  ASN ASN D . n 
D 2 31  LYS 31  31  31  LYS LYS D . n 
D 2 32  PRO 32  32  32  PRO PRO D . n 
D 2 33  MET 33  33  33  MET MET D . n 
D 2 34  ILE 34  34  34  ILE ILE D . n 
D 2 35  LEU 35  35  35  LEU LEU D . n 
D 2 36  HIS 36  36  36  HIS HIS D . n 
D 2 37  GLN 37  37  37  GLN GLN D . n 
D 2 38  ILE 38  38  38  ILE ILE D . n 
D 2 39  GLU 39  39  39  GLU GLU D . n 
D 2 40  ALA 40  40  40  ALA ALA D . n 
D 2 41  LEU 41  41  41  LEU LEU D . n 
D 2 42  LYS 42  42  42  LYS LYS D . n 
D 2 43  ALA 43  43  43  ALA ALA D . n 
D 2 44  VAL 44  44  44  VAL VAL D . n 
D 2 45  GLY 45  45  45  GLY GLY D . n 
D 2 46  VAL 46  46  46  VAL VAL D . n 
D 2 47  ASP 47  47  47  ASP ASP D . n 
D 2 48  GLU 48  48  48  GLU GLU D . n 
D 2 49  VAL 49  49  49  VAL VAL D . n 
D 2 50  VAL 50  50  50  VAL VAL D . n 
D 2 51  LEU 51  51  51  LEU LEU D . n 
D 2 52  ALA 52  52  52  ALA ALA D . n 
D 2 53  ILE 53  53  53  ILE ILE D . n 
D 2 54  ASN 54  54  54  ASN ASN D . n 
D 2 55  TYR 55  55  55  TYR TYR D . n 
D 2 56  GLN 56  56  56  GLN GLN D . n 
D 2 57  PRO 57  57  57  PRO PRO D . n 
D 2 58  GLU 58  58  58  GLU GLU D . n 
D 2 59  VAL 59  59  59  VAL VAL D . n 
D 2 60  MET 60  60  60  MET MET D . n 
D 2 61  LEU 61  61  61  LEU LEU D . n 
D 2 62  ASN 62  62  62  ASN ASN D . n 
D 2 63  PHE 63  63  63  PHE PHE D . n 
D 2 64  LEU 64  64  64  LEU LEU D . n 
D 2 65  LYS 65  65  65  LYS LYS D . n 
D 2 66  ASP 66  66  66  ASP ASP D . n 
D 2 67  PHE 67  67  67  PHE PHE D . n 
D 2 68  GLU 68  68  68  GLU GLU D . n 
D 2 69  THR 69  69  69  THR THR D . n 
D 2 70  LYS 70  70  70  LYS LYS D . n 
D 2 71  LEU 71  71  71  LEU LEU D . n 
D 2 72  GLU 72  72  72  GLU GLU D . n 
D 2 73  ILE 73  73  73  ILE ILE D . n 
D 2 74  LYS 74  74  74  LYS LYS D . n 
D 2 75  ILE 75  75  75  ILE ILE D . n 
D 2 76  THR 76  76  76  THR THR D . n 
D 2 77  CYS 77  77  77  CYS CYS D . n 
D 2 78  SER 78  78  78  SER SER D . n 
D 2 79  GLN 79  79  79  GLN GLN D . n 
D 2 80  GLU 80  80  80  GLU GLU D . n 
D 2 81  THR 81  81  81  THR THR D . n 
D 2 82  GLU 82  82  82  GLU GLU D . n 
D 2 83  PRO 83  83  83  PRO PRO D . n 
D 2 84  LEU 84  84  84  LEU LEU D . n 
D 2 85  GLY 85  85  85  GLY GLY D . n 
D 2 86  THR 86  86  86  THR THR D . n 
D 2 87  ALA 87  87  87  ALA ALA D . n 
D 2 88  GLY 88  88  88  GLY GLY D . n 
D 2 89  PRO 89  89  89  PRO PRO D . n 
D 2 90  LEU 90  90  90  LEU LEU D . n 
D 2 91  ALA 91  91  91  ALA ALA D . n 
D 2 92  LEU 92  92  92  LEU LEU D . n 
D 2 93  ALA 93  93  93  ALA ALA D . n 
D 2 94  ARG 94  94  94  ARG ARG D . n 
D 2 95  ASP 95  95  95  ASP ASP D . n 
D 2 96  LYS 96  96  96  LYS LYS D . n 
D 2 97  LEU 97  97  97  LEU LEU D . n 
D 2 98  LEU 98  98  98  LEU LEU D . n 
D 2 99  ASP 99  99  99  ASP ASP D . n 
D 2 100 GLY 100 100 100 GLY GLY D . n 
D 2 101 SER 101 101 101 SER SER D . n 
D 2 102 GLY 102 102 102 GLY GLY D . n 
D 2 103 GLU 103 103 103 GLU GLU D . n 
D 2 104 PRO 104 104 104 PRO PRO D . n 
D 2 105 PHE 105 105 105 PHE PHE D . n 
D 2 106 PHE 106 106 106 PHE PHE D . n 
D 2 107 VAL 107 107 107 VAL VAL D . n 
D 2 108 LEU 108 108 108 LEU LEU D . n 
D 2 109 ASN 109 109 109 ASN ASN D . n 
D 2 110 SER 110 110 110 SER SER D . n 
D 2 111 ASP 111 111 111 ASP ASP D . n 
D 2 112 VAL 112 112 112 VAL VAL D . n 
D 2 113 ILE 113 113 113 ILE ILE D . n 
D 2 114 SER 114 114 114 SER SER D . n 
D 2 115 GLU 115 115 115 GLU GLU D . n 
D 2 116 TYR 116 116 116 TYR TYR D . n 
D 2 117 PRO 117 117 117 PRO PRO D . n 
D 2 118 LEU 118 118 118 LEU LEU D . n 
D 2 119 LYS 119 119 119 LYS LYS D . n 
D 2 120 GLU 120 120 120 GLU GLU D . n 
D 2 121 MET 121 121 121 MET MET D . n 
D 2 122 LEU 122 122 122 LEU LEU D . n 
D 2 123 GLU 123 123 123 GLU GLU D . n 
D 2 124 PHE 124 124 124 PHE PHE D . n 
D 2 125 HIS 125 125 125 HIS HIS D . n 
D 2 126 LYS 126 126 126 LYS LYS D . n 
D 2 127 SER 127 127 127 SER SER D . n 
D 2 128 HIS 128 128 128 HIS HIS D . n 
D 2 129 GLY 129 129 129 GLY GLY D . n 
D 2 130 GLY 130 130 130 GLY GLY D . n 
D 2 131 GLU 131 131 131 GLU GLU D . n 
D 2 132 ALA 132 132 132 ALA ALA D . n 
D 2 133 SER 133 133 133 SER SER D . n 
D 2 134 ILE 134 134 134 ILE ILE D . n 
D 2 135 MET 135 135 135 MET MET D . n 
D 2 136 VAL 136 136 136 VAL VAL D . n 
D 2 137 THR 137 137 137 THR THR D . n 
D 2 138 LYS 138 138 138 LYS LYS D . n 
D 2 139 VAL 139 139 139 VAL VAL D . n 
D 2 140 ASP 140 140 140 ASP ASP D . n 
D 2 141 GLU 141 141 141 GLU GLU D . n 
D 2 142 PRO 142 142 142 PRO PRO D . n 
D 2 143 SER 143 143 143 SER SER D . n 
D 2 144 LYS 144 144 144 LYS LYS D . n 
D 2 145 TYR 145 145 145 TYR TYR D . n 
D 2 146 GLY 146 146 146 GLY GLY D . n 
D 2 147 VAL 147 147 147 VAL VAL D . n 
D 2 148 VAL 148 148 148 VAL VAL D . n 
D 2 149 VAL 149 149 149 VAL VAL D . n 
D 2 150 MET 150 150 150 MET MET D . n 
D 2 151 GLU 151 151 151 GLU GLU D . n 
D 2 152 GLU 152 152 152 GLU GLU D . n 
D 2 153 SER 153 153 153 SER SER D . n 
D 2 154 THR 154 154 154 THR THR D . n 
D 2 155 GLY 155 155 155 GLY GLY D . n 
D 2 156 ARG 156 156 156 ARG ARG D . n 
D 2 157 VAL 157 157 157 VAL VAL D . n 
D 2 158 GLU 158 158 158 GLU GLU D . n 
D 2 159 LYS 159 159 159 LYS LYS D . n 
D 2 160 PHE 160 160 160 PHE PHE D . n 
D 2 161 VAL 161 161 161 VAL VAL D . n 
D 2 162 GLU 162 162 162 GLU GLU D . n 
D 2 163 LYS 163 163 163 LYS LYS D . n 
D 2 164 PRO 164 164 164 PRO PRO D . n 
D 2 165 LYS 165 165 165 LYS LYS D . n 
D 2 166 LEU 166 166 166 LEU LEU D . n 
D 2 167 TYR 167 167 167 TYR TYR D . n 
D 2 168 VAL 168 168 168 VAL VAL D . n 
D 2 169 GLY 169 169 169 GLY GLY D . n 
D 2 170 ASN 170 170 170 ASN ASN D . n 
D 2 171 LYS 171 171 171 LYS LYS D . n 
D 2 172 ILE 172 172 172 ILE ILE D . n 
D 2 173 ASN 173 173 173 ASN ASN D . n 
D 2 174 ALA 174 174 174 ALA ALA D . n 
D 2 175 GLY 175 175 175 GLY GLY D . n 
D 2 176 ILE 176 176 176 ILE ILE D . n 
D 2 177 TYR 177 177 177 TYR TYR D . n 
D 2 178 LEU 178 178 178 LEU LEU D . n 
D 2 179 LEU 179 179 179 LEU LEU D . n 
D 2 180 ASN 180 180 180 ASN ASN D . n 
D 2 181 PRO 181 181 181 PRO PRO D . n 
D 2 182 SER 182 182 182 SER SER D . n 
D 2 183 VAL 183 183 183 VAL VAL D . n 
D 2 184 LEU 184 184 184 LEU LEU D . n 
D 2 185 ASP 185 185 185 ASP ASP D . n 
D 2 186 LYS 186 186 186 LYS LYS D . n 
D 2 187 ILE 187 187 187 ILE ILE D . n 
D 2 188 GLU 188 188 188 GLU GLU D . n 
D 2 189 LEU 189 189 189 LEU LEU D . n 
D 2 190 ARG 190 190 190 ARG ARG D . n 
D 2 191 PRO 191 191 191 PRO PRO D . n 
D 2 192 THR 192 192 192 THR THR D . n 
D 2 193 SER 193 193 193 SER SER D . n 
D 2 194 ILE 194 194 194 ILE ILE D . n 
D 2 195 GLU 195 195 195 GLU GLU D . n 
D 2 196 LYS 196 196 196 LYS LYS D . n 
D 2 197 GLU 197 197 197 GLU GLU D . n 
D 2 198 THR 198 198 198 THR THR D . n 
D 2 199 PHE 199 199 199 PHE PHE D . n 
D 2 200 PRO 200 200 200 PRO PRO D . n 
D 2 201 LYS 201 201 201 LYS LYS D . n 
D 2 202 ILE 202 202 202 ILE ILE D . n 
D 2 203 ALA 203 203 203 ALA ALA D . n 
D 2 204 ALA 204 204 204 ALA ALA D . n 
D 2 205 ALA 205 205 205 ALA ALA D . n 
D 2 206 GLN 206 206 206 GLN GLN D . n 
D 2 207 GLY 207 207 207 GLY GLY D . n 
D 2 208 LEU 208 208 208 LEU LEU D . n 
D 2 209 TYR 209 209 209 TYR TYR D . n 
D 2 210 ALA 210 210 210 ALA ALA D . n 
D 2 211 MET 211 211 211 MET MET D . n 
D 2 212 VAL 212 212 212 VAL VAL D . n 
D 2 213 LEU 213 213 213 LEU LEU D . n 
D 2 214 PRO 214 214 214 PRO PRO D . n 
D 2 215 GLY 215 215 215 GLY GLY D . n 
D 2 216 PHE 216 216 216 PHE PHE D . n 
D 2 217 TRP 217 217 217 TRP TRP D . n 
D 2 218 MET 218 218 218 MET MET D . n 
D 2 219 ASP 219 219 219 ASP ASP D . n 
D 2 220 ILE 220 220 220 ILE ILE D . n 
D 2 221 GLY 221 221 221 GLY GLY D . n 
D 2 222 GLN 222 222 222 GLN GLN D . n 
D 2 223 PRO 223 223 223 PRO PRO D . n 
D 2 224 ARG 224 224 224 ARG ARG D . n 
D 2 225 ASP 225 225 225 ASP ASP D . n 
D 2 226 TYR 226 226 226 TYR TYR D . n 
D 2 227 ILE 227 227 227 ILE ILE D . n 
D 2 228 THR 228 228 228 THR THR D . n 
D 2 229 GLY 229 229 229 GLY GLY D . n 
D 2 230 LEU 230 230 230 LEU LEU D . n 
D 2 231 ARG 231 231 231 ARG ARG D . n 
D 2 232 LEU 232 232 232 LEU LEU D . n 
D 2 233 TYR 233 233 233 TYR TYR D . n 
D 2 234 LEU 234 234 234 LEU LEU D . n 
D 2 235 ASP 235 235 235 ASP ASP D . n 
D 2 236 SER 236 236 236 SER SER D . n 
D 2 237 LEU 237 237 237 LEU LEU D . n 
D 2 238 ARG 238 238 238 ARG ARG D . n 
D 2 239 LYS 239 239 239 LYS LYS D . n 
D 2 240 LYS 240 240 240 LYS LYS D . n 
D 2 241 SER 241 241 241 SER SER D . n 
D 2 242 PRO 242 242 242 PRO PRO D . n 
D 2 243 ALA 243 243 243 ALA ALA D . n 
D 2 244 LYS 244 244 244 LYS LYS D . n 
D 2 245 LEU 245 245 245 LEU LEU D . n 
D 2 246 THR 246 246 246 THR THR D . n 
D 2 247 SER 247 247 247 SER SER D . n 
D 2 248 GLY 248 248 248 GLY GLY D . n 
D 2 249 PRO 249 249 249 PRO PRO D . n 
D 2 250 HIS 250 250 250 HIS HIS D . n 
D 2 251 ILE 251 251 251 ILE ILE D . n 
D 2 252 VAL 252 252 252 VAL VAL D . n 
D 2 253 GLY 253 253 253 GLY GLY D . n 
D 2 254 ASN 254 254 254 ASN ASN D . n 
D 2 255 VAL 255 255 255 VAL VAL D . n 
D 2 256 LEU 256 256 256 LEU LEU D . n 
D 2 257 VAL 257 257 257 VAL VAL D . n 
D 2 258 ASP 258 258 258 ASP ASP D . n 
D 2 259 GLU 259 259 259 GLU GLU D . n 
D 2 260 THR 260 260 260 THR THR D . n 
D 2 261 ALA 261 261 261 ALA ALA D . n 
D 2 262 THR 262 262 262 THR THR D . n 
D 2 263 ILE 263 263 263 ILE ILE D . n 
D 2 264 GLY 264 264 264 GLY GLY D . n 
D 2 265 GLU 265 265 265 GLU GLU D . n 
D 2 266 GLY 266 266 266 GLY GLY D . n 
D 2 267 CYS 267 267 267 CYS CYS D . n 
D 2 268 LEU 268 268 268 LEU LEU D . n 
D 2 269 ILE 269 269 269 ILE ILE D . n 
D 2 270 GLY 270 270 270 GLY GLY D . n 
D 2 271 PRO 271 271 271 PRO PRO D . n 
D 2 272 ASP 272 272 272 ASP ASP D . n 
D 2 273 VAL 273 273 273 VAL VAL D . n 
D 2 274 ALA 274 274 274 ALA ALA D . n 
D 2 275 ILE 275 275 275 ILE ILE D . n 
D 2 276 GLY 276 276 276 GLY GLY D . n 
D 2 277 PRO 277 277 277 PRO PRO D . n 
D 2 278 GLY 278 278 278 GLY GLY D . n 
D 2 279 CYS 279 279 279 CYS CYS D . n 
D 2 280 ILE 280 280 280 ILE ILE D . n 
D 2 281 VAL 281 281 281 VAL VAL D . n 
D 2 282 GLU 282 282 282 GLU GLU D . n 
D 2 283 SER 283 283 283 SER SER D . n 
D 2 284 GLY 284 284 284 GLY GLY D . n 
D 2 285 VAL 285 285 285 VAL VAL D . n 
D 2 286 ARG 286 286 286 ARG ARG D . n 
D 2 287 LEU 287 287 287 LEU LEU D . n 
D 2 288 SER 288 288 288 SER SER D . n 
D 2 289 ARG 289 289 289 ARG ARG D . n 
D 2 290 CYS 290 290 290 CYS CYS D . n 
D 2 291 THR 291 291 291 THR THR D . n 
D 2 292 VAL 292 292 292 VAL VAL D . n 
D 2 293 MET 293 293 293 MET MET D . n 
D 2 294 ARG 294 294 294 ARG ARG D . n 
D 2 295 GLY 295 295 295 GLY GLY D . n 
D 2 296 VAL 296 296 296 VAL VAL D . n 
D 2 297 ARG 297 297 297 ARG ARG D . n 
D 2 298 ILE 298 298 298 ILE ILE D . n 
D 2 299 LYS 299 299 299 LYS LYS D . n 
D 2 300 LYS 300 300 300 LYS LYS D . n 
D 2 301 HIS 301 301 301 HIS HIS D . n 
D 2 302 ALA 302 302 302 ALA ALA D . n 
D 2 303 CYS 303 303 303 CYS CYS D . n 
D 2 304 ILE 304 304 304 ILE ILE D . n 
D 2 305 SER 305 305 305 SER SER D . n 
D 2 306 SER 306 306 306 SER SER D . n 
D 2 307 SER 307 307 307 SER SER D . n 
D 2 308 ILE 308 308 308 ILE ILE D . n 
D 2 309 ILE 309 309 309 ILE ILE D . n 
D 2 310 GLY 310 310 310 GLY GLY D . n 
D 2 311 TRP 311 311 311 TRP TRP D . n 
D 2 312 HIS 312 312 312 HIS HIS D . n 
D 2 313 SER 313 313 313 SER SER D . n 
D 2 314 THR 314 314 314 THR THR D . n 
D 2 315 VAL 315 315 315 VAL VAL D . n 
D 2 316 GLY 316 316 316 GLY GLY D . n 
D 2 317 GLN 317 317 317 GLN GLN D . n 
D 2 318 TRP 318 318 318 TRP TRP D . n 
D 2 319 ALA 319 319 319 ALA ALA D . n 
D 2 320 ARG 320 320 320 ARG ARG D . n 
D 2 321 ILE 321 321 321 ILE ILE D . n 
D 2 322 GLU 322 322 322 GLU GLU D . n 
D 2 323 ASN 323 323 323 ASN ASN D . n 
D 2 324 MET 324 324 324 MET MET D . n 
D 2 325 THR 325 325 325 THR THR D . n 
D 2 326 ILE 326 326 326 ILE ILE D . n 
D 2 327 LEU 327 327 327 LEU LEU D . n 
D 2 328 GLY 328 328 328 GLY GLY D . n 
D 2 329 GLU 329 329 329 GLU GLU D . n 
D 2 330 ASP 330 330 330 ASP ASP D . n 
D 2 331 VAL 331 331 331 VAL VAL D . n 
D 2 332 HIS 332 332 332 HIS HIS D . n 
D 2 333 VAL 333 333 333 VAL VAL D . n 
D 2 334 SER 334 334 334 SER SER D . n 
D 2 335 ASP 335 335 335 ASP ASP D . n 
D 2 336 GLU 336 336 336 GLU GLU D . n 
D 2 337 ILE 337 337 337 ILE ILE D . n 
D 2 338 TYR 338 338 338 TYR TYR D . n 
D 2 339 SER 339 339 339 SER SER D . n 
D 2 340 ASN 340 340 340 ASN ASN D . n 
D 2 341 GLY 341 341 341 GLY GLY D . n 
D 2 342 GLY 342 342 342 GLY GLY D . n 
D 2 343 VAL 343 343 343 VAL VAL D . n 
D 2 344 VAL 344 344 344 VAL VAL D . n 
D 2 345 LEU 345 345 345 LEU LEU D . n 
D 2 346 PRO 346 346 346 PRO PRO D . n 
D 2 347 HIS 347 347 347 HIS HIS D . n 
D 2 348 LYS 348 348 348 LYS LYS D . n 
D 2 349 GLU 349 349 349 GLU GLU D . n 
D 2 350 ILE 350 350 350 ILE ILE D . n 
D 2 351 LYS 351 351 351 LYS LYS D . n 
D 2 352 SER 352 352 352 SER SER D . n 
D 2 353 ASN 353 353 353 ASN ASN D . n 
D 2 354 ILE 354 354 354 ILE ILE D . n 
D 2 355 LEU 355 355 355 LEU LEU D . n 
D 2 356 LYS 356 356 356 LYS LYS D . n 
D 2 357 PRO 357 357 357 PRO PRO D . n 
D 2 358 GLU 358 358 358 GLU GLU D . n 
D 2 359 ILE 359 359 359 ILE ILE D . n 
D 2 360 VAL 360 360 360 VAL VAL D . n 
D 2 361 MET 361 361 361 MET MET D . n 
E 2 1   MET 1   1   1   MET MET E . n 
E 2 2   LYS 2   2   2   LYS LYS E . n 
E 2 3   ALA 3   3   3   ALA ALA E . n 
E 2 4   LEU 4   4   4   LEU LEU E . n 
E 2 5   ILE 5   5   5   ILE ILE E . n 
E 2 6   LEU 6   6   6   LEU LEU E . n 
E 2 7   VAL 7   7   7   VAL VAL E . n 
E 2 8   GLY 8   8   8   GLY GLY E . n 
E 2 9   GLY 9   9   9   GLY GLY E . n 
E 2 10  PHE 10  10  10  PHE PHE E . n 
E 2 11  GLY 11  11  11  GLY GLY E . n 
E 2 12  THR 12  12  12  THR THR E . n 
E 2 13  ARG 13  13  13  ARG ARG E . n 
E 2 14  LEU 14  14  14  LEU LEU E . n 
E 2 15  ARG 15  15  15  ARG ARG E . n 
E 2 16  PRO 16  16  16  PRO PRO E . n 
E 2 17  LEU 17  17  17  LEU LEU E . n 
E 2 18  THR 18  18  18  THR THR E . n 
E 2 19  LEU 19  19  19  LEU LEU E . n 
E 2 20  SER 20  20  20  SER SER E . n 
E 2 21  PHE 21  21  21  PHE PHE E . n 
E 2 22  PRO 22  22  22  PRO PRO E . n 
E 2 23  LYS 23  23  23  LYS LYS E . n 
E 2 24  PRO 24  24  24  PRO PRO E . n 
E 2 25  LEU 25  25  25  LEU LEU E . n 
E 2 26  VAL 26  26  26  VAL VAL E . n 
E 2 27  ASP 27  27  27  ASP ASP E . n 
E 2 28  PHE 28  28  28  PHE PHE E . n 
E 2 29  ALA 29  29  29  ALA ALA E . n 
E 2 30  ASN 30  30  30  ASN ASN E . n 
E 2 31  LYS 31  31  31  LYS LYS E . n 
E 2 32  PRO 32  32  32  PRO PRO E . n 
E 2 33  MET 33  33  33  MET MET E . n 
E 2 34  ILE 34  34  34  ILE ILE E . n 
E 2 35  LEU 35  35  35  LEU LEU E . n 
E 2 36  HIS 36  36  36  HIS HIS E . n 
E 2 37  GLN 37  37  37  GLN GLN E . n 
E 2 38  ILE 38  38  38  ILE ILE E . n 
E 2 39  GLU 39  39  39  GLU GLU E . n 
E 2 40  ALA 40  40  40  ALA ALA E . n 
E 2 41  LEU 41  41  41  LEU LEU E . n 
E 2 42  LYS 42  42  42  LYS LYS E . n 
E 2 43  ALA 43  43  43  ALA ALA E . n 
E 2 44  VAL 44  44  44  VAL VAL E . n 
E 2 45  GLY 45  45  45  GLY GLY E . n 
E 2 46  VAL 46  46  46  VAL VAL E . n 
E 2 47  ASP 47  47  47  ASP ASP E . n 
E 2 48  GLU 48  48  48  GLU GLU E . n 
E 2 49  VAL 49  49  49  VAL VAL E . n 
E 2 50  VAL 50  50  50  VAL VAL E . n 
E 2 51  LEU 51  51  51  LEU LEU E . n 
E 2 52  ALA 52  52  52  ALA ALA E . n 
E 2 53  ILE 53  53  53  ILE ILE E . n 
E 2 54  ASN 54  54  54  ASN ASN E . n 
E 2 55  TYR 55  55  55  TYR TYR E . n 
E 2 56  GLN 56  56  56  GLN GLN E . n 
E 2 57  PRO 57  57  57  PRO PRO E . n 
E 2 58  GLU 58  58  58  GLU GLU E . n 
E 2 59  VAL 59  59  59  VAL VAL E . n 
E 2 60  MET 60  60  60  MET MET E . n 
E 2 61  LEU 61  61  61  LEU LEU E . n 
E 2 62  ASN 62  62  62  ASN ASN E . n 
E 2 63  PHE 63  63  63  PHE PHE E . n 
E 2 64  LEU 64  64  64  LEU LEU E . n 
E 2 65  LYS 65  65  65  LYS LYS E . n 
E 2 66  ASP 66  66  66  ASP ASP E . n 
E 2 67  PHE 67  67  67  PHE PHE E . n 
E 2 68  GLU 68  68  68  GLU GLU E . n 
E 2 69  THR 69  69  69  THR THR E . n 
E 2 70  LYS 70  70  70  LYS LYS E . n 
E 2 71  LEU 71  71  71  LEU LEU E . n 
E 2 72  GLU 72  72  72  GLU GLU E . n 
E 2 73  ILE 73  73  73  ILE ILE E . n 
E 2 74  LYS 74  74  74  LYS LYS E . n 
E 2 75  ILE 75  75  75  ILE ILE E . n 
E 2 76  THR 76  76  76  THR THR E . n 
E 2 77  CYS 77  77  77  CYS CYS E . n 
E 2 78  SER 78  78  78  SER SER E . n 
E 2 79  GLN 79  79  79  GLN GLN E . n 
E 2 80  GLU 80  80  80  GLU GLU E . n 
E 2 81  THR 81  81  81  THR THR E . n 
E 2 82  GLU 82  82  82  GLU GLU E . n 
E 2 83  PRO 83  83  83  PRO PRO E . n 
E 2 84  LEU 84  84  84  LEU LEU E . n 
E 2 85  GLY 85  85  85  GLY GLY E . n 
E 2 86  THR 86  86  86  THR THR E . n 
E 2 87  ALA 87  87  87  ALA ALA E . n 
E 2 88  GLY 88  88  88  GLY GLY E . n 
E 2 89  PRO 89  89  89  PRO PRO E . n 
E 2 90  LEU 90  90  90  LEU LEU E . n 
E 2 91  ALA 91  91  91  ALA ALA E . n 
E 2 92  LEU 92  92  92  LEU LEU E . n 
E 2 93  ALA 93  93  93  ALA ALA E . n 
E 2 94  ARG 94  94  94  ARG ARG E . n 
E 2 95  ASP 95  95  95  ASP ASP E . n 
E 2 96  LYS 96  96  96  LYS LYS E . n 
E 2 97  LEU 97  97  97  LEU LEU E . n 
E 2 98  LEU 98  98  98  LEU LEU E . n 
E 2 99  ASP 99  99  99  ASP ASP E . n 
E 2 100 GLY 100 100 100 GLY GLY E . n 
E 2 101 SER 101 101 101 SER SER E . n 
E 2 102 GLY 102 102 102 GLY GLY E . n 
E 2 103 GLU 103 103 103 GLU GLU E . n 
E 2 104 PRO 104 104 104 PRO PRO E . n 
E 2 105 PHE 105 105 105 PHE PHE E . n 
E 2 106 PHE 106 106 106 PHE PHE E . n 
E 2 107 VAL 107 107 107 VAL VAL E . n 
E 2 108 LEU 108 108 108 LEU LEU E . n 
E 2 109 ASN 109 109 109 ASN ASN E . n 
E 2 110 SER 110 110 110 SER SER E . n 
E 2 111 ASP 111 111 111 ASP ASP E . n 
E 2 112 VAL 112 112 112 VAL VAL E . n 
E 2 113 ILE 113 113 113 ILE ILE E . n 
E 2 114 SER 114 114 114 SER SER E . n 
E 2 115 GLU 115 115 115 GLU GLU E . n 
E 2 116 TYR 116 116 116 TYR TYR E . n 
E 2 117 PRO 117 117 117 PRO PRO E . n 
E 2 118 LEU 118 118 118 LEU LEU E . n 
E 2 119 LYS 119 119 119 LYS LYS E . n 
E 2 120 GLU 120 120 120 GLU GLU E . n 
E 2 121 MET 121 121 121 MET MET E . n 
E 2 122 LEU 122 122 122 LEU LEU E . n 
E 2 123 GLU 123 123 123 GLU GLU E . n 
E 2 124 PHE 124 124 124 PHE PHE E . n 
E 2 125 HIS 125 125 125 HIS HIS E . n 
E 2 126 LYS 126 126 126 LYS LYS E . n 
E 2 127 SER 127 127 127 SER SER E . n 
E 2 128 HIS 128 128 128 HIS HIS E . n 
E 2 129 GLY 129 129 129 GLY GLY E . n 
E 2 130 GLY 130 130 130 GLY GLY E . n 
E 2 131 GLU 131 131 131 GLU GLU E . n 
E 2 132 ALA 132 132 132 ALA ALA E . n 
E 2 133 SER 133 133 133 SER SER E . n 
E 2 134 ILE 134 134 134 ILE ILE E . n 
E 2 135 MET 135 135 135 MET MET E . n 
E 2 136 VAL 136 136 136 VAL VAL E . n 
E 2 137 THR 137 137 137 THR THR E . n 
E 2 138 LYS 138 138 138 LYS LYS E . n 
E 2 139 VAL 139 139 139 VAL VAL E . n 
E 2 140 ASP 140 140 140 ASP ASP E . n 
E 2 141 GLU 141 141 141 GLU GLU E . n 
E 2 142 PRO 142 142 142 PRO PRO E . n 
E 2 143 SER 143 143 143 SER SER E . n 
E 2 144 LYS 144 144 144 LYS LYS E . n 
E 2 145 TYR 145 145 145 TYR TYR E . n 
E 2 146 GLY 146 146 146 GLY GLY E . n 
E 2 147 VAL 147 147 147 VAL VAL E . n 
E 2 148 VAL 148 148 148 VAL VAL E . n 
E 2 149 VAL 149 149 149 VAL VAL E . n 
E 2 150 MET 150 150 150 MET MET E . n 
E 2 151 GLU 151 151 151 GLU GLU E . n 
E 2 152 GLU 152 152 152 GLU GLU E . n 
E 2 153 SER 153 153 153 SER SER E . n 
E 2 154 THR 154 154 154 THR THR E . n 
E 2 155 GLY 155 155 155 GLY GLY E . n 
E 2 156 ARG 156 156 156 ARG ARG E . n 
E 2 157 VAL 157 157 157 VAL VAL E . n 
E 2 158 GLU 158 158 158 GLU GLU E . n 
E 2 159 LYS 159 159 159 LYS LYS E . n 
E 2 160 PHE 160 160 160 PHE PHE E . n 
E 2 161 VAL 161 161 161 VAL VAL E . n 
E 2 162 GLU 162 162 162 GLU GLU E . n 
E 2 163 LYS 163 163 163 LYS LYS E . n 
E 2 164 PRO 164 164 164 PRO PRO E . n 
E 2 165 LYS 165 165 165 LYS LYS E . n 
E 2 166 LEU 166 166 166 LEU LEU E . n 
E 2 167 TYR 167 167 167 TYR TYR E . n 
E 2 168 VAL 168 168 168 VAL VAL E . n 
E 2 169 GLY 169 169 169 GLY GLY E . n 
E 2 170 ASN 170 170 170 ASN ASN E . n 
E 2 171 LYS 171 171 171 LYS LYS E . n 
E 2 172 ILE 172 172 172 ILE ILE E . n 
E 2 173 ASN 173 173 173 ASN ASN E . n 
E 2 174 ALA 174 174 174 ALA ALA E . n 
E 2 175 GLY 175 175 175 GLY GLY E . n 
E 2 176 ILE 176 176 176 ILE ILE E . n 
E 2 177 TYR 177 177 177 TYR TYR E . n 
E 2 178 LEU 178 178 178 LEU LEU E . n 
E 2 179 LEU 179 179 179 LEU LEU E . n 
E 2 180 ASN 180 180 180 ASN ASN E . n 
E 2 181 PRO 181 181 181 PRO PRO E . n 
E 2 182 SER 182 182 182 SER SER E . n 
E 2 183 VAL 183 183 183 VAL VAL E . n 
E 2 184 LEU 184 184 184 LEU LEU E . n 
E 2 185 ASP 185 185 185 ASP ASP E . n 
E 2 186 LYS 186 186 186 LYS LYS E . n 
E 2 187 ILE 187 187 187 ILE ILE E . n 
E 2 188 GLU 188 188 188 GLU GLU E . n 
E 2 189 LEU 189 189 189 LEU LEU E . n 
E 2 190 ARG 190 190 190 ARG ARG E . n 
E 2 191 PRO 191 191 191 PRO PRO E . n 
E 2 192 THR 192 192 192 THR THR E . n 
E 2 193 SER 193 193 193 SER SER E . n 
E 2 194 ILE 194 194 194 ILE ILE E . n 
E 2 195 GLU 195 195 195 GLU GLU E . n 
E 2 196 LYS 196 196 196 LYS LYS E . n 
E 2 197 GLU 197 197 197 GLU GLU E . n 
E 2 198 THR 198 198 198 THR THR E . n 
E 2 199 PHE 199 199 199 PHE PHE E . n 
E 2 200 PRO 200 200 200 PRO PRO E . n 
E 2 201 LYS 201 201 201 LYS LYS E . n 
E 2 202 ILE 202 202 202 ILE ILE E . n 
E 2 203 ALA 203 203 203 ALA ALA E . n 
E 2 204 ALA 204 204 204 ALA ALA E . n 
E 2 205 ALA 205 205 205 ALA ALA E . n 
E 2 206 GLN 206 206 206 GLN GLN E . n 
E 2 207 GLY 207 207 207 GLY GLY E . n 
E 2 208 LEU 208 208 208 LEU LEU E . n 
E 2 209 TYR 209 209 209 TYR TYR E . n 
E 2 210 ALA 210 210 ?   ?   ?   E . n 
E 2 211 MET 211 211 ?   ?   ?   E . n 
E 2 212 VAL 212 212 212 VAL VAL E . n 
E 2 213 LEU 213 213 213 LEU LEU E . n 
E 2 214 PRO 214 214 214 PRO PRO E . n 
E 2 215 GLY 215 215 215 GLY GLY E . n 
E 2 216 PHE 216 216 216 PHE PHE E . n 
E 2 217 TRP 217 217 217 TRP TRP E . n 
E 2 218 MET 218 218 218 MET MET E . n 
E 2 219 ASP 219 219 219 ASP ASP E . n 
E 2 220 ILE 220 220 220 ILE ILE E . n 
E 2 221 GLY 221 221 221 GLY GLY E . n 
E 2 222 GLN 222 222 222 GLN GLN E . n 
E 2 223 PRO 223 223 223 PRO PRO E . n 
E 2 224 ARG 224 224 224 ARG ARG E . n 
E 2 225 ASP 225 225 225 ASP ASP E . n 
E 2 226 TYR 226 226 226 TYR TYR E . n 
E 2 227 ILE 227 227 227 ILE ILE E . n 
E 2 228 THR 228 228 228 THR THR E . n 
E 2 229 GLY 229 229 229 GLY GLY E . n 
E 2 230 LEU 230 230 230 LEU LEU E . n 
E 2 231 ARG 231 231 231 ARG ARG E . n 
E 2 232 LEU 232 232 232 LEU LEU E . n 
E 2 233 TYR 233 233 233 TYR TYR E . n 
E 2 234 LEU 234 234 234 LEU LEU E . n 
E 2 235 ASP 235 235 235 ASP ASP E . n 
E 2 236 SER 236 236 236 SER SER E . n 
E 2 237 LEU 237 237 237 LEU LEU E . n 
E 2 238 ARG 238 238 238 ARG ARG E . n 
E 2 239 LYS 239 239 239 LYS LYS E . n 
E 2 240 LYS 240 240 240 LYS LYS E . n 
E 2 241 SER 241 241 241 SER SER E . n 
E 2 242 PRO 242 242 242 PRO PRO E . n 
E 2 243 ALA 243 243 243 ALA ALA E . n 
E 2 244 LYS 244 244 244 LYS LYS E . n 
E 2 245 LEU 245 245 245 LEU LEU E . n 
E 2 246 THR 246 246 246 THR THR E . n 
E 2 247 SER 247 247 247 SER SER E . n 
E 2 248 GLY 248 248 248 GLY GLY E . n 
E 2 249 PRO 249 249 249 PRO PRO E . n 
E 2 250 HIS 250 250 250 HIS HIS E . n 
E 2 251 ILE 251 251 251 ILE ILE E . n 
E 2 252 VAL 252 252 252 VAL VAL E . n 
E 2 253 GLY 253 253 253 GLY GLY E . n 
E 2 254 ASN 254 254 254 ASN ASN E . n 
E 2 255 VAL 255 255 255 VAL VAL E . n 
E 2 256 LEU 256 256 256 LEU LEU E . n 
E 2 257 VAL 257 257 257 VAL VAL E . n 
E 2 258 ASP 258 258 258 ASP ASP E . n 
E 2 259 GLU 259 259 259 GLU GLU E . n 
E 2 260 THR 260 260 260 THR THR E . n 
E 2 261 ALA 261 261 261 ALA ALA E . n 
E 2 262 THR 262 262 262 THR THR E . n 
E 2 263 ILE 263 263 263 ILE ILE E . n 
E 2 264 GLY 264 264 264 GLY GLY E . n 
E 2 265 GLU 265 265 265 GLU GLU E . n 
E 2 266 GLY 266 266 266 GLY GLY E . n 
E 2 267 CYS 267 267 267 CYS CYS E . n 
E 2 268 LEU 268 268 268 LEU LEU E . n 
E 2 269 ILE 269 269 269 ILE ILE E . n 
E 2 270 GLY 270 270 270 GLY GLY E . n 
E 2 271 PRO 271 271 271 PRO PRO E . n 
E 2 272 ASP 272 272 272 ASP ASP E . n 
E 2 273 VAL 273 273 273 VAL VAL E . n 
E 2 274 ALA 274 274 274 ALA ALA E . n 
E 2 275 ILE 275 275 275 ILE ILE E . n 
E 2 276 GLY 276 276 276 GLY GLY E . n 
E 2 277 PRO 277 277 277 PRO PRO E . n 
E 2 278 GLY 278 278 278 GLY GLY E . n 
E 2 279 CYS 279 279 279 CYS CYS E . n 
E 2 280 ILE 280 280 280 ILE ILE E . n 
E 2 281 VAL 281 281 281 VAL VAL E . n 
E 2 282 GLU 282 282 282 GLU GLU E . n 
E 2 283 SER 283 283 283 SER SER E . n 
E 2 284 GLY 284 284 284 GLY GLY E . n 
E 2 285 VAL 285 285 285 VAL VAL E . n 
E 2 286 ARG 286 286 286 ARG ARG E . n 
E 2 287 LEU 287 287 287 LEU LEU E . n 
E 2 288 SER 288 288 288 SER SER E . n 
E 2 289 ARG 289 289 289 ARG ARG E . n 
E 2 290 CYS 290 290 290 CYS CYS E . n 
E 2 291 THR 291 291 291 THR THR E . n 
E 2 292 VAL 292 292 292 VAL VAL E . n 
E 2 293 MET 293 293 293 MET MET E . n 
E 2 294 ARG 294 294 294 ARG ARG E . n 
E 2 295 GLY 295 295 295 GLY GLY E . n 
E 2 296 VAL 296 296 296 VAL VAL E . n 
E 2 297 ARG 297 297 297 ARG ARG E . n 
E 2 298 ILE 298 298 298 ILE ILE E . n 
E 2 299 LYS 299 299 299 LYS LYS E . n 
E 2 300 LYS 300 300 300 LYS LYS E . n 
E 2 301 HIS 301 301 301 HIS HIS E . n 
E 2 302 ALA 302 302 302 ALA ALA E . n 
E 2 303 CYS 303 303 303 CYS CYS E . n 
E 2 304 ILE 304 304 304 ILE ILE E . n 
E 2 305 SER 305 305 305 SER SER E . n 
E 2 306 SER 306 306 306 SER SER E . n 
E 2 307 SER 307 307 307 SER SER E . n 
E 2 308 ILE 308 308 308 ILE ILE E . n 
E 2 309 ILE 309 309 309 ILE ILE E . n 
E 2 310 GLY 310 310 310 GLY GLY E . n 
E 2 311 TRP 311 311 311 TRP TRP E . n 
E 2 312 HIS 312 312 312 HIS HIS E . n 
E 2 313 SER 313 313 313 SER SER E . n 
E 2 314 THR 314 314 314 THR THR E . n 
E 2 315 VAL 315 315 315 VAL VAL E . n 
E 2 316 GLY 316 316 316 GLY GLY E . n 
E 2 317 GLN 317 317 317 GLN GLN E . n 
E 2 318 TRP 318 318 318 TRP TRP E . n 
E 2 319 ALA 319 319 319 ALA ALA E . n 
E 2 320 ARG 320 320 320 ARG ARG E . n 
E 2 321 ILE 321 321 321 ILE ILE E . n 
E 2 322 GLU 322 322 322 GLU GLU E . n 
E 2 323 ASN 323 323 323 ASN ASN E . n 
E 2 324 MET 324 324 324 MET MET E . n 
E 2 325 THR 325 325 325 THR THR E . n 
E 2 326 ILE 326 326 326 ILE ILE E . n 
E 2 327 LEU 327 327 327 LEU LEU E . n 
E 2 328 GLY 328 328 328 GLY GLY E . n 
E 2 329 GLU 329 329 329 GLU GLU E . n 
E 2 330 ASP 330 330 330 ASP ASP E . n 
E 2 331 VAL 331 331 331 VAL VAL E . n 
E 2 332 HIS 332 332 332 HIS HIS E . n 
E 2 333 VAL 333 333 333 VAL VAL E . n 
E 2 334 SER 334 334 334 SER SER E . n 
E 2 335 ASP 335 335 335 ASP ASP E . n 
E 2 336 GLU 336 336 336 GLU GLU E . n 
E 2 337 ILE 337 337 337 ILE ILE E . n 
E 2 338 TYR 338 338 338 TYR TYR E . n 
E 2 339 SER 339 339 339 SER SER E . n 
E 2 340 ASN 340 340 340 ASN ASN E . n 
E 2 341 GLY 341 341 341 GLY GLY E . n 
E 2 342 GLY 342 342 342 GLY GLY E . n 
E 2 343 VAL 343 343 343 VAL VAL E . n 
E 2 344 VAL 344 344 344 VAL VAL E . n 
E 2 345 LEU 345 345 345 LEU LEU E . n 
E 2 346 PRO 346 346 346 PRO PRO E . n 
E 2 347 HIS 347 347 347 HIS HIS E . n 
E 2 348 LYS 348 348 348 LYS LYS E . n 
E 2 349 GLU 349 349 349 GLU GLU E . n 
E 2 350 ILE 350 350 350 ILE ILE E . n 
E 2 351 LYS 351 351 351 LYS LYS E . n 
E 2 352 SER 352 352 352 SER SER E . n 
E 2 353 ASN 353 353 353 ASN ASN E . n 
E 2 354 ILE 354 354 354 ILE ILE E . n 
E 2 355 LEU 355 355 355 LEU LEU E . n 
E 2 356 LYS 356 356 356 LYS LYS E . n 
E 2 357 PRO 357 357 357 PRO PRO E . n 
E 2 358 GLU 358 358 358 GLU GLU E . n 
E 2 359 ILE 359 359 359 ILE ILE E . n 
E 2 360 VAL 360 360 360 VAL VAL E . n 
E 2 361 MET 361 361 361 MET MET E . n 
F 2 1   MET 1   1   1   MET MET F . n 
F 2 2   LYS 2   2   2   LYS LYS F . n 
F 2 3   ALA 3   3   3   ALA ALA F . n 
F 2 4   LEU 4   4   4   LEU LEU F . n 
F 2 5   ILE 5   5   5   ILE ILE F . n 
F 2 6   LEU 6   6   6   LEU LEU F . n 
F 2 7   VAL 7   7   7   VAL VAL F . n 
F 2 8   GLY 8   8   8   GLY GLY F . n 
F 2 9   GLY 9   9   9   GLY GLY F . n 
F 2 10  PHE 10  10  10  PHE PHE F . n 
F 2 11  GLY 11  11  11  GLY GLY F . n 
F 2 12  THR 12  12  12  THR THR F . n 
F 2 13  ARG 13  13  13  ARG ARG F . n 
F 2 14  LEU 14  14  14  LEU LEU F . n 
F 2 15  ARG 15  15  15  ARG ARG F . n 
F 2 16  PRO 16  16  16  PRO PRO F . n 
F 2 17  LEU 17  17  17  LEU LEU F . n 
F 2 18  THR 18  18  18  THR THR F . n 
F 2 19  LEU 19  19  19  LEU LEU F . n 
F 2 20  SER 20  20  20  SER SER F . n 
F 2 21  PHE 21  21  21  PHE PHE F . n 
F 2 22  PRO 22  22  22  PRO PRO F . n 
F 2 23  LYS 23  23  23  LYS LYS F . n 
F 2 24  PRO 24  24  24  PRO PRO F . n 
F 2 25  LEU 25  25  25  LEU LEU F . n 
F 2 26  VAL 26  26  26  VAL VAL F . n 
F 2 27  ASP 27  27  27  ASP ASP F . n 
F 2 28  PHE 28  28  28  PHE PHE F . n 
F 2 29  ALA 29  29  29  ALA ALA F . n 
F 2 30  ASN 30  30  30  ASN ASN F . n 
F 2 31  LYS 31  31  31  LYS LYS F . n 
F 2 32  PRO 32  32  32  PRO PRO F . n 
F 2 33  MET 33  33  33  MET MET F . n 
F 2 34  ILE 34  34  34  ILE ILE F . n 
F 2 35  LEU 35  35  35  LEU LEU F . n 
F 2 36  HIS 36  36  36  HIS HIS F . n 
F 2 37  GLN 37  37  37  GLN GLN F . n 
F 2 38  ILE 38  38  38  ILE ILE F . n 
F 2 39  GLU 39  39  39  GLU GLU F . n 
F 2 40  ALA 40  40  40  ALA ALA F . n 
F 2 41  LEU 41  41  41  LEU LEU F . n 
F 2 42  LYS 42  42  42  LYS LYS F . n 
F 2 43  ALA 43  43  43  ALA ALA F . n 
F 2 44  VAL 44  44  44  VAL VAL F . n 
F 2 45  GLY 45  45  45  GLY GLY F . n 
F 2 46  VAL 46  46  46  VAL VAL F . n 
F 2 47  ASP 47  47  47  ASP ASP F . n 
F 2 48  GLU 48  48  48  GLU GLU F . n 
F 2 49  VAL 49  49  49  VAL VAL F . n 
F 2 50  VAL 50  50  50  VAL VAL F . n 
F 2 51  LEU 51  51  51  LEU LEU F . n 
F 2 52  ALA 52  52  52  ALA ALA F . n 
F 2 53  ILE 53  53  53  ILE ILE F . n 
F 2 54  ASN 54  54  54  ASN ASN F . n 
F 2 55  TYR 55  55  55  TYR TYR F . n 
F 2 56  GLN 56  56  56  GLN GLN F . n 
F 2 57  PRO 57  57  57  PRO PRO F . n 
F 2 58  GLU 58  58  58  GLU GLU F . n 
F 2 59  VAL 59  59  59  VAL VAL F . n 
F 2 60  MET 60  60  60  MET MET F . n 
F 2 61  LEU 61  61  61  LEU LEU F . n 
F 2 62  ASN 62  62  62  ASN ASN F . n 
F 2 63  PHE 63  63  63  PHE PHE F . n 
F 2 64  LEU 64  64  64  LEU LEU F . n 
F 2 65  LYS 65  65  65  LYS LYS F . n 
F 2 66  ASP 66  66  66  ASP ASP F . n 
F 2 67  PHE 67  67  67  PHE PHE F . n 
F 2 68  GLU 68  68  68  GLU GLU F . n 
F 2 69  THR 69  69  69  THR THR F . n 
F 2 70  LYS 70  70  70  LYS LYS F . n 
F 2 71  LEU 71  71  71  LEU LEU F . n 
F 2 72  GLU 72  72  72  GLU GLU F . n 
F 2 73  ILE 73  73  73  ILE ILE F . n 
F 2 74  LYS 74  74  74  LYS LYS F . n 
F 2 75  ILE 75  75  75  ILE ILE F . n 
F 2 76  THR 76  76  76  THR THR F . n 
F 2 77  CYS 77  77  77  CYS CYS F . n 
F 2 78  SER 78  78  78  SER SER F . n 
F 2 79  GLN 79  79  79  GLN GLN F . n 
F 2 80  GLU 80  80  80  GLU GLU F . n 
F 2 81  THR 81  81  81  THR THR F . n 
F 2 82  GLU 82  82  82  GLU GLU F . n 
F 2 83  PRO 83  83  83  PRO PRO F . n 
F 2 84  LEU 84  84  84  LEU LEU F . n 
F 2 85  GLY 85  85  85  GLY GLY F . n 
F 2 86  THR 86  86  86  THR THR F . n 
F 2 87  ALA 87  87  87  ALA ALA F . n 
F 2 88  GLY 88  88  88  GLY GLY F . n 
F 2 89  PRO 89  89  89  PRO PRO F . n 
F 2 90  LEU 90  90  90  LEU LEU F . n 
F 2 91  ALA 91  91  91  ALA ALA F . n 
F 2 92  LEU 92  92  92  LEU LEU F . n 
F 2 93  ALA 93  93  93  ALA ALA F . n 
F 2 94  ARG 94  94  94  ARG ARG F . n 
F 2 95  ASP 95  95  95  ASP ASP F . n 
F 2 96  LYS 96  96  96  LYS LYS F . n 
F 2 97  LEU 97  97  97  LEU LEU F . n 
F 2 98  LEU 98  98  98  LEU LEU F . n 
F 2 99  ASP 99  99  99  ASP ASP F . n 
F 2 100 GLY 100 100 100 GLY GLY F . n 
F 2 101 SER 101 101 101 SER SER F . n 
F 2 102 GLY 102 102 102 GLY GLY F . n 
F 2 103 GLU 103 103 103 GLU GLU F . n 
F 2 104 PRO 104 104 104 PRO PRO F . n 
F 2 105 PHE 105 105 105 PHE PHE F . n 
F 2 106 PHE 106 106 106 PHE PHE F . n 
F 2 107 VAL 107 107 107 VAL VAL F . n 
F 2 108 LEU 108 108 108 LEU LEU F . n 
F 2 109 ASN 109 109 109 ASN ASN F . n 
F 2 110 SER 110 110 110 SER SER F . n 
F 2 111 ASP 111 111 111 ASP ASP F . n 
F 2 112 VAL 112 112 112 VAL VAL F . n 
F 2 113 ILE 113 113 113 ILE ILE F . n 
F 2 114 SER 114 114 114 SER SER F . n 
F 2 115 GLU 115 115 115 GLU GLU F . n 
F 2 116 TYR 116 116 116 TYR TYR F . n 
F 2 117 PRO 117 117 117 PRO PRO F . n 
F 2 118 LEU 118 118 118 LEU LEU F . n 
F 2 119 LYS 119 119 119 LYS LYS F . n 
F 2 120 GLU 120 120 120 GLU GLU F . n 
F 2 121 MET 121 121 121 MET MET F . n 
F 2 122 LEU 122 122 122 LEU LEU F . n 
F 2 123 GLU 123 123 123 GLU GLU F . n 
F 2 124 PHE 124 124 124 PHE PHE F . n 
F 2 125 HIS 125 125 125 HIS HIS F . n 
F 2 126 LYS 126 126 126 LYS LYS F . n 
F 2 127 SER 127 127 127 SER SER F . n 
F 2 128 HIS 128 128 128 HIS HIS F . n 
F 2 129 GLY 129 129 129 GLY GLY F . n 
F 2 130 GLY 130 130 130 GLY GLY F . n 
F 2 131 GLU 131 131 131 GLU GLU F . n 
F 2 132 ALA 132 132 132 ALA ALA F . n 
F 2 133 SER 133 133 133 SER SER F . n 
F 2 134 ILE 134 134 134 ILE ILE F . n 
F 2 135 MET 135 135 135 MET MET F . n 
F 2 136 VAL 136 136 136 VAL VAL F . n 
F 2 137 THR 137 137 137 THR THR F . n 
F 2 138 LYS 138 138 138 LYS LYS F . n 
F 2 139 VAL 139 139 139 VAL VAL F . n 
F 2 140 ASP 140 140 140 ASP ASP F . n 
F 2 141 GLU 141 141 141 GLU GLU F . n 
F 2 142 PRO 142 142 142 PRO PRO F . n 
F 2 143 SER 143 143 143 SER SER F . n 
F 2 144 LYS 144 144 144 LYS LYS F . n 
F 2 145 TYR 145 145 145 TYR TYR F . n 
F 2 146 GLY 146 146 146 GLY GLY F . n 
F 2 147 VAL 147 147 147 VAL VAL F . n 
F 2 148 VAL 148 148 148 VAL VAL F . n 
F 2 149 VAL 149 149 149 VAL VAL F . n 
F 2 150 MET 150 150 150 MET MET F . n 
F 2 151 GLU 151 151 ?   ?   ?   F . n 
F 2 152 GLU 152 152 ?   ?   ?   F . n 
F 2 153 SER 153 153 ?   ?   ?   F . n 
F 2 154 THR 154 154 ?   ?   ?   F . n 
F 2 155 GLY 155 155 ?   ?   ?   F . n 
F 2 156 ARG 156 156 156 ARG ARG F . n 
F 2 157 VAL 157 157 157 VAL VAL F . n 
F 2 158 GLU 158 158 158 GLU GLU F . n 
F 2 159 LYS 159 159 159 LYS LYS F . n 
F 2 160 PHE 160 160 160 PHE PHE F . n 
F 2 161 VAL 161 161 161 VAL VAL F . n 
F 2 162 GLU 162 162 162 GLU GLU F . n 
F 2 163 LYS 163 163 163 LYS LYS F . n 
F 2 164 PRO 164 164 164 PRO PRO F . n 
F 2 165 LYS 165 165 165 LYS LYS F . n 
F 2 166 LEU 166 166 166 LEU LEU F . n 
F 2 167 TYR 167 167 167 TYR TYR F . n 
F 2 168 VAL 168 168 168 VAL VAL F . n 
F 2 169 GLY 169 169 169 GLY GLY F . n 
F 2 170 ASN 170 170 170 ASN ASN F . n 
F 2 171 LYS 171 171 171 LYS LYS F . n 
F 2 172 ILE 172 172 172 ILE ILE F . n 
F 2 173 ASN 173 173 173 ASN ASN F . n 
F 2 174 ALA 174 174 174 ALA ALA F . n 
F 2 175 GLY 175 175 175 GLY GLY F . n 
F 2 176 ILE 176 176 176 ILE ILE F . n 
F 2 177 TYR 177 177 177 TYR TYR F . n 
F 2 178 LEU 178 178 178 LEU LEU F . n 
F 2 179 LEU 179 179 179 LEU LEU F . n 
F 2 180 ASN 180 180 180 ASN ASN F . n 
F 2 181 PRO 181 181 181 PRO PRO F . n 
F 2 182 SER 182 182 182 SER SER F . n 
F 2 183 VAL 183 183 183 VAL VAL F . n 
F 2 184 LEU 184 184 184 LEU LEU F . n 
F 2 185 ASP 185 185 185 ASP ASP F . n 
F 2 186 LYS 186 186 186 LYS LYS F . n 
F 2 187 ILE 187 187 187 ILE ILE F . n 
F 2 188 GLU 188 188 188 GLU GLU F . n 
F 2 189 LEU 189 189 189 LEU LEU F . n 
F 2 190 ARG 190 190 190 ARG ARG F . n 
F 2 191 PRO 191 191 191 PRO PRO F . n 
F 2 192 THR 192 192 192 THR THR F . n 
F 2 193 SER 193 193 193 SER SER F . n 
F 2 194 ILE 194 194 194 ILE ILE F . n 
F 2 195 GLU 195 195 195 GLU GLU F . n 
F 2 196 LYS 196 196 196 LYS LYS F . n 
F 2 197 GLU 197 197 197 GLU GLU F . n 
F 2 198 THR 198 198 198 THR THR F . n 
F 2 199 PHE 199 199 199 PHE PHE F . n 
F 2 200 PRO 200 200 200 PRO PRO F . n 
F 2 201 LYS 201 201 201 LYS LYS F . n 
F 2 202 ILE 202 202 202 ILE ILE F . n 
F 2 203 ALA 203 203 203 ALA ALA F . n 
F 2 204 ALA 204 204 204 ALA ALA F . n 
F 2 205 ALA 205 205 205 ALA ALA F . n 
F 2 206 GLN 206 206 206 GLN GLN F . n 
F 2 207 GLY 207 207 207 GLY GLY F . n 
F 2 208 LEU 208 208 208 LEU LEU F . n 
F 2 209 TYR 209 209 209 TYR TYR F . n 
F 2 210 ALA 210 210 ?   ?   ?   F . n 
F 2 211 MET 211 211 211 MET MET F . n 
F 2 212 VAL 212 212 212 VAL VAL F . n 
F 2 213 LEU 213 213 213 LEU LEU F . n 
F 2 214 PRO 214 214 214 PRO PRO F . n 
F 2 215 GLY 215 215 215 GLY GLY F . n 
F 2 216 PHE 216 216 216 PHE PHE F . n 
F 2 217 TRP 217 217 217 TRP TRP F . n 
F 2 218 MET 218 218 218 MET MET F . n 
F 2 219 ASP 219 219 219 ASP ASP F . n 
F 2 220 ILE 220 220 220 ILE ILE F . n 
F 2 221 GLY 221 221 221 GLY GLY F . n 
F 2 222 GLN 222 222 222 GLN GLN F . n 
F 2 223 PRO 223 223 223 PRO PRO F . n 
F 2 224 ARG 224 224 224 ARG ARG F . n 
F 2 225 ASP 225 225 225 ASP ASP F . n 
F 2 226 TYR 226 226 226 TYR TYR F . n 
F 2 227 ILE 227 227 227 ILE ILE F . n 
F 2 228 THR 228 228 228 THR THR F . n 
F 2 229 GLY 229 229 229 GLY GLY F . n 
F 2 230 LEU 230 230 230 LEU LEU F . n 
F 2 231 ARG 231 231 231 ARG ARG F . n 
F 2 232 LEU 232 232 232 LEU LEU F . n 
F 2 233 TYR 233 233 233 TYR TYR F . n 
F 2 234 LEU 234 234 234 LEU LEU F . n 
F 2 235 ASP 235 235 235 ASP ASP F . n 
F 2 236 SER 236 236 236 SER SER F . n 
F 2 237 LEU 237 237 237 LEU LEU F . n 
F 2 238 ARG 238 238 238 ARG ARG F . n 
F 2 239 LYS 239 239 239 LYS LYS F . n 
F 2 240 LYS 240 240 240 LYS LYS F . n 
F 2 241 SER 241 241 241 SER SER F . n 
F 2 242 PRO 242 242 242 PRO PRO F . n 
F 2 243 ALA 243 243 243 ALA ALA F . n 
F 2 244 LYS 244 244 244 LYS LYS F . n 
F 2 245 LEU 245 245 245 LEU LEU F . n 
F 2 246 THR 246 246 246 THR THR F . n 
F 2 247 SER 247 247 247 SER SER F . n 
F 2 248 GLY 248 248 248 GLY GLY F . n 
F 2 249 PRO 249 249 249 PRO PRO F . n 
F 2 250 HIS 250 250 250 HIS HIS F . n 
F 2 251 ILE 251 251 251 ILE ILE F . n 
F 2 252 VAL 252 252 252 VAL VAL F . n 
F 2 253 GLY 253 253 253 GLY GLY F . n 
F 2 254 ASN 254 254 254 ASN ASN F . n 
F 2 255 VAL 255 255 255 VAL VAL F . n 
F 2 256 LEU 256 256 256 LEU LEU F . n 
F 2 257 VAL 257 257 257 VAL VAL F . n 
F 2 258 ASP 258 258 258 ASP ASP F . n 
F 2 259 GLU 259 259 259 GLU GLU F . n 
F 2 260 THR 260 260 260 THR THR F . n 
F 2 261 ALA 261 261 261 ALA ALA F . n 
F 2 262 THR 262 262 262 THR THR F . n 
F 2 263 ILE 263 263 263 ILE ILE F . n 
F 2 264 GLY 264 264 264 GLY GLY F . n 
F 2 265 GLU 265 265 265 GLU GLU F . n 
F 2 266 GLY 266 266 266 GLY GLY F . n 
F 2 267 CYS 267 267 267 CYS CYS F . n 
F 2 268 LEU 268 268 268 LEU LEU F . n 
F 2 269 ILE 269 269 269 ILE ILE F . n 
F 2 270 GLY 270 270 270 GLY GLY F . n 
F 2 271 PRO 271 271 271 PRO PRO F . n 
F 2 272 ASP 272 272 272 ASP ASP F . n 
F 2 273 VAL 273 273 273 VAL VAL F . n 
F 2 274 ALA 274 274 274 ALA ALA F . n 
F 2 275 ILE 275 275 275 ILE ILE F . n 
F 2 276 GLY 276 276 276 GLY GLY F . n 
F 2 277 PRO 277 277 277 PRO PRO F . n 
F 2 278 GLY 278 278 278 GLY GLY F . n 
F 2 279 CYS 279 279 279 CYS CYS F . n 
F 2 280 ILE 280 280 280 ILE ILE F . n 
F 2 281 VAL 281 281 281 VAL VAL F . n 
F 2 282 GLU 282 282 282 GLU GLU F . n 
F 2 283 SER 283 283 283 SER SER F . n 
F 2 284 GLY 284 284 284 GLY GLY F . n 
F 2 285 VAL 285 285 285 VAL VAL F . n 
F 2 286 ARG 286 286 286 ARG ARG F . n 
F 2 287 LEU 287 287 287 LEU LEU F . n 
F 2 288 SER 288 288 288 SER SER F . n 
F 2 289 ARG 289 289 289 ARG ARG F . n 
F 2 290 CYS 290 290 290 CYS CYS F . n 
F 2 291 THR 291 291 291 THR THR F . n 
F 2 292 VAL 292 292 292 VAL VAL F . n 
F 2 293 MET 293 293 293 MET MET F . n 
F 2 294 ARG 294 294 294 ARG ARG F . n 
F 2 295 GLY 295 295 295 GLY GLY F . n 
F 2 296 VAL 296 296 296 VAL VAL F . n 
F 2 297 ARG 297 297 297 ARG ARG F . n 
F 2 298 ILE 298 298 298 ILE ILE F . n 
F 2 299 LYS 299 299 299 LYS LYS F . n 
F 2 300 LYS 300 300 300 LYS LYS F . n 
F 2 301 HIS 301 301 301 HIS HIS F . n 
F 2 302 ALA 302 302 302 ALA ALA F . n 
F 2 303 CYS 303 303 303 CYS CYS F . n 
F 2 304 ILE 304 304 304 ILE ILE F . n 
F 2 305 SER 305 305 305 SER SER F . n 
F 2 306 SER 306 306 306 SER SER F . n 
F 2 307 SER 307 307 307 SER SER F . n 
F 2 308 ILE 308 308 308 ILE ILE F . n 
F 2 309 ILE 309 309 309 ILE ILE F . n 
F 2 310 GLY 310 310 310 GLY GLY F . n 
F 2 311 TRP 311 311 311 TRP TRP F . n 
F 2 312 HIS 312 312 312 HIS HIS F . n 
F 2 313 SER 313 313 313 SER SER F . n 
F 2 314 THR 314 314 314 THR THR F . n 
F 2 315 VAL 315 315 315 VAL VAL F . n 
F 2 316 GLY 316 316 316 GLY GLY F . n 
F 2 317 GLN 317 317 317 GLN GLN F . n 
F 2 318 TRP 318 318 318 TRP TRP F . n 
F 2 319 ALA 319 319 319 ALA ALA F . n 
F 2 320 ARG 320 320 320 ARG ARG F . n 
F 2 321 ILE 321 321 321 ILE ILE F . n 
F 2 322 GLU 322 322 322 GLU GLU F . n 
F 2 323 ASN 323 323 323 ASN ASN F . n 
F 2 324 MET 324 324 324 MET MET F . n 
F 2 325 THR 325 325 325 THR THR F . n 
F 2 326 ILE 326 326 326 ILE ILE F . n 
F 2 327 LEU 327 327 327 LEU LEU F . n 
F 2 328 GLY 328 328 328 GLY GLY F . n 
F 2 329 GLU 329 329 329 GLU GLU F . n 
F 2 330 ASP 330 330 330 ASP ASP F . n 
F 2 331 VAL 331 331 331 VAL VAL F . n 
F 2 332 HIS 332 332 332 HIS HIS F . n 
F 2 333 VAL 333 333 333 VAL VAL F . n 
F 2 334 SER 334 334 334 SER SER F . n 
F 2 335 ASP 335 335 335 ASP ASP F . n 
F 2 336 GLU 336 336 336 GLU GLU F . n 
F 2 337 ILE 337 337 337 ILE ILE F . n 
F 2 338 TYR 338 338 338 TYR TYR F . n 
F 2 339 SER 339 339 339 SER SER F . n 
F 2 340 ASN 340 340 340 ASN ASN F . n 
F 2 341 GLY 341 341 341 GLY GLY F . n 
F 2 342 GLY 342 342 342 GLY GLY F . n 
F 2 343 VAL 343 343 343 VAL VAL F . n 
F 2 344 VAL 344 344 344 VAL VAL F . n 
F 2 345 LEU 345 345 345 LEU LEU F . n 
F 2 346 PRO 346 346 346 PRO PRO F . n 
F 2 347 HIS 347 347 347 HIS HIS F . n 
F 2 348 LYS 348 348 348 LYS LYS F . n 
F 2 349 GLU 349 349 349 GLU GLU F . n 
F 2 350 ILE 350 350 350 ILE ILE F . n 
F 2 351 LYS 351 351 351 LYS LYS F . n 
F 2 352 SER 352 352 352 SER SER F . n 
F 2 353 ASN 353 353 353 ASN ASN F . n 
F 2 354 ILE 354 354 354 ILE ILE F . n 
F 2 355 LEU 355 355 355 LEU LEU F . n 
F 2 356 LYS 356 356 356 LYS LYS F . n 
F 2 357 PRO 357 357 357 PRO PRO F . n 
F 2 358 GLU 358 358 358 GLU GLU F . n 
F 2 359 ILE 359 359 359 ILE ILE F . n 
F 2 360 VAL 360 360 360 VAL VAL F . n 
F 2 361 MET 361 361 361 MET MET F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 3 SO4 1 501 9  SO4 SO4 A . 
H 3 SO4 1 502 10 SO4 SO4 A . 
I 3 SO4 1 503 11 SO4 SO4 A . 
J 3 SO4 1 501 13 SO4 SO4 B . 
K 3 SO4 1 401 3  SO4 SO4 D . 
L 3 SO4 1 402 4  SO4 SO4 D . 
M 3 SO4 1 403 8  SO4 SO4 D . 
N 3 SO4 1 404 14 SO4 SO4 D . 
O 3 SO4 1 401 1  SO4 SO4 E . 
P 3 SO4 1 402 2  SO4 SO4 E . 
Q 3 SO4 1 401 6  SO4 SO4 F . 
R 3 SO4 1 402 15 SO4 SO4 F . 
S 4 HOH 1 601 5  HOH HOH A . 
T 4 HOH 1 601 7  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLN 56  ? CG  ? A GLN 56  CG  
2   1 Y 1 A GLN 56  ? CD  ? A GLN 56  CD  
3   1 Y 1 A GLN 56  ? OE1 ? A GLN 56  OE1 
4   1 Y 1 A GLN 56  ? NE2 ? A GLN 56  NE2 
5   1 Y 1 A LYS 90  ? CG  ? A LYS 90  CG  
6   1 Y 1 A LYS 90  ? CD  ? A LYS 90  CD  
7   1 Y 1 A LYS 90  ? CE  ? A LYS 90  CE  
8   1 Y 1 A LYS 90  ? NZ  ? A LYS 90  NZ  
9   1 Y 1 A GLU 157 ? CG  ? A GLU 157 CG  
10  1 Y 1 A GLU 157 ? CD  ? A GLU 157 CD  
11  1 Y 1 A GLU 157 ? OE1 ? A GLU 157 OE1 
12  1 Y 1 A GLU 157 ? OE2 ? A GLU 157 OE2 
13  1 Y 1 A ASP 161 ? CG  ? A ASP 161 CG  
14  1 Y 1 A ASP 161 ? OD1 ? A ASP 161 OD1 
15  1 Y 1 A ASP 161 ? OD2 ? A ASP 161 OD2 
16  1 Y 1 A GLU 243 ? CG  ? A GLU 243 CG  
17  1 Y 1 A GLU 243 ? CD  ? A GLU 243 CD  
18  1 Y 1 A GLU 243 ? OE1 ? A GLU 243 OE1 
19  1 Y 1 A GLU 243 ? OE2 ? A GLU 243 OE2 
20  1 Y 1 A LYS 245 ? CG  ? A LYS 245 CG  
21  1 Y 1 A LYS 245 ? CD  ? A LYS 245 CD  
22  1 Y 1 A LYS 245 ? CE  ? A LYS 245 CE  
23  1 Y 1 A LYS 245 ? NZ  ? A LYS 245 NZ  
24  1 Y 1 A GLU 249 ? CG  ? A GLU 249 CG  
25  1 Y 1 A GLU 249 ? CD  ? A GLU 249 CD  
26  1 Y 1 A GLU 249 ? OE1 ? A GLU 249 OE1 
27  1 Y 1 A GLU 249 ? OE2 ? A GLU 249 OE2 
28  1 Y 1 A GLU 270 ? CG  ? A GLU 270 CG  
29  1 Y 1 A GLU 270 ? CD  ? A GLU 270 CD  
30  1 Y 1 A GLU 270 ? OE1 ? A GLU 270 OE1 
31  1 Y 1 A GLU 270 ? OE2 ? A GLU 270 OE2 
32  1 Y 1 A LYS 285 ? CG  ? A LYS 285 CG  
33  1 Y 1 A LYS 285 ? CD  ? A LYS 285 CD  
34  1 Y 1 A LYS 285 ? CE  ? A LYS 285 CE  
35  1 Y 1 A LYS 285 ? NZ  ? A LYS 285 NZ  
36  1 Y 1 B GLN 56  ? CG  ? B GLN 56  CG  
37  1 Y 1 B GLN 56  ? CD  ? B GLN 56  CD  
38  1 Y 1 B GLN 56  ? OE1 ? B GLN 56  OE1 
39  1 Y 1 B GLN 56  ? NE2 ? B GLN 56  NE2 
40  1 Y 1 B LYS 90  ? CG  ? B LYS 90  CG  
41  1 Y 1 B LYS 90  ? CD  ? B LYS 90  CD  
42  1 Y 1 B LYS 90  ? CE  ? B LYS 90  CE  
43  1 Y 1 B LYS 90  ? NZ  ? B LYS 90  NZ  
44  1 Y 1 B GLU 157 ? CG  ? B GLU 157 CG  
45  1 Y 1 B GLU 157 ? CD  ? B GLU 157 CD  
46  1 Y 1 B GLU 157 ? OE1 ? B GLU 157 OE1 
47  1 Y 1 B GLU 157 ? OE2 ? B GLU 157 OE2 
48  1 Y 1 B ASP 161 ? CG  ? B ASP 161 CG  
49  1 Y 1 B ASP 161 ? OD1 ? B ASP 161 OD1 
50  1 Y 1 B ASP 161 ? OD2 ? B ASP 161 OD2 
51  1 Y 1 B GLU 243 ? CG  ? B GLU 243 CG  
52  1 Y 1 B GLU 243 ? CD  ? B GLU 243 CD  
53  1 Y 1 B GLU 243 ? OE1 ? B GLU 243 OE1 
54  1 Y 1 B GLU 243 ? OE2 ? B GLU 243 OE2 
55  1 Y 1 B LYS 245 ? CG  ? B LYS 245 CG  
56  1 Y 1 B LYS 245 ? CD  ? B LYS 245 CD  
57  1 Y 1 B LYS 245 ? CE  ? B LYS 245 CE  
58  1 Y 1 B LYS 245 ? NZ  ? B LYS 245 NZ  
59  1 Y 1 B GLU 249 ? CG  ? B GLU 249 CG  
60  1 Y 1 B GLU 249 ? CD  ? B GLU 249 CD  
61  1 Y 1 B GLU 249 ? OE1 ? B GLU 249 OE1 
62  1 Y 1 B GLU 249 ? OE2 ? B GLU 249 OE2 
63  1 Y 1 B GLU 270 ? CG  ? B GLU 270 CG  
64  1 Y 1 B GLU 270 ? CD  ? B GLU 270 CD  
65  1 Y 1 B GLU 270 ? OE1 ? B GLU 270 OE1 
66  1 Y 1 B GLU 270 ? OE2 ? B GLU 270 OE2 
67  1 Y 1 B LYS 285 ? CG  ? B LYS 285 CG  
68  1 Y 1 B LYS 285 ? CD  ? B LYS 285 CD  
69  1 Y 1 B LYS 285 ? CE  ? B LYS 285 CE  
70  1 Y 1 B LYS 285 ? NZ  ? B LYS 285 NZ  
71  1 Y 1 C CYS 48  ? SG  ? C CYS 48  SG  
72  1 Y 1 C GLN 56  ? CG  ? C GLN 56  CG  
73  1 Y 1 C GLN 56  ? CD  ? C GLN 56  CD  
74  1 Y 1 C GLN 56  ? OE1 ? C GLN 56  OE1 
75  1 Y 1 C GLN 56  ? NE2 ? C GLN 56  NE2 
76  1 Y 1 C LYS 90  ? CG  ? C LYS 90  CG  
77  1 Y 1 C LYS 90  ? CD  ? C LYS 90  CD  
78  1 Y 1 C LYS 90  ? CE  ? C LYS 90  CE  
79  1 Y 1 C LYS 90  ? NZ  ? C LYS 90  NZ  
80  1 Y 1 C ILE 105 ? CG1 ? C ILE 105 CG1 
81  1 Y 1 C ILE 105 ? CG2 ? C ILE 105 CG2 
82  1 Y 1 C ILE 105 ? CD1 ? C ILE 105 CD1 
83  1 Y 1 C LEU 116 ? CG  ? C LEU 116 CG  
84  1 Y 1 C LEU 116 ? CD1 ? C LEU 116 CD1 
85  1 Y 1 C LEU 116 ? CD2 ? C LEU 116 CD2 
86  1 Y 1 C GLU 157 ? CG  ? C GLU 157 CG  
87  1 Y 1 C GLU 157 ? CD  ? C GLU 157 CD  
88  1 Y 1 C GLU 157 ? OE1 ? C GLU 157 OE1 
89  1 Y 1 C GLU 157 ? OE2 ? C GLU 157 OE2 
90  1 Y 1 C LEU 158 ? CG  ? C LEU 158 CG  
91  1 Y 1 C LEU 158 ? CD1 ? C LEU 158 CD1 
92  1 Y 1 C LEU 158 ? CD2 ? C LEU 158 CD2 
93  1 Y 1 C ASP 161 ? CG  ? C ASP 161 CG  
94  1 Y 1 C ASP 161 ? OD1 ? C ASP 161 OD1 
95  1 Y 1 C ASP 161 ? OD2 ? C ASP 161 OD2 
96  1 Y 1 C ASP 228 ? CG  ? C ASP 228 CG  
97  1 Y 1 C ASP 228 ? OD1 ? C ASP 228 OD1 
98  1 Y 1 C ASP 228 ? OD2 ? C ASP 228 OD2 
99  1 Y 1 C ILE 229 ? CG1 ? C ILE 229 CG1 
100 1 Y 1 C ILE 229 ? CG2 ? C ILE 229 CG2 
101 1 Y 1 C ILE 229 ? CD1 ? C ILE 229 CD1 
102 1 Y 1 C LYS 245 ? CG  ? C LYS 245 CG  
103 1 Y 1 C LYS 245 ? CD  ? C LYS 245 CD  
104 1 Y 1 C LYS 245 ? CE  ? C LYS 245 CE  
105 1 Y 1 C LYS 245 ? NZ  ? C LYS 245 NZ  
106 1 Y 1 C GLU 249 ? CG  ? C GLU 249 CG  
107 1 Y 1 C GLU 249 ? CD  ? C GLU 249 CD  
108 1 Y 1 C GLU 249 ? OE1 ? C GLU 249 OE1 
109 1 Y 1 C GLU 249 ? OE2 ? C GLU 249 OE2 
110 1 Y 1 C SER 257 ? OG  ? C SER 257 OG  
111 1 Y 1 C CYS 260 ? SG  ? C CYS 260 SG  
112 1 Y 1 C GLU 270 ? CG  ? C GLU 270 CG  
113 1 Y 1 C GLU 270 ? CD  ? C GLU 270 CD  
114 1 Y 1 C GLU 270 ? OE1 ? C GLU 270 OE1 
115 1 Y 1 C GLU 270 ? OE2 ? C GLU 270 OE2 
116 1 Y 1 C LYS 285 ? CG  ? C LYS 285 CG  
117 1 Y 1 C LYS 285 ? CD  ? C LYS 285 CD  
118 1 Y 1 C LYS 285 ? CE  ? C LYS 285 CE  
119 1 Y 1 C LYS 285 ? NZ  ? C LYS 285 NZ  
120 1 Y 1 D GLU 48  ? CG  ? D GLU 48  CG  
121 1 Y 1 D GLU 48  ? CD  ? D GLU 48  CD  
122 1 Y 1 D GLU 48  ? OE1 ? D GLU 48  OE1 
123 1 Y 1 D GLU 48  ? OE2 ? D GLU 48  OE2 
124 1 Y 1 D GLU 152 ? CG  ? D GLU 152 CG  
125 1 Y 1 D GLU 152 ? CD  ? D GLU 152 CD  
126 1 Y 1 D GLU 152 ? OE1 ? D GLU 152 OE1 
127 1 Y 1 D GLU 152 ? OE2 ? D GLU 152 OE2 
128 1 Y 1 E GLU 48  ? CG  ? E GLU 48  CG  
129 1 Y 1 E GLU 48  ? CD  ? E GLU 48  CD  
130 1 Y 1 E GLU 48  ? OE1 ? E GLU 48  OE1 
131 1 Y 1 E GLU 48  ? OE2 ? E GLU 48  OE2 
132 1 Y 1 E PHE 106 ? CG  ? E PHE 106 CG  
133 1 Y 1 E PHE 106 ? CD1 ? E PHE 106 CD1 
134 1 Y 1 E PHE 106 ? CD2 ? E PHE 106 CD2 
135 1 Y 1 E PHE 106 ? CE1 ? E PHE 106 CE1 
136 1 Y 1 E PHE 106 ? CE2 ? E PHE 106 CE2 
137 1 Y 1 E PHE 106 ? CZ  ? E PHE 106 CZ  
138 1 Y 1 E GLU 141 ? CG  ? E GLU 141 CG  
139 1 Y 1 E GLU 141 ? CD  ? E GLU 141 CD  
140 1 Y 1 E GLU 141 ? OE1 ? E GLU 141 OE1 
141 1 Y 1 E GLU 141 ? OE2 ? E GLU 141 OE2 
142 1 Y 1 E GLU 152 ? CG  ? E GLU 152 CG  
143 1 Y 1 E GLU 152 ? CD  ? E GLU 152 CD  
144 1 Y 1 E GLU 152 ? OE1 ? E GLU 152 OE1 
145 1 Y 1 E GLU 152 ? OE2 ? E GLU 152 OE2 
146 1 Y 1 E GLU 195 ? CG  ? E GLU 195 CG  
147 1 Y 1 E GLU 195 ? CD  ? E GLU 195 CD  
148 1 Y 1 E GLU 195 ? OE1 ? E GLU 195 OE1 
149 1 Y 1 E GLU 195 ? OE2 ? E GLU 195 OE2 
150 1 Y 1 F GLU 48  ? CG  ? F GLU 48  CG  
151 1 Y 1 F GLU 48  ? CD  ? F GLU 48  CD  
152 1 Y 1 F GLU 48  ? OE1 ? F GLU 48  OE1 
153 1 Y 1 F GLU 48  ? OE2 ? F GLU 48  OE2 
154 1 Y 1 F PHE 160 ? CG  ? F PHE 160 CG  
155 1 Y 1 F PHE 160 ? CD1 ? F PHE 160 CD1 
156 1 Y 1 F PHE 160 ? CD2 ? F PHE 160 CD2 
157 1 Y 1 F PHE 160 ? CE1 ? F PHE 160 CE1 
158 1 Y 1 F PHE 160 ? CE2 ? F PHE 160 CE2 
159 1 Y 1 F PHE 160 ? CZ  ? F PHE 160 CZ  
160 1 Y 1 F ILE 176 ? CG1 ? F ILE 176 CG1 
161 1 Y 1 F ILE 176 ? CG2 ? F ILE 176 CG2 
162 1 Y 1 F ILE 176 ? CD1 ? F ILE 176 CD1 
163 1 Y 1 F ILE 308 ? CG1 ? F ILE 308 CG1 
164 1 Y 1 F ILE 308 ? CG2 ? F ILE 308 CG2 
165 1 Y 1 F ILE 308 ? CD1 ? F ILE 308 CD1 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.18 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   117.14 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YRE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     158.268 
_cell.length_a_esd                 ? 
_cell.length_b                     134.987 
_cell.length_b_esd                 ? 
_cell.length_c                     168.473 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8YRE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YRE 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.01 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'ammonium sulphate, Bis-Tris propane, PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-12-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9785 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9785 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YRE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.54 
_reflns.d_resolution_low                               149.92 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     37074 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           96.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.075 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.139 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.54 
_reflns_shell.d_res_low                                     3.64 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5264 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.467 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.768 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.616 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8YRE 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.54 
_refine.ls_d_res_low                             149.92 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     37069 
_refine.ls_number_reflns_R_free                  1918 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.33 
_refine.ls_percent_reflns_R_free                 5.34 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2638 
_refine.ls_R_factor_R_free                       0.2952 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2608 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          319.39 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       TWIN_LSQ_F 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 38.04 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        17135 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         60 
_refine_hist.number_atoms_solvent             2 
_refine_hist.number_atoms_total               17197 
_refine_hist.d_res_high                       3.54 
_refine_hist.d_res_low                        149.92 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  ? 17527 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.562  ? 23780 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.318 ? 6488  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.048  ? 2768  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 3014  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.54 3.63   . . 159 2582 94.00 . . . . 0.3246 . . . . . . . . . . . 0.3246 
'X-RAY DIFFRACTION' 3.63 3.73   . . 131 2259 82.00 . . . . 0.3213 . . . . . . . . . . . 0.3457 
'X-RAY DIFFRACTION' 3.73 3.84   . . 159 2560 94.00 . . . . 0.3068 . . . . . . . . . . . 0.3068 
'X-RAY DIFFRACTION' 3.84 3.96   . . 99  1674 61.00 . . . . 0.3137 . . . . . . . . . . . 0.3634 
'X-RAY DIFFRACTION' 3.96 4.11   . . 120 2626 96.00 . . . . 0.3022 . . . . . . . . . . . 0.3365 
'X-RAY DIFFRACTION' 4.11 4.27   . . 127 2595 95.00 . . . . 0.2862 . . . . . . . . . . . 0.3386 
'X-RAY DIFFRACTION' 4.27 4.46   . . 133 2579 95.00 . . . . 0.2698 . . . . . . . . . . . 0.3026 
'X-RAY DIFFRACTION' 4.46 4.70   . . 134 2623 95.00 . . . . 0.2586 . . . . . . . . . . . 0.3161 
'X-RAY DIFFRACTION' 4.70 4.99   . . 161 2576 94.00 . . . . 0.2547 . . . . . . . . . . . 0.2547 
'X-RAY DIFFRACTION' 4.99 5.38   . . 129 2603 95.00 . . . . 0.2665 . . . . . . . . . . . 0.2953 
'X-RAY DIFFRACTION' 5.38 5.92   . . 126 2609 95.00 . . . . 0.2773 . . . . . . . . . . . 0.3399 
'X-RAY DIFFRACTION' 5.92 6.78   . . 130 2641 95.00 . . . . 0.2844 . . . . . . . . . . . 0.3324 
'X-RAY DIFFRACTION' 6.78 8.54   . . 147 2610 94.00 . . . . 0.2311 . . . . . . . . . . . 0.3011 
'X-RAY DIFFRACTION' 8.54 149.92 . . 162 2615 93.00 . . . . 0.1997 . . . . . . . . . . . 0.2552 
# 
_struct.entry_id                     8YRE 
_struct.title                        'Crystal structure of Arabidopsis VTC1-KJC2' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8YRE 
_struct_keywords.text            'nucleotide sugar, oligomerization, allostery, VTC1, KJC2, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 3 ? 
S N N 4 ? 
T N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP F4IFA4_ARATH F4IFA4 ? 1 
;MSEEKVVAVIMVGGPTKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELK
IPVRYLKEDKPHGSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIA
DPDTKELLHYTEKPETFVSDLINCGVYVFTSDIFNAIEEVYSQIRDTSSNYQSATRSVPADFVRLDQDILSPLAGKKQLY
TYENKDFWEQIKTPGKSLKCSALYLSQFRETSPHILASGDGTNRKPTIIGDVYIHPSVKLHPTAKIGPNVSISANVRVGP
GVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRVQASGDYNDRLGITILGEAVTVEDEVAVIGSIVLQNKTLNVSV
QDDIIL
;
1 
2 UNP GMPP1_ARATH  O22287 ? 2 
;MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQE
TEPLGTAGPLALARDKLLDGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEESTGRVEKF
VEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYLDSLRKK
SPAKLTSGPHIVGNVLVDETATIGEGCLIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWAR
IENMTILGEDVHVSDEIYSNGGVVLPHKEIKSNILKPEIVM
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8YRE A 1 ? 406 ? F4IFA4 1 ? 406 ? 1 406 
2 1 8YRE B 1 ? 406 ? F4IFA4 1 ? 406 ? 1 406 
3 1 8YRE C 1 ? 406 ? F4IFA4 1 ? 406 ? 1 406 
4 2 8YRE D 1 ? 361 ? O22287 1 ? 361 ? 1 361 
5 2 8YRE E 1 ? 361 ? O22287 1 ? 361 ? 1 361 
6 2 8YRE F 1 ? 361 ? O22287 1 ? 361 ? 1 361 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PHE A 21  ? PHE A 26  ? PHE A 21  PHE A 26  1 ? 6  
HELX_P HELX_P2  AA2 PRO A 29  ? LEU A 32  ? PRO A 29  LEU A 32  5 ? 4  
HELX_P HELX_P3  AA3 ILE A 41  ? LYS A 49  ? ILE A 41  LYS A 49  1 ? 9  
HELX_P HELX_P4  AA4 GLU A 64  ? SER A 76  ? GLU A 64  SER A 76  1 ? 13 
HELX_P HELX_P5  AA5 SER A 94  ? TYR A 100 ? SER A 94  TYR A 100 1 ? 7  
HELX_P HELX_P6  AA6 PHE A 101 ? MET A 106 ? PHE A 101 MET A 106 1 ? 6  
HELX_P HELX_P7  AA7 GLU A 107 ? LYS A 109 ? GLU A 107 LYS A 109 5 ? 3  
HELX_P HELX_P8  AA8 PRO A 125 ? GLY A 137 ? PRO A 125 GLY A 137 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 192 ? SER A 202 ? ASP A 192 SER A 202 1 ? 11 
HELX_P HELX_P10 AB1 ARG A 224 ? ILE A 229 ? ARG A 224 ILE A 229 1 ? 6  
HELX_P HELX_P11 AB2 GLY A 255 ? THR A 271 ? GLY A 255 THR A 271 1 ? 17 
HELX_P HELX_P12 AB3 SER A 272 ? LEU A 276 ? SER A 272 LEU A 276 5 ? 5  
HELX_P HELX_P13 AB4 ASP A 366 ? ILE A 370 ? ASP A 366 ILE A 370 5 ? 5  
HELX_P HELX_P14 AB5 PHE B 21  ? PHE B 26  ? PHE B 21  PHE B 26  1 ? 6  
HELX_P HELX_P15 AB6 PRO B 29  ? LEU B 32  ? PRO B 29  LEU B 32  5 ? 4  
HELX_P HELX_P16 AB7 ILE B 41  ? LYS B 49  ? ILE B 41  LYS B 49  1 ? 9  
HELX_P HELX_P17 AB8 GLU B 64  ? LYS B 80  ? GLU B 64  LYS B 80  1 ? 17 
HELX_P HELX_P18 AB9 SER B 94  ? TYR B 100 ? SER B 94  TYR B 100 1 ? 7  
HELX_P HELX_P19 AC1 PHE B 101 ? MET B 106 ? PHE B 101 MET B 106 1 ? 6  
HELX_P HELX_P20 AC2 GLU B 107 ? LYS B 109 ? GLU B 107 LYS B 109 5 ? 3  
HELX_P HELX_P21 AC3 PRO B 125 ? GLY B 137 ? PRO B 125 GLY B 137 1 ? 13 
HELX_P HELX_P22 AC4 ASP B 192 ? SER B 202 ? ASP B 192 SER B 202 1 ? 11 
HELX_P HELX_P23 AC5 ARG B 224 ? ILE B 229 ? ARG B 224 ILE B 229 1 ? 6  
HELX_P HELX_P24 AC6 GLY B 255 ? THR B 271 ? GLY B 255 THR B 271 1 ? 17 
HELX_P HELX_P25 AC7 SER B 272 ? LEU B 276 ? SER B 272 LEU B 276 5 ? 5  
HELX_P HELX_P26 AC8 ASP B 366 ? ILE B 370 ? ASP B 366 ILE B 370 5 ? 5  
HELX_P HELX_P27 AC9 PHE C 21  ? PHE C 26  ? PHE C 21  PHE C 26  1 ? 6  
HELX_P HELX_P28 AD1 PRO C 29  ? LEU C 32  ? PRO C 29  LEU C 32  5 ? 4  
HELX_P HELX_P29 AD2 ILE C 41  ? LYS C 49  ? ILE C 41  LYS C 49  1 ? 9  
HELX_P HELX_P30 AD3 GLU C 64  ? LYS C 80  ? GLU C 64  LYS C 80  1 ? 17 
HELX_P HELX_P31 AD4 SER C 94  ? TYR C 100 ? SER C 94  TYR C 100 1 ? 7  
HELX_P HELX_P32 AD5 PHE C 101 ? MET C 106 ? PHE C 101 MET C 106 1 ? 6  
HELX_P HELX_P33 AD6 GLU C 107 ? LYS C 109 ? GLU C 107 LYS C 109 5 ? 3  
HELX_P HELX_P34 AD7 PRO C 125 ? GLY C 137 ? PRO C 125 GLY C 137 1 ? 13 
HELX_P HELX_P35 AD8 ASP C 192 ? SER C 202 ? ASP C 192 SER C 202 1 ? 11 
HELX_P HELX_P36 AD9 ARG C 224 ? ILE C 229 ? ARG C 224 ILE C 229 1 ? 6  
HELX_P HELX_P37 AE1 GLY C 255 ? THR C 271 ? GLY C 255 THR C 271 1 ? 17 
HELX_P HELX_P38 AE2 SER C 272 ? LEU C 276 ? SER C 272 LEU C 276 5 ? 5  
HELX_P HELX_P39 AE3 ASP C 366 ? ILE C 370 ? ASP C 366 ILE C 370 5 ? 5  
HELX_P HELX_P40 AE4 GLY D 11  ? ARG D 15  ? GLY D 11  ARG D 15  5 ? 5  
HELX_P HELX_P41 AE5 PRO D 22  ? LEU D 25  ? PRO D 22  LEU D 25  5 ? 4  
HELX_P HELX_P42 AE6 ILE D 34  ? VAL D 44  ? ILE D 34  VAL D 44  1 ? 11 
HELX_P HELX_P43 AE7 GLN D 56  ? VAL D 59  ? GLN D 56  VAL D 59  5 ? 4  
HELX_P HELX_P44 AE8 MET D 60  ? LEU D 71  ? MET D 60  LEU D 71  1 ? 12 
HELX_P HELX_P45 AE9 ALA D 87  ? ALA D 93  ? ALA D 87  ALA D 93  1 ? 7  
HELX_P HELX_P46 AF1 LEU D 118 ? LYS D 126 ? LEU D 118 LYS D 126 1 ? 9  
HELX_P HELX_P47 AF2 PRO D 181 ? LEU D 184 ? PRO D 181 LEU D 184 5 ? 4  
HELX_P HELX_P48 AF3 GLU D 197 ? ALA D 204 ? GLU D 197 ALA D 204 1 ? 8  
HELX_P HELX_P49 AF4 ARG D 224 ? SER D 241 ? ARG D 224 SER D 241 1 ? 18 
HELX_P HELX_P50 AF5 PRO D 242 ? LEU D 245 ? PRO D 242 LEU D 245 5 ? 4  
HELX_P HELX_P51 AF6 GLY E 11  ? ARG E 15  ? GLY E 11  ARG E 15  5 ? 5  
HELX_P HELX_P52 AF7 PRO E 22  ? LEU E 25  ? PRO E 22  LEU E 25  5 ? 4  
HELX_P HELX_P53 AF8 ILE E 34  ? VAL E 44  ? ILE E 34  VAL E 44  1 ? 11 
HELX_P HELX_P54 AF9 GLN E 56  ? VAL E 59  ? GLN E 56  VAL E 59  5 ? 4  
HELX_P HELX_P55 AG1 MET E 60  ? LEU E 71  ? MET E 60  LEU E 71  1 ? 12 
HELX_P HELX_P56 AG2 ALA E 87  ? ALA E 93  ? ALA E 87  ALA E 93  1 ? 7  
HELX_P HELX_P57 AG3 ALA E 93  ? LEU E 98  ? ALA E 93  LEU E 98  1 ? 6  
HELX_P HELX_P58 AG4 LEU E 118 ? LYS E 126 ? LEU E 118 LYS E 126 1 ? 9  
HELX_P HELX_P59 AG5 PRO E 181 ? LEU E 184 ? PRO E 181 LEU E 184 5 ? 4  
HELX_P HELX_P60 AG6 GLU E 197 ? ALA E 204 ? GLU E 197 ALA E 204 1 ? 8  
HELX_P HELX_P61 AG7 ARG E 224 ? SER E 241 ? ARG E 224 SER E 241 1 ? 18 
HELX_P HELX_P62 AG8 PRO E 242 ? LEU E 245 ? PRO E 242 LEU E 245 5 ? 4  
HELX_P HELX_P63 AG9 GLY F 11  ? ARG F 15  ? GLY F 11  ARG F 15  5 ? 5  
HELX_P HELX_P64 AH1 PRO F 22  ? LEU F 25  ? PRO F 22  LEU F 25  5 ? 4  
HELX_P HELX_P65 AH2 ILE F 34  ? VAL F 44  ? ILE F 34  VAL F 44  1 ? 11 
HELX_P HELX_P66 AH3 GLN F 56  ? VAL F 59  ? GLN F 56  VAL F 59  5 ? 4  
HELX_P HELX_P67 AH4 MET F 60  ? LEU F 71  ? MET F 60  LEU F 71  1 ? 12 
HELX_P HELX_P68 AH5 ALA F 87  ? ALA F 93  ? ALA F 87  ALA F 93  1 ? 7  
HELX_P HELX_P69 AH6 LEU F 118 ? LYS F 126 ? LEU F 118 LYS F 126 1 ? 9  
HELX_P HELX_P70 AH7 PRO F 181 ? LEU F 184 ? PRO F 181 LEU F 184 5 ? 4  
HELX_P HELX_P71 AH8 GLU F 197 ? ALA F 204 ? GLU F 197 ALA F 204 1 ? 8  
HELX_P HELX_P72 AH9 ARG F 224 ? SER F 241 ? ARG F 224 SER F 241 1 ? 18 
HELX_P HELX_P73 AI1 PRO F 242 ? LEU F 245 ? PRO F 242 LEU F 245 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_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 ARG 15  D . ? ARG 15  D PRO 16  D ? PRO 16  D 1 2.43  
2 GLY 270 D . ? GLY 270 D PRO 271 D ? PRO 271 D 1 -2.04 
3 ARG 15  E . ? ARG 15  E PRO 16  E ? PRO 16  E 1 2.61  
4 GLY 270 E . ? GLY 270 E PRO 271 E ? PRO 271 E 1 -1.21 
5 ARG 15  F . ? ARG 15  F PRO 16  F ? PRO 16  F 1 2.14  
6 GLY 270 F . ? GLY 270 F PRO 271 F ? PRO 271 F 1 -1.47 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 7 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 7 ? 
AB3 ? 7 ? 
AB4 ? 4 ? 
AB5 ? 5 ? 
AB6 ? 2 ? 
AB7 ? 2 ? 
AB8 ? 2 ? 
AB9 ? 7 ? 
AC1 ? 7 ? 
AC2 ? 4 ? 
AC3 ? 7 ? 
AC4 ? 2 ? 
AC5 ? 2 ? 
AC6 ? 2 ? 
AC7 ? 4 ? 
AC8 ? 6 ? 
AC9 ? 5 ? 
AD1 ? 2 ? 
AD2 ? 7 ? 
AD3 ? 2 ? 
AD4 ? 2 ? 
AD5 ? 2 ? 
AD6 ? 4 ? 
AD7 ? 6 ? 
AD8 ? 5 ? 
AD9 ? 2 ? 
AE1 ? 7 ? 
AE2 ? 2 ? 
AE3 ? 2 ? 
AE4 ? 2 ? 
AE5 ? 4 ? 
AE6 ? 6 ? 
AE7 ? 5 ? 
AE8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA4 6 7 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA5 6 7 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB2 5 6 ? parallel      
AB2 6 7 ? parallel      
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB3 4 5 ? parallel      
AB3 5 6 ? parallel      
AB3 6 7 ? parallel      
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? parallel      
AB9 3 4 ? parallel      
AB9 4 5 ? parallel      
AB9 5 6 ? parallel      
AB9 6 7 ? parallel      
AC1 1 2 ? parallel      
AC1 2 3 ? parallel      
AC1 3 4 ? parallel      
AC1 4 5 ? parallel      
AC1 5 6 ? parallel      
AC1 6 7 ? parallel      
AC2 1 2 ? parallel      
AC2 2 3 ? parallel      
AC2 3 4 ? parallel      
AC3 1 2 ? parallel      
AC3 2 3 ? parallel      
AC3 3 4 ? parallel      
AC3 4 5 ? anti-parallel 
AC3 5 6 ? anti-parallel 
AC3 6 7 ? parallel      
AC4 1 2 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC7 1 2 ? parallel      
AC7 2 3 ? parallel      
AC7 3 4 ? parallel      
AC8 1 2 ? parallel      
AC8 2 3 ? parallel      
AC8 3 4 ? parallel      
AC8 4 5 ? parallel      
AC8 5 6 ? parallel      
AC9 1 2 ? parallel      
AC9 2 3 ? parallel      
AC9 3 4 ? parallel      
AC9 4 5 ? parallel      
AD1 1 2 ? parallel      
AD2 1 2 ? parallel      
AD2 2 3 ? parallel      
AD2 3 4 ? parallel      
AD2 4 5 ? anti-parallel 
AD2 5 6 ? anti-parallel 
AD2 6 7 ? parallel      
AD3 1 2 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD6 1 2 ? parallel      
AD6 2 3 ? parallel      
AD6 3 4 ? parallel      
AD7 1 2 ? parallel      
AD7 2 3 ? parallel      
AD7 3 4 ? parallel      
AD7 4 5 ? parallel      
AD7 5 6 ? parallel      
AD8 1 2 ? parallel      
AD8 2 3 ? parallel      
AD8 3 4 ? parallel      
AD8 4 5 ? parallel      
AD9 1 2 ? parallel      
AE1 1 2 ? parallel      
AE1 2 3 ? parallel      
AE1 3 4 ? parallel      
AE1 4 5 ? anti-parallel 
AE1 5 6 ? anti-parallel 
AE1 6 7 ? parallel      
AE2 1 2 ? anti-parallel 
AE3 1 2 ? anti-parallel 
AE4 1 2 ? anti-parallel 
AE5 1 2 ? parallel      
AE5 2 3 ? parallel      
AE5 3 4 ? parallel      
AE6 1 2 ? parallel      
AE6 2 3 ? parallel      
AE6 3 4 ? parallel      
AE6 4 5 ? parallel      
AE6 5 6 ? parallel      
AE7 1 2 ? parallel      
AE7 2 3 ? parallel      
AE7 3 4 ? parallel      
AE7 4 5 ? parallel      
AE8 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 83  ? LEU A 86  ? VAL A 83  LEU A 86  
AA1 2 LEU A 54  ? ILE A 60  ? LEU A 54  ILE A 60  
AA1 3 VAL A 6   ? MET A 11  ? VAL A 6   MET A 11  
AA1 4 HIS A 112 ? LEU A 116 ? HIS A 112 LEU A 116 
AA1 5 TYR A 187 ? THR A 190 ? TYR A 187 THR A 190 
AA2 1 PRO A 34  ? LEU A 35  ? PRO A 34  LEU A 35  
AA2 2 GLN A 38  ? PRO A 39  ? GLN A 38  PRO A 39  
AA3 1 GLU A 157 ? ASP A 161 ? GLU A 157 ASP A 161 
AA3 2 GLU A 166 ? THR A 171 ? GLU A 166 THR A 171 
AA4 1 THR A 287 ? ILE A 288 ? THR A 287 ILE A 288 
AA4 2 LYS A 305 ? ILE A 306 ? LYS A 305 ILE A 306 
AA4 3 ARG A 323 ? ILE A 329 ? ARG A 323 ILE A 329 
AA4 4 VAL A 340 ? ILE A 346 ? VAL A 340 ILE A 346 
AA4 5 ARG A 357 ? GLN A 359 ? ARG A 357 GLN A 359 
AA4 6 ALA A 384 ? ILE A 386 ? ALA A 384 ILE A 386 
AA4 7 VAL A 400 ? GLN A 401 ? VAL A 400 GLN A 401 
AA5 1 VAL A 292 ? TYR A 293 ? VAL A 292 TYR A 293 
AA5 2 VAL A 310 ? ILE A 312 ? VAL A 310 ILE A 312 
AA5 3 ARG A 323 ? ILE A 329 ? ARG A 323 ILE A 329 
AA5 4 VAL A 340 ? ILE A 346 ? VAL A 340 ILE A 346 
AA5 5 THR A 371 ? LEU A 373 ? THR A 371 LEU A 373 
AA5 6 ILE A 389 ? VAL A 390 ? ILE A 389 VAL A 390 
AA5 7 ILE A 404 ? ILE A 405 ? ILE A 404 ILE A 405 
AA6 1 GLU A 334 ? ILE A 335 ? GLU A 334 ILE A 335 
AA6 2 SER A 351 ? ILE A 352 ? SER A 351 ILE A 352 
AA6 3 VAL A 377 ? VAL A 379 ? VAL A 377 VAL A 379 
AA6 4 LYS A 394 ? LEU A 396 ? LYS A 394 LEU A 396 
AA7 1 VAL B 83  ? LEU B 86  ? VAL B 83  LEU B 86  
AA7 2 LEU B 54  ? ILE B 60  ? LEU B 54  ILE B 60  
AA7 3 VAL B 6   ? MET B 11  ? VAL B 6   MET B 11  
AA7 4 HIS B 112 ? LEU B 116 ? HIS B 112 LEU B 116 
AA7 5 TYR B 187 ? THR B 190 ? TYR B 187 THR B 190 
AA8 1 PRO B 34  ? LEU B 35  ? PRO B 34  LEU B 35  
AA8 2 GLN B 38  ? PRO B 39  ? GLN B 38  PRO B 39  
AA9 1 VAL B 120 ? CYS B 122 ? VAL B 120 CYS B 122 
AA9 2 TRP B 248 ? GLN B 250 ? TRP B 248 GLN B 250 
AB1 1 GLU B 157 ? ASP B 161 ? GLU B 157 ASP B 161 
AB1 2 GLU B 166 ? THR B 171 ? GLU B 166 THR B 171 
AB2 1 THR B 287 ? ILE B 288 ? THR B 287 ILE B 288 
AB2 2 LYS B 305 ? ILE B 306 ? LYS B 305 ILE B 306 
AB2 3 ARG B 323 ? ILE B 325 ? ARG B 323 ILE B 325 
AB2 4 VAL B 340 ? ILE B 342 ? VAL B 340 ILE B 342 
AB2 5 ARG B 357 ? GLN B 359 ? ARG B 357 GLN B 359 
AB2 6 ALA B 384 ? ILE B 386 ? ALA B 384 ILE B 386 
AB2 7 VAL B 400 ? GLN B 401 ? VAL B 400 GLN B 401 
AB3 1 VAL B 292 ? TYR B 293 ? VAL B 292 TYR B 293 
AB3 2 VAL B 310 ? ILE B 312 ? VAL B 310 ILE B 312 
AB3 3 CYS B 327 ? ILE B 329 ? CYS B 327 ILE B 329 
AB3 4 SER B 344 ? ILE B 346 ? SER B 344 ILE B 346 
AB3 5 THR B 371 ? LEU B 373 ? THR B 371 LEU B 373 
AB3 6 ILE B 389 ? VAL B 390 ? ILE B 389 VAL B 390 
AB3 7 ILE B 404 ? ILE B 405 ? ILE B 404 ILE B 405 
AB4 1 GLU B 334 ? ILE B 335 ? GLU B 334 ILE B 335 
AB4 2 SER B 351 ? ILE B 352 ? SER B 351 ILE B 352 
AB4 3 VAL B 377 ? VAL B 379 ? VAL B 377 VAL B 379 
AB4 4 LYS B 394 ? LEU B 396 ? LYS B 394 LEU B 396 
AB5 1 VAL C 83  ? LEU C 86  ? VAL C 83  LEU C 86  
AB5 2 LEU C 54  ? ILE C 60  ? LEU C 54  ILE C 60  
AB5 3 VAL C 6   ? MET C 11  ? VAL C 6   MET C 11  
AB5 4 HIS C 112 ? LEU C 116 ? HIS C 112 LEU C 116 
AB5 5 PHE C 189 ? THR C 190 ? PHE C 189 THR C 190 
AB6 1 PRO C 34  ? LEU C 35  ? PRO C 34  LEU C 35  
AB6 2 GLN C 38  ? PRO C 39  ? GLN C 38  PRO C 39  
AB7 1 ILE C 145 ? LYS C 146 ? ILE C 145 LYS C 146 
AB7 2 LEU C 181 ? ILE C 182 ? LEU C 181 ILE C 182 
AB8 1 GLU C 157 ? ASP C 161 ? GLU C 157 ASP C 161 
AB8 2 GLU C 166 ? THR C 171 ? GLU C 166 THR C 171 
AB9 1 THR C 287 ? ILE C 288 ? THR C 287 ILE C 288 
AB9 2 LYS C 305 ? ILE C 306 ? LYS C 305 ILE C 306 
AB9 3 ARG C 323 ? ILE C 325 ? ARG C 323 ILE C 325 
AB9 4 VAL C 340 ? ILE C 342 ? VAL C 340 ILE C 342 
AB9 5 ARG C 357 ? GLN C 359 ? ARG C 357 GLN C 359 
AB9 6 ALA C 384 ? ILE C 386 ? ALA C 384 ILE C 386 
AB9 7 VAL C 400 ? GLN C 401 ? VAL C 400 GLN C 401 
AC1 1 VAL C 292 ? ILE C 294 ? VAL C 292 ILE C 294 
AC1 2 VAL C 310 ? ILE C 312 ? VAL C 310 ILE C 312 
AC1 3 CYS C 327 ? ILE C 329 ? CYS C 327 ILE C 329 
AC1 4 SER C 344 ? ILE C 346 ? SER C 344 ILE C 346 
AC1 5 THR C 371 ? LEU C 373 ? THR C 371 LEU C 373 
AC1 6 ILE C 389 ? VAL C 390 ? ILE C 389 VAL C 390 
AC1 7 ILE C 404 ? ILE C 405 ? ILE C 404 ILE C 405 
AC2 1 GLU C 334 ? ILE C 335 ? GLU C 334 ILE C 335 
AC2 2 SER C 351 ? ILE C 352 ? SER C 351 ILE C 352 
AC2 3 THR C 378 ? VAL C 379 ? THR C 378 VAL C 379 
AC2 4 THR C 395 ? LEU C 396 ? THR C 395 LEU C 396 
AC3 1 LYS D 74  ? GLN D 79  ? LYS D 74  GLN D 79  
AC3 2 GLU D 48  ? ILE D 53  ? GLU D 48  ILE D 53  
AC3 3 ALA D 3   ? GLY D 8   ? ALA D 3   GLY D 8   
AC3 4 PHE D 105 ? ASN D 109 ? PHE D 105 ASN D 109 
AC3 5 LYS D 171 ? LEU D 179 ? LYS D 171 LEU D 179 
AC3 6 ALA D 132 ? LYS D 138 ? ALA D 132 LYS D 138 
AC3 7 LEU D 208 ? VAL D 212 ? LEU D 208 VAL D 212 
AC4 1 ASP D 27  ? PHE D 28  ? ASP D 27  PHE D 28  
AC4 2 LYS D 31  ? PRO D 32  ? LYS D 31  PRO D 32  
AC5 1 VAL D 112 ? ILE D 113 ? VAL D 112 ILE D 113 
AC5 2 MET D 218 ? ASP D 219 ? MET D 218 ASP D 219 
AC6 1 GLY D 146 ? MET D 150 ? GLY D 146 MET D 150 
AC6 2 VAL D 157 ? GLU D 162 ? VAL D 157 GLU D 162 
AC7 1 VAL D 255 ? VAL D 257 ? VAL D 255 VAL D 257 
AC7 2 VAL D 273 ? ILE D 275 ? VAL D 273 ILE D 275 
AC7 3 THR D 291 ? VAL D 292 ? THR D 291 VAL D 292 
AC7 4 ILE D 308 ? ILE D 309 ? ILE D 308 ILE D 309 
AC8 1 THR D 262 ? ILE D 263 ? THR D 262 ILE D 263 
AC8 2 ILE D 280 ? VAL D 281 ? ILE D 280 VAL D 281 
AC8 3 ARG D 297 ? ILE D 298 ? ARG D 297 ILE D 298 
AC8 4 THR D 314 ? VAL D 315 ? THR D 314 VAL D 315 
AC8 5 VAL D 331 ? VAL D 333 ? VAL D 331 VAL D 333 
AC8 6 LYS D 348 ? ILE D 350 ? LYS D 348 ILE D 350 
AC9 1 LEU D 268 ? ILE D 269 ? LEU D 268 ILE D 269 
AC9 2 ARG D 286 ? SER D 288 ? ARG D 286 SER D 288 
AC9 3 CYS D 303 ? SER D 305 ? CYS D 303 SER D 305 
AC9 4 ARG D 320 ? GLU D 322 ? ARG D 320 GLU D 322 
AC9 5 TYR D 338 ? ASN D 340 ? TYR D 338 ASN D 340 
AD1 1 GLY D 342 ? VAL D 344 ? GLY D 342 VAL D 344 
AD1 2 GLU D 358 ? VAL D 360 ? GLU D 358 VAL D 360 
AD2 1 LYS E 74  ? GLN E 79  ? LYS E 74  GLN E 79  
AD2 2 GLU E 48  ? ILE E 53  ? GLU E 48  ILE E 53  
AD2 3 ALA E 3   ? GLY E 8   ? ALA E 3   GLY E 8   
AD2 4 PHE E 105 ? ASN E 109 ? PHE E 105 ASN E 109 
AD2 5 LYS E 171 ? LEU E 179 ? LYS E 171 LEU E 179 
AD2 6 ALA E 132 ? LYS E 138 ? ALA E 132 LYS E 138 
AD2 7 LEU E 208 ? TYR E 209 ? LEU E 208 TYR E 209 
AD3 1 ASP E 27  ? PHE E 28  ? ASP E 27  PHE E 28  
AD3 2 LYS E 31  ? PRO E 32  ? LYS E 31  PRO E 32  
AD4 1 VAL E 112 ? ILE E 113 ? VAL E 112 ILE E 113 
AD4 2 MET E 218 ? ASP E 219 ? MET E 218 ASP E 219 
AD5 1 GLY E 146 ? MET E 150 ? GLY E 146 MET E 150 
AD5 2 VAL E 157 ? GLU E 162 ? VAL E 157 GLU E 162 
AD6 1 VAL E 255 ? VAL E 257 ? VAL E 255 VAL E 257 
AD6 2 VAL E 273 ? ILE E 275 ? VAL E 273 ILE E 275 
AD6 3 THR E 291 ? VAL E 292 ? THR E 291 VAL E 292 
AD6 4 ILE E 308 ? ILE E 309 ? ILE E 308 ILE E 309 
AD7 1 THR E 262 ? ILE E 263 ? THR E 262 ILE E 263 
AD7 2 ILE E 280 ? VAL E 281 ? ILE E 280 VAL E 281 
AD7 3 ARG E 297 ? ILE E 298 ? ARG E 297 ILE E 298 
AD7 4 THR E 314 ? VAL E 315 ? THR E 314 VAL E 315 
AD7 5 VAL E 331 ? VAL E 333 ? VAL E 331 VAL E 333 
AD7 6 LYS E 348 ? ILE E 350 ? LYS E 348 ILE E 350 
AD8 1 LEU E 268 ? ILE E 269 ? LEU E 268 ILE E 269 
AD8 2 ARG E 286 ? SER E 288 ? ARG E 286 SER E 288 
AD8 3 CYS E 303 ? SER E 305 ? CYS E 303 SER E 305 
AD8 4 ARG E 320 ? GLU E 322 ? ARG E 320 GLU E 322 
AD8 5 TYR E 338 ? ASN E 340 ? TYR E 338 ASN E 340 
AD9 1 GLY E 342 ? VAL E 344 ? GLY E 342 VAL E 344 
AD9 2 GLU E 358 ? VAL E 360 ? GLU E 358 VAL E 360 
AE1 1 LYS F 74  ? GLN F 79  ? LYS F 74  GLN F 79  
AE1 2 GLU F 48  ? ILE F 53  ? GLU F 48  ILE F 53  
AE1 3 ALA F 3   ? GLY F 8   ? ALA F 3   GLY F 8   
AE1 4 PHE F 105 ? ASN F 109 ? PHE F 105 ASN F 109 
AE1 5 LYS F 171 ? LEU F 179 ? LYS F 171 LEU F 179 
AE1 6 ALA F 132 ? LYS F 138 ? ALA F 132 LYS F 138 
AE1 7 LEU F 208 ? TYR F 209 ? LEU F 208 TYR F 209 
AE2 1 ASP F 27  ? PHE F 28  ? ASP F 27  PHE F 28  
AE2 2 LYS F 31  ? PRO F 32  ? LYS F 31  PRO F 32  
AE3 1 VAL F 112 ? ILE F 113 ? VAL F 112 ILE F 113 
AE3 2 MET F 218 ? ASP F 219 ? MET F 218 ASP F 219 
AE4 1 GLY F 146 ? VAL F 149 ? GLY F 146 VAL F 149 
AE4 2 LYS F 159 ? GLU F 162 ? LYS F 159 GLU F 162 
AE5 1 VAL F 255 ? VAL F 257 ? VAL F 255 VAL F 257 
AE5 2 VAL F 273 ? ILE F 275 ? VAL F 273 ILE F 275 
AE5 3 THR F 291 ? VAL F 292 ? THR F 291 VAL F 292 
AE5 4 ILE F 308 ? ILE F 309 ? ILE F 308 ILE F 309 
AE6 1 THR F 262 ? ILE F 263 ? THR F 262 ILE F 263 
AE6 2 ILE F 280 ? VAL F 281 ? ILE F 280 VAL F 281 
AE6 3 ARG F 297 ? ILE F 298 ? ARG F 297 ILE F 298 
AE6 4 THR F 314 ? VAL F 315 ? THR F 314 VAL F 315 
AE6 5 VAL F 331 ? VAL F 333 ? VAL F 331 VAL F 333 
AE6 6 LYS F 348 ? ILE F 350 ? LYS F 348 ILE F 350 
AE7 1 LEU F 268 ? ILE F 269 ? LEU F 268 ILE F 269 
AE7 2 ARG F 286 ? SER F 288 ? ARG F 286 SER F 288 
AE7 3 CYS F 303 ? SER F 305 ? CYS F 303 SER F 305 
AE7 4 ARG F 320 ? GLU F 322 ? ARG F 320 GLU F 322 
AE7 5 TYR F 338 ? ASN F 340 ? TYR F 338 ASN F 340 
AE8 1 GLY F 342 ? VAL F 344 ? GLY F 342 VAL F 344 
AE8 2 GLU F 358 ? VAL F 360 ? GLU F 358 VAL F 360 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 86  ? O LEU A 86  N LEU A 59  ? N LEU A 59  
AA1 2 3 O PHE A 58  ? O PHE A 58  N ILE A 10  ? N ILE A 10  
AA1 3 4 N VAL A 9   ? N VAL A 9   O PHE A 114 ? O PHE A 114 
AA1 4 5 N LEU A 115 ? N LEU A 115 O TYR A 187 ? O TYR A 187 
AA2 1 2 N LEU A 35  ? N LEU A 35  O GLN A 38  ? O GLN A 38  
AA3 1 2 N ILE A 159 ? N ILE A 159 O HIS A 169 ? O HIS A 169 
AA4 1 2 N THR A 287 ? N THR A 287 O ILE A 306 ? O ILE A 306 
AA4 2 3 N LYS A 305 ? N LYS A 305 O LEU A 324 ? O LEU A 324 
AA4 3 4 N ARG A 323 ? N ARG A 323 O VAL A 341 ? O VAL A 341 
AA4 4 5 N ILE A 342 ? N ILE A 342 O VAL A 358 ? O VAL A 358 
AA4 5 6 N ARG A 357 ? N ARG A 357 O VAL A 385 ? O VAL A 385 
AA4 6 7 N ALA A 384 ? N ALA A 384 O VAL A 400 ? O VAL A 400 
AA5 1 2 N TYR A 293 ? N TYR A 293 O ILE A 312 ? O ILE A 312 
AA5 2 3 N SER A 311 ? N SER A 311 O ILE A 329 ? O ILE A 329 
AA5 3 4 N ARG A 323 ? N ARG A 323 O VAL A 341 ? O VAL A 341 
AA5 4 5 N ILE A 345 ? N ILE A 345 O LEU A 373 ? O LEU A 373 
AA5 5 6 N ILE A 372 ? N ILE A 372 O VAL A 390 ? O VAL A 390 
AA5 6 7 N ILE A 389 ? N ILE A 389 O ILE A 405 ? O ILE A 405 
AA6 1 2 N GLU A 334 ? N GLU A 334 O ILE A 352 ? O ILE A 352 
AA6 2 3 N SER A 351 ? N SER A 351 O VAL A 379 ? O VAL A 379 
AA6 3 4 N THR A 378 ? N THR A 378 O LYS A 394 ? O LYS A 394 
AA7 1 2 O LEU B 86  ? O LEU B 86  N LEU B 59  ? N LEU B 59  
AA7 2 3 O PHE B 58  ? O PHE B 58  N ILE B 10  ? N ILE B 10  
AA7 3 4 N VAL B 9   ? N VAL B 9   O PHE B 114 ? O PHE B 114 
AA7 4 5 N LEU B 115 ? N LEU B 115 O TYR B 187 ? O TYR B 187 
AA8 1 2 N LEU B 35  ? N LEU B 35  O GLN B 38  ? O GLN B 38  
AA9 1 2 N CYS B 121 ? N CYS B 121 O GLU B 249 ? O GLU B 249 
AB1 1 2 N ASP B 161 ? N ASP B 161 O GLU B 166 ? O GLU B 166 
AB2 1 2 N THR B 287 ? N THR B 287 O ILE B 306 ? O ILE B 306 
AB2 2 3 N LYS B 305 ? N LYS B 305 O LEU B 324 ? O LEU B 324 
AB2 3 4 N ARG B 323 ? N ARG B 323 O VAL B 341 ? O VAL B 341 
AB2 4 5 N ILE B 342 ? N ILE B 342 O VAL B 358 ? O VAL B 358 
AB2 5 6 N ARG B 357 ? N ARG B 357 O VAL B 385 ? O VAL B 385 
AB2 6 7 N ALA B 384 ? N ALA B 384 O VAL B 400 ? O VAL B 400 
AB3 1 2 N TYR B 293 ? N TYR B 293 O ILE B 312 ? O ILE B 312 
AB3 2 3 N SER B 311 ? N SER B 311 O ILE B 329 ? O ILE B 329 
AB3 3 4 N ILE B 328 ? N ILE B 328 O ILE B 346 ? O ILE B 346 
AB3 4 5 N ILE B 345 ? N ILE B 345 O LEU B 373 ? O LEU B 373 
AB3 5 6 N ILE B 372 ? N ILE B 372 O VAL B 390 ? O VAL B 390 
AB3 6 7 N ILE B 389 ? N ILE B 389 O ILE B 405 ? O ILE B 405 
AB4 1 2 N GLU B 334 ? N GLU B 334 O ILE B 352 ? O ILE B 352 
AB4 2 3 N SER B 351 ? N SER B 351 O VAL B 379 ? O VAL B 379 
AB4 3 4 N THR B 378 ? N THR B 378 O LYS B 394 ? O LYS B 394 
AB5 1 2 O ARG C 84  ? O ARG C 84  N LEU C 59  ? N LEU C 59  
AB5 2 3 O PHE C 58  ? O PHE C 58  N ILE C 10  ? N ILE C 10  
AB5 3 4 N VAL C 7   ? N VAL C 7   O PHE C 114 ? O PHE C 114 
AB5 4 5 N VAL C 113 ? N VAL C 113 O PHE C 189 ? O PHE C 189 
AB6 1 2 N LEU C 35  ? N LEU C 35  O GLN C 38  ? O GLN C 38  
AB7 1 2 N ILE C 145 ? N ILE C 145 O ILE C 182 ? O ILE C 182 
AB8 1 2 N ILE C 159 ? N ILE C 159 O HIS C 169 ? O HIS C 169 
AB9 1 2 N THR C 287 ? N THR C 287 O ILE C 306 ? O ILE C 306 
AB9 2 3 N LYS C 305 ? N LYS C 305 O LEU C 324 ? O LEU C 324 
AB9 3 4 N ARG C 323 ? N ARG C 323 O VAL C 341 ? O VAL C 341 
AB9 4 5 N VAL C 340 ? N VAL C 340 O VAL C 358 ? O VAL C 358 
AB9 5 6 N ARG C 357 ? N ARG C 357 O VAL C 385 ? O VAL C 385 
AB9 6 7 N ALA C 384 ? N ALA C 384 O VAL C 400 ? O VAL C 400 
AC1 1 2 N TYR C 293 ? N TYR C 293 O ILE C 312 ? O ILE C 312 
AC1 2 3 N SER C 311 ? N SER C 311 O ILE C 329 ? O ILE C 329 
AC1 3 4 N ILE C 328 ? N ILE C 328 O ILE C 346 ? O ILE C 346 
AC1 4 5 N ILE C 345 ? N ILE C 345 O LEU C 373 ? O LEU C 373 
AC1 5 6 N ILE C 372 ? N ILE C 372 O VAL C 390 ? O VAL C 390 
AC1 6 7 N ILE C 389 ? N ILE C 389 O ILE C 405 ? O ILE C 405 
AC2 1 2 N GLU C 334 ? N GLU C 334 O ILE C 352 ? O ILE C 352 
AC2 2 3 N SER C 351 ? N SER C 351 O VAL C 379 ? O VAL C 379 
AC2 3 4 N THR C 378 ? N THR C 378 O LEU C 396 ? O LEU C 396 
AC3 1 2 O LYS D 74  ? O LYS D 74  N VAL D 49  ? N VAL D 49  
AC3 2 3 O VAL D 50  ? O VAL D 50  N ILE D 5   ? N ILE D 5   
AC3 3 4 N LEU D 6   ? N LEU D 6   O LEU D 108 ? O LEU D 108 
AC3 4 5 N PHE D 105 ? N PHE D 105 O LEU D 179 ? O LEU D 179 
AC3 5 6 O LEU D 178 ? O LEU D 178 N SER D 133 ? N SER D 133 
AC3 6 7 N VAL D 136 ? N VAL D 136 O MET D 211 ? O MET D 211 
AC4 1 2 N PHE D 28  ? N PHE D 28  O LYS D 31  ? O LYS D 31  
AC5 1 2 N ILE D 113 ? N ILE D 113 O MET D 218 ? O MET D 218 
AC6 1 2 N VAL D 147 ? N VAL D 147 O VAL D 161 ? O VAL D 161 
AC7 1 2 N LEU D 256 ? N LEU D 256 O VAL D 273 ? O VAL D 273 
AC7 2 3 N ALA D 274 ? N ALA D 274 O VAL D 292 ? O VAL D 292 
AC7 3 4 N THR D 291 ? N THR D 291 O ILE D 309 ? O ILE D 309 
AC8 1 2 N THR D 262 ? N THR D 262 O VAL D 281 ? O VAL D 281 
AC8 2 3 N ILE D 280 ? N ILE D 280 O ILE D 298 ? O ILE D 298 
AC8 3 4 N ARG D 297 ? N ARG D 297 O VAL D 315 ? O VAL D 315 
AC8 4 5 N THR D 314 ? N THR D 314 O VAL D 333 ? O VAL D 333 
AC8 5 6 N HIS D 332 ? N HIS D 332 O ILE D 350 ? O ILE D 350 
AC9 1 2 N LEU D 268 ? N LEU D 268 O LEU D 287 ? O LEU D 287 
AC9 2 3 N ARG D 286 ? N ARG D 286 O ILE D 304 ? O ILE D 304 
AC9 3 4 N CYS D 303 ? N CYS D 303 O ILE D 321 ? O ILE D 321 
AC9 4 5 N ARG D 320 ? N ARG D 320 O SER D 339 ? O SER D 339 
AD1 1 2 N VAL D 343 ? N VAL D 343 O VAL D 360 ? O VAL D 360 
AD2 1 2 O LYS E 74  ? O LYS E 74  N VAL E 49  ? N VAL E 49  
AD2 2 3 O ALA E 52  ? O ALA E 52  N ILE E 5   ? N ILE E 5   
AD2 3 4 N LEU E 6   ? N LEU E 6   O LEU E 108 ? O LEU E 108 
AD2 4 5 N PHE E 105 ? N PHE E 105 O LEU E 179 ? O LEU E 179 
AD2 5 6 O LEU E 178 ? O LEU E 178 N SER E 133 ? N SER E 133 
AD2 6 7 N ALA E 132 ? N ALA E 132 O TYR E 209 ? O TYR E 209 
AD3 1 2 N PHE E 28  ? N PHE E 28  O LYS E 31  ? O LYS E 31  
AD4 1 2 N ILE E 113 ? N ILE E 113 O MET E 218 ? O MET E 218 
AD5 1 2 N VAL E 147 ? N VAL E 147 O VAL E 161 ? O VAL E 161 
AD6 1 2 N LEU E 256 ? N LEU E 256 O VAL E 273 ? O VAL E 273 
AD6 2 3 N ALA E 274 ? N ALA E 274 O VAL E 292 ? O VAL E 292 
AD6 3 4 N THR E 291 ? N THR E 291 O ILE E 309 ? O ILE E 309 
AD7 1 2 N THR E 262 ? N THR E 262 O VAL E 281 ? O VAL E 281 
AD7 2 3 N ILE E 280 ? N ILE E 280 O ILE E 298 ? O ILE E 298 
AD7 3 4 N ARG E 297 ? N ARG E 297 O VAL E 315 ? O VAL E 315 
AD7 4 5 N THR E 314 ? N THR E 314 O VAL E 333 ? O VAL E 333 
AD7 5 6 N HIS E 332 ? N HIS E 332 O ILE E 350 ? O ILE E 350 
AD8 1 2 N LEU E 268 ? N LEU E 268 O LEU E 287 ? O LEU E 287 
AD8 2 3 N ARG E 286 ? N ARG E 286 O ILE E 304 ? O ILE E 304 
AD8 3 4 N SER E 305 ? N SER E 305 O ILE E 321 ? O ILE E 321 
AD8 4 5 N ARG E 320 ? N ARG E 320 O SER E 339 ? O SER E 339 
AD9 1 2 N VAL E 343 ? N VAL E 343 O VAL E 360 ? O VAL E 360 
AE1 1 2 O LYS F 74  ? O LYS F 74  N VAL F 49  ? N VAL F 49  
AE1 2 3 O ALA F 52  ? O ALA F 52  N ILE F 5   ? N ILE F 5   
AE1 3 4 N LEU F 6   ? N LEU F 6   O LEU F 108 ? O LEU F 108 
AE1 4 5 N PHE F 105 ? N PHE F 105 O LEU F 179 ? O LEU F 179 
AE1 5 6 O LEU F 178 ? O LEU F 178 N SER F 133 ? N SER F 133 
AE1 6 7 N ALA F 132 ? N ALA F 132 O TYR F 209 ? O TYR F 209 
AE2 1 2 N PHE F 28  ? N PHE F 28  O LYS F 31  ? O LYS F 31  
AE3 1 2 N ILE F 113 ? N ILE F 113 O MET F 218 ? O MET F 218 
AE4 1 2 N VAL F 147 ? N VAL F 147 O VAL F 161 ? O VAL F 161 
AE5 1 2 N LEU F 256 ? N LEU F 256 O VAL F 273 ? O VAL F 273 
AE5 2 3 N ALA F 274 ? N ALA F 274 O VAL F 292 ? O VAL F 292 
AE5 3 4 N THR F 291 ? N THR F 291 O ILE F 309 ? O ILE F 309 
AE6 1 2 N THR F 262 ? N THR F 262 O VAL F 281 ? O VAL F 281 
AE6 2 3 N ILE F 280 ? N ILE F 280 O ILE F 298 ? O ILE F 298 
AE6 3 4 N ARG F 297 ? N ARG F 297 O VAL F 315 ? O VAL F 315 
AE6 4 5 N THR F 314 ? N THR F 314 O VAL F 333 ? O VAL F 333 
AE6 5 6 N HIS F 332 ? N HIS F 332 O ILE F 350 ? O ILE F 350 
AE7 1 2 N LEU F 268 ? N LEU F 268 O LEU F 287 ? O LEU F 287 
AE7 2 3 N ARG F 286 ? N ARG F 286 O ILE F 304 ? O ILE F 304 
AE7 3 4 N CYS F 303 ? N CYS F 303 O ILE F 321 ? O ILE F 321 
AE7 4 5 N ARG F 320 ? N ARG F 320 O SER F 339 ? O SER F 339 
AE8 1 2 N VAL F 343 ? N VAL F 343 O GLU F 358 ? O GLU F 358 
# 
_pdbx_entry_details.entry_id                   8YRE 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 ALA A 55  ? ? -127.27 -100.44 
2  1 SER A 94  ? ? -123.07 -56.16  
3  1 PHE A 101 ? ? 39.09   53.71   
4  1 PHE A 124 ? ? 55.96   71.59   
5  1 THR A 141 ? ? -147.94 -11.28  
6  1 MET A 142 ? ? 54.69   -155.40 
7  1 PHE A 155 ? ? -115.61 -81.29  
8  1 PRO A 174 ? ? -65.95  98.37   
9  1 THR A 176 ? ? 46.64   72.72   
10 1 PHE A 177 ? ? 71.81   131.37  
11 1 VAL A 178 ? ? -116.63 -169.41 
12 1 ASP A 226 ? ? -94.70  40.32   
13 1 GLN A 227 ? ? -145.99 -43.38  
14 1 ALA A 234 ? ? -108.51 -72.27  
15 1 GLN A 238 ? ? -135.98 -31.26  
16 1 ASP A 246 ? ? -148.37 -121.39 
17 1 SER A 272 ? ? 41.36   75.68   
18 1 ASN A 283 ? ? -110.61 58.07   
19 1 ARG A 284 ? ? 68.75   -3.60   
20 1 GLU A 382 ? ? 65.48   -3.11   
21 1 ALA B 55  ? ? -127.10 -101.12 
22 1 SER B 94  ? ? -122.30 -56.55  
23 1 PHE B 101 ? ? 39.06   51.66   
24 1 PHE B 124 ? ? 56.10   71.96   
25 1 THR B 141 ? ? -147.67 -12.55  
26 1 MET B 142 ? ? 54.87   -156.99 
27 1 PHE B 155 ? ? -116.33 -81.88  
28 1 PRO B 174 ? ? -65.93  98.40   
29 1 THR B 176 ? ? 47.53   72.29   
30 1 PHE B 177 ? ? 71.91   131.36  
31 1 ASP B 180 ? ? 73.40   -2.28   
32 1 ASP B 226 ? ? -94.51  40.48   
33 1 GLN B 227 ? ? -146.06 -43.27  
34 1 ALA B 234 ? ? -109.43 -73.05  
35 1 GLN B 238 ? ? -135.54 -30.85  
36 1 ASP B 246 ? ? -147.69 -121.88 
37 1 SER B 272 ? ? 41.78   75.40   
38 1 ASN B 283 ? ? -109.81 57.19   
39 1 ARG B 284 ? ? 68.89   -3.84   
40 1 GLU B 382 ? ? 65.02   -2.97   
41 1 ALA C 55  ? ? -127.63 -101.11 
42 1 SER C 94  ? ? -122.28 -56.99  
43 1 PHE C 101 ? ? 39.34   52.96   
44 1 MET C 106 ? ? -85.87  30.16   
45 1 PHE C 124 ? ? 56.07   72.10   
46 1 PHE C 155 ? ? -116.19 -82.18  
47 1 PRO C 174 ? ? -66.20  98.61   
48 1 THR C 176 ? ? 46.62   72.17   
49 1 PHE C 177 ? ? 72.40   131.39  
50 1 ASP C 180 ? ? 73.83   -1.94   
51 1 ASP C 226 ? ? -93.77  40.64   
52 1 GLN C 227 ? ? -145.48 -43.25  
53 1 ALA C 234 ? ? -108.85 -71.90  
54 1 GLN C 238 ? ? -135.35 -30.96  
55 1 ASP C 246 ? ? -148.51 -120.84 
56 1 SER C 272 ? ? 42.17   78.42   
57 1 ASN C 283 ? ? -110.41 57.67   
58 1 ARG C 284 ? ? 68.89   -3.42   
59 1 GLU C 382 ? ? 65.48   -3.20   
60 1 ASN D 30  ? ? 76.57   -45.50  
61 1 TYR D 116 ? ? 52.31   74.22   
62 1 GLU D 152 ? ? -86.06  34.75   
63 1 GLU D 158 ? ? -130.25 -50.19  
64 1 LYS D 163 ? ? 47.53   71.25   
65 1 PRO D 214 ? ? -88.40  40.18   
66 1 ARG D 289 ? ? 59.88   17.49   
67 1 TRP D 318 ? ? 58.11   16.72   
68 1 ASN D 323 ? ? 62.71   60.50   
69 1 ASN D 340 ? ? -115.21 62.31   
70 1 ASN E 30  ? ? 76.10   -45.96  
71 1 LEU E 84  ? ? -99.82  58.73   
72 1 TYR E 116 ? ? 53.16   74.70   
73 1 GLU E 152 ? ? -85.83  35.16   
74 1 GLU E 158 ? ? -130.34 -50.85  
75 1 LYS E 163 ? ? 47.81   71.27   
76 1 PRO E 214 ? ? -89.27  39.74   
77 1 ASP E 272 ? ? 57.14   70.86   
78 1 ARG E 289 ? ? 59.53   17.42   
79 1 TRP E 318 ? ? 57.59   17.10   
80 1 ASN E 323 ? ? 63.05   60.62   
81 1 ASN E 340 ? ? -117.67 61.73   
82 1 ASN F 30  ? ? 77.51   -45.81  
83 1 LEU F 84  ? ? -101.05 56.87   
84 1 TYR F 116 ? ? 52.71   74.83   
85 1 GLU F 158 ? ? -130.45 -50.95  
86 1 LYS F 163 ? ? 47.88   71.48   
87 1 PRO F 214 ? ? -89.19  40.05   
88 1 TRP F 318 ? ? 57.59   16.25   
89 1 ASN F 323 ? ? 62.71   62.06   
90 1 ASN F 340 ? ? -116.21 63.59   
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         26.7016 
_pdbx_refine_tls.origin_y         -31.6623 
_pdbx_refine_tls.origin_z         35.7332 
_pdbx_refine_tls.T[1][1]          0.5464 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0403 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0667 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.9514 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0340 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.8298 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.6039 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0146 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0628 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.7109 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.1185 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.4541 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0121 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0093 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.1018 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.3724 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0468 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.1192 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.1203 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0365 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0525 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A GLU 3   ? A GLU 3   
4  1 Y 1 A ASP 206 ? A ASP 206 
5  1 Y 1 A THR 207 ? A THR 207 
6  1 Y 1 A SER 208 ? A SER 208 
7  1 Y 1 A SER 209 ? A SER 209 
8  1 Y 1 A ASN 210 ? A ASN 210 
9  1 Y 1 A TYR 211 ? A TYR 211 
10 1 Y 1 A GLN 212 ? A GLN 212 
11 1 Y 1 A SER 213 ? A SER 213 
12 1 Y 1 A ALA 214 ? A ALA 214 
13 1 Y 1 A THR 215 ? A THR 215 
14 1 Y 1 A ARG 216 ? A ARG 216 
15 1 Y 1 A SER 217 ? A SER 217 
16 1 Y 1 A VAL 218 ? A VAL 218 
17 1 Y 1 A PRO 219 ? A PRO 219 
18 1 Y 1 A ALA 220 ? A ALA 220 
19 1 Y 1 A ASP 221 ? A ASP 221 
20 1 Y 1 B MET 1   ? B MET 1   
21 1 Y 1 B SER 2   ? B SER 2   
22 1 Y 1 B GLU 3   ? B GLU 3   
23 1 Y 1 B ASP 206 ? B ASP 206 
24 1 Y 1 B THR 207 ? B THR 207 
25 1 Y 1 B SER 208 ? B SER 208 
26 1 Y 1 B SER 209 ? B SER 209 
27 1 Y 1 B ASN 210 ? B ASN 210 
28 1 Y 1 B TYR 211 ? B TYR 211 
29 1 Y 1 B GLN 212 ? B GLN 212 
30 1 Y 1 B SER 213 ? B SER 213 
31 1 Y 1 B ALA 214 ? B ALA 214 
32 1 Y 1 B THR 215 ? B THR 215 
33 1 Y 1 B ARG 216 ? B ARG 216 
34 1 Y 1 B SER 217 ? B SER 217 
35 1 Y 1 B VAL 218 ? B VAL 218 
36 1 Y 1 B PRO 219 ? B PRO 219 
37 1 Y 1 B ALA 220 ? B ALA 220 
38 1 Y 1 B ASP 221 ? B ASP 221 
39 1 Y 1 C MET 1   ? C MET 1   
40 1 Y 1 C SER 2   ? C SER 2   
41 1 Y 1 C GLU 3   ? C GLU 3   
42 1 Y 1 C MET 142 ? C MET 142 
43 1 Y 1 C LEU 143 ? C LEU 143 
44 1 Y 1 C VAL 186 ? C VAL 186 
45 1 Y 1 C TYR 187 ? C TYR 187 
46 1 Y 1 C ASP 206 ? C ASP 206 
47 1 Y 1 C THR 207 ? C THR 207 
48 1 Y 1 C SER 208 ? C SER 208 
49 1 Y 1 C SER 209 ? C SER 209 
50 1 Y 1 C ASN 210 ? C ASN 210 
51 1 Y 1 C TYR 211 ? C TYR 211 
52 1 Y 1 C GLN 212 ? C GLN 212 
53 1 Y 1 C SER 213 ? C SER 213 
54 1 Y 1 C ALA 214 ? C ALA 214 
55 1 Y 1 C THR 215 ? C THR 215 
56 1 Y 1 C ARG 216 ? C ARG 216 
57 1 Y 1 C SER 217 ? C SER 217 
58 1 Y 1 C VAL 218 ? C VAL 218 
59 1 Y 1 C PRO 219 ? C PRO 219 
60 1 Y 1 C ALA 220 ? C ALA 220 
61 1 Y 1 C ASP 221 ? C ASP 221 
62 1 Y 1 C TYR 242 ? C TYR 242 
63 1 Y 1 C GLU 243 ? C GLU 243 
64 1 Y 1 E ALA 210 ? E ALA 210 
65 1 Y 1 E MET 211 ? E MET 211 
66 1 Y 1 F GLU 151 ? F GLU 151 
67 1 Y 1 F GLU 152 ? F GLU 152 
68 1 Y 1 F SER 153 ? F SER 153 
69 1 Y 1 F THR 154 ? F THR 154 
70 1 Y 1 F GLY 155 ? F GLY 155 
71 1 Y 1 F ALA 210 ? F ALA 210 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
SO4 S    S N N 304 
SO4 O1   O N N 305 
SO4 O2   O N N 306 
SO4 O3   O N N 307 
SO4 O4   O N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TRP N    N N N 326 
TRP CA   C N S 327 
TRP C    C N N 328 
TRP O    O N N 329 
TRP CB   C N N 330 
TRP CG   C Y N 331 
TRP CD1  C Y N 332 
TRP CD2  C Y N 333 
TRP NE1  N Y N 334 
TRP CE2  C Y N 335 
TRP CE3  C Y N 336 
TRP CZ2  C Y N 337 
TRP CZ3  C Y N 338 
TRP CH2  C Y N 339 
TRP OXT  O N N 340 
TRP H    H N N 341 
TRP H2   H N N 342 
TRP HA   H N N 343 
TRP HB2  H N N 344 
TRP HB3  H N N 345 
TRP HD1  H N N 346 
TRP HE1  H N N 347 
TRP HE3  H N N 348 
TRP HZ2  H N N 349 
TRP HZ3  H N N 350 
TRP HH2  H N N 351 
TRP HXT  H N N 352 
TYR N    N N N 353 
TYR CA   C N S 354 
TYR C    C N N 355 
TYR O    O N N 356 
TYR CB   C N N 357 
TYR CG   C Y N 358 
TYR CD1  C Y N 359 
TYR CD2  C Y N 360 
TYR CE1  C Y N 361 
TYR CE2  C Y N 362 
TYR CZ   C Y N 363 
TYR OH   O N N 364 
TYR OXT  O N N 365 
TYR H    H N N 366 
TYR H2   H N N 367 
TYR HA   H N N 368 
TYR HB2  H N N 369 
TYR HB3  H N N 370 
TYR HD1  H N N 371 
TYR HD2  H N N 372 
TYR HE1  H N N 373 
TYR HE2  H N N 374 
TYR HH   H N N 375 
TYR HXT  H N N 376 
VAL N    N N N 377 
VAL CA   C N S 378 
VAL C    C N N 379 
VAL O    O N N 380 
VAL CB   C N N 381 
VAL CG1  C N N 382 
VAL CG2  C N N 383 
VAL OXT  O N N 384 
VAL H    H N N 385 
VAL H2   H N N 386 
VAL HA   H N N 387 
VAL HB   H N N 388 
VAL HG11 H N N 389 
VAL HG12 H N N 390 
VAL HG13 H N N 391 
VAL HG21 H N N 392 
VAL HG22 H N N 393 
VAL HG23 H N N 394 
VAL HXT  H N N 395 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7X8J 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YRE 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.006318 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003239 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007408 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006670 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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   . GLU A 1 4   ? -23.397 -67.185 15.589  1.00 91.08  ? 4   GLU A N   1 
ATOM   2     C CA  . GLU A 1 4   ? -23.195 -65.796 15.981  1.00 89.87  ? 4   GLU A CA  1 
ATOM   3     C C   . GLU A 1 4   ? -22.404 -65.024 14.938  1.00 88.66  ? 4   GLU A C   1 
ATOM   4     O O   . GLU A 1 4   ? -22.078 -65.545 13.871  1.00 88.81  ? 4   GLU A O   1 
ATOM   5     C CB  . GLU A 1 4   ? -22.462 -65.704 17.320  1.00 92.66  ? 4   GLU A CB  1 
ATOM   6     C CG  . GLU A 1 4   ? -23.219 -66.249 18.509  1.00 99.28  ? 4   GLU A CG  1 
ATOM   7     C CD  . GLU A 1 4   ? -22.441 -66.078 19.798  1.00 103.06 ? 4   GLU A CD  1 
ATOM   8     O OE1 . GLU A 1 4   ? -21.262 -65.668 19.728  1.00 100.13 ? 4   GLU A OE1 1 
ATOM   9     O OE2 . GLU A 1 4   ? -23.007 -66.344 20.878  1.00 107.71 ? 4   GLU A OE2 1 
ATOM   10    N N   . LYS A 1 5   ? -22.101 -63.770 15.265  1.00 90.24  ? 5   LYS A N   1 
ATOM   11    C CA  . LYS A 1 5   ? -21.271 -62.928 14.419  1.00 91.81  ? 5   LYS A CA  1 
ATOM   12    C C   . LYS A 1 5   ? -20.465 -61.996 15.311  1.00 97.13  ? 5   LYS A C   1 
ATOM   13    O O   . LYS A 1 5   ? -20.965 -61.518 16.332  1.00 98.68  ? 5   LYS A O   1 
ATOM   14    C CB  . LYS A 1 5   ? -22.108 -62.126 13.418  1.00 95.74  ? 5   LYS A CB  1 
ATOM   15    C CG  . LYS A 1 5   ? -21.404 -61.899 12.093  1.00 96.13  ? 5   LYS A CG  1 
ATOM   16    C CD  . LYS A 1 5   ? -22.238 -61.050 11.153  1.00 108.37 ? 5   LYS A CD  1 
ATOM   17    C CE  . LYS A 1 5   ? -21.666 -61.101 9.749   1.00 113.72 ? 5   LYS A CE  1 
ATOM   18    N NZ  . LYS A 1 5   ? -21.402 -62.508 9.332   1.00 112.11 ? 5   LYS A NZ  1 
ATOM   19    N N   . VAL A 1 6   ? -19.214 -61.754 14.925  1.00 97.18  ? 6   VAL A N   1 
ATOM   20    C CA  . VAL A 1 6   ? -18.281 -60.959 15.713  1.00 90.11  ? 6   VAL A CA  1 
ATOM   21    C C   . VAL A 1 6   ? -17.744 -59.833 14.843  1.00 88.92  ? 6   VAL A C   1 
ATOM   22    O O   . VAL A 1 6   ? -17.387 -60.049 13.680  1.00 93.62  ? 6   VAL A O   1 
ATOM   23    C CB  . VAL A 1 6   ? -17.123 -61.813 16.269  1.00 86.08  ? 6   VAL A CB  1 
ATOM   24    C CG1 . VAL A 1 6   ? -16.174 -60.954 17.092  1.00 88.35  ? 6   VAL A CG1 1 
ATOM   25    C CG2 . VAL A 1 6   ? -17.663 -62.955 17.111  1.00 91.90  ? 6   VAL A CG2 1 
ATOM   26    N N   . VAL A 1 7   ? -17.690 -58.630 15.412  1.00 85.78  ? 7   VAL A N   1 
ATOM   27    C CA  . VAL A 1 7   ? -17.111 -57.474 14.748  1.00 84.38  ? 7   VAL A CA  1 
ATOM   28    C C   . VAL A 1 7   ? -15.960 -56.959 15.605  1.00 83.17  ? 7   VAL A C   1 
ATOM   29    O O   . VAL A 1 7   ? -15.899 -57.196 16.814  1.00 83.56  ? 7   VAL A O   1 
ATOM   30    C CB  . VAL A 1 7   ? -18.162 -56.371 14.494  1.00 82.05  ? 7   VAL A CB  1 
ATOM   31    C CG1 . VAL A 1 7   ? -18.496 -55.632 15.781  1.00 82.73  ? 7   VAL A CG1 1 
ATOM   32    C CG2 . VAL A 1 7   ? -17.693 -55.419 13.413  1.00 84.02  ? 7   VAL A CG2 1 
ATOM   33    N N   . ALA A 1 8   ? -15.027 -56.263 14.959  1.00 80.85  ? 8   ALA A N   1 
ATOM   34    C CA  . ALA A 1 8   ? -13.831 -55.762 15.622  1.00 76.69  ? 8   ALA A CA  1 
ATOM   35    C C   . ALA A 1 8   ? -13.641 -54.288 15.300  1.00 77.06  ? 8   ALA A C   1 
ATOM   36    O O   . ALA A 1 8   ? -13.766 -53.880 14.140  1.00 81.52  ? 8   ALA A O   1 
ATOM   37    C CB  . ALA A 1 8   ? -12.592 -56.558 15.201  1.00 83.33  ? 8   ALA A CB  1 
ATOM   38    N N   . VAL A 1 9   ? -13.342 -53.495 16.326  1.00 78.47  ? 9   VAL A N   1 
ATOM   39    C CA  . VAL A 1 9   ? -13.091 -52.065 16.180  1.00 79.99  ? 9   VAL A CA  1 
ATOM   40    C C   . VAL A 1 9   ? -11.763 -51.747 16.853  1.00 86.61  ? 9   VAL A C   1 
ATOM   41    O O   . VAL A 1 9   ? -11.575 -52.054 18.037  1.00 86.12  ? 9   VAL A O   1 
ATOM   42    C CB  . VAL A 1 9   ? -14.217 -51.210 16.781  1.00 77.84  ? 9   VAL A CB  1 
ATOM   43    C CG1 . VAL A 1 9   ? -13.875 -49.736 16.660  1.00 79.08  ? 9   VAL A CG1 1 
ATOM   44    C CG2 . VAL A 1 9   ? -15.538 -51.514 16.094  1.00 84.61  ? 9   VAL A CG2 1 
ATOM   45    N N   . ILE A 1 10  ? -10.844 -51.143 16.104  1.00 90.86  ? 10  ILE A N   1 
ATOM   46    C CA  . ILE A 1 10  ? -9.513  -50.806 16.596  1.00 89.74  ? 10  ILE A CA  1 
ATOM   47    C C   . ILE A 1 10  ? -9.406  -49.292 16.711  1.00 88.10  ? 10  ILE A C   1 
ATOM   48    O O   . ILE A 1 10  ? -9.751  -48.565 15.772  1.00 87.11  ? 10  ILE A O   1 
ATOM   49    C CB  . ILE A 1 10  ? -8.411  -51.356 15.673  1.00 91.35  ? 10  ILE A CB  1 
ATOM   50    C CG1 . ILE A 1 10  ? -8.545  -52.872 15.508  1.00 94.24  ? 10  ILE A CG1 1 
ATOM   51    C CG2 . ILE A 1 10  ? -7.032  -50.983 16.202  1.00 89.99  ? 10  ILE A CG2 1 
ATOM   52    C CD1 . ILE A 1 10  ? -7.491  -53.481 14.606  1.00 90.75  ? 10  ILE A CD1 1 
ATOM   53    N N   . MET A 1 11  ? -8.927  -48.821 17.859  1.00 84.01  ? 11  MET A N   1 
ATOM   54    C CA  . MET A 1 11  ? -8.627  -47.407 18.027  1.00 83.76  ? 11  MET A CA  1 
ATOM   55    C C   . MET A 1 11  ? -7.318  -47.070 17.326  1.00 85.07  ? 11  MET A C   1 
ATOM   56    O O   . MET A 1 11  ? -6.386  -47.879 17.295  1.00 82.52  ? 11  MET A O   1 
ATOM   57    C CB  . MET A 1 11  ? -8.543  -47.048 19.510  1.00 86.83  ? 11  MET A CB  1 
ATOM   58    C CG  . MET A 1 11  ? -9.887  -47.037 20.219  1.00 84.72  ? 11  MET A CG  1 
ATOM   59    S SD  . MET A 1 11  ? -10.984 -45.734 19.625  1.00 70.13  ? 11  MET A SD  1 
ATOM   60    C CE  . MET A 1 11  ? -12.437 -46.037 20.627  1.00 89.11  ? 11  MET A CE  1 
ATOM   61    N N   . VAL A 1 12  ? -7.256  -45.870 16.750  1.00 89.56  ? 12  VAL A N   1 
ATOM   62    C CA  . VAL A 1 12  ? -6.115  -45.423 15.960  1.00 88.14  ? 12  VAL A CA  1 
ATOM   63    C C   . VAL A 1 12  ? -5.479  -44.170 16.554  1.00 97.64  ? 12  VAL A C   1 
ATOM   64    O O   . VAL A 1 12  ? -4.254  -44.086 16.687  1.00 99.53  ? 12  VAL A O   1 
ATOM   65    C CB  . VAL A 1 12  ? -6.513  -45.192 14.483  1.00 82.87  ? 12  VAL A CB  1 
ATOM   66    C CG1 . VAL A 1 12  ? -5.431  -44.429 13.749  1.00 87.16  ? 12  VAL A CG1 1 
ATOM   67    C CG2 . VAL A 1 12  ? -6.781  -46.524 13.796  1.00 78.12  ? 12  VAL A CG2 1 
ATOM   68    N N   . GLY A 1 13  ? -6.297  -43.193 16.933  1.00 127.48 ? 13  GLY A N   1 
ATOM   69    C CA  . GLY A 1 13  ? -5.797  -41.918 17.403  1.00 126.58 ? 13  GLY A CA  1 
ATOM   70    C C   . GLY A 1 13  ? -5.477  -40.984 16.250  1.00 125.11 ? 13  GLY A C   1 
ATOM   71    O O   . GLY A 1 13  ? -5.450  -41.365 15.081  1.00 124.54 ? 13  GLY A O   1 
ATOM   72    N N   . GLY A 1 14  ? -5.242  -39.720 16.594  1.00 95.92  ? 14  GLY A N   1 
ATOM   73    C CA  . GLY A 1 14  ? -4.979  -38.708 15.598  1.00 88.75  ? 14  GLY A CA  1 
ATOM   74    C C   . GLY A 1 14  ? -3.564  -38.168 15.638  1.00 88.21  ? 14  GLY A C   1 
ATOM   75    O O   . GLY A 1 14  ? -2.691  -38.698 16.331  1.00 82.60  ? 14  GLY A O   1 
ATOM   76    N N   . PRO A 1 15  ? -3.313  -37.088 14.889  1.00 73.99  ? 15  PRO A N   1 
ATOM   77    C CA  . PRO A 1 15  ? -1.956  -36.525 14.821  1.00 82.52  ? 15  PRO A CA  1 
ATOM   78    C C   . PRO A 1 15  ? -1.489  -35.890 16.116  1.00 80.57  ? 15  PRO A C   1 
ATOM   79    O O   . PRO A 1 15  ? -0.328  -35.476 16.202  1.00 81.86  ? 15  PRO A O   1 
ATOM   80    C CB  . PRO A 1 15  ? -2.072  -35.476 13.705  1.00 80.54  ? 15  PRO A CB  1 
ATOM   81    C CG  . PRO A 1 15  ? -3.509  -35.088 13.707  1.00 69.07  ? 15  PRO A CG  1 
ATOM   82    C CD  . PRO A 1 15  ? -4.267  -36.338 14.057  1.00 76.27  ? 15  PRO A CD  1 
ATOM   83    N N   . THR A 1 16  ? -2.351  -35.801 17.119  1.00 74.52  ? 16  THR A N   1 
ATOM   84    C CA  . THR A 1 16  ? -1.972  -35.278 18.419  1.00 75.30  ? 16  THR A CA  1 
ATOM   85    C C   . THR A 1 16  ? -1.516  -36.369 19.372  1.00 80.49  ? 16  THR A C   1 
ATOM   86    O O   . THR A 1 16  ? -0.999  -36.056 20.448  1.00 78.76  ? 16  THR A O   1 
ATOM   87    C CB  . THR A 1 16  ? -3.145  -34.526 19.041  1.00 76.47  ? 16  THR A CB  1 
ATOM   88    O OG1 . THR A 1 16  ? -4.268  -35.409 19.139  1.00 79.69  ? 16  THR A OG1 1 
ATOM   89    C CG2 . THR A 1 16  ? -3.517  -33.340 18.175  1.00 74.64  ? 16  THR A CG2 1 
ATOM   90    N N   . LYS A 1 17  ? -1.722  -37.634 19.015  1.00 81.13  ? 17  LYS A N   1 
ATOM   91    C CA  . LYS A 1 17  ? -1.231  -38.753 19.806  1.00 90.03  ? 17  LYS A CA  1 
ATOM   92    C C   . LYS A 1 17  ? 0.147   -39.208 19.349  1.00 93.75  ? 17  LYS A C   1 
ATOM   93    O O   . LYS A 1 17  ? 1.017   -39.485 20.182  1.00 93.52  ? 17  LYS A O   1 
ATOM   94    C CB  . LYS A 1 17  ? -2.216  -39.919 19.732  1.00 91.62  ? 17  LYS A CB  1 
ATOM   95    C CG  . LYS A 1 17  ? -3.656  -39.499 19.936  1.00 89.23  ? 17  LYS A CG  1 
ATOM   96    C CD  . LYS A 1 17  ? -3.861  -38.843 21.287  1.00 89.07  ? 17  LYS A CD  1 
ATOM   97    C CE  . LYS A 1 17  ? -5.300  -38.382 21.446  1.00 86.69  ? 17  LYS A CE  1 
ATOM   98    N NZ  . LYS A 1 17  ? -6.267  -39.504 21.302  1.00 84.78  ? 17  LYS A NZ  1 
ATOM   99    N N   . GLY A 1 18  ? 0.360   -39.294 18.037  1.00 98.23  ? 18  GLY A N   1 
ATOM   100   C CA  . GLY A 1 18  ? 1.663   -39.626 17.497  1.00 96.81  ? 18  GLY A CA  1 
ATOM   101   C C   . GLY A 1 18  ? 2.611   -38.446 17.541  1.00 96.79  ? 18  GLY A C   1 
ATOM   102   O O   . GLY A 1 18  ? 3.550   -38.358 16.744  1.00 98.59  ? 18  GLY A O   1 
ATOM   103   N N   . THR A 1 19  ? 2.365   -37.525 18.470  1.00 89.22  ? 19  THR A N   1 
ATOM   104   C CA  . THR A 1 19  ? 3.232   -36.374 18.668  1.00 89.13  ? 19  THR A CA  1 
ATOM   105   C C   . THR A 1 19  ? 4.476   -36.708 19.478  1.00 85.60  ? 19  THR A C   1 
ATOM   106   O O   . THR A 1 19  ? 5.249   -35.799 19.799  1.00 85.98  ? 19  THR A O   1 
ATOM   107   C CB  . THR A 1 19  ? 2.469   -35.238 19.347  1.00 84.54  ? 19  THR A CB  1 
ATOM   108   O OG1 . THR A 1 19  ? 3.291   -34.067 19.383  1.00 78.84  ? 19  THR A OG1 1 
ATOM   109   C CG2 . THR A 1 19  ? 2.103   -35.632 20.766  1.00 92.12  ? 19  THR A CG2 1 
ATOM   110   N N   . ARG A 1 20  ? 4.668   -37.974 19.849  1.00 84.76  ? 20  ARG A N   1 
ATOM   111   C CA  . ARG A 1 20  ? 5.914   -38.418 20.455  1.00 84.68  ? 20  ARG A CA  1 
ATOM   112   C C   . ARG A 1 20  ? 6.823   -39.117 19.459  1.00 86.79  ? 20  ARG A C   1 
ATOM   113   O O   . ARG A 1 20  ? 8.038   -39.165 19.674  1.00 90.77  ? 20  ARG A O   1 
ATOM   114   C CB  . ARG A 1 20  ? 5.633   -39.358 21.633  1.00 89.56  ? 20  ARG A CB  1 
ATOM   115   C CG  . ARG A 1 20  ? 4.170   -39.424 22.042  1.00 102.16 ? 20  ARG A CG  1 
ATOM   116   C CD  . ARG A 1 20  ? 4.017   -39.426 23.556  1.00 113.86 ? 20  ARG A CD  1 
ATOM   117   N NE  . ARG A 1 20  ? 5.001   -40.281 24.213  1.00 114.08 ? 20  ARG A NE  1 
ATOM   118   C CZ  . ARG A 1 20  ? 5.059   -40.480 25.526  1.00 111.67 ? 20  ARG A CZ  1 
ATOM   119   N NH1 . ARG A 1 20  ? 4.183   -39.891 26.330  1.00 117.44 ? 20  ARG A NH1 1 
ATOM   120   N NH2 . ARG A 1 20  ? 5.992   -41.271 26.036  1.00 106.14 ? 20  ARG A NH2 1 
ATOM   121   N N   . PHE A 1 21  ? 6.254   -39.662 18.385  1.00 89.13  ? 21  PHE A N   1 
ATOM   122   C CA  . PHE A 1 21  ? 6.997   -40.297 17.309  1.00 92.73  ? 21  PHE A CA  1 
ATOM   123   C C   . PHE A 1 21  ? 7.382   -39.310 16.206  1.00 102.31 ? 21  PHE A C   1 
ATOM   124   O O   . PHE A 1 21  ? 7.602   -39.732 15.065  1.00 108.96 ? 21  PHE A O   1 
ATOM   125   C CB  . PHE A 1 21  ? 6.179   -41.451 16.717  1.00 85.03  ? 21  PHE A CB  1 
ATOM   126   C CG  . PHE A 1 21  ? 5.960   -42.610 17.664  1.00 81.75  ? 21  PHE A CG  1 
ATOM   127   C CD1 . PHE A 1 21  ? 6.532   -43.846 17.404  1.00 81.81  ? 21  PHE A CD1 1 
ATOM   128   C CD2 . PHE A 1 21  ? 5.174   -42.473 18.800  1.00 84.32  ? 21  PHE A CD2 1 
ATOM   129   C CE1 . PHE A 1 21  ? 6.333   -44.916 18.259  1.00 77.95  ? 21  PHE A CE1 1 
ATOM   130   C CE2 . PHE A 1 21  ? 4.974   -43.540 19.660  1.00 83.37  ? 21  PHE A CE2 1 
ATOM   131   C CZ  . PHE A 1 21  ? 5.554   -44.762 19.389  1.00 79.17  ? 21  PHE A CZ  1 
ATOM   132   N N   . ARG A 1 22  ? 7.450   -38.008 16.525  1.00 100.65 ? 22  ARG A N   1 
ATOM   133   C CA  . ARG A 1 22  ? 7.594   -36.885 15.592  1.00 106.63 ? 22  ARG A CA  1 
ATOM   134   C C   . ARG A 1 22  ? 8.538   -37.140 14.417  1.00 120.57 ? 22  ARG A C   1 
ATOM   135   O O   . ARG A 1 22  ? 8.115   -36.964 13.265  1.00 114.74 ? 22  ARG A O   1 
ATOM   136   C CB  . ARG A 1 22  ? 8.032   -35.620 16.343  1.00 97.63  ? 22  ARG A CB  1 
ATOM   137   C CG  . ARG A 1 22  ? 7.036   -35.172 17.378  1.00 94.30  ? 22  ARG A CG  1 
ATOM   138   C CD  . ARG A 1 22  ? 5.683   -34.877 16.746  1.00 96.35  ? 22  ARG A CD  1 
ATOM   139   N NE  . ARG A 1 22  ? 5.644   -33.597 16.050  1.00 93.03  ? 22  ARG A NE  1 
ATOM   140   C CZ  . ARG A 1 22  ? 5.057   -32.507 16.538  1.00 91.44  ? 22  ARG A CZ  1 
ATOM   141   N NH1 . ARG A 1 22  ? 4.456   -32.548 17.722  1.00 91.92  ? 22  ARG A NH1 1 
ATOM   142   N NH2 . ARG A 1 22  ? 5.062   -31.377 15.843  1.00 91.75  ? 22  ARG A NH2 1 
ATOM   143   N N   . PRO A 1 23  ? 9.812   -37.514 14.639  1.00 161.03 ? 23  PRO A N   1 
ATOM   144   C CA  . PRO A 1 23  ? 10.716  -37.698 13.486  1.00 159.91 ? 23  PRO A CA  1 
ATOM   145   C C   . PRO A 1 23  ? 10.169  -38.665 12.449  1.00 159.86 ? 23  PRO A C   1 
ATOM   146   O O   . PRO A 1 23  ? 10.295  -38.419 11.242  1.00 158.90 ? 23  PRO A O   1 
ATOM   147   C CB  . PRO A 1 23  ? 12.009  -38.221 14.128  1.00 160.11 ? 23  PRO A CB  1 
ATOM   148   C CG  . PRO A 1 23  ? 11.614  -38.722 15.462  1.00 161.63 ? 23  PRO A CG  1 
ATOM   149   C CD  . PRO A 1 23  ? 10.476  -37.875 15.907  1.00 161.68 ? 23  PRO A CD  1 
ATOM   150   N N   . LEU A 1 24  ? 9.562   -39.765 12.895  1.00 121.65 ? 24  LEU A N   1 
ATOM   151   C CA  . LEU A 1 24  ? 8.921   -40.712 11.994  1.00 104.64 ? 24  LEU A CA  1 
ATOM   152   C C   . LEU A 1 24  ? 7.475   -40.349 11.704  1.00 93.74  ? 24  LEU A C   1 
ATOM   153   O O   . LEU A 1 24  ? 6.982   -40.643 10.609  1.00 90.73  ? 24  LEU A O   1 
ATOM   154   C CB  . LEU A 1 24  ? 8.967   -42.125 12.581  1.00 100.00 ? 24  LEU A CB  1 
ATOM   155   C CG  . LEU A 1 24  ? 10.218  -42.527 13.362  1.00 98.16  ? 24  LEU A CG  1 
ATOM   156   C CD1 . LEU A 1 24  ? 9.941   -43.717 14.281  1.00 89.62  ? 24  LEU A CD1 1 
ATOM   157   C CD2 . LEU A 1 24  ? 11.346  -42.842 12.392  1.00 91.35  ? 24  LEU A CD2 1 
ATOM   158   N N   . SER A 1 25  ? 6.786   -39.721 12.661  1.00 96.57  ? 25  SER A N   1 
ATOM   159   C CA  . SER A 1 25  ? 5.390   -39.350 12.454  1.00 88.51  ? 25  SER A CA  1 
ATOM   160   C C   . SER A 1 25  ? 5.236   -38.348 11.316  1.00 88.75  ? 25  SER A C   1 
ATOM   161   O O   . SER A 1 25  ? 4.178   -38.293 10.676  1.00 83.85  ? 25  SER A O   1 
ATOM   162   C CB  . SER A 1 25  ? 4.802   -38.789 13.748  1.00 88.26  ? 25  SER A CB  1 
ATOM   163   O OG  . SER A 1 25  ? 4.221   -39.818 14.529  1.00 87.35  ? 25  SER A OG  1 
ATOM   164   N N   . PHE A 1 26  ? 6.271   -37.546 11.053  1.00 89.52  ? 26  PHE A N   1 
ATOM   165   C CA  . PHE A 1 26  ? 6.204   -36.586 9.956   1.00 87.85  ? 26  PHE A CA  1 
ATOM   166   C C   . PHE A 1 26  ? 6.096   -37.291 8.611   1.00 79.65  ? 26  PHE A C   1 
ATOM   167   O O   . PHE A 1 26  ? 5.462   -36.772 7.685   1.00 74.82  ? 26  PHE A O   1 
ATOM   168   C CB  . PHE A 1 26  ? 7.420   -35.660 9.997   1.00 90.57  ? 26  PHE A CB  1 
ATOM   169   C CG  . PHE A 1 26  ? 7.379   -34.666 11.122  1.00 91.20  ? 26  PHE A CG  1 
ATOM   170   C CD1 . PHE A 1 26  ? 8.541   -34.247 11.747  1.00 96.68  ? 26  PHE A CD1 1 
ATOM   171   C CD2 . PHE A 1 26  ? 6.168   -34.149 11.555  1.00 93.37  ? 26  PHE A CD2 1 
ATOM   172   C CE1 . PHE A 1 26  ? 8.496   -33.334 12.787  1.00 93.75  ? 26  PHE A CE1 1 
ATOM   173   C CE2 . PHE A 1 26  ? 6.116   -33.237 12.593  1.00 94.83  ? 26  PHE A CE2 1 
ATOM   174   C CZ  . PHE A 1 26  ? 7.282   -32.828 13.209  1.00 90.72  ? 26  PHE A CZ  1 
ATOM   175   N N   . ASN A 1 27  ? 6.701   -38.471 8.484   1.00 78.09  ? 27  ASN A N   1 
ATOM   176   C CA  . ASN A 1 27  ? 6.587   -39.251 7.261   1.00 71.71  ? 27  ASN A CA  1 
ATOM   177   C C   . ASN A 1 27  ? 5.411   -40.224 7.328   1.00 72.71  ? 27  ASN A C   1 
ATOM   178   O O   . ASN A 1 27  ? 4.599   -40.286 6.400   1.00 73.98  ? 27  ASN A O   1 
ATOM   179   C CB  . ASN A 1 27  ? 7.892   -40.008 6.994   1.00 68.94  ? 27  ASN A CB  1 
ATOM   180   C CG  . ASN A 1 27  ? 7.868   -40.763 5.679   1.00 68.79  ? 27  ASN A CG  1 
ATOM   181   O OD1 . ASN A 1 27  ? 8.045   -40.177 4.611   1.00 70.44  ? 27  ASN A OD1 1 
ATOM   182   N ND2 . ASN A 1 27  ? 7.628   -42.066 5.748   1.00 68.15  ? 27  ASN A ND2 1 
ATOM   183   N N   . THR A 1 28  ? 5.303   -40.985 8.418   1.00 72.76  ? 28  THR A N   1 
ATOM   184   C CA  . THR A 1 28  ? 4.266   -41.998 8.569   1.00 70.65  ? 28  THR A CA  1 
ATOM   185   C C   . THR A 1 28  ? 3.632   -41.896 9.953   1.00 73.83  ? 28  THR A C   1 
ATOM   186   O O   . THR A 1 28  ? 4.356   -41.861 10.961  1.00 75.31  ? 28  THR A O   1 
ATOM   187   C CB  . THR A 1 28  ? 4.857   -43.398 8.342   1.00 70.06  ? 28  THR A CB  1 
ATOM   188   O OG1 . THR A 1 28  ? 5.155   -43.572 6.949   1.00 68.06  ? 28  THR A OG1 1 
ATOM   189   C CG2 . THR A 1 28  ? 3.890   -44.473 8.783   1.00 67.14  ? 28  THR A CG2 1 
ATOM   190   N N   . PRO A 1 29  ? 2.300   -41.862 10.051  1.00 74.98  ? 29  PRO A N   1 
ATOM   191   C CA  . PRO A 1 29  ? 1.648   -41.782 11.366  1.00 73.97  ? 29  PRO A CA  1 
ATOM   192   C C   . PRO A 1 29  ? 1.999   -42.964 12.263  1.00 73.67  ? 29  PRO A C   1 
ATOM   193   O O   . PRO A 1 29  ? 2.504   -43.995 11.815  1.00 72.96  ? 29  PRO A O   1 
ATOM   194   C CB  . PRO A 1 29  ? 0.154   -41.776 11.019  1.00 77.09  ? 29  PRO A CB  1 
ATOM   195   C CG  . PRO A 1 29  ? 0.089   -41.269 9.620   1.00 79.64  ? 29  PRO A CG  1 
ATOM   196   C CD  . PRO A 1 29  ? 1.328   -41.794 8.946   1.00 79.13  ? 29  PRO A CD  1 
ATOM   197   N N   . LYS A 1 30  ? 1.722   -42.788 13.558  1.00 71.39  ? 30  LYS A N   1 
ATOM   198   C CA  . LYS A 1 30  ? 2.045   -43.790 14.577  1.00 64.50  ? 30  LYS A CA  1 
ATOM   199   C C   . LYS A 1 30  ? 1.543   -45.198 14.262  1.00 65.05  ? 30  LYS A C   1 
ATOM   200   O O   . LYS A 1 30  ? 2.351   -46.139 14.326  1.00 64.70  ? 30  LYS A O   1 
ATOM   201   C CB  . LYS A 1 30  ? 1.499   -43.317 15.934  1.00 68.40  ? 30  LYS A CB  1 
ATOM   202   C CG  . LYS A 1 30  ? 1.792   -44.253 17.099  1.00 69.81  ? 30  LYS A CG  1 
ATOM   203   C CD  . LYS A 1 30  ? 0.654   -44.249 18.111  1.00 72.31  ? 30  LYS A CD  1 
ATOM   204   C CE  . LYS A 1 30  ? 1.170   -44.215 19.540  1.00 75.82  ? 30  LYS A CE  1 
ATOM   205   N NZ  . LYS A 1 30  ? 1.649   -42.855 19.908  1.00 85.33  ? 30  LYS A NZ  1 
ATOM   206   N N   . PRO A 1 31  ? 0.265   -45.424 13.923  1.00 71.87  ? 31  PRO A N   1 
ATOM   207   C CA  . PRO A 1 31  ? -0.201  -46.810 13.740  1.00 70.75  ? 31  PRO A CA  1 
ATOM   208   C C   . PRO A 1 31  ? 0.433   -47.516 12.560  1.00 71.89  ? 31  PRO A C   1 
ATOM   209   O O   . PRO A 1 31  ? 0.397   -48.751 12.505  1.00 73.72  ? 31  PRO A O   1 
ATOM   210   C CB  . PRO A 1 31  ? -1.716  -46.654 13.536  1.00 73.49  ? 31  PRO A CB  1 
ATOM   211   C CG  . PRO A 1 31  ? -2.037  -45.290 14.031  1.00 71.54  ? 31  PRO A CG  1 
ATOM   212   C CD  . PRO A 1 31  ? -0.837  -44.468 13.718  1.00 74.51  ? 31  PRO A CD  1 
ATOM   213   N N   . LEU A 1 32  ? 0.997   -46.779 11.610  1.00 67.99  ? 32  LEU A N   1 
ATOM   214   C CA  . LEU A 1 32  ? 1.533   -47.362 10.393  1.00 70.09  ? 32  LEU A CA  1 
ATOM   215   C C   . LEU A 1 32  ? 3.046   -47.526 10.440  1.00 65.50  ? 32  LEU A C   1 
ATOM   216   O O   . LEU A 1 32  ? 3.647   -47.924 9.437   1.00 66.30  ? 32  LEU A O   1 
ATOM   217   C CB  . LEU A 1 32  ? 1.125   -46.507 9.194   1.00 73.22  ? 32  LEU A CB  1 
ATOM   218   C CG  . LEU A 1 32  ? -0.316  -45.995 9.228   1.00 70.42  ? 32  LEU A CG  1 
ATOM   219   C CD1 . LEU A 1 32  ? -0.587  -45.085 8.043   1.00 75.31  ? 32  LEU A CD1 1 
ATOM   220   C CD2 . LEU A 1 32  ? -1.306  -47.151 9.260   1.00 74.22  ? 32  LEU A CD2 1 
ATOM   221   N N   . ILE A 1 33  ? 3.670   -47.232 11.573  1.00 67.74  ? 33  ILE A N   1 
ATOM   222   C CA  . ILE A 1 33  ? 5.125   -47.357 11.694  1.00 68.32  ? 33  ILE A CA  1 
ATOM   223   C C   . ILE A 1 33  ? 5.482   -48.837 11.822  1.00 69.59  ? 33  ILE A C   1 
ATOM   224   O O   . ILE A 1 33  ? 4.936   -49.524 12.702  1.00 77.34  ? 33  ILE A O   1 
ATOM   225   C CB  . ILE A 1 33  ? 5.636   -46.560 12.892  1.00 64.13  ? 33  ILE A CB  1 
ATOM   226   C CG1 . ILE A 1 33  ? 5.389   -45.062 12.681  1.00 63.61  ? 33  ILE A CG1 1 
ATOM   227   C CG2 . ILE A 1 33  ? 7.116   -46.830 13.122  1.00 65.76  ? 33  ILE A CG2 1 
ATOM   228   C CD1 . ILE A 1 33  ? 5.833   -44.183 13.838  1.00 67.19  ? 33  ILE A CD1 1 
ATOM   229   N N   . PRO A 1 34  ? 6.383   -49.356 10.985  1.00 65.67  ? 34  PRO A N   1 
ATOM   230   C CA  . PRO A 1 34  ? 6.634   -50.807 10.944  1.00 74.59  ? 34  PRO A CA  1 
ATOM   231   C C   . PRO A 1 34  ? 7.325   -51.308 12.204  1.00 79.01  ? 34  PRO A C   1 
ATOM   232   O O   . PRO A 1 34  ? 8.456   -50.920 12.505  1.00 78.66  ? 34  PRO A O   1 
ATOM   233   C CB  . PRO A 1 34  ? 7.526   -50.976 9.708   1.00 74.55  ? 34  PRO A CB  1 
ATOM   234   C CG  . PRO A 1 34  ? 7.333   -49.721 8.909   1.00 73.65  ? 34  PRO A CG  1 
ATOM   235   C CD  . PRO A 1 34  ? 7.102   -48.644 9.918   1.00 70.62  ? 34  PRO A CD  1 
ATOM   236   N N   . LEU A 1 35  ? 6.638   -52.177 12.941  1.00 94.46  ? 35  LEU A N   1 
ATOM   237   C CA  . LEU A 1 35  ? 7.216   -52.881 14.080  1.00 96.06  ? 35  LEU A CA  1 
ATOM   238   C C   . LEU A 1 35  ? 7.512   -54.317 13.666  1.00 97.69  ? 35  LEU A C   1 
ATOM   239   O O   . LEU A 1 35  ? 6.604   -55.043 13.247  1.00 98.70  ? 35  LEU A O   1 
ATOM   240   C CB  . LEU A 1 35  ? 6.277   -52.846 15.284  1.00 97.28  ? 35  LEU A CB  1 
ATOM   241   C CG  . LEU A 1 35  ? 6.114   -51.476 15.943  1.00 95.84  ? 35  LEU A CG  1 
ATOM   242   C CD1 . LEU A 1 35  ? 5.280   -51.575 17.211  1.00 100.80 ? 35  LEU A CD1 1 
ATOM   243   C CD2 . LEU A 1 35  ? 7.476   -50.867 16.235  1.00 95.15  ? 35  LEU A CD2 1 
ATOM   244   N N   . ALA A 1 36  ? 8.776   -54.724 13.798  1.00 85.98  ? 36  ALA A N   1 
ATOM   245   C CA  . ALA A 1 36  ? 9.236   -56.043 13.362  1.00 83.38  ? 36  ALA A CA  1 
ATOM   246   C C   . ALA A 1 36  ? 8.939   -56.278 11.885  1.00 82.78  ? 36  ALA A C   1 
ATOM   247   O O   . ALA A 1 36  ? 8.644   -57.401 11.467  1.00 86.18  ? 36  ALA A O   1 
ATOM   248   C CB  . ALA A 1 36  ? 8.631   -57.162 14.216  1.00 88.22  ? 36  ALA A CB  1 
ATOM   249   N N   . GLY A 1 37  ? 9.020   -55.214 11.084  1.00 80.34  ? 37  GLY A N   1 
ATOM   250   C CA  . GLY A 1 37  ? 8.782   -55.265 9.665   1.00 81.82  ? 37  GLY A CA  1 
ATOM   251   C C   . GLY A 1 37  ? 7.370   -54.887 9.263   1.00 82.72  ? 37  GLY A C   1 
ATOM   252   O O   . GLY A 1 37  ? 7.165   -54.387 8.150   1.00 82.86  ? 37  GLY A O   1 
ATOM   253   N N   . GLN A 1 38  ? 6.395   -55.106 10.143  1.00 82.68  ? 38  GLN A N   1 
ATOM   254   C CA  . GLN A 1 38  ? 5.009   -54.810 9.829   1.00 80.08  ? 38  GLN A CA  1 
ATOM   255   C C   . GLN A 1 38  ? 4.511   -53.614 10.635  1.00 76.00  ? 38  GLN A C   1 
ATOM   256   O O   . GLN A 1 38  ? 4.988   -53.370 11.747  1.00 78.94  ? 38  GLN A O   1 
ATOM   257   C CB  . GLN A 1 38  ? 4.121   -56.028 10.114  1.00 77.59  ? 38  GLN A CB  1 
ATOM   258   C CG  . GLN A 1 38  ? 4.626   -57.311 9.471   1.00 76.76  ? 38  GLN A CG  1 
ATOM   259   C CD  . GLN A 1 38  ? 4.700   -57.230 7.957   1.00 76.48  ? 38  GLN A CD  1 
ATOM   260   O OE1 . GLN A 1 38  ? 4.006   -56.430 7.327   1.00 75.10  ? 38  GLN A OE1 1 
ATOM   261   N NE2 . GLN A 1 38  ? 5.555   -58.056 7.365   1.00 83.76  ? 38  GLN A NE2 1 
ATOM   262   N N   . PRO A 1 39  ? 3.555   -52.852 10.104  1.00 86.49  ? 39  PRO A N   1 
ATOM   263   C CA  . PRO A 1 39  ? 3.043   -51.680 10.828  1.00 72.79  ? 39  PRO A CA  1 
ATOM   264   C C   . PRO A 1 39  ? 2.532   -52.036 12.217  1.00 77.22  ? 39  PRO A C   1 
ATOM   265   O O   . PRO A 1 39  ? 2.330   -53.199 12.568  1.00 72.68  ? 39  PRO A O   1 
ATOM   266   C CB  . PRO A 1 39  ? 1.916   -51.174 9.922   1.00 72.34  ? 39  PRO A CB  1 
ATOM   267   C CG  . PRO A 1 39  ? 2.331   -51.603 8.553   1.00 72.98  ? 39  PRO A CG  1 
ATOM   268   C CD  . PRO A 1 39  ? 3.013   -52.935 8.734   1.00 72.86  ? 39  PRO A CD  1 
ATOM   269   N N   . MET A 1 40  ? 2.337   -50.989 13.022  1.00 68.68  ? 40  MET A N   1 
ATOM   270   C CA  . MET A 1 40  ? 1.965   -51.172 14.422  1.00 76.74  ? 40  MET A CA  1 
ATOM   271   C C   . MET A 1 40  ? 0.663   -51.957 14.548  1.00 83.90  ? 40  MET A C   1 
ATOM   272   O O   . MET A 1 40  ? 0.586   -52.945 15.289  1.00 84.43  ? 40  MET A O   1 
ATOM   273   C CB  . MET A 1 40  ? 1.847   -49.808 15.106  1.00 73.54  ? 40  MET A CB  1 
ATOM   274   C CG  . MET A 1 40  ? 1.496   -49.859 16.580  1.00 74.47  ? 40  MET A CG  1 
ATOM   275   S SD  . MET A 1 40  ? 1.536   -48.216 17.324  1.00 76.84  ? 40  MET A SD  1 
ATOM   276   C CE  . MET A 1 40  ? 3.242   -47.750 17.026  1.00 77.51  ? 40  MET A CE  1 
ATOM   277   N N   . ILE A 1 41  ? -0.378  -51.526 13.826  1.00 99.05  ? 41  ILE A N   1 
ATOM   278   C CA  . ILE A 1 41  ? -1.673  -52.203 13.861  1.00 99.34  ? 41  ILE A CA  1 
ATOM   279   C C   . ILE A 1 41  ? -1.716  -53.454 12.999  1.00 99.94  ? 41  ILE A C   1 
ATOM   280   O O   . ILE A 1 41  ? -2.747  -54.137 12.972  1.00 100.73 ? 41  ILE A O   1 
ATOM   281   C CB  . ILE A 1 41  ? -2.792  -51.230 13.440  1.00 97.34  ? 41  ILE A CB  1 
ATOM   282   C CG1 . ILE A 1 41  ? -2.480  -50.615 12.074  1.00 95.49  ? 41  ILE A CG1 1 
ATOM   283   C CG2 . ILE A 1 41  ? -2.980  -50.151 14.495  1.00 96.86  ? 41  ILE A CG2 1 
ATOM   284   C CD1 . ILE A 1 41  ? -3.513  -49.610 11.605  1.00 94.03  ? 41  ILE A CD1 1 
ATOM   285   N N   . HIS A 1 42  ? -0.630  -53.780 12.291  1.00 85.25  ? 42  HIS A N   1 
ATOM   286   C CA  . HIS A 1 42  ? -0.623  -54.958 11.430  1.00 79.11  ? 42  HIS A CA  1 
ATOM   287   C C   . HIS A 1 42  ? -0.652  -56.264 12.213  1.00 81.70  ? 42  HIS A C   1 
ATOM   288   O O   . HIS A 1 42  ? -0.961  -57.311 11.635  1.00 83.67  ? 42  HIS A O   1 
ATOM   289   C CB  . HIS A 1 42  ? 0.613   -54.933 10.530  1.00 77.49  ? 42  HIS A CB  1 
ATOM   290   C CG  . HIS A 1 42  ? 0.537   -55.867 9.364   1.00 77.11  ? 42  HIS A CG  1 
ATOM   291   N ND1 . HIS A 1 42  ? -0.014  -55.506 8.154   1.00 77.35  ? 42  HIS A ND1 1 
ATOM   292   C CD2 . HIS A 1 42  ? 0.949   -57.149 9.223   1.00 77.77  ? 42  HIS A CD2 1 
ATOM   293   C CE1 . HIS A 1 42  ? 0.060   -56.526 7.318   1.00 83.05  ? 42  HIS A CE1 1 
ATOM   294   N NE2 . HIS A 1 42  ? 0.639   -57.536 7.942   1.00 81.79  ? 42  HIS A NE2 1 
ATOM   295   N N   . HIS A 1 43  ? -0.349  -56.227 13.505  1.00 83.34  ? 43  HIS A N   1 
ATOM   296   C CA  . HIS A 1 43  ? -0.359  -57.435 14.321  1.00 84.17  ? 43  HIS A CA  1 
ATOM   297   C C   . HIS A 1 43  ? -1.720  -57.687 14.971  1.00 82.72  ? 43  HIS A C   1 
ATOM   298   O O   . HIS A 1 43  ? -2.157  -58.845 15.025  1.00 84.41  ? 43  HIS A O   1 
ATOM   299   C CB  . HIS A 1 43  ? 0.756   -57.373 15.366  1.00 86.37  ? 43  HIS A CB  1 
ATOM   300   C CG  . HIS A 1 43  ? 2.121   -57.208 14.774  1.00 89.87  ? 43  HIS A CG  1 
ATOM   301   N ND1 . HIS A 1 43  ? 2.509   -56.069 14.102  1.00 86.85  ? 43  HIS A ND1 1 
ATOM   302   C CD2 . HIS A 1 43  ? 3.181   -58.049 14.731  1.00 96.94  ? 43  HIS A CD2 1 
ATOM   303   C CE1 . HIS A 1 43  ? 3.753   -56.210 13.681  1.00 86.85  ? 43  HIS A CE1 1 
ATOM   304   N NE2 . HIS A 1 43  ? 4.184   -57.403 14.050  1.00 92.74  ? 43  HIS A NE2 1 
ATOM   305   N N   . PRO A 1 44  ? -2.414  -56.665 15.493  1.00 85.76  ? 44  PRO A N   1 
ATOM   306   C CA  . PRO A 1 44  ? -3.805  -56.902 15.925  1.00 81.79  ? 44  PRO A CA  1 
ATOM   307   C C   . PRO A 1 44  ? -4.685  -57.423 14.803  1.00 80.93  ? 44  PRO A C   1 
ATOM   308   O O   . PRO A 1 44  ? -5.459  -58.368 15.009  1.00 82.28  ? 44  PRO A O   1 
ATOM   309   C CB  . PRO A 1 44  ? -4.252  -55.524 16.427  1.00 85.20  ? 44  PRO A CB  1 
ATOM   310   C CG  . PRO A 1 44  ? -3.004  -54.884 16.886  1.00 88.07  ? 44  PRO A CG  1 
ATOM   311   C CD  . PRO A 1 44  ? -1.941  -55.337 15.928  1.00 86.89  ? 44  PRO A CD  1 
ATOM   312   N N   . ILE A 1 45  ? -4.596  -56.816 13.617  1.00 81.22  ? 45  ILE A N   1 
ATOM   313   C CA  . ILE A 1 45  ? -5.376  -57.284 12.476  1.00 80.64  ? 45  ILE A CA  1 
ATOM   314   C C   . ILE A 1 45  ? -4.997  -58.715 12.126  1.00 84.67  ? 45  ILE A C   1 
ATOM   315   O O   . ILE A 1 45  ? -5.846  -59.503 11.691  1.00 88.53  ? 45  ILE A O   1 
ATOM   316   C CB  . ILE A 1 45  ? -5.183  -56.333 11.278  1.00 80.30  ? 45  ILE A CB  1 
ATOM   317   C CG1 . ILE A 1 45  ? -5.547  -54.905 11.669  1.00 78.83  ? 45  ILE A CG1 1 
ATOM   318   C CG2 . ILE A 1 45  ? -6.025  -56.777 10.091  1.00 95.23  ? 45  ILE A CG2 1 
ATOM   319   C CD1 . ILE A 1 45  ? -5.292  -53.904 10.574  1.00 85.25  ? 45  ILE A CD1 1 
ATOM   320   N N   . SER A 1 46  ? -3.725  -59.075 12.311  1.00 79.16  ? 46  SER A N   1 
ATOM   321   C CA  . SER A 1 46  ? -3.290  -60.439 12.032  1.00 81.07  ? 46  SER A CA  1 
ATOM   322   C C   . SER A 1 46  ? -3.975  -61.439 12.951  1.00 81.68  ? 46  SER A C   1 
ATOM   323   O O   . SER A 1 46  ? -4.180  -62.597 12.568  1.00 85.25  ? 46  SER A O   1 
ATOM   324   C CB  . SER A 1 46  ? -1.771  -60.541 12.176  1.00 81.50  ? 46  SER A CB  1 
ATOM   325   O OG  . SER A 1 46  ? -1.112  -59.951 11.067  1.00 85.17  ? 46  SER A OG  1 
ATOM   326   N N   . ALA A 1 47  ? -4.337  -61.013 14.159  1.00 80.56  ? 47  ALA A N   1 
ATOM   327   C CA  . ALA A 1 47  ? -5.023  -61.879 15.103  1.00 86.84  ? 47  ALA A CA  1 
ATOM   328   C C   . ALA A 1 47  ? -6.521  -61.943 14.847  1.00 94.97  ? 47  ALA A C   1 
ATOM   329   O O   . ALA A 1 47  ? -7.193  -62.815 15.407  1.00 101.16 ? 47  ALA A O   1 
ATOM   330   C CB  . ALA A 1 47  ? -4.760  -61.405 16.535  1.00 89.83  ? 47  ALA A CB  1 
ATOM   331   N N   . CYS A 1 48  ? -7.055  -61.039 14.022  1.00 90.19  ? 48  CYS A N   1 
ATOM   332   C CA  . CYS A 1 48  ? -8.483  -61.036 13.732  1.00 91.65  ? 48  CYS A CA  1 
ATOM   333   C C   . CYS A 1 48  ? -8.881  -62.145 12.768  1.00 97.85  ? 48  CYS A C   1 
ATOM   334   O O   . CYS A 1 48  ? -10.040 -62.574 12.771  1.00 102.21 ? 48  CYS A O   1 
ATOM   335   C CB  . CYS A 1 48  ? -8.898  -59.679 13.159  1.00 91.24  ? 48  CYS A CB  1 
ATOM   336   S SG  . CYS A 1 48  ? -8.700  -58.302 14.310  1.00 83.69  ? 48  CYS A SG  1 
ATOM   337   N N   . LYS A 1 49  ? -7.950  -62.617 11.935  1.00 99.92  ? 49  LYS A N   1 
ATOM   338   C CA  . LYS A 1 49  ? -8.293  -63.664 10.981  1.00 110.39 ? 49  LYS A CA  1 
ATOM   339   C C   . LYS A 1 49  ? -8.492  -65.015 11.657  1.00 112.36 ? 49  LYS A C   1 
ATOM   340   O O   . LYS A 1 49  ? -9.207  -65.866 11.116  1.00 113.44 ? 49  LYS A O   1 
ATOM   341   C CB  . LYS A 1 49  ? -7.221  -63.762 9.891   1.00 115.59 ? 49  LYS A CB  1 
ATOM   342   C CG  . LYS A 1 49  ? -7.628  -64.634 8.711   1.00 122.51 ? 49  LYS A CG  1 
ATOM   343   C CD  . LYS A 1 49  ? -9.052  -64.314 8.269   1.00 128.46 ? 49  LYS A CD  1 
ATOM   344   C CE  . LYS A 1 49  ? -9.594  -65.364 7.310   1.00 127.74 ? 49  LYS A CE  1 
ATOM   345   N NZ  . LYS A 1 49  ? -10.413 -64.759 6.222   1.00 132.99 ? 49  LYS A NZ  1 
ATOM   346   N N   . LYS A 1 50  ? -7.896  -65.227 12.830  1.00 126.78 ? 50  LYS A N   1 
ATOM   347   C CA  . LYS A 1 50  ? -8.062  -66.498 13.522  1.00 129.39 ? 50  LYS A CA  1 
ATOM   348   C C   . LYS A 1 50  ? -9.471  -66.695 14.070  1.00 129.96 ? 50  LYS A C   1 
ATOM   349   O O   . LYS A 1 50  ? -9.801  -67.811 14.486  1.00 132.19 ? 50  LYS A O   1 
ATOM   350   C CB  . LYS A 1 50  ? -7.035  -66.624 14.648  1.00 130.73 ? 50  LYS A CB  1 
ATOM   351   C CG  . LYS A 1 50  ? -7.463  -66.003 15.960  1.00 131.33 ? 50  LYS A CG  1 
ATOM   352   C CD  . LYS A 1 50  ? -6.583  -66.498 17.095  1.00 133.66 ? 50  LYS A CD  1 
ATOM   353   C CE  . LYS A 1 50  ? -6.456  -65.466 18.203  1.00 133.00 ? 50  LYS A CE  1 
ATOM   354   N NZ  . LYS A 1 50  ? -5.926  -64.173 17.694  1.00 130.42 ? 50  LYS A NZ  1 
ATOM   355   N N   . ILE A 1 51  ? -10.305 -65.658 14.078  1.00 114.32 ? 51  ILE A N   1 
ATOM   356   C CA  . ILE A 1 51  ? -11.703 -65.787 14.472  1.00 108.05 ? 51  ILE A CA  1 
ATOM   357   C C   . ILE A 1 51  ? -12.516 -66.048 13.209  1.00 103.64 ? 51  ILE A C   1 
ATOM   358   O O   . ILE A 1 51  ? -12.703 -65.151 12.383  1.00 99.79  ? 51  ILE A O   1 
ATOM   359   C CB  . ILE A 1 51  ? -12.205 -64.540 15.206  1.00 103.75 ? 51  ILE A CB  1 
ATOM   360   C CG1 . ILE A 1 51  ? -11.356 -64.270 16.447  1.00 107.06 ? 51  ILE A CG1 1 
ATOM   361   C CG2 . ILE A 1 51  ? -13.671 -64.700 15.582  1.00 101.18 ? 51  ILE A CG2 1 
ATOM   362   C CD1 . ILE A 1 51  ? -10.262 -63.255 16.221  1.00 111.25 ? 51  ILE A CD1 1 
ATOM   363   N N   . SER A 1 52  ? -12.996 -67.284 13.056  1.00 100.71 ? 52  SER A N   1 
ATOM   364   C CA  . SER A 1 52  ? -13.717 -67.650 11.842  1.00 100.18 ? 52  SER A CA  1 
ATOM   365   C C   . SER A 1 52  ? -15.073 -66.963 11.757  1.00 99.35  ? 52  SER A C   1 
ATOM   366   O O   . SER A 1 52  ? -15.593 -66.754 10.655  1.00 99.77  ? 52  SER A O   1 
ATOM   367   C CB  . SER A 1 52  ? -13.886 -69.167 11.772  1.00 101.21 ? 52  SER A CB  1 
ATOM   368   O OG  . SER A 1 52  ? -14.610 -69.647 12.892  1.00 105.06 ? 52  SER A OG  1 
ATOM   369   N N   . ASN A 1 53  ? -15.663 -66.611 12.900  1.00 98.61  ? 53  ASN A N   1 
ATOM   370   C CA  . ASN A 1 53  ? -16.950 -65.932 12.942  1.00 96.32  ? 53  ASN A CA  1 
ATOM   371   C C   . ASN A 1 53  ? -16.811 -64.415 13.009  1.00 97.64  ? 53  ASN A C   1 
ATOM   372   O O   . ASN A 1 53  ? -17.775 -63.726 13.366  1.00 96.51  ? 53  ASN A O   1 
ATOM   373   C CB  . ASN A 1 53  ? -17.775 -66.437 14.126  1.00 95.06  ? 53  ASN A CB  1 
ATOM   374   C CG  . ASN A 1 53  ? -16.943 -66.614 15.379  1.00 94.76  ? 53  ASN A CG  1 
ATOM   375   O OD1 . ASN A 1 53  ? -15.839 -67.158 15.335  1.00 97.85  ? 53  ASN A OD1 1 
ATOM   376   N ND2 . ASN A 1 53  ? -17.468 -66.154 16.507  1.00 88.52  ? 53  ASN A ND2 1 
ATOM   377   N N   . LEU A 1 54  ? -15.639 -63.883 12.675  1.00 98.76  ? 54  LEU A N   1 
ATOM   378   C CA  . LEU A 1 54  ? -15.420 -62.448 12.617  1.00 99.34  ? 54  LEU A CA  1 
ATOM   379   C C   . LEU A 1 54  ? -15.609 -61.969 11.184  1.00 100.60 ? 54  LEU A C   1 
ATOM   380   O O   . LEU A 1 54  ? -15.286 -62.676 10.226  1.00 99.53  ? 54  LEU A O   1 
ATOM   381   C CB  . LEU A 1 54  ? -14.020 -62.086 13.118  1.00 97.79  ? 54  LEU A CB  1 
ATOM   382   C CG  . LEU A 1 54  ? -13.818 -60.651 13.614  1.00 93.29  ? 54  LEU A CG  1 
ATOM   383   C CD1 . LEU A 1 54  ? -12.908 -60.642 14.835  1.00 87.44  ? 54  LEU A CD1 1 
ATOM   384   C CD2 . LEU A 1 54  ? -13.249 -59.768 12.518  1.00 94.53  ? 54  LEU A CD2 1 
ATOM   385   N N   . ALA A 1 55  ? -16.129 -60.751 11.048  1.00 113.29 ? 55  ALA A N   1 
ATOM   386   C CA  . ALA A 1 55  ? -16.424 -60.201 9.732   1.00 111.86 ? 55  ALA A CA  1 
ATOM   387   C C   . ALA A 1 55  ? -15.782 -58.833 9.554   1.00 112.11 ? 55  ALA A C   1 
ATOM   388   O O   . ALA A 1 55  ? -14.583 -58.732 9.276   1.00 123.27 ? 55  ALA A O   1 
ATOM   389   C CB  . ALA A 1 55  ? -17.937 -60.108 9.523   1.00 115.31 ? 55  ALA A CB  1 
ATOM   390   N N   . GLN A 1 56  ? -16.574 -57.777 9.713   1.00 101.59 ? 56  GLN A N   1 
ATOM   391   C CA  . GLN A 1 56  ? -16.085 -56.430 9.468   1.00 96.02  ? 56  GLN A CA  1 
ATOM   392   C C   . GLN A 1 56  ? -15.055 -56.022 10.516  1.00 91.91  ? 56  GLN A C   1 
ATOM   393   O O   . GLN A 1 56  ? -15.099 -56.457 11.670  1.00 88.21  ? 56  GLN A O   1 
ATOM   394   C CB  . GLN A 1 56  ? -17.246 -55.437 9.466   1.00 91.24  ? 56  GLN A CB  1 
ATOM   395   N N   . ILE A 1 57  ? -14.113 -55.182 10.093  1.00 95.15  ? 57  ILE A N   1 
ATOM   396   C CA  . ILE A 1 57  ? -13.105 -54.595 10.966  1.00 91.13  ? 57  ILE A CA  1 
ATOM   397   C C   . ILE A 1 57  ? -13.180 -53.085 10.806  1.00 87.94  ? 57  ILE A C   1 
ATOM   398   O O   . ILE A 1 57  ? -13.337 -52.577 9.690   1.00 93.00  ? 57  ILE A O   1 
ATOM   399   C CB  . ILE A 1 57  ? -11.687 -55.116 10.643  1.00 93.15  ? 57  ILE A CB  1 
ATOM   400   C CG1 . ILE A 1 57  ? -11.671 -56.647 10.616  1.00 101.63 ? 57  ILE A CG1 1 
ATOM   401   C CG2 . ILE A 1 57  ? -10.672 -54.580 11.645  1.00 84.72  ? 57  ILE A CG2 1 
ATOM   402   C CD1 . ILE A 1 57  ? -10.282 -57.243 10.684  1.00 108.10 ? 57  ILE A CD1 1 
ATOM   403   N N   . PHE A 1 58  ? -13.062 -52.367 11.920  1.00 82.63  ? 58  PHE A N   1 
ATOM   404   C CA  . PHE A 1 58  ? -13.289 -50.928 11.947  1.00 81.08  ? 58  PHE A CA  1 
ATOM   405   C C   . PHE A 1 58  ? -12.092 -50.252 12.594  1.00 76.09  ? 58  PHE A C   1 
ATOM   406   O O   . PHE A 1 58  ? -11.768 -50.534 13.751  1.00 79.74  ? 58  PHE A O   1 
ATOM   407   C CB  . PHE A 1 58  ? -14.572 -50.585 12.717  1.00 82.12  ? 58  PHE A CB  1 
ATOM   408   C CG  . PHE A 1 58  ? -15.841 -50.980 12.008  1.00 85.10  ? 58  PHE A CG  1 
ATOM   409   C CD1 . PHE A 1 58  ? -16.440 -50.123 11.101  1.00 89.64  ? 58  PHE A CD1 1 
ATOM   410   C CD2 . PHE A 1 58  ? -16.448 -52.198 12.267  1.00 87.73  ? 58  PHE A CD2 1 
ATOM   411   C CE1 . PHE A 1 58  ? -17.612 -50.480 10.452  1.00 97.34  ? 58  PHE A CE1 1 
ATOM   412   C CE2 . PHE A 1 58  ? -17.619 -52.557 11.622  1.00 89.76  ? 58  PHE A CE2 1 
ATOM   413   C CZ  . PHE A 1 58  ? -18.200 -51.699 10.716  1.00 94.53  ? 58  PHE A CZ  1 
ATOM   414   N N   . LEU A 1 59  ? -11.433 -49.374 11.848  1.00 75.93  ? 59  LEU A N   1 
ATOM   415   C CA  . LEU A 1 59  ? -10.370 -48.530 12.375  1.00 78.81  ? 59  LEU A CA  1 
ATOM   416   C C   . LEU A 1 59  ? -10.917 -47.116 12.496  1.00 76.16  ? 59  LEU A C   1 
ATOM   417   O O   . LEU A 1 59  ? -11.295 -46.507 11.490  1.00 80.33  ? 59  LEU A O   1 
ATOM   418   C CB  . LEU A 1 59  ? -9.136  -48.557 11.473  1.00 82.46  ? 59  LEU A CB  1 
ATOM   419   C CG  . LEU A 1 59  ? -8.623  -49.917 10.994  1.00 79.00  ? 59  LEU A CG  1 
ATOM   420   C CD1 . LEU A 1 59  ? -7.494  -49.730 9.996   1.00 77.99  ? 59  LEU A CD1 1 
ATOM   421   C CD2 . LEU A 1 59  ? -8.163  -50.772 12.159  1.00 76.94  ? 59  LEU A CD2 1 
ATOM   422   N N   . ILE A 1 60  ? -10.972 -46.599 13.720  1.00 75.11  ? 60  ILE A N   1 
ATOM   423   C CA  . ILE A 1 60  ? -11.541 -45.282 13.976  1.00 75.71  ? 60  ILE A CA  1 
ATOM   424   C C   . ILE A 1 60  ? -10.486 -44.388 14.610  1.00 79.00  ? 60  ILE A C   1 
ATOM   425   O O   . ILE A 1 60  ? -9.644  -44.849 15.388  1.00 79.73  ? 60  ILE A O   1 
ATOM   426   C CB  . ILE A 1 60  ? -12.801 -45.356 14.863  1.00 74.92  ? 60  ILE A CB  1 
ATOM   427   C CG1 . ILE A 1 60  ? -12.477 -45.976 16.218  1.00 78.44  ? 60  ILE A CG1 1 
ATOM   428   C CG2 . ILE A 1 60  ? -13.897 -46.142 14.166  1.00 81.12  ? 60  ILE A CG2 1 
ATOM   429   C CD1 . ILE A 1 60  ? -13.668 -46.034 17.133  1.00 86.73  ? 60  ILE A CD1 1 
ATOM   430   N N   . GLY A 1 61  ? -10.526 -43.109 14.248  1.00 79.22  ? 61  GLY A N   1 
ATOM   431   C CA  . GLY A 1 61  ? -9.602  -42.111 14.745  1.00 84.02  ? 61  GLY A CA  1 
ATOM   432   C C   . GLY A 1 61  ? -9.643  -40.877 13.869  1.00 81.09  ? 61  GLY A C   1 
ATOM   433   O O   . GLY A 1 61  ? -9.961  -40.980 12.679  1.00 82.34  ? 61  GLY A O   1 
ATOM   434   N N   . PHE A 1 62  ? -9.321  -39.706 14.426  1.00 82.07  ? 62  PHE A N   1 
ATOM   435   C CA  . PHE A 1 62  ? -9.453  -38.445 13.706  1.00 82.18  ? 62  PHE A CA  1 
ATOM   436   C C   . PHE A 1 62  ? -8.236  -38.127 12.845  1.00 83.70  ? 62  PHE A C   1 
ATOM   437   O O   . PHE A 1 62  ? -7.934  -36.950 12.611  1.00 80.51  ? 62  PHE A O   1 
ATOM   438   C CB  . PHE A 1 62  ? -9.756  -37.295 14.673  1.00 86.57  ? 62  PHE A CB  1 
ATOM   439   C CG  . PHE A 1 62  ? -8.760  -37.143 15.793  1.00 86.40  ? 62  PHE A CG  1 
ATOM   440   C CD1 . PHE A 1 62  ? -8.810  -37.965 16.911  1.00 89.05  ? 62  PHE A CD1 1 
ATOM   441   C CD2 . PHE A 1 62  ? -7.799  -36.145 15.753  1.00 84.72  ? 62  PHE A CD2 1 
ATOM   442   C CE1 . PHE A 1 62  ? -7.907  -37.814 17.945  1.00 87.71  ? 62  PHE A CE1 1 
ATOM   443   C CE2 . PHE A 1 62  ? -6.891  -35.986 16.788  1.00 83.09  ? 62  PHE A CE2 1 
ATOM   444   C CZ  . PHE A 1 62  ? -6.948  -36.824 17.885  1.00 84.82  ? 62  PHE A CZ  1 
ATOM   445   N N   . TYR A 1 63  ? -7.533  -39.149 12.363  1.00 92.38  ? 63  TYR A N   1 
ATOM   446   C CA  . TYR A 1 63  ? -6.570  -38.989 11.284  1.00 92.81  ? 63  TYR A CA  1 
ATOM   447   C C   . TYR A 1 63  ? -7.315  -38.723 9.979   1.00 94.11  ? 63  TYR A C   1 
ATOM   448   O O   . TYR A 1 63  ? -8.548  -38.754 9.916   1.00 94.54  ? 63  TYR A O   1 
ATOM   449   C CB  . TYR A 1 63  ? -5.702  -40.240 11.144  1.00 94.37  ? 63  TYR A CB  1 
ATOM   450   C CG  . TYR A 1 63  ? -4.385  -40.215 11.887  1.00 92.41  ? 63  TYR A CG  1 
ATOM   451   C CD1 . TYR A 1 63  ? -3.597  -39.074 11.913  1.00 92.19  ? 63  TYR A CD1 1 
ATOM   452   C CD2 . TYR A 1 63  ? -3.915  -41.350 12.536  1.00 93.33  ? 63  TYR A CD2 1 
ATOM   453   C CE1 . TYR A 1 63  ? -2.390  -39.060 12.580  1.00 96.23  ? 63  TYR A CE1 1 
ATOM   454   C CE2 . TYR A 1 63  ? -2.713  -41.342 13.211  1.00 94.35  ? 63  TYR A CE2 1 
ATOM   455   C CZ  . TYR A 1 63  ? -1.954  -40.196 13.232  1.00 96.37  ? 63  TYR A CZ  1 
ATOM   456   O OH  . TYR A 1 63  ? -0.751  -40.187 13.901  1.00 91.48  ? 63  TYR A OH  1 
ATOM   457   N N   . GLU A 1 64  ? -6.560  -38.471 8.917   1.00 97.29  ? 64  GLU A N   1 
ATOM   458   C CA  . GLU A 1 64  ? -7.144  -38.298 7.596   1.00 100.42 ? 64  GLU A CA  1 
ATOM   459   C C   . GLU A 1 64  ? -7.248  -39.645 6.891   1.00 99.71  ? 64  GLU A C   1 
ATOM   460   O O   . GLU A 1 64  ? -6.299  -40.435 6.902   1.00 99.16  ? 64  GLU A O   1 
ATOM   461   C CB  . GLU A 1 64  ? -6.328  -37.313 6.758   1.00 105.62 ? 64  GLU A CB  1 
ATOM   462   C CG  . GLU A 1 64  ? -6.465  -35.861 7.200   1.00 106.74 ? 64  GLU A CG  1 
ATOM   463   C CD  . GLU A 1 64  ? -7.896  -35.349 7.118   1.00 110.39 ? 64  GLU A CD  1 
ATOM   464   O OE1 . GLU A 1 64  ? -8.690  -35.904 6.326   1.00 114.10 ? 64  GLU A OE1 1 
ATOM   465   O OE2 . GLU A 1 64  ? -8.230  -34.391 7.845   1.00 110.99 ? 64  GLU A OE2 1 
ATOM   466   N N   . GLU A 1 65  ? -8.411  -39.904 6.286   1.00 107.48 ? 65  GLU A N   1 
ATOM   467   C CA  . GLU A 1 65  ? -8.649  -41.181 5.621   1.00 108.03 ? 65  GLU A CA  1 
ATOM   468   C C   . GLU A 1 65  ? -7.707  -41.401 4.444   1.00 106.76 ? 65  GLU A C   1 
ATOM   469   O O   . GLU A 1 65  ? -7.482  -42.551 4.047   1.00 106.63 ? 65  GLU A O   1 
ATOM   470   C CB  . GLU A 1 65  ? -10.101 -41.250 5.139   1.00 110.26 ? 65  GLU A CB  1 
ATOM   471   C CG  . GLU A 1 65  ? -10.530 -42.603 4.591   1.00 111.31 ? 65  GLU A CG  1 
ATOM   472   C CD  . GLU A 1 65  ? -12.004 -42.650 4.240   1.00 118.77 ? 65  GLU A CD  1 
ATOM   473   O OE1 . GLU A 1 65  ? -12.707 -41.645 4.476   1.00 117.94 ? 65  GLU A OE1 1 
ATOM   474   O OE2 . GLU A 1 65  ? -12.456 -43.690 3.717   1.00 122.68 ? 65  GLU A OE2 1 
ATOM   475   N N   . ARG A 1 66  ? -7.146  -40.325 3.888   1.00 104.90 ? 66  ARG A N   1 
ATOM   476   C CA  . ARG A 1 66  ? -6.279  -40.448 2.720   1.00 107.58 ? 66  ARG A CA  1 
ATOM   477   C C   . ARG A 1 66  ? -5.050  -41.301 3.011   1.00 108.25 ? 66  ARG A C   1 
ATOM   478   O O   . ARG A 1 66  ? -4.579  -42.036 2.136   1.00 104.61 ? 66  ARG A O   1 
ATOM   479   C CB  . ARG A 1 66  ? -5.860  -39.059 2.241   1.00 111.87 ? 66  ARG A CB  1 
ATOM   480   C CG  . ARG A 1 66  ? -7.009  -38.074 2.100   1.00 116.27 ? 66  ARG A CG  1 
ATOM   481   C CD  . ARG A 1 66  ? -6.483  -36.653 2.027   1.00 121.80 ? 66  ARG A CD  1 
ATOM   482   N NE  . ARG A 1 66  ? -5.699  -36.314 3.212   1.00 125.15 ? 66  ARG A NE  1 
ATOM   483   C CZ  . ARG A 1 66  ? -5.096  -35.146 3.404   1.00 128.40 ? 66  ARG A CZ  1 
ATOM   484   N NH1 . ARG A 1 66  ? -5.184  -34.194 2.485   1.00 129.87 ? 66  ARG A NH1 1 
ATOM   485   N NH2 . ARG A 1 66  ? -4.404  -34.927 4.514   1.00 128.02 ? 66  ARG A NH2 1 
ATOM   486   N N   . GLU A 1 67  ? -4.514  -41.217 4.230   1.00 125.09 ? 67  GLU A N   1 
ATOM   487   C CA  . GLU A 1 67  ? -3.321  -41.995 4.551   1.00 126.19 ? 67  GLU A CA  1 
ATOM   488   C C   . GLU A 1 67  ? -3.645  -43.473 4.731   1.00 126.71 ? 67  GLU A C   1 
ATOM   489   O O   . GLU A 1 67  ? -2.857  -44.339 4.331   1.00 127.22 ? 67  GLU A O   1 
ATOM   490   C CB  . GLU A 1 67  ? -2.639  -41.441 5.805   1.00 127.28 ? 67  GLU A CB  1 
ATOM   491   C CG  . GLU A 1 67  ? -1.933  -40.109 5.598   1.00 125.88 ? 67  GLU A CG  1 
ATOM   492   C CD  . GLU A 1 67  ? -1.387  -39.537 6.892   1.00 125.71 ? 67  GLU A CD  1 
ATOM   493   O OE1 . GLU A 1 67  ? -2.178  -39.346 7.840   1.00 124.44 ? 67  GLU A OE1 1 
ATOM   494   O OE2 . GLU A 1 67  ? -0.166  -39.280 6.961   1.00 124.07 ? 67  GLU A OE2 1 
ATOM   495   N N   . PHE A 1 68  ? -4.794  -43.781 5.331   1.00 102.98 ? 68  PHE A N   1 
ATOM   496   C CA  . PHE A 1 68  ? -5.146  -45.159 5.647   1.00 95.81  ? 68  PHE A CA  1 
ATOM   497   C C   . PHE A 1 68  ? -5.803  -45.898 4.490   1.00 94.24  ? 68  PHE A C   1 
ATOM   498   O O   . PHE A 1 68  ? -5.746  -47.132 4.454   1.00 93.91  ? 68  PHE A O   1 
ATOM   499   C CB  . PHE A 1 68  ? -6.074  -45.198 6.865   1.00 92.44  ? 68  PHE A CB  1 
ATOM   500   C CG  . PHE A 1 68  ? -5.386  -44.872 8.161   1.00 86.65  ? 68  PHE A CG  1 
ATOM   501   C CD1 . PHE A 1 68  ? -5.088  -45.872 9.071   1.00 83.85  ? 68  PHE A CD1 1 
ATOM   502   C CD2 . PHE A 1 68  ? -5.015  -43.570 8.457   1.00 88.42  ? 68  PHE A CD2 1 
ATOM   503   C CE1 . PHE A 1 68  ? -4.449  -45.576 10.259  1.00 84.76  ? 68  PHE A CE1 1 
ATOM   504   C CE2 . PHE A 1 68  ? -4.376  -43.269 9.643   1.00 85.93  ? 68  PHE A CE2 1 
ATOM   505   C CZ  . PHE A 1 68  ? -4.091  -44.272 10.544  1.00 84.60  ? 68  PHE A CZ  1 
ATOM   506   N N   . ALA A 1 69  ? -6.424  -45.178 3.552   1.00 94.58  ? 69  ALA A N   1 
ATOM   507   C CA  . ALA A 1 69  ? -7.113  -45.833 2.443   1.00 94.41  ? 69  ALA A CA  1 
ATOM   508   C C   . ALA A 1 69  ? -6.159  -46.685 1.614   1.00 92.98  ? 69  ALA A C   1 
ATOM   509   O O   . ALA A 1 69  ? -6.527  -47.774 1.157   1.00 99.74  ? 69  ALA A O   1 
ATOM   510   C CB  . ALA A 1 69  ? -7.803  -44.788 1.564   1.00 97.62  ? 69  ALA A CB  1 
ATOM   511   N N   . LEU A 1 70  ? -4.930  -46.206 1.407   1.00 88.96  ? 70  LEU A N   1 
ATOM   512   C CA  . LEU A 1 70  ? -3.959  -46.972 0.632   1.00 93.37  ? 70  LEU A CA  1 
ATOM   513   C C   . LEU A 1 70  ? -3.487  -48.205 1.391   1.00 93.64  ? 70  LEU A C   1 
ATOM   514   O O   . LEU A 1 70  ? -3.209  -49.242 0.778   1.00 91.11  ? 70  LEU A O   1 
ATOM   515   C CB  . LEU A 1 70  ? -2.760  -46.097 0.260   1.00 95.69  ? 70  LEU A CB  1 
ATOM   516   C CG  . LEU A 1 70  ? -2.895  -45.069 -0.870  1.00 94.69  ? 70  LEU A CG  1 
ATOM   517   C CD1 . LEU A 1 70  ? -3.784  -43.892 -0.482  1.00 92.33  ? 70  LEU A CD1 1 
ATOM   518   C CD2 . LEU A 1 70  ? -1.519  -44.588 -1.310  1.00 87.46  ? 70  LEU A CD2 1 
ATOM   519   N N   . TYR A 1 71  ? -3.396  -48.112 2.718   1.00 91.53  ? 71  TYR A N   1 
ATOM   520   C CA  . TYR A 1 71  ? -2.906  -49.221 3.527   1.00 91.10  ? 71  TYR A CA  1 
ATOM   521   C C   . TYR A 1 71  ? -3.968  -50.300 3.694   1.00 95.37  ? 71  TYR A C   1 
ATOM   522   O O   . TYR A 1 71  ? -3.672  -51.494 3.587   1.00 101.72 ? 71  TYR A O   1 
ATOM   523   C CB  . TYR A 1 71  ? -2.446  -48.704 4.892   1.00 90.02  ? 71  TYR A CB  1 
ATOM   524   C CG  . TYR A 1 71  ? -2.137  -49.795 5.891   1.00 94.46  ? 71  TYR A CG  1 
ATOM   525   C CD1 . TYR A 1 71  ? -1.185  -50.768 5.615   1.00 96.35  ? 71  TYR A CD1 1 
ATOM   526   C CD2 . TYR A 1 71  ? -2.785  -49.841 7.117   1.00 94.22  ? 71  TYR A CD2 1 
ATOM   527   C CE1 . TYR A 1 71  ? -0.898  -51.763 6.530   1.00 94.09  ? 71  TYR A CE1 1 
ATOM   528   C CE2 . TYR A 1 71  ? -2.502  -50.829 8.039   1.00 93.78  ? 71  TYR A CE2 1 
ATOM   529   C CZ  . TYR A 1 71  ? -1.560  -51.788 7.741   1.00 92.10  ? 71  TYR A CZ  1 
ATOM   530   O OH  . TYR A 1 71  ? -1.279  -52.774 8.659   1.00 90.53  ? 71  TYR A OH  1 
ATOM   531   N N   . VAL A 1 72  ? -5.207  -49.893 3.979   1.00 99.76  ? 72  VAL A N   1 
ATOM   532   C CA  . VAL A 1 72  ? -6.289  -50.853 4.170   1.00 101.91 ? 72  VAL A CA  1 
ATOM   533   C C   . VAL A 1 72  ? -6.507  -51.681 2.911   1.00 110.15 ? 72  VAL A C   1 
ATOM   534   O O   . VAL A 1 72  ? -6.918  -52.846 2.986   1.00 115.86 ? 72  VAL A O   1 
ATOM   535   C CB  . VAL A 1 72  ? -7.572  -50.117 4.604   1.00 100.35 ? 72  VAL A CB  1 
ATOM   536   C CG1 . VAL A 1 72  ? -8.748  -51.068 4.656   1.00 103.48 ? 72  VAL A CG1 1 
ATOM   537   C CG2 . VAL A 1 72  ? -7.365  -49.462 5.961   1.00 100.59 ? 72  VAL A CG2 1 
ATOM   538   N N   . SER A 1 73  ? -6.218  -51.109 1.740   1.00 120.36 ? 73  SER A N   1 
ATOM   539   C CA  . SER A 1 73  ? -6.402  -51.829 0.486   1.00 120.57 ? 73  SER A CA  1 
ATOM   540   C C   . SER A 1 73  ? -5.497  -53.049 0.378   1.00 122.86 ? 73  SER A C   1 
ATOM   541   O O   . SER A 1 73  ? -5.810  -53.974 -0.380  1.00 125.43 ? 73  SER A O   1 
ATOM   542   C CB  . SER A 1 73  ? -6.147  -50.891 -0.694  1.00 119.12 ? 73  SER A CB  1 
ATOM   543   O OG  . SER A 1 73  ? -7.010  -49.768 -0.644  1.00 122.09 ? 73  SER A OG  1 
ATOM   544   N N   . SER A 1 74  ? -4.384  -53.073 1.111   1.00 114.79 ? 74  SER A N   1 
ATOM   545   C CA  . SER A 1 74  ? -3.423  -54.163 1.013   1.00 113.86 ? 74  SER A CA  1 
ATOM   546   C C   . SER A 1 74  ? -3.645  -55.258 2.046   1.00 117.89 ? 74  SER A C   1 
ATOM   547   O O   . SER A 1 74  ? -3.228  -56.399 1.815   1.00 114.55 ? 74  SER A O   1 
ATOM   548   C CB  . SER A 1 74  ? -1.996  -53.622 1.153   1.00 113.29 ? 74  SER A CB  1 
ATOM   549   O OG  . SER A 1 74  ? -1.765  -52.556 0.249   1.00 104.24 ? 74  SER A OG  1 
ATOM   550   N N   . ILE A 1 75  ? -4.283  -54.942 3.174   1.00 133.84 ? 75  ILE A N   1 
ATOM   551   C CA  . ILE A 1 75  ? -4.465  -55.935 4.228   1.00 135.77 ? 75  ILE A CA  1 
ATOM   552   C C   . ILE A 1 75  ? -5.452  -57.007 3.784   1.00 137.42 ? 75  ILE A C   1 
ATOM   553   O O   . ILE A 1 75  ? -5.180  -58.209 3.889   1.00 140.15 ? 75  ILE A O   1 
ATOM   554   C CB  . ILE A 1 75  ? -4.930  -55.259 5.530   1.00 135.50 ? 75  ILE A CB  1 
ATOM   555   C CG1 . ILE A 1 75  ? -4.224  -53.917 5.723   1.00 133.66 ? 75  ILE A CG1 1 
ATOM   556   C CG2 . ILE A 1 75  ? -4.675  -56.170 6.719   1.00 136.46 ? 75  ILE A CG2 1 
ATOM   557   C CD1 . ILE A 1 75  ? -4.811  -53.091 6.843   1.00 132.77 ? 75  ILE A CD1 1 
ATOM   558   N N   . SER A 1 76  ? -6.616  -56.587 3.283   1.00 131.60 ? 76  SER A N   1 
ATOM   559   C CA  . SER A 1 76  ? -7.642  -57.527 2.851   1.00 137.71 ? 76  SER A CA  1 
ATOM   560   C C   . SER A 1 76  ? -7.192  -58.392 1.680   1.00 130.73 ? 76  SER A C   1 
ATOM   561   O O   . SER A 1 76  ? -7.851  -59.393 1.382   1.00 130.87 ? 76  SER A O   1 
ATOM   562   C CB  . SER A 1 76  ? -8.919  -56.770 2.490   1.00 137.75 ? 76  SER A CB  1 
ATOM   563   O OG  . SER A 1 76  ? -9.411  -56.044 3.602   1.00 139.08 ? 76  SER A OG  1 
ATOM   564   N N   . ASN A 1 77  ? -6.103  -58.026 1.003   1.00 126.32 ? 77  ASN A N   1 
ATOM   565   C CA  . ASN A 1 77  ? -5.524  -58.896 -0.011  1.00 118.46 ? 77  ASN A CA  1 
ATOM   566   C C   . ASN A 1 77  ? -4.757  -60.061 0.600   1.00 117.11 ? 77  ASN A C   1 
ATOM   567   O O   . ASN A 1 77  ? -4.510  -61.055 -0.092  1.00 117.48 ? 77  ASN A O   1 
ATOM   568   C CB  . ASN A 1 77  ? -4.599  -58.092 -0.928  1.00 112.82 ? 77  ASN A CB  1 
ATOM   569   C CG  . ASN A 1 77  ? -5.329  -56.996 -1.679  1.00 108.94 ? 77  ASN A CG  1 
ATOM   570   O OD1 . ASN A 1 77  ? -6.523  -57.109 -1.960  1.00 109.68 ? 77  ASN A OD1 1 
ATOM   571   N ND2 . ASN A 1 77  ? -4.615  -55.924 -2.006  1.00 105.44 ? 77  ASN A ND2 1 
ATOM   572   N N   . GLU A 1 78  ? -4.378  -59.960 1.875   1.00 117.25 ? 78  GLU A N   1 
ATOM   573   C CA  . GLU A 1 78  ? -3.623  -61.003 2.561   1.00 119.02 ? 78  GLU A CA  1 
ATOM   574   C C   . GLU A 1 78  ? -4.530  -61.918 3.377   1.00 126.82 ? 78  GLU A C   1 
ATOM   575   O O   . GLU A 1 78  ? -4.544  -63.135 3.167   1.00 129.48 ? 78  GLU A O   1 
ATOM   576   C CB  . GLU A 1 78  ? -2.556  -60.369 3.464   1.00 114.29 ? 78  GLU A CB  1 
ATOM   577   C CG  . GLU A 1 78  ? -1.486  -59.594 2.714   1.00 114.34 ? 78  GLU A CG  1 
ATOM   578   C CD  . GLU A 1 78  ? -0.385  -59.094 3.627   1.00 104.69 ? 78  GLU A CD  1 
ATOM   579   O OE1 . GLU A 1 78  ? -0.489  -59.299 4.855   1.00 98.33  ? 78  GLU A OE1 1 
ATOM   580   O OE2 . GLU A 1 78  ? 0.582   -58.489 3.117   1.00 105.13 ? 78  GLU A OE2 1 
ATOM   581   N N   . LEU A 1 79  ? -5.293  -61.348 4.311   1.00 128.47 ? 79  LEU A N   1 
ATOM   582   C CA  . LEU A 1 79  ? -6.124  -62.128 5.218   1.00 140.18 ? 79  LEU A CA  1 
ATOM   583   C C   . LEU A 1 79  ? -7.584  -62.199 4.790   1.00 150.91 ? 79  LEU A C   1 
ATOM   584   O O   . LEU A 1 79  ? -8.354  -62.941 5.410   1.00 155.04 ? 79  LEU A O   1 
ATOM   585   C CB  . LEU A 1 79  ? -6.042  -61.556 6.640   1.00 141.37 ? 79  LEU A CB  1 
ATOM   586   C CG  . LEU A 1 79  ? -4.755  -61.808 7.431   1.00 131.33 ? 79  LEU A CG  1 
ATOM   587   C CD1 . LEU A 1 79  ? -4.296  -63.250 7.262   1.00 129.75 ? 79  LEU A CD1 1 
ATOM   588   C CD2 . LEU A 1 79  ? -3.653  -60.833 7.036   1.00 125.55 ? 79  LEU A CD2 1 
ATOM   589   N N   . LYS A 1 80  ? -7.978  -61.451 3.759   1.00 147.88 ? 80  LYS A N   1 
ATOM   590   C CA  . LYS A 1 80  ? -9.337  -61.480 3.216   1.00 158.19 ? 80  LYS A CA  1 
ATOM   591   C C   . LYS A 1 80  ? -10.365 -61.122 4.291   1.00 174.04 ? 80  LYS A C   1 
ATOM   592   O O   . LYS A 1 80  ? -11.290 -61.880 4.588   1.00 173.73 ? 80  LYS A O   1 
ATOM   593   C CB  . LYS A 1 80  ? -9.652  -62.842 2.581   1.00 151.40 ? 80  LYS A CB  1 
ATOM   594   C CG  . LYS A 1 80  ? -8.698  -63.273 1.472   1.00 146.81 ? 80  LYS A CG  1 
ATOM   595   C CD  . LYS A 1 80  ? -7.536  -64.095 2.013   1.00 148.11 ? 80  LYS A CD  1 
ATOM   596   C CE  . LYS A 1 80  ? -8.030  -65.203 2.930   1.00 149.94 ? 80  LYS A CE  1 
ATOM   597   N NZ  . LYS A 1 80  ? -6.915  -65.884 3.644   1.00 146.18 ? 80  LYS A NZ  1 
ATOM   598   N N   . ILE A 1 81  ? -10.188 -59.939 4.871   1.00 238.43 ? 81  ILE A N   1 
ATOM   599   C CA  . ILE A 1 81  ? -11.098 -59.442 5.899   1.00 238.25 ? 81  ILE A CA  1 
ATOM   600   C C   . ILE A 1 81  ? -11.510 -58.012 5.572   1.00 236.31 ? 81  ILE A C   1 
ATOM   601   O O   . ILE A 1 81  ? -10.654 -57.177 5.247   1.00 235.13 ? 81  ILE A O   1 
ATOM   602   C CB  . ILE A 1 81  ? -10.466 -59.531 7.297   1.00 239.06 ? 81  ILE A CB  1 
ATOM   603   C CG1 . ILE A 1 81  ? -8.958  -59.282 7.222   1.00 238.71 ? 81  ILE A CG1 1 
ATOM   604   C CG2 . ILE A 1 81  ? -10.768 -60.879 7.933   1.00 241.18 ? 81  ILE A CG2 1 
ATOM   605   C CD1 . ILE A 1 81  ? -8.256  -59.431 8.552   1.00 239.69 ? 81  ILE A CD1 1 
ATOM   606   N N   . PRO A 1 82  ? -12.800 -57.688 5.642   1.00 160.22 ? 82  PRO A N   1 
ATOM   607   C CA  . PRO A 1 82  ? -13.242 -56.324 5.323   1.00 137.23 ? 82  PRO A CA  1 
ATOM   608   C C   . PRO A 1 82  ? -12.813 -55.306 6.366   1.00 124.20 ? 82  PRO A C   1 
ATOM   609   O O   . PRO A 1 82  ? -13.490 -55.123 7.383   1.00 119.37 ? 82  PRO A O   1 
ATOM   610   C CB  . PRO A 1 82  ? -14.772 -56.452 5.269   1.00 131.76 ? 82  PRO A CB  1 
ATOM   611   C CG  . PRO A 1 82  ? -15.043 -57.922 5.143   1.00 133.97 ? 82  PRO A CG  1 
ATOM   612   C CD  . PRO A 1 82  ? -13.935 -58.593 5.883   1.00 149.70 ? 82  PRO A CD  1 
ATOM   613   N N   . VAL A 1 83  ? -11.693 -54.637 6.123   1.00 120.72 ? 83  VAL A N   1 
ATOM   614   C CA  . VAL A 1 83  ? -11.186 -53.598 7.011   1.00 110.35 ? 83  VAL A CA  1 
ATOM   615   C C   . VAL A 1 83  ? -11.653 -52.252 6.480   1.00 103.77 ? 83  VAL A C   1 
ATOM   616   O O   . VAL A 1 83  ? -11.673 -52.027 5.264   1.00 103.15 ? 83  VAL A O   1 
ATOM   617   C CB  . VAL A 1 83  ? -9.650  -53.657 7.112   1.00 109.30 ? 83  VAL A CB  1 
ATOM   618   C CG1 . VAL A 1 83  ? -9.144  -52.692 8.173   1.00 98.67  ? 83  VAL A CG1 1 
ATOM   619   C CG2 . VAL A 1 83  ? -9.195  -55.077 7.407   1.00 125.74 ? 83  VAL A CG2 1 
ATOM   620   N N   . ARG A 1 84  ? -12.037 -51.355 7.385   1.00 99.24  ? 84  ARG A N   1 
ATOM   621   C CA  . ARG A 1 84  ? -12.541 -50.045 7.001   1.00 97.30  ? 84  ARG A CA  1 
ATOM   622   C C   . ARG A 1 84  ? -12.078 -49.008 8.012   1.00 90.19  ? 84  ARG A C   1 
ATOM   623   O O   . ARG A 1 84  ? -12.056 -49.275 9.217   1.00 89.25  ? 84  ARG A O   1 
ATOM   624   C CB  . ARG A 1 84  ? -14.074 -50.046 6.910   1.00 99.13  ? 84  ARG A CB  1 
ATOM   625   C CG  . ARG A 1 84  ? -14.686 -48.716 6.499   1.00 100.48 ? 84  ARG A CG  1 
ATOM   626   C CD  . ARG A 1 84  ? -16.204 -48.795 6.478   1.00 107.73 ? 84  ARG A CD  1 
ATOM   627   N NE  . ARG A 1 84  ? -16.692 -49.740 5.478   1.00 119.84 ? 84  ARG A NE  1 
ATOM   628   C CZ  . ARG A 1 84  ? -16.968 -49.418 4.218   1.00 121.00 ? 84  ARG A CZ  1 
ATOM   629   N NH1 . ARG A 1 84  ? -16.804 -48.171 3.797   1.00 124.98 ? 84  ARG A NH1 1 
ATOM   630   N NH2 . ARG A 1 84  ? -17.409 -50.344 3.377   1.00 118.17 ? 84  ARG A NH2 1 
ATOM   631   N N   . TYR A 1 85  ? -11.707 -47.830 7.518   1.00 83.50  ? 85  TYR A N   1 
ATOM   632   C CA  . TYR A 1 85  ? -11.312 -46.717 8.369   1.00 82.49  ? 85  TYR A CA  1 
ATOM   633   C C   . TYR A 1 85  ? -12.441 -45.696 8.442   1.00 84.53  ? 85  TYR A C   1 
ATOM   634   O O   . TYR A 1 85  ? -13.035 -45.343 7.417   1.00 90.14  ? 85  TYR A O   1 
ATOM   635   C CB  . TYR A 1 85  ? -10.031 -46.052 7.860   1.00 84.37  ? 85  TYR A CB  1 
ATOM   636   C CG  . TYR A 1 85  ? -9.639  -44.827 8.657   1.00 81.74  ? 85  TYR A CG  1 
ATOM   637   C CD1 . TYR A 1 85  ? -9.008  -44.951 9.887   1.00 80.44  ? 85  TYR A CD1 1 
ATOM   638   C CD2 . TYR A 1 85  ? -9.899  -43.548 8.179   1.00 83.37  ? 85  TYR A CD2 1 
ATOM   639   C CE1 . TYR A 1 85  ? -8.652  -43.838 10.622  1.00 78.57  ? 85  TYR A CE1 1 
ATOM   640   C CE2 . TYR A 1 85  ? -9.545  -42.429 8.907   1.00 83.00  ? 85  TYR A CE2 1 
ATOM   641   C CZ  . TYR A 1 85  ? -8.922  -42.581 10.126  1.00 80.40  ? 85  TYR A CZ  1 
ATOM   642   O OH  . TYR A 1 85  ? -8.568  -41.472 10.856  1.00 81.79  ? 85  TYR A OH  1 
ATOM   643   N N   . LEU A 1 86  ? -12.730 -45.224 9.654   1.00 81.75  ? 86  LEU A N   1 
ATOM   644   C CA  . LEU A 1 86  ? -13.749 -44.210 9.891   1.00 81.09  ? 86  LEU A CA  1 
ATOM   645   C C   . LEU A 1 86  ? -13.127 -43.059 10.666  1.00 81.03  ? 86  LEU A C   1 
ATOM   646   O O   . LEU A 1 86  ? -12.526 -43.273 11.723  1.00 81.62  ? 86  LEU A O   1 
ATOM   647   C CB  . LEU A 1 86  ? -14.937 -44.790 10.668  1.00 87.66  ? 86  LEU A CB  1 
ATOM   648   C CG  . LEU A 1 86  ? -15.639 -46.007 10.061  1.00 87.98  ? 86  LEU A CG  1 
ATOM   649   C CD1 . LEU A 1 86  ? -16.791 -46.468 10.944  1.00 92.07  ? 86  LEU A CD1 1 
ATOM   650   C CD2 . LEU A 1 86  ? -16.125 -45.707 8.652   1.00 90.48  ? 86  LEU A CD2 1 
ATOM   651   N N   . LYS A 1 87  ? -13.272 -41.845 10.146  1.00 83.56  ? 87  LYS A N   1 
ATOM   652   C CA  . LYS A 1 87  ? -12.721 -40.655 10.788  1.00 88.64  ? 87  LYS A CA  1 
ATOM   653   C C   . LYS A 1 87  ? -13.791 -40.023 11.669  1.00 94.16  ? 87  LYS A C   1 
ATOM   654   O O   . LYS A 1 87  ? -14.761 -39.450 11.163  1.00 100.36 ? 87  LYS A O   1 
ATOM   655   C CB  . LYS A 1 87  ? -12.214 -39.662 9.744   1.00 88.77  ? 87  LYS A CB  1 
ATOM   656   C CG  . LYS A 1 87  ? -11.902 -38.286 10.309  1.00 92.62  ? 87  LYS A CG  1 
ATOM   657   C CD  . LYS A 1 87  ? -11.444 -37.326 9.228   1.00 87.48  ? 87  LYS A CD  1 
ATOM   658   C CE  . LYS A 1 87  ? -11.395 -35.901 9.753   1.00 89.05  ? 87  LYS A CE  1 
ATOM   659   N NZ  . LYS A 1 87  ? -10.740 -35.823 11.088  1.00 90.24  ? 87  LYS A NZ  1 
ATOM   660   N N   . GLU A 1 88  ? -13.628 -40.139 12.985  1.00 92.00  ? 88  GLU A N   1 
ATOM   661   C CA  . GLU A 1 88  ? -14.536 -39.468 13.909  1.00 104.21 ? 88  GLU A CA  1 
ATOM   662   C C   . GLU A 1 88  ? -14.300 -37.964 13.825  1.00 114.73 ? 88  GLU A C   1 
ATOM   663   O O   . GLU A 1 88  ? -13.277 -37.457 14.299  1.00 110.18 ? 88  GLU A O   1 
ATOM   664   C CB  . GLU A 1 88  ? -14.355 -39.986 15.335  1.00 103.14 ? 88  GLU A CB  1 
ATOM   665   C CG  . GLU A 1 88  ? -12.921 -40.063 15.834  1.00 99.89  ? 88  GLU A CG  1 
ATOM   666   C CD  . GLU A 1 88  ? -12.844 -40.345 17.323  1.00 105.95 ? 88  GLU A CD  1 
ATOM   667   O OE1 . GLU A 1 88  ? -13.881 -40.214 18.008  1.00 113.74 ? 88  GLU A OE1 1 
ATOM   668   O OE2 . GLU A 1 88  ? -11.746 -40.683 17.811  1.00 109.27 ? 88  GLU A OE2 1 
ATOM   669   N N   . ASP A 1 89  ? -15.237 -37.250 13.197  1.00 143.70 ? 89  ASP A N   1 
ATOM   670   C CA  . ASP A 1 89  ? -15.099 -35.804 13.056  1.00 143.13 ? 89  ASP A CA  1 
ATOM   671   C C   . ASP A 1 89  ? -15.041 -35.126 14.417  1.00 143.80 ? 89  ASP A C   1 
ATOM   672   O O   . ASP A 1 89  ? -14.294 -34.159 14.609  1.00 142.55 ? 89  ASP A O   1 
ATOM   673   C CB  . ASP A 1 89  ? -16.258 -35.245 12.231  1.00 149.02 ? 89  ASP A CB  1 
ATOM   674   C CG  . ASP A 1 89  ? -16.638 -36.147 11.073  1.00 151.09 ? 89  ASP A CG  1 
ATOM   675   O OD1 . ASP A 1 89  ? -17.577 -36.956 11.234  1.00 147.81 ? 89  ASP A OD1 1 
ATOM   676   O OD2 . ASP A 1 89  ? -15.987 -36.061 10.012  1.00 150.92 ? 89  ASP A OD2 1 
ATOM   677   N N   . LYS A 1 90  ? -15.822 -35.622 15.374  1.00 128.40 ? 90  LYS A N   1 
ATOM   678   C CA  . LYS A 1 90  ? -15.797 -35.128 16.746  1.00 127.47 ? 90  LYS A CA  1 
ATOM   679   C C   . LYS A 1 90  ? -15.125 -36.171 17.627  1.00 127.74 ? 90  LYS A C   1 
ATOM   680   O O   . LYS A 1 90  ? -15.781 -37.128 18.067  1.00 126.97 ? 90  LYS A O   1 
ATOM   681   C CB  . LYS A 1 90  ? -17.216 -34.831 17.239  1.00 129.47 ? 90  LYS A CB  1 
ATOM   682   N N   . PRO A 1 91  ? -13.827 -36.048 17.903  1.00 124.80 ? 91  PRO A N   1 
ATOM   683   C CA  . PRO A 1 91  ? -13.144 -37.065 18.713  1.00 125.61 ? 91  PRO A CA  1 
ATOM   684   C C   . PRO A 1 91  ? -13.587 -36.988 20.166  1.00 134.45 ? 91  PRO A C   1 
ATOM   685   O O   . PRO A 1 91  ? -13.539 -35.926 20.788  1.00 132.37 ? 91  PRO A O   1 
ATOM   686   C CB  . PRO A 1 91  ? -11.658 -36.712 18.556  1.00 114.93 ? 91  PRO A CB  1 
ATOM   687   C CG  . PRO A 1 91  ? -11.594 -35.764 17.388  1.00 112.68 ? 91  PRO A CG  1 
ATOM   688   C CD  . PRO A 1 91  ? -12.894 -35.035 17.388  1.00 120.60 ? 91  PRO A CD  1 
ATOM   689   N N   . HIS A 1 92  ? -14.019 -38.127 20.702  1.00 157.04 ? 92  HIS A N   1 
ATOM   690   C CA  . HIS A 1 92  ? -14.479 -38.178 22.083  1.00 158.33 ? 92  HIS A CA  1 
ATOM   691   C C   . HIS A 1 92  ? -13.672 -39.196 22.875  1.00 159.78 ? 92  HIS A C   1 
ATOM   692   O O   . HIS A 1 92  ? -14.244 -40.019 23.597  1.00 161.23 ? 92  HIS A O   1 
ATOM   693   C CB  . HIS A 1 92  ? -15.963 -38.539 22.140  1.00 158.89 ? 92  HIS A CB  1 
ATOM   694   C CG  . HIS A 1 92  ? -16.817 -37.748 21.201  1.00 157.78 ? 92  HIS A CG  1 
ATOM   695   N ND1 . HIS A 1 92  ? -17.723 -38.338 20.347  1.00 157.58 ? 92  HIS A ND1 1 
ATOM   696   C CD2 . HIS A 1 92  ? -16.904 -36.415 20.980  1.00 160.09 ? 92  HIS A CD2 1 
ATOM   697   C CE1 . HIS A 1 92  ? -18.332 -37.403 19.640  1.00 157.41 ? 92  HIS A CE1 1 
ATOM   698   N NE2 . HIS A 1 92  ? -17.854 -36.228 20.007  1.00 162.85 ? 92  HIS A NE2 1 
ATOM   699   N N   . GLY A 1 93  ? -12.349 -39.139 22.759  1.00 145.07 ? 93  GLY A N   1 
ATOM   700   C CA  . GLY A 1 93  ? -11.504 -40.091 23.449  1.00 140.69 ? 93  GLY A CA  1 
ATOM   701   C C   . GLY A 1 93  ? -11.770 -41.514 23.007  1.00 131.76 ? 93  GLY A C   1 
ATOM   702   O O   . GLY A 1 93  ? -11.377 -41.913 21.907  1.00 120.75 ? 93  GLY A O   1 
ATOM   703   N N   . SER A 1 94  ? -12.442 -42.292 23.857  1.00 131.57 ? 94  SER A N   1 
ATOM   704   C CA  . SER A 1 94  ? -12.725 -43.693 23.565  1.00 125.49 ? 94  SER A CA  1 
ATOM   705   C C   . SER A 1 94  ? -14.213 -44.011 23.605  1.00 118.22 ? 94  SER A C   1 
ATOM   706   O O   . SER A 1 94  ? -14.753 -44.517 22.616  1.00 112.25 ? 94  SER A O   1 
ATOM   707   C CB  . SER A 1 94  ? -11.958 -44.594 24.540  1.00 127.94 ? 94  SER A CB  1 
ATOM   708   O OG  . SER A 1 94  ? -10.564 -44.349 24.469  1.00 135.55 ? 94  SER A OG  1 
ATOM   709   N N   . ALA A 1 95  ? -14.895 -43.733 24.720  1.00 119.51 ? 95  ALA A N   1 
ATOM   710   C CA  . ALA A 1 95  ? -16.285 -44.155 24.871  1.00 117.96 ? 95  ALA A CA  1 
ATOM   711   C C   . ALA A 1 95  ? -17.187 -43.475 23.849  1.00 116.05 ? 95  ALA A C   1 
ATOM   712   O O   . ALA A 1 95  ? -17.971 -44.136 23.157  1.00 112.67 ? 95  ALA A O   1 
ATOM   713   C CB  . ALA A 1 95  ? -16.769 -43.868 26.292  1.00 123.13 ? 95  ALA A CB  1 
ATOM   714   N N   . GLY A 1 96  ? -17.104 -42.149 23.750  1.00 124.82 ? 96  GLY A N   1 
ATOM   715   C CA  . GLY A 1 96  ? -17.875 -41.448 22.740  1.00 128.23 ? 96  GLY A CA  1 
ATOM   716   C C   . GLY A 1 96  ? -17.434 -41.738 21.323  1.00 121.39 ? 96  GLY A C   1 
ATOM   717   O O   . GLY A 1 96  ? -18.213 -41.527 20.387  1.00 119.79 ? 96  GLY A O   1 
ATOM   718   N N   . ALA A 1 97  ? -16.196 -42.207 21.144  1.00 119.42 ? 97  ALA A N   1 
ATOM   719   C CA  . ALA A 1 97  ? -15.698 -42.516 19.807  1.00 112.87 ? 97  ALA A CA  1 
ATOM   720   C C   . ALA A 1 97  ? -16.495 -43.644 19.164  1.00 103.78 ? 97  ALA A C   1 
ATOM   721   O O   . ALA A 1 97  ? -16.863 -43.564 17.987  1.00 102.22 ? 97  ALA A O   1 
ATOM   722   C CB  . ALA A 1 97  ? -14.213 -42.871 19.870  1.00 112.11 ? 97  ALA A CB  1 
ATOM   723   N N   . LEU A 1 98  ? -16.773 -44.708 19.922  1.00 103.14 ? 98  LEU A N   1 
ATOM   724   C CA  . LEU A 1 98  ? -17.479 -45.851 19.359  1.00 102.60 ? 98  LEU A CA  1 
ATOM   725   C C   . LEU A 1 98  ? -18.994 -45.729 19.464  1.00 107.00 ? 98  LEU A C   1 
ATOM   726   O O   . LEU A 1 98  ? -19.705 -46.371 18.683  1.00 108.25 ? 98  LEU A O   1 
ATOM   727   C CB  . LEU A 1 98  ? -17.025 -47.158 20.024  1.00 99.17  ? 98  LEU A CB  1 
ATOM   728   C CG  . LEU A 1 98  ? -17.601 -47.546 21.387  1.00 102.94 ? 98  LEU A CG  1 
ATOM   729   C CD1 . LEU A 1 98  ? -17.714 -49.056 21.491  1.00 98.55  ? 98  LEU A CD1 1 
ATOM   730   C CD2 . LEU A 1 98  ? -16.724 -47.013 22.498  1.00 105.81 ? 98  LEU A CD2 1 
ATOM   731   N N   . TYR A 1 99  ? -19.509 -44.927 20.400  1.00 108.77 ? 99  TYR A N   1 
ATOM   732   C CA  . TYR A 1 99  ? -20.941 -44.650 20.392  1.00 106.27 ? 99  TYR A CA  1 
ATOM   733   C C   . TYR A 1 99  ? -21.325 -43.861 19.148  1.00 107.74 ? 99  TYR A C   1 
ATOM   734   O O   . TYR A 1 99  ? -22.389 -44.090 18.564  1.00 106.34 ? 99  TYR A O   1 
ATOM   735   C CB  . TYR A 1 99  ? -21.360 -43.897 21.653  1.00 109.06 ? 99  TYR A CB  1 
ATOM   736   C CG  . TYR A 1 99  ? -22.819 -43.507 21.623  1.00 114.11 ? 99  TYR A CG  1 
ATOM   737   C CD1 . TYR A 1 99  ? -23.809 -44.479 21.550  1.00 116.50 ? 99  TYR A CD1 1 
ATOM   738   C CD2 . TYR A 1 99  ? -23.209 -42.175 21.648  1.00 122.09 ? 99  TYR A CD2 1 
ATOM   739   C CE1 . TYR A 1 99  ? -25.142 -44.138 21.511  1.00 119.98 ? 99  TYR A CE1 1 
ATOM   740   C CE2 . TYR A 1 99  ? -24.548 -41.823 21.611  1.00 126.77 ? 99  TYR A CE2 1 
ATOM   741   C CZ  . TYR A 1 99  ? -25.509 -42.811 21.544  1.00 125.47 ? 99  TYR A CZ  1 
ATOM   742   O OH  . TYR A 1 99  ? -26.843 -42.475 21.506  1.00 125.94 ? 99  TYR A OH  1 
ATOM   743   N N   . TYR A 1 100 ? -20.480 -42.910 18.750  1.00 109.48 ? 100 TYR A N   1 
ATOM   744   C CA  . TYR A 1 100 ? -20.561 -42.326 17.419  1.00 106.72 ? 100 TYR A CA  1 
ATOM   745   C C   . TYR A 1 100 ? -20.571 -43.439 16.378  1.00 106.40 ? 100 TYR A C   1 
ATOM   746   O O   . TYR A 1 100 ? -19.801 -44.399 16.471  1.00 107.20 ? 100 TYR A O   1 
ATOM   747   C CB  . TYR A 1 100 ? -19.369 -41.386 17.201  1.00 106.53 ? 100 TYR A CB  1 
ATOM   748   C CG  . TYR A 1 100 ? -19.531 -40.328 16.127  1.00 104.30 ? 100 TYR A CG  1 
ATOM   749   C CD1 . TYR A 1 100 ? -18.617 -39.287 16.021  1.00 108.87 ? 100 TYR A CD1 1 
ATOM   750   C CD2 . TYR A 1 100 ? -20.585 -40.366 15.223  1.00 103.64 ? 100 TYR A CD2 1 
ATOM   751   C CE1 . TYR A 1 100 ? -18.745 -38.318 15.046  1.00 112.28 ? 100 TYR A CE1 1 
ATOM   752   C CE2 . TYR A 1 100 ? -20.720 -39.401 14.241  1.00 106.55 ? 100 TYR A CE2 1 
ATOM   753   C CZ  . TYR A 1 100 ? -19.798 -38.379 14.159  1.00 108.57 ? 100 TYR A CZ  1 
ATOM   754   O OH  . TYR A 1 100 ? -19.928 -37.414 13.187  1.00 108.94 ? 100 TYR A OH  1 
ATOM   755   N N   . PHE A 1 101 ? -21.447 -43.294 15.384  1.00 105.69 ? 101 PHE A N   1 
ATOM   756   C CA  . PHE A 1 101 ? -21.719 -44.312 14.362  1.00 108.18 ? 101 PHE A CA  1 
ATOM   757   C C   . PHE A 1 101 ? -21.730 -45.723 14.952  1.00 107.89 ? 101 PHE A C   1 
ATOM   758   O O   . PHE A 1 101 ? -21.036 -46.633 14.491  1.00 106.66 ? 101 PHE A O   1 
ATOM   759   C CB  . PHE A 1 101 ? -20.754 -44.205 13.173  1.00 109.46 ? 101 PHE A CB  1 
ATOM   760   C CG  . PHE A 1 101 ? -19.311 -43.985 13.543  1.00 107.21 ? 101 PHE A CG  1 
ATOM   761   C CD1 . PHE A 1 101 ? -18.774 -42.708 13.547  1.00 104.21 ? 101 PHE A CD1 1 
ATOM   762   C CD2 . PHE A 1 101 ? -18.484 -45.054 13.843  1.00 100.70 ? 101 PHE A CD2 1 
ATOM   763   C CE1 . PHE A 1 101 ? -17.446 -42.498 13.871  1.00 97.57  ? 101 PHE A CE1 1 
ATOM   764   C CE2 . PHE A 1 101 ? -17.158 -44.851 14.171  1.00 93.30  ? 101 PHE A CE2 1 
ATOM   765   C CZ  . PHE A 1 101 ? -16.637 -43.572 14.183  1.00 93.07  ? 101 PHE A CZ  1 
ATOM   766   N N   . ARG A 1 102 ? -22.548 -45.901 15.994  1.00 108.44 ? 102 ARG A N   1 
ATOM   767   C CA  . ARG A 1 102 ? -22.816 -47.237 16.513  1.00 108.82 ? 102 ARG A CA  1 
ATOM   768   C C   . ARG A 1 102 ? -23.621 -48.073 15.529  1.00 108.12 ? 102 ARG A C   1 
ATOM   769   O O   . ARG A 1 102 ? -23.620 -49.305 15.628  1.00 108.17 ? 102 ARG A O   1 
ATOM   770   C CB  . ARG A 1 102 ? -23.571 -47.148 17.842  1.00 112.48 ? 102 ARG A CB  1 
ATOM   771   C CG  . ARG A 1 102 ? -24.930 -46.470 17.738  1.00 114.77 ? 102 ARG A CG  1 
ATOM   772   C CD  . ARG A 1 102 ? -25.770 -46.676 18.992  1.00 115.17 ? 102 ARG A CD  1 
ATOM   773   N NE  . ARG A 1 102 ? -26.193 -48.066 19.151  1.00 116.17 ? 102 ARG A NE  1 
ATOM   774   C CZ  . ARG A 1 102 ? -26.999 -48.496 20.117  1.00 116.79 ? 102 ARG A CZ  1 
ATOM   775   N NH1 . ARG A 1 102 ? -27.464 -47.645 21.021  1.00 116.78 ? 102 ARG A NH1 1 
ATOM   776   N NH2 . ARG A 1 102 ? -27.334 -49.777 20.184  1.00 116.48 ? 102 ARG A NH2 1 
ATOM   777   N N   . ASP A 1 103 ? -24.304 -47.425 14.583  1.00 106.82 ? 103 ASP A N   1 
ATOM   778   C CA  . ASP A 1 103 ? -25.078 -48.144 13.578  1.00 109.02 ? 103 ASP A CA  1 
ATOM   779   C C   . ASP A 1 103 ? -24.174 -48.902 12.612  1.00 111.76 ? 103 ASP A C   1 
ATOM   780   O O   . ASP A 1 103 ? -24.467 -50.048 12.249  1.00 112.46 ? 103 ASP A O   1 
ATOM   781   C CB  . ASP A 1 103 ? -25.975 -47.163 12.825  1.00 113.30 ? 103 ASP A CB  1 
ATOM   782   C CG  . ASP A 1 103 ? -25.238 -45.899 12.418  1.00 115.44 ? 103 ASP A CG  1 
ATOM   783   O OD1 . ASP A 1 103 ? -24.003 -45.844 12.601  1.00 112.34 ? 103 ASP A OD1 1 
ATOM   784   O OD2 . ASP A 1 103 ? -25.892 -44.959 11.920  1.00 122.75 ? 103 ASP A OD2 1 
ATOM   785   N N   . ARG A 1 104 ? -23.078 -48.275 12.178  1.00 118.36 ? 104 ARG A N   1 
ATOM   786   C CA  . ARG A 1 104 ? -22.185 -48.914 11.216  1.00 117.99 ? 104 ARG A CA  1 
ATOM   787   C C   . ARG A 1 104 ? -21.524 -50.157 11.795  1.00 118.04 ? 104 ARG A C   1 
ATOM   788   O O   . ARG A 1 104 ? -21.266 -51.120 11.064  1.00 119.14 ? 104 ARG A O   1 
ATOM   789   C CB  . ARG A 1 104 ? -21.116 -47.922 10.760  1.00 115.39 ? 104 ARG A CB  1 
ATOM   790   C CG  . ARG A 1 104 ? -21.666 -46.579 10.302  1.00 117.43 ? 104 ARG A CG  1 
ATOM   791   C CD  . ARG A 1 104 ? -20.547 -45.597 9.983   1.00 115.21 ? 104 ARG A CD  1 
ATOM   792   N NE  . ARG A 1 104 ? -19.849 -45.903 8.739   1.00 124.74 ? 104 ARG A NE  1 
ATOM   793   C CZ  . ARG A 1 104 ? -20.038 -45.246 7.600   1.00 125.74 ? 104 ARG A CZ  1 
ATOM   794   N NH1 . ARG A 1 104 ? -20.902 -44.240 7.546   1.00 126.06 ? 104 ARG A NH1 1 
ATOM   795   N NH2 . ARG A 1 104 ? -19.361 -45.590 6.514   1.00 121.61 ? 104 ARG A NH2 1 
ATOM   796   N N   . ILE A 1 105 ? -21.247 -50.159 13.098  1.00 110.75 ? 105 ILE A N   1 
ATOM   797   C CA  . ILE A 1 105 ? -20.594 -51.307 13.718  1.00 107.90 ? 105 ILE A CA  1 
ATOM   798   C C   . ILE A 1 105 ? -21.587 -52.444 13.924  1.00 110.48 ? 105 ILE A C   1 
ATOM   799   O O   . ILE A 1 105 ? -21.307 -53.601 13.592  1.00 110.16 ? 105 ILE A O   1 
ATOM   800   C CB  . ILE A 1 105 ? -19.927 -50.891 15.041  1.00 102.71 ? 105 ILE A CB  1 
ATOM   801   C CG1 . ILE A 1 105 ? -19.040 -49.664 14.825  1.00 98.70  ? 105 ILE A CG1 1 
ATOM   802   C CG2 . ILE A 1 105 ? -19.120 -52.043 15.610  1.00 97.30  ? 105 ILE A CG2 1 
ATOM   803   C CD1 . ILE A 1 105 ? -18.420 -49.135 16.094  1.00 95.30  ? 105 ILE A CD1 1 
ATOM   804   N N   . MET A 1 106 ? -22.764 -52.134 14.472  1.00 110.53 ? 106 MET A N   1 
ATOM   805   C CA  . MET A 1 106 ? -23.823 -53.118 14.660  1.00 109.63 ? 106 MET A CA  1 
ATOM   806   C C   . MET A 1 106 ? -24.705 -53.271 13.427  1.00 114.00 ? 106 MET A C   1 
ATOM   807   O O   . MET A 1 106 ? -25.891 -53.603 13.552  1.00 114.06 ? 106 MET A O   1 
ATOM   808   C CB  . MET A 1 106 ? -24.667 -52.753 15.882  1.00 111.31 ? 106 MET A CB  1 
ATOM   809   C CG  . MET A 1 106 ? -23.976 -53.024 17.212  1.00 113.04 ? 106 MET A CG  1 
ATOM   810   S SD  . MET A 1 106 ? -23.804 -54.782 17.580  1.00 110.95 ? 106 MET A SD  1 
ATOM   811   C CE  . MET A 1 106 ? -22.334 -54.786 18.602  1.00 109.88 ? 106 MET A CE  1 
ATOM   812   N N   . GLU A 1 107 ? -24.151 -53.045 12.233  1.00 128.60 ? 107 GLU A N   1 
ATOM   813   C CA  . GLU A 1 107 ? -24.950 -53.118 11.015  1.00 129.95 ? 107 GLU A CA  1 
ATOM   814   C C   . GLU A 1 107 ? -25.275 -54.558 10.637  1.00 130.35 ? 107 GLU A C   1 
ATOM   815   O O   . GLU A 1 107 ? -26.331 -54.818 10.050  1.00 130.38 ? 107 GLU A O   1 
ATOM   816   C CB  . GLU A 1 107 ? -24.220 -52.418 9.869   1.00 132.17 ? 107 GLU A CB  1 
ATOM   817   C CG  . GLU A 1 107 ? -25.048 -52.267 8.605   1.00 145.21 ? 107 GLU A CG  1 
ATOM   818   C CD  . GLU A 1 107 ? -24.376 -51.378 7.581   1.00 151.55 ? 107 GLU A CD  1 
ATOM   819   O OE1 . GLU A 1 107 ? -24.101 -50.203 7.905   1.00 151.13 ? 107 GLU A OE1 1 
ATOM   820   O OE2 . GLU A 1 107 ? -24.119 -51.852 6.455   1.00 151.18 ? 107 GLU A OE2 1 
ATOM   821   N N   . GLU A 1 108 ? -24.393 -55.502 10.964  1.00 123.81 ? 108 GLU A N   1 
ATOM   822   C CA  . GLU A 1 108 ? -24.614 -56.913 10.680  1.00 122.59 ? 108 GLU A CA  1 
ATOM   823   C C   . GLU A 1 108 ? -25.093 -57.676 11.908  1.00 121.71 ? 108 GLU A C   1 
ATOM   824   O O   . GLU A 1 108 ? -25.017 -58.910 11.932  1.00 122.58 ? 108 GLU A O   1 
ATOM   825   C CB  . GLU A 1 108 ? -23.328 -57.542 10.139  1.00 127.06 ? 108 GLU A CB  1 
ATOM   826   C CG  . GLU A 1 108 ? -22.810 -56.904 8.859   1.00 130.84 ? 108 GLU A CG  1 
ATOM   827   C CD  . GLU A 1 108 ? -21.550 -57.574 8.341   1.00 128.06 ? 108 GLU A CD  1 
ATOM   828   O OE1 . GLU A 1 108 ? -20.748 -58.059 9.168   1.00 126.05 ? 108 GLU A OE1 1 
ATOM   829   O OE2 . GLU A 1 108 ? -21.362 -57.616 7.107   1.00 130.34 ? 108 GLU A OE2 1 
ATOM   830   N N   . LYS A 1 109 ? -25.611 -56.964 12.907  1.00 112.96 ? 109 LYS A N   1 
ATOM   831   C CA  . LYS A 1 109 ? -26.017 -57.546 14.180  1.00 105.49 ? 109 LYS A CA  1 
ATOM   832   C C   . LYS A 1 109 ? -24.948 -58.487 14.731  1.00 106.70 ? 109 LYS A C   1 
ATOM   833   O O   . LYS A 1 109 ? -25.212 -59.682 14.945  1.00 107.31 ? 109 LYS A O   1 
ATOM   834   C CB  . LYS A 1 109 ? -27.358 -58.264 14.051  1.00 100.69 ? 109 LYS A CB  1 
ATOM   835   C CG  . LYS A 1 109 ? -28.564 -57.337 13.991  1.00 96.60  ? 109 LYS A CG  1 
ATOM   836   C CD  . LYS A 1 109 ? -29.841 -58.129 13.765  1.00 91.57  ? 109 LYS A CD  1 
ATOM   837   C CE  . LYS A 1 109 ? -30.027 -59.205 14.826  1.00 90.96  ? 109 LYS A CE  1 
ATOM   838   N NZ  . LYS A 1 109 ? -30.294 -58.626 16.167  1.00 90.86  ? 109 LYS A NZ  1 
ATOM   839   N N   . PRO A 1 110 ? -23.734 -57.997 14.983  1.00 104.32 ? 110 PRO A N   1 
ATOM   840   C CA  . PRO A 1 110 ? -22.703 -58.870 15.548  1.00 101.50 ? 110 PRO A CA  1 
ATOM   841   C C   . PRO A 1 110 ? -22.986 -59.144 17.012  1.00 105.44 ? 110 PRO A C   1 
ATOM   842   O O   . PRO A 1 110 ? -23.404 -58.258 17.761  1.00 104.36 ? 110 PRO A O   1 
ATOM   843   C CB  . PRO A 1 110 ? -21.408 -58.066 15.368  1.00 97.61  ? 110 PRO A CB  1 
ATOM   844   C CG  . PRO A 1 110 ? -21.755 -56.937 14.448  1.00 101.22 ? 110 PRO A CG  1 
ATOM   845   C CD  . PRO A 1 110 ? -23.197 -56.659 14.690  1.00 106.12 ? 110 PRO A CD  1 
ATOM   846   N N   . SER A 1 111 ? -22.741 -60.387 17.419  1.00 120.53 ? 111 SER A N   1 
ATOM   847   C CA  . SER A 1 111 ? -22.988 -60.765 18.804  1.00 122.08 ? 111 SER A CA  1 
ATOM   848   C C   . SER A 1 111 ? -22.022 -60.054 19.742  1.00 122.10 ? 111 SER A C   1 
ATOM   849   O O   . SER A 1 111 ? -22.437 -59.454 20.740  1.00 121.87 ? 111 SER A O   1 
ATOM   850   C CB  . SER A 1 111 ? -22.878 -62.281 18.960  1.00 123.99 ? 111 SER A CB  1 
ATOM   851   O OG  . SER A 1 111 ? -22.921 -62.650 20.327  1.00 126.48 ? 111 SER A OG  1 
ATOM   852   N N   . HIS A 1 112 ? -20.732 -60.110 19.438  1.00 107.69 ? 112 HIS A N   1 
ATOM   853   C CA  . HIS A 1 112 ? -19.711 -59.480 20.257  1.00 102.26 ? 112 HIS A CA  1 
ATOM   854   C C   . HIS A 1 112 ? -18.871 -58.533 19.411  1.00 96.09  ? 112 HIS A C   1 
ATOM   855   O O   . HIS A 1 112 ? -18.654 -58.765 18.217  1.00 95.54  ? 112 HIS A O   1 
ATOM   856   C CB  . HIS A 1 112 ? -18.821 -60.533 20.919  1.00 104.36 ? 112 HIS A CB  1 
ATOM   857   C CG  . HIS A 1 112 ? -19.589 -61.596 21.640  1.00 107.69 ? 112 HIS A CG  1 
ATOM   858   N ND1 . HIS A 1 112 ? -20.315 -61.343 22.784  1.00 110.48 ? 112 HIS A ND1 1 
ATOM   859   C CD2 . HIS A 1 112 ? -19.754 -62.913 21.372  1.00 107.73 ? 112 HIS A CD2 1 
ATOM   860   C CE1 . HIS A 1 112 ? -20.889 -62.461 23.193  1.00 112.92 ? 112 HIS A CE1 1 
ATOM   861   N NE2 . HIS A 1 112 ? -20.565 -63.428 22.354  1.00 109.13 ? 112 HIS A NE2 1 
ATOM   862   N N   . VAL A 1 113 ? -18.398 -57.461 20.041  1.00 95.13  ? 113 VAL A N   1 
ATOM   863   C CA  . VAL A 1 113 ? -17.581 -56.454 19.378  1.00 90.36  ? 113 VAL A CA  1 
ATOM   864   C C   . VAL A 1 113 ? -16.236 -56.371 20.086  1.00 86.45  ? 113 VAL A C   1 
ATOM   865   O O   . VAL A 1 113 ? -16.179 -56.195 21.308  1.00 86.63  ? 113 VAL A O   1 
ATOM   866   C CB  . VAL A 1 113 ? -18.280 -55.081 19.354  1.00 89.33  ? 113 VAL A CB  1 
ATOM   867   C CG1 . VAL A 1 113 ? -18.909 -54.772 20.704  1.00 96.34  ? 113 VAL A CG1 1 
ATOM   868   C CG2 . VAL A 1 113 ? -17.288 -53.996 18.957  1.00 86.72  ? 113 VAL A CG2 1 
ATOM   869   N N   . PHE A 1 114 ? -15.158 -56.504 19.318  1.00 84.58  ? 114 PHE A N   1 
ATOM   870   C CA  . PHE A 1 114 ? -13.807 -56.380 19.844  1.00 84.97  ? 114 PHE A CA  1 
ATOM   871   C C   . PHE A 1 114 ? -13.385 -54.917 19.850  1.00 84.82  ? 114 PHE A C   1 
ATOM   872   O O   . PHE A 1 114 ? -13.618 -54.186 18.882  1.00 84.72  ? 114 PHE A O   1 
ATOM   873   C CB  . PHE A 1 114 ? -12.829 -57.205 19.006  1.00 86.49  ? 114 PHE A CB  1 
ATOM   874   C CG  . PHE A 1 114 ? -12.875 -58.681 19.290  1.00 86.86  ? 114 PHE A CG  1 
ATOM   875   C CD1 . PHE A 1 114 ? -13.489 -59.169 20.430  1.00 87.08  ? 114 PHE A CD1 1 
ATOM   876   C CD2 . PHE A 1 114 ? -12.315 -59.583 18.400  1.00 93.34  ? 114 PHE A CD2 1 
ATOM   877   C CE1 . PHE A 1 114 ? -13.533 -60.531 20.682  1.00 89.24  ? 114 PHE A CE1 1 
ATOM   878   C CE2 . PHE A 1 114 ? -12.359 -60.940 18.647  1.00 95.62  ? 114 PHE A CE2 1 
ATOM   879   C CZ  . PHE A 1 114 ? -12.968 -61.414 19.789  1.00 93.44  ? 114 PHE A CZ  1 
ATOM   880   N N   . LEU A 1 115 ? -12.769 -54.490 20.952  1.00 85.48  ? 115 LEU A N   1 
ATOM   881   C CA  . LEU A 1 115 ? -12.244 -53.134 21.083  1.00 86.13  ? 115 LEU A CA  1 
ATOM   882   C C   . LEU A 1 115 ? -10.855 -53.214 21.703  1.00 87.25  ? 115 LEU A C   1 
ATOM   883   O O   . LEU A 1 115 ? -10.717 -53.537 22.888  1.00 88.45  ? 115 LEU A O   1 
ATOM   884   C CB  . LEU A 1 115 ? -13.177 -52.252 21.919  1.00 87.28  ? 115 LEU A CB  1 
ATOM   885   C CG  . LEU A 1 115 ? -12.820 -50.761 22.012  1.00 87.97  ? 115 LEU A CG  1 
ATOM   886   C CD1 . LEU A 1 115 ? -14.080 -49.913 21.993  1.00 97.71  ? 115 LEU A CD1 1 
ATOM   887   C CD2 . LEU A 1 115 ? -11.990 -50.454 23.252  1.00 91.54  ? 115 LEU A CD2 1 
ATOM   888   N N   . LEU A 1 116 ? -9.831  -52.919 20.904  1.00 86.86  ? 116 LEU A N   1 
ATOM   889   C CA  . LEU A 1 116 ? -8.452  -52.893 21.366  1.00 86.95  ? 116 LEU A CA  1 
ATOM   890   C C   . LEU A 1 116 ? -7.788  -51.604 20.902  1.00 85.24  ? 116 LEU A C   1 
ATOM   891   O O   . LEU A 1 116 ? -8.232  -50.957 19.950  1.00 82.30  ? 116 LEU A O   1 
ATOM   892   C CB  . LEU A 1 116 ? -7.656  -54.111 20.863  1.00 90.54  ? 116 LEU A CB  1 
ATOM   893   C CG  . LEU A 1 116 ? -7.762  -54.462 19.376  1.00 90.03  ? 116 LEU A CG  1 
ATOM   894   C CD1 . LEU A 1 116 ? -6.671  -53.775 18.565  1.00 87.94  ? 116 LEU A CD1 1 
ATOM   895   C CD2 . LEU A 1 116 ? -7.716  -55.970 19.167  1.00 90.88  ? 116 LEU A CD2 1 
ATOM   896   N N   . ASN A 1 117 ? -6.716  -51.236 21.593  1.00 84.25  ? 117 ASN A N   1 
ATOM   897   C CA  . ASN A 1 117 ? -6.026  -49.988 21.312  1.00 82.35  ? 117 ASN A CA  1 
ATOM   898   C C   . ASN A 1 117 ? -4.887  -50.210 20.322  1.00 82.24  ? 117 ASN A C   1 
ATOM   899   O O   . ASN A 1 117 ? -4.434  -51.333 20.092  1.00 81.45  ? 117 ASN A O   1 
ATOM   900   C CB  . ASN A 1 117 ? -5.486  -49.371 22.604  1.00 84.19  ? 117 ASN A CB  1 
ATOM   901   C CG  . ASN A 1 117 ? -5.101  -47.913 22.442  1.00 84.63  ? 117 ASN A CG  1 
ATOM   902   O OD1 . ASN A 1 117 ? -5.492  -47.256 21.476  1.00 83.98  ? 117 ASN A OD1 1 
ATOM   903   N ND2 . ASN A 1 117 ? -4.322  -47.401 23.388  1.00 84.21  ? 117 ASN A ND2 1 
ATOM   904   N N   . CYS A 1 118 ? -4.431  -49.106 19.731  1.00 82.40  ? 118 CYS A N   1 
ATOM   905   C CA  . CYS A 1 118 ? -3.360  -49.170 18.743  1.00 79.29  ? 118 CYS A CA  1 
ATOM   906   C C   . CYS A 1 118 ? -2.017  -49.470 19.400  1.00 79.61  ? 118 CYS A C   1 
ATOM   907   O O   . CYS A 1 118 ? -1.311  -50.402 18.998  1.00 83.16  ? 118 CYS A O   1 
ATOM   908   C CB  . CYS A 1 118 ? -3.304  -47.858 17.962  1.00 77.53  ? 118 CYS A CB  1 
ATOM   909   S SG  . CYS A 1 118 ? -1.829  -47.653 16.966  1.00 67.36  ? 118 CYS A SG  1 
ATOM   910   N N   . ASP A 1 119 ? -1.648  -48.689 20.415  1.00 82.26  ? 119 ASP A N   1 
ATOM   911   C CA  . ASP A 1 119 ? -0.333  -48.798 21.048  1.00 84.99  ? 119 ASP A CA  1 
ATOM   912   C C   . ASP A 1 119 ? -0.381  -49.841 22.167  1.00 89.59  ? 119 ASP A C   1 
ATOM   913   O O   . ASP A 1 119 ? -0.338  -49.538 23.360  1.00 93.30  ? 119 ASP A O   1 
ATOM   914   C CB  . ASP A 1 119 ? 0.119   -47.438 21.563  1.00 84.72  ? 119 ASP A CB  1 
ATOM   915   C CG  . ASP A 1 119 ? -0.976  -46.708 22.315  1.00 82.18  ? 119 ASP A CG  1 
ATOM   916   O OD1 . ASP A 1 119 ? -2.082  -47.271 22.449  1.00 80.55  ? 119 ASP A OD1 1 
ATOM   917   O OD2 . ASP A 1 119 ? -0.731  -45.571 22.774  1.00 81.64  ? 119 ASP A OD2 1 
ATOM   918   N N   . VAL A 1 120 ? -0.470  -51.102 21.748  1.00 100.09 ? 120 VAL A N   1 
ATOM   919   C CA  . VAL A 1 120 ? -0.519  -52.241 22.658  1.00 103.13 ? 120 VAL A CA  1 
ATOM   920   C C   . VAL A 1 120 ? 0.332   -53.358 22.069  1.00 103.86 ? 120 VAL A C   1 
ATOM   921   O O   . VAL A 1 120 ? 0.287   -53.610 20.861  1.00 102.85 ? 120 VAL A O   1 
ATOM   922   C CB  . VAL A 1 120 ? -1.972  -52.714 22.890  1.00 103.61 ? 120 VAL A CB  1 
ATOM   923   C CG1 . VAL A 1 120 ? -1.999  -54.081 23.550  1.00 106.34 ? 120 VAL A CG1 1 
ATOM   924   C CG2 . VAL A 1 120 ? -2.742  -51.702 23.729  1.00 103.05 ? 120 VAL A CG2 1 
ATOM   925   N N   . CYS A 1 121 ? 1.124   -54.022 22.920  1.00 97.58  ? 121 CYS A N   1 
ATOM   926   C CA  . CYS A 1 121 ? 2.031   -55.088 22.482  1.00 99.87  ? 121 CYS A CA  1 
ATOM   927   C C   . CYS A 1 121 ? 1.849   -56.309 23.378  1.00 99.59  ? 121 CYS A C   1 
ATOM   928   O O   . CYS A 1 121 ? 2.664   -56.564 24.266  1.00 96.90  ? 121 CYS A O   1 
ATOM   929   C CB  . CYS A 1 121 ? 3.470   -54.602 22.486  1.00 100.37 ? 121 CYS A CB  1 
ATOM   930   S SG  . CYS A 1 121 ? 3.818   -53.391 21.208  1.00 105.51 ? 121 CYS A SG  1 
ATOM   931   N N   . CYS A 1 122 ? 0.797   -57.077 23.119  1.00 101.45 ? 122 CYS A N   1 
ATOM   932   C CA  . CYS A 1 122 ? 0.521   -58.324 23.820  1.00 99.70  ? 122 CYS A CA  1 
ATOM   933   C C   . CYS A 1 122 ? 0.506   -59.477 22.818  1.00 100.17 ? 122 CYS A C   1 
ATOM   934   O O   . CYS A 1 122 ? 0.794   -59.305 21.631  1.00 100.20 ? 122 CYS A O   1 
ATOM   935   C CB  . CYS A 1 122 ? -0.803  -58.238 24.588  1.00 97.17  ? 122 CYS A CB  1 
ATOM   936   S SG  . CYS A 1 122 ? -2.226  -57.754 23.583  1.00 96.51  ? 122 CYS A SG  1 
ATOM   937   N N   . SER A 1 123 ? 0.173   -60.670 23.313  1.00 98.19  ? 123 SER A N   1 
ATOM   938   C CA  . SER A 1 123 ? 0.123   -61.853 22.462  1.00 101.85 ? 123 SER A CA  1 
ATOM   939   C C   . SER A 1 123 ? -1.161  -61.946 21.648  1.00 109.54 ? 123 SER A C   1 
ATOM   940   O O   . SER A 1 123 ? -1.208  -62.716 20.682  1.00 112.12 ? 123 SER A O   1 
ATOM   941   C CB  . SER A 1 123 ? 0.283   -63.115 23.312  1.00 105.45 ? 123 SER A CB  1 
ATOM   942   O OG  . SER A 1 123 ? -0.744  -63.198 24.286  1.00 110.23 ? 123 SER A OG  1 
ATOM   943   N N   . PHE A 1 124 ? -2.194  -61.187 22.018  1.00 113.38 ? 124 PHE A N   1 
ATOM   944   C CA  . PHE A 1 124 ? -3.485  -61.160 21.337  1.00 118.06 ? 124 PHE A CA  1 
ATOM   945   C C   . PHE A 1 124 ? -4.111  -62.548 21.246  1.00 130.36 ? 124 PHE A C   1 
ATOM   946   O O   . PHE A 1 124 ? -4.164  -63.136 20.157  1.00 126.17 ? 124 PHE A O   1 
ATOM   947   C CB  . PHE A 1 124 ? -3.345  -60.561 19.935  1.00 112.32 ? 124 PHE A CB  1 
ATOM   948   C CG  . PHE A 1 124 ? -2.951  -59.114 19.931  1.00 104.31 ? 124 PHE A CG  1 
ATOM   949   C CD1 . PHE A 1 124 ? -3.897  -58.125 20.145  1.00 98.14  ? 124 PHE A CD1 1 
ATOM   950   C CD2 . PHE A 1 124 ? -1.637  -58.740 19.704  1.00 101.68 ? 124 PHE A CD2 1 
ATOM   951   C CE1 . PHE A 1 124 ? -3.537  -56.790 20.139  1.00 92.77  ? 124 PHE A CE1 1 
ATOM   952   C CE2 . PHE A 1 124 ? -1.271  -57.409 19.696  1.00 98.16  ? 124 PHE A CE2 1 
ATOM   953   C CZ  . PHE A 1 124 ? -2.223  -56.432 19.915  1.00 93.87  ? 124 PHE A CZ  1 
ATOM   954   N N   . PRO A 1 125 ? -4.593  -63.109 22.359  1.00 168.69 ? 125 PRO A N   1 
ATOM   955   C CA  . PRO A 1 125 ? -5.323  -64.388 22.314  1.00 170.35 ? 125 PRO A CA  1 
ATOM   956   C C   . PRO A 1 125 ? -6.819  -64.166 22.101  1.00 169.16 ? 125 PRO A C   1 
ATOM   957   O O   . PRO A 1 125 ? -7.650  -64.472 22.963  1.00 170.21 ? 125 PRO A O   1 
ATOM   958   C CB  . PRO A 1 125 ? -5.008  -64.995 23.688  1.00 172.95 ? 125 PRO A CB  1 
ATOM   959   C CG  . PRO A 1 125 ? -4.347  -63.876 24.515  1.00 172.26 ? 125 PRO A CG  1 
ATOM   960   C CD  . PRO A 1 125 ? -4.479  -62.610 23.736  1.00 169.31 ? 125 PRO A CD  1 
ATOM   961   N N   . LEU A 1 126 ? -7.165  -63.620 20.932  1.00 138.74 ? 126 LEU A N   1 
ATOM   962   C CA  . LEU A 1 126 ? -8.531  -63.164 20.694  1.00 127.96 ? 126 LEU A CA  1 
ATOM   963   C C   . LEU A 1 126 ? -9.535  -64.307 20.775  1.00 121.89 ? 126 LEU A C   1 
ATOM   964   O O   . LEU A 1 126 ? -10.660 -64.120 21.252  1.00 118.12 ? 126 LEU A O   1 
ATOM   965   C CB  . LEU A 1 126 ? -8.623  -62.477 19.332  1.00 120.45 ? 126 LEU A CB  1 
ATOM   966   C CG  . LEU A 1 126 ? -7.710  -61.273 19.096  1.00 116.17 ? 126 LEU A CG  1 
ATOM   967   C CD1 . LEU A 1 126 ? -8.024  -60.621 17.757  1.00 107.57 ? 126 LEU A CD1 1 
ATOM   968   C CD2 . LEU A 1 126 ? -7.820  -60.268 20.229  1.00 112.85 ? 126 LEU A CD2 1 
ATOM   969   N N   . GLN A 1 127 ? -9.155  -65.497 20.310  1.00 121.99 ? 127 GLN A N   1 
ATOM   970   C CA  . GLN A 1 127 ? -10.079 -66.624 20.336  1.00 120.82 ? 127 GLN A CA  1 
ATOM   971   C C   . GLN A 1 127 ? -10.247 -67.207 21.734  1.00 118.20 ? 127 GLN A C   1 
ATOM   972   O O   . GLN A 1 127 ? -11.282 -67.819 22.016  1.00 112.63 ? 127 GLN A O   1 
ATOM   973   C CB  . GLN A 1 127 ? -9.617  -67.699 19.348  1.00 123.77 ? 127 GLN A CB  1 
ATOM   974   C CG  . GLN A 1 127 ? -10.674 -68.741 19.012  1.00 122.31 ? 127 GLN A CG  1 
ATOM   975   C CD  . GLN A 1 127 ? -10.258 -69.639 17.864  1.00 131.94 ? 127 GLN A CD  1 
ATOM   976   O OE1 . GLN A 1 127 ? -9.263  -69.380 17.188  1.00 131.01 ? 127 GLN A OE1 1 
ATOM   977   N NE2 . GLN A 1 127 ? -11.026 -70.698 17.632  1.00 142.43 ? 127 GLN A NE2 1 
ATOM   978   N N   . GLY A 1 128 ? -9.266  -67.018 22.614  1.00 123.93 ? 128 GLY A N   1 
ATOM   979   C CA  . GLY A 1 128 ? -9.367  -67.506 23.975  1.00 121.72 ? 128 GLY A CA  1 
ATOM   980   C C   . GLY A 1 128 ? -10.185 -66.591 24.863  1.00 122.40 ? 128 GLY A C   1 
ATOM   981   O O   . GLY A 1 128 ? -10.932 -67.060 25.728  1.00 119.08 ? 128 GLY A O   1 
ATOM   982   N N   . ILE A 1 129 ? -10.051 -65.279 24.661  1.00 133.64 ? 129 ILE A N   1 
ATOM   983   C CA  . ILE A 1 129 ? -10.835 -64.326 25.442  1.00 132.91 ? 129 ILE A CA  1 
ATOM   984   C C   . ILE A 1 129 ? -12.281 -64.290 24.957  1.00 131.63 ? 129 ILE A C   1 
ATOM   985   O O   . ILE A 1 129 ? -13.202 -64.064 25.753  1.00 131.50 ? 129 ILE A O   1 
ATOM   986   C CB  . ILE A 1 129 ? -10.175 -62.935 25.395  1.00 131.21 ? 129 ILE A CB  1 
ATOM   987   C CG1 . ILE A 1 129 ? -10.976 -61.911 26.203  1.00 130.41 ? 129 ILE A CG1 1 
ATOM   988   C CG2 . ILE A 1 129 ? -10.013 -62.459 23.962  1.00 131.00 ? 129 ILE A CG2 1 
ATOM   989   C CD1 . ILE A 1 129 ? -11.261 -62.317 27.624  1.00 132.38 ? 129 ILE A CD1 1 
ATOM   990   N N   . LEU A 1 130 ? -12.508 -64.523 23.662  1.00 121.20 ? 130 LEU A N   1 
ATOM   991   C CA  . LEU A 1 130 ? -13.869 -64.603 23.145  1.00 113.39 ? 130 LEU A CA  1 
ATOM   992   C C   . LEU A 1 130 ? -14.633 -65.736 23.819  1.00 111.92 ? 130 LEU A C   1 
ATOM   993   O O   . LEU A 1 130 ? -15.774 -65.558 24.263  1.00 111.07 ? 130 LEU A O   1 
ATOM   994   C CB  . LEU A 1 130 ? -13.831 -64.797 21.627  1.00 109.16 ? 130 LEU A CB  1 
ATOM   995   C CG  . LEU A 1 130 ? -14.999 -64.348 20.741  1.00 100.36 ? 130 LEU A CG  1 
ATOM   996   C CD1 . LEU A 1 130 ? -14.614 -64.492 19.277  1.00 100.48 ? 130 LEU A CD1 1 
ATOM   997   C CD2 . LEU A 1 130 ? -16.270 -65.123 21.027  1.00 109.11 ? 130 LEU A CD2 1 
ATOM   998   N N   . ASP A 1 131 ? -14.013 -66.914 23.907  1.00 111.29 ? 131 ASP A N   1 
ATOM   999   C CA  . ASP A 1 131 ? -14.672 -68.053 24.535  1.00 106.63 ? 131 ASP A CA  1 
ATOM   1000  C C   . ASP A 1 131 ? -14.781 -67.876 26.043  1.00 112.52 ? 131 ASP A C   1 
ATOM   1001  O O   . ASP A 1 131 ? -15.737 -68.364 26.655  1.00 113.43 ? 131 ASP A O   1 
ATOM   1002  C CB  . ASP A 1 131 ? -13.918 -69.338 24.204  1.00 105.30 ? 131 ASP A CB  1 
ATOM   1003  C CG  . ASP A 1 131 ? -13.703 -69.513 22.717  1.00 106.82 ? 131 ASP A CG  1 
ATOM   1004  O OD1 . ASP A 1 131 ? -14.489 -68.943 21.931  1.00 105.66 ? 131 ASP A OD1 1 
ATOM   1005  O OD2 . ASP A 1 131 ? -12.743 -70.214 22.333  1.00 109.50 ? 131 ASP A OD2 1 
ATOM   1006  N N   . ALA A 1 132 ? -13.812 -67.193 26.658  1.00 115.85 ? 132 ALA A N   1 
ATOM   1007  C CA  . ALA A 1 132 ? -13.918 -66.896 28.081  1.00 115.55 ? 132 ALA A CA  1 
ATOM   1008  C C   . ALA A 1 132 ? -15.059 -65.931 28.366  1.00 116.94 ? 132 ALA A C   1 
ATOM   1009  O O   . ALA A 1 132 ? -15.699 -66.026 29.420  1.00 118.43 ? 132 ALA A O   1 
ATOM   1010  C CB  . ALA A 1 132 ? -12.599 -66.325 28.602  1.00 116.64 ? 132 ALA A CB  1 
ATOM   1011  N N   . HIS A 1 133 ? -15.341 -65.013 27.440  1.00 125.04 ? 133 HIS A N   1 
ATOM   1012  C CA  . HIS A 1 133 ? -16.444 -64.078 27.634  1.00 123.62 ? 133 HIS A CA  1 
ATOM   1013  C C   . HIS A 1 133 ? -17.794 -64.752 27.425  1.00 123.42 ? 133 HIS A C   1 
ATOM   1014  O O   . HIS A 1 133 ? -18.762 -64.437 28.126  1.00 123.06 ? 133 HIS A O   1 
ATOM   1015  C CB  . HIS A 1 133 ? -16.296 -62.884 26.693  1.00 122.36 ? 133 HIS A CB  1 
ATOM   1016  C CG  . HIS A 1 133 ? -17.427 -61.907 26.780  1.00 121.32 ? 133 HIS A CG  1 
ATOM   1017  N ND1 . HIS A 1 133 ? -17.950 -61.484 27.982  1.00 122.39 ? 133 HIS A ND1 1 
ATOM   1018  C CD2 . HIS A 1 133 ? -18.131 -61.267 25.816  1.00 119.62 ? 133 HIS A CD2 1 
ATOM   1019  C CE1 . HIS A 1 133 ? -18.930 -60.627 27.756  1.00 121.85 ? 133 HIS A CE1 1 
ATOM   1020  N NE2 . HIS A 1 133 ? -19.060 -60.477 26.451  1.00 120.26 ? 133 HIS A NE2 1 
ATOM   1021  N N   . ARG A 1 134 ? -17.878 -65.670 26.458  1.00 118.12 ? 134 ARG A N   1 
ATOM   1022  C CA  . ARG A 1 134 ? -19.119 -66.407 26.243  1.00 113.29 ? 134 ARG A CA  1 
ATOM   1023  C C   . ARG A 1 134 ? -19.499 -67.213 27.476  1.00 114.45 ? 134 ARG A C   1 
ATOM   1024  O O   . ARG A 1 134 ? -20.686 -67.360 27.791  1.00 114.29 ? 134 ARG A O   1 
ATOM   1025  C CB  . ARG A 1 134 ? -18.978 -67.322 25.027  1.00 110.24 ? 134 ARG A CB  1 
ATOM   1026  C CG  . ARG A 1 134 ? -19.032 -66.598 23.696  1.00 105.78 ? 134 ARG A CG  1 
ATOM   1027  C CD  . ARG A 1 134 ? -18.719 -67.542 22.551  1.00 103.68 ? 134 ARG A CD  1 
ATOM   1028  N NE  . ARG A 1 134 ? -18.984 -66.931 21.254  1.00 105.50 ? 134 ARG A NE  1 
ATOM   1029  C CZ  . ARG A 1 134 ? -18.617 -67.460 20.092  1.00 107.56 ? 134 ARG A CZ  1 
ATOM   1030  N NH1 . ARG A 1 134 ? -17.958 -68.610 20.063  1.00 109.31 ? 134 ARG A NH1 1 
ATOM   1031  N NH2 . ARG A 1 134 ? -18.902 -66.834 18.958  1.00 104.98 ? 134 ARG A NH2 1 
ATOM   1032  N N   . ARG A 1 135 ? -18.504 -67.747 28.185  1.00 126.92 ? 135 ARG A N   1 
ATOM   1033  C CA  . ARG A 1 135 ? -18.781 -68.470 29.420  1.00 128.84 ? 135 ARG A CA  1 
ATOM   1034  C C   . ARG A 1 135 ? -19.086 -67.509 30.563  1.00 128.49 ? 135 ARG A C   1 
ATOM   1035  O O   . ARG A 1 135 ? -20.029 -67.733 31.331  1.00 128.95 ? 135 ARG A O   1 
ATOM   1036  C CB  . ARG A 1 135 ? -17.600 -69.372 29.778  1.00 131.60 ? 135 ARG A CB  1 
ATOM   1037  C CG  . ARG A 1 135 ? -17.709 -70.005 31.153  1.00 139.48 ? 135 ARG A CG  1 
ATOM   1038  C CD  . ARG A 1 135 ? -16.569 -70.973 31.411  1.00 147.30 ? 135 ARG A CD  1 
ATOM   1039  N NE  . ARG A 1 135 ? -16.523 -71.391 32.809  1.00 155.37 ? 135 ARG A NE  1 
ATOM   1040  C CZ  . ARG A 1 135 ? -15.743 -70.838 33.731  1.00 153.51 ? 135 ARG A CZ  1 
ATOM   1041  N NH1 . ARG A 1 135 ? -14.934 -69.839 33.406  1.00 151.67 ? 135 ARG A NH1 1 
ATOM   1042  N NH2 . ARG A 1 135 ? -15.769 -71.286 34.979  1.00 156.14 ? 135 ARG A NH2 1 
ATOM   1043  N N   . TYR A 1 136 ? -18.298 -66.437 30.690  1.00 119.15 ? 136 TYR A N   1 
ATOM   1044  C CA  . TYR A 1 136 ? -18.553 -65.445 31.731  1.00 115.51 ? 136 TYR A CA  1 
ATOM   1045  C C   . TYR A 1 136 ? -19.877 -64.729 31.509  1.00 112.79 ? 136 TYR A C   1 
ATOM   1046  O O   . TYR A 1 136 ? -20.635 -64.505 32.459  1.00 111.64 ? 136 TYR A O   1 
ATOM   1047  C CB  . TYR A 1 136 ? -17.417 -64.423 31.785  1.00 116.25 ? 136 TYR A CB  1 
ATOM   1048  C CG  . TYR A 1 136 ? -16.093 -64.964 32.262  1.00 116.90 ? 136 TYR A CG  1 
ATOM   1049  C CD1 . TYR A 1 136 ? -16.034 -66.052 33.120  1.00 121.52 ? 136 TYR A CD1 1 
ATOM   1050  C CD2 . TYR A 1 136 ? -14.900 -64.380 31.860  1.00 115.16 ? 136 TYR A CD2 1 
ATOM   1051  C CE1 . TYR A 1 136 ? -14.821 -66.544 33.560  1.00 126.36 ? 136 TYR A CE1 1 
ATOM   1052  C CE2 . TYR A 1 136 ? -13.685 -64.864 32.292  1.00 118.75 ? 136 TYR A CE2 1 
ATOM   1053  C CZ  . TYR A 1 136 ? -13.650 -65.946 33.142  1.00 124.56 ? 136 TYR A CZ  1 
ATOM   1054  O OH  . TYR A 1 136 ? -12.439 -66.433 33.576  1.00 130.11 ? 136 TYR A OH  1 
ATOM   1055  N N   . GLY A 1 137 ? -20.172 -64.358 30.266  1.00 114.50 ? 137 GLY A N   1 
ATOM   1056  C CA  . GLY A 1 137 ? -21.339 -63.539 30.013  1.00 112.89 ? 137 GLY A CA  1 
ATOM   1057  C C   . GLY A 1 137 ? -21.078 -62.091 30.398  1.00 111.43 ? 137 GLY A C   1 
ATOM   1058  O O   . GLY A 1 137 ? -19.943 -61.610 30.376  1.00 115.38 ? 137 GLY A O   1 
ATOM   1059  N N   . GLY A 1 138 ? -22.147 -61.396 30.772  1.00 107.81 ? 138 GLY A N   1 
ATOM   1060  C CA  . GLY A 1 138 ? -22.022 -59.996 31.115  1.00 106.58 ? 138 GLY A CA  1 
ATOM   1061  C C   . GLY A 1 138 ? -21.674 -59.158 29.893  1.00 106.36 ? 138 GLY A C   1 
ATOM   1062  O O   . GLY A 1 138 ? -21.744 -59.600 28.747  1.00 107.85 ? 138 GLY A O   1 
ATOM   1063  N N   . ILE A 1 139 ? -21.291 -57.913 30.165  1.00 107.39 ? 139 ILE A N   1 
ATOM   1064  C CA  . ILE A 1 139 ? -20.991 -56.970 29.094  1.00 105.43 ? 139 ILE A CA  1 
ATOM   1065  C C   . ILE A 1 139 ? -19.603 -57.259 28.540  1.00 106.74 ? 139 ILE A C   1 
ATOM   1066  O O   . ILE A 1 139 ? -19.461 -57.707 27.398  1.00 108.48 ? 139 ILE A O   1 
ATOM   1067  C CB  . ILE A 1 139 ? -21.105 -55.513 29.574  1.00 103.51 ? 139 ILE A CB  1 
ATOM   1068  C CG1 . ILE A 1 139 ? -22.495 -55.258 30.161  1.00 102.38 ? 139 ILE A CG1 1 
ATOM   1069  C CG2 . ILE A 1 139 ? -20.843 -54.558 28.418  1.00 102.77 ? 139 ILE A CG2 1 
ATOM   1070  C CD1 . ILE A 1 139 ? -23.615 -55.330 29.150  1.00 105.25 ? 139 ILE A CD1 1 
ATOM   1071  N N   . GLY A 1 140 ? -18.572 -57.011 29.346  1.00 108.30 ? 140 GLY A N   1 
ATOM   1072  C CA  . GLY A 1 140 ? -17.202 -57.138 28.886  1.00 107.82 ? 140 GLY A CA  1 
ATOM   1073  C C   . GLY A 1 140 ? -16.410 -58.198 29.627  1.00 113.72 ? 140 GLY A C   1 
ATOM   1074  O O   . GLY A 1 140 ? -16.962 -58.943 30.444  1.00 115.72 ? 140 GLY A O   1 
ATOM   1075  N N   . THR A 1 141 ? -15.108 -58.275 29.346  1.00 112.80 ? 141 THR A N   1 
ATOM   1076  C CA  . THR A 1 141 ? -14.245 -59.259 29.987  1.00 115.02 ? 141 THR A CA  1 
ATOM   1077  C C   . THR A 1 141 ? -12.822 -58.754 30.174  1.00 117.50 ? 141 THR A C   1 
ATOM   1078  O O   . THR A 1 141 ? -12.027 -59.402 30.859  1.00 121.47 ? 141 THR A O   1 
ATOM   1079  C CB  . THR A 1 141 ? -14.226 -60.555 29.181  1.00 115.18 ? 141 THR A CB  1 
ATOM   1080  O OG1 . THR A 1 141 ? -14.694 -60.292 27.855  1.00 114.00 ? 141 THR A OG1 1 
ATOM   1081  C CG2 . THR A 1 141 ? -15.121 -61.588 29.826  1.00 117.85 ? 141 THR A CG2 1 
ATOM   1082  N N   . MET A 1 142 ? -12.481 -57.626 29.549  1.00 106.67 ? 142 MET A N   1 
ATOM   1083  C CA  . MET A 1 142 ? -11.176 -56.995 29.727  1.00 107.98 ? 142 MET A CA  1 
ATOM   1084  C C   . MET A 1 142 ? -10.033 -57.960 29.431  1.00 109.46 ? 142 MET A C   1 
ATOM   1085  O O   . MET A 1 142 ? -10.201 -58.927 28.681  1.00 108.77 ? 142 MET A O   1 
ATOM   1086  C CB  . MET A 1 142 ? -11.025 -56.442 31.149  1.00 111.77 ? 142 MET A CB  1 
ATOM   1087  C CG  . MET A 1 142 ? -11.069 -54.926 31.250  1.00 111.55 ? 142 MET A CG  1 
ATOM   1088  S SD  . MET A 1 142 ? -10.383 -54.314 32.805  1.00 114.74 ? 142 MET A SD  1 
ATOM   1089  C CE  . MET A 1 142 ? -8.769  -55.086 32.792  1.00 118.44 ? 142 MET A CE  1 
ATOM   1090  N N   . LEU A 1 143 ? -8.872  -57.688 30.023  1.00 110.40 ? 143 LEU A N   1 
ATOM   1091  C CA  . LEU A 1 143 ? -7.724  -58.582 30.027  1.00 112.14 ? 143 LEU A CA  1 
ATOM   1092  C C   . LEU A 1 143 ? -6.753  -58.089 31.086  1.00 114.76 ? 143 LEU A C   1 
ATOM   1093  O O   . LEU A 1 143 ? -6.566  -56.881 31.244  1.00 116.16 ? 143 LEU A O   1 
ATOM   1094  C CB  . LEU A 1 143 ? -7.027  -58.634 28.664  1.00 109.53 ? 143 LEU A CB  1 
ATOM   1095  C CG  . LEU A 1 143 ? -6.068  -59.814 28.501  1.00 110.04 ? 143 LEU A CG  1 
ATOM   1096  C CD1 . LEU A 1 143 ? -6.758  -60.963 27.785  1.00 117.12 ? 143 LEU A CD1 1 
ATOM   1097  C CD2 . LEU A 1 143 ? -4.791  -59.416 27.780  1.00 104.41 ? 143 LEU A CD2 1 
ATOM   1098  N N   . VAL A 1 144 ? -6.127  -59.028 31.793  1.00 117.67 ? 144 VAL A N   1 
ATOM   1099  C CA  . VAL A 1 144 ? -5.240  -58.710 32.901  1.00 120.22 ? 144 VAL A CA  1 
ATOM   1100  C C   . VAL A 1 144 ? -3.958  -59.519 32.756  1.00 124.06 ? 144 VAL A C   1 
ATOM   1101  O O   . VAL A 1 144 ? -3.877  -60.472 31.980  1.00 121.65 ? 144 VAL A O   1 
ATOM   1102  C CB  . VAL A 1 144 ? -5.898  -58.978 34.270  1.00 118.96 ? 144 VAL A CB  1 
ATOM   1103  C CG1 . VAL A 1 144 ? -6.978  -57.947 34.550  1.00 118.56 ? 144 VAL A CG1 1 
ATOM   1104  C CG2 . VAL A 1 144 ? -6.476  -60.384 34.312  1.00 117.42 ? 144 VAL A CG2 1 
ATOM   1105  N N   . ILE A 1 145 ? -2.949  -59.119 33.521  1.00 128.30 ? 145 ILE A N   1 
ATOM   1106  C CA  . ILE A 1 145 ? -1.658  -59.797 33.528  1.00 127.21 ? 145 ILE A CA  1 
ATOM   1107  C C   . ILE A 1 145 ? -0.994  -59.535 34.872  1.00 134.38 ? 145 ILE A C   1 
ATOM   1108  O O   . ILE A 1 145 ? -0.989  -58.402 35.363  1.00 130.99 ? 145 ILE A O   1 
ATOM   1109  C CB  . ILE A 1 145 ? -0.766  -59.340 32.354  1.00 124.93 ? 145 ILE A CB  1 
ATOM   1110  C CG1 . ILE A 1 145 ? 0.601   -60.025 32.410  1.00 126.67 ? 145 ILE A CG1 1 
ATOM   1111  C CG2 . ILE A 1 145 ? -0.634  -57.821 32.329  1.00 124.31 ? 145 ILE A CG2 1 
ATOM   1112  C CD1 . ILE A 1 145 ? 1.451   -59.790 31.179  1.00 121.38 ? 145 ILE A CD1 1 
ATOM   1113  N N   . LYS A 1 146 ? -0.460  -60.590 35.482  1.00 149.65 ? 146 LYS A N   1 
ATOM   1114  C CA  . LYS A 1 146 ? 0.152   -60.470 36.799  1.00 151.90 ? 146 LYS A CA  1 
ATOM   1115  C C   . LYS A 1 146 ? 1.463   -59.701 36.702  1.00 151.41 ? 146 LYS A C   1 
ATOM   1116  O O   . LYS A 1 146 ? 2.387   -60.120 35.998  1.00 151.67 ? 146 LYS A O   1 
ATOM   1117  C CB  . LYS A 1 146 ? 0.386   -61.853 37.401  1.00 157.84 ? 146 LYS A CB  1 
ATOM   1118  C CG  . LYS A 1 146 ? -0.877  -62.665 37.625  1.00 162.23 ? 146 LYS A CG  1 
ATOM   1119  C CD  . LYS A 1 146 ? -0.553  -64.004 38.270  1.00 173.78 ? 146 LYS A CD  1 
ATOM   1120  C CE  . LYS A 1 146 ? -1.813  -64.809 38.543  1.00 182.06 ? 146 LYS A CE  1 
ATOM   1121  N NZ  . LYS A 1 146 ? -1.506  -66.115 39.190  1.00 181.25 ? 146 LYS A NZ  1 
ATOM   1122  N N   . VAL A 1 147 ? 1.544   -58.575 37.409  1.00 140.09 ? 147 VAL A N   1 
ATOM   1123  C CA  . VAL A 1 147 ? 2.747   -57.758 37.453  1.00 135.65 ? 147 VAL A CA  1 
ATOM   1124  C C   . VAL A 1 147 ? 3.155   -57.590 38.912  1.00 136.27 ? 147 VAL A C   1 
ATOM   1125  O O   . VAL A 1 147 ? 2.392   -57.882 39.832  1.00 138.66 ? 147 VAL A O   1 
ATOM   1126  C CB  . VAL A 1 147 ? 2.555   -56.382 36.785  1.00 131.29 ? 147 VAL A CB  1 
ATOM   1127  C CG1 . VAL A 1 147 ? 2.017   -56.540 35.371  1.00 133.10 ? 147 VAL A CG1 1 
ATOM   1128  C CG2 . VAL A 1 147 ? 1.651   -55.494 37.628  1.00 130.90 ? 147 VAL A CG2 1 
ATOM   1129  N N   . SER A 1 148 ? 4.382   -57.120 39.111  1.00 132.54 ? 148 SER A N   1 
ATOM   1130  C CA  . SER A 1 148 ? 4.861   -56.869 40.461  1.00 129.36 ? 148 SER A CA  1 
ATOM   1131  C C   . SER A 1 148 ? 4.133   -55.676 41.070  1.00 130.30 ? 148 SER A C   1 
ATOM   1132  O O   . SER A 1 148 ? 3.724   -54.744 40.372  1.00 130.53 ? 148 SER A O   1 
ATOM   1133  C CB  . SER A 1 148 ? 6.370   -56.620 40.456  1.00 125.61 ? 148 SER A CB  1 
ATOM   1134  O OG  . SER A 1 148 ? 6.693   -55.436 39.749  1.00 124.89 ? 148 SER A OG  1 
ATOM   1135  N N   . ALA A 1 149 ? 3.972   -55.715 42.396  1.00 131.87 ? 149 ALA A N   1 
ATOM   1136  C CA  . ALA A 1 149 ? 3.319   -54.609 43.087  1.00 128.36 ? 149 ALA A CA  1 
ATOM   1137  C C   . ALA A 1 149 ? 4.158   -53.341 43.016  1.00 133.70 ? 149 ALA A C   1 
ATOM   1138  O O   . ALA A 1 149 ? 3.613   -52.233 43.088  1.00 136.70 ? 149 ALA A O   1 
ATOM   1139  C CB  . ALA A 1 149 ? 3.036   -54.987 44.540  1.00 121.21 ? 149 ALA A CB  1 
ATOM   1140  N N   . GLU A 1 150 ? 5.478   -53.483 42.877  1.00 132.33 ? 150 GLU A N   1 
ATOM   1141  C CA  . GLU A 1 150 ? 6.332   -52.316 42.686  1.00 133.31 ? 150 GLU A CA  1 
ATOM   1142  C C   . GLU A 1 150 ? 5.994   -51.594 41.391  1.00 135.53 ? 150 GLU A C   1 
ATOM   1143  O O   . GLU A 1 150 ? 6.118   -50.367 41.311  1.00 136.23 ? 150 GLU A O   1 
ATOM   1144  C CB  . GLU A 1 150 ? 7.803   -52.739 42.697  1.00 132.64 ? 150 GLU A CB  1 
ATOM   1145  C CG  . GLU A 1 150 ? 8.712   -51.847 43.525  1.00 137.54 ? 150 GLU A CG  1 
ATOM   1146  C CD  . GLU A 1 150 ? 8.898   -50.477 42.906  1.00 137.57 ? 150 GLU A CD  1 
ATOM   1147  O OE1 . GLU A 1 150 ? 8.960   -50.391 41.662  1.00 133.52 ? 150 GLU A OE1 1 
ATOM   1148  O OE2 . GLU A 1 150 ? 8.982   -49.487 43.661  1.00 141.25 ? 150 GLU A OE2 1 
ATOM   1149  N N   . ALA A 1 151 ? 5.561   -52.336 40.372  1.00 141.45 ? 151 ALA A N   1 
ATOM   1150  C CA  . ALA A 1 151 ? 5.099   -51.745 39.117  1.00 147.20 ? 151 ALA A CA  1 
ATOM   1151  C C   . ALA A 1 151 ? 3.627   -51.359 39.258  1.00 150.59 ? 151 ALA A C   1 
ATOM   1152  O O   . ALA A 1 151 ? 2.720   -51.981 38.701  1.00 149.42 ? 151 ALA A O   1 
ATOM   1153  C CB  . ALA A 1 151 ? 5.321   -52.713 37.962  1.00 143.92 ? 151 ALA A CB  1 
ATOM   1154  N N   . ALA A 1 152 ? 3.402   -50.296 40.029  1.00 154.73 ? 152 ALA A N   1 
ATOM   1155  C CA  . ALA A 1 152 ? 2.055   -49.807 40.292  1.00 155.15 ? 152 ALA A CA  1 
ATOM   1156  C C   . ALA A 1 152 ? 1.856   -48.328 39.998  1.00 159.49 ? 152 ALA A C   1 
ATOM   1157  O O   . ALA A 1 152 ? 0.703   -47.901 39.862  1.00 157.71 ? 152 ALA A O   1 
ATOM   1158  C CB  . ALA A 1 152 ? 1.660   -50.077 41.752  1.00 154.37 ? 152 ALA A CB  1 
ATOM   1159  N N   . SER A 1 153 ? 2.924   -47.533 39.904  1.00 162.66 ? 153 SER A N   1 
ATOM   1160  C CA  . SER A 1 153 ? 2.776   -46.122 39.561  1.00 162.30 ? 153 SER A CA  1 
ATOM   1161  C C   . SER A 1 153 ? 2.360   -45.938 38.107  1.00 163.22 ? 153 SER A C   1 
ATOM   1162  O O   . SER A 1 153 ? 1.728   -44.931 37.767  1.00 160.77 ? 153 SER A O   1 
ATOM   1163  C CB  . SER A 1 153 ? 4.080   -45.376 39.838  1.00 159.09 ? 153 SER A CB  1 
ATOM   1164  O OG  . SER A 1 153 ? 5.145   -45.915 39.076  1.00 157.08 ? 153 SER A OG  1 
ATOM   1165  N N   . GLN A 1 154 ? 2.716   -46.890 37.241  1.00 181.02 ? 154 GLN A N   1 
ATOM   1166  C CA  . GLN A 1 154 ? 2.377   -46.782 35.826  1.00 179.41 ? 154 GLN A CA  1 
ATOM   1167  C C   . GLN A 1 154 ? 0.870   -46.740 35.617  1.00 177.08 ? 154 GLN A C   1 
ATOM   1168  O O   . GLN A 1 154 ? 0.372   -45.969 34.789  1.00 174.43 ? 154 GLN A O   1 
ATOM   1169  C CB  . GLN A 1 154 ? 3.007   -47.940 35.051  1.00 180.87 ? 154 GLN A CB  1 
ATOM   1170  C CG  . GLN A 1 154 ? 3.075   -49.237 35.837  1.00 182.15 ? 154 GLN A CG  1 
ATOM   1171  C CD  . GLN A 1 154 ? 4.382   -49.380 36.602  1.00 184.57 ? 154 GLN A CD  1 
ATOM   1172  O OE1 . GLN A 1 154 ? 4.539   -48.831 37.694  1.00 185.58 ? 154 GLN A OE1 1 
ATOM   1173  N NE2 . GLN A 1 154 ? 5.328   -50.112 36.028  1.00 188.02 ? 154 GLN A NE2 1 
ATOM   1174  N N   . PHE A 1 155 ? 0.128   -47.565 36.352  1.00 155.04 ? 155 PHE A N   1 
ATOM   1175  C CA  . PHE A 1 155 ? -1.323  -47.579 36.241  1.00 146.18 ? 155 PHE A CA  1 
ATOM   1176  C C   . PHE A 1 155 ? -1.964  -47.135 37.549  1.00 145.21 ? 155 PHE A C   1 
ATOM   1177  O O   . PHE A 1 155 ? -2.349  -45.970 37.696  1.00 143.06 ? 155 PHE A O   1 
ATOM   1178  C CB  . PHE A 1 155 ? -1.822  -48.972 35.839  1.00 144.30 ? 155 PHE A CB  1 
ATOM   1179  C CG  . PHE A 1 155 ? -3.280  -49.196 36.122  1.00 140.37 ? 155 PHE A CG  1 
ATOM   1180  C CD1 . PHE A 1 155 ? -4.249  -48.413 35.520  1.00 138.43 ? 155 PHE A CD1 1 
ATOM   1181  C CD2 . PHE A 1 155 ? -3.677  -50.180 37.012  1.00 137.90 ? 155 PHE A CD2 1 
ATOM   1182  C CE1 . PHE A 1 155 ? -5.583  -48.617 35.799  1.00 137.14 ? 155 PHE A CE1 1 
ATOM   1183  C CE2 . PHE A 1 155 ? -5.004  -50.386 37.292  1.00 136.40 ? 155 PHE A CE2 1 
ATOM   1184  C CZ  . PHE A 1 155 ? -5.955  -49.607 36.690  1.00 136.90 ? 155 PHE A CZ  1 
ATOM   1185  N N   . GLY A 1 156 ? -2.070  -48.043 38.497  1.00 148.42 ? 156 GLY A N   1 
ATOM   1186  C CA  . GLY A 1 156 ? -2.809  -47.811 39.709  1.00 148.60 ? 156 GLY A CA  1 
ATOM   1187  C C   . GLY A 1 156 ? -3.325  -49.135 40.259  1.00 147.59 ? 156 GLY A C   1 
ATOM   1188  O O   . GLY A 1 156 ? -2.605  -50.136 40.254  1.00 146.86 ? 156 GLY A O   1 
ATOM   1189  N N   . GLU A 1 157 ? -4.578  -49.124 40.702  1.00 149.68 ? 157 GLU A N   1 
ATOM   1190  C CA  . GLU A 1 157 ? -5.181  -50.262 41.378  1.00 148.44 ? 157 GLU A CA  1 
ATOM   1191  C C   . GLU A 1 157 ? -6.244  -50.913 40.504  1.00 134.45 ? 157 GLU A C   1 
ATOM   1192  O O   . GLU A 1 157 ? -6.960  -50.231 39.764  1.00 133.45 ? 157 GLU A O   1 
ATOM   1193  C CB  . GLU A 1 157 ? -5.802  -49.838 42.711  1.00 156.43 ? 157 GLU A CB  1 
ATOM   1194  N N   . LEU A 1 158 ? -6.341  -52.237 40.601  1.00 129.81 ? 158 LEU A N   1 
ATOM   1195  C CA  . LEU A 1 158 ? -7.377  -52.998 39.911  1.00 127.96 ? 158 LEU A CA  1 
ATOM   1196  C C   . LEU A 1 158 ? -7.611  -54.273 40.704  1.00 127.84 ? 158 LEU A C   1 
ATOM   1197  O O   . LEU A 1 158 ? -6.675  -55.047 40.923  1.00 129.82 ? 158 LEU A O   1 
ATOM   1198  C CB  . LEU A 1 158 ? -6.979  -53.312 38.467  1.00 126.81 ? 158 LEU A CB  1 
ATOM   1199  C CG  . LEU A 1 158 ? -8.096  -53.730 37.502  1.00 124.49 ? 158 LEU A CG  1 
ATOM   1200  C CD1 . LEU A 1 158 ? -7.674  -53.458 36.072  1.00 125.76 ? 158 LEU A CD1 1 
ATOM   1201  C CD2 . LEU A 1 158 ? -8.467  -55.199 37.664  1.00 121.68 ? 158 LEU A CD2 1 
ATOM   1202  N N   . ILE A 1 159 ? -8.857  -54.495 41.114  1.00 127.95 ? 159 ILE A N   1 
ATOM   1203  C CA  . ILE A 1 159 ? -9.229  -55.609 41.979  1.00 127.49 ? 159 ILE A CA  1 
ATOM   1204  C C   . ILE A 1 159 ? -10.127 -56.552 41.190  1.00 123.68 ? 159 ILE A C   1 
ATOM   1205  O O   . ILE A 1 159 ? -11.089 -56.112 40.548  1.00 123.91 ? 159 ILE A O   1 
ATOM   1206  C CB  . ILE A 1 159 ? -9.941  -55.117 43.250  1.00 129.65 ? 159 ILE A CB  1 
ATOM   1207  C CG1 . ILE A 1 159 ? -9.142  -53.997 43.924  1.00 131.78 ? 159 ILE A CG1 1 
ATOM   1208  C CG2 . ILE A 1 159 ? -10.151 -56.272 44.217  1.00 125.82 ? 159 ILE A CG2 1 
ATOM   1209  C CD1 . ILE A 1 159 ? -7.835  -54.443 44.526  1.00 133.60 ? 159 ILE A CD1 1 
ATOM   1210  N N   . ALA A 1 160 ? -9.811  -57.845 41.233  1.00 124.81 ? 160 ALA A N   1 
ATOM   1211  C CA  . ALA A 1 160 ? -10.597 -58.859 40.542  1.00 124.02 ? 160 ALA A CA  1 
ATOM   1212  C C   . ALA A 1 160 ? -10.618 -60.135 41.368  1.00 125.33 ? 160 ALA A C   1 
ATOM   1213  O O   . ALA A 1 160 ? -9.563  -60.642 41.758  1.00 123.67 ? 160 ALA A O   1 
ATOM   1214  C CB  . ALA A 1 160 ? -10.032 -59.142 39.144  1.00 122.70 ? 160 ALA A CB  1 
ATOM   1215  N N   . ASP A 1 161 ? -11.821 -60.653 41.626  1.00 126.02 ? 161 ASP A N   1 
ATOM   1216  C CA  . ASP A 1 161 ? -11.997 -61.870 42.409  1.00 123.88 ? 161 ASP A CA  1 
ATOM   1217  C C   . ASP A 1 161 ? -11.659 -63.087 41.558  1.00 122.67 ? 161 ASP A C   1 
ATOM   1218  O O   . ASP A 1 161 ? -12.386 -63.397 40.608  1.00 121.73 ? 161 ASP A O   1 
ATOM   1219  C CB  . ASP A 1 161 ? -13.429 -61.971 42.938  1.00 120.56 ? 161 ASP A CB  1 
ATOM   1220  N N   . PRO A 1 162 ? -10.586 -63.816 41.880  1.00 117.15 ? 162 PRO A N   1 
ATOM   1221  C CA  . PRO A 1 162 ? -10.118 -64.880 40.976  1.00 114.20 ? 162 PRO A CA  1 
ATOM   1222  C C   . PRO A 1 162 ? -11.066 -66.064 40.858  1.00 111.36 ? 162 PRO A C   1 
ATOM   1223  O O   . PRO A 1 162 ? -10.862 -66.903 39.970  1.00 110.09 ? 162 PRO A O   1 
ATOM   1224  C CB  . PRO A 1 162 ? -8.783  -65.301 41.601  1.00 112.61 ? 162 PRO A CB  1 
ATOM   1225  C CG  . PRO A 1 162 ? -8.950  -64.996 43.054  1.00 112.79 ? 162 PRO A CG  1 
ATOM   1226  C CD  . PRO A 1 162 ? -9.780  -63.740 43.111  1.00 115.46 ? 162 PRO A CD  1 
ATOM   1227  N N   . ASP A 1 163 ? -12.089 -66.163 41.710  1.00 110.00 ? 163 ASP A N   1 
ATOM   1228  C CA  . ASP A 1 163 ? -13.035 -67.268 41.603  1.00 109.16 ? 163 ASP A CA  1 
ATOM   1229  C C   . ASP A 1 163 ? -14.002 -67.056 40.444  1.00 110.11 ? 163 ASP A C   1 
ATOM   1230  O O   . ASP A 1 163 ? -14.163 -67.933 39.589  1.00 105.08 ? 163 ASP A O   1 
ATOM   1231  C CB  . ASP A 1 163 ? -13.798 -67.440 42.916  1.00 107.89 ? 163 ASP A CB  1 
ATOM   1232  C CG  . ASP A 1 163 ? -13.218 -68.537 43.785  1.00 107.60 ? 163 ASP A CG  1 
ATOM   1233  O OD1 . ASP A 1 163 ? -12.348 -69.290 43.296  1.00 105.84 ? 163 ASP A OD1 1 
ATOM   1234  O OD2 . ASP A 1 163 ? -13.631 -68.647 44.959  1.00 113.59 ? 163 ASP A OD2 1 
ATOM   1235  N N   . THR A 1 164 ? -14.646 -65.893 40.397  1.00 111.54 ? 164 THR A N   1 
ATOM   1236  C CA  . THR A 1 164 ? -15.525 -65.535 39.295  1.00 114.33 ? 164 THR A CA  1 
ATOM   1237  C C   . THR A 1 164 ? -14.832 -64.662 38.260  1.00 117.78 ? 164 THR A C   1 
ATOM   1238  O O   . THR A 1 164 ? -15.446 -64.330 37.240  1.00 117.65 ? 164 THR A O   1 
ATOM   1239  C CB  . THR A 1 164 ? -16.775 -64.815 39.824  1.00 113.60 ? 164 THR A CB  1 
ATOM   1240  O OG1 . THR A 1 164 ? -16.391 -63.619 40.515  1.00 110.32 ? 164 THR A OG1 1 
ATOM   1241  C CG2 . THR A 1 164 ? -17.547 -65.715 40.778  1.00 107.58 ? 164 THR A CG2 1 
ATOM   1242  N N   . LYS A 1 165 ? -13.570 -64.296 38.496  1.00 125.77 ? 165 LYS A N   1 
ATOM   1243  C CA  . LYS A 1 165 ? -12.805 -63.440 37.590  1.00 124.34 ? 165 LYS A CA  1 
ATOM   1244  C C   . LYS A 1 165 ? -13.567 -62.160 37.270  1.00 124.36 ? 165 LYS A C   1 
ATOM   1245  O O   . LYS A 1 165 ? -13.594 -61.699 36.130  1.00 126.09 ? 165 LYS A O   1 
ATOM   1246  C CB  . LYS A 1 165 ? -12.433 -64.195 36.313  1.00 124.30 ? 165 LYS A CB  1 
ATOM   1247  C CG  . LYS A 1 165 ? -11.768 -65.535 36.580  1.00 126.58 ? 165 LYS A CG  1 
ATOM   1248  C CD  . LYS A 1 165 ? -10.302 -65.369 36.936  1.00 127.71 ? 165 LYS A CD  1 
ATOM   1249  C CE  . LYS A 1 165 ? -9.472  -65.024 35.711  1.00 126.92 ? 165 LYS A CE  1 
ATOM   1250  N NZ  . LYS A 1 165 ? -9.157  -66.232 34.901  1.00 127.79 ? 165 LYS A NZ  1 
ATOM   1251  N N   . GLU A 1 166 ? -14.176 -61.572 38.295  1.00 119.32 ? 166 GLU A N   1 
ATOM   1252  C CA  . GLU A 1 166 ? -15.019 -60.394 38.151  1.00 116.78 ? 166 GLU A CA  1 
ATOM   1253  C C   . GLU A 1 166 ? -14.312 -59.171 38.719  1.00 116.42 ? 166 GLU A C   1 
ATOM   1254  O O   . GLU A 1 166 ? -13.724 -59.232 39.803  1.00 117.75 ? 166 GLU A O   1 
ATOM   1255  C CB  . GLU A 1 166 ? -16.358 -60.606 38.867  1.00 115.71 ? 166 GLU A CB  1 
ATOM   1256  C CG  . GLU A 1 166 ? -17.516 -59.779 38.331  1.00 115.90 ? 166 GLU A CG  1 
ATOM   1257  C CD  . GLU A 1 166 ? -17.718 -58.486 39.100  1.00 115.47 ? 166 GLU A CD  1 
ATOM   1258  O OE1 . GLU A 1 166 ? -17.882 -58.548 40.337  1.00 110.35 ? 166 GLU A OE1 1 
ATOM   1259  O OE2 . GLU A 1 166 ? -17.727 -57.410 38.465  1.00 117.83 ? 166 GLU A OE2 1 
ATOM   1260  N N   . LEU A 1 167 ? -14.373 -58.059 37.987  1.00 117.38 ? 167 LEU A N   1 
ATOM   1261  C CA  . LEU A 1 167 ? -13.718 -56.830 38.428  1.00 120.19 ? 167 LEU A CA  1 
ATOM   1262  C C   . LEU A 1 167 ? -14.488 -56.252 39.606  1.00 118.97 ? 167 LEU A C   1 
ATOM   1263  O O   . LEU A 1 167 ? -15.597 -55.735 39.442  1.00 117.82 ? 167 LEU A O   1 
ATOM   1264  C CB  . LEU A 1 167 ? -13.635 -55.816 37.291  1.00 122.84 ? 167 LEU A CB  1 
ATOM   1265  C CG  . LEU A 1 167 ? -12.971 -54.492 37.692  1.00 120.15 ? 167 LEU A CG  1 
ATOM   1266  C CD1 . LEU A 1 167 ? -11.861 -54.114 36.724  1.00 120.71 ? 167 LEU A CD1 1 
ATOM   1267  C CD2 . LEU A 1 167 ? -13.993 -53.365 37.810  1.00 121.37 ? 167 LEU A CD2 1 
ATOM   1268  N N   . LEU A 1 168 ? -13.901 -56.338 40.799  1.00 118.57 ? 168 LEU A N   1 
ATOM   1269  C CA  . LEU A 1 168 ? -14.569 -55.855 41.998  1.00 118.39 ? 168 LEU A CA  1 
ATOM   1270  C C   . LEU A 1 168 ? -14.388 -54.359 42.215  1.00 121.32 ? 168 LEU A C   1 
ATOM   1271  O O   . LEU A 1 168 ? -15.204 -53.746 42.912  1.00 116.93 ? 168 LEU A O   1 
ATOM   1272  C CB  . LEU A 1 168 ? -14.071 -56.625 43.221  1.00 118.65 ? 168 LEU A CB  1 
ATOM   1273  C CG  . LEU A 1 168 ? -15.074 -57.658 43.734  1.00 113.44 ? 168 LEU A CG  1 
ATOM   1274  C CD1 . LEU A 1 168 ? -16.309 -56.962 44.278  1.00 106.47 ? 168 LEU A CD1 1 
ATOM   1275  C CD2 . LEU A 1 168 ? -15.451 -58.642 42.632  1.00 112.52 ? 168 LEU A CD2 1 
ATOM   1276  N N   . HIS A 1 169 ? -13.338 -53.765 41.654  1.00 142.51 ? 169 HIS A N   1 
ATOM   1277  C CA  . HIS A 1 169 ? -13.049 -52.352 41.853  1.00 141.32 ? 169 HIS A CA  1 
ATOM   1278  C C   . HIS A 1 169 ? -12.034 -51.915 40.809  1.00 140.39 ? 169 HIS A C   1 
ATOM   1279  O O   . HIS A 1 169 ? -11.213 -52.716 40.355  1.00 141.28 ? 169 HIS A O   1 
ATOM   1280  C CB  . HIS A 1 169 ? -12.517 -52.080 43.267  1.00 143.48 ? 169 HIS A CB  1 
ATOM   1281  C CG  . HIS A 1 169 ? -11.835 -50.755 43.413  1.00 148.72 ? 169 HIS A CG  1 
ATOM   1282  N ND1 . HIS A 1 169 ? -10.464 -50.614 43.374  1.00 152.19 ? 169 HIS A ND1 1 
ATOM   1283  C CD2 . HIS A 1 169 ? -12.337 -49.510 43.592  1.00 147.18 ? 169 HIS A CD2 1 
ATOM   1284  C CE1 . HIS A 1 169 ? -10.151 -49.340 43.525  1.00 151.93 ? 169 HIS A CE1 1 
ATOM   1285  N NE2 . HIS A 1 169 ? -11.269 -48.649 43.660  1.00 148.46 ? 169 HIS A NE2 1 
ATOM   1286  N N   . TYR A 1 170 ? -12.098 -50.639 40.434  1.00 135.82 ? 170 TYR A N   1 
ATOM   1287  C CA  . TYR A 1 170 ? -11.208 -50.109 39.408  1.00 131.15 ? 170 TYR A CA  1 
ATOM   1288  C C   . TYR A 1 170 ? -11.007 -48.618 39.629  1.00 132.05 ? 170 TYR A C   1 
ATOM   1289  O O   . TYR A 1 170 ? -11.972 -47.850 39.600  1.00 129.36 ? 170 TYR A O   1 
ATOM   1290  C CB  . TYR A 1 170 ? -11.763 -50.358 38.008  1.00 124.46 ? 170 TYR A CB  1 
ATOM   1291  C CG  . TYR A 1 170 ? -11.010 -49.592 36.951  1.00 126.57 ? 170 TYR A CG  1 
ATOM   1292  C CD1 . TYR A 1 170 ? -9.663  -49.827 36.735  1.00 130.24 ? 170 TYR A CD1 1 
ATOM   1293  C CD2 . TYR A 1 170 ? -11.634 -48.612 36.194  1.00 127.11 ? 170 TYR A CD2 1 
ATOM   1294  C CE1 . TYR A 1 170 ? -8.965  -49.126 35.784  1.00 130.24 ? 170 TYR A CE1 1 
ATOM   1295  C CE2 . TYR A 1 170 ? -10.935 -47.901 35.237  1.00 131.20 ? 170 TYR A CE2 1 
ATOM   1296  C CZ  . TYR A 1 170 ? -9.596  -48.166 35.041  1.00 130.55 ? 170 TYR A CZ  1 
ATOM   1297  O OH  . TYR A 1 170 ? -8.867  -47.479 34.101  1.00 128.99 ? 170 TYR A OH  1 
ATOM   1298  N N   . THR A 1 171 ? -9.756  -48.218 39.843  1.00 133.67 ? 171 THR A N   1 
ATOM   1299  C CA  . THR A 1 171 ? -9.355  -46.818 39.881  1.00 135.45 ? 171 THR A CA  1 
ATOM   1300  C C   . THR A 1 171 ? -8.227  -46.610 38.882  1.00 136.22 ? 171 THR A C   1 
ATOM   1301  O O   . THR A 1 171 ? -7.238  -47.352 38.893  1.00 137.24 ? 171 THR A O   1 
ATOM   1302  C CB  . THR A 1 171 ? -8.905  -46.391 41.280  1.00 140.35 ? 171 THR A CB  1 
ATOM   1303  O OG1 . THR A 1 171 ? -8.157  -47.450 41.892  1.00 144.15 ? 171 THR A OG1 1 
ATOM   1304  C CG2 . THR A 1 171 ? -10.107 -46.041 42.143  1.00 142.33 ? 171 THR A CG2 1 
ATOM   1305  N N   . GLU A 1 172 ? -8.384  -45.606 38.018  1.00 144.09 ? 172 GLU A N   1 
ATOM   1306  C CA  . GLU A 1 172 ? -7.437  -45.395 36.928  1.00 146.11 ? 172 GLU A CA  1 
ATOM   1307  C C   . GLU A 1 172 ? -6.049  -45.040 37.454  1.00 147.98 ? 172 GLU A C   1 
ATOM   1308  O O   . GLU A 1 172 ? -5.088  -45.793 37.263  1.00 146.56 ? 172 GLU A O   1 
ATOM   1309  C CB  . GLU A 1 172 ? -7.962  -44.308 35.986  1.00 145.14 ? 172 GLU A CB  1 
ATOM   1310  C CG  . GLU A 1 172 ? -9.114  -43.490 36.553  1.00 147.77 ? 172 GLU A CG  1 
ATOM   1311  C CD  . GLU A 1 172 ? -8.672  -42.498 37.611  1.00 148.67 ? 172 GLU A CD  1 
ATOM   1312  O OE1 . GLU A 1 172 ? -7.658  -41.803 37.391  1.00 147.41 ? 172 GLU A OE1 1 
ATOM   1313  O OE2 . GLU A 1 172 ? -9.339  -42.418 38.664  1.00 145.86 ? 172 GLU A OE2 1 
ATOM   1314  N N   . LYS A 1 173 ? -5.925  -43.896 38.127  1.00 146.69 ? 173 LYS A N   1 
ATOM   1315  C CA  . LYS A 1 173 ? -4.606  -43.424 38.536  1.00 144.59 ? 173 LYS A CA  1 
ATOM   1316  C C   . LYS A 1 173 ? -4.434  -43.427 40.053  1.00 148.55 ? 173 LYS A C   1 
ATOM   1317  O O   . LYS A 1 173 ? -3.413  -43.930 40.541  1.00 150.62 ? 173 LYS A O   1 
ATOM   1318  C CB  . LYS A 1 173 ? -4.329  -42.030 37.965  1.00 140.49 ? 173 LYS A CB  1 
ATOM   1319  C CG  . LYS A 1 173 ? -3.054  -41.963 37.142  1.00 135.69 ? 173 LYS A CG  1 
ATOM   1320  C CD  . LYS A 1 173 ? -3.080  -42.989 36.020  1.00 133.03 ? 173 LYS A CD  1 
ATOM   1321  C CE  . LYS A 1 173 ? -1.684  -43.257 35.488  1.00 130.50 ? 173 LYS A CE  1 
ATOM   1322  N NZ  . LYS A 1 173 ? -0.801  -43.828 36.543  1.00 141.76 ? 173 LYS A NZ  1 
ATOM   1323  N N   . PRO A 1 174 ? -5.383  -42.885 40.849  1.00 149.16 ? 174 PRO A N   1 
ATOM   1324  C CA  . PRO A 1 174 ? -5.228  -42.994 42.307  1.00 154.89 ? 174 PRO A CA  1 
ATOM   1325  C C   . PRO A 1 174 ? -5.325  -44.438 42.766  1.00 164.33 ? 174 PRO A C   1 
ATOM   1326  O O   . PRO A 1 174 ? -6.425  -44.974 42.932  1.00 162.13 ? 174 PRO A O   1 
ATOM   1327  C CB  . PRO A 1 174 ? -6.386  -42.151 42.858  1.00 149.23 ? 174 PRO A CB  1 
ATOM   1328  C CG  . PRO A 1 174 ? -6.804  -41.275 41.728  1.00 147.23 ? 174 PRO A CG  1 
ATOM   1329  C CD  . PRO A 1 174 ? -6.579  -42.096 40.502  1.00 147.21 ? 174 PRO A CD  1 
ATOM   1330  N N   . GLU A 1 175 ? -4.171  -45.073 42.977  1.00 186.19 ? 175 GLU A N   1 
ATOM   1331  C CA  . GLU A 1 175 ? -4.155  -46.500 43.279  1.00 189.02 ? 175 GLU A CA  1 
ATOM   1332  C C   . GLU A 1 175 ? -4.702  -46.774 44.675  1.00 194.23 ? 175 GLU A C   1 
ATOM   1333  O O   . GLU A 1 175 ? -5.724  -47.454 44.829  1.00 194.52 ? 175 GLU A O   1 
ATOM   1334  C CB  . GLU A 1 175 ? -2.734  -47.050 43.118  1.00 190.78 ? 175 GLU A CB  1 
ATOM   1335  C CG  . GLU A 1 175 ? -1.644  -46.239 43.810  1.00 194.70 ? 175 GLU A CG  1 
ATOM   1336  C CD  . GLU A 1 175 ? -0.267  -46.831 43.612  1.00 192.54 ? 175 GLU A CD  1 
ATOM   1337  O OE1 . GLU A 1 175 ? -0.187  -47.966 43.104  1.00 191.86 ? 175 GLU A OE1 1 
ATOM   1338  O OE2 . GLU A 1 175 ? 0.732   -46.168 43.963  1.00 190.79 ? 175 GLU A OE2 1 
ATOM   1339  N N   . THR A 1 176 ? -4.061  -46.213 45.700  1.00 217.38 ? 176 THR A N   1 
ATOM   1340  C CA  . THR A 1 176 ? -4.398  -46.470 47.099  1.00 219.17 ? 176 THR A CA  1 
ATOM   1341  C C   . THR A 1 176 ? -4.566  -47.973 47.339  1.00 221.03 ? 176 THR A C   1 
ATOM   1342  O O   . THR A 1 176 ? -5.673  -48.492 47.491  1.00 221.09 ? 176 THR A O   1 
ATOM   1343  C CB  . THR A 1 176 ? -5.653  -45.694 47.502  1.00 217.87 ? 176 THR A CB  1 
ATOM   1344  O OG1 . THR A 1 176 ? -5.705  -44.460 46.776  1.00 215.35 ? 176 THR A OG1 1 
ATOM   1345  C CG2 . THR A 1 176 ? -5.624  -45.389 48.990  1.00 219.18 ? 176 THR A CG2 1 
ATOM   1346  N N   . PHE A 1 177 ? -3.415  -48.655 47.332  1.00 193.09 ? 177 PHE A N   1 
ATOM   1347  C CA  . PHE A 1 177 ? -3.309  -50.109 47.455  1.00 177.66 ? 177 PHE A CA  1 
ATOM   1348  C C   . PHE A 1 177 ? -3.792  -50.793 46.183  1.00 176.23 ? 177 PHE A C   1 
ATOM   1349  O O   . PHE A 1 177 ? -4.873  -50.482 45.672  1.00 178.58 ? 177 PHE A O   1 
ATOM   1350  C CB  . PHE A 1 177 ? -4.082  -50.633 48.670  1.00 168.84 ? 177 PHE A CB  1 
ATOM   1351  C CG  . PHE A 1 177 ? -4.229  -52.129 48.695  1.00 162.75 ? 177 PHE A CG  1 
ATOM   1352  C CD1 . PHE A 1 177 ? -3.161  -52.939 49.046  1.00 157.67 ? 177 PHE A CD1 1 
ATOM   1353  C CD2 . PHE A 1 177 ? -5.438  -52.724 48.373  1.00 161.39 ? 177 PHE A CD2 1 
ATOM   1354  C CE1 . PHE A 1 177 ? -3.297  -54.317 49.069  1.00 153.57 ? 177 PHE A CE1 1 
ATOM   1355  C CE2 . PHE A 1 177 ? -5.580  -54.098 48.395  1.00 154.53 ? 177 PHE A CE2 1 
ATOM   1356  C CZ  . PHE A 1 177 ? -4.509  -54.895 48.744  1.00 152.09 ? 177 PHE A CZ  1 
ATOM   1357  N N   . VAL A 1 178 ? -2.999  -51.731 45.670  1.00 174.75 ? 178 VAL A N   1 
ATOM   1358  C CA  . VAL A 1 178 ? -3.277  -52.373 44.391  1.00 168.58 ? 178 VAL A CA  1 
ATOM   1359  C C   . VAL A 1 178 ? -3.523  -53.857 44.614  1.00 165.94 ? 178 VAL A C   1 
ATOM   1360  O O   . VAL A 1 178 ? -3.665  -54.312 45.755  1.00 169.25 ? 178 VAL A O   1 
ATOM   1361  C CB  . VAL A 1 178 ? -2.122  -52.155 43.397  1.00 166.30 ? 178 VAL A CB  1 
ATOM   1362  C CG1 . VAL A 1 178 ? -1.851  -50.676 43.225  1.00 170.81 ? 178 VAL A CG1 1 
ATOM   1363  C CG2 . VAL A 1 178 ? -0.866  -52.878 43.867  1.00 163.53 ? 178 VAL A CG2 1 
ATOM   1364  N N   . SER A 1 179 ? -3.575  -54.619 43.522  1.00 155.25 ? 179 SER A N   1 
ATOM   1365  C CA  . SER A 1 179 ? -3.759  -56.061 43.606  1.00 156.36 ? 179 SER A CA  1 
ATOM   1366  C C   . SER A 1 179 ? -2.855  -56.795 42.628  1.00 152.91 ? 179 SER A C   1 
ATOM   1367  O O   . SER A 1 179 ? -3.130  -57.955 42.302  1.00 155.07 ? 179 SER A O   1 
ATOM   1368  C CB  . SER A 1 179 ? -5.211  -56.456 43.341  1.00 155.17 ? 179 SER A CB  1 
ATOM   1369  O OG  . SER A 1 179 ? -5.438  -57.817 43.661  1.00 154.96 ? 179 SER A OG  1 
ATOM   1370  N N   . ASP A 1 180 ? -1.817  -56.129 42.120  1.00 143.52 ? 180 ASP A N   1 
ATOM   1371  C CA  . ASP A 1 180 ? -0.817  -56.643 41.190  1.00 140.79 ? 180 ASP A CA  1 
ATOM   1372  C C   . ASP A 1 180 ? -1.410  -56.809 39.793  1.00 138.90 ? 180 ASP A C   1 
ATOM   1373  O O   . ASP A 1 180 ? -0.688  -57.181 38.862  1.00 139.15 ? 180 ASP A O   1 
ATOM   1374  C CB  . ASP A 1 180 ? -0.156  -57.944 41.695  1.00 141.24 ? 180 ASP A CB  1 
ATOM   1375  C CG  . ASP A 1 180 ? -0.591  -59.190 40.930  1.00 145.84 ? 180 ASP A CG  1 
ATOM   1376  O OD1 . ASP A 1 180 ? 0.045   -59.525 39.908  1.00 145.27 ? 180 ASP A OD1 1 
ATOM   1377  O OD2 . ASP A 1 180 ? -1.546  -59.860 41.371  1.00 148.24 ? 180 ASP A OD2 1 
ATOM   1378  N N   . LEU A 1 181 ? -2.687  -56.485 39.602  1.00 134.83 ? 181 LEU A N   1 
ATOM   1379  C CA  . LEU A 1 181 ? -3.355  -56.596 38.317  1.00 131.13 ? 181 LEU A CA  1 
ATOM   1380  C C   . LEU A 1 181 ? -3.531  -55.219 37.689  1.00 130.12 ? 181 LEU A C   1 
ATOM   1381  O O   . LEU A 1 181 ? -3.717  -54.217 38.386  1.00 127.74 ? 181 LEU A O   1 
ATOM   1382  C CB  . LEU A 1 181 ? -4.720  -57.268 38.479  1.00 130.67 ? 181 LEU A CB  1 
ATOM   1383  C CG  . LEU A 1 181 ? -4.679  -58.777 38.706  1.00 132.21 ? 181 LEU A CG  1 
ATOM   1384  C CD1 . LEU A 1 181 ? -6.084  -59.348 38.718  1.00 130.01 ? 181 LEU A CD1 1 
ATOM   1385  C CD2 . LEU A 1 181 ? -3.829  -59.455 37.643  1.00 134.33 ? 181 LEU A CD2 1 
ATOM   1386  N N   . ILE A 1 182 ? -3.469  -55.184 36.355  1.00 131.42 ? 182 ILE A N   1 
ATOM   1387  C CA  . ILE A 1 182 ? -3.530  -53.944 35.587  1.00 129.19 ? 182 ILE A CA  1 
ATOM   1388  C C   . ILE A 1 182 ? -4.284  -54.210 34.292  1.00 127.19 ? 182 ILE A C   1 
ATOM   1389  O O   . ILE A 1 182 ? -4.388  -55.349 33.832  1.00 123.36 ? 182 ILE A O   1 
ATOM   1390  C CB  . ILE A 1 182 ? -2.124  -53.375 35.272  1.00 125.85 ? 182 ILE A CB  1 
ATOM   1391  C CG1 . ILE A 1 182 ? -1.234  -54.455 34.655  1.00 122.40 ? 182 ILE A CG1 1 
ATOM   1392  C CG2 . ILE A 1 182 ? -1.469  -52.797 36.516  1.00 128.64 ? 182 ILE A CG2 1 
ATOM   1393  C CD1 . ILE A 1 182 ? -0.220  -53.911 33.679  1.00 121.31 ? 182 ILE A CD1 1 
ATOM   1394  N N   . ASN A 1 183 ? -4.820  -53.142 33.702  1.00 137.70 ? 183 ASN A N   1 
ATOM   1395  C CA  . ASN A 1 183 ? -5.468  -53.249 32.401  1.00 133.91 ? 183 ASN A CA  1 
ATOM   1396  C C   . ASN A 1 183 ? -4.449  -53.591 31.316  1.00 132.71 ? 183 ASN A C   1 
ATOM   1397  O O   . ASN A 1 183 ? -3.245  -53.359 31.456  1.00 133.31 ? 183 ASN A O   1 
ATOM   1398  C CB  . ASN A 1 183 ? -6.188  -51.948 32.037  1.00 135.13 ? 183 ASN A CB  1 
ATOM   1399  C CG  . ASN A 1 183 ? -7.197  -51.520 33.084  1.00 137.64 ? 183 ASN A CG  1 
ATOM   1400  O OD1 . ASN A 1 183 ? -6.834  -51.018 34.146  1.00 143.21 ? 183 ASN A OD1 1 
ATOM   1401  N ND2 . ASN A 1 183 ? -8.476  -51.716 32.787  1.00 130.52 ? 183 ASN A ND2 1 
ATOM   1402  N N   . CYS A 1 184 ? -4.952  -54.157 30.217  1.00 117.19 ? 184 CYS A N   1 
ATOM   1403  C CA  . CYS A 1 184 ? -4.138  -54.420 29.041  1.00 109.97 ? 184 CYS A CA  1 
ATOM   1404  C C   . CYS A 1 184 ? -4.568  -53.645 27.808  1.00 106.43 ? 184 CYS A C   1 
ATOM   1405  O O   . CYS A 1 184 ? -3.787  -53.562 26.854  1.00 104.85 ? 184 CYS A O   1 
ATOM   1406  C CB  . CYS A 1 184 ? -4.144  -55.919 28.704  1.00 110.19 ? 184 CYS A CB  1 
ATOM   1407  S SG  . CYS A 1 184 ? -3.115  -56.909 29.802  1.00 111.96 ? 184 CYS A SG  1 
ATOM   1408  N N   . GLY A 1 185 ? -5.774  -53.081 27.797  1.00 111.89 ? 185 GLY A N   1 
ATOM   1409  C CA  . GLY A 1 185 ? -6.271  -52.324 26.674  1.00 115.12 ? 185 GLY A CA  1 
ATOM   1410  C C   . GLY A 1 185 ? -7.038  -53.127 25.644  1.00 109.27 ? 185 GLY A C   1 
ATOM   1411  O O   . GLY A 1 185 ? -7.763  -52.536 24.836  1.00 109.87 ? 185 GLY A O   1 
ATOM   1412  N N   . VAL A 1 186 ? -6.904  -54.449 25.646  1.00 98.70  ? 186 VAL A N   1 
ATOM   1413  C CA  . VAL A 1 186 ? -7.634  -55.308 24.720  1.00 94.89  ? 186 VAL A CA  1 
ATOM   1414  C C   . VAL A 1 186 ? -8.911  -55.774 25.416  1.00 96.83  ? 186 VAL A C   1 
ATOM   1415  O O   . VAL A 1 186 ? -8.862  -56.540 26.381  1.00 96.11  ? 186 VAL A O   1 
ATOM   1416  C CB  . VAL A 1 186 ? -6.771  -56.486 24.253  1.00 90.61  ? 186 VAL A CB  1 
ATOM   1417  C CG1 . VAL A 1 186 ? -5.893  -56.984 25.391  1.00 96.12  ? 186 VAL A CG1 1 
ATOM   1418  C CG2 . VAL A 1 186 ? -7.640  -57.607 23.702  1.00 94.12  ? 186 VAL A CG2 1 
ATOM   1419  N N   . TYR A 1 187 ? -10.057 -55.286 24.945  1.00 91.66  ? 187 TYR A N   1 
ATOM   1420  C CA  . TYR A 1 187 ? -11.346 -55.562 25.556  1.00 91.08  ? 187 TYR A CA  1 
ATOM   1421  C C   . TYR A 1 187 ? -12.280 -56.189 24.527  1.00 87.49  ? 187 TYR A C   1 
ATOM   1422  O O   . TYR A 1 187 ? -12.112 -56.021 23.316  1.00 85.76  ? 187 TYR A O   1 
ATOM   1423  C CB  . TYR A 1 187 ? -11.976 -54.284 26.134  1.00 91.46  ? 187 TYR A CB  1 
ATOM   1424  C CG  . TYR A 1 187 ? -11.106 -53.514 27.117  1.00 96.89  ? 187 TYR A CG  1 
ATOM   1425  C CD1 . TYR A 1 187 ? -11.288 -52.149 27.309  1.00 99.30  ? 187 TYR A CD1 1 
ATOM   1426  C CD2 . TYR A 1 187 ? -10.102 -54.143 27.844  1.00 103.90 ? 187 TYR A CD2 1 
ATOM   1427  C CE1 . TYR A 1 187 ? -10.494 -51.437 28.195  1.00 109.02 ? 187 TYR A CE1 1 
ATOM   1428  C CE2 . TYR A 1 187 ? -9.300  -53.438 28.728  1.00 108.13 ? 187 TYR A CE2 1 
ATOM   1429  C CZ  . TYR A 1 187 ? -9.502  -52.089 28.903  1.00 111.54 ? 187 TYR A CZ  1 
ATOM   1430  O OH  . TYR A 1 187 ? -8.708  -51.393 29.787  1.00 111.95 ? 187 TYR A OH  1 
ATOM   1431  N N   . VAL A 1 188 ? -13.276 -56.916 25.028  1.00 89.23  ? 188 VAL A N   1 
ATOM   1432  C CA  . VAL A 1 188 ? -14.314 -57.510 24.191  1.00 89.32  ? 188 VAL A CA  1 
ATOM   1433  C C   . VAL A 1 188 ? -15.643 -57.384 24.918  1.00 95.29  ? 188 VAL A C   1 
ATOM   1434  O O   . VAL A 1 188 ? -15.763 -57.806 26.074  1.00 102.60 ? 188 VAL A O   1 
ATOM   1435  C CB  . VAL A 1 188 ? -14.028 -58.982 23.859  1.00 91.02  ? 188 VAL A CB  1 
ATOM   1436  C CG1 . VAL A 1 188 ? -13.387 -59.666 25.040  1.00 102.91 ? 188 VAL A CG1 1 
ATOM   1437  C CG2 . VAL A 1 188 ? -15.314 -59.695 23.470  1.00 94.71  ? 188 VAL A CG2 1 
ATOM   1438  N N   . PHE A 1 189 ? -16.628 -56.786 24.258  1.00 95.41  ? 189 PHE A N   1 
ATOM   1439  C CA  . PHE A 1 189 ? -17.950 -56.609 24.832  1.00 99.46  ? 189 PHE A CA  1 
ATOM   1440  C C   . PHE A 1 189 ? -18.981 -57.438 24.073  1.00 103.85 ? 189 PHE A C   1 
ATOM   1441  O O   . PHE A 1 189 ? -18.667 -58.172 23.133  1.00 102.65 ? 189 PHE A O   1 
ATOM   1442  C CB  . PHE A 1 189 ? -18.345 -55.132 24.838  1.00 98.85  ? 189 PHE A CB  1 
ATOM   1443  C CG  . PHE A 1 189 ? -17.418 -54.262 25.631  1.00 96.91  ? 189 PHE A CG  1 
ATOM   1444  C CD1 . PHE A 1 189 ? -17.655 -54.032 26.975  1.00 96.89  ? 189 PHE A CD1 1 
ATOM   1445  C CD2 . PHE A 1 189 ? -16.317 -53.667 25.039  1.00 96.79  ? 189 PHE A CD2 1 
ATOM   1446  C CE1 . PHE A 1 189 ? -16.814 -53.231 27.716  1.00 95.71  ? 189 PHE A CE1 1 
ATOM   1447  C CE2 . PHE A 1 189 ? -15.469 -52.862 25.778  1.00 99.78  ? 189 PHE A CE2 1 
ATOM   1448  C CZ  . PHE A 1 189 ? -15.720 -52.645 27.119  1.00 101.71 ? 189 PHE A CZ  1 
ATOM   1449  N N   . THR A 1 190 ? -20.230 -57.297 24.498  1.00 112.25 ? 190 THR A N   1 
ATOM   1450  C CA  . THR A 1 190 ? -21.391 -57.815 23.799  1.00 113.57 ? 190 THR A CA  1 
ATOM   1451  C C   . THR A 1 190 ? -22.093 -56.660 23.091  1.00 116.12 ? 190 THR A C   1 
ATOM   1452  O O   . THR A 1 190 ? -21.653 -55.510 23.140  1.00 113.47 ? 190 THR A O   1 
ATOM   1453  C CB  . THR A 1 190 ? -22.330 -58.530 24.772  1.00 117.85 ? 190 THR A CB  1 
ATOM   1454  O OG1 . THR A 1 190 ? -23.442 -59.080 24.052  1.00 124.22 ? 190 THR A OG1 1 
ATOM   1455  C CG2 . THR A 1 190 ? -22.840 -57.560 25.830  1.00 114.63 ? 190 THR A CG2 1 
ATOM   1456  N N   . SER A 1 191 ? -23.197 -56.971 22.411  1.00 112.49 ? 191 SER A N   1 
ATOM   1457  C CA  . SER A 1 191 ? -23.937 -55.923 21.719  1.00 108.86 ? 191 SER A CA  1 
ATOM   1458  C C   . SER A 1 191 ? -24.569 -54.920 22.677  1.00 109.69 ? 191 SER A C   1 
ATOM   1459  O O   . SER A 1 191 ? -25.018 -53.860 22.228  1.00 111.01 ? 191 SER A O   1 
ATOM   1460  C CB  . SER A 1 191 ? -25.018 -56.537 20.828  1.00 111.61 ? 191 SER A CB  1 
ATOM   1461  O OG  . SER A 1 191 ? -25.741 -55.526 20.149  1.00 119.12 ? 191 SER A OG  1 
ATOM   1462  N N   . ASP A 1 192 ? -24.607 -55.224 23.973  1.00 110.75 ? 192 ASP A N   1 
ATOM   1463  C CA  . ASP A 1 192 ? -25.253 -54.382 24.972  1.00 110.69 ? 192 ASP A CA  1 
ATOM   1464  C C   . ASP A 1 192 ? -24.383 -53.216 25.432  1.00 110.64 ? 192 ASP A C   1 
ATOM   1465  O O   . ASP A 1 192 ? -24.844 -52.405 26.242  1.00 111.86 ? 192 ASP A O   1 
ATOM   1466  C CB  . ASP A 1 192 ? -25.656 -55.242 26.176  1.00 106.99 ? 192 ASP A CB  1 
ATOM   1467  C CG  . ASP A 1 192 ? -26.696 -54.574 27.053  1.00 107.63 ? 192 ASP A CG  1 
ATOM   1468  O OD1 . ASP A 1 192 ? -27.301 -53.578 26.608  1.00 113.52 ? 192 ASP A OD1 1 
ATOM   1469  O OD2 . ASP A 1 192 ? -26.902 -55.044 28.192  1.00 102.09 ? 192 ASP A OD2 1 
ATOM   1470  N N   . ILE A 1 193 ? -23.145 -53.108 24.944  1.00 111.61 ? 193 ILE A N   1 
ATOM   1471  C CA  . ILE A 1 193 ? -22.256 -52.058 25.433  1.00 114.96 ? 193 ILE A CA  1 
ATOM   1472  C C   . ILE A 1 193 ? -22.722 -50.686 24.958  1.00 121.60 ? 193 ILE A C   1 
ATOM   1473  O O   . ILE A 1 193 ? -22.557 -49.686 25.669  1.00 122.42 ? 193 ILE A O   1 
ATOM   1474  C CB  . ILE A 1 193 ? -20.798 -52.343 25.016  1.00 108.63 ? 193 ILE A CB  1 
ATOM   1475  C CG1 . ILE A 1 193 ? -19.857 -51.263 25.551  1.00 104.65 ? 193 ILE A CG1 1 
ATOM   1476  C CG2 . ILE A 1 193 ? -20.671 -52.438 23.505  1.00 112.07 ? 193 ILE A CG2 1 
ATOM   1477  C CD1 . ILE A 1 193 ? -19.919 -51.087 27.047  1.00 106.19 ? 193 ILE A CD1 1 
ATOM   1478  N N   . PHE A 1 194 ? -23.323 -50.611 23.768  1.00 130.50 ? 194 PHE A N   1 
ATOM   1479  C CA  . PHE A 1 194 ? -23.797 -49.327 23.261  1.00 129.93 ? 194 PHE A CA  1 
ATOM   1480  C C   . PHE A 1 194 ? -24.934 -48.770 24.107  1.00 130.83 ? 194 PHE A C   1 
ATOM   1481  O O   . PHE A 1 194 ? -25.109 -47.549 24.179  1.00 131.60 ? 194 PHE A O   1 
ATOM   1482  C CB  . PHE A 1 194 ? -24.242 -49.468 21.808  1.00 127.59 ? 194 PHE A CB  1 
ATOM   1483  C CG  . PHE A 1 194 ? -23.131 -49.816 20.866  1.00 126.88 ? 194 PHE A CG  1 
ATOM   1484  C CD1 . PHE A 1 194 ? -22.211 -48.857 20.481  1.00 124.30 ? 194 PHE A CD1 1 
ATOM   1485  C CD2 . PHE A 1 194 ? -23.006 -51.097 20.361  1.00 126.68 ? 194 PHE A CD2 1 
ATOM   1486  C CE1 . PHE A 1 194 ? -21.187 -49.169 19.610  1.00 122.37 ? 194 PHE A CE1 1 
ATOM   1487  C CE2 . PHE A 1 194 ? -21.982 -51.414 19.492  1.00 125.77 ? 194 PHE A CE2 1 
ATOM   1488  C CZ  . PHE A 1 194 ? -21.073 -50.449 19.115  1.00 123.41 ? 194 PHE A CZ  1 
ATOM   1489  N N   . ASN A 1 195 ? -25.710 -49.642 24.752  1.00 123.01 ? 195 ASN A N   1 
ATOM   1490  C CA  . ASN A 1 195 ? -26.774 -49.169 25.629  1.00 124.37 ? 195 ASN A CA  1 
ATOM   1491  C C   . ASN A 1 195 ? -26.212 -48.587 26.919  1.00 128.26 ? 195 ASN A C   1 
ATOM   1492  O O   . ASN A 1 195 ? -26.833 -47.704 27.522  1.00 129.16 ? 195 ASN A O   1 
ATOM   1493  C CB  . ASN A 1 195 ? -27.749 -50.307 25.931  1.00 120.39 ? 195 ASN A CB  1 
ATOM   1494  C CG  . ASN A 1 195 ? -28.294 -50.957 24.671  1.00 116.99 ? 195 ASN A CG  1 
ATOM   1495  O OD1 . ASN A 1 195 ? -28.440 -50.305 23.638  1.00 117.40 ? 195 ASN A OD1 1 
ATOM   1496  N ND2 . ASN A 1 195 ? -28.601 -52.247 24.753  1.00 112.87 ? 195 ASN A ND2 1 
ATOM   1497  N N   . ALA A 1 196 ? -25.046 -49.072 27.358  1.00 138.87 ? 196 ALA A N   1 
ATOM   1498  C CA  . ALA A 1 196 ? -24.429 -48.542 28.569  1.00 142.46 ? 196 ALA A CA  1 
ATOM   1499  C C   . ALA A 1 196 ? -23.912 -47.124 28.369  1.00 143.76 ? 196 ALA A C   1 
ATOM   1500  O O   . ALA A 1 196 ? -23.878 -46.338 29.323  1.00 143.42 ? 196 ALA A O   1 
ATOM   1501  C CB  . ALA A 1 196 ? -23.295 -49.461 29.026  1.00 141.20 ? 196 ALA A CB  1 
ATOM   1502  N N   . ILE A 1 197 ? -23.514 -46.773 27.146  1.00 132.40 ? 197 ILE A N   1 
ATOM   1503  C CA  . ILE A 1 197 ? -23.034 -45.419 26.896  1.00 131.82 ? 197 ILE A CA  1 
ATOM   1504  C C   . ILE A 1 197 ? -24.195 -44.435 26.828  1.00 134.91 ? 197 ILE A C   1 
ATOM   1505  O O   . ILE A 1 197 ? -24.056 -43.275 27.232  1.00 142.28 ? 197 ILE A O   1 
ATOM   1506  C CB  . ILE A 1 197 ? -22.186 -45.376 25.613  1.00 127.49 ? 197 ILE A CB  1 
ATOM   1507  C CG1 . ILE A 1 197 ? -21.086 -46.435 25.665  1.00 120.14 ? 197 ILE A CG1 1 
ATOM   1508  C CG2 . ILE A 1 197 ? -21.568 -43.996 25.428  1.00 130.19 ? 197 ILE A CG2 1 
ATOM   1509  C CD1 . ILE A 1 197 ? -20.170 -46.412 24.463  1.00 109.78 ? 197 ILE A CD1 1 
ATOM   1510  N N   . GLU A 1 198 ? -25.353 -44.873 26.330  1.00 130.03 ? 198 GLU A N   1 
ATOM   1511  C CA  . GLU A 1 198 ? -26.519 -43.997 26.290  1.00 132.23 ? 198 GLU A CA  1 
ATOM   1512  C C   . GLU A 1 198 ? -26.992 -43.630 27.690  1.00 137.95 ? 198 GLU A C   1 
ATOM   1513  O O   . GLU A 1 198 ? -27.534 -42.539 27.896  1.00 141.26 ? 198 GLU A O   1 
ATOM   1514  C CB  . GLU A 1 198 ? -27.645 -44.667 25.504  1.00 127.36 ? 198 GLU A CB  1 
ATOM   1515  C CG  . GLU A 1 198 ? -27.304 -44.909 24.045  1.00 128.58 ? 198 GLU A CG  1 
ATOM   1516  C CD  . GLU A 1 198 ? -28.465 -45.473 23.248  1.00 128.52 ? 198 GLU A CD  1 
ATOM   1517  O OE1 . GLU A 1 198 ? -29.493 -45.836 23.858  1.00 129.39 ? 198 GLU A OE1 1 
ATOM   1518  O OE2 . GLU A 1 198 ? -28.344 -45.559 22.008  1.00 126.89 ? 198 GLU A OE2 1 
ATOM   1519  N N   . GLU A 1 199 ? -26.805 -44.522 28.658  1.00 135.51 ? 199 GLU A N   1 
ATOM   1520  C CA  . GLU A 1 199 ? -27.169 -44.226 30.036  1.00 138.08 ? 199 GLU A CA  1 
ATOM   1521  C C   . GLU A 1 199 ? -26.145 -43.350 30.742  1.00 144.90 ? 199 GLU A C   1 
ATOM   1522  O O   . GLU A 1 199 ? -26.361 -42.984 31.901  1.00 148.28 ? 199 GLU A O   1 
ATOM   1523  C CB  . GLU A 1 199 ? -27.384 -45.527 30.811  1.00 136.06 ? 199 GLU A CB  1 
ATOM   1524  C CG  . GLU A 1 199 ? -28.552 -46.335 30.278  1.00 134.70 ? 199 GLU A CG  1 
ATOM   1525  C CD  . GLU A 1 199 ? -29.802 -45.497 30.090  1.00 135.96 ? 199 GLU A CD  1 
ATOM   1526  O OE1 . GLU A 1 199 ? -30.186 -44.772 31.033  1.00 143.15 ? 199 GLU A OE1 1 
ATOM   1527  O OE2 . GLU A 1 199 ? -30.393 -45.551 28.991  1.00 129.59 ? 199 GLU A OE2 1 
ATOM   1528  N N   . VAL A 1 200 ? -25.040 -43.017 30.083  1.00 146.47 ? 200 VAL A N   1 
ATOM   1529  C CA  . VAL A 1 200 ? -24.096 -42.045 30.614  1.00 149.74 ? 200 VAL A CA  1 
ATOM   1530  C C   . VAL A 1 200 ? -23.938 -40.829 29.712  1.00 157.61 ? 200 VAL A C   1 
ATOM   1531  O O   . VAL A 1 200 ? -23.527 -39.764 30.200  1.00 159.42 ? 200 VAL A O   1 
ATOM   1532  C CB  . VAL A 1 200 ? -22.720 -42.694 30.885  1.00 147.12 ? 200 VAL A CB  1 
ATOM   1533  C CG1 . VAL A 1 200 ? -21.934 -42.869 29.594  1.00 146.61 ? 200 VAL A CG1 1 
ATOM   1534  C CG2 . VAL A 1 200 ? -21.932 -41.877 31.901  1.00 153.28 ? 200 VAL A CG2 1 
ATOM   1535  N N   . TYR A 1 201 ? -24.251 -40.936 28.422  1.00 185.48 ? 201 TYR A N   1 
ATOM   1536  C CA  . TYR A 1 201 ? -24.196 -39.804 27.506  1.00 184.00 ? 201 TYR A CA  1 
ATOM   1537  C C   . TYR A 1 201 ? -25.535 -39.087 27.384  1.00 183.48 ? 201 TYR A C   1 
ATOM   1538  O O   . TYR A 1 201 ? -25.565 -37.858 27.254  1.00 182.68 ? 201 TYR A O   1 
ATOM   1539  C CB  . TYR A 1 201 ? -23.723 -40.269 26.128  1.00 183.23 ? 201 TYR A CB  1 
ATOM   1540  C CG  . TYR A 1 201 ? -22.388 -39.696 25.729  1.00 182.51 ? 201 TYR A CG  1 
ATOM   1541  C CD1 . TYR A 1 201 ? -22.077 -38.367 25.985  1.00 181.81 ? 201 TYR A CD1 1 
ATOM   1542  C CD2 . TYR A 1 201 ? -21.434 -40.486 25.108  1.00 182.55 ? 201 TYR A CD2 1 
ATOM   1543  C CE1 . TYR A 1 201 ? -20.856 -37.840 25.621  1.00 182.58 ? 201 TYR A CE1 1 
ATOM   1544  C CE2 . TYR A 1 201 ? -20.212 -39.969 24.745  1.00 181.83 ? 201 TYR A CE2 1 
ATOM   1545  C CZ  . TYR A 1 201 ? -19.927 -38.647 25.002  1.00 181.37 ? 201 TYR A CZ  1 
ATOM   1546  O OH  . TYR A 1 201 ? -18.704 -38.136 24.637  1.00 180.23 ? 201 TYR A OH  1 
ATOM   1547  N N   . SER A 1 202 ? -26.641 -39.829 27.399  1.00 158.48 ? 202 SER A N   1 
ATOM   1548  C CA  . SER A 1 202 ? -27.980 -39.253 27.338  1.00 153.86 ? 202 SER A CA  1 
ATOM   1549  C C   . SER A 1 202 ? -28.610 -39.069 28.712  1.00 151.43 ? 202 SER A C   1 
ATOM   1550  O O   . SER A 1 202 ? -29.280 -38.061 28.949  1.00 150.61 ? 202 SER A O   1 
ATOM   1551  C CB  . SER A 1 202 ? -28.898 -40.124 26.473  1.00 150.13 ? 202 SER A CB  1 
ATOM   1552  O OG  . SER A 1 202 ? -28.321 -40.399 25.211  1.00 148.97 ? 202 SER A OG  1 
ATOM   1553  N N   . GLN A 1 203 ? -28.414 -40.027 29.620  1.00 155.41 ? 203 GLN A N   1 
ATOM   1554  C CA  . GLN A 1 203 ? -29.043 -39.953 30.934  1.00 157.19 ? 203 GLN A CA  1 
ATOM   1555  C C   . GLN A 1 203 ? -28.231 -39.093 31.896  1.00 154.00 ? 203 GLN A C   1 
ATOM   1556  O O   . GLN A 1 203 ? -28.786 -38.231 32.587  1.00 150.28 ? 203 GLN A O   1 
ATOM   1557  C CB  . GLN A 1 203 ? -29.236 -41.361 31.502  1.00 159.95 ? 203 GLN A CB  1 
ATOM   1558  C CG  . GLN A 1 203 ? -29.860 -41.390 32.890  1.00 168.08 ? 203 GLN A CG  1 
ATOM   1559  C CD  . GLN A 1 203 ? -29.039 -42.193 33.883  1.00 167.58 ? 203 GLN A CD  1 
ATOM   1560  O OE1 . GLN A 1 203 ? -28.579 -43.294 33.581  1.00 164.86 ? 203 GLN A OE1 1 
ATOM   1561  N NE2 . GLN A 1 203 ? -28.849 -41.641 35.075  1.00 168.07 ? 203 GLN A NE2 1 
ATOM   1562  N N   . ILE A 1 204 ? -26.918 -39.308 31.949  1.00 155.11 ? 204 ILE A N   1 
ATOM   1563  C CA  . ILE A 1 204 ? -26.056 -38.583 32.876  1.00 157.63 ? 204 ILE A CA  1 
ATOM   1564  C C   . ILE A 1 204 ? -25.381 -37.433 32.140  1.00 157.67 ? 204 ILE A C   1 
ATOM   1565  O O   . ILE A 1 204 ? -25.060 -36.401 32.742  1.00 154.20 ? 204 ILE A O   1 
ATOM   1566  C CB  . ILE A 1 204 ? -25.017 -39.521 33.519  1.00 158.87 ? 204 ILE A CB  1 
ATOM   1567  C CG1 . ILE A 1 204 ? -25.708 -40.736 34.139  1.00 159.09 ? 204 ILE A CG1 1 
ATOM   1568  C CG2 . ILE A 1 204 ? -24.211 -38.787 34.579  1.00 156.08 ? 204 ILE A CG2 1 
ATOM   1569  C CD1 . ILE A 1 204 ? -24.755 -41.715 34.794  1.00 160.26 ? 204 ILE A CD1 1 
ATOM   1570  N N   . ARG A 1 205 ? -25.170 -37.605 30.837  1.00 155.44 ? 205 ARG A N   1 
ATOM   1571  C CA  . ARG A 1 205 ? -24.567 -36.579 29.986  1.00 154.10 ? 205 ARG A CA  1 
ATOM   1572  C C   . ARG A 1 205 ? -23.186 -36.162 30.485  1.00 151.08 ? 205 ARG A C   1 
ATOM   1573  O O   . ARG A 1 205 ? -22.166 -36.595 29.948  1.00 148.70 ? 205 ARG A O   1 
ATOM   1574  C CB  . ARG A 1 205 ? -25.487 -35.357 29.893  1.00 149.10 ? 205 ARG A CB  1 
ATOM   1575  C CG  . ARG A 1 205 ? -26.851 -35.653 29.287  1.00 144.31 ? 205 ARG A CG  1 
ATOM   1576  C CD  . ARG A 1 205 ? -27.956 -34.863 29.975  1.00 137.18 ? 205 ARG A CD  1 
ATOM   1577  N NE  . ARG A 1 205 ? -28.187 -35.315 31.345  1.00 136.10 ? 205 ARG A NE  1 
ATOM   1578  C CZ  . ARG A 1 205 ? -27.704 -34.711 32.427  1.00 132.36 ? 205 ARG A CZ  1 
ATOM   1579  N NH1 . ARG A 1 205 ? -26.959 -33.621 32.305  1.00 123.80 ? 205 ARG A NH1 1 
ATOM   1580  N NH2 . ARG A 1 205 ? -27.968 -35.197 33.632  1.00 134.73 ? 205 ARG A NH2 1 
ATOM   1581  N N   . PHE A 1 222 ? -16.520 -36.717 25.348  1.00 165.96 ? 222 PHE A N   1 
ATOM   1582  C CA  . PHE A 1 222 ? -15.776 -36.363 26.552  1.00 168.56 ? 222 PHE A CA  1 
ATOM   1583  C C   . PHE A 1 222 ? -15.949 -37.423 27.634  1.00 167.79 ? 222 PHE A C   1 
ATOM   1584  O O   . PHE A 1 222 ? -15.438 -37.276 28.744  1.00 166.06 ? 222 PHE A O   1 
ATOM   1585  C CB  . PHE A 1 222 ? -16.223 -34.998 27.079  1.00 166.56 ? 222 PHE A CB  1 
ATOM   1586  C CG  . PHE A 1 222 ? -17.699 -34.903 27.341  1.00 166.93 ? 222 PHE A CG  1 
ATOM   1587  C CD1 . PHE A 1 222 ? -18.221 -35.247 28.577  1.00 166.46 ? 222 PHE A CD1 1 
ATOM   1588  C CD2 . PHE A 1 222 ? -18.563 -34.472 26.349  1.00 170.54 ? 222 PHE A CD2 1 
ATOM   1589  C CE1 . PHE A 1 222 ? -19.578 -35.163 28.819  1.00 168.74 ? 222 PHE A CE1 1 
ATOM   1590  C CE2 . PHE A 1 222 ? -19.921 -34.386 26.585  1.00 170.93 ? 222 PHE A CE2 1 
ATOM   1591  C CZ  . PHE A 1 222 ? -20.429 -34.732 27.822  1.00 168.56 ? 222 PHE A CZ  1 
ATOM   1592  N N   . VAL A 1 223 ? -16.676 -38.487 27.309  1.00 162.97 ? 223 VAL A N   1 
ATOM   1593  C CA  . VAL A 1 223 ? -16.897 -39.589 28.237  1.00 155.97 ? 223 VAL A CA  1 
ATOM   1594  C C   . VAL A 1 223 ? -15.724 -40.551 28.118  1.00 152.90 ? 223 VAL A C   1 
ATOM   1595  O O   . VAL A 1 223 ? -15.440 -41.068 27.032  1.00 151.21 ? 223 VAL A O   1 
ATOM   1596  C CB  . VAL A 1 223 ? -18.231 -40.298 27.957  1.00 154.79 ? 223 VAL A CB  1 
ATOM   1597  C CG1 . VAL A 1 223 ? -18.306 -41.607 28.723  1.00 148.87 ? 223 VAL A CG1 1 
ATOM   1598  C CG2 . VAL A 1 223 ? -19.392 -39.401 28.345  1.00 159.13 ? 223 VAL A CG2 1 
ATOM   1599  N N   . ARG A 1 224 ? -15.036 -40.783 29.232  1.00 150.75 ? 224 ARG A N   1 
ATOM   1600  C CA  . ARG A 1 224 ? -13.876 -41.662 29.263  1.00 150.09 ? 224 ARG A CA  1 
ATOM   1601  C C   . ARG A 1 224 ? -14.322 -43.071 29.625  1.00 144.32 ? 224 ARG A C   1 
ATOM   1602  O O   . ARG A 1 224 ? -15.044 -43.265 30.608  1.00 143.76 ? 224 ARG A O   1 
ATOM   1603  C CB  . ARG A 1 224 ? -12.833 -41.166 30.267  1.00 148.75 ? 224 ARG A CB  1 
ATOM   1604  C CG  . ARG A 1 224 ? -12.295 -39.758 30.017  1.00 148.98 ? 224 ARG A CG  1 
ATOM   1605  C CD  . ARG A 1 224 ? -13.214 -38.693 30.602  1.00 147.65 ? 224 ARG A CD  1 
ATOM   1606  N NE  . ARG A 1 224 ? -13.715 -39.087 31.917  1.00 149.77 ? 224 ARG A NE  1 
ATOM   1607  C CZ  . ARG A 1 224 ? -14.902 -38.739 32.403  1.00 149.14 ? 224 ARG A CZ  1 
ATOM   1608  N NH1 . ARG A 1 224 ? -15.724 -37.987 31.683  1.00 150.29 ? 224 ARG A NH1 1 
ATOM   1609  N NH2 . ARG A 1 224 ? -15.271 -39.148 33.609  1.00 146.62 ? 224 ARG A NH2 1 
ATOM   1610  N N   . LEU A 1 225 ? -13.877 -44.051 28.838  1.00 138.75 ? 225 LEU A N   1 
ATOM   1611  C CA  . LEU A 1 225 ? -14.309 -45.429 29.052  1.00 132.08 ? 225 LEU A CA  1 
ATOM   1612  C C   . LEU A 1 225 ? -13.869 -45.940 30.420  1.00 132.71 ? 225 LEU A C   1 
ATOM   1613  O O   . LEU A 1 225 ? -14.650 -46.572 31.140  1.00 130.54 ? 225 LEU A O   1 
ATOM   1614  C CB  . LEU A 1 225 ? -13.759 -46.321 27.936  1.00 129.09 ? 225 LEU A CB  1 
ATOM   1615  C CG  . LEU A 1 225 ? -14.544 -47.576 27.545  1.00 124.75 ? 225 LEU A CG  1 
ATOM   1616  C CD1 . LEU A 1 225 ? -14.216 -47.976 26.112  1.00 119.51 ? 225 LEU A CD1 1 
ATOM   1617  C CD2 . LEU A 1 225 ? -14.255 -48.722 28.497  1.00 120.82 ? 225 LEU A CD2 1 
ATOM   1618  N N   . ASP A 1 226 ? -12.620 -45.676 30.795  1.00 138.85 ? 226 ASP A N   1 
ATOM   1619  C CA  . ASP A 1 226 ? -12.043 -46.216 32.027  1.00 140.05 ? 226 ASP A CA  1 
ATOM   1620  C C   . ASP A 1 226 ? -12.157 -45.260 33.207  1.00 142.49 ? 226 ASP A C   1 
ATOM   1621  O O   . ASP A 1 226 ? -11.215 -45.128 33.993  1.00 146.55 ? 226 ASP A O   1 
ATOM   1622  C CB  . ASP A 1 226 ? -10.588 -46.602 31.781  1.00 139.25 ? 226 ASP A CB  1 
ATOM   1623  C CG  . ASP A 1 226 ? -9.841  -45.575 30.961  1.00 141.61 ? 226 ASP A CG  1 
ATOM   1624  O OD1 . ASP A 1 226 ? -9.805  -44.396 31.370  1.00 141.32 ? 226 ASP A OD1 1 
ATOM   1625  O OD2 . ASP A 1 226 ? -9.286  -45.948 29.907  1.00 146.88 ? 226 ASP A OD2 1 
ATOM   1626  N N   . GLN A 1 227 ? -13.285 -44.570 33.356  1.00 139.79 ? 227 GLN A N   1 
ATOM   1627  C CA  . GLN A 1 227 ? -13.465 -43.650 34.473  1.00 142.23 ? 227 GLN A CA  1 
ATOM   1628  C C   . GLN A 1 227 ? -14.914 -43.633 34.935  1.00 146.76 ? 227 GLN A C   1 
ATOM   1629  O O   . GLN A 1 227 ? -15.191 -43.648 36.139  1.00 140.64 ? 227 GLN A O   1 
ATOM   1630  C CB  . GLN A 1 227 ? -13.012 -42.241 34.088  1.00 146.39 ? 227 GLN A CB  1 
ATOM   1631  C CG  . GLN A 1 227 ? -11.584 -41.921 34.495  1.00 147.41 ? 227 GLN A CG  1 
ATOM   1632  C CD  . GLN A 1 227 ? -10.698 -41.583 33.316  1.00 146.52 ? 227 GLN A CD  1 
ATOM   1633  O OE1 . GLN A 1 227 ? -10.450 -40.413 33.027  1.00 146.02 ? 227 GLN A OE1 1 
ATOM   1634  N NE2 . GLN A 1 227 ? -10.208 -42.608 32.631  1.00 145.43 ? 227 GLN A NE2 1 
ATOM   1635  N N   . ASP A 1 228 ? -15.848 -43.601 33.987  1.00 180.24 ? 228 ASP A N   1 
ATOM   1636  C CA  . ASP A 1 228 ? -17.269 -43.545 34.302  1.00 180.17 ? 228 ASP A CA  1 
ATOM   1637  C C   . ASP A 1 228 ? -18.032 -44.718 33.705  1.00 180.33 ? 228 ASP A C   1 
ATOM   1638  O O   . ASP A 1 228 ? -19.269 -44.714 33.717  1.00 180.20 ? 228 ASP A O   1 
ATOM   1639  C CB  . ASP A 1 228 ? -17.870 -42.214 33.832  1.00 178.63 ? 228 ASP A CB  1 
ATOM   1640  C CG  . ASP A 1 228 ? -17.615 -41.935 32.360  1.00 177.63 ? 228 ASP A CG  1 
ATOM   1641  O OD1 . ASP A 1 228 ? -17.510 -42.893 31.568  1.00 177.69 ? 228 ASP A OD1 1 
ATOM   1642  O OD2 . ASP A 1 228 ? -17.512 -40.745 31.993  1.00 178.03 ? 228 ASP A OD2 1 
ATOM   1643  N N   . ILE A 1 229 ? -17.326 -45.720 33.184  1.00 143.58 ? 229 ILE A N   1 
ATOM   1644  C CA  . ILE A 1 229 ? -17.950 -46.919 32.639  1.00 134.26 ? 229 ILE A CA  1 
ATOM   1645  C C   . ILE A 1 229 ? -17.300 -48.147 33.263  1.00 124.27 ? 229 ILE A C   1 
ATOM   1646  O O   . ILE A 1 229 ? -17.992 -49.088 33.670  1.00 120.71 ? 229 ILE A O   1 
ATOM   1647  C CB  . ILE A 1 229 ? -17.851 -46.951 31.102  1.00 130.87 ? 229 ILE A CB  1 
ATOM   1648  C CG1 . ILE A 1 229 ? -18.641 -45.791 30.490  1.00 134.56 ? 229 ILE A CG1 1 
ATOM   1649  C CG2 . ILE A 1 229 ? -18.343 -48.284 30.559  1.00 120.19 ? 229 ILE A CG2 1 
ATOM   1650  C CD1 . ILE A 1 229 ? -18.587 -45.742 28.977  1.00 128.71 ? 229 ILE A CD1 1 
ATOM   1651  N N   . LEU A 1 230 ? -15.967 -48.153 33.338  1.00 123.60 ? 230 LEU A N   1 
ATOM   1652  C CA  . LEU A 1 230 ? -15.266 -49.285 33.937  1.00 116.90 ? 230 LEU A CA  1 
ATOM   1653  C C   . LEU A 1 230 ? -15.343 -49.250 35.460  1.00 115.62 ? 230 LEU A C   1 
ATOM   1654  O O   . LEU A 1 230 ? -15.620 -50.272 36.098  1.00 111.95 ? 230 LEU A O   1 
ATOM   1655  C CB  . LEU A 1 230 ? -13.809 -49.322 33.469  1.00 119.42 ? 230 LEU A CB  1 
ATOM   1656  C CG  . LEU A 1 230 ? -13.586 -49.653 31.991  1.00 120.82 ? 230 LEU A CG  1 
ATOM   1657  C CD1 . LEU A 1 230 ? -12.106 -49.841 31.689  1.00 123.33 ? 230 LEU A CD1 1 
ATOM   1658  C CD2 . LEU A 1 230 ? -14.379 -50.888 31.589  1.00 121.11 ? 230 LEU A CD2 1 
ATOM   1659  N N   . SER A 1 231 ? -15.096 -48.085 36.060  1.00 117.48 ? 231 SER A N   1 
ATOM   1660  C CA  . SER A 1 231 ? -15.159 -47.975 37.517  1.00 113.48 ? 231 SER A CA  1 
ATOM   1661  C C   . SER A 1 231 ? -16.551 -48.248 38.078  1.00 112.28 ? 231 SER A C   1 
ATOM   1662  O O   . SER A 1 231 ? -16.651 -48.978 39.079  1.00 113.25 ? 231 SER A O   1 
ATOM   1663  C CB  . SER A 1 231 ? -14.638 -46.600 37.956  1.00 114.55 ? 231 SER A CB  1 
ATOM   1664  O OG  . SER A 1 231 ? -13.340 -46.358 37.447  1.00 118.82 ? 231 SER A OG  1 
ATOM   1665  N N   . PRO A 1 232 ? -17.645 -47.709 37.522  1.00 115.33 ? 232 PRO A N   1 
ATOM   1666  C CA  . PRO A 1 232 ? -18.968 -48.000 38.105  1.00 114.73 ? 232 PRO A CA  1 
ATOM   1667  C C   . PRO A 1 232 ? -19.366 -49.465 38.060  1.00 115.20 ? 232 PRO A C   1 
ATOM   1668  O O   . PRO A 1 232 ? -20.029 -49.941 38.991  1.00 112.80 ? 232 PRO A O   1 
ATOM   1669  C CB  . PRO A 1 232 ? -19.916 -47.142 37.256  1.00 116.57 ? 232 PRO A CB  1 
ATOM   1670  C CG  . PRO A 1 232 ? -19.067 -46.041 36.750  1.00 124.02 ? 232 PRO A CG  1 
ATOM   1671  C CD  . PRO A 1 232 ? -17.742 -46.677 36.475  1.00 122.71 ? 232 PRO A CD  1 
ATOM   1672  N N   . LEU A 1 233 ? -18.988 -50.202 37.016  1.00 125.44 ? 233 LEU A N   1 
ATOM   1673  C CA  . LEU A 1 233 ? -19.343 -51.618 36.913  1.00 126.08 ? 233 LEU A CA  1 
ATOM   1674  C C   . LEU A 1 233 ? -18.363 -52.446 37.745  1.00 128.96 ? 233 LEU A C   1 
ATOM   1675  O O   . LEU A 1 233 ? -17.482 -53.144 37.239  1.00 134.02 ? 233 LEU A O   1 
ATOM   1676  C CB  . LEU A 1 233 ? -19.367 -52.064 35.459  1.00 130.05 ? 233 LEU A CB  1 
ATOM   1677  C CG  . LEU A 1 233 ? -20.666 -52.765 35.056  1.00 133.53 ? 233 LEU A CG  1 
ATOM   1678  C CD1 . LEU A 1 233 ? -21.848 -51.815 35.197  1.00 135.90 ? 233 LEU A CD1 1 
ATOM   1679  C CD2 . LEU A 1 233 ? -20.575 -53.313 33.641  1.00 136.07 ? 233 LEU A CD2 1 
ATOM   1680  N N   . ALA A 1 234 ? -18.534 -52.351 39.063  1.00 113.24 ? 234 ALA A N   1 
ATOM   1681  C CA  . ALA A 1 234 ? -17.681 -53.052 40.015  1.00 111.34 ? 234 ALA A CA  1 
ATOM   1682  C C   . ALA A 1 234 ? -18.433 -54.198 40.682  1.00 107.55 ? 234 ALA A C   1 
ATOM   1683  O O   . ALA A 1 234 ? -18.161 -55.364 40.391  1.00 108.85 ? 234 ALA A O   1 
ATOM   1684  C CB  . ALA A 1 234 ? -17.133 -52.068 41.051  1.00 110.44 ? 234 ALA A CB  1 
ATOM   1685  N N   . GLY A 1 235 ? -19.373 -53.900 41.580  1.00 105.90 ? 235 GLY A N   1 
ATOM   1686  C CA  . GLY A 1 235 ? -20.102 -54.963 42.256  1.00 102.34 ? 235 GLY A CA  1 
ATOM   1687  C C   . GLY A 1 235 ? -20.995 -55.767 41.328  1.00 103.37 ? 235 GLY A C   1 
ATOM   1688  O O   . GLY A 1 235 ? -21.143 -56.981 41.496  1.00 104.01 ? 235 GLY A O   1 
ATOM   1689  N N   . LYS A 1 236 ? -21.595 -55.109 40.337  1.00 104.32 ? 236 LYS A N   1 
ATOM   1690  C CA  . LYS A 1 236 ? -22.476 -55.800 39.404  1.00 101.84 ? 236 LYS A CA  1 
ATOM   1691  C C   . LYS A 1 236 ? -21.694 -56.812 38.577  1.00 104.44 ? 236 LYS A C   1 
ATOM   1692  O O   . LYS A 1 236 ? -20.713 -56.464 37.911  1.00 105.91 ? 236 LYS A O   1 
ATOM   1693  C CB  . LYS A 1 236 ? -23.181 -54.794 38.498  1.00 101.94 ? 236 LYS A CB  1 
ATOM   1694  C CG  . LYS A 1 236 ? -22.550 -53.414 38.471  1.00 104.79 ? 236 LYS A CG  1 
ATOM   1695  C CD  . LYS A 1 236 ? -23.529 -52.353 38.951  1.00 98.28  ? 236 LYS A CD  1 
ATOM   1696  C CE  . LYS A 1 236 ? -23.528 -52.232 40.467  1.00 93.94  ? 236 LYS A CE  1 
ATOM   1697  N NZ  . LYS A 1 236 ? -22.239 -51.685 40.978  1.00 101.50 ? 236 LYS A NZ  1 
ATOM   1698  N N   . LYS A 1 237 ? -22.140 -58.067 38.616  1.00 105.33 ? 237 LYS A N   1 
ATOM   1699  C CA  . LYS A 1 237 ? -21.449 -59.177 37.960  1.00 107.62 ? 237 LYS A CA  1 
ATOM   1700  C C   . LYS A 1 237 ? -21.640 -59.094 36.448  1.00 110.61 ? 237 LYS A C   1 
ATOM   1701  O O   . LYS A 1 237 ? -22.438 -59.815 35.843  1.00 109.58 ? 237 LYS A O   1 
ATOM   1702  C CB  . LYS A 1 237 ? -21.952 -60.511 38.500  1.00 113.73 ? 237 LYS A CB  1 
ATOM   1703  C CG  . LYS A 1 237 ? -21.609 -60.773 39.957  1.00 115.46 ? 237 LYS A CG  1 
ATOM   1704  C CD  . LYS A 1 237 ? -20.236 -61.415 40.081  1.00 119.97 ? 237 LYS A CD  1 
ATOM   1705  C CE  . LYS A 1 237 ? -20.087 -62.576 39.114  1.00 117.10 ? 237 LYS A CE  1 
ATOM   1706  N NZ  . LYS A 1 237 ? -20.873 -63.762 39.544  1.00 113.94 ? 237 LYS A NZ  1 
ATOM   1707  N N   . GLN A 1 238 ? -20.892 -58.183 35.826  1.00 115.65 ? 238 GLN A N   1 
ATOM   1708  C CA  . GLN A 1 238 ? -20.871 -58.051 34.373  1.00 117.61 ? 238 GLN A CA  1 
ATOM   1709  C C   . GLN A 1 238 ? -19.476 -57.875 33.792  1.00 122.48 ? 238 GLN A C   1 
ATOM   1710  O O   . GLN A 1 238 ? -19.242 -58.315 32.662  1.00 119.61 ? 238 GLN A O   1 
ATOM   1711  C CB  . GLN A 1 238 ? -21.750 -56.870 33.935  1.00 115.41 ? 238 GLN A CB  1 
ATOM   1712  C CG  . GLN A 1 238 ? -23.243 -57.134 34.022  1.00 112.77 ? 238 GLN A CG  1 
ATOM   1713  C CD  . GLN A 1 238 ? -23.896 -56.392 35.169  1.00 110.76 ? 238 GLN A CD  1 
ATOM   1714  O OE1 . GLN A 1 238 ? -23.916 -55.161 35.198  1.00 106.79 ? 238 GLN A OE1 1 
ATOM   1715  N NE2 . GLN A 1 238 ? -24.429 -57.139 36.126  1.00 112.65 ? 238 GLN A NE2 1 
ATOM   1716  N N   . LEU A 1 239 ? -18.548 -57.250 34.510  1.00 148.54 ? 239 LEU A N   1 
ATOM   1717  C CA  . LEU A 1 239 ? -17.183 -57.059 34.041  1.00 148.48 ? 239 LEU A CA  1 
ATOM   1718  C C   . LEU A 1 239 ? -16.308 -58.197 34.548  1.00 150.68 ? 239 LEU A C   1 
ATOM   1719  O O   . LEU A 1 239 ? -16.270 -58.468 35.752  1.00 152.17 ? 239 LEU A O   1 
ATOM   1720  C CB  . LEU A 1 239 ? -16.633 -55.711 34.508  1.00 147.92 ? 239 LEU A CB  1 
ATOM   1721  C CG  . LEU A 1 239 ? -15.917 -54.898 33.432  1.00 147.52 ? 239 LEU A CG  1 
ATOM   1722  C CD1 . LEU A 1 239 ? -14.631 -55.587 33.006  1.00 147.33 ? 239 LEU A CD1 1 
ATOM   1723  C CD2 . LEU A 1 239 ? -16.840 -54.703 32.240  1.00 144.47 ? 239 LEU A CD2 1 
ATOM   1724  N N   . TYR A 1 240 ? -15.616 -58.862 33.633  1.00 128.74 ? 240 TYR A N   1 
ATOM   1725  C CA  . TYR A 1 240 ? -14.818 -60.019 33.998  1.00 124.49 ? 240 TYR A CA  1 
ATOM   1726  C C   . TYR A 1 240 ? -13.348 -59.788 33.645  1.00 122.19 ? 240 TYR A C   1 
ATOM   1727  O O   . TYR A 1 240 ? -12.941 -58.685 33.274  1.00 123.52 ? 240 TYR A O   1 
ATOM   1728  C CB  . TYR A 1 240 ? -15.389 -61.272 33.335  1.00 121.37 ? 240 TYR A CB  1 
ATOM   1729  C CG  . TYR A 1 240 ? -16.715 -61.687 33.926  1.00 122.79 ? 240 TYR A CG  1 
ATOM   1730  C CD1 . TYR A 1 240 ? -16.769 -62.476 35.067  1.00 122.58 ? 240 TYR A CD1 1 
ATOM   1731  C CD2 . TYR A 1 240 ? -17.911 -61.269 33.360  1.00 121.75 ? 240 TYR A CD2 1 
ATOM   1732  C CE1 . TYR A 1 240 ? -17.977 -62.850 35.618  1.00 120.54 ? 240 TYR A CE1 1 
ATOM   1733  C CE2 . TYR A 1 240 ? -19.125 -61.638 33.905  1.00 119.62 ? 240 TYR A CE2 1 
ATOM   1734  C CZ  . TYR A 1 240 ? -19.151 -62.429 35.035  1.00 117.76 ? 240 TYR A CZ  1 
ATOM   1735  O OH  . TYR A 1 240 ? -20.354 -62.803 35.587  1.00 117.75 ? 240 TYR A OH  1 
ATOM   1736  N N   . THR A 1 241 ? -12.548 -60.846 33.778  1.00 119.44 ? 241 THR A N   1 
ATOM   1737  C CA  . THR A 1 241 ? -11.108 -60.772 33.562  1.00 116.79 ? 241 THR A CA  1 
ATOM   1738  C C   . THR A 1 241 ? -10.613 -62.091 32.986  1.00 116.83 ? 241 THR A C   1 
ATOM   1739  O O   . THR A 1 241 ? -11.237 -63.140 33.159  1.00 119.71 ? 241 THR A O   1 
ATOM   1740  C CB  . THR A 1 241 ? -10.350 -60.458 34.858  1.00 119.89 ? 241 THR A CB  1 
ATOM   1741  O OG1 . THR A 1 241 ? -10.929 -61.196 35.940  1.00 122.79 ? 241 THR A OG1 1 
ATOM   1742  C CG2 . THR A 1 241 ? -10.403 -58.968 35.173  1.00 119.94 ? 241 THR A CG2 1 
ATOM   1743  N N   . TYR A 1 242 ? -9.472  -62.024 32.304  1.00 114.85 ? 242 TYR A N   1 
ATOM   1744  C CA  . TYR A 1 242 ? -8.844  -63.203 31.715  1.00 117.36 ? 242 TYR A CA  1 
ATOM   1745  C C   . TYR A 1 242 ? -7.351  -62.941 31.603  1.00 121.26 ? 242 TYR A C   1 
ATOM   1746  O O   . TYR A 1 242 ? -6.941  -61.953 30.986  1.00 122.65 ? 242 TYR A O   1 
ATOM   1747  C CB  . TYR A 1 242 ? -9.449  -63.522 30.348  1.00 116.14 ? 242 TYR A CB  1 
ATOM   1748  C CG  . TYR A 1 242 ? -8.698  -64.556 29.537  1.00 115.86 ? 242 TYR A CG  1 
ATOM   1749  C CD1 . TYR A 1 242 ? -8.831  -65.912 29.803  1.00 115.95 ? 242 TYR A CD1 1 
ATOM   1750  C CD2 . TYR A 1 242 ? -7.870  -64.174 28.490  1.00 116.99 ? 242 TYR A CD2 1 
ATOM   1751  C CE1 . TYR A 1 242 ? -8.148  -66.858 29.057  1.00 116.25 ? 242 TYR A CE1 1 
ATOM   1752  C CE2 . TYR A 1 242 ? -7.184  -65.110 27.738  1.00 119.54 ? 242 TYR A CE2 1 
ATOM   1753  C CZ  . TYR A 1 242 ? -7.326  -66.451 28.025  1.00 116.66 ? 242 TYR A CZ  1 
ATOM   1754  O OH  . TYR A 1 242 ? -6.644  -67.386 27.277  1.00 120.98 ? 242 TYR A OH  1 
ATOM   1755  N N   . GLU A 1 243 ? -6.546  -63.823 32.191  1.00 131.40 ? 243 GLU A N   1 
ATOM   1756  C CA  . GLU A 1 243 ? -5.110  -63.595 32.276  1.00 131.87 ? 243 GLU A CA  1 
ATOM   1757  C C   . GLU A 1 243 ? -4.443  -63.696 30.907  1.00 130.75 ? 243 GLU A C   1 
ATOM   1758  O O   . GLU A 1 243 ? -4.886  -64.437 30.023  1.00 130.64 ? 243 GLU A O   1 
ATOM   1759  C CB  . GLU A 1 243 ? -4.472  -64.596 33.240  1.00 134.59 ? 243 GLU A CB  1 
ATOM   1760  N N   . ASN A 1 244 ? -3.362  -62.930 30.742  1.00 114.69 ? 244 ASN A N   1 
ATOM   1761  C CA  . ASN A 1 244 ? -2.580  -62.956 29.510  1.00 108.30 ? 244 ASN A CA  1 
ATOM   1762  C C   . ASN A 1 244 ? -1.707  -64.205 29.442  1.00 105.33 ? 244 ASN A C   1 
ATOM   1763  O O   . ASN A 1 244 ? -1.787  -64.979 28.481  1.00 103.45 ? 244 ASN A O   1 
ATOM   1764  C CB  . ASN A 1 244 ? -1.720  -61.691 29.412  1.00 108.01 ? 244 ASN A CB  1 
ATOM   1765  C CG  . ASN A 1 244 ? -1.131  -61.485 28.025  1.00 102.45 ? 244 ASN A CG  1 
ATOM   1766  O OD1 . ASN A 1 244 ? -1.003  -62.427 27.242  1.00 104.63 ? 244 ASN A OD1 1 
ATOM   1767  N ND2 . ASN A 1 244 ? -0.758  -60.247 27.721  1.00 99.73  ? 244 ASN A ND2 1 
ATOM   1768  N N   . LYS A 1 245 ? -0.842  -64.389 30.445  1.00 102.88 ? 245 LYS A N   1 
ATOM   1769  C CA  . LYS A 1 245 ? 0.111   -65.500 30.519  1.00 95.20  ? 245 LYS A CA  1 
ATOM   1770  C C   . LYS A 1 245 ? 1.168   -65.425 29.421  1.00 90.47  ? 245 LYS A C   1 
ATOM   1771  O O   . LYS A 1 245 ? 1.688   -66.452 28.978  1.00 84.62  ? 245 LYS A O   1 
ATOM   1772  C CB  . LYS A 1 245 ? -0.595  -66.861 30.488  1.00 98.61  ? 245 LYS A CB  1 
ATOM   1773  N N   . ASP A 1 246 ? 1.495   -64.212 28.978  1.00 94.36  ? 246 ASP A N   1 
ATOM   1774  C CA  . ASP A 1 246 ? 2.540   -64.020 27.980  1.00 92.01  ? 246 ASP A CA  1 
ATOM   1775  C C   . ASP A 1 246 ? 3.258   -62.689 28.183  1.00 88.58  ? 246 ASP A C   1 
ATOM   1776  O O   . ASP A 1 246 ? 3.823   -62.444 29.254  1.00 85.93  ? 246 ASP A O   1 
ATOM   1777  C CB  . ASP A 1 246 ? 1.950   -64.113 26.572  1.00 93.51  ? 246 ASP A CB  1 
ATOM   1778  C CG  . ASP A 1 246 ? 1.870   -65.543 26.072  1.00 88.48  ? 246 ASP A CG  1 
ATOM   1779  O OD1 . ASP A 1 246 ? 2.925   -66.209 26.019  1.00 89.08  ? 246 ASP A OD1 1 
ATOM   1780  O OD2 . ASP A 1 246 ? 0.758   -66.002 25.732  1.00 88.12  ? 246 ASP A OD2 1 
ATOM   1781  N N   . PHE A 1 247 ? 3.243   -61.823 27.172  1.00 90.71  ? 247 PHE A N   1 
ATOM   1782  C CA  . PHE A 1 247 ? 3.960   -60.559 27.224  1.00 93.83  ? 247 PHE A CA  1 
ATOM   1783  C C   . PHE A 1 247 ? 3.000   -59.393 27.030  1.00 101.72 ? 247 PHE A C   1 
ATOM   1784  O O   . PHE A 1 247 ? 1.909   -59.542 26.474  1.00 103.83 ? 247 PHE A O   1 
ATOM   1785  C CB  . PHE A 1 247 ? 5.063   -60.492 26.154  1.00 93.24  ? 247 PHE A CB  1 
ATOM   1786  C CG  . PHE A 1 247 ? 4.586   -60.821 24.760  1.00 93.85  ? 247 PHE A CG  1 
ATOM   1787  C CD1 . PHE A 1 247 ? 4.529   -62.133 24.317  1.00 94.82  ? 247 PHE A CD1 1 
ATOM   1788  C CD2 . PHE A 1 247 ? 4.214   -59.810 23.888  1.00 93.88  ? 247 PHE A CD2 1 
ATOM   1789  C CE1 . PHE A 1 247 ? 4.095   -62.429 23.035  1.00 93.85  ? 247 PHE A CE1 1 
ATOM   1790  C CE2 . PHE A 1 247 ? 3.783   -60.100 22.607  1.00 95.53  ? 247 PHE A CE2 1 
ATOM   1791  C CZ  . PHE A 1 247 ? 3.723   -61.411 22.180  1.00 96.72  ? 247 PHE A CZ  1 
ATOM   1792  N N   . TRP A 1 248 ? 3.424   -58.220 27.498  1.00 109.26 ? 248 TRP A N   1 
ATOM   1793  C CA  . TRP A 1 248 ? 2.685   -56.985 27.270  1.00 106.74 ? 248 TRP A CA  1 
ATOM   1794  C C   . TRP A 1 248 ? 3.594   -55.799 27.548  1.00 105.93 ? 248 TRP A C   1 
ATOM   1795  O O   . TRP A 1 248 ? 4.324   -55.788 28.542  1.00 107.65 ? 248 TRP A O   1 
ATOM   1796  C CB  . TRP A 1 248 ? 1.425   -56.881 28.130  1.00 107.33 ? 248 TRP A CB  1 
ATOM   1797  C CG  . TRP A 1 248 ? 0.617   -55.672 27.774  1.00 106.26 ? 248 TRP A CG  1 
ATOM   1798  C CD1 . TRP A 1 248 ? -0.193  -55.516 26.686  1.00 106.64 ? 248 TRP A CD1 1 
ATOM   1799  C CD2 . TRP A 1 248 ? 0.562   -54.437 28.496  1.00 104.63 ? 248 TRP A CD2 1 
ATOM   1800  N NE1 . TRP A 1 248 ? -0.758  -54.262 26.694  1.00 102.78 ? 248 TRP A NE1 1 
ATOM   1801  C CE2 . TRP A 1 248 ? -0.310  -53.581 27.795  1.00 104.86 ? 248 TRP A CE2 1 
ATOM   1802  C CE3 . TRP A 1 248 ? 1.161   -53.976 29.671  1.00 105.31 ? 248 TRP A CE3 1 
ATOM   1803  C CZ2 . TRP A 1 248 ? -0.598  -52.289 28.232  1.00 109.22 ? 248 TRP A CZ2 1 
ATOM   1804  C CZ3 . TRP A 1 248 ? 0.875   -52.695 30.104  1.00 108.74 ? 248 TRP A CZ3 1 
ATOM   1805  C CH2 . TRP A 1 248 ? 0.003   -51.866 29.386  1.00 111.26 ? 248 TRP A CH2 1 
ATOM   1806  N N   . GLU A 1 249 ? 3.543   -54.808 26.661  1.00 104.26 ? 249 GLU A N   1 
ATOM   1807  C CA  . GLU A 1 249 ? 4.356   -53.607 26.807  1.00 106.35 ? 249 GLU A CA  1 
ATOM   1808  C C   . GLU A 1 249 ? 3.654   -52.452 26.111  1.00 107.25 ? 249 GLU A C   1 
ATOM   1809  O O   . GLU A 1 249 ? 3.426   -52.506 24.900  1.00 104.63 ? 249 GLU A O   1 
ATOM   1810  C CB  . GLU A 1 249 ? 5.758   -53.820 26.231  1.00 105.40 ? 249 GLU A CB  1 
ATOM   1811  N N   . GLN A 1 250 ? 3.309   -51.418 26.875  1.00 122.68 ? 250 GLN A N   1 
ATOM   1812  C CA  . GLN A 1 250 ? 2.703   -50.222 26.303  1.00 119.94 ? 250 GLN A CA  1 
ATOM   1813  C C   . GLN A 1 250 ? 3.735   -49.461 25.479  1.00 117.90 ? 250 GLN A C   1 
ATOM   1814  O O   . GLN A 1 250 ? 4.854   -49.219 25.941  1.00 118.32 ? 250 GLN A O   1 
ATOM   1815  C CB  . GLN A 1 250 ? 2.144   -49.333 27.415  1.00 120.07 ? 250 GLN A CB  1 
ATOM   1816  C CG  . GLN A 1 250 ? 0.687   -48.933 27.233  1.00 119.19 ? 250 GLN A CG  1 
ATOM   1817  C CD  . GLN A 1 250 ? 0.524   -47.499 26.766  1.00 116.67 ? 250 GLN A CD  1 
ATOM   1818  O OE1 . GLN A 1 250 ? 0.100   -46.630 27.529  1.00 115.99 ? 250 GLN A OE1 1 
ATOM   1819  N NE2 . GLN A 1 250 ? 0.858   -47.244 25.506  1.00 114.71 ? 250 GLN A NE2 1 
ATOM   1820  N N   . ILE A 1 251 ? 3.359   -49.080 24.257  1.00 101.87 ? 251 ILE A N   1 
ATOM   1821  C CA  . ILE A 1 251 ? 4.308   -48.469 23.334  1.00 95.46  ? 251 ILE A CA  1 
ATOM   1822  C C   . ILE A 1 251 ? 3.839   -47.089 22.893  1.00 90.84  ? 251 ILE A C   1 
ATOM   1823  O O   . ILE A 1 251 ? 3.526   -46.870 21.717  1.00 86.98  ? 251 ILE A O   1 
ATOM   1824  C CB  . ILE A 1 251 ? 4.546   -49.374 22.111  1.00 92.69  ? 251 ILE A CB  1 
ATOM   1825  C CG1 . ILE A 1 251 ? 3.219   -49.923 21.581  1.00 93.24  ? 251 ILE A CG1 1 
ATOM   1826  C CG2 . ILE A 1 251 ? 5.491   -50.506 22.467  1.00 99.20  ? 251 ILE A CG2 1 
ATOM   1827  C CD1 . ILE A 1 251 ? 3.208   -50.119 20.085  1.00 88.72  ? 251 ILE A CD1 1 
ATOM   1828  N N   . LYS A 1 252 ? 3.813   -46.142 23.826  1.00 90.03  ? 252 LYS A N   1 
ATOM   1829  C CA  . LYS A 1 252 ? 3.598   -44.745 23.482  1.00 90.92  ? 252 LYS A CA  1 
ATOM   1830  C C   . LYS A 1 252 ? 4.900   -44.013 23.196  1.00 90.40  ? 252 LYS A C   1 
ATOM   1831  O O   . LYS A 1 252 ? 4.868   -42.906 22.649  1.00 92.85  ? 252 LYS A O   1 
ATOM   1832  C CB  . LYS A 1 252 ? 2.852   -44.021 24.607  1.00 100.97 ? 252 LYS A CB  1 
ATOM   1833  C CG  . LYS A 1 252 ? 3.640   -43.935 25.902  1.00 102.73 ? 252 LYS A CG  1 
ATOM   1834  C CD  . LYS A 1 252 ? 3.114   -44.911 26.942  1.00 104.56 ? 252 LYS A CD  1 
ATOM   1835  C CE  . LYS A 1 252 ? 4.205   -45.328 27.917  1.00 103.03 ? 252 LYS A CE  1 
ATOM   1836  N NZ  . LYS A 1 252 ? 5.189   -46.246 27.276  1.00 104.52 ? 252 LYS A NZ  1 
ATOM   1837  N N   . THR A 1 253 ? 6.035   -44.600 23.560  1.00 91.06  ? 253 THR A N   1 
ATOM   1838  C CA  . THR A 1 253 ? 7.390   -44.104 23.360  1.00 90.83  ? 253 THR A CA  1 
ATOM   1839  C C   . THR A 1 253 ? 7.962   -44.646 22.054  1.00 89.55  ? 253 THR A C   1 
ATOM   1840  O O   . THR A 1 253 ? 7.794   -45.831 21.748  1.00 86.19  ? 253 THR A O   1 
ATOM   1841  C CB  . THR A 1 253 ? 8.297   -44.523 24.515  1.00 90.71  ? 253 THR A CB  1 
ATOM   1842  O OG1 . THR A 1 253 ? 7.506   -44.738 25.693  1.00 96.16  ? 253 THR A OG1 1 
ATOM   1843  C CG2 . THR A 1 253 ? 9.335   -43.443 24.801  1.00 88.14  ? 253 THR A CG2 1 
ATOM   1844  N N   . PRO A 1 254 ? 8.631   -43.806 21.262  1.00 94.40  ? 254 PRO A N   1 
ATOM   1845  C CA  . PRO A 1 254 ? 9.354   -44.335 20.096  1.00 90.32  ? 254 PRO A CA  1 
ATOM   1846  C C   . PRO A 1 254 ? 10.509  -45.238 20.485  1.00 87.36  ? 254 PRO A C   1 
ATOM   1847  O O   . PRO A 1 254 ? 10.945  -46.053 19.664  1.00 86.55  ? 254 PRO A O   1 
ATOM   1848  C CB  . PRO A 1 254 ? 9.835   -43.068 19.377  1.00 89.30  ? 254 PRO A CB  1 
ATOM   1849  C CG  . PRO A 1 254 ? 9.897   -42.027 20.450  1.00 92.44  ? 254 PRO A CG  1 
ATOM   1850  C CD  . PRO A 1 254 ? 8.760   -42.343 21.382  1.00 94.69  ? 254 PRO A CD  1 
ATOM   1851  N N   . GLY A 1 255 ? 11.020  -45.115 21.712  1.00 82.73  ? 255 GLY A N   1 
ATOM   1852  C CA  . GLY A 1 255 ? 12.073  -46.009 22.163  1.00 81.68  ? 255 GLY A CA  1 
ATOM   1853  C C   . GLY A 1 255 ? 11.565  -47.411 22.439  1.00 81.76  ? 255 GLY A C   1 
ATOM   1854  O O   . GLY A 1 255 ? 12.272  -48.394 22.200  1.00 82.49  ? 255 GLY A O   1 
ATOM   1855  N N   . LYS A 1 256 ? 10.336  -47.525 22.952  1.00 80.45  ? 256 LYS A N   1 
ATOM   1856  C CA  . LYS A 1 256 ? 9.741   -48.834 23.198  1.00 83.53  ? 256 LYS A CA  1 
ATOM   1857  C C   . LYS A 1 256 ? 9.550   -49.641 21.922  1.00 79.79  ? 256 LYS A C   1 
ATOM   1858  O O   . LYS A 1 256 ? 9.258   -50.839 22.006  1.00 81.48  ? 256 LYS A O   1 
ATOM   1859  C CB  . LYS A 1 256 ? 8.396   -48.684 23.914  1.00 89.19  ? 256 LYS A CB  1 
ATOM   1860  C CG  . LYS A 1 256 ? 8.502   -48.430 25.411  1.00 93.07  ? 256 LYS A CG  1 
ATOM   1861  C CD  . LYS A 1 256 ? 9.077   -49.641 26.132  1.00 95.39  ? 256 LYS A CD  1 
ATOM   1862  C CE  . LYS A 1 256 ? 8.743   -49.622 27.616  1.00 97.68  ? 256 LYS A CE  1 
ATOM   1863  N NZ  . LYS A 1 256 ? 7.272   -49.579 27.850  1.00 97.23  ? 256 LYS A NZ  1 
ATOM   1864  N N   . SER A 1 257 ? 9.705   -49.020 20.751  1.00 77.64  ? 257 SER A N   1 
ATOM   1865  C CA  . SER A 1 257 ? 9.533   -49.719 19.485  1.00 78.30  ? 257 SER A CA  1 
ATOM   1866  C C   . SER A 1 257 ? 10.545  -50.840 19.283  1.00 78.73  ? 257 SER A C   1 
ATOM   1867  O O   . SER A 1 257 ? 10.389  -51.623 18.340  1.00 84.76  ? 257 SER A O   1 
ATOM   1868  C CB  . SER A 1 257 ? 9.632   -48.723 18.329  1.00 79.62  ? 257 SER A CB  1 
ATOM   1869  O OG  . SER A 1 257 ? 8.735   -47.642 18.516  1.00 81.62  ? 257 SER A OG  1 
ATOM   1870  N N   . LEU A 1 258 ? 11.578  -50.930 20.121  1.00 79.15  ? 258 LEU A N   1 
ATOM   1871  C CA  . LEU A 1 258 ? 12.558  -52.008 20.049  1.00 81.41  ? 258 LEU A CA  1 
ATOM   1872  C C   . LEU A 1 258 ? 12.283  -53.131 21.042  1.00 80.87  ? 258 LEU A C   1 
ATOM   1873  O O   . LEU A 1 258 ? 12.308  -54.307 20.663  1.00 79.60  ? 258 LEU A O   1 
ATOM   1874  C CB  . LEU A 1 258 ? 13.971  -51.454 20.272  1.00 81.31  ? 258 LEU A CB  1 
ATOM   1875  C CG  . LEU A 1 258 ? 14.579  -50.698 19.090  1.00 78.38  ? 258 LEU A CG  1 
ATOM   1876  C CD1 . LEU A 1 258 ? 15.940  -50.130 19.454  1.00 75.76  ? 258 LEU A CD1 1 
ATOM   1877  C CD2 . LEU A 1 258 ? 14.682  -51.609 17.876  1.00 81.89  ? 258 LEU A CD2 1 
ATOM   1878  N N   . LYS A 1 259 ? 12.043  -52.792 22.312  1.00 84.46  ? 259 LYS A N   1 
ATOM   1879  C CA  . LYS A 1 259 ? 11.776  -53.813 23.322  1.00 86.92  ? 259 LYS A CA  1 
ATOM   1880  C C   . LYS A 1 259 ? 10.586  -54.680 22.930  1.00 85.02  ? 259 LYS A C   1 
ATOM   1881  O O   . LYS A 1 259 ? 10.607  -55.902 23.120  1.00 86.06  ? 259 LYS A O   1 
ATOM   1882  C CB  . LYS A 1 259 ? 11.535  -53.157 24.683  1.00 90.56  ? 259 LYS A CB  1 
ATOM   1883  C CG  . LYS A 1 259 ? 11.420  -54.139 25.840  1.00 91.82  ? 259 LYS A CG  1 
ATOM   1884  C CD  . LYS A 1 259 ? 11.203  -53.413 27.159  1.00 95.47  ? 259 LYS A CD  1 
ATOM   1885  C CE  . LYS A 1 259 ? 11.251  -54.378 28.334  1.00 94.03  ? 259 LYS A CE  1 
ATOM   1886  N NZ  . LYS A 1 259 ? 12.581  -55.039 28.465  1.00 95.69  ? 259 LYS A NZ  1 
ATOM   1887  N N   . CYS A 1 260 ? 9.542   -54.065 22.372  1.00 88.21  ? 260 CYS A N   1 
ATOM   1888  C CA  . CYS A 1 260 ? 8.394   -54.828 21.901  1.00 89.65  ? 260 CYS A CA  1 
ATOM   1889  C C   . CYS A 1 260 ? 8.686   -55.538 20.586  1.00 86.92  ? 260 CYS A C   1 
ATOM   1890  O O   . CYS A 1 260 ? 8.126   -56.609 20.328  1.00 94.85  ? 260 CYS A O   1 
ATOM   1891  C CB  . CYS A 1 260 ? 7.187   -53.907 21.738  1.00 86.92  ? 260 CYS A CB  1 
ATOM   1892  S SG  . CYS A 1 260 ? 7.336   -52.743 20.361  1.00 86.11  ? 260 CYS A SG  1 
ATOM   1893  N N   . SER A 1 261 ? 9.542   -54.953 19.743  1.00 82.21  ? 261 SER A N   1 
ATOM   1894  C CA  . SER A 1 261 ? 9.897   -55.595 18.482  1.00 80.82  ? 261 SER A CA  1 
ATOM   1895  C C   . SER A 1 261 ? 10.569  -56.939 18.713  1.00 91.71  ? 261 SER A C   1 
ATOM   1896  O O   . SER A 1 261 ? 10.411  -57.860 17.903  1.00 88.08  ? 261 SER A O   1 
ATOM   1897  C CB  . SER A 1 261 ? 10.809  -54.680 17.667  1.00 76.31  ? 261 SER A CB  1 
ATOM   1898  O OG  . SER A 1 261 ? 11.191  -55.294 16.451  1.00 75.65  ? 261 SER A OG  1 
ATOM   1899  N N   . ALA A 1 262 ? 11.331  -57.065 19.802  1.00 81.60  ? 262 ALA A N   1 
ATOM   1900  C CA  . ALA A 1 262 ? 11.972  -58.337 20.116  1.00 86.47  ? 262 ALA A CA  1 
ATOM   1901  C C   . ALA A 1 262 ? 10.945  -59.396 20.498  1.00 94.04  ? 262 ALA A C   1 
ATOM   1902  O O   . ALA A 1 262 ? 11.118  -60.578 20.181  1.00 98.82  ? 262 ALA A O   1 
ATOM   1903  C CB  . ALA A 1 262 ? 12.989  -58.147 21.242  1.00 85.92  ? 262 ALA A CB  1 
ATOM   1904  N N   . LEU A 1 263 ? 9.872   -58.990 21.182  1.00 93.98  ? 263 LEU A N   1 
ATOM   1905  C CA  . LEU A 1 263 ? 8.851   -59.947 21.600  1.00 97.58  ? 263 LEU A CA  1 
ATOM   1906  C C   . LEU A 1 263 ? 8.071   -60.494 20.410  1.00 104.69 ? 263 LEU A C   1 
ATOM   1907  O O   . LEU A 1 263 ? 7.761   -61.690 20.363  1.00 106.80 ? 263 LEU A O   1 
ATOM   1908  C CB  . LEU A 1 263 ? 7.905   -59.292 22.606  1.00 96.58  ? 263 LEU A CB  1 
ATOM   1909  C CG  . LEU A 1 263 ? 8.558   -58.711 23.861  1.00 94.43  ? 263 LEU A CG  1 
ATOM   1910  C CD1 . LEU A 1 263 ? 7.530   -57.996 24.725  1.00 92.12  ? 263 LEU A CD1 1 
ATOM   1911  C CD2 . LEU A 1 263 ? 9.264   -59.805 24.648  1.00 95.51  ? 263 LEU A CD2 1 
ATOM   1912  N N   . TYR A 1 264 ? 7.742   -59.636 19.441  1.00 122.71 ? 264 TYR A N   1 
ATOM   1913  C CA  . TYR A 1 264 ? 7.045   -60.101 18.246  1.00 121.92 ? 264 TYR A CA  1 
ATOM   1914  C C   . TYR A 1 264 ? 7.913   -61.056 17.437  1.00 122.39 ? 264 TYR A C   1 
ATOM   1915  O O   . TYR A 1 264 ? 7.418   -62.055 16.902  1.00 123.42 ? 264 TYR A O   1 
ATOM   1916  C CB  . TYR A 1 264 ? 6.600   -58.909 17.400  1.00 121.34 ? 264 TYR A CB  1 
ATOM   1917  C CG  . TYR A 1 264 ? 5.348   -58.235 17.921  1.00 122.31 ? 264 TYR A CG  1 
ATOM   1918  C CD1 . TYR A 1 264 ? 4.364   -58.967 18.579  1.00 123.62 ? 264 TYR A CD1 1 
ATOM   1919  C CD2 . TYR A 1 264 ? 5.154   -56.870 17.767  1.00 116.57 ? 264 TYR A CD2 1 
ATOM   1920  C CE1 . TYR A 1 264 ? 3.221   -58.356 19.062  1.00 120.25 ? 264 TYR A CE1 1 
ATOM   1921  C CE2 . TYR A 1 264 ? 4.013   -56.250 18.247  1.00 116.95 ? 264 TYR A CE2 1 
ATOM   1922  C CZ  . TYR A 1 264 ? 3.051   -56.999 18.893  1.00 117.60 ? 264 TYR A CZ  1 
ATOM   1923  O OH  . TYR A 1 264 ? 1.915   -56.389 19.372  1.00 116.90 ? 264 TYR A OH  1 
ATOM   1924  N N   . LEU A 1 265 ? 9.209   -60.757 17.320  1.00 107.68 ? 265 LEU A N   1 
ATOM   1925  C CA  . LEU A 1 265 ? 10.118  -61.680 16.648  1.00 105.17 ? 265 LEU A CA  1 
ATOM   1926  C C   . LEU A 1 265 ? 10.235  -62.986 17.421  1.00 103.84 ? 265 LEU A C   1 
ATOM   1927  O O   . LEU A 1 265 ? 10.296  -64.067 16.823  1.00 106.83 ? 265 LEU A O   1 
ATOM   1928  C CB  . LEU A 1 265 ? 11.491  -61.033 16.467  1.00 100.15 ? 265 LEU A CB  1 
ATOM   1929  C CG  . LEU A 1 265 ? 11.519  -59.826 15.526  1.00 93.31  ? 265 LEU A CG  1 
ATOM   1930  C CD1 . LEU A 1 265 ? 12.913  -59.228 15.457  1.00 93.60  ? 265 LEU A CD1 1 
ATOM   1931  C CD2 . LEU A 1 265 ? 11.034  -60.225 14.140  1.00 99.53  ? 265 LEU A CD2 1 
ATOM   1932  N N   . SER A 1 266 ? 10.278  -62.905 18.753  1.00 102.03 ? 266 SER A N   1 
ATOM   1933  C CA  . SER A 1 266 ? 10.214  -64.116 19.564  1.00 101.94 ? 266 SER A CA  1 
ATOM   1934  C C   . SER A 1 266 ? 8.915   -64.871 19.316  1.00 106.52 ? 266 SER A C   1 
ATOM   1935  O O   . SER A 1 266 ? 8.891   -66.106 19.343  1.00 109.97 ? 266 SER A O   1 
ATOM   1936  C CB  . SER A 1 266 ? 10.355  -63.766 21.044  1.00 100.06 ? 266 SER A CB  1 
ATOM   1937  O OG  . SER A 1 266 ? 10.169  -64.913 21.854  1.00 99.28  ? 266 SER A OG  1 
ATOM   1938  N N   . GLN A 1 267 ? 7.822   -64.140 19.077  1.00 108.01 ? 267 GLN A N   1 
ATOM   1939  C CA  . GLN A 1 267 ? 6.563   -64.779 18.707  1.00 109.16 ? 267 GLN A CA  1 
ATOM   1940  C C   . GLN A 1 267 ? 6.649   -65.423 17.330  1.00 114.78 ? 267 GLN A C   1 
ATOM   1941  O O   . GLN A 1 267 ? 6.022   -66.460 17.091  1.00 116.23 ? 267 GLN A O   1 
ATOM   1942  C CB  . GLN A 1 267 ? 5.426   -63.755 18.744  1.00 107.64 ? 267 GLN A CB  1 
ATOM   1943  C CG  . GLN A 1 267 ? 4.035   -64.344 18.598  1.00 106.39 ? 267 GLN A CG  1 
ATOM   1944  C CD  . GLN A 1 267 ? 2.962   -63.277 18.498  1.00 110.85 ? 267 GLN A CD  1 
ATOM   1945  O OE1 . GLN A 1 267 ? 3.206   -62.180 17.994  1.00 114.05 ? 267 GLN A OE1 1 
ATOM   1946  N NE2 . GLN A 1 267 ? 1.765   -63.593 18.979  1.00 108.97 ? 267 GLN A NE2 1 
ATOM   1947  N N   . PHE A 1 268 ? 7.418   -64.832 16.419  1.00 127.61 ? 268 PHE A N   1 
ATOM   1948  C CA  . PHE A 1 268 ? 7.665   -65.428 15.113  1.00 127.35 ? 268 PHE A CA  1 
ATOM   1949  C C   . PHE A 1 268 ? 8.823   -66.412 15.131  1.00 129.85 ? 268 PHE A C   1 
ATOM   1950  O O   . PHE A 1 268 ? 9.109   -67.032 14.102  1.00 133.25 ? 268 PHE A O   1 
ATOM   1951  C CB  . PHE A 1 268 ? 7.937   -64.342 14.069  1.00 126.47 ? 268 PHE A CB  1 
ATOM   1952  C CG  . PHE A 1 268 ? 6.855   -63.307 13.972  1.00 125.98 ? 268 PHE A CG  1 
ATOM   1953  C CD1 . PHE A 1 268 ? 5.537   -63.624 14.264  1.00 129.33 ? 268 PHE A CD1 1 
ATOM   1954  C CD2 . PHE A 1 268 ? 7.154   -62.017 13.572  1.00 125.92 ? 268 PHE A CD2 1 
ATOM   1955  C CE1 . PHE A 1 268 ? 4.543   -62.669 14.170  1.00 128.85 ? 268 PHE A CE1 1 
ATOM   1956  C CE2 . PHE A 1 268 ? 6.168   -61.061 13.474  1.00 124.96 ? 268 PHE A CE2 1 
ATOM   1957  C CZ  . PHE A 1 268 ? 4.862   -61.385 13.773  1.00 129.75 ? 268 PHE A CZ  1 
ATOM   1958  N N   . ARG A 1 269 ? 9.490   -66.569 16.270  1.00 117.34 ? 269 ARG A N   1 
ATOM   1959  C CA  . ARG A 1 269 ? 10.504  -67.597 16.442  1.00 118.52 ? 269 ARG A CA  1 
ATOM   1960  C C   . ARG A 1 269 ? 9.958   -68.826 17.152  1.00 123.20 ? 269 ARG A C   1 
ATOM   1961  O O   . ARG A 1 269 ? 10.468  -69.930 16.943  1.00 123.54 ? 269 ARG A O   1 
ATOM   1962  C CB  . ARG A 1 269 ? 11.705  -67.039 17.219  1.00 113.49 ? 269 ARG A CB  1 
ATOM   1963  C CG  . ARG A 1 269 ? 13.044  -67.648 16.825  1.00 106.98 ? 269 ARG A CG  1 
ATOM   1964  C CD  . ARG A 1 269 ? 13.229  -67.643 15.314  1.00 105.28 ? 269 ARG A CD  1 
ATOM   1965  N NE  . ARG A 1 269 ? 14.388  -66.863 14.890  1.00 102.78 ? 269 ARG A NE  1 
ATOM   1966  C CZ  . ARG A 1 269 ? 14.970  -66.987 13.701  1.00 107.13 ? 269 ARG A CZ  1 
ATOM   1967  N NH1 . ARG A 1 269 ? 14.502  -67.866 12.826  1.00 110.54 ? 269 ARG A NH1 1 
ATOM   1968  N NH2 . ARG A 1 269 ? 16.022  -66.244 13.388  1.00 108.26 ? 269 ARG A NH2 1 
ATOM   1969  N N   . GLU A 1 270 ? 8.939   -68.650 17.995  1.00 132.27 ? 270 GLU A N   1 
ATOM   1970  C CA  . GLU A 1 270 ? 8.177   -69.786 18.502  1.00 134.31 ? 270 GLU A CA  1 
ATOM   1971  C C   . GLU A 1 270 ? 7.266   -70.352 17.420  1.00 133.74 ? 270 GLU A C   1 
ATOM   1972  O O   . GLU A 1 270 ? 7.349   -71.538 17.078  1.00 135.58 ? 270 GLU A O   1 
ATOM   1973  C CB  . GLU A 1 270 ? 7.369   -69.368 19.732  1.00 134.76 ? 270 GLU A CB  1 
ATOM   1974  N N   . THR A 1 271 ? 6.389   -69.515 16.867  1.00 122.53 ? 271 THR A N   1 
ATOM   1975  C CA  . THR A 1 271 ? 5.483   -69.919 15.800  1.00 122.61 ? 271 THR A CA  1 
ATOM   1976  C C   . THR A 1 271 ? 6.084   -69.550 14.451  1.00 125.93 ? 271 THR A C   1 
ATOM   1977  O O   . THR A 1 271 ? 6.537   -68.415 14.258  1.00 125.03 ? 271 THR A O   1 
ATOM   1978  C CB  . THR A 1 271 ? 4.116   -69.254 15.963  1.00 116.24 ? 271 THR A CB  1 
ATOM   1979  O OG1 . THR A 1 271 ? 4.142   -67.957 15.356  1.00 115.25 ? 271 THR A OG1 1 
ATOM   1980  C CG2 . THR A 1 271 ? 3.764   -69.111 17.435  1.00 113.37 ? 271 THR A CG2 1 
ATOM   1981  N N   . SER A 1 272 ? 6.053   -70.506 13.513  1.00 128.84 ? 272 SER A N   1 
ATOM   1982  C CA  . SER A 1 272 ? 6.577   -70.377 12.156  1.00 127.31 ? 272 SER A CA  1 
ATOM   1983  C C   . SER A 1 272 ? 7.912   -69.642 12.146  1.00 130.91 ? 272 SER A C   1 
ATOM   1984  O O   . SER A 1 272 ? 7.964   -68.463 11.773  1.00 129.02 ? 272 SER A O   1 
ATOM   1985  C CB  . SER A 1 272 ? 5.570   -69.655 11.258  1.00 118.40 ? 272 SER A CB  1 
ATOM   1986  O OG  . SER A 1 272 ? 5.363   -68.322 11.693  1.00 112.24 ? 272 SER A OG  1 
ATOM   1987  N N   . PRO A 1 273 ? 9.008   -70.295 12.547  1.00 136.24 ? 273 PRO A N   1 
ATOM   1988  C CA  . PRO A 1 273 ? 10.306  -69.605 12.564  1.00 133.94 ? 273 PRO A CA  1 
ATOM   1989  C C   . PRO A 1 273 ? 10.931  -69.452 11.191  1.00 130.94 ? 273 PRO A C   1 
ATOM   1990  O O   . PRO A 1 273 ? 11.834  -68.620 11.026  1.00 127.41 ? 273 PRO A O   1 
ATOM   1991  C CB  . PRO A 1 273 ? 11.155  -70.503 13.470  1.00 137.95 ? 273 PRO A CB  1 
ATOM   1992  C CG  . PRO A 1 273 ? 10.612  -71.870 13.207  1.00 144.69 ? 273 PRO A CG  1 
ATOM   1993  C CD  . PRO A 1 273 ? 9.119   -71.687 13.018  1.00 140.86 ? 273 PRO A CD  1 
ATOM   1994  N N   . HIS A 1 274 ? 10.479  -70.230 10.209  1.00 143.37 ? 274 HIS A N   1 
ATOM   1995  C CA  . HIS A 1 274 ? 10.996  -70.129 8.853   1.00 142.71 ? 274 HIS A CA  1 
ATOM   1996  C C   . HIS A 1 274 ? 10.651  -68.794 8.204   1.00 139.98 ? 274 HIS A C   1 
ATOM   1997  O O   . HIS A 1 274 ? 11.331  -68.383 7.260   1.00 138.70 ? 274 HIS A O   1 
ATOM   1998  C CB  . HIS A 1 274 ? 10.444  -71.286 8.024   1.00 144.10 ? 274 HIS A CB  1 
ATOM   1999  C CG  . HIS A 1 274 ? 9.021   -71.616 8.344   1.00 146.98 ? 274 HIS A CG  1 
ATOM   2000  N ND1 . HIS A 1 274 ? 8.670   -72.578 9.266   1.00 148.64 ? 274 HIS A ND1 1 
ATOM   2001  C CD2 . HIS A 1 274 ? 7.860   -71.089 7.890   1.00 148.47 ? 274 HIS A CD2 1 
ATOM   2002  C CE1 . HIS A 1 274 ? 7.354   -72.640 9.355   1.00 150.20 ? 274 HIS A CE1 1 
ATOM   2003  N NE2 . HIS A 1 274 ? 6.838   -71.747 8.530   1.00 149.41 ? 274 HIS A NE2 1 
ATOM   2004  N N   . ILE A 1 275 ? 9.629   -68.096 8.701   1.00 128.24 ? 275 ILE A N   1 
ATOM   2005  C CA  . ILE A 1 275 ? 9.343   -66.753 8.214   1.00 123.05 ? 275 ILE A CA  1 
ATOM   2006  C C   . ILE A 1 275 ? 10.428  -65.772 8.632   1.00 115.74 ? 275 ILE A C   1 
ATOM   2007  O O   . ILE A 1 275 ? 10.581  -64.714 8.009   1.00 109.83 ? 275 ILE A O   1 
ATOM   2008  C CB  . ILE A 1 275 ? 7.961   -66.275 8.702   1.00 118.79 ? 275 ILE A CB  1 
ATOM   2009  C CG1 . ILE A 1 275 ? 8.043   -65.787 10.148  1.00 115.04 ? 275 ILE A CG1 1 
ATOM   2010  C CG2 . ILE A 1 275 ? 6.944   -67.402 8.595   1.00 121.47 ? 275 ILE A CG2 1 
ATOM   2011  C CD1 . ILE A 1 275 ? 6.896   -64.895 10.558  1.00 111.72 ? 275 ILE A CD1 1 
ATOM   2012  N N   . LEU A 1 276 ? 11.187  -66.095 9.674   1.00 115.66 ? 276 LEU A N   1 
ATOM   2013  C CA  . LEU A 1 276 ? 12.301  -65.267 10.106  1.00 111.33 ? 276 LEU A CA  1 
ATOM   2014  C C   . LEU A 1 276 ? 13.571  -65.735 9.416   1.00 107.93 ? 276 LEU A C   1 
ATOM   2015  O O   . LEU A 1 276 ? 13.802  -66.939 9.262   1.00 109.63 ? 276 LEU A O   1 
ATOM   2016  C CB  . LEU A 1 276 ? 12.477  -65.327 11.626  1.00 112.72 ? 276 LEU A CB  1 
ATOM   2017  C CG  . LEU A 1 276 ? 11.428  -64.630 12.498  1.00 112.32 ? 276 LEU A CG  1 
ATOM   2018  C CD1 . LEU A 1 276 ? 12.008  -64.286 13.865  1.00 109.26 ? 276 LEU A CD1 1 
ATOM   2019  C CD2 . LEU A 1 276 ? 10.886  -63.378 11.819  1.00 115.09 ? 276 LEU A CD2 1 
ATOM   2020  N N   . ALA A 1 277 ? 14.388  -64.776 8.990   1.00 105.95 ? 277 ALA A N   1 
ATOM   2021  C CA  . ALA A 1 277 ? 15.660  -65.114 8.370   1.00 103.22 ? 277 ALA A CA  1 
ATOM   2022  C C   . ALA A 1 277 ? 16.550  -65.834 9.374   1.00 103.52 ? 277 ALA A C   1 
ATOM   2023  O O   . ALA A 1 277 ? 16.778  -65.347 10.485  1.00 103.64 ? 277 ALA A O   1 
ATOM   2024  C CB  . ALA A 1 277 ? 16.347  -63.850 7.857   1.00 106.86 ? 277 ALA A CB  1 
ATOM   2025  N N   . SER A 1 278 ? 17.039  -67.015 8.983   1.00 103.24 ? 278 SER A N   1 
ATOM   2026  C CA  . SER A 1 278 ? 17.933  -67.809 9.808   1.00 104.90 ? 278 SER A CA  1 
ATOM   2027  C C   . SER A 1 278 ? 19.029  -68.362 8.895   1.00 109.68 ? 278 SER A C   1 
ATOM   2028  O O   . SER A 1 278 ? 19.097  -69.554 8.602   1.00 113.78 ? 278 SER A O   1 
ATOM   2029  C CB  . SER A 1 278 ? 17.186  -68.930 10.535  1.00 100.62 ? 278 SER A CB  1 
ATOM   2030  O OG  . SER A 1 278 ? 16.161  -69.472 9.721   1.00 99.32  ? 278 SER A OG  1 
ATOM   2031  N N   . GLY A 1 279 ? 19.903  -67.471 8.435   1.00 109.51 ? 279 GLY A N   1 
ATOM   2032  C CA  . GLY A 1 279 ? 20.997  -67.864 7.573   1.00 113.42 ? 279 GLY A CA  1 
ATOM   2033  C C   . GLY A 1 279 ? 22.052  -68.639 8.330   1.00 120.39 ? 279 GLY A C   1 
ATOM   2034  O O   . GLY A 1 279 ? 22.300  -69.812 8.031   1.00 124.18 ? 279 GLY A O   1 
ATOM   2035  N N   . ASP A 1 280 ? 22.666  -67.992 9.322   1.00 133.64 ? 280 ASP A N   1 
ATOM   2036  C CA  . ASP A 1 280 ? 23.640  -68.630 10.208  1.00 135.62 ? 280 ASP A CA  1 
ATOM   2037  C C   . ASP A 1 280 ? 24.745  -69.315 9.404   1.00 137.11 ? 280 ASP A C   1 
ATOM   2038  O O   . ASP A 1 280 ? 25.031  -70.502 9.567   1.00 138.15 ? 280 ASP A O   1 
ATOM   2039  C CB  . ASP A 1 280 ? 22.947  -69.608 11.158  1.00 138.15 ? 280 ASP A CB  1 
ATOM   2040  C CG  . ASP A 1 280 ? 21.996  -68.910 12.116  1.00 137.80 ? 280 ASP A CG  1 
ATOM   2041  O OD1 . ASP A 1 280 ? 20.938  -68.428 11.659  1.00 136.75 ? 280 ASP A OD1 1 
ATOM   2042  O OD2 . ASP A 1 280 ? 22.306  -68.840 13.324  1.00 138.47 ? 280 ASP A OD2 1 
ATOM   2043  N N   . GLY A 1 281 ? 25.366  -68.541 8.520   1.00 121.04 ? 281 GLY A N   1 
ATOM   2044  C CA  . GLY A 1 281 ? 26.390  -69.071 7.639   1.00 111.56 ? 281 GLY A CA  1 
ATOM   2045  C C   . GLY A 1 281 ? 26.777  -68.030 6.607   1.00 105.98 ? 281 GLY A C   1 
ATOM   2046  O O   . GLY A 1 281 ? 26.489  -66.844 6.774   1.00 107.15 ? 281 GLY A O   1 
ATOM   2047  N N   . THR A 1 282 ? 27.430  -68.494 5.534   1.00 106.42 ? 282 THR A N   1 
ATOM   2048  C CA  . THR A 1 282 ? 27.874  -67.613 4.448   1.00 107.09 ? 282 THR A CA  1 
ATOM   2049  C C   . THR A 1 282 ? 27.823  -68.372 3.117   1.00 102.74 ? 282 THR A C   1 
ATOM   2050  O O   . THR A 1 282 ? 28.835  -68.711 2.506   1.00 100.46 ? 282 THR A O   1 
ATOM   2051  C CB  . THR A 1 282 ? 29.276  -67.054 4.709   1.00 106.80 ? 282 THR A CB  1 
ATOM   2052  O OG1 . THR A 1 282 ? 30.084  -68.053 5.344   1.00 110.20 ? 282 THR A OG1 1 
ATOM   2053  C CG2 . THR A 1 282 ? 29.214  -65.808 5.586   1.00 99.57  ? 282 THR A CG2 1 
ATOM   2054  N N   . ASN A 1 283 ? 26.605  -68.645 2.647   1.00 101.79 ? 283 ASN A N   1 
ATOM   2055  C CA  . ASN A 1 283 ? 26.398  -69.182 1.306   1.00 101.68 ? 283 ASN A CA  1 
ATOM   2056  C C   . ASN A 1 283 ? 25.735  -68.118 0.444   1.00 99.98  ? 283 ASN A C   1 
ATOM   2057  O O   . ASN A 1 283 ? 24.646  -68.340 -0.094  1.00 98.19  ? 283 ASN A O   1 
ATOM   2058  C CB  . ASN A 1 283 ? 25.538  -70.446 1.340   1.00 106.90 ? 283 ASN A CB  1 
ATOM   2059  C CG  . ASN A 1 283 ? 25.808  -71.301 2.560   1.00 112.64 ? 283 ASN A CG  1 
ATOM   2060  O OD1 . ASN A 1 283 ? 26.931  -71.344 3.066   1.00 106.11 ? 283 ASN A OD1 1 
ATOM   2061  N ND2 . ASN A 1 283 ? 24.779  -71.987 3.041   1.00 124.27 ? 283 ASN A ND2 1 
ATOM   2062  N N   . ARG A 1 284 ? 26.390  -66.962 0.321   1.00 101.42 ? 284 ARG A N   1 
ATOM   2063  C CA  . ARG A 1 284 ? 25.841  -65.698 -0.166  1.00 100.41 ? 284 ARG A CA  1 
ATOM   2064  C C   . ARG A 1 284 ? 24.831  -65.115 0.814   1.00 100.58 ? 284 ARG A C   1 
ATOM   2065  O O   . ARG A 1 284 ? 24.325  -64.010 0.580   1.00 96.64  ? 284 ARG A O   1 
ATOM   2066  C CB  . ARG A 1 284 ? 25.195  -65.809 -1.557  1.00 97.03  ? 284 ARG A CB  1 
ATOM   2067  C CG  . ARG A 1 284 ? 26.034  -65.221 -2.684  1.00 97.97  ? 284 ARG A CG  1 
ATOM   2068  C CD  . ARG A 1 284 ? 25.217  -65.082 -3.958  1.00 105.32 ? 284 ARG A CD  1 
ATOM   2069  N NE  . ARG A 1 284 ? 25.914  -64.304 -4.978  1.00 105.64 ? 284 ARG A NE  1 
ATOM   2070  C CZ  . ARG A 1 284 ? 25.505  -63.121 -5.423  1.00 103.48 ? 284 ARG A CZ  1 
ATOM   2071  N NH1 . ARG A 1 284 ? 24.393  -62.581 -4.942  1.00 99.68  ? 284 ARG A NH1 1 
ATOM   2072  N NH2 . ARG A 1 284 ? 26.199  -62.484 -6.357  1.00 101.53 ? 284 ARG A NH2 1 
ATOM   2073  N N   . LYS A 1 285 ? 24.520  -65.823 1.911   1.00 104.92 ? 285 LYS A N   1 
ATOM   2074  C CA  . LYS A 1 285 ? 23.648  -65.375 2.987   1.00 105.04 ? 285 LYS A CA  1 
ATOM   2075  C C   . LYS A 1 285 ? 24.489  -64.898 4.157   1.00 104.88 ? 285 LYS A C   1 
ATOM   2076  O O   . LYS A 1 285 ? 25.411  -65.612 4.574   1.00 108.95 ? 285 LYS A O   1 
ATOM   2077  C CB  . LYS A 1 285 ? 22.727  -66.506 3.437   1.00 108.52 ? 285 LYS A CB  1 
ATOM   2078  N N   . PRO A 1 286 ? 24.219  -63.718 4.707   1.00 95.60  ? 286 PRO A N   1 
ATOM   2079  C CA  . PRO A 1 286 ? 25.051  -63.197 5.798   1.00 96.74  ? 286 PRO A CA  1 
ATOM   2080  C C   . PRO A 1 286 ? 24.881  -64.004 7.077   1.00 96.80  ? 286 PRO A C   1 
ATOM   2081  O O   . PRO A 1 286 ? 24.048  -64.907 7.185   1.00 99.23  ? 286 PRO A O   1 
ATOM   2082  C CB  . PRO A 1 286 ? 24.547  -61.762 5.977   1.00 92.79  ? 286 PRO A CB  1 
ATOM   2083  C CG  . PRO A 1 286 ? 23.859  -61.430 4.688   1.00 94.26  ? 286 PRO A CG  1 
ATOM   2084  C CD  . PRO A 1 286 ? 23.256  -62.718 4.221   1.00 97.63  ? 286 PRO A CD  1 
ATOM   2085  N N   . THR A 1 287 ? 25.702  -63.654 8.066   1.00 94.51  ? 287 THR A N   1 
ATOM   2086  C CA  . THR A 1 287 ? 25.671  -64.302 9.375   1.00 94.19  ? 287 THR A CA  1 
ATOM   2087  C C   . THR A 1 287 ? 24.505  -63.737 10.172  1.00 90.20  ? 287 THR A C   1 
ATOM   2088  O O   . THR A 1 287 ? 24.589  -62.645 10.739  1.00 86.67  ? 287 THR A O   1 
ATOM   2089  C CB  . THR A 1 287 ? 26.988  -64.105 10.116  1.00 88.72  ? 287 THR A CB  1 
ATOM   2090  O OG1 . THR A 1 287 ? 27.577  -62.857 9.730   1.00 85.03  ? 287 THR A OG1 1 
ATOM   2091  C CG2 . THR A 1 287 ? 27.951  -65.244 9.809   1.00 90.69  ? 287 THR A CG2 1 
ATOM   2092  N N   . ILE A 1 288 ? 23.412  -64.484 10.214  1.00 99.72  ? 288 ILE A N   1 
ATOM   2093  C CA  . ILE A 1 288 ? 22.226  -64.093 10.963  1.00 99.62  ? 288 ILE A CA  1 
ATOM   2094  C C   . ILE A 1 288 ? 22.306  -64.734 12.340  1.00 104.54 ? 288 ILE A C   1 
ATOM   2095  O O   . ILE A 1 288 ? 22.524  -65.946 12.460  1.00 108.88 ? 288 ILE A O   1 
ATOM   2096  C CB  . ILE A 1 288 ? 20.948  -64.512 10.220  1.00 102.83 ? 288 ILE A CB  1 
ATOM   2097  C CG1 . ILE A 1 288 ? 20.737  -63.616 8.996   1.00 100.40 ? 288 ILE A CG1 1 
ATOM   2098  C CG2 . ILE A 1 288 ? 19.749  -64.467 11.147  1.00 104.76 ? 288 ILE A CG2 1 
ATOM   2099  C CD1 . ILE A 1 288 ? 19.909  -64.247 7.911   1.00 107.73 ? 288 ILE A CD1 1 
ATOM   2100  N N   . ILE A 1 289 ? 22.130  -63.926 13.382  1.00 103.46 ? 289 ILE A N   1 
ATOM   2101  C CA  . ILE A 1 289 ? 22.335  -64.406 14.743  1.00 105.23 ? 289 ILE A CA  1 
ATOM   2102  C C   . ILE A 1 289 ? 20.999  -64.477 15.469  1.00 112.24 ? 289 ILE A C   1 
ATOM   2103  O O   . ILE A 1 289 ? 20.864  -63.995 16.599  1.00 104.74 ? 289 ILE A O   1 
ATOM   2104  C CB  . ILE A 1 289 ? 23.329  -63.507 15.501  1.00 99.46  ? 289 ILE A CB  1 
ATOM   2105  C CG1 . ILE A 1 289 ? 24.382  -62.943 14.542  1.00 92.78  ? 289 ILE A CG1 1 
ATOM   2106  C CG2 . ILE A 1 289 ? 24.011  -64.287 16.615  1.00 97.64  ? 289 ILE A CG2 1 
ATOM   2107  C CD1 . ILE A 1 289 ? 25.349  -63.974 14.002  1.00 95.05  ? 289 ILE A CD1 1 
ATOM   2108  N N   . GLY A 1 290 ? 20.004  -65.084 14.826  1.00 152.04 ? 290 GLY A N   1 
ATOM   2109  C CA  . GLY A 1 290 ? 18.728  -65.327 15.468  1.00 153.48 ? 290 GLY A CA  1 
ATOM   2110  C C   . GLY A 1 290 ? 17.872  -64.089 15.638  1.00 151.83 ? 290 GLY A C   1 
ATOM   2111  O O   . GLY A 1 290 ? 18.390  -62.983 15.827  1.00 150.09 ? 290 GLY A O   1 
ATOM   2112  N N   . ASP A 1 291 ? 16.552  -64.272 15.573  1.00 117.00 ? 291 ASP A N   1 
ATOM   2113  C CA  . ASP A 1 291 ? 15.577  -63.201 15.765  1.00 104.34 ? 291 ASP A CA  1 
ATOM   2114  C C   . ASP A 1 291 ? 15.834  -62.045 14.796  1.00 99.00  ? 291 ASP A C   1 
ATOM   2115  O O   . ASP A 1 291 ? 16.045  -60.897 15.190  1.00 91.82  ? 291 ASP A O   1 
ATOM   2116  C CB  . ASP A 1 291 ? 15.583  -62.721 17.221  1.00 100.73 ? 291 ASP A CB  1 
ATOM   2117  C CG  . ASP A 1 291 ? 14.446  -63.311 18.030  1.00 104.34 ? 291 ASP A CG  1 
ATOM   2118  O OD1 . ASP A 1 291 ? 13.880  -64.335 17.593  1.00 106.96 ? 291 ASP A OD1 1 
ATOM   2119  O OD2 . ASP A 1 291 ? 14.128  -62.763 19.107  1.00 101.39 ? 291 ASP A OD2 1 
ATOM   2120  N N   . VAL A 1 292 ? 15.819  -62.378 13.508  1.00 102.37 ? 292 VAL A N   1 
ATOM   2121  C CA  . VAL A 1 292 ? 16.038  -61.419 12.433  1.00 102.06 ? 292 VAL A CA  1 
ATOM   2122  C C   . VAL A 1 292 ? 14.937  -61.604 11.403  1.00 108.61 ? 292 VAL A C   1 
ATOM   2123  O O   . VAL A 1 292 ? 14.694  -62.726 10.945  1.00 109.70 ? 292 VAL A O   1 
ATOM   2124  C CB  . VAL A 1 292 ? 17.420  -61.595 11.774  1.00 102.80 ? 292 VAL A CB  1 
ATOM   2125  C CG1 . VAL A 1 292 ? 17.643  -60.524 10.712  1.00 99.77  ? 292 VAL A CG1 1 
ATOM   2126  C CG2 . VAL A 1 292 ? 18.520  -61.558 12.816  1.00 103.15 ? 292 VAL A CG2 1 
ATOM   2127  N N   . TYR A 1 293 ? 14.277  -60.512 11.034  1.00 123.18 ? 293 TYR A N   1 
ATOM   2128  C CA  . TYR A 1 293 ? 13.321  -60.516 9.936   1.00 123.90 ? 293 TYR A CA  1 
ATOM   2129  C C   . TYR A 1 293 ? 13.933  -59.768 8.763   1.00 120.37 ? 293 TYR A C   1 
ATOM   2130  O O   . TYR A 1 293 ? 14.206  -58.567 8.863   1.00 119.21 ? 293 TYR A O   1 
ATOM   2131  C CB  . TYR A 1 293 ? 11.989  -59.883 10.338  1.00 123.84 ? 293 TYR A CB  1 
ATOM   2132  C CG  . TYR A 1 293 ? 11.068  -59.668 9.159   1.00 126.27 ? 293 TYR A CG  1 
ATOM   2133  C CD1 . TYR A 1 293 ? 10.929  -58.416 8.577   1.00 123.50 ? 293 TYR A CD1 1 
ATOM   2134  C CD2 . TYR A 1 293 ? 10.351  -60.727 8.616   1.00 126.43 ? 293 TYR A CD2 1 
ATOM   2135  C CE1 . TYR A 1 293 ? 10.093  -58.220 7.495   1.00 120.09 ? 293 TYR A CE1 1 
ATOM   2136  C CE2 . TYR A 1 293 ? 9.513   -60.541 7.534   1.00 123.81 ? 293 TYR A CE2 1 
ATOM   2137  C CZ  . TYR A 1 293 ? 9.388   -59.286 6.978   1.00 120.03 ? 293 TYR A CZ  1 
ATOM   2138  O OH  . TYR A 1 293 ? 8.554   -59.096 5.901   1.00 118.63 ? 293 TYR A OH  1 
ATOM   2139  N N   . ILE A 1 294 ? 14.144  -60.475 7.659   1.00 136.25 ? 294 ILE A N   1 
ATOM   2140  C CA  . ILE A 1 294 ? 14.748  -59.909 6.461   1.00 135.55 ? 294 ILE A CA  1 
ATOM   2141  C C   . ILE A 1 294 ? 13.705  -59.913 5.352   1.00 135.31 ? 294 ILE A C   1 
ATOM   2142  O O   . ILE A 1 294 ? 13.160  -60.968 5.004   1.00 137.08 ? 294 ILE A O   1 
ATOM   2143  C CB  . ILE A 1 294 ? 16.007  -60.685 6.049   1.00 139.42 ? 294 ILE A CB  1 
ATOM   2144  C CG1 . ILE A 1 294 ? 17.161  -60.366 7.004   1.00 137.69 ? 294 ILE A CG1 1 
ATOM   2145  C CG2 . ILE A 1 294 ? 16.385  -60.368 4.613   1.00 143.05 ? 294 ILE A CG2 1 
ATOM   2146  C CD1 . ILE A 1 294 ? 18.452  -61.075 6.669   1.00 138.35 ? 294 ILE A CD1 1 
ATOM   2147  N N   . HIS A 1 295 ? 13.430  -58.735 4.801   1.00 116.06 ? 295 HIS A N   1 
ATOM   2148  C CA  . HIS A 1 295 ? 12.507  -58.623 3.685   1.00 113.92 ? 295 HIS A CA  1 
ATOM   2149  C C   . HIS A 1 295 ? 13.154  -59.161 2.407   1.00 113.41 ? 295 HIS A C   1 
ATOM   2150  O O   . HIS A 1 295 ? 14.368  -59.048 2.222   1.00 115.21 ? 295 HIS A O   1 
ATOM   2151  C CB  . HIS A 1 295 ? 12.083  -57.170 3.490   1.00 111.65 ? 295 HIS A CB  1 
ATOM   2152  C CG  . HIS A 1 295 ? 10.900  -57.003 2.589   1.00 111.76 ? 295 HIS A CG  1 
ATOM   2153  N ND1 . HIS A 1 295 ? 11.010  -56.968 1.217   1.00 111.29 ? 295 HIS A ND1 1 
ATOM   2154  C CD2 . HIS A 1 295 ? 9.579   -56.879 2.862   1.00 114.75 ? 295 HIS A CD2 1 
ATOM   2155  C CE1 . HIS A 1 295 ? 9.811   -56.826 0.683   1.00 116.86 ? 295 HIS A CE1 1 
ATOM   2156  N NE2 . HIS A 1 295 ? 8.925   -56.765 1.660   1.00 115.96 ? 295 HIS A NE2 1 
ATOM   2157  N N   . PRO A 1 296 ? 12.368  -59.775 1.517   1.00 112.11 ? 296 PRO A N   1 
ATOM   2158  C CA  . PRO A 1 296 ? 12.949  -60.282 0.262   1.00 111.24 ? 296 PRO A CA  1 
ATOM   2159  C C   . PRO A 1 296 ? 13.479  -59.196 -0.662  1.00 108.46 ? 296 PRO A C   1 
ATOM   2160  O O   . PRO A 1 296 ? 14.276  -59.509 -1.556  1.00 111.70 ? 296 PRO A O   1 
ATOM   2161  C CB  . PRO A 1 296 ? 11.781  -61.041 -0.384  1.00 123.98 ? 296 PRO A CB  1 
ATOM   2162  C CG  . PRO A 1 296 ? 10.551  -60.482 0.262   1.00 121.65 ? 296 PRO A CG  1 
ATOM   2163  C CD  . PRO A 1 296 ? 10.960  -60.176 1.669   1.00 116.05 ? 296 PRO A CD  1 
ATOM   2164  N N   . SER A 1 297 ? 13.068  -57.943 -0.489  1.00 106.56 ? 297 SER A N   1 
ATOM   2165  C CA  . SER A 1 297 ? 13.493  -56.853 -1.356  1.00 114.30 ? 297 SER A CA  1 
ATOM   2166  C C   . SER A 1 297 ? 14.790  -56.191 -0.900  1.00 106.96 ? 297 SER A C   1 
ATOM   2167  O O   . SER A 1 297 ? 15.179  -55.168 -1.470  1.00 107.66 ? 297 SER A O   1 
ATOM   2168  C CB  . SER A 1 297 ? 12.388  -55.800 -1.462  1.00 118.82 ? 297 SER A CB  1 
ATOM   2169  O OG  . SER A 1 297 ? 12.736  -54.788 -2.391  1.00 122.80 ? 297 SER A OG  1 
ATOM   2170  N N   . VAL A 1 298 ? 15.459  -56.736 0.112   1.00 103.92 ? 298 VAL A N   1 
ATOM   2171  C CA  . VAL A 1 298 ? 16.685  -56.123 0.605   1.00 97.20  ? 298 VAL A CA  1 
ATOM   2172  C C   . VAL A 1 298 ? 17.872  -56.578 -0.237  1.00 98.24  ? 298 VAL A C   1 
ATOM   2173  O O   . VAL A 1 298 ? 17.823  -57.587 -0.944  1.00 101.54 ? 298 VAL A O   1 
ATOM   2174  C CB  . VAL A 1 298 ? 16.907  -56.447 2.091   1.00 98.32  ? 298 VAL A CB  1 
ATOM   2175  C CG1 . VAL A 1 298 ? 15.627  -56.246 2.868   1.00 104.37 ? 298 VAL A CG1 1 
ATOM   2176  C CG2 . VAL A 1 298 ? 17.404  -57.866 2.247   1.00 101.10 ? 298 VAL A CG2 1 
ATOM   2177  N N   . LYS A 1 299 ? 18.957  -55.812 -0.154  1.00 98.58  ? 299 LYS A N   1 
ATOM   2178  C CA  . LYS A 1 299 ? 20.224  -56.150 -0.792  1.00 95.01  ? 299 LYS A CA  1 
ATOM   2179  C C   . LYS A 1 299 ? 21.268  -56.349 0.297   1.00 93.06  ? 299 LYS A C   1 
ATOM   2180  O O   . LYS A 1 299 ? 21.480  -55.459 1.129   1.00 90.98  ? 299 LYS A O   1 
ATOM   2181  C CB  . LYS A 1 299 ? 20.657  -55.059 -1.772  1.00 94.98  ? 299 LYS A CB  1 
ATOM   2182  C CG  . LYS A 1 299 ? 22.025  -55.290 -2.377  1.00 101.97 ? 299 LYS A CG  1 
ATOM   2183  C CD  . LYS A 1 299 ? 22.370  -54.204 -3.380  1.00 111.99 ? 299 LYS A CD  1 
ATOM   2184  C CE  . LYS A 1 299 ? 21.527  -54.318 -4.640  1.00 121.35 ? 299 LYS A CE  1 
ATOM   2185  N NZ  . LYS A 1 299 ? 21.827  -55.561 -5.403  1.00 121.98 ? 299 LYS A NZ  1 
ATOM   2186  N N   . LEU A 1 300 ? 21.912  -57.514 0.296   1.00 100.80 ? 300 LEU A N   1 
ATOM   2187  C CA  . LEU A 1 300 ? 22.799  -57.914 1.377   1.00 100.39 ? 300 LEU A CA  1 
ATOM   2188  C C   . LEU A 1 300 ? 24.177  -58.282 0.840   1.00 102.22 ? 300 LEU A C   1 
ATOM   2189  O O   . LEU A 1 300 ? 24.362  -58.537 -0.355  1.00 103.43 ? 300 LEU A O   1 
ATOM   2190  C CB  . LEU A 1 300 ? 22.210  -59.097 2.158   1.00 99.19  ? 300 LEU A CB  1 
ATOM   2191  C CG  . LEU A 1 300 ? 20.819  -58.844 2.751   1.00 97.70  ? 300 LEU A CG  1 
ATOM   2192  C CD1 . LEU A 1 300 ? 20.261  -60.080 3.449   1.00 103.99 ? 300 LEU A CD1 1 
ATOM   2193  C CD2 . LEU A 1 300 ? 20.837  -57.651 3.694   1.00 95.68  ? 300 LEU A CD2 1 
ATOM   2194  N N   . HIS A 1 301 ? 25.148  -58.305 1.754   1.00 95.73  ? 301 HIS A N   1 
ATOM   2195  C CA  . HIS A 1 301 ? 26.508  -58.745 1.497   1.00 93.32  ? 301 HIS A CA  1 
ATOM   2196  C C   . HIS A 1 301 ? 26.893  -59.812 2.512   1.00 93.00  ? 301 HIS A C   1 
ATOM   2197  O O   . HIS A 1 301 ? 26.623  -59.657 3.708   1.00 91.22  ? 301 HIS A O   1 
ATOM   2198  C CB  . HIS A 1 301 ? 27.495  -57.574 1.571   1.00 90.19  ? 301 HIS A CB  1 
ATOM   2199  C CG  . HIS A 1 301 ? 28.822  -57.862 0.941   1.00 88.87  ? 301 HIS A CG  1 
ATOM   2200  N ND1 . HIS A 1 301 ? 29.794  -58.617 1.561   1.00 88.39  ? 301 HIS A ND1 1 
ATOM   2201  C CD2 . HIS A 1 301 ? 29.335  -57.499 -0.258  1.00 88.87  ? 301 HIS A CD2 1 
ATOM   2202  C CE1 . HIS A 1 301 ? 30.849  -58.706 0.771   1.00 91.17  ? 301 HIS A CE1 1 
ATOM   2203  N NE2 . HIS A 1 301 ? 30.597  -58.036 -0.339  1.00 90.71  ? 301 HIS A NE2 1 
ATOM   2204  N N   . PRO A 1 302 ? 27.523  -60.904 2.069   1.00 100.86 ? 302 PRO A N   1 
ATOM   2205  C CA  . PRO A 1 302 ? 27.791  -62.025 2.987   1.00 103.12 ? 302 PRO A CA  1 
ATOM   2206  C C   . PRO A 1 302 ? 28.760  -61.698 4.116   1.00 103.53 ? 302 PRO A C   1 
ATOM   2207  O O   . PRO A 1 302 ? 28.848  -62.482 5.072   1.00 104.45 ? 302 PRO A O   1 
ATOM   2208  C CB  . PRO A 1 302 ? 28.366  -63.109 2.062   1.00 104.05 ? 302 PRO A CB  1 
ATOM   2209  C CG  . PRO A 1 302 ? 27.943  -62.708 0.676   1.00 103.19 ? 302 PRO A CG  1 
ATOM   2210  C CD  . PRO A 1 302 ? 27.921  -61.213 0.686   1.00 101.06 ? 302 PRO A CD  1 
ATOM   2211  N N   . THR A 1 303 ? 29.483  -60.583 4.050   1.00 94.46  ? 303 THR A N   1 
ATOM   2212  C CA  . THR A 1 303 ? 30.450  -60.242 5.085   1.00 83.81  ? 303 THR A CA  1 
ATOM   2213  C C   . THR A 1 303 ? 29.840  -59.496 6.265   1.00 84.71  ? 303 THR A C   1 
ATOM   2214  O O   . THR A 1 303 ? 30.544  -59.256 7.251   1.00 85.61  ? 303 THR A O   1 
ATOM   2215  C CB  . THR A 1 303 ? 31.586  -59.400 4.497   1.00 80.70  ? 303 THR A CB  1 
ATOM   2216  O OG1 . THR A 1 303 ? 31.042  -58.229 3.876   1.00 80.21  ? 303 THR A OG1 1 
ATOM   2217  C CG2 . THR A 1 303 ? 32.367  -60.207 3.471   1.00 83.83  ? 303 THR A CG2 1 
ATOM   2218  N N   . ALA A 1 304 ? 28.566  -59.127 6.194   1.00 85.57  ? 304 ALA A N   1 
ATOM   2219  C CA  . ALA A 1 304 ? 27.911  -58.396 7.269   1.00 80.88  ? 304 ALA A CA  1 
ATOM   2220  C C   . ALA A 1 304 ? 27.372  -59.353 8.323   1.00 78.31  ? 304 ALA A C   1 
ATOM   2221  O O   . ALA A 1 304 ? 26.896  -60.447 8.005   1.00 82.45  ? 304 ALA A O   1 
ATOM   2222  C CB  . ALA A 1 304 ? 26.775  -57.533 6.719   1.00 79.21  ? 304 ALA A CB  1 
ATOM   2223  N N   . LYS A 1 305 ? 27.456  -58.935 9.585   1.00 77.20  ? 305 LYS A N   1 
ATOM   2224  C CA  . LYS A 1 305 ? 26.939  -59.702 10.715  1.00 74.72  ? 305 LYS A CA  1 
ATOM   2225  C C   . LYS A 1 305 ? 25.665  -59.034 11.223  1.00 77.91  ? 305 LYS A C   1 
ATOM   2226  O O   . LYS A 1 305 ? 25.716  -57.950 11.817  1.00 69.19  ? 305 LYS A O   1 
ATOM   2227  C CB  . LYS A 1 305 ? 27.987  -59.820 11.819  1.00 73.31  ? 305 LYS A CB  1 
ATOM   2228  C CG  . LYS A 1 305 ? 27.547  -60.675 12.989  1.00 76.94  ? 305 LYS A CG  1 
ATOM   2229  C CD  . LYS A 1 305 ? 28.653  -60.821 14.017  1.00 73.76  ? 305 LYS A CD  1 
ATOM   2230  C CE  . LYS A 1 305 ? 29.659  -61.869 13.579  1.00 75.12  ? 305 LYS A CE  1 
ATOM   2231  N NZ  . LYS A 1 305 ? 30.689  -62.143 14.618  1.00 77.16  ? 305 LYS A NZ  1 
ATOM   2232  N N   . ILE A 1 306 ? 24.529  -59.684 10.978  1.00 78.29  ? 306 ILE A N   1 
ATOM   2233  C CA  . ILE A 1 306 ? 23.214  -59.195 11.381  1.00 77.42  ? 306 ILE A CA  1 
ATOM   2234  C C   . ILE A 1 306 ? 22.864  -59.877 12.700  1.00 81.96  ? 306 ILE A C   1 
ATOM   2235  O O   . ILE A 1 306 ? 22.417  -61.026 12.718  1.00 84.18  ? 306 ILE A O   1 
ATOM   2236  C CB  . ILE A 1 306 ? 22.159  -59.474 10.308  1.00 80.48  ? 306 ILE A CB  1 
ATOM   2237  C CG1 . ILE A 1 306 ? 22.734  -59.232 8.911   1.00 81.12  ? 306 ILE A CG1 1 
ATOM   2238  C CG2 . ILE A 1 306 ? 20.943  -58.596 10.506  1.00 77.69  ? 306 ILE A CG2 1 
ATOM   2239  C CD1 . ILE A 1 306 ? 23.104  -57.792 8.647   1.00 76.48  ? 306 ILE A CD1 1 
ATOM   2240  N N   . GLY A 1 307 ? 23.074  -59.175 13.810  1.00 82.84  ? 307 GLY A N   1 
ATOM   2241  C CA  . GLY A 1 307 ? 22.895  -59.746 15.125  1.00 84.68  ? 307 GLY A CA  1 
ATOM   2242  C C   . GLY A 1 307 ? 21.447  -59.940 15.529  1.00 87.56  ? 307 GLY A C   1 
ATOM   2243  O O   . GLY A 1 307 ? 20.548  -60.041 14.690  1.00 90.73  ? 307 GLY A O   1 
ATOM   2244  N N   . PRO A 1 308 ? 21.197  -59.992 16.835  1.00 85.95  ? 308 PRO A N   1 
ATOM   2245  C CA  . PRO A 1 308 ? 19.844  -60.275 17.320  1.00 91.89  ? 308 PRO A CA  1 
ATOM   2246  C C   . PRO A 1 308 ? 18.956  -59.042 17.330  1.00 89.94  ? 308 PRO A C   1 
ATOM   2247  O O   . PRO A 1 308 ? 19.421  -57.905 17.441  1.00 87.82  ? 308 PRO A O   1 
ATOM   2248  C CB  . PRO A 1 308 ? 20.087  -60.782 18.746  1.00 89.95  ? 308 PRO A CB  1 
ATOM   2249  C CG  . PRO A 1 308 ? 21.318  -60.056 19.172  1.00 88.34  ? 308 PRO A CG  1 
ATOM   2250  C CD  . PRO A 1 308 ? 22.173  -59.913 17.936  1.00 86.39  ? 308 PRO A CD  1 
ATOM   2251  N N   . ASN A 1 309 ? 17.653  -59.296 17.206  1.00 84.43  ? 309 ASN A N   1 
ATOM   2252  C CA  . ASN A 1 309 ? 16.617  -58.275 17.345  1.00 74.83  ? 309 ASN A CA  1 
ATOM   2253  C C   . ASN A 1 309 ? 16.829  -57.136 16.346  1.00 73.98  ? 309 ASN A C   1 
ATOM   2254  O O   . ASN A 1 309 ? 17.047  -55.980 16.708  1.00 75.23  ? 309 ASN A O   1 
ATOM   2255  C CB  . ASN A 1 309 ? 16.557  -57.750 18.784  1.00 76.59  ? 309 ASN A CB  1 
ATOM   2256  C CG  . ASN A 1 309 ? 15.420  -56.777 19.001  1.00 79.40  ? 309 ASN A CG  1 
ATOM   2257  O OD1 . ASN A 1 309 ? 14.475  -56.726 18.214  1.00 80.34  ? 309 ASN A OD1 1 
ATOM   2258  N ND2 . ASN A 1 309 ? 15.504  -55.996 20.071  1.00 80.43  ? 309 ASN A ND2 1 
ATOM   2259  N N   . VAL A 1 310 ? 16.773  -57.490 15.067  1.00 78.35  ? 310 VAL A N   1 
ATOM   2260  C CA  . VAL A 1 310 ? 16.896  -56.526 13.984  1.00 77.45  ? 310 VAL A CA  1 
ATOM   2261  C C   . VAL A 1 310 ? 15.803  -56.810 12.965  1.00 81.17  ? 310 VAL A C   1 
ATOM   2262  O O   . VAL A 1 310 ? 15.617  -57.959 12.548  1.00 89.18  ? 310 VAL A O   1 
ATOM   2263  C CB  . VAL A 1 310 ? 18.294  -56.571 13.339  1.00 72.31  ? 310 VAL A CB  1 
ATOM   2264  C CG1 . VAL A 1 310 ? 18.715  -57.997 13.113  1.00 80.77  ? 310 VAL A CG1 1 
ATOM   2265  C CG2 . VAL A 1 310 ? 18.314  -55.780 12.037  1.00 72.60  ? 310 VAL A CG2 1 
ATOM   2266  N N   . SER A 1 311 ? 15.080  -55.766 12.572  1.00 79.84  ? 311 SER A N   1 
ATOM   2267  C CA  . SER A 1 311 ? 13.941  -55.882 11.667  1.00 83.47  ? 311 SER A CA  1 
ATOM   2268  C C   . SER A 1 311 ? 14.222  -55.004 10.454  1.00 83.11  ? 311 SER A C   1 
ATOM   2269  O O   . SER A 1 311 ? 14.090  -53.778 10.521  1.00 83.25  ? 311 SER A O   1 
ATOM   2270  C CB  . SER A 1 311 ? 12.648  -55.476 12.363  1.00 79.82  ? 311 SER A CB  1 
ATOM   2271  O OG  . SER A 1 311 ? 12.527  -56.121 13.620  1.00 80.37  ? 311 SER A OG  1 
ATOM   2272  N N   . ILE A 1 312 ? 14.606  -55.630 9.356   0.18 93.29  ? 312 ILE A N   1 
ATOM   2273  C CA  . ILE A 1 312 ? 14.990  -54.921 8.144   0.18 98.27  ? 312 ILE A CA  1 
ATOM   2274  C C   . ILE A 1 312 ? 13.781  -54.823 7.224   0.18 104.94 ? 312 ILE A C   1 
ATOM   2275  O O   . ILE A 1 312 ? 13.047  -55.800 7.032   0.18 107.04 ? 312 ILE A O   1 
ATOM   2276  C CB  . ILE A 1 312 ? 16.159  -55.630 7.433   0.18 98.76  ? 312 ILE A CB  1 
ATOM   2277  C CG1 . ILE A 1 312 ? 17.429  -55.545 8.281   0.18 91.91  ? 312 ILE A CG1 1 
ATOM   2278  C CG2 . ILE A 1 312 ? 16.390  -55.025 6.057   0.18 99.25  ? 312 ILE A CG2 1 
ATOM   2279  C CD1 . ILE A 1 312 ? 18.551  -56.432 7.789   0.18 89.62  ? 312 ILE A CD1 1 
ATOM   2280  N N   . SER A 1 313 ? 13.571  -53.639 6.653   1.00 114.72 ? 313 SER A N   1 
ATOM   2281  C CA  . SER A 1 313 ? 12.416  -53.377 5.808   1.00 112.13 ? 313 SER A CA  1 
ATOM   2282  C C   . SER A 1 313 ? 12.782  -53.593 4.341   1.00 113.52 ? 313 SER A C   1 
ATOM   2283  O O   . SER A 1 313 ? 13.891  -54.016 4.010   1.00 116.13 ? 313 SER A O   1 
ATOM   2284  C CB  . SER A 1 313 ? 11.894  -51.963 6.054   1.00 109.90 ? 313 SER A CB  1 
ATOM   2285  O OG  . SER A 1 313 ? 11.474  -51.799 7.397   1.00 110.05 ? 313 SER A OG  1 
ATOM   2286  N N   . ALA A 1 314 ? 11.854  -53.278 3.443   1.00 109.17 ? 314 ALA A N   1 
ATOM   2287  C CA  . ALA A 1 314 ? 12.043  -53.545 2.026   1.00 109.05 ? 314 ALA A CA  1 
ATOM   2288  C C   . ALA A 1 314 ? 12.888  -52.462 1.367   1.00 106.34 ? 314 ALA A C   1 
ATOM   2289  O O   . ALA A 1 314 ? 12.951  -51.320 1.831   1.00 103.34 ? 314 ALA A O   1 
ATOM   2290  C CB  . ALA A 1 314 ? 10.693  -53.644 1.315   1.00 113.32 ? 314 ALA A CB  1 
ATOM   2291  N N   . ASN A 1 315 ? 13.546  -52.843 0.270   1.00 110.98 ? 315 ASN A N   1 
ATOM   2292  C CA  . ASN A 1 315 ? 14.266  -51.909 -0.599  1.00 114.53 ? 315 ASN A CA  1 
ATOM   2293  C C   . ASN A 1 315 ? 15.303  -51.099 0.176   1.00 113.56 ? 315 ASN A C   1 
ATOM   2294  O O   . ASN A 1 315 ? 15.363  -49.872 0.087   1.00 114.44 ? 315 ASN A O   1 
ATOM   2295  C CB  . ASN A 1 315 ? 13.298  -50.990 -1.342  1.00 115.52 ? 315 ASN A CB  1 
ATOM   2296  C CG  . ASN A 1 315 ? 12.531  -51.715 -2.420  1.00 113.76 ? 315 ASN A CG  1 
ATOM   2297  O OD1 . ASN A 1 315 ? 11.426  -52.206 -2.193  1.00 118.53 ? 315 ASN A OD1 1 
ATOM   2298  N ND2 . ASN A 1 315 ? 13.120  -51.795 -3.606  1.00 110.44 ? 315 ASN A ND2 1 
ATOM   2299  N N   . VAL A 1 316 ? 16.123  -51.802 0.947   1.00 106.31 ? 316 VAL A N   1 
ATOM   2300  C CA  . VAL A 1 316 ? 17.214  -51.198 1.696   1.00 98.82  ? 316 VAL A CA  1 
ATOM   2301  C C   . VAL A 1 316 ? 18.510  -51.839 1.226   1.00 93.72  ? 316 VAL A C   1 
ATOM   2302  O O   . VAL A 1 316 ? 18.561  -53.049 0.980   1.00 95.88  ? 316 VAL A O   1 
ATOM   2303  C CB  . VAL A 1 316 ? 17.018  -51.374 3.217   1.00 96.77  ? 316 VAL A CB  1 
ATOM   2304  C CG1 . VAL A 1 316 ? 16.902  -52.844 3.568   1.00 98.74  ? 316 VAL A CG1 1 
ATOM   2305  C CG2 . VAL A 1 316 ? 18.154  -50.728 3.984   1.00 91.92  ? 316 VAL A CG2 1 
ATOM   2306  N N   . ARG A 1 317 ? 19.555  -51.028 1.093   1.00 92.95  ? 317 ARG A N   1 
ATOM   2307  C CA  . ARG A 1 317 ? 20.843  -51.496 0.594   1.00 95.19  ? 317 ARG A CA  1 
ATOM   2308  C C   . ARG A 1 317 ? 21.809  -51.623 1.766   1.00 93.40  ? 317 ARG A C   1 
ATOM   2309  O O   . ARG A 1 317 ? 22.246  -50.619 2.338   1.00 90.57  ? 317 ARG A O   1 
ATOM   2310  C CB  . ARG A 1 317 ? 21.395  -50.562 -0.481  1.00 101.80 ? 317 ARG A CB  1 
ATOM   2311  C CG  . ARG A 1 317 ? 20.575  -50.548 -1.765  1.00 101.26 ? 317 ARG A CG  1 
ATOM   2312  C CD  . ARG A 1 317 ? 21.399  -50.055 -2.948  1.00 107.69 ? 317 ARG A CD  1 
ATOM   2313  N NE  . ARG A 1 317 ? 21.861  -48.678 -2.789  1.00 112.40 ? 317 ARG A NE  1 
ATOM   2314  C CZ  . ARG A 1 317 ? 21.294  -47.625 -3.370  1.00 117.50 ? 317 ARG A CZ  1 
ATOM   2315  N NH1 . ARG A 1 317 ? 20.238  -47.787 -4.158  1.00 120.99 ? 317 ARG A NH1 1 
ATOM   2316  N NH2 . ARG A 1 317 ? 21.786  -46.409 -3.171  1.00 114.20 ? 317 ARG A NH2 1 
ATOM   2317  N N   . VAL A 1 318 ? 22.141  -52.861 2.117   1.00 91.05  ? 318 VAL A N   1 
ATOM   2318  C CA  . VAL A 1 318 ? 23.046  -53.161 3.219   1.00 89.04  ? 318 VAL A CA  1 
ATOM   2319  C C   . VAL A 1 318 ? 24.439  -53.385 2.645   1.00 90.74  ? 318 VAL A C   1 
ATOM   2320  O O   . VAL A 1 318 ? 24.626  -54.221 1.752   1.00 94.59  ? 318 VAL A O   1 
ATOM   2321  C CB  . VAL A 1 318 ? 22.566  -54.387 4.009   1.00 85.74  ? 318 VAL A CB  1 
ATOM   2322  C CG1 . VAL A 1 318 ? 23.645  -54.866 4.956   1.00 82.42  ? 318 VAL A CG1 1 
ATOM   2323  C CG2 . VAL A 1 318 ? 21.287  -54.054 4.765   1.00 86.79  ? 318 VAL A CG2 1 
ATOM   2324  N N   . GLY A 1 319 ? 25.418  -52.639 3.155   1.00 94.09  ? 319 GLY A N   1 
ATOM   2325  C CA  . GLY A 1 319 ? 26.778  -52.760 2.691   1.00 89.55  ? 319 GLY A CA  1 
ATOM   2326  C C   . GLY A 1 319 ? 27.484  -53.957 3.289   1.00 86.74  ? 319 GLY A C   1 
ATOM   2327  O O   . GLY A 1 319 ? 26.912  -54.759 4.041   1.00 84.77  ? 319 GLY A O   1 
ATOM   2328  N N   . PRO A 1 320 ? 28.764  -54.091 2.950   1.00 89.93  ? 320 PRO A N   1 
ATOM   2329  C CA  . PRO A 1 320 ? 29.551  -55.224 3.435   1.00 88.09  ? 320 PRO A CA  1 
ATOM   2330  C C   . PRO A 1 320 ? 30.185  -54.960 4.790   1.00 85.67  ? 320 PRO A C   1 
ATOM   2331  O O   . PRO A 1 320 ? 30.547  -53.834 5.139   1.00 87.61  ? 320 PRO A O   1 
ATOM   2332  C CB  . PRO A 1 320 ? 30.623  -55.372 2.348   1.00 89.24  ? 320 PRO A CB  1 
ATOM   2333  C CG  . PRO A 1 320 ? 30.871  -53.972 1.919   1.00 93.81  ? 320 PRO A CG  1 
ATOM   2334  C CD  . PRO A 1 320 ? 29.535  -53.254 2.013   1.00 93.84  ? 320 PRO A CD  1 
ATOM   2335  N N   . GLY A 1 321 ? 30.317  -56.040 5.555   1.00 82.18  ? 321 GLY A N   1 
ATOM   2336  C CA  . GLY A 1 321 ? 30.967  -55.974 6.852   1.00 77.60  ? 321 GLY A CA  1 
ATOM   2337  C C   . GLY A 1 321 ? 30.313  -55.027 7.833   1.00 77.22  ? 321 GLY A C   1 
ATOM   2338  O O   . GLY A 1 321 ? 31.005  -54.436 8.668   1.00 78.37  ? 321 GLY A O   1 
ATOM   2339  N N   . VAL A 1 322 ? 28.993  -54.868 7.759   1.00 76.85  ? 322 VAL A N   1 
ATOM   2340  C CA  . VAL A 1 322 ? 28.259  -53.989 8.661   1.00 76.65  ? 322 VAL A CA  1 
ATOM   2341  C C   . VAL A 1 322 ? 27.633  -54.830 9.764   1.00 72.29  ? 322 VAL A C   1 
ATOM   2342  O O   . VAL A 1 322 ? 27.337  -56.017 9.584   1.00 71.82  ? 322 VAL A O   1 
ATOM   2343  C CB  . VAL A 1 322 ? 27.197  -53.155 7.907   1.00 76.58  ? 322 VAL A CB  1 
ATOM   2344  C CG1 . VAL A 1 322 ? 27.836  -52.395 6.753   1.00 81.22  ? 322 VAL A CG1 1 
ATOM   2345  C CG2 . VAL A 1 322 ? 26.077  -54.040 7.412   1.00 77.33  ? 322 VAL A CG2 1 
ATOM   2346  N N   . ARG A 1 323 ? 27.431  -54.207 10.922  1.00 67.44  ? 323 ARG A N   1 
ATOM   2347  C CA  . ARG A 1 323 ? 26.957  -54.887 12.120  1.00 67.57  ? 323 ARG A CA  1 
ATOM   2348  C C   . ARG A 1 323 ? 25.613  -54.308 12.541  1.00 69.95  ? 323 ARG A C   1 
ATOM   2349  O O   . ARG A 1 323 ? 25.492  -53.094 12.737  1.00 72.86  ? 323 ARG A O   1 
ATOM   2350  C CB  . ARG A 1 323 ? 27.978  -54.749 13.252  1.00 67.81  ? 323 ARG A CB  1 
ATOM   2351  C CG  . ARG A 1 323 ? 27.655  -55.572 14.481  1.00 67.85  ? 323 ARG A CG  1 
ATOM   2352  C CD  . ARG A 1 323 ? 28.065  -57.017 14.284  1.00 68.78  ? 323 ARG A CD  1 
ATOM   2353  N NE  . ARG A 1 323 ? 27.861  -57.794 15.500  1.00 72.96  ? 323 ARG A NE  1 
ATOM   2354  C CZ  . ARG A 1 323 ? 26.790  -58.548 15.719  1.00 75.47  ? 323 ARG A CZ  1 
ATOM   2355  N NH1 . ARG A 1 323 ? 25.846  -58.622 14.794  1.00 76.18  ? 323 ARG A NH1 1 
ATOM   2356  N NH2 . ARG A 1 323 ? 26.666  -59.227 16.850  1.00 81.47  ? 323 ARG A NH2 1 
ATOM   2357  N N   . LEU A 1 324 ? 24.606  -55.173 12.685  1.00 70.63  ? 324 LEU A N   1 
ATOM   2358  C CA  . LEU A 1 324 ? 23.246  -54.742 13.004  1.00 66.91  ? 324 LEU A CA  1 
ATOM   2359  C C   . LEU A 1 324 ? 22.695  -55.574 14.155  1.00 67.23  ? 324 LEU A C   1 
ATOM   2360  O O   . LEU A 1 324 ? 22.394  -56.759 13.980  1.00 72.08  ? 324 LEU A O   1 
ATOM   2361  C CB  . LEU A 1 324 ? 22.336  -54.845 11.780  1.00 72.33  ? 324 LEU A CB  1 
ATOM   2362  C CG  . LEU A 1 324 ? 22.808  -54.122 10.518  1.00 71.06  ? 324 LEU A CG  1 
ATOM   2363  C CD1 . LEU A 1 324 ? 21.862  -54.383 9.359   1.00 75.89  ? 324 LEU A CD1 1 
ATOM   2364  C CD2 . LEU A 1 324 ? 22.925  -52.630 10.785  1.00 69.15  ? 324 LEU A CD2 1 
ATOM   2365  N N   . ILE A 1 325 ? 22.564  -54.950 15.327  1.00 66.86  ? 325 ILE A N   1 
ATOM   2366  C CA  . ILE A 1 325 ? 21.941  -55.569 16.492  1.00 73.04  ? 325 ILE A CA  1 
ATOM   2367  C C   . ILE A 1 325 ? 21.002  -54.549 17.123  1.00 73.95  ? 325 ILE A C   1 
ATOM   2368  O O   . ILE A 1 325 ? 21.267  -53.343 17.110  1.00 74.73  ? 325 ILE A O   1 
ATOM   2369  C CB  . ILE A 1 325 ? 22.963  -56.069 17.547  1.00 74.23  ? 325 ILE A CB  1 
ATOM   2370  C CG1 . ILE A 1 325 ? 23.647  -54.900 18.257  1.00 74.91  ? 325 ILE A CG1 1 
ATOM   2371  C CG2 . ILE A 1 325 ? 24.016  -56.947 16.914  1.00 77.86  ? 325 ILE A CG2 1 
ATOM   2372  C CD1 . ILE A 1 325 ? 24.703  -55.324 19.264  1.00 74.59  ? 325 ILE A CD1 1 
ATOM   2373  N N   . SER A 1 326 ? 19.882  -55.047 17.653  1.00 74.14  ? 326 SER A N   1 
ATOM   2374  C CA  . SER A 1 326 ? 18.973  -54.249 18.479  1.00 73.06  ? 326 SER A CA  1 
ATOM   2375  C C   . SER A 1 326 ? 18.497  -52.995 17.746  1.00 72.04  ? 326 SER A C   1 
ATOM   2376  O O   . SER A 1 326 ? 18.487  -51.893 18.294  1.00 69.82  ? 326 SER A O   1 
ATOM   2377  C CB  . SER A 1 326 ? 19.631  -53.879 19.810  1.00 71.83  ? 326 SER A CB  1 
ATOM   2378  O OG  . SER A 1 326 ? 20.165  -55.020 20.457  1.00 71.36  ? 326 SER A OG  1 
ATOM   2379  N N   . CYS A 1 327 ? 18.093  -53.168 16.491  1.00 78.19  ? 327 CYS A N   1 
ATOM   2380  C CA  . CYS A 1 327 ? 17.717  -52.019 15.684  1.00 78.61  ? 327 CYS A CA  1 
ATOM   2381  C C   . CYS A 1 327 ? 16.603  -52.398 14.721  1.00 79.22  ? 327 CYS A C   1 
ATOM   2382  O O   . CYS A 1 327 ? 16.366  -53.574 14.439  1.00 81.77  ? 327 CYS A O   1 
ATOM   2383  C CB  . CYS A 1 327 ? 18.919  -51.473 14.901  1.00 74.77  ? 327 CYS A CB  1 
ATOM   2384  S SG  . CYS A 1 327 ? 19.713  -52.692 13.822  1.00 72.82  ? 327 CYS A SG  1 
ATOM   2385  N N   . ILE A 1 328 ? 15.905  -51.378 14.231  1.00 78.64  ? 328 ILE A N   1 
ATOM   2386  C CA  . ILE A 1 328 ? 14.902  -51.529 13.185  1.00 78.19  ? 328 ILE A CA  1 
ATOM   2387  C C   . ILE A 1 328 ? 15.185  -50.469 12.130  1.00 78.39  ? 328 ILE A C   1 
ATOM   2388  O O   . ILE A 1 328 ? 15.424  -49.303 12.463  1.00 72.31  ? 328 ILE A O   1 
ATOM   2389  C CB  . ILE A 1 328 ? 13.465  -51.413 13.734  1.00 74.39  ? 328 ILE A CB  1 
ATOM   2390  C CG1 . ILE A 1 328 ? 13.302  -50.162 14.594  1.00 73.31  ? 328 ILE A CG1 1 
ATOM   2391  C CG2 . ILE A 1 328 ? 13.098  -52.650 14.546  1.00 75.97  ? 328 ILE A CG2 1 
ATOM   2392  C CD1 . ILE A 1 328 ? 11.906  -49.990 15.134  1.00 74.36  ? 328 ILE A CD1 1 
ATOM   2393  N N   . ILE A 1 329 ? 15.175  -50.876 10.865  1.00 92.63  ? 329 ILE A N   1 
ATOM   2394  C CA  . ILE A 1 329 ? 15.582  -50.024 9.755   1.00 91.17  ? 329 ILE A CA  1 
ATOM   2395  C C   . ILE A 1 329 ? 14.395  -49.850 8.819   1.00 91.50  ? 329 ILE A C   1 
ATOM   2396  O O   . ILE A 1 329 ? 13.749  -50.834 8.442   1.00 94.20  ? 329 ILE A O   1 
ATOM   2397  C CB  . ILE A 1 329 ? 16.791  -50.618 9.010   1.00 92.59  ? 329 ILE A CB  1 
ATOM   2398  C CG1 . ILE A 1 329 ? 17.963  -50.809 9.976   1.00 92.42  ? 329 ILE A CG1 1 
ATOM   2399  C CG2 . ILE A 1 329 ? 17.203  -49.720 7.857   1.00 90.79  ? 329 ILE A CG2 1 
ATOM   2400  C CD1 . ILE A 1 329 ? 19.127  -51.571 9.383   1.00 97.93  ? 329 ILE A CD1 1 
ATOM   2401  N N   . LEU A 1 330 ? 14.110  -48.606 8.447   1.00 82.96  ? 330 LEU A N   1 
ATOM   2402  C CA  . LEU A 1 330 ? 12.978  -48.314 7.583   1.00 83.04  ? 330 LEU A CA  1 
ATOM   2403  C C   . LEU A 1 330 ? 13.401  -48.426 6.117   1.00 88.10  ? 330 LEU A C   1 
ATOM   2404  O O   . LEU A 1 330 ? 14.507  -48.866 5.795   1.00 94.17  ? 330 LEU A O   1 
ATOM   2405  C CB  . LEU A 1 330 ? 12.391  -46.947 7.932   1.00 77.69  ? 330 LEU A CB  1 
ATOM   2406  C CG  . LEU A 1 330 ? 11.811  -46.871 9.350   1.00 75.84  ? 330 LEU A CG  1 
ATOM   2407  C CD1 . LEU A 1 330 ? 11.206  -45.506 9.638   1.00 74.57  ? 330 LEU A CD1 1 
ATOM   2408  C CD2 . LEU A 1 330 ? 10.781  -47.971 9.567   1.00 75.22  ? 330 LEU A CD2 1 
ATOM   2409  N N   . ASP A 1 331 ? 12.511  -48.034 5.213   1.00 90.28  ? 331 ASP A N   1 
ATOM   2410  C CA  . ASP A 1 331 ? 12.716  -48.255 3.790   1.00 94.92  ? 331 ASP A CA  1 
ATOM   2411  C C   . ASP A 1 331 ? 13.714  -47.261 3.207   1.00 99.06  ? 331 ASP A C   1 
ATOM   2412  O O   . ASP A 1 331 ? 13.903  -46.155 3.724   1.00 92.60  ? 331 ASP A O   1 
ATOM   2413  C CB  . ASP A 1 331 ? 11.388  -48.157 3.039   1.00 100.71 ? 331 ASP A CB  1 
ATOM   2414  C CG  . ASP A 1 331 ? 10.409  -49.244 3.441   1.00 97.80  ? 331 ASP A CG  1 
ATOM   2415  O OD1 . ASP A 1 331 ? 9.334   -48.907 3.976   1.00 92.25  ? 331 ASP A OD1 1 
ATOM   2416  O OD2 . ASP A 1 331 ? 10.727  -50.436 3.253   1.00 103.63 ? 331 ASP A OD2 1 
ATOM   2417  N N   . ASP A 1 332 ? 14.367  -47.687 2.122   1.00 129.98 ? 332 ASP A N   1 
ATOM   2418  C CA  . ASP A 1 332 ? 15.195  -46.828 1.276   1.00 129.29 ? 332 ASP A CA  1 
ATOM   2419  C C   . ASP A 1 332 ? 16.432  -46.303 2.002   1.00 128.53 ? 332 ASP A C   1 
ATOM   2420  O O   . ASP A 1 332 ? 16.971  -45.255 1.641   1.00 127.32 ? 332 ASP A O   1 
ATOM   2421  C CB  . ASP A 1 332 ? 14.381  -45.662 0.708   1.00 128.37 ? 332 ASP A CB  1 
ATOM   2422  C CG  . ASP A 1 332 ? 14.571  -45.491 -0.785  1.00 132.48 ? 332 ASP A CG  1 
ATOM   2423  O OD1 . ASP A 1 332 ? 15.676  -45.786 -1.286  1.00 140.09 ? 332 ASP A OD1 1 
ATOM   2424  O OD2 . ASP A 1 332 ? 13.609  -45.067 -1.461  1.00 137.01 ? 332 ASP A OD2 1 
ATOM   2425  N N   . VAL A 1 333 ? 16.910  -47.029 3.001   1.00 102.40 ? 333 VAL A N   1 
ATOM   2426  C CA  . VAL A 1 333 ? 18.106  -46.640 3.736   1.00 91.73  ? 333 VAL A CA  1 
ATOM   2427  C C   . VAL A 1 333 ? 19.329  -47.157 2.996   1.00 92.13  ? 333 VAL A C   1 
ATOM   2428  O O   . VAL A 1 333 ? 19.300  -48.237 2.395   1.00 94.76  ? 333 VAL A O   1 
ATOM   2429  C CB  . VAL A 1 333 ? 18.060  -47.170 5.182   1.00 91.17  ? 333 VAL A CB  1 
ATOM   2430  C CG1 . VAL A 1 333 ? 19.302  -46.747 5.946   1.00 91.93  ? 333 VAL A CG1 1 
ATOM   2431  C CG2 . VAL A 1 333 ? 16.818  -46.666 5.886   1.00 88.42  ? 333 VAL A CG2 1 
ATOM   2432  N N   . GLU A 1 334 ? 20.411  -46.383 3.036   1.00 93.34  ? 334 GLU A N   1 
ATOM   2433  C CA  . GLU A 1 334 ? 21.671  -46.741 2.394   1.00 94.12  ? 334 GLU A CA  1 
ATOM   2434  C C   . GLU A 1 334 ? 22.739  -46.885 3.471   1.00 95.83  ? 334 GLU A C   1 
ATOM   2435  O O   . GLU A 1 334 ? 23.103  -45.903 4.129   1.00 88.52  ? 334 GLU A O   1 
ATOM   2436  C CB  . GLU A 1 334 ? 22.076  -45.696 1.357   1.00 92.75  ? 334 GLU A CB  1 
ATOM   2437  C CG  . GLU A 1 334 ? 23.371  -46.015 0.627   1.00 96.18  ? 334 GLU A CG  1 
ATOM   2438  C CD  . GLU A 1 334 ? 23.718  -44.971 -0.414  1.00 100.07 ? 334 GLU A CD  1 
ATOM   2439  O OE1 . GLU A 1 334 ? 22.863  -44.102 -0.687  1.00 105.72 ? 334 GLU A OE1 1 
ATOM   2440  O OE2 . GLU A 1 334 ? 24.839  -45.019 -0.962  1.00 101.81 ? 334 GLU A OE2 1 
ATOM   2441  N N   . ILE A 1 335 ? 23.238  -48.105 3.650   1.00 112.90 ? 335 ILE A N   1 
ATOM   2442  C CA  . ILE A 1 335 ? 24.277  -48.401 4.629   1.00 113.45 ? 335 ILE A CA  1 
ATOM   2443  C C   . ILE A 1 335 ? 25.590  -48.574 3.879   1.00 113.73 ? 335 ILE A C   1 
ATOM   2444  O O   . ILE A 1 335 ? 25.707  -49.445 3.008   1.00 114.47 ? 335 ILE A O   1 
ATOM   2445  C CB  . ILE A 1 335 ? 23.938  -49.656 5.447   1.00 115.01 ? 335 ILE A CB  1 
ATOM   2446  C CG1 . ILE A 1 335 ? 22.561  -49.513 6.100   1.00 115.07 ? 335 ILE A CG1 1 
ATOM   2447  C CG2 . ILE A 1 335 ? 25.007  -49.906 6.498   1.00 115.78 ? 335 ILE A CG2 1 
ATOM   2448  C CD1 . ILE A 1 335 ? 22.504  -48.459 7.180   1.00 114.32 ? 335 ILE A CD1 1 
ATOM   2449  N N   . LYS A 1 336 ? 26.580  -47.750 4.209   1.00 101.58 ? 336 LYS A N   1 
ATOM   2450  C CA  . LYS A 1 336 ? 27.840  -47.740 3.482   1.00 99.83  ? 336 LYS A CA  1 
ATOM   2451  C C   . LYS A 1 336 ? 28.870  -48.643 4.165   1.00 103.32 ? 336 LYS A C   1 
ATOM   2452  O O   . LYS A 1 336 ? 28.558  -49.415 5.076   1.00 101.66 ? 336 LYS A O   1 
ATOM   2453  C CB  . LYS A 1 336 ? 28.356  -46.310 3.326   1.00 93.33  ? 336 LYS A CB  1 
ATOM   2454  C CG  . LYS A 1 336 ? 27.650  -45.505 2.243   1.00 86.39  ? 336 LYS A CG  1 
ATOM   2455  C CD  . LYS A 1 336 ? 28.361  -44.184 1.989   1.00 80.44  ? 336 LYS A CD  1 
ATOM   2456  C CE  . LYS A 1 336 ? 27.739  -43.426 0.827   1.00 73.93  ? 336 LYS A CE  1 
ATOM   2457  N NZ  . LYS A 1 336 ? 28.459  -42.152 0.547   1.00 68.19  ? 336 LYS A NZ  1 
ATOM   2458  N N   . GLU A 1 337 ? 30.118  -48.541 3.709   1.00 110.81 ? 337 GLU A N   1 
ATOM   2459  C CA  . GLU A 1 337 ? 31.181  -49.450 4.119   1.00 111.69 ? 337 GLU A CA  1 
ATOM   2460  C C   . GLU A 1 337 ? 31.427  -49.405 5.622   1.00 111.95 ? 337 GLU A C   1 
ATOM   2461  O O   . GLU A 1 337 ? 31.650  -48.336 6.197   1.00 111.04 ? 337 GLU A O   1 
ATOM   2462  C CB  . GLU A 1 337 ? 32.468  -49.104 3.371   1.00 111.27 ? 337 GLU A CB  1 
ATOM   2463  C CG  . GLU A 1 337 ? 32.257  -48.836 1.890   1.00 116.38 ? 337 GLU A CG  1 
ATOM   2464  C CD  . GLU A 1 337 ? 32.156  -50.111 1.078   1.00 132.12 ? 337 GLU A CD  1 
ATOM   2465  O OE1 . GLU A 1 337 ? 32.336  -51.202 1.659   1.00 133.31 ? 337 GLU A OE1 1 
ATOM   2466  O OE2 . GLU A 1 337 ? 31.886  -50.024 -0.138  1.00 135.80 ? 337 GLU A OE2 1 
ATOM   2467  N N   . ASN A 1 338 ? 31.402  -50.582 6.247   1.00 97.66  ? 338 ASN A N   1 
ATOM   2468  C CA  . ASN A 1 338 ? 31.816  -50.777 7.635   1.00 97.99  ? 338 ASN A CA  1 
ATOM   2469  C C   . ASN A 1 338 ? 31.071  -49.839 8.585   1.00 99.29  ? 338 ASN A C   1 
ATOM   2470  O O   . ASN A 1 338 ? 31.662  -49.049 9.322   1.00 100.51 ? 338 ASN A O   1 
ATOM   2471  C CB  . ASN A 1 338 ? 33.330  -50.602 7.766   1.00 95.95  ? 338 ASN A CB  1 
ATOM   2472  C CG  . ASN A 1 338 ? 34.097  -51.571 6.898   1.00 96.16  ? 338 ASN A CG  1 
ATOM   2473  O OD1 . ASN A 1 338 ? 33.705  -52.726 6.747   1.00 96.98  ? 338 ASN A OD1 1 
ATOM   2474  N ND2 . ASN A 1 338 ? 35.196  -51.105 6.317   1.00 97.47  ? 338 ASN A ND2 1 
ATOM   2475  N N   . ALA A 1 339 ? 29.749  -49.951 8.560   1.00 93.87  ? 339 ALA A N   1 
ATOM   2476  C CA  . ALA A 1 339 ? 28.883  -49.184 9.440   1.00 93.01  ? 339 ALA A CA  1 
ATOM   2477  C C   . ALA A 1 339 ? 28.443  -50.032 10.627  1.00 93.42  ? 339 ALA A C   1 
ATOM   2478  O O   . ALA A 1 339 ? 28.403  -51.264 10.563  1.00 93.40  ? 339 ALA A O   1 
ATOM   2479  C CB  . ALA A 1 339 ? 27.659  -48.667 8.678   1.00 93.01  ? 339 ALA A CB  1 
ATOM   2480  N N   . VAL A 1 340 ? 28.111  -49.350 11.722  1.00 86.56  ? 340 VAL A N   1 
ATOM   2481  C CA  . VAL A 1 340 ? 27.696  -49.992 12.964  1.00 82.92  ? 340 VAL A CA  1 
ATOM   2482  C C   . VAL A 1 340 ? 26.423  -49.311 13.446  1.00 84.05  ? 340 VAL A C   1 
ATOM   2483  O O   . VAL A 1 340 ? 26.364  -48.078 13.521  1.00 83.93  ? 340 VAL A O   1 
ATOM   2484  C CB  . VAL A 1 340 ? 28.793  -49.917 14.046  1.00 80.57  ? 340 VAL A CB  1 
ATOM   2485  C CG1 . VAL A 1 340 ? 28.349  -50.650 15.300  1.00 82.05  ? 340 VAL A CG1 1 
ATOM   2486  C CG2 . VAL A 1 340 ? 30.107  -50.491 13.528  1.00 79.65  ? 340 VAL A CG2 1 
ATOM   2487  N N   . VAL A 1 341 ? 25.405  -50.110 13.768  1.00 79.06  ? 341 VAL A N   1 
ATOM   2488  C CA  . VAL A 1 341 ? 24.108  -49.608 14.216  1.00 74.79  ? 341 VAL A CA  1 
ATOM   2489  C C   . VAL A 1 341 ? 23.706  -50.392 15.459  1.00 79.18  ? 341 VAL A C   1 
ATOM   2490  O O   . VAL A 1 341 ? 23.467  -51.604 15.384  1.00 76.17  ? 341 VAL A O   1 
ATOM   2491  C CB  . VAL A 1 341 ? 23.032  -49.723 13.126  1.00 70.55  ? 341 VAL A CB  1 
ATOM   2492  C CG1 . VAL A 1 341 ? 21.686  -49.276 13.665  1.00 73.49  ? 341 VAL A CG1 1 
ATOM   2493  C CG2 . VAL A 1 341 ? 23.417  -48.895 11.908  1.00 72.20  ? 341 VAL A CG2 1 
ATOM   2494  N N   . ILE A 1 342 ? 23.627  -49.705 16.598  1.00 80.75  ? 342 ILE A N   1 
ATOM   2495  C CA  . ILE A 1 342 ? 23.280  -50.308 17.881  1.00 82.52  ? 342 ILE A CA  1 
ATOM   2496  C C   . ILE A 1 342 ? 22.162  -49.488 18.509  1.00 82.75  ? 342 ILE A C   1 
ATOM   2497  O O   . ILE A 1 342 ? 22.276  -48.263 18.616  1.00 82.86  ? 342 ILE A O   1 
ATOM   2498  C CB  . ILE A 1 342 ? 24.488  -50.373 18.837  1.00 83.55  ? 342 ILE A CB  1 
ATOM   2499  C CG1 . ILE A 1 342 ? 25.772  -50.750 18.092  1.00 87.39  ? 342 ILE A CG1 1 
ATOM   2500  C CG2 . ILE A 1 342 ? 24.217  -51.354 19.968  1.00 86.18  ? 342 ILE A CG2 1 
ATOM   2501  C CD1 . ILE A 1 342 ? 25.794  -52.164 17.558  1.00 87.43  ? 342 ILE A CD1 1 
ATOM   2502  N N   . ASN A 1 343 ? 21.084  -50.158 18.917  1.00 77.47  ? 343 ASN A N   1 
ATOM   2503  C CA  . ASN A 1 343 ? 19.975  -49.525 19.636  1.00 72.39  ? 343 ASN A CA  1 
ATOM   2504  C C   . ASN A 1 343 ? 19.486  -48.270 18.913  1.00 71.43  ? 343 ASN A C   1 
ATOM   2505  O O   . ASN A 1 343 ? 19.420  -47.178 19.478  1.00 67.60  ? 343 ASN A O   1 
ATOM   2506  C CB  . ASN A 1 343 ? 20.378  -49.195 21.076  1.00 73.33  ? 343 ASN A CB  1 
ATOM   2507  C CG  . ASN A 1 343 ? 20.669  -50.431 21.901  1.00 72.64  ? 343 ASN A CG  1 
ATOM   2508  O OD1 . ASN A 1 343 ? 19.950  -51.427 21.820  1.00 67.45  ? 343 ASN A OD1 1 
ATOM   2509  N ND2 . ASN A 1 343 ? 21.729  -50.375 22.699  1.00 73.57  ? 343 ASN A ND2 1 
ATOM   2510  N N   . SER A 1 344 ? 19.126  -48.447 17.645  1.00 66.45  ? 344 SER A N   1 
ATOM   2511  C CA  . SER A 1 344 ? 18.799  -47.320 16.785  1.00 67.45  ? 344 SER A CA  1 
ATOM   2512  C C   . SER A 1 344 ? 17.527  -47.618 16.004  1.00 68.10  ? 344 SER A C   1 
ATOM   2513  O O   . SER A 1 344 ? 17.076  -48.763 15.913  1.00 69.64  ? 344 SER A O   1 
ATOM   2514  C CB  . SER A 1 344 ? 19.948  -46.999 15.818  1.00 65.99  ? 344 SER A CB  1 
ATOM   2515  O OG  . SER A 1 344 ? 21.199  -47.002 16.486  1.00 70.02  ? 344 SER A OG  1 
ATOM   2516  N N   . ILE A 1 345 ? 16.948  -46.559 15.439  1.00 65.92  ? 345 ILE A N   1 
ATOM   2517  C CA  . ILE A 1 345 ? 15.795  -46.650 14.548  1.00 64.83  ? 345 ILE A CA  1 
ATOM   2518  C C   . ILE A 1 345 ? 16.091  -45.731 13.370  1.00 64.00  ? 345 ILE A C   1 
ATOM   2519  O O   . ILE A 1 345 ? 16.011  -44.504 13.501  1.00 61.86  ? 345 ILE A O   1 
ATOM   2520  C CB  . ILE A 1 345 ? 14.479  -46.248 15.232  1.00 68.46  ? 345 ILE A CB  1 
ATOM   2521  C CG1 . ILE A 1 345 ? 14.220  -47.113 16.469  1.00 69.94  ? 345 ILE A CG1 1 
ATOM   2522  C CG2 . ILE A 1 345 ? 13.316  -46.354 14.252  1.00 68.03  ? 345 ILE A CG2 1 
ATOM   2523  C CD1 . ILE A 1 345 ? 12.913  -46.809 17.168  1.00 71.33  ? 345 ILE A CD1 1 
ATOM   2524  N N   . ILE A 1 346 ? 16.431  -46.313 12.226  1.00 65.78  ? 346 ILE A N   1 
ATOM   2525  C CA  . ILE A 1 346 ? 16.832  -45.540 11.059  1.00 68.06  ? 346 ILE A CA  1 
ATOM   2526  C C   . ILE A 1 346 ? 15.591  -45.197 10.248  1.00 68.05  ? 346 ILE A C   1 
ATOM   2527  O O   . ILE A 1 346 ? 14.797  -46.081 9.905   1.00 72.50  ? 346 ILE A O   1 
ATOM   2528  C CB  . ILE A 1 346 ? 17.855  -46.314 10.213  1.00 71.88  ? 346 ILE A CB  1 
ATOM   2529  C CG1 . ILE A 1 346 ? 19.002  -46.820 11.093  1.00 67.68  ? 346 ILE A CG1 1 
ATOM   2530  C CG2 . ILE A 1 346 ? 18.409  -45.419 9.122   1.00 72.62  ? 346 ILE A CG2 1 
ATOM   2531  C CD1 . ILE A 1 346 ? 19.772  -45.728 11.810  1.00 69.47  ? 346 ILE A CD1 1 
ATOM   2532  N N   . GLY A 1 347 ? 15.425  -43.913 9.940   1.00 70.43  ? 347 GLY A N   1 
ATOM   2533  C CA  . GLY A 1 347 ? 14.241  -43.431 9.258   1.00 69.34  ? 347 GLY A CA  1 
ATOM   2534  C C   . GLY A 1 347 ? 14.182  -43.762 7.783   1.00 84.74  ? 347 GLY A C   1 
ATOM   2535  O O   . GLY A 1 347 ? 14.921  -44.619 7.292   1.00 67.61  ? 347 GLY A O   1 
ATOM   2536  N N   . TRP A 1 348 ? 13.292  -43.087 7.067   1.00 65.47  ? 348 TRP A N   1 
ATOM   2537  C CA  . TRP A 1 348 ? 13.100  -43.347 5.650   1.00 68.52  ? 348 TRP A CA  1 
ATOM   2538  C C   . TRP A 1 348 ? 14.148  -42.608 4.829   1.00 69.40  ? 348 TRP A C   1 
ATOM   2539  O O   . TRP A 1 348 ? 14.510  -41.471 5.141   1.00 67.80  ? 348 TRP A O   1 
ATOM   2540  C CB  . TRP A 1 348 ? 11.699  -42.913 5.228   1.00 75.98  ? 348 TRP A CB  1 
ATOM   2541  C CG  . TRP A 1 348 ? 10.655  -43.234 6.252   1.00 74.98  ? 348 TRP A CG  1 
ATOM   2542  C CD1 . TRP A 1 348 ? 10.341  -42.500 7.361   1.00 68.91  ? 348 TRP A CD1 1 
ATOM   2543  C CD2 . TRP A 1 348 ? 9.787   -44.372 6.267   1.00 72.58  ? 348 TRP A CD2 1 
ATOM   2544  N NE1 . TRP A 1 348 ? 9.333   -43.110 8.064   1.00 64.82  ? 348 TRP A NE1 1 
ATOM   2545  C CE2 . TRP A 1 348 ? 8.974   -44.261 7.413   1.00 68.23  ? 348 TRP A CE2 1 
ATOM   2546  C CE3 . TRP A 1 348 ? 9.617   -45.472 5.422   1.00 74.12  ? 348 TRP A CE3 1 
ATOM   2547  C CZ2 . TRP A 1 348 ? 8.007   -45.208 7.735   1.00 69.56  ? 348 TRP A CZ2 1 
ATOM   2548  C CZ3 . TRP A 1 348 ? 8.656   -46.410 5.745   1.00 73.30  ? 348 TRP A CZ3 1 
ATOM   2549  C CH2 . TRP A 1 348 ? 7.863   -46.274 6.890   1.00 70.80  ? 348 TRP A CH2 1 
ATOM   2550  N N   . LYS A 1 349 ? 14.626  -43.261 3.768   1.00 82.07  ? 349 LYS A N   1 
ATOM   2551  C CA  . LYS A 1 349 ? 15.585  -42.680 2.820   1.00 83.89  ? 349 LYS A CA  1 
ATOM   2552  C C   . LYS A 1 349 ? 16.840  -42.145 3.507   1.00 75.71  ? 349 LYS A C   1 
ATOM   2553  O O   . LYS A 1 349 ? 17.555  -41.311 2.940   1.00 70.65  ? 349 LYS A O   1 
ATOM   2554  C CB  . LYS A 1 349 ? 14.943  -41.573 1.973   1.00 82.36  ? 349 LYS A CB  1 
ATOM   2555  C CG  . LYS A 1 349 ? 14.039  -42.066 0.849   1.00 94.16  ? 349 LYS A CG  1 
ATOM   2556  C CD  . LYS A 1 349 ? 12.672  -42.503 1.350   1.00 93.26  ? 349 LYS A CD  1 
ATOM   2557  C CE  . LYS A 1 349 ? 11.768  -42.916 0.198   1.00 104.89 ? 349 LYS A CE  1 
ATOM   2558  N NZ  . LYS A 1 349 ? 10.412  -43.308 0.674   1.00 108.27 ? 349 LYS A NZ  1 
ATOM   2559  N N   . SER A 1 350 ? 17.133  -42.613 4.716   1.00 79.67  ? 350 SER A N   1 
ATOM   2560  C CA  . SER A 1 350 ? 18.307  -42.132 5.423   1.00 66.93  ? 350 SER A CA  1 
ATOM   2561  C C   . SER A 1 350 ? 19.567  -42.710 4.794   1.00 71.61  ? 350 SER A C   1 
ATOM   2562  O O   . SER A 1 350 ? 19.556  -43.795 4.205   1.00 78.49  ? 350 SER A O   1 
ATOM   2563  C CB  . SER A 1 350 ? 18.233  -42.506 6.899   1.00 65.63  ? 350 SER A CB  1 
ATOM   2564  O OG  . SER A 1 350 ? 17.015  -42.060 7.460   1.00 65.15  ? 350 SER A OG  1 
ATOM   2565  N N   . SER A 1 351 ? 20.667  -41.979 4.938   1.00 68.71  ? 351 SER A N   1 
ATOM   2566  C CA  . SER A 1 351 ? 21.939  -42.356 4.336   1.00 72.91  ? 351 SER A CA  1 
ATOM   2567  C C   . SER A 1 351 ? 23.004  -42.419 5.419   1.00 68.77  ? 351 SER A C   1 
ATOM   2568  O O   . SER A 1 351 ? 23.300  -41.409 6.063   1.00 64.10  ? 351 SER A O   1 
ATOM   2569  C CB  . SER A 1 351 ? 22.338  -41.368 3.240   1.00 72.70  ? 351 SER A CB  1 
ATOM   2570  O OG  . SER A 1 351 ? 23.520  -41.792 2.590   1.00 72.14  ? 351 SER A OG  1 
ATOM   2571  N N   . ILE A 1 352 ? 23.576  -43.603 5.609   1.00 75.65  ? 352 ILE A N   1 
ATOM   2572  C CA  . ILE A 1 352 ? 24.589  -43.848 6.628   1.00 77.28  ? 352 ILE A CA  1 
ATOM   2573  C C   . ILE A 1 352 ? 25.939  -43.947 5.929   1.00 81.53  ? 352 ILE A C   1 
ATOM   2574  O O   . ILE A 1 352 ? 26.172  -44.869 5.141   1.00 85.18  ? 352 ILE A O   1 
ATOM   2575  C CB  . ILE A 1 352 ? 24.285  -45.121 7.427   1.00 82.15  ? 352 ILE A CB  1 
ATOM   2576  C CG1 . ILE A 1 352 ? 22.948  -44.987 8.160   1.00 80.19  ? 352 ILE A CG1 1 
ATOM   2577  C CG2 . ILE A 1 352 ? 25.407  -45.409 8.408   1.00 83.02  ? 352 ILE A CG2 1 
ATOM   2578  C CD1 . ILE A 1 352 ? 22.864  -43.790 9.067   1.00 76.66  ? 352 ILE A CD1 1 
ATOM   2579  N N   . GLY A 1 353 ? 26.826  -42.997 6.209   1.00 81.10  ? 353 GLY A N   1 
ATOM   2580  C CA  . GLY A 1 353 ? 28.120  -42.967 5.559   1.00 82.92  ? 353 GLY A CA  1 
ATOM   2581  C C   . GLY A 1 353 ? 29.008  -44.130 5.960   1.00 86.20  ? 353 GLY A C   1 
ATOM   2582  O O   . GLY A 1 353 ? 28.721  -44.904 6.875   1.00 85.30  ? 353 GLY A O   1 
ATOM   2583  N N   . ARG A 1 354 ? 30.126  -44.252 5.250   1.00 88.25  ? 354 ARG A N   1 
ATOM   2584  C CA  . ARG A 1 354 ? 31.054  -45.347 5.492   1.00 86.79  ? 354 ARG A CA  1 
ATOM   2585  C C   . ARG A 1 354 ? 31.870  -45.084 6.750   1.00 86.52  ? 354 ARG A C   1 
ATOM   2586  O O   . ARG A 1 354 ? 32.261  -43.946 7.029   1.00 87.88  ? 354 ARG A O   1 
ATOM   2587  C CB  . ARG A 1 354 ? 31.973  -45.545 4.289   1.00 86.37  ? 354 ARG A CB  1 
ATOM   2588  C CG  . ARG A 1 354 ? 32.690  -44.292 3.852   1.00 84.30  ? 354 ARG A CG  1 
ATOM   2589  C CD  . ARG A 1 354 ? 33.454  -44.518 2.567   1.00 86.13  ? 354 ARG A CD  1 
ATOM   2590  N NE  . ARG A 1 354 ? 32.573  -44.978 1.497   1.00 86.99  ? 354 ARG A NE  1 
ATOM   2591  C CZ  . ARG A 1 354 ? 31.942  -44.171 0.650   1.00 85.40  ? 354 ARG A CZ  1 
ATOM   2592  N NH1 . ARG A 1 354 ? 32.087  -42.856 0.750   1.00 82.65  ? 354 ARG A NH1 1 
ATOM   2593  N NH2 . ARG A 1 354 ? 31.161  -44.677 -0.296  1.00 85.46  ? 354 ARG A NH2 1 
ATOM   2594  N N   . TRP A 1 355 ? 32.117  -46.152 7.510   1.00 90.10  ? 355 TRP A N   1 
ATOM   2595  C CA  . TRP A 1 355 ? 32.805  -46.094 8.800   1.00 91.52  ? 355 TRP A CA  1 
ATOM   2596  C C   . TRP A 1 355 ? 32.108  -45.168 9.796   1.00 94.49  ? 355 TRP A C   1 
ATOM   2597  O O   . TRP A 1 355 ? 32.741  -44.668 10.731  1.00 93.93  ? 355 TRP A O   1 
ATOM   2598  C CB  . TRP A 1 355 ? 34.274  -45.683 8.634   1.00 92.12  ? 355 TRP A CB  1 
ATOM   2599  C CG  . TRP A 1 355 ? 35.143  -46.770 8.079   1.00 88.16  ? 355 TRP A CG  1 
ATOM   2600  C CD1 . TRP A 1 355 ? 35.477  -47.941 8.693   1.00 86.31  ? 355 TRP A CD1 1 
ATOM   2601  C CD2 . TRP A 1 355 ? 35.792  -46.788 6.801   1.00 87.54  ? 355 TRP A CD2 1 
ATOM   2602  N NE1 . TRP A 1 355 ? 36.292  -48.688 7.879   1.00 87.51  ? 355 TRP A NE1 1 
ATOM   2603  C CE2 . TRP A 1 355 ? 36.500  -48.003 6.710   1.00 85.35  ? 355 TRP A CE2 1 
ATOM   2604  C CE3 . TRP A 1 355 ? 35.842  -45.897 5.724   1.00 86.93  ? 355 TRP A CE3 1 
ATOM   2605  C CZ2 . TRP A 1 355 ? 37.249  -48.350 5.587   1.00 80.07  ? 355 TRP A CZ2 1 
ATOM   2606  C CZ3 . TRP A 1 355 ? 36.586  -46.243 4.609   1.00 80.76  ? 355 TRP A CZ3 1 
ATOM   2607  C CH2 . TRP A 1 355 ? 37.279  -47.459 4.550   1.00 79.55  ? 355 TRP A CH2 1 
ATOM   2608  N N   . SER A 1 356 ? 30.807  -44.952 9.629   1.00 91.00  ? 356 SER A N   1 
ATOM   2609  C CA  . SER A 1 356 ? 30.011  -44.161 10.554  1.00 90.05  ? 356 SER A CA  1 
ATOM   2610  C C   . SER A 1 356 ? 29.276  -45.072 11.528  1.00 89.35  ? 356 SER A C   1 
ATOM   2611  O O   . SER A 1 356 ? 28.948  -46.217 11.208  1.00 87.66  ? 356 SER A O   1 
ATOM   2612  C CB  . SER A 1 356 ? 29.004  -43.289 9.796   1.00 87.49  ? 356 SER A CB  1 
ATOM   2613  O OG  . SER A 1 356 ? 28.254  -44.057 8.874   1.00 88.58  ? 356 SER A OG  1 
ATOM   2614  N N   . ARG A 1 357 ? 29.017  -44.551 12.725  1.00 82.42  ? 357 ARG A N   1 
ATOM   2615  C CA  . ARG A 1 357 ? 28.464  -45.341 13.816  1.00 76.58  ? 357 ARG A CA  1 
ATOM   2616  C C   . ARG A 1 357 ? 27.255  -44.639 14.416  1.00 73.44  ? 357 ARG A C   1 
ATOM   2617  O O   . ARG A 1 357 ? 27.278  -43.427 14.648  1.00 76.60  ? 357 ARG A O   1 
ATOM   2618  C CB  . ARG A 1 357 ? 29.515  -45.591 14.905  1.00 76.54  ? 357 ARG A CB  1 
ATOM   2619  C CG  . ARG A 1 357 ? 29.107  -46.614 15.951  1.00 73.01  ? 357 ARG A CG  1 
ATOM   2620  C CD  . ARG A 1 357 ? 30.141  -46.699 17.060  1.00 73.67  ? 357 ARG A CD  1 
ATOM   2621  N NE  . ARG A 1 357 ? 29.835  -47.753 18.024  1.00 69.85  ? 357 ARG A NE  1 
ATOM   2622  C CZ  . ARG A 1 357 ? 30.372  -48.968 18.003  1.00 70.99  ? 357 ARG A CZ  1 
ATOM   2623  N NH1 . ARG A 1 357 ? 31.248  -49.294 17.062  1.00 70.16  ? 357 ARG A NH1 1 
ATOM   2624  N NH2 . ARG A 1 357 ? 30.032  -49.858 18.924  1.00 72.57  ? 357 ARG A NH2 1 
ATOM   2625  N N   . VAL A 1 358 ? 26.198  -45.413 14.662  1.00 77.79  ? 358 VAL A N   1 
ATOM   2626  C CA  . VAL A 1 358 ? 24.961  -44.919 15.260  1.00 63.43  ? 358 VAL A CA  1 
ATOM   2627  C C   . VAL A 1 358 ? 24.600  -45.882 16.384  1.00 70.12  ? 358 VAL A C   1 
ATOM   2628  O O   . VAL A 1 358 ? 24.075  -46.971 16.127  1.00 67.62  ? 358 VAL A O   1 
ATOM   2629  C CB  . VAL A 1 358 ? 23.821  -44.809 14.241  1.00 64.24  ? 358 VAL A CB  1 
ATOM   2630  C CG1 . VAL A 1 358 ? 22.580  -44.230 14.900  1.00 69.20  ? 358 VAL A CG1 1 
ATOM   2631  C CG2 . VAL A 1 358 ? 24.245  -43.958 13.050  1.00 68.93  ? 358 VAL A CG2 1 
ATOM   2632  N N   . GLN A 1 359 ? 24.889  -45.498 17.626  1.00 62.76  ? 359 GLN A N   1 
ATOM   2633  C CA  . GLN A 1 359 ? 24.635  -46.364 18.766  1.00 68.96  ? 359 GLN A CA  1 
ATOM   2634  C C   . GLN A 1 359 ? 23.862  -45.617 19.843  1.00 63.34  ? 359 GLN A C   1 
ATOM   2635  O O   . GLN A 1 359 ? 23.656  -44.401 19.775  1.00 61.82  ? 359 GLN A O   1 
ATOM   2636  C CB  . GLN A 1 359 ? 25.930  -46.923 19.366  1.00 69.58  ? 359 GLN A CB  1 
ATOM   2637  C CG  . GLN A 1 359 ? 26.799  -45.872 20.034  1.00 65.68  ? 359 GLN A CG  1 
ATOM   2638  C CD  . GLN A 1 359 ? 27.754  -46.472 21.047  1.00 70.11  ? 359 GLN A CD  1 
ATOM   2639  O OE1 . GLN A 1 359 ? 28.184  -47.618 20.910  1.00 69.67  ? 359 GLN A OE1 1 
ATOM   2640  N NE2 . GLN A 1 359 ? 28.088  -45.699 22.075  1.00 73.52  ? 359 GLN A NE2 1 
ATOM   2641  N N   . ALA A 1 360 ? 23.435  -46.380 20.846  1.00 67.08  ? 360 ALA A N   1 
ATOM   2642  C CA  . ALA A 1 360 ? 22.741  -45.847 22.010  1.00 69.79  ? 360 ALA A CA  1 
ATOM   2643  C C   . ALA A 1 360 ? 22.883  -46.853 23.143  1.00 69.85  ? 360 ALA A C   1 
ATOM   2644  O O   . ALA A 1 360 ? 23.350  -47.977 22.948  1.00 69.59  ? 360 ALA A O   1 
ATOM   2645  C CB  . ALA A 1 360 ? 21.266  -45.562 21.716  1.00 68.64  ? 360 ALA A CB  1 
ATOM   2646  N N   . SER A 1 361 ? 22.466  -46.431 24.338  1.00 75.70  ? 361 SER A N   1 
ATOM   2647  C CA  . SER A 1 361 ? 22.614  -47.282 25.514  1.00 79.27  ? 361 SER A CA  1 
ATOM   2648  C C   . SER A 1 361 ? 21.638  -48.452 25.483  1.00 79.02  ? 361 SER A C   1 
ATOM   2649  O O   . SER A 1 361 ? 21.991  -49.573 25.866  1.00 75.13  ? 361 SER A O   1 
ATOM   2650  C CB  . SER A 1 361 ? 22.429  -46.456 26.788  1.00 83.56  ? 361 SER A CB  1 
ATOM   2651  O OG  . SER A 1 361 ? 22.026  -45.131 26.489  1.00 84.47  ? 361 SER A OG  1 
ATOM   2652  N N   . GLY A 1 362 ? 20.410  -48.214 25.037  1.00 80.33  ? 362 GLY A N   1 
ATOM   2653  C CA  . GLY A 1 362 ? 19.371  -49.218 25.078  1.00 79.17  ? 362 GLY A CA  1 
ATOM   2654  C C   . GLY A 1 362 ? 18.423  -49.098 26.246  1.00 82.06  ? 362 GLY A C   1 
ATOM   2655  O O   . GLY A 1 362 ? 17.579  -49.982 26.428  1.00 85.27  ? 362 GLY A O   1 
ATOM   2656  N N   . ASP A 1 363 ? 18.541  -48.041 27.045  1.00 84.92  ? 363 ASP A N   1 
ATOM   2657  C CA  . ASP A 1 363 ? 17.676  -47.828 28.200  1.00 91.42  ? 363 ASP A CA  1 
ATOM   2658  C C   . ASP A 1 363 ? 16.305  -47.370 27.713  1.00 95.35  ? 363 ASP A C   1 
ATOM   2659  O O   . ASP A 1 363 ? 16.147  -46.228 27.267  1.00 93.84  ? 363 ASP A O   1 
ATOM   2660  C CB  . ASP A 1 363 ? 18.304  -46.801 29.139  1.00 89.99  ? 363 ASP A CB  1 
ATOM   2661  C CG  . ASP A 1 363 ? 17.647  -46.776 30.507  1.00 91.16  ? 363 ASP A CG  1 
ATOM   2662  O OD1 . ASP A 1 363 ? 17.019  -47.786 30.888  1.00 92.16  ? 363 ASP A OD1 1 
ATOM   2663  O OD2 . ASP A 1 363 ? 17.763  -45.747 31.204  1.00 91.38  ? 363 ASP A OD2 1 
ATOM   2664  N N   . TYR A 1 364 ? 15.309  -48.256 27.794  1.00 100.06 ? 364 TYR A N   1 
ATOM   2665  C CA  . TYR A 1 364 ? 13.953  -47.903 27.384  1.00 100.18 ? 364 TYR A CA  1 
ATOM   2666  C C   . TYR A 1 364 ? 13.264  -46.959 28.359  1.00 101.32 ? 364 TYR A C   1 
ATOM   2667  O O   . TYR A 1 364 ? 12.128  -46.548 28.098  1.00 100.95 ? 364 TYR A O   1 
ATOM   2668  C CB  . TYR A 1 364 ? 13.106  -49.167 27.204  1.00 101.66 ? 364 TYR A CB  1 
ATOM   2669  C CG  . TYR A 1 364 ? 13.685  -50.156 26.218  1.00 102.39 ? 364 TYR A CG  1 
ATOM   2670  C CD1 . TYR A 1 364 ? 13.555  -49.958 24.849  1.00 100.40 ? 364 TYR A CD1 1 
ATOM   2671  C CD2 . TYR A 1 364 ? 14.357  -51.291 26.655  1.00 104.77 ? 364 TYR A CD2 1 
ATOM   2672  C CE1 . TYR A 1 364 ? 14.084  -50.857 23.942  1.00 100.40 ? 364 TYR A CE1 1 
ATOM   2673  C CE2 . TYR A 1 364 ? 14.888  -52.198 25.756  1.00 105.61 ? 364 TYR A CE2 1 
ATOM   2674  C CZ  . TYR A 1 364 ? 14.749  -51.976 24.401  1.00 103.65 ? 364 TYR A CZ  1 
ATOM   2675  O OH  . TYR A 1 364 ? 15.273  -52.874 23.500  1.00 101.74 ? 364 TYR A OH  1 
ATOM   2676  N N   . ASN A 1 365 ? 13.918  -46.604 29.463  1.00 106.08 ? 365 ASN A N   1 
ATOM   2677  C CA  . ASN A 1 365 ? 13.413  -45.594 30.383  1.00 106.51 ? 365 ASN A CA  1 
ATOM   2678  C C   . ASN A 1 365 ? 14.015  -44.220 30.137  1.00 104.58 ? 365 ASN A C   1 
ATOM   2679  O O   . ASN A 1 365 ? 13.372  -43.208 30.436  1.00 108.37 ? 365 ASN A O   1 
ATOM   2680  C CB  . ASN A 1 365 ? 13.685  -46.014 31.831  1.00 110.21 ? 365 ASN A CB  1 
ATOM   2681  C CG  . ASN A 1 365 ? 13.428  -47.489 32.066  1.00 112.47 ? 365 ASN A CG  1 
ATOM   2682  O OD1 . ASN A 1 365 ? 12.466  -48.054 31.543  1.00 112.22 ? 365 ASN A OD1 1 
ATOM   2683  N ND2 . ASN A 1 365 ? 14.288  -48.123 32.854  1.00 115.03 ? 365 ASN A ND2 1 
ATOM   2684  N N   . ASP A 1 366 ? 15.227  -44.164 29.594  1.00 97.89  ? 366 ASP A N   1 
ATOM   2685  C CA  . ASP A 1 366 ? 15.858  -42.899 29.256  1.00 93.14  ? 366 ASP A CA  1 
ATOM   2686  C C   . ASP A 1 366 ? 15.348  -42.398 27.911  1.00 93.76  ? 366 ASP A C   1 
ATOM   2687  O O   . ASP A 1 366 ? 15.085  -43.186 26.998  1.00 94.39  ? 366 ASP A O   1 
ATOM   2688  C CB  . ASP A 1 366 ? 17.378  -43.062 29.215  1.00 92.45  ? 366 ASP A CB  1 
ATOM   2689  C CG  . ASP A 1 366 ? 18.100  -41.759 28.943  1.00 92.24  ? 366 ASP A CG  1 
ATOM   2690  O OD1 . ASP A 1 366 ? 17.479  -40.686 29.090  1.00 92.15  ? 366 ASP A OD1 1 
ATOM   2691  O OD2 . ASP A 1 366 ? 19.293  -41.811 28.576  1.00 93.94  ? 366 ASP A OD2 1 
ATOM   2692  N N   . ARG A 1 367 ? 15.201  -41.075 27.799  1.00 99.44  ? 367 ARG A N   1 
ATOM   2693  C CA  . ARG A 1 367 ? 14.712  -40.490 26.554  1.00 99.42  ? 367 ARG A CA  1 
ATOM   2694  C C   . ARG A 1 367 ? 15.683  -40.742 25.409  1.00 95.81  ? 367 ARG A C   1 
ATOM   2695  O O   . ARG A 1 367 ? 15.269  -41.095 24.298  1.00 93.08  ? 367 ARG A O   1 
ATOM   2696  C CB  . ARG A 1 367 ? 14.483  -38.990 26.731  1.00 95.79  ? 367 ARG A CB  1 
ATOM   2697  C CG  . ARG A 1 367 ? 13.609  -38.374 25.657  1.00 95.05  ? 367 ARG A CG  1 
ATOM   2698  C CD  . ARG A 1 367 ? 13.430  -36.885 25.883  1.00 96.32  ? 367 ARG A CD  1 
ATOM   2699  N NE  . ARG A 1 367 ? 12.514  -36.296 24.913  1.00 96.84  ? 367 ARG A NE  1 
ATOM   2700  C CZ  . ARG A 1 367 ? 12.266  -34.995 24.818  1.00 89.10  ? 367 ARG A CZ  1 
ATOM   2701  N NH1 . ARG A 1 367 ? 12.871  -34.143 25.634  1.00 84.92  ? 367 ARG A NH1 1 
ATOM   2702  N NH2 . ARG A 1 367 ? 11.418  -34.544 23.904  1.00 82.65  ? 367 ARG A NH2 1 
ATOM   2703  N N   . LEU A 1 368 ? 16.979  -40.565 25.660  1.00 91.96  ? 368 LEU A N   1 
ATOM   2704  C CA  . LEU A 1 368 ? 18.009  -40.800 24.661  1.00 88.88  ? 368 LEU A CA  1 
ATOM   2705  C C   . LEU A 1 368 ? 18.566  -42.216 24.721  1.00 89.27  ? 368 LEU A C   1 
ATOM   2706  O O   . LEU A 1 368 ? 19.668  -42.464 24.219  1.00 87.97  ? 368 LEU A O   1 
ATOM   2707  C CB  . LEU A 1 368 ? 19.137  -39.779 24.823  1.00 87.72  ? 368 LEU A CB  1 
ATOM   2708  C CG  . LEU A 1 368 ? 18.724  -38.312 24.677  1.00 83.38  ? 368 LEU A CG  1 
ATOM   2709  C CD1 . LEU A 1 368 ? 19.941  -37.402 24.738  1.00 81.43  ? 368 LEU A CD1 1 
ATOM   2710  C CD2 . LEU A 1 368 ? 17.947  -38.092 23.387  1.00 75.85  ? 368 LEU A CD2 1 
ATOM   2711  N N   . GLY A 1 369 ? 17.827  -43.151 25.323  1.00 88.63  ? 369 GLY A N   1 
ATOM   2712  C CA  . GLY A 1 369 ? 18.273  -44.531 25.375  1.00 86.33  ? 369 GLY A CA  1 
ATOM   2713  C C   . GLY A 1 369 ? 18.194  -45.245 24.045  1.00 80.55  ? 369 GLY A C   1 
ATOM   2714  O O   . GLY A 1 369 ? 18.873  -46.258 23.854  1.00 80.40  ? 369 GLY A O   1 
ATOM   2715  N N   . ILE A 1 370 ? 17.379  -44.741 23.122  1.00 79.53  ? 370 ILE A N   1 
ATOM   2716  C CA  . ILE A 1 370 ? 17.238  -45.301 21.784  1.00 72.66  ? 370 ILE A CA  1 
ATOM   2717  C C   . ILE A 1 370 ? 17.427  -44.156 20.799  1.00 70.88  ? 370 ILE A C   1 
ATOM   2718  O O   . ILE A 1 370 ? 16.550  -43.292 20.673  1.00 73.47  ? 370 ILE A O   1 
ATOM   2719  C CB  . ILE A 1 370 ? 15.877  -45.978 21.576  1.00 73.13  ? 370 ILE A CB  1 
ATOM   2720  C CG1 . ILE A 1 370 ? 15.664  -47.098 22.600  1.00 77.05  ? 370 ILE A CG1 1 
ATOM   2721  C CG2 . ILE A 1 370 ? 15.768  -46.523 20.162  1.00 73.29  ? 370 ILE A CG2 1 
ATOM   2722  C CD1 . ILE A 1 370 ? 16.682  -48.209 22.514  1.00 77.44  ? 370 ILE A CD1 1 
ATOM   2723  N N   . THR A 1 371 ? 18.565  -44.138 20.109  1.00 61.47  ? 371 THR A N   1 
ATOM   2724  C CA  . THR A 1 371 ? 18.812  -43.088 19.130  1.00 61.05  ? 371 THR A CA  1 
ATOM   2725  C C   . THR A 1 371 ? 17.908  -43.286 17.920  1.00 69.57  ? 371 THR A C   1 
ATOM   2726  O O   . THR A 1 371 ? 17.793  -44.394 17.389  1.00 66.07  ? 371 THR A O   1 
ATOM   2727  C CB  . THR A 1 371 ? 20.282  -43.066 18.707  1.00 69.24  ? 371 THR A CB  1 
ATOM   2728  O OG1 . THR A 1 371 ? 20.440  -42.203 17.571  1.00 61.37  ? 371 THR A OG1 1 
ATOM   2729  C CG2 . THR A 1 371 ? 20.768  -44.456 18.350  1.00 68.86  ? 371 THR A CG2 1 
ATOM   2730  N N   . ILE A 1 372 ? 17.250  -42.212 17.497  1.00 62.90  ? 372 ILE A N   1 
ATOM   2731  C CA  . ILE A 1 372 ? 16.244  -42.267 16.445  1.00 64.29  ? 372 ILE A CA  1 
ATOM   2732  C C   . ILE A 1 372 ? 16.645  -41.309 15.333  1.00 65.01  ? 372 ILE A C   1 
ATOM   2733  O O   . ILE A 1 372 ? 16.936  -40.136 15.593  1.00 72.51  ? 372 ILE A O   1 
ATOM   2734  C CB  . ILE A 1 372 ? 14.847  -41.924 16.991  1.00 67.30  ? 372 ILE A CB  1 
ATOM   2735  C CG1 . ILE A 1 372 ? 14.479  -42.882 18.129  1.00 68.89  ? 372 ILE A CG1 1 
ATOM   2736  C CG2 . ILE A 1 372 ? 13.816  -41.991 15.877  1.00 74.98  ? 372 ILE A CG2 1 
ATOM   2737  C CD1 . ILE A 1 372 ? 13.269  -42.462 18.924  1.00 71.78  ? 372 ILE A CD1 1 
ATOM   2738  N N   . LEU A 1 373 ? 16.661  -41.809 14.100  1.00 73.50  ? 373 LEU A N   1 
ATOM   2739  C CA  . LEU A 1 373 ? 17.028  -41.021 12.930  1.00 70.69  ? 373 LEU A CA  1 
ATOM   2740  C C   . LEU A 1 373 ? 15.787  -40.737 12.095  1.00 71.40  ? 373 LEU A C   1 
ATOM   2741  O O   . LEU A 1 373 ? 14.972  -41.635 11.858  1.00 66.14  ? 373 LEU A O   1 
ATOM   2742  C CB  . LEU A 1 373 ? 18.084  -41.745 12.089  1.00 64.63  ? 373 LEU A CB  1 
ATOM   2743  C CG  . LEU A 1 373 ? 19.543  -41.313 12.281  1.00 69.26  ? 373 LEU A CG  1 
ATOM   2744  C CD1 . LEU A 1 373 ? 19.983  -41.483 13.728  1.00 70.09  ? 373 LEU A CD1 1 
ATOM   2745  C CD2 . LEU A 1 373 ? 20.462  -42.079 11.341  1.00 70.34  ? 373 LEU A CD2 1 
ATOM   2746  N N   . GLY A 1 374 ? 15.644  -39.488 11.665  1.00 72.38  ? 374 GLY A N   1 
ATOM   2747  C CA  . GLY A 1 374 ? 14.488  -39.068 10.908  1.00 77.90  ? 374 GLY A CA  1 
ATOM   2748  C C   . GLY A 1 374 ? 14.523  -39.576 9.475   1.00 74.02  ? 374 GLY A C   1 
ATOM   2749  O O   . GLY A 1 374 ? 15.323  -40.427 9.086   1.00 72.64  ? 374 GLY A O   1 
ATOM   2750  N N   . GLU A 1 375 ? 13.622  -39.018 8.673   1.00 73.51  ? 375 GLU A N   1 
ATOM   2751  C CA  . GLU A 1 375 ? 13.528  -39.379 7.266   1.00 67.20  ? 375 GLU A CA  1 
ATOM   2752  C C   . GLU A 1 375 ? 14.604  -38.665 6.458   1.00 68.60  ? 375 GLU A C   1 
ATOM   2753  O O   . GLU A 1 375 ? 14.764  -37.446 6.566   1.00 63.02  ? 375 GLU A O   1 
ATOM   2754  C CB  . GLU A 1 375 ? 12.150  -39.020 6.716   1.00 68.90  ? 375 GLU A CB  1 
ATOM   2755  C CG  . GLU A 1 375 ? 12.012  -39.252 5.226   1.00 65.20  ? 375 GLU A CG  1 
ATOM   2756  C CD  . GLU A 1 375 ? 10.793  -38.573 4.644   1.00 64.80  ? 375 GLU A CD  1 
ATOM   2757  O OE1 . GLU A 1 375 ? 10.094  -37.857 5.392   1.00 69.38  ? 375 GLU A OE1 1 
ATOM   2758  O OE2 . GLU A 1 375 ? 10.544  -38.741 3.433   1.00 63.33  ? 375 GLU A OE2 1 
ATOM   2759  N N   . ALA A 1 376 ? 15.326  -39.425 5.634   1.00 65.66  ? 376 ALA A N   1 
ATOM   2760  C CA  . ALA A 1 376 ? 16.344  -38.874 4.738   1.00 72.52  ? 376 ALA A CA  1 
ATOM   2761  C C   . ALA A 1 376 ? 17.389  -38.074 5.509   1.00 61.30  ? 376 ALA A C   1 
ATOM   2762  O O   . ALA A 1 376 ? 17.758  -36.959 5.138   1.00 61.13  ? 376 ALA A O   1 
ATOM   2763  C CB  . ALA A 1 376 ? 15.707  -38.022 3.637   1.00 71.91  ? 376 ALA A CB  1 
ATOM   2764  N N   . VAL A 1 377 ? 17.866  -38.652 6.591   1.00 61.16  ? 377 VAL A N   1 
ATOM   2765  C CA  . VAL A 1 377 ? 18.975  -38.075 7.332   1.00 67.16  ? 377 VAL A CA  1 
ATOM   2766  C C   . VAL A 1 377 ? 20.255  -38.702 6.809   1.00 64.04  ? 377 VAL A C   1 
ATOM   2767  O O   . VAL A 1 377 ? 20.362  -39.930 6.702   1.00 64.45  ? 377 VAL A O   1 
ATOM   2768  C CB  . VAL A 1 377 ? 18.816  -38.299 8.843   1.00 67.78  ? 377 VAL A CB  1 
ATOM   2769  C CG1 . VAL A 1 377 ? 18.444  -39.735 9.114   1.00 72.39  ? 377 VAL A CG1 1 
ATOM   2770  C CG2 . VAL A 1 377 ? 20.102  -37.945 9.551   1.00 66.34  ? 377 VAL A CG2 1 
ATOM   2771  N N   . THR A 1 378 ? 21.226  -37.867 6.475   1.00 64.77  ? 378 THR A N   1 
ATOM   2772  C CA  . THR A 1 378 ? 22.450  -38.326 5.831   1.00 61.51  ? 378 THR A CA  1 
ATOM   2773  C C   . THR A 1 378 ? 23.579  -38.231 6.845   1.00 61.32  ? 378 THR A C   1 
ATOM   2774  O O   . THR A 1 378 ? 24.106  -37.147 7.104   1.00 61.04  ? 378 THR A O   1 
ATOM   2775  C CB  . THR A 1 378 ? 22.758  -37.505 4.586   1.00 61.69  ? 378 THR A CB  1 
ATOM   2776  O OG1 . THR A 1 378 ? 23.039  -36.156 4.969   1.00 61.29  ? 378 THR A OG1 1 
ATOM   2777  C CG2 . THR A 1 378 ? 21.571  -37.516 3.646   1.00 63.68  ? 378 THR A CG2 1 
ATOM   2778  N N   . VAL A 1 379 ? 23.945  -39.374 7.410   1.00 67.28  ? 379 VAL A N   1 
ATOM   2779  C CA  . VAL A 1 379 ? 25.114  -39.463 8.273   1.00 67.04  ? 379 VAL A CA  1 
ATOM   2780  C C   . VAL A 1 379 ? 26.332  -39.632 7.378   1.00 68.59  ? 379 VAL A C   1 
ATOM   2781  O O   . VAL A 1 379 ? 26.447  -40.623 6.651   1.00 73.87  ? 379 VAL A O   1 
ATOM   2782  C CB  . VAL A 1 379 ? 24.987  -40.630 9.263   1.00 70.20  ? 379 VAL A CB  1 
ATOM   2783  C CG1 . VAL A 1 379 ? 26.258  -40.762 10.087  1.00 73.76  ? 379 VAL A CG1 1 
ATOM   2784  C CG2 . VAL A 1 379 ? 23.775  -40.432 10.157  1.00 75.59  ? 379 VAL A CG2 1 
ATOM   2785  N N   . GLU A 1 380 ? 27.231  -38.656 7.414   1.00 68.34  ? 380 GLU A N   1 
ATOM   2786  C CA  . GLU A 1 380 ? 28.382  -38.693 6.531   1.00 70.64  ? 380 GLU A CA  1 
ATOM   2787  C C   . GLU A 1 380 ? 29.377  -39.748 7.010   1.00 76.12  ? 380 GLU A C   1 
ATOM   2788  O O   . GLU A 1 380 ? 29.213  -40.369 8.064   1.00 78.86  ? 380 GLU A O   1 
ATOM   2789  C CB  . GLU A 1 380 ? 29.035  -37.314 6.453   1.00 69.29  ? 380 GLU A CB  1 
ATOM   2790  C CG  . GLU A 1 380 ? 29.575  -36.953 5.088   1.00 72.36  ? 380 GLU A CG  1 
ATOM   2791  C CD  . GLU A 1 380 ? 29.673  -35.455 4.888   1.00 73.71  ? 380 GLU A CD  1 
ATOM   2792  O OE1 . GLU A 1 380 ? 29.144  -34.705 5.734   1.00 64.23  ? 380 GLU A OE1 1 
ATOM   2793  O OE2 . GLU A 1 380 ? 30.278  -35.027 3.885   1.00 85.87  ? 380 GLU A OE2 1 
ATOM   2794  N N   . ASP A 1 381 ? 30.418  -39.952 6.210   1.00 80.55  ? 381 ASP A N   1 
ATOM   2795  C CA  . ASP A 1 381 ? 31.421  -40.959 6.522   1.00 83.89  ? 381 ASP A CA  1 
ATOM   2796  C C   . ASP A 1 381 ? 32.144  -40.625 7.823   1.00 92.16  ? 381 ASP A C   1 
ATOM   2797  O O   . ASP A 1 381 ? 32.460  -39.464 8.097   1.00 92.94  ? 381 ASP A O   1 
ATOM   2798  C CB  . ASP A 1 381 ? 32.405  -41.068 5.363   1.00 87.38  ? 381 ASP A CB  1 
ATOM   2799  C CG  . ASP A 1 381 ? 31.704  -41.071 4.019   1.00 81.23  ? 381 ASP A CG  1 
ATOM   2800  O OD1 . ASP A 1 381 ? 30.632  -41.702 3.919   1.00 78.05  ? 381 ASP A OD1 1 
ATOM   2801  O OD2 . ASP A 1 381 ? 32.216  -40.443 3.070   1.00 81.93  ? 381 ASP A OD2 1 
ATOM   2802  N N   . GLU A 1 382 ? 32.398  -41.661 8.626   1.00 113.81 ? 382 GLU A N   1 
ATOM   2803  C CA  . GLU A 1 382 ? 33.046  -41.610 9.938   1.00 114.59 ? 382 GLU A CA  1 
ATOM   2804  C C   . GLU A 1 382 ? 32.240  -40.863 10.995  1.00 114.41 ? 382 GLU A C   1 
ATOM   2805  O O   . GLU A 1 382 ? 32.672  -40.815 12.152  1.00 115.17 ? 382 GLU A O   1 
ATOM   2806  C CB  . GLU A 1 382 ? 34.448  -40.985 9.889   1.00 114.61 ? 382 GLU A CB  1 
ATOM   2807  C CG  . GLU A 1 382 ? 35.508  -41.834 9.227   1.00 116.98 ? 382 GLU A CG  1 
ATOM   2808  C CD  . GLU A 1 382 ? 36.903  -41.328 9.529   1.00 121.34 ? 382 GLU A CD  1 
ATOM   2809  O OE1 . GLU A 1 382 ? 37.068  -40.601 10.533  1.00 118.08 ? 382 GLU A OE1 1 
ATOM   2810  O OE2 . GLU A 1 382 ? 37.834  -41.651 8.767   1.00 120.49 ? 382 GLU A OE2 1 
ATOM   2811  N N   . VAL A 1 383 ? 31.091  -40.283 10.648  1.00 96.13  ? 383 VAL A N   1 
ATOM   2812  C CA  . VAL A 1 383 ? 30.318  -39.510 11.612  1.00 92.70  ? 383 VAL A CA  1 
ATOM   2813  C C   . VAL A 1 383 ? 29.656  -40.443 12.619  1.00 91.39  ? 383 VAL A C   1 
ATOM   2814  O O   . VAL A 1 383 ? 29.095  -41.484 12.257  1.00 89.03  ? 383 VAL A O   1 
ATOM   2815  C CB  . VAL A 1 383 ? 29.283  -38.642 10.876  1.00 88.03  ? 383 VAL A CB  1 
ATOM   2816  C CG1 . VAL A 1 383 ? 28.445  -37.850 11.863  1.00 89.23  ? 383 VAL A CG1 1 
ATOM   2817  C CG2 . VAL A 1 383 ? 29.982  -37.708 9.902   1.00 83.46  ? 383 VAL A CG2 1 
ATOM   2818  N N   . ALA A 1 384 ? 29.703  -40.064 13.894  1.00 92.40  ? 384 ALA A N   1 
ATOM   2819  C CA  . ALA A 1 384 ? 29.190  -40.888 14.979  1.00 84.99  ? 384 ALA A CA  1 
ATOM   2820  C C   . ALA A 1 384 ? 27.978  -40.227 15.622  1.00 85.90  ? 384 ALA A C   1 
ATOM   2821  O O   . ALA A 1 384 ? 27.957  -39.011 15.829  1.00 86.19  ? 384 ALA A O   1 
ATOM   2822  C CB  . ALA A 1 384 ? 30.268  -41.135 16.037  1.00 88.41  ? 384 ALA A CB  1 
ATOM   2823  N N   . VAL A 1 385 ? 26.969  -41.037 15.931  1.00 72.14  ? 385 VAL A N   1 
ATOM   2824  C CA  . VAL A 1 385 ? 25.745  -40.574 16.577  1.00 69.94  ? 385 VAL A CA  1 
ATOM   2825  C C   . VAL A 1 385 ? 25.480  -41.495 17.760  1.00 69.43  ? 385 VAL A C   1 
ATOM   2826  O O   . VAL A 1 385 ? 25.089  -42.654 17.573  1.00 69.22  ? 385 VAL A O   1 
ATOM   2827  C CB  . VAL A 1 385 ? 24.547  -40.559 15.617  1.00 68.47  ? 385 VAL A CB  1 
ATOM   2828  C CG1 . VAL A 1 385 ? 23.285  -40.125 16.348  1.00 69.06  ? 385 VAL A CG1 1 
ATOM   2829  C CG2 . VAL A 1 385 ? 24.825  -39.645 14.434  1.00 68.52  ? 385 VAL A CG2 1 
ATOM   2830  N N   . ILE A 1 386 ? 25.695  -40.990 18.971  1.00 69.45  ? 386 ILE A N   1 
ATOM   2831  C CA  . ILE A 1 386 ? 25.533  -41.769 20.191  1.00 67.42  ? 386 ILE A CA  1 
ATOM   2832  C C   . ILE A 1 386 ? 24.363  -41.178 20.964  1.00 65.56  ? 386 ILE A C   1 
ATOM   2833  O O   . ILE A 1 386 ? 24.455  -40.060 21.487  1.00 66.28  ? 386 ILE A O   1 
ATOM   2834  C CB  . ILE A 1 386 ? 26.808  -41.780 21.044  1.00 66.05  ? 386 ILE A CB  1 
ATOM   2835  C CG1 . ILE A 1 386 ? 27.959  -42.470 20.300  1.00 68.04  ? 386 ILE A CG1 1 
ATOM   2836  C CG2 . ILE A 1 386 ? 26.546  -42.467 22.378  1.00 65.11  ? 386 ILE A CG2 1 
ATOM   2837  C CD1 . ILE A 1 386 ? 28.824  -41.528 19.477  1.00 72.31  ? 386 ILE A CD1 1 
ATOM   2838  N N   . GLY A 1 387 ? 23.269  -41.935 21.051  1.00 63.96  ? 387 GLY A N   1 
ATOM   2839  C CA  . GLY A 1 387 ? 22.112  -41.561 21.846  1.00 67.17  ? 387 GLY A CA  1 
ATOM   2840  C C   . GLY A 1 387 ? 21.568  -40.171 21.588  1.00 67.07  ? 387 GLY A C   1 
ATOM   2841  O O   . GLY A 1 387 ? 21.540  -39.332 22.493  1.00 71.15  ? 387 GLY A O   1 
ATOM   2842  N N   . SER A 1 388 ? 21.129  -39.916 20.358  1.00 68.09  ? 388 SER A N   1 
ATOM   2843  C CA  . SER A 1 388 ? 20.606  -38.612 19.985  1.00 66.95  ? 388 SER A CA  1 
ATOM   2844  C C   . SER A 1 388 ? 19.423  -38.801 19.046  1.00 66.25  ? 388 SER A C   1 
ATOM   2845  O O   . SER A 1 388 ? 19.178  -39.894 18.530  1.00 69.66  ? 388 SER A O   1 
ATOM   2846  C CB  . SER A 1 388 ? 21.686  -37.742 19.334  1.00 66.70  ? 388 SER A CB  1 
ATOM   2847  O OG  . SER A 1 388 ? 22.705  -37.421 20.266  1.00 71.51  ? 388 SER A OG  1 
ATOM   2848  N N   . ILE A 1 389 ? 18.685  -37.713 18.829  1.00 77.80  ? 389 ILE A N   1 
ATOM   2849  C CA  . ILE A 1 389 ? 17.490  -37.712 17.992  1.00 77.78  ? 389 ILE A CA  1 
ATOM   2850  C C   . ILE A 1 389 ? 17.694  -36.696 16.879  1.00 76.45  ? 389 ILE A C   1 
ATOM   2851  O O   . ILE A 1 389 ? 17.848  -35.498 17.145  1.00 81.43  ? 389 ILE A O   1 
ATOM   2852  C CB  . ILE A 1 389 ? 16.226  -37.380 18.798  1.00 67.46  ? 389 ILE A CB  1 
ATOM   2853  C CG1 . ILE A 1 389 ? 16.134  -38.264 20.043  1.00 70.59  ? 389 ILE A CG1 1 
ATOM   2854  C CG2 . ILE A 1 389 ? 14.993  -37.549 17.928  1.00 80.89  ? 389 ILE A CG2 1 
ATOM   2855  C CD1 . ILE A 1 389 ? 16.122  -39.738 19.739  1.00 72.05  ? 389 ILE A CD1 1 
ATOM   2856  N N   . VAL A 1 390 ? 17.683  -37.172 15.636  1.00 100.06 ? 390 VAL A N   1 
ATOM   2857  C CA  . VAL A 1 390 ? 17.866  -36.333 14.457  1.00 98.66  ? 390 VAL A CA  1 
ATOM   2858  C C   . VAL A 1 390 ? 16.547  -36.239 13.701  1.00 98.27  ? 390 VAL A C   1 
ATOM   2859  O O   . VAL A 1 390 ? 15.843  -37.242 13.535  1.00 99.04  ? 390 VAL A O   1 
ATOM   2860  C CB  . VAL A 1 390 ? 18.983  -36.876 13.545  1.00 98.17  ? 390 VAL A CB  1 
ATOM   2861  C CG1 . VAL A 1 390 ? 19.248  -35.914 12.400  1.00 96.88  ? 390 VAL A CG1 1 
ATOM   2862  C CG2 . VAL A 1 390 ? 20.249  -37.117 14.353  1.00 98.66  ? 390 VAL A CG2 1 
ATOM   2863  N N   . LEU A 1 391 ? 16.218  -35.034 13.241  1.00 100.95 ? 391 LEU A N   1 
ATOM   2864  C CA  . LEU A 1 391 ? 14.993  -34.808 12.491  1.00 100.63 ? 391 LEU A CA  1 
ATOM   2865  C C   . LEU A 1 391 ? 15.157  -35.263 11.042  1.00 100.44 ? 391 LEU A C   1 
ATOM   2866  O O   . LEU A 1 391 ? 16.242  -35.649 10.598  1.00 100.49 ? 391 LEU A O   1 
ATOM   2867  C CB  . LEU A 1 391 ? 14.601  -33.334 12.540  1.00 99.47  ? 391 LEU A CB  1 
ATOM   2868  C CG  . LEU A 1 391 ? 13.641  -32.905 13.650  1.00 99.72  ? 391 LEU A CG  1 
ATOM   2869  C CD1 . LEU A 1 391 ? 14.213  -33.211 15.027  1.00 100.55 ? 391 LEU A CD1 1 
ATOM   2870  C CD2 . LEU A 1 391 ? 13.323  -31.426 13.518  1.00 99.17  ? 391 LEU A CD2 1 
ATOM   2871  N N   . GLN A 1 392 ? 14.055  -35.216 10.300  1.00 85.41  ? 392 GLN A N   1 
ATOM   2872  C CA  . GLN A 1 392 ? 14.083  -35.678 8.923   1.00 74.98  ? 392 GLN A CA  1 
ATOM   2873  C C   . GLN A 1 392 ? 14.780  -34.661 8.028   1.00 102.99 ? 392 GLN A C   1 
ATOM   2874  O O   . GLN A 1 392 ? 14.836  -33.464 8.327   1.00 67.07  ? 392 GLN A O   1 
ATOM   2875  C CB  . GLN A 1 392 ? 12.672  -35.945 8.392   1.00 78.32  ? 392 GLN A CB  1 
ATOM   2876  C CG  . GLN A 1 392 ? 11.832  -34.714 8.118   1.00 81.45  ? 392 GLN A CG  1 
ATOM   2877  C CD  . GLN A 1 392 ? 11.192  -34.149 9.366   1.00 87.39  ? 392 GLN A CD  1 
ATOM   2878  O OE1 . GLN A 1 392 ? 11.387  -34.664 10.466  1.00 94.04  ? 392 GLN A OE1 1 
ATOM   2879  N NE2 . GLN A 1 392 ? 10.406  -33.092 9.200   1.00 83.28  ? 392 GLN A NE2 1 
ATOM   2880  N N   . ASN A 1 393 ? 15.311  -35.160 6.910   1.00 74.67  ? 393 ASN A N   1 
ATOM   2881  C CA  . ASN A 1 393 ? 15.972  -34.335 5.898   1.00 76.00  ? 393 ASN A CA  1 
ATOM   2882  C C   . ASN A 1 393 ? 17.123  -33.540 6.518   1.00 73.19  ? 393 ASN A C   1 
ATOM   2883  O O   . ASN A 1 393 ? 17.145  -32.307 6.509   1.00 75.38  ? 393 ASN A O   1 
ATOM   2884  C CB  . ASN A 1 393 ? 14.962  -33.407 5.213   1.00 78.35  ? 393 ASN A CB  1 
ATOM   2885  C CG  . ASN A 1 393 ? 13.639  -34.095 4.923   1.00 78.82  ? 393 ASN A CG  1 
ATOM   2886  O OD1 . ASN A 1 393 ? 13.601  -35.267 4.549   1.00 76.03  ? 393 ASN A OD1 1 
ATOM   2887  N ND2 . ASN A 1 393 ? 12.543  -33.365 5.104   1.00 76.16  ? 393 ASN A ND2 1 
ATOM   2888  N N   . LYS A 1 394 ? 18.092  -34.275 7.062   1.00 70.16  ? 394 LYS A N   1 
ATOM   2889  C CA  . LYS A 1 394 ? 19.165  -33.666 7.831   1.00 64.79  ? 394 LYS A CA  1 
ATOM   2890  C C   . LYS A 1 394 ? 20.506  -34.256 7.426   1.00 66.45  ? 394 LYS A C   1 
ATOM   2891  O O   . LYS A 1 394 ? 20.625  -35.464 7.210   1.00 64.69  ? 394 LYS A O   1 
ATOM   2892  C CB  . LYS A 1 394 ? 18.944  -33.866 9.334   1.00 67.02  ? 394 LYS A CB  1 
ATOM   2893  C CG  . LYS A 1 394 ? 19.677  -32.859 10.187  1.00 67.08  ? 394 LYS A CG  1 
ATOM   2894  C CD  . LYS A 1 394 ? 19.071  -31.486 9.995   1.00 69.58  ? 394 LYS A CD  1 
ATOM   2895  C CE  . LYS A 1 394 ? 19.816  -30.439 10.788  1.00 74.91  ? 394 LYS A CE  1 
ATOM   2896  N NZ  . LYS A 1 394 ? 19.112  -29.130 10.724  1.00 83.25  ? 394 LYS A NZ  1 
ATOM   2897  N N   . THR A 1 395 ? 21.515  -33.396 7.329   1.00 59.94  ? 395 THR A N   1 
ATOM   2898  C CA  . THR A 1 395 ? 22.862  -33.806 6.965   1.00 61.99  ? 395 THR A CA  1 
ATOM   2899  C C   . THR A 1 395 ? 23.799  -33.634 8.153   1.00 66.68  ? 395 THR A C   1 
ATOM   2900  O O   . THR A 1 395 ? 23.751  -32.618 8.854   1.00 64.93  ? 395 THR A O   1 
ATOM   2901  C CB  . THR A 1 395 ? 23.378  -33.006 5.769   1.00 60.94  ? 395 THR A CB  1 
ATOM   2902  O OG1 . THR A 1 395 ? 24.792  -33.200 5.637   1.00 60.72  ? 395 THR A OG1 1 
ATOM   2903  C CG2 . THR A 1 395 ? 23.077  -31.527 5.948   1.00 66.00  ? 395 THR A CG2 1 
ATOM   2904  N N   . LEU A 1 396 ? 24.647  -34.636 8.378   1.00 69.36  ? 396 LEU A N   1 
ATOM   2905  C CA  . LEU A 1 396 ? 25.556  -34.659 9.520   1.00 70.75  ? 396 LEU A CA  1 
ATOM   2906  C C   . LEU A 1 396 ? 26.982  -34.875 9.033   1.00 75.08  ? 396 LEU A C   1 
ATOM   2907  O O   . LEU A 1 396 ? 27.326  -35.974 8.587   1.00 77.11  ? 396 LEU A O   1 
ATOM   2908  C CB  . LEU A 1 396 ? 25.161  -35.751 10.512  1.00 69.01  ? 396 LEU A CB  1 
ATOM   2909  C CG  . LEU A 1 396 ? 23.835  -35.533 11.236  1.00 74.47  ? 396 LEU A CG  1 
ATOM   2910  C CD1 . LEU A 1 396 ? 23.545  -36.685 12.184  1.00 79.70  ? 396 LEU A CD1 1 
ATOM   2911  C CD2 . LEU A 1 396 ? 23.871  -34.211 11.982  1.00 78.70  ? 396 LEU A CD2 1 
ATOM   2912  N N   . ASN A 1 397 ? 27.811  -33.835 9.130   1.00 79.43  ? 397 ASN A N   1 
ATOM   2913  C CA  . ASN A 1 397 ? 29.237  -33.952 8.856   1.00 75.37  ? 397 ASN A CA  1 
ATOM   2914  C C   . ASN A 1 397 ? 30.074  -34.135 10.113  1.00 78.51  ? 397 ASN A C   1 
ATOM   2915  O O   . ASN A 1 397 ? 31.232  -34.554 10.010  1.00 78.72  ? 397 ASN A O   1 
ATOM   2916  C CB  . ASN A 1 397 ? 29.741  -32.717 8.100   1.00 74.12  ? 397 ASN A CB  1 
ATOM   2917  C CG  . ASN A 1 397 ? 29.432  -31.425 8.829   1.00 76.57  ? 397 ASN A CG  1 
ATOM   2918  O OD1 . ASN A 1 397 ? 28.412  -31.313 9.508   1.00 76.84  ? 397 ASN A OD1 1 
ATOM   2919  N ND2 . ASN A 1 397 ? 30.311  -30.439 8.688   1.00 80.26  ? 397 ASN A ND2 1 
ATOM   2920  N N   . VAL A 1 398 ? 29.519  -33.832 11.285  1.00 86.23  ? 398 VAL A N   1 
ATOM   2921  C CA  . VAL A 1 398 ? 30.234  -33.899 12.552  1.00 92.11  ? 398 VAL A CA  1 
ATOM   2922  C C   . VAL A 1 398 ? 29.518  -34.874 13.478  1.00 96.79  ? 398 VAL A C   1 
ATOM   2923  O O   . VAL A 1 398 ? 28.296  -35.043 13.413  1.00 89.52  ? 398 VAL A O   1 
ATOM   2924  C CB  . VAL A 1 398 ? 30.351  -32.497 13.194  1.00 93.33  ? 398 VAL A CB  1 
ATOM   2925  C CG1 . VAL A 1 398 ? 28.977  -31.956 13.561  1.00 94.28  ? 398 VAL A CG1 1 
ATOM   2926  C CG2 . VAL A 1 398 ? 31.276  -32.521 14.405  1.00 99.91  ? 398 VAL A CG2 1 
ATOM   2927  N N   . SER A 1 399 ? 30.295  -35.521 14.344  1.00 125.41 ? 399 SER A N   1 
ATOM   2928  C CA  . SER A 1 399 ? 29.740  -36.477 15.293  1.00 126.63 ? 399 SER A CA  1 
ATOM   2929  C C   . SER A 1 399 ? 28.942  -35.768 16.382  1.00 126.79 ? 399 SER A C   1 
ATOM   2930  O O   . SER A 1 399 ? 29.336  -34.707 16.872  1.00 126.34 ? 399 SER A O   1 
ATOM   2931  C CB  . SER A 1 399 ? 30.860  -37.305 15.925  1.00 127.62 ? 399 SER A CB  1 
ATOM   2932  O OG  . SER A 1 399 ? 31.574  -38.040 14.945  1.00 127.56 ? 399 SER A OG  1 
ATOM   2933  N N   . VAL A 1 400 ? 27.809  -36.364 16.756  1.00 97.76  ? 400 VAL A N   1 
ATOM   2934  C CA  . VAL A 1 400 ? 26.948  -35.842 17.809  1.00 88.39  ? 400 VAL A CA  1 
ATOM   2935  C C   . VAL A 1 400 ? 26.855  -36.871 18.930  1.00 79.17  ? 400 VAL A C   1 
ATOM   2936  O O   . VAL A 1 400 ? 27.097  -38.065 18.734  1.00 78.72  ? 400 VAL A O   1 
ATOM   2937  C CB  . VAL A 1 400 ? 25.544  -35.481 17.285  1.00 84.89  ? 400 VAL A CB  1 
ATOM   2938  C CG1 . VAL A 1 400 ? 25.641  -34.411 16.210  1.00 87.68  ? 400 VAL A CG1 1 
ATOM   2939  C CG2 . VAL A 1 400 ? 24.847  -36.719 16.749  1.00 78.80  ? 400 VAL A CG2 1 
ATOM   2940  N N   . GLN A 1 401 ? 26.496  -36.393 20.120  1.00 73.45  ? 401 GLN A N   1 
ATOM   2941  C CA  . GLN A 1 401 ? 26.441  -37.259 21.296  1.00 67.10  ? 401 GLN A CA  1 
ATOM   2942  C C   . GLN A 1 401 ? 25.555  -36.618 22.352  1.00 65.51  ? 401 GLN A C   1 
ATOM   2943  O O   . GLN A 1 401 ? 25.801  -35.475 22.751  1.00 65.08  ? 401 GLN A O   1 
ATOM   2944  C CB  . GLN A 1 401 ? 27.847  -37.503 21.846  1.00 72.80  ? 401 GLN A CB  1 
ATOM   2945  C CG  . GLN A 1 401 ? 27.885  -38.303 23.138  1.00 76.19  ? 401 GLN A CG  1 
ATOM   2946  C CD  . GLN A 1 401 ? 29.288  -38.440 23.701  1.00 76.16  ? 401 GLN A CD  1 
ATOM   2947  O OE1 . GLN A 1 401 ? 30.276  -38.146 23.024  1.00 78.62  ? 401 GLN A OE1 1 
ATOM   2948  N NE2 . GLN A 1 401 ? 29.382  -38.881 24.950  1.00 79.86  ? 401 GLN A NE2 1 
ATOM   2949  N N   . ASP A 1 402 ? 24.538  -37.352 22.807  1.00 66.46  ? 402 ASP A N   1 
ATOM   2950  C CA  . ASP A 1 402 ? 23.665  -36.933 23.906  1.00 66.27  ? 402 ASP A CA  1 
ATOM   2951  C C   . ASP A 1 402 ? 23.065  -35.550 23.649  1.00 67.17  ? 402 ASP A C   1 
ATOM   2952  O O   . ASP A 1 402 ? 23.219  -34.612 24.434  1.00 67.19  ? 402 ASP A O   1 
ATOM   2953  C CB  . ASP A 1 402 ? 24.412  -36.967 25.241  1.00 66.00  ? 402 ASP A CB  1 
ATOM   2954  C CG  . ASP A 1 402 ? 24.986  -38.333 25.551  1.00 66.27  ? 402 ASP A CG  1 
ATOM   2955  O OD1 . ASP A 1 402 ? 24.391  -39.338 25.108  1.00 61.01  ? 402 ASP A OD1 1 
ATOM   2956  O OD2 . ASP A 1 402 ? 26.025  -38.403 26.242  1.00 72.72  ? 402 ASP A OD2 1 
ATOM   2957  N N   . ASP A 1 403 ? 22.364  -35.440 22.524  1.00 68.06  ? 403 ASP A N   1 
ATOM   2958  C CA  . ASP A 1 403 ? 21.747  -34.187 22.116  1.00 72.74  ? 403 ASP A CA  1 
ATOM   2959  C C   . ASP A 1 403 ? 20.469  -34.498 21.349  1.00 71.36  ? 403 ASP A C   1 
ATOM   2960  O O   . ASP A 1 403 ? 20.127  -35.660 21.113  1.00 69.43  ? 403 ASP A O   1 
ATOM   2961  C CB  . ASP A 1 403 ? 22.713  -33.349 21.272  1.00 71.79  ? 403 ASP A CB  1 
ATOM   2962  C CG  . ASP A 1 403 ? 22.375  -31.870 21.288  1.00 76.98  ? 403 ASP A CG  1 
ATOM   2963  O OD1 . ASP A 1 403 ? 21.198  -31.523 21.529  1.00 80.37  ? 403 ASP A OD1 1 
ATOM   2964  O OD2 . ASP A 1 403 ? 23.289  -31.052 21.056  1.00 80.69  ? 403 ASP A OD2 1 
ATOM   2965  N N   . ILE A 1 404 ? 19.748  -33.443 20.980  1.00 76.37  ? 404 ILE A N   1 
ATOM   2966  C CA  . ILE A 1 404 ? 18.538  -33.543 20.172  1.00 70.66  ? 404 ILE A CA  1 
ATOM   2967  C C   . ILE A 1 404 ? 18.730  -32.572 19.013  1.00 73.84  ? 404 ILE A C   1 
ATOM   2968  O O   . ILE A 1 404 ? 18.584  -31.356 19.183  1.00 75.45  ? 404 ILE A O   1 
ATOM   2969  C CB  . ILE A 1 404 ? 17.269  -33.221 20.966  1.00 76.06  ? 404 ILE A CB  1 
ATOM   2970  C CG1 . ILE A 1 404 ? 17.157  -34.133 22.189  1.00 78.60  ? 404 ILE A CG1 1 
ATOM   2971  C CG2 . ILE A 1 404 ? 16.040  -33.370 20.085  1.00 73.87  ? 404 ILE A CG2 1 
ATOM   2972  C CD1 . ILE A 1 404 ? 15.942  -33.865 23.043  1.00 82.30  ? 404 ILE A CD1 1 
ATOM   2973  N N   . ILE A 1 405 ? 19.044  -33.102 17.835  1.00 77.15  ? 405 ILE A N   1 
ATOM   2974  C CA  . ILE A 1 405 ? 19.418  -32.289 16.682  1.00 75.29  ? 405 ILE A CA  1 
ATOM   2975  C C   . ILE A 1 405 ? 18.175  -31.979 15.859  1.00 79.05  ? 405 ILE A C   1 
ATOM   2976  O O   . ILE A 1 405 ? 17.482  -32.891 15.394  1.00 83.05  ? 405 ILE A O   1 
ATOM   2977  C CB  . ILE A 1 405 ? 20.486  -32.990 15.828  1.00 78.15  ? 405 ILE A CB  1 
ATOM   2978  C CG1 . ILE A 1 405 ? 21.835  -33.005 16.555  1.00 76.10  ? 405 ILE A CG1 1 
ATOM   2979  C CG2 . ILE A 1 405 ? 20.619  -32.308 14.478  1.00 83.08  ? 405 ILE A CG2 1 
ATOM   2980  C CD1 . ILE A 1 405 ? 22.037  -34.180 17.491  1.00 77.83  ? 405 ILE A CD1 1 
ATOM   2981  N N   . LEU A 1 406 ? 17.894  -30.692 15.682  1.00 81.73  ? 406 LEU A N   1 
ATOM   2982  C CA  . LEU A 1 406 ? 16.746  -30.245 14.903  1.00 84.97  ? 406 LEU A CA  1 
ATOM   2983  C C   . LEU A 1 406 ? 17.095  -30.089 13.426  1.00 83.51  ? 406 LEU A C   1 
ATOM   2984  O O   . LEU A 1 406 ? 18.065  -29.416 13.087  1.00 81.28  ? 406 LEU A O   1 
ATOM   2985  C CB  . LEU A 1 406 ? 16.227  -28.920 15.460  1.00 84.03  ? 406 LEU A CB  1 
ATOM   2986  C CG  . LEU A 1 406 ? 15.857  -28.946 16.944  1.00 75.87  ? 406 LEU A CG  1 
ATOM   2987  C CD1 . LEU A 1 406 ? 15.411  -27.573 17.419  1.00 71.89  ? 406 LEU A CD1 1 
ATOM   2988  C CD2 . LEU A 1 406 ? 14.778  -29.984 17.205  1.00 79.39  ? 406 LEU A CD2 1 
ATOM   2989  O OXT . LEU A 1 406 ? 16.415  -30.607 12.539  1.00 83.51  ? 406 LEU A OXT 1 
ATOM   2990  N N   . GLU B 1 4   ? 21.549  4.762   -17.412 1.00 104.93 ? 4   GLU B N   1 
ATOM   2991  C CA  . GLU B 1 4   ? 21.838  3.343   -17.241 1.00 102.28 ? 4   GLU B CA  1 
ATOM   2992  C C   . GLU B 1 4   ? 20.606  2.573   -16.781 1.00 100.81 ? 4   GLU B C   1 
ATOM   2993  O O   . GLU B 1 4   ? 19.511  3.127   -16.684 1.00 101.93 ? 4   GLU B O   1 
ATOM   2994  C CB  . GLU B 1 4   ? 22.978  3.136   -16.242 1.00 100.06 ? 4   GLU B CB  1 
ATOM   2995  C CG  . GLU B 1 4   ? 24.322  3.678   -16.698 1.00 102.08 ? 4   GLU B CG  1 
ATOM   2996  C CD  . GLU B 1 4   ? 25.422  3.409   -15.691 1.00 103.89 ? 4   GLU B CD  1 
ATOM   2997  O OE1 . GLU B 1 4   ? 25.105  2.930   -14.582 1.00 107.45 ? 4   GLU B OE1 1 
ATOM   2998  O OE2 . GLU B 1 4   ? 26.602  3.670   -16.009 1.00 99.24  ? 4   GLU B OE2 1 
ATOM   2999  N N   . LYS B 1 5   ? 20.797  1.287   -16.500 1.00 86.39  ? 5   LYS B N   1 
ATOM   3000  C CA  . LYS B 1 5   ? 19.728  0.449   -15.981 1.00 85.05  ? 5   LYS B CA  1 
ATOM   3001  C C   . LYS B 1 5   ? 20.333  -0.557  -15.016 1.00 82.75  ? 5   LYS B C   1 
ATOM   3002  O O   . LYS B 1 5   ? 21.423  -1.082  -15.257 1.00 83.11  ? 5   LYS B O   1 
ATOM   3003  C CB  . LYS B 1 5   ? 18.976  -0.263  -17.110 1.00 90.01  ? 5   LYS B CB  1 
ATOM   3004  C CG  . LYS B 1 5   ? 17.499  -0.458  -16.825 1.00 89.14  ? 5   LYS B CG  1 
ATOM   3005  C CD  . LYS B 1 5   ? 16.811  -1.215  -17.945 1.00 102.13 ? 5   LYS B CD  1 
ATOM   3006  C CE  . LYS B 1 5   ? 15.305  -1.123  -17.794 1.00 116.30 ? 5   LYS B CE  1 
ATOM   3007  N NZ  . LYS B 1 5   ? 14.880  0.288   -17.567 1.00 113.36 ? 5   LYS B NZ  1 
ATOM   3008  N N   . VAL B 1 6   ? 19.618  -0.820  -13.925 1.00 82.08  ? 6   VAL B N   1 
ATOM   3009  C CA  . VAL B 1 6   ? 20.114  -1.650  -12.836 1.00 73.30  ? 6   VAL B CA  1 
ATOM   3010  C C   . VAL B 1 6   ? 19.123  -2.771  -12.560 1.00 73.04  ? 6   VAL B C   1 
ATOM   3011  O O   . VAL B 1 6   ? 17.908  -2.546  -12.522 1.00 80.58  ? 6   VAL B O   1 
ATOM   3012  C CB  . VAL B 1 6   ? 20.352  -0.818  -11.559 1.00 76.96  ? 6   VAL B CB  1 
ATOM   3013  C CG1 . VAL B 1 6   ? 20.886  -1.699  -10.442 1.00 81.14  ? 6   VAL B CG1 1 
ATOM   3014  C CG2 . VAL B 1 6   ? 21.306  0.331   -11.841 1.00 78.47  ? 6   VAL B CG2 1 
ATOM   3015  N N   . VAL B 1 7   ? 19.646  -3.980  -12.368 1.00 72.05  ? 7   VAL B N   1 
ATOM   3016  C CA  . VAL B 1 7   ? 18.846  -5.132  -11.982 1.00 71.33  ? 7   VAL B CA  1 
ATOM   3017  C C   . VAL B 1 7   ? 19.382  -5.663  -10.657 1.00 70.25  ? 7   VAL B C   1 
ATOM   3018  O O   . VAL B 1 7   ? 20.539  -5.441  -10.292 1.00 70.16  ? 7   VAL B O   1 
ATOM   3019  C CB  . VAL B 1 7   ? 18.856  -6.232  -13.062 1.00 71.75  ? 7   VAL B CB  1 
ATOM   3020  C CG1 . VAL B 1 7   ? 20.179  -6.979  -13.052 1.00 72.38  ? 7   VAL B CG1 1 
ATOM   3021  C CG2 . VAL B 1 7   ? 17.689  -7.180  -12.876 1.00 74.11  ? 7   VAL B CG2 1 
ATOM   3022  N N   . ALA B 1 8   ? 18.519  -6.364  -9.927  1.00 69.49  ? 8   ALA B N   1 
ATOM   3023  C CA  . ALA B 1 8   ? 18.865  -6.894  -8.616  1.00 68.49  ? 8   ALA B CA  1 
ATOM   3024  C C   . ALA B 1 8   ? 18.502  -8.369  -8.548  1.00 69.72  ? 8   ALA B C   1 
ATOM   3025  O O   . ALA B 1 8   ? 17.404  -8.762  -8.956  1.00 77.46  ? 8   ALA B O   1 
ATOM   3026  C CB  . ALA B 1 8   ? 18.158  -6.123  -7.498  1.00 67.99  ? 8   ALA B CB  1 
ATOM   3027  N N   . VAL B 1 9   ? 19.420  -9.178  -8.027  1.00 67.51  ? 9   VAL B N   1 
ATOM   3028  C CA  . VAL B 1 9   ? 19.211  -10.612 -7.867  1.00 71.61  ? 9   VAL B CA  1 
ATOM   3029  C C   . VAL B 1 9   ? 19.514  -10.976 -6.423  1.00 70.84  ? 9   VAL B C   1 
ATOM   3030  O O   . VAL B 1 9   ? 20.618  -10.716 -5.933  1.00 82.13  ? 9   VAL B O   1 
ATOM   3031  C CB  . VAL B 1 9   ? 20.084  -11.437 -8.824  1.00 71.18  ? 9   VAL B CB  1 
ATOM   3032  C CG1 . VAL B 1 9   ? 19.882  -12.915 -8.566  1.00 72.68  ? 9   VAL B CG1 1 
ATOM   3033  C CG2 . VAL B 1 9   ? 19.750  -11.093 -10.267 1.00 80.67  ? 9   VAL B CG2 1 
ATOM   3034  N N   . ILE B 1 10  ? 18.542  -11.580 -5.747  1.00 74.43  ? 10  ILE B N   1 
ATOM   3035  C CA  . ILE B 1 10  ? 18.660  -11.946 -4.342  1.00 77.35  ? 10  ILE B CA  1 
ATOM   3036  C C   . ILE B 1 10  ? 18.696  -13.462 -4.227  1.00 77.87  ? 10  ILE B C   1 
ATOM   3037  O O   . ILE B 1 10  ? 17.869  -14.157 -4.829  1.00 78.43  ? 10  ILE B O   1 
ATOM   3038  C CB  . ILE B 1 10  ? 17.505  -11.365 -3.512  1.00 84.36  ? 10  ILE B CB  1 
ATOM   3039  C CG1 . ILE B 1 10  ? 17.439  -9.844  -3.677  1.00 87.87  ? 10  ILE B CG1 1 
ATOM   3040  C CG2 . ILE B 1 10  ? 17.668  -11.744 -2.051  1.00 89.04  ? 10  ILE B CG2 1 
ATOM   3041  C CD1 . ILE B 1 10  ? 16.327  -9.188  -2.886  1.00 88.04  ? 10  ILE B CD1 1 
ATOM   3042  N N   . MET B 1 11  ? 19.650  -13.975 -3.457  1.00 81.82  ? 11  MET B N   1 
ATOM   3043  C CA  . MET B 1 11  ? 19.673  -15.395 -3.148  1.00 81.24  ? 11  MET B CA  1 
ATOM   3044  C C   . MET B 1 11  ? 18.622  -15.720 -2.094  1.00 84.23  ? 11  MET B C   1 
ATOM   3045  O O   . MET B 1 11  ? 18.349  -14.925 -1.191  1.00 85.92  ? 11  MET B O   1 
ATOM   3046  C CB  . MET B 1 11  ? 21.054  -15.828 -2.658  1.00 86.57  ? 11  MET B CB  1 
ATOM   3047  C CG  . MET B 1 11  ? 22.100  -15.854 -3.748  1.00 85.88  ? 11  MET B CG  1 
ATOM   3048  S SD  . MET B 1 11  ? 21.739  -17.094 -5.005  1.00 69.01  ? 11  MET B SD  1 
ATOM   3049  C CE  . MET B 1 11  ? 23.126  -16.841 -6.107  1.00 94.55  ? 11  MET B CE  1 
ATOM   3050  N N   . VAL B 1 12  ? 18.028  -16.906 -2.219  1.00 80.74  ? 12  VAL B N   1 
ATOM   3051  C CA  . VAL B 1 12  ? 16.933  -17.340 -1.361  1.00 77.04  ? 12  VAL B CA  1 
ATOM   3052  C C   . VAL B 1 12  ? 17.301  -18.593 -0.574  1.00 75.21  ? 12  VAL B C   1 
ATOM   3053  O O   . VAL B 1 12  ? 17.070  -18.669 0.637   1.00 78.44  ? 12  VAL B O   1 
ATOM   3054  C CB  . VAL B 1 12  ? 15.639  -17.569 -2.174  1.00 76.39  ? 12  VAL B CB  1 
ATOM   3055  C CG1 . VAL B 1 12  ? 14.620  -18.310 -1.336  1.00 76.40  ? 12  VAL B CG1 1 
ATOM   3056  C CG2 . VAL B 1 12  ? 15.074  -16.243 -2.660  1.00 77.41  ? 12  VAL B CG2 1 
ATOM   3057  N N   . GLY B 1 13  ? 17.884  -19.581 -1.243  1.00 76.90  ? 13  GLY B N   1 
ATOM   3058  C CA  . GLY B 1 13  ? 18.168  -20.855 -0.620  1.00 83.96  ? 13  GLY B CA  1 
ATOM   3059  C C   . GLY B 1 13  ? 16.952  -21.760 -0.628  1.00 84.95  ? 13  GLY B C   1 
ATOM   3060  O O   . GLY B 1 13  ? 15.826  -21.352 -0.915  1.00 85.17  ? 13  GLY B O   1 
ATOM   3061  N N   . GLY B 1 14  ? 17.190  -23.027 -0.307  1.00 92.11  ? 14  GLY B N   1 
ATOM   3062  C CA  . GLY B 1 14  ? 16.141  -24.017 -0.329  1.00 89.72  ? 14  GLY B CA  1 
ATOM   3063  C C   . GLY B 1 14  ? 15.795  -24.551 1.044   1.00 90.14  ? 14  GLY B C   1 
ATOM   3064  O O   . GLY B 1 14  ? 16.228  -24.021 2.072   1.00 97.91  ? 14  GLY B O   1 
ATOM   3065  N N   . PRO B 1 15  ? 15.000  -25.625 1.083   1.00 88.24  ? 15  PRO B N   1 
ATOM   3066  C CA  . PRO B 1 15  ? 14.569  -26.183 2.375   1.00 92.85  ? 15  PRO B CA  1 
ATOM   3067  C C   . PRO B 1 15  ? 15.697  -26.812 3.171   1.00 95.41  ? 15  PRO B C   1 
ATOM   3068  O O   . PRO B 1 15  ? 15.470  -27.221 4.317   1.00 91.09  ? 15  PRO B O   1 
ATOM   3069  C CB  . PRO B 1 15  ? 13.525  -27.231 1.971   1.00 86.50  ? 15  PRO B CB  1 
ATOM   3070  C CG  . PRO B 1 15  ? 13.910  -27.622 0.583   1.00 82.84  ? 15  PRO B CG  1 
ATOM   3071  C CD  . PRO B 1 15  ? 14.450  -26.374 -0.058  1.00 85.06  ? 15  PRO B CD  1 
ATOM   3072  N N   . THR B 1 16  ? 16.896  -26.898 2.606   1.00 98.98  ? 16  THR B N   1 
ATOM   3073  C CA  . THR B 1 16  ? 18.054  -27.412 3.319   1.00 101.18 ? 16  THR B CA  1 
ATOM   3074  C C   . THR B 1 16  ? 18.861  -26.314 3.995   1.00 112.12 ? 16  THR B C   1 
ATOM   3075  O O   . THR B 1 16  ? 19.757  -26.622 4.787   1.00 108.72 ? 16  THR B O   1 
ATOM   3076  C CB  . THR B 1 16  ? 18.959  -28.190 2.363   1.00 93.08  ? 16  THR B CB  1 
ATOM   3077  O OG1 . THR B 1 16  ? 19.352  -27.337 1.282   1.00 97.71  ? 16  THR B OG1 1 
ATOM   3078  C CG2 . THR B 1 16  ? 18.223  -29.396 1.809   1.00 86.38  ? 16  THR B CG2 1 
ATOM   3079  N N   . LYS B 1 17  ? 18.575  -25.048 3.693   1.00 152.07 ? 17  LYS B N   1 
ATOM   3080  C CA  . LYS B 1 17  ? 19.219  -23.927 4.364   1.00 152.47 ? 17  LYS B CA  1 
ATOM   3081  C C   . LYS B 1 17  ? 18.437  -23.477 5.589   1.00 152.89 ? 17  LYS B C   1 
ATOM   3082  O O   . LYS B 1 17  ? 19.031  -23.198 6.636   1.00 153.21 ? 17  LYS B O   1 
ATOM   3083  C CB  . LYS B 1 17  ? 19.385  -22.753 3.397   1.00 152.64 ? 17  LYS B CB  1 
ATOM   3084  C CG  . LYS B 1 17  ? 19.964  -23.142 2.052   1.00 153.02 ? 17  LYS B CG  1 
ATOM   3085  C CD  . LYS B 1 17  ? 21.337  -23.770 2.206   1.00 153.78 ? 17  LYS B CD  1 
ATOM   3086  C CE  . LYS B 1 17  ? 21.896  -24.197 0.860   1.00 154.50 ? 17  LYS B CE  1 
ATOM   3087  N NZ  . LYS B 1 17  ? 22.001  -23.053 -0.087  1.00 158.83 ? 17  LYS B NZ  1 
ATOM   3088  N N   . GLY B 1 18  ? 17.113  -23.394 5.476   1.00 116.71 ? 18  GLY B N   1 
ATOM   3089  C CA  . GLY B 1 18  ? 16.268  -23.075 6.609   1.00 103.89 ? 18  GLY B CA  1 
ATOM   3090  C C   . GLY B 1 18  ? 16.068  -24.262 7.528   1.00 96.66  ? 18  GLY B C   1 
ATOM   3091  O O   . GLY B 1 18  ? 15.057  -24.347 8.232   1.00 92.17  ? 18  GLY B O   1 
ATOM   3092  N N   . THR B 1 19  ? 17.029  -25.186 7.531   1.00 98.90  ? 19  THR B N   1 
ATOM   3093  C CA  . THR B 1 19  ? 16.975  -26.355 8.397   1.00 92.30  ? 19  THR B CA  1 
ATOM   3094  C C   . THR B 1 19  ? 17.372  -26.048 9.834   1.00 86.76  ? 19  THR B C   1 
ATOM   3095  O O   . THR B 1 19  ? 17.450  -26.973 10.649  1.00 79.74  ? 19  THR B O   1 
ATOM   3096  C CB  . THR B 1 19  ? 17.869  -27.469 7.847   1.00 92.11  ? 19  THR B CB  1 
ATOM   3097  O OG1 . THR B 1 19  ? 17.676  -28.662 8.617   1.00 84.69  ? 19  THR B OG1 1 
ATOM   3098  C CG2 . THR B 1 19  ? 19.331  -27.060 7.925   1.00 98.19  ? 19  THR B CG2 1 
ATOM   3099  N N   . ARG B 1 20  ? 17.653  -24.786 10.154  1.00 90.01  ? 20  ARG B N   1 
ATOM   3100  C CA  . ARG B 1 20  ? 17.858  -24.365 11.531  1.00 85.94  ? 20  ARG B CA  1 
ATOM   3101  C C   . ARG B 1 20  ? 16.632  -23.685 12.120  1.00 88.44  ? 20  ARG B C   1 
ATOM   3102  O O   . ARG B 1 20  ? 16.476  -23.670 13.345  1.00 89.62  ? 20  ARG B O   1 
ATOM   3103  C CB  . ARG B 1 20  ? 19.060  -23.421 11.625  1.00 92.60  ? 20  ARG B CB  1 
ATOM   3104  C CG  . ARG B 1 20  ? 19.891  -23.356 10.353  1.00 101.86 ? 20  ARG B CG  1 
ATOM   3105  C CD  . ARG B 1 20  ? 21.378  -23.399 10.656  1.00 108.67 ? 20  ARG B CD  1 
ATOM   3106  N NE  . ARG B 1 20  ? 21.733  -22.547 11.787  1.00 110.96 ? 20  ARG B NE  1 
ATOM   3107  C CZ  . ARG B 1 20  ? 22.976  -22.350 12.212  1.00 112.07 ? 20  ARG B CZ  1 
ATOM   3108  N NH1 . ARG B 1 20  ? 23.992  -22.940 11.596  1.00 111.69 ? 20  ARG B NH1 1 
ATOM   3109  N NH2 . ARG B 1 20  ? 23.205  -21.560 13.252  1.00 110.40 ? 20  ARG B NH2 1 
ATOM   3110  N N   . PHE B 1 21  ? 15.765  -23.128 11.275  1.00 85.42  ? 21  PHE B N   1 
ATOM   3111  C CA  . PHE B 1 21  ? 14.524  -22.504 11.702  1.00 81.72  ? 21  PHE B CA  1 
ATOM   3112  C C   . PHE B 1 21  ? 13.367  -23.498 11.763  1.00 82.34  ? 21  PHE B C   1 
ATOM   3113  O O   . PHE B 1 21  ? 12.207  -23.078 11.695  1.00 84.32  ? 21  PHE B O   1 
ATOM   3114  C CB  . PHE B 1 21  ? 14.152  -21.357 10.755  1.00 81.41  ? 21  PHE B CB  1 
ATOM   3115  C CG  . PHE B 1 21  ? 15.112  -20.193 10.768  1.00 80.74  ? 21  PHE B CG  1 
ATOM   3116  C CD1 . PHE B 1 21  ? 14.708  -18.956 11.242  1.00 82.13  ? 21  PHE B CD1 1 
ATOM   3117  C CD2 . PHE B 1 21  ? 16.406  -20.327 10.284  1.00 87.18  ? 21  PHE B CD2 1 
ATOM   3118  C CE1 . PHE B 1 21  ? 15.575  -17.879 11.245  1.00 84.68  ? 21  PHE B CE1 1 
ATOM   3119  C CE2 . PHE B 1 21  ? 17.279  -19.254 10.287  1.00 92.08  ? 21  PHE B CE2 1 
ATOM   3120  C CZ  . PHE B 1 21  ? 16.863  -18.029 10.769  1.00 90.84  ? 21  PHE B CZ  1 
ATOM   3121  N N   . ARG B 1 22  ? 13.664  -24.803 11.884  1.00 80.88  ? 22  ARG B N   1 
ATOM   3122  C CA  . ARG B 1 22  ? 12.723  -25.918 11.739  1.00 82.81  ? 22  ARG B CA  1 
ATOM   3123  C C   . ARG B 1 22  ? 11.341  -25.643 12.332  1.00 87.45  ? 22  ARG B C   1 
ATOM   3124  O O   . ARG B 1 22  ? 10.342  -25.786 11.611  1.00 84.84  ? 22  ARG B O   1 
ATOM   3125  C CB  . ARG B 1 22  ? 13.309  -27.205 12.336  1.00 76.99  ? 22  ARG B CB  1 
ATOM   3126  C CG  . ARG B 1 22  ? 14.585  -27.657 11.666  1.00 77.44  ? 22  ARG B CG  1 
ATOM   3127  C CD  . ARG B 1 22  ? 14.389  -27.915 10.177  1.00 76.92  ? 22  ARG B CD  1 
ATOM   3128  N NE  . ARG B 1 22  ? 13.718  -29.178 9.887   1.00 73.81  ? 22  ARG B NE  1 
ATOM   3129  C CZ  . ARG B 1 22  ? 14.345  -30.268 9.450   1.00 71.22  ? 22  ARG B CZ  1 
ATOM   3130  N NH1 . ARG B 1 22  ? 15.657  -30.245 9.252   1.00 74.89  ? 22  ARG B NH1 1 
ATOM   3131  N NH2 . ARG B 1 22  ? 13.664  -31.380 9.205   1.00 74.40  ? 22  ARG B NH2 1 
ATOM   3132  N N   . PRO B 1 23  ? 11.217  -25.286 13.625  1.00 87.54  ? 23  PRO B N   1 
ATOM   3133  C CA  . PRO B 1 23  ? 9.865   -25.060 14.174  1.00 87.72  ? 23  PRO B CA  1 
ATOM   3134  C C   . PRO B 1 23  ? 9.066   -24.043 13.376  1.00 87.48  ? 23  PRO B C   1 
ATOM   3135  O O   . PRO B 1 23  ? 7.864   -24.231 13.149  1.00 88.36  ? 23  PRO B O   1 
ATOM   3136  C CB  . PRO B 1 23  ? 10.137  -24.579 15.606  1.00 78.60  ? 23  PRO B CB  1 
ATOM   3137  C CG  . PRO B 1 23  ? 11.551  -24.140 15.613  1.00 75.96  ? 23  PRO B CG  1 
ATOM   3138  C CD  . PRO B 1 23  ? 12.261  -24.999 14.628  1.00 76.69  ? 23  PRO B CD  1 
ATOM   3139  N N   . LEU B 1 24  ? 9.711   -22.961 12.946  1.00 80.54  ? 24  LEU B N   1 
ATOM   3140  C CA  . LEU B 1 24  ? 9.070   -21.970 12.096  1.00 78.14  ? 24  LEU B CA  1 
ATOM   3141  C C   . LEU B 1 24  ? 9.210   -22.297 10.617  1.00 79.42  ? 24  LEU B C   1 
ATOM   3142  O O   . LEU B 1 24  ? 8.332   -21.936 9.825   1.00 84.40  ? 24  LEU B O   1 
ATOM   3143  C CB  . LEU B 1 24  ? 9.646   -20.582 12.388  1.00 78.10  ? 24  LEU B CB  1 
ATOM   3144  C CG  . LEU B 1 24  ? 9.986   -20.344 13.862  1.00 76.70  ? 24  LEU B CG  1 
ATOM   3145  C CD1 . LEU B 1 24  ? 10.962  -19.189 14.021  1.00 79.42  ? 24  LEU B CD1 1 
ATOM   3146  C CD2 . LEU B 1 24  ? 8.725   -20.113 14.686  1.00 76.43  ? 24  LEU B CD2 1 
ATOM   3147  N N   . SER B 1 25  ? 10.298  -22.966 10.227  1.00 78.88  ? 25  SER B N   1 
ATOM   3148  C CA  . SER B 1 25  ? 10.494  -23.322 8.825   1.00 77.06  ? 25  SER B CA  1 
ATOM   3149  C C   . SER B 1 25  ? 9.415   -24.274 8.329   1.00 81.01  ? 25  SER B C   1 
ATOM   3150  O O   . SER B 1 25  ? 9.112   -24.298 7.130   1.00 86.98  ? 25  SER B O   1 
ATOM   3151  C CB  . SER B 1 25  ? 11.873  -23.950 8.634   1.00 79.71  ? 25  SER B CB  1 
ATOM   3152  O OG  . SER B 1 25  ? 12.840  -22.966 8.325   1.00 85.13  ? 25  SER B OG  1 
ATOM   3153  N N   . PHE B 1 26  ? 8.836   -25.071 9.229   1.00 82.81  ? 26  PHE B N   1 
ATOM   3154  C CA  . PHE B 1 26  ? 7.792   -26.007 8.827   1.00 86.02  ? 26  PHE B CA  1 
ATOM   3155  C C   . PHE B 1 26  ? 6.539   -25.297 8.329   1.00 89.21  ? 26  PHE B C   1 
ATOM   3156  O O   . PHE B 1 26  ? 5.853   -25.813 7.440   1.00 84.33  ? 26  PHE B O   1 
ATOM   3157  C CB  . PHE B 1 26  ? 7.458   -26.943 9.985   1.00 87.38  ? 26  PHE B CB  1 
ATOM   3158  C CG  . PHE B 1 26  ? 8.516   -27.972 10.245  1.00 82.44  ? 26  PHE B CG  1 
ATOM   3159  C CD1 . PHE B 1 26  ? 8.765   -28.420 11.530  1.00 82.42  ? 26  PHE B CD1 1 
ATOM   3160  C CD2 . PHE B 1 26  ? 9.256   -28.499 9.199   1.00 80.90  ? 26  PHE B CD2 1 
ATOM   3161  C CE1 . PHE B 1 26  ? 9.737   -29.369 11.770  1.00 80.87  ? 26  PHE B CE1 1 
ATOM   3162  C CE2 . PHE B 1 26  ? 10.230  -29.450 9.432   1.00 78.55  ? 26  PHE B CE2 1 
ATOM   3163  C CZ  . PHE B 1 26  ? 10.470  -29.885 10.719  1.00 78.00  ? 26  PHE B CZ  1 
ATOM   3164  N N   . ASN B 1 27  ? 6.221   -24.125 8.878   1.00 101.63 ? 27  ASN B N   1 
ATOM   3165  C CA  . ASN B 1 27  ? 5.066   -23.372 8.404   1.00 100.82 ? 27  ASN B CA  1 
ATOM   3166  C C   . ASN B 1 27  ? 5.440   -22.390 7.301   1.00 100.58 ? 27  ASN B C   1 
ATOM   3167  O O   . ASN B 1 27  ? 4.782   -22.344 6.257   1.00 101.92 ? 27  ASN B O   1 
ATOM   3168  C CB  . ASN B 1 27  ? 4.400   -22.621 9.562   1.00 101.10 ? 27  ASN B CB  1 
ATOM   3169  C CG  . ASN B 1 27  ? 3.147   -21.875 9.127   1.00 102.26 ? 27  ASN B CG  1 
ATOM   3170  O OD1 . ASN B 1 27  ? 2.087   -22.474 8.944   1.00 102.50 ? 27  ASN B OD1 1 
ATOM   3171  N ND2 . ASN B 1 27  ? 3.267   -20.563 8.956   1.00 102.04 ? 27  ASN B ND2 1 
ATOM   3172  N N   . THR B 1 28  ? 6.491   -21.602 7.517   1.00 86.15  ? 28  THR B N   1 
ATOM   3173  C CA  . THR B 1 28  ? 6.905   -20.576 6.576   1.00 80.58  ? 28  THR B CA  1 
ATOM   3174  C C   . THR B 1 28  ? 8.411   -20.685 6.366   1.00 79.22  ? 28  THR B C   1 
ATOM   3175  O O   . THR B 1 28  ? 9.170   -20.749 7.349   1.00 80.71  ? 28  THR B O   1 
ATOM   3176  C CB  . THR B 1 28  ? 6.522   -19.181 7.093   1.00 80.19  ? 28  THR B CB  1 
ATOM   3177  O OG1 . THR B 1 28  ? 5.099   -19.018 7.020   1.00 86.26  ? 28  THR B OG1 1 
ATOM   3178  C CG2 . THR B 1 28  ? 7.187   -18.100 6.268   1.00 73.42  ? 28  THR B CG2 1 
ATOM   3179  N N   . PRO B 1 29  ? 8.884   -20.714 5.119   1.00 74.19  ? 29  PRO B N   1 
ATOM   3180  C CA  . PRO B 1 29  ? 10.327  -20.825 4.874   1.00 72.90  ? 29  PRO B CA  1 
ATOM   3181  C C   . PRO B 1 29  ? 11.105  -19.670 5.488   1.00 81.06  ? 29  PRO B C   1 
ATOM   3182  O O   . PRO B 1 29  ? 10.556  -18.619 5.824   1.00 66.04  ? 29  PRO B O   1 
ATOM   3183  C CB  . PRO B 1 29  ? 10.430  -20.806 3.345   1.00 75.09  ? 29  PRO B CB  1 
ATOM   3184  C CG  . PRO B 1 29  ? 9.102   -21.273 2.872   1.00 77.48  ? 29  PRO B CG  1 
ATOM   3185  C CD  . PRO B 1 29  ? 8.109   -20.748 3.868   1.00 79.37  ? 29  PRO B CD  1 
ATOM   3186  N N   . LYS B 1 30  ? 12.414  -19.887 5.620   1.00 66.89  ? 30  LYS B N   1 
ATOM   3187  C CA  . LYS B 1 30  ? 13.311  -18.909 6.237   1.00 64.02  ? 30  LYS B CA  1 
ATOM   3188  C C   . LYS B 1 30  ? 13.190  -17.503 5.659   1.00 65.64  ? 30  LYS B C   1 
ATOM   3189  O O   . LYS B 1 30  ? 13.033  -16.554 6.445   1.00 62.61  ? 30  LYS B O   1 
ATOM   3190  C CB  . LYS B 1 30  ? 14.754  -19.422 6.131   1.00 69.57  ? 30  LYS B CB  1 
ATOM   3191  C CG  . LYS B 1 30  ? 15.801  -18.462 6.661   1.00 72.39  ? 30  LYS B CG  1 
ATOM   3192  C CD  . LYS B 1 30  ? 17.006  -18.407 5.737   1.00 75.90  ? 30  LYS B CD  1 
ATOM   3193  C CE  . LYS B 1 30  ? 18.308  -18.487 6.514   1.00 84.08  ? 30  LYS B CE  1 
ATOM   3194  N NZ  . LYS B 1 30  ? 18.452  -19.796 7.208   1.00 96.36  ? 30  LYS B NZ  1 
ATOM   3195  N N   . PRO B 1 31  ? 13.249  -17.285 4.338   1.00 60.15  ? 31  PRO B N   1 
ATOM   3196  C CA  . PRO B 1 31  ? 13.236  -15.901 3.834   1.00 61.27  ? 31  PRO B CA  1 
ATOM   3197  C C   . PRO B 1 31  ? 11.930  -15.171 4.088   1.00 82.85  ? 31  PRO B C   1 
ATOM   3198  O O   . PRO B 1 31  ? 11.911  -13.935 4.034   1.00 71.74  ? 31  PRO B O   1 
ATOM   3199  C CB  . PRO B 1 31  ? 13.492  -16.067 2.328   1.00 60.99  ? 31  PRO B CB  1 
ATOM   3200  C CG  . PRO B 1 31  ? 14.039  -17.450 2.173   1.00 61.80  ? 31  PRO B CG  1 
ATOM   3201  C CD  . PRO B 1 31  ? 13.361  -18.250 3.229   1.00 62.22  ? 31  PRO B CD  1 
ATOM   3202  N N   . LEU B 1 32  ? 10.839  -15.887 4.344   1.00 60.52  ? 32  LEU B N   1 
ATOM   3203  C CA  . LEU B 1 32  ? 9.529   -15.277 4.496   1.00 60.72  ? 32  LEU B CA  1 
ATOM   3204  C C   . LEU B 1 32  ? 9.104   -15.123 5.951   1.00 64.01  ? 32  LEU B C   1 
ATOM   3205  O O   . LEU B 1 32  ? 7.977   -14.690 6.208   1.00 71.95  ? 32  LEU B O   1 
ATOM   3206  C CB  . LEU B 1 32  ? 8.493   -16.103 3.730   1.00 68.78  ? 32  LEU B CB  1 
ATOM   3207  C CG  . LEU B 1 32  ? 8.953   -16.605 2.360   1.00 61.93  ? 32  LEU B CG  1 
ATOM   3208  C CD1 . LEU B 1 32  ? 7.891   -17.491 1.734   1.00 67.85  ? 32  LEU B CD1 1 
ATOM   3209  C CD2 . LEU B 1 32  ? 9.306   -15.447 1.432   1.00 61.87  ? 32  LEU B CD2 1 
ATOM   3210  N N   . ILE B 1 33  ? 9.966   -15.464 6.900   1.00 61.99  ? 33  ILE B N   1 
ATOM   3211  C CA  . ILE B 1 33  ? 9.624   -15.350 8.321   1.00 68.78  ? 33  ILE B CA  1 
ATOM   3212  C C   . ILE B 1 33  ? 9.699   -13.880 8.731   1.00 68.26  ? 33  ILE B C   1 
ATOM   3213  O O   . ILE B 1 33  ? 10.718  -13.224 8.465   1.00 71.10  ? 33  ILE B O   1 
ATOM   3214  C CB  . ILE B 1 33  ? 10.554  -16.212 9.171   1.00 67.80  ? 33  ILE B CB  1 
ATOM   3215  C CG1 . ILE B 1 33  ? 10.357  -17.692 8.829   1.00 66.03  ? 33  ILE B CG1 1 
ATOM   3216  C CG2 . ILE B 1 33  ? 10.294  -15.976 10.654  1.00 68.37  ? 33  ILE B CG2 1 
ATOM   3217  C CD1 . ILE B 1 33  ? 11.264  -18.639 9.591   1.00 67.31  ? 33  ILE B CD1 1 
ATOM   3218  N N   . PRO B 1 34  ? 8.666   -13.338 9.379   1.00 66.61  ? 34  PRO B N   1 
ATOM   3219  C CA  . PRO B 1 34  ? 8.597   -11.885 9.619   1.00 71.39  ? 34  PRO B CA  1 
ATOM   3220  C C   . PRO B 1 34  ? 9.673   -11.391 10.577  1.00 77.50  ? 34  PRO B C   1 
ATOM   3221  O O   . PRO B 1 34  ? 9.716   -11.784 11.744  1.00 78.63  ? 34  PRO B O   1 
ATOM   3222  C CB  . PRO B 1 34  ? 7.194   -11.689 10.207  1.00 74.96  ? 34  PRO B CB  1 
ATOM   3223  C CG  . PRO B 1 34  ? 6.436   -12.917 9.824   1.00 76.20  ? 34  PRO B CG  1 
ATOM   3224  C CD  . PRO B 1 34  ? 7.440   -14.022 9.819   1.00 72.55  ? 34  PRO B CD  1 
ATOM   3225  N N   . LEU B 1 35  ? 10.543  -10.521 10.069  1.00 88.36  ? 35  LEU B N   1 
ATOM   3226  C CA  . LEU B 1 35  ? 11.532  -9.815  10.875  1.00 90.16  ? 35  LEU B CA  1 
ATOM   3227  C C   . LEU B 1 35  ? 11.059  -8.380  11.082  1.00 90.75  ? 35  LEU B C   1 
ATOM   3228  O O   . LEU B 1 35  ? 10.836  -7.653  10.109  1.00 90.14  ? 35  LEU B O   1 
ATOM   3229  C CB  . LEU B 1 35  ? 12.900  -9.836  10.195  1.00 90.99  ? 35  LEU B CB  1 
ATOM   3230  C CG  . LEU B 1 35  ? 13.623  -11.181 10.126  1.00 91.15  ? 35  LEU B CG  1 
ATOM   3231  C CD1 . LEU B 1 35  ? 15.010  -10.999 9.538   1.00 93.21  ? 35  LEU B CD1 1 
ATOM   3232  C CD2 . LEU B 1 35  ? 13.705  -11.816 11.505  1.00 94.40  ? 35  LEU B CD2 1 
ATOM   3233  N N   . ALA B 1 36  ? 10.905  -7.980  12.345  1.00 84.02  ? 36  ALA B N   1 
ATOM   3234  C CA  . ALA B 1 36  ? 10.410  -6.646  12.696  1.00 78.41  ? 36  ALA B CA  1 
ATOM   3235  C C   . ALA B 1 36  ? 9.058   -6.358  12.046  1.00 80.18  ? 36  ALA B C   1 
ATOM   3236  O O   . ALA B 1 36  ? 8.765   -5.226  11.655  1.00 83.27  ? 36  ALA B O   1 
ATOM   3237  C CB  . ALA B 1 36  ? 11.430  -5.562  12.336  1.00 75.88  ? 36  ALA B CB  1 
ATOM   3238  N N   . GLY B 1 37  ? 8.223   -7.393  11.930  1.00 78.87  ? 37  GLY B N   1 
ATOM   3239  C CA  . GLY B 1 37  ? 6.900   -7.287  11.359  1.00 74.69  ? 37  GLY B CA  1 
ATOM   3240  C C   . GLY B 1 37  ? 6.820   -7.670  9.894   1.00 78.41  ? 37  GLY B C   1 
ATOM   3241  O O   . GLY B 1 37  ? 5.760   -8.110  9.434   1.00 73.56  ? 37  GLY B O   1 
ATOM   3242  N N   . GLN B 1 38  ? 7.913   -7.508  9.153   1.00 74.51  ? 38  GLN B N   1 
ATOM   3243  C CA  . GLN B 1 38  ? 8.005   -7.819  7.736   1.00 71.30  ? 38  GLN B CA  1 
ATOM   3244  C C   . GLN B 1 38  ? 8.878   -9.048  7.516   1.00 110.85 ? 38  GLN B C   1 
ATOM   3245  O O   . GLN B 1 38  ? 9.785   -9.316  8.308   1.00 83.47  ? 38  GLN B O   1 
ATOM   3246  C CB  . GLN B 1 38  ? 8.594   -6.643  6.946   1.00 76.41  ? 38  GLN B CB  1 
ATOM   3247  C CG  . GLN B 1 38  ? 7.882   -5.318  7.141   1.00 76.56  ? 38  GLN B CG  1 
ATOM   3248  C CD  . GLN B 1 38  ? 6.443   -5.347  6.663   1.00 70.46  ? 38  GLN B CD  1 
ATOM   3249  O OE1 . GLN B 1 38  ? 6.072   -6.165  5.820   1.00 69.24  ? 38  GLN B OE1 1 
ATOM   3250  N NE2 . GLN B 1 38  ? 5.627   -4.444  7.192   1.00 75.31  ? 38  GLN B NE2 1 
ATOM   3251  N N   . PRO B 1 39  ? 8.630   -9.817  6.457   1.00 63.20  ? 39  PRO B N   1 
ATOM   3252  C CA  . PRO B 1 39  ? 9.455   -11.002 6.190   1.00 82.30  ? 39  PRO B CA  1 
ATOM   3253  C C   . PRO B 1 39  ? 10.933  -10.656 6.084   1.00 62.49  ? 39  PRO B C   1 
ATOM   3254  O O   . PRO B 1 39  ? 11.334  -9.495  5.964   1.00 87.56  ? 39  PRO B O   1 
ATOM   3255  C CB  . PRO B 1 39  ? 8.902   -11.524 4.863   1.00 64.45  ? 39  PRO B CB  1 
ATOM   3256  C CG  . PRO B 1 39  ? 7.479   -11.086 4.872   1.00 74.55  ? 39  PRO B CG  1 
ATOM   3257  C CD  . PRO B 1 39  ? 7.468   -9.742  5.555   1.00 74.80  ? 39  PRO B CD  1 
ATOM   3258  N N   . MET B 1 40  ? 11.756  -11.706 6.133   1.00 65.61  ? 40  MET B N   1 
ATOM   3259  C CA  . MET B 1 40  ? 13.204  -11.524 6.170   1.00 70.14  ? 40  MET B CA  1 
ATOM   3260  C C   . MET B 1 40  ? 13.691  -10.731 4.963   1.00 70.26  ? 40  MET B C   1 
ATOM   3261  O O   . MET B 1 40  ? 14.407  -9.733  5.108   1.00 77.16  ? 40  MET B O   1 
ATOM   3262  C CB  . MET B 1 40  ? 13.893  -12.887 6.228   1.00 67.99  ? 40  MET B CB  1 
ATOM   3263  C CG  . MET B 1 40  ? 15.405  -12.822 6.291   1.00 72.38  ? 40  MET B CG  1 
ATOM   3264  S SD  . MET B 1 40  ? 16.135  -14.457 6.493   1.00 79.91  ? 40  MET B SD  1 
ATOM   3265  C CE  . MET B 1 40  ? 15.389  -14.970 8.040   1.00 79.29  ? 40  MET B CE  1 
ATOM   3266  N N   . ILE B 1 41  ? 13.299  -11.155 3.757   1.00 75.87  ? 41  ILE B N   1 
ATOM   3267  C CA  . ILE B 1 41  ? 13.720  -10.468 2.537   1.00 66.96  ? 41  ILE B CA  1 
ATOM   3268  C C   . ILE B 1 41  ? 12.931  -9.202  2.260   1.00 82.05  ? 41  ILE B C   1 
ATOM   3269  O O   . ILE B 1 41  ? 13.220  -8.508  1.276   1.00 70.80  ? 41  ILE B O   1 
ATOM   3270  C CB  . ILE B 1 41  ? 13.608  -11.401 1.317   1.00 62.34  ? 41  ILE B CB  1 
ATOM   3271  C CG1 . ILE B 1 41  ? 12.187  -11.945 1.203   1.00 63.97  ? 41  ILE B CG1 1 
ATOM   3272  C CG2 . ILE B 1 41  ? 14.603  -12.536 1.431   1.00 71.38  ? 41  ILE B CG2 1 
ATOM   3273  C CD1 . ILE B 1 41  ? 12.007  -12.895 0.053   1.00 67.11  ? 41  ILE B CD1 1 
ATOM   3274  N N   . HIS B 1 42  ? 11.939  -8.878  3.089   1.00 77.30  ? 42  HIS B N   1 
ATOM   3275  C CA  . HIS B 1 42  ? 11.147  -7.677  2.866   1.00 79.75  ? 42  HIS B CA  1 
ATOM   3276  C C   . HIS B 1 42  ? 11.942  -6.405  3.120   1.00 83.53  ? 42  HIS B C   1 
ATOM   3277  O O   . HIS B 1 42  ? 11.502  -5.321  2.720   1.00 86.98  ? 42  HIS B O   1 
ATOM   3278  C CB  . HIS B 1 42  ? 9.907   -7.700  3.757   1.00 80.69  ? 42  HIS B CB  1 
ATOM   3279  C CG  . HIS B 1 42  ? 8.835   -6.750  3.326   1.00 84.28  ? 42  HIS B CG  1 
ATOM   3280  N ND1 . HIS B 1 42  ? 7.855   -7.097  2.421   1.00 85.58  ? 42  HIS B ND1 1 
ATOM   3281  C CD2 . HIS B 1 42  ? 8.591   -5.464  3.671   1.00 86.35  ? 42  HIS B CD2 1 
ATOM   3282  C CE1 . HIS B 1 42  ? 7.051   -6.067  2.231   1.00 91.40  ? 42  HIS B CE1 1 
ATOM   3283  N NE2 . HIS B 1 42  ? 7.476   -5.063  2.977   1.00 94.34  ? 42  HIS B NE2 1 
ATOM   3284  N N   . HIS B 1 43  ? 13.096  -6.509  3.769   1.00 74.15  ? 43  HIS B N   1 
ATOM   3285  C CA  . HIS B 1 43  ? 13.914  -5.336  4.043   1.00 80.04  ? 43  HIS B CA  1 
ATOM   3286  C C   . HIS B 1 43  ? 14.882  -5.072  2.892   1.00 86.78  ? 43  HIS B C   1 
ATOM   3287  O O   . HIS B 1 43  ? 15.074  -3.908  2.516   1.00 91.02  ? 43  HIS B O   1 
ATOM   3288  C CB  . HIS B 1 43  ? 14.681  -5.507  5.355   1.00 76.45  ? 43  HIS B CB  1 
ATOM   3289  C CG  . HIS B 1 43  ? 13.806  -5.817  6.525   1.00 75.07  ? 43  HIS B CG  1 
ATOM   3290  N ND1 . HIS B 1 43  ? 13.114  -7.003  6.638   1.00 76.65  ? 43  HIS B ND1 1 
ATOM   3291  C CD2 . HIS B 1 43  ? 13.489  -5.090  7.622   1.00 79.42  ? 43  HIS B CD2 1 
ATOM   3292  C CE1 . HIS B 1 43  ? 12.419  -6.999  7.760   1.00 74.99  ? 43  HIS B CE1 1 
ATOM   3293  N NE2 . HIS B 1 43  ? 12.629  -5.850  8.376   1.00 79.05  ? 43  HIS B NE2 1 
ATOM   3294  N N   . PRO B 1 44  ? 15.527  -6.099  2.320   1.00 78.90  ? 44  PRO B N   1 
ATOM   3295  C CA  . PRO B 1 44  ? 16.315  -5.852  1.098   1.00 85.04  ? 44  PRO B CA  1 
ATOM   3296  C C   . PRO B 1 44  ? 15.491  -5.292  -0.051  1.00 89.88  ? 44  PRO B C   1 
ATOM   3297  O O   . PRO B 1 44  ? 15.913  -4.326  -0.700  1.00 93.07  ? 44  PRO B O   1 
ATOM   3298  C CB  . PRO B 1 44  ? 16.893  -7.236  0.778   1.00 82.16  ? 44  PRO B CB  1 
ATOM   3299  C CG  . PRO B 1 44  ? 16.992  -7.903  2.093   1.00 75.87  ? 44  PRO B CG  1 
ATOM   3300  C CD  . PRO B 1 44  ? 15.795  -7.445  2.863   1.00 77.02  ? 44  PRO B CD  1 
ATOM   3301  N N   . ILE B 1 45  ? 14.326  -5.882  -0.332  1.00 91.66  ? 45  ILE B N   1 
ATOM   3302  C CA  . ILE B 1 45  ? 13.483  -5.385  -1.416  1.00 89.64  ? 45  ILE B CA  1 
ATOM   3303  C C   . ILE B 1 45  ? 13.034  -3.957  -1.141  1.00 101.18 ? 45  ILE B C   1 
ATOM   3304  O O   . ILE B 1 45  ? 12.860  -3.161  -2.073  1.00 104.72 ? 45  ILE B O   1 
ATOM   3305  C CB  . ILE B 1 45  ? 12.286  -6.328  -1.641  1.00 79.89  ? 45  ILE B CB  1 
ATOM   3306  C CG1 . ILE B 1 45  ? 12.781  -7.744  -1.917  1.00 73.39  ? 45  ILE B CG1 1 
ATOM   3307  C CG2 . ILE B 1 45  ? 11.437  -5.851  -2.809  1.00 97.59  ? 45  ILE B CG2 1 
ATOM   3308  C CD1 . ILE B 1 45  ? 11.671  -8.745  -2.068  1.00 71.61  ? 45  ILE B CD1 1 
ATOM   3309  N N   . SER B 1 46  ? 12.836  -3.610  0.133   1.00 125.53 ? 46  SER B N   1 
ATOM   3310  C CA  . SER B 1 46  ? 12.430  -2.252  0.478   1.00 126.86 ? 46  SER B CA  1 
ATOM   3311  C C   . SER B 1 46  ? 13.492  -1.233  0.088   1.00 128.12 ? 46  SER B C   1 
ATOM   3312  O O   . SER B 1 46  ? 13.167  -0.074  -0.192  1.00 129.73 ? 46  SER B O   1 
ATOM   3313  C CB  . SER B 1 46  ? 12.138  -2.164  1.977   1.00 126.07 ? 46  SER B CB  1 
ATOM   3314  O OG  . SER B 1 46  ? 10.895  -2.770  2.292   1.00 125.75 ? 46  SER B OG  1 
ATOM   3315  N N   . ALA B 1 47  ? 14.761  -1.641  0.066   1.00 103.96 ? 47  ALA B N   1 
ATOM   3316  C CA  . ALA B 1 47  ? 15.840  -0.737  -0.305  1.00 102.23 ? 47  ALA B CA  1 
ATOM   3317  C C   . ALA B 1 47  ? 16.023  -0.614  -1.812  1.00 98.35  ? 47  ALA B C   1 
ATOM   3318  O O   . ALA B 1 47  ? 16.721  0.303   -2.257  1.00 96.29  ? 47  ALA B O   1 
ATOM   3319  C CB  . ALA B 1 47  ? 17.154  -1.193  0.337   1.00 96.76  ? 47  ALA B CB  1 
ATOM   3320  N N   . CYS B 1 48  ? 15.415  -1.500  -2.605  1.00 95.28  ? 48  CYS B N   1 
ATOM   3321  C CA  . CYS B 1 48  ? 15.566  -1.441  -4.054  1.00 92.97  ? 48  CYS B CA  1 
ATOM   3322  C C   . CYS B 1 48  ? 14.761  -0.322  -4.700  1.00 89.45  ? 48  CYS B C   1 
ATOM   3323  O O   . CYS B 1 48  ? 15.122  0.126   -5.794  1.00 88.09  ? 48  CYS B O   1 
ATOM   3324  C CB  . CYS B 1 48  ? 15.167  -2.777  -4.684  1.00 93.93  ? 48  CYS B CB  1 
ATOM   3325  S SG  . CYS B 1 48  ? 16.240  -4.151  -4.226  1.00 92.75  ? 48  CYS B SG  1 
ATOM   3326  N N   . LYS B 1 49  ? 13.685  0.139   -4.058  1.00 93.64  ? 49  LYS B N   1 
ATOM   3327  C CA  . LYS B 1 49  ? 12.874  1.194   -4.652  1.00 95.88  ? 49  LYS B CA  1 
ATOM   3328  C C   . LYS B 1 49  ? 13.587  2.539   -4.646  1.00 92.96  ? 49  LYS B C   1 
ATOM   3329  O O   . LYS B 1 49  ? 13.265  3.402   -5.469  1.00 94.32  ? 49  LYS B O   1 
ATOM   3330  C CB  . LYS B 1 49  ? 11.527  1.299   -3.928  1.00 103.20 ? 49  LYS B CB  1 
ATOM   3331  C CG  . LYS B 1 49  ? 10.511  2.183   -4.642  1.00 106.46 ? 49  LYS B CG  1 
ATOM   3332  C CD  . LYS B 1 49  ? 10.478  1.869   -6.131  1.00 113.10 ? 49  LYS B CD  1 
ATOM   3333  C CE  . LYS B 1 49  ? 9.723   2.930   -6.915  1.00 118.37 ? 49  LYS B CE  1 
ATOM   3334  N NZ  . LYS B 1 49  ? 8.894   2.345   -8.007  1.00 128.48 ? 49  LYS B NZ  1 
ATOM   3335  N N   . LYS B 1 50  ? 14.555  2.735   -3.748  1.00 89.24  ? 50  LYS B N   1 
ATOM   3336  C CA  . LYS B 1 50  ? 15.284  3.995   -3.710  1.00 88.23  ? 50  LYS B CA  1 
ATOM   3337  C C   . LYS B 1 50  ? 16.196  4.182   -4.917  1.00 91.42  ? 50  LYS B C   1 
ATOM   3338  O O   . LYS B 1 50  ? 16.690  5.295   -5.128  1.00 95.67  ? 50  LYS B O   1 
ATOM   3339  C CB  . LYS B 1 50  ? 16.101  4.094   -2.420  1.00 92.69  ? 50  LYS B CB  1 
ATOM   3340  C CG  . LYS B 1 50  ? 17.480  3.461   -2.512  1.00 101.94 ? 50  LYS B CG  1 
ATOM   3341  C CD  . LYS B 1 50  ? 18.376  3.903   -1.363  1.00 106.07 ? 50  LYS B CD  1 
ATOM   3342  C CE  . LYS B 1 50  ? 19.404  2.835   -1.017  1.00 100.69 ? 50  LYS B CE  1 
ATOM   3343  N NZ  . LYS B 1 50  ? 18.763  1.532   -0.685  1.00 96.24  ? 50  LYS B NZ  1 
ATOM   3344  N N   . ILE B 1 51  ? 16.426  3.138   -5.709  1.00 90.05  ? 51  ILE B N   1 
ATOM   3345  C CA  . ILE B 1 51  ? 17.188  3.249   -6.947  1.00 88.91  ? 51  ILE B CA  1 
ATOM   3346  C C   . ILE B 1 51  ? 16.193  3.500   -8.073  1.00 85.50  ? 51  ILE B C   1 
ATOM   3347  O O   . ILE B 1 51  ? 15.454  2.598   -8.474  1.00 82.13  ? 51  ILE B O   1 
ATOM   3348  C CB  . ILE B 1 51  ? 18.028  1.994   -7.210  1.00 92.21  ? 51  ILE B CB  1 
ATOM   3349  C CG1 . ILE B 1 51  ? 18.984  1.735   -6.045  1.00 91.69  ? 51  ILE B CG1 1 
ATOM   3350  C CG2 . ILE B 1 51  ? 18.803  2.133   -8.511  1.00 90.82  ? 51  ILE B CG2 1 
ATOM   3351  C CD1 . ILE B 1 51  ? 18.465  0.734   -5.036  1.00 88.58  ? 51  ILE B CD1 1 
ATOM   3352  N N   . SER B 1 52  ? 16.172  4.734   -8.584  1.00 80.48  ? 52  SER B N   1 
ATOM   3353  C CA  . SER B 1 52  ? 15.184  5.102   -9.593  1.00 83.96  ? 52  SER B CA  1 
ATOM   3354  C C   . SER B 1 52  ? 15.445  4.427   -10.935 1.00 82.83  ? 52  SER B C   1 
ATOM   3355  O O   . SER B 1 52  ? 14.504  4.207   -11.706 1.00 85.25  ? 52  SER B O   1 
ATOM   3356  C CB  . SER B 1 52  ? 15.151  6.621   -9.762  1.00 87.22  ? 52  SER B CB  1 
ATOM   3357  O OG  . SER B 1 52  ? 16.419  7.114   -10.158 1.00 91.63  ? 52  SER B OG  1 
ATOM   3358  N N   . ASN B 1 53  ? 16.697  4.084   -11.234 1.00 83.53  ? 53  ASN B N   1 
ATOM   3359  C CA  . ASN B 1 53  ? 17.028  3.422   -12.488 1.00 84.25  ? 53  ASN B CA  1 
ATOM   3360  C C   . ASN B 1 53  ? 17.039  1.904   -12.357 1.00 84.93  ? 53  ASN B C   1 
ATOM   3361  O O   . ASN B 1 53  ? 17.619  1.220   -13.208 1.00 87.56  ? 53  ASN B O   1 
ATOM   3362  C CB  . ASN B 1 53  ? 18.377  3.915   -13.015 1.00 86.18  ? 53  ASN B CB  1 
ATOM   3363  C CG  . ASN B 1 53  ? 19.415  4.042   -11.924 1.00 84.10  ? 53  ASN B CG  1 
ATOM   3364  O OD1 . ASN B 1 53  ? 19.136  4.556   -10.841 1.00 83.59  ? 53  ASN B OD1 1 
ATOM   3365  N ND2 . ASN B 1 53  ? 20.625  3.579   -12.207 1.00 83.85  ? 53  ASN B ND2 1 
ATOM   3366  N N   . LEU B 1 54  ? 16.411  1.367   -11.316 1.00 96.95  ? 54  LEU B N   1 
ATOM   3367  C CA  . LEU B 1 54  ? 16.296  -0.070  -11.131 1.00 95.51  ? 54  LEU B CA  1 
ATOM   3368  C C   . LEU B 1 54  ? 14.974  -0.563  -11.706 1.00 97.65  ? 54  LEU B C   1 
ATOM   3369  O O   . LEU B 1 54  ? 13.962  0.142   -11.679 1.00 104.60 ? 54  LEU B O   1 
ATOM   3370  C CB  . LEU B 1 54  ? 16.392  -0.430  -9.647  1.00 93.90  ? 54  LEU B CB  1 
ATOM   3371  C CG  . LEU B 1 54  ? 16.795  -1.861  -9.287  1.00 91.83  ? 54  LEU B CG  1 
ATOM   3372  C CD1 . LEU B 1 54  ? 17.709  -1.863  -8.070  1.00 89.71  ? 54  LEU B CD1 1 
ATOM   3373  C CD2 . LEU B 1 54  ? 15.564  -2.713  -9.030  1.00 92.94  ? 54  LEU B CD2 1 
ATOM   3374  N N   . ALA B 1 55  ? 14.991  -1.789  -12.231 1.00 87.53  ? 55  ALA B N   1 
ATOM   3375  C CA  . ALA B 1 55  ? 13.804  -2.350  -12.863 1.00 86.46  ? 55  ALA B CA  1 
ATOM   3376  C C   . ALA B 1 55  ? 13.443  -3.715  -12.290 1.00 88.08  ? 55  ALA B C   1 
ATOM   3377  O O   . ALA B 1 55  ? 12.848  -3.806  -11.211 1.00 101.59 ? 55  ALA B O   1 
ATOM   3378  C CB  . ALA B 1 55  ? 14.006  -2.457  -14.375 1.00 86.62  ? 55  ALA B CB  1 
ATOM   3379  N N   . GLN B 1 56  ? 13.792  -4.778  -13.009 1.00 82.62  ? 56  GLN B N   1 
ATOM   3380  C CA  . GLN B 1 56  ? 13.401  -6.122  -12.609 1.00 79.75  ? 56  GLN B CA  1 
ATOM   3381  C C   . GLN B 1 56  ? 14.129  -6.557  -11.342 1.00 77.16  ? 56  GLN B C   1 
ATOM   3382  O O   . GLN B 1 56  ? 15.260  -6.146  -11.073 1.00 78.50  ? 56  GLN B O   1 
ATOM   3383  C CB  . GLN B 1 56  ? 13.682  -7.117  -13.734 1.00 74.38  ? 56  GLN B CB  1 
ATOM   3384  N N   . ILE B 1 57  ? 13.457  -7.396  -10.558 1.00 79.64  ? 57  ILE B N   1 
ATOM   3385  C CA  . ILE B 1 57  ? 14.024  -7.995  -9.357  1.00 77.21  ? 57  ILE B CA  1 
ATOM   3386  C C   . ILE B 1 57  ? 13.877  -9.505  -9.466  1.00 85.59  ? 57  ILE B C   1 
ATOM   3387  O O   . ILE B 1 57  ? 12.843  -10.007 -9.922  1.00 86.61  ? 57  ILE B O   1 
ATOM   3388  C CB  . ILE B 1 57  ? 13.344  -7.464  -8.079  1.00 79.22  ? 57  ILE B CB  1 
ATOM   3389  C CG1 . ILE B 1 57  ? 13.340  -5.932  -8.081  1.00 89.98  ? 57  ILE B CG1 1 
ATOM   3390  C CG2 . ILE B 1 57  ? 14.036  -8.011  -6.842  1.00 76.72  ? 57  ILE B CG2 1 
ATOM   3391  C CD1 . ILE B 1 57  ? 13.045  -5.325  -6.733  1.00 107.47 ? 57  ILE B CD1 1 
ATOM   3392  N N   . PHE B 1 58  ? 14.910  -10.230 -9.042  1.00 92.73  ? 58  PHE B N   1 
ATOM   3393  C CA  . PHE B 1 58  ? 15.000  -11.670 -9.252  1.00 91.66  ? 58  PHE B CA  1 
ATOM   3394  C C   . PHE B 1 58  ? 15.298  -12.362 -7.932  1.00 89.67  ? 58  PHE B C   1 
ATOM   3395  O O   . PHE B 1 58  ? 16.318  -12.076 -7.296  1.00 91.46  ? 58  PHE B O   1 
ATOM   3396  C CB  . PHE B 1 58  ? 16.085  -12.005 -10.280 1.00 92.80  ? 58  PHE B CB  1 
ATOM   3397  C CG  . PHE B 1 58  ? 15.734  -11.609 -11.684 1.00 97.37  ? 58  PHE B CG  1 
ATOM   3398  C CD1 . PHE B 1 58  ? 15.039  -12.478 -12.511 1.00 106.42 ? 58  PHE B CD1 1 
ATOM   3399  C CD2 . PHE B 1 58  ? 16.089  -10.366 -12.174 1.00 98.71  ? 58  PHE B CD2 1 
ATOM   3400  C CE1 . PHE B 1 58  ? 14.715  -12.112 -13.806 1.00 113.02 ? 58  PHE B CE1 1 
ATOM   3401  C CE2 . PHE B 1 58  ? 15.766  -9.995  -13.465 1.00 103.35 ? 58  PHE B CE2 1 
ATOM   3402  C CZ  . PHE B 1 58  ? 15.079  -10.868 -14.282 1.00 110.81 ? 58  PHE B CZ  1 
ATOM   3403  N N   . LEU B 1 59  ? 14.409  -13.259 -7.520  1.00 83.75  ? 59  LEU B N   1 
ATOM   3404  C CA  . LEU B 1 59  ? 14.626  -14.124 -6.368  1.00 82.48  ? 59  LEU B CA  1 
ATOM   3405  C C   . LEU B 1 59  ? 14.910  -15.529 -6.879  1.00 84.06  ? 59  LEU B C   1 
ATOM   3406  O O   . LEU B 1 59  ? 14.051  -16.143 -7.520  1.00 89.82  ? 59  LEU B O   1 
ATOM   3407  C CB  . LEU B 1 59  ? 13.411  -14.123 -5.438  1.00 78.60  ? 59  LEU B CB  1 
ATOM   3408  C CG  . LEU B 1 59  ? 12.812  -12.764 -5.074  1.00 76.05  ? 59  LEU B CG  1 
ATOM   3409  C CD1 . LEU B 1 59  ? 11.534  -12.938 -4.264  1.00 74.84  ? 59  LEU B CD1 1 
ATOM   3410  C CD2 . LEU B 1 59  ? 13.823  -11.918 -4.316  1.00 72.61  ? 59  LEU B CD2 1 
ATOM   3411  N N   . ILE B 1 60  ? 16.107  -16.038 -6.597  1.00 81.23  ? 60  ILE B N   1 
ATOM   3412  C CA  . ILE B 1 60  ? 16.523  -17.347 -7.080  1.00 81.14  ? 60  ILE B CA  1 
ATOM   3413  C C   . ILE B 1 60  ? 16.827  -18.243 -5.888  1.00 80.71  ? 60  ILE B C   1 
ATOM   3414  O O   . ILE B 1 60  ? 17.387  -17.795 -4.881  1.00 73.34  ? 60  ILE B O   1 
ATOM   3415  C CB  . ILE B 1 60  ? 17.735  -17.253 -8.034  1.00 87.16  ? 60  ILE B CB  1 
ATOM   3416  C CG1 . ILE B 1 60  ? 18.946  -16.624 -7.342  1.00 87.25  ? 60  ILE B CG1 1 
ATOM   3417  C CG2 . ILE B 1 60  ? 17.367  -16.458 -9.283  1.00 95.08  ? 60  ILE B CG2 1 
ATOM   3418  C CD1 . ILE B 1 60  ? 20.170  -16.546 -8.230  1.00 93.93  ? 60  ILE B CD1 1 
ATOM   3419  N N   . GLY B 1 61  ? 16.458  -19.513 -6.015  1.00 83.06  ? 61  GLY B N   1 
ATOM   3420  C CA  . GLY B 1 61  ? 16.645  -20.500 -4.973  1.00 83.64  ? 61  GLY B CA  1 
ATOM   3421  C C   . GLY B 1 61  ? 15.796  -21.718 -5.272  1.00 91.00  ? 61  GLY B C   1 
ATOM   3422  O O   . GLY B 1 61  ? 14.754  -21.601 -5.924  1.00 92.25  ? 61  GLY B O   1 
ATOM   3423  N N   . PHE B 1 62  ? 16.219  -22.889 -4.803  1.00 91.10  ? 62  PHE B N   1 
ATOM   3424  C CA  . PHE B 1 62  ? 15.531  -24.118 -5.176  1.00 95.18  ? 62  PHE B CA  1 
ATOM   3425  C C   . PHE B 1 62  ? 14.346  -24.414 -4.265  1.00 88.56  ? 62  PHE B C   1 
ATOM   3426  O O   . PHE B 1 62  ? 13.992  -25.576 -4.053  1.00 84.97  ? 62  PHE B O   1 
ATOM   3427  C CB  . PHE B 1 62  ? 16.507  -25.299 -5.207  1.00 103.25 ? 62  PHE B CB  1 
ATOM   3428  C CG  . PHE B 1 62  ? 17.301  -25.482 -3.946  1.00 100.75 ? 62  PHE B CG  1 
ATOM   3429  C CD1 . PHE B 1 62  ? 18.416  -24.696 -3.699  1.00 99.78  ? 62  PHE B CD1 1 
ATOM   3430  C CD2 . PHE B 1 62  ? 16.959  -26.459 -3.029  1.00 98.07  ? 62  PHE B CD2 1 
ATOM   3431  C CE1 . PHE B 1 62  ? 19.160  -24.863 -2.551  1.00 101.75 ? 62  PHE B CE1 1 
ATOM   3432  C CE2 . PHE B 1 62  ? 17.704  -26.635 -1.876  1.00 95.96  ? 62  PHE B CE2 1 
ATOM   3433  C CZ  . PHE B 1 62  ? 18.806  -25.834 -1.637  1.00 100.67 ? 62  PHE B CZ  1 
ATOM   3434  N N   . TYR B 1 63  ? 13.729  -23.368 -3.730  1.00 90.34  ? 63  TYR B N   1 
ATOM   3435  C CA  . TYR B 1 63  ? 12.424  -23.520 -3.117  1.00 88.58  ? 63  TYR B CA  1 
ATOM   3436  C C   . TYR B 1 63  ? 11.370  -23.753 -4.200  1.00 90.58  ? 63  TYR B C   1 
ATOM   3437  O O   . TYR B 1 63  ? 11.644  -23.682 -5.401  1.00 91.96  ? 63  TYR B O   1 
ATOM   3438  C CB  . TYR B 1 63  ? 12.076  -22.280 -2.297  1.00 87.25  ? 63  TYR B CB  1 
ATOM   3439  C CG  . TYR B 1 63  ? 12.421  -22.354 -0.828  1.00 85.60  ? 63  TYR B CG  1 
ATOM   3440  C CD1 . TYR B 1 63  ? 12.275  -23.533 -0.111  1.00 88.04  ? 63  TYR B CD1 1 
ATOM   3441  C CD2 . TYR B 1 63  ? 12.875  -21.230 -0.153  1.00 87.41  ? 63  TYR B CD2 1 
ATOM   3442  C CE1 . TYR B 1 63  ? 12.575  -23.588 1.238   1.00 92.69  ? 63  TYR B CE1 1 
ATOM   3443  C CE2 . TYR B 1 63  ? 13.183  -21.277 1.190   1.00 89.60  ? 63  TYR B CE2 1 
ATOM   3444  C CZ  . TYR B 1 63  ? 13.034  -22.456 1.882   1.00 90.21  ? 63  TYR B CZ  1 
ATOM   3445  O OH  . TYR B 1 63  ? 13.341  -22.493 3.223   1.00 83.57  ? 63  TYR B OH  1 
ATOM   3446  N N   . GLU B 1 64  ? 10.144  -24.029 -3.769  1.00 88.60  ? 64  GLU B N   1 
ATOM   3447  C CA  . GLU B 1 64  ? 9.039   -24.202 -4.701  1.00 86.90  ? 64  GLU B CA  1 
ATOM   3448  C C   . GLU B 1 64  ? 8.361   -22.862 -4.955  1.00 90.46  ? 64  GLU B C   1 
ATOM   3449  O O   . GLU B 1 64  ? 8.074   -22.114 -4.014  1.00 88.38  ? 64  GLU B O   1 
ATOM   3450  C CB  . GLU B 1 64  ? 8.037   -25.229 -4.172  1.00 90.96  ? 64  GLU B CB  1 
ATOM   3451  C CG  . GLU B 1 64  ? 8.581   -26.656 -4.175  1.00 87.84  ? 64  GLU B CG  1 
ATOM   3452  C CD  . GLU B 1 64  ? 9.004   -27.138 -5.556  1.00 87.37  ? 64  GLU B CD  1 
ATOM   3453  O OE1 . GLU B 1 64  ? 8.493   -26.613 -6.570  1.00 92.14  ? 64  GLU B OE1 1 
ATOM   3454  O OE2 . GLU B 1 64  ? 9.873   -28.033 -5.626  1.00 79.16  ? 64  GLU B OE2 1 
ATOM   3455  N N   . GLU B 1 65  ? 8.108   -22.566 -6.234  1.00 99.76  ? 65  GLU B N   1 
ATOM   3456  C CA  . GLU B 1 65  ? 7.537   -21.280 -6.621  1.00 103.40 ? 65  GLU B CA  1 
ATOM   3457  C C   . GLU B 1 65  ? 6.136   -21.069 -6.061  1.00 100.04 ? 65  GLU B C   1 
ATOM   3458  O O   . GLU B 1 65  ? 5.696   -19.919 -5.947  1.00 100.18 ? 65  GLU B O   1 
ATOM   3459  C CB  . GLU B 1 65  ? 7.513   -21.158 -8.147  1.00 106.90 ? 65  GLU B CB  1 
ATOM   3460  C CG  . GLU B 1 65  ? 7.119   -19.778 -8.663  1.00 108.05 ? 65  GLU B CG  1 
ATOM   3461  C CD  . GLU B 1 65  ? 7.245   -19.656 -10.167 1.00 112.98 ? 65  GLU B CD  1 
ATOM   3462  O OE1 . GLU B 1 65  ? 7.692   -20.630 -10.810 1.00 114.42 ? 65  GLU B OE1 1 
ATOM   3463  O OE2 . GLU B 1 65  ? 6.896   -18.584 -10.706 1.00 114.12 ? 65  GLU B OE2 1 
ATOM   3464  N N   . ARG B 1 66  ? 5.428   -22.146 -5.708  1.00 94.46  ? 66  ARG B N   1 
ATOM   3465  C CA  . ARG B 1 66  ? 4.072   -22.000 -5.190  1.00 95.44  ? 66  ARG B CA  1 
ATOM   3466  C C   . ARG B 1 66  ? 4.051   -21.152 -3.926  1.00 94.66  ? 66  ARG B C   1 
ATOM   3467  O O   . ARG B 1 66  ? 3.092   -20.409 -3.691  1.00 96.64  ? 66  ARG B O   1 
ATOM   3468  C CB  . ARG B 1 66  ? 3.458   -23.374 -4.922  1.00 100.43 ? 66  ARG B CB  1 
ATOM   3469  C CG  . ARG B 1 66  ? 3.592   -24.350 -6.081  1.00 104.04 ? 66  ARG B CG  1 
ATOM   3470  C CD  . ARG B 1 66  ? 3.330   -25.777 -5.632  1.00 108.99 ? 66  ARG B CD  1 
ATOM   3471  N NE  . ARG B 1 66  ? 4.248   -26.192 -4.574  1.00 110.41 ? 66  ARG B NE  1 
ATOM   3472  C CZ  . ARG B 1 66  ? 4.221   -27.383 -3.986  1.00 114.95 ? 66  ARG B CZ  1 
ATOM   3473  N NH1 . ARG B 1 66  ? 3.320   -28.285 -4.351  1.00 117.51 ? 66  ARG B NH1 1 
ATOM   3474  N NH2 . ARG B 1 66  ? 5.096   -27.675 -3.034  1.00 114.65 ? 66  ARG B NH2 1 
ATOM   3475  N N   . GLU B 1 67  ? 5.098   -21.248 -3.106  1.00 89.70  ? 67  GLU B N   1 
ATOM   3476  C CA  . GLU B 1 67  ? 5.157   -20.447 -1.890  1.00 86.19  ? 67  GLU B CA  1 
ATOM   3477  C C   . GLU B 1 67  ? 5.457   -18.990 -2.213  1.00 79.10  ? 67  GLU B C   1 
ATOM   3478  O O   . GLU B 1 67  ? 4.923   -18.080 -1.568  1.00 79.73  ? 67  GLU B O   1 
ATOM   3479  C CB  . GLU B 1 67  ? 6.216   -21.010 -0.944  1.00 88.12  ? 67  GLU B CB  1 
ATOM   3480  C CG  . GLU B 1 67  ? 5.840   -22.333 -0.307  1.00 96.05  ? 67  GLU B CG  1 
ATOM   3481  C CD  . GLU B 1 67  ? 6.980   -22.924 0.497   1.00 95.32  ? 67  GLU B CD  1 
ATOM   3482  O OE1 . GLU B 1 67  ? 8.071   -23.125 -0.077  1.00 86.61  ? 67  GLU B OE1 1 
ATOM   3483  O OE2 . GLU B 1 67  ? 6.786   -23.187 1.702   1.00 96.73  ? 67  GLU B OE2 1 
ATOM   3484  N N   . PHE B 1 68  ? 6.312   -18.752 -3.209  1.00 83.76  ? 68  PHE B N   1 
ATOM   3485  C CA  . PHE B 1 68  ? 6.744   -17.397 -3.524  1.00 82.36  ? 68  PHE B CA  1 
ATOM   3486  C C   . PHE B 1 68  ? 5.773   -16.674 -4.445  1.00 85.19  ? 68  PHE B C   1 
ATOM   3487  O O   . PHE B 1 68  ? 5.710   -15.441 -4.415  1.00 82.49  ? 68  PHE B O   1 
ATOM   3488  C CB  . PHE B 1 68  ? 8.136   -17.436 -4.160  1.00 82.44  ? 68  PHE B CB  1 
ATOM   3489  C CG  . PHE B 1 68  ? 9.231   -17.776 -3.194  1.00 80.83  ? 68  PHE B CG  1 
ATOM   3490  C CD1 . PHE B 1 68  ? 10.119  -16.806 -2.761  1.00 79.38  ? 68  PHE B CD1 1 
ATOM   3491  C CD2 . PHE B 1 68  ? 9.364   -19.066 -2.708  1.00 82.11  ? 68  PHE B CD2 1 
ATOM   3492  C CE1 . PHE B 1 68  ? 11.125  -17.121 -1.866  1.00 76.83  ? 68  PHE B CE1 1 
ATOM   3493  C CE2 . PHE B 1 68  ? 10.361  -19.383 -1.812  1.00 79.31  ? 68  PHE B CE2 1 
ATOM   3494  C CZ  . PHE B 1 68  ? 11.241  -18.413 -1.391  1.00 76.33  ? 68  PHE B CZ  1 
ATOM   3495  N N   . ALA B 1 69  ? 5.010   -17.412 -5.252  1.00 99.16  ? 69  ALA B N   1 
ATOM   3496  C CA  . ALA B 1 69  ? 4.077   -16.772 -6.175  1.00 101.30 ? 69  ALA B CA  1 
ATOM   3497  C C   . ALA B 1 69  ? 3.033   -15.950 -5.430  1.00 100.89 ? 69  ALA B C   1 
ATOM   3498  O O   . ALA B 1 69  ? 2.675   -14.847 -5.862  1.00 102.14 ? 69  ALA B O   1 
ATOM   3499  C CB  . ALA B 1 69  ? 3.402   -17.824 -7.056  1.00 104.29 ? 69  ALA B CB  1 
ATOM   3500  N N   . LEU B 1 70  ? 2.539   -16.466 -4.302  1.00 83.91  ? 70  LEU B N   1 
ATOM   3501  C CA  . LEU B 1 70  ? 1.538   -15.733 -3.533  1.00 83.42  ? 70  LEU B CA  1 
ATOM   3502  C C   . LEU B 1 70  ? 2.137   -14.523 -2.826  1.00 83.86  ? 70  LEU B C   1 
ATOM   3503  O O   . LEU B 1 70  ? 1.459   -13.501 -2.675  1.00 79.75  ? 70  LEU B O   1 
ATOM   3504  C CB  . LEU B 1 70  ? 0.856   -16.660 -2.525  1.00 87.22  ? 70  LEU B CB  1 
ATOM   3505  C CG  . LEU B 1 70  ? -0.210  -17.636 -3.033  1.00 87.76  ? 70  LEU B CG  1 
ATOM   3506  C CD1 . LEU B 1 70  ? 0.380   -18.762 -3.870  1.00 82.38  ? 70  LEU B CD1 1 
ATOM   3507  C CD2 . LEU B 1 70  ? -1.004  -18.195 -1.863  1.00 81.31  ? 70  LEU B CD2 1 
ATOM   3508  N N   . TYR B 1 71  ? 3.393   -14.617 -2.386  1.00 82.42  ? 71  TYR B N   1 
ATOM   3509  C CA  . TYR B 1 71  ? 4.009   -13.514 -1.655  1.00 82.89  ? 71  TYR B CA  1 
ATOM   3510  C C   . TYR B 1 71  ? 4.449   -12.400 -2.599  1.00 88.47  ? 71  TYR B C   1 
ATOM   3511  O O   . TYR B 1 71  ? 4.256   -11.217 -2.298  1.00 92.34  ? 71  TYR B O   1 
ATOM   3512  C CB  . TYR B 1 71  ? 5.192   -14.021 -0.827  1.00 78.57  ? 71  TYR B CB  1 
ATOM   3513  C CG  . TYR B 1 71  ? 6.006   -12.922 -0.177  1.00 85.23  ? 71  TYR B CG  1 
ATOM   3514  C CD1 . TYR B 1 71  ? 5.414   -12.013 0.696   1.00 90.03  ? 71  TYR B CD1 1 
ATOM   3515  C CD2 . TYR B 1 71  ? 7.368   -12.800 -0.422  1.00 84.41  ? 71  TYR B CD2 1 
ATOM   3516  C CE1 . TYR B 1 71  ? 6.156   -11.010 1.294   1.00 90.32  ? 71  TYR B CE1 1 
ATOM   3517  C CE2 . TYR B 1 71  ? 8.117   -11.802 0.176   1.00 83.23  ? 71  TYR B CE2 1 
ATOM   3518  C CZ  . TYR B 1 71  ? 7.506   -10.909 1.029   1.00 86.00  ? 71  TYR B CZ  1 
ATOM   3519  O OH  . TYR B 1 71  ? 8.254   -9.916  1.619   1.00 81.82  ? 71  TYR B OH  1 
ATOM   3520  N N   . VAL B 1 72  ? 5.057   -12.763 -3.733  1.00 88.93  ? 72  VAL B N   1 
ATOM   3521  C CA  . VAL B 1 72  ? 5.528   -11.772 -4.699  1.00 87.39  ? 72  VAL B CA  1 
ATOM   3522  C C   . VAL B 1 72  ? 4.376   -10.913 -5.208  1.00 91.10  ? 72  VAL B C   1 
ATOM   3523  O O   . VAL B 1 72  ? 4.571   -9.741  -5.554  1.00 96.71  ? 72  VAL B O   1 
ATOM   3524  C CB  . VAL B 1 72  ? 6.273   -12.481 -5.851  1.00 81.48  ? 72  VAL B CB  1 
ATOM   3525  C CG1 . VAL B 1 72  ? 6.619   -11.508 -6.966  1.00 88.33  ? 72  VAL B CG1 1 
ATOM   3526  C CG2 . VAL B 1 72  ? 7.540   -13.134 -5.328  1.00 82.25  ? 72  VAL B CG2 1 
ATOM   3527  N N   . SER B 1 73  ? 3.161   -11.465 -5.241  1.00 89.36  ? 73  SER B N   1 
ATOM   3528  C CA  . SER B 1 73  ? 2.012   -10.708 -5.726  1.00 89.83  ? 73  SER B CA  1 
ATOM   3529  C C   . SER B 1 73  ? 1.699   -9.495  -4.858  1.00 91.66  ? 73  SER B C   1 
ATOM   3530  O O   . SER B 1 73  ? 1.073   -8.546  -5.344  1.00 94.51  ? 73  SER B O   1 
ATOM   3531  C CB  . SER B 1 73  ? 0.782   -11.616 -5.806  1.00 85.13  ? 73  SER B CB  1 
ATOM   3532  O OG  . SER B 1 73  ? 1.017   -12.722 -6.660  1.00 81.99  ? 73  SER B OG  1 
ATOM   3533  N N   . SER B 1 74  ? 2.124   -9.494  -3.594  1.00 91.22  ? 74  SER B N   1 
ATOM   3534  C CA  . SER B 1 74  ? 1.771   -8.414  -2.680  1.00 94.47  ? 74  SER B CA  1 
ATOM   3535  C C   . SER B 1 74  ? 2.816   -7.308  -2.605  1.00 104.47 ? 74  SER B C   1 
ATOM   3536  O O   . SER B 1 74  ? 2.470   -6.166  -2.278  1.00 108.04 ? 74  SER B O   1 
ATOM   3537  C CB  . SER B 1 74  ? 1.538   -8.976  -1.275  1.00 94.92  ? 74  SER B CB  1 
ATOM   3538  O OG  . SER B 1 74  ? 0.619   -10.053 -1.306  1.00 94.20  ? 74  SER B OG  1 
ATOM   3539  N N   . ILE B 1 75  ? 4.082   -7.611  -2.894  1.00 111.65 ? 75  ILE B N   1 
ATOM   3540  C CA  . ILE B 1 75  ? 5.133   -6.604  -2.767  1.00 115.91 ? 75  ILE B CA  1 
ATOM   3541  C C   . ILE B 1 75  ? 4.998   -5.545  -3.854  1.00 120.81 ? 75  ILE B C   1 
ATOM   3542  O O   . ILE B 1 75  ? 5.028   -4.340  -3.577  1.00 122.97 ? 75  ILE B O   1 
ATOM   3543  C CB  . ILE B 1 75  ? 6.521   -7.263  -2.797  1.00 112.34 ? 75  ILE B CB  1 
ATOM   3544  C CG1 . ILE B 1 75  ? 6.500   -8.586  -2.037  1.00 107.35 ? 75  ILE B CG1 1 
ATOM   3545  C CG2 . ILE B 1 75  ? 7.558   -6.328  -2.198  1.00 106.03 ? 75  ILE B CG2 1 
ATOM   3546  C CD1 . ILE B 1 75  ? 7.750   -9.397  -2.232  1.00 104.40 ? 75  ILE B CD1 1 
ATOM   3547  N N   . SER B 1 76  ? 4.855   -5.978  -5.110  1.00 138.44 ? 76  SER B N   1 
ATOM   3548  C CA  . SER B 1 76  ? 4.754   -5.039  -6.221  1.00 140.92 ? 76  SER B CA  1 
ATOM   3549  C C   . SER B 1 76  ? 3.532   -4.139  -6.111  1.00 141.63 ? 76  SER B C   1 
ATOM   3550  O O   . SER B 1 76  ? 3.460   -3.129  -6.820  1.00 144.28 ? 76  SER B O   1 
ATOM   3551  C CB  . SER B 1 76  ? 4.729   -5.800  -7.549  1.00 141.91 ? 76  SER B CB  1 
ATOM   3552  O OG  . SER B 1 76  ? 5.908   -6.567  -7.716  1.00 141.24 ? 76  SER B OG  1 
ATOM   3553  N N   . ASN B 1 77  ? 2.575   -4.480  -5.248  1.00 123.56 ? 77  ASN B N   1 
ATOM   3554  C CA  . ASN B 1 77  ? 1.461   -3.593  -4.952  1.00 120.39 ? 77  ASN B CA  1 
ATOM   3555  C C   . ASN B 1 77  ? 1.865   -2.445  -4.036  1.00 123.61 ? 77  ASN B C   1 
ATOM   3556  O O   . ASN B 1 77  ? 1.141   -1.446  -3.961  1.00 126.89 ? 77  ASN B O   1 
ATOM   3557  C CB  . ASN B 1 77  ? 0.318   -4.386  -4.314  1.00 114.99 ? 77  ASN B CB  1 
ATOM   3558  C CG  . ASN B 1 77  ? -0.221  -5.472  -5.229  1.00 104.18 ? 77  ASN B CG  1 
ATOM   3559  O OD1 . ASN B 1 77  ? -0.168  -5.353  -6.452  1.00 99.77  ? 77  ASN B OD1 1 
ATOM   3560  N ND2 . ASN B 1 77  ? -0.734  -6.545  -4.635  1.00 104.61 ? 77  ASN B ND2 1 
ATOM   3561  N N   . GLU B 1 78  ? 2.994   -2.570  -3.333  1.00 121.25 ? 78  GLU B N   1 
ATOM   3562  C CA  . GLU B 1 78  ? 3.458   -1.546  -2.401  1.00 120.64 ? 78  GLU B CA  1 
ATOM   3563  C C   . GLU B 1 78  ? 4.494   -0.616  -3.027  1.00 125.32 ? 78  GLU B C   1 
ATOM   3564  O O   . GLU B 1 78  ? 4.289   0.601   -3.077  1.00 126.15 ? 78  GLU B O   1 
ATOM   3565  C CB  . GLU B 1 78  ? 4.031   -2.208  -1.139  1.00 116.17 ? 78  GLU B CB  1 
ATOM   3566  C CG  . GLU B 1 78  ? 3.010   -2.985  -0.322  1.00 118.18 ? 78  GLU B CG  1 
ATOM   3567  C CD  . GLU B 1 78  ? 3.581   -3.506  0.985   1.00 116.33 ? 78  GLU B CD  1 
ATOM   3568  O OE1 . GLU B 1 78  ? 4.792   -3.318  1.224   1.00 115.25 ? 78  GLU B OE1 1 
ATOM   3569  O OE2 . GLU B 1 78  ? 2.817   -4.102  1.775   1.00 114.61 ? 78  GLU B OE2 1 
ATOM   3570  N N   . LEU B 1 79  ? 5.607   -1.168  -3.511  1.00 125.88 ? 79  LEU B N   1 
ATOM   3571  C CA  . LEU B 1 79  ? 6.710   -0.368  -4.029  1.00 131.45 ? 79  LEU B CA  1 
ATOM   3572  C C   . LEU B 1 79  ? 6.718   -0.249  -5.548  1.00 138.01 ? 79  LEU B C   1 
ATOM   3573  O O   . LEU B 1 79  ? 7.544   0.497   -6.086  1.00 137.63 ? 79  LEU B O   1 
ATOM   3574  C CB  . LEU B 1 79  ? 8.056   -0.937  -3.558  1.00 135.08 ? 79  LEU B CB  1 
ATOM   3575  C CG  . LEU B 1 79  ? 8.446   -0.713  -2.093  1.00 127.52 ? 79  LEU B CG  1 
ATOM   3576  C CD1 . LEU B 1 79  ? 8.137   0.717   -1.660  1.00 130.27 ? 79  LEU B CD1 1 
ATOM   3577  C CD2 . LEU B 1 79  ? 7.782   -1.724  -1.168  1.00 120.48 ? 79  LEU B CD2 1 
ATOM   3578  N N   . LYS B 1 80  ? 5.831   -0.962  -6.245  1.00 140.56 ? 80  LYS B N   1 
ATOM   3579  C CA  . LYS B 1 80  ? 5.702   -0.886  -7.702  1.00 144.84 ? 80  LYS B CA  1 
ATOM   3580  C C   . LYS B 1 80  ? 7.010   -1.276  -8.396  1.00 158.38 ? 80  LYS B C   1 
ATOM   3581  O O   . LYS B 1 80  ? 7.593   -0.509  -9.165  1.00 156.16 ? 80  LYS B O   1 
ATOM   3582  C CB  . LYS B 1 80  ? 5.246   0.512   -8.148  1.00 135.03 ? 80  LYS B CB  1 
ATOM   3583  C CG  . LYS B 1 80  ? 3.937   1.004   -7.538  1.00 130.41 ? 80  LYS B CG  1 
ATOM   3584  C CD  . LYS B 1 80  ? 4.168   1.791   -6.250  1.00 133.49 ? 80  LYS B CD  1 
ATOM   3585  C CE  . LYS B 1 80  ? 5.248   2.850   -6.430  1.00 134.01 ? 80  LYS B CE  1 
ATOM   3586  N NZ  . LYS B 1 80  ? 5.646   3.482   -5.139  1.00 130.40 ? 80  LYS B NZ  1 
ATOM   3587  N N   . ILE B 1 81  ? 7.467   -2.492  -8.109  1.00 206.91 ? 81  ILE B N   1 
ATOM   3588  C CA  . ILE B 1 81  ? 8.688   -3.016  -8.719  1.00 207.16 ? 81  ILE B CA  1 
ATOM   3589  C C   . ILE B 1 81  ? 8.444   -4.424  -9.253  1.00 206.20 ? 81  ILE B C   1 
ATOM   3590  O O   . ILE B 1 81  ? 7.874   -5.267  -8.545  1.00 204.48 ? 81  ILE B O   1 
ATOM   3591  C CB  . ILE B 1 81  ? 9.857   -2.996  -7.723  1.00 206.23 ? 81  ILE B CB  1 
ATOM   3592  C CG1 . ILE B 1 81  ? 9.358   -3.305  -6.311  1.00 204.38 ? 81  ILE B CG1 1 
ATOM   3593  C CG2 . ILE B 1 81  ? 10.574  -1.654  -7.769  1.00 207.91 ? 81  ILE B CG2 1 
ATOM   3594  C CD1 . ILE B 1 81  ? 10.423  -3.168  -5.249  1.00 203.61 ? 81  ILE B CD1 1 
ATOM   3595  N N   . PRO B 1 82  ? 8.849   -4.720  -10.495 1.00 138.94 ? 82  PRO B N   1 
ATOM   3596  C CA  . PRO B 1 82  ? 8.632   -6.063  -11.052 1.00 117.59 ? 82  PRO B CA  1 
ATOM   3597  C C   . PRO B 1 82  ? 9.520   -7.123  -10.417 1.00 107.47 ? 82  PRO B C   1 
ATOM   3598  O O   . PRO B 1 82  ? 10.669  -7.309  -10.831 1.00 100.74 ? 82  PRO B O   1 
ATOM   3599  C CB  . PRO B 1 82  ? 8.962   -5.886  -12.540 1.00 110.11 ? 82  PRO B CB  1 
ATOM   3600  C CG  . PRO B 1 82  ? 8.930   -4.405  -12.782 1.00 112.22 ? 82  PRO B CG  1 
ATOM   3601  C CD  . PRO B 1 82  ? 9.382   -3.788  -11.500 1.00 127.00 ? 82  PRO B CD  1 
ATOM   3602  N N   . VAL B 1 83  ? 8.995   -7.824  -9.416  1.00 103.82 ? 83  VAL B N   1 
ATOM   3603  C CA  . VAL B 1 83  ? 9.712   -8.894  -8.731  1.00 95.01  ? 83  VAL B CA  1 
ATOM   3604  C C   . VAL B 1 83  ? 9.298   -10.234 -9.322  1.00 87.74  ? 83  VAL B C   1 
ATOM   3605  O O   . VAL B 1 83  ? 8.124   -10.447 -9.648  1.00 88.59  ? 83  VAL B O   1 
ATOM   3606  C CB  . VAL B 1 83  ? 9.447   -8.857  -7.214  1.00 92.20  ? 83  VAL B CB  1 
ATOM   3607  C CG1 . VAL B 1 83  ? 10.336  -9.861  -6.496  1.00 82.65  ? 83  VAL B CG1 1 
ATOM   3608  C CG2 . VAL B 1 83  ? 9.663   -7.455  -6.673  1.00 107.72 ? 83  VAL B CG2 1 
ATOM   3609  N N   . ARG B 1 84  ? 10.261  -11.148 -9.448  1.00 83.22  ? 84  ARG B N   1 
ATOM   3610  C CA  . ARG B 1 84  ? 10.027  -12.468 -10.018 1.00 80.62  ? 84  ARG B CA  1 
ATOM   3611  C C   . ARG B 1 84  ? 10.854  -13.498 -9.268  1.00 77.85  ? 84  ARG B C   1 
ATOM   3612  O O   . ARG B 1 84  ? 12.006  -13.240 -8.910  1.00 85.47  ? 84  ARG B O   1 
ATOM   3613  C CB  . ARG B 1 84  ? 10.384  -12.512 -11.511 1.00 84.38  ? 84  ARG B CB  1 
ATOM   3614  C CG  . ARG B 1 84  ? 10.166  -13.878 -12.162 1.00 85.47  ? 84  ARG B CG  1 
ATOM   3615  C CD  . ARG B 1 84  ? 10.575  -13.888 -13.630 1.00 90.79  ? 84  ARG B CD  1 
ATOM   3616  N NE  . ARG B 1 84  ? 9.753   -12.998 -14.445 1.00 96.19  ? 84  ARG B NE  1 
ATOM   3617  C CZ  . ARG B 1 84  ? 8.625   -13.362 -15.048 1.00 99.14  ? 84  ARG B CZ  1 
ATOM   3618  N NH1 . ARG B 1 84  ? 8.172   -14.604 -14.933 1.00 99.27  ? 84  ARG B NH1 1 
ATOM   3619  N NH2 . ARG B 1 84  ? 7.947   -12.479 -15.770 1.00 99.98  ? 84  ARG B NH2 1 
ATOM   3620  N N   . TYR B 1 85  ? 10.263  -14.666 -9.038  1.00 79.36  ? 85  TYR B N   1 
ATOM   3621  C CA  . TYR B 1 85  ? 10.957  -15.776 -8.404  1.00 85.57  ? 85  TYR B CA  1 
ATOM   3622  C C   . TYR B 1 85  ? 11.358  -16.802 -9.453  1.00 91.06  ? 85  TYR B C   1 
ATOM   3623  O O   . TYR B 1 85  ? 10.562  -17.160 -10.325 1.00 93.36  ? 85  TYR B O   1 
ATOM   3624  C CB  . TYR B 1 85  ? 10.091  -16.447 -7.338  1.00 87.33  ? 85  TYR B CB  1 
ATOM   3625  C CG  . TYR B 1 85  ? 10.745  -17.669 -6.736  1.00 85.59  ? 85  TYR B CG  1 
ATOM   3626  C CD1 . TYR B 1 85  ? 11.716  -17.545 -5.752  1.00 82.75  ? 85  TYR B CD1 1 
ATOM   3627  C CD2 . TYR B 1 85  ? 10.403  -18.946 -7.162  1.00 88.03  ? 85  TYR B CD2 1 
ATOM   3628  C CE1 . TYR B 1 85  ? 12.322  -18.657 -5.205  1.00 81.46  ? 85  TYR B CE1 1 
ATOM   3629  C CE2 . TYR B 1 85  ? 11.004  -20.062 -6.622  1.00 84.59  ? 85  TYR B CE2 1 
ATOM   3630  C CZ  . TYR B 1 85  ? 11.961  -19.911 -5.644  1.00 83.47  ? 85  TYR B CZ  1 
ATOM   3631  O OH  . TYR B 1 85  ? 12.562  -21.020 -5.106  1.00 82.36  ? 85  TYR B OH  1 
ATOM   3632  N N   . LEU B 1 86  ? 12.597  -17.277 -9.358  1.00 109.16 ? 86  LEU B N   1 
ATOM   3633  C CA  . LEU B 1 86  ? 13.107  -18.307 -10.250 1.00 110.04 ? 86  LEU B CA  1 
ATOM   3634  C C   . LEU B 1 86  ? 13.652  -19.457 -9.421  1.00 109.57 ? 86  LEU B C   1 
ATOM   3635  O O   . LEU B 1 86  ? 14.500  -19.250 -8.550  1.00 108.90 ? 86  LEU B O   1 
ATOM   3636  C CB  . LEU B 1 86  ? 14.196  -17.756 -11.173 1.00 111.43 ? 86  LEU B CB  1 
ATOM   3637  C CG  . LEU B 1 86  ? 13.810  -16.557 -12.037 1.00 116.38 ? 86  LEU B CG  1 
ATOM   3638  C CD1 . LEU B 1 86  ? 14.989  -16.125 -12.891 1.00 118.37 ? 86  LEU B CD1 1 
ATOM   3639  C CD2 . LEU B 1 86  ? 12.609  -16.895 -12.906 1.00 120.10 ? 86  LEU B CD2 1 
ATOM   3640  N N   . LYS B 1 87  ? 13.167  -20.665 -9.694  1.00 103.03 ? 87  LYS B N   1 
ATOM   3641  C CA  . LYS B 1 87  ? 13.628  -21.858 -8.994  1.00 104.89 ? 87  LYS B CA  1 
ATOM   3642  C C   . LYS B 1 87  ? 14.746  -22.490 -9.811  1.00 118.10 ? 87  LYS B C   1 
ATOM   3643  O O   . LYS B 1 87  ? 14.500  -23.053 -10.883 1.00 128.09 ? 87  LYS B O   1 
ATOM   3644  C CB  . LYS B 1 87  ? 12.497  -22.858 -8.772  1.00 101.33 ? 87  LYS B CB  1 
ATOM   3645  C CG  . LYS B 1 87  ? 13.015  -24.224 -8.345  1.00 104.78 ? 87  LYS B CG  1 
ATOM   3646  C CD  . LYS B 1 87  ? 11.912  -25.246 -8.159  1.00 103.28 ? 87  LYS B CD  1 
ATOM   3647  C CE  . LYS B 1 87  ? 12.503  -26.638 -8.011  1.00 107.94 ? 87  LYS B CE  1 
ATOM   3648  N NZ  . LYS B 1 87  ? 13.663  -26.640 -7.076  1.00 105.96 ? 87  LYS B NZ  1 
ATOM   3649  N N   . GLU B 1 88  ? 15.973  -22.385 -9.313  1.00 118.01 ? 88  GLU B N   1 
ATOM   3650  C CA  . GLU B 1 88  ? 17.102  -23.049 -9.951  1.00 132.75 ? 88  GLU B CA  1 
ATOM   3651  C C   . GLU B 1 88  ? 16.949  -24.557 -9.785  1.00 145.30 ? 88  GLU B C   1 
ATOM   3652  O O   . GLU B 1 88  ? 17.144  -25.095 -8.690  1.00 138.76 ? 88  GLU B O   1 
ATOM   3653  C CB  . GLU B 1 88  ? 18.415  -22.539 -9.360  1.00 130.13 ? 88  GLU B CB  1 
ATOM   3654  C CG  . GLU B 1 88  ? 18.454  -22.478 -7.836  1.00 123.06 ? 88  GLU B CG  1 
ATOM   3655  C CD  . GLU B 1 88  ? 19.842  -22.188 -7.296  1.00 130.89 ? 88  GLU B CD  1 
ATOM   3656  O OE1 . GLU B 1 88  ? 20.816  -22.304 -8.068  1.00 141.36 ? 88  GLU B OE1 1 
ATOM   3657  O OE2 . GLU B 1 88  ? 19.958  -21.853 -6.098  1.00 122.35 ? 88  GLU B OE2 1 
ATOM   3658  N N   . ASP B 1 89  ? 16.576  -25.238 -10.872 1.00 184.03 ? 89  ASP B N   1 
ATOM   3659  C CA  . ASP B 1 89  ? 16.397  -26.686 -10.816 1.00 183.89 ? 89  ASP B CA  1 
ATOM   3660  C C   . ASP B 1 89  ? 17.697  -27.383 -10.442 1.00 183.27 ? 89  ASP B C   1 
ATOM   3661  O O   . ASP B 1 89  ? 17.690  -28.375 -9.704  1.00 182.56 ? 89  ASP B O   1 
ATOM   3662  C CB  . ASP B 1 89  ? 15.872  -27.201 -12.157 1.00 187.41 ? 89  ASP B CB  1 
ATOM   3663  C CG  . ASP B 1 89  ? 14.834  -26.280 -12.769 1.00 188.68 ? 89  ASP B CG  1 
ATOM   3664  O OD1 . ASP B 1 89  ? 15.209  -25.440 -13.614 1.00 190.71 ? 89  ASP B OD1 1 
ATOM   3665  O OD2 . ASP B 1 89  ? 13.648  -26.383 -12.393 1.00 185.93 ? 89  ASP B OD2 1 
ATOM   3666  N N   . LYS B 1 90  ? 18.823  -26.878 -10.944 1.00 170.30 ? 90  LYS B N   1 
ATOM   3667  C CA  . LYS B 1 90  ? 20.142  -27.389 -10.587 1.00 172.15 ? 90  LYS B CA  1 
ATOM   3668  C C   . LYS B 1 90  ? 20.837  -26.371 -9.692  1.00 171.37 ? 90  LYS B C   1 
ATOM   3669  O O   . LYS B 1 90  ? 21.444  -25.414 -10.198 1.00 171.76 ? 90  LYS B O   1 
ATOM   3670  C CB  . LYS B 1 90  ? 20.974  -27.663 -11.842 1.00 177.19 ? 90  LYS B CB  1 
ATOM   3671  N N   . PRO B 1 91  ? 20.773  -26.518 -8.369  1.00 167.42 ? 91  PRO B N   1 
ATOM   3672  C CA  . PRO B 1 91  ? 21.396  -25.521 -7.487  1.00 164.60 ? 91  PRO B CA  1 
ATOM   3673  C C   . PRO B 1 91  ? 22.913  -25.618 -7.537  1.00 177.13 ? 91  PRO B C   1 
ATOM   3674  O O   . PRO B 1 91  ? 23.489  -26.690 -7.344  1.00 179.01 ? 91  PRO B O   1 
ATOM   3675  C CB  . PRO B 1 91  ? 20.854  -25.882 -6.096  1.00 146.75 ? 91  PRO B CB  1 
ATOM   3676  C CG  . PRO B 1 91  ? 19.693  -26.805 -6.346  1.00 143.14 ? 91  PRO B CG  1 
ATOM   3677  C CD  . PRO B 1 91  ? 20.016  -27.526 -7.612  1.00 157.19 ? 91  PRO B CD  1 
ATOM   3678  N N   . HIS B 1 92  ? 23.557  -24.483 -7.802  1.00 207.34 ? 92  HIS B N   1 
ATOM   3679  C CA  . HIS B 1 92  ? 25.011  -24.435 -7.870  1.00 207.55 ? 92  HIS B CA  1 
ATOM   3680  C C   . HIS B 1 92  ? 25.559  -23.417 -6.880  1.00 206.99 ? 92  HIS B C   1 
ATOM   3681  O O   . HIS B 1 92  ? 26.396  -22.581 -7.238  1.00 207.55 ? 92  HIS B O   1 
ATOM   3682  C CB  . HIS B 1 92  ? 25.474  -24.100 -9.288  1.00 208.91 ? 92  HIS B CB  1 
ATOM   3683  C CG  . HIS B 1 92  ? 24.828  -24.933 -10.350 1.00 209.99 ? 92  HIS B CG  1 
ATOM   3684  N ND1 . HIS B 1 92  ? 24.250  -24.386 -11.475 1.00 211.28 ? 92  HIS B ND1 1 
ATOM   3685  C CD2 . HIS B 1 92  ? 24.677  -26.274 -10.463 1.00 210.14 ? 92  HIS B CD2 1 
ATOM   3686  C CE1 . HIS B 1 92  ? 23.765  -25.353 -12.233 1.00 211.79 ? 92  HIS B CE1 1 
ATOM   3687  N NE2 . HIS B 1 92  ? 24.012  -26.508 -11.642 1.00 211.36 ? 92  HIS B NE2 1 
ATOM   3688  N N   . GLY B 1 93  ? 25.097  -23.482 -5.633  1.00 167.85 ? 93  GLY B N   1 
ATOM   3689  C CA  . GLY B 1 93  ? 25.542  -22.556 -4.611  1.00 149.61 ? 93  GLY B CA  1 
ATOM   3690  C C   . GLY B 1 93  ? 25.216  -21.111 -4.923  1.00 132.49 ? 93  GLY B C   1 
ATOM   3691  O O   . GLY B 1 93  ? 24.061  -20.689 -4.818  1.00 129.97 ? 93  GLY B O   1 
ATOM   3692  N N   . SER B 1 94  ? 26.230  -20.337 -5.305  1.00 127.25 ? 94  SER B N   1 
ATOM   3693  C CA  . SER B 1 94  ? 26.049  -18.920 -5.597  1.00 115.33 ? 94  SER B CA  1 
ATOM   3694  C C   . SER B 1 94  ? 26.484  -18.569 -7.012  1.00 117.76 ? 94  SER B C   1 
ATOM   3695  O O   . SER B 1 94  ? 25.680  -18.032 -7.781  1.00 113.71 ? 94  SER B O   1 
ATOM   3696  C CB  . SER B 1 94  ? 26.812  -18.072 -4.573  1.00 109.38 ? 94  SER B CB  1 
ATOM   3697  O OG  . SER B 1 94  ? 26.385  -18.361 -3.253  1.00 111.04 ? 94  SER B OG  1 
ATOM   3698  N N   . ALA B 1 95  ? 27.734  -18.859 -7.380  1.00 121.43 ? 95  ALA B N   1 
ATOM   3699  C CA  . ALA B 1 95  ? 28.256  -18.430 -8.674  1.00 118.89 ? 95  ALA B CA  1 
ATOM   3700  C C   . ALA B 1 95  ? 27.513  -19.100 -9.824  1.00 121.27 ? 95  ALA B C   1 
ATOM   3701  O O   . ALA B 1 95  ? 27.067  -18.433 -10.764 1.00 117.39 ? 95  ALA B O   1 
ATOM   3702  C CB  . ALA B 1 95  ? 29.754  -18.722 -8.757  1.00 120.66 ? 95  ALA B CB  1 
ATOM   3703  N N   . GLY B 1 96  ? 27.386  -20.427 -9.776  1.00 134.08 ? 96  GLY B N   1 
ATOM   3704  C CA  . GLY B 1 96  ? 26.641  -21.130 -10.805 1.00 141.81 ? 96  GLY B CA  1 
ATOM   3705  C C   . GLY B 1 96  ? 25.155  -20.842 -10.804 1.00 136.25 ? 96  GLY B C   1 
ATOM   3706  O O   . GLY B 1 96  ? 24.492  -21.054 -11.825 1.00 129.85 ? 96  GLY B O   1 
ATOM   3707  N N   . ALA B 1 97  ? 24.615  -20.376 -9.676  1.00 140.33 ? 97  ALA B N   1 
ATOM   3708  C CA  . ALA B 1 97  ? 23.193  -20.060 -9.610  1.00 138.82 ? 97  ALA B CA  1 
ATOM   3709  C C   . ALA B 1 97  ? 22.829  -18.927 -10.562 1.00 135.01 ? 97  ALA B C   1 
ATOM   3710  O O   . ALA B 1 97  ? 21.812  -18.998 -11.261 1.00 140.87 ? 97  ALA B O   1 
ATOM   3711  C CB  . ALA B 1 97  ? 22.800  -19.707 -8.178  1.00 139.66 ? 97  ALA B CB  1 
ATOM   3712  N N   . LEU B 1 98  ? 23.644  -17.871 -10.605 1.00 111.72 ? 98  LEU B N   1 
ATOM   3713  C CA  . LEU B 1 98  ? 23.323  -16.727 -11.447 1.00 106.96 ? 98  LEU B CA  1 
ATOM   3714  C C   . LEU B 1 98  ? 23.863  -16.863 -12.863 1.00 105.86 ? 98  LEU B C   1 
ATOM   3715  O O   . LEU B 1 98  ? 23.333  -16.219 -13.775 1.00 104.59 ? 98  LEU B O   1 
ATOM   3716  C CB  . LEU B 1 98  ? 23.846  -15.429 -10.823 1.00 98.14  ? 98  LEU B CB  1 
ATOM   3717  C CG  . LEU B 1 98  ? 25.331  -15.107 -10.984 1.00 98.48  ? 98  LEU B CG  1 
ATOM   3718  C CD1 . LEU B 1 98  ? 25.527  -13.616 -11.202 1.00 92.45  ? 98  LEU B CD1 1 
ATOM   3719  C CD2 . LEU B 1 98  ? 26.113  -15.582 -9.774  1.00 102.38 ? 98  LEU B CD2 1 
ATOM   3720  N N   . TYR B 1 99  ? 24.896  -17.682 -13.075 1.00 106.10 ? 99  TYR B N   1 
ATOM   3721  C CA  . TYR B 1 99  ? 25.306  -17.984 -14.441 1.00 100.10 ? 99  TYR B CA  1 
ATOM   3722  C C   . TYR B 1 99  ? 24.211  -18.749 -15.170 1.00 106.29 ? 99  TYR B C   1 
ATOM   3723  O O   . TYR B 1 99  ? 23.957  -18.509 -16.357 1.00 106.36 ? 99  TYR B O   1 
ATOM   3724  C CB  . TYR B 1 99  ? 26.606  -18.782 -14.445 1.00 102.21 ? 99  TYR B CB  1 
ATOM   3725  C CG  . TYR B 1 99  ? 26.996  -19.235 -15.825 1.00 102.27 ? 99  TYR B CG  1 
ATOM   3726  C CD1 . TYR B 1 99  ? 27.241  -18.312 -16.830 1.00 103.32 ? 99  TYR B CD1 1 
ATOM   3727  C CD2 . TYR B 1 99  ? 27.112  -20.584 -16.127 1.00 106.04 ? 99  TYR B CD2 1 
ATOM   3728  C CE1 . TYR B 1 99  ? 27.589  -18.717 -18.096 1.00 106.06 ? 99  TYR B CE1 1 
ATOM   3729  C CE2 . TYR B 1 99  ? 27.465  -21.000 -17.392 1.00 105.27 ? 99  TYR B CE2 1 
ATOM   3730  C CZ  . TYR B 1 99  ? 27.704  -20.063 -18.373 1.00 105.70 ? 99  TYR B CZ  1 
ATOM   3731  O OH  . TYR B 1 99  ? 28.057  -20.472 -19.636 1.00 104.69 ? 99  TYR B OH  1 
ATOM   3732  N N   . TYR B 1 100 ? 23.575  -19.694 -14.481 1.00 110.47 ? 100 TYR B N   1 
ATOM   3733  C CA  . TYR B 1 100 ? 22.307  -20.243 -14.936 1.00 111.24 ? 100 TYR B CA  1 
ATOM   3734  C C   . TYR B 1 100 ? 21.319  -19.110 -15.184 1.00 110.10 ? 100 TYR B C   1 
ATOM   3735  O O   . TYR B 1 100 ? 21.237  -18.160 -14.401 1.00 108.73 ? 100 TYR B O   1 
ATOM   3736  C CB  . TYR B 1 100 ? 21.755  -21.219 -13.892 1.00 120.29 ? 100 TYR B CB  1 
ATOM   3737  C CG  . TYR B 1 100 ? 20.754  -22.235 -14.409 1.00 123.45 ? 100 TYR B CG  1 
ATOM   3738  C CD1 . TYR B 1 100 ? 20.337  -23.289 -13.608 1.00 129.69 ? 100 TYR B CD1 1 
ATOM   3739  C CD2 . TYR B 1 100 ? 20.211  -22.132 -15.685 1.00 123.03 ? 100 TYR B CD2 1 
ATOM   3740  C CE1 . TYR B 1 100 ? 19.417  -24.214 -14.064 1.00 132.18 ? 100 TYR B CE1 1 
ATOM   3741  C CE2 . TYR B 1 100 ? 19.290  -23.051 -16.150 1.00 123.49 ? 100 TYR B CE2 1 
ATOM   3742  C CZ  . TYR B 1 100 ? 18.897  -24.090 -15.335 1.00 126.31 ? 100 TYR B CZ  1 
ATOM   3743  O OH  . TYR B 1 100 ? 17.981  -25.009 -15.794 1.00 127.06 ? 100 TYR B OH  1 
ATOM   3744  N N   . PHE B 1 101 ? 20.572  -19.226 -16.282 1.00 115.10 ? 101 PHE B N   1 
ATOM   3745  C CA  . PHE B 1 101 ? 19.648  -18.199 -16.772 1.00 117.45 ? 101 PHE B CA  1 
ATOM   3746  C C   . PHE B 1 101 ? 20.220  -16.793 -16.599 1.00 115.29 ? 101 PHE B C   1 
ATOM   3747  O O   . PHE B 1 101 ? 19.587  -15.888 -16.052 1.00 114.81 ? 101 PHE B O   1 
ATOM   3748  C CB  . PHE B 1 101 ? 18.265  -18.323 -16.116 1.00 119.00 ? 101 PHE B CB  1 
ATOM   3749  C CG  . PHE B 1 101 ? 18.295  -18.563 -14.629 1.00 119.30 ? 101 PHE B CG  1 
ATOM   3750  C CD1 . PHE B 1 101 ? 18.215  -19.850 -14.121 1.00 118.82 ? 101 PHE B CD1 1 
ATOM   3751  C CD2 . PHE B 1 101 ? 18.384  -17.503 -13.742 1.00 119.42 ? 101 PHE B CD2 1 
ATOM   3752  C CE1 . PHE B 1 101 ? 18.237  -20.075 -12.756 1.00 115.17 ? 101 PHE B CE1 1 
ATOM   3753  C CE2 . PHE B 1 101 ? 18.408  -17.723 -12.378 1.00 114.93 ? 101 PHE B CE2 1 
ATOM   3754  C CZ  . PHE B 1 101 ? 18.333  -19.010 -11.884 1.00 112.19 ? 101 PHE B CZ  1 
ATOM   3755  N N   . ARG B 1 102 ? 21.448  -16.617 -17.091 1.00 103.89 ? 102 ARG B N   1 
ATOM   3756  C CA  . ARG B 1 102 ? 22.019  -15.283 -17.202 1.00 100.03 ? 102 ARG B CA  1 
ATOM   3757  C C   . ARG B 1 102 ? 21.314  -14.459 -18.268 1.00 100.11 ? 102 ARG B C   1 
ATOM   3758  O O   . ARG B 1 102 ? 21.407  -13.226 -18.251 1.00 97.01  ? 102 ARG B O   1 
ATOM   3759  C CB  . ARG B 1 102 ? 23.506  -15.373 -17.529 1.00 99.97  ? 102 ARG B CB  1 
ATOM   3760  C CG  . ARG B 1 102 ? 23.792  -16.073 -18.840 1.00 99.10  ? 102 ARG B CG  1 
ATOM   3761  C CD  . ARG B 1 102 ? 25.214  -15.827 -19.279 1.00 97.32  ? 102 ARG B CD  1 
ATOM   3762  N NE  . ARG B 1 102 ? 25.389  -14.425 -19.645 1.00 96.97  ? 102 ARG B NE  1 
ATOM   3763  C CZ  . ARG B 1 102 ? 26.506  -13.916 -20.150 1.00 96.62  ? 102 ARG B CZ  1 
ATOM   3764  N NH1 . ARG B 1 102 ? 27.561  -14.693 -20.341 1.00 101.61 ? 102 ARG B NH1 1 
ATOM   3765  N NH2 . ARG B 1 102 ? 26.570  -12.626 -20.452 1.00 93.74  ? 102 ARG B NH2 1 
ATOM   3766  N N   . ASP B 1 103 ? 20.616  -15.122 -19.190 1.00 109.15 ? 103 ASP B N   1 
ATOM   3767  C CA  . ASP B 1 103 ? 19.876  -14.423 -20.234 1.00 111.17 ? 103 ASP B CA  1 
ATOM   3768  C C   . ASP B 1 103 ? 18.697  -13.657 -19.653 1.00 111.29 ? 103 ASP B C   1 
ATOM   3769  O O   . ASP B 1 103 ? 18.446  -12.506 -20.032 1.00 109.97 ? 103 ASP B O   1 
ATOM   3770  C CB  . ASP B 1 103 ? 19.395  -15.432 -21.277 1.00 111.75 ? 103 ASP B CB  1 
ATOM   3771  C CG  . ASP B 1 103 ? 18.776  -16.669 -20.643 1.00 118.82 ? 103 ASP B CG  1 
ATOM   3772  O OD1 . ASP B 1 103 ? 18.595  -16.680 -19.406 1.00 113.30 ? 103 ASP B OD1 1 
ATOM   3773  O OD2 . ASP B 1 103 ? 18.472  -17.631 -21.379 1.00 127.41 ? 103 ASP B OD2 1 
ATOM   3774  N N   . ARG B 1 104 ? 17.959  -14.284 -18.734 1.00 104.86 ? 104 ARG B N   1 
ATOM   3775  C CA  . ARG B 1 104 ? 16.809  -13.626 -18.127 1.00 103.60 ? 104 ARG B CA  1 
ATOM   3776  C C   . ARG B 1 104 ? 17.235  -12.423 -17.301 1.00 103.10 ? 104 ARG B C   1 
ATOM   3777  O O   . ARG B 1 104 ? 16.486  -11.445 -17.194 1.00 105.96 ? 104 ARG B O   1 
ATOM   3778  C CB  . ARG B 1 104 ? 16.038  -14.617 -17.259 1.00 105.66 ? 104 ARG B CB  1 
ATOM   3779  C CG  . ARG B 1 104 ? 15.700  -15.918 -17.962 1.00 107.04 ? 104 ARG B CG  1 
ATOM   3780  C CD  . ARG B 1 104 ? 15.037  -16.895 -17.008 1.00 109.90 ? 104 ARG B CD  1 
ATOM   3781  N NE  . ARG B 1 104 ? 13.671  -16.499 -16.679 1.00 112.82 ? 104 ARG B NE  1 
ATOM   3782  C CZ  . ARG B 1 104 ? 12.588  -17.056 -17.209 1.00 112.38 ? 104 ARG B CZ  1 
ATOM   3783  N NH1 . ARG B 1 104 ? 12.710  -18.037 -18.094 1.00 116.95 ? 104 ARG B NH1 1 
ATOM   3784  N NH2 . ARG B 1 104 ? 11.382  -16.635 -16.855 1.00 103.96 ? 104 ARG B NH2 1 
ATOM   3785  N N   . ILE B 1 105 ? 18.427  -12.475 -16.711 1.00 99.11  ? 105 ILE B N   1 
ATOM   3786  C CA  . ILE B 1 105 ? 18.902  -11.371 -15.887 1.00 97.91  ? 105 ILE B CA  1 
ATOM   3787  C C   . ILE B 1 105 ? 19.353  -10.208 -16.760 1.00 97.79  ? 105 ILE B C   1 
ATOM   3788  O O   . ILE B 1 105 ? 18.994  -9.051  -16.516 1.00 96.08  ? 105 ILE B O   1 
ATOM   3789  C CB  . ILE B 1 105 ? 20.031  -11.854 -14.961 1.00 94.02  ? 105 ILE B CB  1 
ATOM   3790  C CG1 . ILE B 1 105 ? 19.599  -13.120 -14.223 1.00 95.99  ? 105 ILE B CG1 1 
ATOM   3791  C CG2 . ILE B 1 105 ? 20.411  -10.761 -13.978 1.00 88.38  ? 105 ILE B CG2 1 
ATOM   3792  C CD1 . ILE B 1 105 ? 20.679  -13.722 -13.365 1.00 97.58  ? 105 ILE B CD1 1 
ATOM   3793  N N   . MET B 1 106 ? 20.148  -10.499 -17.791 1.00 97.60  ? 106 MET B N   1 
ATOM   3794  C CA  . MET B 1 106 ? 20.591  -9.498  -18.754 1.00 96.61  ? 106 MET B CA  1 
ATOM   3795  C C   . MET B 1 106 ? 19.602  -9.311  -19.899 1.00 101.81 ? 106 MET B C   1 
ATOM   3796  O O   . MET B 1 106 ? 20.012  -8.970  -21.017 1.00 101.43 ? 106 MET B O   1 
ATOM   3797  C CB  . MET B 1 106 ? 21.974  -9.869  -19.292 1.00 96.17  ? 106 MET B CB  1 
ATOM   3798  C CG  . MET B 1 106 ? 23.097  -9.640  -18.294 1.00 92.81  ? 106 MET B CG  1 
ATOM   3799  S SD  . MET B 1 106 ? 23.404  -7.887  -18.010 1.00 103.37 ? 106 MET B SD  1 
ATOM   3800  C CE  . MET B 1 106 ? 24.039  -7.896  -16.334 1.00 90.00  ? 106 MET B CE  1 
ATOM   3801  N N   . GLU B 1 107 ? 18.307  -9.526  -19.652 1.00 104.55 ? 107 GLU B N   1 
ATOM   3802  C CA  . GLU B 1 107 ? 17.322  -9.414  -20.722 1.00 109.63 ? 107 GLU B CA  1 
ATOM   3803  C C   . GLU B 1 107 ? 17.053  -7.963  -21.095 1.00 117.47 ? 107 GLU B C   1 
ATOM   3804  O O   . GLU B 1 107 ? 16.773  -7.668  -22.263 1.00 122.11 ? 107 GLU B O   1 
ATOM   3805  C CB  . GLU B 1 107 ? 16.017  -10.099 -20.313 1.00 110.89 ? 107 GLU B CB  1 
ATOM   3806  C CG  . GLU B 1 107 ? 14.992  -10.199 -21.436 1.00 122.24 ? 107 GLU B CG  1 
ATOM   3807  C CD  . GLU B 1 107 ? 13.802  -11.060 -21.062 1.00 125.46 ? 107 GLU B CD  1 
ATOM   3808  O OE1 . GLU B 1 107 ? 14.007  -12.247 -20.734 1.00 122.64 ? 107 GLU B OE1 1 
ATOM   3809  O OE2 . GLU B 1 107 ? 12.662  -10.549 -21.096 1.00 128.15 ? 107 GLU B OE2 1 
ATOM   3810  N N   . GLU B 1 108 ? 17.134  -7.045  -20.132 1.00 131.75 ? 108 GLU B N   1 
ATOM   3811  C CA  . GLU B 1 108 ? 16.937  -5.625  -20.391 1.00 133.86 ? 108 GLU B CA  1 
ATOM   3812  C C   . GLU B 1 108 ? 18.252  -4.863  -20.469 1.00 134.64 ? 108 GLU B C   1 
ATOM   3813  O O   . GLU B 1 108 ? 18.259  -3.635  -20.324 1.00 135.89 ? 108 GLU B O   1 
ATOM   3814  C CB  . GLU B 1 108 ? 16.026  -5.006  -19.329 1.00 132.62 ? 108 GLU B CB  1 
ATOM   3815  C CG  . GLU B 1 108 ? 14.637  -5.619  -19.279 1.00 132.17 ? 108 GLU B CG  1 
ATOM   3816  C CD  . GLU B 1 108 ? 13.736  -4.947  -18.261 1.00 144.60 ? 108 GLU B CD  1 
ATOM   3817  O OE1 . GLU B 1 108 ? 14.248  -4.481  -17.221 1.00 143.97 ? 108 GLU B OE1 1 
ATOM   3818  O OE2 . GLU B 1 108 ? 12.512  -4.883  -18.507 1.00 150.67 ? 108 GLU B OE2 1 
ATOM   3819  N N   . LYS B 1 109 ? 19.355  -5.565  -20.715 1.00 109.20 ? 109 LYS B N   1 
ATOM   3820  C CA  . LYS B 1 109 ? 20.685  -4.974  -20.768 1.00 99.58  ? 109 LYS B CA  1 
ATOM   3821  C C   . LYS B 1 109 ? 20.970  -4.067  -19.565 1.00 95.61  ? 109 LYS B C   1 
ATOM   3822  O O   . LYS B 1 109 ? 21.226  -2.879  -19.724 1.00 93.05  ? 109 LYS B O   1 
ATOM   3823  C CB  . LYS B 1 109 ? 20.857  -4.198  -22.071 1.00 99.12  ? 109 LYS B CB  1 
ATOM   3824  C CG  . LYS B 1 109 ? 21.044  -5.082  -23.292 1.00 100.34 ? 109 LYS B CG  1 
ATOM   3825  C CD  . LYS B 1 109 ? 21.093  -4.262  -24.572 1.00 96.55  ? 109 LYS B CD  1 
ATOM   3826  C CE  . LYS B 1 109 ? 22.174  -3.192  -24.528 1.00 101.33 ? 109 LYS B CE  1 
ATOM   3827  N NZ  . LYS B 1 109 ? 23.551  -3.757  -24.531 1.00 105.56 ? 109 LYS B NZ  1 
ATOM   3828  N N   . PRO B 1 110 ? 20.940  -4.615  -18.345 1.00 92.84  ? 110 PRO B N   1 
ATOM   3829  C CA  . PRO B 1 110 ? 21.241  -3.779  -17.178 1.00 87.79  ? 110 PRO B CA  1 
ATOM   3830  C C   . PRO B 1 110 ? 22.728  -3.485  -17.088 1.00 85.74  ? 110 PRO B C   1 
ATOM   3831  O O   . PRO B 1 110 ? 23.571  -4.344  -17.358 1.00 85.68  ? 110 PRO B O   1 
ATOM   3832  C CB  . PRO B 1 110 ? 20.767  -4.630  -15.991 1.00 81.65  ? 110 PRO B CB  1 
ATOM   3833  C CG  . PRO B 1 110 ? 19.960  -5.749  -16.589 1.00 90.15  ? 110 PRO B CG  1 
ATOM   3834  C CD  . PRO B 1 110 ? 20.540  -5.970  -17.943 1.00 94.44  ? 110 PRO B CD  1 
ATOM   3835  N N   . SER B 1 111 ? 23.044  -2.248  -16.704 1.00 81.65  ? 111 SER B N   1 
ATOM   3836  C CA  . SER B 1 111 ? 24.441  -1.857  -16.562 1.00 76.64  ? 111 SER B CA  1 
ATOM   3837  C C   . SER B 1 111 ? 25.092  -2.594  -15.401 1.00 75.52  ? 111 SER B C   1 
ATOM   3838  O O   . SER B 1 111 ? 26.171  -3.180  -15.548 1.00 75.61  ? 111 SER B O   1 
ATOM   3839  C CB  . SER B 1 111 ? 24.545  -0.344  -16.366 1.00 81.27  ? 111 SER B CB  1 
ATOM   3840  O OG  . SER B 1 111 ? 25.866  0.038   -16.021 1.00 87.14  ? 111 SER B OG  1 
ATOM   3841  N N   . HIS B 1 112 ? 24.448  -2.573  -14.239 1.00 78.60  ? 112 HIS B N   1 
ATOM   3842  C CA  . HIS B 1 112 ? 24.950  -3.224  -13.041 1.00 73.43  ? 112 HIS B CA  1 
ATOM   3843  C C   . HIS B 1 112 ? 23.894  -4.170  -12.489 1.00 72.52  ? 112 HIS B C   1 
ATOM   3844  O O   . HIS B 1 112 ? 22.692  -3.929  -12.622 1.00 72.54  ? 112 HIS B O   1 
ATOM   3845  C CB  . HIS B 1 112 ? 25.346  -2.182  -11.997 1.00 73.13  ? 112 HIS B CB  1 
ATOM   3846  C CG  . HIS B 1 112 ? 26.233  -1.109  -12.544 1.00 74.11  ? 112 HIS B CG  1 
ATOM   3847  N ND1 . HIS B 1 112 ? 27.528  -1.350  -12.951 1.00 76.37  ? 112 HIS B ND1 1 
ATOM   3848  C CD2 . HIS B 1 112 ? 26.002  0.203   -12.783 1.00 80.39  ? 112 HIS B CD2 1 
ATOM   3849  C CE1 . HIS B 1 112 ? 28.060  -0.230  -13.404 1.00 83.99  ? 112 HIS B CE1 1 
ATOM   3850  N NE2 . HIS B 1 112 ? 27.156  0.729   -13.312 1.00 85.48  ? 112 HIS B NE2 1 
ATOM   3851  N N   . VAL B 1 113 ? 24.354  -5.254  -11.872 1.00 71.77  ? 113 VAL B N   1 
ATOM   3852  C CA  . VAL B 1 113 ? 23.480  -6.259  -11.280 1.00 70.90  ? 113 VAL B CA  1 
ATOM   3853  C C   . VAL B 1 113 ? 23.790  -6.369  -9.794  1.00 69.88  ? 113 VAL B C   1 
ATOM   3854  O O   . VAL B 1 113 ? 24.946  -6.572  -9.409  1.00 69.74  ? 113 VAL B O   1 
ATOM   3855  C CB  . VAL B 1 113 ? 23.631  -7.626  -11.975 1.00 70.99  ? 113 VAL B CB  1 
ATOM   3856  C CG1 . VAL B 1 113 ? 25.089  -7.914  -12.279 1.00 71.35  ? 113 VAL B CG1 1 
ATOM   3857  C CG2 . VAL B 1 113 ? 23.042  -8.732  -11.104 1.00 69.99  ? 113 VAL B CG2 1 
ATOM   3858  N N   . PHE B 1 114 ? 22.756  -6.241  -8.967  1.00 69.24  ? 114 PHE B N   1 
ATOM   3859  C CA  . PHE B 1 114 ? 22.895  -6.413  -7.527  1.00 68.29  ? 114 PHE B CA  1 
ATOM   3860  C C   . PHE B 1 114 ? 22.792  -7.888  -7.165  1.00 67.62  ? 114 PHE B C   1 
ATOM   3861  O O   . PHE B 1 114 ? 21.926  -8.609  -7.671  1.00 69.09  ? 114 PHE B O   1 
ATOM   3862  C CB  . PHE B 1 114 ? 21.814  -5.632  -6.772  1.00 67.94  ? 114 PHE B CB  1 
ATOM   3863  C CG  . PHE B 1 114 ? 22.098  -4.160  -6.621  1.00 68.37  ? 114 PHE B CG  1 
ATOM   3864  C CD1 . PHE B 1 114 ? 23.357  -3.640  -6.848  1.00 71.15  ? 114 PHE B CD1 1 
ATOM   3865  C CD2 . PHE B 1 114 ? 21.091  -3.295  -6.218  1.00 78.27  ? 114 PHE B CD2 1 
ATOM   3866  C CE1 . PHE B 1 114 ? 23.605  -2.284  -6.693  1.00 77.67  ? 114 PHE B CE1 1 
ATOM   3867  C CE2 . PHE B 1 114 ? 21.333  -1.943  -6.062  1.00 81.74  ? 114 PHE B CE2 1 
ATOM   3868  C CZ  . PHE B 1 114 ? 22.590  -1.437  -6.299  1.00 79.35  ? 114 PHE B CZ  1 
ATOM   3869  N N   . LEU B 1 115 ? 23.682  -8.339  -6.284  1.00 72.88  ? 115 LEU B N   1 
ATOM   3870  C CA  . LEU B 1 115 ? 23.639  -9.707  -5.772  1.00 75.74  ? 115 LEU B CA  1 
ATOM   3871  C C   . LEU B 1 115 ? 23.844  -9.647  -4.265  1.00 84.58  ? 115 LEU B C   1 
ATOM   3872  O O   . LEU B 1 115 ? 24.946  -9.346  -3.796  1.00 88.35  ? 115 LEU B O   1 
ATOM   3873  C CB  . LEU B 1 115 ? 24.691  -10.598 -6.436  1.00 76.17  ? 115 LEU B CB  1 
ATOM   3874  C CG  . LEU B 1 115 ? 24.621  -12.085 -6.063  1.00 76.40  ? 115 LEU B CG  1 
ATOM   3875  C CD1 . LEU B 1 115 ? 24.939  -12.949 -7.268  1.00 83.15  ? 115 LEU B CD1 1 
ATOM   3876  C CD2 . LEU B 1 115 ? 25.558  -12.421 -4.908  1.00 81.72  ? 115 LEU B CD2 1 
ATOM   3877  N N   . LEU B 1 116 ? 22.781  -9.922  -3.514  1.00 101.25 ? 116 LEU B N   1 
ATOM   3878  C CA  . LEU B 1 116 ? 22.838  -9.970  -2.063  1.00 100.54 ? 116 LEU B CA  1 
ATOM   3879  C C   . LEU B 1 116 ? 22.148  -11.238 -1.575  1.00 104.20 ? 116 LEU B C   1 
ATOM   3880  O O   . LEU B 1 116 ? 21.316  -11.828 -2.269  1.00 100.09 ? 116 LEU B O   1 
ATOM   3881  C CB  . LEU B 1 116 ? 22.215  -8.710  -1.445  1.00 101.28 ? 116 LEU B CB  1 
ATOM   3882  C CG  . LEU B 1 116 ? 20.855  -8.253  -1.973  1.00 101.99 ? 116 LEU B CG  1 
ATOM   3883  C CD1 . LEU B 1 116 ? 19.730  -8.843  -1.140  1.00 106.61 ? 116 LEU B CD1 1 
ATOM   3884  C CD2 . LEU B 1 116 ? 20.768  -6.734  -2.018  1.00 103.66 ? 116 LEU B CD2 1 
ATOM   3885  N N   . ASN B 1 117 ? 22.511  -11.656 -0.366  1.00 131.68 ? 117 ASN B N   1 
ATOM   3886  C CA  . ASN B 1 117 ? 22.039  -12.911 0.201   1.00 130.82 ? 117 ASN B CA  1 
ATOM   3887  C C   . ASN B 1 117 ? 20.791  -12.709 1.061   1.00 130.42 ? 117 ASN B C   1 
ATOM   3888  O O   . ASN B 1 117 ? 20.416  -11.592 1.425   1.00 130.87 ? 117 ASN B O   1 
ATOM   3889  C CB  . ASN B 1 117 ? 23.147  -13.580 1.018   1.00 130.29 ? 117 ASN B CB  1 
ATOM   3890  C CG  . ASN B 1 117 ? 22.860  -15.045 1.309   1.00 129.91 ? 117 ASN B CG  1 
ATOM   3891  O OD1 . ASN B 1 117 ? 22.001  -15.663 0.679   1.00 130.26 ? 117 ASN B OD1 1 
ATOM   3892  N ND2 . ASN B 1 117 ? 23.576  -15.603 2.278   1.00 128.71 ? 117 ASN B ND2 1 
ATOM   3893  N N   . CYS B 1 118 ? 20.138  -13.831 1.371   1.00 107.20 ? 118 CYS B N   1 
ATOM   3894  C CA  . CYS B 1 118 ? 18.907  -13.807 2.152   1.00 94.59  ? 118 CYS B CA  1 
ATOM   3895  C C   . CYS B 1 118 ? 19.169  -13.433 3.609   1.00 98.29  ? 118 CYS B C   1 
ATOM   3896  O O   . CYS B 1 118 ? 18.550  -12.504 4.143   1.00 96.19  ? 118 CYS B O   1 
ATOM   3897  C CB  . CYS B 1 118 ? 18.229  -15.174 2.054   1.00 86.00  ? 118 CYS B CB  1 
ATOM   3898  S SG  . CYS B 1 118 ? 16.919  -15.463 3.246   1.00 77.01  ? 118 CYS B SG  1 
ATOM   3899  N N   . ASP B 1 119 ? 20.080  -14.148 4.268   1.00 104.61 ? 119 ASP B N   1 
ATOM   3900  C CA  . ASP B 1 119 ? 20.331  -13.983 5.704   1.00 103.11 ? 119 ASP B CA  1 
ATOM   3901  C C   . ASP B 1 119 ? 21.406  -12.921 5.962   1.00 99.86  ? 119 ASP B C   1 
ATOM   3902  O O   . ASP B 1 119 ? 22.541  -13.210 6.343   1.00 99.11  ? 119 ASP B O   1 
ATOM   3903  C CB  . ASP B 1 119 ? 20.701  -15.324 6.325   1.00 103.26 ? 119 ASP B CB  1 
ATOM   3904  C CG  . ASP B 1 119 ? 21.704  -16.093 5.490   1.00 102.32 ? 119 ASP B CG  1 
ATOM   3905  O OD1 . ASP B 1 119 ? 22.121  -15.572 4.434   1.00 104.00 ? 119 ASP B OD1 1 
ATOM   3906  O OD2 . ASP B 1 119 ? 22.072  -17.220 5.886   1.00 100.72 ? 119 ASP B OD2 1 
ATOM   3907  N N   . VAL B 1 120 ? 21.017  -11.663 5.753   1.00 99.77  ? 120 VAL B N   1 
ATOM   3908  C CA  . VAL B 1 120 ? 21.891  -10.513 5.977   1.00 95.44  ? 120 VAL B CA  1 
ATOM   3909  C C   . VAL B 1 120 ? 21.070  -9.403  6.622   1.00 94.52  ? 120 VAL B C   1 
ATOM   3910  O O   . VAL B 1 120 ? 19.931  -9.147  6.217   1.00 97.76  ? 120 VAL B O   1 
ATOM   3911  C CB  . VAL B 1 120 ? 22.540  -10.023 4.664   1.00 93.47  ? 120 VAL B CB  1 
ATOM   3912  C CG1 . VAL B 1 120 ? 23.156  -8.644  4.846   1.00 89.79  ? 120 VAL B CG1 1 
ATOM   3913  C CG2 . VAL B 1 120 ? 23.589  -11.012 4.180   1.00 98.40  ? 120 VAL B CG2 1 
ATOM   3914  N N   . CYS B 1 121 ? 21.647  -8.743  7.638   1.00 92.89  ? 121 CYS B N   1 
ATOM   3915  C CA  . CYS B 1 121 ? 20.960  -7.684  8.388   1.00 92.22  ? 121 CYS B CA  1 
ATOM   3916  C C   . CYS B 1 121 ? 21.875  -6.464  8.505   1.00 93.05  ? 121 CYS B C   1 
ATOM   3917  O O   . CYS B 1 121 ? 22.497  -6.242  9.547   1.00 98.80  ? 121 CYS B O   1 
ATOM   3918  C CB  . CYS B 1 121 ? 20.525  -8.191  9.753   1.00 91.84  ? 121 CYS B CB  1 
ATOM   3919  S SG  . CYS B 1 121 ? 19.199  -9.405  9.675   1.00 99.48  ? 121 CYS B SG  1 
ATOM   3920  N N   . CYS B 1 122 ? 21.937  -5.671  7.440   1.00 89.60  ? 122 CYS B N   1 
ATOM   3921  C CA  . CYS B 1 122 ? 22.692  -4.424  7.399   1.00 94.82  ? 122 CYS B CA  1 
ATOM   3922  C C   . CYS B 1 122 ? 21.749  -3.258  7.107   1.00 94.41  ? 122 CYS B C   1 
ATOM   3923  O O   . CYS B 1 122 ? 20.528  -3.415  7.044   1.00 94.80  ? 122 CYS B O   1 
ATOM   3924  C CB  . CYS B 1 122 ? 23.811  -4.497  6.356   1.00 92.31  ? 122 CYS B CB  1 
ATOM   3925  S SG  . CYS B 1 122 ? 23.241  -4.952  4.703   1.00 81.01  ? 122 CYS B SG  1 
ATOM   3926  N N   . SER B 1 123 ? 22.331  -2.068  6.941   1.00 93.67  ? 123 SER B N   1 
ATOM   3927  C CA  . SER B 1 123 ? 21.539  -0.878  6.653   1.00 88.58  ? 123 SER B CA  1 
ATOM   3928  C C   . SER B 1 123 ? 21.134  -0.776  5.186   1.00 87.02  ? 123 SER B C   1 
ATOM   3929  O O   . SER B 1 123 ? 20.237  0.010   4.863   1.00 90.69  ? 123 SER B O   1 
ATOM   3930  C CB  . SER B 1 123 ? 22.307  0.380   7.067   1.00 92.92  ? 123 SER B CB  1 
ATOM   3931  O OG  . SER B 1 123 ? 23.543  0.481   6.378   1.00 90.32  ? 123 SER B OG  1 
ATOM   3932  N N   . PHE B 1 124 ? 21.780  -1.538  4.298   1.00 83.80  ? 124 PHE B N   1 
ATOM   3933  C CA  . PHE B 1 124 ? 21.496  -1.577  2.863   1.00 82.58  ? 124 PHE B CA  1 
ATOM   3934  C C   . PHE B 1 124 ? 21.582  -0.203  2.199   1.00 84.26  ? 124 PHE B C   1 
ATOM   3935  O O   . PHE B 1 124 ? 20.547  0.371   1.835   1.00 84.53  ? 124 PHE B O   1 
ATOM   3936  C CB  . PHE B 1 124 ? 20.110  -2.181  2.611   1.00 79.39  ? 124 PHE B CB  1 
ATOM   3937  C CG  . PHE B 1 124 ? 19.994  -3.622  3.010   1.00 77.44  ? 124 PHE B CG  1 
ATOM   3938  C CD1 . PHE B 1 124 ? 20.473  -4.624  2.182   1.00 74.37  ? 124 PHE B CD1 1 
ATOM   3939  C CD2 . PHE B 1 124 ? 19.400  -3.979  4.211   1.00 82.13  ? 124 PHE B CD2 1 
ATOM   3940  C CE1 . PHE B 1 124 ? 20.369  -5.953  2.545   1.00 77.15  ? 124 PHE B CE1 1 
ATOM   3941  C CE2 . PHE B 1 124 ? 19.292  -5.306  4.581   1.00 82.40  ? 124 PHE B CE2 1 
ATOM   3942  C CZ  . PHE B 1 124 ? 19.777  -6.294  3.747   1.00 80.80  ? 124 PHE B CZ  1 
ATOM   3943  N N   . PRO B 1 125 ? 22.789  0.362   2.027   1.00 84.72  ? 125 PRO B N   1 
ATOM   3944  C CA  . PRO B 1 125 ? 22.944  1.635   1.285   1.00 85.64  ? 125 PRO B CA  1 
ATOM   3945  C C   . PRO B 1 125 ? 23.165  1.403   -0.208  1.00 89.04  ? 125 PRO B C   1 
ATOM   3946  O O   . PRO B 1 125 ? 24.225  1.704   -0.775  1.00 93.45  ? 125 PRO B O   1 
ATOM   3947  C CB  . PRO B 1 125 ? 24.157  2.273   1.973   1.00 84.66  ? 125 PRO B CB  1 
ATOM   3948  C CG  . PRO B 1 125 ? 24.767  1.187   2.873   1.00 87.18  ? 125 PRO B CG  1 
ATOM   3949  C CD  . PRO B 1 125 ? 24.079  -0.102  2.555   1.00 86.76  ? 125 PRO B CD  1 
ATOM   3950  N N   . LEU B 1 126 ? 22.141  0.847   -0.862  1.00 92.78  ? 126 LEU B N   1 
ATOM   3951  C CA  . LEU B 1 126 ? 22.283  0.415   -2.249  1.00 90.35  ? 126 LEU B CA  1 
ATOM   3952  C C   . LEU B 1 126 ? 22.616  1.582   -3.172  1.00 102.44 ? 126 LEU B C   1 
ATOM   3953  O O   . LEU B 1 126 ? 23.368  1.419   -4.140  1.00 95.86  ? 126 LEU B O   1 
ATOM   3954  C CB  . LEU B 1 126 ? 21.011  -0.293  -2.712  1.00 89.22  ? 126 LEU B CB  1 
ATOM   3955  C CG  . LEU B 1 126 ? 20.600  -1.531  -1.913  1.00 84.72  ? 126 LEU B CG  1 
ATOM   3956  C CD1 . LEU B 1 126 ? 19.395  -2.204  -2.549  1.00 87.16  ? 126 LEU B CD1 1 
ATOM   3957  C CD2 . LEU B 1 126 ? 21.765  -2.499  -1.804  1.00 84.74  ? 126 LEU B CD2 1 
ATOM   3958  N N   . GLN B 1 127 ? 22.071  2.768   -2.892  1.00 135.69 ? 127 GLN B N   1 
ATOM   3959  C CA  . GLN B 1 127 ? 22.342  3.916   -3.750  1.00 137.89 ? 127 GLN B CA  1 
ATOM   3960  C C   . GLN B 1 127 ? 23.749  4.461   -3.539  1.00 138.43 ? 127 GLN B C   1 
ATOM   3961  O O   . GLN B 1 127 ? 24.317  5.072   -4.450  1.00 139.84 ? 127 GLN B O   1 
ATOM   3962  C CB  . GLN B 1 127 ? 21.310  5.015   -3.497  1.00 139.75 ? 127 GLN B CB  1 
ATOM   3963  C CG  . GLN B 1 127 ? 21.278  6.110   -4.552  1.00 143.19 ? 127 GLN B CG  1 
ATOM   3964  C CD  . GLN B 1 127 ? 20.108  7.053   -4.362  1.00 151.64 ? 127 GLN B CD  1 
ATOM   3965  O OE1 . GLN B 1 127 ? 19.213  6.791   -3.559  1.00 144.36 ? 127 GLN B OE1 1 
ATOM   3966  N NE2 . GLN B 1 127 ? 20.108  8.157   -5.100  1.00 162.06 ? 127 GLN B NE2 1 
ATOM   3967  N N   . GLY B 1 128 ? 24.330  4.240   -2.363  1.00 109.92 ? 128 GLY B N   1 
ATOM   3968  C CA  . GLY B 1 128 ? 25.676  4.706   -2.095  1.00 109.58 ? 128 GLY B CA  1 
ATOM   3969  C C   . GLY B 1 128 ? 26.735  3.784   -2.658  1.00 105.31 ? 128 GLY B C   1 
ATOM   3970  O O   . GLY B 1 128 ? 27.776  4.239   -3.145  1.00 105.72 ? 128 GLY B O   1 
ATOM   3971  N N   . ILE B 1 129 ? 26.481  2.476   -2.593  1.00 101.03 ? 129 ILE B N   1 
ATOM   3972  C CA  . ILE B 1 129 ? 27.432  1.514   -3.135  1.00 98.09  ? 129 ILE B CA  1 
ATOM   3973  C C   . ILE B 1 129 ? 27.360  1.479   -4.658  1.00 94.58  ? 129 ILE B C   1 
ATOM   3974  O O   . ILE B 1 129 ? 28.374  1.245   -5.328  1.00 97.02  ? 129 ILE B O   1 
ATOM   3975  C CB  . ILE B 1 129 ? 27.189  0.129   -2.506  1.00 91.86  ? 129 ILE B CB  1 
ATOM   3976  C CG1 . ILE B 1 129 ? 28.176  -0.904  -3.045  1.00 90.22  ? 129 ILE B CG1 1 
ATOM   3977  C CG2 . ILE B 1 129 ? 25.768  -0.331  -2.756  1.00 96.13  ? 129 ILE B CG2 1 
ATOM   3978  C CD1 . ILE B 1 129 ? 29.619  -0.503  -2.926  1.00 100.38 ? 129 ILE B CD1 1 
ATOM   3979  N N   . LEU B 1 130 ? 26.179  1.718   -5.234  1.00 101.79 ? 130 LEU B N   1 
ATOM   3980  C CA  . LEU B 1 130 ? 26.068  1.794   -6.688  1.00 93.71  ? 130 LEU B CA  1 
ATOM   3981  C C   . LEU B 1 130 ? 26.926  2.929   -7.232  1.00 101.95 ? 130 LEU B C   1 
ATOM   3982  O O   . LEU B 1 130 ? 27.674  2.753   -8.200  1.00 101.80 ? 130 LEU B O   1 
ATOM   3983  C CB  . LEU B 1 130 ? 24.603  1.975   -7.092  1.00 95.57  ? 130 LEU B CB  1 
ATOM   3984  C CG  . LEU B 1 130 ? 24.129  1.503   -8.473  1.00 86.47  ? 130 LEU B CG  1 
ATOM   3985  C CD1 . LEU B 1 130 ? 22.617  1.622   -8.553  1.00 90.44  ? 130 LEU B CD1 1 
ATOM   3986  C CD2 . LEU B 1 130 ? 24.777  2.266   -9.620  1.00 93.55  ? 130 LEU B CD2 1 
ATOM   3987  N N   . ASP B 1 131 ? 26.830  4.108   -6.614  1.00 115.16 ? 131 ASP B N   1 
ATOM   3988  C CA  . ASP B 1 131 ? 27.611  5.252   -7.070  1.00 117.09 ? 131 ASP B CA  1 
ATOM   3989  C C   . ASP B 1 131 ? 29.093  5.085   -6.760  1.00 116.53 ? 131 ASP B C   1 
ATOM   3990  O O   . ASP B 1 131 ? 29.941  5.579   -7.512  1.00 117.81 ? 131 ASP B O   1 
ATOM   3991  C CB  . ASP B 1 131 ? 27.073  6.532   -6.439  1.00 118.48 ? 131 ASP B CB  1 
ATOM   3992  C CG  . ASP B 1 131 ? 25.590  6.718   -6.678  1.00 119.63 ? 131 ASP B CG  1 
ATOM   3993  O OD1 . ASP B 1 131 ? 25.075  6.156   -7.668  1.00 120.07 ? 131 ASP B OD1 1 
ATOM   3994  O OD2 . ASP B 1 131 ? 24.941  7.429   -5.882  1.00 120.60 ? 131 ASP B OD2 1 
ATOM   3995  N N   . ALA B 1 132 ? 29.425  4.408   -5.659  1.00 105.36 ? 132 ALA B N   1 
ATOM   3996  C CA  . ALA B 1 132 ? 30.825  4.109   -5.381  1.00 101.19 ? 132 ALA B CA  1 
ATOM   3997  C C   . ALA B 1 132 ? 31.395  3.139   -6.406  1.00 102.58 ? 132 ALA B C   1 
ATOM   3998  O O   . ALA B 1 132 ? 32.588  3.201   -6.720  1.00 107.58 ? 132 ALA B O   1 
ATOM   3999  C CB  . ALA B 1 132 ? 30.977  3.545   -3.968  1.00 99.69  ? 132 ALA B CB  1 
ATOM   4000  N N   . HIS B 1 133 ? 30.559  2.246   -6.939  1.00 91.95  ? 133 HIS B N   1 
ATOM   4001  C CA  . HIS B 1 133 ? 31.019  1.307   -7.956  1.00 91.15  ? 133 HIS B CA  1 
ATOM   4002  C C   . HIS B 1 133 ? 31.220  1.991   -9.301  1.00 98.62  ? 133 HIS B C   1 
ATOM   4003  O O   . HIS B 1 133 ? 32.157  1.660   -10.037 1.00 102.01 ? 133 HIS B O   1 
ATOM   4004  C CB  . HIS B 1 133 ? 30.025  0.156   -8.088  1.00 85.88  ? 133 HIS B CB  1 
ATOM   4005  C CG  . HIS B 1 133 ? 30.351  -0.794  -9.197  1.00 80.54  ? 133 HIS B CG  1 
ATOM   4006  N ND1 . HIS B 1 133 ? 31.628  -1.256  -9.430  1.00 81.09  ? 133 HIS B ND1 1 
ATOM   4007  C CD2 . HIS B 1 133 ? 29.564  -1.370  -10.137 1.00 76.53  ? 133 HIS B CD2 1 
ATOM   4008  C CE1 . HIS B 1 133 ? 31.615  -2.072  -10.469 1.00 80.20  ? 133 HIS B CE1 1 
ATOM   4009  N NE2 . HIS B 1 133 ? 30.374  -2.160  -10.915 1.00 77.52  ? 133 HIS B NE2 1 
ATOM   4010  N N   . ARG B 1 134 ? 30.344  2.938   -9.646  1.00 103.91 ? 134 ARG B N   1 
ATOM   4011  C CA  . ARG B 1 134 ? 30.508  3.678   -10.893 1.00 106.60 ? 134 ARG B CA  1 
ATOM   4012  C C   . ARG B 1 134 ? 31.815  4.459   -10.914 1.00 116.31 ? 134 ARG B C   1 
ATOM   4013  O O   . ARG B 1 134 ? 32.447  4.587   -11.968 1.00 108.72 ? 134 ARG B O   1 
ATOM   4014  C CB  . ARG B 1 134 ? 29.322  4.619   -11.102 1.00 104.81 ? 134 ARG B CB  1 
ATOM   4015  C CG  . ARG B 1 134 ? 28.041  3.918   -11.518 1.00 97.87  ? 134 ARG B CG  1 
ATOM   4016  C CD  . ARG B 1 134 ? 26.878  4.892   -11.565 1.00 94.83  ? 134 ARG B CD  1 
ATOM   4017  N NE  . ARG B 1 134 ? 25.692  4.291   -12.165 1.00 97.63  ? 134 ARG B NE  1 
ATOM   4018  C CZ  . ARG B 1 134 ? 24.489  4.856   -12.173 1.00 98.29  ? 134 ARG B CZ  1 
ATOM   4019  N NH1 . ARG B 1 134 ? 24.305  6.042   -11.610 1.00 101.62 ? 134 ARG B NH1 1 
ATOM   4020  N NH2 . ARG B 1 134 ? 23.468  4.232   -12.744 1.00 93.33  ? 134 ARG B NH2 1 
ATOM   4021  N N   . ARG B 1 135 ? 32.241  4.976   -9.762  1.00 186.30 ? 135 ARG B N   1 
ATOM   4022  C CA  . ARG B 1 135 ? 33.506  5.695   -9.681  1.00 186.71 ? 135 ARG B CA  1 
ATOM   4023  C C   . ARG B 1 135 ? 34.699  4.748   -9.707  1.00 185.27 ? 135 ARG B C   1 
ATOM   4024  O O   . ARG B 1 135 ? 35.680  5.005   -10.414 1.00 186.02 ? 135 ARG B O   1 
ATOM   4025  C CB  . ARG B 1 135 ? 33.529  6.554   -8.419  1.00 186.62 ? 135 ARG B CB  1 
ATOM   4026  C CG  . ARG B 1 135 ? 34.888  7.117   -8.070  1.00 186.83 ? 135 ARG B CG  1 
ATOM   4027  C CD  . ARG B 1 135 ? 34.794  8.056   -6.884  1.00 187.27 ? 135 ARG B CD  1 
ATOM   4028  N NE  . ARG B 1 135 ? 36.107  8.351   -6.322  1.00 187.31 ? 135 ARG B NE  1 
ATOM   4029  C CZ  . ARG B 1 135 ? 36.609  7.723   -5.264  1.00 185.73 ? 135 ARG B CZ  1 
ATOM   4030  N NH1 . ARG B 1 135 ? 35.900  6.785   -4.655  1.00 184.85 ? 135 ARG B NH1 1 
ATOM   4031  N NH2 . ARG B 1 135 ? 37.811  8.036   -4.806  1.00 184.79 ? 135 ARG B NH2 1 
ATOM   4032  N N   . TYR B 1 136 ? 34.635  3.655   -8.945  1.00 129.01 ? 136 TYR B N   1 
ATOM   4033  C CA  . TYR B 1 136 ? 35.724  2.683   -8.947  1.00 109.32 ? 136 TYR B CA  1 
ATOM   4034  C C   . TYR B 1 136 ? 35.860  2.008   -10.304 1.00 101.82 ? 136 TYR B C   1 
ATOM   4035  O O   . TYR B 1 136 ? 36.976  1.801   -10.794 1.00 98.29  ? 136 TYR B O   1 
ATOM   4036  C CB  . TYR B 1 136 ? 35.494  1.630   -7.862  1.00 97.62  ? 136 TYR B CB  1 
ATOM   4037  C CG  . TYR B 1 136 ? 35.556  2.163   -6.452  1.00 96.00  ? 136 TYR B CG  1 
ATOM   4038  C CD1 . TYR B 1 136 ? 36.320  3.276   -6.138  1.00 106.54 ? 136 TYR B CD1 1 
ATOM   4039  C CD2 . TYR B 1 136 ? 34.840  1.553   -5.433  1.00 91.18  ? 136 TYR B CD2 1 
ATOM   4040  C CE1 . TYR B 1 136 ? 36.373  3.758   -4.847  1.00 107.14 ? 136 TYR B CE1 1 
ATOM   4041  C CE2 . TYR B 1 136 ? 34.884  2.029   -4.141  1.00 92.62  ? 136 TYR B CE2 1 
ATOM   4042  C CZ  . TYR B 1 136 ? 35.651  3.133   -3.852  1.00 96.34  ? 136 TYR B CZ  1 
ATOM   4043  O OH  . TYR B 1 136 ? 35.697  3.611   -2.563  1.00 97.85  ? 136 TYR B OH  1 
ATOM   4044  N N   . GLY B 1 137 ? 34.736  1.662   -10.925 1.00 102.50 ? 137 GLY B N   1 
ATOM   4045  C CA  . GLY B 1 137 ? 34.773  0.866   -12.134 1.00 93.50  ? 137 GLY B CA  1 
ATOM   4046  C C   . GLY B 1 137 ? 35.032  -0.595  -11.801 1.00 84.13  ? 137 GLY B C   1 
ATOM   4047  O O   . GLY B 1 137 ? 34.697  -1.081  -10.718 1.00 83.93  ? 137 GLY B O   1 
ATOM   4048  N N   . GLY B 1 138 ? 35.641  -1.298  -12.745 1.00 81.73  ? 138 GLY B N   1 
ATOM   4049  C CA  . GLY B 1 138 ? 35.904  -2.704  -12.537 1.00 84.20  ? 138 GLY B CA  1 
ATOM   4050  C C   . GLY B 1 138 ? 34.629  -3.534  -12.495 1.00 78.28  ? 138 GLY B C   1 
ATOM   4051  O O   . GLY B 1 138 ? 33.534  -3.093  -12.847 1.00 75.45  ? 138 GLY B O   1 
ATOM   4052  N N   . ILE B 1 139 ? 34.800  -4.775  -12.047 1.00 76.19  ? 139 ILE B N   1 
ATOM   4053  C CA  . ILE B 1 139 ? 33.706  -5.738  -12.015 1.00 75.47  ? 139 ILE B CA  1 
ATOM   4054  C C   . ILE B 1 139 ? 32.800  -5.479  -10.820 1.00 74.57  ? 139 ILE B C   1 
ATOM   4055  O O   . ILE B 1 139 ? 31.651  -5.056  -10.984 1.00 79.92  ? 139 ILE B O   1 
ATOM   4056  C CB  . ILE B 1 139 ? 34.238  -7.181  -11.998 1.00 77.30  ? 139 ILE B CB  1 
ATOM   4057  C CG1 . ILE B 1 139 ? 35.143  -7.422  -13.208 1.00 83.13  ? 139 ILE B CG1 1 
ATOM   4058  C CG2 . ILE B 1 139 ? 33.081  -8.168  -11.979 1.00 76.59  ? 139 ILE B CG2 1 
ATOM   4059  C CD1 . ILE B 1 139 ? 34.427  -7.385  -14.536 1.00 81.19  ? 139 ILE B CD1 1 
ATOM   4060  N N   . GLY B 1 140 ? 33.307  -5.724  -9.612  1.00 72.15  ? 140 GLY B N   1 
ATOM   4061  C CA  . GLY B 1 140 ? 32.484  -5.639  -8.420  1.00 71.13  ? 140 GLY B CA  1 
ATOM   4062  C C   . GLY B 1 140 ? 32.927  -4.572  -7.440  1.00 72.00  ? 140 GLY B C   1 
ATOM   4063  O O   . GLY B 1 140 ? 33.835  -3.788  -7.735  1.00 78.19  ? 140 GLY B O   1 
ATOM   4064  N N   . THR B 1 141 ? 32.291  -4.531  -6.267  1.00 71.18  ? 141 THR B N   1 
ATOM   4065  C CA  . THR B 1 141 ? 32.633  -3.529  -5.264  1.00 76.00  ? 141 THR B CA  1 
ATOM   4066  C C   . THR B 1 141 ? 32.458  -4.030  -3.835  1.00 85.54  ? 141 THR B C   1 
ATOM   4067  O O   . THR B 1 141 ? 32.920  -3.375  -2.895  1.00 92.48  ? 141 THR B O   1 
ATOM   4068  C CB  . THR B 1 141 ? 31.792  -2.271  -5.473  1.00 76.31  ? 141 THR B CB  1 
ATOM   4069  O OG1 . THR B 1 141 ? 30.911  -2.474  -6.582  1.00 77.35  ? 141 THR B OG1 1 
ATOM   4070  C CG2 . THR B 1 141 ? 32.685  -1.090  -5.766  1.00 81.38  ? 141 THR B CG2 1 
ATOM   4071  N N   . MET B 1 142 ? 31.793  -5.174  -3.658  1.00 82.60  ? 142 MET B N   1 
ATOM   4072  C CA  . MET B 1 142 ? 31.636  -5.810  -2.350  1.00 91.39  ? 142 MET B CA  1 
ATOM   4073  C C   . MET B 1 142 ? 31.025  -4.881  -1.304  1.00 96.99  ? 142 MET B C   1 
ATOM   4074  O O   . MET B 1 142 ? 30.340  -3.910  -1.644  1.00 98.37  ? 142 MET B O   1 
ATOM   4075  C CB  . MET B 1 142 ? 32.983  -6.327  -1.843  1.00 90.62  ? 142 MET B CB  1 
ATOM   4076  C CG  . MET B 1 142 ? 33.126  -7.835  -1.860  1.00 92.96  ? 142 MET B CG  1 
ATOM   4077  S SD  . MET B 1 142 ? 34.496  -8.372  -0.817  1.00 98.34  ? 142 MET B SD  1 
ATOM   4078  C CE  . MET B 1 142 ? 34.061  -7.585  0.730   1.00 113.87 ? 142 MET B CE  1 
ATOM   4079  N N   . LEU B 1 143 ? 31.276  -5.183  -0.030  1.00 98.66  ? 143 LEU B N   1 
ATOM   4080  C CA  . LEU B 1 143 ? 30.945  -4.325  1.098   1.00 105.08 ? 143 LEU B CA  1 
ATOM   4081  C C   . LEU B 1 143 ? 31.695  -4.845  2.312   1.00 109.52 ? 143 LEU B C   1 
ATOM   4082  O O   . LEU B 1 143 ? 31.812  -6.058  2.497   1.00 109.00 ? 143 LEU B O   1 
ATOM   4083  C CB  . LEU B 1 143 ? 29.441  -4.296  1.383   1.00 104.93 ? 143 LEU B CB  1 
ATOM   4084  C CG  . LEU B 1 143 ? 29.011  -3.145  2.300   1.00 107.44 ? 143 LEU B CG  1 
ATOM   4085  C CD1 . LEU B 1 143 ? 28.497  -1.983  1.461   1.00 110.54 ? 143 LEU B CD1 1 
ATOM   4086  C CD2 . LEU B 1 143 ? 27.977  -3.557  3.339   1.00 98.74  ? 143 LEU B CD2 1 
ATOM   4087  N N   . VAL B 1 144 ? 32.182  -3.926  3.145   1.00 120.63 ? 144 VAL B N   1 
ATOM   4088  C CA  . VAL B 1 144 ? 33.004  -4.266  4.299   1.00 118.56 ? 144 VAL B CA  1 
ATOM   4089  C C   . VAL B 1 144 ? 32.495  -3.503  5.514   1.00 117.07 ? 144 VAL B C   1 
ATOM   4090  O O   . VAL B 1 144 ? 31.685  -2.582  5.408   1.00 117.79 ? 144 VAL B O   1 
ATOM   4091  C CB  . VAL B 1 144 ? 34.498  -3.964  4.063   1.00 125.19 ? 144 VAL B CB  1 
ATOM   4092  C CG1 . VAL B 1 144 ? 35.098  -4.951  3.075   1.00 126.03 ? 144 VAL B CG1 1 
ATOM   4093  C CG2 . VAL B 1 144 ? 34.674  -2.539  3.570   1.00 124.90 ? 144 VAL B CG2 1 
ATOM   4094  N N   . ILE B 1 145 ? 32.981  -3.910  6.682   1.00 112.32 ? 145 ILE B N   1 
ATOM   4095  C CA  . ILE B 1 145 ? 32.633  -3.267  7.945   1.00 115.17 ? 145 ILE B CA  1 
ATOM   4096  C C   . ILE B 1 145 ? 33.771  -3.494  8.930   1.00 122.19 ? 145 ILE B C   1 
ATOM   4097  O O   . ILE B 1 145 ? 34.278  -4.612  9.059   1.00 126.03 ? 145 ILE B O   1 
ATOM   4098  C CB  . ILE B 1 145 ? 31.293  -3.790  8.506   1.00 113.26 ? 145 ILE B CB  1 
ATOM   4099  C CG1 . ILE B 1 145 ? 30.979  -3.135  9.852   1.00 114.11 ? 145 ILE B CG1 1 
ATOM   4100  C CG2 . ILE B 1 145 ? 31.303  -5.310  8.618   1.00 108.97 ? 145 ILE B CG2 1 
ATOM   4101  C CD1 . ILE B 1 145 ? 29.589  -3.434  10.368  1.00 113.51 ? 145 ILE B CD1 1 
ATOM   4102  N N   . LYS B 1 146 ? 34.189  -2.428  9.609   1.00 123.93 ? 146 LYS B N   1 
ATOM   4103  C CA  . LYS B 1 146 ? 35.305  -2.519  10.541  1.00 130.95 ? 146 LYS B CA  1 
ATOM   4104  C C   . LYS B 1 146 ? 34.882  -3.288  11.787  1.00 141.21 ? 146 LYS B C   1 
ATOM   4105  O O   . LYS B 1 146 ? 33.976  -2.862  12.512  1.00 135.10 ? 146 LYS B O   1 
ATOM   4106  C CB  . LYS B 1 146 ? 35.798  -1.123  10.912  1.00 126.53 ? 146 LYS B CB  1 
ATOM   4107  C CG  . LYS B 1 146 ? 36.318  -0.311  9.734   1.00 124.86 ? 146 LYS B CG  1 
ATOM   4108  C CD  . LYS B 1 146 ? 36.841  1.050   10.180  1.00 117.64 ? 146 LYS B CD  1 
ATOM   4109  C CE  . LYS B 1 146 ? 37.399  1.844   9.007   1.00 110.67 ? 146 LYS B CE  1 
ATOM   4110  N NZ  . LYS B 1 146 ? 37.929  3.171   9.428   1.00 102.29 ? 146 LYS B NZ  1 
ATOM   4111  N N   . VAL B 1 147 ? 35.543  -4.417  12.042  1.00 174.37 ? 147 VAL B N   1 
ATOM   4112  C CA  . VAL B 1 147 ? 35.275  -5.240  13.211  1.00 175.79 ? 147 VAL B CA  1 
ATOM   4113  C C   . VAL B 1 147 ? 36.579  -5.445  13.972  1.00 184.35 ? 147 VAL B C   1 
ATOM   4114  O O   . VAL B 1 147 ? 37.670  -5.176  13.469  1.00 183.98 ? 147 VAL B O   1 
ATOM   4115  C CB  . VAL B 1 147 ? 34.642  -6.599  12.842  1.00 173.50 ? 147 VAL B CB  1 
ATOM   4116  C CG1 . VAL B 1 147 ? 33.395  -6.391  11.996  1.00 171.61 ? 147 VAL B CG1 1 
ATOM   4117  C CG2 . VAL B 1 147 ? 35.647  -7.474  12.114  1.00 173.02 ? 147 VAL B CG2 1 
ATOM   4118  N N   . SER B 1 148 ? 36.448  -5.926  15.205  1.00 194.96 ? 148 SER B N   1 
ATOM   4119  C CA  . SER B 1 148 ? 37.612  -6.199  16.034  1.00 195.55 ? 148 SER B CA  1 
ATOM   4120  C C   . SER B 1 148 ? 38.397  -7.390  15.494  1.00 194.84 ? 148 SER B C   1 
ATOM   4121  O O   . SER B 1 148 ? 37.841  -8.309  14.885  1.00 193.81 ? 148 SER B O   1 
ATOM   4122  C CB  . SER B 1 148 ? 37.187  -6.465  17.478  1.00 195.98 ? 148 SER B CB  1 
ATOM   4123  O OG  . SER B 1 148 ? 36.409  -7.645  17.569  1.00 195.34 ? 148 SER B OG  1 
ATOM   4124  N N   . ALA B 1 149 ? 39.714  -7.363  15.723  1.00 171.10 ? 149 ALA B N   1 
ATOM   4125  C CA  . ALA B 1 149 ? 40.568  -8.458  15.276  1.00 161.35 ? 149 ALA B CA  1 
ATOM   4126  C C   . ALA B 1 149 ? 40.276  -9.747  16.032  1.00 152.30 ? 149 ALA B C   1 
ATOM   4127  O O   . ALA B 1 149 ? 40.511  -10.840 15.503  1.00 148.72 ? 149 ALA B O   1 
ATOM   4128  C CB  . ALA B 1 149 ? 42.041  -8.074  15.425  1.00 155.60 ? 149 ALA B CB  1 
ATOM   4129  N N   . GLU B 1 150 ? 39.779  -9.645  17.268  1.00 151.69 ? 150 GLU B N   1 
ATOM   4130  C CA  . GLU B 1 150 ? 39.391  -10.842 18.007  1.00 142.58 ? 150 GLU B CA  1 
ATOM   4131  C C   . GLU B 1 150 ? 38.235  -11.561 17.327  1.00 140.56 ? 150 GLU B C   1 
ATOM   4132  O O   . GLU B 1 150 ? 38.148  -12.793 17.385  1.00 133.85 ? 150 GLU B O   1 
ATOM   4133  C CB  . GLU B 1 150 ? 39.020  -10.479 19.445  1.00 133.85 ? 150 GLU B CB  1 
ATOM   4134  C CG  . GLU B 1 150 ? 39.622  -11.399 20.499  1.00 123.94 ? 150 GLU B CG  1 
ATOM   4135  C CD  . GLU B 1 150 ? 39.034  -12.795 20.464  1.00 120.06 ? 150 GLU B CD  1 
ATOM   4136  O OE1 . GLU B 1 150 ? 37.822  -12.928 20.195  1.00 121.85 ? 150 GLU B OE1 1 
ATOM   4137  O OE2 . GLU B 1 150 ? 39.784  -13.761 20.713  1.00 116.01 ? 150 GLU B OE2 1 
ATOM   4138  N N   . ALA B 1 151 ? 37.351  -10.813 16.665  1.00 145.56 ? 151 ALA B N   1 
ATOM   4139  C CA  . ALA B 1 151 ? 36.251  -11.396 15.900  1.00 152.22 ? 151 ALA B CA  1 
ATOM   4140  C C   . ALA B 1 151 ? 36.773  -11.788 14.518  1.00 153.51 ? 151 ALA B C   1 
ATOM   4141  O O   . ALA B 1 151 ? 36.494  -11.158 13.496  1.00 154.69 ? 151 ALA B O   1 
ATOM   4142  C CB  . ALA B 1 151 ? 35.086  -10.422 15.804  1.00 158.87 ? 151 ALA B CB  1 
ATOM   4143  N N   . ALA B 1 152 ? 37.553  -12.863 14.507  1.00 161.73 ? 152 ALA B N   1 
ATOM   4144  C CA  . ALA B 1 152 ? 38.167  -13.360 13.286  1.00 162.58 ? 152 ALA B CA  1 
ATOM   4145  C C   . ALA B 1 152 ? 37.890  -14.829 13.010  1.00 167.40 ? 152 ALA B C   1 
ATOM   4146  O O   . ALA B 1 152 ? 38.086  -15.266 11.869  1.00 163.05 ? 152 ALA B O   1 
ATOM   4147  C CB  . ALA B 1 152 ? 39.684  -13.132 13.324  1.00 156.87 ? 152 ALA B CB  1 
ATOM   4148  N N   . SER B 1 153 ? 37.460  -15.607 14.007  1.00 181.35 ? 153 SER B N   1 
ATOM   4149  C CA  . SER B 1 153 ? 37.117  -17.005 13.770  1.00 183.51 ? 153 SER B CA  1 
ATOM   4150  C C   . SER B 1 153 ? 35.836  -17.145 12.957  1.00 179.24 ? 153 SER B C   1 
ATOM   4151  O O   . SER B 1 153 ? 35.658  -18.146 12.252  1.00 177.66 ? 153 SER B O   1 
ATOM   4152  C CB  . SER B 1 153 ? 36.981  -17.742 15.102  1.00 184.02 ? 153 SER B CB  1 
ATOM   4153  O OG  . SER B 1 153 ? 35.970  -17.158 15.904  1.00 180.57 ? 153 SER B OG  1 
ATOM   4154  N N   . GLN B 1 154 ? 34.931  -16.167 13.052  1.00 165.43 ? 154 GLN B N   1 
ATOM   4155  C CA  . GLN B 1 154 ? 33.670  -16.245 12.319  1.00 165.75 ? 154 GLN B CA  1 
ATOM   4156  C C   . GLN B 1 154 ? 33.901  -16.278 10.814  1.00 167.80 ? 154 GLN B C   1 
ATOM   4157  O O   . GLN B 1 154 ? 33.236  -17.033 10.094  1.00 167.92 ? 154 GLN B O   1 
ATOM   4158  C CB  . GLN B 1 154 ? 32.760  -15.078 12.707  1.00 168.18 ? 154 GLN B CB  1 
ATOM   4159  C CG  . GLN B 1 154 ? 33.492  -13.786 13.021  1.00 165.73 ? 154 GLN B CG  1 
ATOM   4160  C CD  . GLN B 1 154 ? 33.816  -13.647 14.501  1.00 166.30 ? 154 GLN B CD  1 
ATOM   4161  O OE1 . GLN B 1 154 ? 34.800  -14.204 14.990  1.00 165.84 ? 154 GLN B OE1 1 
ATOM   4162  N NE2 . GLN B 1 154 ? 32.985  -12.903 15.221  1.00 166.22 ? 154 GLN B NE2 1 
ATOM   4163  N N   . PHE B 1 155 ? 34.827  -15.461 10.318  1.00 158.29 ? 155 PHE B N   1 
ATOM   4164  C CA  . PHE B 1 155 ? 35.128  -15.442 8.894   1.00 152.57 ? 155 PHE B CA  1 
ATOM   4165  C C   . PHE B 1 155 ? 36.564  -15.887 8.635   1.00 156.47 ? 155 PHE B C   1 
ATOM   4166  O O   . PHE B 1 155 ? 36.806  -17.055 8.313   1.00 158.23 ? 155 PHE B O   1 
ATOM   4167  C CB  . PHE B 1 155 ? 34.871  -14.047 8.310   1.00 147.09 ? 155 PHE B CB  1 
ATOM   4168  C CG  . PHE B 1 155 ? 35.539  -13.812 6.989   1.00 147.08 ? 155 PHE B CG  1 
ATOM   4169  C CD1 . PHE B 1 155 ? 35.230  -14.594 5.889   1.00 154.55 ? 155 PHE B CD1 1 
ATOM   4170  C CD2 . PHE B 1 155 ? 36.491  -12.816 6.853   1.00 146.90 ? 155 PHE B CD2 1 
ATOM   4171  C CE1 . PHE B 1 155 ? 35.859  -14.383 4.681   1.00 159.82 ? 155 PHE B CE1 1 
ATOM   4172  C CE2 . PHE B 1 155 ? 37.120  -12.601 5.652   1.00 145.30 ? 155 PHE B CE2 1 
ATOM   4173  C CZ  . PHE B 1 155 ? 36.807  -13.385 4.567   1.00 153.49 ? 155 PHE B CZ  1 
ATOM   4174  N N   . GLY B 1 156 ? 37.511  -14.982 8.786   1.00 159.03 ? 156 GLY B N   1 
ATOM   4175  C CA  . GLY B 1 156 ? 38.878  -15.226 8.392   1.00 162.20 ? 156 GLY B CA  1 
ATOM   4176  C C   . GLY B 1 156 ? 39.566  -13.911 8.041   1.00 158.30 ? 156 GLY B C   1 
ATOM   4177  O O   . GLY B 1 156 ? 39.394  -12.911 8.741   1.00 153.89 ? 156 GLY B O   1 
ATOM   4178  N N   . GLU B 1 157 ? 40.324  -13.931 6.946   1.00 158.13 ? 157 GLU B N   1 
ATOM   4179  C CA  . GLU B 1 157 ? 41.159  -12.806 6.546   1.00 159.36 ? 157 GLU B CA  1 
ATOM   4180  C C   . GLU B 1 157 ? 40.615  -12.126 5.294   1.00 155.35 ? 157 GLU B C   1 
ATOM   4181  O O   . GLU B 1 157 ? 40.054  -12.773 4.406   1.00 150.83 ? 157 GLU B O   1 
ATOM   4182  C CB  . GLU B 1 157 ? 42.600  -13.254 6.294   1.00 162.47 ? 157 GLU B CB  1 
ATOM   4183  N N   . LEU B 1 158 ? 40.793  -10.805 5.239   1.00 148.60 ? 158 LEU B N   1 
ATOM   4184  C CA  . LEU B 1 158 ? 40.398  -10.010 4.080   1.00 139.36 ? 158 LEU B CA  1 
ATOM   4185  C C   . LEU B 1 158 ? 41.261  -8.758  4.032   1.00 139.71 ? 158 LEU B C   1 
ATOM   4186  O O   . LEU B 1 158 ? 41.291  -7.993  4.999   1.00 145.06 ? 158 LEU B O   1 
ATOM   4187  C CB  . LEU B 1 158 ? 38.913  -9.648  4.153   1.00 136.23 ? 158 LEU B CB  1 
ATOM   4188  C CG  . LEU B 1 158 ? 38.207  -9.186  2.876   1.00 134.96 ? 158 LEU B CG  1 
ATOM   4189  C CD1 . LEU B 1 158 ? 36.715  -9.425  3.005   1.00 129.13 ? 158 LEU B CD1 1 
ATOM   4190  C CD2 . LEU B 1 158 ? 38.476  -7.717  2.581   1.00 130.42 ? 158 LEU B CD2 1 
ATOM   4191  N N   . ILE B 1 159 ? 41.946  -8.542  2.909   1.00 139.65 ? 159 ILE B N   1 
ATOM   4192  C CA  . ILE B 1 159 ? 42.885  -7.437  2.740   1.00 135.39 ? 159 ILE B CA  1 
ATOM   4193  C C   . ILE B 1 159 ? 42.348  -6.499  1.667   1.00 124.77 ? 159 ILE B C   1 
ATOM   4194  O O   . ILE B 1 159 ? 41.958  -6.948  0.583   1.00 124.94 ? 159 ILE B O   1 
ATOM   4195  C CB  . ILE B 1 159 ? 44.291  -7.939  2.362   1.00 139.19 ? 159 ILE B CB  1 
ATOM   4196  C CG1 . ILE B 1 159 ? 44.756  -9.026  3.335   1.00 152.69 ? 159 ILE B CG1 1 
ATOM   4197  C CG2 . ILE B 1 159 ? 45.280  -6.785  2.342   1.00 130.65 ? 159 ILE B CG2 1 
ATOM   4198  C CD1 . ILE B 1 159 ? 45.026  -8.522  4.734   1.00 159.96 ? 159 ILE B CD1 1 
ATOM   4199  N N   . ALA B 1 160 ? 42.326  -5.201  1.969   1.00 113.02 ? 160 ALA B N   1 
ATOM   4200  C CA  . ALA B 1 160 ? 41.860  -4.196  1.021   1.00 105.40 ? 160 ALA B CA  1 
ATOM   4201  C C   . ALA B 1 160 ? 42.670  -2.918  1.198   1.00 103.50 ? 160 ALA B C   1 
ATOM   4202  O O   . ALA B 1 160 ? 42.786  -2.411  2.317   1.00 103.02 ? 160 ALA B O   1 
ATOM   4203  C CB  . ALA B 1 160 ? 40.365  -3.916  1.209   1.00 101.97 ? 160 ALA B CB  1 
ATOM   4204  N N   . ASP B 1 161 ? 43.229  -2.401  0.092   1.00 105.21 ? 161 ASP B N   1 
ATOM   4205  C CA  . ASP B 1 161 ? 44.051  -1.192  0.106   1.00 101.18 ? 161 ASP B CA  1 
ATOM   4206  C C   . ASP B 1 161 ? 43.189  0.061   0.209   1.00 95.08  ? 161 ASP B C   1 
ATOM   4207  O O   . ASP B 1 161 ? 42.487  0.407   -0.746  1.00 93.93  ? 161 ASP B O   1 
ATOM   4208  C CB  . ASP B 1 161 ? 44.925  -1.120  -1.148  1.00 86.75  ? 161 ASP B CB  1 
ATOM   4209  N N   . PRO B 1 162 ? 43.248  0.788   1.329   1.00 90.30  ? 162 PRO B N   1 
ATOM   4210  C CA  . PRO B 1 162 ? 42.296  1.891   1.553   1.00 87.12  ? 162 PRO B CA  1 
ATOM   4211  C C   . PRO B 1 162 ? 42.483  3.095   0.639   1.00 81.46  ? 162 PRO B C   1 
ATOM   4212  O O   . PRO B 1 162 ? 41.601  3.964   0.618   1.00 83.54  ? 162 PRO B O   1 
ATOM   4213  C CB  . PRO B 1 162 ? 42.546  2.269   3.017   1.00 89.20  ? 162 PRO B CB  1 
ATOM   4214  C CG  . PRO B 1 162 ? 43.972  1.900   3.248   1.00 91.85  ? 162 PRO B CG  1 
ATOM   4215  C CD  . PRO B 1 162 ? 44.207  0.652   2.439   1.00 93.41  ? 162 PRO B CD  1 
ATOM   4216  N N   . ASP B 1 163 ? 43.578  3.183   -0.114  1.00 80.17  ? 163 ASP B N   1 
ATOM   4217  C CA  . ASP B 1 163 ? 43.748  4.329   -1.000  1.00 76.62  ? 163 ASP B CA  1 
ATOM   4218  C C   . ASP B 1 163 ? 42.852  4.208   -2.224  1.00 75.57  ? 163 ASP B C   1 
ATOM   4219  O O   . ASP B 1 163 ? 42.119  5.143   -2.562  1.00 75.75  ? 163 ASP B O   1 
ATOM   4220  C CB  . ASP B 1 163 ? 45.212  4.469   -1.409  1.00 81.79  ? 163 ASP B CB  1 
ATOM   4221  C CG  . ASP B 1 163 ? 45.947  5.494   -0.577  1.00 76.82  ? 163 ASP B CG  1 
ATOM   4222  O OD1 . ASP B 1 163 ? 45.283  6.231   0.184   1.00 76.44  ? 163 ASP B OD1 1 
ATOM   4223  O OD2 . ASP B 1 163 ? 47.190  5.561   -0.680  1.00 81.16  ? 163 ASP B OD2 1 
ATOM   4224  N N   . THR B 1 164 ? 42.905  3.068   -2.903  1.00 78.89  ? 164 THR B N   1 
ATOM   4225  C CA  . THR B 1 164 ? 42.019  2.778   -4.020  1.00 78.77  ? 164 THR B CA  1 
ATOM   4226  C C   . THR B 1 164 ? 40.833  1.922   -3.610  1.00 80.04  ? 164 THR B C   1 
ATOM   4227  O O   . THR B 1 164 ? 39.982  1.624   -4.455  1.00 79.53  ? 164 THR B O   1 
ATOM   4228  C CB  . THR B 1 164 ? 42.786  2.072   -5.144  1.00 83.02  ? 164 THR B CB  1 
ATOM   4229  O OG1 . THR B 1 164 ? 43.331  0.840   -4.652  1.00 86.04  ? 164 THR B OG1 1 
ATOM   4230  C CG2 . THR B 1 164 ? 43.913  2.953   -5.660  1.00 84.46  ? 164 THR B CG2 1 
ATOM   4231  N N   . LYS B 1 165 ? 40.759  1.528   -2.337  1.00 83.91  ? 165 LYS B N   1 
ATOM   4232  C CA  . LYS B 1 165 ? 39.705  0.649   -1.829  1.00 82.85  ? 165 LYS B CA  1 
ATOM   4233  C C   . LYS B 1 165 ? 39.614  -0.638  -2.641  1.00 81.81  ? 165 LYS B C   1 
ATOM   4234  O O   . LYS B 1 165 ? 38.527  -1.117  -2.955  1.00 83.45  ? 165 LYS B O   1 
ATOM   4235  C CB  . LYS B 1 165 ? 38.357  1.370   -1.785  1.00 80.57  ? 165 LYS B CB  1 
ATOM   4236  C CG  . LYS B 1 165 ? 38.381  2.692   -1.031  1.00 81.03  ? 165 LYS B CG  1 
ATOM   4237  C CD  . LYS B 1 165 ? 38.330  2.463   0.474   1.00 88.21  ? 165 LYS B CD  1 
ATOM   4238  C CE  . LYS B 1 165 ? 36.941  2.019   0.919   1.00 98.51  ? 165 LYS B CE  1 
ATOM   4239  N NZ  . LYS B 1 165 ? 35.978  3.146   1.047   1.00 102.86 ? 165 LYS B NZ  1 
ATOM   4240  N N   . GLU B 1 166 ? 40.768  -1.222  -2.956  1.00 88.22  ? 166 GLU B N   1 
ATOM   4241  C CA  . GLU B 1 166 ? 40.847  -2.413  -3.790  1.00 85.12  ? 166 GLU B CA  1 
ATOM   4242  C C   . GLU B 1 166 ? 41.219  -3.627  -2.948  1.00 94.00  ? 166 GLU B C   1 
ATOM   4243  O O   . GLU B 1 166 ? 42.124  -3.561  -2.110  1.00 99.42  ? 166 GLU B O   1 
ATOM   4244  C CB  . GLU B 1 166 ? 41.870  -2.217  -4.912  1.00 90.26  ? 166 GLU B CB  1 
ATOM   4245  C CG  . GLU B 1 166 ? 41.608  -3.054  -6.153  1.00 96.77  ? 166 GLU B CG  1 
ATOM   4246  C CD  . GLU B 1 166 ? 42.375  -4.361  -6.156  1.00 102.94 ? 166 GLU B CD  1 
ATOM   4247  O OE1 . GLU B 1 166 ? 43.616  -4.323  -6.027  1.00 108.40 ? 166 GLU B OE1 1 
ATOM   4248  O OE2 . GLU B 1 166 ? 41.738  -5.424  -6.302  1.00 103.53 ? 166 GLU B OE2 1 
ATOM   4249  N N   . LEU B 1 167 ? 40.524  -4.738  -3.186  1.00 90.34  ? 167 LEU B N   1 
ATOM   4250  C CA  . LEU B 1 167 ? 40.741  -5.972  -2.434  1.00 102.83 ? 167 LEU B CA  1 
ATOM   4251  C C   . LEU B 1 167 ? 42.071  -6.599  -2.840  1.00 116.44 ? 167 LEU B C   1 
ATOM   4252  O O   . LEU B 1 167 ? 42.202  -7.131  -3.946  1.00 116.92 ? 167 LEU B O   1 
ATOM   4253  C CB  . LEU B 1 167 ? 39.587  -6.939  -2.679  1.00 102.65 ? 167 LEU B CB  1 
ATOM   4254  C CG  . LEU B 1 167 ? 39.662  -8.294  -1.974  1.00 116.86 ? 167 LEU B CG  1 
ATOM   4255  C CD1 . LEU B 1 167 ? 38.370  -8.569  -1.227  1.00 109.99 ? 167 LEU B CD1 1 
ATOM   4256  C CD2 . LEU B 1 167 ? 39.959  -9.402  -2.973  1.00 135.59 ? 167 LEU B CD2 1 
ATOM   4257  N N   . LEU B 1 168 ? 43.058  -6.548  -1.942  1.00 117.30 ? 168 LEU B N   1 
ATOM   4258  C CA  . LEU B 1 168 ? 44.386  -7.072  -2.241  1.00 120.52 ? 168 LEU B CA  1 
ATOM   4259  C C   . LEU B 1 168 ? 44.517  -8.573  -2.001  1.00 134.35 ? 168 LEU B C   1 
ATOM   4260  O O   . LEU B 1 168 ? 45.389  -9.204  -2.609  1.00 136.85 ? 168 LEU B O   1 
ATOM   4261  C CB  . LEU B 1 168 ? 45.437  -6.328  -1.417  1.00 112.17 ? 168 LEU B CB  1 
ATOM   4262  C CG  . LEU B 1 168 ? 46.291  -5.324  -2.192  1.00 103.41 ? 168 LEU B CG  1 
ATOM   4263  C CD1 . LEU B 1 168 ? 47.185  -6.045  -3.188  1.00 102.33 ? 168 LEU B CD1 1 
ATOM   4264  C CD2 . LEU B 1 168 ? 45.410  -4.311  -2.901  1.00 99.16  ? 168 LEU B CD2 1 
ATOM   4265  N N   . HIS B 1 169 ? 43.691  -9.155  -1.133  1.00 164.88 ? 169 HIS B N   1 
ATOM   4266  C CA  . HIS B 1 169 ? 43.805  -10.571 -0.803  1.00 164.23 ? 169 HIS B CA  1 
ATOM   4267  C C   . HIS B 1 169 ? 42.529  -11.015 -0.105  1.00 163.68 ? 169 HIS B C   1 
ATOM   4268  O O   . HIS B 1 169 ? 41.870  -10.217 0.568   1.00 163.63 ? 169 HIS B O   1 
ATOM   4269  C CB  . HIS B 1 169 ? 45.025  -10.846 0.088   1.00 164.37 ? 169 HIS B CB  1 
ATOM   4270  C CG  . HIS B 1 169 ? 44.979  -12.171 0.786   1.00 171.33 ? 169 HIS B CG  1 
ATOM   4271  N ND1 . HIS B 1 169 ? 44.578  -12.306 2.098   1.00 174.87 ? 169 HIS B ND1 1 
ATOM   4272  C CD2 . HIS B 1 169 ? 45.276  -13.419 0.353   1.00 172.92 ? 169 HIS B CD2 1 
ATOM   4273  C CE1 . HIS B 1 169 ? 44.633  -13.580 2.444   1.00 175.37 ? 169 HIS B CE1 1 
ATOM   4274  N NE2 . HIS B 1 169 ? 45.054  -14.276 1.404   1.00 175.21 ? 169 HIS B NE2 1 
ATOM   4275  N N   . TYR B 1 170 ? 42.188  -12.292 -0.271  1.00 149.69 ? 170 TYR B N   1 
ATOM   4276  C CA  . TYR B 1 170 ? 40.955  -12.825 0.298   1.00 144.98 ? 170 TYR B CA  1 
ATOM   4277  C C   . TYR B 1 170 ? 41.090  -14.321 0.540   1.00 148.01 ? 170 TYR B C   1 
ATOM   4278  O O   . TYR B 1 170 ? 41.318  -15.084 -0.403  1.00 146.30 ? 170 TYR B O   1 
ATOM   4279  C CB  . TYR B 1 170 ? 39.771  -12.545 -0.626  1.00 139.52 ? 170 TYR B CB  1 
ATOM   4280  C CG  . TYR B 1 170 ? 38.526  -13.298 -0.240  1.00 144.18 ? 170 TYR B CG  1 
ATOM   4281  C CD1 . TYR B 1 170 ? 37.931  -13.096 0.995   1.00 148.01 ? 170 TYR B CD1 1 
ATOM   4282  C CD2 . TYR B 1 170 ? 37.951  -14.219 -1.104  1.00 143.50 ? 170 TYR B CD2 1 
ATOM   4283  C CE1 . TYR B 1 170 ? 36.798  -13.782 1.357   1.00 151.91 ? 170 TYR B CE1 1 
ATOM   4284  C CE2 . TYR B 1 170 ? 36.812  -14.913 -0.745  1.00 152.18 ? 170 TYR B CE2 1 
ATOM   4285  C CZ  . TYR B 1 170 ? 36.242  -14.688 0.491   1.00 156.69 ? 170 TYR B CZ  1 
ATOM   4286  O OH  . TYR B 1 170 ? 35.112  -15.363 0.880   1.00 157.82 ? 170 TYR B OH  1 
ATOM   4287  N N   . THR B 1 171 ? 40.949  -14.733 1.800   1.00 152.97 ? 171 THR B N   1 
ATOM   4288  C CA  . THR B 1 171 ? 40.854  -16.139 2.180   1.00 171.94 ? 171 THR B CA  1 
ATOM   4289  C C   . THR B 1 171 ? 39.592  -16.335 3.007   1.00 192.57 ? 171 THR B C   1 
ATOM   4290  O O   . THR B 1 171 ? 39.359  -15.600 3.973   1.00 182.90 ? 171 THR B O   1 
ATOM   4291  C CB  . THR B 1 171 ? 42.082  -16.602 2.971   1.00 168.53 ? 171 THR B CB  1 
ATOM   4292  O OG1 . THR B 1 171 ? 42.500  -15.565 3.867   1.00 169.37 ? 171 THR B OG1 1 
ATOM   4293  C CG2 . THR B 1 171 ? 43.221  -16.954 2.027   1.00 158.00 ? 171 THR B CG2 1 
ATOM   4294  N N   . GLU B 1 172 ? 38.779  -17.323 2.624   1.00 276.41 ? 172 GLU B N   1 
ATOM   4295  C CA  . GLU B 1 172 ? 37.471  -17.507 3.247   1.00 276.20 ? 172 GLU B CA  1 
ATOM   4296  C C   . GLU B 1 172 ? 37.592  -17.874 4.724   1.00 275.59 ? 172 GLU B C   1 
ATOM   4297  O O   . GLU B 1 172 ? 37.179  -17.108 5.601   1.00 275.59 ? 172 GLU B O   1 
ATOM   4298  C CB  . GLU B 1 172 ? 36.675  -18.570 2.485   1.00 276.14 ? 172 GLU B CB  1 
ATOM   4299  C CG  . GLU B 1 172 ? 37.486  -19.351 1.463   1.00 276.42 ? 172 GLU B CG  1 
ATOM   4300  C CD  . GLU B 1 172 ? 38.380  -20.399 2.095   1.00 276.58 ? 172 GLU B CD  1 
ATOM   4301  O OE1 . GLU B 1 172 ? 37.932  -21.071 3.048   1.00 276.05 ? 172 GLU B OE1 1 
ATOM   4302  O OE2 . GLU B 1 172 ? 39.532  -20.548 1.638   1.00 277.01 ? 172 GLU B OE2 1 
ATOM   4303  N N   . LYS B 1 173 ? 38.162  -19.043 5.022   1.00 217.80 ? 173 LYS B N   1 
ATOM   4304  C CA  . LYS B 1 173 ? 38.172  -19.517 6.403   1.00 192.51 ? 173 LYS B CA  1 
ATOM   4305  C C   . LYS B 1 173 ? 39.583  -19.559 6.986   1.00 188.77 ? 173 LYS B C   1 
ATOM   4306  O O   . LYS B 1 173 ? 39.791  -19.051 8.095   1.00 176.49 ? 173 LYS B O   1 
ATOM   4307  C CB  . LYS B 1 173 ? 37.503  -20.892 6.510   1.00 178.99 ? 173 LYS B CB  1 
ATOM   4308  C CG  . LYS B 1 173 ? 36.354  -20.933 7.505   1.00 161.39 ? 173 LYS B CG  1 
ATOM   4309  C CD  . LYS B 1 173 ? 35.256  -19.956 7.112   1.00 155.90 ? 173 LYS B CD  1 
ATOM   4310  C CE  . LYS B 1 173 ? 34.259  -19.762 8.242   1.00 137.63 ? 173 LYS B CE  1 
ATOM   4311  N NZ  . LYS B 1 173 ? 34.903  -19.157 9.441   1.00 145.57 ? 173 LYS B NZ  1 
ATOM   4312  N N   . PRO B 1 174 ? 40.587  -20.148 6.297   1.00 187.58 ? 174 PRO B N   1 
ATOM   4313  C CA  . PRO B 1 174 ? 41.952  -20.072 6.836   1.00 179.40 ? 174 PRO B CA  1 
ATOM   4314  C C   . PRO B 1 174 ? 42.461  -18.642 6.835   1.00 172.29 ? 174 PRO B C   1 
ATOM   4315  O O   . PRO B 1 174 ? 42.929  -18.135 5.811   1.00 168.62 ? 174 PRO B O   1 
ATOM   4316  C CB  . PRO B 1 174 ? 42.766  -20.963 5.888   1.00 178.00 ? 174 PRO B CB  1 
ATOM   4317  C CG  . PRO B 1 174 ? 41.762  -21.826 5.206   1.00 187.50 ? 174 PRO B CG  1 
ATOM   4318  C CD  . PRO B 1 174 ? 40.546  -20.971 5.073   1.00 194.83 ? 174 PRO B CD  1 
ATOM   4319  N N   . GLU B 1 175 ? 42.371  -17.986 7.991   1.00 173.78 ? 175 GLU B N   1 
ATOM   4320  C CA  . GLU B 1 175 ? 42.683  -16.564 8.065   1.00 172.44 ? 175 GLU B CA  1 
ATOM   4321  C C   . GLU B 1 175 ? 44.178  -16.314 7.901   1.00 176.53 ? 175 GLU B C   1 
ATOM   4322  O O   . GLU B 1 175 ? 44.604  -15.640 6.955   1.00 178.23 ? 175 GLU B O   1 
ATOM   4323  C CB  . GLU B 1 175 ? 42.152  -15.991 9.381   1.00 170.98 ? 175 GLU B CB  1 
ATOM   4324  C CG  . GLU B 1 175 ? 42.504  -16.800 10.618  1.00 179.43 ? 175 GLU B CG  1 
ATOM   4325  C CD  . GLU B 1 175 ? 41.937  -16.189 11.874  1.00 182.43 ? 175 GLU B CD  1 
ATOM   4326  O OE1 . GLU B 1 175 ? 41.441  -15.053 11.787  1.00 176.01 ? 175 GLU B OE1 1 
ATOM   4327  O OE2 . GLU B 1 175 ? 41.989  -16.832 12.943  1.00 188.44 ? 175 GLU B OE2 1 
ATOM   4328  N N   . THR B 1 176 ? 44.994  -16.886 8.787   1.00 171.68 ? 176 THR B N   1 
ATOM   4329  C CA  . THR B 1 176 ? 46.435  -16.645 8.823   1.00 169.97 ? 176 THR B CA  1 
ATOM   4330  C C   . THR B 1 176 ? 46.728  -15.143 8.745   1.00 170.44 ? 176 THR B C   1 
ATOM   4331  O O   . THR B 1 176 ? 47.173  -14.614 7.725   1.00 169.41 ? 176 THR B O   1 
ATOM   4332  C CB  . THR B 1 176 ? 47.137  -17.409 7.697   1.00 167.36 ? 176 THR B CB  1 
ATOM   4333  O OG1 . THR B 1 176 ? 46.452  -18.645 7.457   1.00 167.72 ? 176 THR B OG1 1 
ATOM   4334  C CG2 . THR B 1 176 ? 48.577  -17.708 8.079   1.00 162.56 ? 176 THR B CG2 1 
ATOM   4335  N N   . PHE B 1 177 ? 46.425  -14.476 9.865   1.00 166.51 ? 177 PHE B N   1 
ATOM   4336  C CA  . PHE B 1 177 ? 46.536  -13.027 10.027  1.00 165.54 ? 177 PHE B CA  1 
ATOM   4337  C C   . PHE B 1 177 ? 45.445  -12.310 9.237   1.00 169.09 ? 177 PHE B C   1 
ATOM   4338  O O   . PHE B 1 177 ? 45.234  -12.600 8.056   1.00 169.01 ? 177 PHE B O   1 
ATOM   4339  C CB  . PHE B 1 177 ? 47.924  -12.527 9.615   1.00 163.59 ? 177 PHE B CB  1 
ATOM   4340  C CG  . PHE B 1 177 ? 48.023  -11.034 9.510   1.00 165.09 ? 177 PHE B CG  1 
ATOM   4341  C CD1 . PHE B 1 177 ? 48.099  -10.249 10.649  1.00 164.18 ? 177 PHE B CD1 1 
ATOM   4342  C CD2 . PHE B 1 177 ? 48.043  -10.416 8.272   1.00 167.49 ? 177 PHE B CD2 1 
ATOM   4343  C CE1 . PHE B 1 177 ? 48.188  -8.873  10.550  1.00 166.99 ? 177 PHE B CE1 1 
ATOM   4344  C CE2 . PHE B 1 177 ? 48.133  -9.045  8.167   1.00 168.19 ? 177 PHE B CE2 1 
ATOM   4345  C CZ  . PHE B 1 177 ? 48.205  -8.272  9.306   1.00 168.51 ? 177 PHE B CZ  1 
ATOM   4346  N N   . VAL B 1 178 ? 44.750  -11.371 9.882   1.00 173.07 ? 178 VAL B N   1 
ATOM   4347  C CA  . VAL B 1 178 ? 43.592  -10.707 9.288   1.00 175.95 ? 178 VAL B CA  1 
ATOM   4348  C C   . VAL B 1 178 ? 43.857  -9.217  9.123   1.00 183.76 ? 178 VAL B C   1 
ATOM   4349  O O   . VAL B 1 178 ? 44.990  -8.754  9.298   1.00 179.47 ? 178 VAL B O   1 
ATOM   4350  C CB  . VAL B 1 178 ? 42.328  -10.943 10.135  1.00 171.51 ? 178 VAL B CB  1 
ATOM   4351  C CG1 . VAL B 1 178 ? 42.083  -12.423 10.298  1.00 165.91 ? 178 VAL B CG1 1 
ATOM   4352  C CG2 . VAL B 1 178 ? 42.468  -10.276 11.497  1.00 170.08 ? 178 VAL B CG2 1 
ATOM   4353  N N   . SER B 1 179 ? 42.809  -8.454  8.780   1.00 218.79 ? 179 SER B N   1 
ATOM   4354  C CA  . SER B 1 179 ? 42.947  -7.013  8.609   1.00 219.92 ? 179 SER B CA  1 
ATOM   4355  C C   . SER B 1 179 ? 41.765  -6.231  9.178   1.00 220.02 ? 179 SER B C   1 
ATOM   4356  O O   . SER B 1 179 ? 41.568  -5.070  8.797   1.00 220.79 ? 179 SER B O   1 
ATOM   4357  C CB  . SER B 1 179 ? 43.121  -6.659  7.132   1.00 220.01 ? 179 SER B CB  1 
ATOM   4358  O OG  . SER B 1 179 ? 44.202  -5.763  6.941   1.00 221.31 ? 179 SER B OG  1 
ATOM   4359  N N   . ASP B 1 180 ? 40.956  -6.848  10.040  1.00 173.08 ? 180 ASP B N   1 
ATOM   4360  C CA  . ASP B 1 180 ? 39.805  -6.269  10.734  1.00 157.80 ? 180 ASP B CA  1 
ATOM   4361  C C   . ASP B 1 180 ? 38.609  -6.059  9.802   1.00 146.86 ? 180 ASP B C   1 
ATOM   4362  O O   . ASP B 1 180 ? 37.532  -5.672  10.271  1.00 142.48 ? 180 ASP B O   1 
ATOM   4363  C CB  . ASP B 1 180 ? 40.166  -4.960  11.467  1.00 155.42 ? 180 ASP B CB  1 
ATOM   4364  C CG  . ASP B 1 180 ? 39.500  -3.726  10.870  1.00 148.74 ? 180 ASP B CG  1 
ATOM   4365  O OD1 . ASP B 1 180 ? 38.424  -3.329  11.366  1.00 147.31 ? 180 ASP B OD1 1 
ATOM   4366  O OD2 . ASP B 1 180 ? 40.057  -3.143  9.918   1.00 147.19 ? 180 ASP B OD2 1 
ATOM   4367  N N   . LEU B 1 181 ? 38.740  -6.361  8.513   1.00 143.80 ? 181 LEU B N   1 
ATOM   4368  C CA  . LEU B 1 181 ? 37.655  -6.227  7.555   1.00 126.69 ? 181 LEU B CA  1 
ATOM   4369  C C   . LEU B 1 181 ? 37.106  -7.601  7.196   1.00 120.63 ? 181 LEU B C   1 
ATOM   4370  O O   . LEU B 1 181 ? 37.837  -8.596  7.184   1.00 124.76 ? 181 LEU B O   1 
ATOM   4371  C CB  . LEU B 1 181 ? 38.119  -5.501  6.291   1.00 125.07 ? 181 LEU B CB  1 
ATOM   4372  C CG  . LEU B 1 181 ? 38.289  -3.988  6.425   1.00 119.31 ? 181 LEU B CG  1 
ATOM   4373  C CD1 . LEU B 1 181 ? 38.611  -3.369  5.078   1.00 104.77 ? 181 LEU B CD1 1 
ATOM   4374  C CD2 . LEU B 1 181 ? 37.040  -3.357  7.024   1.00 118.62 ? 181 LEU B CD2 1 
ATOM   4375  N N   . ILE B 1 182 ? 35.805  -7.647  6.903   1.00 121.49 ? 182 ILE B N   1 
ATOM   4376  C CA  . ILE B 1 182 ? 35.095  -8.891  6.630   1.00 119.07 ? 182 ILE B CA  1 
ATOM   4377  C C   . ILE B 1 182 ? 34.063  -8.644  5.538   1.00 114.68 ? 182 ILE B C   1 
ATOM   4378  O O   . ILE B 1 182 ? 33.640  -7.512  5.294   1.00 112.84 ? 182 ILE B O   1 
ATOM   4379  C CB  . ILE B 1 182 ? 34.392  -9.461  7.884   1.00 116.59 ? 182 ILE B CB  1 
ATOM   4380  C CG1 . ILE B 1 182 ? 33.534  -8.383  8.552   1.00 114.36 ? 182 ILE B CG1 1 
ATOM   4381  C CG2 . ILE B 1 182 ? 35.400  -10.038 8.865   1.00 123.10 ? 182 ILE B CG2 1 
ATOM   4382  C CD1 . ILE B 1 182 ? 32.302  -8.925  9.238   1.00 116.27 ? 182 ILE B CD1 1 
ATOM   4383  N N   . ASN B 1 183 ? 33.665  -9.726  4.872   1.00 115.79 ? 183 ASN B N   1 
ATOM   4384  C CA  . ASN B 1 183 ? 32.597  -9.637  3.890   1.00 109.77 ? 183 ASN B CA  1 
ATOM   4385  C C   . ASN B 1 183 ? 31.274  -9.295  4.566   1.00 108.47 ? 183 ASN B C   1 
ATOM   4386  O O   . ASN B 1 183 ? 31.072  -9.528  5.761   1.00 106.56 ? 183 ASN B O   1 
ATOM   4387  C CB  . ASN B 1 183 ? 32.440  -10.950 3.120   1.00 108.95 ? 183 ASN B CB  1 
ATOM   4388  C CG  . ASN B 1 183 ? 33.721  -11.396 2.451   1.00 122.40 ? 183 ASN B CG  1 
ATOM   4389  O OD1 . ASN B 1 183 ? 34.636  -11.888 3.106   1.00 130.84 ? 183 ASN B OD1 1 
ATOM   4390  N ND2 . ASN B 1 183 ? 33.787  -11.239 1.135   1.00 118.63 ? 183 ASN B ND2 1 
ATOM   4391  N N   . CYS B 1 184 ? 30.364  -8.725  3.777   1.00 106.35 ? 184 CYS B N   1 
ATOM   4392  C CA  . CYS B 1 184 ? 28.999  -8.484  4.217   1.00 100.15 ? 184 CYS B CA  1 
ATOM   4393  C C   . CYS B 1 184 ? 27.961  -9.247  3.409   1.00 95.67  ? 184 CYS B C   1 
ATOM   4394  O O   . CYS B 1 184 ? 26.818  -9.359  3.864   1.00 99.53  ? 184 CYS B O   1 
ATOM   4395  C CB  . CYS B 1 184 ? 28.673  -6.983  4.169   1.00 104.23 ? 184 CYS B CB  1 
ATOM   4396  S SG  . CYS B 1 184 ? 29.411  -6.018  5.516   1.00 102.00 ? 184 CYS B SG  1 
ATOM   4397  N N   . GLY B 1 185 ? 28.322  -9.773  2.237   1.00 94.80  ? 185 GLY B N   1 
ATOM   4398  C CA  . GLY B 1 185 ? 27.417  -10.536 1.407   1.00 94.86  ? 185 GLY B CA  1 
ATOM   4399  C C   . GLY B 1 185 ? 26.639  -9.736  0.383   1.00 93.70  ? 185 GLY B C   1 
ATOM   4400  O O   . GLY B 1 185 ? 26.098  -10.326 -0.561  1.00 92.51  ? 185 GLY B O   1 
ATOM   4401  N N   . VAL B 1 186 ? 26.573  -8.415  0.530   1.00 94.80  ? 186 VAL B N   1 
ATOM   4402  C CA  . VAL B 1 186 ? 25.863  -7.556  -0.412  1.00 94.82  ? 186 VAL B CA  1 
ATOM   4403  C C   . VAL B 1 186 ? 26.858  -7.078  -1.465  1.00 92.62  ? 186 VAL B C   1 
ATOM   4404  O O   . VAL B 1 186 ? 27.794  -6.334  -1.163  1.00 93.16  ? 186 VAL B O   1 
ATOM   4405  C CB  . VAL B 1 186 ? 25.183  -6.381  0.301   1.00 99.66  ? 186 VAL B CB  1 
ATOM   4406  C CG1 . VAL B 1 186 ? 26.082  -5.830  1.393   1.00 98.35  ? 186 VAL B CG1 1 
ATOM   4407  C CG2 . VAL B 1 186 ? 24.810  -5.295  -0.700  1.00 94.20  ? 186 VAL B CG2 1 
ATOM   4408  N N   . TYR B 1 187 ? 26.668  -7.529  -2.702  1.00 85.63  ? 187 TYR B N   1 
ATOM   4409  C CA  . TYR B 1 187 ? 27.594  -7.268  -3.789  1.00 78.09  ? 187 TYR B CA  1 
ATOM   4410  C C   . TYR B 1 187 ? 26.874  -6.555  -4.927  1.00 70.81  ? 187 TYR B C   1 
ATOM   4411  O O   . TYR B 1 187 ? 25.657  -6.679  -5.091  1.00 75.18  ? 187 TYR B O   1 
ATOM   4412  C CB  . TYR B 1 187 ? 28.205  -8.582  -4.290  1.00 80.56  ? 187 TYR B CB  1 
ATOM   4413  C CG  . TYR B 1 187 ? 28.869  -9.421  -3.211  1.00 84.12  ? 187 TYR B CG  1 
ATOM   4414  C CD1 . TYR B 1 187 ? 28.929  -10.804 -3.323  1.00 85.08  ? 187 TYR B CD1 1 
ATOM   4415  C CD2 . TYR B 1 187 ? 29.391  -8.838  -2.062  1.00 88.57  ? 187 TYR B CD2 1 
ATOM   4416  C CE1 . TYR B 1 187 ? 29.512  -11.575 -2.336  1.00 90.56  ? 187 TYR B CE1 1 
ATOM   4417  C CE2 . TYR B 1 187 ? 29.977  -9.601  -1.070  1.00 92.51  ? 187 TYR B CE2 1 
ATOM   4418  C CZ  . TYR B 1 187 ? 30.035  -10.968 -1.212  1.00 94.56  ? 187 TYR B CZ  1 
ATOM   4419  O OH  . TYR B 1 187 ? 30.617  -11.732 -0.225  1.00 100.11 ? 187 TYR B OH  1 
ATOM   4420  N N   . VAL B 1 188 ? 27.646  -5.820  -5.724  1.00 68.16  ? 188 VAL B N   1 
ATOM   4421  C CA  . VAL B 1 188 ? 27.141  -5.153  -6.920  1.00 68.99  ? 188 VAL B CA  1 
ATOM   4422  C C   . VAL B 1 188 ? 28.200  -5.284  -8.001  1.00 69.85  ? 188 VAL B C   1 
ATOM   4423  O O   . VAL B 1 188 ? 29.359  -4.913  -7.785  1.00 71.29  ? 188 VAL B O   1 
ATOM   4424  C CB  . VAL B 1 188 ? 26.806  -3.673  -6.674  1.00 69.28  ? 188 VAL B CB  1 
ATOM   4425  C CG1 . VAL B 1 188 ? 27.843  -3.042  -5.776  1.00 71.64  ? 188 VAL B CG1 1 
ATOM   4426  C CG2 . VAL B 1 188 ? 26.719  -2.928  -7.994  1.00 70.36  ? 188 VAL B CG2 1 
ATOM   4427  N N   . PHE B 1 189 ? 27.820  -5.838  -9.143  1.00 70.33  ? 189 PHE B N   1 
ATOM   4428  C CA  . PHE B 1 189 ? 28.757  -6.048  -10.232 1.00 71.21  ? 189 PHE B CA  1 
ATOM   4429  C C   . PHE B 1 189 ? 28.377  -5.198  -11.438 1.00 72.24  ? 189 PHE B C   1 
ATOM   4430  O O   . PHE B 1 189 ? 27.426  -4.415  -11.410 1.00 72.28  ? 189 PHE B O   1 
ATOM   4431  C CB  . PHE B 1 189 ? 28.812  -7.533  -10.587 1.00 71.01  ? 189 PHE B CB  1 
ATOM   4432  C CG  . PHE B 1 189 ? 29.186  -8.409  -9.427  1.00 74.90  ? 189 PHE B CG  1 
ATOM   4433  C CD1 . PHE B 1 189 ? 30.512  -8.700  -9.156  1.00 77.59  ? 189 PHE B CD1 1 
ATOM   4434  C CD2 . PHE B 1 189 ? 28.209  -8.936  -8.596  1.00 72.54  ? 189 PHE B CD2 1 
ATOM   4435  C CE1 . PHE B 1 189 ? 30.856  -9.506  -8.085  1.00 75.49  ? 189 PHE B CE1 1 
ATOM   4436  C CE2 . PHE B 1 189 ? 28.547  -9.742  -7.525  1.00 72.33  ? 189 PHE B CE2 1 
ATOM   4437  C CZ  . PHE B 1 189 ? 29.872  -10.026 -7.269  1.00 76.49  ? 189 PHE B CZ  1 
ATOM   4438  N N   . THR B 1 190 ? 29.140  -5.366  -12.509 1.00 73.14  ? 190 THR B N   1 
ATOM   4439  C CA  . THR B 1 190 ? 28.804  -4.822  -13.812 1.00 74.22  ? 190 THR B CA  1 
ATOM   4440  C C   . THR B 1 190 ? 28.276  -5.957  -14.683 1.00 82.98  ? 190 THR B C   1 
ATOM   4441  O O   . THR B 1 190 ? 28.185  -7.109  -14.254 1.00 73.67  ? 190 THR B O   1 
ATOM   4442  C CB  . THR B 1 190 ? 30.021  -4.141  -14.443 1.00 76.85  ? 190 THR B CB  1 
ATOM   4443  O OG1 . THR B 1 190 ? 29.650  -3.557  -15.700 1.00 78.10  ? 190 THR B OG1 1 
ATOM   4444  C CG2 . THR B 1 190 ? 31.141  -5.146  -14.665 1.00 75.50  ? 190 THR B CG2 1 
ATOM   4445  N N   . SER B 1 191 ? 27.911  -5.631  -15.922 1.00 89.35  ? 191 SER B N   1 
ATOM   4446  C CA  . SER B 1 191 ? 27.407  -6.668  -16.815 1.00 89.75  ? 191 SER B CA  1 
ATOM   4447  C C   . SER B 1 191 ? 28.473  -7.690  -17.191 1.00 89.11  ? 191 SER B C   1 
ATOM   4448  O O   . SER B 1 191 ? 28.130  -8.742  -17.741 1.00 89.14  ? 191 SER B O   1 
ATOM   4449  C CB  . SER B 1 191 ? 26.818  -6.041  -18.080 1.00 93.63  ? 191 SER B CB  1 
ATOM   4450  O OG  . SER B 1 191 ? 26.320  -7.043  -18.951 1.00 102.50 ? 191 SER B OG  1 
ATOM   4451  N N   . ASP B 1 192 ? 29.743  -7.413  -16.900 1.00 85.10  ? 192 ASP B N   1 
ATOM   4452  C CA  . ASP B 1 192 ? 30.857  -8.275  -17.277 1.00 84.93  ? 192 ASP B CA  1 
ATOM   4453  C C   . ASP B 1 192 ? 31.051  -9.454  -16.328 1.00 85.85  ? 192 ASP B C   1 
ATOM   4454  O O   . ASP B 1 192 ? 31.929  -10.289 -16.574 1.00 86.67  ? 192 ASP B O   1 
ATOM   4455  C CB  . ASP B 1 192 ? 32.144  -7.445  -17.343 1.00 84.39  ? 192 ASP B CB  1 
ATOM   4456  C CG  . ASP B 1 192 ? 33.251  -8.130  -18.126 1.00 93.79  ? 192 ASP B CG  1 
ATOM   4457  O OD1 . ASP B 1 192 ? 32.962  -9.110  -18.844 1.00 94.46  ? 192 ASP B OD1 1 
ATOM   4458  O OD2 . ASP B 1 192 ? 34.418  -7.694  -18.010 1.00 96.76  ? 192 ASP B OD2 1 
ATOM   4459  N N   . ILE B 1 193 ? 30.255  -9.553  -15.261 1.00 87.27  ? 193 ILE B N   1 
ATOM   4460  C CA  . ILE B 1 193 ? 30.484  -10.602 -14.272 1.00 86.99  ? 193 ILE B CA  1 
ATOM   4461  C C   . ILE B 1 193 ? 30.153  -11.975 -14.845 1.00 89.46  ? 193 ILE B C   1 
ATOM   4462  O O   . ILE B 1 193 ? 30.800  -12.971 -14.497 1.00 90.00  ? 193 ILE B O   1 
ATOM   4463  C CB  . ILE B 1 193 ? 29.682  -10.312 -12.988 1.00 87.31  ? 193 ILE B CB  1 
ATOM   4464  C CG1 . ILE B 1 193 ? 29.925  -11.397 -11.937 1.00 90.47  ? 193 ILE B CG1 1 
ATOM   4465  C CG2 . ILE B 1 193 ? 28.199  -10.185 -13.293 1.00 92.88  ? 193 ILE B CG2 1 
ATOM   4466  C CD1 . ILE B 1 193 ? 31.379  -11.592 -11.579 1.00 95.07  ? 193 ILE B CD1 1 
ATOM   4467  N N   . PHE B 1 194 ? 29.169  -12.057 -15.741 1.00 88.65  ? 194 PHE B N   1 
ATOM   4468  C CA  . PHE B 1 194 ? 28.819  -13.349 -16.320 1.00 90.46  ? 194 PHE B CA  1 
ATOM   4469  C C   . PHE B 1 194 ? 29.947  -13.902 -17.181 1.00 93.54  ? 194 PHE B C   1 
ATOM   4470  O O   . PHE B 1 194 ? 30.067  -15.123 -17.335 1.00 96.76  ? 194 PHE B O   1 
ATOM   4471  C CB  . PHE B 1 194 ? 27.538  -13.232 -17.142 1.00 91.82  ? 194 PHE B CB  1 
ATOM   4472  C CG  . PHE B 1 194 ? 26.329  -12.859 -16.336 1.00 90.37  ? 194 PHE B CG  1 
ATOM   4473  C CD1 . PHE B 1 194 ? 25.718  -13.785 -15.508 1.00 89.94  ? 194 PHE B CD1 1 
ATOM   4474  C CD2 . PHE B 1 194 ? 25.789  -11.589 -16.425 1.00 90.15  ? 194 PHE B CD2 1 
ATOM   4475  C CE1 . PHE B 1 194 ? 24.598  -13.444 -14.772 1.00 91.62  ? 194 PHE B CE1 1 
ATOM   4476  C CE2 . PHE B 1 194 ? 24.672  -11.246 -15.692 1.00 85.79  ? 194 PHE B CE2 1 
ATOM   4477  C CZ  . PHE B 1 194 ? 24.075  -12.173 -14.866 1.00 88.75  ? 194 PHE B CZ  1 
ATOM   4478  N N   . ASN B 1 195 ? 30.783  -13.025 -17.743 1.00 91.55  ? 195 ASN B N   1 
ATOM   4479  C CA  . ASN B 1 195 ? 31.909  -13.488 -18.546 1.00 96.72  ? 195 ASN B CA  1 
ATOM   4480  C C   . ASN B 1 195 ? 33.003  -14.100 -17.682 1.00 99.23  ? 195 ASN B C   1 
ATOM   4481  O O   . ASN B 1 195 ? 33.719  -15.000 -18.136 1.00 104.74 ? 195 ASN B O   1 
ATOM   4482  C CB  . ASN B 1 195 ? 32.476  -12.328 -19.362 1.00 92.88  ? 195 ASN B CB  1 
ATOM   4483  C CG  . ASN B 1 195 ? 31.417  -11.626 -20.179 1.00 90.87  ? 195 ASN B CG  1 
ATOM   4484  O OD1 . ASN B 1 195 ? 30.443  -12.242 -20.608 1.00 96.18  ? 195 ASN B OD1 1 
ATOM   4485  N ND2 . ASN B 1 195 ? 31.598  -10.329 -20.396 1.00 91.43  ? 195 ASN B ND2 1 
ATOM   4486  N N   . ALA B 1 196 ? 33.147  -13.629 -16.442 1.00 94.94  ? 196 ALA B N   1 
ATOM   4487  C CA  . ALA B 1 196 ? 34.151  -14.195 -15.550 1.00 97.65  ? 196 ALA B CA  1 
ATOM   4488  C C   . ALA B 1 196 ? 33.775  -15.604 -15.111 1.00 105.30 ? 196 ALA B C   1 
ATOM   4489  O O   . ALA B 1 196 ? 34.660  -16.416 -14.817 1.00 108.05 ? 196 ALA B O   1 
ATOM   4490  C CB  . ALA B 1 196 ? 34.351  -13.288 -14.336 1.00 100.28 ? 196 ALA B CB  1 
ATOM   4491  N N   . ILE B 1 197 ? 32.477  -15.913 -15.062 1.00 104.10 ? 197 ILE B N   1 
ATOM   4492  C CA  . ILE B 1 197 ? 32.053  -17.255 -14.680 1.00 106.75 ? 197 ILE B CA  1 
ATOM   4493  C C   . ILE B 1 197 ? 32.299  -18.227 -15.822 1.00 115.60 ? 197 ILE B C   1 
ATOM   4494  O O   . ILE B 1 197 ? 32.642  -19.394 -15.596 1.00 125.71 ? 197 ILE B O   1 
ATOM   4495  C CB  . ILE B 1 197 ? 30.570  -17.245 -14.264 1.00 103.48 ? 197 ILE B CB  1 
ATOM   4496  C CG1 . ILE B 1 197 ? 30.322  -16.163 -13.212 1.00 99.46  ? 197 ILE B CG1 1 
ATOM   4497  C CG2 . ILE B 1 197 ? 30.148  -18.615 -13.737 1.00 112.57 ? 197 ILE B CG2 1 
ATOM   4498  C CD1 . ILE B 1 197 ? 28.893  -16.112 -12.705 1.00 99.87  ? 197 ILE B CD1 1 
ATOM   4499  N N   . GLU B 1 198 ? 32.151  -17.763 -17.062 1.00 114.72 ? 198 GLU B N   1 
ATOM   4500  C CA  . GLU B 1 198 ? 32.442  -18.609 -18.211 1.00 118.12 ? 198 GLU B CA  1 
ATOM   4501  C C   . GLU B 1 198 ? 33.923  -18.958 -18.282 1.00 119.48 ? 198 GLU B C   1 
ATOM   4502  O O   . GLU B 1 198 ? 34.284  -20.032 -18.773 1.00 121.90 ? 198 GLU B O   1 
ATOM   4503  C CB  . GLU B 1 198 ? 31.974  -17.915 -19.489 1.00 118.42 ? 198 GLU B CB  1 
ATOM   4504  C CG  . GLU B 1 198 ? 30.471  -17.694 -19.513 1.00 118.91 ? 198 GLU B CG  1 
ATOM   4505  C CD  . GLU B 1 198 ? 29.967  -17.116 -20.818 1.00 122.00 ? 198 GLU B CD  1 
ATOM   4506  O OE1 . GLU B 1 198 ? 30.799  -16.725 -21.661 1.00 120.55 ? 198 GLU B OE1 1 
ATOM   4507  O OE2 . GLU B 1 198 ? 28.732  -17.052 -20.997 1.00 125.18 ? 198 GLU B OE2 1 
ATOM   4508  N N   . GLU B 1 199 ? 34.792  -18.072 -17.800 1.00 116.06 ? 199 GLU B N   1 
ATOM   4509  C CA  . GLU B 1 199 ? 36.218  -18.359 -17.760 1.00 114.60 ? 199 GLU B CA  1 
ATOM   4510  C C   . GLU B 1 199 ? 36.600  -19.277 -16.608 1.00 118.13 ? 199 GLU B C   1 
ATOM   4511  O O   . GLU B 1 199 ? 37.771  -19.651 -16.496 1.00 118.96 ? 199 GLU B O   1 
ATOM   4512  C CB  . GLU B 1 199 ? 37.015  -17.055 -17.688 1.00 110.26 ? 199 GLU B CB  1 
ATOM   4513  C CG  . GLU B 1 199 ? 36.856  -16.199 -18.933 1.00 111.76 ? 199 GLU B CG  1 
ATOM   4514  C CD  . GLU B 1 199 ? 37.078  -16.989 -20.213 1.00 121.19 ? 199 GLU B CD  1 
ATOM   4515  O OE1 . GLU B 1 199 ? 38.107  -17.691 -20.313 1.00 125.18 ? 199 GLU B OE1 1 
ATOM   4516  O OE2 . GLU B 1 199 ? 36.215  -16.920 -21.114 1.00 121.82 ? 199 GLU B OE2 1 
ATOM   4517  N N   . VAL B 1 200 ? 35.651  -19.633 -15.747 1.00 121.96 ? 200 VAL B N   1 
ATOM   4518  C CA  . VAL B 1 200 ? 35.878  -20.650 -14.731 1.00 129.59 ? 200 VAL B CA  1 
ATOM   4519  C C   . VAL B 1 200 ? 34.931  -21.836 -14.866 1.00 142.36 ? 200 VAL B C   1 
ATOM   4520  O O   . VAL B 1 200 ? 35.264  -22.933 -14.388 1.00 143.15 ? 200 VAL B O   1 
ATOM   4521  C CB  . VAL B 1 200 ? 35.790  -20.049 -13.311 1.00 127.25 ? 200 VAL B CB  1 
ATOM   4522  C CG1 . VAL B 1 200 ? 34.342  -19.838 -12.898 1.00 131.36 ? 200 VAL B CG1 1 
ATOM   4523  C CG2 . VAL B 1 200 ? 36.527  -20.926 -12.305 1.00 128.11 ? 200 VAL B CG2 1 
ATOM   4524  N N   . TYR B 1 201 ? 33.774  -21.673 -15.510 1.00 182.43 ? 201 TYR B N   1 
ATOM   4525  C CA  . TYR B 1 201 ? 32.845  -22.774 -15.733 1.00 182.37 ? 201 TYR B CA  1 
ATOM   4526  C C   . TYR B 1 201 ? 33.086  -23.464 -17.070 1.00 183.85 ? 201 TYR B C   1 
ATOM   4527  O O   . TYR B 1 201 ? 32.955  -24.689 -17.166 1.00 183.72 ? 201 TYR B O   1 
ATOM   4528  C CB  . TYR B 1 201 ? 31.402  -22.269 -15.664 1.00 182.46 ? 201 TYR B CB  1 
ATOM   4529  C CG  . TYR B 1 201 ? 30.583  -22.892 -14.559 1.00 181.05 ? 201 TYR B CG  1 
ATOM   4530  C CD1 . TYR B 1 201 ? 30.768  -24.219 -14.193 1.00 180.62 ? 201 TYR B CD1 1 
ATOM   4531  C CD2 . TYR B 1 201 ? 29.628  -22.151 -13.879 1.00 180.41 ? 201 TYR B CD2 1 
ATOM   4532  C CE1 . TYR B 1 201 ? 30.020  -24.791 -13.183 1.00 181.23 ? 201 TYR B CE1 1 
ATOM   4533  C CE2 . TYR B 1 201 ? 28.877  -22.714 -12.868 1.00 180.93 ? 201 TYR B CE2 1 
ATOM   4534  C CZ  . TYR B 1 201 ? 29.077  -24.033 -12.523 1.00 182.64 ? 201 TYR B CZ  1 
ATOM   4535  O OH  . TYR B 1 201 ? 28.327  -24.593 -11.515 1.00 181.53 ? 201 TYR B OH  1 
ATOM   4536  N N   . SER B 1 202 ? 33.420  -22.699 -18.107 1.00 147.91 ? 202 SER B N   1 
ATOM   4537  C CA  . SER B 1 202 ? 33.727  -23.249 -19.422 1.00 138.67 ? 202 SER B CA  1 
ATOM   4538  C C   . SER B 1 202 ? 35.220  -23.441 -19.643 1.00 130.54 ? 202 SER B C   1 
ATOM   4539  O O   . SER B 1 202 ? 35.629  -24.435 -20.252 1.00 130.77 ? 202 SER B O   1 
ATOM   4540  C CB  . SER B 1 202 ? 33.158  -22.348 -20.523 1.00 133.14 ? 202 SER B CB  1 
ATOM   4541  O OG  . SER B 1 202 ? 31.789  -22.063 -20.292 1.00 131.31 ? 202 SER B OG  1 
ATOM   4542  N N   . GLN B 1 203 ? 36.045  -22.508 -19.164 1.00 126.92 ? 203 GLN B N   1 
ATOM   4543  C CA  . GLN B 1 203 ? 37.482  -22.588 -19.401 1.00 125.00 ? 203 GLN B CA  1 
ATOM   4544  C C   . GLN B 1 203 ? 38.172  -23.496 -18.389 1.00 126.15 ? 203 GLN B C   1 
ATOM   4545  O O   . GLN B 1 203 ? 38.978  -24.354 -18.765 1.00 125.40 ? 203 GLN B O   1 
ATOM   4546  C CB  . GLN B 1 203 ? 38.101  -21.188 -19.363 1.00 122.16 ? 203 GLN B CB  1 
ATOM   4547  C CG  . GLN B 1 203 ? 39.612  -21.182 -19.570 1.00 118.39 ? 203 GLN B CG  1 
ATOM   4548  C CD  . GLN B 1 203 ? 40.359  -20.440 -18.474 1.00 116.01 ? 203 GLN B CD  1 
ATOM   4549  O OE1 . GLN B 1 203 ? 39.972  -19.343 -18.073 1.00 113.29 ? 203 GLN B OE1 1 
ATOM   4550  N NE2 . GLN B 1 203 ? 41.440  -21.039 -17.987 1.00 116.58 ? 203 GLN B NE2 1 
ATOM   4551  N N   . ILE B 1 204 ? 37.868  -23.325 -17.104 1.00 128.45 ? 204 ILE B N   1 
ATOM   4552  C CA  . ILE B 1 204 ? 38.527  -24.090 -16.052 1.00 129.44 ? 204 ILE B CA  1 
ATOM   4553  C C   . ILE B 1 204 ? 37.638  -25.252 -15.626 1.00 129.75 ? 204 ILE B C   1 
ATOM   4554  O O   . ILE B 1 204 ? 38.134  -26.294 -15.181 1.00 128.57 ? 204 ILE B O   1 
ATOM   4555  C CB  . ILE B 1 204 ? 38.882  -23.186 -14.856 1.00 128.59 ? 204 ILE B CB  1 
ATOM   4556  C CG1 . ILE B 1 204 ? 39.670  -21.965 -15.338 1.00 121.65 ? 204 ILE B CG1 1 
ATOM   4557  C CG2 . ILE B 1 204 ? 39.695  -23.953 -13.826 1.00 131.23 ? 204 ILE B CG2 1 
ATOM   4558  C CD1 . ILE B 1 204 ? 40.065  -21.005 -14.234 1.00 117.63 ? 204 ILE B CD1 1 
ATOM   4559  N N   . ARG B 1 205 ? 36.325  -25.078 -15.760 1.00 131.83 ? 205 ARG B N   1 
ATOM   4560  C CA  . ARG B 1 205 ? 35.350  -26.117 -15.427 1.00 136.33 ? 205 ARG B CA  1 
ATOM   4561  C C   . ARG B 1 205 ? 35.482  -26.570 -13.977 1.00 139.66 ? 205 ARG B C   1 
ATOM   4562  O O   . ARG B 1 205 ? 34.891  -25.977 -13.076 1.00 148.04 ? 205 ARG B O   1 
ATOM   4563  C CB  . ARG B 1 205 ? 35.500  -27.314 -16.365 1.00 130.72 ? 205 ARG B CB  1 
ATOM   4564  C CG  . ARG B 1 205 ? 35.279  -26.980 -17.823 1.00 129.05 ? 205 ARG B CG  1 
ATOM   4565  C CD  . ARG B 1 205 ? 36.236  -27.754 -18.712 1.00 122.81 ? 205 ARG B CD  1 
ATOM   4566  N NE  . ARG B 1 205 ? 37.620  -27.316 -18.548 1.00 123.95 ? 205 ARG B NE  1 
ATOM   4567  C CZ  . ARG B 1 205 ? 38.523  -27.943 -17.799 1.00 127.82 ? 205 ARG B CZ  1 
ATOM   4568  N NH1 . ARG B 1 205 ? 38.193  -29.044 -17.137 1.00 125.34 ? 205 ARG B NH1 1 
ATOM   4569  N NH2 . ARG B 1 205 ? 39.759  -27.470 -17.715 1.00 129.59 ? 205 ARG B NH2 1 
ATOM   4570  N N   . PHE B 1 222 ? 28.505  -25.980 -8.664  1.00 170.75 ? 222 PHE B N   1 
ATOM   4571  C CA  . PHE B 1 222 ? 29.460  -26.368 -7.632  1.00 165.94 ? 222 PHE B CA  1 
ATOM   4572  C C   . PHE B 1 222 ? 30.580  -25.340 -7.503  1.00 157.52 ? 222 PHE B C   1 
ATOM   4573  O O   . PHE B 1 222 ? 31.509  -25.517 -6.714  1.00 148.21 ? 222 PHE B O   1 
ATOM   4574  C CB  . PHE B 1 222 ? 30.045  -27.750 -7.934  1.00 161.77 ? 222 PHE B CB  1 
ATOM   4575  C CG  . PHE B 1 222 ? 30.678  -27.857 -9.294  1.00 161.90 ? 222 PHE B CG  1 
ATOM   4576  C CD1 . PHE B 1 222 ? 32.017  -27.550 -9.478  1.00 157.63 ? 222 PHE B CD1 1 
ATOM   4577  C CD2 . PHE B 1 222 ? 29.934  -28.268 -10.387 1.00 163.97 ? 222 PHE B CD2 1 
ATOM   4578  C CE1 . PHE B 1 222 ? 32.600  -27.646 -10.726 1.00 155.93 ? 222 PHE B CE1 1 
ATOM   4579  C CE2 . PHE B 1 222 ? 30.512  -28.367 -11.638 1.00 162.70 ? 222 PHE B CE2 1 
ATOM   4580  C CZ  . PHE B 1 222 ? 31.847  -28.056 -11.807 1.00 156.48 ? 222 PHE B CZ  1 
ATOM   4581  N N   . VAL B 1 223 ? 30.488  -24.271 -8.286  1.00 166.87 ? 223 VAL B N   1 
ATOM   4582  C CA  . VAL B 1 223 ? 31.472  -23.195 -8.257  1.00 157.46 ? 223 VAL B CA  1 
ATOM   4583  C C   . VAL B 1 223 ? 31.073  -22.216 -7.161  1.00 154.28 ? 223 VAL B C   1 
ATOM   4584  O O   . VAL B 1 223 ? 29.966  -21.668 -7.178  1.00 154.74 ? 223 VAL B O   1 
ATOM   4585  C CB  . VAL B 1 223 ? 31.571  -22.491 -9.619  1.00 157.72 ? 223 VAL B CB  1 
ATOM   4586  C CG1 . VAL B 1 223 ? 32.386  -21.210 -9.499  1.00 148.32 ? 223 VAL B CG1 1 
ATOM   4587  C CG2 . VAL B 1 223 ? 32.182  -23.424 -10.653 1.00 158.20 ? 223 VAL B CG2 1 
ATOM   4588  N N   . ARG B 1 224 ? 31.974  -21.996 -6.209  1.00 136.20 ? 224 ARG B N   1 
ATOM   4589  C CA  . ARG B 1 224 ? 31.715  -21.097 -5.095  1.00 133.17 ? 224 ARG B CA  1 
ATOM   4590  C C   . ARG B 1 224 ? 32.201  -19.704 -5.466  1.00 127.93 ? 224 ARG B C   1 
ATOM   4591  O O   . ARG B 1 224 ? 33.340  -19.537 -5.910  1.00 123.04 ? 224 ARG B O   1 
ATOM   4592  C CB  . ARG B 1 224 ? 32.414  -21.574 -3.819  1.00 134.70 ? 224 ARG B CB  1 
ATOM   4593  C CG  . ARG B 1 224 ? 32.034  -22.974 -3.334  1.00 134.16 ? 224 ARG B CG  1 
ATOM   4594  C CD  . ARG B 1 224 ? 32.837  -24.030 -4.075  1.00 132.63 ? 224 ARG B CD  1 
ATOM   4595  N NE  . ARG B 1 224 ? 34.222  -23.602 -4.246  1.00 132.51 ? 224 ARG B NE  1 
ATOM   4596  C CZ  . ARG B 1 224 ? 34.981  -23.927 -5.287  1.00 132.44 ? 224 ARG B CZ  1 
ATOM   4597  N NH1 . ARG B 1 224 ? 34.487  -24.680 -6.260  1.00 138.90 ? 224 ARG B NH1 1 
ATOM   4598  N NH2 . ARG B 1 224 ? 36.231  -23.489 -5.361  1.00 124.95 ? 224 ARG B NH2 1 
ATOM   4599  N N   . LEU B 1 225 ? 31.335  -18.709 -5.273  1.00 129.11 ? 225 LEU B N   1 
ATOM   4600  C CA  . LEU B 1 225 ? 31.671  -17.343 -5.661  1.00 126.77 ? 225 LEU B CA  1 
ATOM   4601  C C   . LEU B 1 225 ? 32.879  -16.834 -4.885  1.00 131.75 ? 225 LEU B C   1 
ATOM   4602  O O   . LEU B 1 225 ? 33.790  -16.226 -5.460  1.00 124.17 ? 225 LEU B O   1 
ATOM   4603  C CB  . LEU B 1 225 ? 30.462  -16.434 -5.432  1.00 122.44 ? 225 LEU B CB  1 
ATOM   4604  C CG  . LEU B 1 225 ? 30.275  -15.182 -6.289  1.00 113.73 ? 225 LEU B CG  1 
ATOM   4605  C CD1 . LEU B 1 225 ? 28.802  -14.799 -6.326  1.00 108.66 ? 225 LEU B CD1 1 
ATOM   4606  C CD2 . LEU B 1 225 ? 31.110  -14.032 -5.758  1.00 115.86 ? 225 LEU B CD2 1 
ATOM   4607  N N   . ASP B 1 226 ? 32.904  -17.083 -3.579  1.00 161.00 ? 226 ASP B N   1 
ATOM   4608  C CA  . ASP B 1 226 ? 33.921  -16.558 -2.673  1.00 160.74 ? 226 ASP B CA  1 
ATOM   4609  C C   . ASP B 1 226 ? 35.078  -17.525 -2.448  1.00 160.90 ? 226 ASP B C   1 
ATOM   4610  O O   . ASP B 1 226 ? 35.558  -17.667 -1.320  1.00 170.45 ? 226 ASP B O   1 
ATOM   4611  C CB  . ASP B 1 226 ? 33.256  -16.180 -1.355  1.00 160.31 ? 226 ASP B CB  1 
ATOM   4612  C CG  . ASP B 1 226 ? 32.221  -17.194 -0.913  1.00 166.40 ? 226 ASP B CG  1 
ATOM   4613  O OD1 . ASP B 1 226 ? 32.569  -18.385 -0.778  1.00 167.41 ? 226 ASP B OD1 1 
ATOM   4614  O OD2 . ASP B 1 226 ? 31.051  -16.802 -0.714  1.00 172.17 ? 226 ASP B OD2 1 
ATOM   4615  N N   . GLN B 1 227 ? 35.543  -18.213 -3.490  1.00 139.39 ? 227 GLN B N   1 
ATOM   4616  C CA  . GLN B 1 227 ? 36.659  -19.142 -3.345  1.00 133.68 ? 227 GLN B CA  1 
ATOM   4617  C C   . GLN B 1 227 ? 37.525  -19.165 -4.596  1.00 120.24 ? 227 GLN B C   1 
ATOM   4618  O O   . GLN B 1 227 ? 38.757  -19.162 -4.509  1.00 118.49 ? 227 GLN B O   1 
ATOM   4619  C CB  . GLN B 1 227 ? 36.147  -20.550 -3.033  1.00 138.68 ? 227 GLN B CB  1 
ATOM   4620  C CG  . GLN B 1 227 ? 36.127  -20.887 -1.551  1.00 152.49 ? 227 GLN B CG  1 
ATOM   4621  C CD  . GLN B 1 227 ? 34.823  -21.523 -1.113  1.00 142.84 ? 227 GLN B CD  1 
ATOM   4622  O OE1 . GLN B 1 227 ? 33.889  -20.830 -0.711  1.00 148.32 ? 227 GLN B OE1 1 
ATOM   4623  N NE2 . GLN B 1 227 ? 34.753  -22.847 -1.185  1.00 130.09 ? 227 GLN B NE2 1 
ATOM   4624  N N   . ASP B 1 228 ? 36.888  -19.187 -5.766  1.00 115.68 ? 228 ASP B N   1 
ATOM   4625  C CA  . ASP B 1 228 ? 37.594  -19.266 -7.039  1.00 114.31 ? 228 ASP B CA  1 
ATOM   4626  C C   . ASP B 1 228 ? 37.272  -18.097 -7.960  1.00 114.75 ? 228 ASP B C   1 
ATOM   4627  O O   . ASP B 1 228 ? 37.648  -18.125 -9.138  1.00 113.45 ? 228 ASP B O   1 
ATOM   4628  C CB  . ASP B 1 228 ? 37.281  -20.599 -7.732  1.00 113.59 ? 228 ASP B CB  1 
ATOM   4629  C CG  . ASP B 1 228 ? 35.789  -20.851 -7.887  1.00 121.61 ? 228 ASP B CG  1 
ATOM   4630  O OD1 . ASP B 1 228 ? 35.013  -19.880 -8.010  1.00 124.38 ? 228 ASP B OD1 1 
ATOM   4631  O OD2 . ASP B 1 228 ? 35.387  -22.033 -7.871  1.00 126.20 ? 228 ASP B OD2 1 
ATOM   4632  N N   . ILE B 1 229 ? 36.590  -17.072 -7.456  1.00 117.80 ? 229 ILE B N   1 
ATOM   4633  C CA  . ILE B 1 229 ? 36.294  -15.879 -8.238  1.00 120.64 ? 229 ILE B CA  1 
ATOM   4634  C C   . ILE B 1 229 ? 36.727  -14.657 -7.441  1.00 128.19 ? 229 ILE B C   1 
ATOM   4635  O O   . ILE B 1 229 ? 37.357  -13.739 -7.978  1.00 135.05 ? 229 ILE B O   1 
ATOM   4636  C CB  . ILE B 1 229 ? 34.802  -15.802 -8.607  1.00 119.38 ? 229 ILE B CB  1 
ATOM   4637  C CG1 . ILE B 1 229 ? 34.414  -16.970 -9.516  1.00 120.24 ? 229 ILE B CG1 1 
ATOM   4638  C CG2 . ILE B 1 229 ? 34.489  -14.476 -9.281  1.00 115.13 ? 229 ILE B CG2 1 
ATOM   4639  C CD1 . ILE B 1 229 ? 32.955  -16.974 -9.915  1.00 117.45 ? 229 ILE B CD1 1 
ATOM   4640  N N   . LEU B 1 230 ? 36.386  -14.641 -6.151  1.00 133.37 ? 230 LEU B N   1 
ATOM   4641  C CA  . LEU B 1 230 ? 36.763  -13.525 -5.291  1.00 135.85 ? 230 LEU B CA  1 
ATOM   4642  C C   . LEU B 1 230 ? 38.236  -13.600 -4.904  1.00 135.61 ? 230 LEU B C   1 
ATOM   4643  O O   . LEU B 1 230 ? 38.947  -12.590 -4.946  1.00 141.65 ? 230 LEU B O   1 
ATOM   4644  C CB  . LEU B 1 230 ? 35.871  -13.491 -4.048  1.00 135.42 ? 230 LEU B CB  1 
ATOM   4645  C CG  . LEU B 1 230 ? 34.402  -13.144 -4.311  1.00 131.53 ? 230 LEU B CG  1 
ATOM   4646  C CD1 . LEU B 1 230 ? 33.639  -12.959 -3.008  1.00 132.44 ? 230 LEU B CD1 1 
ATOM   4647  C CD2 . LEU B 1 230 ? 34.285  -11.904 -5.187  1.00 126.88 ? 230 LEU B CD2 1 
ATOM   4648  N N   . SER B 1 231 ? 38.707  -14.784 -4.514  1.00 133.14 ? 231 SER B N   1 
ATOM   4649  C CA  . SER B 1 231 ? 40.117  -14.934 -4.158  1.00 134.07 ? 231 SER B CA  1 
ATOM   4650  C C   . SER B 1 231 ? 41.051  -14.666 -5.334  1.00 141.53 ? 231 SER B C   1 
ATOM   4651  O O   . SER B 1 231 ? 42.057  -13.962 -5.141  1.00 145.27 ? 231 SER B O   1 
ATOM   4652  C CB  . SER B 1 231 ? 40.355  -16.324 -3.557  1.00 130.52 ? 231 SER B CB  1 
ATOM   4653  O OG  . SER B 1 231 ? 39.486  -16.561 -2.466  1.00 130.23 ? 231 SER B OG  1 
ATOM   4654  N N   . PRO B 1 232 ? 40.812  -15.187 -6.546  1.00 138.83 ? 232 PRO B N   1 
ATOM   4655  C CA  . PRO B 1 232 ? 41.735  -14.885 -7.654  1.00 147.99 ? 232 PRO B CA  1 
ATOM   4656  C C   . PRO B 1 232 ? 41.787  -13.416 -8.039  1.00 173.33 ? 232 PRO B C   1 
ATOM   4657  O O   . PRO B 1 232 ? 42.861  -12.927 -8.413  1.00 175.06 ? 232 PRO B O   1 
ATOM   4658  C CB  . PRO B 1 232 ? 41.192  -15.747 -8.803  1.00 137.15 ? 232 PRO B CB  1 
ATOM   4659  C CG  . PRO B 1 232 ? 40.482  -16.858 -8.129  1.00 127.02 ? 232 PRO B CG  1 
ATOM   4660  C CD  . PRO B 1 232 ? 39.842  -16.227 -6.933  1.00 131.33 ? 232 PRO B CD  1 
ATOM   4661  N N   . LEU B 1 233 ? 40.670  -12.690 -7.962  1.00 243.98 ? 233 LEU B N   1 
ATOM   4662  C CA  . LEU B 1 233 ? 40.655  -11.268 -8.313  1.00 245.18 ? 233 LEU B CA  1 
ATOM   4663  C C   . LEU B 1 233 ? 41.158  -10.448 -7.123  1.00 244.77 ? 233 LEU B C   1 
ATOM   4664  O O   . LEU B 1 233 ? 40.413  -9.748  -6.434  1.00 245.08 ? 233 LEU B O   1 
ATOM   4665  C CB  . LEU B 1 233 ? 39.262  -10.836 -8.748  1.00 245.94 ? 233 LEU B CB  1 
ATOM   4666  C CG  . LEU B 1 233 ? 39.192  -10.166 -10.122 1.00 247.76 ? 233 LEU B CG  1 
ATOM   4667  C CD1 . LEU B 1 233 ? 39.502  -11.168 -11.223 1.00 247.97 ? 233 LEU B CD1 1 
ATOM   4668  C CD2 . LEU B 1 233 ? 37.834  -9.520  -10.341 1.00 248.43 ? 233 LEU B CD2 1 
ATOM   4669  N N   . ALA B 1 234 ? 42.467  -10.548 -6.891  1.00 173.04 ? 234 ALA B N   1 
ATOM   4670  C CA  . ALA B 1 234 ? 43.123  -9.855  -5.788  1.00 156.46 ? 234 ALA B CA  1 
ATOM   4671  C C   . ALA B 1 234 ? 44.007  -8.723  -6.299  1.00 142.98 ? 234 ALA B C   1 
ATOM   4672  O O   . ALA B 1 234 ? 43.651  -7.551  -6.162  1.00 135.10 ? 234 ALA B O   1 
ATOM   4673  C CB  . ALA B 1 234 ? 43.929  -10.850 -4.949  1.00 156.52 ? 234 ALA B CB  1 
ATOM   4674  N N   . GLY B 1 235 ? 45.153  -9.041  -6.903  1.00 145.95 ? 235 GLY B N   1 
ATOM   4675  C CA  . GLY B 1 235 ? 46.034  -7.990  -7.386  1.00 137.96 ? 235 GLY B CA  1 
ATOM   4676  C C   . GLY B 1 235 ? 45.424  -7.181  -8.513  1.00 139.18 ? 235 GLY B C   1 
ATOM   4677  O O   . GLY B 1 235 ? 45.652  -5.972  -8.614  1.00 137.60 ? 235 GLY B O   1 
ATOM   4678  N N   . LYS B 1 236 ? 44.640  -7.832  -9.372  1.00 135.42 ? 236 LYS B N   1 
ATOM   4679  C CA  . LYS B 1 236 ? 44.007  -7.144  -10.490 1.00 128.71 ? 236 LYS B CA  1 
ATOM   4680  C C   . LYS B 1 236 ? 42.989  -6.123  -9.993  1.00 123.86 ? 236 LYS B C   1 
ATOM   4681  O O   . LYS B 1 236 ? 42.071  -6.453  -9.236  1.00 126.40 ? 236 LYS B O   1 
ATOM   4682  C CB  . LYS B 1 236 ? 43.348  -8.159  -11.425 1.00 135.40 ? 236 LYS B CB  1 
ATOM   4683  C CG  . LYS B 1 236 ? 43.069  -9.516  -10.792 1.00 154.56 ? 236 LYS B CG  1 
ATOM   4684  C CD  . LYS B 1 236 ? 43.877  -10.625 -11.459 1.00 152.83 ? 236 LYS B CD  1 
ATOM   4685  C CE  . LYS B 1 236 ? 45.292  -10.710 -10.907 1.00 144.77 ? 236 LYS B CE  1 
ATOM   4686  N NZ  . LYS B 1 236 ? 45.310  -11.185 -9.494  1.00 152.14 ? 236 LYS B NZ  1 
ATOM   4687  N N   . LYS B 1 237 ? 43.161  -4.873  -10.426 1.00 120.32 ? 237 LYS B N   1 
ATOM   4688  C CA  . LYS B 1 237 ? 42.346  -3.752  -9.953  1.00 117.58 ? 237 LYS B CA  1 
ATOM   4689  C C   . LYS B 1 237 ? 40.939  -3.793  -10.552 1.00 116.91 ? 237 LYS B C   1 
ATOM   4690  O O   . LYS B 1 237 ? 40.589  -3.050  -11.474 1.00 117.13 ? 237 LYS B O   1 
ATOM   4691  C CB  . LYS B 1 237 ? 43.034  -2.428  -10.266 1.00 119.95 ? 237 LYS B CB  1 
ATOM   4692  C CG  . LYS B 1 237 ? 44.335  -2.202  -9.504  1.00 120.44 ? 237 LYS B CG  1 
ATOM   4693  C CD  . LYS B 1 237 ? 44.090  -1.592  -8.119  1.00 120.02 ? 237 LYS B CD  1 
ATOM   4694  C CE  . LYS B 1 237 ? 43.135  -0.413  -8.182  1.00 117.77 ? 237 LYS B CE  1 
ATOM   4695  N NZ  . LYS B 1 237 ? 43.746  0.798   -8.791  1.00 120.25 ? 237 LYS B NZ  1 
ATOM   4696  N N   . GLN B 1 238 ? 40.116  -4.696  -10.003 1.00 108.63 ? 238 GLN B N   1 
ATOM   4697  C CA  . GLN B 1 238 ? 38.697  -4.790  -10.331 1.00 99.94  ? 238 GLN B CA  1 
ATOM   4698  C C   . GLN B 1 238 ? 37.796  -4.963  -9.118  1.00 92.39  ? 238 GLN B C   1 
ATOM   4699  O O   . GLN B 1 238 ? 36.655  -4.497  -9.162  1.00 84.92  ? 238 GLN B O   1 
ATOM   4700  C CB  . GLN B 1 238 ? 38.428  -5.940  -11.315 1.00 100.79 ? 238 GLN B CB  1 
ATOM   4701  C CG  . GLN B 1 238 ? 38.858  -5.670  -12.734 1.00 100.64 ? 238 GLN B CG  1 
ATOM   4702  C CD  . GLN B 1 238 ? 40.051  -6.490  -13.117 1.00 114.44 ? 238 GLN B CD  1 
ATOM   4703  O OE1 . GLN B 1 238 ? 39.977  -7.716  -13.149 1.00 118.02 ? 238 GLN B OE1 1 
ATOM   4704  N NE2 . GLN B 1 238 ? 41.159  -5.829  -13.417 1.00 118.52 ? 238 GLN B NE2 1 
ATOM   4705  N N   . LEU B 1 239 ? 38.251  -5.606  -8.048  1.00 96.37  ? 239 LEU B N   1 
ATOM   4706  C CA  . LEU B 1 239 ? 37.453  -5.800  -6.842  1.00 88.95  ? 239 LEU B CA  1 
ATOM   4707  C C   . LEU B 1 239 ? 37.707  -4.649  -5.878  1.00 86.03  ? 239 LEU B C   1 
ATOM   4708  O O   . LEU B 1 239 ? 38.857  -4.372  -5.529  1.00 89.04  ? 239 LEU B O   1 
ATOM   4709  C CB  . LEU B 1 239 ? 37.797  -7.136  -6.176  1.00 103.29 ? 239 LEU B CB  1 
ATOM   4710  C CG  . LEU B 1 239 ? 36.630  -8.065  -5.915  1.00 101.35 ? 239 LEU B CG  1 
ATOM   4711  C CD1 . LEU B 1 239 ? 35.757  -7.449  -4.849  1.00 96.01  ? 239 LEU B CD1 1 
ATOM   4712  C CD2 . LEU B 1 239 ? 35.852  -8.247  -7.209  1.00 104.29 ? 239 LEU B CD2 1 
ATOM   4713  N N   . TYR B 1 240 ? 36.643  -3.975  -5.461  1.00 80.31  ? 240 TYR B N   1 
ATOM   4714  C CA  . TYR B 1 240 ? 36.791  -2.810  -4.609  1.00 81.67  ? 240 TYR B CA  1 
ATOM   4715  C C   . TYR B 1 240 ? 36.062  -3.023  -3.279  1.00 84.34  ? 240 TYR B C   1 
ATOM   4716  O O   . TYR B 1 240 ? 35.596  -4.120  -2.968  1.00 85.10  ? 240 TYR B O   1 
ATOM   4717  C CB  . TYR B 1 240 ? 36.311  -1.565  -5.353  1.00 81.10  ? 240 TYR B CB  1 
ATOM   4718  C CG  . TYR B 1 240 ? 37.237  -1.152  -6.482  1.00 84.14  ? 240 TYR B CG  1 
ATOM   4719  C CD1 . TYR B 1 240 ? 38.351  -0.353  -6.241  1.00 86.66  ? 240 TYR B CD1 1 
ATOM   4720  C CD2 . TYR B 1 240 ? 37.017  -1.590  -7.780  1.00 84.64  ? 240 TYR B CD2 1 
ATOM   4721  C CE1 . TYR B 1 240 ? 39.201  0.013   -7.266  1.00 87.66  ? 240 TYR B CE1 1 
ATOM   4722  C CE2 . TYR B 1 240 ? 37.866  -1.230  -8.812  1.00 90.33  ? 240 TYR B CE2 1 
ATOM   4723  C CZ  . TYR B 1 240 ? 38.957  -0.428  -8.547  1.00 91.66  ? 240 TYR B CZ  1 
ATOM   4724  O OH  . TYR B 1 240 ? 39.810  -0.061  -9.563  1.00 89.08  ? 240 TYR B OH  1 
ATOM   4725  N N   . THR B 1 241 ? 35.973  -1.958  -2.483  1.00 81.90  ? 241 THR B N   1 
ATOM   4726  C CA  . THR B 1 241 ? 35.388  -2.037  -1.148  1.00 88.99  ? 241 THR B CA  1 
ATOM   4727  C C   . THR B 1 241 ? 34.669  -0.735  -0.829  1.00 97.64  ? 241 THR B C   1 
ATOM   4728  O O   . THR B 1 241 ? 34.958  0.316   -1.407  1.00 94.39  ? 241 THR B O   1 
ATOM   4729  C CB  . THR B 1 241 ? 36.445  -2.320  -0.070  1.00 87.79  ? 241 THR B CB  1 
ATOM   4730  O OG1 . THR B 1 241 ? 37.623  -1.556  -0.350  1.00 88.03  ? 241 THR B OG1 1 
ATOM   4731  C CG2 . THR B 1 241 ? 36.795  -3.802  -0.028  1.00 89.59  ? 241 THR B CG2 1 
ATOM   4732  N N   . TYR B 1 242 ? 33.719  -0.822  0.101   1.00 119.07 ? 242 TYR B N   1 
ATOM   4733  C CA  . TYR B 1 242 ? 32.955  0.339   0.546   1.00 120.66 ? 242 TYR B CA  1 
ATOM   4734  C C   . TYR B 1 242 ? 32.471  0.071   1.963   1.00 119.06 ? 242 TYR B C   1 
ATOM   4735  O O   . TYR B 1 242 ? 31.786  -0.928  2.204   1.00 113.40 ? 242 TYR B O   1 
ATOM   4736  C CB  . TYR B 1 242 ? 31.785  0.606   -0.401  1.00 119.85 ? 242 TYR B CB  1 
ATOM   4737  C CG  . TYR B 1 242 ? 30.769  1.617   0.080   1.00 119.48 ? 242 TYR B CG  1 
ATOM   4738  C CD1 . TYR B 1 242 ? 31.017  2.980   -0.012  1.00 122.01 ? 242 TYR B CD1 1 
ATOM   4739  C CD2 . TYR B 1 242 ? 29.546  1.208   0.593   1.00 118.75 ? 242 TYR B CD2 1 
ATOM   4740  C CE1 . TYR B 1 242 ? 30.083  3.907   0.415   1.00 121.49 ? 242 TYR B CE1 1 
ATOM   4741  C CE2 . TYR B 1 242 ? 28.605  2.126   1.022   1.00 119.42 ? 242 TYR B CE2 1 
ATOM   4742  C CZ  . TYR B 1 242 ? 28.879  3.475   0.931   1.00 118.62 ? 242 TYR B CZ  1 
ATOM   4743  O OH  . TYR B 1 242 ? 27.945  4.393   1.357   1.00 119.50 ? 242 TYR B OH  1 
ATOM   4744  N N   . GLU B 1 243 ? 32.822  0.961   2.889   1.00 126.66 ? 243 GLU B N   1 
ATOM   4745  C CA  . GLU B 1 243 ? 32.544  0.742   4.303   1.00 124.39 ? 243 GLU B CA  1 
ATOM   4746  C C   . GLU B 1 243 ? 31.049  0.834   4.598   1.00 124.14 ? 243 GLU B C   1 
ATOM   4747  O O   . GLU B 1 243 ? 30.303  1.563   3.938   1.00 125.62 ? 243 GLU B O   1 
ATOM   4748  C CB  . GLU B 1 243 ? 33.309  1.755   5.156   1.00 125.26 ? 243 GLU B CB  1 
ATOM   4749  N N   . ASN B 1 244 ? 30.616  0.077   5.610   1.00 106.96 ? 244 ASN B N   1 
ATOM   4750  C CA  . ASN B 1 244 ? 29.218  0.095   6.028   1.00 102.25 ? 244 ASN B CA  1 
ATOM   4751  C C   . ASN B 1 244 ? 28.891  1.352   6.828   1.00 99.50  ? 244 ASN B C   1 
ATOM   4752  O O   . ASN B 1 244 ? 28.001  2.125   6.453   1.00 103.46 ? 244 ASN B O   1 
ATOM   4753  C CB  . ASN B 1 244 ? 28.905  -1.161  6.849   1.00 99.98  ? 244 ASN B CB  1 
ATOM   4754  C CG  . ASN B 1 244 ? 27.412  -1.386  7.042   1.00 100.00 ? 244 ASN B CG  1 
ATOM   4755  O OD1 . ASN B 1 244 ? 26.607  -0.456  6.945   1.00 99.76  ? 244 ASN B OD1 1 
ATOM   4756  N ND2 . ASN B 1 244 ? 27.038  -2.626  7.322   1.00 100.29 ? 244 ASN B ND2 1 
ATOM   4757  N N   . LYS B 1 245 ? 29.586  1.551   7.952   1.00 93.36  ? 245 LYS B N   1 
ATOM   4758  C CA  . LYS B 1 245 ? 29.354  2.673   8.864   1.00 93.57  ? 245 LYS B CA  1 
ATOM   4759  C C   . LYS B 1 245 ? 27.972  2.604   9.514   1.00 97.96  ? 245 LYS B C   1 
ATOM   4760  O O   . LYS B 1 245 ? 27.386  3.635   9.853   1.00 100.91 ? 245 LYS B O   1 
ATOM   4761  C CB  . LYS B 1 245 ? 29.553  4.026   8.172   1.00 93.66  ? 245 LYS B CB  1 
ATOM   4762  N N   . ASP B 1 246 ? 27.442  1.393   9.695   1.00 100.03 ? 246 ASP B N   1 
ATOM   4763  C CA  . ASP B 1 246 ? 26.163  1.201   10.370  1.00 102.54 ? 246 ASP B CA  1 
ATOM   4764  C C   . ASP B 1 246 ? 26.145  -0.119  11.133  1.00 106.11 ? 246 ASP B C   1 
ATOM   4765  O O   . ASP B 1 246 ? 26.986  -0.343  12.009  1.00 107.75 ? 246 ASP B O   1 
ATOM   4766  C CB  . ASP B 1 246 ? 25.009  1.252   9.363   1.00 103.19 ? 246 ASP B CB  1 
ATOM   4767  C CG  . ASP B 1 246 ? 24.525  2.666   9.100   1.00 102.34 ? 246 ASP B CG  1 
ATOM   4768  O OD1 . ASP B 1 246 ? 24.112  3.345   10.065  1.00 104.52 ? 246 ASP B OD1 1 
ATOM   4769  O OD2 . ASP B 1 246 ? 24.553  3.098   7.927   1.00 97.87  ? 246 ASP B OD2 1 
ATOM   4770  N N   . PHE B 1 247 ? 25.195  -0.997  10.816  1.00 132.42 ? 247 PHE B N   1 
ATOM   4771  C CA  . PHE B 1 247 ? 25.037  -2.263  11.516  1.00 131.57 ? 247 PHE B CA  1 
ATOM   4772  C C   . PHE B 1 247 ? 25.140  -3.430  10.540  1.00 130.21 ? 247 PHE B C   1 
ATOM   4773  O O   . PHE B 1 247 ? 24.957  -3.276  9.331   1.00 130.30 ? 247 PHE B O   1 
ATOM   4774  C CB  . PHE B 1 247 ? 23.703  -2.317  12.285  1.00 131.55 ? 247 PHE B CB  1 
ATOM   4775  C CG  . PHE B 1 247 ? 22.501  -1.913  11.469  1.00 131.65 ? 247 PHE B CG  1 
ATOM   4776  C CD1 . PHE B 1 247 ? 22.139  -0.579  11.354  1.00 133.25 ? 247 PHE B CD1 1 
ATOM   4777  C CD2 . PHE B 1 247 ? 21.714  -2.867  10.846  1.00 130.49 ? 247 PHE B CD2 1 
ATOM   4778  C CE1 . PHE B 1 247 ? 21.030  -0.205  10.615  1.00 133.56 ? 247 PHE B CE1 1 
ATOM   4779  C CE2 . PHE B 1 247 ? 20.603  -2.499  10.109  1.00 130.96 ? 247 PHE B CE2 1 
ATOM   4780  C CZ  . PHE B 1 247 ? 20.261  -1.167  9.993   1.00 132.54 ? 247 PHE B CZ  1 
ATOM   4781  N N   . TRP B 1 248 ? 25.450  -4.607  11.085  1.00 112.35 ? 248 TRP B N   1 
ATOM   4782  C CA  . TRP B 1 248 ? 25.495  -5.837  10.305  1.00 104.47 ? 248 TRP B CA  1 
ATOM   4783  C C   . TRP B 1 248 ? 25.442  -7.029  11.249  1.00 102.72 ? 248 TRP B C   1 
ATOM   4784  O O   . TRP B 1 248 ? 26.133  -7.046  12.271  1.00 103.26 ? 248 TRP B O   1 
ATOM   4785  C CB  . TRP B 1 248 ? 26.759  -5.914  9.444   1.00 105.36 ? 248 TRP B CB  1 
ATOM   4786  C CG  . TRP B 1 248 ? 26.762  -7.090  8.518   1.00 104.67 ? 248 TRP B CG  1 
ATOM   4787  C CD1 . TRP B 1 248 ? 26.076  -7.212  7.346   1.00 106.21 ? 248 TRP B CD1 1 
ATOM   4788  C CD2 . TRP B 1 248 ? 27.466  -8.324  8.702   1.00 102.17 ? 248 TRP B CD2 1 
ATOM   4789  N NE1 . TRP B 1 248 ? 26.320  -8.442  6.781   1.00 102.82 ? 248 TRP B NE1 1 
ATOM   4790  C CE2 . TRP B 1 248 ? 27.169  -9.144  7.596   1.00 100.96 ? 248 TRP B CE2 1 
ATOM   4791  C CE3 . TRP B 1 248 ? 28.323  -8.813  9.693   1.00 101.92 ? 248 TRP B CE3 1 
ATOM   4792  C CZ2 . TRP B 1 248 ? 27.699  -10.425 7.452   1.00 102.58 ? 248 TRP B CZ2 1 
ATOM   4793  C CZ3 . TRP B 1 248 ? 28.848  -10.084 9.550   1.00 101.91 ? 248 TRP B CZ3 1 
ATOM   4794  C CH2 . TRP B 1 248 ? 28.534  -10.876 8.437   1.00 105.01 ? 248 TRP B CH2 1 
ATOM   4795  N N   . GLU B 1 249 ? 24.617  -8.018  10.906  1.00 100.94 ? 249 GLU B N   1 
ATOM   4796  C CA  . GLU B 1 249 ? 24.481  -9.221  11.724  1.00 97.67  ? 249 GLU B CA  1 
ATOM   4797  C C   . GLU B 1 249 ? 24.043  -10.382 10.844  1.00 97.16  ? 249 GLU B C   1 
ATOM   4798  O O   . GLU B 1 249 ? 22.967  -10.331 10.242  1.00 99.35  ? 249 GLU B O   1 
ATOM   4799  C CB  . GLU B 1 249 ? 23.484  -8.999  12.861  1.00 97.78  ? 249 GLU B CB  1 
ATOM   4800  N N   . GLN B 1 250 ? 24.876  -11.419 10.768  1.00 98.34  ? 250 GLN B N   1 
ATOM   4801  C CA  . GLN B 1 250 ? 24.526  -12.624 10.023  1.00 103.23 ? 250 GLN B CA  1 
ATOM   4802  C C   . GLN B 1 250 ? 23.435  -13.400 10.756  1.00 107.41 ? 250 GLN B C   1 
ATOM   4803  O O   . GLN B 1 250 ? 23.536  -13.639 11.964  1.00 105.42 ? 250 GLN B O   1 
ATOM   4804  C CB  . GLN B 1 250 ? 25.765  -13.499 9.826   1.00 105.65 ? 250 GLN B CB  1 
ATOM   4805  C CG  . GLN B 1 250 ? 25.912  -14.098 8.431   1.00 106.36 ? 250 GLN B CG  1 
ATOM   4806  C CD  . GLN B 1 250 ? 25.288  -15.475 8.308   1.00 106.60 ? 250 GLN B CD  1 
ATOM   4807  O OE1 . GLN B 1 250 ? 24.094  -15.653 8.548   1.00 108.79 ? 250 GLN B OE1 1 
ATOM   4808  N NE2 . GLN B 1 250 ? 26.098  -16.460 7.933   1.00 105.66 ? 250 GLN B NE2 1 
ATOM   4809  N N   . ILE B 1 251 ? 22.390  -13.794 10.027  1.00 126.07 ? 251 ILE B N   1 
ATOM   4810  C CA  . ILE B 1 251 ? 21.229  -14.424 10.649  1.00 125.67 ? 251 ILE B CA  1 
ATOM   4811  C C   . ILE B 1 251 ? 20.936  -15.798 10.055  1.00 124.98 ? 251 ILE B C   1 
ATOM   4812  O O   . ILE B 1 251 ? 19.908  -15.994 9.396   1.00 124.51 ? 251 ILE B O   1 
ATOM   4813  C CB  . ILE B 1 251 ? 19.989  -13.517 10.542  1.00 125.44 ? 251 ILE B CB  1 
ATOM   4814  C CG1 . ILE B 1 251 ? 19.878  -12.918 9.138   1.00 125.69 ? 251 ILE B CG1 1 
ATOM   4815  C CG2 . ILE B 1 251 ? 20.034  -12.423 11.594  1.00 126.07 ? 251 ILE B CG2 1 
ATOM   4816  C CD1 . ILE B 1 251 ? 18.456  -12.707 8.688   1.00 126.11 ? 251 ILE B CD1 1 
ATOM   4817  N N   . LYS B 1 252 ? 21.819  -16.763 10.297  1.00 109.49 ? 252 LYS B N   1 
ATOM   4818  C CA  . LYS B 1 252 ? 21.515  -18.150 9.974   1.00 105.35 ? 252 LYS B CA  1 
ATOM   4819  C C   . LYS B 1 252 ? 20.842  -18.880 11.128  1.00 100.31 ? 252 LYS B C   1 
ATOM   4820  O O   . LYS B 1 252 ? 20.289  -19.965 10.921  1.00 97.23  ? 252 LYS B O   1 
ATOM   4821  C CB  . LYS B 1 252 ? 22.786  -18.907 9.574   1.00 108.38 ? 252 LYS B CB  1 
ATOM   4822  C CG  . LYS B 1 252 ? 23.778  -19.090 10.708  1.00 107.55 ? 252 LYS B CG  1 
ATOM   4823  C CD  . LYS B 1 252 ? 24.964  -18.154 10.560  1.00 105.92 ? 252 LYS B CD  1 
ATOM   4824  C CE  . LYS B 1 252 ? 25.484  -17.706 11.914  1.00 106.64 ? 252 LYS B CE  1 
ATOM   4825  N NZ  . LYS B 1 252 ? 24.477  -16.868 12.621  1.00 108.53 ? 252 LYS B NZ  1 
ATOM   4826  N N   . THR B 1 253 ? 20.881  -18.314 12.333  1.00 103.40 ? 253 THR B N   1 
ATOM   4827  C CA  . THR B 1 253 ? 20.292  -18.797 13.575  1.00 101.61 ? 253 THR B CA  1 
ATOM   4828  C C   . THR B 1 253 ? 18.900  -18.203 13.772  1.00 98.50  ? 253 THR B C   1 
ATOM   4829  O O   . THR B 1 253 ? 18.702  -17.003 13.561  1.00 99.99  ? 253 THR B O   1 
ATOM   4830  C CB  . THR B 1 253 ? 21.167  -18.427 14.769  1.00 105.62 ? 253 THR B CB  1 
ATOM   4831  O OG1 . THR B 1 253 ? 22.453  -17.992 14.306  1.00 105.89 ? 253 THR B OG1 1 
ATOM   4832  C CG2 . THR B 1 253 ? 21.345  -19.626 15.690  1.00 106.25 ? 253 THR B CG2 1 
ATOM   4833  N N   . PRO B 1 254 ? 17.919  -19.015 14.176  1.00 98.48  ? 254 PRO B N   1 
ATOM   4834  C CA  . PRO B 1 254 ? 16.610  -18.450 14.539  1.00 96.50  ? 254 PRO B CA  1 
ATOM   4835  C C   . PRO B 1 254 ? 16.655  -17.581 15.783  1.00 102.66 ? 254 PRO B C   1 
ATOM   4836  O O   . PRO B 1 254 ? 15.768  -16.737 15.958  1.00 98.42  ? 254 PRO B O   1 
ATOM   4837  C CB  . PRO B 1 254 ? 15.736  -19.693 14.751  1.00 88.99  ? 254 PRO B CB  1 
ATOM   4838  C CG  . PRO B 1 254 ? 16.703  -20.774 15.099  1.00 96.07  ? 254 PRO B CG  1 
ATOM   4839  C CD  . PRO B 1 254 ? 17.945  -20.483 14.302  1.00 97.86  ? 254 PRO B CD  1 
ATOM   4840  N N   . GLY B 1 255 ? 17.654  -17.757 16.650  1.00 131.95 ? 255 GLY B N   1 
ATOM   4841  C CA  . GLY B 1 255 ? 17.761  -16.904 17.823  1.00 132.94 ? 255 GLY B CA  1 
ATOM   4842  C C   . GLY B 1 255 ? 18.209  -15.496 17.484  1.00 132.92 ? 255 GLY B C   1 
ATOM   4843  O O   . GLY B 1 255 ? 17.759  -14.527 18.102  1.00 133.41 ? 255 GLY B O   1 
ATOM   4844  N N   . LYS B 1 256 ? 19.101  -15.362 16.497  1.00 107.11 ? 256 LYS B N   1 
ATOM   4845  C CA  . LYS B 1 256 ? 19.559  -14.050 16.050  1.00 101.66 ? 256 LYS B CA  1 
ATOM   4846  C C   . LYS B 1 256 ? 18.438  -13.204 15.460  1.00 96.22  ? 256 LYS B C   1 
ATOM   4847  O O   . LYS B 1 256 ? 18.636  -12.001 15.259  1.00 89.33  ? 256 LYS B O   1 
ATOM   4848  C CB  . LYS B 1 256 ? 20.674  -14.208 15.013  1.00 105.84 ? 256 LYS B CB  1 
ATOM   4849  C CG  . LYS B 1 256 ? 22.057  -14.512 15.578  1.00 102.45 ? 256 LYS B CG  1 
ATOM   4850  C CD  . LYS B 1 256 ? 22.603  -13.334 16.370  1.00 99.73  ? 256 LYS B CD  1 
ATOM   4851  C CE  . LYS B 1 256 ? 24.116  -13.406 16.491  1.00 97.53  ? 256 LYS B CE  1 
ATOM   4852  N NZ  . LYS B 1 256 ? 24.758  -13.440 15.146  1.00 95.83  ? 256 LYS B NZ  1 
ATOM   4853  N N   . SER B 1 257 ? 17.272  -13.797 15.190  1.00 98.37  ? 257 SER B N   1 
ATOM   4854  C CA  . SER B 1 257 ? 16.152  -13.070 14.604  1.00 92.19  ? 257 SER B CA  1 
ATOM   4855  C C   . SER B 1 257 ? 15.639  -11.949 15.497  1.00 82.67  ? 257 SER B C   1 
ATOM   4856  O O   . SER B 1 257 ? 14.817  -11.147 15.041  1.00 82.15  ? 257 SER B O   1 
ATOM   4857  C CB  . SER B 1 257 ? 15.016  -14.044 14.284  1.00 89.47  ? 257 SER B CB  1 
ATOM   4858  O OG  . SER B 1 257 ? 15.485  -15.117 13.484  1.00 90.32  ? 257 SER B OG  1 
ATOM   4859  N N   . LEU B 1 258 ? 16.092  -11.875 16.749  1.00 82.58  ? 258 LEU B N   1 
ATOM   4860  C CA  . LEU B 1 258 ? 15.738  -10.799 17.665  1.00 80.60  ? 258 LEU B CA  1 
ATOM   4861  C C   . LEU B 1 258 ? 16.792  -9.699  17.694  1.00 85.47  ? 258 LEU B C   1 
ATOM   4862  O O   . LEU B 1 258 ? 16.454  -8.514  17.614  1.00 77.20  ? 258 LEU B O   1 
ATOM   4863  C CB  . LEU B 1 258 ? 15.534  -11.355 19.078  1.00 89.97  ? 258 LEU B CB  1 
ATOM   4864  C CG  . LEU B 1 258 ? 14.242  -12.127 19.346  1.00 82.95  ? 258 LEU B CG  1 
ATOM   4865  C CD1 . LEU B 1 258 ? 14.246  -12.669 20.763  1.00 78.66  ? 258 LEU B CD1 1 
ATOM   4866  C CD2 . LEU B 1 258 ? 13.033  -11.241 19.112  1.00 86.04  ? 258 LEU B CD2 1 
ATOM   4867  N N   . LYS B 1 259 ? 18.068  -10.078 17.828  1.00 81.59  ? 259 LYS B N   1 
ATOM   4868  C CA  . LYS B 1 259 ? 19.151  -9.099  17.856  1.00 83.02  ? 259 LYS B CA  1 
ATOM   4869  C C   . LYS B 1 259 ? 19.140  -8.224  16.611  1.00 75.45  ? 259 LYS B C   1 
ATOM   4870  O O   . LYS B 1 259 ? 19.364  -7.011  16.691  1.00 77.93  ? 259 LYS B O   1 
ATOM   4871  C CB  . LYS B 1 259 ? 20.494  -9.821  17.982  1.00 89.94  ? 259 LYS B CB  1 
ATOM   4872  C CG  . LYS B 1 259 ? 21.695  -8.910  18.161  1.00 91.71  ? 259 LYS B CG  1 
ATOM   4873  C CD  . LYS B 1 259 ? 22.974  -9.726  18.277  1.00 93.08  ? 259 LYS B CD  1 
ATOM   4874  C CE  . LYS B 1 259 ? 24.169  -8.850  18.607  1.00 93.94  ? 259 LYS B CE  1 
ATOM   4875  N NZ  . LYS B 1 259 ? 24.007  -8.176  19.924  1.00 103.13 ? 259 LYS B NZ  1 
ATOM   4876  N N   . CYS B 1 260 ? 18.884  -8.823  15.451  1.00 75.77  ? 260 CYS B N   1 
ATOM   4877  C CA  . CYS B 1 260 ? 18.781  -8.046  14.225  1.00 78.74  ? 260 CYS B CA  1 
ATOM   4878  C C   . CYS B 1 260 ? 17.454  -7.305  14.133  1.00 75.65  ? 260 CYS B C   1 
ATOM   4879  O O   . CYS B 1 260 ? 17.392  -6.229  13.528  1.00 80.60  ? 260 CYS B O   1 
ATOM   4880  C CB  . CYS B 1 260 ? 18.958  -8.961  13.018  1.00 80.40  ? 260 CYS B CB  1 
ATOM   4881  S SG  . CYS B 1 260 ? 17.581  -10.100 12.775  1.00 92.76  ? 260 CYS B SG  1 
ATOM   4882  N N   . SER B 1 261 ? 16.388  -7.869  14.708  1.00 75.05  ? 261 SER B N   1 
ATOM   4883  C CA  . SER B 1 261 ? 15.091  -7.200  14.689  1.00 75.15  ? 261 SER B CA  1 
ATOM   4884  C C   . SER B 1 261 ? 15.140  -5.861  15.411  1.00 76.62  ? 261 SER B C   1 
ATOM   4885  O O   . SER B 1 261 ? 14.432  -4.923  15.027  1.00 75.28  ? 261 SER B O   1 
ATOM   4886  C CB  . SER B 1 261 ? 14.026  -8.103  15.313  1.00 73.55  ? 261 SER B CB  1 
ATOM   4887  O OG  . SER B 1 261 ? 12.758  -7.472  15.331  1.00 77.11  ? 261 SER B OG  1 
ATOM   4888  N N   . ALA B 1 262 ? 15.958  -5.756  16.461  1.00 74.53  ? 262 ALA B N   1 
ATOM   4889  C CA  . ALA B 1 262 ? 16.088  -4.490  17.173  1.00 76.35  ? 262 ALA B CA  1 
ATOM   4890  C C   . ALA B 1 262 ? 16.769  -3.438  16.306  1.00 77.13  ? 262 ALA B C   1 
ATOM   4891  O O   . ALA B 1 262 ? 16.433  -2.251  16.383  1.00 79.81  ? 262 ALA B O   1 
ATOM   4892  C CB  . ALA B 1 262 ? 16.859  -4.694  18.477  1.00 78.31  ? 262 ALA B CB  1 
ATOM   4893  N N   . LEU B 1 263 ? 17.727  -3.855  15.475  1.00 80.74  ? 263 LEU B N   1 
ATOM   4894  C CA  . LEU B 1 263 ? 18.424  -2.905  14.613  1.00 81.22  ? 263 LEU B CA  1 
ATOM   4895  C C   . LEU B 1 263 ? 17.494  -2.345  13.542  1.00 86.30  ? 263 LEU B C   1 
ATOM   4896  O O   . LEU B 1 263 ? 17.569  -1.157  13.207  1.00 87.62  ? 263 LEU B O   1 
ATOM   4897  C CB  . LEU B 1 263 ? 19.648  -3.569  13.982  1.00 90.55  ? 263 LEU B CB  1 
ATOM   4898  C CG  . LEU B 1 263 ? 20.657  -4.151  14.976  1.00 84.78  ? 263 LEU B CG  1 
ATOM   4899  C CD1 . LEU B 1 263 ? 21.779  -4.882  14.253  1.00 90.16  ? 263 LEU B CD1 1 
ATOM   4900  C CD2 . LEU B 1 263 ? 21.213  -3.059  15.879  1.00 82.60  ? 263 LEU B CD2 1 
ATOM   4901  N N   . TYR B 1 264 ? 16.616  -3.188  12.988  1.00 79.10  ? 264 TYR B N   1 
ATOM   4902  C CA  . TYR B 1 264 ? 15.641  -2.713  12.010  1.00 80.59  ? 264 TYR B CA  1 
ATOM   4903  C C   . TYR B 1 264 ? 14.666  -1.719  12.632  1.00 79.23  ? 264 TYR B C   1 
ATOM   4904  O O   . TYR B 1 264 ? 14.314  -0.710  12.010  1.00 84.65  ? 264 TYR B O   1 
ATOM   4905  C CB  . TYR B 1 264 ? 14.875  -3.896  11.414  1.00 78.65  ? 264 TYR B CB  1 
ATOM   4906  C CG  . TYR B 1 264 ? 15.610  -4.653  10.331  1.00 78.68  ? 264 TYR B CG  1 
ATOM   4907  C CD1 . TYR B 1 264 ? 16.499  -4.005  9.483   1.00 87.78  ? 264 TYR B CD1 1 
ATOM   4908  C CD2 . TYR B 1 264 ? 15.414  -6.018  10.156  1.00 77.11  ? 264 TYR B CD2 1 
ATOM   4909  C CE1 . TYR B 1 264 ? 17.172  -4.696  8.490   1.00 87.83  ? 264 TYR B CE1 1 
ATOM   4910  C CE2 . TYR B 1 264 ? 16.084  -6.718  9.165   1.00 81.32  ? 264 TYR B CE2 1 
ATOM   4911  C CZ  . TYR B 1 264 ? 16.962  -6.049  8.335   1.00 82.95  ? 264 TYR B CZ  1 
ATOM   4912  O OH  . TYR B 1 264 ? 17.632  -6.734  7.348   1.00 78.28  ? 264 TYR B OH  1 
ATOM   4913  N N   . LEU B 1 265 ? 14.208  -1.996  13.857  1.00 88.35  ? 265 LEU B N   1 
ATOM   4914  C CA  . LEU B 1 265 ? 13.314  -1.067  14.543  1.00 84.10  ? 265 LEU B CA  1 
ATOM   4915  C C   . LEU B 1 265 ? 14.012  0.248   14.868  1.00 86.09  ? 265 LEU B C   1 
ATOM   4916  O O   . LEU B 1 265 ? 13.416  1.323   14.728  1.00 89.65  ? 265 LEU B O   1 
ATOM   4917  C CB  . LEU B 1 265 ? 12.763  -1.713  15.814  1.00 88.85  ? 265 LEU B CB  1 
ATOM   4918  C CG  . LEU B 1 265 ? 11.862  -2.933  15.604  1.00 86.20  ? 265 LEU B CG  1 
ATOM   4919  C CD1 . LEU B 1 265 ? 11.403  -3.513  16.936  1.00 87.77  ? 265 LEU B CD1 1 
ATOM   4920  C CD2 . LEU B 1 265 ? 10.673  -2.579  14.724  1.00 87.94  ? 265 LEU B CD2 1 
ATOM   4921  N N   . SER B 1 266 ? 15.273  0.188   15.307  1.00 91.17  ? 266 SER B N   1 
ATOM   4922  C CA  . SER B 1 266 ? 16.050  1.411   15.483  1.00 92.44  ? 266 SER B CA  1 
ATOM   4923  C C   . SER B 1 266 ? 16.198  2.165   14.170  1.00 92.85  ? 266 SER B C   1 
ATOM   4924  O O   . SER B 1 266 ? 16.222  3.401   14.162  1.00 92.54  ? 266 SER B O   1 
ATOM   4925  C CB  . SER B 1 266 ? 17.422  1.088   16.070  1.00 92.42  ? 266 SER B CB  1 
ATOM   4926  O OG  . SER B 1 266 ? 18.231  2.248   16.135  1.00 101.69 ? 266 SER B OG  1 
ATOM   4927  N N   . GLN B 1 267 ? 16.292  1.439   13.054  1.00 90.01  ? 267 GLN B N   1 
ATOM   4928  C CA  . GLN B 1 267 ? 16.315  2.071   11.741  1.00 87.65  ? 267 GLN B CA  1 
ATOM   4929  C C   . GLN B 1 267 ? 14.989  2.746   11.429  1.00 87.40  ? 267 GLN B C   1 
ATOM   4930  O O   . GLN B 1 267 ? 14.963  3.791   10.767  1.00 88.68  ? 267 GLN B O   1 
ATOM   4931  C CB  . GLN B 1 267 ? 16.633  1.025   10.674  1.00 87.06  ? 267 GLN B CB  1 
ATOM   4932  C CG  . GLN B 1 267 ? 16.898  1.576   9.291   1.00 92.34  ? 267 GLN B CG  1 
ATOM   4933  C CD  . GLN B 1 267 ? 17.051  0.474   8.265   1.00 93.99  ? 267 GLN B CD  1 
ATOM   4934  O OE1 . GLN B 1 267 ? 16.453  -0.596  8.393   1.00 90.98  ? 267 GLN B OE1 1 
ATOM   4935  N NE2 . GLN B 1 267 ? 17.856  0.725   7.240   1.00 94.93  ? 267 GLN B NE2 1 
ATOM   4936  N N   . PHE B 1 268 ? 13.886  2.172   11.903  1.00 86.43  ? 268 PHE B N   1 
ATOM   4937  C CA  . PHE B 1 268 ? 12.575  2.791   11.794  1.00 90.35  ? 268 PHE B CA  1 
ATOM   4938  C C   . PHE B 1 268 ? 12.308  3.761   12.931  1.00 91.23  ? 268 PHE B C   1 
ATOM   4939  O O   . PHE B 1 268 ? 11.245  4.384   12.962  1.00 99.93  ? 268 PHE B O   1 
ATOM   4940  C CB  . PHE B 1 268 ? 11.474  1.726   11.750  1.00 91.97  ? 268 PHE B CB  1 
ATOM   4941  C CG  . PHE B 1 268 ? 11.662  0.701   10.665  1.00 92.00  ? 268 PHE B CG  1 
ATOM   4942  C CD1 . PHE B 1 268 ? 12.326  1.024   9.492   1.00 95.00  ? 268 PHE B CD1 1 
ATOM   4943  C CD2 . PHE B 1 268 ? 11.146  -0.577  10.804  1.00 88.51  ? 268 PHE B CD2 1 
ATOM   4944  C CE1 . PHE B 1 268 ? 12.496  0.087   8.490   1.00 94.24  ? 268 PHE B CE1 1 
ATOM   4945  C CE2 . PHE B 1 268 ? 11.308  -1.517  9.805   1.00 87.85  ? 268 PHE B CE2 1 
ATOM   4946  C CZ  . PHE B 1 268 ? 11.983  -1.186  8.647   1.00 91.94  ? 268 PHE B CZ  1 
ATOM   4947  N N   . ARG B 1 269 ? 13.243  3.888   13.868  1.00 91.59  ? 269 ARG B N   1 
ATOM   4948  C CA  . ARG B 1 269 ? 13.176  4.906   14.904  1.00 93.51  ? 269 ARG B CA  1 
ATOM   4949  C C   . ARG B 1 269 ? 14.030  6.120   14.571  1.00 94.73  ? 269 ARG B C   1 
ATOM   4950  O O   . ARG B 1 269 ? 13.711  7.230   15.007  1.00 97.03  ? 269 ARG B O   1 
ATOM   4951  C CB  . ARG B 1 269 ? 13.611  4.320   16.253  1.00 93.47  ? 269 ARG B CB  1 
ATOM   4952  C CG  . ARG B 1 269 ? 12.907  4.934   17.449  1.00 97.46  ? 269 ARG B CG  1 
ATOM   4953  C CD  . ARG B 1 269 ? 11.408  4.991   17.221  1.00 99.60  ? 269 ARG B CD  1 
ATOM   4954  N NE  . ARG B 1 269 ? 10.661  4.240   18.223  1.00 106.12 ? 269 ARG B NE  1 
ATOM   4955  C CZ  . ARG B 1 269 ? 9.343   4.320   18.375  1.00 113.69 ? 269 ARG B CZ  1 
ATOM   4956  N NH1 . ARG B 1 269 ? 8.637   5.123   17.592  1.00 119.31 ? 269 ARG B NH1 1 
ATOM   4957  N NH2 . ARG B 1 269 ? 8.731   3.607   19.311  1.00 115.37 ? 269 ARG B NH2 1 
ATOM   4958  N N   . GLU B 1 270 ? 15.113  5.927   13.815  1.00 92.91  ? 270 GLU B N   1 
ATOM   4959  C CA  . GLU B 1 270 ? 15.825  7.050   13.216  1.00 89.92  ? 270 GLU B CA  1 
ATOM   4960  C C   . GLU B 1 270 ? 15.037  7.621   12.044  1.00 90.58  ? 270 GLU B C   1 
ATOM   4961  O O   . GLU B 1 270 ? 14.705  8.812   12.023  1.00 94.24  ? 270 GLU B O   1 
ATOM   4962  C CB  . GLU B 1 270 ? 17.220  6.609   12.770  1.00 86.26  ? 270 GLU B CB  1 
ATOM   4963  N N   . THR B 1 271 ? 14.734  6.781   11.056  1.00 90.84  ? 271 THR B N   1 
ATOM   4964  C CA  . THR B 1 271 ? 13.944  7.176   9.900   1.00 91.86  ? 271 THR B CA  1 
ATOM   4965  C C   . THR B 1 271 ? 12.490  6.789   10.134  1.00 104.09 ? 271 THR B C   1 
ATOM   4966  O O   . THR B 1 271 ? 12.201  5.651   10.521  1.00 105.42 ? 271 THR B O   1 
ATOM   4967  C CB  . THR B 1 271 ? 14.465  6.507   8.629   1.00 84.07  ? 271 THR B CB  1 
ATOM   4968  O OG1 . THR B 1 271 ? 13.883  5.205   8.503   1.00 78.06  ? 271 THR B OG1 1 
ATOM   4969  C CG2 . THR B 1 271 ? 15.978  6.371   8.687   1.00 92.35  ? 271 THR B CG2 1 
ATOM   4970  N N   . SER B 1 272 ? 11.581  7.730   9.864   1.00 113.69 ? 272 SER B N   1 
ATOM   4971  C CA  . SER B 1 272 ? 10.137  7.572   10.025  1.00 114.11 ? 272 SER B CA  1 
ATOM   4972  C C   . SER B 1 272 ? 9.776   6.840   11.313  1.00 115.75 ? 272 SER B C   1 
ATOM   4973  O O   . SER B 1 272 ? 9.407   5.660   11.270  1.00 111.15 ? 272 SER B O   1 
ATOM   4974  C CB  . SER B 1 272 ? 9.551   6.827   8.826   1.00 107.10 ? 272 SER B CB  1 
ATOM   4975  O OG  . SER B 1 272 ? 10.062  5.507   8.747   1.00 96.83  ? 272 SER B OG  1 
ATOM   4976  N N   . PRO B 1 273 ? 9.863   7.498   12.475  1.00 130.22 ? 273 PRO B N   1 
ATOM   4977  C CA  . PRO B 1 273 ? 9.513   6.816   13.728  1.00 130.74 ? 273 PRO B CA  1 
ATOM   4978  C C   . PRO B 1 273 ? 8.017   6.705   13.951  1.00 129.23 ? 273 PRO B C   1 
ATOM   4979  O O   . PRO B 1 273 ? 7.585   5.878   14.766  1.00 128.27 ? 273 PRO B O   1 
ATOM   4980  C CB  . PRO B 1 273 ? 10.175  7.696   14.792  1.00 132.70 ? 273 PRO B CB  1 
ATOM   4981  C CG  . PRO B 1 273 ? 10.088  9.060   14.205  1.00 136.43 ? 273 PRO B CG  1 
ATOM   4982  C CD  . PRO B 1 273 ? 10.297  8.886   12.714  1.00 132.35 ? 273 PRO B CD  1 
ATOM   4983  N N   . HIS B 1 274 ? 7.216   7.508   13.248  1.00 129.29 ? 274 HIS B N   1 
ATOM   4984  C CA  . HIS B 1 274 ? 5.769   7.450   13.388  1.00 129.26 ? 274 HIS B CA  1 
ATOM   4985  C C   . HIS B 1 274 ? 5.198   6.131   12.893  1.00 127.72 ? 274 HIS B C   1 
ATOM   4986  O O   . HIS B 1 274 ? 4.084   5.766   13.279  1.00 126.82 ? 274 HIS B O   1 
ATOM   4987  C CB  . HIS B 1 274 ? 5.131   8.607   12.624  1.00 130.84 ? 274 HIS B CB  1 
ATOM   4988  C CG  . HIS B 1 274 ? 5.797   8.893   11.316  1.00 133.46 ? 274 HIS B CG  1 
ATOM   4989  N ND1 . HIS B 1 274 ? 6.826   9.800   11.188  1.00 138.51 ? 274 HIS B ND1 1 
ATOM   4990  C CD2 . HIS B 1 274 ? 5.598   8.375   10.081  1.00 132.62 ? 274 HIS B CD2 1 
ATOM   4991  C CE1 . HIS B 1 274 ? 7.227   9.836   9.930   1.00 137.64 ? 274 HIS B CE1 1 
ATOM   4992  N NE2 . HIS B 1 274 ? 6.497   8.980   9.237   1.00 133.68 ? 274 HIS B NE2 1 
ATOM   4993  N N   . ILE B 1 275 ? 5.934   5.407   12.046  1.00 120.10 ? 275 ILE B N   1 
ATOM   4994  C CA  . ILE B 1 275 ? 5.507   4.075   11.635  1.00 117.35 ? 275 ILE B CA  1 
ATOM   4995  C C   . ILE B 1 275 ? 5.576   3.088   12.790  1.00 115.25 ? 275 ILE B C   1 
ATOM   4996  O O   . ILE B 1 275 ? 4.941   2.030   12.736  1.00 110.68 ? 275 ILE B O   1 
ATOM   4997  C CB  . ILE B 1 275 ? 6.346   3.594   10.436  1.00 116.88 ? 275 ILE B CB  1 
ATOM   4998  C CG1 . ILE B 1 275 ? 7.709   3.078   10.898  1.00 110.83 ? 275 ILE B CG1 1 
ATOM   4999  C CG2 . ILE B 1 275 ? 6.535   4.719   9.428   1.00 121.99 ? 275 ILE B CG2 1 
ATOM   5000  C CD1 . ILE B 1 275 ? 8.395   2.192   9.884   1.00 104.81 ? 275 ILE B CD1 1 
ATOM   5001  N N   . LEU B 1 276 ? 6.348   3.397   13.828  1.00 119.40 ? 276 LEU B N   1 
ATOM   5002  C CA  . LEU B 1 276 ? 6.431   2.567   15.021  1.00 118.21 ? 276 LEU B CA  1 
ATOM   5003  C C   . LEU B 1 276 ? 5.406   3.026   16.047  1.00 121.29 ? 276 LEU B C   1 
ATOM   5004  O O   . LEU B 1 276 ? 5.189   4.227   16.229  1.00 124.62 ? 276 LEU B O   1 
ATOM   5005  C CB  . LEU B 1 276 ? 7.833   2.634   15.628  1.00 117.51 ? 276 LEU B CB  1 
ATOM   5006  C CG  . LEU B 1 276 ? 8.978   1.944   14.884  1.00 116.75 ? 276 LEU B CG  1 
ATOM   5007  C CD1 . LEU B 1 276 ? 10.110  1.621   15.846  1.00 113.43 ? 276 LEU B CD1 1 
ATOM   5008  C CD2 . LEU B 1 276 ? 8.491   0.682   14.189  1.00 118.95 ? 276 LEU B CD2 1 
ATOM   5009  N N   . ALA B 1 277 ? 4.769   2.060   16.707  1.00 116.84 ? 277 ALA B N   1 
ATOM   5010  C CA  . ALA B 1 277 ? 3.811   2.380   17.758  1.00 123.79 ? 277 ALA B CA  1 
ATOM   5011  C C   . ALA B 1 277 ? 4.507   3.078   18.922  1.00 128.26 ? 277 ALA B C   1 
ATOM   5012  O O   . ALA B 1 277 ? 5.501   2.579   19.458  1.00 121.50 ? 277 ALA B O   1 
ATOM   5013  C CB  . ALA B 1 277 ? 3.113   1.109   18.243  1.00 112.05 ? 277 ALA B CB  1 
ATOM   5014  N N   . SER B 1 278 ? 3.975   4.248   19.315  1.00 149.50 ? 278 SER B N   1 
ATOM   5015  C CA  . SER B 1 278 ? 4.503   5.031   20.428  1.00 151.86 ? 278 SER B CA  1 
ATOM   5016  C C   . SER B 1 278 ? 3.330   5.559   21.262  1.00 155.67 ? 278 SER B C   1 
ATOM   5017  O O   . SER B 1 278 ? 3.007   6.746   21.263  1.00 159.23 ? 278 SER B O   1 
ATOM   5018  C CB  . SER B 1 278 ? 5.397   6.174   19.937  1.00 152.09 ? 278 SER B CB  1 
ATOM   5019  O OG  . SER B 1 278 ? 4.911   6.723   18.722  1.00 151.98 ? 278 SER B OG  1 
ATOM   5020  N N   . GLY B 1 279 ? 2.672   4.658   21.986  1.00 145.13 ? 279 GLY B N   1 
ATOM   5021  C CA  . GLY B 1 279 ? 1.556   5.047   22.825  1.00 151.61 ? 279 GLY B CA  1 
ATOM   5022  C C   . GLY B 1 279 ? 2.000   5.833   24.041  1.00 167.25 ? 279 GLY B C   1 
ATOM   5023  O O   . GLY B 1 279 ? 1.625   6.999   24.202  1.00 173.60 ? 279 GLY B O   1 
ATOM   5024  N N   . ASP B 1 280 ? 2.806   5.201   24.896  1.00 199.27 ? 280 ASP B N   1 
ATOM   5025  C CA  . ASP B 1 280 ? 3.395   5.846   26.071  1.00 201.08 ? 280 ASP B CA  1 
ATOM   5026  C C   . ASP B 1 280 ? 2.323   6.514   26.929  1.00 202.47 ? 280 ASP B C   1 
ATOM   5027  O O   . ASP B 1 280 ? 2.399   7.698   27.263  1.00 204.14 ? 280 ASP B O   1 
ATOM   5028  C CB  . ASP B 1 280 ? 4.479   6.844   25.659  1.00 202.34 ? 280 ASP B CB  1 
ATOM   5029  C CG  . ASP B 1 280 ? 5.671   6.172   25.002  1.00 200.85 ? 280 ASP B CG  1 
ATOM   5030  O OD1 . ASP B 1 280 ? 5.522   5.684   23.862  1.00 199.36 ? 280 ASP B OD1 1 
ATOM   5031  O OD2 . ASP B 1 280 ? 6.754   6.131   25.624  1.00 201.51 ? 280 ASP B OD2 1 
ATOM   5032  N N   . GLY B 1 281 ? 1.312   5.732   27.289  1.00 147.95 ? 281 GLY B N   1 
ATOM   5033  C CA  . GLY B 1 281 ? 0.195   6.259   28.048  1.00 136.83 ? 281 GLY B CA  1 
ATOM   5034  C C   . GLY B 1 281 ? -0.912  5.229   28.136  1.00 126.43 ? 281 GLY B C   1 
ATOM   5035  O O   . GLY B 1 281 ? -0.686  4.040   27.909  1.00 121.01 ? 281 GLY B O   1 
ATOM   5036  N N   . THR B 1 282 ? -2.114  5.707   28.473  1.00 124.57 ? 282 THR B N   1 
ATOM   5037  C CA  . THR B 1 282 ? -3.293  4.851   28.590  1.00 120.55 ? 282 THR B CA  1 
ATOM   5038  C C   . THR B 1 282 ? -4.522  5.660   28.166  1.00 124.64 ? 282 THR B C   1 
ATOM   5039  O O   . THR B 1 282 ? -5.387  6.023   28.961  1.00 122.32 ? 282 THR B O   1 
ATOM   5040  C CB  . THR B 1 282 ? -3.461  4.289   30.004  1.00 114.25 ? 282 THR B CB  1 
ATOM   5041  O OG1 . THR B 1 282 ? -3.067  5.275   30.967  1.00 116.51 ? 282 THR B OG1 1 
ATOM   5042  C CG2 . THR B 1 282 ? -2.628  3.025   30.189  1.00 111.11 ? 282 THR B CG2 1 
ATOM   5043  N N   . ASN B 1 283 ? -4.603  5.942   26.868  1.00 143.10 ? 283 ASN B N   1 
ATOM   5044  C CA  . ASN B 1 283 ? -5.795  6.539   26.280  1.00 143.27 ? 283 ASN B CA  1 
ATOM   5045  C C   . ASN B 1 283 ? -6.470  5.491   25.412  1.00 141.73 ? 283 ASN B C   1 
ATOM   5046  O O   . ASN B 1 283 ? -6.673  5.711   24.213  1.00 142.26 ? 283 ASN B O   1 
ATOM   5047  C CB  . ASN B 1 283 ? -5.440  7.766   25.442  1.00 145.23 ? 283 ASN B CB  1 
ATOM   5048  C CG  . ASN B 1 283 ? -4.283  8.546   26.021  1.00 147.69 ? 283 ASN B CG  1 
ATOM   5049  O OD1 . ASN B 1 283 ? -4.102  8.597   27.237  1.00 147.17 ? 283 ASN B OD1 1 
ATOM   5050  N ND2 . ASN B 1 283 ? -3.482  9.149   25.150  1.00 148.18 ? 283 ASN B ND2 1 
ATOM   5051  N N   . ARG B 1 284 ? -6.812  4.352   26.016  1.00 122.02 ? 284 ARG B N   1 
ATOM   5052  C CA  . ARG B 1 284 ? -7.166  3.098   25.354  1.00 118.77 ? 284 ARG B CA  1 
ATOM   5053  C C   . ARG B 1 284 ? -5.961  2.468   24.667  1.00 116.23 ? 284 ARG B C   1 
ATOM   5054  O O   . ARG B 1 284 ? -6.080  1.361   24.127  1.00 112.65 ? 284 ARG B O   1 
ATOM   5055  C CB  . ARG B 1 284 ? -8.309  3.253   24.338  1.00 122.32 ? 284 ARG B CB  1 
ATOM   5056  C CG  . ARG B 1 284 ? -9.654  2.721   24.808  1.00 123.57 ? 284 ARG B CG  1 
ATOM   5057  C CD  . ARG B 1 284 ? -10.635 2.636   23.648  1.00 126.11 ? 284 ARG B CD  1 
ATOM   5058  N NE  . ARG B 1 284 ? -11.849 1.904   23.997  1.00 126.22 ? 284 ARG B NE  1 
ATOM   5059  C CZ  . ARG B 1 284 ? -12.200 0.744   23.452  1.00 125.54 ? 284 ARG B CZ  1 
ATOM   5060  N NH1 . ARG B 1 284 ? -11.430 0.190   22.525  1.00 125.47 ? 284 ARG B NH1 1 
ATOM   5061  N NH2 . ARG B 1 284 ? -13.323 0.145   23.825  1.00 123.72 ? 284 ARG B NH2 1 
ATOM   5062  N N   . LYS B 1 285 ? -4.796  3.134   24.674  1.00 116.97 ? 285 LYS B N   1 
ATOM   5063  C CA  . LYS B 1 285 ? -3.529  2.656   24.136  1.00 114.05 ? 285 LYS B CA  1 
ATOM   5064  C C   . LYS B 1 285 ? -2.652  2.146   25.266  1.00 112.36 ? 285 LYS B C   1 
ATOM   5065  O O   . LYS B 1 285 ? -2.517  2.831   26.290  1.00 115.36 ? 285 LYS B O   1 
ATOM   5066  C CB  . LYS B 1 285 ? -2.811  3.774   23.385  1.00 111.18 ? 285 LYS B CB  1 
ATOM   5067  N N   . PRO B 1 286 ? -2.059  0.963   25.140  1.00 107.42 ? 286 PRO B N   1 
ATOM   5068  C CA  . PRO B 1 286 ? -1.250  0.416   26.236  1.00 102.91 ? 286 PRO B CA  1 
ATOM   5069  C C   . PRO B 1 286 ? 0.029   1.214   26.456  1.00 104.92 ? 286 PRO B C   1 
ATOM   5070  O O   . PRO B 1 286 ? 0.369   2.132   25.708  1.00 110.00 ? 286 PRO B O   1 
ATOM   5071  C CB  . PRO B 1 286 ? -0.945  -1.013  25.774  1.00 99.62  ? 286 PRO B CB  1 
ATOM   5072  C CG  . PRO B 1 286 ? -1.991  -1.317  24.740  1.00 106.62 ? 286 PRO B CG  1 
ATOM   5073  C CD  . PRO B 1 286 ? -2.258  -0.014  24.057  1.00 108.81 ? 286 PRO B CD  1 
ATOM   5074  N N   . THR B 1 287 ? 0.747   0.839   27.514  1.00 102.12 ? 287 THR B N   1 
ATOM   5075  C CA  . THR B 1 287 ? 2.010   1.484   27.874  1.00 103.16 ? 287 THR B CA  1 
ATOM   5076  C C   . THR B 1 287 ? 3.113   0.954   26.966  1.00 102.37 ? 287 THR B C   1 
ATOM   5077  O O   . THR B 1 287 ? 3.648   -0.138  27.184  1.00 97.23  ? 287 THR B O   1 
ATOM   5078  C CB  . THR B 1 287 ? 2.341   1.241   29.343  1.00 91.64  ? 287 THR B CB  1 
ATOM   5079  O OG1 . THR B 1 287 ? 1.469   0.233   29.872  1.00 92.07  ? 287 THR B OG1 1 
ATOM   5080  C CG2 . THR B 1 287 ? 2.176   2.524   30.151  1.00 92.54  ? 287 THR B CG2 1 
ATOM   5081  N N   . ILE B 1 288 ? 3.454   1.731   25.939  1.00 110.23 ? 288 ILE B N   1 
ATOM   5082  C CA  . ILE B 1 288 ? 4.499   1.380   24.983  1.00 112.31 ? 288 ILE B CA  1 
ATOM   5083  C C   . ILE B 1 288 ? 5.804   2.031   25.416  1.00 120.10 ? 288 ILE B C   1 
ATOM   5084  O O   . ILE B 1 288 ? 5.844   3.237   25.690  1.00 129.50 ? 288 ILE B O   1 
ATOM   5085  C CB  . ILE B 1 288 ? 4.106   1.804   23.558  1.00 120.51 ? 288 ILE B CB  1 
ATOM   5086  C CG1 . ILE B 1 288 ? 3.005   0.882   23.027  1.00 110.28 ? 288 ILE B CG1 1 
ATOM   5087  C CG2 . ILE B 1 288 ? 5.318   1.795   22.634  1.00 122.06 ? 288 ILE B CG2 1 
ATOM   5088  C CD1 . ILE B 1 288 ? 2.153   1.490   21.947  1.00 117.78 ? 288 ILE B CD1 1 
ATOM   5089  N N   . ILE B 1 289 ? 6.872   1.235   25.482  1.00 115.13 ? 289 ILE B N   1 
ATOM   5090  C CA  . ILE B 1 289 ? 8.155   1.703   25.997  1.00 113.56 ? 289 ILE B CA  1 
ATOM   5091  C C   . ILE B 1 289 ? 9.190   1.757   24.878  1.00 111.75 ? 289 ILE B C   1 
ATOM   5092  O O   . ILE B 1 289 ? 10.307  1.248   25.027  1.00 108.92 ? 289 ILE B O   1 
ATOM   5093  C CB  . ILE B 1 289 ? 8.645   0.810   27.153  1.00 109.58 ? 289 ILE B CB  1 
ATOM   5094  C CG1 . ILE B 1 289 ? 7.460   0.286   27.967  1.00 107.14 ? 289 ILE B CG1 1 
ATOM   5095  C CG2 . ILE B 1 289 ? 9.592   1.583   28.062  1.00 105.96 ? 289 ILE B CG2 1 
ATOM   5096  C CD1 . ILE B 1 289 ? 6.748   1.355   28.769  1.00 103.90 ? 289 ILE B CD1 1 
ATOM   5097  N N   . GLY B 1 290 ? 8.828   2.368   23.750  1.00 119.33 ? 290 GLY B N   1 
ATOM   5098  C CA  . GLY B 1 290 ? 9.776   2.610   22.677  1.00 112.83 ? 290 GLY B CA  1 
ATOM   5099  C C   . GLY B 1 290 ? 10.180  1.399   21.856  1.00 115.22 ? 290 GLY B C   1 
ATOM   5100  O O   . GLY B 1 290 ? 10.241  0.278   22.370  1.00 115.77 ? 290 GLY B O   1 
ATOM   5101  N N   . ASP B 1 291 ? 10.463  1.629   20.571  1.00 102.93 ? 291 ASP B N   1 
ATOM   5102  C CA  . ASP B 1 291 ? 10.916  0.595   19.640  1.00 97.66  ? 291 ASP B CA  1 
ATOM   5103  C C   . ASP B 1 291 ? 9.928   -0.571  19.585  1.00 97.21  ? 291 ASP B C   1 
ATOM   5104  O O   . ASP B 1 291 ? 10.261  -1.723  19.870  1.00 94.62  ? 291 ASP B O   1 
ATOM   5105  C CB  . ASP B 1 291 ? 12.325  0.113   20.000  1.00 96.54  ? 291 ASP B CB  1 
ATOM   5106  C CG  . ASP B 1 291 ? 13.390  0.725   19.113  1.00 99.06  ? 291 ASP B CG  1 
ATOM   5107  O OD1 . ASP B 1 291 ? 13.108  1.766   18.480  1.00 100.40 ? 291 ASP B OD1 1 
ATOM   5108  O OD2 . ASP B 1 291 ? 14.507  0.169   19.048  1.00 97.08  ? 291 ASP B OD2 1 
ATOM   5109  N N   . VAL B 1 292 ? 8.692   -0.244  19.215  1.00 101.03 ? 292 VAL B N   1 
ATOM   5110  C CA  . VAL B 1 292 ? 7.611   -1.216  19.117  1.00 97.68  ? 292 VAL B CA  1 
ATOM   5111  C C   . VAL B 1 292 ? 6.919   -1.044  17.773  1.00 100.37 ? 292 VAL B C   1 
ATOM   5112  O O   . VAL B 1 292 ? 6.536   0.072   17.405  1.00 106.33 ? 292 VAL B O   1 
ATOM   5113  C CB  . VAL B 1 292 ? 6.590   -1.061  20.260  1.00 98.84  ? 292 VAL B CB  1 
ATOM   5114  C CG1 . VAL B 1 292 ? 5.523   -2.141  20.158  1.00 99.98  ? 292 VAL B CG1 1 
ATOM   5115  C CG2 . VAL B 1 292 ? 7.280   -1.113  21.611  1.00 103.82 ? 292 VAL B CG2 1 
ATOM   5116  N N   . TYR B 1 293 ? 6.756   -2.146  17.047  1.00 94.78  ? 293 TYR B N   1 
ATOM   5117  C CA  . TYR B 1 293 ? 5.940   -2.185  15.840  1.00 91.20  ? 293 TYR B CA  1 
ATOM   5118  C C   . TYR B 1 293 ? 4.663   -2.954  16.138  1.00 96.81  ? 293 TYR B C   1 
ATOM   5119  O O   . TYR B 1 293 ? 4.712   -4.143  16.470  1.00 103.59 ? 293 TYR B O   1 
ATOM   5120  C CB  . TYR B 1 293 ? 6.669   -2.832  14.663  1.00 91.33  ? 293 TYR B CB  1 
ATOM   5121  C CG  . TYR B 1 293 ? 5.726   -3.137  13.516  1.00 91.10  ? 293 TYR B CG  1 
ATOM   5122  C CD1 . TYR B 1 293 ? 5.242   -4.424  13.313  1.00 93.33  ? 293 TYR B CD1 1 
ATOM   5123  C CD2 . TYR B 1 293 ? 5.294   -2.134  12.658  1.00 94.13  ? 293 TYR B CD2 1 
ATOM   5124  C CE1 . TYR B 1 293 ? 4.369   -4.707  12.280  1.00 88.40  ? 293 TYR B CE1 1 
ATOM   5125  C CE2 . TYR B 1 293 ? 4.419   -2.409  11.618  1.00 91.38  ? 293 TYR B CE2 1 
ATOM   5126  C CZ  . TYR B 1 293 ? 3.961   -3.697  11.435  1.00 86.30  ? 293 TYR B CZ  1 
ATOM   5127  O OH  . TYR B 1 293 ? 3.094   -3.973  10.403  1.00 81.88  ? 293 TYR B OH  1 
ATOM   5128  N N   . ILE B 1 294 ? 3.529   -2.273  16.023  1.00 95.35  ? 294 ILE B N   1 
ATOM   5129  C CA  . ILE B 1 294 ? 2.218   -2.855  16.274  1.00 96.87  ? 294 ILE B CA  1 
ATOM   5130  C C   . ILE B 1 294 ? 1.451   -2.868  14.959  1.00 87.67  ? 294 ILE B C   1 
ATOM   5131  O O   . ILE B 1 294 ? 1.287   -1.823  14.317  1.00 85.56  ? 294 ILE B O   1 
ATOM   5132  C CB  . ILE B 1 294 ? 1.453   -2.079  17.357  1.00 97.75  ? 294 ILE B CB  1 
ATOM   5133  C CG1 . ILE B 1 294 ? 2.035   -2.379  18.743  1.00 100.99 ? 294 ILE B CG1 1 
ATOM   5134  C CG2 . ILE B 1 294 ? -0.029  -2.401  17.298  1.00 98.18  ? 294 ILE B CG2 1 
ATOM   5135  C CD1 . ILE B 1 294 ? 1.327   -1.665  19.876  1.00 102.63 ? 294 ILE B CD1 1 
ATOM   5136  N N   . HIS B 1 295 ? 0.990   -4.046  14.554  1.00 90.59  ? 295 HIS B N   1 
ATOM   5137  C CA  . HIS B 1 295 ? 0.169   -4.139  13.358  1.00 87.78  ? 295 HIS B CA  1 
ATOM   5138  C C   . HIS B 1 295 ? -1.211  -3.551  13.644  1.00 94.74  ? 295 HIS B C   1 
ATOM   5139  O O   . HIS B 1 295 ? -1.716  -3.667  14.763  1.00 93.93  ? 295 HIS B O   1 
ATOM   5140  C CB  . HIS B 1 295 ? 0.037   -5.595  12.905  1.00 86.53  ? 295 HIS B CB  1 
ATOM   5141  C CG  . HIS B 1 295 ? -0.498  -5.750  11.515  1.00 85.25  ? 295 HIS B CG  1 
ATOM   5142  N ND1 . HIS B 1 295 ? -1.844  -5.711  11.227  1.00 89.60  ? 295 HIS B ND1 1 
ATOM   5143  C CD2 . HIS B 1 295 ? 0.132   -5.956  10.335  1.00 91.01  ? 295 HIS B CD2 1 
ATOM   5144  C CE1 . HIS B 1 295 ? -2.021  -5.871  9.928   1.00 95.00  ? 295 HIS B CE1 1 
ATOM   5145  N NE2 . HIS B 1 295 ? -0.837  -6.028  9.364   1.00 95.05  ? 295 HIS B NE2 1 
ATOM   5146  N N   . PRO B 1 296 ? -1.837  -2.894  12.665  1.00 90.50  ? 296 PRO B N   1 
ATOM   5147  C CA  . PRO B 1 296 ? -3.178  -2.330  12.904  1.00 91.94  ? 296 PRO B CA  1 
ATOM   5148  C C   . PRO B 1 296 ? -4.259  -3.373  13.143  1.00 89.89  ? 296 PRO B C   1 
ATOM   5149  O O   . PRO B 1 296 ? -5.314  -3.026  13.688  1.00 86.57  ? 296 PRO B O   1 
ATOM   5150  C CB  . PRO B 1 296 ? -3.455  -1.528  11.623  1.00 99.15  ? 296 PRO B CB  1 
ATOM   5151  C CG  . PRO B 1 296 ? -2.527  -2.109  10.595  1.00 95.59  ? 296 PRO B CG  1 
ATOM   5152  C CD  . PRO B 1 296 ? -1.297  -2.491  11.355  1.00 88.13  ? 296 PRO B CD  1 
ATOM   5153  N N   . SER B 1 297 ? -4.037  -4.630  12.768  1.00 90.00  ? 297 SER B N   1 
ATOM   5154  C CA  . SER B 1 297 ? -5.038  -5.678  12.906  1.00 93.54  ? 297 SER B CA  1 
ATOM   5155  C C   . SER B 1 297 ? -5.018  -6.351  14.273  1.00 95.67  ? 297 SER B C   1 
ATOM   5156  O O   . SER B 1 297 ? -5.724  -7.345  14.468  1.00 97.25  ? 297 SER B O   1 
ATOM   5157  C CB  . SER B 1 297 ? -4.852  -6.730  11.810  1.00 95.67  ? 297 SER B CB  1 
ATOM   5158  O OG  . SER B 1 297 ? -5.880  -7.702  11.856  1.00 101.45 ? 297 SER B OG  1 
ATOM   5159  N N   . VAL B 1 298 ? -4.226  -5.847  15.215  1.00 99.87  ? 298 VAL B N   1 
ATOM   5160  C CA  . VAL B 1 298 ? -4.125  -6.450  16.537  1.00 109.73 ? 298 VAL B CA  1 
ATOM   5161  C C   . VAL B 1 298 ? -5.242  -5.929  17.433  1.00 116.67 ? 298 VAL B C   1 
ATOM   5162  O O   . VAL B 1 298 ? -5.865  -4.900  17.166  1.00 112.66 ? 298 VAL B O   1 
ATOM   5163  C CB  . VAL B 1 298 ? -2.747  -6.189  17.177  1.00 113.91 ? 298 VAL B CB  1 
ATOM   5164  C CG1 . VAL B 1 298 ? -1.639  -6.452  16.178  1.00 103.94 ? 298 VAL B CG1 1 
ATOM   5165  C CG2 . VAL B 1 298 ? -2.675  -4.769  17.702  1.00 119.56 ? 298 VAL B CG2 1 
ATOM   5166  N N   . LYS B 1 299 ? -5.492  -6.664  18.515  1.00 153.30 ? 299 LYS B N   1 
ATOM   5167  C CA  . LYS B 1 299 ? -6.427  -6.274  19.562  1.00 154.67 ? 299 LYS B CA  1 
ATOM   5168  C C   . LYS B 1 299 ? -5.647  -6.094  20.857  1.00 155.49 ? 299 LYS B C   1 
ATOM   5169  O O   . LYS B 1 299 ? -4.936  -7.007  21.286  1.00 155.04 ? 299 LYS B O   1 
ATOM   5170  C CB  . LYS B 1 299 ? -7.525  -7.325  19.745  1.00 155.08 ? 299 LYS B CB  1 
ATOM   5171  C CG  . LYS B 1 299 ? -8.465  -7.049  20.909  1.00 161.28 ? 299 LYS B CG  1 
ATOM   5172  C CD  . LYS B 1 299 ? -9.549  -8.112  21.019  1.00 161.83 ? 299 LYS B CD  1 
ATOM   5173  C CE  . LYS B 1 299 ? -10.553 -8.020  19.883  1.00 167.67 ? 299 LYS B CE  1 
ATOM   5174  N NZ  . LYS B 1 299 ? -11.333 -6.756  19.951  1.00 170.93 ? 299 LYS B NZ  1 
ATOM   5175  N N   . LEU B 1 300 ? -5.778  -4.925  21.480  1.00 131.78 ? 300 LEU B N   1 
ATOM   5176  C CA  . LEU B 1 300 ? -4.966  -4.577  22.634  1.00 124.79 ? 300 LEU B CA  1 
ATOM   5177  C C   . LEU B 1 300 ? -5.830  -4.212  23.832  1.00 125.59 ? 300 LEU B C   1 
ATOM   5178  O O   . LEU B 1 300 ? -7.020  -3.921  23.711  1.00 129.09 ? 300 LEU B O   1 
ATOM   5179  C CB  . LEU B 1 300 ? -4.017  -3.412  22.316  1.00 125.00 ? 300 LEU B CB  1 
ATOM   5180  C CG  . LEU B 1 300 ? -3.038  -3.640  21.165  1.00 129.02 ? 300 LEU B CG  1 
ATOM   5181  C CD1 . LEU B 1 300 ? -2.214  -2.390  20.921  1.00 131.79 ? 300 LEU B CD1 1 
ATOM   5182  C CD2 . LEU B 1 300 ? -2.140  -4.831  21.464  1.00 127.00 ? 300 LEU B CD2 1 
ATOM   5183  N N   . HIS B 1 301 ? -5.198  -4.242  25.002  1.00 109.65 ? 301 HIS B N   1 
ATOM   5184  C CA  . HIS B 1 301 ? -5.812  -3.819  26.254  1.00 100.99 ? 301 HIS B CA  1 
ATOM   5185  C C   . HIS B 1 301 ? -4.886  -2.781  26.879  1.00 99.68  ? 301 HIS B C   1 
ATOM   5186  O O   . HIS B 1 301 ? -3.660  -2.990  26.921  1.00 101.47 ? 301 HIS B O   1 
ATOM   5187  C CB  . HIS B 1 301 ? -6.024  -5.008  27.194  1.00 94.64  ? 301 HIS B CB  1 
ATOM   5188  C CG  . HIS B 1 301 ? -6.984  -4.741  28.313  1.00 94.73  ? 301 HIS B CG  1 
ATOM   5189  N ND1 . HIS B 1 301 ? -6.639  -4.019  29.435  1.00 92.70  ? 301 HIS B ND1 1 
ATOM   5190  C CD2 . HIS B 1 301 ? -8.270  -5.127  28.496  1.00 94.47  ? 301 HIS B CD2 1 
ATOM   5191  C CE1 . HIS B 1 301 ? -7.675  -3.957  30.252  1.00 91.92  ? 301 HIS B CE1 1 
ATOM   5192  N NE2 . HIS B 1 301 ? -8.677  -4.622  29.707  1.00 92.06  ? 301 HIS B NE2 1 
ATOM   5193  N N   . PRO B 1 302 ? -5.415  -1.654  27.367  1.00 98.87  ? 302 PRO B N   1 
ATOM   5194  C CA  . PRO B 1 302 ? -4.535  -0.575  27.853  1.00 96.50  ? 302 PRO B CA  1 
ATOM   5195  C C   . PRO B 1 302 ? -3.711  -0.952  29.074  1.00 95.49  ? 302 PRO B C   1 
ATOM   5196  O O   . PRO B 1 302 ? -2.766  -0.224  29.403  1.00 97.59  ? 302 PRO B O   1 
ATOM   5197  C CB  . PRO B 1 302 ? -5.517  0.558   28.180  1.00 102.94 ? 302 PRO B CB  1 
ATOM   5198  C CG  . PRO B 1 302 ? -6.774  0.216   27.438  1.00 108.11 ? 302 PRO B CG  1 
ATOM   5199  C CD  . PRO B 1 302 ? -6.838  -1.277  27.423  1.00 101.77 ? 302 PRO B CD  1 
ATOM   5200  N N   . THR B 1 303 ? -4.029  -2.059  29.745  1.00 92.27  ? 303 THR B N   1 
ATOM   5201  C CA  . THR B 1 303 ? -3.335  -2.462  30.961  1.00 90.34  ? 303 THR B CA  1 
ATOM   5202  C C   . THR B 1 303 ? -2.064  -3.259  30.698  1.00 88.19  ? 303 THR B C   1 
ATOM   5203  O O   . THR B 1 303 ? -1.324  -3.542  31.647  1.00 86.14  ? 303 THR B O   1 
ATOM   5204  C CB  . THR B 1 303 ? -4.270  -3.286  31.855  1.00 87.40  ? 303 THR B CB  1 
ATOM   5205  O OG1 . THR B 1 303 ? -4.749  -4.426  31.128  1.00 86.99  ? 303 THR B OG1 1 
ATOM   5206  C CG2 . THR B 1 303 ? -5.448  -2.442  32.313  1.00 87.60  ? 303 THR B CG2 1 
ATOM   5207  N N   . ALA B 1 304 ? -1.787  -3.609  29.446  1.00 87.75  ? 304 ALA B N   1 
ATOM   5208  C CA  . ALA B 1 304 ? -0.597  -4.368  29.102  1.00 83.16  ? 304 ALA B CA  1 
ATOM   5209  C C   . ALA B 1 304 ? 0.581   -3.424  28.921  1.00 82.56  ? 304 ALA B C   1 
ATOM   5210  O O   . ALA B 1 304 ? 0.434   -2.327  28.376  1.00 87.21  ? 304 ALA B O   1 
ATOM   5211  C CB  . ALA B 1 304 ? -0.825  -5.167  27.820  1.00 82.88  ? 304 ALA B CB  1 
ATOM   5212  N N   . LYS B 1 305 ? 1.754   -3.859  29.369  1.00 79.09  ? 305 LYS B N   1 
ATOM   5213  C CA  . LYS B 1 305 ? 2.987   -3.099  29.197  1.00 79.13  ? 305 LYS B CA  1 
ATOM   5214  C C   . LYS B 1 305 ? 3.797   -3.769  28.098  1.00 92.37  ? 305 LYS B C   1 
ATOM   5215  O O   . LYS B 1 305 ? 4.360   -4.850  28.301  1.00 86.55  ? 305 LYS B O   1 
ATOM   5216  C CB  . LYS B 1 305 ? 3.789   -3.020  30.493  1.00 77.14  ? 305 LYS B CB  1 
ATOM   5217  C CG  . LYS B 1 305 ? 5.051   -2.185  30.353  1.00 81.86  ? 305 LYS B CG  1 
ATOM   5218  C CD  . LYS B 1 305 ? 5.838   -2.074  31.649  1.00 81.50  ? 305 LYS B CD  1 
ATOM   5219  C CE  . LYS B 1 305 ? 5.264   -1.032  32.585  1.00 86.61  ? 305 LYS B CE  1 
ATOM   5220  N NZ  . LYS B 1 305 ? 6.138   -0.848  33.779  1.00 76.33  ? 305 LYS B NZ  1 
ATOM   5221  N N   . ILE B 1 306 ? 3.854   -3.126  26.940  1.00 86.32  ? 306 ILE B N   1 
ATOM   5222  C CA  . ILE B 1 306 ? 4.579   -3.639  25.785  1.00 92.32  ? 306 ILE B CA  1 
ATOM   5223  C C   . ILE B 1 306 ? 5.946   -2.962  25.797  1.00 105.53 ? 306 ILE B C   1 
ATOM   5224  O O   . ILE B 1 306 ? 6.095   -1.821  25.353  1.00 106.49 ? 306 ILE B O   1 
ATOM   5225  C CB  . ILE B 1 306 ? 3.816   -3.383  24.484  1.00 89.70  ? 306 ILE B CB  1 
ATOM   5226  C CG1 . ILE B 1 306 ? 2.315   -3.597  24.705  1.00 85.81  ? 306 ILE B CG1 1 
ATOM   5227  C CG2 . ILE B 1 306 ? 4.297   -4.320  23.398  1.00 92.85  ? 306 ILE B CG2 1 
ATOM   5228  C CD1 . ILE B 1 306 ? 1.937   -5.021  25.058  1.00 83.30  ? 306 ILE B CD1 1 
ATOM   5229  N N   . GLY B 1 307 ? 6.945   -3.665  26.322  1.00 143.91 ? 307 GLY B N   1 
ATOM   5230  C CA  . GLY B 1 307 ? 8.260   -3.105  26.524  1.00 144.36 ? 307 GLY B CA  1 
ATOM   5231  C C   . GLY B 1 307 ? 9.064   -2.928  25.254  1.00 143.57 ? 307 GLY B C   1 
ATOM   5232  O O   . GLY B 1 307 ? 8.523   -2.801  24.151  1.00 142.79 ? 307 GLY B O   1 
ATOM   5233  N N   . PRO B 1 308 ? 10.386  -2.917  25.393  1.00 114.20 ? 308 PRO B N   1 
ATOM   5234  C CA  . PRO B 1 308 ? 11.254  -2.653  24.243  1.00 112.30 ? 308 PRO B CA  1 
ATOM   5235  C C   . PRO B 1 308 ? 11.470  -3.882  23.375  1.00 107.13 ? 308 PRO B C   1 
ATOM   5236  O O   . PRO B 1 308 ? 11.390  -5.023  23.835  1.00 104.94 ? 308 PRO B O   1 
ATOM   5237  C CB  . PRO B 1 308 ? 12.567  -2.210  24.899  1.00 113.93 ? 308 PRO B CB  1 
ATOM   5238  C CG  . PRO B 1 308 ? 12.585  -2.955  26.198  1.00 111.52 ? 308 PRO B CG  1 
ATOM   5239  C CD  . PRO B 1 308 ? 11.148  -3.039  26.650  1.00 110.60 ? 308 PRO B CD  1 
ATOM   5240  N N   . ASN B 1 309 ? 11.742  -3.619  22.095  1.00 98.63  ? 309 ASN B N   1 
ATOM   5241  C CA  . ASN B 1 309 ? 12.148  -4.636  21.124  1.00 95.01  ? 309 ASN B CA  1 
ATOM   5242  C C   . ASN B 1 309 ? 11.094  -5.739  20.989  1.00 92.23  ? 309 ASN B C   1 
ATOM   5243  O O   . ASN B 1 309 ? 11.337  -6.913  21.272  1.00 90.65  ? 309 ASN B O   1 
ATOM   5244  C CB  . ASN B 1 309 ? 13.522  -5.213  21.501  1.00 94.31  ? 309 ASN B CB  1 
ATOM   5245  C CG  . ASN B 1 309 ? 14.067  -6.184  20.464  1.00 89.23  ? 309 ASN B CG  1 
ATOM   5246  O OD1 . ASN B 1 309 ? 13.629  -6.199  19.313  1.00 87.29  ? 309 ASN B OD1 1 
ATOM   5247  N ND2 . ASN B 1 309 ? 15.030  -7.001  20.875  1.00 84.21  ? 309 ASN B ND2 1 
ATOM   5248  N N   . VAL B 1 310 ? 9.902   -5.336  20.555  1.00 92.09  ? 310 VAL B N   1 
ATOM   5249  C CA  . VAL B 1 310 ? 8.803   -6.261  20.311  1.00 92.80  ? 310 VAL B CA  1 
ATOM   5250  C C   . VAL B 1 310 ? 8.156   -5.906  18.978  1.00 99.94  ? 310 VAL B C   1 
ATOM   5251  O O   . VAL B 1 310 ? 7.851   -4.735  18.720  1.00 102.53 ? 310 VAL B O   1 
ATOM   5252  C CB  . VAL B 1 310 ? 7.769   -6.231  21.453  1.00 91.95  ? 310 VAL B CB  1 
ATOM   5253  C CG1 . VAL B 1 310 ? 7.474   -4.803  21.861  1.00 99.01  ? 310 VAL B CG1 1 
ATOM   5254  C CG2 . VAL B 1 310 ? 6.498   -6.967  21.049  1.00 95.93  ? 310 VAL B CG2 1 
ATOM   5255  N N   . SER B 1 311 ? 7.960   -6.914  18.129  1.00 106.12 ? 311 SER B N   1 
ATOM   5256  C CA  . SER B 1 311 ? 7.405   -6.745  16.786  1.00 104.93 ? 311 SER B CA  1 
ATOM   5257  C C   . SER B 1 311 ? 6.167   -7.631  16.680  1.00 118.43 ? 311 SER B C   1 
ATOM   5258  O O   . SER B 1 311 ? 6.279   -8.852  16.532  1.00 109.49 ? 311 SER B O   1 
ATOM   5259  C CB  . SER B 1 311 ? 8.437   -7.090  15.718  1.00 87.97  ? 311 SER B CB  1 
ATOM   5260  O OG  . SER B 1 311 ? 9.663   -6.424  15.968  1.00 84.54  ? 311 SER B OG  1 
ATOM   5261  N N   . ILE B 1 312 ? 4.994   -7.016  16.753  1.00 165.78 ? 312 ILE B N   1 
ATOM   5262  C CA  . ILE B 1 312 ? 3.726   -7.738  16.768  1.00 165.30 ? 312 ILE B CA  1 
ATOM   5263  C C   . ILE B 1 312 ? 3.168   -7.828  15.354  1.00 164.67 ? 312 ILE B C   1 
ATOM   5264  O O   . ILE B 1 312 ? 3.196   -6.853  14.592  1.00 165.08 ? 312 ILE B O   1 
ATOM   5265  C CB  . ILE B 1 312 ? 2.729   -7.058  17.724  1.00 166.23 ? 312 ILE B CB  1 
ATOM   5266  C CG1 . ILE B 1 312 ? 3.468   -6.459  18.923  1.00 167.27 ? 312 ILE B CG1 1 
ATOM   5267  C CG2 . ILE B 1 312 ? 1.706   -8.056  18.210  1.00 165.84 ? 312 ILE B CG2 1 
ATOM   5268  C CD1 . ILE B 1 312 ? 2.554   -5.805  19.942  1.00 168.34 ? 312 ILE B CD1 1 
ATOM   5269  N N   . SER B 1 313 ? 2.658   -9.008  15.000  1.00 122.70 ? 313 SER B N   1 
ATOM   5270  C CA  . SER B 1 313 ? 2.150   -9.276  13.663  1.00 106.82 ? 313 SER B CA  1 
ATOM   5271  C C   . SER B 1 313 ? 0.641   -9.032  13.612  1.00 102.12 ? 313 SER B C   1 
ATOM   5272  O O   . SER B 1 313 ? 0.033   -8.545  14.568  1.00 104.38 ? 313 SER B O   1 
ATOM   5273  C CB  . SER B 1 313 ? 2.500   -10.702 13.241  1.00 91.13  ? 313 SER B CB  1 
ATOM   5274  O OG  . SER B 1 313 ? 3.901   -10.892 13.196  1.00 90.94  ? 313 SER B OG  1 
ATOM   5275  N N   . ALA B 1 314 ? 0.022   -9.372  12.485  1.00 95.46  ? 314 ALA B N   1 
ATOM   5276  C CA  . ALA B 1 314 ? -1.388  -9.092  12.264  1.00 91.13  ? 314 ALA B CA  1 
ATOM   5277  C C   . ALA B 1 314 ? -2.276  -10.142 12.922  1.00 93.03  ? 314 ALA B C   1 
ATOM   5278  O O   . ALA B 1 314 ? -1.869  -11.287 13.138  1.00 90.90  ? 314 ALA B O   1 
ATOM   5279  C CB  . ALA B 1 314 ? -1.692  -9.039  10.767  1.00 87.17  ? 314 ALA B CB  1 
ATOM   5280  N N   . ASN B 1 315 ? -3.505  -9.729  13.243  1.00 91.94  ? 315 ASN B N   1 
ATOM   5281  C CA  . ASN B 1 315 ? -4.566  -10.632 13.695  1.00 90.71  ? 315 ASN B CA  1 
ATOM   5282  C C   . ASN B 1 315 ? -4.138  -11.452 14.912  1.00 95.91  ? 315 ASN B C   1 
ATOM   5283  O O   . ASN B 1 315 ? -4.288  -12.674 14.950  1.00 95.19  ? 315 ASN B O   1 
ATOM   5284  C CB  . ASN B 1 315 ? -5.019  -11.546 12.554  1.00 87.52  ? 315 ASN B CB  1 
ATOM   5285  C CG  . ASN B 1 315 ? -5.783  -10.801 11.483  1.00 85.67  ? 315 ASN B CG  1 
ATOM   5286  O OD1 . ASN B 1 315 ? -5.204  -10.342 10.497  1.00 85.85  ? 315 ASN B OD1 1 
ATOM   5287  N ND2 . ASN B 1 315 ? -7.092  -10.683 11.664  1.00 89.78  ? 315 ASN B ND2 1 
ATOM   5288  N N   . VAL B 1 316 ? -3.603  -10.767 15.917  1.00 106.61 ? 316 VAL B N   1 
ATOM   5289  C CA  . VAL B 1 316 ? -3.180  -11.390 17.164  1.00 104.16 ? 316 VAL B CA  1 
ATOM   5290  C C   . VAL B 1 316 ? -3.955  -10.755 18.312  1.00 103.45 ? 316 VAL B C   1 
ATOM   5291  O O   . VAL B 1 316 ? -4.202  -9.544  18.313  1.00 104.26 ? 316 VAL B O   1 
ATOM   5292  C CB  . VAL B 1 316 ? -1.655  -11.257 17.364  1.00 103.27 ? 316 VAL B CB  1 
ATOM   5293  C CG1 . VAL B 1 316 ? -1.244  -9.804  17.347  1.00 107.59 ? 316 VAL B CG1 1 
ATOM   5294  C CG2 . VAL B 1 316 ? -1.212  -11.928 18.651  1.00 104.61 ? 316 VAL B CG2 1 
ATOM   5295  N N   . ARG B 1 317 ? -4.344  -11.578 19.286  1.00 97.04  ? 317 ARG B N   1 
ATOM   5296  C CA  . ARG B 1 317 ? -5.171  -11.143 20.409  1.00 102.74 ? 317 ARG B CA  1 
ATOM   5297  C C   . ARG B 1 317 ? -4.316  -11.002 21.666  1.00 98.25  ? 317 ARG B C   1 
ATOM   5298  O O   . ARG B 1 317 ? -3.835  -11.997 22.216  1.00 93.30  ? 317 ARG B O   1 
ATOM   5299  C CB  . ARG B 1 317 ? -6.324  -12.119 20.638  1.00 106.24 ? 317 ARG B CB  1 
ATOM   5300  C CG  . ARG B 1 317 ? -7.344  -12.137 19.506  1.00 104.37 ? 317 ARG B CG  1 
ATOM   5301  C CD  . ARG B 1 317 ? -8.687  -12.692 19.962  1.00 108.05 ? 317 ARG B CD  1 
ATOM   5302  N NE  . ARG B 1 317 ? -8.622  -14.090 20.384  1.00 110.03 ? 317 ARG B NE  1 
ATOM   5303  C CZ  . ARG B 1 317 ? -9.012  -15.114 19.630  1.00 109.54 ? 317 ARG B CZ  1 
ATOM   5304  N NH1 . ARG B 1 317 ? -9.498  -14.896 18.416  1.00 106.37 ? 317 ARG B NH1 1 
ATOM   5305  N NH2 . ARG B 1 317 ? -8.925  -16.355 20.091  1.00 113.02 ? 317 ARG B NH2 1 
ATOM   5306  N N   . VAL B 1 318 ? -4.127  -9.762  22.111  1.00 104.10 ? 318 VAL B N   1 
ATOM   5307  C CA  . VAL B 1 318 ? -3.347  -9.449  23.304  1.00 99.03  ? 318 VAL B CA  1 
ATOM   5308  C C   . VAL B 1 318 ? -4.293  -9.269  24.483  1.00 97.75  ? 318 VAL B C   1 
ATOM   5309  O O   . VAL B 1 318 ? -5.236  -8.470  24.418  1.00 103.70 ? 318 VAL B O   1 
ATOM   5310  C CB  . VAL B 1 318 ? -2.492  -8.189  23.093  1.00 101.41 ? 318 VAL B CB  1 
ATOM   5311  C CG1 . VAL B 1 318 ? -1.927  -7.703  24.414  1.00 94.24  ? 318 VAL B CG1 1 
ATOM   5312  C CG2 . VAL B 1 318 ? -1.375  -8.473  22.104  1.00 104.31 ? 318 VAL B CG2 1 
ATOM   5313  N N   . GLY B 1 319 ? -4.046  -10.015 25.561  1.00 92.42  ? 319 GLY B N   1 
ATOM   5314  C CA  . GLY B 1 319 ? -4.855  -9.911  26.752  1.00 91.26  ? 319 GLY B CA  1 
ATOM   5315  C C   . GLY B 1 319 ? -4.474  -8.712  27.594  1.00 87.79  ? 319 GLY B C   1 
ATOM   5316  O O   . GLY B 1 319 ? -3.602  -7.905  27.241  1.00 89.97  ? 319 GLY B O   1 
ATOM   5317  N N   . PRO B 1 320 ? -5.135  -8.580  28.740  1.00 86.96  ? 320 PRO B N   1 
ATOM   5318  C CA  . PRO B 1 320 ? -4.870  -7.441  29.619  1.00 85.10  ? 320 PRO B CA  1 
ATOM   5319  C C   . PRO B 1 320 ? -3.722  -7.704  30.576  1.00 87.64  ? 320 PRO B C   1 
ATOM   5320  O O   . PRO B 1 320 ? -3.486  -8.827  31.030  1.00 88.96  ? 320 PRO B O   1 
ATOM   5321  C CB  . PRO B 1 320 ? -6.195  -7.295  30.378  1.00 88.93  ? 320 PRO B CB  1 
ATOM   5322  C CG  . PRO B 1 320 ? -6.663  -8.693  30.520  1.00 94.90  ? 320 PRO B CG  1 
ATOM   5323  C CD  . PRO B 1 320 ? -6.230  -9.420  29.256  1.00 95.61  ? 320 PRO B CD  1 
ATOM   5324  N N   . GLY B 1 321 ? -3.008  -6.626  30.890  1.00 84.46  ? 321 GLY B N   1 
ATOM   5325  C CA  . GLY B 1 321 ? -1.924  -6.701  31.853  1.00 81.84  ? 321 GLY B CA  1 
ATOM   5326  C C   . GLY B 1 321 ? -0.812  -7.655  31.481  1.00 74.03  ? 321 GLY B C   1 
ATOM   5327  O O   . GLY B 1 321 ? -0.218  -8.276  32.367  1.00 80.59  ? 321 GLY B O   1 
ATOM   5328  N N   . VAL B 1 322 ? -0.512  -7.795  30.193  1.00 75.96  ? 322 VAL B N   1 
ATOM   5329  C CA  . VAL B 1 322 ? 0.546   -8.691  29.747  1.00 82.45  ? 322 VAL B CA  1 
ATOM   5330  C C   . VAL B 1 322 ? 1.809   -7.876  29.512  1.00 82.20  ? 322 VAL B C   1 
ATOM   5331  O O   . VAL B 1 322 ? 1.759   -6.681  29.202  1.00 78.63  ? 322 VAL B O   1 
ATOM   5332  C CB  . VAL B 1 322 ? 0.142   -9.474  28.478  1.00 80.20  ? 322 VAL B CB  1 
ATOM   5333  C CG1 . VAL B 1 322 ? -1.191  -10.184 28.689  1.00 86.43  ? 322 VAL B CG1 1 
ATOM   5334  C CG2 . VAL B 1 322 ? 0.094   -8.564  27.270  1.00 78.72  ? 322 VAL B CG2 1 
ATOM   5335  N N   . ARG B 1 323 ? 2.956   -8.533  29.669  1.00 76.13  ? 323 ARG B N   1 
ATOM   5336  C CA  . ARG B 1 323 ? 4.263   -7.895  29.582  1.00 72.78  ? 323 ARG B CA  1 
ATOM   5337  C C   . ARG B 1 323 ? 5.030   -8.528  28.429  1.00 72.73  ? 323 ARG B C   1 
ATOM   5338  O O   . ARG B 1 323 ? 5.208   -9.750  28.396  1.00 70.94  ? 323 ARG B O   1 
ATOM   5339  C CB  . ARG B 1 323 ? 5.028   -8.045  30.900  1.00 74.22  ? 323 ARG B CB  1 
ATOM   5340  C CG  . ARG B 1 323 ? 6.332   -7.270  30.949  1.00 77.69  ? 323 ARG B CG  1 
ATOM   5341  C CD  . ARG B 1 323 ? 6.109   -5.804  31.273  1.00 78.67  ? 323 ARG B CD  1 
ATOM   5342  N NE  . ARG B 1 323 ? 7.377   -5.094  31.410  1.00 86.05  ? 323 ARG B NE  1 
ATOM   5343  C CZ  . ARG B 1 323 ? 7.922   -4.371  30.439  1.00 89.03  ? 323 ARG B CZ  1 
ATOM   5344  N NH1 . ARG B 1 323 ? 7.292   -4.260  29.280  1.00 90.52  ? 323 ARG B NH1 1 
ATOM   5345  N NH2 . ARG B 1 323 ? 9.081   -3.753  30.627  1.00 91.93  ? 323 ARG B NH2 1 
ATOM   5346  N N   . LEU B 1 324 ? 5.486   -7.700  27.488  1.00 77.19  ? 324 LEU B N   1 
ATOM   5347  C CA  . LEU B 1 324 ? 6.143   -8.178  26.272  1.00 77.79  ? 324 LEU B CA  1 
ATOM   5348  C C   . LEU B 1 324 ? 7.430   -7.392  26.052  1.00 85.73  ? 324 LEU B C   1 
ATOM   5349  O O   . LEU B 1 324 ? 7.381   -6.211  25.697  1.00 93.73  ? 324 LEU B O   1 
ATOM   5350  C CB  . LEU B 1 324 ? 5.214   -8.034  25.066  1.00 79.68  ? 324 LEU B CB  1 
ATOM   5351  C CG  . LEU B 1 324 ? 3.812   -8.640  25.202  1.00 74.89  ? 324 LEU B CG  1 
ATOM   5352  C CD1 . LEU B 1 324 ? 2.961   -8.353  23.972  1.00 73.86  ? 324 LEU B CD1 1 
ATOM   5353  C CD2 . LEU B 1 324 ? 3.883   -10.135 25.473  1.00 77.09  ? 324 LEU B CD2 1 
ATOM   5354  N N   . ILE B 1 325 ? 8.580   -8.038  26.248  1.00 86.02  ? 325 ILE B N   1 
ATOM   5355  C CA  . ILE B 1 325 ? 9.869   -7.413  25.966  1.00 87.76  ? 325 ILE B CA  1 
ATOM   5356  C C   . ILE B 1 325 ? 10.752  -8.399  25.213  1.00 82.02  ? 325 ILE B C   1 
ATOM   5357  O O   . ILE B 1 325 ? 10.701  -9.610  25.455  1.00 79.44  ? 325 ILE B O   1 
ATOM   5358  C CB  . ILE B 1 325 ? 10.586  -6.923  27.247  1.00 88.72  ? 325 ILE B CB  1 
ATOM   5359  C CG1 . ILE B 1 325 ? 11.058  -8.096  28.103  1.00 79.46  ? 325 ILE B CG1 1 
ATOM   5360  C CG2 . ILE B 1 325 ? 9.690   -6.018  28.063  1.00 91.52  ? 325 ILE B CG2 1 
ATOM   5361  C CD1 . ILE B 1 325 ? 11.711  -7.676  29.398  1.00 82.04  ? 325 ILE B CD1 1 
ATOM   5362  N N   . SER B 1 326 ? 11.548  -7.869  24.282  1.00 85.99  ? 326 SER B N   1 
ATOM   5363  C CA  . SER B 1 326 ? 12.613  -8.614  23.605  1.00 84.32  ? 326 SER B CA  1 
ATOM   5364  C C   . SER B 1 326 ? 12.090  -9.878  22.927  1.00 86.90  ? 326 SER B C   1 
ATOM   5365  O O   . SER B 1 326 ? 12.711  -10.937 23.001  1.00 83.28  ? 326 SER B O   1 
ATOM   5366  C CB  . SER B 1 326 ? 13.743  -8.961  24.578  1.00 78.27  ? 326 SER B CB  1 
ATOM   5367  O OG  . SER B 1 326 ? 14.192  -7.822  25.290  1.00 76.66  ? 326 SER B OG  1 
ATOM   5368  N N   . CYS B 1 327 ? 10.960  -9.766  22.231  1.00 98.73  ? 327 CYS B N   1 
ATOM   5369  C CA  . CYS B 1 327 ? 10.334  -10.935 21.628  1.00 97.57  ? 327 CYS B CA  1 
ATOM   5370  C C   . CYS B 1 327 ? 9.616   -10.532 20.348  1.00 97.01  ? 327 CYS B C   1 
ATOM   5371  O O   . CYS B 1 327 ? 9.336   -9.355  20.115  1.00 99.70  ? 327 CYS B O   1 
ATOM   5372  C CB  . CYS B 1 327 ? 9.370   -11.604 22.609  1.00 98.01  ? 327 CYS B CB  1 
ATOM   5373  S SG  . CYS B 1 327 ? 8.093   -10.495 23.235  1.00 98.74  ? 327 CYS B SG  1 
ATOM   5374  N N   . ILE B 1 328 ? 9.324   -11.530 19.513  1.00 80.35  ? 328 ILE B N   1 
ATOM   5375  C CA  . ILE B 1 328 ? 8.556   -11.339 18.288  1.00 77.07  ? 328 ILE B CA  1 
ATOM   5376  C C   . ILE B 1 328 ? 7.440   -12.374 18.231  1.00 75.85  ? 328 ILE B C   1 
ATOM   5377  O O   . ILE B 1 328 ? 7.654   -13.553 18.533  1.00 73.69  ? 328 ILE B O   1 
ATOM   5378  C CB  . ILE B 1 328 ? 9.443   -11.425 17.028  1.00 71.11  ? 328 ILE B CB  1 
ATOM   5379  C CG1 . ILE B 1 328 ? 10.296  -12.689 17.052  1.00 67.20  ? 328 ILE B CG1 1 
ATOM   5380  C CG2 . ILE B 1 328 ? 10.314  -10.187 16.895  1.00 78.79  ? 328 ILE B CG2 1 
ATOM   5381  C CD1 . ILE B 1 328 ? 11.160  -12.848 15.835  1.00 70.56  ? 328 ILE B CD1 1 
ATOM   5382  N N   . ILE B 1 329 ? 6.244   -11.923 17.860  1.00 76.35  ? 329 ILE B N   1 
ATOM   5383  C CA  . ILE B 1 329 ? 5.036   -12.739 17.875  1.00 71.40  ? 329 ILE B CA  1 
ATOM   5384  C C   . ILE B 1 329 ? 4.486   -12.839 16.458  1.00 78.76  ? 329 ILE B C   1 
ATOM   5385  O O   . ILE B 1 329 ? 4.361   -11.826 15.761  1.00 88.73  ? 329 ILE B O   1 
ATOM   5386  C CB  . ILE B 1 329 ? 3.982   -12.162 18.836  1.00 69.75  ? 329 ILE B CB  1 
ATOM   5387  C CG1 . ILE B 1 329 ? 4.547   -12.093 20.257  1.00 68.08  ? 329 ILE B CG1 1 
ATOM   5388  C CG2 . ILE B 1 329 ? 2.710   -12.987 18.793  1.00 71.17  ? 329 ILE B CG2 1 
ATOM   5389  C CD1 . ILE B 1 329 ? 3.656   -11.364 21.235  1.00 77.38  ? 329 ILE B CD1 1 
ATOM   5390  N N   . LEU B 1 330 ? 4.163   -14.060 16.036  1.00 76.36  ? 330 LEU B N   1 
ATOM   5391  C CA  . LEU B 1 330 ? 3.652   -14.326 14.699  1.00 75.68  ? 330 LEU B CA  1 
ATOM   5392  C C   . LEU B 1 330 ? 2.130   -14.170 14.686  1.00 74.89  ? 330 LEU B C   1 
ATOM   5393  O O   . LEU B 1 330 ? 1.525   -13.707 15.655  1.00 80.54  ? 330 LEU B O   1 
ATOM   5394  C CB  . LEU B 1 330 ? 4.112   -15.710 14.242  1.00 77.01  ? 330 LEU B CB  1 
ATOM   5395  C CG  . LEU B 1 330 ? 5.633   -15.856 14.130  1.00 73.57  ? 330 LEU B CG  1 
ATOM   5396  C CD1 . LEU B 1 330 ? 6.020   -17.240 13.637  1.00 74.66  ? 330 LEU B CD1 1 
ATOM   5397  C CD2 . LEU B 1 330 ? 6.221   -14.778 13.229  1.00 71.44  ? 330 LEU B CD2 1 
ATOM   5398  N N   . ASP B 1 331 ? 1.493   -14.552 13.581  1.00 73.12  ? 331 ASP B N   1 
ATOM   5399  C CA  . ASP B 1 331 ? 0.069   -14.303 13.401  1.00 77.08  ? 331 ASP B CA  1 
ATOM   5400  C C   . ASP B 1 331 ? -0.783  -15.271 14.215  1.00 78.94  ? 331 ASP B C   1 
ATOM   5401  O O   . ASP B 1 331 ? -0.370  -16.393 14.525  1.00 80.04  ? 331 ASP B O   1 
ATOM   5402  C CB  . ASP B 1 331 ? -0.324  -14.413 11.924  1.00 79.02  ? 331 ASP B CB  1 
ATOM   5403  C CG  . ASP B 1 331 ? 0.313   -13.339 11.060  1.00 78.21  ? 331 ASP B CG  1 
ATOM   5404  O OD1 . ASP B 1 331 ? 1.080   -13.690 10.142  1.00 74.26  ? 331 ASP B OD1 1 
ATOM   5405  O OD2 . ASP B 1 331 ? 0.059   -12.142 11.304  1.00 84.12  ? 331 ASP B OD2 1 
ATOM   5406  N N   . ASP B 1 332 ? -1.989  -14.809 14.563  1.00 84.06  ? 332 ASP B N   1 
ATOM   5407  C CA  . ASP B 1 332 ? -3.057  -15.634 15.132  1.00 88.24  ? 332 ASP B CA  1 
ATOM   5408  C C   . ASP B 1 332 ? -2.715  -16.195 16.512  1.00 88.05  ? 332 ASP B C   1 
ATOM   5409  O O   . ASP B 1 332 ? -3.260  -17.223 16.918  1.00 88.85  ? 332 ASP B O   1 
ATOM   5410  C CB  . ASP B 1 332 ? -3.436  -16.775 14.182  1.00 90.73  ? 332 ASP B CB  1 
ATOM   5411  C CG  . ASP B 1 332 ? -4.936  -16.897 13.978  1.00 96.17  ? 332 ASP B CG  1 
ATOM   5412  O OD1 . ASP B 1 332 ? -5.697  -16.592 14.921  1.00 101.07 ? 332 ASP B OD1 1 
ATOM   5413  O OD2 . ASP B 1 332 ? -5.354  -17.298 12.870  1.00 100.31 ? 332 ASP B OD2 1 
ATOM   5414  N N   . VAL B 1 333 ? -1.855  -15.522 17.261  1.00 86.73  ? 333 VAL B N   1 
ATOM   5415  C CA  . VAL B 1 333 ? -1.490  -15.973 18.599  1.00 86.02  ? 333 VAL B CA  1 
ATOM   5416  C C   . VAL B 1 333 ? -2.521  -15.454 19.592  1.00 87.31  ? 333 VAL B C   1 
ATOM   5417  O O   . VAL B 1 333 ? -3.067  -14.357 19.435  1.00 88.43  ? 333 VAL B O   1 
ATOM   5418  C CB  . VAL B 1 333 ? -0.062  -15.513 18.962  1.00 84.07  ? 333 VAL B CB  1 
ATOM   5419  C CG1 . VAL B 1 333 ? 0.336   -16.017 20.341  1.00 86.00  ? 333 VAL B CG1 1 
ATOM   5420  C CG2 . VAL B 1 333 ? 0.923   -15.988 17.913  1.00 77.30  ? 333 VAL B CG2 1 
ATOM   5421  N N   . GLU B 1 334 ? -2.805  -16.249 20.621  1.00 87.29  ? 334 GLU B N   1 
ATOM   5422  C CA  . GLU B 1 334 ? -3.774  -15.883 21.650  1.00 91.57  ? 334 GLU B CA  1 
ATOM   5423  C C   . GLU B 1 334 ? -3.056  -15.786 22.992  1.00 89.12  ? 334 GLU B C   1 
ATOM   5424  O O   . GLU B 1 334 ? -2.561  -16.792 23.514  1.00 88.31  ? 334 GLU B O   1 
ATOM   5425  C CB  . GLU B 1 334 ? -4.919  -16.892 21.701  1.00 100.29 ? 334 GLU B CB  1 
ATOM   5426  C CG  . GLU B 1 334 ? -5.993  -16.560 22.717  1.00 103.10 ? 334 GLU B CG  1 
ATOM   5427  C CD  . GLU B 1 334 ? -7.127  -17.564 22.705  1.00 108.52 ? 334 GLU B CD  1 
ATOM   5428  O OE1 . GLU B 1 334 ? -7.166  -18.409 21.784  1.00 112.90 ? 334 GLU B OE1 1 
ATOM   5429  O OE2 . GLU B 1 334 ? -7.977  -17.514 23.618  1.00 108.83 ? 334 GLU B OE2 1 
ATOM   5430  N N   . ILE B 1 335 ? -3.002  -14.575 23.540  1.00 89.78  ? 335 ILE B N   1 
ATOM   5431  C CA  . ILE B 1 335 ? -2.359  -14.290 24.820  1.00 93.58  ? 335 ILE B CA  1 
ATOM   5432  C C   . ILE B 1 335 ? -3.448  -14.090 25.867  1.00 95.52  ? 335 ILE B C   1 
ATOM   5433  O O   . ILE B 1 335 ? -4.312  -13.219 25.715  1.00 95.30  ? 335 ILE B O   1 
ATOM   5434  C CB  . ILE B 1 335 ? -1.443  -13.059 24.725  1.00 97.59  ? 335 ILE B CB  1 
ATOM   5435  C CG1 . ILE B 1 335 ? -0.414  -13.244 23.605  1.00 98.63  ? 335 ILE B CG1 1 
ATOM   5436  C CG2 . ILE B 1 335 ? -0.755  -12.796 26.051  1.00 96.14  ? 335 ILE B CG2 1 
ATOM   5437  C CD1 . ILE B 1 335 ? 0.605   -14.327 23.884  1.00 97.73  ? 335 ILE B CD1 1 
ATOM   5438  N N   . LYS B 1 336 ? -3.409  -14.895 26.928  1.00 97.33  ? 336 LYS B N   1 
ATOM   5439  C CA  . LYS B 1 336 ? -4.448  -14.895 27.949  1.00 99.80  ? 336 LYS B CA  1 
ATOM   5440  C C   . LYS B 1 336 ? -4.077  -13.962 29.104  1.00 106.57 ? 336 LYS B C   1 
ATOM   5441  O O   . LYS B 1 336 ? -3.135  -13.169 29.022  1.00 106.12 ? 336 LYS B O   1 
ATOM   5442  C CB  . LYS B 1 336 ? -4.702  -16.314 28.455  1.00 98.23  ? 336 LYS B CB  1 
ATOM   5443  C CG  . LYS B 1 336 ? -5.532  -17.192 27.534  1.00 91.91  ? 336 LYS B CG  1 
ATOM   5444  C CD  . LYS B 1 336 ? -5.909  -18.488 28.238  1.00 85.46  ? 336 LYS B CD  1 
ATOM   5445  C CE  . LYS B 1 336 ? -6.834  -19.344 27.392  1.00 80.03  ? 336 LYS B CE  1 
ATOM   5446  N NZ  . LYS B 1 336 ? -7.221  -20.585 28.117  1.00 82.58  ? 336 LYS B NZ  1 
ATOM   5447  N N   . GLU B 1 337 ? -4.839  -14.054 30.195  1.00 124.57 ? 337 GLU B N   1 
ATOM   5448  C CA  . GLU B 1 337 ? -4.708  -13.132 31.318  1.00 125.76 ? 337 GLU B CA  1 
ATOM   5449  C C   . GLU B 1 337 ? -3.308  -13.186 31.922  1.00 126.39 ? 337 GLU B C   1 
ATOM   5450  O O   . GLU B 1 337 ? -2.819  -14.258 32.294  1.00 126.79 ? 337 GLU B O   1 
ATOM   5451  C CB  . GLU B 1 337 ? -5.750  -13.467 32.389  1.00 127.25 ? 337 GLU B CB  1 
ATOM   5452  C CG  . GLU B 1 337 ? -7.154  -13.733 31.856  1.00 126.65 ? 337 GLU B CG  1 
ATOM   5453  C CD  . GLU B 1 337 ? -7.934  -12.457 31.595  1.00 135.80 ? 337 GLU B CD  1 
ATOM   5454  O OE1 . GLU B 1 337 ? -7.412  -11.367 31.907  1.00 138.41 ? 337 GLU B OE1 1 
ATOM   5455  O OE2 . GLU B 1 337 ? -9.069  -12.542 31.081  1.00 138.75 ? 337 GLU B OE2 1 
ATOM   5456  N N   . ASN B 1 338 ? -2.676  -12.019 32.031  1.00 107.44 ? 338 ASN B N   1 
ATOM   5457  C CA  . ASN B 1 338 ? -1.420  -11.843 32.759  1.00 106.73 ? 338 ASN B CA  1 
ATOM   5458  C C   . ASN B 1 338 ? -0.339  -12.810 32.275  1.00 110.02 ? 338 ASN B C   1 
ATOM   5459  O O   . ASN B 1 338 ? 0.204   -13.612 33.037  1.00 119.27 ? 338 ASN B O   1 
ATOM   5460  C CB  . ASN B 1 338 ? -1.645  -11.991 34.266  1.00 105.78 ? 338 ASN B CB  1 
ATOM   5461  C CG  . ASN B 1 338 ? -2.629  -10.983 34.806  1.00 100.10 ? 338 ASN B CG  1 
ATOM   5462  O OD1 . ASN B 1 338 ? -2.651  -9.833  34.372  1.00 97.64  ? 338 ASN B OD1 1 
ATOM   5463  N ND2 . ASN B 1 338 ? -3.440  -11.402 35.768  1.00 103.54 ? 338 ASN B ND2 1 
ATOM   5464  N N   . ALA B 1 339 ? -0.029  -12.721 30.986  1.00 111.76 ? 339 ALA B N   1 
ATOM   5465  C CA  . ALA B 1 339 ? 1.033   -13.521 30.395  1.00 110.90 ? 339 ALA B CA  1 
ATOM   5466  C C   . ALA B 1 339 ? 2.302   -12.689 30.257  1.00 111.09 ? 339 ALA B C   1 
ATOM   5467  O O   . ALA B 1 339 ? 2.254   -11.461 30.149  1.00 111.48 ? 339 ALA B O   1 
ATOM   5468  C CB  . ALA B 1 339 ? 0.615   -14.072 29.032  1.00 109.94 ? 339 ALA B CB  1 
ATOM   5469  N N   . VAL B 1 340 ? 3.444   -13.374 30.256  1.00 88.04  ? 340 VAL B N   1 
ATOM   5470  C CA  . VAL B 1 340 ? 4.753   -12.732 30.194  1.00 77.64  ? 340 VAL B CA  1 
ATOM   5471  C C   . VAL B 1 340 ? 5.591   -13.435 29.136  1.00 74.42  ? 340 VAL B C   1 
ATOM   5472  O O   . VAL B 1 340 ? 5.669   -14.669 29.119  1.00 73.91  ? 340 VAL B O   1 
ATOM   5473  C CB  . VAL B 1 340 ? 5.466   -12.763 31.560  1.00 76.71  ? 340 VAL B CB  1 
ATOM   5474  C CG1 . VAL B 1 340 ? 6.791   -12.036 31.482  1.00 77.40  ? 340 VAL B CG1 1 
ATOM   5475  C CG2 . VAL B 1 340 ? 4.582   -12.142 32.633  1.00 82.98  ? 340 VAL B CG2 1 
ATOM   5476  N N   . VAL B 1 341 ? 6.206   -12.655 28.249  1.00 71.57  ? 341 VAL B N   1 
ATOM   5477  C CA  . VAL B 1 341 ? 7.018   -13.191 27.163  1.00 65.50  ? 341 VAL B CA  1 
ATOM   5478  C C   . VAL B 1 341 ? 8.338   -12.432 27.133  1.00 68.30  ? 341 VAL B C   1 
ATOM   5479  O O   . VAL B 1 341 ? 8.357   -11.222 26.874  1.00 71.17  ? 341 VAL B O   1 
ATOM   5480  C CB  . VAL B 1 341 ? 6.305   -13.095 25.805  1.00 67.45  ? 341 VAL B CB  1 
ATOM   5481  C CG1 . VAL B 1 341 ? 7.214   -13.600 24.706  1.00 68.33  ? 341 VAL B CG1 1 
ATOM   5482  C CG2 . VAL B 1 341 ? 5.012   -13.892 25.832  1.00 68.30  ? 341 VAL B CG2 1 
ATOM   5483  N N   . ILE B 1 342 ? 9.437   -13.138 27.395  1.00 62.80  ? 342 ILE B N   1 
ATOM   5484  C CA  . ILE B 1 342 ? 10.769  -12.545 27.447  1.00 64.06  ? 342 ILE B CA  1 
ATOM   5485  C C   . ILE B 1 342 ? 11.695  -13.351 26.548  1.00 66.18  ? 342 ILE B C   1 
ATOM   5486  O O   . ILE B 1 342 ? 11.764  -14.578 26.671  1.00 73.14  ? 342 ILE B O   1 
ATOM   5487  C CB  . ILE B 1 342 ? 11.339  -12.518 28.878  1.00 66.19  ? 342 ILE B CB  1 
ATOM   5488  C CG1 . ILE B 1 342 ? 10.257  -12.191 29.912  1.00 70.02  ? 342 ILE B CG1 1 
ATOM   5489  C CG2 . ILE B 1 342 ? 12.487  -11.522 28.958  1.00 69.59  ? 342 ILE B CG2 1 
ATOM   5490  C CD1 . ILE B 1 342 ? 9.714   -10.789 29.835  1.00 71.28  ? 342 ILE B CD1 1 
ATOM   5491  N N   . ASN B 1 343 ? 12.402  -12.666 25.649  1.00 67.28  ? 343 ASN B N   1 
ATOM   5492  C CA  . ASN B 1 343 ? 13.418  -13.291 24.797  1.00 65.71  ? 343 ASN B CA  1 
ATOM   5493  C C   . ASN B 1 343 ? 12.874  -14.544 24.117  1.00 60.41  ? 343 ASN B C   1 
ATOM   5494  O O   . ASN B 1 343 ? 13.453  -15.629 24.197  1.00 62.82  ? 343 ASN B O   1 
ATOM   5495  C CB  . ASN B 1 343 ? 14.677  -13.619 25.602  1.00 68.17  ? 343 ASN B CB  1 
ATOM   5496  C CG  . ASN B 1 343 ? 15.380  -12.381 26.120  1.00 66.64  ? 343 ASN B CG  1 
ATOM   5497  O OD1 . ASN B 1 343 ? 15.521  -11.391 25.406  1.00 70.86  ? 343 ASN B OD1 1 
ATOM   5498  N ND2 . ASN B 1 343 ? 15.821  -12.430 27.373  1.00 62.82  ? 343 ASN B ND2 1 
ATOM   5499  N N   . SER B 1 344 ? 11.751  -14.383 23.426  1.00 73.63  ? 344 SER B N   1 
ATOM   5500  C CA  . SER B 1 344 ? 11.029  -15.522 22.883  1.00 61.23  ? 344 SER B CA  1 
ATOM   5501  C C   . SER B 1 344 ? 10.593  -15.229 21.457  1.00 60.32  ? 344 SER B C   1 
ATOM   5502  O O   . SER B 1 344 ? 10.602  -14.086 20.999  1.00 76.09  ? 344 SER B O   1 
ATOM   5503  C CB  . SER B 1 344 ? 9.806   -15.865 23.743  1.00 58.01  ? 344 SER B CB  1 
ATOM   5504  O OG  . SER B 1 344 ? 10.132  -15.840 25.120  1.00 63.02  ? 344 SER B OG  1 
ATOM   5505  N N   . ILE B 1 345 ? 10.207  -16.290 20.754  1.00 57.80  ? 345 ILE B N   1 
ATOM   5506  C CA  . ILE B 1 345 ? 9.629   -16.184 19.419  1.00 63.95  ? 345 ILE B CA  1 
ATOM   5507  C C   . ILE B 1 345 ? 8.420   -17.111 19.372  1.00 60.14  ? 345 ILE B C   1 
ATOM   5508  O O   . ILE B 1 345 ? 8.575   -18.336 19.293  1.00 67.64  ? 345 ILE B O   1 
ATOM   5509  C CB  . ILE B 1 345 ? 10.628  -16.539 18.309  1.00 59.30  ? 345 ILE B CB  1 
ATOM   5510  C CG1 . ILE B 1 345 ? 11.864  -15.639 18.378  1.00 63.72  ? 345 ILE B CG1 1 
ATOM   5511  C CG2 . ILE B 1 345 ? 9.965   -16.431 16.949  1.00 58.03  ? 345 ILE B CG2 1 
ATOM   5512  C CD1 . ILE B 1 345 ? 12.857  -15.883 17.270  1.00 71.03  ? 345 ILE B CD1 1 
ATOM   5513  N N   . ILE B 1 346 ? 7.223   -16.536 19.413  1.00 67.29  ? 346 ILE B N   1 
ATOM   5514  C CA  . ILE B 1 346 ? 5.992   -17.313 19.455  1.00 62.01  ? 346 ILE B CA  1 
ATOM   5515  C C   . ILE B 1 346 ? 5.533   -17.606 18.032  1.00 65.70  ? 346 ILE B C   1 
ATOM   5516  O O   . ILE B 1 346 ? 5.428   -16.699 17.203  1.00 66.00  ? 346 ILE B O   1 
ATOM   5517  C CB  . ILE B 1 346 ? 4.903   -16.578 20.250  1.00 64.48  ? 346 ILE B CB  1 
ATOM   5518  C CG1 . ILE B 1 346 ? 5.433   -16.163 21.626  1.00 62.04  ? 346 ILE B CG1 1 
ATOM   5519  C CG2 . ILE B 1 346 ? 3.684   -17.458 20.394  1.00 69.32  ? 346 ILE B CG2 1 
ATOM   5520  C CD1 . ILE B 1 346 ? 5.890   -17.331 22.474  1.00 63.70  ? 346 ILE B CD1 1 
ATOM   5521  N N   . GLY B 1 347 ? 5.245   -18.873 17.751  1.00 67.82  ? 347 GLY B N   1 
ATOM   5522  C CA  . GLY B 1 347 ? 4.879   -19.305 16.412  1.00 72.90  ? 347 GLY B CA  1 
ATOM   5523  C C   . GLY B 1 347 ? 3.475   -18.915 15.991  1.00 75.76  ? 347 GLY B C   1 
ATOM   5524  O O   . GLY B 1 347 ? 2.855   -18.056 16.620  1.00 74.11  ? 347 GLY B O   1 
ATOM   5525  N N   . TRP B 1 348 ? 2.970   -19.518 14.916  1.00 79.04  ? 348 TRP B N   1 
ATOM   5526  C CA  . TRP B 1 348 ? 1.661   -19.173 14.380  1.00 79.17  ? 348 TRP B CA  1 
ATOM   5527  C C   . TRP B 1 348 ? 0.562   -19.884 15.157  1.00 79.14  ? 348 TRP B C   1 
ATOM   5528  O O   . TRP B 1 348 ? 0.728   -21.030 15.581  1.00 79.15  ? 348 TRP B O   1 
ATOM   5529  C CB  . TRP B 1 348 ? 1.579   -19.555 12.902  1.00 81.75  ? 348 TRP B CB  1 
ATOM   5530  C CG  . TRP B 1 348 ? 2.835   -19.277 12.158  1.00 82.23  ? 348 TRP B CG  1 
ATOM   5531  C CD1 . TRP B 1 348 ? 3.940   -20.070 12.099  1.00 80.19  ? 348 TRP B CD1 1 
ATOM   5532  C CD2 . TRP B 1 348 ? 3.120   -18.128 11.357  1.00 79.06  ? 348 TRP B CD2 1 
ATOM   5533  N NE1 . TRP B 1 348 ? 4.904   -19.483 11.322  1.00 78.36  ? 348 TRP B NE1 1 
ATOM   5534  C CE2 . TRP B 1 348 ? 4.424   -18.291 10.849  1.00 80.77  ? 348 TRP B CE2 1 
ATOM   5535  C CE3 . TRP B 1 348 ? 2.402   -16.978 11.019  1.00 77.82  ? 348 TRP B CE3 1 
ATOM   5536  C CZ2 . TRP B 1 348 ? 5.026   -17.345 10.026  1.00 83.36  ? 348 TRP B CZ2 1 
ATOM   5537  C CZ3 . TRP B 1 348 ? 3.001   -16.043 10.201  1.00 79.07  ? 348 TRP B CZ3 1 
ATOM   5538  C CH2 . TRP B 1 348 ? 4.299   -16.230 9.713   1.00 80.15  ? 348 TRP B CH2 1 
ATOM   5539  N N   . LYS B 1 349 ? -0.569  -19.199 15.335  1.00 80.04  ? 349 LYS B N   1 
ATOM   5540  C CA  . LYS B 1 349 ? -1.767  -19.766 15.970  1.00 82.42  ? 349 LYS B CA  1 
ATOM   5541  C C   . LYS B 1 349 ? -1.479  -20.335 17.362  1.00 81.43  ? 349 LYS B C   1 
ATOM   5542  O O   . LYS B 1 349 ? -2.241  -21.164 17.875  1.00 84.00  ? 349 LYS B O   1 
ATOM   5543  C CB  . LYS B 1 349 ? -2.417  -20.842 15.085  1.00 81.04  ? 349 LYS B CB  1 
ATOM   5544  C CG  . LYS B 1 349 ? -3.192  -20.297 13.885  1.00 83.11  ? 349 LYS B CG  1 
ATOM   5545  C CD  . LYS B 1 349 ? -2.265  -19.866 12.747  1.00 88.96  ? 349 LYS B CD  1 
ATOM   5546  C CE  . LYS B 1 349 ? -3.047  -19.386 11.529  1.00 96.89  ? 349 LYS B CE  1 
ATOM   5547  N NZ  . LYS B 1 349 ? -2.150  -18.993 10.402  1.00 90.89  ? 349 LYS B NZ  1 
ATOM   5548  N N   . SER B 1 350 ? -0.393  -19.895 17.990  1.00 76.35  ? 350 SER B N   1 
ATOM   5549  C CA  . SER B 1 350 ? -0.031  -20.406 19.301  1.00 87.28  ? 350 SER B CA  1 
ATOM   5550  C C   . SER B 1 350 ? -0.960  -19.846 20.371  1.00 85.69  ? 350 SER B C   1 
ATOM   5551  O O   . SER B 1 350 ? -1.530  -18.761 20.227  1.00 87.17  ? 350 SER B O   1 
ATOM   5552  C CB  . SER B 1 350 ? 1.419   -20.054 19.621  1.00 74.57  ? 350 SER B CB  1 
ATOM   5553  O OG  . SER B 1 350 ? 2.280   -20.483 18.583  1.00 79.79  ? 350 SER B OG  1 
ATOM   5554  N N   . SER B 1 351 ? -1.106  -20.600 21.457  1.00 101.66 ? 351 SER B N   1 
ATOM   5555  C CA  . SER B 1 351 ? -1.999  -20.233 22.548  1.00 102.89 ? 351 SER B CA  1 
ATOM   5556  C C   . SER B 1 351 ? -1.215  -20.224 23.849  1.00 103.86 ? 351 SER B C   1 
ATOM   5557  O O   . SER B 1 351 ? -0.681  -21.257 24.265  1.00 104.42 ? 351 SER B O   1 
ATOM   5558  C CB  . SER B 1 351 ? -3.182  -21.200 22.642  1.00 107.24 ? 351 SER B CB  1 
ATOM   5559  O OG  . SER B 1 351 ? -4.096  -20.786 23.643  1.00 106.53 ? 351 SER B OG  1 
ATOM   5560  N N   . ILE B 1 352 ? -1.141  -19.059 24.482  1.00 91.86  ? 352 ILE B N   1 
ATOM   5561  C CA  . ILE B 1 352 ? -0.427  -18.872 25.739  1.00 90.09  ? 352 ILE B CA  1 
ATOM   5562  C C   . ILE B 1 352 ? -1.475  -18.748 26.837  1.00 88.36  ? 352 ILE B C   1 
ATOM   5563  O O   . ILE B 1 352 ? -2.251  -17.786 26.858  1.00 88.29  ? 352 ILE B O   1 
ATOM   5564  C CB  . ILE B 1 352 ? 0.491   -17.643 25.694  1.00 90.37  ? 352 ILE B CB  1 
ATOM   5565  C CG1 . ILE B 1 352 ? 1.563   -17.816 24.615  1.00 82.10  ? 352 ILE B CG1 1 
ATOM   5566  C CG2 . ILE B 1 352 ? 1.146   -17.414 27.040  1.00 92.02  ? 352 ILE B CG2 1 
ATOM   5567  C CD1 . ILE B 1 352 ? 2.397   -19.061 24.781  1.00 76.58  ? 352 ILE B CD1 1 
ATOM   5568  N N   . GLY B 1 353 ? -1.503  -19.716 27.749  1.00 85.07  ? 353 GLY B N   1 
ATOM   5569  C CA  . GLY B 1 353 ? -2.508  -19.732 28.792  1.00 89.31  ? 353 GLY B CA  1 
ATOM   5570  C C   . GLY B 1 353 ? -2.367  -18.573 29.762  1.00 92.17  ? 353 GLY B C   1 
ATOM   5571  O O   . GLY B 1 353 ? -1.399  -17.809 29.745  1.00 93.85  ? 353 GLY B O   1 
ATOM   5572  N N   . ARG B 1 354 ? -3.364  -18.440 30.634  1.00 94.79  ? 354 ARG B N   1 
ATOM   5573  C CA  . ARG B 1 354 ? -3.385  -17.337 31.583  1.00 99.92  ? 354 ARG B CA  1 
ATOM   5574  C C   . ARG B 1 354 ? -2.391  -17.588 32.708  1.00 105.93 ? 354 ARG B C   1 
ATOM   5575  O O   . ARG B 1 354 ? -2.249  -18.713 33.194  1.00 107.72 ? 354 ARG B O   1 
ATOM   5576  C CB  . ARG B 1 354 ? -4.796  -17.139 32.141  1.00 100.95 ? 354 ARG B CB  1 
ATOM   5577  C CG  . ARG B 1 354 ? -5.429  -18.389 32.727  1.00 96.97  ? 354 ARG B CG  1 
ATOM   5578  C CD  . ARG B 1 354 ? -6.883  -18.158 33.121  1.00 98.80  ? 354 ARG B CD  1 
ATOM   5579  N NE  . ARG B 1 354 ? -7.697  -17.707 31.993  1.00 93.11  ? 354 ARG B NE  1 
ATOM   5580  C CZ  . ARG B 1 354 ? -8.365  -18.519 31.177  1.00 87.98  ? 354 ARG B CZ  1 
ATOM   5581  N NH1 . ARG B 1 354 ? -8.318  -19.832 31.358  1.00 84.34  ? 354 ARG B NH1 1 
ATOM   5582  N NH2 . ARG B 1 354 ? -9.081  -18.019 30.178  1.00 85.85  ? 354 ARG B NH2 1 
ATOM   5583  N N   . TRP B 1 355 ? -1.703  -16.520 33.118  1.00 136.90 ? 355 TRP B N   1 
ATOM   5584  C CA  . TRP B 1 355 ? -0.636  -16.585 34.119  1.00 138.71 ? 355 TRP B CA  1 
ATOM   5585  C C   . TRP B 1 355 ? 0.477   -17.552 33.713  1.00 138.22 ? 355 TRP B C   1 
ATOM   5586  O O   . TRP B 1 355 ? 1.202   -18.071 34.563  1.00 139.80 ? 355 TRP B O   1 
ATOM   5587  C CB  . TRP B 1 355 ? -1.188  -16.950 35.501  1.00 140.49 ? 355 TRP B CB  1 
ATOM   5588  C CG  . TRP B 1 355 ? -1.934  -15.829 36.165  1.00 141.37 ? 355 TRP B CG  1 
ATOM   5589  C CD1 . TRP B 1 355 ? -1.412  -14.649 36.610  1.00 141.96 ? 355 TRP B CD1 1 
ATOM   5590  C CD2 . TRP B 1 355 ? -3.335  -15.785 36.467  1.00 141.97 ? 355 TRP B CD2 1 
ATOM   5591  N NE1 . TRP B 1 355 ? -2.398  -13.873 37.166  1.00 142.62 ? 355 TRP B NE1 1 
ATOM   5592  C CE2 . TRP B 1 355 ? -3.588  -14.546 37.091  1.00 142.51 ? 355 TRP B CE2 1 
ATOM   5593  C CE3 . TRP B 1 355 ? -4.399  -16.671 36.271  1.00 142.43 ? 355 TRP B CE3 1 
ATOM   5594  C CZ2 . TRP B 1 355 ? -4.860  -14.172 37.520  1.00 142.97 ? 355 TRP B CZ2 1 
ATOM   5595  C CZ3 . TRP B 1 355 ? -5.662  -16.296 36.697  1.00 142.54 ? 355 TRP B CZ3 1 
ATOM   5596  C CH2 . TRP B 1 355 ? -5.881  -15.058 37.313  1.00 142.88 ? 355 TRP B CH2 1 
ATOM   5597  N N   . SER B 1 356 ? 0.636   -17.791 32.415  1.00 104.74 ? 356 SER B N   1 
ATOM   5598  C CA  . SER B 1 356 ? 1.717   -18.617 31.900  1.00 94.36  ? 356 SER B CA  1 
ATOM   5599  C C   . SER B 1 356 ? 2.862   -17.727 31.434  1.00 89.68  ? 356 SER B C   1 
ATOM   5600  O O   . SER B 1 356 ? 2.653   -16.582 31.030  1.00 91.75  ? 356 SER B O   1 
ATOM   5601  C CB  . SER B 1 356 ? 1.232   -19.503 30.752  1.00 92.04  ? 356 SER B CB  1 
ATOM   5602  O OG  . SER B 1 356 ? 0.823   -18.720 29.653  1.00 95.89  ? 356 SER B OG  1 
ATOM   5603  N N   . ARG B 1 357 ? 4.079   -18.266 31.489  1.00 86.34  ? 357 ARG B N   1 
ATOM   5604  C CA  . ARG B 1 357 ? 5.282   -17.476 31.268  1.00 75.42  ? 357 ARG B CA  1 
ATOM   5605  C C   . ARG B 1 357 ? 6.191   -18.146 30.246  1.00 71.53  ? 357 ARG B C   1 
ATOM   5606  O O   . ARG B 1 357 ? 6.412   -19.359 30.296  1.00 75.20  ? 357 ARG B O   1 
ATOM   5607  C CB  . ARG B 1 357 ? 6.028   -17.277 32.591  1.00 71.52  ? 357 ARG B CB  1 
ATOM   5608  C CG  . ARG B 1 357 ? 7.124   -16.235 32.571  1.00 67.82  ? 357 ARG B CG  1 
ATOM   5609  C CD  . ARG B 1 357 ? 7.857   -16.230 33.899  1.00 66.55  ? 357 ARG B CD  1 
ATOM   5610  N NE  . ARG B 1 357 ? 8.821   -15.141 34.003  1.00 63.72  ? 357 ARG B NE  1 
ATOM   5611  C CZ  . ARG B 1 357 ? 8.567   -13.988 34.614  1.00 61.59  ? 357 ARG B CZ  1 
ATOM   5612  N NH1 . ARG B 1 357 ? 7.380   -13.777 35.167  1.00 60.79  ? 357 ARG B NH1 1 
ATOM   5613  N NH2 . ARG B 1 357 ? 9.496   -13.044 34.668  1.00 62.26  ? 357 ARG B NH2 1 
ATOM   5614  N N   . VAL B 1 358 ? 6.715   -17.345 29.318  1.00 68.15  ? 358 VAL B N   1 
ATOM   5615  C CA  . VAL B 1 358 ? 7.630   -17.808 28.275  1.00 68.23  ? 358 VAL B CA  1 
ATOM   5616  C C   . VAL B 1 358 ? 8.815   -16.850 28.268  1.00 58.64  ? 358 VAL B C   1 
ATOM   5617  O O   . VAL B 1 358 ? 8.729   -15.749 27.713  1.00 70.83  ? 358 VAL B O   1 
ATOM   5618  C CB  . VAL B 1 358 ? 6.965   -17.872 26.895  1.00 64.93  ? 358 VAL B CB  1 
ATOM   5619  C CG1 . VAL B 1 358 ? 7.941   -18.406 25.856  1.00 67.02  ? 358 VAL B CG1 1 
ATOM   5620  C CG2 . VAL B 1 358 ? 5.721   -18.744 26.947  1.00 68.74  ? 358 VAL B CG2 1 
ATOM   5621  N N   . GLN B 1 359 ? 9.921   -17.256 28.886  1.00 64.87  ? 359 GLN B N   1 
ATOM   5622  C CA  . GLN B 1 359 ? 11.091  -16.402 29.007  1.00 58.43  ? 359 GLN B CA  1 
ATOM   5623  C C   . GLN B 1 359 ? 12.344  -17.148 28.564  1.00 58.15  ? 359 GLN B C   1 
ATOM   5624  O O   . GLN B 1 359 ? 12.338  -18.368 28.380  1.00 70.36  ? 359 GLN B O   1 
ATOM   5625  C CB  . GLN B 1 359 ? 11.234  -15.889 30.445  1.00 63.39  ? 359 GLN B CB  1 
ATOM   5626  C CG  . GLN B 1 359 ? 11.507  -16.993 31.454  1.00 64.74  ? 359 GLN B CG  1 
ATOM   5627  C CD  . GLN B 1 359 ? 12.128  -16.478 32.735  1.00 61.01  ? 359 GLN B CD  1 
ATOM   5628  O OE1 . GLN B 1 359 ? 11.895  -15.339 33.140  1.00 59.31  ? 359 GLN B OE1 1 
ATOM   5629  N NE2 . GLN B 1 359 ? 12.917  -17.323 33.388  1.00 69.32  ? 359 GLN B NE2 1 
ATOM   5630  N N   . ALA B 1 360 ? 13.433  -16.397 28.417  1.00 58.06  ? 360 ALA B N   1 
ATOM   5631  C CA  . ALA B 1 360 ? 14.721  -16.975 28.055  1.00 63.83  ? 360 ALA B CA  1 
ATOM   5632  C C   . ALA B 1 360 ? 15.826  -16.012 28.466  1.00 66.23  ? 360 ALA B C   1 
ATOM   5633  O O   . ALA B 1 360 ? 15.571  -14.873 28.863  1.00 68.97  ? 360 ALA B O   1 
ATOM   5634  C CB  . ALA B 1 360 ? 14.805  -17.294 26.559  1.00 64.66  ? 360 ALA B CB  1 
ATOM   5635  N N   . SER B 1 361 ? 17.069  -16.494 28.361  1.00 68.31  ? 361 SER B N   1 
ATOM   5636  C CA  . SER B 1 361 ? 18.216  -15.710 28.810  1.00 70.97  ? 361 SER B CA  1 
ATOM   5637  C C   . SER B 1 361 ? 18.508  -14.544 27.875  1.00 66.45  ? 361 SER B C   1 
ATOM   5638  O O   . SER B 1 361 ? 18.854  -13.448 28.331  1.00 68.86  ? 361 SER B O   1 
ATOM   5639  C CB  . SER B 1 361 ? 19.447  -16.609 28.945  1.00 73.23  ? 361 SER B CB  1 
ATOM   5640  O OG  . SER B 1 361 ? 19.521  -17.560 27.898  1.00 74.51  ? 361 SER B OG  1 
ATOM   5641  N N   . GLY B 1 362 ? 18.396  -14.761 26.573  1.00 79.43  ? 362 GLY B N   1 
ATOM   5642  C CA  . GLY B 1 362 ? 18.774  -13.763 25.600  1.00 71.99  ? 362 GLY B CA  1 
ATOM   5643  C C   . GLY B 1 362 ? 20.155  -13.943 25.017  1.00 86.90  ? 362 GLY B C   1 
ATOM   5644  O O   . GLY B 1 362 ? 20.598  -13.082 24.251  1.00 94.24  ? 362 GLY B O   1 
ATOM   5645  N N   . ASP B 1 363 ? 20.849  -15.029 25.351  1.00 99.10  ? 363 ASP B N   1 
ATOM   5646  C CA  . ASP B 1 363 ? 22.187  -15.272 24.823  1.00 98.25  ? 363 ASP B CA  1 
ATOM   5647  C C   . ASP B 1 363 ? 22.067  -15.714 23.373  1.00 97.37  ? 363 ASP B C   1 
ATOM   5648  O O   . ASP B 1 363 ? 21.661  -16.846 23.091  1.00 96.23  ? 363 ASP B O   1 
ATOM   5649  C CB  . ASP B 1 363 ? 22.919  -16.323 25.650  1.00 98.38  ? 363 ASP B CB  1 
ATOM   5650  C CG  . ASP B 1 363 ? 23.191  -15.864 27.062  1.00 103.06 ? 363 ASP B CG  1 
ATOM   5651  O OD1 . ASP B 1 363 ? 23.184  -14.637 27.296  1.00 107.21 ? 363 ASP B OD1 1 
ATOM   5652  O OD2 . ASP B 1 363 ? 23.413  -16.727 27.936  1.00 105.11 ? 363 ASP B OD2 1 
ATOM   5653  N N   . TYR B 1 364 ? 22.422  -14.822 22.450  1.00 109.20 ? 364 TYR B N   1 
ATOM   5654  C CA  . TYR B 1 364 ? 22.392  -15.158 21.034  1.00 107.75 ? 364 TYR B CA  1 
ATOM   5655  C C   . TYR B 1 364 ? 23.522  -16.098 20.643  1.00 110.68 ? 364 TYR B C   1 
ATOM   5656  O O   . TYR B 1 364 ? 23.595  -16.510 19.480  1.00 109.95 ? 364 TYR B O   1 
ATOM   5657  C CB  . TYR B 1 364 ? 22.437  -13.875 20.205  1.00 107.97 ? 364 TYR B CB  1 
ATOM   5658  C CG  . TYR B 1 364 ? 21.345  -12.901 20.594  1.00 111.14 ? 364 TYR B CG  1 
ATOM   5659  C CD1 . TYR B 1 364 ? 20.036  -13.080 20.162  1.00 109.30 ? 364 TYR B CD1 1 
ATOM   5660  C CD2 . TYR B 1 364 ? 21.622  -11.813 21.411  1.00 112.12 ? 364 TYR B CD2 1 
ATOM   5661  C CE1 . TYR B 1 364 ? 19.035  -12.196 20.529  1.00 108.13 ? 364 TYR B CE1 1 
ATOM   5662  C CE2 . TYR B 1 364 ? 20.630  -10.925 21.781  1.00 114.62 ? 364 TYR B CE2 1 
ATOM   5663  C CZ  . TYR B 1 364 ? 19.339  -11.120 21.338  1.00 109.99 ? 364 TYR B CZ  1 
ATOM   5664  O OH  . TYR B 1 364 ? 18.349  -10.236 21.706  1.00 109.35 ? 364 TYR B OH  1 
ATOM   5665  N N   . ASN B 1 365 ? 24.396  -16.442 21.591  1.00 103.64 ? 365 ASN B N   1 
ATOM   5666  C CA  . ASN B 1 365 ? 25.417  -17.463 21.404  1.00 100.29 ? 365 ASN B CA  1 
ATOM   5667  C C   . ASN B 1 365 ? 24.992  -18.815 21.954  1.00 98.62  ? 365 ASN B C   1 
ATOM   5668  O O   . ASN B 1 365 ? 25.437  -19.850 21.445  1.00 99.56  ? 365 ASN B O   1 
ATOM   5669  C CB  . ASN B 1 365 ? 26.724  -17.039 22.083  1.00 100.87 ? 365 ASN B CB  1 
ATOM   5670  C CG  . ASN B 1 365 ? 27.034  -15.569 21.882  1.00 100.13 ? 365 ASN B CG  1 
ATOM   5671  O OD1 . ASN B 1 365 ? 27.212  -14.823 22.846  1.00 108.87 ? 365 ASN B OD1 1 
ATOM   5672  N ND2 . ASN B 1 365 ? 27.100  -15.145 20.627  1.00 96.04  ? 365 ASN B ND2 1 
ATOM   5673  N N   . ASP B 1 366 ? 24.143  -18.827 22.980  1.00 91.69  ? 366 ASP B N   1 
ATOM   5674  C CA  . ASP B 1 366 ? 23.604  -20.069 23.511  1.00 84.59  ? 366 ASP B CA  1 
ATOM   5675  C C   . ASP B 1 366 ? 22.411  -20.509 22.675  1.00 76.40  ? 366 ASP B C   1 
ATOM   5676  O O   . ASP B 1 366 ? 21.632  -19.682 22.192  1.00 83.60  ? 366 ASP B O   1 
ATOM   5677  C CB  . ASP B 1 366 ? 23.184  -19.899 24.972  1.00 86.40  ? 366 ASP B CB  1 
ATOM   5678  C CG  . ASP B 1 366 ? 22.688  -21.196 25.594  1.00 85.35  ? 366 ASP B CG  1 
ATOM   5679  O OD1 . ASP B 1 366 ? 22.951  -22.274 25.020  1.00 84.87  ? 366 ASP B OD1 1 
ATOM   5680  O OD2 . ASP B 1 366 ? 22.031  -21.137 26.656  1.00 80.85  ? 366 ASP B OD2 1 
ATOM   5681  N N   . ARG B 1 367 ? 22.279  -21.824 22.501  1.00 76.13  ? 367 ARG B N   1 
ATOM   5682  C CA  . ARG B 1 367 ? 21.183  -22.359 21.700  1.00 76.59  ? 367 ARG B CA  1 
ATOM   5683  C C   . ARG B 1 367 ? 19.833  -22.068 22.346  1.00 79.85  ? 367 ARG B C   1 
ATOM   5684  O O   . ARG B 1 367 ? 18.880  -21.674 21.663  1.00 78.78  ? 367 ARG B O   1 
ATOM   5685  C CB  . ARG B 1 367 ? 21.374  -23.861 21.501  1.00 77.47  ? 367 ARG B CB  1 
ATOM   5686  C CG  . ARG B 1 367 ? 20.590  -24.441 20.342  1.00 77.13  ? 367 ARG B CG  1 
ATOM   5687  C CD  . ARG B 1 367 ? 20.852  -25.928 20.207  1.00 79.14  ? 367 ARG B CD  1 
ATOM   5688  N NE  . ARG B 1 367 ? 20.223  -26.490 19.016  1.00 85.88  ? 367 ARG B NE  1 
ATOM   5689  C CZ  . ARG B 1 367 ? 20.216  -27.784 18.717  1.00 84.93  ? 367 ARG B CZ  1 
ATOM   5690  N NH1 . ARG B 1 367 ? 20.803  -28.655 19.528  1.00 83.51  ? 367 ARG B NH1 1 
ATOM   5691  N NH2 . ARG B 1 367 ? 19.624  -28.208 17.609  1.00 83.49  ? 367 ARG B NH2 1 
ATOM   5692  N N   . LEU B 1 368 ? 19.734  -22.252 23.662  1.00 85.82  ? 368 LEU B N   1 
ATOM   5693  C CA  . LEU B 1 368 ? 18.506  -21.998 24.399  1.00 82.41  ? 368 LEU B CA  1 
ATOM   5694  C C   . LEU B 1 368 ? 18.437  -20.583 24.961  1.00 81.38  ? 368 LEU B C   1 
ATOM   5695  O O   . LEU B 1 368 ? 17.668  -20.333 25.895  1.00 80.06  ? 368 LEU B O   1 
ATOM   5696  C CB  . LEU B 1 368 ? 18.352  -23.024 25.525  1.00 85.25  ? 368 LEU B CB  1 
ATOM   5697  C CG  . LEU B 1 368 ? 18.277  -24.480 25.060  1.00 83.59  ? 368 LEU B CG  1 
ATOM   5698  C CD1 . LEU B 1 368 ? 18.023  -25.416 26.229  1.00 82.27  ? 368 LEU B CD1 1 
ATOM   5699  C CD2 . LEU B 1 368 ? 17.193  -24.638 24.004  1.00 79.02  ? 368 LEU B CD2 1 
ATOM   5700  N N   . GLY B 1 369 ? 19.220  -19.653 24.413  1.00 79.18  ? 369 GLY B N   1 
ATOM   5701  C CA  . GLY B 1 369 ? 19.152  -18.278 24.869  1.00 76.14  ? 369 GLY B CA  1 
ATOM   5702  C C   . GLY B 1 369 ? 17.890  -17.566 24.441  1.00 75.93  ? 369 GLY B C   1 
ATOM   5703  O O   . GLY B 1 369 ? 17.511  -16.569 25.062  1.00 77.13  ? 369 GLY B O   1 
ATOM   5704  N N   . ILE B 1 370 ? 17.232  -18.057 23.394  1.00 68.96  ? 370 ILE B N   1 
ATOM   5705  C CA  . ILE B 1 370 ? 15.973  -17.512 22.900  1.00 68.63  ? 370 ILE B CA  1 
ATOM   5706  C C   . ILE B 1 370 ? 15.004  -18.678 22.769  1.00 63.19  ? 370 ILE B C   1 
ATOM   5707  O O   . ILE B 1 370 ? 15.140  -19.503 21.857  1.00 64.95  ? 370 ILE B O   1 
ATOM   5708  C CB  . ILE B 1 370 ? 16.135  -16.790 21.556  1.00 73.63  ? 370 ILE B CB  1 
ATOM   5709  C CG1 . ILE B 1 370 ? 17.145  -15.645 21.676  1.00 80.14  ? 370 ILE B CG1 1 
ATOM   5710  C CG2 . ILE B 1 370 ? 14.789  -16.283 21.064  1.00 71.38  ? 370 ILE B CG2 1 
ATOM   5711  C CD1 . ILE B 1 370 ? 16.742  -14.582 22.665  1.00 80.68  ? 370 ILE B CD1 1 
ATOM   5712  N N   . THR B 1 371 ? 14.030  -18.751 23.672  1.00 65.59  ? 371 THR B N   1 
ATOM   5713  C CA  . THR B 1 371 ? 13.045  -19.822 23.606  1.00 75.74  ? 371 THR B CA  1 
ATOM   5714  C C   . THR B 1 371 ? 12.117  -19.598 22.417  1.00 57.43  ? 371 THR B C   1 
ATOM   5715  O O   . THR B 1 371 ? 11.622  -18.488 22.199  1.00 68.62  ? 371 THR B O   1 
ATOM   5716  C CB  . THR B 1 371 ? 12.241  -19.906 24.905  1.00 63.04  ? 371 THR B CB  1 
ATOM   5717  O OG1 . THR B 1 371 ? 11.129  -20.791 24.726  1.00 58.28  ? 371 THR B OG1 1 
ATOM   5718  C CG2 . THR B 1 371 ? 11.728  -18.543 25.311  1.00 61.55  ? 371 THR B CG2 1 
ATOM   5719  N N   . ILE B 1 372 ? 11.898  -20.646 21.631  1.00 78.26  ? 372 ILE B N   1 
ATOM   5720  C CA  . ILE B 1 372 ? 11.130  -20.551 20.397  1.00 57.48  ? 372 ILE B CA  1 
ATOM   5721  C C   . ILE B 1 372 ? 9.964   -21.522 20.476  1.00 71.43  ? 372 ILE B C   1 
ATOM   5722  O O   . ILE B 1 372 ? 10.153  -22.707 20.773  1.00 61.00  ? 372 ILE B O   1 
ATOM   5723  C CB  . ILE B 1 372 ? 12.003  -20.837 19.162  1.00 66.58  ? 372 ILE B CB  1 
ATOM   5724  C CG1 . ILE B 1 372 ? 13.183  -19.858 19.116  1.00 66.69  ? 372 ILE B CG1 1 
ATOM   5725  C CG2 . ILE B 1 372 ? 11.169  -20.741 17.890  1.00 67.15  ? 372 ILE B CG2 1 
ATOM   5726  C CD1 . ILE B 1 372 ? 14.255  -20.217 18.113  1.00 74.96  ? 372 ILE B CD1 1 
ATOM   5727  N N   . LEU B 1 373 ? 8.764   -21.017 20.214  1.00 64.88  ? 373 LEU B N   1 
ATOM   5728  C CA  . LEU B 1 373 ? 7.544   -21.808 20.247  1.00 65.96  ? 373 LEU B CA  1 
ATOM   5729  C C   . LEU B 1 373 ? 7.058   -22.020 18.821  1.00 66.78  ? 373 LEU B C   1 
ATOM   5730  O O   . LEU B 1 373 ? 7.032   -21.078 18.024  1.00 67.70  ? 373 LEU B O   1 
ATOM   5731  C CB  . LEU B 1 373 ? 6.472   -21.118 21.094  1.00 65.00  ? 373 LEU B CB  1 
ATOM   5732  C CG  . LEU B 1 373 ? 6.329   -21.640 22.527  1.00 62.43  ? 373 LEU B CG  1 
ATOM   5733  C CD1 . LEU B 1 373 ? 7.642   -21.526 23.289  1.00 62.61  ? 373 LEU B CD1 1 
ATOM   5734  C CD2 . LEU B 1 373 ? 5.219   -20.899 23.250  1.00 67.84  ? 373 LEU B CD2 1 
ATOM   5735  N N   . GLY B 1 374 ? 6.685   -23.254 18.506  1.00 68.73  ? 374 GLY B N   1 
ATOM   5736  C CA  . GLY B 1 374 ? 6.287   -23.602 17.162  1.00 77.18  ? 374 GLY B CA  1 
ATOM   5737  C C   . GLY B 1 374 ? 4.917   -23.053 16.800  1.00 80.65  ? 374 GLY B C   1 
ATOM   5738  O O   . GLY B 1 374 ? 4.325   -22.219 17.487  1.00 77.45  ? 374 GLY B O   1 
ATOM   5739  N N   . GLU B 1 375 ? 4.408   -23.551 15.678  1.00 87.13  ? 375 GLU B N   1 
ATOM   5740  C CA  . GLU B 1 375 ? 3.099   -23.144 15.188  1.00 86.20  ? 375 GLU B CA  1 
ATOM   5741  C C   . GLU B 1 375 ? 2.005   -23.879 15.952  1.00 85.16  ? 375 GLU B C   1 
ATOM   5742  O O   . GLU B 1 375 ? 2.050   -25.106 16.088  1.00 87.52  ? 375 GLU B O   1 
ATOM   5743  C CB  . GLU B 1 375 ? 2.988   -23.428 13.691  1.00 86.63  ? 375 GLU B CB  1 
ATOM   5744  C CG  . GLU B 1 375 ? 1.627   -23.138 13.092  1.00 85.08  ? 375 GLU B CG  1 
ATOM   5745  C CD  . GLU B 1 375 ? 1.471   -23.728 11.706  1.00 89.51  ? 375 GLU B CD  1 
ATOM   5746  O OE1 . GLU B 1 375 ? 2.396   -24.433 11.251  1.00 93.46  ? 375 GLU B OE1 1 
ATOM   5747  O OE2 . GLU B 1 375 ? 0.425   -23.486 11.070  1.00 94.86  ? 375 GLU B OE2 1 
ATOM   5748  N N   . ALA B 1 376 ? 1.017   -23.126 16.437  1.00 81.56  ? 376 ALA B N   1 
ATOM   5749  C CA  . ALA B 1 376 ? -0.132  -23.683 17.156  1.00 80.80  ? 376 ALA B CA  1 
ATOM   5750  C C   . ALA B 1 376 ? 0.314   -24.504 18.366  1.00 78.87  ? 376 ALA B C   1 
ATOM   5751  O O   . ALA B 1 376 ? -0.145  -25.625 18.593  1.00 76.88  ? 376 ALA B O   1 
ATOM   5752  C CB  . ALA B 1 376 ? -1.019  -24.514 16.225  1.00 88.21  ? 376 ALA B CB  1 
ATOM   5753  N N   . VAL B 1 377 ? 1.221   -23.936 19.148  1.00 79.10  ? 377 VAL B N   1 
ATOM   5754  C CA  . VAL B 1 377 ? 1.621   -24.532 20.414  1.00 82.59  ? 377 VAL B CA  1 
ATOM   5755  C C   . VAL B 1 377 ? 0.764   -23.925 21.514  1.00 84.80  ? 377 VAL B C   1 
ATOM   5756  O O   . VAL B 1 377 ? 0.639   -22.699 21.614  1.00 85.54  ? 377 VAL B O   1 
ATOM   5757  C CB  . VAL B 1 377 ? 3.119   -24.313 20.687  1.00 81.56  ? 377 VAL B CB  1 
ATOM   5758  C CG1 . VAL B 1 377 ? 3.496   -22.874 20.430  1.00 85.09  ? 377 VAL B CG1 1 
ATOM   5759  C CG2 . VAL B 1 377 ? 3.451   -24.695 22.117  1.00 79.41  ? 377 VAL B CG2 1 
ATOM   5760  N N   . THR B 1 378 ? 0.163   -24.776 22.334  1.00 88.99  ? 378 THR B N   1 
ATOM   5761  C CA  . THR B 1 378 ? -0.779  -24.326 23.351  1.00 91.12  ? 378 THR B CA  1 
ATOM   5762  C C   . THR B 1 378 ? -0.125  -24.492 24.717  1.00 90.56  ? 378 THR B C   1 
ATOM   5763  O O   . THR B 1 378 ? -0.068  -25.597 25.263  1.00 90.27  ? 378 THR B O   1 
ATOM   5764  C CB  . THR B 1 378 ? -2.098  -25.090 23.260  1.00 92.82  ? 378 THR B CB  1 
ATOM   5765  O OG1 . THR B 1 378 ? -1.878  -26.473 23.555  1.00 98.40  ? 378 THR B OG1 1 
ATOM   5766  C CG2 . THR B 1 378 ? -2.687  -24.966 21.866  1.00 90.37  ? 378 THR B CG2 1 
ATOM   5767  N N   . VAL B 1 379 ? 0.371   -23.386 25.259  1.00 89.34  ? 379 VAL B N   1 
ATOM   5768  C CA  . VAL B 1 379 ? 0.879   -23.344 26.623  1.00 85.76  ? 379 VAL B CA  1 
ATOM   5769  C C   . VAL B 1 379 ? -0.311  -23.109 27.540  1.00 85.21  ? 379 VAL B C   1 
ATOM   5770  O O   . VAL B 1 379 ? -0.979  -22.075 27.450  1.00 83.03  ? 379 VAL B O   1 
ATOM   5771  C CB  . VAL B 1 379 ? 1.940   -22.246 26.792  1.00 82.17  ? 379 VAL B CB  1 
ATOM   5772  C CG1 . VAL B 1 379 ? 2.385   -22.159 28.239  1.00 80.71  ? 379 VAL B CG1 1 
ATOM   5773  C CG2 . VAL B 1 379 ? 3.131   -22.516 25.885  1.00 84.35  ? 379 VAL B CG2 1 
ATOM   5774  N N   . GLU B 1 380 ? -0.592  -24.076 28.409  1.00 85.89  ? 380 GLU B N   1 
ATOM   5775  C CA  . GLU B 1 380 ? -1.768  -23.998 29.261  1.00 85.34  ? 380 GLU B CA  1 
ATOM   5776  C C   . GLU B 1 380 ? -1.558  -22.951 30.355  1.00 82.83  ? 380 GLU B C   1 
ATOM   5777  O O   . GLU B 1 380 ? -0.496  -22.335 30.478  1.00 85.19  ? 380 GLU B O   1 
ATOM   5778  C CB  . GLU B 1 380 ? -2.088  -25.368 29.854  1.00 86.55  ? 380 GLU B CB  1 
ATOM   5779  C CG  . GLU B 1 380 ? -3.579  -25.658 29.976  1.00 91.59  ? 380 GLU B CG  1 
ATOM   5780  C CD  . GLU B 1 380 ? -3.880  -27.142 30.026  1.00 104.25 ? 380 GLU B CD  1 
ATOM   5781  O OE1 . GLU B 1 380 ? -2.953  -27.945 29.790  1.00 100.45 ? 380 GLU B OE1 1 
ATOM   5782  O OE2 . GLU B 1 380 ? -5.043  -27.508 30.293  1.00 116.29 ? 380 GLU B OE2 1 
ATOM   5783  N N   . ASP B 1 381 ? -2.604  -22.738 31.147  1.00 86.31  ? 381 ASP B N   1 
ATOM   5784  C CA  . ASP B 1 381 ? -2.556  -21.741 32.206  1.00 87.41  ? 381 ASP B CA  1 
ATOM   5785  C C   . ASP B 1 381 ? -1.484  -22.092 33.233  1.00 89.85  ? 381 ASP B C   1 
ATOM   5786  O O   . ASP B 1 381 ? -1.303  -23.259 33.595  1.00 91.06  ? 381 ASP B O   1 
ATOM   5787  C CB  . ASP B 1 381 ? -3.926  -21.635 32.871  1.00 86.36  ? 381 ASP B CB  1 
ATOM   5788  C CG  . ASP B 1 381 ? -5.060  -21.622 31.861  1.00 85.19  ? 381 ASP B CG  1 
ATOM   5789  O OD1 . ASP B 1 381 ? -4.901  -20.984 30.799  1.00 86.23  ? 381 ASP B OD1 1 
ATOM   5790  O OD2 . ASP B 1 381 ? -6.107  -22.250 32.125  1.00 82.80  ? 381 ASP B OD2 1 
ATOM   5791  N N   . GLU B 1 382 ? -0.764  -21.062 33.689  1.00 95.27  ? 382 GLU B N   1 
ATOM   5792  C CA  . GLU B 1 382 ? 0.333   -21.161 34.652  1.00 95.10  ? 382 GLU B CA  1 
ATOM   5793  C C   . GLU B 1 382 ? 1.545   -21.938 34.144  1.00 93.42  ? 382 GLU B C   1 
ATOM   5794  O O   . GLU B 1 382 ? 2.551   -22.032 34.855  1.00 91.77  ? 382 GLU B O   1 
ATOM   5795  C CB  . GLU B 1 382 ? -0.128  -21.790 35.972  1.00 94.18  ? 382 GLU B CB  1 
ATOM   5796  C CG  . GLU B 1 382 ? -1.006  -20.916 36.842  1.00 94.58  ? 382 GLU B CG  1 
ATOM   5797  C CD  . GLU B 1 382 ? -1.111  -21.462 38.253  1.00 98.40  ? 382 GLU B CD  1 
ATOM   5798  O OE1 . GLU B 1 382 ? -0.225  -22.252 38.644  1.00 94.41  ? 382 GLU B OE1 1 
ATOM   5799  O OE2 . GLU B 1 382 ? -2.071  -21.108 38.968  1.00 103.09 ? 382 GLU B OE2 1 
ATOM   5800  N N   . VAL B 1 383 ? 1.480   -22.494 32.933  1.00 89.25  ? 383 VAL B N   1 
ATOM   5801  C CA  . VAL B 1 383 ? 2.593   -23.289 32.424  1.00 89.06  ? 383 VAL B CA  1 
ATOM   5802  C C   . VAL B 1 383 ? 3.757   -22.378 32.052  1.00 91.92  ? 383 VAL B C   1 
ATOM   5803  O O   . VAL B 1 383 ? 3.577   -21.329 31.422  1.00 87.39  ? 383 VAL B O   1 
ATOM   5804  C CB  . VAL B 1 383 ? 2.133   -24.140 31.229  1.00 88.73  ? 383 VAL B CB  1 
ATOM   5805  C CG1 . VAL B 1 383 ? 3.289   -24.953 30.671  1.00 91.42  ? 383 VAL B CG1 1 
ATOM   5806  C CG2 . VAL B 1 383 ? 0.994   -25.051 31.648  1.00 90.45  ? 383 VAL B CG2 1 
ATOM   5807  N N   . ALA B 1 384 ? 4.965   -22.783 32.434  1.00 104.48 ? 384 ALA B N   1 
ATOM   5808  C CA  . ALA B 1 384 ? 6.165   -21.986 32.229  1.00 98.68  ? 384 ALA B CA  1 
ATOM   5809  C C   . ALA B 1 384 ? 7.105   -22.677 31.250  1.00 96.09  ? 384 ALA B C   1 
ATOM   5810  O O   . ALA B 1 384 ? 7.286   -23.897 31.300  1.00 95.21  ? 384 ALA B O   1 
ATOM   5811  C CB  . ALA B 1 384 ? 6.887   -21.735 33.555  1.00 97.58  ? 384 ALA B CB  1 
ATOM   5812  N N   . VAL B 1 385 ? 7.700   -21.888 30.358  1.00 87.57  ? 385 VAL B N   1 
ATOM   5813  C CA  . VAL B 1 385 ? 8.658   -22.379 29.374  1.00 81.40  ? 385 VAL B CA  1 
ATOM   5814  C C   . VAL B 1 385 ? 9.881   -21.474 29.451  1.00 82.97  ? 385 VAL B C   1 
ATOM   5815  O O   . VAL B 1 385 ? 9.836   -20.325 28.995  1.00 80.12  ? 385 VAL B O   1 
ATOM   5816  C CB  . VAL B 1 385 ? 8.076   -22.400 27.954  1.00 74.69  ? 385 VAL B CB  1 
ATOM   5817  C CG1 . VAL B 1 385 ? 9.126   -22.865 26.960  1.00 81.25  ? 385 VAL B CG1 1 
ATOM   5818  C CG2 . VAL B 1 385 ? 6.845   -23.295 27.896  1.00 73.08  ? 385 VAL B CG2 1 
ATOM   5819  N N   . ILE B 1 386 ? 10.969  -21.986 30.021  1.00 97.58  ? 386 ILE B N   1 
ATOM   5820  C CA  . ILE B 1 386 ? 12.191  -21.218 30.241  1.00 97.43  ? 386 ILE B CA  1 
ATOM   5821  C C   . ILE B 1 386 ? 13.291  -21.802 29.368  1.00 96.44  ? 386 ILE B C   1 
ATOM   5822  O O   . ILE B 1 386 ? 13.743  -22.931 29.597  1.00 96.99  ? 386 ILE B O   1 
ATOM   5823  C CB  . ILE B 1 386 ? 12.611  -21.214 31.716  1.00 100.09 ? 386 ILE B CB  1 
ATOM   5824  C CG1 . ILE B 1 386 ? 11.567  -20.498 32.577  1.00 101.10 ? 386 ILE B CG1 1 
ATOM   5825  C CG2 . ILE B 1 386 ? 13.988  -20.580 31.875  1.00 100.84 ? 386 ILE B CG2 1 
ATOM   5826  C CD1 . ILE B 1 386 ? 10.510  -21.416 33.140  1.00 102.58 ? 386 ILE B CD1 1 
ATOM   5827  N N   . GLY B 1 387 ? 13.731  -21.025 28.379  1.00 78.73  ? 387 GLY B N   1 
ATOM   5828  C CA  . GLY B 1 387 ? 14.849  -21.389 27.528  1.00 79.51  ? 387 GLY B CA  1 
ATOM   5829  C C   . GLY B 1 387 ? 14.726  -22.777 26.940  1.00 79.19  ? 387 GLY B C   1 
ATOM   5830  O O   . GLY B 1 387 ? 15.579  -23.638 27.173  1.00 80.48  ? 387 GLY B O   1 
ATOM   5831  N N   . SER B 1 388 ? 13.659  -23.004 26.179  1.00 75.96  ? 388 SER B N   1 
ATOM   5832  C CA  . SER B 1 388 ? 13.397  -24.299 25.575  1.00 73.14  ? 388 SER B CA  1 
ATOM   5833  C C   . SER B 1 388 ? 12.806  -24.086 24.190  1.00 68.40  ? 388 SER B C   1 
ATOM   5834  O O   . SER B 1 388 ? 12.404  -22.978 23.826  1.00 70.99  ? 388 SER B O   1 
ATOM   5835  C CB  . SER B 1 388 ? 12.462  -25.143 26.451  1.00 73.89  ? 388 SER B CB  1 
ATOM   5836  O OG  . SER B 1 388 ? 13.089  -25.487 27.675  1.00 77.40  ? 388 SER B OG  1 
ATOM   5837  N N   . ILE B 1 389 ? 12.754  -25.163 23.412  1.00 75.73  ? 389 ILE B N   1 
ATOM   5838  C CA  . ILE B 1 389 ? 12.252  -25.130 22.043  1.00 76.43  ? 389 ILE B CA  1 
ATOM   5839  C C   . ILE B 1 389 ? 11.095  -26.112 21.942  1.00 74.87  ? 389 ILE B C   1 
ATOM   5840  O O   . ILE B 1 389 ? 11.271  -27.314 22.177  1.00 74.62  ? 389 ILE B O   1 
ATOM   5841  C CB  . ILE B 1 389 ? 13.348  -25.467 21.020  1.00 74.50  ? 389 ILE B CB  1 
ATOM   5842  C CG1 . ILE B 1 389 ? 14.589  -24.601 21.253  1.00 70.95  ? 389 ILE B CG1 1 
ATOM   5843  C CG2 . ILE B 1 389 ? 12.828  -25.274 19.604  1.00 72.90  ? 389 ILE B CG2 1 
ATOM   5844  C CD1 . ILE B 1 389 ? 14.324  -23.112 21.171  1.00 70.17  ? 389 ILE B CD1 1 
ATOM   5845  N N   . VAL B 1 390 ? 9.916   -25.601 21.600  1.00 68.51  ? 390 VAL B N   1 
ATOM   5846  C CA  . VAL B 1 390 ? 8.715   -26.413 21.456  1.00 70.51  ? 390 VAL B CA  1 
ATOM   5847  C C   . VAL B 1 390 ? 8.374   -26.510 19.977  1.00 73.02  ? 390 VAL B C   1 
ATOM   5848  O O   . VAL B 1 390 ? 8.435   -25.513 19.247  1.00 75.56  ? 390 VAL B O   1 
ATOM   5849  C CB  . VAL B 1 390 ? 7.534   -25.829 22.254  1.00 66.92  ? 390 VAL B CB  1 
ATOM   5850  C CG1 . VAL B 1 390 ? 6.346   -26.772 22.201  1.00 66.97  ? 390 VAL B CG1 1 
ATOM   5851  C CG2 . VAL B 1 390 ? 7.950   -25.560 23.691  1.00 65.05  ? 390 VAL B CG2 1 
ATOM   5852  N N   . LEU B 1 391 ? 8.028   -27.715 19.533  1.00 72.16  ? 391 LEU B N   1 
ATOM   5853  C CA  . LEU B 1 391 ? 7.665   -27.930 18.142  1.00 77.44  ? 391 LEU B CA  1 
ATOM   5854  C C   . LEU B 1 391 ? 6.226   -27.481 17.894  1.00 81.50  ? 391 LEU B C   1 
ATOM   5855  O O   . LEU B 1 391 ? 5.489   -27.118 18.815  1.00 77.66  ? 391 LEU B O   1 
ATOM   5856  C CB  . LEU B 1 391 ? 7.852   -29.399 17.765  1.00 78.89  ? 391 LEU B CB  1 
ATOM   5857  C CG  . LEU B 1 391 ? 9.202   -29.783 17.152  1.00 70.59  ? 391 LEU B CG  1 
ATOM   5858  C CD1 . LEU B 1 391 ? 10.351  -29.449 18.088  1.00 70.12  ? 391 LEU B CD1 1 
ATOM   5859  C CD2 . LEU B 1 391 ? 9.223   -31.262 16.797  1.00 74.04  ? 391 LEU B CD2 1 
ATOM   5860  N N   . GLN B 1 392 ? 5.828   -27.510 16.624  1.00 89.30  ? 392 GLN B N   1 
ATOM   5861  C CA  . GLN B 1 392 ? 4.502   -27.045 16.251  1.00 87.84  ? 392 GLN B CA  1 
ATOM   5862  C C   . GLN B 1 392 ? 3.440   -28.067 16.643  1.00 85.90  ? 392 GLN B C   1 
ATOM   5863  O O   . GLN B 1 392 ? 3.711   -29.262 16.791  1.00 85.20  ? 392 GLN B O   1 
ATOM   5864  C CB  . GLN B 1 392 ? 4.416   -26.752 14.749  1.00 88.33  ? 392 GLN B CB  1 
ATOM   5865  C CG  . GLN B 1 392 ? 4.407   -27.974 13.843  1.00 91.19  ? 392 GLN B CG  1 
ATOM   5866  C CD  . GLN B 1 392 ? 5.792   -28.535 13.599  1.00 92.81  ? 392 GLN B CD  1 
ATOM   5867  O OE1 . GLN B 1 392 ? 6.782   -28.024 14.120  1.00 91.73  ? 392 GLN B OE1 1 
ATOM   5868  N NE2 . GLN B 1 392 ? 5.868   -29.589 12.795  1.00 92.59  ? 392 GLN B NE2 1 
ATOM   5869  N N   . ASN B 1 393 ? 2.213   -27.569 16.814  1.00 84.14  ? 393 ASN B N   1 
ATOM   5870  C CA  . ASN B 1 393 ? 1.048   -28.389 17.151  1.00 79.42  ? 393 ASN B CA  1 
ATOM   5871  C C   . ASN B 1 393 ? 1.304   -29.172 18.440  1.00 78.78  ? 393 ASN B C   1 
ATOM   5872  O O   . ASN B 1 393 ? 1.257   -30.404 18.475  1.00 79.72  ? 393 ASN B O   1 
ATOM   5873  C CB  . ASN B 1 393 ? 0.695   -29.333 15.997  1.00 82.32  ? 393 ASN B CB  1 
ATOM   5874  C CG  . ASN B 1 393 ? 0.826   -28.669 14.642  1.00 85.10  ? 393 ASN B CG  1 
ATOM   5875  O OD1 . ASN B 1 393 ? 0.495   -27.496 14.477  1.00 84.30  ? 393 ASN B OD1 1 
ATOM   5876  N ND2 . ASN B 1 393 ? 1.325   -29.418 13.664  1.00 84.15  ? 393 ASN B ND2 1 
ATOM   5877  N N   . LYS B 1 394 ? 1.571   -28.429 19.512  1.00 78.84  ? 394 LYS B N   1 
ATOM   5878  C CA  . LYS B 1 394 ? 2.000   -29.039 20.760  1.00 77.07  ? 394 LYS B CA  1 
ATOM   5879  C C   . LYS B 1 394 ? 1.268   -28.409 21.934  1.00 73.79  ? 394 LYS B C   1 
ATOM   5880  O O   . LYS B 1 394 ? 1.074   -27.192 21.976  1.00 73.81  ? 394 LYS B O   1 
ATOM   5881  C CB  . LYS B 1 394 ? 3.514   -28.884 20.949  1.00 80.42  ? 394 LYS B CB  1 
ATOM   5882  C CG  . LYS B 1 394 ? 4.124   -29.916 21.872  1.00 78.10  ? 394 LYS B CG  1 
ATOM   5883  C CD  . LYS B 1 394 ? 4.081   -31.284 21.213  1.00 80.61  ? 394 LYS B CD  1 
ATOM   5884  C CE  . LYS B 1 394 ? 4.633   -32.366 22.119  1.00 80.37  ? 394 LYS B CE  1 
ATOM   5885  N NZ  . LYS B 1 394 ? 4.745   -33.668 21.401  1.00 83.64  ? 394 LYS B NZ  1 
ATOM   5886  N N   . THR B 1 395 ? 0.865   -29.243 22.886  1.00 73.44  ? 395 THR B N   1 
ATOM   5887  C CA  . THR B 1 395 ? 0.182   -28.787 24.087  1.00 77.48  ? 395 THR B CA  1 
ATOM   5888  C C   . THR B 1 395 ? 1.072   -29.009 25.301  1.00 74.79  ? 395 THR B C   1 
ATOM   5889  O O   . THR B 1 395 ? 1.699   -30.063 25.438  1.00 77.05  ? 395 THR B O   1 
ATOM   5890  C CB  . THR B 1 395 ? -1.158  -29.508 24.276  1.00 79.23  ? 395 THR B CB  1 
ATOM   5891  O OG1 . THR B 1 395 ? -1.645  -29.276 25.604  1.00 76.54  ? 395 THR B OG1 1 
ATOM   5892  C CG2 . THR B 1 395 ? -1.006  -31.003 24.040  1.00 88.64  ? 395 THR B CG2 1 
ATOM   5893  N N   . LEU B 1 396 ? 1.131   -28.009 26.177  1.00 77.11  ? 396 LEU B N   1 
ATOM   5894  C CA  . LEU B 1 396 ? 1.987   -28.054 27.359  1.00 78.86  ? 396 LEU B CA  1 
ATOM   5895  C C   . LEU B 1 396 ? 1.139   -27.800 28.596  1.00 79.64  ? 396 LEU B C   1 
ATOM   5896  O O   . LEU B 1 396 ? 0.671   -26.678 28.815  1.00 82.52  ? 396 LEU B O   1 
ATOM   5897  C CB  . LEU B 1 396 ? 3.129   -27.041 27.265  1.00 83.51  ? 396 LEU B CB  1 
ATOM   5898  C CG  . LEU B 1 396 ? 4.191   -27.311 26.197  1.00 78.06  ? 396 LEU B CG  1 
ATOM   5899  C CD1 . LEU B 1 396 ? 5.256   -26.224 26.208  1.00 74.67  ? 396 LEU B CD1 1 
ATOM   5900  C CD2 . LEU B 1 396 ? 4.817   -28.680 26.408  1.00 73.52  ? 396 LEU B CD2 1 
ATOM   5901  N N   . ASN B 1 397 ? 0.940   -28.845 29.398  1.00 87.64  ? 397 ASN B N   1 
ATOM   5902  C CA  . ASN B 1 397 ? 0.287   -28.726 30.693  1.00 85.84  ? 397 ASN B CA  1 
ATOM   5903  C C   . ASN B 1 397 ? 1.273   -28.614 31.844  1.00 94.41  ? 397 ASN B C   1 
ATOM   5904  O O   . ASN B 1 397 ? 0.878   -28.206 32.941  1.00 91.74  ? 397 ASN B O   1 
ATOM   5905  C CB  . ASN B 1 397 ? -0.631  -29.928 30.936  1.00 85.35  ? 397 ASN B CB  1 
ATOM   5906  C CG  . ASN B 1 397 ? 0.099   -31.249 30.805  1.00 88.73  ? 397 ASN B CG  1 
ATOM   5907  O OD1 . ASN B 1 397 ? 1.028   -31.379 30.008  1.00 88.43  ? 397 ASN B OD1 1 
ATOM   5908  N ND2 . ASN B 1 397 ? -0.322  -32.240 31.583  1.00 87.17  ? 397 ASN B ND2 1 
ATOM   5909  N N   . VAL B 1 398 ? 2.536   -28.964 31.618  1.00 114.59 ? 398 VAL B N   1 
ATOM   5910  C CA  . VAL B 1 398 ? 3.561   -28.947 32.650  1.00 115.91 ? 398 VAL B CA  1 
ATOM   5911  C C   . VAL B 1 398 ? 4.660   -27.987 32.217  1.00 115.03 ? 398 VAL B C   1 
ATOM   5912  O O   . VAL B 1 398 ? 4.919   -27.804 31.023  1.00 113.00 ? 398 VAL B O   1 
ATOM   5913  C CB  . VAL B 1 398 ? 4.122   -30.365 32.905  1.00 117.59 ? 398 VAL B CB  1 
ATOM   5914  C CG1 . VAL B 1 398 ? 4.837   -30.889 31.670  1.00 117.36 ? 398 VAL B CG1 1 
ATOM   5915  C CG2 . VAL B 1 398 ? 5.040   -30.381 34.121  1.00 119.99 ? 398 VAL B CG2 1 
ATOM   5916  N N   . SER B 1 399 ? 5.297   -27.360 33.200  1.00 99.14  ? 399 SER B N   1 
ATOM   5917  C CA  . SER B 1 399 ? 6.370   -26.420 32.912  1.00 95.24  ? 399 SER B CA  1 
ATOM   5918  C C   . SER B 1 399 ? 7.614   -27.149 32.424  1.00 92.05  ? 399 SER B C   1 
ATOM   5919  O O   . SER B 1 399 ? 7.968   -28.217 32.930  1.00 89.65  ? 399 SER B O   1 
ATOM   5920  C CB  . SER B 1 399 ? 6.704   -25.597 34.155  1.00 93.91  ? 399 SER B CB  1 
ATOM   5921  O OG  . SER B 1 399 ? 5.584   -24.845 34.587  1.00 98.12  ? 399 SER B OG  1 
ATOM   5922  N N   . VAL B 1 400 ? 8.277   -26.565 31.429  1.00 86.80  ? 400 VAL B N   1 
ATOM   5923  C CA  . VAL B 1 400 ? 9.516   -27.108 30.897  1.00 79.04  ? 400 VAL B CA  1 
ATOM   5924  C C   . VAL B 1 400 ? 10.618  -26.085 31.128  1.00 81.97  ? 400 VAL B C   1 
ATOM   5925  O O   . VAL B 1 400 ? 10.370  -24.888 31.287  1.00 82.29  ? 400 VAL B O   1 
ATOM   5926  C CB  . VAL B 1 400 ? 9.413   -27.465 29.401  1.00 79.71  ? 400 VAL B CB  1 
ATOM   5927  C CG1 . VAL B 1 400 ? 8.339   -28.515 29.180  1.00 86.22  ? 400 VAL B CG1 1 
ATOM   5928  C CG2 . VAL B 1 400 ? 9.135   -26.221 28.577  1.00 81.79  ? 400 VAL B CG2 1 
ATOM   5929  N N   . GLN B 1 401 ? 11.854  -26.576 31.135  1.00 81.15  ? 401 GLN B N   1 
ATOM   5930  C CA  . GLN B 1 401 ? 13.004  -25.725 31.424  1.00 83.65  ? 401 GLN B CA  1 
ATOM   5931  C C   . GLN B 1 401 ? 14.249  -26.388 30.866  1.00 81.32  ? 401 GLN B C   1 
ATOM   5932  O O   . GLN B 1 401 ? 14.549  -27.533 31.223  1.00 81.75  ? 401 GLN B O   1 
ATOM   5933  C CB  . GLN B 1 401 ? 13.148  -25.498 32.929  1.00 87.03  ? 401 GLN B CB  1 
ATOM   5934  C CG  . GLN B 1 401 ? 14.395  -24.718 33.317  1.00 94.82  ? 401 GLN B CG  1 
ATOM   5935  C CD  . GLN B 1 401 ? 14.573  -24.601 34.820  1.00 96.12  ? 401 GLN B CD  1 
ATOM   5936  O OE1 . GLN B 1 401 ? 13.662  -24.900 35.592  1.00 93.62  ? 401 GLN B OE1 1 
ATOM   5937  N NE2 . GLN B 1 401 ? 15.756  -24.169 35.242  1.00 92.84  ? 401 GLN B NE2 1 
ATOM   5938  N N   . ASP B 1 402 ? 14.974  -25.669 30.014  1.00 78.67  ? 402 ASP B N   1 
ATOM   5939  C CA  . ASP B 1 402 ? 16.262  -26.111 29.485  1.00 80.12  ? 402 ASP B CA  1 
ATOM   5940  C C   . ASP B 1 402 ? 16.149  -27.494 28.841  1.00 79.34  ? 402 ASP B C   1 
ATOM   5941  O O   . ASP B 1 402 ? 16.853  -28.441 29.193  1.00 79.37  ? 402 ASP B O   1 
ATOM   5942  C CB  . ASP B 1 402 ? 17.318  -26.102 30.592  1.00 81.02  ? 402 ASP B CB  1 
ATOM   5943  C CG  . ASP B 1 402 ? 17.442  -24.750 31.263  1.00 79.65  ? 402 ASP B CG  1 
ATOM   5944  O OD1 . ASP B 1 402 ? 17.197  -23.728 30.589  1.00 80.06  ? 402 ASP B OD1 1 
ATOM   5945  O OD2 . ASP B 1 402 ? 17.775  -24.708 32.468  1.00 78.89  ? 402 ASP B OD2 1 
ATOM   5946  N N   . ASP B 1 403 ? 15.239  -27.591 27.876  1.00 77.58  ? 403 ASP B N   1 
ATOM   5947  C CA  . ASP B 1 403 ? 14.997  -28.842 27.173  1.00 78.84  ? 403 ASP B CA  1 
ATOM   5948  C C   . ASP B 1 403 ? 14.576  -28.518 25.747  1.00 78.86  ? 403 ASP B C   1 
ATOM   5949  O O   . ASP B 1 403 ? 14.411  -27.354 25.374  1.00 78.60  ? 403 ASP B O   1 
ATOM   5950  C CB  . ASP B 1 403 ? 13.933  -29.686 27.888  1.00 78.56  ? 403 ASP B CB  1 
ATOM   5951  C CG  . ASP B 1 403 ? 14.041  -31.167 27.563  1.00 82.61  ? 403 ASP B CG  1 
ATOM   5952  O OD1 . ASP B 1 403 ? 14.576  -31.510 26.488  1.00 82.54  ? 403 ASP B OD1 1 
ATOM   5953  O OD2 . ASP B 1 403 ? 13.588  -31.989 28.389  1.00 86.83  ? 403 ASP B OD2 1 
ATOM   5954  N N   . ILE B 1 404 ? 14.411  -29.565 24.945  1.00 78.51  ? 404 ILE B N   1 
ATOM   5955  C CA  . ILE B 1 404 ? 13.962  -29.441 23.563  1.00 72.69  ? 404 ILE B CA  1 
ATOM   5956  C C   . ILE B 1 404 ? 12.787  -30.395 23.408  1.00 72.88  ? 404 ILE B C   1 
ATOM   5957  O O   . ILE B 1 404 ? 12.975  -31.613 23.307  1.00 72.08  ? 404 ILE B O   1 
ATOM   5958  C CB  . ILE B 1 404 ? 15.070  -29.753 22.556  1.00 72.34  ? 404 ILE B CB  1 
ATOM   5959  C CG1 . ILE B 1 404 ? 16.275  -28.846 22.810  1.00 81.24  ? 404 ILE B CG1 1 
ATOM   5960  C CG2 . ILE B 1 404 ? 14.556  -29.571 21.137  1.00 71.66  ? 404 ILE B CG2 1 
ATOM   5961  C CD1 . ILE B 1 404 ? 17.435  -29.097 21.887  1.00 88.67  ? 404 ILE B CD1 1 
ATOM   5962  N N   . ILE B 1 405 ? 11.577  -29.848 23.373  1.00 77.13  ? 405 ILE B N   1 
ATOM   5963  C CA  . ILE B 1 405 ? 10.356  -30.644 23.398  1.00 65.54  ? 405 ILE B CA  1 
ATOM   5964  C C   . ILE B 1 405 ? 9.937   -30.949 21.966  1.00 71.96  ? 405 ILE B C   1 
ATOM   5965  O O   . ILE B 1 405 ? 9.675   -30.035 21.176  1.00 71.02  ? 405 ILE B O   1 
ATOM   5966  C CB  . ILE B 1 405 ? 9.235   -29.918 24.155  1.00 65.08  ? 405 ILE B CB  1 
ATOM   5967  C CG1 . ILE B 1 405 ? 9.542   -29.868 25.654  1.00 69.30  ? 405 ILE B CG1 1 
ATOM   5968  C CG2 . ILE B 1 405 ? 7.900   -30.598 23.906  1.00 71.50  ? 405 ILE B CG2 1 
ATOM   5969  C CD1 . ILE B 1 405 ? 10.388  -28.684 26.075  1.00 73.06  ? 405 ILE B CD1 1 
ATOM   5970  N N   . LEU B 1 406 ? 9.859   -32.236 21.640  1.00 67.69  ? 406 LEU B N   1 
ATOM   5971  C CA  . LEU B 1 406 ? 9.455   -32.681 20.313  1.00 71.04  ? 406 LEU B CA  1 
ATOM   5972  C C   . LEU B 1 406 ? 7.941   -32.837 20.214  1.00 77.08  ? 406 LEU B C   1 
ATOM   5973  O O   . LEU B 1 406 ? 7.323   -33.508 21.040  1.00 75.91  ? 406 LEU B O   1 
ATOM   5974  C CB  . LEU B 1 406 ? 10.136  -34.007 19.970  1.00 69.52  ? 406 LEU B CB  1 
ATOM   5975  C CG  . LEU B 1 406 ? 11.663  -34.043 20.026  1.00 65.78  ? 406 LEU B CG  1 
ATOM   5976  C CD1 . LEU B 1 406 ? 12.178  -35.439 19.710  1.00 67.56  ? 406 LEU B CD1 1 
ATOM   5977  C CD2 . LEU B 1 406 ? 12.256  -33.021 19.071  1.00 70.09  ? 406 LEU B CD2 1 
ATOM   5978  O OXT . LEU B 1 406 ? 7.302   -32.316 19.301  1.00 82.42  ? 406 LEU B OXT 1 
ATOM   5979  N N   . GLU C 1 4   ? 40.566  -90.134 61.319  1.00 225.05 ? 4   GLU C N   1 
ATOM   5980  C CA  . GLU C 1 4   ? 40.479  -89.544 59.989  1.00 229.84 ? 4   GLU C CA  1 
ATOM   5981  C C   . GLU C 1 4   ? 41.660  -88.623 59.704  1.00 240.35 ? 4   GLU C C   1 
ATOM   5982  O O   . GLU C 1 4   ? 42.577  -88.498 60.516  1.00 238.25 ? 4   GLU C O   1 
ATOM   5983  C CB  . GLU C 1 4   ? 39.173  -88.760 59.832  1.00 218.78 ? 4   GLU C CB  1 
ATOM   5984  C CG  . GLU C 1 4   ? 37.912  -89.600 59.894  1.00 209.42 ? 4   GLU C CG  1 
ATOM   5985  C CD  . GLU C 1 4   ? 36.659  -88.771 59.695  1.00 200.62 ? 4   GLU C CD  1 
ATOM   5986  O OE1 . GLU C 1 4   ? 36.771  -87.527 59.652  1.00 197.92 ? 4   GLU C OE1 1 
ATOM   5987  O OE2 . GLU C 1 4   ? 35.565  -89.360 59.575  1.00 200.84 ? 4   GLU C OE2 1 
ATOM   5988  N N   . LYS C 1 5   ? 41.625  -87.980 58.539  1.00 257.23 ? 5   LYS C N   1 
ATOM   5989  C CA  . LYS C 1 5   ? 42.627  -86.997 58.155  1.00 255.69 ? 5   LYS C CA  1 
ATOM   5990  C C   . LYS C 1 5   ? 41.958  -85.936 57.296  1.00 255.27 ? 5   LYS C C   1 
ATOM   5991  O O   . LYS C 1 5   ? 41.082  -86.249 56.485  1.00 255.74 ? 5   LYS C O   1 
ATOM   5992  C CB  . LYS C 1 5   ? 43.797  -87.636 57.397  1.00 255.12 ? 5   LYS C CB  1 
ATOM   5993  C CG  . LYS C 1 5   ? 45.134  -86.949 57.641  1.00 256.42 ? 5   LYS C CG  1 
ATOM   5994  C CD  . LYS C 1 5   ? 46.241  -87.577 56.809  1.00 260.26 ? 5   LYS C CD  1 
ATOM   5995  C CE  . LYS C 1 5   ? 47.611  -87.099 57.266  1.00 260.00 ? 5   LYS C CE  1 
ATOM   5996  N NZ  . LYS C 1 5   ? 47.777  -87.204 58.743  1.00 256.12 ? 5   LYS C NZ  1 
ATOM   5997  N N   . VAL C 1 6   ? 42.372  -84.685 57.479  1.00 234.57 ? 6   VAL C N   1 
ATOM   5998  C CA  . VAL C 1 6   ? 41.764  -83.545 56.807  1.00 225.69 ? 6   VAL C CA  1 
ATOM   5999  C C   . VAL C 1 6   ? 42.850  -82.779 56.066  1.00 218.74 ? 6   VAL C C   1 
ATOM   6000  O O   . VAL C 1 6   ? 43.943  -82.556 56.599  1.00 216.83 ? 6   VAL C O   1 
ATOM   6001  C CB  . VAL C 1 6   ? 41.021  -82.624 57.799  1.00 218.65 ? 6   VAL C CB  1 
ATOM   6002  C CG1 . VAL C 1 6   ? 40.392  -81.448 57.069  1.00 208.55 ? 6   VAL C CG1 1 
ATOM   6003  C CG2 . VAL C 1 6   ? 39.954  -83.405 58.544  1.00 215.34 ? 6   VAL C CG2 1 
ATOM   6004  N N   . VAL C 1 7   ? 42.548  -82.388 54.829  1.00 213.43 ? 7   VAL C N   1 
ATOM   6005  C CA  . VAL C 1 7   ? 43.436  -81.567 54.020  1.00 205.89 ? 7   VAL C CA  1 
ATOM   6006  C C   . VAL C 1 7   ? 42.699  -80.277 53.678  1.00 199.31 ? 7   VAL C C   1 
ATOM   6007  O O   . VAL C 1 7   ? 41.467  -80.217 53.683  1.00 198.37 ? 7   VAL C O   1 
ATOM   6008  C CB  . VAL C 1 7   ? 43.905  -82.301 52.743  1.00 204.41 ? 7   VAL C CB  1 
ATOM   6009  C CG1 . VAL C 1 7   ? 42.789  -82.357 51.708  1.00 197.03 ? 7   VAL C CG1 1 
ATOM   6010  C CG2 . VAL C 1 7   ? 45.158  -81.655 52.165  1.00 202.94 ? 7   VAL C CG2 1 
ATOM   6011  N N   . ALA C 1 8   ? 43.472  -79.232 53.389  1.00 197.54 ? 8   ALA C N   1 
ATOM   6012  C CA  . ALA C 1 8   ? 42.919  -77.915 53.107  1.00 190.10 ? 8   ALA C CA  1 
ATOM   6013  C C   . ALA C 1 8   ? 43.506  -77.380 51.812  1.00 197.91 ? 8   ALA C C   1 
ATOM   6014  O O   . ALA C 1 8   ? 44.721  -77.443 51.601  1.00 202.92 ? 8   ALA C O   1 
ATOM   6015  C CB  . ALA C 1 8   ? 43.199  -76.940 54.256  1.00 184.89 ? 8   ALA C CB  1 
ATOM   6016  N N   . VAL C 1 9   ? 42.637  -76.855 50.950  1.00 205.99 ? 9   VAL C N   1 
ATOM   6017  C CA  . VAL C 1 9   ? 43.032  -76.259 49.679  1.00 210.51 ? 9   VAL C CA  1 
ATOM   6018  C C   . VAL C 1 9   ? 42.401  -74.877 49.599  1.00 209.67 ? 9   VAL C C   1 
ATOM   6019  O O   . VAL C 1 9   ? 41.177  -74.743 49.710  1.00 203.62 ? 9   VAL C O   1 
ATOM   6020  C CB  . VAL C 1 9   ? 42.607  -77.118 48.476  1.00 212.73 ? 9   VAL C CB  1 
ATOM   6021  C CG1 . VAL C 1 9   ? 42.975  -76.424 47.174  1.00 213.94 ? 9   VAL C CG1 1 
ATOM   6022  C CG2 . VAL C 1 9   ? 43.251  -78.495 48.553  1.00 214.32 ? 9   VAL C CG2 1 
ATOM   6023  N N   . ILE C 1 10  ? 43.230  -73.856 49.408  1.00 213.32 ? 10  ILE C N   1 
ATOM   6024  C CA  . ILE C 1 10  ? 42.784  -72.471 49.343  1.00 210.27 ? 10  ILE C CA  1 
ATOM   6025  C C   . ILE C 1 10  ? 42.976  -71.968 47.919  1.00 230.51 ? 10  ILE C C   1 
ATOM   6026  O O   . ILE C 1 10  ? 44.050  -72.144 47.332  1.00 226.11 ? 10  ILE C O   1 
ATOM   6027  C CB  . ILE C 1 10  ? 43.548  -71.588 50.345  1.00 200.31 ? 10  ILE C CB  1 
ATOM   6028  C CG1 . ILE C 1 10  ? 43.398  -72.134 51.769  1.00 186.24 ? 10  ILE C CG1 1 
ATOM   6029  C CG2 . ILE C 1 10  ? 43.070  -70.144 50.265  1.00 195.00 ? 10  ILE C CG2 1 
ATOM   6030  C CD1 . ILE C 1 10  ? 44.127  -71.325 52.818  1.00 176.90 ? 10  ILE C CD1 1 
ATOM   6031  N N   . MET C 1 11  ? 41.938  -71.342 47.369  1.00 292.56 ? 11  MET C N   1 
ATOM   6032  C CA  . MET C 1 11  ? 42.051  -70.687 46.074  1.00 290.70 ? 11  MET C CA  1 
ATOM   6033  C C   . MET C 1 11  ? 42.797  -69.367 46.207  1.00 288.47 ? 11  MET C C   1 
ATOM   6034  O O   . MET C 1 11  ? 42.656  -68.655 47.205  1.00 288.51 ? 11  MET C O   1 
ATOM   6035  C CB  . MET C 1 11  ? 40.669  -70.443 45.466  1.00 292.22 ? 11  MET C CB  1 
ATOM   6036  C CG  . MET C 1 11  ? 39.987  -71.690 44.939  1.00 294.13 ? 11  MET C CG  1 
ATOM   6037  S SD  . MET C 1 11  ? 40.867  -72.370 43.522  1.00 302.04 ? 11  MET C SD  1 
ATOM   6038  C CE  . MET C 1 11  ? 39.861  -73.805 43.155  1.00 295.39 ? 11  MET C CE  1 
ATOM   6039  N N   . VAL C 1 12  ? 43.590  -69.043 45.189  1.00 253.80 ? 12  VAL C N   1 
ATOM   6040  C CA  . VAL C 1 12  ? 44.441  -67.861 45.188  1.00 248.28 ? 12  VAL C CA  1 
ATOM   6041  C C   . VAL C 1 12  ? 44.085  -66.917 44.047  1.00 243.16 ? 12  VAL C C   1 
ATOM   6042  O O   . VAL C 1 12  ? 43.942  -65.707 44.247  1.00 243.24 ? 12  VAL C O   1 
ATOM   6043  C CB  . VAL C 1 12  ? 45.937  -68.249 45.127  1.00 245.56 ? 12  VAL C CB  1 
ATOM   6044  C CG1 . VAL C 1 12  ? 46.788  -67.034 44.812  1.00 244.47 ? 12  VAL C CG1 1 
ATOM   6045  C CG2 . VAL C 1 12  ? 46.373  -68.891 46.433  1.00 246.37 ? 12  VAL C CG2 1 
ATOM   6046  N N   . GLY C 1 13  ? 43.924  -67.455 42.843  1.00 221.55 ? 13  GLY C N   1 
ATOM   6047  C CA  . GLY C 1 13  ? 43.702  -66.635 41.674  1.00 199.53 ? 13  GLY C CA  1 
ATOM   6048  C C   . GLY C 1 13  ? 45.010  -66.098 41.124  1.00 199.84 ? 13  GLY C C   1 
ATOM   6049  O O   . GLY C 1 13  ? 46.071  -66.185 41.742  1.00 200.72 ? 13  GLY C O   1 
ATOM   6050  N N   . GLY C 1 14  ? 44.928  -65.538 39.924  1.00 187.53 ? 14  GLY C N   1 
ATOM   6051  C CA  . GLY C 1 14  ? 46.096  -65.021 39.255  1.00 187.86 ? 14  GLY C CA  1 
ATOM   6052  C C   . GLY C 1 14  ? 46.068  -63.516 39.104  1.00 174.59 ? 14  GLY C C   1 
ATOM   6053  O O   . GLY C 1 14  ? 45.235  -62.821 39.696  1.00 166.26 ? 14  GLY C O   1 
ATOM   6054  N N   . PRO C 1 15  ? 46.989  -62.981 38.297  1.00 175.55 ? 15  PRO C N   1 
ATOM   6055  C CA  . PRO C 1 15  ? 47.080  -61.523 38.132  1.00 170.58 ? 15  PRO C CA  1 
ATOM   6056  C C   . PRO C 1 15  ? 45.899  -60.902 37.403  1.00 163.17 ? 15  PRO C C   1 
ATOM   6057  O O   . PRO C 1 15  ? 45.849  -59.672 37.284  1.00 158.72 ? 15  PRO C O   1 
ATOM   6058  C CB  . PRO C 1 15  ? 48.380  -61.347 37.333  1.00 171.26 ? 15  PRO C CB  1 
ATOM   6059  C CG  . PRO C 1 15  ? 48.540  -62.632 36.596  1.00 175.26 ? 15  PRO C CG  1 
ATOM   6060  C CD  . PRO C 1 15  ? 48.006  -63.697 37.508  1.00 182.04 ? 15  PRO C CD  1 
ATOM   6061  N N   . THR C 1 16  ? 44.951  -61.699 36.912  1.00 159.44 ? 16  THR C N   1 
ATOM   6062  C CA  . THR C 1 16  ? 43.765  -61.168 36.253  1.00 150.44 ? 16  THR C CA  1 
ATOM   6063  C C   . THR C 1 16  ? 42.595  -60.960 37.207  1.00 141.92 ? 16  THR C C   1 
ATOM   6064  O O   . THR C 1 16  ? 41.614  -60.312 36.827  1.00 133.21 ? 16  THR C O   1 
ATOM   6065  C CB  . THR C 1 16  ? 43.328  -62.096 35.111  1.00 153.16 ? 16  THR C CB  1 
ATOM   6066  O OG1 . THR C 1 16  ? 43.077  -63.408 35.627  1.00 155.84 ? 16  THR C OG1 1 
ATOM   6067  C CG2 . THR C 1 16  ? 44.409  -62.174 34.045  1.00 150.46 ? 16  THR C CG2 1 
ATOM   6068  N N   . LYS C 1 17  ? 42.677  -61.485 38.429  1.00 142.55 ? 17  LYS C N   1 
ATOM   6069  C CA  . LYS C 1 17  ? 41.659  -61.247 39.446  1.00 135.97 ? 17  LYS C CA  1 
ATOM   6070  C C   . LYS C 1 17  ? 41.988  -60.029 40.299  1.00 132.08 ? 17  LYS C C   1 
ATOM   6071  O O   . LYS C 1 17  ? 41.099  -59.226 40.602  1.00 125.09 ? 17  LYS C O   1 
ATOM   6072  C CB  . LYS C 1 17  ? 41.493  -62.481 40.338  1.00 136.10 ? 17  LYS C CB  1 
ATOM   6073  C CG  . LYS C 1 17  ? 41.354  -63.785 39.572  1.00 138.97 ? 17  LYS C CG  1 
ATOM   6074  C CD  . LYS C 1 17  ? 40.145  -63.754 38.651  1.00 125.91 ? 17  LYS C CD  1 
ATOM   6075  C CE  . LYS C 1 17  ? 40.024  -65.041 37.856  1.00 127.96 ? 17  LYS C CE  1 
ATOM   6076  N NZ  . LYS C 1 17  ? 39.910  -66.226 38.748  1.00 127.64 ? 17  LYS C NZ  1 
ATOM   6077  N N   . GLY C 1 18  ? 43.253  -59.871 40.686  1.00 136.20 ? 18  GLY C N   1 
ATOM   6078  C CA  . GLY C 1 18  ? 43.688  -58.703 41.425  1.00 133.46 ? 18  GLY C CA  1 
ATOM   6079  C C   . GLY C 1 18  ? 43.838  -57.472 40.555  1.00 126.97 ? 18  GLY C C   1 
ATOM   6080  O O   . GLY C 1 18  ? 44.620  -56.569 40.868  1.00 122.60 ? 18  GLY C O   1 
ATOM   6081  N N   . THR C 1 19  ? 43.089  -57.427 39.454  1.00 134.60 ? 19  THR C N   1 
ATOM   6082  C CA  . THR C 1 19  ? 43.081  -56.280 38.557  1.00 129.74 ? 19  THR C CA  1 
ATOM   6083  C C   . THR C 1 19  ? 42.230  -55.132 39.082  1.00 125.01 ? 19  THR C C   1 
ATOM   6084  O O   . THR C 1 19  ? 42.071  -54.128 38.380  1.00 120.14 ? 19  THR C O   1 
ATOM   6085  C CB  . THR C 1 19  ? 42.583  -56.694 37.170  1.00 129.43 ? 19  THR C CB  1 
ATOM   6086  O OG1 . THR C 1 19  ? 42.728  -55.597 36.259  1.00 117.95 ? 19  THR C OG1 1 
ATOM   6087  C CG2 . THR C 1 19  ? 41.118  -57.099 37.233  1.00 132.17 ? 19  THR C CG2 1 
ATOM   6088  N N   . ARG C 1 20  ? 41.664  -55.267 40.280  1.00 119.28 ? 20  ARG C N   1 
ATOM   6089  C CA  . ARG C 1 20  ? 40.972  -54.171 40.939  1.00 117.11 ? 20  ARG C CA  1 
ATOM   6090  C C   . ARG C 1 20  ? 41.816  -53.497 42.010  1.00 121.18 ? 20  ARG C C   1 
ATOM   6091  O O   . ARG C 1 20  ? 41.568  -52.330 42.332  1.00 123.32 ? 20  ARG C O   1 
ATOM   6092  C CB  . ARG C 1 20  ? 39.671  -54.677 41.566  1.00 120.03 ? 20  ARG C CB  1 
ATOM   6093  C CG  . ARG C 1 20  ? 39.298  -56.087 41.137  1.00 120.17 ? 20  ARG C CG  1 
ATOM   6094  C CD  . ARG C 1 20  ? 37.844  -56.148 40.730  1.00 121.99 ? 20  ARG C CD  1 
ATOM   6095  N NE  . ARG C 1 20  ? 37.029  -55.293 41.584  1.00 123.57 ? 20  ARG C NE  1 
ATOM   6096  C CZ  . ARG C 1 20  ? 35.724  -55.103 41.425  1.00 121.47 ? 20  ARG C CZ  1 
ATOM   6097  N NH1 . ARG C 1 20  ? 35.078  -55.713 40.441  1.00 118.96 ? 20  ARG C NH1 1 
ATOM   6098  N NH2 . ARG C 1 20  ? 35.065  -54.303 42.252  1.00 123.61 ? 20  ARG C NH2 1 
ATOM   6099  N N   . PHE C 1 21  ? 42.796  -54.207 42.564  1.00 124.28 ? 21  PHE C N   1 
ATOM   6100  C CA  . PHE C 1 21  ? 43.720  -53.674 43.553  1.00 125.99 ? 21  PHE C CA  1 
ATOM   6101  C C   . PHE C 1 21  ? 44.955  -53.048 42.913  1.00 129.23 ? 21  PHE C C   1 
ATOM   6102  O O   . PHE C 1 21  ? 46.002  -52.968 43.566  1.00 141.53 ? 21  PHE C O   1 
ATOM   6103  C CB  . PHE C 1 21  ? 44.140  -54.776 44.530  1.00 131.57 ? 21  PHE C CB  1 
ATOM   6104  C CG  . PHE C 1 21  ? 43.019  -55.296 45.397  1.00 132.79 ? 21  PHE C CG  1 
ATOM   6105  C CD1 . PHE C 1 21  ? 43.027  -55.077 46.764  1.00 138.18 ? 21  PHE C CD1 1 
ATOM   6106  C CD2 . PHE C 1 21  ? 41.962  -56.007 44.847  1.00 132.41 ? 21  PHE C CD2 1 
ATOM   6107  C CE1 . PHE C 1 21  ? 42.007  -55.554 47.565  1.00 141.15 ? 21  PHE C CE1 1 
ATOM   6108  C CE2 . PHE C 1 21  ? 40.937  -56.480 45.642  1.00 135.75 ? 21  PHE C CE2 1 
ATOM   6109  C CZ  . PHE C 1 21  ? 40.960  -56.255 47.002  1.00 140.82 ? 21  PHE C CZ  1 
ATOM   6110  N N   . ARG C 1 22  ? 44.852  -52.621 41.647  1.00 121.30 ? 22  ARG C N   1 
ATOM   6111  C CA  . ARG C 1 22  ? 45.953  -52.194 40.783  1.00 121.02 ? 22  ARG C CA  1 
ATOM   6112  C C   . ARG C 1 22  ? 47.044  -51.394 41.494  1.00 133.92 ? 22  ARG C C   1 
ATOM   6113  O O   . ARG C 1 22  ? 48.217  -51.782 41.406  1.00 140.26 ? 22  ARG C O   1 
ATOM   6114  C CB  . ARG C 1 22  ? 45.419  -51.399 39.587  1.00 106.16 ? 22  ARG C CB  1 
ATOM   6115  C CG  . ARG C 1 22  ? 44.505  -52.197 38.701  1.00 103.70 ? 22  ARG C CG  1 
ATOM   6116  C CD  . ARG C 1 22  ? 45.235  -53.425 38.200  1.00 107.07 ? 22  ARG C CD  1 
ATOM   6117  N NE  . ARG C 1 22  ? 46.223  -53.088 37.182  1.00 100.97 ? 22  ARG C NE  1 
ATOM   6118  C CZ  . ARG C 1 22  ? 46.052  -53.284 35.880  1.00 91.50  ? 22  ARG C CZ  1 
ATOM   6119  N NH1 . ARG C 1 22  ? 44.925  -53.821 35.431  1.00 93.50  ? 22  ARG C NH1 1 
ATOM   6120  N NH2 . ARG C 1 22  ? 47.009  -52.946 35.026  1.00 87.02  ? 22  ARG C NH2 1 
ATOM   6121  N N   . PRO C 1 23  ? 46.735  -50.272 42.166  1.00 133.92 ? 23  PRO C N   1 
ATOM   6122  C CA  . PRO C 1 23  ? 47.821  -49.513 42.811  1.00 145.61 ? 23  PRO C CA  1 
ATOM   6123  C C   . PRO C 1 23  ? 48.646  -50.363 43.764  1.00 160.60 ? 23  PRO C C   1 
ATOM   6124  O O   . PRO C 1 23  ? 49.876  -50.228 43.813  1.00 156.43 ? 23  PRO C O   1 
ATOM   6125  C CB  . PRO C 1 23  ? 47.083  -48.382 43.541  1.00 135.21 ? 23  PRO C CB  1 
ATOM   6126  C CG  . PRO C 1 23  ? 45.678  -48.827 43.646  1.00 128.72 ? 23  PRO C CG  1 
ATOM   6127  C CD  . PRO C 1 23  ? 45.417  -49.668 42.444  1.00 121.01 ? 23  PRO C CD  1 
ATOM   6128  N N   . LEU C 1 24  ? 47.992  -51.236 44.528  1.00 214.60 ? 24  LEU C N   1 
ATOM   6129  C CA  . LEU C 1 24  ? 48.680  -52.149 45.430  1.00 215.63 ? 24  LEU C CA  1 
ATOM   6130  C C   . LEU C 1 24  ? 49.062  -53.467 44.771  1.00 215.49 ? 24  LEU C C   1 
ATOM   6131  O O   . LEU C 1 24  ? 50.074  -54.067 45.152  1.00 215.56 ? 24  LEU C O   1 
ATOM   6132  C CB  . LEU C 1 24  ? 47.798  -52.432 46.649  1.00 218.06 ? 24  LEU C CB  1 
ATOM   6133  C CG  . LEU C 1 24  ? 46.943  -51.255 47.130  1.00 218.38 ? 24  LEU C CG  1 
ATOM   6134  C CD1 . LEU C 1 24  ? 45.778  -51.740 47.981  1.00 220.74 ? 24  LEU C CD1 1 
ATOM   6135  C CD2 . LEU C 1 24  ? 47.781  -50.238 47.891  1.00 217.65 ? 24  LEU C CD2 1 
ATOM   6136  N N   . SER C 1 25  ? 48.276  -53.933 43.797  1.00 162.37 ? 25  SER C N   1 
ATOM   6137  C CA  . SER C 1 25  ? 48.560  -55.210 43.148  1.00 153.53 ? 25  SER C CA  1 
ATOM   6138  C C   . SER C 1 25  ? 49.888  -55.202 42.399  1.00 150.98 ? 25  SER C C   1 
ATOM   6139  O O   . SER C 1 25  ? 50.505  -56.260 42.224  1.00 150.88 ? 25  SER C O   1 
ATOM   6140  C CB  . SER C 1 25  ? 47.419  -55.573 42.200  1.00 143.53 ? 25  SER C CB  1 
ATOM   6141  O OG  . SER C 1 25  ? 46.436  -56.338 42.872  1.00 146.10 ? 25  SER C OG  1 
ATOM   6142  N N   . PHE C 1 26  ? 50.341  -54.032 41.943  1.00 144.88 ? 26  PHE C N   1 
ATOM   6143  C CA  . PHE C 1 26  ? 51.599  -53.968 41.205  1.00 140.40 ? 26  PHE C CA  1 
ATOM   6144  C C   . PHE C 1 26  ? 52.788  -54.363 42.072  1.00 148.28 ? 26  PHE C C   1 
ATOM   6145  O O   . PHE C 1 26  ? 53.749  -54.959 41.570  1.00 140.12 ? 26  PHE C O   1 
ATOM   6146  C CB  . PHE C 1 26  ? 51.796  -52.564 40.636  1.00 129.84 ? 26  PHE C CB  1 
ATOM   6147  C CG  . PHE C 1 26  ? 50.881  -52.244 39.492  1.00 123.94 ? 26  PHE C CG  1 
ATOM   6148  C CD1 . PHE C 1 26  ? 50.410  -50.955 39.308  1.00 125.82 ? 26  PHE C CD1 1 
ATOM   6149  C CD2 . PHE C 1 26  ? 50.490  -53.230 38.599  1.00 117.99 ? 26  PHE C CD2 1 
ATOM   6150  C CE1 . PHE C 1 26  ? 49.566  -50.654 38.259  1.00 114.75 ? 26  PHE C CE1 1 
ATOM   6151  C CE2 . PHE C 1 26  ? 49.645  -52.934 37.545  1.00 112.98 ? 26  PHE C CE2 1 
ATOM   6152  C CZ  . PHE C 1 26  ? 49.183  -51.643 37.375  1.00 109.51 ? 26  PHE C CZ  1 
ATOM   6153  N N   . ASN C 1 27  ? 52.741  -54.055 43.366  1.00 161.61 ? 27  ASN C N   1 
ATOM   6154  C CA  . ASN C 1 27  ? 53.807  -54.435 44.285  1.00 164.83 ? 27  ASN C CA  1 
ATOM   6155  C C   . ASN C 1 27  ? 53.539  -55.786 44.937  1.00 169.22 ? 27  ASN C C   1 
ATOM   6156  O O   . ASN C 1 27  ? 54.423  -56.647 44.979  1.00 173.53 ? 27  ASN C O   1 
ATOM   6157  C CB  . ASN C 1 27  ? 53.990  -53.361 45.362  1.00 175.65 ? 27  ASN C CB  1 
ATOM   6158  C CG  . ASN C 1 27  ? 55.133  -53.676 46.311  1.00 182.58 ? 27  ASN C CG  1 
ATOM   6159  O OD1 . ASN C 1 27  ? 56.303  -53.493 45.974  1.00 191.29 ? 27  ASN C OD1 1 
ATOM   6160  N ND2 . ASN C 1 27  ? 54.798  -54.155 47.504  1.00 182.48 ? 27  ASN C ND2 1 
ATOM   6161  N N   . THR C 1 28  ? 52.324  -55.985 45.444  1.00 163.61 ? 28  THR C N   1 
ATOM   6162  C CA  . THR C 1 28  ? 51.968  -57.198 46.156  1.00 165.61 ? 28  THR C CA  1 
ATOM   6163  C C   . THR C 1 28  ? 50.647  -57.729 45.613  1.00 164.99 ? 28  THR C C   1 
ATOM   6164  O O   . THR C 1 28  ? 49.662  -56.974 45.530  1.00 165.72 ? 28  THR C O   1 
ATOM   6165  C CB  . THR C 1 28  ? 51.852  -56.928 47.664  1.00 169.64 ? 28  THR C CB  1 
ATOM   6166  O OG1 . THR C 1 28  ? 53.156  -56.703 48.214  1.00 172.40 ? 28  THR C OG1 1 
ATOM   6167  C CG2 . THR C 1 28  ? 51.199  -58.100 48.375  1.00 173.85 ? 28  THR C CG2 1 
ATOM   6168  N N   . PRO C 1 29  ? 50.580  -59.005 45.240  1.00 171.46 ? 29  PRO C N   1 
ATOM   6169  C CA  . PRO C 1 29  ? 49.323  -59.566 44.739  1.00 175.86 ? 29  PRO C CA  1 
ATOM   6170  C C   . PRO C 1 29  ? 48.218  -59.486 45.781  1.00 193.40 ? 29  PRO C C   1 
ATOM   6171  O O   . PRO C 1 29  ? 48.459  -59.291 46.974  1.00 199.76 ? 29  PRO C O   1 
ATOM   6172  C CB  . PRO C 1 29  ? 49.685  -61.021 44.421  1.00 186.54 ? 29  PRO C CB  1 
ATOM   6173  C CG  . PRO C 1 29  ? 51.161  -61.004 44.202  1.00 183.42 ? 29  PRO C CG  1 
ATOM   6174  C CD  . PRO C 1 29  ? 51.693  -59.965 45.144  1.00 174.97 ? 29  PRO C CD  1 
ATOM   6175  N N   . LYS C 1 30  ? 46.984  -59.638 45.301  1.00 193.35 ? 30  LYS C N   1 
ATOM   6176  C CA  . LYS C 1 30  ? 45.801  -59.547 46.157  1.00 204.88 ? 30  LYS C CA  1 
ATOM   6177  C C   . LYS C 1 30  ? 45.863  -60.432 47.399  1.00 233.61 ? 30  LYS C C   1 
ATOM   6178  O O   . LYS C 1 30  ? 45.613  -59.917 48.501  1.00 231.77 ? 30  LYS C O   1 
ATOM   6179  C CB  . LYS C 1 30  ? 44.554  -59.869 45.321  1.00 182.31 ? 30  LYS C CB  1 
ATOM   6180  C CG  . LYS C 1 30  ? 43.238  -59.645 46.045  1.00 170.94 ? 30  LYS C CG  1 
ATOM   6181  C CD  . LYS C 1 30  ? 42.201  -60.677 45.630  1.00 160.80 ? 30  LYS C CD  1 
ATOM   6182  C CE  . LYS C 1 30  ? 40.839  -60.045 45.398  1.00 141.75 ? 30  LYS C CE  1 
ATOM   6183  N NZ  . LYS C 1 30  ? 40.813  -59.242 44.143  1.00 137.38 ? 30  LYS C NZ  1 
ATOM   6184  N N   . PRO C 1 31  ? 46.177  -61.733 47.315  1.00 320.70 ? 31  PRO C N   1 
ATOM   6185  C CA  . PRO C 1 31  ? 46.098  -62.577 48.521  1.00 322.34 ? 31  PRO C CA  1 
ATOM   6186  C C   . PRO C 1 31  ? 47.106  -62.215 49.598  1.00 321.53 ? 31  PRO C C   1 
ATOM   6187  O O   . PRO C 1 31  ? 46.907  -62.601 50.757  1.00 322.97 ? 31  PRO C O   1 
ATOM   6188  C CB  . PRO C 1 31  ? 46.350  -63.994 47.983  1.00 323.30 ? 31  PRO C CB  1 
ATOM   6189  C CG  . PRO C 1 31  ? 46.129  -63.900 46.511  1.00 322.30 ? 31  PRO C CG  1 
ATOM   6190  C CD  . PRO C 1 31  ? 46.580  -62.529 46.142  1.00 320.01 ? 31  PRO C CD  1 
ATOM   6191  N N   . LEU C 1 32  ? 48.182  -61.509 49.263  1.00 241.05 ? 32  LEU C N   1 
ATOM   6192  C CA  . LEU C 1 32  ? 49.231  -61.190 50.220  1.00 220.64 ? 32  LEU C CA  1 
ATOM   6193  C C   . LEU C 1 32  ? 49.104  -59.776 50.770  1.00 216.40 ? 32  LEU C C   1 
ATOM   6194  O O   . LEU C 1 32  ? 49.986  -59.326 51.507  1.00 210.74 ? 32  LEU C O   1 
ATOM   6195  C CB  . LEU C 1 32  ? 50.605  -61.391 49.582  1.00 206.47 ? 32  LEU C CB  1 
ATOM   6196  C CG  . LEU C 1 32  ? 50.763  -62.649 48.728  1.00 214.49 ? 32  LEU C CG  1 
ATOM   6197  C CD1 . LEU C 1 32  ? 52.138  -62.687 48.085  1.00 206.10 ? 32  LEU C CD1 1 
ATOM   6198  C CD2 . LEU C 1 32  ? 50.523  -63.902 49.559  1.00 211.41 ? 32  LEU C CD2 1 
ATOM   6199  N N   . ILE C 1 33  ? 48.031  -59.074 50.432  1.00 211.70 ? 33  ILE C N   1 
ATOM   6200  C CA  . ILE C 1 33  ? 47.849  -57.697 50.904  1.00 209.83 ? 33  ILE C CA  1 
ATOM   6201  C C   . ILE C 1 33  ? 47.463  -57.721 52.378  1.00 213.56 ? 33  ILE C C   1 
ATOM   6202  O O   . ILE C 1 33  ? 46.504  -58.420 52.753  1.00 213.98 ? 33  ILE C O   1 
ATOM   6203  C CB  . ILE C 1 33  ? 46.783  -56.988 50.069  1.00 205.83 ? 33  ILE C CB  1 
ATOM   6204  C CG1 . ILE C 1 33  ? 47.246  -56.850 48.618  1.00 192.43 ? 33  ILE C CG1 1 
ATOM   6205  C CG2 . ILE C 1 33  ? 46.451  -55.628 50.665  1.00 214.24 ? 33  ILE C CG2 1 
ATOM   6206  C CD1 . ILE C 1 33  ? 46.232  -56.193 47.714  1.00 178.88 ? 33  ILE C CD1 1 
ATOM   6207  N N   . PRO C 1 34  ? 48.166  -56.988 53.247  1.00 224.55 ? 34  PRO C N   1 
ATOM   6208  C CA  . PRO C 1 34  ? 47.909  -57.108 54.689  1.00 226.52 ? 34  PRO C CA  1 
ATOM   6209  C C   . PRO C 1 34  ? 46.551  -56.560 55.096  1.00 221.21 ? 34  PRO C C   1 
ATOM   6210  O O   . PRO C 1 34  ? 46.294  -55.357 54.983  1.00 212.86 ? 34  PRO C O   1 
ATOM   6211  C CB  . PRO C 1 34  ? 49.051  -56.296 55.321  1.00 225.01 ? 34  PRO C CB  1 
ATOM   6212  C CG  . PRO C 1 34  ? 50.090  -56.183 54.250  1.00 218.19 ? 34  PRO C CG  1 
ATOM   6213  C CD  . PRO C 1 34  ? 49.329  -56.132 52.965  1.00 220.33 ? 34  PRO C CD  1 
ATOM   6214  N N   . LEU C 1 35  ? 45.677  -57.441 55.575  1.00 214.26 ? 35  LEU C N   1 
ATOM   6215  C CA  . LEU C 1 35  ? 44.395  -57.052 56.147  1.00 204.69 ? 35  LEU C CA  1 
ATOM   6216  C C   . LEU C 1 35  ? 44.500  -57.159 57.662  1.00 201.96 ? 35  LEU C C   1 
ATOM   6217  O O   . LEU C 1 35  ? 44.813  -58.232 58.190  1.00 207.38 ? 35  LEU C O   1 
ATOM   6218  C CB  . LEU C 1 35  ? 43.266  -57.931 55.609  1.00 199.57 ? 35  LEU C CB  1 
ATOM   6219  C CG  . LEU C 1 35  ? 42.924  -57.720 54.132  1.00 200.31 ? 35  LEU C CG  1 
ATOM   6220  C CD1 . LEU C 1 35  ? 41.703  -58.534 53.732  1.00 201.71 ? 35  LEU C CD1 1 
ATOM   6221  C CD2 . LEU C 1 35  ? 42.709  -56.244 53.839  1.00 183.57 ? 35  LEU C CD2 1 
ATOM   6222  N N   . ALA C 1 36  ? 44.240  -56.048 58.354  1.00 190.85 ? 36  ALA C N   1 
ATOM   6223  C CA  . ALA C 1 36  ? 44.392  -55.966 59.807  1.00 185.59 ? 36  ALA C CA  1 
ATOM   6224  C C   . ALA C 1 36  ? 45.807  -56.336 60.245  1.00 192.66 ? 36  ALA C C   1 
ATOM   6225  O O   . ALA C 1 36  ? 46.004  -56.937 61.304  1.00 192.59 ? 36  ALA C O   1 
ATOM   6226  C CB  . ALA C 1 36  ? 43.359  -56.836 60.530  1.00 172.65 ? 36  ALA C CB  1 
ATOM   6227  N N   . GLY C 1 37  ? 46.802  -55.982 59.428  1.00 206.90 ? 37  GLY C N   1 
ATOM   6228  C CA  . GLY C 1 37  ? 48.196  -56.228 59.712  1.00 211.08 ? 37  GLY C CA  1 
ATOM   6229  C C   . GLY C 1 37  ? 48.758  -57.487 59.080  1.00 234.71 ? 37  GLY C C   1 
ATOM   6230  O O   . GLY C 1 37  ? 49.961  -57.542 58.796  1.00 229.61 ? 37  GLY C O   1 
ATOM   6231  N N   . GLN C 1 38  ? 47.921  -58.495 58.850  1.00 285.69 ? 38  GLN C N   1 
ATOM   6232  C CA  . GLN C 1 38  ? 48.347  -59.761 58.275  1.00 285.76 ? 38  GLN C CA  1 
ATOM   6233  C C   . GLN C 1 38  ? 47.818  -59.908 56.852  1.00 285.39 ? 38  GLN C C   1 
ATOM   6234  O O   . GLN C 1 38  ? 46.768  -59.350 56.521  1.00 285.64 ? 38  GLN C O   1 
ATOM   6235  C CB  . GLN C 1 38  ? 47.853  -60.939 59.124  1.00 287.68 ? 38  GLN C CB  1 
ATOM   6236  C CG  . GLN C 1 38  ? 48.197  -60.835 60.603  1.00 288.36 ? 38  GLN C CG  1 
ATOM   6237  C CD  . GLN C 1 38  ? 49.691  -60.802 60.866  1.00 287.32 ? 38  GLN C CD  1 
ATOM   6238  O OE1 . GLN C 1 38  ? 50.490  -61.268 60.053  1.00 286.58 ? 38  GLN C OE1 1 
ATOM   6239  N NE2 . GLN C 1 38  ? 50.075  -60.252 62.011  1.00 287.33 ? 38  GLN C NE2 1 
ATOM   6240  N N   . PRO C 1 39  ? 48.518  -60.649 55.987  1.00 230.09 ? 39  PRO C N   1 
ATOM   6241  C CA  . PRO C 1 39  ? 48.051  -60.810 54.604  1.00 222.50 ? 39  PRO C CA  1 
ATOM   6242  C C   . PRO C 1 39  ? 46.630  -61.352 54.529  1.00 223.04 ? 39  PRO C C   1 
ATOM   6243  O O   . PRO C 1 39  ? 46.081  -61.880 55.497  1.00 217.76 ? 39  PRO C O   1 
ATOM   6244  C CB  . PRO C 1 39  ? 49.053  -61.804 54.009  1.00 207.26 ? 39  PRO C CB  1 
ATOM   6245  C CG  . PRO C 1 39  ? 50.299  -61.580 54.793  1.00 189.93 ? 39  PRO C CG  1 
ATOM   6246  C CD  . PRO C 1 39  ? 49.845  -61.259 56.195  1.00 211.61 ? 39  PRO C CD  1 
ATOM   6247  N N   . MET C 1 40  ? 46.039  -61.220 53.338  1.00 224.08 ? 40  MET C N   1 
ATOM   6248  C CA  . MET C 1 40  ? 44.634  -61.577 53.150  1.00 224.34 ? 40  MET C CA  1 
ATOM   6249  C C   . MET C 1 40  ? 44.384  -63.043 53.485  1.00 222.79 ? 40  MET C C   1 
ATOM   6250  O O   . MET C 1 40  ? 43.462  -63.371 54.242  1.00 220.27 ? 40  MET C O   1 
ATOM   6251  C CB  . MET C 1 40  ? 44.196  -61.257 51.718  1.00 226.49 ? 40  MET C CB  1 
ATOM   6252  C CG  . MET C 1 40  ? 42.734  -61.559 51.420  1.00 222.44 ? 40  MET C CG  1 
ATOM   6253  S SD  . MET C 1 40  ? 42.234  -60.996 49.780  1.00 218.83 ? 40  MET C SD  1 
ATOM   6254  C CE  . MET C 1 40  ? 42.554  -59.240 49.920  1.00 207.32 ? 40  MET C CE  1 
ATOM   6255  N N   . ILE C 1 41  ? 45.197  -63.947 52.927  1.00 213.42 ? 41  ILE C N   1 
ATOM   6256  C CA  . ILE C 1 41  ? 45.022  -65.374 53.192  1.00 203.91 ? 41  ILE C CA  1 
ATOM   6257  C C   . ILE C 1 41  ? 45.569  -65.801 54.543  1.00 193.05 ? 41  ILE C C   1 
ATOM   6258  O O   . ILE C 1 41  ? 45.432  -66.976 54.908  1.00 191.40 ? 41  ILE C O   1 
ATOM   6259  C CB  . ILE C 1 41  ? 45.701  -66.243 52.116  1.00 213.29 ? 41  ILE C CB  1 
ATOM   6260  C CG1 . ILE C 1 41  ? 47.184  -65.882 52.002  1.00 206.16 ? 41  ILE C CG1 1 
ATOM   6261  C CG2 . ILE C 1 41  ? 44.998  -66.082 50.779  1.00 224.57 ? 41  ILE C CG2 1 
ATOM   6262  C CD1 . ILE C 1 41  ? 47.928  -66.670 50.947  1.00 209.83 ? 41  ILE C CD1 1 
ATOM   6263  N N   . HIS C 1 42  ? 46.184  -64.891 55.299  1.00 196.25 ? 42  HIS C N   1 
ATOM   6264  C CA  . HIS C 1 42  ? 46.761  -65.259 56.586  1.00 190.20 ? 42  HIS C CA  1 
ATOM   6265  C C   . HIS C 1 42  ? 45.706  -65.565 57.644  1.00 195.51 ? 42  HIS C C   1 
ATOM   6266  O O   . HIS C 1 42  ? 46.050  -66.142 58.682  1.00 204.34 ? 42  HIS C O   1 
ATOM   6267  C CB  . HIS C 1 42  ? 47.700  -64.153 57.071  1.00 193.94 ? 42  HIS C CB  1 
ATOM   6268  C CG  . HIS C 1 42  ? 48.682  -64.605 58.107  1.00 186.22 ? 42  HIS C CG  1 
ATOM   6269  N ND1 . HIS C 1 42  ? 49.909  -65.141 57.780  1.00 166.69 ? 42  HIS C ND1 1 
ATOM   6270  C CD2 . HIS C 1 42  ? 48.620  -64.603 59.459  1.00 185.13 ? 42  HIS C CD2 1 
ATOM   6271  C CE1 . HIS C 1 42  ? 50.561  -65.450 58.887  1.00 166.16 ? 42  HIS C CE1 1 
ATOM   6272  N NE2 . HIS C 1 42  ? 49.801  -65.133 59.920  1.00 177.68 ? 42  HIS C NE2 1 
ATOM   6273  N N   . HIS C 1 43  ? 44.441  -65.203 57.411  1.00 187.98 ? 43  HIS C N   1 
ATOM   6274  C CA  . HIS C 1 43  ? 43.373  -65.489 58.363  1.00 190.56 ? 43  HIS C CA  1 
ATOM   6275  C C   . HIS C 1 43  ? 42.762  -66.867 58.105  1.00 200.68 ? 43  HIS C C   1 
ATOM   6276  O O   . HIS C 1 43  ? 42.497  -67.601 59.066  1.00 211.51 ? 43  HIS C O   1 
ATOM   6277  C CB  . HIS C 1 43  ? 42.280  -64.413 58.320  1.00 175.56 ? 43  HIS C CB  1 
ATOM   6278  C CG  . HIS C 1 43  ? 42.767  -63.026 58.608  1.00 171.39 ? 43  HIS C CG  1 
ATOM   6279  N ND1 . HIS C 1 43  ? 43.633  -62.350 57.776  1.00 182.10 ? 43  HIS C ND1 1 
ATOM   6280  C CD2 . HIS C 1 43  ? 42.493  -62.182 59.631  1.00 165.37 ? 43  HIS C CD2 1 
ATOM   6281  C CE1 . HIS C 1 43  ? 43.879  -61.153 58.279  1.00 187.59 ? 43  HIS C CE1 1 
ATOM   6282  N NE2 . HIS C 1 43  ? 43.199  -61.026 59.404  1.00 171.81 ? 43  HIS C NE2 1 
ATOM   6283  N N   . PRO C 1 44  ? 42.509  -67.262 56.848  1.00 194.82 ? 44  PRO C N   1 
ATOM   6284  C CA  . PRO C 1 44  ? 42.105  -68.662 56.615  1.00 199.35 ? 44  PRO C CA  1 
ATOM   6285  C C   . PRO C 1 44  ? 43.130  -69.669 57.107  1.00 213.20 ? 44  PRO C C   1 
ATOM   6286  O O   . PRO C 1 44  ? 42.763  -70.658 57.755  1.00 218.13 ? 44  PRO C O   1 
ATOM   6287  C CB  . PRO C 1 44  ? 41.918  -68.718 55.093  1.00 189.89 ? 44  PRO C CB  1 
ATOM   6288  C CG  . PRO C 1 44  ? 41.535  -67.337 54.723  1.00 187.96 ? 44  PRO C CG  1 
ATOM   6289  C CD  . PRO C 1 44  ? 42.331  -66.447 55.631  1.00 190.12 ? 44  PRO C CD  1 
ATOM   6290  N N   . ILE C 1 45  ? 44.413  -69.445 56.811  1.00 211.46 ? 45  ILE C N   1 
ATOM   6291  C CA  . ILE C 1 45  ? 45.455  -70.369 57.253  1.00 220.46 ? 45  ILE C CA  1 
ATOM   6292  C C   . ILE C 1 45  ? 45.495  -70.446 58.775  1.00 243.66 ? 45  ILE C C   1 
ATOM   6293  O O   . ILE C 1 45  ? 45.752  -71.510 59.352  1.00 240.68 ? 45  ILE C O   1 
ATOM   6294  C CB  . ILE C 1 45  ? 46.817  -69.946 56.672  1.00 209.96 ? 45  ILE C CB  1 
ATOM   6295  C CG1 . ILE C 1 45  ? 46.748  -69.862 55.147  1.00 207.00 ? 45  ILE C CG1 1 
ATOM   6296  C CG2 . ILE C 1 45  ? 47.908  -70.917 57.095  1.00 213.10 ? 45  ILE C CG2 1 
ATOM   6297  C CD1 . ILE C 1 45  ? 48.024  -69.357 54.504  1.00 195.86 ? 45  ILE C CD1 1 
ATOM   6298  N N   . SER C 1 46  ? 45.235  -69.322 59.450  1.00 314.74 ? 46  SER C N   1 
ATOM   6299  C CA  . SER C 1 46  ? 45.230  -69.322 60.910  1.00 315.83 ? 46  SER C CA  1 
ATOM   6300  C C   . SER C 1 46  ? 44.108  -70.183 61.476  1.00 317.70 ? 46  SER C C   1 
ATOM   6301  O O   . SER C 1 46  ? 44.249  -70.742 62.569  1.00 318.26 ? 46  SER C O   1 
ATOM   6302  C CB  . SER C 1 46  ? 45.116  -67.889 61.430  1.00 314.64 ? 46  SER C CB  1 
ATOM   6303  O OG  . SER C 1 46  ? 46.349  -67.202 61.295  1.00 312.51 ? 46  SER C OG  1 
ATOM   6304  N N   . ALA C 1 47  ? 42.996  -70.309 60.750  1.00 246.39 ? 47  ALA C N   1 
ATOM   6305  C CA  . ALA C 1 47  ? 41.878  -71.115 61.217  1.00 231.09 ? 47  ALA C CA  1 
ATOM   6306  C C   . ALA C 1 47  ? 42.051  -72.597 60.921  1.00 220.80 ? 47  ALA C C   1 
ATOM   6307  O O   . ALA C 1 47  ? 41.320  -73.413 61.491  1.00 213.69 ? 47  ALA C O   1 
ATOM   6308  C CB  . ALA C 1 47  ? 40.570  -70.620 60.594  1.00 221.37 ? 47  ALA C CB  1 
ATOM   6309  N N   . CYS C 1 48  ? 43.001  -72.966 60.060  0.42 219.55 ? 48  CYS C N   1 
ATOM   6310  C CA  . CYS C 1 48  ? 43.215  -74.373 59.749  0.42 205.38 ? 48  CYS C CA  1 
ATOM   6311  C C   . CYS C 1 48  ? 43.921  -75.106 60.881  0.42 199.27 ? 48  CYS C C   1 
ATOM   6312  O O   . CYS C 1 48  ? 43.804  -76.332 60.977  0.42 191.77 ? 48  CYS C O   1 
ATOM   6313  C CB  . CYS C 1 48  ? 44.024  -74.511 58.459  0.42 201.15 ? 48  CYS C CB  1 
ATOM   6314  N N   . LYS C 1 49  ? 44.655  -74.385 61.730  1.00 197.40 ? 49  LYS C N   1 
ATOM   6315  C CA  . LYS C 1 49  ? 45.389  -75.019 62.817  1.00 190.83 ? 49  LYS C CA  1 
ATOM   6316  C C   . LYS C 1 49  ? 44.469  -75.531 63.919  1.00 187.09 ? 49  LYS C C   1 
ATOM   6317  O O   . LYS C 1 49  ? 44.851  -76.453 64.647  1.00 184.52 ? 49  LYS C O   1 
ATOM   6318  C CB  . LYS C 1 49  ? 46.406  -74.034 63.399  1.00 199.23 ? 49  LYS C CB  1 
ATOM   6319  C CG  . LYS C 1 49  ? 47.438  -74.654 64.331  1.00 193.83 ? 49  LYS C CG  1 
ATOM   6320  C CD  . LYS C 1 49  ? 48.026  -75.919 63.723  1.00 194.58 ? 49  LYS C CD  1 
ATOM   6321  C CE  . LYS C 1 49  ? 48.831  -76.709 64.740  1.00 188.59 ? 49  LYS C CE  1 
ATOM   6322  N NZ  . LYS C 1 49  ? 50.067  -77.280 64.131  1.00 194.63 ? 49  LYS C NZ  1 
ATOM   6323  N N   . LYS C 1 50  ? 43.265  -74.967 64.054  1.00 183.48 ? 50  LYS C N   1 
ATOM   6324  C CA  . LYS C 1 50  ? 42.347  -75.408 65.099  1.00 176.67 ? 50  LYS C CA  1 
ATOM   6325  C C   . LYS C 1 50  ? 41.791  -76.805 64.850  1.00 175.93 ? 50  LYS C C   1 
ATOM   6326  O O   . LYS C 1 50  ? 41.189  -77.382 65.762  1.00 176.33 ? 50  LYS C O   1 
ATOM   6327  C CB  . LYS C 1 50  ? 41.198  -74.410 65.250  1.00 174.08 ? 50  LYS C CB  1 
ATOM   6328  C CG  . LYS C 1 50  ? 40.023  -74.655 64.320  1.00 167.02 ? 50  LYS C CG  1 
ATOM   6329  C CD  . LYS C 1 50  ? 38.802  -73.877 64.783  1.00 168.83 ? 50  LYS C CD  1 
ATOM   6330  C CE  . LYS C 1 50  ? 37.897  -73.505 63.620  1.00 186.80 ? 50  LYS C CE  1 
ATOM   6331  N NZ  . LYS C 1 50  ? 38.611  -72.724 62.571  1.00 195.60 ? 50  LYS C NZ  1 
ATOM   6332  N N   . ILE C 1 51  ? 41.974  -77.356 63.654  1.00 183.49 ? 51  ILE C N   1 
ATOM   6333  C CA  . ILE C 1 51  ? 41.588  -78.731 63.357  1.00 185.19 ? 51  ILE C CA  1 
ATOM   6334  C C   . ILE C 1 51  ? 42.807  -79.610 63.607  1.00 191.51 ? 51  ILE C C   1 
ATOM   6335  O O   . ILE C 1 51  ? 43.775  -79.577 62.842  1.00 194.01 ? 51  ILE C O   1 
ATOM   6336  C CB  . ILE C 1 51  ? 41.081  -78.881 61.919  1.00 181.51 ? 51  ILE C CB  1 
ATOM   6337  C CG1 . ILE C 1 51  ? 39.886  -77.963 61.668  1.00 170.94 ? 51  ILE C CG1 1 
ATOM   6338  C CG2 . ILE C 1 51  ? 40.723  -80.326 61.629  1.00 190.49 ? 51  ILE C CG2 1 
ATOM   6339  C CD1 . ILE C 1 51  ? 40.268  -76.662 61.014  1.00 180.05 ? 51  ILE C CD1 1 
ATOM   6340  N N   . SER C 1 52  ? 42.761  -80.403 64.680  1.00 184.92 ? 52  SER C N   1 
ATOM   6341  C CA  . SER C 1 52  ? 43.907  -81.222 65.059  1.00 189.10 ? 52  SER C CA  1 
ATOM   6342  C C   . SER C 1 52  ? 44.179  -82.336 64.056  1.00 196.66 ? 52  SER C C   1 
ATOM   6343  O O   . SER C 1 52  ? 45.323  -82.792 63.948  1.00 199.37 ? 52  SER C O   1 
ATOM   6344  C CB  . SER C 1 52  ? 43.687  -81.813 66.453  1.00 191.62 ? 52  SER C CB  1 
ATOM   6345  O OG  . SER C 1 52  ? 42.519  -82.617 66.489  1.00 197.24 ? 52  SER C OG  1 
ATOM   6346  N N   . ASN C 1 53  ? 43.161  -82.773 63.318  1.00 199.79 ? 53  ASN C N   1 
ATOM   6347  C CA  . ASN C 1 53  ? 43.298  -83.825 62.322  1.00 204.11 ? 53  ASN C CA  1 
ATOM   6348  C C   . ASN C 1 53  ? 43.586  -83.288 60.920  1.00 214.05 ? 53  ASN C C   1 
ATOM   6349  O O   . ASN C 1 53  ? 43.398  -84.015 59.938  1.00 222.10 ? 53  ASN C O   1 
ATOM   6350  C CB  . ASN C 1 53  ? 42.040  -84.697 62.314  1.00 203.77 ? 53  ASN C CB  1 
ATOM   6351  C CG  . ASN C 1 53  ? 40.768  -83.883 62.481  1.00 195.45 ? 53  ASN C CG  1 
ATOM   6352  O OD1 . ASN C 1 53  ? 40.692  -83.000 63.336  1.00 194.67 ? 53  ASN C OD1 1 
ATOM   6353  N ND2 . ASN C 1 53  ? 39.766  -84.172 61.664  1.00 193.52 ? 53  ASN C ND2 1 
ATOM   6354  N N   . LEU C 1 54  ? 44.032  -82.040 60.805  1.00 225.65 ? 54  LEU C N   1 
ATOM   6355  C CA  . LEU C 1 54  ? 44.421  -81.458 59.529  1.00 225.36 ? 54  LEU C CA  1 
ATOM   6356  C C   . LEU C 1 54  ? 45.930  -81.559 59.334  1.00 227.28 ? 54  LEU C C   1 
ATOM   6357  O O   . LEU C 1 54  ? 46.704  -81.490 60.293  1.00 227.31 ? 54  LEU C O   1 
ATOM   6358  C CB  . LEU C 1 54  ? 43.980  -79.995 59.431  1.00 222.88 ? 54  LEU C CB  1 
ATOM   6359  C CG  . LEU C 1 54  ? 43.848  -79.417 58.019  1.00 222.01 ? 54  LEU C CG  1 
ATOM   6360  C CD1 . LEU C 1 54  ? 42.644  -78.490 57.929  1.00 222.33 ? 54  LEU C CD1 1 
ATOM   6361  C CD2 . LEU C 1 54  ? 45.118  -78.682 57.614  1.00 220.30 ? 54  LEU C CD2 1 
ATOM   6362  N N   . ALA C 1 55  ? 46.341  -81.724 58.076  1.00 214.31 ? 55  ALA C N   1 
ATOM   6363  C CA  . ALA C 1 55  ? 47.755  -81.876 57.758  1.00 207.65 ? 55  ALA C CA  1 
ATOM   6364  C C   . ALA C 1 55  ? 48.203  -80.894 56.680  1.00 204.54 ? 55  ALA C C   1 
ATOM   6365  O O   . ALA C 1 55  ? 48.443  -79.715 56.964  1.00 207.83 ? 55  ALA C O   1 
ATOM   6366  C CB  . ALA C 1 55  ? 48.049  -83.311 57.319  1.00 211.27 ? 55  ALA C CB  1 
ATOM   6367  N N   . GLN C 1 56  ? 48.323  -81.372 55.443  1.00 199.97 ? 56  GLN C N   1 
ATOM   6368  C CA  . GLN C 1 56  ? 48.846  -80.555 54.356  1.00 196.04 ? 56  GLN C CA  1 
ATOM   6369  C C   . GLN C 1 56  ? 47.876  -79.439 53.981  1.00 195.42 ? 56  GLN C C   1 
ATOM   6370  O O   . GLN C 1 56  ? 46.656  -79.571 54.112  1.00 196.36 ? 56  GLN C O   1 
ATOM   6371  C CB  . GLN C 1 56  ? 49.133  -81.423 53.131  1.00 197.04 ? 56  GLN C CB  1 
ATOM   6372  N N   . ILE C 1 57  ? 48.436  -78.322 53.515  1.00 199.72 ? 57  ILE C N   1 
ATOM   6373  C CA  . ILE C 1 57  ? 47.666  -77.185 53.029  1.00 200.26 ? 57  ILE C CA  1 
ATOM   6374  C C   . ILE C 1 57  ? 48.141  -76.841 51.624  1.00 206.64 ? 57  ILE C C   1 
ATOM   6375  O O   . ILE C 1 57  ? 49.343  -76.881 51.338  1.00 204.43 ? 57  ILE C O   1 
ATOM   6376  C CB  . ILE C 1 57  ? 47.795  -75.966 53.968  1.00 196.24 ? 57  ILE C CB  1 
ATOM   6377  C CG1 . ILE C 1 57  ? 47.487  -76.375 55.412  1.00 198.60 ? 57  ILE C CG1 1 
ATOM   6378  C CG2 . ILE C 1 57  ? 46.874  -74.844 53.514  1.00 193.70 ? 57  ILE C CG2 1 
ATOM   6379  C CD1 . ILE C 1 57  ? 47.221  -75.207 56.336  1.00 202.55 ? 57  ILE C CD1 1 
ATOM   6380  N N   . PHE C 1 58  ? 47.198  -76.499 50.748  1.00 232.22 ? 58  PHE C N   1 
ATOM   6381  C CA  . PHE C 1 58  ? 47.474  -76.303 49.329  1.00 231.10 ? 58  PHE C CA  1 
ATOM   6382  C C   . PHE C 1 58  ? 46.929  -74.955 48.883  1.00 230.09 ? 58  PHE C C   1 
ATOM   6383  O O   . PHE C 1 58  ? 45.729  -74.694 49.011  1.00 231.13 ? 58  PHE C O   1 
ATOM   6384  C CB  . PHE C 1 58  ? 46.863  -77.425 48.484  1.00 232.48 ? 58  PHE C CB  1 
ATOM   6385  C CG  . PHE C 1 58  ? 47.563  -78.742 48.628  1.00 234.30 ? 58  PHE C CG  1 
ATOM   6386  C CD1 . PHE C 1 58  ? 48.649  -79.054 47.826  1.00 232.00 ? 58  PHE C CD1 1 
ATOM   6387  C CD2 . PHE C 1 58  ? 47.139  -79.668 49.565  1.00 234.74 ? 58  PHE C CD2 1 
ATOM   6388  C CE1 . PHE C 1 58  ? 49.298  -80.267 47.956  1.00 232.32 ? 58  PHE C CE1 1 
ATOM   6389  C CE2 . PHE C 1 58  ? 47.783  -80.880 49.700  1.00 235.12 ? 58  PHE C CE2 1 
ATOM   6390  C CZ  . PHE C 1 58  ? 48.864  -81.181 48.896  1.00 233.96 ? 58  PHE C CZ  1 
ATOM   6391  N N   . LEU C 1 59  ? 47.810  -74.104 48.370  1.00 215.34 ? 59  LEU C N   1 
ATOM   6392  C CA  . LEU C 1 59  ? 47.431  -72.843 47.749  1.00 216.28 ? 59  LEU C CA  1 
ATOM   6393  C C   . LEU C 1 59  ? 47.592  -72.999 46.244  1.00 209.88 ? 59  LEU C C   1 
ATOM   6394  O O   . LEU C 1 59  ? 48.705  -73.226 45.760  1.00 206.63 ? 59  LEU C O   1 
ATOM   6395  C CB  . LEU C 1 59  ? 48.296  -71.695 48.267  1.00 217.24 ? 59  LEU C CB  1 
ATOM   6396  C CG  . LEU C 1 59  ? 48.496  -71.618 49.782  1.00 221.15 ? 59  LEU C CG  1 
ATOM   6397  C CD1 . LEU C 1 59  ? 49.487  -70.522 50.139  1.00 219.50 ? 59  LEU C CD1 1 
ATOM   6398  C CD2 . LEU C 1 59  ? 47.170  -71.399 50.489  1.00 224.05 ? 59  LEU C CD2 1 
ATOM   6399  N N   . ILE C 1 60  ? 46.492  -72.875 45.505  1.00 202.79 ? 60  ILE C N   1 
ATOM   6400  C CA  . ILE C 1 60  ? 46.500  -73.085 44.062  1.00 193.68 ? 60  ILE C CA  1 
ATOM   6401  C C   . ILE C 1 60  ? 46.064  -71.806 43.362  1.00 194.58 ? 60  ILE C C   1 
ATOM   6402  O O   . ILE C 1 60  ? 45.189  -71.084 43.848  1.00 207.73 ? 60  ILE C O   1 
ATOM   6403  C CB  . ILE C 1 60  ? 45.602  -74.272 43.646  1.00 191.73 ? 60  ILE C CB  1 
ATOM   6404  C CG1 . ILE C 1 60  ? 44.148  -74.037 44.058  1.00 204.94 ? 60  ILE C CG1 1 
ATOM   6405  C CG2 . ILE C 1 60  ? 46.120  -75.575 44.246  1.00 195.54 ? 60  ILE C CG2 1 
ATOM   6406  C CD1 . ILE C 1 60  ? 43.218  -75.155 43.634  1.00 206.33 ? 60  ILE C CD1 1 
ATOM   6407  N N   . GLY C 1 61  ? 46.682  -71.530 42.218  1.00 194.55 ? 61  GLY C N   1 
ATOM   6408  C CA  . GLY C 1 61  ? 46.398  -70.348 41.425  1.00 199.82 ? 61  GLY C CA  1 
ATOM   6409  C C   . GLY C 1 61  ? 47.491  -70.091 40.413  1.00 201.47 ? 61  GLY C C   1 
ATOM   6410  O O   . GLY C 1 61  ? 48.633  -70.492 40.636  1.00 196.64 ? 61  GLY C O   1 
ATOM   6411  N N   . PHE C 1 62  ? 47.166  -69.430 39.298  1.00 231.22 ? 62  PHE C N   1 
ATOM   6412  C CA  . PHE C 1 62  ? 48.112  -69.245 38.203  1.00 229.57 ? 62  PHE C CA  1 
ATOM   6413  C C   . PHE C 1 62  ? 49.007  -68.025 38.394  1.00 227.23 ? 62  PHE C C   1 
ATOM   6414  O O   . PHE C 1 62  ? 49.462  -67.431 37.408  1.00 225.22 ? 62  PHE C O   1 
ATOM   6415  C CB  . PHE C 1 62  ? 47.370  -69.184 36.864  1.00 229.28 ? 62  PHE C CB  1 
ATOM   6416  C CG  . PHE C 1 62  ? 46.280  -68.150 36.805  1.00 228.93 ? 62  PHE C CG  1 
ATOM   6417  C CD1 . PHE C 1 62  ? 45.044  -68.395 37.383  1.00 230.61 ? 62  PHE C CD1 1 
ATOM   6418  C CD2 . PHE C 1 62  ? 46.475  -66.953 36.139  1.00 226.74 ? 62  PHE C CD2 1 
ATOM   6419  C CE1 . PHE C 1 62  ? 44.037  -67.455 37.327  1.00 230.18 ? 62  PHE C CE1 1 
ATOM   6420  C CE2 . PHE C 1 62  ? 45.464  -66.005 36.070  1.00 226.25 ? 62  PHE C CE2 1 
ATOM   6421  C CZ  . PHE C 1 62  ? 44.241  -66.261 36.670  1.00 227.88 ? 62  PHE C CZ  1 
ATOM   6422  N N   . TYR C 1 63  ? 49.278  -67.645 39.640  1.00 195.40 ? 63  TYR C N   1 
ATOM   6423  C CA  . TYR C 1 63  ? 50.344  -66.704 39.948  1.00 186.29 ? 63  TYR C CA  1 
ATOM   6424  C C   . TYR C 1 63  ? 51.704  -67.368 39.742  1.00 179.05 ? 63  TYR C C   1 
ATOM   6425  O O   . TYR C 1 63  ? 51.813  -68.563 39.449  1.00 178.59 ? 63  TYR C O   1 
ATOM   6426  C CB  . TYR C 1 63  ? 50.210  -66.202 41.385  1.00 192.93 ? 63  TYR C CB  1 
ATOM   6427  C CG  . TYR C 1 63  ? 49.477  -64.889 41.525  1.00 193.29 ? 63  TYR C CG  1 
ATOM   6428  C CD1 . TYR C 1 63  ? 49.703  -63.851 40.634  1.00 186.08 ? 63  TYR C CD1 1 
ATOM   6429  C CD2 . TYR C 1 63  ? 48.571  -64.682 42.557  1.00 200.93 ? 63  TYR C CD2 1 
ATOM   6430  C CE1 . TYR C 1 63  ? 49.046  -62.645 40.762  1.00 184.09 ? 63  TYR C CE1 1 
ATOM   6431  C CE2 . TYR C 1 63  ? 47.903  -63.480 42.689  1.00 197.01 ? 63  TYR C CE2 1 
ATOM   6432  C CZ  . TYR C 1 63  ? 48.145  -62.465 41.788  1.00 185.68 ? 63  TYR C CZ  1 
ATOM   6433  O OH  . TYR C 1 63  ? 47.487  -61.263 41.915  1.00 182.83 ? 63  TYR C OH  1 
ATOM   6434  N N   . GLU C 1 64  ? 52.759  -66.578 39.903  1.00 169.93 ? 64  GLU C N   1 
ATOM   6435  C CA  . GLU C 1 64  ? 54.112  -67.103 39.836  1.00 156.60 ? 64  GLU C CA  1 
ATOM   6436  C C   . GLU C 1 64  ? 54.539  -67.565 41.222  1.00 168.19 ? 64  GLU C C   1 
ATOM   6437  O O   . GLU C 1 64  ? 54.373  -66.838 42.208  1.00 184.57 ? 64  GLU C O   1 
ATOM   6438  C CB  . GLU C 1 64  ? 55.078  -66.052 39.290  1.00 143.39 ? 64  GLU C CB  1 
ATOM   6439  C CG  . GLU C 1 64  ? 54.895  -65.777 37.805  1.00 133.81 ? 64  GLU C CG  1 
ATOM   6440  C CD  . GLU C 1 64  ? 55.103  -67.015 36.947  1.00 133.02 ? 64  GLU C CD  1 
ATOM   6441  O OE1 . GLU C 1 64  ? 55.813  -67.943 37.389  1.00 134.32 ? 64  GLU C OE1 1 
ATOM   6442  O OE2 . GLU C 1 64  ? 54.540  -67.067 35.833  1.00 127.70 ? 64  GLU C OE2 1 
ATOM   6443  N N   . GLU C 1 65  ? 55.088  -68.779 41.288  1.00 160.63 ? 65  GLU C N   1 
ATOM   6444  C CA  . GLU C 1 65  ? 55.462  -69.376 42.565  1.00 171.57 ? 65  GLU C CA  1 
ATOM   6445  C C   . GLU C 1 65  ? 56.573  -68.599 43.260  1.00 185.15 ? 65  GLU C C   1 
ATOM   6446  O O   . GLU C 1 65  ? 56.731  -68.720 44.480  1.00 196.86 ? 65  GLU C O   1 
ATOM   6447  C CB  . GLU C 1 65  ? 55.864  -70.835 42.338  1.00 167.19 ? 65  GLU C CB  1 
ATOM   6448  C CG  . GLU C 1 65  ? 56.069  -71.655 43.601  1.00 167.81 ? 65  GLU C CG  1 
ATOM   6449  C CD  . GLU C 1 65  ? 56.305  -73.122 43.301  1.00 165.55 ? 65  GLU C CD  1 
ATOM   6450  O OE1 . GLU C 1 65  ? 56.254  -73.503 42.112  1.00 164.68 ? 65  GLU C OE1 1 
ATOM   6451  O OE2 . GLU C 1 65  ? 56.538  -73.895 44.253  1.00 165.27 ? 65  GLU C OE2 1 
ATOM   6452  N N   . ARG C 1 66  ? 57.344  -67.805 42.511  1.00 179.70 ? 66  ARG C N   1 
ATOM   6453  C CA  . ARG C 1 66  ? 58.440  -67.043 43.102  1.00 184.60 ? 66  ARG C CA  1 
ATOM   6454  C C   . ARG C 1 66  ? 57.942  -66.077 44.168  1.00 200.77 ? 66  ARG C C   1 
ATOM   6455  O O   . ARG C 1 66  ? 58.636  -65.835 45.162  1.00 203.34 ? 66  ARG C O   1 
ATOM   6456  C CB  . ARG C 1 66  ? 59.182  -66.276 42.010  1.00 162.26 ? 66  ARG C CB  1 
ATOM   6457  C CG  . ARG C 1 66  ? 59.565  -67.121 40.811  1.00 150.41 ? 66  ARG C CG  1 
ATOM   6458  C CD  . ARG C 1 66  ? 59.882  -66.236 39.625  1.00 130.46 ? 66  ARG C CD  1 
ATOM   6459  N NE  . ARG C 1 66  ? 58.730  -65.406 39.283  1.00 130.59 ? 66  ARG C NE  1 
ATOM   6460  C CZ  . ARG C 1 66  ? 58.713  -64.510 38.301  1.00 124.66 ? 66  ARG C CZ  1 
ATOM   6461  N NH1 . ARG C 1 66  ? 59.792  -64.321 37.555  1.00 123.03 ? 66  ARG C NH1 1 
ATOM   6462  N NH2 . ARG C 1 66  ? 57.616  -63.804 38.065  1.00 121.03 ? 66  ARG C NH2 1 
ATOM   6463  N N   . GLU C 1 67  ? 56.747  -65.514 43.978  1.00 229.54 ? 67  GLU C N   1 
ATOM   6464  C CA  . GLU C 1 67  ? 56.211  -64.565 44.946  1.00 230.95 ? 67  GLU C CA  1 
ATOM   6465  C C   . GLU C 1 67  ? 55.733  -65.269 46.211  1.00 235.93 ? 67  GLU C C   1 
ATOM   6466  O O   . GLU C 1 67  ? 55.900  -64.746 47.319  1.00 233.49 ? 67  GLU C O   1 
ATOM   6467  C CB  . GLU C 1 67  ? 55.071  -63.765 44.314  1.00 230.28 ? 67  GLU C CB  1 
ATOM   6468  C CG  . GLU C 1 67  ? 55.521  -62.760 43.262  1.00 233.08 ? 67  GLU C CG  1 
ATOM   6469  C CD  . GLU C 1 67  ? 54.353  -62.100 42.552  1.00 234.42 ? 67  GLU C CD  1 
ATOM   6470  O OE1 . GLU C 1 67  ? 53.517  -62.826 41.973  1.00 228.24 ? 67  GLU C OE1 1 
ATOM   6471  O OE2 . GLU C 1 67  ? 54.273  -60.853 42.570  1.00 235.48 ? 67  GLU C OE2 1 
ATOM   6472  N N   . PHE C 1 68  ? 55.133  -66.451 46.068  1.00 265.60 ? 68  PHE C N   1 
ATOM   6473  C CA  . PHE C 1 68  ? 54.551  -67.150 47.207  1.00 267.36 ? 68  PHE C CA  1 
ATOM   6474  C C   . PHE C 1 68  ? 55.560  -67.995 47.972  1.00 267.49 ? 68  PHE C C   1 
ATOM   6475  O O   . PHE C 1 68  ? 55.334  -68.281 49.153  1.00 268.48 ? 68  PHE C O   1 
ATOM   6476  C CB  . PHE C 1 68  ? 53.382  -68.027 46.750  1.00 268.81 ? 68  PHE C CB  1 
ATOM   6477  C CG  . PHE C 1 68  ? 52.156  -67.247 46.375  1.00 268.88 ? 68  PHE C CG  1 
ATOM   6478  C CD1 . PHE C 1 68  ? 51.058  -67.213 47.220  1.00 270.47 ? 68  PHE C CD1 1 
ATOM   6479  C CD2 . PHE C 1 68  ? 52.108  -66.525 45.195  1.00 267.28 ? 68  PHE C CD2 1 
ATOM   6480  C CE1 . PHE C 1 68  ? 49.930  -66.489 46.884  1.00 270.73 ? 68  PHE C CE1 1 
ATOM   6481  C CE2 . PHE C 1 68  ? 50.983  -65.800 44.854  1.00 267.31 ? 68  PHE C CE2 1 
ATOM   6482  C CZ  . PHE C 1 68  ? 49.894  -65.781 45.699  1.00 269.17 ? 68  PHE C CZ  1 
ATOM   6483  N N   . ALA C 1 69  ? 56.655  -68.406 47.328  1.00 231.65 ? 69  ALA C N   1 
ATOM   6484  C CA  . ALA C 1 69  ? 57.644  -69.242 48.001  1.00 225.37 ? 69  ALA C CA  1 
ATOM   6485  C C   . ALA C 1 69  ? 58.215  -68.542 49.228  1.00 216.78 ? 69  ALA C C   1 
ATOM   6486  O O   . ALA C 1 69  ? 58.467  -69.181 50.257  1.00 217.32 ? 69  ALA C O   1 
ATOM   6487  C CB  . ALA C 1 69  ? 58.761  -69.620 47.029  1.00 221.18 ? 69  ALA C CB  1 
ATOM   6488  N N   . LEU C 1 70  ? 58.429  -67.228 49.138  1.00 206.94 ? 70  LEU C N   1 
ATOM   6489  C CA  . LEU C 1 70  ? 58.975  -66.489 50.271  1.00 195.64 ? 70  LEU C CA  1 
ATOM   6490  C C   . LEU C 1 70  ? 57.963  -66.358 51.404  1.00 191.49 ? 70  LEU C C   1 
ATOM   6491  O O   . LEU C 1 70  ? 58.350  -66.351 52.578  1.00 187.72 ? 70  LEU C O   1 
ATOM   6492  C CB  . LEU C 1 70  ? 59.453  -65.107 49.820  1.00 186.39 ? 70  LEU C CB  1 
ATOM   6493  C CG  . LEU C 1 70  ? 60.780  -65.011 49.056  1.00 179.05 ? 70  LEU C CG  1 
ATOM   6494  C CD1 . LEU C 1 70  ? 60.684  -65.594 47.653  1.00 186.71 ? 70  LEU C CD1 1 
ATOM   6495  C CD2 . LEU C 1 70  ? 61.248  -63.568 49.003  1.00 167.82 ? 70  LEU C CD2 1 
ATOM   6496  N N   . TYR C 1 71  ? 56.673  -66.250 51.078  1.00 194.78 ? 71  TYR C N   1 
ATOM   6497  C CA  . TYR C 1 71  ? 55.654  -66.066 52.108  1.00 187.06 ? 71  TYR C CA  1 
ATOM   6498  C C   . TYR C 1 71  ? 55.326  -67.373 52.824  1.00 189.32 ? 71  TYR C C   1 
ATOM   6499  O O   . TYR C 1 71  ? 55.211  -67.394 54.055  1.00 185.24 ? 71  TYR C O   1 
ATOM   6500  C CB  . TYR C 1 71  ? 54.391  -65.458 51.492  1.00 179.91 ? 71  TYR C CB  1 
ATOM   6501  C CG  . TYR C 1 71  ? 53.195  -65.427 52.422  1.00 166.94 ? 71  TYR C CG  1 
ATOM   6502  C CD1 . TYR C 1 71  ? 53.259  -64.777 53.649  1.00 161.23 ? 71  TYR C CD1 1 
ATOM   6503  C CD2 . TYR C 1 71  ? 51.995  -66.026 52.060  1.00 165.42 ? 71  TYR C CD2 1 
ATOM   6504  C CE1 . TYR C 1 71  ? 52.167  -64.742 54.496  1.00 156.11 ? 71  TYR C CE1 1 
ATOM   6505  C CE2 . TYR C 1 71  ? 50.896  -65.991 52.898  1.00 160.20 ? 71  TYR C CE2 1 
ATOM   6506  C CZ  . TYR C 1 71  ? 50.989  -65.351 54.115  1.00 160.61 ? 71  TYR C CZ  1 
ATOM   6507  O OH  . TYR C 1 71  ? 49.898  -65.317 54.953  1.00 162.03 ? 71  TYR C OH  1 
ATOM   6508  N N   . VAL C 1 72  ? 55.160  -68.464 52.072  1.00 200.19 ? 72  VAL C N   1 
ATOM   6509  C CA  . VAL C 1 72  ? 54.801  -69.749 52.669  1.00 202.48 ? 72  VAL C CA  1 
ATOM   6510  C C   . VAL C 1 72  ? 55.864  -70.222 53.655  1.00 200.92 ? 72  VAL C C   1 
ATOM   6511  O O   . VAL C 1 72  ? 55.548  -70.891 54.647  1.00 201.61 ? 72  VAL C O   1 
ATOM   6512  C CB  . VAL C 1 72  ? 54.551  -70.787 51.554  1.00 202.63 ? 72  VAL C CB  1 
ATOM   6513  C CG1 . VAL C 1 72  ? 54.329  -72.175 52.136  1.00 201.41 ? 72  VAL C CG1 1 
ATOM   6514  C CG2 . VAL C 1 72  ? 53.357  -70.371 50.703  1.00 200.64 ? 72  VAL C CG2 1 
ATOM   6515  N N   . SER C 1 73  ? 57.129  -69.861 53.424  1.00 195.58 ? 73  SER C N   1 
ATOM   6516  C CA  . SER C 1 73  ? 58.205  -70.292 54.311  1.00 187.04 ? 73  SER C CA  1 
ATOM   6517  C C   . SER C 1 73  ? 58.061  -69.729 55.719  1.00 189.30 ? 73  SER C C   1 
ATOM   6518  O O   . SER C 1 73  ? 58.603  -70.312 56.666  1.00 187.35 ? 73  SER C O   1 
ATOM   6519  C CB  . SER C 1 73  ? 59.558  -69.889 53.724  1.00 178.95 ? 73  SER C CB  1 
ATOM   6520  O OG  . SER C 1 73  ? 59.741  -70.454 52.438  1.00 177.38 ? 73  SER C OG  1 
ATOM   6521  N N   . SER C 1 74  ? 57.344  -68.619 55.882  1.00 198.11 ? 74  SER C N   1 
ATOM   6522  C CA  . SER C 1 74  ? 57.213  -67.975 57.182  1.00 201.35 ? 74  SER C CA  1 
ATOM   6523  C C   . SER C 1 74  ? 55.980  -68.433 57.950  1.00 204.51 ? 74  SER C C   1 
ATOM   6524  O O   . SER C 1 74  ? 55.968  -68.340 59.183  1.00 208.22 ? 74  SER C O   1 
ATOM   6525  C CB  . SER C 1 74  ? 57.177  -66.451 57.019  1.00 203.93 ? 74  SER C CB  1 
ATOM   6526  O OG  . SER C 1 74  ? 58.285  -65.992 56.261  1.00 200.69 ? 74  SER C OG  1 
ATOM   6527  N N   . ILE C 1 75  ? 54.949  -68.920 57.257  1.00 192.40 ? 75  ILE C N   1 
ATOM   6528  C CA  . ILE C 1 75  ? 53.725  -69.336 57.935  1.00 191.06 ? 75  ILE C CA  1 
ATOM   6529  C C   . ILE C 1 75  ? 53.973  -70.601 58.746  1.00 201.51 ? 75  ILE C C   1 
ATOM   6530  O O   . ILE C 1 75  ? 53.612  -70.684 59.926  1.00 209.13 ? 75  ILE C O   1 
ATOM   6531  C CB  . ILE C 1 75  ? 52.590  -69.545 56.918  1.00 179.00 ? 75  ILE C CB  1 
ATOM   6532  C CG1 . ILE C 1 75  ? 52.649  -68.490 55.816  1.00 172.85 ? 75  ILE C CG1 1 
ATOM   6533  C CG2 . ILE C 1 75  ? 51.239  -69.500 57.615  1.00 169.59 ? 75  ILE C CG2 1 
ATOM   6534  C CD1 . ILE C 1 75  ? 51.724  -68.790 54.664  1.00 172.30 ? 75  ILE C CD1 1 
ATOM   6535  N N   . SER C 1 76  ? 54.588  -71.610 58.120  1.00 194.48 ? 76  SER C N   1 
ATOM   6536  C CA  . SER C 1 76  ? 54.833  -72.883 58.788  1.00 201.77 ? 76  SER C CA  1 
ATOM   6537  C C   . SER C 1 76  ? 55.767  -72.751 59.983  1.00 198.10 ? 76  SER C C   1 
ATOM   6538  O O   . SER C 1 76  ? 55.838  -73.672 60.803  1.00 198.26 ? 76  SER C O   1 
ATOM   6539  C CB  . SER C 1 76  ? 55.405  -73.892 57.791  1.00 204.09 ? 76  SER C CB  1 
ATOM   6540  O OG  . SER C 1 76  ? 54.510  -74.109 56.715  1.00 207.82 ? 76  SER C OG  1 
ATOM   6541  N N   . ASN C 1 77  ? 56.487  -71.635 60.102  1.00 199.54 ? 77  ASN C N   1 
ATOM   6542  C CA  . ASN C 1 77  ? 57.279  -71.384 61.299  1.00 201.61 ? 77  ASN C CA  1 
ATOM   6543  C C   . ASN C 1 77  ? 56.426  -70.955 62.486  1.00 212.44 ? 77  ASN C C   1 
ATOM   6544  O O   . ASN C 1 77  ? 56.894  -71.036 63.628  1.00 209.08 ? 77  ASN C O   1 
ATOM   6545  C CB  . ASN C 1 77  ? 58.343  -70.321 61.016  1.00 191.50 ? 77  ASN C CB  1 
ATOM   6546  C CG  . ASN C 1 77  ? 59.331  -70.755 59.952  1.00 181.16 ? 77  ASN C CG  1 
ATOM   6547  O OD1 . ASN C 1 77  ? 59.589  -71.946 59.776  1.00 178.12 ? 77  ASN C OD1 1 
ATOM   6548  N ND2 . ASN C 1 77  ? 59.892  -69.787 59.237  1.00 173.35 ? 77  ASN C ND2 1 
ATOM   6549  N N   . GLU C 1 78  ? 55.195  -70.502 62.246  1.00 240.26 ? 78  GLU C N   1 
ATOM   6550  C CA  . GLU C 1 78  ? 54.308  -70.037 63.308  1.00 241.18 ? 78  GLU C CA  1 
ATOM   6551  C C   . GLU C 1 78  ? 53.335  -71.121 63.762  1.00 242.31 ? 78  GLU C C   1 
ATOM   6552  O O   . GLU C 1 78  ? 53.306  -71.479 64.944  1.00 243.06 ? 78  GLU C O   1 
ATOM   6553  C CB  . GLU C 1 78  ? 53.542  -68.793 62.840  1.00 240.51 ? 78  GLU C CB  1 
ATOM   6554  C CG  . GLU C 1 78  ? 54.421  -67.583 62.569  1.00 239.06 ? 78  GLU C CG  1 
ATOM   6555  C CD  . GLU C 1 78  ? 53.614  -66.344 62.234  1.00 238.43 ? 78  GLU C CD  1 
ATOM   6556  O OE1 . GLU C 1 78  ? 52.373  -66.448 62.146  1.00 238.65 ? 78  GLU C OE1 1 
ATOM   6557  O OE2 . GLU C 1 78  ? 54.221  -65.268 62.055  1.00 239.10 ? 78  GLU C OE2 1 
ATOM   6558  N N   . LEU C 1 79  ? 52.533  -71.653 62.840  1.00 221.90 ? 79  LEU C N   1 
ATOM   6559  C CA  . LEU C 1 79  ? 51.497  -72.618 63.183  1.00 221.01 ? 79  LEU C CA  1 
ATOM   6560  C C   . LEU C 1 79  ? 51.911  -74.063 62.939  1.00 218.99 ? 79  LEU C C   1 
ATOM   6561  O O   . LEU C 1 79  ? 51.165  -74.972 63.321  1.00 215.27 ? 79  LEU C O   1 
ATOM   6562  C CB  . LEU C 1 79  ? 50.209  -72.324 62.400  1.00 228.18 ? 79  LEU C CB  1 
ATOM   6563  C CG  . LEU C 1 79  ? 49.357  -71.123 62.821  1.00 231.29 ? 79  LEU C CG  1 
ATOM   6564  C CD1 . LEU C 1 79  ? 49.219  -71.059 64.337  1.00 229.20 ? 79  LEU C CD1 1 
ATOM   6565  C CD2 . LEU C 1 79  ? 49.910  -69.816 62.266  1.00 232.81 ? 79  LEU C CD2 1 
ATOM   6566  N N   . LYS C 1 80  ? 53.069  -74.296 62.319  1.00 218.23 ? 80  LYS C N   1 
ATOM   6567  C CA  . LYS C 1 80  ? 53.598  -75.641 62.084  1.00 215.97 ? 80  LYS C CA  1 
ATOM   6568  C C   . LYS C 1 80  ? 52.616  -76.483 61.265  1.00 229.08 ? 80  LYS C C   1 
ATOM   6569  O O   . LYS C 1 80  ? 52.162  -77.549 61.684  1.00 221.07 ? 80  LYS C O   1 
ATOM   6570  C CB  . LYS C 1 80  ? 53.955  -76.340 63.404  1.00 196.07 ? 80  LYS C CB  1 
ATOM   6571  C CG  . LYS C 1 80  ? 54.964  -75.598 64.274  1.00 189.30 ? 80  LYS C CG  1 
ATOM   6572  C CD  . LYS C 1 80  ? 54.286  -74.658 65.262  1.00 187.40 ? 80  LYS C CD  1 
ATOM   6573  C CE  . LYS C 1 80  ? 53.165  -75.358 66.015  1.00 184.17 ? 80  LYS C CE  1 
ATOM   6574  N NZ  . LYS C 1 80  ? 52.356  -74.403 66.823  1.00 176.19 ? 80  LYS C NZ  1 
ATOM   6575  N N   . ILE C 1 81  ? 52.293  -75.979 60.078  1.00 280.47 ? 81  ILE C N   1 
ATOM   6576  C CA  . ILE C 1 81  ? 51.390  -76.675 59.164  1.00 281.27 ? 81  ILE C CA  1 
ATOM   6577  C C   . ILE C 1 81  ? 52.024  -76.731 57.779  1.00 280.09 ? 81  ILE C C   1 
ATOM   6578  O O   . ILE C 1 81  ? 52.521  -75.710 57.282  1.00 278.55 ? 81  ILE C O   1 
ATOM   6579  C CB  . ILE C 1 81  ? 50.010  -76.001 59.122  1.00 281.80 ? 81  ILE C CB  1 
ATOM   6580  C CG1 . ILE C 1 81  ? 50.152  -74.481 59.227  1.00 280.59 ? 81  ILE C CG1 1 
ATOM   6581  C CG2 . ILE C 1 81  ? 49.114  -76.547 60.226  1.00 283.55 ? 81  ILE C CG2 1 
ATOM   6582  C CD1 . ILE C 1 81  ? 48.832  -73.750 59.315  1.00 281.12 ? 81  ILE C CD1 1 
ATOM   6583  N N   . PRO C 1 82  ? 52.034  -77.895 57.124  1.00 230.09 ? 82  PRO C N   1 
ATOM   6584  C CA  . PRO C 1 82  ? 52.653  -77.993 55.795  1.00 215.87 ? 82  PRO C CA  1 
ATOM   6585  C C   . PRO C 1 82  ? 51.860  -77.269 54.719  1.00 207.14 ? 82  PRO C C   1 
ATOM   6586  O O   . PRO C 1 82  ? 50.911  -77.825 54.155  1.00 199.27 ? 82  PRO C O   1 
ATOM   6587  C CB  . PRO C 1 82  ? 52.692  -79.506 55.534  1.00 205.93 ? 82  PRO C CB  1 
ATOM   6588  C CG  . PRO C 1 82  ? 52.489  -80.147 56.878  1.00 205.55 ? 82  PRO C CG  1 
ATOM   6589  C CD  . PRO C 1 82  ? 51.606  -79.208 57.631  1.00 218.53 ? 82  PRO C CD  1 
ATOM   6590  N N   . VAL C 1 83  ? 52.239  -76.028 54.428  1.00 202.06 ? 83  VAL C N   1 
ATOM   6591  C CA  . VAL C 1 83  ? 51.600  -75.228 53.390  1.00 198.36 ? 83  VAL C CA  1 
ATOM   6592  C C   . VAL C 1 83  ? 52.414  -75.355 52.111  1.00 191.94 ? 83  VAL C C   1 
ATOM   6593  O O   . VAL C 1 83  ? 53.651  -75.381 52.148  1.00 190.88 ? 83  VAL C O   1 
ATOM   6594  C CB  . VAL C 1 83  ? 51.472  -73.755 53.824  1.00 203.91 ? 83  VAL C CB  1 
ATOM   6595  C CG1 . VAL C 1 83  ? 50.649  -72.968 52.813  1.00 199.34 ? 83  VAL C CG1 1 
ATOM   6596  C CG2 . VAL C 1 83  ? 50.857  -73.663 55.210  1.00 210.09 ? 83  VAL C CG2 1 
ATOM   6597  N N   . ARG C 1 84  ? 51.723  -75.439 50.977  1.00 192.35 ? 84  ARG C N   1 
ATOM   6598  C CA  . ARG C 1 84  ? 52.374  -75.596 49.686  1.00 189.17 ? 84  ARG C CA  1 
ATOM   6599  C C   . ARG C 1 84  ? 51.601  -74.828 48.626  1.00 191.16 ? 84  ARG C C   1 
ATOM   6600  O O   . ARG C 1 84  ? 50.367  -74.816 48.635  1.00 196.76 ? 84  ARG C O   1 
ATOM   6601  C CB  . ARG C 1 84  ? 52.475  -77.074 49.290  1.00 189.37 ? 84  ARG C CB  1 
ATOM   6602  C CG  . ARG C 1 84  ? 53.148  -77.316 47.951  1.00 188.64 ? 84  ARG C CG  1 
ATOM   6603  C CD  . ARG C 1 84  ? 53.182  -78.794 47.616  1.00 188.74 ? 84  ARG C CD  1 
ATOM   6604  N NE  . ARG C 1 84  ? 53.989  -79.534 48.579  1.00 185.44 ? 84  ARG C NE  1 
ATOM   6605  C CZ  . ARG C 1 84  ? 55.297  -79.733 48.456  1.00 180.94 ? 84  ARG C CZ  1 
ATOM   6606  N NH1 . ARG C 1 84  ? 55.949  -79.242 47.411  1.00 183.81 ? 84  ARG C NH1 1 
ATOM   6607  N NH2 . ARG C 1 84  ? 55.955  -80.417 49.381  1.00 177.30 ? 84  ARG C NH2 1 
ATOM   6608  N N   . TYR C 1 85  ? 52.332  -74.188 47.718  1.00 189.37 ? 85  TYR C N   1 
ATOM   6609  C CA  . TYR C 1 85  ? 51.736  -73.486 46.590  1.00 189.66 ? 85  TYR C CA  1 
ATOM   6610  C C   . TYR C 1 85  ? 51.898  -74.318 45.326  1.00 185.29 ? 85  TYR C C   1 
ATOM   6611  O O   . TYR C 1 85  ? 52.984  -74.843 45.056  1.00 181.20 ? 85  TYR C O   1 
ATOM   6612  C CB  . TYR C 1 85  ? 52.365  -72.107 46.388  1.00 189.71 ? 85  TYR C CB  1 
ATOM   6613  C CG  . TYR C 1 85  ? 51.849  -71.398 45.154  1.00 189.23 ? 85  TYR C CG  1 
ATOM   6614  C CD1 . TYR C 1 85  ? 50.620  -70.752 45.164  1.00 196.35 ? 85  TYR C CD1 1 
ATOM   6615  C CD2 . TYR C 1 85  ? 52.585  -71.386 43.975  1.00 181.80 ? 85  TYR C CD2 1 
ATOM   6616  C CE1 . TYR C 1 85  ? 50.142  -70.108 44.037  1.00 197.79 ? 85  TYR C CE1 1 
ATOM   6617  C CE2 . TYR C 1 85  ? 52.115  -70.746 42.844  1.00 181.14 ? 85  TYR C CE2 1 
ATOM   6618  C CZ  . TYR C 1 85  ? 50.894  -70.108 42.881  1.00 184.95 ? 85  TYR C CZ  1 
ATOM   6619  O OH  . TYR C 1 85  ? 50.424  -69.470 41.756  1.00 186.10 ? 85  TYR C OH  1 
ATOM   6620  N N   . LEU C 1 86  ? 50.819  -74.432 44.556  1.00 184.93 ? 86  LEU C N   1 
ATOM   6621  C CA  . LEU C 1 86  ? 50.827  -75.131 43.279  1.00 180.63 ? 86  LEU C CA  1 
ATOM   6622  C C   . LEU C 1 86  ? 50.277  -74.196 42.214  1.00 180.05 ? 86  LEU C C   1 
ATOM   6623  O O   . LEU C 1 86  ? 49.178  -73.654 42.369  1.00 183.25 ? 86  LEU C O   1 
ATOM   6624  C CB  . LEU C 1 86  ? 50.000  -76.419 43.338  1.00 185.94 ? 86  LEU C CB  1 
ATOM   6625  C CG  . LEU C 1 86  ? 50.393  -77.444 44.405  1.00 190.46 ? 86  LEU C CG  1 
ATOM   6626  C CD1 . LEU C 1 86  ? 49.489  -78.667 44.344  1.00 193.92 ? 86  LEU C CD1 1 
ATOM   6627  C CD2 . LEU C 1 86  ? 51.852  -77.847 44.248  1.00 185.68 ? 86  LEU C CD2 1 
ATOM   6628  N N   . LYS C 1 87  ? 51.034  -74.010 41.139  1.00 171.29 ? 87  LYS C N   1 
ATOM   6629  C CA  . LYS C 1 87  ? 50.623  -73.138 40.045  1.00 169.74 ? 87  LYS C CA  1 
ATOM   6630  C C   . LYS C 1 87  ? 49.915  -73.976 38.988  1.00 164.04 ? 87  LYS C C   1 
ATOM   6631  O O   . LYS C 1 87  ? 50.553  -74.763 38.280  1.00 162.84 ? 87  LYS C O   1 
ATOM   6632  C CB  . LYS C 1 87  ? 51.825  -72.411 39.448  1.00 166.18 ? 87  LYS C CB  1 
ATOM   6633  C CG  . LYS C 1 87  ? 51.522  -71.732 38.123  1.00 167.61 ? 87  LYS C CG  1 
ATOM   6634  C CD  . LYS C 1 87  ? 52.748  -71.061 37.538  1.00 159.34 ? 87  LYS C CD  1 
ATOM   6635  C CE  . LYS C 1 87  ? 52.491  -70.633 36.104  1.00 155.67 ? 87  LYS C CE  1 
ATOM   6636  N NZ  . LYS C 1 87  ? 51.172  -69.956 35.956  1.00 166.27 ? 87  LYS C NZ  1 
ATOM   6637  N N   . GLU C 1 88  ? 48.596  -73.822 38.889  1.00 169.27 ? 88  GLU C N   1 
ATOM   6638  C CA  . GLU C 1 88  ? 47.848  -74.490 37.831  1.00 168.11 ? 88  GLU C CA  1 
ATOM   6639  C C   . GLU C 1 88  ? 48.212  -73.852 36.495  1.00 171.85 ? 88  GLU C C   1 
ATOM   6640  O O   . GLU C 1 88  ? 47.806  -72.723 36.202  1.00 173.04 ? 88  GLU C O   1 
ATOM   6641  C CB  . GLU C 1 88  ? 46.345  -74.420 38.092  1.00 164.81 ? 88  GLU C CB  1 
ATOM   6642  C CG  . GLU C 1 88  ? 45.806  -73.046 38.457  1.00 167.92 ? 88  GLU C CG  1 
ATOM   6643  C CD  . GLU C 1 88  ? 44.291  -73.005 38.448  1.00 162.43 ? 88  GLU C CD  1 
ATOM   6644  O OE1 . GLU C 1 88  ? 43.677  -73.945 37.901  1.00 157.98 ? 88  GLU C OE1 1 
ATOM   6645  O OE2 . GLU C 1 88  ? 43.716  -72.033 38.980  1.00 164.17 ? 88  GLU C OE2 1 
ATOM   6646  N N   . ASP C 1 89  ? 49.004  -74.566 35.692  1.00 176.73 ? 89  ASP C N   1 
ATOM   6647  C CA  . ASP C 1 89  ? 49.409  -74.039 34.394  1.00 175.72 ? 89  ASP C CA  1 
ATOM   6648  C C   . ASP C 1 89  ? 48.203  -73.798 33.495  1.00 173.72 ? 89  ASP C C   1 
ATOM   6649  O O   . ASP C 1 89  ? 48.171  -72.824 32.734  1.00 171.24 ? 89  ASP C O   1 
ATOM   6650  C CB  . ASP C 1 89  ? 50.402  -74.993 33.730  1.00 176.62 ? 89  ASP C CB  1 
ATOM   6651  C CG  . ASP C 1 89  ? 51.401  -75.570 34.714  1.00 175.46 ? 89  ASP C CG  1 
ATOM   6652  O OD1 . ASP C 1 89  ? 51.162  -76.687 35.217  1.00 179.34 ? 89  ASP C OD1 1 
ATOM   6653  O OD2 . ASP C 1 89  ? 52.413  -74.897 35.001  1.00 170.73 ? 89  ASP C OD2 1 
ATOM   6654  N N   . LYS C 1 90  ? 47.203  -74.676 33.566  1.00 171.66 ? 90  LYS C N   1 
ATOM   6655  C CA  . LYS C 1 90  ? 45.962  -74.506 32.818  1.00 172.06 ? 90  LYS C CA  1 
ATOM   6656  C C   . LYS C 1 90  ? 44.845  -74.118 33.778  1.00 176.77 ? 90  LYS C C   1 
ATOM   6657  O O   . LYS C 1 90  ? 44.234  -74.997 34.405  1.00 176.97 ? 90  LYS C O   1 
ATOM   6658  C CB  . LYS C 1 90  ? 45.605  -75.790 32.066  1.00 173.33 ? 90  LYS C CB  1 
ATOM   6659  N N   . PRO C 1 91  ? 44.544  -72.829 33.938  1.00 171.40 ? 91  PRO C N   1 
ATOM   6660  C CA  . PRO C 1 91  ? 43.499  -72.427 34.889  1.00 170.27 ? 91  PRO C CA  1 
ATOM   6661  C C   . PRO C 1 91  ? 42.119  -72.799 34.369  1.00 170.34 ? 91  PRO C C   1 
ATOM   6662  O O   . PRO C 1 91  ? 41.753  -72.462 33.240  1.00 167.12 ? 91  PRO C O   1 
ATOM   6663  C CB  . PRO C 1 91  ? 43.672  -70.906 34.993  1.00 174.21 ? 91  PRO C CB  1 
ATOM   6664  C CG  . PRO C 1 91  ? 45.015  -70.611 34.381  1.00 176.30 ? 91  PRO C CG  1 
ATOM   6665  C CD  . PRO C 1 91  ? 45.225  -71.668 33.346  1.00 170.27 ? 91  PRO C CD  1 
ATOM   6666  N N   . HIS C 1 92  ? 41.355  -73.502 35.202  1.00 171.25 ? 92  HIS C N   1 
ATOM   6667  C CA  . HIS C 1 92  ? 40.009  -73.919 34.830  1.00 176.21 ? 92  HIS C CA  1 
ATOM   6668  C C   . HIS C 1 92  ? 38.990  -73.393 35.831  1.00 179.76 ? 92  HIS C C   1 
ATOM   6669  O O   . HIS C 1 92  ? 38.138  -74.148 36.313  1.00 187.41 ? 92  HIS C O   1 
ATOM   6670  C CB  . HIS C 1 92  ? 39.922  -75.442 34.743  1.00 181.23 ? 92  HIS C CB  1 
ATOM   6671  C CG  . HIS C 1 92  ? 41.017  -76.067 33.939  1.00 180.24 ? 92  HIS C CG  1 
ATOM   6672  N ND1 . HIS C 1 92  ? 41.765  -77.130 34.399  1.00 179.85 ? 92  HIS C ND1 1 
ATOM   6673  C CD2 . HIS C 1 92  ? 41.488  -75.782 32.702  1.00 176.70 ? 92  HIS C CD2 1 
ATOM   6674  C CE1 . HIS C 1 92  ? 42.652  -77.470 33.482  1.00 179.25 ? 92  HIS C CE1 1 
ATOM   6675  N NE2 . HIS C 1 92  ? 42.504  -76.669 32.442  1.00 176.70 ? 92  HIS C NE2 1 
ATOM   6676  N N   . GLY C 1 93  ? 39.063  -72.101 36.140  1.00 179.89 ? 93  GLY C N   1 
ATOM   6677  C CA  . GLY C 1 93  ? 38.155  -71.504 37.099  1.00 185.58 ? 93  GLY C CA  1 
ATOM   6678  C C   . GLY C 1 93  ? 38.280  -72.108 38.482  1.00 193.01 ? 93  GLY C C   1 
ATOM   6679  O O   . GLY C 1 93  ? 39.244  -71.832 39.204  1.00 194.13 ? 93  GLY C O   1 
ATOM   6680  N N   . SER C 1 94  ? 37.304  -72.931 38.865  1.00 199.99 ? 94  SER C N   1 
ATOM   6681  C CA  . SER C 1 94  ? 37.285  -73.548 40.187  1.00 205.60 ? 94  SER C CA  1 
ATOM   6682  C C   . SER C 1 94  ? 37.249  -75.068 40.111  1.00 208.46 ? 94  SER C C   1 
ATOM   6683  O O   . SER C 1 94  ? 38.135  -75.725 40.667  1.00 208.54 ? 94  SER C O   1 
ATOM   6684  C CB  . SER C 1 94  ? 36.090  -73.019 40.990  1.00 221.61 ? 94  SER C CB  1 
ATOM   6685  O OG  . SER C 1 94  ? 36.134  -71.606 41.102  1.00 215.52 ? 94  SER C OG  1 
ATOM   6686  N N   . ALA C 1 95  ? 36.252  -75.648 39.437  1.00 220.29 ? 95  ALA C N   1 
ATOM   6687  C CA  . ALA C 1 95  ? 36.090  -77.100 39.441  1.00 220.30 ? 95  ALA C CA  1 
ATOM   6688  C C   . ALA C 1 95  ? 37.263  -77.792 38.755  1.00 206.94 ? 95  ALA C C   1 
ATOM   6689  O O   . ALA C 1 95  ? 37.847  -78.735 39.299  1.00 207.97 ? 95  ALA C O   1 
ATOM   6690  C CB  . ALA C 1 95  ? 34.770  -77.483 38.774  1.00 231.15 ? 95  ALA C CB  1 
ATOM   6691  N N   . GLY C 1 96  ? 37.608  -77.352 37.545  1.00 206.30 ? 96  GLY C N   1 
ATOM   6692  C CA  . GLY C 1 96  ? 38.763  -77.919 36.873  1.00 201.62 ? 96  GLY C CA  1 
ATOM   6693  C C   . GLY C 1 96  ? 40.082  -77.597 37.538  1.00 197.72 ? 96  GLY C C   1 
ATOM   6694  O O   . GLY C 1 96  ? 41.070  -78.303 37.308  1.00 196.33 ? 96  GLY C O   1 
ATOM   6695  N N   . ALA C 1 97  ? 40.122  -76.538 38.350  1.00 193.39 ? 97  ALA C N   1 
ATOM   6696  C CA  . ALA C 1 97  ? 41.353  -76.173 39.043  1.00 194.64 ? 97  ALA C CA  1 
ATOM   6697  C C   . ALA C 1 97  ? 41.799  -77.262 40.009  1.00 204.57 ? 97  ALA C C   1 
ATOM   6698  O O   . ALA C 1 97  ? 42.986  -77.606 40.061  1.00 200.02 ? 97  ALA C O   1 
ATOM   6699  C CB  . ALA C 1 97  ? 41.164  -74.851 39.785  1.00 195.13 ? 97  ALA C CB  1 
ATOM   6700  N N   . LEU C 1 98  ? 40.866  -77.813 40.783  1.00 227.03 ? 98  LEU C N   1 
ATOM   6701  C CA  . LEU C 1 98  ? 41.208  -78.804 41.791  1.00 228.15 ? 98  LEU C CA  1 
ATOM   6702  C C   . LEU C 1 98  ? 41.180  -80.233 41.267  1.00 229.48 ? 98  LEU C C   1 
ATOM   6703  O O   . LEU C 1 98  ? 41.857  -81.095 41.840  1.00 229.76 ? 98  LEU C O   1 
ATOM   6704  C CB  . LEU C 1 98  ? 40.263  -78.683 42.991  1.00 229.74 ? 98  LEU C CB  1 
ATOM   6705  C CG  . LEU C 1 98  ? 38.905  -79.375 42.860  1.00 231.68 ? 98  LEU C CG  1 
ATOM   6706  C CD1 . LEU C 1 98  ? 38.518  -80.089 44.145  1.00 233.75 ? 98  LEU C CD1 1 
ATOM   6707  C CD2 . LEU C 1 98  ? 37.824  -78.396 42.431  1.00 231.56 ? 98  LEU C CD2 1 
ATOM   6708  N N   . TYR C 1 99  ? 40.433  -80.510 40.194  1.00 214.54 ? 99  TYR C N   1 
ATOM   6709  C CA  . TYR C 1 99  ? 40.533  -81.825 39.569  1.00 211.90 ? 99  TYR C CA  1 
ATOM   6710  C C   . TYR C 1 99  ? 41.920  -82.026 38.979  1.00 206.56 ? 99  TYR C C   1 
ATOM   6711  O O   . TYR C 1 99  ? 42.473  -83.131 39.023  1.00 202.95 ? 99  TYR C O   1 
ATOM   6712  C CB  . TYR C 1 99  ? 39.463  -82.004 38.492  1.00 211.93 ? 99  TYR C CB  1 
ATOM   6713  C CG  . TYR C 1 99  ? 39.595  -83.321 37.763  1.00 214.60 ? 99  TYR C CG  1 
ATOM   6714  C CD1 . TYR C 1 99  ? 39.488  -84.522 38.452  1.00 210.27 ? 99  TYR C CD1 1 
ATOM   6715  C CD2 . TYR C 1 99  ? 39.837  -83.367 36.396  1.00 217.74 ? 99  TYR C CD2 1 
ATOM   6716  C CE1 . TYR C 1 99  ? 39.614  -85.728 37.803  1.00 207.71 ? 99  TYR C CE1 1 
ATOM   6717  C CE2 . TYR C 1 99  ? 39.962  -84.577 35.736  1.00 216.26 ? 99  TYR C CE2 1 
ATOM   6718  C CZ  . TYR C 1 99  ? 39.849  -85.752 36.446  1.00 210.88 ? 99  TYR C CZ  1 
ATOM   6719  O OH  . TYR C 1 99  ? 39.972  -86.959 35.800  1.00 209.93 ? 99  TYR C OH  1 
ATOM   6720  N N   . TYR C 1 100 ? 42.482  -80.968 38.395  1.00 199.87 ? 100 TYR C N   1 
ATOM   6721  C CA  . TYR C 1 100 ? 43.905  -80.927 38.100  1.00 194.95 ? 100 TYR C CA  1 
ATOM   6722  C C   . TYR C 1 100 ? 44.696  -81.275 39.355  1.00 197.19 ? 100 TYR C C   1 
ATOM   6723  O O   . TYR C 1 100 ? 44.372  -80.816 40.454  1.00 198.78 ? 100 TYR C O   1 
ATOM   6724  C CB  . TYR C 1 100 ? 44.283  -79.529 37.603  1.00 190.17 ? 100 TYR C CB  1 
ATOM   6725  C CG  . TYR C 1 100 ? 45.553  -79.438 36.785  1.00 186.25 ? 100 TYR C CG  1 
ATOM   6726  C CD1 . TYR C 1 100 ? 45.879  -78.265 36.118  1.00 180.21 ? 100 TYR C CD1 1 
ATOM   6727  C CD2 . TYR C 1 100 ? 46.431  -80.510 36.687  1.00 187.51 ? 100 TYR C CD2 1 
ATOM   6728  C CE1 . TYR C 1 100 ? 47.035  -78.163 35.376  1.00 177.28 ? 100 TYR C CE1 1 
ATOM   6729  C CE2 . TYR C 1 100 ? 47.592  -80.418 35.946  1.00 185.04 ? 100 TYR C CE2 1 
ATOM   6730  C CZ  . TYR C 1 100 ? 47.888  -79.241 35.292  1.00 180.86 ? 100 TYR C CZ  1 
ATOM   6731  O OH  . TYR C 1 100 ? 49.042  -79.141 34.551  1.00 182.44 ? 100 TYR C OH  1 
ATOM   6732  N N   . PHE C 1 101 ? 45.738  -82.088 39.176  1.00 197.77 ? 101 PHE C N   1 
ATOM   6733  C CA  . PHE C 1 101 ? 46.560  -82.638 40.260  1.00 192.64 ? 101 PHE C CA  1 
ATOM   6734  C C   . PHE C 1 101 ? 45.716  -83.035 41.471  1.00 189.51 ? 101 PHE C C   1 
ATOM   6735  O O   . PHE C 1 101 ? 45.976  -82.640 42.609  1.00 187.54 ? 101 PHE C O   1 
ATOM   6736  C CB  . PHE C 1 101 ? 47.689  -81.675 40.659  1.00 194.24 ? 101 PHE C CB  1 
ATOM   6737  C CG  . PHE C 1 101 ? 47.268  -80.234 40.784  1.00 198.91 ? 101 PHE C CG  1 
ATOM   6738  C CD1 . PHE C 1 101 ? 47.419  -79.360 39.719  1.00 198.92 ? 101 PHE C CD1 1 
ATOM   6739  C CD2 . PHE C 1 101 ? 46.735  -79.750 41.969  1.00 197.30 ? 101 PHE C CD2 1 
ATOM   6740  C CE1 . PHE C 1 101 ? 47.037  -78.037 39.829  1.00 194.22 ? 101 PHE C CE1 1 
ATOM   6741  C CE2 . PHE C 1 101 ? 46.350  -78.427 42.085  1.00 195.26 ? 101 PHE C CE2 1 
ATOM   6742  C CZ  . PHE C 1 101 ? 46.502  -77.569 41.014  1.00 192.92 ? 101 PHE C CZ  1 
ATOM   6743  N N   . ARG C 1 102 ? 44.691  -83.850 41.211  1.00 181.61 ? 102 ARG C N   1 
ATOM   6744  C CA  . ARG C 1 102 ? 43.940  -84.466 42.297  1.00 174.03 ? 102 ARG C CA  1 
ATOM   6745  C C   . ARG C 1 102 ? 44.776  -85.493 43.047  1.00 169.19 ? 102 ARG C C   1 
ATOM   6746  O O   . ARG C 1 102 ? 44.439  -85.843 44.183  1.00 168.98 ? 102 ARG C O   1 
ATOM   6747  C CB  . ARG C 1 102 ? 42.665  -85.120 41.757  1.00 170.36 ? 102 ARG C CB  1 
ATOM   6748  C CG  . ARG C 1 102 ? 42.906  -86.237 40.756  1.00 164.31 ? 102 ARG C CG  1 
ATOM   6749  C CD  . ARG C 1 102 ? 41.633  -87.030 40.489  1.00 164.57 ? 102 ARG C CD  1 
ATOM   6750  N NE  . ARG C 1 102 ? 41.209  -87.807 41.650  1.00 159.60 ? 102 ARG C NE  1 
ATOM   6751  C CZ  . ARG C 1 102 ? 40.172  -88.640 41.653  1.00 159.04 ? 102 ARG C CZ  1 
ATOM   6752  N NH1 . ARG C 1 102 ? 39.442  -88.795 40.558  1.00 164.89 ? 102 ARG C NH1 1 
ATOM   6753  N NH2 . ARG C 1 102 ? 39.858  -89.307 42.754  1.00 152.21 ? 102 ARG C NH2 1 
ATOM   6754  N N   . ASP C 1 103 ? 45.856  -85.980 42.433  1.00 165.69 ? 103 ASP C N   1 
ATOM   6755  C CA  . ASP C 1 103 ? 46.731  -86.938 43.098  1.00 165.87 ? 103 ASP C CA  1 
ATOM   6756  C C   . ASP C 1 103 ? 47.475  -86.295 44.261  1.00 172.51 ? 103 ASP C C   1 
ATOM   6757  O O   . ASP C 1 103 ? 47.603  -86.897 45.333  1.00 176.49 ? 103 ASP C O   1 
ATOM   6758  C CB  . ASP C 1 103 ? 47.715  -87.523 42.085  1.00 162.95 ? 103 ASP C CB  1 
ATOM   6759  C CG  . ASP C 1 103 ? 48.337  -86.458 41.201  1.00 165.32 ? 103 ASP C CG  1 
ATOM   6760  O OD1 . ASP C 1 103 ? 48.106  -85.258 41.462  1.00 167.06 ? 103 ASP C OD1 1 
ATOM   6761  O OD2 . ASP C 1 103 ? 49.052  -86.820 40.243  1.00 163.21 ? 103 ASP C OD2 1 
ATOM   6762  N N   . ARG C 1 104 ? 47.981  -85.074 44.065  1.00 173.44 ? 104 ARG C N   1 
ATOM   6763  C CA  . ARG C 1 104 ? 48.734  -84.405 45.120  1.00 174.46 ? 104 ARG C CA  1 
ATOM   6764  C C   . ARG C 1 104 ? 47.864  -84.089 46.330  1.00 177.59 ? 104 ARG C C   1 
ATOM   6765  O O   . ARG C 1 104 ? 48.360  -84.091 47.463  1.00 180.84 ? 104 ARG C O   1 
ATOM   6766  C CB  . ARG C 1 104 ? 49.375  -83.128 44.576  1.00 172.43 ? 104 ARG C CB  1 
ATOM   6767  C CG  . ARG C 1 104 ? 50.169  -83.335 43.294  1.00 169.94 ? 104 ARG C CG  1 
ATOM   6768  C CD  . ARG C 1 104 ? 50.695  -82.020 42.740  1.00 170.27 ? 104 ARG C CD  1 
ATOM   6769  N NE  . ARG C 1 104 ? 51.794  -81.483 43.539  1.00 166.21 ? 104 ARG C NE  1 
ATOM   6770  C CZ  . ARG C 1 104 ? 53.075  -81.561 43.192  1.00 158.92 ? 104 ARG C CZ  1 
ATOM   6771  N NH1 . ARG C 1 104 ? 53.424  -82.153 42.057  1.00 158.07 ? 104 ARG C NH1 1 
ATOM   6772  N NH2 . ARG C 1 104 ? 54.008  -81.045 43.980  1.00 152.35 ? 104 ARG C NH2 1 
ATOM   6773  N N   . ILE C 1 105 ? 46.578  -83.815 46.118  0.35 177.39 ? 105 ILE C N   1 
ATOM   6774  C CA  . ILE C 1 105 ? 45.694  -83.480 47.231  0.35 176.24 ? 105 ILE C CA  1 
ATOM   6775  C C   . ILE C 1 105 ? 45.298  -84.732 48.006  0.35 177.21 ? 105 ILE C C   1 
ATOM   6776  O O   . ILE C 1 105 ? 45.367  -84.765 49.239  0.35 183.53 ? 105 ILE C O   1 
ATOM   6777  C CB  . ILE C 1 105 ? 44.460  -82.715 46.722  0.35 169.02 ? 105 ILE C CB  1 
ATOM   6778  N N   . MET C 1 106 ? 44.884  -85.785 47.297  1.00 175.63 ? 106 MET C N   1 
ATOM   6779  C CA  . MET C 1 106 ? 44.536  -87.061 47.913  1.00 180.70 ? 106 MET C CA  1 
ATOM   6780  C C   . MET C 1 106 ? 45.745  -87.963 48.113  1.00 193.85 ? 106 MET C C   1 
ATOM   6781  O O   . MET C 1 106 ? 45.612  -89.194 48.075  1.00 197.75 ? 106 MET C O   1 
ATOM   6782  C CB  . MET C 1 106 ? 43.472  -87.777 47.080  1.00 168.18 ? 106 MET C CB  1 
ATOM   6783  C CG  . MET C 1 106 ? 42.080  -87.193 47.224  1.00 161.90 ? 106 MET C CG  1 
ATOM   6784  S SD  . MET C 1 106 ? 41.380  -87.526 48.851  1.00 177.67 ? 106 MET C SD  1 
ATOM   6785  C CE  . MET C 1 106 ? 40.272  -86.135 49.053  1.00 174.26 ? 106 MET C CE  1 
ATOM   6786  N N   . GLU C 1 107 ? 46.927  -87.382 48.321  1.00 205.80 ? 107 GLU C N   1 
ATOM   6787  C CA  . GLU C 1 107 ? 48.141  -88.174 48.463  1.00 213.07 ? 107 GLU C CA  1 
ATOM   6788  C C   . GLU C 1 107 ? 48.223  -88.862 49.823  1.00 227.47 ? 107 GLU C C   1 
ATOM   6789  O O   . GLU C 1 107 ? 48.789  -89.957 49.922  1.00 229.91 ? 107 GLU C O   1 
ATOM   6790  C CB  . GLU C 1 107 ? 49.361  -87.282 48.226  1.00 209.82 ? 107 GLU C CB  1 
ATOM   6791  C CG  . GLU C 1 107 ? 50.686  -88.015 48.132  1.00 213.93 ? 107 GLU C CG  1 
ATOM   6792  C CD  . GLU C 1 107 ? 51.805  -87.107 47.661  1.00 213.44 ? 107 GLU C CD  1 
ATOM   6793  O OE1 . GLU C 1 107 ? 51.682  -86.543 46.553  1.00 206.84 ? 107 GLU C OE1 1 
ATOM   6794  O OE2 . GLU C 1 107 ? 52.803  -86.953 48.396  1.00 221.94 ? 107 GLU C OE2 1 
ATOM   6795  N N   . GLU C 1 108 ? 47.672  -88.249 50.875  1.00 255.32 ? 108 GLU C N   1 
ATOM   6796  C CA  . GLU C 1 108 ? 47.649  -88.836 52.210  1.00 256.44 ? 108 GLU C CA  1 
ATOM   6797  C C   . GLU C 1 108 ? 46.291  -89.430 52.572  1.00 258.22 ? 108 GLU C C   1 
ATOM   6798  O O   . GLU C 1 108 ? 46.017  -89.649 53.758  1.00 258.82 ? 108 GLU C O   1 
ATOM   6799  C CB  . GLU C 1 108 ? 48.052  -87.797 53.260  1.00 261.23 ? 108 GLU C CB  1 
ATOM   6800  C CG  . GLU C 1 108 ? 49.444  -87.221 53.093  1.00 263.97 ? 108 GLU C CG  1 
ATOM   6801  C CD  . GLU C 1 108 ? 49.791  -86.234 54.192  1.00 266.95 ? 108 GLU C CD  1 
ATOM   6802  O OE1 . GLU C 1 108 ? 48.873  -85.543 54.685  1.00 263.96 ? 108 GLU C OE1 1 
ATOM   6803  O OE2 . GLU C 1 108 ? 50.979  -86.153 54.568  1.00 269.08 ? 108 GLU C OE2 1 
ATOM   6804  N N   . LYS C 1 109 ? 45.453  -89.709 51.578  1.00 240.36 ? 109 LYS C N   1 
ATOM   6805  C CA  . LYS C 1 109 ? 44.101  -90.220 51.786  1.00 239.03 ? 109 LYS C CA  1 
ATOM   6806  C C   . LYS C 1 109 ? 43.300  -89.429 52.820  1.00 240.35 ? 109 LYS C C   1 
ATOM   6807  O O   . LYS C 1 109 ? 42.886  -89.989 53.854  1.00 243.01 ? 109 LYS C O   1 
ATOM   6808  C CB  . LYS C 1 109 ? 44.148  -91.695 52.155  1.00 244.79 ? 109 LYS C CB  1 
ATOM   6809  C CG  . LYS C 1 109 ? 44.448  -92.626 50.988  1.00 243.43 ? 109 LYS C CG  1 
ATOM   6810  C CD  . LYS C 1 109 ? 44.555  -94.070 51.451  1.00 246.27 ? 109 LYS C CD  1 
ATOM   6811  C CE  . LYS C 1 109 ? 43.295  -94.506 52.183  1.00 246.35 ? 109 LYS C CE  1 
ATOM   6812  N NZ  . LYS C 1 109 ? 42.125  -94.576 51.269  1.00 242.77 ? 109 LYS C NZ  1 
ATOM   6813  N N   . PRO C 1 110 ? 43.055  -88.140 52.599  1.00 238.35 ? 110 PRO C N   1 
ATOM   6814  C CA  . PRO C 1 110 ? 42.238  -87.370 53.547  1.00 237.56 ? 110 PRO C CA  1 
ATOM   6815  C C   . PRO C 1 110 ? 40.756  -87.695 53.417  1.00 232.14 ? 110 PRO C C   1 
ATOM   6816  O O   . PRO C 1 110 ? 40.232  -87.878 52.315  1.00 225.37 ? 110 PRO C O   1 
ATOM   6817  C CB  . PRO C 1 110 ? 42.515  -85.910 53.155  1.00 228.65 ? 110 PRO C CB  1 
ATOM   6818  C CG  . PRO C 1 110 ? 43.693  -85.954 52.217  1.00 225.58 ? 110 PRO C CG  1 
ATOM   6819  C CD  . PRO C 1 110 ? 43.609  -87.277 51.542  1.00 225.59 ? 110 PRO C CD  1 
ATOM   6820  N N   . SER C 1 111 ? 40.079  -87.767 54.567  1.00 233.45 ? 111 SER C N   1 
ATOM   6821  C CA  . SER C 1 111 ? 38.644  -88.046 54.571  1.00 225.30 ? 111 SER C CA  1 
ATOM   6822  C C   . SER C 1 111 ? 37.853  -86.872 54.005  1.00 215.53 ? 111 SER C C   1 
ATOM   6823  O O   . SER C 1 111 ? 37.011  -87.047 53.117  1.00 210.45 ? 111 SER C O   1 
ATOM   6824  C CB  . SER C 1 111 ? 38.173  -88.378 55.988  1.00 222.04 ? 111 SER C CB  1 
ATOM   6825  O OG  . SER C 1 111 ? 36.757  -88.458 56.048  1.00 217.32 ? 111 SER C OG  1 
ATOM   6826  N N   . HIS C 1 112 ? 38.112  -85.667 54.507  1.00 221.88 ? 112 HIS C N   1 
ATOM   6827  C CA  . HIS C 1 112 ? 37.444  -84.457 54.053  1.00 216.46 ? 112 HIS C CA  1 
ATOM   6828  C C   . HIS C 1 112 ? 38.484  -83.451 53.581  1.00 215.41 ? 112 HIS C C   1 
ATOM   6829  O O   . HIS C 1 112 ? 39.596  -83.387 54.114  1.00 216.09 ? 112 HIS C O   1 
ATOM   6830  C CB  . HIS C 1 112 ? 36.589  -83.822 55.162  1.00 215.17 ? 112 HIS C CB  1 
ATOM   6831  C CG  . HIS C 1 112 ? 35.632  -84.769 55.817  1.00 216.39 ? 112 HIS C CG  1 
ATOM   6832  N ND1 . HIS C 1 112 ? 34.545  -85.301 55.159  1.00 216.72 ? 112 HIS C ND1 1 
ATOM   6833  C CD2 . HIS C 1 112 ? 35.590  -85.264 57.076  1.00 215.69 ? 112 HIS C CD2 1 
ATOM   6834  C CE1 . HIS C 1 112 ? 33.879  -86.091 55.982  1.00 217.64 ? 112 HIS C CE1 1 
ATOM   6835  N NE2 . HIS C 1 112 ? 34.493  -86.087 57.152  1.00 216.77 ? 112 HIS C NE2 1 
ATOM   6836  N N   . VAL C 1 113 ? 38.113  -82.661 52.576  1.00 193.34 ? 113 VAL C N   1 
ATOM   6837  C CA  . VAL C 1 113 ? 38.985  -81.644 51.999  1.00 177.90 ? 113 VAL C CA  1 
ATOM   6838  C C   . VAL C 1 113 ? 38.306  -80.287 52.131  1.00 170.60 ? 113 VAL C C   1 
ATOM   6839  O O   . VAL C 1 113 ? 37.146  -80.125 51.734  1.00 173.80 ? 113 VAL C O   1 
ATOM   6840  C CB  . VAL C 1 113 ? 39.329  -81.958 50.530  1.00 168.60 ? 113 VAL C CB  1 
ATOM   6841  C CG1 . VAL C 1 113 ? 38.084  -82.377 49.760  1.00 178.86 ? 113 VAL C CG1 1 
ATOM   6842  C CG2 . VAL C 1 113 ? 39.992  -80.754 49.875  1.00 168.09 ? 113 VAL C CG2 1 
ATOM   6843  N N   . PHE C 1 114 ? 39.025  -79.318 52.693  0.55 168.60 ? 114 PHE C N   1 
ATOM   6844  C CA  . PHE C 1 114 ? 38.519  -77.959 52.835  0.55 159.06 ? 114 PHE C CA  1 
ATOM   6845  C C   . PHE C 1 114 ? 38.773  -77.165 51.560  0.55 157.97 ? 114 PHE C C   1 
ATOM   6846  O O   . PHE C 1 114 ? 39.860  -77.231 50.977  0.55 168.71 ? 114 PHE C O   1 
ATOM   6847  C CB  . PHE C 1 114 ? 39.180  -77.260 54.025  0.55 155.19 ? 114 PHE C CB  1 
ATOM   6848  C CG  . PHE C 1 114 ? 38.623  -77.669 55.361  0.55 151.42 ? 114 PHE C CG  1 
ATOM   6849  C CD1 . PHE C 1 114 ? 37.420  -78.349 55.452  0.55 151.39 ? 114 PHE C CD1 1 
ATOM   6850  C CD2 . PHE C 1 114 ? 39.310  -77.375 56.527  0.55 153.98 ? 114 PHE C CD2 1 
ATOM   6851  C CE1 . PHE C 1 114 ? 36.912  -78.727 56.684  0.55 157.91 ? 114 PHE C CE1 1 
ATOM   6852  C CE2 . PHE C 1 114 ? 38.806  -77.750 57.759  0.55 160.35 ? 114 PHE C CE2 1 
ATOM   6853  C CZ  . PHE C 1 114 ? 37.606  -78.426 57.837  0.55 161.97 ? 114 PHE C CZ  1 
ATOM   6854  N N   . LEU C 1 115 ? 37.760  -76.417 51.127  0.31 141.31 ? 115 LEU C N   1 
ATOM   6855  C CA  . LEU C 1 115 ? 37.875  -75.552 49.955  0.31 136.93 ? 115 LEU C CA  1 
ATOM   6856  C C   . LEU C 1 115 ? 37.241  -74.206 50.279  0.31 133.02 ? 115 LEU C C   1 
ATOM   6857  O O   . LEU C 1 115 ? 36.018  -74.110 50.422  0.31 128.24 ? 115 LEU C O   1 
ATOM   6858  C CB  . LEU C 1 115 ? 37.219  -76.188 48.726  0.31 137.85 ? 115 LEU C CB  1 
ATOM   6859  C CG  . LEU C 1 115 ? 37.380  -75.444 47.393  0.31 133.62 ? 115 LEU C CG  1 
ATOM   6860  C CD1 . LEU C 1 115 ? 37.568  -76.430 46.256  0.31 153.23 ? 115 LEU C CD1 1 
ATOM   6861  C CD2 . LEU C 1 115 ? 36.181  -74.544 47.123  0.31 134.56 ? 115 LEU C CD2 1 
ATOM   6862  N N   . LEU C 1 116 ? 38.072  -73.174 50.403  0.05 141.31 ? 116 LEU C N   1 
ATOM   6863  C CA  . LEU C 1 116 ? 37.607  -71.816 50.635  0.05 141.10 ? 116 LEU C CA  1 
ATOM   6864  C C   . LEU C 1 116 ? 38.314  -70.866 49.677  0.05 153.52 ? 116 LEU C C   1 
ATOM   6865  O O   . LEU C 1 116 ? 39.399  -71.156 49.167  0.05 171.96 ? 116 LEU C O   1 
ATOM   6866  C CB  . LEU C 1 116 ? 37.835  -71.391 52.094  0.05 136.81 ? 116 LEU C CB  1 
ATOM   6867  N N   . ASN C 1 117 ? 37.684  -69.720 49.436  1.00 148.42 ? 117 ASN C N   1 
ATOM   6868  C CA  . ASN C 1 117 ? 38.198  -68.751 48.479  1.00 160.50 ? 117 ASN C CA  1 
ATOM   6869  C C   . ASN C 1 117 ? 39.066  -67.705 49.175  1.00 160.66 ? 117 ASN C C   1 
ATOM   6870  O O   . ASN C 1 117 ? 39.034  -67.543 50.397  1.00 156.77 ? 117 ASN C O   1 
ATOM   6871  C CB  . ASN C 1 117 ? 37.048  -68.071 47.732  1.00 151.18 ? 117 ASN C CB  1 
ATOM   6872  C CG  . ASN C 1 117 ? 37.508  -67.350 46.479  1.00 151.38 ? 117 ASN C CG  1 
ATOM   6873  O OD1 . ASN C 1 117 ? 38.612  -67.579 45.985  1.00 161.89 ? 117 ASN C OD1 1 
ATOM   6874  N ND2 . ASN C 1 117 ? 36.661  -66.468 45.961  1.00 144.61 ? 117 ASN C ND2 1 
ATOM   6875  N N   . CYS C 1 118 ? 39.850  -66.989 48.367  1.00 166.74 ? 118 CYS C N   1 
ATOM   6876  C CA  . CYS C 1 118 ? 40.749  -65.972 48.905  1.00 164.35 ? 118 CYS C CA  1 
ATOM   6877  C C   . CYS C 1 118 ? 39.974  -64.758 49.404  1.00 155.87 ? 118 CYS C C   1 
ATOM   6878  O O   . CYS C 1 118 ? 40.148  -64.325 50.549  1.00 154.12 ? 118 CYS C O   1 
ATOM   6879  C CB  . CYS C 1 118 ? 41.771  -65.565 47.843  1.00 185.89 ? 118 CYS C CB  1 
ATOM   6880  S SG  . CYS C 1 118 ? 42.708  -64.072 48.229  1.00 201.93 ? 118 CYS C SG  1 
ATOM   6881  N N   . ASP C 1 119 ? 39.112  -64.195 48.558  1.00 153.33 ? 119 ASP C N   1 
ATOM   6882  C CA  . ASP C 1 119 ? 38.405  -62.958 48.889  1.00 151.12 ? 119 ASP C CA  1 
ATOM   6883  C C   . ASP C 1 119 ? 37.111  -63.280 49.639  1.00 149.72 ? 119 ASP C C   1 
ATOM   6884  O O   . ASP C 1 119 ? 35.994  -63.116 49.142  1.00 149.60 ? 119 ASP C O   1 
ATOM   6885  C CB  . ASP C 1 119 ? 38.145  -62.146 47.626  1.00 148.72 ? 119 ASP C CB  1 
ATOM   6886  C CG  . ASP C 1 119 ? 37.622  -62.995 46.485  1.00 146.69 ? 119 ASP C CG  1 
ATOM   6887  O OD1 . ASP C 1 119 ? 37.446  -64.215 46.685  1.00 148.84 ? 119 ASP C OD1 1 
ATOM   6888  O OD2 . ASP C 1 119 ? 37.391  -62.443 45.388  1.00 146.06 ? 119 ASP C OD2 1 
ATOM   6889  N N   . VAL C 1 120 ? 37.289  -63.745 50.874  1.00 152.03 ? 120 VAL C N   1 
ATOM   6890  C CA  . VAL C 1 120 ? 36.190  -64.075 51.775  1.00 158.56 ? 120 VAL C CA  1 
ATOM   6891  C C   . VAL C 1 120 ? 36.585  -63.624 53.175  1.00 168.32 ? 120 VAL C C   1 
ATOM   6892  O O   . VAL C 1 120 ? 37.720  -63.848 53.610  1.00 166.07 ? 120 VAL C O   1 
ATOM   6893  C CB  . VAL C 1 120 ? 35.861  -65.584 51.750  1.00 157.76 ? 120 VAL C CB  1 
ATOM   6894  C CG1 . VAL C 1 120 ? 34.973  -65.965 52.925  1.00 171.63 ? 120 VAL C CG1 1 
ATOM   6895  C CG2 . VAL C 1 120 ? 35.194  -65.968 50.436  1.00 155.13 ? 120 VAL C CG2 1 
ATOM   6896  N N   . CYS C 1 121 ? 35.648  -62.986 53.884  1.00 186.27 ? 121 CYS C N   1 
ATOM   6897  C CA  . CYS C 1 121 ? 35.897  -62.444 55.224  1.00 186.90 ? 121 CYS C CA  1 
ATOM   6898  C C   . CYS C 1 121 ? 34.774  -62.888 56.156  1.00 194.36 ? 121 CYS C C   1 
ATOM   6899  O O   . CYS C 1 121 ? 33.852  -62.124 56.444  1.00 201.05 ? 121 CYS C O   1 
ATOM   6900  C CB  . CYS C 1 121 ? 36.028  -60.928 55.184  1.00 184.44 ? 121 CYS C CB  1 
ATOM   6901  S SG  . CYS C 1 121 ? 37.535  -60.350 54.385  1.00 190.06 ? 121 CYS C SG  1 
ATOM   6902  N N   . CYS C 1 122 ? 34.869  -64.119 56.640  1.00 203.08 ? 122 CYS C N   1 
ATOM   6903  C CA  . CYS C 1 122 ? 33.926  -64.669 57.602  1.00 215.60 ? 122 CYS C CA  1 
ATOM   6904  C C   . CYS C 1 122 ? 34.670  -65.035 58.883  1.00 216.76 ? 122 CYS C C   1 
ATOM   6905  O O   . CYS C 1 122 ? 35.865  -64.768 59.033  1.00 208.63 ? 122 CYS C O   1 
ATOM   6906  C CB  . CYS C 1 122 ? 33.195  -65.883 57.019  1.00 210.76 ? 122 CYS C CB  1 
ATOM   6907  S SG  . CYS C 1 122 ? 34.289  -67.176 56.393  1.00 206.63 ? 122 CYS C SG  1 
ATOM   6908  N N   . SER C 1 123 ? 33.944  -65.641 59.823  1.00 222.00 ? 123 SER C N   1 
ATOM   6909  C CA  . SER C 1 123 ? 34.550  -66.043 61.086  1.00 218.39 ? 123 SER C CA  1 
ATOM   6910  C C   . SER C 1 123 ? 35.340  -67.338 60.967  1.00 215.33 ? 123 SER C C   1 
ATOM   6911  O O   . SER C 1 123 ? 36.139  -67.642 61.859  1.00 213.80 ? 123 SER C O   1 
ATOM   6912  C CB  . SER C 1 123 ? 33.475  -66.192 62.165  1.00 221.00 ? 123 SER C CB  1 
ATOM   6913  O OG  . SER C 1 123 ? 32.509  -67.161 61.796  1.00 216.63 ? 123 SER C OG  1 
ATOM   6914  N N   . PHE C 1 124 ? 35.131  -68.100 59.891  1.00 217.83 ? 124 PHE C N   1 
ATOM   6915  C CA  . PHE C 1 124 ? 35.817  -69.359 59.625  1.00 216.70 ? 124 PHE C CA  1 
ATOM   6916  C C   . PHE C 1 124 ? 35.641  -70.345 60.775  1.00 222.98 ? 124 PHE C C   1 
ATOM   6917  O O   . PHE C 1 124 ? 36.592  -70.596 61.527  1.00 219.18 ? 124 PHE C O   1 
ATOM   6918  C CB  . PHE C 1 124 ? 37.306  -69.119 59.362  1.00 207.12 ? 124 PHE C CB  1 
ATOM   6919  C CG  . PHE C 1 124 ? 37.581  -68.328 58.116  1.00 199.30 ? 124 PHE C CG  1 
ATOM   6920  C CD1 . PHE C 1 124 ? 37.564  -68.941 56.875  1.00 189.75 ? 124 PHE C CD1 1 
ATOM   6921  C CD2 . PHE C 1 124 ? 37.865  -66.975 58.186  1.00 196.30 ? 124 PHE C CD2 1 
ATOM   6922  C CE1 . PHE C 1 124 ? 37.819  -68.218 55.726  1.00 181.80 ? 124 PHE C CE1 1 
ATOM   6923  C CE2 . PHE C 1 124 ? 38.121  -66.245 57.041  1.00 186.76 ? 124 PHE C CE2 1 
ATOM   6924  C CZ  . PHE C 1 124 ? 38.098  -66.868 55.809  1.00 181.89 ? 124 PHE C CZ  1 
ATOM   6925  N N   . PRO C 1 125 ? 34.448  -70.918 60.954  1.00 247.45 ? 125 PRO C N   1 
ATOM   6926  C CA  . PRO C 1 125 ? 34.256  -71.960 61.978  1.00 247.93 ? 125 PRO C CA  1 
ATOM   6927  C C   . PRO C 1 125 ? 34.559  -73.348 61.417  1.00 248.34 ? 125 PRO C C   1 
ATOM   6928  O O   . PRO C 1 125 ? 33.685  -74.217 61.317  1.00 249.41 ? 125 PRO C O   1 
ATOM   6929  C CB  . PRO C 1 125 ? 32.779  -71.783 62.357  1.00 249.31 ? 125 PRO C CB  1 
ATOM   6930  C CG  . PRO C 1 125 ? 32.174  -70.831 61.308  1.00 248.75 ? 125 PRO C CG  1 
ATOM   6931  C CD  . PRO C 1 125 ? 33.195  -70.643 60.236  1.00 247.54 ? 125 PRO C CD  1 
ATOM   6932  N N   . LEU C 1 126 ? 35.824  -73.553 61.043  1.00 215.70 ? 126 LEU C N   1 
ATOM   6933  C CA  . LEU C 1 126 ? 36.210  -74.756 60.313  1.00 205.19 ? 126 LEU C CA  1 
ATOM   6934  C C   . LEU C 1 126 ? 35.951  -76.019 61.129  1.00 200.80 ? 126 LEU C C   1 
ATOM   6935  O O   . LEU C 1 126 ? 35.570  -77.056 60.574  1.00 202.22 ? 126 LEU C O   1 
ATOM   6936  C CB  . LEU C 1 126 ? 37.680  -74.664 59.910  1.00 191.78 ? 126 LEU C CB  1 
ATOM   6937  C CG  . LEU C 1 126 ? 38.098  -73.477 59.039  1.00 191.63 ? 126 LEU C CG  1 
ATOM   6938  C CD1 . LEU C 1 126 ? 39.560  -73.597 58.634  1.00 186.13 ? 126 LEU C CD1 1 
ATOM   6939  C CD2 . LEU C 1 126 ? 37.208  -73.370 57.812  1.00 192.88 ? 126 LEU C CD2 1 
ATOM   6940  N N   . GLN C 1 127 ? 36.149  -75.952 62.448  1.00 191.41 ? 127 GLN C N   1 
ATOM   6941  C CA  . GLN C 1 127 ? 35.931  -77.118 63.294  1.00 180.43 ? 127 GLN C CA  1 
ATOM   6942  C C   . GLN C 1 127 ? 34.452  -77.411 63.515  1.00 189.52 ? 127 GLN C C   1 
ATOM   6943  O O   . GLN C 1 127 ? 34.094  -78.564 63.780  1.00 184.54 ? 127 GLN C O   1 
ATOM   6944  C CB  . GLN C 1 127 ? 36.633  -76.923 64.640  1.00 165.33 ? 127 GLN C CB  1 
ATOM   6945  C CG  . GLN C 1 127 ? 36.777  -78.194 65.467  1.00 154.59 ? 127 GLN C CG  1 
ATOM   6946  C CD  . GLN C 1 127 ? 37.653  -77.997 66.687  1.00 152.40 ? 127 GLN C CD  1 
ATOM   6947  O OE1 . GLN C 1 127 ? 38.307  -76.964 66.835  1.00 156.23 ? 127 GLN C OE1 1 
ATOM   6948  N NE2 . GLN C 1 127 ? 37.679  -78.993 67.565  1.00 145.98 ? 127 GLN C NE2 1 
ATOM   6949  N N   . GLY C 1 128 ? 33.590  -76.403 63.400  1.00 202.41 ? 128 GLY C N   1 
ATOM   6950  C CA  . GLY C 1 128 ? 32.164  -76.603 63.562  1.00 208.13 ? 128 GLY C CA  1 
ATOM   6951  C C   . GLY C 1 128 ? 31.506  -77.140 62.308  1.00 226.66 ? 128 GLY C C   1 
ATOM   6952  O O   . GLY C 1 128 ? 30.595  -77.971 62.378  1.00 216.11 ? 128 GLY C O   1 
ATOM   6953  N N   . ILE C 1 129 ? 31.963  -76.665 61.149  1.00 297.41 ? 129 ILE C N   1 
ATOM   6954  C CA  . ILE C 1 129 ? 31.415  -77.148 59.888  1.00 298.14 ? 129 ILE C CA  1 
ATOM   6955  C C   . ILE C 1 129 ? 31.944  -78.543 59.563  1.00 298.47 ? 129 ILE C C   1 
ATOM   6956  O O   . ILE C 1 129 ? 31.240  -79.347 58.940  1.00 299.32 ? 129 ILE C O   1 
ATOM   6957  C CB  . ILE C 1 129 ? 31.716  -76.136 58.766  1.00 297.24 ? 129 ILE C CB  1 
ATOM   6958  C CG1 . ILE C 1 129 ? 31.142  -76.608 57.433  1.00 297.97 ? 129 ILE C CG1 1 
ATOM   6959  C CG2 . ILE C 1 129 ? 33.211  -75.914 58.631  1.00 295.91 ? 129 ILE C CG2 1 
ATOM   6960  C CD1 . ILE C 1 129 ? 29.686  -76.960 57.470  1.00 299.46 ? 129 ILE C CD1 1 
ATOM   6961  N N   . LEU C 1 130 ? 33.172  -78.859 59.982  1.00 229.59 ? 130 LEU C N   1 
ATOM   6962  C CA  . LEU C 1 130 ? 33.703  -80.205 59.786  1.00 207.69 ? 130 LEU C CA  1 
ATOM   6963  C C   . LEU C 1 130 ? 32.846  -81.235 60.511  1.00 200.85 ? 130 LEU C C   1 
ATOM   6964  O O   . LEU C 1 130 ? 32.468  -82.264 59.938  1.00 197.96 ? 130 LEU C O   1 
ATOM   6965  C CB  . LEU C 1 130 ? 35.153  -80.268 60.273  1.00 199.95 ? 130 LEU C CB  1 
ATOM   6966  C CG  . LEU C 1 130 ? 36.128  -81.308 59.703  1.00 192.96 ? 130 LEU C CG  1 
ATOM   6967  C CD1 . LEU C 1 130 ? 37.528  -81.028 60.214  1.00 188.07 ? 130 LEU C CD1 1 
ATOM   6968  C CD2 . LEU C 1 130 ? 35.732  -82.736 60.039  1.00 186.62 ? 130 LEU C CD2 1 
ATOM   6969  N N   . ASP C 1 131 ? 32.529  -80.973 61.781  1.00 196.99 ? 131 ASP C N   1 
ATOM   6970  C CA  . ASP C 1 131 ? 31.713  -81.906 62.548  1.00 183.66 ? 131 ASP C CA  1 
ATOM   6971  C C   . ASP C 1 131 ? 30.267  -81.901 62.074  1.00 188.08 ? 131 ASP C C   1 
ATOM   6972  O O   . ASP C 1 131 ? 29.592  -82.935 62.137  1.00 182.54 ? 131 ASP C O   1 
ATOM   6973  C CB  . ASP C 1 131 ? 31.797  -81.570 64.034  1.00 169.05 ? 131 ASP C CB  1 
ATOM   6974  C CG  . ASP C 1 131 ? 33.227  -81.488 64.529  1.00 164.19 ? 131 ASP C CG  1 
ATOM   6975  O OD1 . ASP C 1 131 ? 34.109  -82.119 63.908  1.00 163.29 ? 131 ASP C OD1 1 
ATOM   6976  O OD2 . ASP C 1 131 ? 33.471  -80.786 65.531  1.00 163.38 ? 131 ASP C OD2 1 
ATOM   6977  N N   . ALA C 1 132 ? 29.773  -80.753 61.604  1.00 193.27 ? 132 ALA C N   1 
ATOM   6978  C CA  . ALA C 1 132 ? 28.438  -80.718 61.021  1.00 192.36 ? 132 ALA C CA  1 
ATOM   6979  C C   . ALA C 1 132 ? 28.379  -81.517 59.726  1.00 192.26 ? 132 ALA C C   1 
ATOM   6980  O O   . ALA C 1 132 ? 27.343  -82.115 59.416  1.00 191.25 ? 132 ALA C O   1 
ATOM   6981  C CB  . ALA C 1 132 ? 28.003  -79.273 60.777  1.00 198.69 ? 132 ALA C CB  1 
ATOM   6982  N N   . HIS C 1 133 ? 29.480  -81.555 58.970  1.00 196.25 ? 133 HIS C N   1 
ATOM   6983  C CA  . HIS C 1 133 ? 29.503  -82.345 57.745  1.00 191.19 ? 133 HIS C CA  1 
ATOM   6984  C C   . HIS C 1 133 ? 29.595  -83.832 58.055  1.00 188.47 ? 133 HIS C C   1 
ATOM   6985  O O   . HIS C 1 133 ? 29.004  -84.658 57.348  1.00 188.13 ? 133 HIS C O   1 
ATOM   6986  C CB  . HIS C 1 133 ? 30.667  -81.918 56.854  1.00 191.97 ? 133 HIS C CB  1 
ATOM   6987  C CG  . HIS C 1 133 ? 30.798  -82.735 55.607  1.00 190.74 ? 133 HIS C CG  1 
ATOM   6988  N ND1 . HIS C 1 133 ? 29.714  -83.071 54.825  1.00 186.82 ? 133 HIS C ND1 1 
ATOM   6989  C CD2 . HIS C 1 133 ? 31.881  -83.279 55.002  1.00 193.10 ? 133 HIS C CD2 1 
ATOM   6990  C CE1 . HIS C 1 133 ? 30.122  -83.790 53.795  1.00 186.99 ? 133 HIS C CE1 1 
ATOM   6991  N NE2 . HIS C 1 133 ? 31.433  -83.930 53.878  1.00 188.72 ? 133 HIS C NE2 1 
ATOM   6992  N N   . ARG C 1 134 ? 30.344  -84.191 59.099  1.00 189.92 ? 134 ARG C N   1 
ATOM   6993  C CA  . ARG C 1 134 ? 30.423  -85.588 59.507  1.00 185.34 ? 134 ARG C CA  1 
ATOM   6994  C C   . ARG C 1 134 ? 29.052  -86.122 59.898  1.00 190.98 ? 134 ARG C C   1 
ATOM   6995  O O   . ARG C 1 134 ? 28.736  -87.290 59.645  1.00 188.52 ? 134 ARG C O   1 
ATOM   6996  C CB  . ARG C 1 134 ? 31.407  -85.736 60.667  1.00 174.49 ? 134 ARG C CB  1 
ATOM   6997  C CG  . ARG C 1 134 ? 32.864  -85.642 60.263  1.00 174.35 ? 134 ARG C CG  1 
ATOM   6998  C CD  . ARG C 1 134 ? 33.762  -85.630 61.485  1.00 168.74 ? 134 ARG C CD  1 
ATOM   6999  N NE  . ARG C 1 134 ? 35.166  -85.776 61.125  1.00 171.06 ? 134 ARG C NE  1 
ATOM   7000  C CZ  . ARG C 1 134 ? 36.177  -85.611 61.970  1.00 168.03 ? 134 ARG C CZ  1 
ATOM   7001  N NH1 . ARG C 1 134 ? 35.945  -85.283 63.234  1.00 150.99 ? 134 ARG C NH1 1 
ATOM   7002  N NH2 . ARG C 1 134 ? 37.421  -85.772 61.547  1.00 176.01 ? 134 ARG C NH2 1 
ATOM   7003  N N   . ARG C 1 135 ? 28.222  -85.280 60.516  1.00 202.79 ? 135 ARG C N   1 
ATOM   7004  C CA  . ARG C 1 135 ? 26.869  -85.700 60.859  1.00 203.99 ? 135 ARG C CA  1 
ATOM   7005  C C   . ARG C 1 135 ? 25.956  -85.696 59.640  1.00 204.81 ? 135 ARG C C   1 
ATOM   7006  O O   . ARG C 1 135 ? 25.192  -86.644 59.432  1.00 207.41 ? 135 ARG C O   1 
ATOM   7007  C CB  . ARG C 1 135 ? 26.294  -84.802 61.954  1.00 207.12 ? 135 ARG C CB  1 
ATOM   7008  C CG  . ARG C 1 135 ? 24.813  -85.028 62.199  1.00 213.50 ? 135 ARG C CG  1 
ATOM   7009  C CD  . ARG C 1 135 ? 24.300  -84.213 63.370  1.00 221.22 ? 135 ARG C CD  1 
ATOM   7010  N NE  . ARG C 1 135 ? 22.841  -84.226 63.432  1.00 222.52 ? 135 ARG C NE  1 
ATOM   7011  C CZ  . ARG C 1 135 ? 22.063  -83.268 62.941  1.00 219.36 ? 135 ARG C CZ  1 
ATOM   7012  N NH1 . ARG C 1 135 ? 22.603  -82.209 62.355  1.00 210.08 ? 135 ARG C NH1 1 
ATOM   7013  N NH2 . ARG C 1 135 ? 20.745  -83.365 63.039  1.00 224.21 ? 135 ARG C NH2 1 
ATOM   7014  N N   . TYR C 1 136 ? 26.024  -84.641 58.823  1.00 193.44 ? 136 TYR C N   1 
ATOM   7015  C CA  . TYR C 1 136 ? 25.195  -84.585 57.623  1.00 191.18 ? 136 TYR C CA  1 
ATOM   7016  C C   . TYR C 1 136 ? 25.574  -85.681 56.637  1.00 194.73 ? 136 TYR C C   1 
ATOM   7017  O O   . TYR C 1 136 ? 24.698  -86.311 56.033  1.00 192.40 ? 136 TYR C O   1 
ATOM   7018  C CB  . TYR C 1 136 ? 25.304  -83.205 56.970  1.00 187.44 ? 136 TYR C CB  1 
ATOM   7019  C CG  . TYR C 1 136 ? 24.701  -82.087 57.790  1.00 185.07 ? 136 TYR C CG  1 
ATOM   7020  C CD1 . TYR C 1 136 ? 23.661  -82.332 58.675  1.00 187.74 ? 136 TYR C CD1 1 
ATOM   7021  C CD2 . TYR C 1 136 ? 25.173  -80.785 57.682  1.00 181.33 ? 136 TYR C CD2 1 
ATOM   7022  C CE1 . TYR C 1 136 ? 23.106  -81.312 59.425  1.00 187.08 ? 136 TYR C CE1 1 
ATOM   7023  C CE2 . TYR C 1 136 ? 24.628  -79.761 58.431  1.00 179.00 ? 136 TYR C CE2 1 
ATOM   7024  C CZ  . TYR C 1 136 ? 23.594  -80.029 59.300  1.00 179.77 ? 136 TYR C CZ  1 
ATOM   7025  O OH  . TYR C 1 136 ? 23.046  -79.012 60.048  1.00 175.59 ? 136 TYR C OH  1 
ATOM   7026  N N   . GLY C 1 137 ? 26.870  -85.919 56.455  1.00 220.93 ? 137 GLY C N   1 
ATOM   7027  C CA  . GLY C 1 137 ? 27.300  -86.862 55.445  1.00 220.98 ? 137 GLY C CA  1 
ATOM   7028  C C   . GLY C 1 137 ? 27.193  -86.263 54.053  1.00 220.66 ? 137 GLY C C   1 
ATOM   7029  O O   . GLY C 1 137 ? 27.292  -85.050 53.860  1.00 220.01 ? 137 GLY C O   1 
ATOM   7030  N N   . GLY C 1 138 ? 26.977  -87.136 53.073  1.00 190.17 ? 138 GLY C N   1 
ATOM   7031  C CA  . GLY C 1 138 ? 26.897  -86.678 51.706  1.00 178.25 ? 138 GLY C CA  1 
ATOM   7032  C C   . GLY C 1 138 ? 28.248  -86.177 51.226  1.00 174.73 ? 138 GLY C C   1 
ATOM   7033  O O   . GLY C 1 138 ? 29.295  -86.415 51.828  1.00 175.00 ? 138 GLY C O   1 
ATOM   7034  N N   . ILE C 1 139 ? 28.204  -85.465 50.106  1.00 166.03 ? 139 ILE C N   1 
ATOM   7035  C CA  . ILE C 1 139 ? 29.423  -84.954 49.496  1.00 168.85 ? 139 ILE C CA  1 
ATOM   7036  C C   . ILE C 1 139 ? 29.910  -83.735 50.272  1.00 177.30 ? 139 ILE C C   1 
ATOM   7037  O O   . ILE C 1 139 ? 30.931  -83.806 50.963  1.00 181.12 ? 139 ILE C O   1 
ATOM   7038  C CB  . ILE C 1 139 ? 29.206  -84.614 48.013  1.00 168.99 ? 139 ILE C CB  1 
ATOM   7039  C CG1 . ILE C 1 139 ? 28.693  -85.839 47.250  1.00 169.21 ? 139 ILE C CG1 1 
ATOM   7040  C CG2 . ILE C 1 139 ? 30.504  -84.110 47.402  1.00 189.46 ? 139 ILE C CG2 1 
ATOM   7041  C CD1 . ILE C 1 139 ? 29.689  -86.968 47.143  1.00 176.88 ? 139 ILE C CD1 1 
ATOM   7042  N N   . GLY C 1 140 ? 29.164  -82.626 50.195  1.00 189.41 ? 140 GLY C N   1 
ATOM   7043  C CA  . GLY C 1 140 ? 29.573  -81.348 50.761  1.00 199.16 ? 140 GLY C CA  1 
ATOM   7044  C C   . GLY C 1 140 ? 28.676  -80.800 51.857  1.00 198.90 ? 140 GLY C C   1 
ATOM   7045  O O   . GLY C 1 140 ? 27.769  -81.492 52.323  1.00 192.68 ? 140 GLY C O   1 
ATOM   7046  N N   . THR C 1 141 ? 28.925  -79.561 52.293  1.00 202.91 ? 141 THR C N   1 
ATOM   7047  C CA  . THR C 1 141 ? 28.118  -78.959 53.348  1.00 203.64 ? 141 THR C CA  1 
ATOM   7048  C C   . THR C 1 141 ? 27.963  -77.454 53.176  1.00 200.73 ? 141 THR C C   1 
ATOM   7049  O O   . THR C 1 141 ? 27.141  -76.841 53.856  1.00 198.93 ? 141 THR C O   1 
ATOM   7050  C CB  . THR C 1 141 ? 28.729  -79.263 54.713  1.00 206.50 ? 141 THR C CB  1 
ATOM   7051  O OG1 . THR C 1 141 ? 29.947  -79.985 54.515  1.00 206.09 ? 141 THR C OG1 1 
ATOM   7052  C CG2 . THR C 1 141 ? 27.786  -80.107 55.545  1.00 200.81 ? 141 THR C CG2 1 
ATOM   7053  N N   . VAL C 1 144 ? 26.152  -70.940 54.724  1.00 202.58 ? 144 VAL C N   1 
ATOM   7054  C CA  . VAL C 1 144 ? 25.157  -69.918 54.428  1.00 202.90 ? 144 VAL C CA  1 
ATOM   7055  C C   . VAL C 1 144 ? 25.127  -68.897 55.560  1.00 203.87 ? 144 VAL C C   1 
ATOM   7056  O O   . VAL C 1 144 ? 25.697  -69.100 56.633  1.00 202.82 ? 144 VAL C O   1 
ATOM   7057  C CB  . VAL C 1 144 ? 23.748  -70.507 54.200  1.00 202.52 ? 144 VAL C CB  1 
ATOM   7058  C CG1 . VAL C 1 144 ? 23.681  -71.256 52.876  1.00 200.26 ? 144 VAL C CG1 1 
ATOM   7059  C CG2 . VAL C 1 144 ? 23.349  -71.407 55.352  1.00 202.11 ? 144 VAL C CG2 1 
ATOM   7060  N N   . ILE C 1 145 ? 24.453  -67.780 55.298  1.00 195.63 ? 145 ILE C N   1 
ATOM   7061  C CA  . ILE C 1 145 ? 24.290  -66.715 56.286  1.00 192.77 ? 145 ILE C CA  1 
ATOM   7062  C C   . ILE C 1 145 ? 23.003  -65.962 55.977  1.00 188.51 ? 145 ILE C C   1 
ATOM   7063  O O   . ILE C 1 145 ? 22.738  -65.611 54.823  1.00 187.41 ? 145 ILE C O   1 
ATOM   7064  C CB  . ILE C 1 145 ? 25.505  -65.760 56.321  1.00 191.13 ? 145 ILE C CB  1 
ATOM   7065  C CG1 . ILE C 1 145 ? 25.284  -64.635 57.338  1.00 191.50 ? 145 ILE C CG1 1 
ATOM   7066  C CG2 . ILE C 1 145 ? 25.800  -65.189 54.938  1.00 189.24 ? 145 ILE C CG2 1 
ATOM   7067  C CD1 . ILE C 1 145 ? 26.515  -63.780 57.584  1.00 203.22 ? 145 ILE C CD1 1 
ATOM   7068  N N   . LYS C 1 146 ? 22.197  -65.726 57.009  1.00 188.27 ? 146 LYS C N   1 
ATOM   7069  C CA  . LYS C 1 146 ? 20.907  -65.073 56.826  1.00 186.78 ? 146 LYS C CA  1 
ATOM   7070  C C   . LYS C 1 146 ? 21.102  -63.601 56.483  1.00 187.50 ? 146 LYS C C   1 
ATOM   7071  O O   . LYS C 1 146 ? 21.675  -62.841 57.270  1.00 183.97 ? 146 LYS C O   1 
ATOM   7072  C CB  . LYS C 1 146 ? 20.055  -65.224 58.083  1.00 179.74 ? 146 LYS C CB  1 
ATOM   7073  C CG  . LYS C 1 146 ? 19.729  -66.663 58.442  1.00 172.89 ? 146 LYS C CG  1 
ATOM   7074  C CD  . LYS C 1 146 ? 18.834  -66.736 59.669  1.00 160.88 ? 146 LYS C CD  1 
ATOM   7075  C CE  . LYS C 1 146 ? 18.467  -68.174 59.997  1.00 157.84 ? 146 LYS C CE  1 
ATOM   7076  N NZ  . LYS C 1 146 ? 17.573  -68.268 61.184  1.00 156.41 ? 146 LYS C NZ  1 
ATOM   7077  N N   . VAL C 1 147 ? 20.619  -63.201 55.309  1.00 192.51 ? 147 VAL C N   1 
ATOM   7078  C CA  . VAL C 1 147 ? 20.686  -61.821 54.855  1.00 190.53 ? 147 VAL C CA  1 
ATOM   7079  C C   . VAL C 1 147 ? 19.271  -61.361 54.522  1.00 199.30 ? 147 VAL C C   1 
ATOM   7080  O O   . VAL C 1 147 ? 18.345  -62.162 54.398  1.00 206.04 ? 147 VAL C O   1 
ATOM   7081  C CB  . VAL C 1 147 ? 21.621  -61.644 53.641  1.00 185.48 ? 147 VAL C CB  1 
ATOM   7082  C CG1 . VAL C 1 147 ? 23.004  -62.204 53.944  1.00 182.81 ? 147 VAL C CG1 1 
ATOM   7083  C CG2 . VAL C 1 147 ? 21.029  -62.312 52.408  1.00 188.82 ? 147 VAL C CG2 1 
ATOM   7084  N N   . SER C 1 148 ? 19.116  -60.049 54.378  1.00 195.81 ? 148 SER C N   1 
ATOM   7085  C CA  . SER C 1 148 ? 17.819  -59.487 54.033  1.00 203.63 ? 148 SER C CA  1 
ATOM   7086  C C   . SER C 1 148 ? 17.436  -59.855 52.604  1.00 211.52 ? 148 SER C C   1 
ATOM   7087  O O   . SER C 1 148 ? 18.292  -60.033 51.732  1.00 210.98 ? 148 SER C O   1 
ATOM   7088  C CB  . SER C 1 148 ? 17.835  -57.968 54.197  1.00 204.05 ? 148 SER C CB  1 
ATOM   7089  O OG  . SER C 1 148 ? 18.732  -57.369 53.279  1.00 207.77 ? 148 SER C OG  1 
ATOM   7090  N N   . ALA C 1 149 ? 16.126  -59.974 52.369  1.00 226.58 ? 149 ALA C N   1 
ATOM   7091  C CA  . ALA C 1 149 ? 15.648  -60.296 51.029  1.00 227.59 ? 149 ALA C CA  1 
ATOM   7092  C C   . ALA C 1 149 ? 15.928  -59.165 50.051  1.00 227.24 ? 149 ALA C C   1 
ATOM   7093  O O   . ALA C 1 149 ? 16.073  -59.409 48.848  1.00 225.85 ? 149 ALA C O   1 
ATOM   7094  C CB  . ALA C 1 149 ? 14.153  -60.614 51.063  1.00 228.01 ? 149 ALA C CB  1 
ATOM   7095  N N   . GLU C 1 150 ? 16.001  -57.926 50.544  1.00 219.19 ? 150 GLU C N   1 
ATOM   7096  C CA  . GLU C 1 150 ? 16.372  -56.810 49.682  1.00 216.31 ? 150 GLU C CA  1 
ATOM   7097  C C   . GLU C 1 150 ? 17.797  -56.960 49.170  1.00 214.07 ? 150 GLU C C   1 
ATOM   7098  O O   . GLU C 1 150 ? 18.108  -56.528 48.054  1.00 211.72 ? 150 GLU C O   1 
ATOM   7099  C CB  . GLU C 1 150 ? 16.209  -55.488 50.432  1.00 215.91 ? 150 GLU C CB  1 
ATOM   7100  C CG  . GLU C 1 150 ? 15.493  -54.404 49.638  1.00 214.47 ? 150 GLU C CG  1 
ATOM   7101  C CD  . GLU C 1 150 ? 16.309  -53.896 48.466  1.00 213.15 ? 150 GLU C CD  1 
ATOM   7102  O OE1 . GLU C 1 150 ? 17.546  -53.799 48.597  1.00 213.30 ? 150 GLU C OE1 1 
ATOM   7103  O OE2 . GLU C 1 150 ? 15.709  -53.592 47.415  1.00 211.68 ? 150 GLU C OE2 1 
ATOM   7104  N N   . ALA C 1 151 ? 18.673  -57.576 49.966  1.00 216.08 ? 151 ALA C N   1 
ATOM   7105  C CA  . ALA C 1 151 ? 20.046  -57.862 49.552  1.00 215.74 ? 151 ALA C CA  1 
ATOM   7106  C C   . ALA C 1 151 ? 20.058  -59.163 48.749  1.00 213.93 ? 151 ALA C C   1 
ATOM   7107  O O   . ALA C 1 151 ? 20.501  -60.220 49.202  1.00 212.69 ? 151 ALA C O   1 
ATOM   7108  C CB  . ALA C 1 151 ? 20.966  -57.939 50.762  1.00 210.81 ? 151 ALA C CB  1 
ATOM   7109  N N   . ALA C 1 152 ? 19.559  -59.062 47.520  1.00 220.54 ? 152 ALA C N   1 
ATOM   7110  C CA  . ALA C 1 152 ? 19.459  -60.207 46.625  1.00 217.76 ? 152 ALA C CA  1 
ATOM   7111  C C   . ALA C 1 152 ? 20.114  -59.995 45.270  1.00 224.39 ? 152 ALA C C   1 
ATOM   7112  O O   . ALA C 1 152 ? 20.365  -60.984 44.572  1.00 225.56 ? 152 ALA C O   1 
ATOM   7113  C CB  . ALA C 1 152 ? 17.988  -60.593 46.404  1.00 218.05 ? 152 ALA C CB  1 
ATOM   7114  N N   . SER C 1 153 ? 20.393  -58.752 44.869  1.00 214.03 ? 153 SER C N   1 
ATOM   7115  C CA  . SER C 1 153 ? 21.073  -58.521 43.600  1.00 215.86 ? 153 SER C CA  1 
ATOM   7116  C C   . SER C 1 153 ? 22.524  -58.983 43.646  1.00 218.30 ? 153 SER C C   1 
ATOM   7117  O O   . SER C 1 153 ? 23.095  -59.326 42.605  1.00 214.84 ? 153 SER C O   1 
ATOM   7118  C CB  . SER C 1 153 ? 20.998  -57.040 43.228  1.00 217.04 ? 153 SER C CB  1 
ATOM   7119  O OG  . SER C 1 153 ? 21.611  -56.233 44.219  1.00 218.05 ? 153 SER C OG  1 
ATOM   7120  N N   . GLN C 1 154 ? 23.137  -58.983 44.833  1.00 235.42 ? 154 GLN C N   1 
ATOM   7121  C CA  . GLN C 1 154 ? 24.531  -59.399 44.947  1.00 235.01 ? 154 GLN C CA  1 
ATOM   7122  C C   . GLN C 1 154 ? 24.719  -60.854 44.533  1.00 235.21 ? 154 GLN C C   1 
ATOM   7123  O O   . GLN C 1 154 ? 25.689  -61.188 43.842  1.00 237.38 ? 154 GLN C O   1 
ATOM   7124  C CB  . GLN C 1 154 ? 25.033  -59.176 46.374  1.00 233.52 ? 154 GLN C CB  1 
ATOM   7125  C CG  . GLN C 1 154 ? 23.986  -59.396 47.451  1.00 232.34 ? 154 GLN C CG  1 
ATOM   7126  C CD  . GLN C 1 154 ? 23.268  -58.116 47.831  1.00 233.05 ? 154 GLN C CD  1 
ATOM   7127  O OE1 . GLN C 1 154 ? 22.330  -57.690 47.156  1.00 233.26 ? 154 GLN C OE1 1 
ATOM   7128  N NE2 . GLN C 1 154 ? 23.711  -57.491 48.915  1.00 231.66 ? 154 GLN C NE2 1 
ATOM   7129  N N   . PHE C 1 155 ? 23.809  -61.736 44.946  1.00 219.01 ? 155 PHE C N   1 
ATOM   7130  C CA  . PHE C 1 155 ? 23.924  -63.147 44.593  1.00 210.09 ? 155 PHE C CA  1 
ATOM   7131  C C   . PHE C 1 155 ? 22.763  -63.608 43.718  1.00 209.30 ? 155 PHE C C   1 
ATOM   7132  O O   . PHE C 1 155 ? 22.894  -63.672 42.491  1.00 203.46 ? 155 PHE C O   1 
ATOM   7133  C CB  . PHE C 1 155 ? 24.022  -64.004 45.861  1.00 201.16 ? 155 PHE C CB  1 
ATOM   7134  C CG  . PHE C 1 155 ? 23.731  -65.463 45.634  1.00 196.55 ? 155 PHE C CG  1 
ATOM   7135  C CD1 . PHE C 1 155 ? 24.512  -66.217 44.777  1.00 195.88 ? 155 PHE C CD1 1 
ATOM   7136  C CD2 . PHE C 1 155 ? 22.665  -66.073 46.274  1.00 199.75 ? 155 PHE C CD2 1 
ATOM   7137  C CE1 . PHE C 1 155 ? 24.232  -67.552 44.566  1.00 199.99 ? 155 PHE C CE1 1 
ATOM   7138  C CE2 . PHE C 1 155 ? 22.383  -67.404 46.069  1.00 202.54 ? 155 PHE C CE2 1 
ATOM   7139  C CZ  . PHE C 1 155 ? 23.164  -68.144 45.214  1.00 204.77 ? 155 PHE C CZ  1 
ATOM   7140  N N   . GLY C 1 156 ? 21.640  -63.930 44.328  1.00 219.94 ? 156 GLY C N   1 
ATOM   7141  C CA  . GLY C 1 156 ? 20.537  -64.547 43.627  1.00 227.95 ? 156 GLY C CA  1 
ATOM   7142  C C   . GLY C 1 156 ? 19.721  -65.404 44.588  1.00 231.49 ? 156 GLY C C   1 
ATOM   7143  O O   . GLY C 1 156 ? 19.460  -64.997 45.723  1.00 230.67 ? 156 GLY C O   1 
ATOM   7144  N N   . GLU C 1 157 ? 19.354  -66.595 44.123  1.00 247.03 ? 157 GLU C N   1 
ATOM   7145  C CA  . GLU C 1 157 ? 18.460  -67.484 44.849  1.00 248.96 ? 157 GLU C CA  1 
ATOM   7146  C C   . GLU C 1 157 ? 19.215  -68.697 45.377  1.00 246.10 ? 157 GLU C C   1 
ATOM   7147  O O   . GLU C 1 157 ? 20.139  -69.199 44.730  1.00 242.02 ? 157 GLU C O   1 
ATOM   7148  C CB  . GLU C 1 157 ? 17.305  -67.949 43.959  1.00 250.97 ? 157 GLU C CB  1 
ATOM   7149  N N   . LEU C 1 158 ? 18.808  -69.160 46.556  1.00 240.97 ? 158 LEU C N   1 
ATOM   7150  C CA  . LEU C 1 158 ? 19.361  -70.366 47.161  1.00 242.81 ? 158 LEU C CA  1 
ATOM   7151  C C   . LEU C 1 158 ? 18.295  -70.942 48.077  1.00 256.57 ? 158 LEU C C   1 
ATOM   7152  O O   . LEU C 1 158 ? 17.834  -70.256 48.993  1.00 249.73 ? 158 LEU C O   1 
ATOM   7153  C CB  . LEU C 1 158 ? 20.645  -70.056 47.938  1.00 221.47 ? 158 LEU C CB  1 
ATOM   7154  N N   . ILE C 1 159 ? 17.912  -72.194 47.841  1.00 279.54 ? 159 ILE C N   1 
ATOM   7155  C CA  . ILE C 1 159 ? 16.835  -72.847 48.578  1.00 280.02 ? 159 ILE C CA  1 
ATOM   7156  C C   . ILE C 1 159 ? 17.425  -73.991 49.389  1.00 280.52 ? 159 ILE C C   1 
ATOM   7157  O O   . ILE C 1 159 ? 18.165  -74.824 48.852  1.00 280.80 ? 159 ILE C O   1 
ATOM   7158  C CB  . ILE C 1 159 ? 15.732  -73.356 47.635  1.00 280.32 ? 159 ILE C CB  1 
ATOM   7159  C CG1 . ILE C 1 159 ? 15.272  -72.241 46.694  1.00 279.55 ? 159 ILE C CG1 1 
ATOM   7160  C CG2 . ILE C 1 159 ? 14.559  -73.903 48.436  1.00 280.59 ? 159 ILE C CG2 1 
ATOM   7161  C CD1 . ILE C 1 159 ? 14.538  -71.122 47.389  1.00 279.08 ? 159 ILE C CD1 1 
ATOM   7162  N N   . ALA C 1 160 ? 17.095  -74.031 50.679  1.00 245.37 ? 160 ALA C N   1 
ATOM   7163  C CA  . ALA C 1 160 ? 17.571  -75.083 51.566  1.00 229.41 ? 160 ALA C CA  1 
ATOM   7164  C C   . ALA C 1 160 ? 16.498  -75.398 52.597  1.00 212.61 ? 160 ALA C C   1 
ATOM   7165  O O   . ALA C 1 160 ? 15.993  -74.492 53.265  1.00 207.14 ? 160 ALA C O   1 
ATOM   7166  C CB  . ALA C 1 160 ? 18.875  -74.673 52.258  1.00 222.55 ? 160 ALA C CB  1 
ATOM   7167  N N   . ASP C 1 161 ? 16.154  -76.679 52.717  1.00 214.26 ? 161 ASP C N   1 
ATOM   7168  C CA  . ASP C 1 161 ? 15.151  -77.141 53.668  1.00 207.06 ? 161 ASP C CA  1 
ATOM   7169  C C   . ASP C 1 161 ? 15.763  -77.178 55.063  1.00 203.45 ? 161 ASP C C   1 
ATOM   7170  O O   . ASP C 1 161 ? 16.675  -77.974 55.324  1.00 204.60 ? 161 ASP C O   1 
ATOM   7171  C CB  . ASP C 1 161 ? 14.613  -78.520 53.279  1.00 205.33 ? 161 ASP C CB  1 
ATOM   7172  N N   . PRO C 1 162 ? 15.287  -76.334 55.982  1.00 186.47 ? 162 PRO C N   1 
ATOM   7173  C CA  . PRO C 1 162 ? 15.959  -76.195 57.282  1.00 180.01 ? 162 PRO C CA  1 
ATOM   7174  C C   . PRO C 1 162 ? 15.869  -77.427 58.169  1.00 183.26 ? 162 PRO C C   1 
ATOM   7175  O O   . PRO C 1 162 ? 16.549  -77.467 59.204  1.00 180.64 ? 162 PRO C O   1 
ATOM   7176  C CB  . PRO C 1 162 ? 15.239  -74.999 57.917  1.00 165.45 ? 162 PRO C CB  1 
ATOM   7177  C CG  . PRO C 1 162 ? 13.877  -75.028 57.302  1.00 163.93 ? 162 PRO C CG  1 
ATOM   7178  C CD  . PRO C 1 162 ? 14.078  -75.497 55.888  1.00 175.80 ? 162 PRO C CD  1 
ATOM   7179  N N   . ASP C 1 163 ? 15.067  -78.429 57.802  1.00 183.22 ? 163 ASP C N   1 
ATOM   7180  C CA  . ASP C 1 163 ? 14.952  -79.623 58.633  1.00 187.97 ? 163 ASP C CA  1 
ATOM   7181  C C   . ASP C 1 163 ? 16.190  -80.503 58.511  1.00 193.49 ? 163 ASP C C   1 
ATOM   7182  O O   . ASP C 1 163 ? 16.811  -80.859 59.519  1.00 192.17 ? 163 ASP C O   1 
ATOM   7183  C CB  . ASP C 1 163 ? 13.696  -80.406 58.249  1.00 189.62 ? 163 ASP C CB  1 
ATOM   7184  C CG  . ASP C 1 163 ? 12.524  -80.111 59.163  1.00 190.01 ? 163 ASP C CG  1 
ATOM   7185  O OD1 . ASP C 1 163 ? 12.732  -79.447 60.201  1.00 189.93 ? 163 ASP C OD1 1 
ATOM   7186  O OD2 . ASP C 1 163 ? 11.395  -80.541 58.843  1.00 191.28 ? 163 ASP C OD2 1 
ATOM   7187  N N   . THR C 1 164 ? 16.572  -80.854 57.287  1.00 209.12 ? 164 THR C N   1 
ATOM   7188  C CA  . THR C 1 164 ? 17.789  -81.613 57.038  1.00 209.33 ? 164 THR C CA  1 
ATOM   7189  C C   . THR C 1 164 ? 18.951  -80.723 56.627  1.00 208.73 ? 164 THR C C   1 
ATOM   7190  O O   . THR C 1 164 ? 20.053  -81.233 56.397  1.00 208.00 ? 164 THR C O   1 
ATOM   7191  C CB  . THR C 1 164 ? 17.549  -82.677 55.959  1.00 210.09 ? 164 THR C CB  1 
ATOM   7192  O OG1 . THR C 1 164 ? 17.142  -82.045 54.739  1.00 211.48 ? 164 THR C OG1 1 
ATOM   7193  C CG2 . THR C 1 164 ? 16.472  -83.653 56.405  1.00 209.47 ? 164 THR C CG2 1 
ATOM   7194  N N   . LYS C 1 165 ? 18.726  -79.411 56.537  1.00 193.74 ? 165 LYS C N   1 
ATOM   7195  C CA  . LYS C 1 165 ? 19.739  -78.454 56.102  1.00 187.99 ? 165 LYS C CA  1 
ATOM   7196  C C   . LYS C 1 165 ? 20.307  -78.842 54.740  1.00 192.15 ? 165 LYS C C   1 
ATOM   7197  O O   . LYS C 1 165 ? 21.511  -78.757 54.500  1.00 188.75 ? 165 LYS C O   1 
ATOM   7198  C CB  . LYS C 1 165 ? 20.851  -78.333 57.146  1.00 179.92 ? 165 LYS C CB  1 
ATOM   7199  C CG  . LYS C 1 165 ? 20.345  -78.081 58.560  1.00 175.68 ? 165 LYS C CG  1 
ATOM   7200  C CD  . LYS C 1 165 ? 19.981  -76.626 58.790  1.00 166.58 ? 165 LYS C CD  1 
ATOM   7201  C CE  . LYS C 1 165 ? 21.227  -75.769 58.924  1.00 158.35 ? 165 LYS C CE  1 
ATOM   7202  N NZ  . LYS C 1 165 ? 21.815  -75.867 60.286  1.00 152.55 ? 165 LYS C NZ  1 
ATOM   7203  N N   . GLU C 1 166 ? 19.425  -79.258 53.835  1.00 201.70 ? 166 GLU C N   1 
ATOM   7204  C CA  . GLU C 1 166 ? 19.807  -79.736 52.513  1.00 206.19 ? 166 GLU C CA  1 
ATOM   7205  C C   . GLU C 1 166 ? 19.400  -78.720 51.452  1.00 220.84 ? 166 GLU C C   1 
ATOM   7206  O O   . GLU C 1 166 ? 18.288  -78.185 51.486  1.00 217.13 ? 166 GLU C O   1 
ATOM   7207  C CB  . GLU C 1 166 ? 19.163  -81.094 52.224  1.00 202.22 ? 166 GLU C CB  1 
ATOM   7208  C CG  . GLU C 1 166 ? 19.933  -81.964 51.240  1.00 200.66 ? 166 GLU C CG  1 
ATOM   7209  C CD  . GLU C 1 166 ? 19.440  -81.826 49.812  1.00 208.49 ? 166 GLU C CD  1 
ATOM   7210  O OE1 . GLU C 1 166 ? 18.232  -82.036 49.577  1.00 208.44 ? 166 GLU C OE1 1 
ATOM   7211  O OE2 . GLU C 1 166 ? 20.265  -81.524 48.924  1.00 214.46 ? 166 GLU C OE2 1 
ATOM   7212  N N   . LEU C 1 167 ? 20.304  -78.467 50.506  1.00 282.42 ? 167 LEU C N   1 
ATOM   7213  C CA  . LEU C 1 167 ? 20.076  -77.483 49.449  1.00 282.25 ? 167 LEU C CA  1 
ATOM   7214  C C   . LEU C 1 167 ? 19.041  -78.012 48.459  1.00 282.96 ? 167 LEU C C   1 
ATOM   7215  O O   . LEU C 1 167 ? 19.321  -78.941 47.696  1.00 283.17 ? 167 LEU C O   1 
ATOM   7216  C CB  . LEU C 1 167 ? 21.393  -77.162 48.747  1.00 281.52 ? 167 LEU C CB  1 
ATOM   7217  C CG  . LEU C 1 167 ? 21.361  -76.149 47.601  1.00 280.88 ? 167 LEU C CG  1 
ATOM   7218  C CD1 . LEU C 1 167 ? 22.410  -75.070 47.815  1.00 279.78 ? 167 LEU C CD1 1 
ATOM   7219  C CD2 . LEU C 1 167 ? 21.572  -76.847 46.266  1.00 280.83 ? 167 LEU C CD2 1 
ATOM   7220  N N   . LEU C 1 168 ? 17.843  -77.418 48.468  1.00 243.72 ? 168 LEU C N   1 
ATOM   7221  C CA  . LEU C 1 168 ? 16.762  -77.866 47.596  1.00 227.26 ? 168 LEU C CA  1 
ATOM   7222  C C   . LEU C 1 168 ? 16.840  -77.288 46.189  1.00 223.29 ? 168 LEU C C   1 
ATOM   7223  O O   . LEU C 1 168 ? 16.314  -77.903 45.256  1.00 205.88 ? 168 LEU C O   1 
ATOM   7224  C CB  . LEU C 1 168 ? 15.407  -77.508 48.206  1.00 208.22 ? 168 LEU C CB  1 
ATOM   7225  C CG  . LEU C 1 168 ? 14.595  -78.657 48.800  1.00 176.42 ? 168 LEU C CG  1 
ATOM   7226  C CD1 . LEU C 1 168 ? 14.136  -79.608 47.702  1.00 148.50 ? 168 LEU C CD1 1 
ATOM   7227  C CD2 . LEU C 1 168 ? 15.404  -79.402 49.846  1.00 179.99 ? 168 LEU C CD2 1 
ATOM   7228  N N   . HIS C 1 169 ? 17.478  -76.134 46.010  1.00 222.49 ? 169 HIS C N   1 
ATOM   7229  C CA  . HIS C 1 169 ? 17.535  -75.480 44.709  1.00 221.43 ? 169 HIS C CA  1 
ATOM   7230  C C   . HIS C 1 169 ? 18.623  -74.419 44.753  1.00 224.24 ? 169 HIS C C   1 
ATOM   7231  O O   . HIS C 1 169 ? 18.884  -73.829 45.805  1.00 231.22 ? 169 HIS C O   1 
ATOM   7232  C CB  . HIS C 1 169 ? 16.177  -74.859 44.343  1.00 215.32 ? 169 HIS C CB  1 
ATOM   7233  C CG  . HIS C 1 169 ? 16.243  -73.836 43.252  1.00 210.55 ? 169 HIS C CG  1 
ATOM   7234  N ND1 . HIS C 1 169 ? 16.262  -72.481 43.504  1.00 214.14 ? 169 HIS C ND1 1 
ATOM   7235  C CD2 . HIS C 1 169 ? 16.290  -73.968 41.905  1.00 206.23 ? 169 HIS C CD2 1 
ATOM   7236  C CE1 . HIS C 1 169 ? 16.322  -71.823 42.360  1.00 208.74 ? 169 HIS C CE1 1 
ATOM   7237  N NE2 . HIS C 1 169 ? 16.340  -72.702 41.375  1.00 203.77 ? 169 HIS C NE2 1 
ATOM   7238  N N   . TYR C 1 170 ? 19.251  -74.183 43.603  1.00 213.77 ? 170 TYR C N   1 
ATOM   7239  C CA  . TYR C 1 170 ? 20.352  -73.229 43.525  1.00 205.09 ? 170 TYR C CA  1 
ATOM   7240  C C   . TYR C 1 170 ? 20.457  -72.675 42.114  1.00 198.84 ? 170 TYR C C   1 
ATOM   7241  O O   . TYR C 1 170 ? 20.663  -73.433 41.162  1.00 194.55 ? 170 TYR C O   1 
ATOM   7242  C CB  . TYR C 1 170 ? 21.678  -73.871 43.934  1.00 204.79 ? 170 TYR C CB  1 
ATOM   7243  C CG  . TYR C 1 170 ? 22.873  -73.012 43.588  1.00 201.08 ? 170 TYR C CG  1 
ATOM   7244  C CD1 . TYR C 1 170 ? 23.022  -71.747 44.136  1.00 201.88 ? 170 TYR C CD1 1 
ATOM   7245  C CD2 . TYR C 1 170 ? 23.840  -73.457 42.696  1.00 195.36 ? 170 TYR C CD2 1 
ATOM   7246  C CE1 . TYR C 1 170 ? 24.102  -70.953 43.815  1.00 198.01 ? 170 TYR C CE1 1 
ATOM   7247  C CE2 . TYR C 1 170 ? 24.926  -72.666 42.369  1.00 199.50 ? 170 TYR C CE2 1 
ATOM   7248  C CZ  . TYR C 1 170 ? 25.049  -71.414 42.934  1.00 199.83 ? 170 TYR C CZ  1 
ATOM   7249  O OH  . TYR C 1 170 ? 26.121  -70.611 42.622  1.00 202.37 ? 170 TYR C OH  1 
ATOM   7250  N N   . THR C 1 171 ? 20.318  -71.358 41.987  1.00 210.98 ? 171 THR C N   1 
ATOM   7251  C CA  . THR C 1 171 ? 20.591  -70.642 40.749  1.00 212.49 ? 171 THR C CA  1 
ATOM   7252  C C   . THR C 1 171 ? 21.586  -69.536 41.061  1.00 225.81 ? 171 THR C C   1 
ATOM   7253  O O   . THR C 1 171 ? 21.377  -68.758 41.998  1.00 224.66 ? 171 THR C O   1 
ATOM   7254  C CB  . THR C 1 171 ? 19.314  -70.057 40.136  1.00 205.98 ? 171 THR C CB  1 
ATOM   7255  O OG1 . THR C 1 171 ? 18.473  -69.539 41.175  1.00 216.96 ? 171 THR C OG1 1 
ATOM   7256  C CG2 . THR C 1 171 ? 18.560  -71.129 39.364  1.00 191.34 ? 171 THR C CG2 1 
ATOM   7257  N N   . GLU C 1 172 ? 22.670  -69.477 40.285  1.00 261.05 ? 172 GLU C N   1 
ATOM   7258  C CA  . GLU C 1 172 ? 23.754  -68.547 40.586  1.00 258.78 ? 172 GLU C CA  1 
ATOM   7259  C C   . GLU C 1 172 ? 23.286  -67.099 40.485  1.00 257.53 ? 172 GLU C C   1 
ATOM   7260  O O   . GLU C 1 172 ? 23.283  -66.363 41.478  1.00 257.71 ? 172 GLU C O   1 
ATOM   7261  C CB  . GLU C 1 172 ? 24.942  -68.810 39.656  1.00 256.63 ? 172 GLU C CB  1 
ATOM   7262  C CG  . GLU C 1 172 ? 24.620  -69.696 38.463  1.00 257.10 ? 172 GLU C CG  1 
ATOM   7263  C CD  . GLU C 1 172 ? 23.838  -68.970 37.389  1.00 255.85 ? 172 GLU C CD  1 
ATOM   7264  O OE1 . GLU C 1 172 ? 24.191  -67.814 37.073  1.00 253.09 ? 172 GLU C OE1 1 
ATOM   7265  O OE2 . GLU C 1 172 ? 22.866  -69.553 36.865  1.00 257.23 ? 172 GLU C OE2 1 
ATOM   7266  N N   . LYS C 1 173 ? 22.884  -66.670 39.290  1.00 223.46 ? 173 LYS C N   1 
ATOM   7267  C CA  . LYS C 1 173 ? 22.549  -65.264 39.094  1.00 209.44 ? 173 LYS C CA  1 
ATOM   7268  C C   . LYS C 1 173 ? 21.056  -65.054 38.840  1.00 208.29 ? 173 LYS C C   1 
ATOM   7269  O O   . LYS C 1 173 ? 20.459  -64.171 39.469  1.00 208.58 ? 173 LYS C O   1 
ATOM   7270  C CB  . LYS C 1 173 ? 23.380  -64.665 37.956  1.00 194.99 ? 173 LYS C CB  1 
ATOM   7271  C CG  . LYS C 1 173 ? 24.164  -63.437 38.378  1.00 180.26 ? 173 LYS C CG  1 
ATOM   7272  C CD  . LYS C 1 173 ? 25.034  -63.743 39.588  1.00 176.23 ? 173 LYS C CD  1 
ATOM   7273  C CE  . LYS C 1 173 ? 25.526  -62.467 40.251  1.00 173.78 ? 173 LYS C CE  1 
ATOM   7274  N NZ  . LYS C 1 173 ? 24.400  -61.658 40.798  1.00 185.67 ? 173 LYS C NZ  1 
ATOM   7275  N N   . PRO C 1 174 ? 20.402  -65.821 37.939  1.00 207.94 ? 174 PRO C N   1 
ATOM   7276  C CA  . PRO C 1 174 ? 18.948  -65.656 37.793  1.00 211.28 ? 174 PRO C CA  1 
ATOM   7277  C C   . PRO C 1 174 ? 18.208  -66.090 39.047  1.00 234.74 ? 174 PRO C C   1 
ATOM   7278  O O   . PRO C 1 174 ? 17.965  -67.284 39.246  1.00 225.82 ? 174 PRO C O   1 
ATOM   7279  C CB  . PRO C 1 174 ? 18.602  -66.555 36.598  1.00 195.29 ? 174 PRO C CB  1 
ATOM   7280  C CG  . PRO C 1 174 ? 19.891  -66.779 35.888  1.00 194.04 ? 174 PRO C CG  1 
ATOM   7281  C CD  . PRO C 1 174 ? 20.924  -66.798 36.965  1.00 205.88 ? 174 PRO C CD  1 
ATOM   7282  N N   . GLU C 1 175 ? 17.839  -65.130 39.896  1.00 314.92 ? 175 GLU C N   1 
ATOM   7283  C CA  . GLU C 1 175 ? 17.258  -65.476 41.189  1.00 317.23 ? 175 GLU C CA  1 
ATOM   7284  C C   . GLU C 1 175 ? 15.855  -66.054 41.026  1.00 318.45 ? 175 GLU C C   1 
ATOM   7285  O O   . GLU C 1 175 ? 15.607  -67.214 41.376  1.00 319.22 ? 175 GLU C O   1 
ATOM   7286  C CB  . GLU C 1 175 ? 17.254  -64.250 42.113  1.00 316.63 ? 175 GLU C CB  1 
ATOM   7287  C CG  . GLU C 1 175 ? 16.687  -62.975 41.498  1.00 315.76 ? 175 GLU C CG  1 
ATOM   7288  C CD  . GLU C 1 175 ? 16.699  -61.803 42.459  1.00 315.70 ? 175 GLU C CD  1 
ATOM   7289  O OE1 . GLU C 1 175 ? 16.972  -62.021 43.656  1.00 315.99 ? 175 GLU C OE1 1 
ATOM   7290  O OE2 . GLU C 1 175 ? 16.421  -60.666 42.022  1.00 318.58 ? 175 GLU C OE2 1 
ATOM   7291  N N   . THR C 1 176 ? 14.939  -65.275 40.451  1.00 262.98 ? 176 THR C N   1 
ATOM   7292  C CA  . THR C 1 176 ? 13.529  -65.643 40.327  1.00 245.27 ? 176 THR C CA  1 
ATOM   7293  C C   . THR C 1 176 ? 13.000  -66.185 41.658  1.00 250.92 ? 176 THR C C   1 
ATOM   7294  O O   . THR C 1 176 ? 12.777  -67.383 41.836  1.00 245.86 ? 176 THR C O   1 
ATOM   7295  C CB  . THR C 1 176 ? 13.332  -66.651 39.191  1.00 223.62 ? 176 THR C CB  1 
ATOM   7296  O OG1 . THR C 1 176 ? 14.326  -66.433 38.183  1.00 217.97 ? 176 THR C OG1 1 
ATOM   7297  C CG2 . THR C 1 176 ? 11.955  -66.480 38.569  1.00 205.72 ? 176 THR C CG2 1 
ATOM   7298  N N   . PHE C 1 177 ? 12.842  -65.246 42.598  1.00 256.02 ? 177 PHE C N   1 
ATOM   7299  C CA  . PHE C 1 177 ? 12.423  -65.506 43.975  1.00 253.62 ? 177 PHE C CA  1 
ATOM   7300  C C   . PHE C 1 177 ? 13.541  -66.173 44.769  1.00 254.41 ? 177 PHE C C   1 
ATOM   7301  O O   . PHE C 1 177 ? 14.143  -67.149 44.309  1.00 255.73 ? 177 PHE C O   1 
ATOM   7302  C CB  . PHE C 1 177 ? 11.149  -66.356 44.018  1.00 252.21 ? 177 PHE C CB  1 
ATOM   7303  C CG  . PHE C 1 177 ? 10.813  -66.876 45.385  1.00 254.45 ? 177 PHE C CG  1 
ATOM   7304  C CD1 . PHE C 1 177 ? 10.263  -66.042 46.345  1.00 256.25 ? 177 PHE C CD1 1 
ATOM   7305  C CD2 . PHE C 1 177 ? 11.040  -68.204 45.708  1.00 255.41 ? 177 PHE C CD2 1 
ATOM   7306  C CE1 . PHE C 1 177 ? 9.953   -66.524 47.603  1.00 258.54 ? 177 PHE C CE1 1 
ATOM   7307  C CE2 . PHE C 1 177 ? 10.733  -68.690 46.961  1.00 258.66 ? 177 PHE C CE2 1 
ATOM   7308  C CZ  . PHE C 1 177 ? 10.188  -67.851 47.910  1.00 259.51 ? 177 PHE C CZ  1 
ATOM   7309  N N   . VAL C 1 178 ? 13.823  -65.650 45.962  1.00 247.69 ? 178 VAL C N   1 
ATOM   7310  C CA  . VAL C 1 178 ? 14.950  -66.109 46.765  1.00 243.87 ? 178 VAL C CA  1 
ATOM   7311  C C   . VAL C 1 178 ? 14.444  -66.706 48.070  1.00 242.70 ? 178 VAL C C   1 
ATOM   7312  O O   . VAL C 1 178 ? 13.237  -66.914 48.246  1.00 244.92 ? 178 VAL C O   1 
ATOM   7313  C CB  . VAL C 1 178 ? 15.937  -64.959 47.035  1.00 240.07 ? 178 VAL C CB  1 
ATOM   7314  C CG1 . VAL C 1 178 ? 16.399  -64.352 45.727  1.00 249.93 ? 178 VAL C CG1 1 
ATOM   7315  C CG2 . VAL C 1 178 ? 15.291  -63.898 47.914  1.00 235.47 ? 178 VAL C CG2 1 
ATOM   7316  N N   . SER C 1 179 ? 15.371  -66.989 48.993  1.00 236.73 ? 179 SER C N   1 
ATOM   7317  C CA  . SER C 1 179 ? 15.009  -67.537 50.295  1.00 234.60 ? 179 SER C CA  1 
ATOM   7318  C C   . SER C 1 179 ? 15.824  -66.926 51.431  1.00 235.26 ? 179 SER C C   1 
ATOM   7319  O O   . SER C 1 179 ? 15.893  -67.518 52.514  1.00 235.12 ? 179 SER C O   1 
ATOM   7320  C CB  . SER C 1 179 ? 15.175  -69.060 50.311  1.00 236.05 ? 179 SER C CB  1 
ATOM   7321  O OG  . SER C 1 179 ? 14.599  -69.630 51.475  1.00 233.08 ? 179 SER C OG  1 
ATOM   7322  N N   . ASP C 1 180 ? 16.469  -65.785 51.196  1.00 242.04 ? 180 ASP C N   1 
ATOM   7323  C CA  . ASP C 1 180 ? 17.264  -65.008 52.146  1.00 238.50 ? 180 ASP C CA  1 
ATOM   7324  C C   . ASP C 1 180 ? 18.614  -65.662 52.452  1.00 235.70 ? 180 ASP C C   1 
ATOM   7325  O O   . ASP C 1 180 ? 19.432  -65.059 53.157  1.00 233.26 ? 180 ASP C O   1 
ATOM   7326  C CB  . ASP C 1 180 ? 16.489  -64.711 53.449  1.00 238.73 ? 180 ASP C CB  1 
ATOM   7327  C CG  . ASP C 1 180 ? 17.011  -65.489 54.657  1.00 235.75 ? 180 ASP C CG  1 
ATOM   7328  O OD1 . ASP C 1 180 ? 17.923  -64.980 55.343  1.00 234.43 ? 180 ASP C OD1 1 
ATOM   7329  O OD2 . ASP C 1 180 ? 16.489  -66.586 54.945  1.00 236.07 ? 180 ASP C OD2 1 
ATOM   7330  N N   . LEU C 1 181 ? 18.908  -66.832 51.890  1.00 219.84 ? 181 LEU C N   1 
ATOM   7331  C CA  . LEU C 1 181 ? 20.182  -67.498 52.108  1.00 206.99 ? 181 LEU C CA  1 
ATOM   7332  C C   . LEU C 1 181 ? 21.069  -67.349 50.881  1.00 195.09 ? 181 LEU C C   1 
ATOM   7333  O O   . LEU C 1 181 ? 20.590  -67.292 49.745  1.00 198.69 ? 181 LEU C O   1 
ATOM   7334  C CB  . LEU C 1 181 ? 19.986  -68.980 52.435  1.00 211.00 ? 181 LEU C CB  1 
ATOM   7335  C CG  . LEU C 1 181 ? 19.527  -69.314 53.854  1.00 212.63 ? 181 LEU C CG  1 
ATOM   7336  C CD1 . LEU C 1 181 ? 19.509  -70.817 54.077  1.00 214.06 ? 181 LEU C CD1 1 
ATOM   7337  C CD2 . LEU C 1 181 ? 20.428  -68.635 54.879  1.00 203.93 ? 181 LEU C CD2 1 
ATOM   7338  N N   . ILE C 1 182 ? 22.378  -67.290 51.126  1.00 188.79 ? 182 ILE C N   1 
ATOM   7339  C CA  . ILE C 1 182 ? 23.367  -67.044 50.087  1.00 179.74 ? 182 ILE C CA  1 
ATOM   7340  C C   . ILE C 1 182 ? 24.602  -67.880 50.388  1.00 178.17 ? 182 ILE C C   1 
ATOM   7341  O O   . ILE C 1 182 ? 24.843  -68.289 51.525  1.00 182.42 ? 182 ILE C O   1 
ATOM   7342  C CB  . ILE C 1 182 ? 23.753  -65.550 49.994  1.00 175.88 ? 182 ILE C CB  1 
ATOM   7343  C CG1 . ILE C 1 182 ? 24.146  -65.020 51.375  1.00 176.12 ? 182 ILE C CG1 1 
ATOM   7344  C CG2 . ILE C 1 182 ? 22.609  -64.724 49.430  1.00 177.06 ? 182 ILE C CG2 1 
ATOM   7345  C CD1 . ILE C 1 182 ? 25.195  -63.931 51.344  1.00 172.49 ? 182 ILE C CD1 1 
ATOM   7346  N N   . ASN C 1 183 ? 25.386  -68.139 49.344  1.00 173.87 ? 183 ASN C N   1 
ATOM   7347  C CA  . ASN C 1 183 ? 26.653  -68.830 49.522  1.00 175.33 ? 183 ASN C CA  1 
ATOM   7348  C C   . ASN C 1 183 ? 27.626  -67.961 50.312  1.00 182.37 ? 183 ASN C C   1 
ATOM   7349  O O   . ASN C 1 183 ? 27.512  -66.734 50.358  1.00 180.08 ? 183 ASN C O   1 
ATOM   7350  C CB  . ASN C 1 183 ? 27.269  -69.197 48.172  1.00 174.91 ? 183 ASN C CB  1 
ATOM   7351  C CG  . ASN C 1 183 ? 26.334  -70.010 47.305  1.00 175.98 ? 183 ASN C CG  1 
ATOM   7352  O OD1 . ASN C 1 183 ? 25.387  -69.480 46.730  1.00 174.92 ? 183 ASN C OD1 1 
ATOM   7353  N ND2 . ASN C 1 183 ? 26.597  -71.307 47.206  1.00 175.34 ? 183 ASN C ND2 1 
ATOM   7354  N N   . CYS C 1 184 ? 28.601  -68.621 50.940  1.00 213.72 ? 184 CYS C N   1 
ATOM   7355  C CA  . CYS C 1 184 ? 29.681  -67.936 51.631  1.00 212.37 ? 184 CYS C CA  1 
ATOM   7356  C C   . CYS C 1 184 ? 31.057  -68.199 51.041  1.00 211.74 ? 184 CYS C C   1 
ATOM   7357  O O   . CYS C 1 184 ? 31.993  -67.455 51.357  1.00 209.79 ? 184 CYS C O   1 
ATOM   7358  C CB  . CYS C 1 184 ? 29.700  -68.327 53.118  1.00 213.32 ? 184 CYS C CB  1 
ATOM   7359  S SG  . CYS C 1 184 ? 28.400  -67.557 54.115  1.00 216.72 ? 184 CYS C SG  1 
ATOM   7360  N N   . GLY C 1 185 ? 31.211  -69.225 50.204  1.00 177.31 ? 185 GLY C N   1 
ATOM   7361  C CA  . GLY C 1 185 ? 32.476  -69.550 49.588  1.00 162.79 ? 185 GLY C CA  1 
ATOM   7362  C C   . GLY C 1 185 ? 33.336  -70.532 50.358  1.00 150.47 ? 185 GLY C C   1 
ATOM   7363  O O   . GLY C 1 185 ? 34.260  -71.111 49.774  1.00 142.75 ? 185 GLY C O   1 
ATOM   7364  N N   . VAL C 1 188 ? 33.216  -77.544 52.490  1.00 178.46 ? 188 VAL C N   1 
ATOM   7365  C CA  . VAL C 1 188 ? 33.916  -78.747 52.931  1.00 184.80 ? 188 VAL C CA  1 
ATOM   7366  C C   . VAL C 1 188 ? 33.196  -79.952 52.346  1.00 201.13 ? 188 VAL C C   1 
ATOM   7367  O O   . VAL C 1 188 ? 31.983  -80.106 52.533  1.00 199.73 ? 188 VAL C O   1 
ATOM   7368  C CB  . VAL C 1 188 ? 33.998  -78.865 54.462  1.00 177.81 ? 188 VAL C CB  1 
ATOM   7369  C CG1 . VAL C 1 188 ? 32.682  -78.493 55.083  1.00 197.38 ? 188 VAL C CG1 1 
ATOM   7370  C CG2 . VAL C 1 188 ? 34.384  -80.280 54.862  1.00 182.16 ? 188 VAL C CG2 1 
ATOM   7371  N N   . PHE C 1 189 ? 33.931  -80.789 51.623  1.00 234.31 ? 189 PHE C N   1 
ATOM   7372  C CA  . PHE C 1 189 ? 33.384  -81.973 50.988  1.00 234.88 ? 189 PHE C CA  1 
ATOM   7373  C C   . PHE C 1 189 ? 33.972  -83.236 51.613  1.00 234.42 ? 189 PHE C C   1 
ATOM   7374  O O   . PHE C 1 189 ? 34.732  -83.186 52.586  1.00 234.26 ? 189 PHE C O   1 
ATOM   7375  C CB  . PHE C 1 189 ? 33.639  -81.921 49.481  1.00 237.31 ? 189 PHE C CB  1 
ATOM   7376  C CG  . PHE C 1 189 ? 33.045  -80.717 48.806  1.00 239.31 ? 189 PHE C CG  1 
ATOM   7377  C CD1 . PHE C 1 189 ? 31.778  -80.774 48.254  1.00 239.75 ? 189 PHE C CD1 1 
ATOM   7378  C CD2 . PHE C 1 189 ? 33.760  -79.534 48.708  1.00 244.40 ? 189 PHE C CD2 1 
ATOM   7379  C CE1 . PHE C 1 189 ? 31.226  -79.674 47.627  1.00 243.23 ? 189 PHE C CE1 1 
ATOM   7380  C CE2 . PHE C 1 189 ? 33.214  -78.428 48.079  1.00 247.29 ? 189 PHE C CE2 1 
ATOM   7381  C CZ  . PHE C 1 189 ? 31.944  -78.500 47.539  1.00 252.42 ? 189 PHE C CZ  1 
ATOM   7382  N N   . THR C 1 190 ? 33.613  -84.380 51.046  1.00 200.01 ? 190 THR C N   1 
ATOM   7383  C CA  . THR C 1 190 ? 34.249  -85.644 51.369  1.00 193.96 ? 190 THR C CA  1 
ATOM   7384  C C   . THR C 1 190 ? 35.213  -86.011 50.244  1.00 193.77 ? 190 THR C C   1 
ATOM   7385  O O   . THR C 1 190 ? 35.367  -85.281 49.260  1.00 197.73 ? 190 THR C O   1 
ATOM   7386  C CB  . THR C 1 190 ? 33.204  -86.739 51.590  1.00 181.68 ? 190 THR C CB  1 
ATOM   7387  O OG1 . THR C 1 190 ? 33.859  -87.955 51.975  1.00 178.82 ? 190 THR C OG1 1 
ATOM   7388  C CG2 . THR C 1 190 ? 32.411  -86.976 50.317  1.00 178.17 ? 190 THR C CG2 1 
ATOM   7389  N N   . SER C 1 191 ? 35.882  -87.155 50.394  1.00 184.72 ? 191 SER C N   1 
ATOM   7390  C CA  . SER C 1 191 ? 36.836  -87.596 49.382  1.00 181.76 ? 191 SER C CA  1 
ATOM   7391  C C   . SER C 1 191 ? 36.178  -87.949 48.053  1.00 185.81 ? 191 SER C C   1 
ATOM   7392  O O   . SER C 1 191 ? 36.889  -88.115 47.056  1.00 185.20 ? 191 SER C O   1 
ATOM   7393  C CB  . SER C 1 191 ? 37.636  -88.794 49.897  1.00 176.28 ? 191 SER C CB  1 
ATOM   7394  O OG  . SER C 1 191 ? 38.572  -89.234 48.927  1.00 169.69 ? 191 SER C OG  1 
ATOM   7395  N N   . ASP C 1 192 ? 34.852  -88.058 48.011  1.00 193.25 ? 192 ASP C N   1 
ATOM   7396  C CA  . ASP C 1 192 ? 34.130  -88.468 46.813  1.00 199.30 ? 192 ASP C CA  1 
ATOM   7397  C C   . ASP C 1 192 ? 33.943  -87.333 45.810  1.00 206.28 ? 192 ASP C C   1 
ATOM   7398  O O   . ASP C 1 192 ? 33.376  -87.564 44.736  1.00 205.38 ? 192 ASP C O   1 
ATOM   7399  C CB  . ASP C 1 192 ? 32.765  -89.038 47.214  1.00 198.44 ? 192 ASP C CB  1 
ATOM   7400  C CG  . ASP C 1 192 ? 32.129  -89.874 46.119  1.00 201.29 ? 192 ASP C CG  1 
ATOM   7401  O OD1 . ASP C 1 192 ? 32.832  -90.244 45.156  1.00 198.87 ? 192 ASP C OD1 1 
ATOM   7402  O OD2 . ASP C 1 192 ? 30.915  -90.151 46.219  1.00 202.65 ? 192 ASP C OD2 1 
ATOM   7403  N N   . ILE C 1 193 ? 34.407  -86.122 46.126  1.00 259.19 ? 193 ILE C N   1 
ATOM   7404  C CA  . ILE C 1 193 ? 34.142  -84.978 45.259  1.00 258.61 ? 193 ILE C CA  1 
ATOM   7405  C C   . ILE C 1 193 ? 34.906  -85.087 43.943  1.00 257.39 ? 193 ILE C C   1 
ATOM   7406  O O   . ILE C 1 193 ? 34.415  -84.641 42.898  1.00 257.24 ? 193 ILE C O   1 
ATOM   7407  C CB  . ILE C 1 193 ? 34.471  -83.668 45.999  1.00 257.76 ? 193 ILE C CB  1 
ATOM   7408  C CG1 . ILE C 1 193 ? 34.165  -82.454 45.118  1.00 259.39 ? 193 ILE C CG1 1 
ATOM   7409  C CG2 . ILE C 1 193 ? 35.926  -83.657 46.449  1.00 256.40 ? 193 ILE C CG2 1 
ATOM   7410  C CD1 . ILE C 1 193 ? 32.735  -82.399 44.625  1.00 261.59 ? 193 ILE C CD1 1 
ATOM   7411  N N   . PHE C 1 194 ? 36.100  -85.686 43.955  1.00 207.89 ? 194 PHE C N   1 
ATOM   7412  C CA  . PHE C 1 194 ? 36.865  -85.807 42.717  1.00 192.47 ? 194 PHE C CA  1 
ATOM   7413  C C   . PHE C 1 194 ? 36.173  -86.716 41.711  1.00 189.11 ? 194 PHE C C   1 
ATOM   7414  O O   . PHE C 1 194 ? 36.350  -86.544 40.499  1.00 188.40 ? 194 PHE C O   1 
ATOM   7415  C CB  . PHE C 1 194 ? 38.271  -86.324 43.011  1.00 177.92 ? 194 PHE C CB  1 
ATOM   7416  C CG  . PHE C 1 194 ? 39.110  -85.379 43.815  1.00 175.33 ? 194 PHE C CG  1 
ATOM   7417  C CD1 . PHE C 1 194 ? 39.668  -84.258 43.224  1.00 180.21 ? 194 PHE C CD1 1 
ATOM   7418  C CD2 . PHE C 1 194 ? 39.343  -85.608 45.158  1.00 171.24 ? 194 PHE C CD2 1 
ATOM   7419  C CE1 . PHE C 1 194 ? 40.445  -83.385 43.958  1.00 179.30 ? 194 PHE C CE1 1 
ATOM   7420  C CE2 . PHE C 1 194 ? 40.116  -84.735 45.896  1.00 167.70 ? 194 PHE C CE2 1 
ATOM   7421  C CZ  . PHE C 1 194 ? 40.669  -83.624 45.296  1.00 171.66 ? 194 PHE C CZ  1 
ATOM   7422  N N   . ASN C 1 195 ? 35.385  -87.680 42.188  1.00 188.35 ? 195 ASN C N   1 
ATOM   7423  C CA  . ASN C 1 195 ? 34.639  -88.537 41.275  1.00 184.32 ? 195 ASN C CA  1 
ATOM   7424  C C   . ASN C 1 195 ? 33.471  -87.792 40.643  1.00 189.61 ? 195 ASN C C   1 
ATOM   7425  O O   . ASN C 1 195 ? 33.062  -88.119 39.523  1.00 191.60 ? 195 ASN C O   1 
ATOM   7426  C CB  . ASN C 1 195 ? 34.153  -89.784 42.011  1.00 174.93 ? 195 ASN C CB  1 
ATOM   7427  C CG  . ASN C 1 195 ? 35.281  -90.524 42.702  1.00 169.34 ? 195 ASN C CG  1 
ATOM   7428  O OD1 . ASN C 1 195 ? 36.421  -90.511 42.239  1.00 166.23 ? 195 ASN C OD1 1 
ATOM   7429  N ND2 . ASN C 1 195 ? 34.970  -91.167 43.821  1.00 170.33 ? 195 ASN C ND2 1 
ATOM   7430  N N   . ALA C 1 196 ? 32.919  -86.798 41.345  1.00 192.01 ? 196 ALA C N   1 
ATOM   7431  C CA  . ALA C 1 196 ? 31.822  -86.017 40.785  1.00 195.20 ? 196 ALA C CA  1 
ATOM   7432  C C   . ALA C 1 196 ? 32.292  -85.134 39.637  1.00 204.77 ? 196 ALA C C   1 
ATOM   7433  O O   . ALA C 1 196 ? 31.512  -84.840 38.724  1.00 202.62 ? 196 ALA C O   1 
ATOM   7434  C CB  . ALA C 1 196 ? 31.167  -85.170 41.878  1.00 189.24 ? 196 ALA C CB  1 
ATOM   7435  N N   . ILE C 1 197 ? 33.556  -84.708 39.659  1.00 224.29 ? 197 ILE C N   1 
ATOM   7436  C CA  . ILE C 1 197 ? 34.077  -83.896 38.565  1.00 224.25 ? 197 ILE C CA  1 
ATOM   7437  C C   . ILE C 1 197 ? 34.368  -84.762 37.344  1.00 224.51 ? 197 ILE C C   1 
ATOM   7438  O O   . ILE C 1 197 ? 34.204  -84.311 36.205  1.00 226.79 ? 197 ILE C O   1 
ATOM   7439  C CB  . ILE C 1 197 ? 35.327  -83.120 39.016  1.00 223.83 ? 197 ILE C CB  1 
ATOM   7440  C CG1 . ILE C 1 197 ? 35.036  -82.329 40.291  1.00 226.73 ? 197 ILE C CG1 1 
ATOM   7441  C CG2 . ILE C 1 197 ? 35.805  -82.181 37.915  1.00 226.31 ? 197 ILE C CG2 1 
ATOM   7442  C CD1 . ILE C 1 197 ? 36.202  -81.485 40.760  1.00 226.76 ? 197 ILE C CD1 1 
ATOM   7443  N N   . GLU C 1 198 ? 34.785  -86.012 37.554  1.00 204.75 ? 198 GLU C N   1 
ATOM   7444  C CA  . GLU C 1 198 ? 35.021  -86.910 36.428  1.00 203.30 ? 198 GLU C CA  1 
ATOM   7445  C C   . GLU C 1 198 ? 33.732  -87.214 35.675  1.00 211.58 ? 198 GLU C C   1 
ATOM   7446  O O   . GLU C 1 198 ? 33.764  -87.454 34.463  1.00 215.27 ? 198 GLU C O   1 
ATOM   7447  C CB  . GLU C 1 198 ? 35.675  -88.203 36.916  1.00 196.38 ? 198 GLU C CB  1 
ATOM   7448  C CG  . GLU C 1 198 ? 37.055  -88.002 37.524  1.00 190.08 ? 198 GLU C CG  1 
ATOM   7449  C CD  . GLU C 1 198 ? 37.734  -89.309 37.891  1.00 179.85 ? 198 GLU C CD  1 
ATOM   7450  O OE1 . GLU C 1 198 ? 37.070  -90.365 37.829  1.00 178.20 ? 198 GLU C OE1 1 
ATOM   7451  O OE2 . GLU C 1 198 ? 38.931  -89.277 38.247  1.00 176.57 ? 198 GLU C OE2 1 
ATOM   7452  N N   . GLU C 1 199 ? 32.595  -87.211 36.367  1.00 212.68 ? 199 GLU C N   1 
ATOM   7453  C CA  . GLU C 1 199 ? 31.309  -87.435 35.719  1.00 212.35 ? 199 GLU C CA  1 
ATOM   7454  C C   . GLU C 1 199 ? 30.790  -86.207 34.983  1.00 209.74 ? 199 GLU C C   1 
ATOM   7455  O O   . GLU C 1 199 ? 29.745  -86.294 34.332  1.00 206.65 ? 199 GLU C O   1 
ATOM   7456  C CB  . GLU C 1 199 ? 30.276  -87.904 36.746  1.00 209.42 ? 199 GLU C CB  1 
ATOM   7457  C CG  . GLU C 1 199 ? 30.597  -89.260 37.353  1.00 210.09 ? 199 GLU C CG  1 
ATOM   7458  C CD  . GLU C 1 199 ? 30.927  -90.303 36.301  1.00 215.87 ? 199 GLU C CD  1 
ATOM   7459  O OE1 . GLU C 1 199 ? 30.152  -90.440 35.330  1.00 219.72 ? 199 GLU C OE1 1 
ATOM   7460  O OE2 . GLU C 1 199 ? 31.968  -90.980 36.439  1.00 214.39 ? 199 GLU C OE2 1 
ATOM   7461  N N   . VAL C 1 200 ? 31.481  -85.073 35.070  1.00 210.63 ? 200 VAL C N   1 
ATOM   7462  C CA  . VAL C 1 200 ? 31.142  -83.908 34.265  1.00 203.30 ? 200 VAL C CA  1 
ATOM   7463  C C   . VAL C 1 200 ? 32.275  -83.477 33.343  1.00 210.94 ? 200 VAL C C   1 
ATOM   7464  O O   . VAL C 1 200 ? 32.008  -82.812 32.329  1.00 203.54 ? 200 VAL C O   1 
ATOM   7465  C CB  . VAL C 1 200 ? 30.696  -82.725 35.153  1.00 190.71 ? 200 VAL C CB  1 
ATOM   7466  C CG1 . VAL C 1 200 ? 31.896  -82.033 35.783  1.00 200.55 ? 200 VAL C CG1 1 
ATOM   7467  C CG2 . VAL C 1 200 ? 29.844  -81.738 34.357  1.00 176.26 ? 200 VAL C CG2 1 
ATOM   7468  N N   . TYR C 1 201 ? 33.526  -83.835 33.638  1.00 243.42 ? 201 TYR C N   1 
ATOM   7469  C CA  . TYR C 1 201 ? 34.659  -83.511 32.778  1.00 241.60 ? 201 TYR C CA  1 
ATOM   7470  C C   . TYR C 1 201 ? 34.961  -84.620 31.779  1.00 241.86 ? 201 TYR C C   1 
ATOM   7471  O O   . TYR C 1 201 ? 35.359  -84.338 30.643  1.00 240.52 ? 201 TYR C O   1 
ATOM   7472  C CB  . TYR C 1 201 ? 35.899  -83.225 33.627  1.00 240.97 ? 201 TYR C CB  1 
ATOM   7473  C CG  . TYR C 1 201 ? 36.384  -81.799 33.532  1.00 241.52 ? 201 TYR C CG  1 
ATOM   7474  C CD1 . TYR C 1 201 ? 36.458  -81.148 32.307  1.00 238.22 ? 201 TYR C CD1 1 
ATOM   7475  C CD2 . TYR C 1 201 ? 36.757  -81.100 34.668  1.00 239.78 ? 201 TYR C CD2 1 
ATOM   7476  C CE1 . TYR C 1 201 ? 36.901  -79.841 32.218  1.00 235.13 ? 201 TYR C CE1 1 
ATOM   7477  C CE2 . TYR C 1 201 ? 37.195  -79.797 34.590  1.00 239.27 ? 201 TYR C CE2 1 
ATOM   7478  C CZ  . TYR C 1 201 ? 37.268  -79.171 33.364  1.00 236.50 ? 201 TYR C CZ  1 
ATOM   7479  O OH  . TYR C 1 201 ? 37.707  -77.869 33.289  1.00 232.20 ? 201 TYR C OH  1 
ATOM   7480  N N   . SER C 1 202 ? 34.815  -85.878 32.191  1.00 218.41 ? 202 SER C N   1 
ATOM   7481  C CA  . SER C 1 202 ? 35.018  -87.019 31.308  1.00 217.99 ? 202 SER C CA  1 
ATOM   7482  C C   . SER C 1 202 ? 33.719  -87.532 30.705  1.00 214.31 ? 202 SER C C   1 
ATOM   7483  O O   . SER C 1 202 ? 33.690  -87.902 29.529  1.00 212.26 ? 202 SER C O   1 
ATOM   7484  C CB  . SER C 1 202 ? 35.710  -88.157 32.063  1.00 219.07 ? 202 SER C CB  1 
ATOM   7485  O OG  . SER C 1 202 ? 36.873  -87.693 32.730  1.00 219.56 ? 202 SER C OG  1 
ATOM   7486  N N   . GLN C 1 203 ? 32.639  -87.561 31.485  1.00 223.11 ? 203 GLN C N   1 
ATOM   7487  C CA  . GLN C 1 203 ? 31.379  -88.100 30.986  1.00 222.69 ? 203 GLN C CA  1 
ATOM   7488  C C   . GLN C 1 203 ? 30.597  -87.051 30.203  1.00 220.24 ? 203 GLN C C   1 
ATOM   7489  O O   . GLN C 1 203 ? 30.108  -87.326 29.101  1.00 219.83 ? 203 GLN C O   1 
ATOM   7490  C CB  . GLN C 1 203 ? 30.540  -88.642 32.147  1.00 222.88 ? 203 GLN C CB  1 
ATOM   7491  C CG  . GLN C 1 203 ? 29.192  -89.199 31.727  1.00 223.82 ? 203 GLN C CG  1 
ATOM   7492  C CD  . GLN C 1 203 ? 28.045  -88.585 32.503  1.00 223.75 ? 203 GLN C CD  1 
ATOM   7493  O OE1 . GLN C 1 203 ? 28.110  -88.447 33.723  1.00 223.44 ? 203 GLN C OE1 1 
ATOM   7494  N NE2 . GLN C 1 203 ? 26.985  -88.210 31.795  1.00 223.57 ? 203 GLN C NE2 1 
ATOM   7495  N N   . ILE C 1 204 ? 30.474  -85.843 30.752  1.00 204.24 ? 204 ILE C N   1 
ATOM   7496  C CA  . ILE C 1 204 ? 29.700  -84.784 30.117  1.00 192.35 ? 204 ILE C CA  1 
ATOM   7497  C C   . ILE C 1 204 ? 30.644  -83.852 29.368  1.00 188.86 ? 204 ILE C C   1 
ATOM   7498  O O   . ILE C 1 204 ? 30.264  -83.243 28.361  1.00 183.11 ? 204 ILE C O   1 
ATOM   7499  C CB  . ILE C 1 204 ? 28.864  -84.015 31.156  1.00 181.50 ? 204 ILE C CB  1 
ATOM   7500  C CG1 . ILE C 1 204 ? 28.023  -84.983 31.986  1.00 182.97 ? 204 ILE C CG1 1 
ATOM   7501  C CG2 . ILE C 1 204 ? 27.962  -82.994 30.478  1.00 164.71 ? 204 ILE C CG2 1 
ATOM   7502  C CD1 . ILE C 1 204 ? 27.172  -84.304 33.034  1.00 167.72 ? 204 ILE C CD1 1 
ATOM   7503  N N   . ARG C 1 205 ? 31.880  -83.745 29.852  1.00 191.18 ? 205 ARG C N   1 
ATOM   7504  C CA  . ARG C 1 205 ? 32.910  -82.915 29.227  1.00 186.33 ? 205 ARG C CA  1 
ATOM   7505  C C   . ARG C 1 205 ? 32.472  -81.459 29.108  1.00 179.11 ? 205 ARG C C   1 
ATOM   7506  O O   . ARG C 1 205 ? 33.082  -80.569 29.701  1.00 183.95 ? 205 ARG C O   1 
ATOM   7507  C CB  . ARG C 1 205 ? 33.285  -83.469 27.848  1.00 182.54 ? 205 ARG C CB  1 
ATOM   7508  C CG  . ARG C 1 205 ? 33.872  -84.871 27.877  1.00 187.71 ? 205 ARG C CG  1 
ATOM   7509  C CD  . ARG C 1 205 ? 33.400  -85.701 26.696  1.00 182.73 ? 205 ARG C CD  1 
ATOM   7510  N NE  . ARG C 1 205 ? 31.979  -86.028 26.789  1.00 186.88 ? 205 ARG C NE  1 
ATOM   7511  C CZ  . ARG C 1 205 ? 31.013  -85.377 26.148  1.00 182.82 ? 205 ARG C CZ  1 
ATOM   7512  N NH1 . ARG C 1 205 ? 31.307  -84.355 25.356  1.00 177.71 ? 205 ARG C NH1 1 
ATOM   7513  N NH2 . ARG C 1 205 ? 29.750  -85.751 26.299  1.00 181.82 ? 205 ARG C NH2 1 
ATOM   7514  N N   . PHE C 1 222 ? 37.304  -75.163 32.341  1.00 199.85 ? 222 PHE C N   1 
ATOM   7515  C CA  . PHE C 1 222 ? 36.181  -74.307 31.975  1.00 197.33 ? 222 PHE C CA  1 
ATOM   7516  C C   . PHE C 1 222 ? 34.902  -74.715 32.702  1.00 218.78 ? 222 PHE C C   1 
ATOM   7517  O O   . PHE C 1 222 ? 33.839  -74.137 32.474  1.00 222.75 ? 222 PHE C O   1 
ATOM   7518  C CB  . PHE C 1 222 ? 35.961  -74.331 30.458  1.00 183.64 ? 222 PHE C CB  1 
ATOM   7519  C CG  . PHE C 1 222 ? 35.784  -75.711 29.887  1.00 182.77 ? 222 PHE C CG  1 
ATOM   7520  C CD1 . PHE C 1 222 ? 34.528  -76.290 29.811  1.00 180.88 ? 222 PHE C CD1 1 
ATOM   7521  C CD2 . PHE C 1 222 ? 36.873  -76.422 29.411  1.00 179.36 ? 222 PHE C CD2 1 
ATOM   7522  C CE1 . PHE C 1 222 ? 34.363  -77.556 29.284  1.00 173.73 ? 222 PHE C CE1 1 
ATOM   7523  C CE2 . PHE C 1 222 ? 36.715  -77.688 28.881  1.00 175.45 ? 222 PHE C CE2 1 
ATOM   7524  C CZ  . PHE C 1 222 ? 35.458  -78.256 28.818  1.00 173.61 ? 222 PHE C CZ  1 
ATOM   7525  N N   . VAL C 1 223 ? 35.008  -75.712 33.575  1.00 251.21 ? 223 VAL C N   1 
ATOM   7526  C CA  . VAL C 1 223 ? 33.871  -76.189 34.354  1.00 254.76 ? 223 VAL C CA  1 
ATOM   7527  C C   . VAL C 1 223 ? 33.749  -75.333 35.607  1.00 256.09 ? 223 VAL C C   1 
ATOM   7528  O O   . VAL C 1 223 ? 34.694  -75.233 36.397  1.00 254.34 ? 223 VAL C O   1 
ATOM   7529  C CB  . VAL C 1 223 ? 34.020  -77.675 34.710  1.00 256.59 ? 223 VAL C CB  1 
ATOM   7530  C CG1 . VAL C 1 223 ? 32.979  -78.076 35.742  1.00 259.67 ? 223 VAL C CG1 1 
ATOM   7531  C CG2 . VAL C 1 223 ? 33.883  -78.530 33.465  1.00 256.24 ? 223 VAL C CG2 1 
ATOM   7532  N N   . ARG C 1 224 ? 32.587  -74.711 35.785  1.00 251.65 ? 224 ARG C N   1 
ATOM   7533  C CA  . ARG C 1 224 ? 32.332  -73.855 36.935  1.00 253.06 ? 224 ARG C CA  1 
ATOM   7534  C C   . ARG C 1 224 ? 31.707  -74.687 38.045  1.00 255.14 ? 224 ARG C C   1 
ATOM   7535  O O   . ARG C 1 224 ? 30.738  -75.416 37.809  1.00 245.19 ? 224 ARG C O   1 
ATOM   7536  C CB  . ARG C 1 224 ? 31.405  -72.693 36.566  1.00 245.44 ? 224 ARG C CB  1 
ATOM   7537  C CG  . ARG C 1 224 ? 31.901  -71.774 35.450  1.00 247.70 ? 224 ARG C CG  1 
ATOM   7538  C CD  . ARG C 1 224 ? 31.565  -72.336 34.075  1.00 246.51 ? 224 ARG C CD  1 
ATOM   7539  N NE  . ARG C 1 224 ? 30.220  -72.903 34.051  1.00 244.45 ? 224 ARG C NE  1 
ATOM   7540  C CZ  . ARG C 1 224 ? 29.854  -73.932 33.294  1.00 241.95 ? 224 ARG C CZ  1 
ATOM   7541  N NH1 . ARG C 1 224 ? 30.737  -74.516 32.494  1.00 243.26 ? 224 ARG C NH1 1 
ATOM   7542  N NH2 . ARG C 1 224 ? 28.608  -74.382 33.340  1.00 237.27 ? 224 ARG C NH2 1 
ATOM   7543  N N   . LEU C 1 225 ? 32.262  -74.574 39.253  1.00 301.03 ? 225 LEU C N   1 
ATOM   7544  C CA  . LEU C 1 225 ? 31.779  -75.383 40.368  1.00 303.34 ? 225 LEU C CA  1 
ATOM   7545  C C   . LEU C 1 225 ? 30.326  -75.061 40.697  1.00 305.00 ? 225 LEU C C   1 
ATOM   7546  O O   . LEU C 1 225 ? 29.516  -75.969 40.921  1.00 306.93 ? 225 LEU C O   1 
ATOM   7547  C CB  . LEU C 1 225 ? 32.669  -75.169 41.594  1.00 302.77 ? 225 LEU C CB  1 
ATOM   7548  C CG  . LEU C 1 225 ? 32.793  -76.320 42.598  1.00 304.53 ? 225 LEU C CG  1 
ATOM   7549  C CD1 . LEU C 1 225 ? 34.100  -76.206 43.369  1.00 303.24 ? 225 LEU C CD1 1 
ATOM   7550  C CD2 . LEU C 1 225 ? 31.611  -76.352 43.555  1.00 306.50 ? 225 LEU C CD2 1 
ATOM   7551  N N   . ASP C 1 226 ? 29.978  -73.777 40.731  1.00 244.63 ? 226 ASP C N   1 
ATOM   7552  C CA  . ASP C 1 226 ? 28.654  -73.325 41.154  1.00 223.60 ? 226 ASP C CA  1 
ATOM   7553  C C   . ASP C 1 226 ? 27.688  -73.141 39.990  1.00 212.31 ? 226 ASP C C   1 
ATOM   7554  O O   . ASP C 1 226 ? 26.920  -72.176 39.961  1.00 207.34 ? 226 ASP C O   1 
ATOM   7555  C CB  . ASP C 1 226 ? 28.795  -72.035 41.956  1.00 213.56 ? 226 ASP C CB  1 
ATOM   7556  C CG  . ASP C 1 226 ? 29.812  -71.085 41.357  1.00 210.74 ? 226 ASP C CG  1 
ATOM   7557  O OD1 . ASP C 1 226 ? 29.669  -70.731 40.169  1.00 205.37 ? 226 ASP C OD1 1 
ATOM   7558  O OD2 . ASP C 1 226 ? 30.759  -70.696 42.074  1.00 201.24 ? 226 ASP C OD2 1 
ATOM   7559  N N   . GLN C 1 227 ? 27.703  -74.049 39.012  1.00 214.78 ? 227 GLN C N   1 
ATOM   7560  C CA  . GLN C 1 227 ? 26.800  -73.955 37.871  1.00 208.71 ? 227 GLN C CA  1 
ATOM   7561  C C   . GLN C 1 227 ? 26.370  -75.336 37.391  1.00 202.00 ? 227 GLN C C   1 
ATOM   7562  O O   . GLN C 1 227 ? 25.191  -75.557 37.096  1.00 191.90 ? 227 GLN C O   1 
ATOM   7563  C CB  . GLN C 1 227 ? 27.457  -73.178 36.729  1.00 209.01 ? 227 GLN C CB  1 
ATOM   7564  C CG  . GLN C 1 227 ? 27.002  -71.731 36.629  1.00 204.29 ? 227 GLN C CG  1 
ATOM   7565  C CD  . GLN C 1 227 ? 28.158  -70.758 36.552  1.00 202.08 ? 227 GLN C CD  1 
ATOM   7566  O OE1 . GLN C 1 227 ? 28.737  -70.384 37.571  1.00 200.54 ? 227 GLN C OE1 1 
ATOM   7567  N NE2 . GLN C 1 227 ? 28.502  -70.341 35.339  1.00 194.26 ? 227 GLN C NE2 1 
ATOM   7568  N N   . ASP C 1 228 ? 27.314  -76.273 37.314  1.00 210.74 ? 228 ASP C N   1 
ATOM   7569  C CA  . ASP C 1 228 ? 27.035  -77.616 36.821  1.00 211.19 ? 228 ASP C CA  1 
ATOM   7570  C C   . ASP C 1 228 ? 27.380  -78.700 37.835  1.00 212.41 ? 228 ASP C C   1 
ATOM   7571  O O   . ASP C 1 228 ? 27.392  -79.885 37.480  1.00 216.10 ? 228 ASP C O   1 
ATOM   7572  C CB  . ASP C 1 228 ? 27.779  -77.865 35.503  1.00 212.77 ? 228 ASP C CB  1 
ATOM   7573  N N   . ILE C 1 229 ? 27.660  -78.328 39.083  0.27 202.07 ? 229 ILE C N   1 
ATOM   7574  C CA  . ILE C 1 229 ? 27.948  -79.298 40.133  0.27 194.57 ? 229 ILE C CA  1 
ATOM   7575  C C   . ILE C 1 229 ? 27.053  -79.012 41.330  0.27 188.43 ? 229 ILE C C   1 
ATOM   7576  O O   . ILE C 1 229 ? 26.466  -79.930 41.915  0.27 181.42 ? 229 ILE C O   1 
ATOM   7577  C CB  . ILE C 1 229 ? 29.436  -79.269 40.529  0.27 203.08 ? 229 ILE C CB  1 
ATOM   7578  N N   . LEU C 1 230 ? 26.944  -77.735 41.705  1.00 188.82 ? 230 LEU C N   1 
ATOM   7579  C CA  . LEU C 1 230 ? 26.094  -77.357 42.829  1.00 184.00 ? 230 LEU C CA  1 
ATOM   7580  C C   . LEU C 1 230 ? 24.620  -77.367 42.440  1.00 181.39 ? 230 LEU C C   1 
ATOM   7581  O O   . LEU C 1 230 ? 23.781  -77.895 43.178  1.00 184.41 ? 230 LEU C O   1 
ATOM   7582  C CB  . LEU C 1 230 ? 26.500  -75.981 43.360  1.00 195.12 ? 230 LEU C CB  1 
ATOM   7583  C CG  . LEU C 1 230 ? 27.861  -75.884 44.051  1.00 203.41 ? 230 LEU C CG  1 
ATOM   7584  C CD1 . LEU C 1 230 ? 28.053  -74.507 44.667  1.00 204.85 ? 230 LEU C CD1 1 
ATOM   7585  C CD2 . LEU C 1 230 ? 27.995  -76.969 45.108  1.00 201.62 ? 230 LEU C CD2 1 
ATOM   7586  N N   . SER C 1 231 ? 24.288  -76.783 41.287  1.00 180.50 ? 231 SER C N   1 
ATOM   7587  C CA  . SER C 1 231 ? 22.895  -76.759 40.844  1.00 177.72 ? 231 SER C CA  1 
ATOM   7588  C C   . SER C 1 231 ? 22.333  -78.152 40.583  1.00 177.00 ? 231 SER C C   1 
ATOM   7589  O O   . SER C 1 231 ? 21.202  -78.424 41.022  1.00 178.42 ? 231 SER C O   1 
ATOM   7590  C CB  . SER C 1 231 ? 22.759  -75.860 39.609  1.00 176.80 ? 231 SER C CB  1 
ATOM   7591  O OG  . SER C 1 231 ? 23.273  -74.565 39.859  1.00 181.64 ? 231 SER C OG  1 
ATOM   7592  N N   . PRO C 1 232 ? 23.024  -79.062 39.882  1.00 177.81 ? 232 PRO C N   1 
ATOM   7593  C CA  . PRO C 1 232 ? 22.445  -80.402 39.687  1.00 174.50 ? 232 PRO C CA  1 
ATOM   7594  C C   . PRO C 1 232 ? 22.246  -81.168 40.981  1.00 179.88 ? 232 PRO C C   1 
ATOM   7595  O O   . PRO C 1 232 ? 21.270  -81.919 41.100  1.00 181.60 ? 232 PRO C O   1 
ATOM   7596  C CB  . PRO C 1 232 ? 23.466  -81.094 38.774  1.00 168.72 ? 232 PRO C CB  1 
ATOM   7597  C CG  . PRO C 1 232 ? 24.138  -79.982 38.059  1.00 173.97 ? 232 PRO C CG  1 
ATOM   7598  C CD  . PRO C 1 232 ? 24.247  -78.890 39.078  1.00 178.04 ? 232 PRO C CD  1 
ATOM   7599  N N   . LEU C 1 233 ? 23.138  -81.002 41.961  1.00 178.98 ? 233 LEU C N   1 
ATOM   7600  C CA  . LEU C 1 233 ? 23.000  -81.684 43.247  1.00 185.28 ? 233 LEU C CA  1 
ATOM   7601  C C   . LEU C 1 233 ? 22.029  -80.893 44.126  1.00 205.19 ? 233 LEU C C   1 
ATOM   7602  O O   . LEU C 1 233 ? 22.396  -80.245 45.109  1.00 210.37 ? 233 LEU C O   1 
ATOM   7603  C CB  . LEU C 1 233 ? 24.357  -81.856 43.915  1.00 177.33 ? 233 LEU C CB  1 
ATOM   7604  C CG  . LEU C 1 233 ? 24.703  -83.289 44.330  1.00 168.34 ? 233 LEU C CG  1 
ATOM   7605  C CD1 . LEU C 1 233 ? 24.924  -84.168 43.107  1.00 159.51 ? 233 LEU C CD1 1 
ATOM   7606  C CD2 . LEU C 1 233 ? 25.917  -83.319 45.245  1.00 165.49 ? 233 LEU C CD2 1 
ATOM   7607  N N   . ALA C 1 234 ? 20.754  -80.964 43.747  1.00 258.29 ? 234 ALA C N   1 
ATOM   7608  C CA  . ALA C 1 234 ? 19.682  -80.270 44.452  1.00 258.74 ? 234 ALA C CA  1 
ATOM   7609  C C   . ALA C 1 234 ? 18.810  -81.268 45.203  1.00 259.48 ? 234 ALA C C   1 
ATOM   7610  O O   . ALA C 1 234 ? 18.865  -81.333 46.433  1.00 259.79 ? 234 ALA C O   1 
ATOM   7611  C CB  . ALA C 1 234 ? 18.853  -79.432 43.475  1.00 258.54 ? 234 ALA C CB  1 
ATOM   7612  N N   . GLY C 1 235 ? 18.001  -82.057 44.494  1.00 232.17 ? 235 GLY C N   1 
ATOM   7613  C CA  . GLY C 1 235 ? 17.153  -83.026 45.165  1.00 229.61 ? 235 GLY C CA  1 
ATOM   7614  C C   . GLY C 1 235 ? 17.931  -84.122 45.864  1.00 229.64 ? 235 GLY C C   1 
ATOM   7615  O O   . GLY C 1 235 ? 17.517  -84.602 46.923  1.00 230.11 ? 235 GLY C O   1 
ATOM   7616  N N   . LYS C 1 236 ? 19.059  -84.535 45.287  1.00 208.79 ? 236 LYS C N   1 
ATOM   7617  C CA  . LYS C 1 236 ? 19.881  -85.581 45.885  1.00 192.91 ? 236 LYS C CA  1 
ATOM   7618  C C   . LYS C 1 236 ? 20.469  -85.102 47.209  1.00 191.23 ? 236 LYS C C   1 
ATOM   7619  O O   . LYS C 1 236 ? 21.141  -84.065 47.265  1.00 190.69 ? 236 LYS C O   1 
ATOM   7620  C CB  . LYS C 1 236 ? 20.983  -86.004 44.919  1.00 181.55 ? 236 LYS C CB  1 
ATOM   7621  C CG  . LYS C 1 236 ? 21.374  -84.945 43.900  1.00 183.65 ? 236 LYS C CG  1 
ATOM   7622  C CD  . LYS C 1 236 ? 21.091  -85.410 42.476  1.00 173.12 ? 236 LYS C CD  1 
ATOM   7623  C CE  . LYS C 1 236 ? 19.623  -85.249 42.107  1.00 173.56 ? 236 LYS C CE  1 
ATOM   7624  N NZ  . LYS C 1 236 ? 19.234  -83.815 41.990  1.00 185.44 ? 236 LYS C NZ  1 
ATOM   7625  N N   . LYS C 1 237 ? 20.209  -85.863 48.272  1.00 185.06 ? 237 LYS C N   1 
ATOM   7626  C CA  . LYS C 1 237 ? 20.611  -85.513 49.634  1.00 185.86 ? 237 LYS C CA  1 
ATOM   7627  C C   . LYS C 1 237 ? 22.115  -85.729 49.797  1.00 183.43 ? 237 LYS C C   1 
ATOM   7628  O O   . LYS C 1 237 ? 22.581  -86.711 50.383  1.00 179.68 ? 237 LYS C O   1 
ATOM   7629  C CB  . LYS C 1 237 ? 19.825  -86.337 50.645  1.00 184.63 ? 237 LYS C CB  1 
ATOM   7630  C CG  . LYS C 1 237 ? 18.331  -86.043 50.676  1.00 185.68 ? 237 LYS C CG  1 
ATOM   7631  C CD  . LYS C 1 237 ? 17.998  -84.895 51.619  1.00 189.41 ? 237 LYS C CD  1 
ATOM   7632  C CE  . LYS C 1 237 ? 18.676  -85.078 52.965  1.00 187.58 ? 237 LYS C CE  1 
ATOM   7633  N NZ  . LYS C 1 237 ? 18.043  -86.152 53.778  1.00 188.60 ? 237 LYS C NZ  1 
ATOM   7634  N N   . GLN C 1 238 ? 22.894  -84.786 49.263  1.00 180.48 ? 238 GLN C N   1 
ATOM   7635  C CA  . GLN C 1 238 ? 24.341  -84.834 49.432  1.00 173.99 ? 238 GLN C CA  1 
ATOM   7636  C C   . GLN C 1 238 ? 24.890  -83.461 49.792  1.00 177.48 ? 238 GLN C C   1 
ATOM   7637  O O   . GLN C 1 238 ? 25.897  -83.354 50.500  1.00 176.47 ? 238 GLN C O   1 
ATOM   7638  C CB  . GLN C 1 238 ? 25.011  -85.355 48.162  1.00 168.88 ? 238 GLN C CB  1 
ATOM   7639  C CG  . GLN C 1 238 ? 24.859  -86.847 47.943  1.00 168.20 ? 238 GLN C CG  1 
ATOM   7640  C CD  . GLN C 1 238 ? 23.907  -87.168 46.810  1.00 166.88 ? 238 GLN C CD  1 
ATOM   7641  O OE1 . GLN C 1 238 ? 24.159  -86.822 45.656  1.00 165.09 ? 238 GLN C OE1 1 
ATOM   7642  N NE2 . GLN C 1 238 ? 22.806  -87.835 47.134  1.00 167.22 ? 238 GLN C NE2 1 
ATOM   7643  N N   . LEU C 1 239 ? 24.238  -82.411 49.306  1.00 187.03 ? 239 LEU C N   1 
ATOM   7644  C CA  . LEU C 1 239 ? 24.654  -81.041 49.576  1.00 189.51 ? 239 LEU C CA  1 
ATOM   7645  C C   . LEU C 1 239 ? 23.898  -80.520 50.793  1.00 193.19 ? 239 LEU C C   1 
ATOM   7646  O O   . LEU C 1 239 ? 22.662  -80.547 50.816  1.00 195.64 ? 239 LEU C O   1 
ATOM   7647  C CB  . LEU C 1 239 ? 24.394  -80.158 48.357  1.00 192.77 ? 239 LEU C CB  1 
ATOM   7648  C CG  . LEU C 1 239 ? 25.546  -79.255 47.906  1.00 193.73 ? 239 LEU C CG  1 
ATOM   7649  C CD1 . LEU C 1 239 ? 25.838  -78.193 48.952  1.00 197.27 ? 239 LEU C CD1 1 
ATOM   7650  C CD2 . LEU C 1 239 ? 26.780  -80.093 47.624  1.00 190.47 ? 239 LEU C CD2 1 
ATOM   7651  N N   . TYR C 1 240 ? 24.629  -80.050 51.800  1.00 191.16 ? 240 TYR C N   1 
ATOM   7652  C CA  . TYR C 1 240 ? 24.020  -79.601 53.045  1.00 189.60 ? 240 TYR C CA  1 
ATOM   7653  C C   . TYR C 1 240 ? 24.359  -78.131 53.309  1.00 189.47 ? 240 TYR C C   1 
ATOM   7654  O O   . TYR C 1 240 ? 24.929  -77.441 52.459  1.00 189.35 ? 240 TYR C O   1 
ATOM   7655  C CB  . TYR C 1 240 ? 24.443  -80.516 54.195  1.00 184.41 ? 240 TYR C CB  1 
ATOM   7656  C CG  . TYR C 1 240 ? 23.806  -81.886 54.118  1.00 182.09 ? 240 TYR C CG  1 
ATOM   7657  C CD1 . TYR C 1 240 ? 22.538  -82.112 54.641  1.00 181.28 ? 240 TYR C CD1 1 
ATOM   7658  C CD2 . TYR C 1 240 ? 24.461  -82.947 53.508  1.00 181.45 ? 240 TYR C CD2 1 
ATOM   7659  C CE1 . TYR C 1 240 ? 21.945  -83.358 54.567  1.00 180.13 ? 240 TYR C CE1 1 
ATOM   7660  C CE2 . TYR C 1 240 ? 23.876  -84.198 53.430  1.00 180.85 ? 240 TYR C CE2 1 
ATOM   7661  C CZ  . TYR C 1 240 ? 22.617  -84.396 53.961  1.00 177.91 ? 240 TYR C CZ  1 
ATOM   7662  O OH  . TYR C 1 240 ? 22.027  -85.637 53.887  1.00 172.35 ? 240 TYR C OH  1 
ATOM   7663  N N   . THR C 1 241 ? 23.995  -77.654 54.501  1.00 181.05 ? 241 THR C N   1 
ATOM   7664  C CA  . THR C 1 241 ? 24.173  -76.254 54.870  1.00 178.96 ? 241 THR C CA  1 
ATOM   7665  C C   . THR C 1 241 ? 24.471  -76.151 56.360  1.00 175.79 ? 241 THR C C   1 
ATOM   7666  O O   . THR C 1 241 ? 24.117  -77.030 57.149  1.00 172.47 ? 241 THR C O   1 
ATOM   7667  C CB  . THR C 1 241 ? 22.936  -75.409 54.529  1.00 177.55 ? 241 THR C CB  1 
ATOM   7668  O OG1 . THR C 1 241 ? 21.747  -76.140 54.855  1.00 173.71 ? 241 THR C OG1 1 
ATOM   7669  C CG2 . THR C 1 241 ? 22.917  -75.039 53.052  1.00 180.14 ? 241 THR C CG2 1 
ATOM   7670  N N   . ASN C 1 244 ? 26.416  -69.456 59.519  1.00 190.35 ? 244 ASN C N   1 
ATOM   7671  C CA  . ASN C 1 244 ? 27.616  -68.757 59.964  1.00 194.23 ? 244 ASN C CA  1 
ATOM   7672  C C   . ASN C 1 244 ? 27.464  -68.269 61.402  1.00 197.69 ? 244 ASN C C   1 
ATOM   7673  O O   . ASN C 1 244 ? 28.286  -68.590 62.268  1.00 198.54 ? 244 ASN C O   1 
ATOM   7674  C CB  . ASN C 1 244 ? 27.914  -67.586 59.022  1.00 196.47 ? 244 ASN C CB  1 
ATOM   7675  C CG  . ASN C 1 244 ? 29.311  -67.021 59.210  1.00 205.27 ? 244 ASN C CG  1 
ATOM   7676  O OD1 . ASN C 1 244 ? 29.929  -67.186 60.264  1.00 206.88 ? 244 ASN C OD1 1 
ATOM   7677  N ND2 . ASN C 1 244 ? 29.814  -66.344 58.186  1.00 208.84 ? 244 ASN C ND2 1 
ATOM   7678  N N   . LYS C 1 245 ? 26.431  -67.461 61.657  1.00 196.06 ? 245 LYS C N   1 
ATOM   7679  C CA  . LYS C 1 245 ? 26.157  -66.865 62.967  1.00 200.41 ? 245 LYS C CA  1 
ATOM   7680  C C   . LYS C 1 245 ? 27.229  -65.860 63.382  1.00 203.41 ? 245 LYS C C   1 
ATOM   7681  O O   . LYS C 1 245 ? 27.485  -65.670 64.573  1.00 203.26 ? 245 LYS C O   1 
ATOM   7682  C CB  . LYS C 1 245 ? 25.980  -67.931 64.054  1.00 199.94 ? 245 LYS C CB  1 
ATOM   7683  N N   . ASP C 1 246 ? 27.860  -65.209 62.407  1.00 208.60 ? 246 ASP C N   1 
ATOM   7684  C CA  . ASP C 1 246 ? 28.838  -64.166 62.689  1.00 219.71 ? 246 ASP C CA  1 
ATOM   7685  C C   . ASP C 1 246 ? 28.832  -63.108 61.592  1.00 231.76 ? 246 ASP C C   1 
ATOM   7686  O O   . ASP C 1 246 ? 27.802  -62.473 61.338  1.00 231.59 ? 246 ASP C O   1 
ATOM   7687  C CB  . ASP C 1 246 ? 30.238  -64.761 62.855  1.00 219.65 ? 246 ASP C CB  1 
ATOM   7688  C CG  . ASP C 1 246 ? 30.512  -65.221 64.275  1.00 211.17 ? 246 ASP C CG  1 
ATOM   7689  O OD1 . ASP C 1 246 ? 30.418  -64.383 65.197  1.00 211.52 ? 246 ASP C OD1 1 
ATOM   7690  O OD2 . ASP C 1 246 ? 30.826  -66.414 64.469  1.00 204.26 ? 246 ASP C OD2 1 
ATOM   7691  N N   . PHE C 1 247 ? 29.974  -62.910 60.940  1.00 269.54 ? 247 PHE C N   1 
ATOM   7692  C CA  . PHE C 1 247 ? 30.131  -61.884 59.924  1.00 268.36 ? 247 PHE C CA  1 
ATOM   7693  C C   . PHE C 1 247 ? 30.549  -62.504 58.597  1.00 267.88 ? 247 PHE C C   1 
ATOM   7694  O O   . PHE C 1 247 ? 31.073  -63.620 58.543  1.00 268.00 ? 247 PHE C O   1 
ATOM   7695  C CB  . PHE C 1 247 ? 31.160  -60.827 60.357  1.00 266.78 ? 247 PHE C CB  1 
ATOM   7696  C CG  . PHE C 1 247 ? 32.457  -61.404 60.866  1.00 266.11 ? 247 PHE C CG  1 
ATOM   7697  C CD1 . PHE C 1 247 ? 32.594  -61.767 62.198  1.00 266.67 ? 247 PHE C CD1 1 
ATOM   7698  C CD2 . PHE C 1 247 ? 33.539  -61.574 60.017  1.00 264.82 ? 247 PHE C CD2 1 
ATOM   7699  C CE1 . PHE C 1 247 ? 33.783  -62.293 62.670  1.00 265.95 ? 247 PHE C CE1 1 
ATOM   7700  C CE2 . PHE C 1 247 ? 34.731  -62.099 60.485  1.00 264.11 ? 247 PHE C CE2 1 
ATOM   7701  C CZ  . PHE C 1 247 ? 34.852  -62.459 61.813  1.00 264.74 ? 247 PHE C CZ  1 
ATOM   7702  N N   . TRP C 1 248 ? 30.301  -61.761 57.519  1.00 226.71 ? 248 TRP C N   1 
ATOM   7703  C CA  . TRP C 1 248 ? 30.748  -62.148 56.186  1.00 209.07 ? 248 TRP C CA  1 
ATOM   7704  C C   . TRP C 1 248 ? 30.706  -60.930 55.279  1.00 195.38 ? 248 TRP C C   1 
ATOM   7705  O O   . TRP C 1 248 ? 29.729  -60.176 55.296  1.00 195.07 ? 248 TRP C O   1 
ATOM   7706  C CB  . TRP C 1 248 ? 29.887  -63.264 55.589  1.00 203.67 ? 248 TRP C CB  1 
ATOM   7707  C CG  . TRP C 1 248 ? 30.436  -63.763 54.283  1.00 196.78 ? 248 TRP C CG  1 
ATOM   7708  C CD1 . TRP C 1 248 ? 31.493  -64.609 54.109  1.00 195.60 ? 248 TRP C CD1 1 
ATOM   7709  C CD2 . TRP C 1 248 ? 29.983  -63.410 52.970  1.00 188.95 ? 248 TRP C CD2 1 
ATOM   7710  N NE1 . TRP C 1 248 ? 31.712  -64.821 52.768  1.00 185.65 ? 248 TRP C NE1 1 
ATOM   7711  C CE2 . TRP C 1 248 ? 30.799  -64.095 52.048  1.00 184.00 ? 248 TRP C CE2 1 
ATOM   7712  C CE3 . TRP C 1 248 ? 28.960  -62.589 52.485  1.00 183.48 ? 248 TRP C CE3 1 
ATOM   7713  C CZ2 . TRP C 1 248 ? 30.624  -63.985 50.668  1.00 179.54 ? 248 TRP C CZ2 1 
ATOM   7714  C CZ3 . TRP C 1 248 ? 28.787  -62.480 51.116  1.00 179.04 ? 248 TRP C CZ3 1 
ATOM   7715  C CH2 . TRP C 1 248 ? 29.615  -63.175 50.223  1.00 179.52 ? 248 TRP C CH2 1 
ATOM   7716  N N   . GLU C 1 249 ? 31.763  -60.745 54.492  1.00 187.63 ? 249 GLU C N   1 
ATOM   7717  C CA  . GLU C 1 249 ? 31.844  -59.625 53.560  1.00 177.13 ? 249 GLU C CA  1 
ATOM   7718  C C   . GLU C 1 249 ? 32.741  -60.026 52.400  1.00 171.17 ? 249 GLU C C   1 
ATOM   7719  O O   . GLU C 1 249 ? 33.926  -60.310 52.601  1.00 169.72 ? 249 GLU C O   1 
ATOM   7720  C CB  . GLU C 1 249 ? 32.382  -58.370 54.252  1.00 170.27 ? 249 GLU C CB  1 
ATOM   7721  N N   . GLN C 1 250 ? 32.176  -60.050 51.194  1.00 160.22 ? 250 GLN C N   1 
ATOM   7722  C CA  . GLN C 1 250 ? 32.955  -60.349 49.999  1.00 153.22 ? 250 GLN C CA  1 
ATOM   7723  C C   . GLN C 1 250 ? 33.897  -59.191 49.684  1.00 149.72 ? 250 GLN C C   1 
ATOM   7724  O O   . GLN C 1 250 ? 33.480  -58.028 49.659  1.00 146.38 ? 250 GLN C O   1 
ATOM   7725  C CB  . GLN C 1 250 ? 32.019  -60.620 48.821  1.00 155.03 ? 250 GLN C CB  1 
ATOM   7726  C CG  . GLN C 1 250 ? 32.364  -61.859 48.007  1.00 155.57 ? 250 GLN C CG  1 
ATOM   7727  C CD  . GLN C 1 250 ? 33.423  -61.595 46.956  1.00 150.73 ? 250 GLN C CD  1 
ATOM   7728  O OE1 . GLN C 1 250 ? 34.585  -61.346 47.275  1.00 149.46 ? 250 GLN C OE1 1 
ATOM   7729  N NE2 . GLN C 1 250 ? 33.022  -61.645 45.691  1.00 155.61 ? 250 GLN C NE2 1 
ATOM   7730  N N   . ILE C 1 251 ? 35.170  -59.507 49.443  1.00 150.13 ? 251 ILE C N   1 
ATOM   7731  C CA  . ILE C 1 251 ? 36.186  -58.473 49.270  1.00 147.82 ? 251 ILE C CA  1 
ATOM   7732  C C   . ILE C 1 251 ? 36.905  -58.601 47.931  1.00 146.89 ? 251 ILE C C   1 
ATOM   7733  O O   . ILE C 1 251 ? 38.102  -58.907 47.884  1.00 144.88 ? 251 ILE C O   1 
ATOM   7734  C CB  . ILE C 1 251 ? 37.198  -58.501 50.430  1.00 145.75 ? 251 ILE C CB  1 
ATOM   7735  C CG1 . ILE C 1 251 ? 37.617  -59.940 50.745  1.00 150.42 ? 251 ILE C CG1 1 
ATOM   7736  C CG2 . ILE C 1 251 ? 36.614  -57.829 51.663  1.00 148.59 ? 251 ILE C CG2 1 
ATOM   7737  C CD1 . ILE C 1 251 ? 39.044  -60.064 51.221  1.00 156.02 ? 251 ILE C CD1 1 
ATOM   7738  N N   . LYS C 1 252 ? 36.192  -58.349 46.835  1.00 150.30 ? 252 LYS C N   1 
ATOM   7739  C CA  . LYS C 1 252 ? 36.838  -58.224 45.535  1.00 147.37 ? 252 LYS C CA  1 
ATOM   7740  C C   . LYS C 1 252 ? 37.260  -56.794 45.231  1.00 144.48 ? 252 LYS C C   1 
ATOM   7741  O O   . LYS C 1 252 ? 38.055  -56.578 44.309  1.00 143.14 ? 252 LYS C O   1 
ATOM   7742  C CB  . LYS C 1 252 ? 35.913  -58.724 44.419  1.00 148.25 ? 252 LYS C CB  1 
ATOM   7743  C CG  . LYS C 1 252 ? 34.684  -57.857 44.197  1.00 149.92 ? 252 LYS C CG  1 
ATOM   7744  C CD  . LYS C 1 252 ? 33.455  -58.451 44.863  1.00 152.28 ? 252 LYS C CD  1 
ATOM   7745  C CE  . LYS C 1 252 ? 32.528  -57.367 45.386  1.00 152.47 ? 252 LYS C CE  1 
ATOM   7746  N NZ  . LYS C 1 252 ? 33.107  -56.679 46.574  1.00 151.02 ? 252 LYS C NZ  1 
ATOM   7747  N N   . THR C 1 253 ? 36.751  -55.820 45.982  1.00 143.19 ? 253 THR C N   1 
ATOM   7748  C CA  . THR C 1 253 ? 37.004  -54.386 45.923  1.00 143.52 ? 253 THR C CA  1 
ATOM   7749  C C   . THR C 1 253 ? 38.133  -54.005 46.877  1.00 147.08 ? 253 THR C C   1 
ATOM   7750  O O   . THR C 1 253 ? 38.170  -54.483 48.015  1.00 145.02 ? 253 THR C O   1 
ATOM   7751  C CB  . THR C 1 253 ? 35.749  -53.600 46.289  1.00 145.55 ? 253 THR C CB  1 
ATOM   7752  O OG1 . THR C 1 253 ? 34.645  -54.502 46.442  1.00 145.51 ? 253 THR C OG1 1 
ATOM   7753  C CG2 . THR C 1 253 ? 35.420  -52.585 45.203  1.00 143.52 ? 253 THR C CG2 1 
ATOM   7754  N N   . PRO C 1 254 ? 39.062  -53.152 46.439  1.00 164.63 ? 254 PRO C N   1 
ATOM   7755  C CA  . PRO C 1 254 ? 40.075  -52.636 47.373  1.00 164.08 ? 254 PRO C CA  1 
ATOM   7756  C C   . PRO C 1 254 ? 39.495  -51.754 48.465  1.00 165.58 ? 254 PRO C C   1 
ATOM   7757  O O   . PRO C 1 254 ? 40.132  -51.600 49.513  1.00 165.54 ? 254 PRO C O   1 
ATOM   7758  C CB  . PRO C 1 254 ? 41.024  -51.847 46.461  1.00 161.32 ? 254 PRO C CB  1 
ATOM   7759  C CG  . PRO C 1 254 ? 40.183  -51.469 45.285  1.00 160.69 ? 254 PRO C CG  1 
ATOM   7760  C CD  . PRO C 1 254 ? 39.235  -52.616 45.078  1.00 162.53 ? 254 PRO C CD  1 
ATOM   7761  N N   . GLY C 1 255 ? 38.314  -51.172 48.256  1.00 153.56 ? 255 GLY C N   1 
ATOM   7762  C CA  . GLY C 1 255 ? 37.701  -50.363 49.298  1.00 152.50 ? 255 GLY C CA  1 
ATOM   7763  C C   . GLY C 1 255 ? 37.170  -51.190 50.450  1.00 150.85 ? 255 GLY C C   1 
ATOM   7764  O O   . GLY C 1 255 ? 37.232  -50.767 51.608  1.00 149.72 ? 255 GLY C O   1 
ATOM   7765  N N   . LYS C 1 256 ? 36.647  -52.382 50.153  1.00 144.89 ? 256 LYS C N   1 
ATOM   7766  C CA  . LYS C 1 256 ? 36.146  -53.271 51.194  1.00 142.84 ? 256 LYS C CA  1 
ATOM   7767  C C   . LYS C 1 256 ? 37.233  -53.727 52.161  1.00 143.66 ? 256 LYS C C   1 
ATOM   7768  O O   . LYS C 1 256 ? 36.907  -54.299 53.207  1.00 145.17 ? 256 LYS C O   1 
ATOM   7769  C CB  . LYS C 1 256 ? 35.478  -54.491 50.559  1.00 140.14 ? 256 LYS C CB  1 
ATOM   7770  C CG  . LYS C 1 256 ? 34.071  -54.240 50.039  1.00 137.34 ? 256 LYS C CG  1 
ATOM   7771  C CD  . LYS C 1 256 ? 33.107  -53.954 51.177  1.00 136.88 ? 256 LYS C CD  1 
ATOM   7772  C CE  . LYS C 1 256 ? 31.665  -54.193 50.754  1.00 129.96 ? 256 LYS C CE  1 
ATOM   7773  N NZ  . LYS C 1 256 ? 31.453  -55.590 50.278  1.00 129.49 ? 256 LYS C NZ  1 
ATOM   7774  N N   . SER C 1 257 ? 38.509  -53.488 51.843  0.64 144.94 ? 257 SER C N   1 
ATOM   7775  C CA  . SER C 1 257 ? 39.608  -53.910 52.703  0.64 146.05 ? 257 SER C CA  1 
ATOM   7776  C C   . SER C 1 257 ? 39.599  -53.233 54.069  0.64 148.41 ? 257 SER C C   1 
ATOM   7777  O O   . SER C 1 257 ? 40.355  -53.655 54.950  0.64 150.13 ? 257 SER C O   1 
ATOM   7778  C CB  . SER C 1 257 ? 40.943  -53.644 52.004  0.64 142.17 ? 257 SER C CB  1 
ATOM   7779  N N   . LEU C 1 258 ? 38.778  -52.201 54.267  1.00 145.40 ? 258 LEU C N   1 
ATOM   7780  C CA  . LEU C 1 258 ? 38.640  -51.543 55.561  1.00 144.06 ? 258 LEU C CA  1 
ATOM   7781  C C   . LEU C 1 258 ? 37.443  -52.056 56.349  1.00 152.17 ? 258 LEU C C   1 
ATOM   7782  O O   . LEU C 1 258 ? 37.571  -52.366 57.537  1.00 155.76 ? 258 LEU C O   1 
ATOM   7783  C CB  . LEU C 1 258 ? 38.524  -50.026 55.375  1.00 141.31 ? 258 LEU C CB  1 
ATOM   7784  C CG  . LEU C 1 258 ? 39.820  -49.284 55.053  1.00 136.00 ? 258 LEU C CG  1 
ATOM   7785  C CD1 . LEU C 1 258 ? 39.539  -47.813 54.807  1.00 129.81 ? 258 LEU C CD1 1 
ATOM   7786  C CD2 . LEU C 1 258 ? 40.813  -49.459 56.190  1.00 130.57 ? 258 LEU C CD2 1 
ATOM   7787  N N   . LYS C 1 259 ? 36.272  -52.132 55.709  1.00 167.84 ? 259 LYS C N   1 
ATOM   7788  C CA  . LYS C 1 259 ? 35.078  -52.618 56.391  1.00 170.22 ? 259 LYS C CA  1 
ATOM   7789  C C   . LYS C 1 259 ? 35.297  -54.018 56.953  1.00 172.40 ? 259 LYS C C   1 
ATOM   7790  O O   . LYS C 1 259 ? 34.840  -54.331 58.058  1.00 175.04 ? 259 LYS C O   1 
ATOM   7791  C CB  . LYS C 1 259 ? 33.887  -52.597 55.432  1.00 170.86 ? 259 LYS C CB  1 
ATOM   7792  C CG  . LYS C 1 259 ? 32.551  -52.907 56.084  1.00 175.38 ? 259 LYS C CG  1 
ATOM   7793  C CD  . LYS C 1 259 ? 31.423  -52.842 55.069  1.00 180.96 ? 259 LYS C CD  1 
ATOM   7794  C CE  . LYS C 1 259 ? 30.069  -52.983 55.742  1.00 187.10 ? 259 LYS C CE  1 
ATOM   7795  N NZ  . LYS C 1 259 ? 29.813  -51.870 56.695  1.00 185.62 ? 259 LYS C NZ  1 
ATOM   7796  N N   . CYS C 1 260 ? 35.997  -54.874 56.204  0.05 160.06 ? 260 CYS C N   1 
ATOM   7797  C CA  . CYS C 1 260 ? 36.317  -56.209 56.693  0.05 159.95 ? 260 CYS C CA  1 
ATOM   7798  C C   . CYS C 1 260 ? 37.443  -56.191 57.720  0.05 161.22 ? 260 CYS C C   1 
ATOM   7799  O O   . CYS C 1 260 ? 37.468  -57.040 58.618  0.05 160.62 ? 260 CYS C O   1 
ATOM   7800  C CB  . CYS C 1 260 ? 36.698  -57.119 55.524  0.05 153.73 ? 260 CYS C CB  1 
ATOM   7801  N N   . SER C 1 261 ? 38.383  -55.249 57.597  1.00 162.14 ? 261 SER C N   1 
ATOM   7802  C CA  . SER C 1 261 ? 39.480  -55.166 58.556  1.00 165.75 ? 261 SER C CA  1 
ATOM   7803  C C   . SER C 1 261 ? 38.980  -54.882 59.965  1.00 174.65 ? 261 SER C C   1 
ATOM   7804  O O   . SER C 1 261 ? 39.566  -55.366 60.939  1.00 171.48 ? 261 SER C O   1 
ATOM   7805  C CB  . SER C 1 261 ? 40.474  -54.090 58.123  1.00 160.46 ? 261 SER C CB  1 
ATOM   7806  O OG  . SER C 1 261 ? 41.533  -53.968 59.055  1.00 163.79 ? 261 SER C OG  1 
ATOM   7807  N N   . ALA C 1 262 ? 37.903  -54.102 60.095  1.00 213.45 ? 262 ALA C N   1 
ATOM   7808  C CA  . ALA C 1 262 ? 37.358  -53.815 61.417  1.00 213.56 ? 262 ALA C CA  1 
ATOM   7809  C C   . ALA C 1 262 ? 36.763  -55.065 62.051  1.00 214.74 ? 262 ALA C C   1 
ATOM   7810  O O   . ALA C 1 262 ? 36.856  -55.252 63.270  1.00 214.40 ? 262 ALA C O   1 
ATOM   7811  C CB  . ALA C 1 262 ? 36.305  -52.709 61.327  1.00 213.83 ? 262 ALA C CB  1 
ATOM   7812  N N   . LEU C 1 263 ? 36.150  -55.933 61.240  1.00 178.49 ? 263 LEU C N   1 
ATOM   7813  C CA  . LEU C 1 263 ? 35.567  -57.156 61.780  1.00 171.88 ? 263 LEU C CA  1 
ATOM   7814  C C   . LEU C 1 263 ? 36.651  -58.096 62.289  1.00 166.09 ? 263 LEU C C   1 
ATOM   7815  O O   . LEU C 1 263 ? 36.484  -58.740 63.331  1.00 164.81 ? 263 LEU C O   1 
ATOM   7816  C CB  . LEU C 1 263 ? 34.708  -57.842 60.719  1.00 184.82 ? 263 LEU C CB  1 
ATOM   7817  C CG  . LEU C 1 263 ? 33.572  -57.009 60.126  1.00 177.48 ? 263 LEU C CG  1 
ATOM   7818  C CD1 . LEU C 1 263 ? 32.881  -57.777 59.012  1.00 184.33 ? 263 LEU C CD1 1 
ATOM   7819  C CD2 . LEU C 1 263 ? 32.578  -56.612 61.206  1.00 175.79 ? 263 LEU C CD2 1 
ATOM   7820  N N   . TYR C 1 264 ? 37.766  -58.192 61.563  1.00 160.96 ? 264 TYR C N   1 
ATOM   7821  C CA  . TYR C 1 264 ? 38.888  -58.990 62.042  1.00 156.72 ? 264 TYR C CA  1 
ATOM   7822  C C   . TYR C 1 264 ? 39.470  -58.393 63.317  1.00 161.84 ? 264 TYR C C   1 
ATOM   7823  O O   . TYR C 1 264 ? 39.828  -59.125 64.247  1.00 160.49 ? 264 TYR C O   1 
ATOM   7824  C CB  . TYR C 1 264 ? 39.950  -59.110 60.952  1.00 152.74 ? 264 TYR C CB  1 
ATOM   7825  C CG  . TYR C 1 264 ? 39.601  -60.148 59.913  1.00 152.67 ? 264 TYR C CG  1 
ATOM   7826  C CD1 . TYR C 1 264 ? 38.866  -61.276 60.257  1.00 156.91 ? 264 TYR C CD1 1 
ATOM   7827  C CD2 . TYR C 1 264 ? 39.991  -59.998 58.591  1.00 154.29 ? 264 TYR C CD2 1 
ATOM   7828  C CE1 . TYR C 1 264 ? 38.537  -62.229 59.314  1.00 162.37 ? 264 TYR C CE1 1 
ATOM   7829  C CE2 . TYR C 1 264 ? 39.667  -60.947 57.639  1.00 154.30 ? 264 TYR C CE2 1 
ATOM   7830  C CZ  . TYR C 1 264 ? 38.939  -62.060 58.008  1.00 160.29 ? 264 TYR C CZ  1 
ATOM   7831  O OH  . TYR C 1 264 ? 38.613  -63.008 57.067  1.00 164.36 ? 264 TYR C OH  1 
ATOM   7832  N N   . LEU C 1 265 ? 39.579  -57.061 63.378  1.00 170.09 ? 265 LEU C N   1 
ATOM   7833  C CA  . LEU C 1 265 ? 40.014  -56.419 64.613  1.00 169.22 ? 265 LEU C CA  1 
ATOM   7834  C C   . LEU C 1 265 ? 38.993  -56.638 65.721  1.00 169.71 ? 265 LEU C C   1 
ATOM   7835  O O   . LEU C 1 265 ? 39.361  -56.873 66.878  1.00 167.56 ? 265 LEU C O   1 
ATOM   7836  C CB  . LEU C 1 265 ? 40.248  -54.926 64.382  1.00 169.05 ? 265 LEU C CB  1 
ATOM   7837  C CG  . LEU C 1 265 ? 41.399  -54.555 63.443  1.00 168.35 ? 265 LEU C CG  1 
ATOM   7838  C CD1 . LEU C 1 265 ? 41.486  -53.047 63.272  1.00 163.54 ? 265 LEU C CD1 1 
ATOM   7839  C CD2 . LEU C 1 265 ? 42.717  -55.117 63.957  1.00 165.51 ? 265 LEU C CD2 1 
ATOM   7840  N N   . SER C 1 266 ? 37.701  -56.558 65.385  1.00 166.38 ? 266 SER C N   1 
ATOM   7841  C CA  . SER C 1 266 ? 36.664  -56.933 66.340  1.00 161.48 ? 266 SER C CA  1 
ATOM   7842  C C   . SER C 1 266 ? 36.799  -58.397 66.742  1.00 162.46 ? 266 SER C C   1 
ATOM   7843  O O   . SER C 1 266 ? 36.542  -58.761 67.896  1.00 164.54 ? 266 SER C O   1 
ATOM   7844  C CB  . SER C 1 266 ? 35.281  -56.665 65.743  1.00 154.69 ? 266 SER C CB  1 
ATOM   7845  O OG  . SER C 1 266 ? 34.252  -57.141 66.596  1.00 150.56 ? 266 SER C OG  1 
ATOM   7846  N N   . GLN C 1 267 ? 37.204  -59.254 65.799  1.00 159.60 ? 267 GLN C N   1 
ATOM   7847  C CA  . GLN C 1 267 ? 37.484  -60.644 66.138  1.00 155.73 ? 267 GLN C CA  1 
ATOM   7848  C C   . GLN C 1 267 ? 38.717  -60.757 67.024  1.00 159.99 ? 267 GLN C C   1 
ATOM   7849  O O   . GLN C 1 267 ? 38.782  -61.641 67.885  1.00 162.99 ? 267 GLN C O   1 
ATOM   7850  C CB  . GLN C 1 267 ? 37.662  -61.470 64.863  1.00 153.86 ? 267 GLN C CB  1 
ATOM   7851  C CG  . GLN C 1 267 ? 37.726  -62.969 65.096  1.00 151.49 ? 267 GLN C CG  1 
ATOM   7852  C CD  . GLN C 1 267 ? 38.032  -63.742 63.830  1.00 151.54 ? 267 GLN C CD  1 
ATOM   7853  O OE1 . GLN C 1 267 ? 38.717  -63.247 62.935  1.00 143.34 ? 267 GLN C OE1 1 
ATOM   7854  N NE2 . GLN C 1 267 ? 37.523  -64.966 63.749  1.00 155.55 ? 267 GLN C NE2 1 
ATOM   7855  N N   . PHE C 1 268 ? 39.695  -59.872 66.836  1.00 158.76 ? 268 PHE C N   1 
ATOM   7856  C CA  . PHE C 1 268 ? 40.864  -59.805 67.703  1.00 159.75 ? 268 PHE C CA  1 
ATOM   7857  C C   . PHE C 1 268 ? 40.618  -58.946 68.933  1.00 171.01 ? 268 PHE C C   1 
ATOM   7858  O O   . PHE C 1 268 ? 41.493  -58.855 69.801  1.00 172.30 ? 268 PHE C O   1 
ATOM   7859  C CB  . PHE C 1 268 ? 42.069  -59.261 66.929  1.00 155.43 ? 268 PHE C CB  1 
ATOM   7860  C CG  . PHE C 1 268 ? 42.364  -60.013 65.663  1.00 152.25 ? 268 PHE C CG  1 
ATOM   7861  C CD1 . PHE C 1 268 ? 42.059  -61.361 65.550  1.00 149.03 ? 268 PHE C CD1 1 
ATOM   7862  C CD2 . PHE C 1 268 ? 42.937  -59.369 64.580  1.00 152.03 ? 268 PHE C CD2 1 
ATOM   7863  C CE1 . PHE C 1 268 ? 42.323  -62.051 64.382  1.00 145.40 ? 268 PHE C CE1 1 
ATOM   7864  C CE2 . PHE C 1 268 ? 43.203  -60.052 63.412  1.00 150.87 ? 268 PHE C CE2 1 
ATOM   7865  C CZ  . PHE C 1 268 ? 42.897  -61.394 63.312  1.00 145.09 ? 268 PHE C CZ  1 
ATOM   7866  N N   . ARG C 1 269 ? 39.445  -58.324 69.027  1.00 193.92 ? 269 ARG C N   1 
ATOM   7867  C CA  . ARG C 1 269 ? 39.023  -57.619 70.227  1.00 194.25 ? 269 ARG C CA  1 
ATOM   7868  C C   . ARG C 1 269 ? 38.097  -58.461 71.085  1.00 195.80 ? 269 ARG C C   1 
ATOM   7869  O O   . ARG C 1 269 ? 38.001  -58.224 72.289  1.00 199.69 ? 269 ARG C O   1 
ATOM   7870  C CB  . ARG C 1 269 ? 38.338  -56.293 69.871  1.00 193.72 ? 269 ARG C CB  1 
ATOM   7871  C CG  . ARG C 1 269 ? 38.382  -55.264 70.996  1.00 193.42 ? 269 ARG C CG  1 
ATOM   7872  C CD  . ARG C 1 269 ? 39.775  -55.187 71.613  1.00 192.65 ? 269 ARG C CD  1 
ATOM   7873  N NE  . ARG C 1 269 ? 40.421  -53.898 71.383  1.00 192.62 ? 269 ARG C NE  1 
ATOM   7874  C CZ  . ARG C 1 269 ? 41.605  -53.558 71.884  1.00 192.92 ? 269 ARG C CZ  1 
ATOM   7875  N NH1 . ARG C 1 269 ? 42.276  -54.412 72.645  1.00 195.76 ? 269 ARG C NH1 1 
ATOM   7876  N NH2 . ARG C 1 269 ? 42.118  -52.362 71.627  1.00 189.72 ? 269 ARG C NH2 1 
ATOM   7877  N N   . GLU C 1 270 ? 37.375  -59.408 70.486  1.00 181.54 ? 270 GLU C N   1 
ATOM   7878  C CA  . GLU C 1 270 ? 36.710  -60.436 71.277  1.00 181.30 ? 270 GLU C CA  1 
ATOM   7879  C C   . GLU C 1 270 ? 37.727  -61.439 71.813  1.00 180.21 ? 270 GLU C C   1 
ATOM   7880  O O   . GLU C 1 270 ? 37.832  -61.649 73.027  1.00 184.64 ? 270 GLU C O   1 
ATOM   7881  C CB  . GLU C 1 270 ? 35.641  -61.138 70.436  1.00 177.39 ? 270 GLU C CB  1 
ATOM   7882  N N   . THR C 1 271 ? 38.482  -62.071 70.916  1.00 173.63 ? 271 THR C N   1 
ATOM   7883  C CA  . THR C 1 271 ? 39.517  -63.030 71.280  1.00 170.22 ? 271 THR C CA  1 
ATOM   7884  C C   . THR C 1 271 ? 40.895  -62.375 71.293  1.00 172.80 ? 271 THR C C   1 
ATOM   7885  O O   . THR C 1 271 ? 41.255  -61.649 70.362  1.00 170.22 ? 271 THR C O   1 
ATOM   7886  C CB  . THR C 1 271 ? 39.519  -64.214 70.310  1.00 162.33 ? 271 THR C CB  1 
ATOM   7887  O OG1 . THR C 1 271 ? 40.314  -63.894 69.162  1.00 154.92 ? 271 THR C OG1 1 
ATOM   7888  C CG2 . THR C 1 271 ? 38.101  -64.540 69.862  1.00 161.46 ? 271 THR C CG2 1 
ATOM   7889  N N   . SER C 1 272 ? 41.673  -62.665 72.347  1.00 180.57 ? 272 SER C N   1 
ATOM   7890  C CA  . SER C 1 272 ? 43.048  -62.205 72.553  1.00 181.80 ? 272 SER C CA  1 
ATOM   7891  C C   . SER C 1 272 ? 43.269  -60.740 72.187  1.00 186.24 ? 272 SER C C   1 
ATOM   7892  O O   . SER C 1 272 ? 43.796  -60.439 71.110  1.00 180.07 ? 272 SER C O   1 
ATOM   7893  C CB  . SER C 1 272 ? 44.016  -63.077 71.755  1.00 172.60 ? 272 SER C CB  1 
ATOM   7894  O OG  . SER C 1 272 ? 43.786  -62.959 70.361  1.00 164.09 ? 272 SER C OG  1 
ATOM   7895  N N   . PRO C 1 273 ? 42.869  -59.801 73.051  1.00 210.14 ? 273 PRO C N   1 
ATOM   7896  C CA  . PRO C 1 273 ? 43.053  -58.377 72.737  1.00 209.13 ? 273 PRO C CA  1 
ATOM   7897  C C   . PRO C 1 273 ? 44.459  -57.881 72.971  1.00 207.93 ? 273 PRO C C   1 
ATOM   7898  O O   . PRO C 1 273 ? 44.812  -56.822 72.442  1.00 206.86 ? 273 PRO C O   1 
ATOM   7899  C CB  . PRO C 1 273 ? 42.125  -57.690 73.727  1.00 209.89 ? 273 PRO C CB  1 
ATOM   7900  C CG  . PRO C 1 273 ? 42.313  -58.561 74.931  1.00 210.81 ? 273 PRO C CG  1 
ATOM   7901  C CD  . PRO C 1 273 ? 42.393  -59.984 74.430  1.00 211.20 ? 273 PRO C CD  1 
ATOM   7902  N N   . HIS C 1 274 ? 45.267  -58.596 73.758  1.00 191.00 ? 274 HIS C N   1 
ATOM   7903  C CA  . HIS C 1 274 ? 46.615  -58.129 74.040  1.00 189.24 ? 274 HIS C CA  1 
ATOM   7904  C C   . HIS C 1 274 ? 47.451  -58.084 72.777  1.00 185.25 ? 274 HIS C C   1 
ATOM   7905  O O   . HIS C 1 274 ? 48.454  -57.366 72.731  1.00 184.24 ? 274 HIS C O   1 
ATOM   7906  C CB  . HIS C 1 274 ? 47.271  -59.031 75.084  1.00 192.36 ? 274 HIS C CB  1 
ATOM   7907  C CG  . HIS C 1 274 ? 46.963  -60.484 74.893  1.00 196.14 ? 274 HIS C CG  1 
ATOM   7908  N ND1 . HIS C 1 274 ? 45.890  -61.104 75.494  1.00 199.86 ? 274 HIS C ND1 1 
ATOM   7909  C CD2 . HIS C 1 274 ? 47.588  -61.438 74.163  1.00 196.85 ? 274 HIS C CD2 1 
ATOM   7910  C CE1 . HIS C 1 274 ? 45.867  -62.378 75.143  1.00 201.34 ? 274 HIS C CE1 1 
ATOM   7911  N NE2 . HIS C 1 274 ? 46.887  -62.606 74.336  1.00 201.74 ? 274 HIS C NE2 1 
ATOM   7912  N N   . ILE C 1 275 ? 47.056  -58.840 71.750  1.00 177.42 ? 275 ILE C N   1 
ATOM   7913  C CA  . ILE C 1 275 ? 47.676  -58.699 70.444  1.00 169.02 ? 275 ILE C CA  1 
ATOM   7914  C C   . ILE C 1 275 ? 47.294  -57.369 69.813  1.00 165.80 ? 275 ILE C C   1 
ATOM   7915  O O   . ILE C 1 275 ? 48.003  -56.877 68.929  1.00 160.30 ? 275 ILE C O   1 
ATOM   7916  C CB  . ILE C 1 275 ? 47.274  -59.877 69.538  1.00 162.73 ? 275 ILE C CB  1 
ATOM   7917  C CG1 . ILE C 1 275 ? 45.875  -59.660 68.958  1.00 160.50 ? 275 ILE C CG1 1 
ATOM   7918  C CG2 . ILE C 1 275 ? 47.302  -61.182 70.315  1.00 162.88 ? 275 ILE C CG2 1 
ATOM   7919  C CD1 . ILE C 1 275 ? 45.577  -60.499 67.739  1.00 150.56 ? 275 ILE C CD1 1 
ATOM   7920  N N   . LEU C 1 276 ? 46.182  -56.778 70.243  1.00 163.89 ? 276 LEU C N   1 
ATOM   7921  C CA  . LEU C 1 276 ? 45.757  -55.469 69.776  1.00 161.83 ? 276 LEU C CA  1 
ATOM   7922  C C   . LEU C 1 276 ? 46.287  -54.401 70.722  1.00 165.55 ? 276 LEU C C   1 
ATOM   7923  O O   . LEU C 1 276 ? 46.261  -54.570 71.945  1.00 170.58 ? 276 LEU C O   1 
ATOM   7924  C CB  . LEU C 1 276 ? 44.231  -55.391 69.701  1.00 163.11 ? 276 LEU C CB  1 
ATOM   7925  C CG  . LEU C 1 276 ? 43.533  -56.211 68.613  1.00 161.58 ? 276 LEU C CG  1 
ATOM   7926  C CD1 . LEU C 1 276 ? 42.167  -55.622 68.291  1.00 165.33 ? 276 LEU C CD1 1 
ATOM   7927  C CD2 . LEU C 1 276 ? 44.388  -56.309 67.358  1.00 157.09 ? 276 LEU C CD2 1 
ATOM   7928  N N   . ALA C 1 277 ? 46.773  -53.305 70.150  1.00 162.72 ? 277 ALA C N   1 
ATOM   7929  C CA  . ALA C 1 277 ? 47.252  -52.196 70.962  1.00 164.24 ? 277 ALA C CA  1 
ATOM   7930  C C   . ALA C 1 277 ? 46.105  -51.573 71.751  1.00 169.08 ? 277 ALA C C   1 
ATOM   7931  O O   . ALA C 1 277 ? 45.069  -51.212 71.186  1.00 166.34 ? 277 ALA C O   1 
ATOM   7932  C CB  . ALA C 1 277 ? 47.920  -51.148 70.075  1.00 163.09 ? 277 ALA C CB  1 
ATOM   7933  N N   . SER C 1 278 ? 46.292  -51.455 73.074  1.00 172.33 ? 278 SER C N   1 
ATOM   7934  C CA  . SER C 1 278 ? 45.319  -50.830 73.963  1.00 172.83 ? 278 SER C CA  1 
ATOM   7935  C C   . SER C 1 278 ? 46.099  -49.940 74.934  1.00 176.94 ? 278 SER C C   1 
ATOM   7936  O O   . SER C 1 278 ? 46.214  -50.215 76.128  1.00 180.32 ? 278 SER C O   1 
ATOM   7937  C CB  . SER C 1 278 ? 44.471  -51.865 74.707  1.00 173.69 ? 278 SER C CB  1 
ATOM   7938  O OG  . SER C 1 278 ? 45.239  -53.007 75.050  1.00 173.97 ? 278 SER C OG  1 
ATOM   7939  N N   . GLY C 1 279 ? 46.643  -48.847 74.404  1.00 186.60 ? 279 GLY C N   1 
ATOM   7940  C CA  . GLY C 1 279 ? 47.414  -47.913 75.202  1.00 185.13 ? 279 GLY C CA  1 
ATOM   7941  C C   . GLY C 1 279 ? 46.552  -47.112 76.151  1.00 189.31 ? 279 GLY C C   1 
ATOM   7942  O O   . GLY C 1 279 ? 46.718  -47.204 77.371  1.00 195.48 ? 279 GLY C O   1 
ATOM   7943  N N   . ASP C 1 280 ? 45.623  -46.330 75.599  1.00 170.99 ? 280 ASP C N   1 
ATOM   7944  C CA  . ASP C 1 280 ? 44.657  -45.568 76.388  1.00 174.01 ? 280 ASP C CA  1 
ATOM   7945  C C   . ASP C 1 280 ? 45.358  -44.697 77.429  1.00 182.47 ? 280 ASP C C   1 
ATOM   7946  O O   . ASP C 1 280 ? 45.069  -44.754 78.626  1.00 182.90 ? 280 ASP C O   1 
ATOM   7947  C CB  . ASP C 1 280 ? 43.646  -46.504 77.052  1.00 175.68 ? 280 ASP C CB  1 
ATOM   7948  C CG  . ASP C 1 280 ? 42.774  -47.228 76.046  1.00 169.76 ? 280 ASP C CG  1 
ATOM   7949  O OD1 . ASP C 1 280 ? 43.290  -48.110 75.327  1.00 168.25 ? 280 ASP C OD1 1 
ATOM   7950  O OD2 . ASP C 1 280 ? 41.567  -46.922 75.988  1.00 168.73 ? 280 ASP C OD2 1 
ATOM   7951  N N   . GLY C 1 281 ? 46.310  -43.898 76.962  1.00 168.23 ? 281 GLY C N   1 
ATOM   7952  C CA  . GLY C 1 281 ? 47.080  -43.067 77.868  1.00 163.13 ? 281 GLY C CA  1 
ATOM   7953  C C   . GLY C 1 281 ? 48.260  -42.445 77.151  1.00 153.61 ? 281 GLY C C   1 
ATOM   7954  O O   . GLY C 1 281 ? 48.299  -42.395 75.920  1.00 147.28 ? 281 GLY C O   1 
ATOM   7955  N N   . THR C 1 282 ? 49.226  -41.976 77.949  1.00 156.62 ? 282 THR C N   1 
ATOM   7956  C CA  . THR C 1 282 ? 50.451  -41.362 77.445  1.00 155.51 ? 282 THR C CA  1 
ATOM   7957  C C   . THR C 1 282 ? 51.591  -41.686 78.416  1.00 163.25 ? 282 THR C C   1 
ATOM   7958  O O   . THR C 1 282 ? 52.119  -40.837 79.133  1.00 166.34 ? 282 THR C O   1 
ATOM   7959  C CB  . THR C 1 282 ? 50.297  -39.851 77.254  1.00 147.34 ? 282 THR C CB  1 
ATOM   7960  O OG1 . THR C 1 282 ? 49.479  -39.313 78.301  1.00 149.68 ? 282 THR C OG1 1 
ATOM   7961  C CG2 . THR C 1 282 ? 49.672  -39.535 75.901  1.00 140.90 ? 282 THR C CG2 1 
ATOM   7962  N N   . ASN C 1 283 ? 51.983  -42.960 78.439  1.00 171.70 ? 283 ASN C N   1 
ATOM   7963  C CA  . ASN C 1 283 ? 53.183  -43.384 79.150  1.00 175.14 ? 283 ASN C CA  1 
ATOM   7964  C C   . ASN C 1 283 ? 54.226  -43.792 78.121  1.00 170.97 ? 283 ASN C C   1 
ATOM   7965  O O   . ASN C 1 283 ? 54.710  -44.929 78.135  1.00 170.83 ? 283 ASN C O   1 
ATOM   7966  C CB  . ASN C 1 283 ? 52.887  -44.539 80.110  1.00 178.99 ? 283 ASN C CB  1 
ATOM   7967  C CG  . ASN C 1 283 ? 51.523  -44.423 80.763  1.00 189.30 ? 283 ASN C CG  1 
ATOM   7968  O OD1 . ASN C 1 283 ? 51.030  -43.321 81.007  1.00 192.90 ? 283 ASN C OD1 1 
ATOM   7969  N ND2 . ASN C 1 283 ? 50.907  -45.563 81.054  1.00 195.86 ? 283 ASN C ND2 1 
ATOM   7970  N N   . ARG C 1 284 ? 54.568  -42.859 77.228  1.00 157.95 ? 284 ARG C N   1 
ATOM   7971  C CA  . ARG C 1 284 ? 55.295  -43.060 75.976  1.00 151.75 ? 284 ARG C CA  1 
ATOM   7972  C C   . ARG C 1 284 ? 54.469  -43.825 74.947  1.00 147.21 ? 284 ARG C C   1 
ATOM   7973  O O   . ARG C 1 284 ? 54.935  -44.017 73.818  1.00 142.62 ? 284 ARG C O   1 
ATOM   7974  C CB  . ARG C 1 284 ? 56.646  -43.769 76.163  1.00 153.74 ? 284 ARG C CB  1 
ATOM   7975  C CG  . ARG C 1 284 ? 57.844  -42.839 76.051  1.00 153.77 ? 284 ARG C CG  1 
ATOM   7976  C CD  . ARG C 1 284 ? 59.141  -43.615 75.919  1.00 159.70 ? 284 ARG C CD  1 
ATOM   7977  N NE  . ARG C 1 284 ? 60.258  -42.749 75.559  1.00 170.49 ? 284 ARG C NE  1 
ATOM   7978  C CZ  . ARG C 1 284 ? 60.908  -42.816 74.403  1.00 175.06 ? 284 ARG C CZ  1 
ATOM   7979  N NH1 . ARG C 1 284 ? 60.553  -43.718 73.498  1.00 171.86 ? 284 ARG C NH1 1 
ATOM   7980  N NH2 . ARG C 1 284 ? 61.915  -41.990 74.154  1.00 181.74 ? 284 ARG C NH2 1 
ATOM   7981  N N   . LYS C 1 285 ? 53.255  -44.274 75.302  1.00 147.45 ? 285 LYS C N   1 
ATOM   7982  C CA  . LYS C 1 285 ? 52.318  -44.932 74.405  1.00 144.91 ? 285 LYS C CA  1 
ATOM   7983  C C   . LYS C 1 285 ? 51.267  -43.935 73.960  1.00 144.61 ? 285 LYS C C   1 
ATOM   7984  O O   . LYS C 1 285 ? 50.705  -43.221 74.801  1.00 147.20 ? 285 LYS C O   1 
ATOM   7985  C CB  . LYS C 1 285 ? 51.647  -46.119 75.088  1.00 145.83 ? 285 LYS C CB  1 
ATOM   7986  N N   . PRO C 1 286 ? 50.974  -43.849 72.666  1.00 141.40 ? 286 PRO C N   1 
ATOM   7987  C CA  . PRO C 1 286 ? 50.021  -42.842 72.184  1.00 138.25 ? 286 PRO C CA  1 
ATOM   7988  C C   . PRO C 1 286 ? 48.609  -43.139 72.670  1.00 140.10 ? 286 PRO C C   1 
ATOM   7989  O O   . PRO C 1 286 ? 48.318  -44.167 73.290  1.00 144.81 ? 286 PRO C O   1 
ATOM   7990  C CB  . PRO C 1 286 ? 50.121  -42.959 70.658  1.00 134.47 ? 286 PRO C CB  1 
ATOM   7991  C CG  . PRO C 1 286 ? 51.430  -43.622 70.407  1.00 141.48 ? 286 PRO C CG  1 
ATOM   7992  C CD  . PRO C 1 286 ? 51.628  -44.560 71.560  1.00 141.53 ? 286 PRO C CD  1 
ATOM   7993  N N   . THR C 1 287 ? 47.718  -42.195 72.367  1.00 139.99 ? 287 THR C N   1 
ATOM   7994  C CA  . THR C 1 287 ? 46.311  -42.299 72.736  1.00 139.30 ? 287 THR C CA  1 
ATOM   7995  C C   . THR C 1 287 ? 45.627  -43.255 71.773  1.00 137.61 ? 287 THR C C   1 
ATOM   7996  O O   . THR C 1 287 ? 45.273  -42.886 70.652  1.00 133.90 ? 287 THR C O   1 
ATOM   7997  C CB  . THR C 1 287 ? 45.646  -40.930 72.722  1.00 131.44 ? 287 THR C CB  1 
ATOM   7998  O OG1 . THR C 1 287 ? 46.332  -40.075 71.801  1.00 128.61 ? 287 THR C OG1 1 
ATOM   7999  C CG2 . THR C 1 287 ? 45.677  -40.319 74.113  1.00 130.50 ? 287 THR C CG2 1 
ATOM   8000  N N   . ILE C 1 288 ? 45.432  -44.486 72.216  1.00 149.43 ? 288 ILE C N   1 
ATOM   8001  C CA  . ILE C 1 288 ? 44.803  -45.519 71.402  1.00 152.75 ? 288 ILE C CA  1 
ATOM   8002  C C   . ILE C 1 288 ? 43.315  -45.573 71.716  1.00 154.99 ? 288 ILE C C   1 
ATOM   8003  O O   . ILE C 1 288 ? 42.918  -45.651 72.887  1.00 154.31 ? 288 ILE C O   1 
ATOM   8004  C CB  . ILE C 1 288 ? 45.476  -46.881 71.634  1.00 157.92 ? 288 ILE C CB  1 
ATOM   8005  C CG1 . ILE C 1 288 ? 46.857  -46.887 70.972  1.00 157.33 ? 288 ILE C CG1 1 
ATOM   8006  C CG2 . ILE C 1 288 ? 44.606  -48.000 71.115  1.00 158.72 ? 288 ILE C CG2 1 
ATOM   8007  C CD1 . ILE C 1 288 ? 47.823  -47.867 71.569  1.00 170.97 ? 288 ILE C CD1 1 
ATOM   8008  N N   . ILE C 1 289 ? 42.489  -45.532 70.668  1.00 153.08 ? 289 ILE C N   1 
ATOM   8009  C CA  . ILE C 1 289 ? 41.040  -45.433 70.819  1.00 156.03 ? 289 ILE C CA  1 
ATOM   8010  C C   . ILE C 1 289 ? 40.346  -46.707 70.345  1.00 163.71 ? 289 ILE C C   1 
ATOM   8011  O O   . ILE C 1 289 ? 39.380  -46.649 69.575  1.00 153.55 ? 289 ILE C O   1 
ATOM   8012  C CB  . ILE C 1 289 ? 40.505  -44.202 70.063  1.00 145.50 ? 289 ILE C CB  1 
ATOM   8013  C CG1 . ILE C 1 289 ? 41.536  -43.070 70.089  1.00 138.75 ? 289 ILE C CG1 1 
ATOM   8014  C CG2 . ILE C 1 289 ? 39.216  -43.709 70.689  1.00 153.21 ? 289 ILE C CG2 1 
ATOM   8015  C CD1 . ILE C 1 289 ? 41.740  -42.452 71.458  1.00 138.35 ? 289 ILE C CD1 1 
ATOM   8016  N N   . GLY C 1 290 ? 40.824  -47.864 70.803  1.00 205.00 ? 290 GLY C N   1 
ATOM   8017  C CA  . GLY C 1 290 ? 40.158  -49.131 70.542  1.00 206.00 ? 290 GLY C CA  1 
ATOM   8018  C C   . GLY C 1 290 ? 40.290  -49.673 69.130  1.00 205.32 ? 290 GLY C C   1 
ATOM   8019  O O   . GLY C 1 290 ? 40.348  -48.905 68.165  1.00 204.41 ? 290 GLY C O   1 
ATOM   8020  N N   . ASP C 1 291 ? 40.327  -51.004 69.005  1.00 174.00 ? 291 ASP C N   1 
ATOM   8021  C CA  . ASP C 1 291 ? 40.410  -51.694 67.716  1.00 164.21 ? 291 ASP C CA  1 
ATOM   8022  C C   . ASP C 1 291 ? 41.613  -51.209 66.906  1.00 159.16 ? 291 ASP C C   1 
ATOM   8023  O O   . ASP C 1 291 ? 41.483  -50.707 65.788  1.00 153.75 ? 291 ASP C O   1 
ATOM   8024  C CB  . ASP C 1 291 ? 39.109  -51.540 66.920  1.00 155.78 ? 291 ASP C CB  1 
ATOM   8025  C CG  . ASP C 1 291 ? 38.242  -52.781 66.978  1.00 159.17 ? 291 ASP C CG  1 
ATOM   8026  O OD1 . ASP C 1 291 ? 38.445  -53.605 67.894  1.00 162.43 ? 291 ASP C OD1 1 
ATOM   8027  O OD2 . ASP C 1 291 ? 37.365  -52.936 66.102  1.00 160.15 ? 291 ASP C OD2 1 
ATOM   8028  N N   . VAL C 1 292 ? 42.796  -51.365 67.495  1.00 157.63 ? 292 VAL C N   1 
ATOM   8029  C CA  . VAL C 1 292 ? 44.045  -50.940 66.876  1.00 154.76 ? 292 VAL C CA  1 
ATOM   8030  C C   . VAL C 1 292 ? 45.048  -52.080 66.958  1.00 157.93 ? 292 VAL C C   1 
ATOM   8031  O O   . VAL C 1 292 ? 45.278  -52.634 68.039  1.00 158.95 ? 292 VAL C O   1 
ATOM   8032  C CB  . VAL C 1 292 ? 44.620  -49.680 67.552  1.00 153.73 ? 292 VAL C CB  1 
ATOM   8033  C CG1 . VAL C 1 292 ? 45.879  -49.222 66.831  1.00 151.31 ? 292 VAL C CG1 1 
ATOM   8034  C CG2 . VAL C 1 292 ? 43.586  -48.567 67.594  1.00 152.32 ? 292 VAL C CG2 1 
ATOM   8035  N N   . TYR C 1 293 ? 45.643  -52.428 65.820  1.00 158.57 ? 293 TYR C N   1 
ATOM   8036  C CA  . TYR C 1 293 ? 46.767  -53.354 65.765  1.00 161.11 ? 293 TYR C CA  1 
ATOM   8037  C C   . TYR C 1 293 ? 48.021  -52.569 65.410  1.00 163.86 ? 293 TYR C C   1 
ATOM   8038  O O   . TYR C 1 293 ? 48.097  -51.971 64.332  1.00 163.84 ? 293 TYR C O   1 
ATOM   8039  C CB  . TYR C 1 293 ? 46.547  -54.476 64.751  1.00 163.03 ? 293 TYR C CB  1 
ATOM   8040  C CG  . TYR C 1 293 ? 47.800  -55.294 64.519  1.00 163.34 ? 293 TYR C CG  1 
ATOM   8041  C CD1 . TYR C 1 293 ? 48.600  -55.079 63.403  1.00 166.49 ? 293 TYR C CD1 1 
ATOM   8042  C CD2 . TYR C 1 293 ? 48.200  -56.260 65.434  1.00 161.95 ? 293 TYR C CD2 1 
ATOM   8043  C CE1 . TYR C 1 293 ? 49.751  -55.815 63.195  1.00 164.53 ? 293 TYR C CE1 1 
ATOM   8044  C CE2 . TYR C 1 293 ? 49.350  -57.003 65.234  1.00 162.54 ? 293 TYR C CE2 1 
ATOM   8045  C CZ  . TYR C 1 293 ? 50.121  -56.776 64.114  1.00 159.72 ? 293 TYR C CZ  1 
ATOM   8046  O OH  . TYR C 1 293 ? 51.266  -57.512 63.910  1.00 152.72 ? 293 TYR C OH  1 
ATOM   8047  N N   . ILE C 1 294 ? 48.990  -52.564 66.318  1.00 180.65 ? 294 ILE C N   1 
ATOM   8048  C CA  . ILE C 1 294 ? 50.249  -51.852 66.137  1.00 179.16 ? 294 ILE C CA  1 
ATOM   8049  C C   . ILE C 1 294 ? 51.367  -52.881 66.070  1.00 178.51 ? 294 ILE C C   1 
ATOM   8050  O O   . ILE C 1 294 ? 51.527  -53.695 66.988  1.00 179.42 ? 294 ILE C O   1 
ATOM   8051  C CB  . ILE C 1 294 ? 50.493  -50.844 67.269  1.00 179.66 ? 294 ILE C CB  1 
ATOM   8052  C CG1 . ILE C 1 294 ? 49.579  -49.627 67.108  1.00 181.76 ? 294 ILE C CG1 1 
ATOM   8053  C CG2 . ILE C 1 294 ? 51.949  -50.422 67.300  1.00 177.86 ? 294 ILE C CG2 1 
ATOM   8054  C CD1 . ILE C 1 294 ? 49.774  -48.581 68.181  1.00 189.90 ? 294 ILE C CD1 1 
ATOM   8055  N N   . HIS C 1 295 ? 52.137  -52.854 64.986  1.00 148.78 ? 295 HIS C N   1 
ATOM   8056  C CA  . HIS C 1 295 ? 53.286  -53.738 64.884  1.00 132.15 ? 295 HIS C CA  1 
ATOM   8057  C C   . HIS C 1 295 ? 54.392  -53.262 65.826  1.00 126.79 ? 295 HIS C C   1 
ATOM   8058  O O   . HIS C 1 295 ? 54.548  -52.062 66.059  1.00 132.77 ? 295 HIS C O   1 
ATOM   8059  C CB  . HIS C 1 295 ? 53.804  -53.796 63.447  1.00 127.47 ? 295 HIS C CB  1 
ATOM   8060  C CG  . HIS C 1 295 ? 54.765  -54.917 63.198  1.00 118.32 ? 295 HIS C CG  1 
ATOM   8061  N ND1 . HIS C 1 295 ? 56.109  -54.823 63.490  1.00 113.69 ? 295 HIS C ND1 1 
ATOM   8062  C CD2 . HIS C 1 295 ? 54.578  -56.160 62.694  1.00 115.30 ? 295 HIS C CD2 1 
ATOM   8063  C CE1 . HIS C 1 295 ? 56.707  -55.958 63.177  1.00 105.92 ? 295 HIS C CE1 1 
ATOM   8064  N NE2 . HIS C 1 295 ? 55.801  -56.785 62.689  1.00 106.04 ? 295 HIS C NE2 1 
ATOM   8065  N N   . PRO C 1 296 ? 55.157  -54.188 66.407  1.00 116.91 ? 296 PRO C N   1 
ATOM   8066  C CA  . PRO C 1 296 ? 56.244  -53.778 67.313  1.00 110.92 ? 296 PRO C CA  1 
ATOM   8067  C C   . PRO C 1 296 ? 57.371  -53.010 66.636  1.00 112.50 ? 296 PRO C C   1 
ATOM   8068  O O   . PRO C 1 296 ? 58.131  -52.327 67.333  1.00 112.36 ? 296 PRO C O   1 
ATOM   8069  C CB  . PRO C 1 296 ? 56.746  -55.112 67.883  1.00 106.70 ? 296 PRO C CB  1 
ATOM   8070  C CG  . PRO C 1 296 ? 56.282  -56.151 66.904  1.00 106.73 ? 296 PRO C CG  1 
ATOM   8071  C CD  . PRO C 1 296 ? 54.967  -55.649 66.402  1.00 116.93 ? 296 PRO C CD  1 
ATOM   8072  N N   . SER C 1 297 ? 57.507  -53.089 65.315  1.00 113.53 ? 297 SER C N   1 
ATOM   8073  C CA  . SER C 1 297 ? 58.593  -52.425 64.604  1.00 114.44 ? 297 SER C CA  1 
ATOM   8074  C C   . SER C 1 297 ? 58.265  -50.984 64.232  1.00 121.86 ? 297 SER C C   1 
ATOM   8075  O O   . SER C 1 297 ? 59.037  -50.355 63.502  1.00 121.62 ? 297 SER C O   1 
ATOM   8076  C CB  . SER C 1 297 ? 58.965  -53.212 63.346  1.00 115.91 ? 297 SER C CB  1 
ATOM   8077  O OG  . SER C 1 297 ? 60.097  -52.645 62.710  1.00 121.11 ? 297 SER C OG  1 
ATOM   8078  N N   . VAL C 1 298 ? 57.142  -50.453 64.710  1.00 128.79 ? 298 VAL C N   1 
ATOM   8079  C CA  . VAL C 1 298 ? 56.747  -49.093 64.370  1.00 137.61 ? 298 VAL C CA  1 
ATOM   8080  C C   . VAL C 1 298 ? 57.443  -48.102 65.296  1.00 142.26 ? 298 VAL C C   1 
ATOM   8081  O O   . VAL C 1 298 ? 57.954  -48.450 66.362  1.00 138.50 ? 298 VAL C O   1 
ATOM   8082  C CB  . VAL C 1 298 ? 55.219  -48.929 64.440  1.00 140.34 ? 298 VAL C CB  1 
ATOM   8083  C CG1 . VAL C 1 298 ? 54.532  -50.089 63.762  1.00 135.49 ? 298 VAL C CG1 1 
ATOM   8084  C CG2 . VAL C 1 298 ? 54.769  -48.803 65.879  1.00 144.74 ? 298 VAL C CG2 1 
ATOM   8085  N N   . LYS C 1 299 ? 57.467  -46.844 64.865  1.00 154.75 ? 299 LYS C N   1 
ATOM   8086  C CA  . LYS C 1 299 ? 57.965  -45.736 65.668  1.00 158.85 ? 299 LYS C CA  1 
ATOM   8087  C C   . LYS C 1 299 ? 56.805  -44.781 65.911  1.00 166.04 ? 299 LYS C C   1 
ATOM   8088  O O   . LYS C 1 299 ? 56.182  -44.307 64.957  1.00 171.02 ? 299 LYS C O   1 
ATOM   8089  C CB  . LYS C 1 299 ? 59.126  -45.031 64.964  1.00 167.09 ? 299 LYS C CB  1 
ATOM   8090  C CG  . LYS C 1 299 ? 59.650  -43.798 65.671  1.00 173.74 ? 299 LYS C CG  1 
ATOM   8091  C CD  . LYS C 1 299 ? 60.836  -43.225 64.918  1.00 190.14 ? 299 LYS C CD  1 
ATOM   8092  C CE  . LYS C 1 299 ? 62.040  -44.147 65.027  1.00 190.99 ? 299 LYS C CE  1 
ATOM   8093  N NZ  . LYS C 1 299 ? 62.541  -44.242 66.424  1.00 185.81 ? 299 LYS C NZ  1 
ATOM   8094  N N   . LEU C 1 300 ? 56.519  -44.502 67.180  1.00 161.19 ? 300 LEU C N   1 
ATOM   8095  C CA  . LEU C 1 300 ? 55.342  -43.739 67.565  1.00 162.94 ? 300 LEU C CA  1 
ATOM   8096  C C   . LEU C 1 300 ? 55.735  -42.532 68.408  1.00 159.89 ? 300 LEU C C   1 
ATOM   8097  O O   . LEU C 1 300 ? 56.838  -42.459 68.960  1.00 165.31 ? 300 LEU C O   1 
ATOM   8098  C CB  . LEU C 1 300 ? 54.345  -44.600 68.352  1.00 160.19 ? 300 LEU C CB  1 
ATOM   8099  C CG  . LEU C 1 300 ? 53.791  -45.860 67.685  1.00 158.51 ? 300 LEU C CG  1 
ATOM   8100  C CD1 . LEU C 1 300 ? 52.888  -46.612 68.648  1.00 161.92 ? 300 LEU C CD1 1 
ATOM   8101  C CD2 . LEU C 1 300 ? 53.040  -45.507 66.417  1.00 160.05 ? 300 LEU C CD2 1 
ATOM   8102  N N   . HIS C 1 301 ? 54.807  -41.579 68.499  1.00 159.94 ? 301 HIS C N   1 
ATOM   8103  C CA  . HIS C 1 301 ? 54.942  -40.416 69.357  1.00 151.47 ? 301 HIS C CA  1 
ATOM   8104  C C   . HIS C 1 301 ? 53.704  -40.316 70.240  1.00 149.18 ? 301 HIS C C   1 
ATOM   8105  O O   . HIS C 1 301 ? 52.577  -40.482 69.746  1.00 147.73 ? 301 HIS C O   1 
ATOM   8106  C CB  . HIS C 1 301 ? 55.120  -39.131 68.536  1.00 154.96 ? 301 HIS C CB  1 
ATOM   8107  C CG  . HIS C 1 301 ? 55.659  -37.980 69.327  1.00 153.99 ? 301 HIS C CG  1 
ATOM   8108  N ND1 . HIS C 1 301 ? 54.878  -37.229 70.179  1.00 148.96 ? 301 HIS C ND1 1 
ATOM   8109  C CD2 . HIS C 1 301 ? 56.904  -37.455 69.400  1.00 156.92 ? 301 HIS C CD2 1 
ATOM   8110  C CE1 . HIS C 1 301 ? 55.618  -36.289 70.739  1.00 146.10 ? 301 HIS C CE1 1 
ATOM   8111  N NE2 . HIS C 1 301 ? 56.851  -36.404 70.283  1.00 151.20 ? 301 HIS C NE2 1 
ATOM   8112  N N   . PRO C 1 302 ? 53.867  -40.056 71.541  1.00 144.30 ? 302 PRO C N   1 
ATOM   8113  C CA  . PRO C 1 302 ? 52.707  -40.069 72.449  1.00 141.04 ? 302 PRO C CA  1 
ATOM   8114  C C   . PRO C 1 302 ? 51.676  -38.988 72.158  1.00 135.99 ? 302 PRO C C   1 
ATOM   8115  O O   . PRO C 1 302 ? 50.560  -39.067 72.691  1.00 131.31 ? 302 PRO C O   1 
ATOM   8116  C CB  . PRO C 1 302 ? 53.338  -39.867 73.836  1.00 138.56 ? 302 PRO C CB  1 
ATOM   8117  C CG  . PRO C 1 302 ? 54.783  -40.232 73.662  1.00 138.27 ? 302 PRO C CG  1 
ATOM   8118  C CD  . PRO C 1 302 ? 55.131  -39.838 72.263  1.00 144.22 ? 302 PRO C CD  1 
ATOM   8119  N N   . THR C 1 303 ? 51.998  -37.994 71.331  1.00 136.16 ? 303 THR C N   1 
ATOM   8120  C CA  . THR C 1 303 ? 51.057  -36.919 71.043  1.00 132.12 ? 303 THR C CA  1 
ATOM   8121  C C   . THR C 1 303 ? 50.082  -37.272 69.930  1.00 128.49 ? 303 THR C C   1 
ATOM   8122  O O   . THR C 1 303 ? 49.158  -36.495 69.670  1.00 123.93 ? 303 THR C O   1 
ATOM   8123  C CB  . THR C 1 303 ? 51.806  -35.635 70.670  1.00 131.96 ? 303 THR C CB  1 
ATOM   8124  O OG1 . THR C 1 303 ? 52.666  -35.885 69.552  1.00 137.47 ? 303 THR C OG1 1 
ATOM   8125  C CG2 . THR C 1 303 ? 52.629  -35.132 71.848  1.00 129.40 ? 303 THR C CG2 1 
ATOM   8126  N N   . ALA C 1 304 ? 50.258  -38.417 69.280  1.00 126.68 ? 304 ALA C N   1 
ATOM   8127  C CA  . ALA C 1 304 ? 49.379  -38.834 68.200  1.00 124.29 ? 304 ALA C CA  1 
ATOM   8128  C C   . ALA C 1 304 ? 48.159  -39.550 68.761  1.00 122.30 ? 304 ALA C C   1 
ATOM   8129  O O   . ALA C 1 304 ? 48.257  -40.303 69.734  1.00 124.88 ? 304 ALA C O   1 
ATOM   8130  C CB  . ALA C 1 304 ? 50.123  -39.752 67.229  1.00 128.72 ? 304 ALA C CB  1 
ATOM   8131  N N   . LYS C 1 305 ? 47.007  -39.309 68.141  1.00 117.81 ? 305 LYS C N   1 
ATOM   8132  C CA  . LYS C 1 305 ? 45.758  -39.969 68.506  1.00 118.00 ? 305 LYS C CA  1 
ATOM   8133  C C   . LYS C 1 305 ? 45.443  -41.006 67.437  1.00 117.20 ? 305 LYS C C   1 
ATOM   8134  O O   . LYS C 1 305 ? 45.083  -40.655 66.307  1.00 117.52 ? 305 LYS C O   1 
ATOM   8135  C CB  . LYS C 1 305 ? 44.614  -38.969 68.652  1.00 118.26 ? 305 LYS C CB  1 
ATOM   8136  C CG  . LYS C 1 305 ? 43.305  -39.612 69.089  1.00 119.50 ? 305 LYS C CG  1 
ATOM   8137  C CD  . LYS C 1 305 ? 42.200  -38.586 69.275  1.00 120.54 ? 305 LYS C CD  1 
ATOM   8138  C CE  . LYS C 1 305 ? 42.315  -37.876 70.611  1.00 131.78 ? 305 LYS C CE  1 
ATOM   8139  N NZ  . LYS C 1 305 ? 41.165  -36.959 70.851  1.00 134.95 ? 305 LYS C NZ  1 
ATOM   8140  N N   . ILE C 1 306 ? 45.579  -42.276 67.795  1.00 120.46 ? 306 ILE C N   1 
ATOM   8141  C CA  . ILE C 1 306 ? 45.326  -43.387 66.887  1.00 120.35 ? 306 ILE C CA  1 
ATOM   8142  C C   . ILE C 1 306 ? 43.896  -43.847 67.149  1.00 125.22 ? 306 ILE C C   1 
ATOM   8143  O O   . ILE C 1 306 ? 43.633  -44.600 68.090  1.00 131.50 ? 306 ILE C O   1 
ATOM   8144  C CB  . ILE C 1 306 ? 46.340  -44.515 67.085  1.00 123.60 ? 306 ILE C CB  1 
ATOM   8145  C CG1 . ILE C 1 306 ? 47.734  -43.933 67.334  1.00 125.12 ? 306 ILE C CG1 1 
ATOM   8146  C CG2 . ILE C 1 306 ? 46.389  -45.400 65.863  1.00 129.07 ? 306 ILE C CG2 1 
ATOM   8147  C CD1 . ILE C 1 306 ? 48.302  -43.160 66.162  1.00 123.55 ? 306 ILE C CD1 1 
ATOM   8148  N N   . GLY C 1 307 ? 42.965  -43.388 66.315  1.00 121.19 ? 307 GLY C N   1 
ATOM   8149  C CA  . GLY C 1 307 ? 41.555  -43.627 66.523  1.00 120.19 ? 307 GLY C CA  1 
ATOM   8150  C C   . GLY C 1 307 ? 41.110  -45.046 66.236  1.00 124.47 ? 307 GLY C C   1 
ATOM   8151  O O   . GLY C 1 307 ? 41.898  -45.995 66.291  1.00 131.02 ? 307 GLY C O   1 
ATOM   8152  N N   . PRO C 1 308 ? 39.827  -45.216 65.925  1.00 120.49 ? 308 PRO C N   1 
ATOM   8153  C CA  . PRO C 1 308 ? 39.288  -46.565 65.737  1.00 125.39 ? 308 PRO C CA  1 
ATOM   8154  C C   . PRO C 1 308 ? 39.577  -47.134 64.357  1.00 122.68 ? 308 PRO C C   1 
ATOM   8155  O O   . PRO C 1 308 ? 39.706  -46.412 63.366  1.00 121.18 ? 308 PRO C O   1 
ATOM   8156  C CB  . PRO C 1 308 ? 37.781  -46.364 65.938  1.00 116.67 ? 308 PRO C CB  1 
ATOM   8157  C CG  . PRO C 1 308 ? 37.540  -44.961 65.486  1.00 110.80 ? 308 PRO C CG  1 
ATOM   8158  C CD  . PRO C 1 308 ? 38.777  -44.184 65.868  1.00 114.79 ? 308 PRO C CD  1 
ATOM   8159  N N   . ASN C 1 309 ? 39.671  -48.465 64.316  1.00 128.04 ? 309 ASN C N   1 
ATOM   8160  C CA  . ASN C 1 309 ? 39.784  -49.242 63.080  1.00 129.02 ? 309 ASN C CA  1 
ATOM   8161  C C   . ASN C 1 309 ? 41.003  -48.811 62.256  1.00 129.59 ? 309 ASN C C   1 
ATOM   8162  O O   . ASN C 1 309 ? 40.888  -48.331 61.128  1.00 127.81 ? 309 ASN C O   1 
ATOM   8163  C CB  . ASN C 1 309 ? 38.488  -49.142 62.262  1.00 126.98 ? 309 ASN C CB  1 
ATOM   8164  C CG  . ASN C 1 309 ? 38.497  -50.037 61.038  1.00 135.98 ? 309 ASN C CG  1 
ATOM   8165  O OD1 . ASN C 1 309 ? 39.287  -50.976 60.948  1.00 142.94 ? 309 ASN C OD1 1 
ATOM   8166  N ND2 . ASN C 1 309 ? 37.612  -49.753 60.089  1.00 139.56 ? 309 ASN C ND2 1 
ATOM   8167  N N   . VAL C 1 310 ? 42.184  -48.984 62.846  1.00 132.62 ? 310 VAL C N   1 
ATOM   8168  C CA  . VAL C 1 310 ? 43.444  -48.666 62.182  1.00 136.38 ? 310 VAL C CA  1 
ATOM   8169  C C   . VAL C 1 310 ? 44.430  -49.806 62.411  1.00 150.59 ? 310 VAL C C   1 
ATOM   8170  O O   . VAL C 1 310 ? 44.603  -50.268 63.545  1.00 154.18 ? 310 VAL C O   1 
ATOM   8171  C CB  . VAL C 1 310 ? 44.019  -47.325 62.675  1.00 131.23 ? 310 VAL C CB  1 
ATOM   8172  C CG1 . VAL C 1 310 ? 43.950  -47.245 64.183  1.00 133.37 ? 310 VAL C CG1 1 
ATOM   8173  C CG2 . VAL C 1 310 ? 45.447  -47.133 62.175  1.00 140.18 ? 310 VAL C CG2 1 
ATOM   8174  N N   . SER C 1 311 ? 45.066  -50.262 61.331  1.00 176.66 ? 311 SER C N   1 
ATOM   8175  C CA  . SER C 1 311 ? 45.990  -51.397 61.357  1.00 176.97 ? 311 SER C CA  1 
ATOM   8176  C C   . SER C 1 311 ? 47.344  -50.947 60.809  1.00 176.57 ? 311 SER C C   1 
ATOM   8177  O O   . SER C 1 311 ? 47.504  -50.785 59.594  1.00 174.48 ? 311 SER C O   1 
ATOM   8178  C CB  . SER C 1 311 ? 45.430  -52.567 60.553  1.00 182.13 ? 311 SER C CB  1 
ATOM   8179  O OG  . SER C 1 311 ? 44.088  -52.835 60.918  1.00 185.01 ? 311 SER C OG  1 
ATOM   8180  N N   . ILE C 1 312 ? 48.314  -50.744 61.703  1.00 182.86 ? 312 ILE C N   1 
ATOM   8181  C CA  . ILE C 1 312 ? 49.639  -50.251 61.341  1.00 181.13 ? 312 ILE C CA  1 
ATOM   8182  C C   . ILE C 1 312 ? 50.588  -51.429 61.158  1.00 180.92 ? 312 ILE C C   1 
ATOM   8183  O O   . ILE C 1 312 ? 50.597  -52.367 61.967  1.00 182.14 ? 312 ILE C O   1 
ATOM   8184  C CB  . ILE C 1 312 ? 50.169  -49.276 62.407  1.00 181.02 ? 312 ILE C CB  1 
ATOM   8185  C CG1 . ILE C 1 312 ? 49.013  -48.474 63.007  1.00 182.04 ? 312 ILE C CG1 1 
ATOM   8186  C CG2 . ILE C 1 312 ? 51.183  -48.326 61.797  1.00 179.12 ? 312 ILE C CG2 1 
ATOM   8187  C CD1 . ILE C 1 312 ? 49.448  -47.461 64.041  1.00 182.10 ? 312 ILE C CD1 1 
ATOM   8188  N N   . SER C 1 313 ? 51.390  -51.380 60.094  1.00 158.56 ? 313 SER C N   1 
ATOM   8189  C CA  . SER C 1 313 ? 52.317  -52.439 59.729  1.00 146.27 ? 313 SER C CA  1 
ATOM   8190  C C   . SER C 1 313 ? 53.711  -52.144 60.281  1.00 141.91 ? 313 SER C C   1 
ATOM   8191  O O   . SER C 1 313 ? 53.924  -51.178 61.015  1.00 145.58 ? 313 SER C O   1 
ATOM   8192  C CB  . SER C 1 313 ? 52.335  -52.618 58.210  1.00 140.80 ? 313 SER C CB  1 
ATOM   8193  O OG  . SER C 1 313 ? 51.063  -53.012 57.731  1.00 148.15 ? 313 SER C OG  1 
ATOM   8194  N N   . ALA C 1 314 ? 54.681  -52.969 59.896  1.00 133.23 ? 314 ALA C N   1 
ATOM   8195  C CA  . ALA C 1 314 ? 56.024  -52.911 60.453  1.00 124.37 ? 314 ALA C CA  1 
ATOM   8196  C C   . ALA C 1 314 ? 56.866  -51.811 59.810  1.00 126.13 ? 314 ALA C C   1 
ATOM   8197  O O   . ALA C 1 314 ? 56.633  -51.388 58.675  1.00 131.51 ? 314 ALA C O   1 
ATOM   8198  C CB  . ALA C 1 314 ? 56.731  -54.256 60.281  1.00 121.52 ? 314 ALA C CB  1 
ATOM   8199  N N   . ASN C 1 315 ? 57.864  -51.353 60.571  1.00 125.58 ? 315 ASN C N   1 
ATOM   8200  C CA  . ASN C 1 315 ? 58.897  -50.434 60.085  1.00 126.33 ? 315 ASN C CA  1 
ATOM   8201  C C   . ASN C 1 315 ? 58.294  -49.154 59.506  1.00 133.65 ? 315 ASN C C   1 
ATOM   8202  O O   . ASN C 1 315 ? 58.645  -48.716 58.409  1.00 136.04 ? 315 ASN C O   1 
ATOM   8203  C CB  . ASN C 1 315 ? 59.803  -51.123 59.058  1.00 122.84 ? 315 ASN C CB  1 
ATOM   8204  C CG  . ASN C 1 315 ? 60.718  -52.163 59.684  1.00 124.95 ? 315 ASN C CG  1 
ATOM   8205  O OD1 . ASN C 1 315 ? 60.387  -53.348 59.743  1.00 125.01 ? 315 ASN C OD1 1 
ATOM   8206  N ND2 . ASN C 1 315 ? 61.882  -51.722 60.148  1.00 125.17 ? 315 ASN C ND2 1 
ATOM   8207  N N   . VAL C 1 316 ? 57.385  -48.544 60.261  1.00 146.71 ? 316 VAL C N   1 
ATOM   8208  C CA  . VAL C 1 316 ? 56.746  -47.292 59.875  1.00 156.48 ? 316 VAL C CA  1 
ATOM   8209  C C   . VAL C 1 316 ? 57.027  -46.244 60.946  1.00 170.49 ? 316 VAL C C   1 
ATOM   8210  O O   . VAL C 1 316 ? 57.051  -46.551 62.143  1.00 164.12 ? 316 VAL C O   1 
ATOM   8211  C CB  . VAL C 1 316 ? 55.229  -47.481 59.656  1.00 153.86 ? 316 VAL C CB  1 
ATOM   8212  C CG1 . VAL C 1 316 ? 54.579  -48.024 60.901  1.00 154.16 ? 316 VAL C CG1 1 
ATOM   8213  C CG2 . VAL C 1 316 ? 54.564  -46.181 59.233  1.00 161.44 ? 316 VAL C CG2 1 
ATOM   8214  N N   . ARG C 1 317 ? 57.263  -45.010 60.505  1.00 209.75 ? 317 ARG C N   1 
ATOM   8215  C CA  . ARG C 1 317 ? 57.589  -43.888 61.380  1.00 209.90 ? 317 ARG C CA  1 
ATOM   8216  C C   . ARG C 1 317 ? 56.356  -42.994 61.484  1.00 211.02 ? 317 ARG C C   1 
ATOM   8217  O O   . ARG C 1 317 ? 55.978  -42.334 60.509  1.00 210.13 ? 317 ARG C O   1 
ATOM   8218  C CB  . ARG C 1 317 ? 58.793  -43.123 60.835  1.00 208.52 ? 317 ARG C CB  1 
ATOM   8219  C CG  . ARG C 1 317 ? 60.083  -43.933 60.847  1.00 209.59 ? 317 ARG C CG  1 
ATOM   8220  C CD  . ARG C 1 317 ? 61.298  -43.036 60.747  1.00 217.50 ? 317 ARG C CD  1 
ATOM   8221  N NE  . ARG C 1 317 ? 61.309  -42.295 59.488  1.00 217.96 ? 317 ARG C NE  1 
ATOM   8222  C CZ  . ARG C 1 317 ? 62.033  -42.636 58.428  1.00 216.63 ? 317 ARG C CZ  1 
ATOM   8223  N NH1 . ARG C 1 317 ? 62.809  -43.709 58.474  1.00 226.93 ? 317 ARG C NH1 1 
ATOM   8224  N NH2 . ARG C 1 317 ? 61.984  -41.904 57.323  1.00 205.89 ? 317 ARG C NH2 1 
ATOM   8225  N N   . VAL C 1 318 ? 55.728  -42.977 62.662  1.00 192.30 ? 318 VAL C N   1 
ATOM   8226  C CA  . VAL C 1 318 ? 54.517  -42.199 62.914  1.00 188.37 ? 318 VAL C CA  1 
ATOM   8227  C C   . VAL C 1 318 ? 54.893  -40.874 63.566  1.00 196.37 ? 318 VAL C C   1 
ATOM   8228  O O   . VAL C 1 318 ? 55.599  -40.851 64.581  1.00 189.73 ? 318 VAL C O   1 
ATOM   8229  C CB  . VAL C 1 318 ? 53.527  -42.982 63.792  1.00 177.08 ? 318 VAL C CB  1 
ATOM   8230  C CG1 . VAL C 1 318 ? 52.411  -42.073 64.288  1.00 171.76 ? 318 VAL C CG1 1 
ATOM   8231  C CG2 . VAL C 1 318 ? 52.955  -44.162 63.019  1.00 169.72 ? 318 VAL C CG2 1 
ATOM   8232  N N   . GLY C 1 319 ? 54.420  -39.771 62.979  1.00 236.73 ? 319 GLY C N   1 
ATOM   8233  C CA  . GLY C 1 319 ? 54.712  -38.447 63.477  1.00 236.45 ? 319 GLY C CA  1 
ATOM   8234  C C   . GLY C 1 319 ? 53.864  -38.058 64.673  1.00 237.84 ? 319 GLY C C   1 
ATOM   8235  O O   . GLY C 1 319 ? 53.054  -38.836 65.199  1.00 239.07 ? 319 GLY C O   1 
ATOM   8236  N N   . PRO C 1 320 ? 54.054  -36.818 65.120  1.00 182.15 ? 320 PRO C N   1 
ATOM   8237  C CA  . PRO C 1 320 ? 53.359  -36.312 66.304  1.00 165.13 ? 320 PRO C CA  1 
ATOM   8238  C C   . PRO C 1 320 ? 52.016  -35.683 65.983  1.00 151.09 ? 320 PRO C C   1 
ATOM   8239  O O   . PRO C 1 320 ? 51.805  -35.096 64.919  1.00 148.40 ? 320 PRO C O   1 
ATOM   8240  C CB  . PRO C 1 320 ? 54.318  -35.228 66.807  1.00 166.44 ? 320 PRO C CB  1 
ATOM   8241  C CG  . PRO C 1 320 ? 54.815  -34.643 65.528  1.00 173.07 ? 320 PRO C CG  1 
ATOM   8242  C CD  . PRO C 1 320 ? 54.933  -35.791 64.539  1.00 177.51 ? 320 PRO C CD  1 
ATOM   8243  N N   . GLY C 1 321 ? 51.100  -35.806 66.940  1.00 144.72 ? 321 GLY C N   1 
ATOM   8244  C CA  . GLY C 1 321 ? 49.816  -35.140 66.814  1.00 135.08 ? 321 GLY C CA  1 
ATOM   8245  C C   . GLY C 1 321 ? 49.072  -35.503 65.553  1.00 126.92 ? 321 GLY C C   1 
ATOM   8246  O O   . GLY C 1 321 ? 48.334  -34.673 65.011  1.00 125.03 ? 321 GLY C O   1 
ATOM   8247  N N   . VAL C 1 322 ? 49.250  -36.718 65.070  1.00 129.81 ? 322 VAL C N   1 
ATOM   8248  C CA  . VAL C 1 322 ? 48.603  -37.176 63.852  1.00 125.51 ? 322 VAL C CA  1 
ATOM   8249  C C   . VAL C 1 322 ? 47.369  -37.970 64.238  1.00 118.11 ? 322 VAL C C   1 
ATOM   8250  O O   . VAL C 1 322 ? 47.287  -38.556 65.324  1.00 118.21 ? 322 VAL C O   1 
ATOM   8251  C CB  . VAL C 1 322 ? 49.561  -38.012 62.974  1.00 131.50 ? 322 VAL C CB  1 
ATOM   8252  C CG1 . VAL C 1 322 ? 50.835  -37.233 62.687  1.00 140.47 ? 322 VAL C CG1 1 
ATOM   8253  C CG2 . VAL C 1 322 ? 49.883  -39.334 63.644  1.00 137.50 ? 322 VAL C CG2 1 
ATOM   8254  N N   . ARG C 1 323 ? 46.392  -37.981 63.338  1.00 115.40 ? 323 ARG C N   1 
ATOM   8255  C CA  . ARG C 1 323 ? 45.097  -38.599 63.581  1.00 113.99 ? 323 ARG C CA  1 
ATOM   8256  C C   . ARG C 1 323 ? 44.923  -39.734 62.585  1.00 115.19 ? 323 ARG C C   1 
ATOM   8257  O O   . ARG C 1 323 ? 45.024  -39.519 61.373  1.00 115.50 ? 323 ARG C O   1 
ATOM   8258  C CB  . ARG C 1 323 ? 43.971  -37.572 63.436  1.00 113.82 ? 323 ARG C CB  1 
ATOM   8259  C CG  . ARG C 1 323 ? 42.603  -38.076 63.861  1.00 116.74 ? 323 ARG C CG  1 
ATOM   8260  C CD  . ARG C 1 323 ? 42.428  -37.986 65.369  1.00 120.53 ? 323 ARG C CD  1 
ATOM   8261  N NE  . ARG C 1 323 ? 41.082  -38.368 65.785  1.00 123.72 ? 323 ARG C NE  1 
ATOM   8262  C CZ  . ARG C 1 323 ? 40.771  -39.569 66.258  1.00 122.08 ? 323 ARG C CZ  1 
ATOM   8263  N NH1 . ARG C 1 323 ? 41.719  -40.484 66.384  1.00 117.79 ? 323 ARG C NH1 1 
ATOM   8264  N NH2 . ARG C 1 323 ? 39.524  -39.852 66.613  1.00 123.27 ? 323 ARG C NH2 1 
ATOM   8265  N N   . LEU C 1 324 ? 44.665  -40.937 63.091  1.00 121.12 ? 324 LEU C N   1 
ATOM   8266  C CA  . LEU C 1 324 ? 44.540  -42.125 62.253  1.00 120.57 ? 324 LEU C CA  1 
ATOM   8267  C C   . LEU C 1 324 ? 43.263  -42.847 62.652  1.00 122.11 ? 324 LEU C C   1 
ATOM   8268  O O   . LEU C 1 324 ? 43.204  -43.463 63.720  1.00 125.04 ? 324 LEU C O   1 
ATOM   8269  C CB  . LEU C 1 324 ? 45.757  -43.042 62.401  1.00 123.39 ? 324 LEU C CB  1 
ATOM   8270  C CG  . LEU C 1 324 ? 47.145  -42.432 62.184  1.00 122.36 ? 324 LEU C CG  1 
ATOM   8271  C CD1 . LEU C 1 324 ? 48.239  -43.454 62.461  1.00 127.92 ? 324 LEU C CD1 1 
ATOM   8272  C CD2 . LEU C 1 324 ? 47.280  -41.874 60.775  1.00 119.02 ? 324 LEU C CD2 1 
ATOM   8273  N N   . ILE C 1 325 ? 42.246  -42.776 61.797  1.00 114.01 ? 325 ILE C N   1 
ATOM   8274  C CA  . ILE C 1 325 ? 40.996  -43.494 62.015  1.00 114.35 ? 325 ILE C CA  1 
ATOM   8275  C C   . ILE C 1 325 ? 40.579  -44.143 60.704  1.00 114.04 ? 325 ILE C C   1 
ATOM   8276  O O   . ILE C 1 325 ? 40.791  -43.580 59.623  1.00 112.49 ? 325 ILE C O   1 
ATOM   8277  C CB  . ILE C 1 325 ? 39.875  -42.571 62.545  1.00 111.21 ? 325 ILE C CB  1 
ATOM   8278  C CG1 . ILE C 1 325 ? 39.422  -41.587 61.472  1.00 104.11 ? 325 ILE C CG1 1 
ATOM   8279  C CG2 . ILE C 1 325 ? 40.336  -41.789 63.752  1.00 116.10 ? 325 ILE C CG2 1 
ATOM   8280  C CD1 . ILE C 1 325 ? 38.377  -40.613 61.953  1.00 105.52 ? 325 ILE C CD1 1 
ATOM   8281  N N   . SER C 1 326 ? 40.013  -45.346 60.805  1.00 115.67 ? 326 SER C N   1 
ATOM   8282  C CA  . SER C 1 326 ? 39.371  -46.021 59.678  1.00 116.30 ? 326 SER C CA  1 
ATOM   8283  C C   . SER C 1 326 ? 40.313  -46.145 58.482  1.00 120.65 ? 326 SER C C   1 
ATOM   8284  O O   . SER C 1 326 ? 39.933  -45.901 57.336  1.00 119.65 ? 326 SER C O   1 
ATOM   8285  C CB  . SER C 1 326 ? 38.080  -45.305 59.283  1.00 111.33 ? 326 SER C CB  1 
ATOM   8286  O OG  . SER C 1 326 ? 37.243  -45.114 60.409  1.00 104.06 ? 326 SER C OG  1 
ATOM   8287  N N   . CYS C 1 327 ? 41.558  -46.533 58.749  1.00 126.82 ? 327 CYS C N   1 
ATOM   8288  C CA  . CYS C 1 327 ? 42.563  -46.613 57.699  1.00 126.46 ? 327 CYS C CA  1 
ATOM   8289  C C   . CYS C 1 327 ? 43.544  -47.729 58.025  1.00 132.13 ? 327 CYS C C   1 
ATOM   8290  O O   . CYS C 1 327 ? 43.630  -48.194 59.163  1.00 138.82 ? 327 CYS C O   1 
ATOM   8291  C CB  . CYS C 1 327 ? 43.298  -45.279 57.524  1.00 119.09 ? 327 CYS C CB  1 
ATOM   8292  S SG  . CYS C 1 327 ? 44.097  -44.682 59.026  1.00 125.37 ? 327 CYS C SG  1 
ATOM   8293  N N   . ILE C 1 328 ? 44.284  -48.164 57.006  1.00 132.28 ? 328 ILE C N   1 
ATOM   8294  C CA  . ILE C 1 328 ? 45.339  -49.158 57.168  1.00 140.38 ? 328 ILE C CA  1 
ATOM   8295  C C   . ILE C 1 328 ? 46.602  -48.648 56.489  1.00 140.67 ? 328 ILE C C   1 
ATOM   8296  O O   . ILE C 1 328 ? 46.550  -48.125 55.370  1.00 127.95 ? 328 ILE C O   1 
ATOM   8297  C CB  . ILE C 1 328 ? 44.929  -50.536 56.606  1.00 136.46 ? 328 ILE C CB  1 
ATOM   8298  C CG1 . ILE C 1 328 ? 44.395  -50.413 55.179  1.00 125.19 ? 328 ILE C CG1 1 
ATOM   8299  C CG2 . ILE C 1 328 ? 43.895  -51.195 57.508  1.00 141.79 ? 328 ILE C CG2 1 
ATOM   8300  C CD1 . ILE C 1 328 ? 44.013  -51.744 54.562  1.00 129.93 ? 328 ILE C CD1 1 
ATOM   8301  N N   . ILE C 1 329 ? 47.735  -48.793 57.171  1.00 163.21 ? 329 ILE C N   1 
ATOM   8302  C CA  . ILE C 1 329 ? 49.013  -48.249 56.728  1.00 161.13 ? 329 ILE C CA  1 
ATOM   8303  C C   . ILE C 1 329 ? 49.977  -49.404 56.496  1.00 161.06 ? 329 ILE C C   1 
ATOM   8304  O O   . ILE C 1 329 ? 50.119  -50.285 57.353  1.00 162.29 ? 329 ILE C O   1 
ATOM   8305  C CB  . ILE C 1 329 ? 49.584  -47.250 57.750  1.00 160.82 ? 329 ILE C CB  1 
ATOM   8306  C CG1 . ILE C 1 329 ? 48.602  -46.098 57.971  1.00 161.12 ? 329 ILE C CG1 1 
ATOM   8307  C CG2 . ILE C 1 329 ? 50.929  -46.720 57.287  1.00 158.83 ? 329 ILE C CG2 1 
ATOM   8308  C CD1 . ILE C 1 329 ? 48.996  -45.171 59.095  1.00 161.19 ? 329 ILE C CD1 1 
ATOM   8309  N N   . LEU C 1 330 ? 50.635  -49.398 55.340  1.00 147.22 ? 330 LEU C N   1 
ATOM   8310  C CA  . LEU C 1 330 ? 51.555  -50.457 54.957  1.00 146.13 ? 330 LEU C CA  1 
ATOM   8311  C C   . LEU C 1 330 ? 52.956  -50.156 55.489  1.00 142.58 ? 330 LEU C C   1 
ATOM   8312  O O   . LEU C 1 330 ? 53.163  -49.234 56.281  1.00 143.08 ? 330 LEU C O   1 
ATOM   8313  C CB  . LEU C 1 330 ? 51.535  -50.639 53.440  1.00 150.19 ? 330 LEU C CB  1 
ATOM   8314  C CG  . LEU C 1 330 ? 50.188  -51.087 52.866  1.00 151.36 ? 330 LEU C CG  1 
ATOM   8315  C CD1 . LEU C 1 330 ? 50.268  -51.281 51.360  1.00 157.87 ? 330 LEU C CD1 1 
ATOM   8316  C CD2 . LEU C 1 330 ? 49.714  -52.363 53.547  1.00 162.13 ? 330 LEU C CD2 1 
ATOM   8317  N N   . ASP C 1 331 ? 53.933  -50.950 55.063  1.00 139.87 ? 331 ASP C N   1 
ATOM   8318  C CA  . ASP C 1 331 ? 55.280  -50.867 55.605  1.00 133.18 ? 331 ASP C CA  1 
ATOM   8319  C C   . ASP C 1 331 ? 56.031  -49.668 55.040  1.00 132.23 ? 331 ASP C C   1 
ATOM   8320  O O   . ASP C 1 331 ? 55.745  -49.188 53.938  1.00 136.01 ? 331 ASP C O   1 
ATOM   8321  C CB  . ASP C 1 331 ? 56.060  -52.146 55.297  1.00 134.16 ? 331 ASP C CB  1 
ATOM   8322  C CG  . ASP C 1 331 ? 55.471  -53.369 55.971  1.00 135.27 ? 331 ASP C CG  1 
ATOM   8323  O OD1 . ASP C 1 331 ? 55.040  -54.291 55.250  1.00 138.03 ? 331 ASP C OD1 1 
ATOM   8324  O OD2 . ASP C 1 331 ? 55.410  -53.400 57.217  1.00 137.79 ? 331 ASP C OD2 1 
ATOM   8325  N N   . ASP C 1 332 ? 56.993  -49.179 55.828  1.00 132.41 ? 332 ASP C N   1 
ATOM   8326  C CA  . ASP C 1 332 ? 57.982  -48.191 55.399  1.00 134.71 ? 332 ASP C CA  1 
ATOM   8327  C C   . ASP C 1 332 ? 57.357  -46.840 55.055  1.00 138.07 ? 332 ASP C C   1 
ATOM   8328  O O   . ASP C 1 332 ? 57.921  -46.072 54.272  1.00 137.43 ? 332 ASP C O   1 
ATOM   8329  C CB  . ASP C 1 332 ? 58.808  -48.709 54.218  1.00 130.41 ? 332 ASP C CB  1 
ATOM   8330  C CG  . ASP C 1 332 ? 60.298  -48.540 54.434  1.00 132.51 ? 332 ASP C CG  1 
ATOM   8331  O OD1 . ASP C 1 332 ? 60.698  -47.563 55.102  1.00 136.47 ? 332 ASP C OD1 1 
ATOM   8332  O OD2 . ASP C 1 332 ? 61.072  -49.390 53.943  1.00 129.00 ? 332 ASP C OD2 1 
ATOM   8333  N N   . VAL C 1 333 ? 56.219  -46.519 55.654  1.00 144.38 ? 333 VAL C N   1 
ATOM   8334  C CA  . VAL C 1 333 ? 55.549  -45.245 55.420  1.00 144.95 ? 333 VAL C CA  1 
ATOM   8335  C C   . VAL C 1 333 ? 56.141  -44.199 56.354  1.00 155.73 ? 333 VAL C C   1 
ATOM   8336  O O   . VAL C 1 333 ? 56.529  -44.497 57.489  1.00 163.96 ? 333 VAL C O   1 
ATOM   8337  C CB  . VAL C 1 333 ? 54.023  -45.382 55.612  1.00 141.46 ? 333 VAL C CB  1 
ATOM   8338  C CG1 . VAL C 1 333 ? 53.321  -44.058 55.338  1.00 141.53 ? 333 VAL C CG1 1 
ATOM   8339  C CG2 . VAL C 1 333 ? 53.478  -46.469 54.709  1.00 140.27 ? 333 VAL C CG2 1 
ATOM   8340  N N   . GLU C 1 334 ? 56.228  -42.962 55.872  1.00 154.85 ? 334 GLU C N   1 
ATOM   8341  C CA  . GLU C 1 334 ? 56.749  -41.847 56.656  1.00 157.19 ? 334 GLU C CA  1 
ATOM   8342  C C   . GLU C 1 334 ? 55.633  -40.824 56.832  1.00 151.60 ? 334 GLU C C   1 
ATOM   8343  O O   . GLU C 1 334 ? 55.192  -40.202 55.858  1.00 145.11 ? 334 GLU C O   1 
ATOM   8344  C CB  . GLU C 1 334 ? 57.972  -41.224 55.985  1.00 161.82 ? 334 GLU C CB  1 
ATOM   8345  C CG  . GLU C 1 334 ? 58.590  -40.075 56.767  1.00 165.71 ? 334 GLU C CG  1 
ATOM   8346  C CD  . GLU C 1 334 ? 59.825  -39.507 56.097  1.00 169.94 ? 334 GLU C CD  1 
ATOM   8347  O OE1 . GLU C 1 334 ? 60.305  -40.119 55.120  1.00 175.49 ? 334 GLU C OE1 1 
ATOM   8348  O OE2 . GLU C 1 334 ? 60.321  -38.455 56.552  1.00 166.74 ? 334 GLU C OE2 1 
ATOM   8349  N N   . ILE C 1 335 ? 55.181  -40.652 58.071  1.00 151.28 ? 335 ILE C N   1 
ATOM   8350  C CA  . ILE C 1 335 ? 54.123  -39.707 58.410  1.00 145.38 ? 335 ILE C CA  1 
ATOM   8351  C C   . ILE C 1 335 ? 54.774  -38.503 59.076  1.00 145.06 ? 335 ILE C C   1 
ATOM   8352  O O   . ILE C 1 335 ? 55.439  -38.641 60.109  1.00 151.78 ? 335 ILE C O   1 
ATOM   8353  C CB  . ILE C 1 335 ? 53.070  -40.349 59.327  1.00 149.35 ? 335 ILE C CB  1 
ATOM   8354  C CG1 . ILE C 1 335 ? 52.526  -41.634 58.696  1.00 141.17 ? 335 ILE C CG1 1 
ATOM   8355  C CG2 . ILE C 1 335 ? 51.938  -39.372 59.601  1.00 142.25 ? 335 ILE C CG2 1 
ATOM   8356  C CD1 . ILE C 1 335 ? 51.703  -41.406 57.452  1.00 134.48 ? 335 ILE C CD1 1 
ATOM   8357  N N   . LYS C 1 336 ? 54.587  -37.324 58.492  1.00 134.33 ? 336 LYS C N   1 
ATOM   8358  C CA  . LYS C 1 336 ? 55.262  -36.123 58.961  1.00 132.95 ? 336 LYS C CA  1 
ATOM   8359  C C   . LYS C 1 336 ? 54.380  -35.354 59.947  1.00 136.22 ? 336 LYS C C   1 
ATOM   8360  O O   . LYS C 1 336 ? 53.354  -35.847 60.425  1.00 141.06 ? 336 LYS C O   1 
ATOM   8361  C CB  . LYS C 1 336 ? 55.684  -35.256 57.777  1.00 132.23 ? 336 LYS C CB  1 
ATOM   8362  C CG  . LYS C 1 336 ? 56.917  -35.772 57.051  1.00 133.59 ? 336 LYS C CG  1 
ATOM   8363  C CD  . LYS C 1 336 ? 57.419  -34.766 56.031  1.00 130.74 ? 336 LYS C CD  1 
ATOM   8364  C CE  . LYS C 1 336 ? 58.716  -35.236 55.392  1.00 131.31 ? 336 LYS C CE  1 
ATOM   8365  N NZ  . LYS C 1 336 ? 59.250  -34.247 54.415  1.00 129.04 ? 336 LYS C NZ  1 
ATOM   8366  N N   . GLU C 1 337 ? 54.798  -34.128 60.260  1.00 134.98 ? 337 GLU C N   1 
ATOM   8367  C CA  . GLU C 1 337 ? 54.182  -33.333 61.316  1.00 136.00 ? 337 GLU C CA  1 
ATOM   8368  C C   . GLU C 1 337 ? 52.703  -33.070 61.049  1.00 137.09 ? 337 GLU C C   1 
ATOM   8369  O O   . GLU C 1 337 ? 52.335  -32.543 59.996  1.00 136.10 ? 337 GLU C O   1 
ATOM   8370  C CB  . GLU C 1 337 ? 54.923  -32.002 61.446  1.00 138.96 ? 337 GLU C CB  1 
ATOM   8371  C CG  . GLU C 1 337 ? 56.437  -32.127 61.387  1.00 144.16 ? 337 GLU C CG  1 
ATOM   8372  C CD  . GLU C 1 337 ? 57.039  -32.542 62.710  1.00 164.99 ? 337 GLU C CD  1 
ATOM   8373  O OE1 . GLU C 1 337 ? 56.288  -32.647 63.700  1.00 168.91 ? 337 GLU C OE1 1 
ATOM   8374  O OE2 . GLU C 1 337 ? 58.264  -32.777 62.761  1.00 172.55 ? 337 GLU C OE2 1 
ATOM   8375  N N   . ASN C 1 338 ? 51.864  -33.416 62.025  1.00 141.52 ? 338 ASN C N   1 
ATOM   8376  C CA  . ASN C 1 338 ? 50.447  -33.047 62.050  1.00 140.58 ? 338 ASN C CA  1 
ATOM   8377  C C   . ASN C 1 338 ? 49.728  -33.452 60.762  1.00 136.96 ? 338 ASN C C   1 
ATOM   8378  O O   . ASN C 1 338 ? 49.159  -32.627 60.045  1.00 133.61 ? 338 ASN C O   1 
ATOM   8379  C CB  . ASN C 1 338 ? 50.292  -31.549 62.321  1.00 142.10 ? 338 ASN C CB  1 
ATOM   8380  C CG  . ASN C 1 338 ? 50.896  -31.133 63.645  1.00 138.99 ? 338 ASN C CG  1 
ATOM   8381  O OD1 . ASN C 1 338 ? 50.803  -31.855 64.636  1.00 137.91 ? 338 ASN C OD1 1 
ATOM   8382  N ND2 . ASN C 1 338 ? 51.522  -29.962 63.669  1.00 139.83 ? 338 ASN C ND2 1 
ATOM   8383  N N   . ALA C 1 339 ? 49.764  -34.747 60.476  1.00 127.63 ? 339 ALA C N   1 
ATOM   8384  C CA  . ALA C 1 339 ? 49.074  -35.313 59.328  1.00 119.15 ? 339 ALA C CA  1 
ATOM   8385  C C   . ALA C 1 339 ? 47.752  -35.934 59.765  1.00 113.01 ? 339 ALA C C   1 
ATOM   8386  O O   . ALA C 1 339 ? 47.574  -36.326 60.920  1.00 118.97 ? 339 ALA C O   1 
ATOM   8387  C CB  . ALA C 1 339 ? 49.949  -36.358 58.630  1.00 121.94 ? 339 ALA C CB  1 
ATOM   8388  N N   . VAL C 1 340 ? 46.818  -36.016 58.819  1.00 106.40 ? 340 VAL C N   1 
ATOM   8389  C CA  . VAL C 1 340 ? 45.481  -36.539 59.071  1.00 103.08 ? 340 VAL C CA  1 
ATOM   8390  C C   . VAL C 1 340 ? 45.155  -37.565 57.994  1.00 103.60 ? 340 VAL C C   1 
ATOM   8391  O O   . VAL C 1 340 ? 45.323  -37.291 56.801  1.00 106.63 ? 340 VAL C O   1 
ATOM   8392  C CB  . VAL C 1 340 ? 44.424  -35.419 59.092  1.00 101.45 ? 340 VAL C CB  1 
ATOM   8393  C CG1 . VAL C 1 340 ? 43.055  -35.990 59.423  1.00 102.24 ? 340 VAL C CG1 1 
ATOM   8394  C CG2 . VAL C 1 340 ? 44.808  -34.331 60.087  1.00 107.01 ? 340 VAL C CG2 1 
ATOM   8395  N N   . VAL C 1 341 ? 44.691  -38.741 58.414  1.00 101.14 ? 341 VAL C N   1 
ATOM   8396  C CA  . VAL C 1 341 ? 44.378  -39.845 57.512  1.00 100.62 ? 341 VAL C CA  1 
ATOM   8397  C C   . VAL C 1 341 ? 43.011  -40.403 57.886  1.00 103.41 ? 341 VAL C C   1 
ATOM   8398  O O   . VAL C 1 341 ? 42.839  -40.945 58.983  1.00 105.18 ? 341 VAL C O   1 
ATOM   8399  C CB  . VAL C 1 341 ? 45.443  -40.952 57.566  1.00 104.67 ? 341 VAL C CB  1 
ATOM   8400  C CG1 . VAL C 1 341 ? 45.038  -42.109 56.675  1.00 107.17 ? 341 VAL C CG1 1 
ATOM   8401  C CG2 . VAL C 1 341 ? 46.805  -40.408 57.155  1.00 99.24  ? 341 VAL C CG2 1 
ATOM   8402  N N   . ILE C 1 342 ? 42.044  -40.277 56.976  1.00 106.50 ? 342 ILE C N   1 
ATOM   8403  C CA  . ILE C 1 342 ? 40.675  -40.740 57.190  1.00 103.13 ? 342 ILE C CA  1 
ATOM   8404  C C   . ILE C 1 342 ? 40.266  -41.597 55.999  1.00 103.83 ? 342 ILE C C   1 
ATOM   8405  O O   . ILE C 1 342 ? 40.393  -41.162 54.850  1.00 104.97 ? 342 ILE C O   1 
ATOM   8406  C CB  . ILE C 1 342 ? 39.686  -39.568 57.353  1.00 99.69  ? 342 ILE C CB  1 
ATOM   8407  C CG1 . ILE C 1 342 ? 40.299  -38.427 58.170  1.00 99.15  ? 342 ILE C CG1 1 
ATOM   8408  C CG2 . ILE C 1 342 ? 38.395  -40.051 57.996  1.00 98.57  ? 342 ILE C CG2 1 
ATOM   8409  C CD1 . ILE C 1 342 ? 40.543  -38.759 59.620  1.00 105.06 ? 342 ILE C CD1 1 
ATOM   8410  N N   . ASN C 1 343 ? 39.779  -42.808 56.268  1.00 105.80 ? 343 ASN C N   1 
ATOM   8411  C CA  . ASN C 1 343 ? 39.241  -43.697 55.234  1.00 105.76 ? 343 ASN C CA  1 
ATOM   8412  C C   . ASN C 1 343 ? 40.207  -43.832 54.056  1.00 106.46 ? 343 ASN C C   1 
ATOM   8413  O O   . ASN C 1 343 ? 39.863  -43.589 52.899  1.00 108.96 ? 343 ASN C O   1 
ATOM   8414  C CB  . ASN C 1 343 ? 37.869  -43.218 54.755  1.00 105.53 ? 343 ASN C CB  1 
ATOM   8415  C CG  . ASN C 1 343 ? 36.816  -43.287 55.837  1.00 107.05 ? 343 ASN C CG  1 
ATOM   8416  O OD1 . ASN C 1 343 ? 36.753  -44.256 56.592  1.00 108.84 ? 343 ASN C OD1 1 
ATOM   8417  N ND2 . ASN C 1 343 ? 35.977  -42.260 55.917  1.00 109.55 ? 343 ASN C ND2 1 
ATOM   8418  N N   . SER C 1 344 ? 41.432  -44.243 54.371  1.00 105.85 ? 344 SER C N   1 
ATOM   8419  C CA  . SER C 1 344 ? 42.508  -44.261 53.392  1.00 103.44 ? 344 SER C CA  1 
ATOM   8420  C C   . SER C 1 344 ? 43.267  -45.577 53.482  1.00 104.71 ? 344 SER C C   1 
ATOM   8421  O O   . SER C 1 344 ? 43.146  -46.328 54.453  1.00 115.43 ? 344 SER C O   1 
ATOM   8422  C CB  . SER C 1 344 ? 43.465  -43.078 53.597  1.00 102.10 ? 344 SER C CB  1 
ATOM   8423  O OG  . SER C 1 344 ? 42.756  -41.867 53.804  1.00 103.21 ? 344 SER C OG  1 
ATOM   8424  N N   . ILE C 1 345 ? 44.056  -45.849 52.441  1.00 100.36 ? 345 ILE C N   1 
ATOM   8425  C CA  . ILE C 1 345 ? 44.965  -46.991 52.390  1.00 105.52 ? 345 ILE C CA  1 
ATOM   8426  C C   . ILE C 1 345 ? 46.290  -46.476 51.838  1.00 106.75 ? 345 ILE C C   1 
ATOM   8427  O O   . ILE C 1 345 ? 46.410  -46.225 50.633  1.00 109.49 ? 345 ILE C O   1 
ATOM   8428  C CB  . ILE C 1 345 ? 44.434  -48.141 51.522  1.00 104.76 ? 345 ILE C CB  1 
ATOM   8429  C CG1 . ILE C 1 345 ? 43.070  -48.614 52.029  1.00 105.91 ? 345 ILE C CG1 1 
ATOM   8430  C CG2 . ILE C 1 345 ? 45.446  -49.296 51.502  1.00 111.46 ? 345 ILE C CG2 1 
ATOM   8431  C CD1 . ILE C 1 345 ? 42.501  -49.781 51.258  1.00 107.27 ? 345 ILE C CD1 1 
ATOM   8432  N N   . ILE C 1 346 ? 47.279  -46.324 52.710  1.00 111.66 ? 346 ILE C N   1 
ATOM   8433  C CA  . ILE C 1 346 ? 48.580  -45.782 52.338  1.00 114.02 ? 346 ILE C CA  1 
ATOM   8434  C C   . ILE C 1 346 ? 49.473  -46.930 51.886  1.00 120.26 ? 346 ILE C C   1 
ATOM   8435  O O   . ILE C 1 346 ? 49.621  -47.929 52.599  1.00 127.31 ? 346 ILE C O   1 
ATOM   8436  C CB  . ILE C 1 346 ? 49.210  -45.021 53.516  1.00 120.21 ? 346 ILE C CB  1 
ATOM   8437  C CG1 . ILE C 1 346 ? 48.223  -43.992 54.068  1.00 112.62 ? 346 ILE C CG1 1 
ATOM   8438  C CG2 . ILE C 1 346 ? 50.490  -44.339 53.085  1.00 120.87 ? 346 ILE C CG2 1 
ATOM   8439  C CD1 . ILE C 1 346 ? 47.797  -42.957 53.055  1.00 109.65 ? 346 ILE C CD1 1 
ATOM   8440  N N   . GLY C 1 347 ? 50.073  -46.788 50.709  1.00 121.81 ? 347 GLY C N   1 
ATOM   8441  C CA  . GLY C 1 347 ? 50.868  -47.846 50.131  1.00 137.83 ? 347 GLY C CA  1 
ATOM   8442  C C   . GLY C 1 347 ? 52.221  -48.007 50.811  1.00 145.71 ? 347 GLY C C   1 
ATOM   8443  O O   . GLY C 1 347 ? 52.491  -47.488 51.895  1.00 141.76 ? 347 GLY C O   1 
ATOM   8444  N N   . TRP C 1 348 ? 53.090  -48.752 50.133  1.00 168.90 ? 348 TRP C N   1 
ATOM   8445  C CA  . TRP C 1 348 ? 54.414  -49.055 50.655  1.00 167.43 ? 348 TRP C CA  1 
ATOM   8446  C C   . TRP C 1 348 ? 55.367  -47.897 50.395  1.00 165.30 ? 348 TRP C C   1 
ATOM   8447  O O   . TRP C 1 348 ? 55.299  -47.240 49.352  1.00 165.49 ? 348 TRP C O   1 
ATOM   8448  C CB  . TRP C 1 348 ? 54.965  -50.327 50.009  1.00 170.34 ? 348 TRP C CB  1 
ATOM   8449  C CG  . TRP C 1 348 ? 53.951  -51.414 49.824  1.00 174.26 ? 348 TRP C CG  1 
ATOM   8450  C CD1 . TRP C 1 348 ? 53.049  -51.526 48.805  1.00 176.88 ? 348 TRP C CD1 1 
ATOM   8451  C CD2 . TRP C 1 348 ? 53.754  -52.563 50.659  1.00 175.76 ? 348 TRP C CD2 1 
ATOM   8452  N NE1 . TRP C 1 348 ? 52.293  -52.661 48.961  1.00 178.85 ? 348 TRP C NE1 1 
ATOM   8453  C CE2 . TRP C 1 348 ? 52.708  -53.317 50.090  1.00 180.29 ? 348 TRP C CE2 1 
ATOM   8454  C CE3 . TRP C 1 348 ? 54.356  -53.024 51.833  1.00 173.47 ? 348 TRP C CE3 1 
ATOM   8455  C CZ2 . TRP C 1 348 ? 52.250  -54.505 50.657  1.00 183.84 ? 348 TRP C CZ2 1 
ATOM   8456  C CZ3 . TRP C 1 348 ? 53.900  -54.205 52.393  1.00 175.75 ? 348 TRP C CZ3 1 
ATOM   8457  C CH2 . TRP C 1 348 ? 52.857  -54.930 51.805  1.00 179.85 ? 348 TRP C CH2 1 
ATOM   8458  N N   . LYS C 1 349 ? 56.262  -47.653 51.353  1.00 141.38 ? 349 LYS C N   1 
ATOM   8459  C CA  . LYS C 1 349 ? 57.308  -46.636 51.248  1.00 137.93 ? 349 LYS C CA  1 
ATOM   8460  C C   . LYS C 1 349 ? 56.746  -45.250 50.942  1.00 137.93 ? 349 LYS C C   1 
ATOM   8461  O O   . LYS C 1 349 ? 57.468  -44.379 50.444  1.00 132.56 ? 349 LYS C O   1 
ATOM   8462  C CB  . LYS C 1 349 ? 58.357  -47.022 50.195  1.00 133.58 ? 349 LYS C CB  1 
ATOM   8463  C CG  . LYS C 1 349 ? 59.319  -48.120 50.638  1.00 130.51 ? 349 LYS C CG  1 
ATOM   8464  C CD  . LYS C 1 349 ? 58.669  -49.496 50.564  1.00 131.68 ? 349 LYS C CD  1 
ATOM   8465  C CE  . LYS C 1 349 ? 59.640  -50.600 50.943  1.00 126.13 ? 349 LYS C CE  1 
ATOM   8466  N NZ  . LYS C 1 349 ? 59.008  -51.946 50.839  1.00 118.13 ? 349 LYS C NZ  1 
ATOM   8467  N N   . SER C 1 350 ? 55.467  -45.032 51.232  1.00 140.79 ? 350 SER C N   1 
ATOM   8468  C CA  . SER C 1 350 ? 54.842  -43.749 50.960  1.00 139.57 ? 350 SER C CA  1 
ATOM   8469  C C   . SER C 1 350 ? 55.307  -42.702 51.964  1.00 137.72 ? 350 SER C C   1 
ATOM   8470  O O   . SER C 1 350 ? 55.696  -43.015 53.092  1.00 140.20 ? 350 SER C O   1 
ATOM   8471  C CB  . SER C 1 350 ? 53.321  -43.876 51.004  1.00 137.24 ? 350 SER C CB  1 
ATOM   8472  O OG  . SER C 1 350 ? 52.870  -44.913 50.154  1.00 140.38 ? 350 SER C OG  1 
ATOM   8473  N N   . SER C 1 351 ? 55.263  -41.442 51.540  1.00 138.38 ? 351 SER C N   1 
ATOM   8474  C CA  . SER C 1 351 ? 55.700  -40.323 52.365  1.00 140.07 ? 351 SER C CA  1 
ATOM   8475  C C   . SER C 1 351 ? 54.569  -39.312 52.449  1.00 138.40 ? 351 SER C C   1 
ATOM   8476  O O   . SER C 1 351 ? 54.146  -38.764 51.427  1.00 143.02 ? 351 SER C O   1 
ATOM   8477  C CB  . SER C 1 351 ? 56.964  -39.673 51.796  1.00 141.18 ? 351 SER C CB  1 
ATOM   8478  O OG  . SER C 1 351 ? 57.436  -38.648 52.654  1.00 137.18 ? 351 SER C OG  1 
ATOM   8479  N N   . ILE C 1 352 ? 54.078  -39.075 53.660  1.00 132.96 ? 352 ILE C N   1 
ATOM   8480  C CA  . ILE C 1 352 ? 52.987  -38.139 53.904  1.00 132.35 ? 352 ILE C CA  1 
ATOM   8481  C C   . ILE C 1 352 ? 53.598  -36.886 54.516  1.00 130.89 ? 352 ILE C C   1 
ATOM   8482  O O   . ILE C 1 352 ? 54.109  -36.920 55.640  1.00 130.73 ? 352 ILE C O   1 
ATOM   8483  C CB  . ILE C 1 352 ? 51.912  -38.747 54.814  1.00 130.47 ? 352 ILE C CB  1 
ATOM   8484  C CG1 . ILE C 1 352 ? 51.277  -39.971 54.147  1.00 125.92 ? 352 ILE C CG1 1 
ATOM   8485  C CG2 . ILE C 1 352 ? 50.854  -37.713 55.156  1.00 128.68 ? 352 ILE C CG2 1 
ATOM   8486  C CD1 . ILE C 1 352 ? 50.684  -39.689 52.786  1.00 124.87 ? 352 ILE C CD1 1 
ATOM   8487  N N   . GLY C 1 353 ? 53.542  -35.780 53.780  1.00 130.55 ? 353 GLY C N   1 
ATOM   8488  C CA  . GLY C 1 353 ? 54.157  -34.548 54.222  1.00 127.82 ? 353 GLY C CA  1 
ATOM   8489  C C   . GLY C 1 353 ? 53.485  -33.964 55.448  1.00 127.14 ? 353 GLY C C   1 
ATOM   8490  O O   . GLY C 1 353 ? 52.431  -34.410 55.906  1.00 125.20 ? 353 GLY C O   1 
ATOM   8491  N N   . ARG C 1 354 ? 54.122  -32.933 55.995  1.00 127.91 ? 354 ARG C N   1 
ATOM   8492  C CA  . ARG C 1 354 ? 53.624  -32.307 57.209  1.00 129.02 ? 354 ARG C CA  1 
ATOM   8493  C C   . ARG C 1 354 ? 52.419  -31.425 56.910  1.00 127.69 ? 354 ARG C C   1 
ATOM   8494  O O   . ARG C 1 354 ? 52.370  -30.732 55.890  1.00 127.93 ? 354 ARG C O   1 
ATOM   8495  C CB  . ARG C 1 354 ? 54.726  -31.493 57.887  1.00 129.24 ? 354 ARG C CB  1 
ATOM   8496  C CG  . ARG C 1 354 ? 55.426  -30.496 56.987  1.00 129.86 ? 354 ARG C CG  1 
ATOM   8497  C CD  . ARG C 1 354 ? 56.587  -29.831 57.709  1.00 135.15 ? 354 ARG C CD  1 
ATOM   8498  N NE  . ARG C 1 354 ? 57.555  -30.801 58.217  1.00 130.55 ? 354 ARG C NE  1 
ATOM   8499  C CZ  . ARG C 1 354 ? 58.613  -31.228 57.535  1.00 128.73 ? 354 ARG C CZ  1 
ATOM   8500  N NH1 . ARG C 1 354 ? 58.842  -30.776 56.310  1.00 134.20 ? 354 ARG C NH1 1 
ATOM   8501  N NH2 . ARG C 1 354 ? 59.442  -32.109 58.076  1.00 122.75 ? 354 ARG C NH2 1 
ATOM   8502  N N   . TRP C 1 355 ? 51.444  -31.461 57.820  1.00 130.07 ? 355 TRP C N   1 
ATOM   8503  C CA  . TRP C 1 355 ? 50.177  -30.743 57.677  1.00 129.28 ? 355 TRP C CA  1 
ATOM   8504  C C   . TRP C 1 355 ? 49.429  -31.138 56.408  1.00 129.59 ? 355 TRP C C   1 
ATOM   8505  O O   . TRP C 1 355 ? 48.613  -30.371 55.892  1.00 129.17 ? 355 TRP C O   1 
ATOM   8506  C CB  . TRP C 1 355 ? 50.394  -29.230 57.723  1.00 130.48 ? 355 TRP C CB  1 
ATOM   8507  C CG  . TRP C 1 355 ? 50.714  -28.756 59.092  1.00 135.63 ? 355 TRP C CG  1 
ATOM   8508  C CD1 . TRP C 1 355 ? 49.885  -28.764 60.173  1.00 136.27 ? 355 TRP C CD1 1 
ATOM   8509  C CD2 . TRP C 1 355 ? 51.960  -28.217 59.544  1.00 136.79 ? 355 TRP C CD2 1 
ATOM   8510  N NE1 . TRP C 1 355 ? 50.533  -28.256 61.270  1.00 137.60 ? 355 TRP C NE1 1 
ATOM   8511  C CE2 . TRP C 1 355 ? 51.810  -27.913 60.911  1.00 137.38 ? 355 TRP C CE2 1 
ATOM   8512  C CE3 . TRP C 1 355 ? 53.188  -27.958 58.926  1.00 133.41 ? 355 TRP C CE3 1 
ATOM   8513  C CZ2 . TRP C 1 355 ? 52.839  -27.362 61.671  1.00 133.59 ? 355 TRP C CZ2 1 
ATOM   8514  C CZ3 . TRP C 1 355 ? 54.208  -27.413 59.682  1.00 134.18 ? 355 TRP C CZ3 1 
ATOM   8515  C CH2 . TRP C 1 355 ? 54.028  -27.120 61.039  1.00 133.81 ? 355 TRP C CH2 1 
ATOM   8516  N N   . SER C 1 356 ? 49.686  -32.338 55.905  1.00 123.60 ? 356 SER C N   1 
ATOM   8517  C CA  . SER C 1 356 ? 48.960  -32.871 54.765  1.00 120.51 ? 356 SER C CA  1 
ATOM   8518  C C   . SER C 1 356 ? 47.847  -33.785 55.257  1.00 114.43 ? 356 SER C C   1 
ATOM   8519  O O   . SER C 1 356 ? 47.957  -34.411 56.313  1.00 115.38 ? 356 SER C O   1 
ATOM   8520  C CB  . SER C 1 356 ? 49.895  -33.639 53.828  1.00 122.68 ? 356 SER C CB  1 
ATOM   8521  O OG  . SER C 1 356 ? 50.661  -34.591 54.543  1.00 120.81 ? 356 SER C OG  1 
ATOM   8522  N N   . ARG C 1 357 ? 46.775  -33.861 54.478  1.00 110.86 ? 357 ARG C N   1 
ATOM   8523  C CA  . ARG C 1 357 ? 45.571  -34.578 54.870  1.00 103.30 ? 357 ARG C CA  1 
ATOM   8524  C C   . ARG C 1 357 ? 45.174  -35.531 53.756  1.00 105.23 ? 357 ARG C C   1 
ATOM   8525  O O   . ARG C 1 357 ? 45.190  -35.165 52.577  1.00 112.02 ? 357 ARG C O   1 
ATOM   8526  C CB  . ARG C 1 357 ? 44.409  -33.623 55.169  1.00 104.35 ? 357 ARG C CB  1 
ATOM   8527  C CG  . ARG C 1 357 ? 43.204  -34.279 55.842  1.00 102.85 ? 357 ARG C CG  1 
ATOM   8528  C CD  . ARG C 1 357 ? 42.047  -33.297 55.945  1.00 102.19 ? 357 ARG C CD  1 
ATOM   8529  N NE  . ARG C 1 357 ? 40.900  -33.802 56.693  1.00 99.81  ? 357 ARG C NE  1 
ATOM   8530  C CZ  . ARG C 1 357 ? 40.660  -33.522 57.970  1.00 102.69 ? 357 ARG C CZ  1 
ATOM   8531  N NH1 . ARG C 1 357 ? 41.491  -32.739 58.647  1.00 103.33 ? 357 ARG C NH1 1 
ATOM   8532  N NH2 . ARG C 1 357 ? 39.589  -34.020 58.571  1.00 107.95 ? 357 ARG C NH2 1 
ATOM   8533  N N   . VAL C 1 358 ? 44.820  -36.756 54.137  1.00 103.39 ? 358 VAL C N   1 
ATOM   8534  C CA  . VAL C 1 358 ? 44.389  -37.792 53.205  1.00 103.16 ? 358 VAL C CA  1 
ATOM   8535  C C   . VAL C 1 358 ? 43.091  -38.359 53.767  1.00 101.75 ? 358 VAL C C   1 
ATOM   8536  O O   . VAL C 1 358 ? 43.117  -39.188 54.683  1.00 102.94 ? 358 VAL C O   1 
ATOM   8537  C CB  . VAL C 1 358 ? 45.441  -38.893 53.024  1.00 100.01 ? 358 VAL C CB  1 
ATOM   8538  C CG1 . VAL C 1 358 ? 44.979  -39.912 51.993  1.00 107.81 ? 358 VAL C CG1 1 
ATOM   8539  C CG2 . VAL C 1 358 ? 46.790  -38.297 52.626  1.00 100.40 ? 358 VAL C CG2 1 
ATOM   8540  N N   . GLN C 1 359 ? 41.955  -37.918 53.228  1.00 99.32  ? 359 GLN C N   1 
ATOM   8541  C CA  . GLN C 1 359 ? 40.660  -38.351 53.732  1.00 100.45 ? 359 GLN C CA  1 
ATOM   8542  C C   . GLN C 1 359 ? 39.782  -38.839 52.589  1.00 101.48 ? 359 GLN C C   1 
ATOM   8543  O O   . GLN C 1 359 ? 40.109  -38.694 51.408  1.00 102.95 ? 359 GLN C O   1 
ATOM   8544  C CB  . GLN C 1 359 ? 39.935  -37.235 54.495  1.00 101.29 ? 359 GLN C CB  1 
ATOM   8545  C CG  . GLN C 1 359 ? 39.490  -36.076 53.624  1.00 98.53  ? 359 GLN C CG  1 
ATOM   8546  C CD  . GLN C 1 359 ? 38.355  -35.293 54.254  1.00 103.09 ? 359 GLN C CD  1 
ATOM   8547  O OE1 . GLN C 1 359 ? 38.241  -35.219 55.478  1.00 105.30 ? 359 GLN C OE1 1 
ATOM   8548  N NE2 . GLN C 1 359 ? 37.504  -34.708 53.418  1.00 106.08 ? 359 GLN C NE2 1 
ATOM   8549  N N   . ALA C 1 360 ? 38.649  -39.421 52.969  1.00 101.79 ? 360 ALA C N   1 
ATOM   8550  C CA  . ALA C 1 360 ? 37.649  -39.896 52.024  1.00 103.64 ? 360 ALA C CA  1 
ATOM   8551  C C   . ALA C 1 360 ? 36.324  -39.998 52.765  1.00 109.51 ? 360 ALA C C   1 
ATOM   8552  O O   . ALA C 1 360 ? 36.262  -39.842 53.986  1.00 109.19 ? 360 ALA C O   1 
ATOM   8553  C CB  . ALA C 1 360 ? 38.046  -41.238 51.403  1.00 103.90 ? 360 ALA C CB  1 
ATOM   8554  N N   . SER C 1 361 ? 35.257  -40.255 52.008  1.00 110.35 ? 361 SER C N   1 
ATOM   8555  C CA  . SER C 1 361 ? 33.931  -40.304 52.614  1.00 110.30 ? 361 SER C CA  1 
ATOM   8556  C C   . SER C 1 361 ? 33.759  -41.549 53.475  1.00 113.19 ? 361 SER C C   1 
ATOM   8557  O O   . SER C 1 361 ? 33.148  -41.490 54.548  1.00 113.74 ? 361 SER C O   1 
ATOM   8558  C CB  . SER C 1 361 ? 32.857  -40.245 51.529  1.00 108.60 ? 361 SER C CB  1 
ATOM   8559  O OG  . SER C 1 361 ? 33.446  -40.154 50.245  1.00 107.71 ? 361 SER C OG  1 
ATOM   8560  N N   . GLY C 1 362 ? 34.284  -42.681 53.023  1.00 119.91 ? 362 GLY C N   1 
ATOM   8561  C CA  . GLY C 1 362 ? 34.075  -43.945 53.690  1.00 123.61 ? 362 GLY C CA  1 
ATOM   8562  C C   . GLY C 1 362 ? 32.986  -44.797 53.087  1.00 128.86 ? 362 GLY C C   1 
ATOM   8563  O O   . GLY C 1 362 ? 32.661  -45.848 53.652  1.00 132.26 ? 362 GLY C O   1 
ATOM   8564  N N   . ASP C 1 363 ? 32.414  -44.380 51.961  1.00 127.75 ? 363 ASP C N   1 
ATOM   8565  C CA  . ASP C 1 363 ? 31.350  -45.128 51.303  1.00 130.32 ? 363 ASP C CA  1 
ATOM   8566  C C   . ASP C 1 363 ? 31.935  -46.349 50.607  1.00 136.25 ? 363 ASP C C   1 
ATOM   8567  O O   . ASP C 1 363 ? 32.612  -46.225 49.582  1.00 135.99 ? 363 ASP C O   1 
ATOM   8568  C CB  . ASP C 1 363 ? 30.620  -44.230 50.311  1.00 126.29 ? 363 ASP C CB  1 
ATOM   8569  C CG  . ASP C 1 363 ? 29.314  -44.829 49.843  1.00 129.98 ? 363 ASP C CG  1 
ATOM   8570  O OD1 . ASP C 1 363 ? 28.769  -45.694 50.560  1.00 131.97 ? 363 ASP C OD1 1 
ATOM   8571  O OD2 . ASP C 1 363 ? 28.833  -44.438 48.758  1.00 130.92 ? 363 ASP C OD2 1 
ATOM   8572  N N   . TYR C 1 364 ? 31.680  -47.533 51.165  1.00 150.43 ? 364 TYR C N   1 
ATOM   8573  C CA  . TYR C 1 364 ? 32.156  -48.777 50.570  1.00 151.30 ? 364 TYR C CA  1 
ATOM   8574  C C   . TYR C 1 364 ? 31.397  -49.166 49.306  1.00 150.75 ? 364 TYR C C   1 
ATOM   8575  O O   . TYR C 1 364 ? 31.737  -50.185 48.695  1.00 151.56 ? 364 TYR C O   1 
ATOM   8576  C CB  . TYR C 1 364 ? 32.079  -49.906 51.600  1.00 155.07 ? 364 TYR C CB  1 
ATOM   8577  C CG  . TYR C 1 364 ? 32.852  -49.615 52.869  1.00 160.78 ? 364 TYR C CG  1 
ATOM   8578  C CD1 . TYR C 1 364 ? 34.232  -49.772 52.913  1.00 162.53 ? 364 TYR C CD1 1 
ATOM   8579  C CD2 . TYR C 1 364 ? 32.207  -49.166 54.015  1.00 161.38 ? 364 TYR C CD2 1 
ATOM   8580  C CE1 . TYR C 1 364 ? 34.947  -49.501 54.065  1.00 158.57 ? 364 TYR C CE1 1 
ATOM   8581  C CE2 . TYR C 1 364 ? 32.915  -48.892 55.173  1.00 160.85 ? 364 TYR C CE2 1 
ATOM   8582  C CZ  . TYR C 1 364 ? 34.284  -49.062 55.192  1.00 158.86 ? 364 TYR C CZ  1 
ATOM   8583  O OH  . TYR C 1 364 ? 34.998  -48.792 56.337  1.00 159.35 ? 364 TYR C OH  1 
ATOM   8584  N N   . ASN C 1 365 ? 30.388  -48.395 48.903  1.00 139.66 ? 365 ASN C N   1 
ATOM   8585  C CA  . ASN C 1 365 ? 29.707  -48.608 47.631  1.00 136.72 ? 365 ASN C CA  1 
ATOM   8586  C C   . ASN C 1 365 ? 30.214  -47.701 46.521  1.00 134.47 ? 365 ASN C C   1 
ATOM   8587  O O   . ASN C 1 365 ? 30.154  -48.082 45.348  1.00 133.89 ? 365 ASN C O   1 
ATOM   8588  C CB  . ASN C 1 365 ? 28.196  -48.400 47.794  1.00 135.77 ? 365 ASN C CB  1 
ATOM   8589  C CG  . ASN C 1 365 ? 27.659  -49.005 49.078  1.00 140.03 ? 365 ASN C CG  1 
ATOM   8590  O OD1 . ASN C 1 365 ? 28.070  -50.091 49.486  1.00 144.07 ? 365 ASN C OD1 1 
ATOM   8591  N ND2 . ASN C 1 365 ? 26.732  -48.303 49.721  1.00 138.89 ? 365 ASN C ND2 1 
ATOM   8592  N N   . ASP C 1 366 ? 30.712  -46.515 46.861  1.00 138.68 ? 366 ASP C N   1 
ATOM   8593  C CA  . ASP C 1 366 ? 31.273  -45.607 45.872  1.00 138.89 ? 366 ASP C CA  1 
ATOM   8594  C C   . ASP C 1 366 ? 32.716  -45.986 45.564  1.00 142.14 ? 366 ASP C C   1 
ATOM   8595  O O   . ASP C 1 366 ? 33.457  -46.434 46.444  1.00 144.06 ? 366 ASP C O   1 
ATOM   8596  C CB  . ASP C 1 366 ? 31.200  -44.165 46.376  1.00 137.83 ? 366 ASP C CB  1 
ATOM   8597  C CG  . ASP C 1 366 ? 31.688  -43.158 45.351  1.00 138.02 ? 366 ASP C CG  1 
ATOM   8598  O OD1 . ASP C 1 366 ? 31.791  -43.514 44.159  1.00 139.43 ? 366 ASP C OD1 1 
ATOM   8599  O OD2 . ASP C 1 366 ? 31.969  -42.006 45.744  1.00 136.07 ? 366 ASP C OD2 1 
ATOM   8600  N N   . ARG C 1 367 ? 33.110  -45.811 44.299  1.00 130.93 ? 367 ARG C N   1 
ATOM   8601  C CA  . ARG C 1 367 ? 34.472  -46.152 43.898  1.00 124.77 ? 367 ARG C CA  1 
ATOM   8602  C C   . ARG C 1 367 ? 35.494  -45.272 44.609  1.00 118.28 ? 367 ARG C C   1 
ATOM   8603  O O   . ARG C 1 367 ? 36.528  -45.762 45.076  1.00 114.35 ? 367 ARG C O   1 
ATOM   8604  C CB  . ARG C 1 367 ? 34.622  -46.034 42.380  1.00 126.52 ? 367 ARG C CB  1 
ATOM   8605  C CG  . ARG C 1 367 ? 35.834  -46.770 41.820  1.00 123.63 ? 367 ARG C CG  1 
ATOM   8606  C CD  . ARG C 1 367 ? 35.934  -46.630 40.307  1.00 119.13 ? 367 ARG C CD  1 
ATOM   8607  N NE  . ARG C 1 367 ? 37.029  -47.425 39.756  1.00 117.77 ? 367 ARG C NE  1 
ATOM   8608  C CZ  . ARG C 1 367 ? 37.401  -47.407 38.480  1.00 115.52 ? 367 ARG C CZ  1 
ATOM   8609  N NH1 . ARG C 1 367 ? 36.766  -46.631 37.612  1.00 116.19 ? 367 ARG C NH1 1 
ATOM   8610  N NH2 . ARG C 1 367 ? 38.410  -48.165 38.070  1.00 106.66 ? 367 ARG C NH2 1 
ATOM   8611  N N   . LEU C 1 368 ? 35.222  -43.970 44.703  1.00 120.08 ? 368 LEU C N   1 
ATOM   8612  C CA  . LEU C 1 368 ? 36.110  -43.034 45.377  1.00 118.32 ? 368 LEU C CA  1 
ATOM   8613  C C   . LEU C 1 368 ? 35.751  -42.830 46.845  1.00 120.87 ? 368 LEU C C   1 
ATOM   8614  O O   . LEU C 1 368 ? 36.144  -41.818 47.437  1.00 118.38 ? 368 LEU C O   1 
ATOM   8615  C CB  . LEU C 1 368 ? 36.113  -41.693 44.640  1.00 115.96 ? 368 LEU C CB  1 
ATOM   8616  C CG  . LEU C 1 368 ? 36.583  -41.752 43.184  1.00 108.36 ? 368 LEU C CG  1 
ATOM   8617  C CD1 . LEU C 1 368 ? 36.660  -40.358 42.583  1.00 107.09 ? 368 LEU C CD1 1 
ATOM   8618  C CD2 . LEU C 1 368 ? 37.928  -42.460 43.079  1.00 106.79 ? 368 LEU C CD2 1 
ATOM   8619  N N   . GLY C 1 369 ? 35.011  -43.764 47.447  1.00 124.43 ? 369 GLY C N   1 
ATOM   8620  C CA  . GLY C 1 369 ? 34.681  -43.651 48.857  1.00 122.76 ? 369 GLY C CA  1 
ATOM   8621  C C   . GLY C 1 369 ? 35.846  -43.922 49.785  1.00 118.32 ? 369 GLY C C   1 
ATOM   8622  O O   . GLY C 1 369 ? 35.812  -43.496 50.944  1.00 115.71 ? 369 GLY C O   1 
ATOM   8623  N N   . ILE C 1 370 ? 36.871  -44.625 49.306  1.00 117.71 ? 370 ILE C N   1 
ATOM   8624  C CA  . ILE C 1 370 ? 38.072  -44.935 50.078  1.00 119.01 ? 370 ILE C CA  1 
ATOM   8625  C C   . ILE C 1 370 ? 39.278  -44.535 49.237  1.00 116.66 ? 370 ILE C C   1 
ATOM   8626  O O   . ILE C 1 370 ? 39.584  -45.191 48.232  1.00 115.68 ? 370 ILE C O   1 
ATOM   8627  C CB  . ILE C 1 370 ? 38.149  -46.418 50.467  1.00 121.86 ? 370 ILE C CB  1 
ATOM   8628  C CG1 . ILE C 1 370 ? 36.929  -46.828 51.297  1.00 124.15 ? 370 ILE C CG1 1 
ATOM   8629  C CG2 . ILE C 1 370 ? 39.429  -46.698 51.239  1.00 116.42 ? 370 ILE C CG2 1 
ATOM   8630  C CD1 . ILE C 1 370 ? 36.803  -46.079 52.604  1.00 124.65 ? 370 ILE C CD1 1 
ATOM   8631  N N   . THR C 1 371 ? 39.962  -43.467 49.640  1.00 112.92 ? 371 THR C N   1 
ATOM   8632  C CA  . THR C 1 371 ? 41.136  -43.012 48.905  1.00 112.78 ? 371 THR C CA  1 
ATOM   8633  C C   . THR C 1 371 ? 42.297  -43.987 49.083  1.00 108.04 ? 371 THR C C   1 
ATOM   8634  O O   . THR C 1 371 ? 42.602  -44.415 50.200  1.00 107.51 ? 371 THR C O   1 
ATOM   8635  C CB  . THR C 1 371 ? 41.539  -41.607 49.358  1.00 108.87 ? 371 THR C CB  1 
ATOM   8636  O OG1 . THR C 1 371 ? 42.829  -41.278 48.822  1.00 107.00 ? 371 THR C OG1 1 
ATOM   8637  C CG2 . THR C 1 371 ? 41.581  -41.515 50.869  1.00 106.14 ? 371 THR C CG2 1 
ATOM   8638  N N   . ILE C 1 372 ? 42.933  -44.352 47.971  1.00 105.89 ? 372 ILE C N   1 
ATOM   8639  C CA  . ILE C 1 372 ? 43.985  -45.361 47.951  1.00 101.90 ? 372 ILE C CA  1 
ATOM   8640  C C   . ILE C 1 372 ? 45.241  -44.746 47.350  1.00 103.15 ? 372 ILE C C   1 
ATOM   8641  O O   . ILE C 1 372 ? 45.191  -44.150 46.268  1.00 105.76 ? 372 ILE C O   1 
ATOM   8642  C CB  . ILE C 1 372 ? 43.557  -46.612 47.163  1.00 105.61 ? 372 ILE C CB  1 
ATOM   8643  C CG1 . ILE C 1 372 ? 42.282  -47.208 47.768  1.00 112.17 ? 372 ILE C CG1 1 
ATOM   8644  C CG2 . ILE C 1 372 ? 44.676  -47.645 47.154  1.00 113.94 ? 372 ILE C CG2 1 
ATOM   8645  C CD1 . ILE C 1 372 ? 41.626  -48.265 46.912  1.00 121.51 ? 372 ILE C CD1 1 
ATOM   8646  N N   . LEU C 1 373 ? 46.360  -44.890 48.054  1.00 106.59 ? 373 LEU C N   1 
ATOM   8647  C CA  . LEU C 1 373 ? 47.648  -44.361 47.631  1.00 110.82 ? 373 LEU C CA  1 
ATOM   8648  C C   . LEU C 1 373 ? 48.569  -45.497 47.205  1.00 116.07 ? 373 LEU C C   1 
ATOM   8649  O O   . LEU C 1 373 ? 48.647  -46.530 47.876  1.00 120.12 ? 373 LEU C O   1 
ATOM   8650  C CB  . LEU C 1 373 ? 48.300  -43.548 48.753  1.00 113.79 ? 373 LEU C CB  1 
ATOM   8651  C CG  . LEU C 1 373 ? 48.144  -42.028 48.658  1.00 113.81 ? 373 LEU C CG  1 
ATOM   8652  C CD1 . LEU C 1 373 ? 46.675  -41.630 48.628  1.00 110.58 ? 373 LEU C CD1 1 
ATOM   8653  C CD2 . LEU C 1 373 ? 48.869  -41.346 49.809  1.00 119.31 ? 373 LEU C CD2 1 
ATOM   8654  N N   . GLY C 1 374 ? 49.258  -45.304 46.085  1.00 124.53 ? 374 GLY C N   1 
ATOM   8655  C CA  . GLY C 1 374 ? 50.122  -46.328 45.541  1.00 141.99 ? 374 GLY C CA  1 
ATOM   8656  C C   . GLY C 1 374 ? 51.402  -46.497 46.348  1.00 155.76 ? 374 GLY C C   1 
ATOM   8657  O O   . GLY C 1 374 ? 51.563  -45.991 47.459  1.00 150.97 ? 374 GLY C O   1 
ATOM   8658  N N   . GLU C 1 375 ? 52.330  -47.245 45.756  1.00 206.14 ? 375 GLU C N   1 
ATOM   8659  C CA  . GLU C 1 375 ? 53.620  -47.508 46.382  1.00 206.43 ? 375 GLU C CA  1 
ATOM   8660  C C   . GLU C 1 375 ? 54.569  -46.332 46.183  1.00 205.20 ? 375 GLU C C   1 
ATOM   8661  O O   . GLU C 1 375 ? 54.728  -45.836 45.063  1.00 203.35 ? 375 GLU C O   1 
ATOM   8662  C CB  . GLU C 1 375 ? 54.241  -48.782 45.810  1.00 206.46 ? 375 GLU C CB  1 
ATOM   8663  C CG  . GLU C 1 375 ? 55.638  -49.078 46.332  1.00 206.70 ? 375 GLU C CG  1 
ATOM   8664  C CD  . GLU C 1 375 ? 56.349  -50.149 45.528  1.00 208.79 ? 375 GLU C CD  1 
ATOM   8665  O OE1 . GLU C 1 375 ? 55.784  -50.608 44.513  1.00 208.30 ? 375 GLU C OE1 1 
ATOM   8666  O OE2 . GLU C 1 375 ? 57.473  -50.533 45.913  1.00 210.04 ? 375 GLU C OE2 1 
ATOM   8667  N N   . ALA C 1 376 ? 55.210  -45.901 47.273  1.00 166.43 ? 376 ALA C N   1 
ATOM   8668  C CA  . ALA C 1 376 ? 56.194  -44.817 47.243  1.00 156.36 ? 376 ALA C CA  1 
ATOM   8669  C C   . ALA C 1 376 ? 55.591  -43.541 46.656  1.00 150.46 ? 376 ALA C C   1 
ATOM   8670  O O   . ALA C 1 376 ? 56.178  -42.883 45.793  1.00 147.65 ? 376 ALA C O   1 
ATOM   8671  C CB  . ALA C 1 376 ? 57.454  -45.234 46.478  1.00 156.82 ? 376 ALA C CB  1 
ATOM   8672  N N   . VAL C 1 377 ? 54.402  -43.196 47.134  1.00 147.18 ? 377 VAL C N   1 
ATOM   8673  C CA  . VAL C 1 377 ? 53.755  -41.940 46.778  1.00 145.26 ? 377 VAL C CA  1 
ATOM   8674  C C   . VAL C 1 377 ? 54.105  -40.899 47.831  1.00 148.13 ? 377 VAL C C   1 
ATOM   8675  O O   . VAL C 1 377 ? 53.985  -41.151 49.037  1.00 144.00 ? 377 VAL C O   1 
ATOM   8676  C CB  . VAL C 1 377 ? 52.232  -42.118 46.650  1.00 137.27 ? 377 VAL C CB  1 
ATOM   8677  C CG1 . VAL C 1 377 ? 51.682  -42.881 47.839  1.00 136.10 ? 377 VAL C CG1 1 
ATOM   8678  C CG2 . VAL C 1 377 ? 51.544  -40.765 46.517  1.00 134.36 ? 377 VAL C CG2 1 
ATOM   8679  N N   . THR C 1 378 ? 54.557  -39.735 47.380  1.00 180.49 ? 378 THR C N   1 
ATOM   8680  C CA  . THR C 1 378 ? 55.034  -38.678 48.266  1.00 180.48 ? 378 THR C CA  1 
ATOM   8681  C C   . THR C 1 378 ? 54.021  -37.538 48.237  1.00 180.52 ? 378 THR C C   1 
ATOM   8682  O O   . THR C 1 378 ? 53.996  -36.739 47.296  1.00 179.28 ? 378 THR C O   1 
ATOM   8683  C CB  . THR C 1 378 ? 56.422  -38.196 47.850  1.00 179.47 ? 378 THR C CB  1 
ATOM   8684  O OG1 . THR C 1 378 ? 56.349  -37.584 46.556  1.00 178.75 ? 378 THR C OG1 1 
ATOM   8685  C CG2 . THR C 1 378 ? 57.397  -39.359 47.799  1.00 179.43 ? 378 THR C CG2 1 
ATOM   8686  N N   . VAL C 1 379 ? 53.189  -37.469 49.271  1.00 154.91 ? 379 VAL C N   1 
ATOM   8687  C CA  . VAL C 1 379 ? 52.290  -36.336 49.454  1.00 148.49 ? 379 VAL C CA  1 
ATOM   8688  C C   . VAL C 1 379 ? 53.075  -35.241 50.161  1.00 144.52 ? 379 VAL C C   1 
ATOM   8689  O O   . VAL C 1 379 ? 53.527  -35.423 51.295  1.00 144.54 ? 379 VAL C O   1 
ATOM   8690  C CB  . VAL C 1 379 ? 51.044  -36.734 50.259  1.00 144.15 ? 379 VAL C CB  1 
ATOM   8691  C CG1 . VAL C 1 379 ? 50.163  -35.517 50.515  1.00 140.84 ? 379 VAL C CG1 1 
ATOM   8692  C CG2 . VAL C 1 379 ? 50.265  -37.820 49.534  1.00 144.95 ? 379 VAL C CG2 1 
ATOM   8693  N N   . GLU C 1 380 ? 53.250  -34.107 49.488  1.00 138.64 ? 380 GLU C N   1 
ATOM   8694  C CA  . GLU C 1 380 ? 54.068  -33.039 50.037  1.00 131.11 ? 380 GLU C CA  1 
ATOM   8695  C C   . GLU C 1 380 ? 53.341  -32.356 51.193  1.00 126.28 ? 380 GLU C C   1 
ATOM   8696  O O   . GLU C 1 380 ? 52.191  -32.665 51.521  1.00 127.18 ? 380 GLU C O   1 
ATOM   8697  C CB  . GLU C 1 380 ? 54.432  -32.029 48.951  1.00 131.09 ? 380 GLU C CB  1 
ATOM   8698  C CG  . GLU C 1 380 ? 55.830  -31.454 49.096  1.00 125.53 ? 380 GLU C CG  1 
ATOM   8699  C CD  . GLU C 1 380 ? 56.372  -30.897 47.797  1.00 127.44 ? 380 GLU C CD  1 
ATOM   8700  O OE1 . GLU C 1 380 ? 55.738  -31.113 46.742  1.00 133.02 ? 380 GLU C OE1 1 
ATOM   8701  O OE2 . GLU C 1 380 ? 57.434  -30.241 47.832  1.00 120.19 ? 380 GLU C OE2 1 
ATOM   8702  N N   . ASP C 1 381 ? 54.040  -31.418 51.825  1.00 125.25 ? 381 ASP C N   1 
ATOM   8703  C CA  . ASP C 1 381 ? 53.488  -30.705 52.965  1.00 126.23 ? 381 ASP C CA  1 
ATOM   8704  C C   . ASP C 1 381 ? 52.252  -29.912 52.557  1.00 125.22 ? 381 ASP C C   1 
ATOM   8705  O O   . ASP C 1 381 ? 52.203  -29.321 51.475  1.00 126.94 ? 381 ASP C O   1 
ATOM   8706  C CB  . ASP C 1 381 ? 54.543  -29.768 53.549  1.00 127.34 ? 381 ASP C CB  1 
ATOM   8707  C CG  . ASP C 1 381 ? 55.910  -30.416 53.636  1.00 127.04 ? 381 ASP C CG  1 
ATOM   8708  O OD1 . ASP C 1 381 ? 55.982  -31.616 53.977  1.00 126.05 ? 381 ASP C OD1 1 
ATOM   8709  O OD2 . ASP C 1 381 ? 56.913  -29.725 53.362  1.00 130.49 ? 381 ASP C OD2 1 
ATOM   8710  N N   . GLU C 1 382 ? 51.245  -29.917 53.431  1.00 127.67 ? 382 GLU C N   1 
ATOM   8711  C CA  . GLU C 1 382 ? 49.969  -29.223 53.273  1.00 128.94 ? 382 GLU C CA  1 
ATOM   8712  C C   . GLU C 1 382 ? 49.116  -29.754 52.124  1.00 129.28 ? 382 GLU C C   1 
ATOM   8713  O O   . GLU C 1 382 ? 47.989  -29.276 51.945  1.00 129.83 ? 382 GLU C O   1 
ATOM   8714  C CB  . GLU C 1 382 ? 50.160  -27.712 53.081  1.00 132.76 ? 382 GLU C CB  1 
ATOM   8715  C CG  . GLU C 1 382 ? 50.644  -26.990 54.325  1.00 134.38 ? 382 GLU C CG  1 
ATOM   8716  C CD  . GLU C 1 382 ? 50.519  -25.485 54.210  1.00 137.85 ? 382 GLU C CD  1 
ATOM   8717  O OE1 . GLU C 1 382 ? 49.725  -25.014 53.368  1.00 140.74 ? 382 GLU C OE1 1 
ATOM   8718  O OE2 . GLU C 1 382 ? 51.214  -24.773 54.965  1.00 136.20 ? 382 GLU C OE2 1 
ATOM   8719  N N   . VAL C 1 383 ? 49.602  -30.720 51.344  1.00 127.35 ? 383 VAL C N   1 
ATOM   8720  C CA  . VAL C 1 383 ? 48.835  -31.222 50.211  1.00 125.92 ? 383 VAL C CA  1 
ATOM   8721  C C   . VAL C 1 383 ? 47.675  -32.074 50.711  1.00 127.51 ? 383 VAL C C   1 
ATOM   8722  O O   . VAL C 1 383 ? 47.833  -32.906 51.614  1.00 124.53 ? 383 VAL C O   1 
ATOM   8723  C CB  . VAL C 1 383 ? 49.748  -32.016 49.261  1.00 128.48 ? 383 VAL C CB  1 
ATOM   8724  C CG1 . VAL C 1 383 ? 48.953  -32.561 48.084  1.00 129.88 ? 383 VAL C CG1 1 
ATOM   8725  C CG2 . VAL C 1 383 ? 50.894  -31.145 48.778  1.00 131.35 ? 383 VAL C CG2 1 
ATOM   8726  N N   . ALA C 1 384 ? 46.503  -31.881 50.115  1.00 142.04 ? 384 ALA C N   1 
ATOM   8727  C CA  . ALA C 1 384 ? 45.288  -32.567 50.528  1.00 143.05 ? 384 ALA C CA  1 
ATOM   8728  C C   . ALA C 1 384 ? 44.829  -33.522 49.434  1.00 142.37 ? 384 ALA C C   1 
ATOM   8729  O O   . ALA C 1 384 ? 44.867  -33.188 48.246  1.00 140.86 ? 384 ALA C O   1 
ATOM   8730  C CB  . ALA C 1 384 ? 44.173  -31.567 50.851  1.00 143.65 ? 384 ALA C CB  1 
ATOM   8731  N N   . VAL C 1 385 ? 44.394  -34.711 49.845  1.00 119.81 ? 385 VAL C N   1 
ATOM   8732  C CA  . VAL C 1 385 ? 43.903  -35.745 48.939  1.00 110.83 ? 385 VAL C CA  1 
ATOM   8733  C C   . VAL C 1 385 ? 42.561  -36.216 49.481  1.00 106.02 ? 385 VAL C C   1 
ATOM   8734  O O   . VAL C 1 385 ? 42.511  -36.905 50.507  1.00 105.56 ? 385 VAL C O   1 
ATOM   8735  C CB  . VAL C 1 385 ? 44.881  -36.921 48.808  1.00 110.35 ? 385 VAL C CB  1 
ATOM   8736  C CG1 . VAL C 1 385 ? 44.300  -37.997 47.902  1.00 112.01 ? 385 VAL C CG1 1 
ATOM   8737  C CG2 . VAL C 1 385 ? 46.225  -36.442 48.278  1.00 116.06 ? 385 VAL C CG2 1 
ATOM   8738  N N   . ILE C 1 386 ? 41.480  -35.847 48.803  1.00 107.96 ? 386 ILE C N   1 
ATOM   8739  C CA  . ILE C 1 386 ? 40.125  -36.162 49.242  1.00 104.18 ? 386 ILE C CA  1 
ATOM   8740  C C   . ILE C 1 386 ? 39.526  -37.139 48.239  1.00 107.48 ? 386 ILE C C   1 
ATOM   8741  O O   . ILE C 1 386 ? 39.252  -36.772 47.090  1.00 111.16 ? 386 ILE C O   1 
ATOM   8742  C CB  . ILE C 1 386 ? 39.259  -34.901 49.372  1.00 101.10 ? 386 ILE C CB  1 
ATOM   8743  C CG1 . ILE C 1 386 ? 39.815  -33.963 50.450  1.00 101.99 ? 386 ILE C CG1 1 
ATOM   8744  C CG2 . ILE C 1 386 ? 37.814  -35.278 49.677  1.00 101.90 ? 386 ILE C CG2 1 
ATOM   8745  C CD1 . ILE C 1 386 ? 40.795  -32.921 49.928  1.00 103.98 ? 386 ILE C CD1 1 
ATOM   8746  N N   . GLY C 1 387 ? 39.314  -38.381 48.675  1.00 109.54 ? 387 GLY C N   1 
ATOM   8747  C CA  . GLY C 1 387 ? 38.649  -39.394 47.876  1.00 114.80 ? 387 GLY C CA  1 
ATOM   8748  C C   . GLY C 1 387 ? 39.193  -39.578 46.474  1.00 119.95 ? 387 GLY C C   1 
ATOM   8749  O O   . GLY C 1 387 ? 38.465  -39.392 45.493  1.00 123.05 ? 387 GLY C O   1 
ATOM   8750  N N   . SER C 1 388 ? 40.466  -39.950 46.360  1.00 139.88 ? 388 SER C N   1 
ATOM   8751  C CA  . SER C 1 388 ? 41.103  -40.127 45.064  1.00 138.03 ? 388 SER C CA  1 
ATOM   8752  C C   . SER C 1 388 ? 42.038  -41.326 45.122  1.00 138.15 ? 388 SER C C   1 
ATOM   8753  O O   . SER C 1 388 ? 42.355  -41.846 46.194  1.00 139.81 ? 388 SER C O   1 
ATOM   8754  C CB  . SER C 1 388 ? 41.862  -38.867 44.636  1.00 136.17 ? 388 SER C CB  1 
ATOM   8755  O OG  . SER C 1 388 ? 40.967  -37.794 44.398  1.00 135.97 ? 388 SER C OG  1 
ATOM   8756  N N   . ILE C 1 389 ? 42.489  -41.757 43.949  1.00 112.32 ? 389 ILE C N   1 
ATOM   8757  C CA  . ILE C 1 389 ? 43.348  -42.926 43.812  1.00 105.73 ? 389 ILE C CA  1 
ATOM   8758  C C   . ILE C 1 389 ? 44.639  -42.486 43.138  1.00 106.03 ? 389 ILE C C   1 
ATOM   8759  O O   . ILE C 1 389 ? 44.618  -41.998 42.001  1.00 107.52 ? 389 ILE C O   1 
ATOM   8760  C CB  . ILE C 1 389 ? 42.667  -44.044 43.007  1.00 103.45 ? 389 ILE C CB  1 
ATOM   8761  C CG1 . ILE C 1 389 ? 41.265  -44.332 43.555  1.00 104.81 ? 389 ILE C CG1 1 
ATOM   8762  C CG2 . ILE C 1 389 ? 43.513  -45.306 43.041  1.00 101.75 ? 389 ILE C CG2 1 
ATOM   8763  C CD1 . ILE C 1 389 ? 41.237  -44.739 45.010  1.00 109.17 ? 389 ILE C CD1 1 
ATOM   8764  N N   . VAL C 1 390 ? 45.758  -42.655 43.837  1.00 107.84 ? 390 VAL C N   1 
ATOM   8765  C CA  . VAL C 1 390 ? 47.073  -42.282 43.331  1.00 107.10 ? 390 VAL C CA  1 
ATOM   8766  C C   . VAL C 1 390 ? 47.861  -43.548 43.028  1.00 111.13 ? 390 VAL C C   1 
ATOM   8767  O O   . VAL C 1 390 ? 47.854  -44.500 43.817  1.00 112.86 ? 390 VAL C O   1 
ATOM   8768  C CB  . VAL C 1 390 ? 47.830  -41.388 44.333  1.00 104.67 ? 390 VAL C CB  1 
ATOM   8769  C CG1 . VAL C 1 390 ? 49.135  -40.896 43.727  1.00 110.62 ? 390 VAL C CG1 1 
ATOM   8770  C CG2 . VAL C 1 390 ? 46.957  -40.218 44.760  1.00 104.99 ? 390 VAL C CG2 1 
ATOM   8771  N N   . LEU C 1 391 ? 48.538  -43.558 41.881  1.00 111.77 ? 391 LEU C N   1 
ATOM   8772  C CA  . LEU C 1 391 ? 49.349  -44.693 41.472  1.00 119.42 ? 391 LEU C CA  1 
ATOM   8773  C C   . LEU C 1 391 ? 50.696  -44.677 42.190  1.00 128.71 ? 391 LEU C C   1 
ATOM   8774  O O   . LEU C 1 391 ? 51.034  -43.746 42.926  1.00 128.14 ? 391 LEU C O   1 
ATOM   8775  C CB  . LEU C 1 391 ? 49.539  -44.700 39.957  1.00 118.35 ? 391 LEU C CB  1 
ATOM   8776  C CG  . LEU C 1 391 ? 48.545  -45.521 39.133  1.00 111.52 ? 391 LEU C CG  1 
ATOM   8777  C CD1 . LEU C 1 391 ? 47.114  -45.041 39.338  1.00 110.97 ? 391 LEU C CD1 1 
ATOM   8778  C CD2 . LEU C 1 391 ? 48.923  -45.495 37.660  1.00 108.86 ? 391 LEU C CD2 1 
ATOM   8779  N N   . GLN C 1 392 ? 51.477  -45.730 41.970  1.00 145.91 ? 392 GLN C N   1 
ATOM   8780  C CA  . GLN C 1 392 ? 52.762  -45.880 42.634  1.00 151.06 ? 392 GLN C CA  1 
ATOM   8781  C C   . GLN C 1 392 ? 53.802  -44.947 42.024  1.00 147.68 ? 392 GLN C C   1 
ATOM   8782  O O   . GLN C 1 392 ? 53.706  -44.550 40.859  1.00 142.24 ? 392 GLN C O   1 
ATOM   8783  C CB  . GLN C 1 392 ? 53.245  -47.328 42.537  1.00 156.57 ? 392 GLN C CB  1 
ATOM   8784  C CG  . GLN C 1 392 ? 53.696  -47.741 41.142  1.00 153.99 ? 392 GLN C CG  1 
ATOM   8785  C CD  . GLN C 1 392 ? 52.537  -48.078 40.222  1.00 150.79 ? 392 GLN C CD  1 
ATOM   8786  O OE1 . GLN C 1 392 ? 51.371  -47.996 40.612  1.00 154.45 ? 392 GLN C OE1 1 
ATOM   8787  N NE2 . GLN C 1 392 ? 52.853  -48.454 38.989  1.00 146.96 ? 392 GLN C NE2 1 
ATOM   8788  N N   . ASN C 1 393 ? 54.803  -44.600 42.835  1.00 142.81 ? 393 ASN C N   1 
ATOM   8789  C CA  . ASN C 1 393 ? 55.928  -43.761 42.420  1.00 135.56 ? 393 ASN C CA  1 
ATOM   8790  C C   . ASN C 1 393 ? 55.440  -42.434 41.837  1.00 130.28 ? 393 ASN C C   1 
ATOM   8791  O O   . ASN C 1 393 ? 55.688  -42.096 40.677  1.00 127.89 ? 393 ASN C O   1 
ATOM   8792  C CB  . ASN C 1 393 ? 56.834  -44.507 41.437  1.00 135.49 ? 393 ASN C CB  1 
ATOM   8793  C CG  . ASN C 1 393 ? 57.089  -45.941 41.856  1.00 138.09 ? 393 ASN C CG  1 
ATOM   8794  O OD1 . ASN C 1 393 ? 57.248  -46.231 43.043  1.00 144.40 ? 393 ASN C OD1 1 
ATOM   8795  N ND2 . ASN C 1 393 ? 57.135  -46.845 40.885  1.00 140.96 ? 393 ASN C ND2 1 
ATOM   8796  N N   . LYS C 1 394 ? 54.728  -41.683 42.672  1.00 131.44 ? 394 LYS C N   1 
ATOM   8797  C CA  . LYS C 1 394 ? 54.088  -40.446 42.253  1.00 131.11 ? 394 LYS C CA  1 
ATOM   8798  C C   . LYS C 1 394 ? 54.327  -39.367 43.295  1.00 137.15 ? 394 LYS C C   1 
ATOM   8799  O O   . LYS C 1 394 ? 54.272  -39.631 44.499  1.00 143.14 ? 394 LYS C O   1 
ATOM   8800  C CB  . LYS C 1 394 ? 52.582  -40.634 42.031  1.00 127.65 ? 394 LYS C CB  1 
ATOM   8801  C CG  . LYS C 1 394 ? 51.954  -39.565 41.150  1.00 126.62 ? 394 LYS C CG  1 
ATOM   8802  C CD  . LYS C 1 394 ? 52.441  -39.668 39.717  1.00 120.74 ? 394 LYS C CD  1 
ATOM   8803  C CE  . LYS C 1 394 ? 51.855  -38.566 38.851  1.00 118.64 ? 394 LYS C CE  1 
ATOM   8804  N NZ  . LYS C 1 394 ? 52.198  -38.759 37.414  1.00 118.36 ? 394 LYS C NZ  1 
ATOM   8805  N N   . THR C 1 395 ? 54.591  -38.153 42.824  1.00 136.15 ? 395 THR C N   1 
ATOM   8806  C CA  . THR C 1 395 ? 54.829  -37.004 43.683  1.00 145.04 ? 395 THR C CA  1 
ATOM   8807  C C   . THR C 1 395 ? 53.673  -36.022 43.548  1.00 146.89 ? 395 THR C C   1 
ATOM   8808  O O   . THR C 1 395 ? 53.198  -35.755 42.440  1.00 143.94 ? 395 THR C O   1 
ATOM   8809  C CB  . THR C 1 395 ? 56.152  -36.314 43.336  1.00 147.07 ? 395 THR C CB  1 
ATOM   8810  O OG1 . THR C 1 395 ? 56.206  -35.030 43.970  1.00 146.44 ? 395 THR C OG1 1 
ATOM   8811  C CG2 . THR C 1 395 ? 56.294  -36.144 41.829  1.00 148.94 ? 395 THR C CG2 1 
ATOM   8812  N N   . LEU C 1 396 ? 53.218  -35.494 44.683  1.00 156.51 ? 396 LEU C N   1 
ATOM   8813  C CA  . LEU C 1 396 ? 52.063  -34.603 44.725  1.00 154.70 ? 396 LEU C CA  1 
ATOM   8814  C C   . LEU C 1 396 ? 52.456  -33.304 45.412  1.00 154.10 ? 396 LEU C C   1 
ATOM   8815  O O   . LEU C 1 396 ? 52.666  -33.280 46.629  1.00 155.17 ? 396 LEU C O   1 
ATOM   8816  C CB  . LEU C 1 396 ? 50.889  -35.262 45.449  1.00 157.09 ? 396 LEU C CB  1 
ATOM   8817  C CG  . LEU C 1 396 ? 50.267  -36.473 44.753  1.00 162.79 ? 396 LEU C CG  1 
ATOM   8818  C CD1 . LEU C 1 396 ? 49.123  -37.038 45.580  1.00 164.40 ? 396 LEU C CD1 1 
ATOM   8819  C CD2 . LEU C 1 396 ? 49.797  -36.106 43.354  1.00 155.59 ? 396 LEU C CD2 1 
ATOM   8820  N N   . ASN C 1 397 ? 52.552  -32.228 44.631  1.00 134.46 ? 397 ASN C N   1 
ATOM   8821  C CA  . ASN C 1 397 ? 52.763  -30.892 45.167  1.00 128.56 ? 397 ASN C CA  1 
ATOM   8822  C C   . ASN C 1 397 ? 51.476  -30.089 45.297  1.00 126.41 ? 397 ASN C C   1 
ATOM   8823  O O   . ASN C 1 397 ? 51.464  -29.087 46.021  1.00 125.45 ? 397 ASN C O   1 
ATOM   8824  C CB  . ASN C 1 397 ? 53.748  -30.114 44.285  1.00 129.86 ? 397 ASN C CB  1 
ATOM   8825  C CG  . ASN C 1 397 ? 53.306  -30.050 42.833  1.00 133.88 ? 397 ASN C CG  1 
ATOM   8826  O OD1 . ASN C 1 397 ? 52.684  -30.980 42.318  1.00 136.94 ? 397 ASN C OD1 1 
ATOM   8827  N ND2 . ASN C 1 397 ? 53.626  -28.946 42.165  1.00 134.56 ? 397 ASN C ND2 1 
ATOM   8828  N N   . VAL C 1 398 ? 50.403  -30.502 44.619  1.00 127.41 ? 398 VAL C N   1 
ATOM   8829  C CA  . VAL C 1 398 ? 49.135  -29.782 44.606  1.00 115.46 ? 398 VAL C CA  1 
ATOM   8830  C C   . VAL C 1 398 ? 48.033  -30.692 45.136  1.00 109.98 ? 398 VAL C C   1 
ATOM   8831  O O   . VAL C 1 398 ? 48.079  -31.917 44.982  1.00 114.59 ? 398 VAL C O   1 
ATOM   8832  C CB  . VAL C 1 398 ? 48.804  -29.266 43.184  1.00 113.01 ? 398 VAL C CB  1 
ATOM   8833  C CG1 . VAL C 1 398 ? 48.585  -30.428 42.218  1.00 109.87 ? 398 VAL C CG1 1 
ATOM   8834  C CG2 . VAL C 1 398 ? 47.603  -28.326 43.203  1.00 108.53 ? 398 VAL C CG2 1 
ATOM   8835  N N   . SER C 1 399 ? 47.038  -30.081 45.775  1.00 107.79 ? 399 SER C N   1 
ATOM   8836  C CA  . SER C 1 399 ? 45.915  -30.832 46.319  1.00 108.14 ? 399 SER C CA  1 
ATOM   8837  C C   . SER C 1 399 ? 45.011  -31.343 45.202  1.00 106.58 ? 399 SER C C   1 
ATOM   8838  O O   . SER C 1 399 ? 44.742  -30.638 44.225  1.00 103.43 ? 399 SER C O   1 
ATOM   8839  C CB  . SER C 1 399 ? 45.118  -29.962 47.289  1.00 107.92 ? 399 SER C CB  1 
ATOM   8840  O OG  . SER C 1 399 ? 45.928  -29.545 48.374  1.00 111.28 ? 399 SER C OG  1 
ATOM   8841  N N   . VAL C 1 400 ? 44.541  -32.581 45.352  1.00 106.72 ? 400 VAL C N   1 
ATOM   8842  C CA  . VAL C 1 400 ? 43.649  -33.217 44.393  1.00 104.82 ? 400 VAL C CA  1 
ATOM   8843  C C   . VAL C 1 400 ? 42.334  -33.556 45.085  1.00 108.82 ? 400 VAL C C   1 
ATOM   8844  O O   . VAL C 1 400 ? 42.254  -33.644 46.312  1.00 108.98 ? 400 VAL C O   1 
ATOM   8845  C CB  . VAL C 1 400 ? 44.278  -34.479 43.770  1.00 105.36 ? 400 VAL C CB  1 
ATOM   8846  C CG1 . VAL C 1 400 ? 45.559  -34.120 43.032  1.00 104.00 ? 400 VAL C CG1 1 
ATOM   8847  C CG2 . VAL C 1 400 ? 44.551  -35.515 44.845  1.00 109.76 ? 400 VAL C CG2 1 
ATOM   8848  N N   . GLN C 1 401 ? 41.291  -33.745 44.275  1.00 120.28 ? 401 GLN C N   1 
ATOM   8849  C CA  . GLN C 1 401 ? 39.957  -34.001 44.806  1.00 123.00 ? 401 GLN C CA  1 
ATOM   8850  C C   . GLN C 1 401 ? 39.094  -34.678 43.751  1.00 121.60 ? 401 GLN C C   1 
ATOM   8851  O O   . GLN C 1 401 ? 38.953  -34.158 42.640  1.00 120.69 ? 401 GLN C O   1 
ATOM   8852  C CB  . GLN C 1 401 ? 39.293  -32.700 45.266  1.00 127.28 ? 401 GLN C CB  1 
ATOM   8853  C CG  . GLN C 1 401 ? 37.854  -32.868 45.728  1.00 131.05 ? 401 GLN C CG  1 
ATOM   8854  C CD  . GLN C 1 401 ? 37.201  -31.548 46.083  1.00 133.98 ? 401 GLN C CD  1 
ATOM   8855  O OE1 . GLN C 1 401 ? 37.872  -30.525 46.208  1.00 136.70 ? 401 GLN C OE1 1 
ATOM   8856  N NE2 . GLN C 1 401 ? 35.883  -31.565 46.247  1.00 133.04 ? 401 GLN C NE2 1 
ATOM   8857  N N   . ASP C 1 402 ? 38.521  -35.829 44.109  1.00 121.19 ? 402 ASP C N   1 
ATOM   8858  C CA  . ASP C 1 402 ? 37.561  -36.559 43.277  1.00 122.25 ? 402 ASP C CA  1 
ATOM   8859  C C   . ASP C 1 402 ? 38.121  -36.827 41.881  1.00 121.64 ? 402 ASP C C   1 
ATOM   8860  O O   . ASP C 1 402 ? 37.540  -36.452 40.862  1.00 124.17 ? 402 ASP C O   1 
ATOM   8861  C CB  . ASP C 1 402 ? 36.227  -35.812 43.188  1.00 128.33 ? 402 ASP C CB  1 
ATOM   8862  C CG  . ASP C 1 402 ? 35.605  -35.552 44.546  1.00 132.77 ? 402 ASP C CG  1 
ATOM   8863  O OD1 . ASP C 1 402 ? 35.819  -36.364 45.470  1.00 132.62 ? 402 ASP C OD1 1 
ATOM   8864  O OD2 . ASP C 1 402 ? 34.892  -34.535 44.684  1.00 133.98 ? 402 ASP C OD2 1 
ATOM   8865  N N   . ASP C 1 403 ? 39.270  -37.495 41.848  1.00 114.97 ? 403 ASP C N   1 
ATOM   8866  C CA  . ASP C 1 403 ? 39.930  -37.794 40.587  1.00 110.66 ? 403 ASP C CA  1 
ATOM   8867  C C   . ASP C 1 403 ? 40.691  -39.106 40.723  1.00 105.75 ? 403 ASP C C   1 
ATOM   8868  O O   . ASP C 1 403 ? 40.728  -39.721 41.792  1.00 108.47 ? 403 ASP C O   1 
ATOM   8869  C CB  . ASP C 1 403 ? 40.852  -36.644 40.172  1.00 113.51 ? 403 ASP C CB  1 
ATOM   8870  C CG  . ASP C 1 403 ? 41.105  -36.609 38.679  1.00 117.21 ? 403 ASP C CG  1 
ATOM   8871  O OD1 . ASP C 1 403 ? 40.985  -37.668 38.029  1.00 114.24 ? 403 ASP C OD1 1 
ATOM   8872  O OD2 . ASP C 1 403 ? 41.420  -35.519 38.156  1.00 122.72 ? 403 ASP C OD2 1 
ATOM   8873  N N   . ILE C 1 404 ? 41.289  -39.540 39.617  1.00 102.92 ? 404 ILE C N   1 
ATOM   8874  C CA  . ILE C 1 404 ? 42.111  -40.744 39.567  1.00 101.66 ? 404 ILE C CA  1 
ATOM   8875  C C   . ILE C 1 404 ? 43.438  -40.329 38.945  1.00 101.24 ? 404 ILE C C   1 
ATOM   8876  O O   . ILE C 1 404 ? 43.524  -40.128 37.729  1.00 100.70 ? 404 ILE C O   1 
ATOM   8877  C CB  . ILE C 1 404 ? 41.453  -41.872 38.767  1.00 101.42 ? 404 ILE C CB  1 
ATOM   8878  C CG1 . ILE C 1 404 ? 40.075  -42.207 39.345  1.00 105.90 ? 404 ILE C CG1 1 
ATOM   8879  C CG2 . ILE C 1 404 ? 42.352  -43.099 38.748  1.00 97.51  ? 404 ILE C CG2 1 
ATOM   8880  C CD1 . ILE C 1 404 ? 39.339  -43.296 38.596  1.00 106.69 ? 404 ILE C CD1 1 
ATOM   8881  N N   . ILE C 1 405 ? 44.472  -40.201 39.769  1.00 102.18 ? 405 ILE C N   1 
ATOM   8882  C CA  . ILE C 1 405 ? 45.757  -39.668 39.330  1.00 103.34 ? 405 ILE C CA  1 
ATOM   8883  C C   . ILE C 1 405 ? 46.659  -40.815 38.894  1.00 106.79 ? 405 ILE C C   1 
ATOM   8884  O O   . ILE C 1 405 ? 46.956  -41.720 39.681  1.00 106.16 ? 405 ILE C O   1 
ATOM   8885  C CB  . ILE C 1 405 ? 46.425  -38.840 40.437  1.00 101.09 ? 405 ILE C CB  1 
ATOM   8886  C CG1 . ILE C 1 405 ? 45.680  -37.519 40.651  1.00 97.69  ? 405 ILE C CG1 1 
ATOM   8887  C CG2 . ILE C 1 405 ? 47.884  -38.585 40.097  1.00 106.85 ? 405 ILE C CG2 1 
ATOM   8888  C CD1 . ILE C 1 405 ? 44.532  -37.604 41.630  1.00 103.38 ? 405 ILE C CD1 1 
ATOM   8889  N N   . LEU C 1 406 ? 47.094  -40.776 37.638  1.00 117.82 ? 406 LEU C N   1 
ATOM   8890  C CA  . LEU C 1 406 ? 48.010  -41.781 37.114  1.00 118.62 ? 406 LEU C CA  1 
ATOM   8891  C C   . LEU C 1 406 ? 49.460  -41.363 37.341  1.00 118.51 ? 406 LEU C C   1 
ATOM   8892  O O   . LEU C 1 406 ? 49.854  -40.249 36.999  1.00 115.63 ? 406 LEU C O   1 
ATOM   8893  C CB  . LEU C 1 406 ? 47.758  -42.018 35.625  1.00 118.79 ? 406 LEU C CB  1 
ATOM   8894  C CG  . LEU C 1 406 ? 46.339  -42.450 35.258  1.00 118.25 ? 406 LEU C CG  1 
ATOM   8895  C CD1 . LEU C 1 406 ? 46.196  -42.616 33.754  1.00 115.03 ? 406 LEU C CD1 1 
ATOM   8896  C CD2 . LEU C 1 406 ? 45.994  -43.736 35.984  1.00 118.93 ? 406 LEU C CD2 1 
ATOM   8897  O OXT . LEU C 1 406 ? 50.271  -42.129 37.861  1.00 122.73 ? 406 LEU C OXT 1 
ATOM   8898  N N   . MET D 2 1   ? 84.792  -37.390 19.055  1.00 129.31 ? 1   MET D N   1 
ATOM   8899  C CA  . MET D 2 1   ? 83.814  -36.410 19.510  1.00 135.17 ? 1   MET D CA  1 
ATOM   8900  C C   . MET D 2 1   ? 82.815  -37.049 20.475  1.00 133.39 ? 1   MET D C   1 
ATOM   8901  O O   . MET D 2 1   ? 82.423  -38.204 20.300  1.00 129.24 ? 1   MET D O   1 
ATOM   8902  C CB  . MET D 2 1   ? 83.089  -35.788 18.314  1.00 131.59 ? 1   MET D CB  1 
ATOM   8903  C CG  . MET D 2 1   ? 82.211  -34.600 18.664  1.00 137.31 ? 1   MET D CG  1 
ATOM   8904  S SD  . MET D 2 1   ? 81.585  -33.750 17.205  1.00 152.10 ? 1   MET D SD  1 
ATOM   8905  C CE  . MET D 2 1   ? 83.110  -33.182 16.457  1.00 157.41 ? 1   MET D CE  1 
ATOM   8906  N N   . LYS D 2 2   ? 82.408  -36.291 21.489  1.00 136.17 ? 2   LYS D N   1 
ATOM   8907  C CA  . LYS D 2 2   ? 81.529  -36.770 22.546  1.00 137.38 ? 2   LYS D CA  1 
ATOM   8908  C C   . LYS D 2 2   ? 80.158  -36.111 22.440  1.00 147.12 ? 2   LYS D C   1 
ATOM   8909  O O   . LYS D 2 2   ? 79.929  -35.218 21.619  1.00 151.54 ? 2   LYS D O   1 
ATOM   8910  C CB  . LYS D 2 2   ? 82.146  -36.498 23.924  1.00 135.12 ? 2   LYS D CB  1 
ATOM   8911  C CG  . LYS D 2 2   ? 83.480  -37.190 24.163  1.00 136.97 ? 2   LYS D CG  1 
ATOM   8912  C CD  . LYS D 2 2   ? 83.299  -38.691 24.319  1.00 132.34 ? 2   LYS D CD  1 
ATOM   8913  C CE  . LYS D 2 2   ? 84.606  -39.373 24.690  1.00 131.57 ? 2   LYS D CE  1 
ATOM   8914  N NZ  . LYS D 2 2   ? 84.405  -40.812 25.019  1.00 122.81 ? 2   LYS D NZ  1 
ATOM   8915  N N   . ALA D 2 3   ? 79.242  -36.564 23.295  1.00 152.72 ? 3   ALA D N   1 
ATOM   8916  C CA  . ALA D 2 3   ? 77.879  -36.049 23.336  1.00 163.93 ? 3   ALA D CA  1 
ATOM   8917  C C   . ALA D 2 3   ? 77.215  -36.496 24.631  1.00 162.56 ? 3   ALA D C   1 
ATOM   8918  O O   . ALA D 2 3   ? 77.583  -37.522 25.210  1.00 152.66 ? 3   ALA D O   1 
ATOM   8919  C CB  . ALA D 2 3   ? 77.059  -36.524 22.128  1.00 151.08 ? 3   ALA D CB  1 
ATOM   8920  N N   . LEU D 2 4   ? 76.234  -35.712 25.074  1.00 185.61 ? 4   LEU D N   1 
ATOM   8921  C CA  . LEU D 2 4   ? 75.470  -35.992 26.283  1.00 184.03 ? 4   LEU D CA  1 
ATOM   8922  C C   . LEU D 2 4   ? 74.003  -35.675 26.028  1.00 185.42 ? 4   LEU D C   1 
ATOM   8923  O O   . LEU D 2 4   ? 73.681  -34.668 25.391  1.00 192.44 ? 4   LEU D O   1 
ATOM   8924  C CB  . LEU D 2 4   ? 75.988  -35.175 27.476  1.00 184.30 ? 4   LEU D CB  1 
ATOM   8925  C CG  . LEU D 2 4   ? 75.187  -35.240 28.781  1.00 183.03 ? 4   LEU D CG  1 
ATOM   8926  C CD1 . LEU D 2 4   ? 75.225  -36.634 29.385  1.00 183.08 ? 4   LEU D CD1 1 
ATOM   8927  C CD2 . LEU D 2 4   ? 75.699  -34.210 29.774  1.00 187.09 ? 4   LEU D CD2 1 
ATOM   8928  N N   . ILE D 2 5   ? 73.117  -36.539 26.519  1.00 167.26 ? 5   ILE D N   1 
ATOM   8929  C CA  . ILE D 2 5   ? 71.676  -36.393 26.330  1.00 165.53 ? 5   ILE D CA  1 
ATOM   8930  C C   . ILE D 2 5   ? 71.008  -36.332 27.698  1.00 160.56 ? 5   ILE D C   1 
ATOM   8931  O O   . ILE D 2 5   ? 71.182  -37.240 28.522  1.00 154.00 ? 5   ILE D O   1 
ATOM   8932  C CB  . ILE D 2 5   ? 71.093  -37.538 25.488  1.00 160.76 ? 5   ILE D CB  1 
ATOM   8933  C CG1 . ILE D 2 5   ? 71.708  -37.542 24.084  1.00 156.77 ? 5   ILE D CG1 1 
ATOM   8934  C CG2 . ILE D 2 5   ? 69.579  -37.422 25.408  1.00 163.07 ? 5   ILE D CG2 1 
ATOM   8935  C CD1 . ILE D 2 5   ? 71.174  -38.636 23.189  1.00 145.28 ? 5   ILE D CD1 1 
ATOM   8936  N N   . LEU D 2 6   ? 70.245  -35.265 27.936  1.00 162.14 ? 6   LEU D N   1 
ATOM   8937  C CA  . LEU D 2 6   ? 69.484  -35.110 29.173  1.00 160.42 ? 6   LEU D CA  1 
ATOM   8938  C C   . LEU D 2 6   ? 68.159  -35.853 29.044  1.00 162.10 ? 6   LEU D C   1 
ATOM   8939  O O   . LEU D 2 6   ? 67.314  -35.494 28.216  1.00 160.93 ? 6   LEU D O   1 
ATOM   8940  C CB  . LEU D 2 6   ? 69.254  -33.632 29.477  1.00 163.89 ? 6   LEU D CB  1 
ATOM   8941  C CG  . LEU D 2 6   ? 70.489  -32.776 29.769  1.00 167.05 ? 6   LEU D CG  1 
ATOM   8942  C CD1 . LEU D 2 6   ? 70.100  -31.314 29.899  1.00 171.18 ? 6   LEU D CD1 1 
ATOM   8943  C CD2 . LEU D 2 6   ? 71.177  -33.256 31.035  1.00 162.88 ? 6   LEU D CD2 1 
ATOM   8944  N N   . VAL D 2 7   ? 67.972  -36.890 29.860  1.00 165.32 ? 7   VAL D N   1 
ATOM   8945  C CA  . VAL D 2 7   ? 66.729  -37.653 29.856  1.00 161.79 ? 7   VAL D CA  1 
ATOM   8946  C C   . VAL D 2 7   ? 65.829  -37.155 30.978  1.00 161.12 ? 7   VAL D C   1 
ATOM   8947  O O   . VAL D 2 7   ? 64.681  -36.758 30.740  1.00 159.65 ? 7   VAL D O   1 
ATOM   8948  C CB  . VAL D 2 7   ? 66.998  -39.160 29.998  1.00 155.48 ? 7   VAL D CB  1 
ATOM   8949  C CG1 . VAL D 2 7   ? 65.691  -39.933 29.988  1.00 152.36 ? 7   VAL D CG1 1 
ATOM   8950  C CG2 . VAL D 2 7   ? 67.915  -39.640 28.887  1.00 153.10 ? 7   VAL D CG2 1 
ATOM   8951  N N   . GLY D 2 8   ? 66.340  -37.169 32.201  1.00 150.89 ? 8   GLY D N   1 
ATOM   8952  C CA  . GLY D 2 8   ? 65.558  -36.772 33.358  1.00 146.53 ? 8   GLY D CA  1 
ATOM   8953  C C   . GLY D 2 8   ? 65.123  -37.980 34.175  1.00 145.17 ? 8   GLY D C   1 
ATOM   8954  O O   . GLY D 2 8   ? 65.947  -38.815 34.550  1.00 142.85 ? 8   GLY D O   1 
ATOM   8955  N N   . GLY D 2 9   ? 63.831  -38.067 34.449  1.00 147.59 ? 9   GLY D N   1 
ATOM   8956  C CA  . GLY D 2 9   ? 63.266  -39.164 35.208  1.00 146.85 ? 9   GLY D CA  1 
ATOM   8957  C C   . GLY D 2 9   ? 62.745  -40.280 34.330  1.00 142.35 ? 9   GLY D C   1 
ATOM   8958  O O   . GLY D 2 9   ? 63.240  -40.519 33.223  1.00 138.63 ? 9   GLY D O   1 
ATOM   8959  N N   . PHE D 2 10  ? 61.724  -40.971 34.833  1.00 128.56 ? 10  PHE D N   1 
ATOM   8960  C CA  . PHE D 2 10  ? 61.152  -42.124 34.155  1.00 117.67 ? 10  PHE D CA  1 
ATOM   8961  C C   . PHE D 2 10  ? 60.083  -41.744 33.140  1.00 116.59 ? 10  PHE D C   1 
ATOM   8962  O O   . PHE D 2 10  ? 59.716  -42.580 32.307  1.00 115.81 ? 10  PHE D O   1 
ATOM   8963  C CB  . PHE D 2 10  ? 60.555  -43.089 35.189  1.00 117.16 ? 10  PHE D CB  1 
ATOM   8964  C CG  . PHE D 2 10  ? 60.752  -44.543 34.856  1.00 114.02 ? 10  PHE D CG  1 
ATOM   8965  C CD1 . PHE D 2 10  ? 61.954  -45.173 35.142  1.00 116.55 ? 10  PHE D CD1 1 
ATOM   8966  C CD2 . PHE D 2 10  ? 59.738  -45.282 34.272  1.00 110.93 ? 10  PHE D CD2 1 
ATOM   8967  C CE1 . PHE D 2 10  ? 62.142  -46.511 34.842  1.00 116.70 ? 10  PHE D CE1 1 
ATOM   8968  C CE2 . PHE D 2 10  ? 59.920  -46.620 33.970  1.00 116.36 ? 10  PHE D CE2 1 
ATOM   8969  C CZ  . PHE D 2 10  ? 61.123  -47.234 34.256  1.00 114.62 ? 10  PHE D CZ  1 
ATOM   8970  N N   . GLY D 2 11  ? 59.586  -40.510 33.180  1.00 121.93 ? 11  GLY D N   1 
ATOM   8971  C CA  . GLY D 2 11  ? 58.491  -40.096 32.324  1.00 121.48 ? 11  GLY D CA  1 
ATOM   8972  C C   . GLY D 2 11  ? 57.152  -40.216 33.020  1.00 120.22 ? 11  GLY D C   1 
ATOM   8973  O O   . GLY D 2 11  ? 56.229  -40.855 32.507  1.00 113.49 ? 11  GLY D O   1 
ATOM   8974  N N   . THR D 2 12  ? 57.036  -39.592 34.194  1.00 124.68 ? 12  THR D N   1 
ATOM   8975  C CA  . THR D 2 12  ? 55.813  -39.712 34.985  1.00 119.93 ? 12  THR D CA  1 
ATOM   8976  C C   . THR D 2 12  ? 54.614  -39.109 34.263  1.00 118.56 ? 12  THR D C   1 
ATOM   8977  O O   . THR D 2 12  ? 53.495  -39.625 34.365  1.00 115.92 ? 12  THR D O   1 
ATOM   8978  C CB  . THR D 2 12  ? 56.006  -39.045 36.346  1.00 123.03 ? 12  THR D CB  1 
ATOM   8979  O OG1 . THR D 2 12  ? 56.325  -37.661 36.160  1.00 131.95 ? 12  THR D OG1 1 
ATOM   8980  C CG2 . THR D 2 12  ? 57.135  -39.720 37.112  1.00 121.00 ? 12  THR D CG2 1 
ATOM   8981  N N   . ARG D 2 13  ? 54.826  -38.025 33.524  1.00 136.39 ? 13  ARG D N   1 
ATOM   8982  C CA  . ARG D 2 13  ? 53.751  -37.340 32.818  1.00 137.39 ? 13  ARG D CA  1 
ATOM   8983  C C   . ARG D 2 13  ? 53.400  -37.990 31.483  1.00 134.97 ? 13  ARG D C   1 
ATOM   8984  O O   . ARG D 2 13  ? 52.598  -37.427 30.730  1.00 134.17 ? 13  ARG D O   1 
ATOM   8985  C CB  . ARG D 2 13  ? 54.126  -35.870 32.608  1.00 142.72 ? 13  ARG D CB  1 
ATOM   8986  C CG  . ARG D 2 13  ? 55.604  -35.640 32.343  1.00 142.65 ? 13  ARG D CG  1 
ATOM   8987  C CD  . ARG D 2 13  ? 56.013  -34.211 32.669  1.00 151.27 ? 13  ARG D CD  1 
ATOM   8988  N NE  . ARG D 2 13  ? 55.677  -33.841 34.041  1.00 160.14 ? 13  ARG D NE  1 
ATOM   8989  C CZ  . ARG D 2 13  ? 54.785  -32.911 34.366  1.00 164.93 ? 13  ARG D CZ  1 
ATOM   8990  N NH1 . ARG D 2 13  ? 54.137  -32.251 33.415  1.00 165.08 ? 13  ARG D NH1 1 
ATOM   8991  N NH2 . ARG D 2 13  ? 54.545  -32.637 35.641  1.00 167.86 ? 13  ARG D NH2 1 
ATOM   8992  N N   . LEU D 2 14  ? 53.975  -39.152 31.174  1.00 116.88 ? 14  LEU D N   1 
ATOM   8993  C CA  . LEU D 2 14  ? 53.684  -39.866 29.936  1.00 110.23 ? 14  LEU D CA  1 
ATOM   8994  C C   . LEU D 2 14  ? 53.011  -41.211 30.184  1.00 102.32 ? 14  LEU D C   1 
ATOM   8995  O O   . LEU D 2 14  ? 52.928  -42.030 29.261  1.00 97.19  ? 14  LEU D O   1 
ATOM   8996  C CB  . LEU D 2 14  ? 54.960  -40.062 29.109  1.00 110.91 ? 14  LEU D CB  1 
ATOM   8997  C CG  . LEU D 2 14  ? 55.595  -38.834 28.448  1.00 113.14 ? 14  LEU D CG  1 
ATOM   8998  C CD1 . LEU D 2 14  ? 56.366  -37.977 29.446  1.00 118.32 ? 14  LEU D CD1 1 
ATOM   8999  C CD2 . LEU D 2 14  ? 56.494  -39.261 27.300  1.00 115.91 ? 14  LEU D CD2 1 
ATOM   9000  N N   . ARG D 2 15  ? 52.535  -41.460 31.405  1.00 99.97  ? 15  ARG D N   1 
ATOM   9001  C CA  . ARG D 2 15  ? 51.836  -42.696 31.719  1.00 95.26  ? 15  ARG D CA  1 
ATOM   9002  C C   . ARG D 2 15  ? 50.538  -42.787 30.915  1.00 91.29  ? 15  ARG D C   1 
ATOM   9003  O O   . ARG D 2 15  ? 49.982  -41.765 30.505  1.00 92.63  ? 15  ARG D O   1 
ATOM   9004  C CB  . ARG D 2 15  ? 51.541  -42.757 33.218  1.00 96.67  ? 15  ARG D CB  1 
ATOM   9005  C CG  . ARG D 2 15  ? 52.781  -42.885 34.090  1.00 102.83 ? 15  ARG D CG  1 
ATOM   9006  C CD  . ARG D 2 15  ? 52.415  -43.185 35.534  1.00 103.46 ? 15  ARG D CD  1 
ATOM   9007  N NE  . ARG D 2 15  ? 53.595  -43.450 36.354  1.00 108.81 ? 15  ARG D NE  1 
ATOM   9008  C CZ  . ARG D 2 15  ? 54.177  -42.549 37.138  1.00 109.05 ? 15  ARG D CZ  1 
ATOM   9009  N NH1 . ARG D 2 15  ? 53.691  -41.318 37.208  1.00 110.74 ? 15  ARG D NH1 1 
ATOM   9010  N NH2 . ARG D 2 15  ? 55.246  -42.876 37.849  1.00 110.60 ? 15  ARG D NH2 1 
ATOM   9011  N N   . PRO D 2 16  ? 50.024  -44.009 30.678  1.00 90.57  ? 16  PRO D N   1 
ATOM   9012  C CA  . PRO D 2 16  ? 50.506  -45.322 31.126  1.00 90.79  ? 16  PRO D CA  1 
ATOM   9013  C C   . PRO D 2 16  ? 51.586  -45.926 30.234  1.00 91.08  ? 16  PRO D C   1 
ATOM   9014  O O   . PRO D 2 16  ? 51.949  -47.088 30.419  1.00 91.97  ? 16  PRO D O   1 
ATOM   9015  C CB  . PRO D 2 16  ? 49.243  -46.180 31.076  1.00 88.68  ? 16  PRO D CB  1 
ATOM   9016  C CG  . PRO D 2 16  ? 48.487  -45.618 29.926  1.00 86.02  ? 16  PRO D CG  1 
ATOM   9017  C CD  . PRO D 2 16  ? 48.759  -44.130 29.930  1.00 89.42  ? 16  PRO D CD  1 
ATOM   9018  N N   . LEU D 2 17  ? 52.088  -45.147 29.274  1.00 91.71  ? 17  LEU D N   1 
ATOM   9019  C CA  . LEU D 2 17  ? 53.113  -45.663 28.374  1.00 95.41  ? 17  LEU D CA  1 
ATOM   9020  C C   . LEU D 2 17  ? 54.454  -45.819 29.077  1.00 100.69 ? 17  LEU D C   1 
ATOM   9021  O O   . LEU D 2 17  ? 55.257  -46.678 28.695  1.00 101.79 ? 17  LEU D O   1 
ATOM   9022  C CB  . LEU D 2 17  ? 53.254  -44.744 27.161  1.00 93.42  ? 17  LEU D CB  1 
ATOM   9023  C CG  . LEU D 2 17  ? 51.991  -44.548 26.320  1.00 91.13  ? 17  LEU D CG  1 
ATOM   9024  C CD1 . LEU D 2 17  ? 52.260  -43.593 25.170  1.00 95.89  ? 17  LEU D CD1 1 
ATOM   9025  C CD2 . LEU D 2 17  ? 51.483  -45.885 25.805  1.00 97.17  ? 17  LEU D CD2 1 
ATOM   9026  N N   . THR D 2 18  ? 54.712  -45.012 30.103  1.00 100.96 ? 18  THR D N   1 
ATOM   9027  C CA  . THR D 2 18  ? 55.956  -45.081 30.856  1.00 100.66 ? 18  THR D CA  1 
ATOM   9028  C C   . THR D 2 18  ? 55.801  -45.835 32.170  1.00 111.40 ? 18  THR D C   1 
ATOM   9029  O O   . THR D 2 18  ? 56.692  -45.764 33.023  1.00 119.22 ? 18  THR D O   1 
ATOM   9030  C CB  . THR D 2 18  ? 56.499  -43.676 31.115  1.00 101.01 ? 18  THR D CB  1 
ATOM   9031  O OG1 . THR D 2 18  ? 55.475  -42.864 31.702  1.00 103.68 ? 18  THR D OG1 1 
ATOM   9032  C CG2 . THR D 2 18  ? 56.968  -43.037 29.816  1.00 100.19 ? 18  THR D CG2 1 
ATOM   9033  N N   . LEU D 2 19  ? 54.690  -46.550 32.354  1.00 111.44 ? 19  LEU D N   1 
ATOM   9034  C CA  . LEU D 2 19  ? 54.531  -47.377 33.544  1.00 118.72 ? 19  LEU D CA  1 
ATOM   9035  C C   . LEU D 2 19  ? 55.445  -48.595 33.509  1.00 139.75 ? 19  LEU D C   1 
ATOM   9036  O O   . LEU D 2 19  ? 55.822  -49.115 34.565  1.00 140.45 ? 19  LEU D O   1 
ATOM   9037  C CB  . LEU D 2 19  ? 53.073  -47.810 33.691  1.00 107.57 ? 19  LEU D CB  1 
ATOM   9038  C CG  . LEU D 2 19  ? 52.179  -46.885 34.515  1.00 102.16 ? 19  LEU D CG  1 
ATOM   9039  C CD1 . LEU D 2 19  ? 50.766  -47.431 34.567  1.00 100.61 ? 19  LEU D CD1 1 
ATOM   9040  C CD2 . LEU D 2 19  ? 52.741  -46.730 35.918  1.00 109.10 ? 19  LEU D CD2 1 
ATOM   9041  N N   . SER D 2 20  ? 55.812  -49.060 32.314  1.00 189.01 ? 20  SER D N   1 
ATOM   9042  C CA  . SER D 2 20  ? 56.685  -50.215 32.151  1.00 189.49 ? 20  SER D CA  1 
ATOM   9043  C C   . SER D 2 20  ? 58.042  -49.828 31.576  1.00 188.29 ? 20  SER D C   1 
ATOM   9044  O O   . SER D 2 20  ? 59.069  -50.001 32.238  1.00 188.64 ? 20  SER D O   1 
ATOM   9045  C CB  . SER D 2 20  ? 56.005  -51.262 31.256  1.00 190.26 ? 20  SER D CB  1 
ATOM   9046  O OG  . SER D 2 20  ? 54.771  -51.687 31.811  1.00 191.69 ? 20  SER D OG  1 
ATOM   9047  N N   . PHE D 2 21  ? 58.071  -49.298 30.356  1.00 141.84 ? 21  PHE D N   1 
ATOM   9048  C CA  . PHE D 2 21  ? 59.311  -48.855 29.729  1.00 130.30 ? 21  PHE D CA  1 
ATOM   9049  C C   . PHE D 2 21  ? 59.594  -47.405 30.106  1.00 119.47 ? 21  PHE D C   1 
ATOM   9050  O O   . PHE D 2 21  ? 58.664  -46.599 30.202  1.00 116.49 ? 21  PHE D O   1 
ATOM   9051  C CB  . PHE D 2 21  ? 59.226  -48.976 28.208  1.00 126.65 ? 21  PHE D CB  1 
ATOM   9052  C CG  . PHE D 2 21  ? 59.139  -50.392 27.714  1.00 132.66 ? 21  PHE D CG  1 
ATOM   9053  C CD1 . PHE D 2 21  ? 59.695  -51.429 28.443  1.00 137.44 ? 21  PHE D CD1 1 
ATOM   9054  C CD2 . PHE D 2 21  ? 58.489  -50.688 26.525  1.00 129.40 ? 21  PHE D CD2 1 
ATOM   9055  C CE1 . PHE D 2 21  ? 59.610  -52.735 27.996  1.00 133.01 ? 21  PHE D CE1 1 
ATOM   9056  C CE2 . PHE D 2 21  ? 58.400  -51.992 26.073  1.00 129.27 ? 21  PHE D CE2 1 
ATOM   9057  C CZ  . PHE D 2 21  ? 58.961  -53.016 26.809  1.00 130.44 ? 21  PHE D CZ  1 
ATOM   9058  N N   . PRO D 2 22  ? 60.852  -47.039 30.333  1.00 113.86 ? 22  PRO D N   1 
ATOM   9059  C CA  . PRO D 2 22  ? 61.152  -45.659 30.723  1.00 108.23 ? 22  PRO D CA  1 
ATOM   9060  C C   . PRO D 2 22  ? 60.877  -44.697 29.577  1.00 104.22 ? 22  PRO D C   1 
ATOM   9061  O O   . PRO D 2 22  ? 60.598  -45.087 28.442  1.00 101.93 ? 22  PRO D O   1 
ATOM   9062  C CB  . PRO D 2 22  ? 62.636  -45.688 31.096  1.00 109.68 ? 22  PRO D CB  1 
ATOM   9063  C CG  . PRO D 2 22  ? 63.182  -46.967 30.544  1.00 112.07 ? 22  PRO D CG  1 
ATOM   9064  C CD  . PRO D 2 22  ? 62.061  -47.821 30.032  1.00 115.11 ? 22  PRO D CD  1 
ATOM   9065  N N   . LYS D 2 23  ? 60.961  -43.409 29.903  1.00 100.89 ? 23  LYS D N   1 
ATOM   9066  C CA  . LYS D 2 23  ? 60.609  -42.355 28.952  1.00 100.56 ? 23  LYS D CA  1 
ATOM   9067  C C   . LYS D 2 23  ? 61.327  -42.451 27.607  1.00 99.00  ? 23  LYS D C   1 
ATOM   9068  O O   . LYS D 2 23  ? 60.648  -42.370 26.572  1.00 100.98 ? 23  LYS D O   1 
ATOM   9069  C CB  . LYS D 2 23  ? 60.842  -40.990 29.615  1.00 103.92 ? 23  LYS D CB  1 
ATOM   9070  C CG  . LYS D 2 23  ? 60.593  -39.813 28.692  1.00 106.95 ? 23  LYS D CG  1 
ATOM   9071  C CD  . LYS D 2 23  ? 60.615  -38.501 29.455  1.00 110.69 ? 23  LYS D CD  1 
ATOM   9072  C CE  . LYS D 2 23  ? 61.916  -38.324 30.215  1.00 121.73 ? 23  LYS D CE  1 
ATOM   9073  N NZ  . LYS D 2 23  ? 61.972  -37.012 30.918  1.00 129.79 ? 23  LYS D NZ  1 
ATOM   9074  N N   . PRO D 2 24  ? 62.653  -42.625 27.531  1.00 102.76 ? 24  PRO D N   1 
ATOM   9075  C CA  . PRO D 2 24  ? 63.315  -42.617 26.217  1.00 101.49 ? 24  PRO D CA  1 
ATOM   9076  C C   . PRO D 2 24  ? 63.132  -43.883 25.394  1.00 96.35  ? 24  PRO D C   1 
ATOM   9077  O O   . PRO D 2 24  ? 63.549  -43.901 24.229  1.00 92.96  ? 24  PRO D O   1 
ATOM   9078  C CB  . PRO D 2 24  ? 64.792  -42.422 26.582  1.00 103.90 ? 24  PRO D CB  1 
ATOM   9079  C CG  . PRO D 2 24  ? 64.923  -43.058 27.909  1.00 103.14 ? 24  PRO D CG  1 
ATOM   9080  C CD  . PRO D 2 24  ? 63.634  -42.763 28.626  1.00 104.50 ? 24  PRO D CD  1 
ATOM   9081  N N   . LEU D 2 25  ? 62.528  -44.936 25.942  1.00 94.82  ? 25  LEU D N   1 
ATOM   9082  C CA  . LEU D 2 25  ? 62.373  -46.200 25.234  1.00 94.33  ? 25  LEU D CA  1 
ATOM   9083  C C   . LEU D 2 25  ? 61.008  -46.353 24.573  1.00 94.74  ? 25  LEU D C   1 
ATOM   9084  O O   . LEU D 2 25  ? 60.709  -47.425 24.034  1.00 96.88  ? 25  LEU D O   1 
ATOM   9085  C CB  . LEU D 2 25  ? 62.615  -47.375 26.186  1.00 99.99  ? 25  LEU D CB  1 
ATOM   9086  C CG  . LEU D 2 25  ? 64.055  -47.630 26.634  1.00 102.15 ? 25  LEU D CG  1 
ATOM   9087  C CD1 . LEU D 2 25  ? 64.170  -48.975 27.342  1.00 105.55 ? 25  LEU D CD1 1 
ATOM   9088  C CD2 . LEU D 2 25  ? 65.018  -47.554 25.458  1.00 104.27 ? 25  LEU D CD2 1 
ATOM   9089  N N   . VAL D 2 26  ? 60.177  -45.316 24.592  1.00 92.48  ? 26  VAL D N   1 
ATOM   9090  C CA  . VAL D 2 26  ? 58.870  -45.382 23.948  1.00 91.03  ? 26  VAL D CA  1 
ATOM   9091  C C   . VAL D 2 26  ? 59.043  -45.206 22.445  1.00 90.60  ? 26  VAL D C   1 
ATOM   9092  O O   . VAL D 2 26  ? 59.666  -44.241 21.987  1.00 91.25  ? 26  VAL D O   1 
ATOM   9093  C CB  . VAL D 2 26  ? 57.922  -44.321 24.527  1.00 94.02  ? 26  VAL D CB  1 
ATOM   9094  C CG1 . VAL D 2 26  ? 56.609  -44.320 23.764  1.00 102.10 ? 26  VAL D CG1 1 
ATOM   9095  C CG2 . VAL D 2 26  ? 57.683  -44.580 26.006  1.00 93.42  ? 26  VAL D CG2 1 
ATOM   9096  N N   . ASP D 2 27  ? 58.498  -46.145 21.675  1.00 90.37  ? 27  ASP D N   1 
ATOM   9097  C CA  . ASP D 2 27  ? 58.577  -46.071 20.222  1.00 84.18  ? 27  ASP D CA  1 
ATOM   9098  C C   . ASP D 2 27  ? 57.773  -44.881 19.716  1.00 83.50  ? 27  ASP D C   1 
ATOM   9099  O O   . ASP D 2 27  ? 56.550  -44.836 19.878  1.00 87.48  ? 27  ASP D O   1 
ATOM   9100  C CB  . ASP D 2 27  ? 58.061  -47.364 19.592  1.00 85.93  ? 27  ASP D CB  1 
ATOM   9101  C CG  . ASP D 2 27  ? 59.008  -48.526 19.783  1.00 87.95  ? 27  ASP D CG  1 
ATOM   9102  O OD1 . ASP D 2 27  ? 59.927  -48.413 20.621  1.00 89.96  ? 27  ASP D OD1 1 
ATOM   9103  O OD2 . ASP D 2 27  ? 58.837  -49.554 19.095  1.00 88.17  ? 27  ASP D OD2 1 
ATOM   9104  N N   . PHE D 2 28  ? 58.457  -43.922 19.102  1.00 85.04  ? 28  PHE D N   1 
ATOM   9105  C CA  . PHE D 2 28  ? 57.816  -42.794 18.440  1.00 86.74  ? 28  PHE D CA  1 
ATOM   9106  C C   . PHE D 2 28  ? 58.056  -42.919 16.945  1.00 87.34  ? 28  PHE D C   1 
ATOM   9107  O O   . PHE D 2 28  ? 59.203  -42.854 16.493  1.00 91.87  ? 28  PHE D O   1 
ATOM   9108  C CB  . PHE D 2 28  ? 58.351  -41.459 18.951  1.00 93.62  ? 28  PHE D CB  1 
ATOM   9109  C CG  . PHE D 2 28  ? 57.866  -40.277 18.159  1.00 97.37  ? 28  PHE D CG  1 
ATOM   9110  C CD1 . PHE D 2 28  ? 58.716  -39.611 17.290  1.00 100.02 ? 28  PHE D CD1 1 
ATOM   9111  C CD2 . PHE D 2 28  ? 56.552  -39.853 18.257  1.00 99.67  ? 28  PHE D CD2 1 
ATOM   9112  C CE1 . PHE D 2 28  ? 58.270  -38.530 16.551  1.00 103.27 ? 28  PHE D CE1 1 
ATOM   9113  C CE2 . PHE D 2 28  ? 56.099  -38.772 17.522  1.00 105.36 ? 28  PHE D CE2 1 
ATOM   9114  C CZ  . PHE D 2 28  ? 56.960  -38.111 16.667  1.00 105.13 ? 28  PHE D CZ  1 
ATOM   9115  N N   . ALA D 2 29  ? 56.977  -43.074 16.185  1.00 89.17  ? 29  ALA D N   1 
ATOM   9116  C CA  . ALA D 2 29  ? 57.062  -43.332 14.752  1.00 90.88  ? 29  ALA D CA  1 
ATOM   9117  C C   . ALA D 2 29  ? 57.985  -44.522 14.490  1.00 85.47  ? 29  ALA D C   1 
ATOM   9118  O O   . ALA D 2 29  ? 59.043  -44.401 13.868  1.00 85.40  ? 29  ALA D O   1 
ATOM   9119  C CB  . ALA D 2 29  ? 57.525  -42.084 13.994  1.00 95.06  ? 29  ALA D CB  1 
ATOM   9120  N N   . ASN D 2 30  ? 57.575  -45.671 15.039  1.00 84.92  ? 30  ASN D N   1 
ATOM   9121  C CA  . ASN D 2 30  ? 58.245  -46.963 14.904  1.00 86.59  ? 30  ASN D CA  1 
ATOM   9122  C C   . ASN D 2 30  ? 59.484  -47.061 15.785  1.00 85.22  ? 30  ASN D C   1 
ATOM   9123  O O   . ASN D 2 30  ? 59.692  -48.071 16.466  1.00 84.00  ? 30  ASN D O   1 
ATOM   9124  C CB  . ASN D 2 30  ? 58.616  -47.236 13.445  1.00 91.08  ? 30  ASN D CB  1 
ATOM   9125  C CG  . ASN D 2 30  ? 57.413  -47.576 12.596  1.00 96.47  ? 30  ASN D CG  1 
ATOM   9126  O OD1 . ASN D 2 30  ? 57.159  -48.743 12.309  1.00 100.14 ? 30  ASN D OD1 1 
ATOM   9127  N ND2 . ASN D 2 30  ? 56.657  -46.558 12.203  1.00 94.42  ? 30  ASN D ND2 1 
ATOM   9128  N N   . LYS D 2 31  ? 60.305  -46.025 15.783  1.00 88.09  ? 31  LYS D N   1 
ATOM   9129  C CA  . LYS D 2 31  ? 61.576  -46.074 16.487  1.00 83.23  ? 31  LYS D CA  1 
ATOM   9130  C C   . LYS D 2 31  ? 61.446  -45.477 17.883  1.00 86.21  ? 31  LYS D C   1 
ATOM   9131  O O   . LYS D 2 31  ? 60.654  -44.553 18.100  1.00 86.17  ? 31  LYS D O   1 
ATOM   9132  C CB  . LYS D 2 31  ? 62.639  -45.310 15.705  1.00 81.82  ? 31  LYS D CB  1 
ATOM   9133  C CG  . LYS D 2 31  ? 63.064  -46.004 14.425  1.00 81.24  ? 31  LYS D CG  1 
ATOM   9134  C CD  . LYS D 2 31  ? 63.585  -45.004 13.403  1.00 81.43  ? 31  LYS D CD  1 
ATOM   9135  C CE  . LYS D 2 31  ? 63.637  -45.617 12.008  1.00 81.94  ? 31  LYS D CE  1 
ATOM   9136  N NZ  . LYS D 2 31  ? 63.526  -44.604 10.918  1.00 81.67  ? 31  LYS D NZ  1 
ATOM   9137  N N   . PRO D 2 32  ? 62.189  -46.006 18.853  1.00 82.12  ? 32  PRO D N   1 
ATOM   9138  C CA  . PRO D 2 32  ? 62.203  -45.384 20.179  1.00 84.24  ? 32  PRO D CA  1 
ATOM   9139  C C   . PRO D 2 32  ? 62.675  -43.943 20.083  1.00 94.13  ? 32  PRO D C   1 
ATOM   9140  O O   . PRO D 2 32  ? 63.424  -43.570 19.177  1.00 94.20  ? 32  PRO D O   1 
ATOM   9141  C CB  . PRO D 2 32  ? 63.191  -46.248 20.968  1.00 87.27  ? 32  PRO D CB  1 
ATOM   9142  C CG  . PRO D 2 32  ? 63.169  -47.566 20.275  1.00 88.21  ? 32  PRO D CG  1 
ATOM   9143  C CD  . PRO D 2 32  ? 62.973  -47.251 18.818  1.00 84.97  ? 32  PRO D CD  1 
ATOM   9144  N N   . MET D 2 33  ? 62.229  -43.128 21.041  1.00 92.34  ? 33  MET D N   1 
ATOM   9145  C CA  . MET D 2 33  ? 62.547  -41.706 20.994  1.00 99.66  ? 33  MET D CA  1 
ATOM   9146  C C   . MET D 2 33  ? 64.040  -41.451 21.111  1.00 104.44 ? 33  MET D C   1 
ATOM   9147  O O   . MET D 2 33  ? 64.532  -40.420 20.639  1.00 105.08 ? 33  MET D O   1 
ATOM   9148  C CB  . MET D 2 33  ? 61.799  -40.947 22.086  1.00 98.58  ? 33  MET D CB  1 
ATOM   9149  C CG  . MET D 2 33  ? 60.627  -40.149 21.561  1.00 103.15 ? 33  MET D CG  1 
ATOM   9150  S SD  . MET D 2 33  ? 61.162  -39.057 20.223  1.00 118.85 ? 33  MET D SD  1 
ATOM   9151  C CE  . MET D 2 33  ? 62.353  -38.002 21.053  1.00 121.39 ? 33  MET D CE  1 
ATOM   9152  N N   . ILE D 2 34  ? 64.779  -42.372 21.729  1.00 104.79 ? 34  ILE D N   1 
ATOM   9153  C CA  . ILE D 2 34  ? 66.206  -42.146 21.915  1.00 107.41 ? 34  ILE D CA  1 
ATOM   9154  C C   . ILE D 2 34  ? 66.953  -42.300 20.594  1.00 108.03 ? 34  ILE D C   1 
ATOM   9155  O O   . ILE D 2 34  ? 68.008  -41.688 20.396  1.00 113.34 ? 34  ILE D O   1 
ATOM   9156  C CB  . ILE D 2 34  ? 66.752  -43.090 23.004  1.00 106.75 ? 34  ILE D CB  1 
ATOM   9157  C CG1 . ILE D 2 34  ? 68.136  -42.634 23.465  1.00 113.65 ? 34  ILE D CG1 1 
ATOM   9158  C CG2 . ILE D 2 34  ? 66.795  -44.528 22.508  1.00 106.43 ? 34  ILE D CG2 1 
ATOM   9159  C CD1 . ILE D 2 34  ? 68.138  -41.303 24.183  1.00 121.08 ? 34  ILE D CD1 1 
ATOM   9160  N N   . LEU D 2 35  ? 66.423  -43.098 19.668  1.00 106.56 ? 35  LEU D N   1 
ATOM   9161  C CA  . LEU D 2 35  ? 67.098  -43.338 18.399  1.00 108.32 ? 35  LEU D CA  1 
ATOM   9162  C C   . LEU D 2 35  ? 66.938  -42.195 17.401  1.00 114.38 ? 35  LEU D C   1 
ATOM   9163  O O   . LEU D 2 35  ? 67.625  -42.195 16.373  1.00 115.11 ? 35  LEU D O   1 
ATOM   9164  C CB  . LEU D 2 35  ? 66.586  -44.642 17.786  1.00 101.83 ? 35  LEU D CB  1 
ATOM   9165  C CG  . LEU D 2 35  ? 66.881  -45.872 18.646  1.00 105.13 ? 35  LEU D CG  1 
ATOM   9166  C CD1 . LEU D 2 35  ? 66.568  -47.156 17.895  1.00 109.06 ? 35  LEU D CD1 1 
ATOM   9167  C CD2 . LEU D 2 35  ? 68.327  -45.859 19.125  1.00 110.07 ? 35  LEU D CD2 1 
ATOM   9168  N N   . HIS D 2 36  ? 66.058  -41.227 17.672  1.00 121.89 ? 36  HIS D N   1 
ATOM   9169  C CA  . HIS D 2 36  ? 65.829  -40.151 16.712  1.00 120.40 ? 36  HIS D CA  1 
ATOM   9170  C C   . HIS D 2 36  ? 66.993  -39.172 16.663  1.00 122.18 ? 36  HIS D C   1 
ATOM   9171  O O   . HIS D 2 36  ? 67.229  -38.549 15.623  1.00 121.47 ? 36  HIS D O   1 
ATOM   9172  C CB  . HIS D 2 36  ? 64.537  -39.415 17.057  1.00 118.76 ? 36  HIS D CB  1 
ATOM   9173  C CG  . HIS D 2 36  ? 63.310  -40.250 16.881  1.00 117.72 ? 36  HIS D CG  1 
ATOM   9174  N ND1 . HIS D 2 36  ? 62.884  -41.144 17.837  1.00 117.84 ? 36  HIS D ND1 1 
ATOM   9175  C CD2 . HIS D 2 36  ? 62.419  -40.330 15.865  1.00 116.65 ? 36  HIS D CD2 1 
ATOM   9176  C CE1 . HIS D 2 36  ? 61.784  -41.742 17.418  1.00 117.73 ? 36  HIS D CE1 1 
ATOM   9177  N NE2 . HIS D 2 36  ? 61.480  -41.265 16.225  1.00 116.65 ? 36  HIS D NE2 1 
ATOM   9178  N N   . GLN D 2 37  ? 67.717  -39.007 17.768  1.00 133.94 ? 37  GLN D N   1 
ATOM   9179  C CA  . GLN D 2 37  ? 68.862  -38.112 17.803  1.00 135.18 ? 37  GLN D CA  1 
ATOM   9180  C C   . GLN D 2 37  ? 70.186  -38.834 17.992  1.00 136.39 ? 37  GLN D C   1 
ATOM   9181  O O   . GLN D 2 37  ? 71.238  -38.204 17.843  1.00 137.46 ? 37  GLN D O   1 
ATOM   9182  C CB  . GLN D 2 37  ? 68.690  -37.053 18.904  1.00 136.28 ? 37  GLN D CB  1 
ATOM   9183  C CG  . GLN D 2 37  ? 68.910  -37.545 20.321  1.00 138.48 ? 37  GLN D CG  1 
ATOM   9184  C CD  . GLN D 2 37  ? 67.810  -38.466 20.792  1.00 134.64 ? 37  GLN D CD  1 
ATOM   9185  O OE1 . GLN D 2 37  ? 66.628  -38.143 20.687  1.00 133.41 ? 37  GLN D OE1 1 
ATOM   9186  N NE2 . GLN D 2 37  ? 68.193  -39.611 21.340  1.00 134.68 ? 37  GLN D NE2 1 
ATOM   9187  N N   . ILE D 2 38  ? 70.168  -40.129 18.311  1.00 125.67 ? 38  ILE D N   1 
ATOM   9188  C CA  . ILE D 2 38  ? 71.414  -40.887 18.358  1.00 124.02 ? 38  ILE D CA  1 
ATOM   9189  C C   . ILE D 2 38  ? 71.939  -41.123 16.948  1.00 124.21 ? 38  ILE D C   1 
ATOM   9190  O O   . ILE D 2 38  ? 73.140  -40.979 16.685  1.00 127.59 ? 38  ILE D O   1 
ATOM   9191  C CB  . ILE D 2 38  ? 71.219  -42.210 19.119  1.00 120.45 ? 38  ILE D CB  1 
ATOM   9192  C CG1 . ILE D 2 38  ? 71.122  -41.955 20.623  1.00 117.35 ? 38  ILE D CG1 1 
ATOM   9193  C CG2 . ILE D 2 38  ? 72.359  -43.172 18.826  1.00 123.72 ? 38  ILE D CG2 1 
ATOM   9194  C CD1 . ILE D 2 38  ? 71.029  -43.223 21.437  1.00 115.39 ? 38  ILE D CD1 1 
ATOM   9195  N N   . GLU D 2 39  ? 71.053  -41.495 16.018  1.00 120.79 ? 39  GLU D N   1 
ATOM   9196  C CA  . GLU D 2 39  ? 71.468  -41.618 14.625  1.00 121.15 ? 39  GLU D CA  1 
ATOM   9197  C C   . GLU D 2 39  ? 71.860  -40.266 14.047  1.00 124.09 ? 39  GLU D C   1 
ATOM   9198  O O   . GLU D 2 39  ? 72.730  -40.195 13.171  1.00 126.87 ? 39  GLU D O   1 
ATOM   9199  C CB  . GLU D 2 39  ? 70.352  -42.252 13.791  1.00 124.91 ? 39  GLU D CB  1 
ATOM   9200  C CG  . GLU D 2 39  ? 70.791  -42.694 12.397  1.00 128.72 ? 39  GLU D CG  1 
ATOM   9201  C CD  . GLU D 2 39  ? 70.716  -41.581 11.363  1.00 133.24 ? 39  GLU D CD  1 
ATOM   9202  O OE1 . GLU D 2 39  ? 70.081  -40.541 11.643  1.00 135.00 ? 39  GLU D OE1 1 
ATOM   9203  O OE2 . GLU D 2 39  ? 71.303  -41.742 10.273  1.00 133.54 ? 39  GLU D OE2 1 
ATOM   9204  N N   . ALA D 2 40  ? 71.243  -39.186 14.532  1.00 124.60 ? 40  ALA D N   1 
ATOM   9205  C CA  . ALA D 2 40  ? 71.649  -37.854 14.103  1.00 126.63 ? 40  ALA D CA  1 
ATOM   9206  C C   . ALA D 2 40  ? 73.037  -37.508 14.623  1.00 129.06 ? 40  ALA D C   1 
ATOM   9207  O O   . ALA D 2 40  ? 73.773  -36.759 13.972  1.00 129.69 ? 40  ALA D O   1 
ATOM   9208  C CB  . ALA D 2 40  ? 70.627  -36.815 14.566  1.00 125.49 ? 40  ALA D CB  1 
ATOM   9209  N N   . LEU D 2 41  ? 73.412  -38.045 15.787  1.00 128.14 ? 41  LEU D N   1 
ATOM   9210  C CA  . LEU D 2 41  ? 74.771  -37.873 16.284  1.00 124.31 ? 41  LEU D CA  1 
ATOM   9211  C C   . LEU D 2 41  ? 75.776  -38.701 15.496  1.00 121.30 ? 41  LEU D C   1 
ATOM   9212  O O   . LEU D 2 41  ? 76.970  -38.386 15.515  1.00 121.67 ? 41  LEU D O   1 
ATOM   9213  C CB  . LEU D 2 41  ? 74.840  -38.238 17.769  1.00 124.60 ? 41  LEU D CB  1 
ATOM   9214  C CG  . LEU D 2 41  ? 74.165  -37.256 18.732  1.00 127.84 ? 41  LEU D CG  1 
ATOM   9215  C CD1 . LEU D 2 41  ? 74.127  -37.820 20.144  1.00 129.89 ? 41  LEU D CD1 1 
ATOM   9216  C CD2 . LEU D 2 41  ? 74.870  -35.909 18.709  1.00 140.51 ? 41  LEU D CD2 1 
ATOM   9217  N N   . LYS D 2 42  ? 75.325  -39.748 14.802  1.00 124.67 ? 42  LYS D N   1 
ATOM   9218  C CA  . LYS D 2 42  ? 76.204  -40.486 13.906  1.00 126.60 ? 42  LYS D CA  1 
ATOM   9219  C C   . LYS D 2 42  ? 76.423  -39.761 12.586  1.00 130.63 ? 42  LYS D C   1 
ATOM   9220  O O   . LYS D 2 42  ? 77.409  -40.042 11.894  1.00 127.50 ? 42  LYS D O   1 
ATOM   9221  C CB  . LYS D 2 42  ? 75.640  -41.884 13.641  1.00 126.74 ? 42  LYS D CB  1 
ATOM   9222  C CG  . LYS D 2 42  ? 76.594  -43.019 13.991  1.00 131.82 ? 42  LYS D CG  1 
ATOM   9223  C CD  . LYS D 2 42  ? 77.872  -42.953 13.169  1.00 138.72 ? 42  LYS D CD  1 
ATOM   9224  C CE  . LYS D 2 42  ? 78.828  -44.079 13.537  1.00 138.26 ? 42  LYS D CE  1 
ATOM   9225  N NZ  . LYS D 2 42  ? 79.270  -44.005 14.959  1.00 135.33 ? 42  LYS D NZ  1 
ATOM   9226  N N   . ALA D 2 43  ? 75.531  -38.836 12.223  1.00 127.40 ? 43  ALA D N   1 
ATOM   9227  C CA  . ALA D 2 43  ? 75.742  -38.041 11.018  1.00 127.78 ? 43  ALA D CA  1 
ATOM   9228  C C   . ALA D 2 43  ? 76.926  -37.097 11.173  1.00 130.79 ? 43  ALA D C   1 
ATOM   9229  O O   . ALA D 2 43  ? 77.540  -36.707 10.174  1.00 132.29 ? 43  ALA D O   1 
ATOM   9230  C CB  . ALA D 2 43  ? 74.477  -37.255 10.672  1.00 127.15 ? 43  ALA D CB  1 
ATOM   9231  N N   . VAL D 2 44  ? 77.260  -36.718 12.406  1.00 128.66 ? 44  VAL D N   1 
ATOM   9232  C CA  . VAL D 2 44  ? 78.435  -35.901 12.678  1.00 127.27 ? 44  VAL D CA  1 
ATOM   9233  C C   . VAL D 2 44  ? 79.585  -36.734 13.233  1.00 120.50 ? 44  VAL D C   1 
ATOM   9234  O O   . VAL D 2 44  ? 80.589  -36.177 13.685  1.00 121.94 ? 44  VAL D O   1 
ATOM   9235  C CB  . VAL D 2 44  ? 78.096  -34.737 13.621  1.00 129.71 ? 44  VAL D CB  1 
ATOM   9236  C CG1 . VAL D 2 44  ? 77.202  -33.731 12.918  1.00 146.38 ? 44  VAL D CG1 1 
ATOM   9237  C CG2 . VAL D 2 44  ? 77.424  -35.256 14.879  1.00 128.22 ? 44  VAL D CG2 1 
ATOM   9238  N N   . GLY D 2 45  ? 79.458  -38.059 13.212  1.00 116.13 ? 45  GLY D N   1 
ATOM   9239  C CA  . GLY D 2 45  ? 80.535  -38.938 13.622  1.00 117.42 ? 45  GLY D CA  1 
ATOM   9240  C C   . GLY D 2 45  ? 80.841  -38.893 15.104  1.00 120.97 ? 45  GLY D C   1 
ATOM   9241  O O   . GLY D 2 45  ? 82.006  -38.775 15.497  1.00 123.82 ? 45  GLY D O   1 
ATOM   9242  N N   . VAL D 2 46  ? 79.811  -38.993 15.938  1.00 119.54 ? 46  VAL D N   1 
ATOM   9243  C CA  . VAL D 2 46  ? 79.987  -39.049 17.384  1.00 119.95 ? 46  VAL D CA  1 
ATOM   9244  C C   . VAL D 2 46  ? 80.045  -40.509 17.808  1.00 121.09 ? 46  VAL D C   1 
ATOM   9245  O O   . VAL D 2 46  ? 79.135  -41.292 17.508  1.00 124.55 ? 46  VAL D O   1 
ATOM   9246  C CB  . VAL D 2 46  ? 78.854  -38.307 18.111  1.00 121.16 ? 46  VAL D CB  1 
ATOM   9247  C CG1 . VAL D 2 46  ? 78.957  -38.528 19.612  1.00 124.85 ? 46  VAL D CG1 1 
ATOM   9248  C CG2 . VAL D 2 46  ? 78.897  -36.824 17.789  1.00 123.19 ? 46  VAL D CG2 1 
ATOM   9249  N N   . ASP D 2 47  ? 81.116  -40.873 18.511  1.00 123.54 ? 47  ASP D N   1 
ATOM   9250  C CA  . ASP D 2 47  ? 81.347  -42.255 18.912  1.00 126.20 ? 47  ASP D CA  1 
ATOM   9251  C C   . ASP D 2 47  ? 80.706  -42.593 20.253  1.00 130.33 ? 47  ASP D C   1 
ATOM   9252  O O   . ASP D 2 47  ? 80.097  -43.658 20.392  1.00 132.93 ? 47  ASP D O   1 
ATOM   9253  C CB  . ASP D 2 47  ? 82.852  -42.543 18.965  1.00 123.09 ? 47  ASP D CB  1 
ATOM   9254  C CG  . ASP D 2 47  ? 83.690  -41.278 19.006  1.00 119.85 ? 47  ASP D CG  1 
ATOM   9255  O OD1 . ASP D 2 47  ? 83.406  -40.347 18.222  1.00 122.34 ? 47  ASP D OD1 1 
ATOM   9256  O OD2 . ASP D 2 47  ? 84.634  -41.214 19.822  1.00 111.25 ? 47  ASP D OD2 1 
ATOM   9257  N N   . GLU D 2 48  ? 80.827  -41.714 21.244  1.00 129.02 ? 48  GLU D N   1 
ATOM   9258  C CA  . GLU D 2 48  ? 80.349  -41.983 22.592  1.00 130.68 ? 48  GLU D CA  1 
ATOM   9259  C C   . GLU D 2 48  ? 79.226  -41.019 22.952  1.00 135.00 ? 48  GLU D C   1 
ATOM   9260  O O   . GLU D 2 48  ? 79.286  -39.830 22.625  1.00 135.08 ? 48  GLU D O   1 
ATOM   9261  C CB  . GLU D 2 48  ? 81.488  -41.868 23.613  1.00 126.45 ? 48  GLU D CB  1 
ATOM   9262  N N   . VAL D 2 49  ? 78.202  -41.542 23.627  1.00 142.12 ? 49  VAL D N   1 
ATOM   9263  C CA  . VAL D 2 49  ? 77.044  -40.763 24.058  1.00 139.61 ? 49  VAL D CA  1 
ATOM   9264  C C   . VAL D 2 49  ? 76.700  -41.157 25.489  1.00 142.99 ? 49  VAL D C   1 
ATOM   9265  O O   . VAL D 2 49  ? 76.606  -42.348 25.804  1.00 150.82 ? 49  VAL D O   1 
ATOM   9266  C CB  . VAL D 2 49  ? 75.823  -40.979 23.140  1.00 134.04 ? 49  VAL D CB  1 
ATOM   9267  C CG1 . VAL D 2 49  ? 74.631  -40.186 23.650  1.00 140.55 ? 49  VAL D CG1 1 
ATOM   9268  C CG2 . VAL D 2 49  ? 76.149  -40.585 21.705  1.00 127.75 ? 49  VAL D CG2 1 
ATOM   9269  N N   . VAL D 2 50  ? 76.511  -40.161 26.353  1.00 137.10 ? 50  VAL D N   1 
ATOM   9270  C CA  . VAL D 2 50  ? 76.173  -40.379 27.756  1.00 138.86 ? 50  VAL D CA  1 
ATOM   9271  C C   . VAL D 2 50  ? 74.750  -39.892 28.004  1.00 145.25 ? 50  VAL D C   1 
ATOM   9272  O O   . VAL D 2 50  ? 74.290  -38.919 27.395  1.00 150.82 ? 50  VAL D O   1 
ATOM   9273  C CB  . VAL D 2 50  ? 77.177  -39.675 28.695  1.00 139.61 ? 50  VAL D CB  1 
ATOM   9274  C CG1 . VAL D 2 50  ? 76.918  -40.052 30.147  1.00 132.20 ? 50  VAL D CG1 1 
ATOM   9275  C CG2 . VAL D 2 50  ? 78.605  -40.024 28.298  1.00 136.82 ? 50  VAL D CG2 1 
ATOM   9276  N N   . LEU D 2 51  ? 74.045  -40.589 28.894  1.00 139.52 ? 51  LEU D N   1 
ATOM   9277  C CA  . LEU D 2 51  ? 72.660  -40.283 29.238  1.00 140.03 ? 51  LEU D CA  1 
ATOM   9278  C C   . LEU D 2 51  ? 72.589  -39.810 30.685  1.00 138.94 ? 51  LEU D C   1 
ATOM   9279  O O   . LEU D 2 51  ? 72.992  -40.537 31.599  1.00 137.58 ? 51  LEU D O   1 
ATOM   9280  C CB  . LEU D 2 51  ? 71.761  -41.501 29.030  1.00 138.60 ? 51  LEU D CB  1 
ATOM   9281  C CG  . LEU D 2 51  ? 71.724  -42.080 27.614  1.00 140.41 ? 51  LEU D CG  1 
ATOM   9282  C CD1 . LEU D 2 51  ? 70.815  -43.296 27.563  1.00 141.81 ? 51  LEU D CD1 1 
ATOM   9283  C CD2 . LEU D 2 51  ? 71.273  -41.026 26.617  1.00 141.37 ? 51  LEU D CD2 1 
ATOM   9284  N N   . ALA D 2 52  ? 72.082  -38.593 30.888  1.00 142.63 ? 52  ALA D N   1 
ATOM   9285  C CA  . ALA D 2 52  ? 71.929  -38.025 32.230  1.00 145.41 ? 52  ALA D CA  1 
ATOM   9286  C C   . ALA D 2 52  ? 70.547  -38.371 32.790  1.00 140.60 ? 52  ALA D C   1 
ATOM   9287  O O   . ALA D 2 52  ? 69.641  -37.541 32.884  1.00 142.29 ? 52  ALA D O   1 
ATOM   9288  C CB  . ALA D 2 52  ? 72.164  -36.521 32.202  1.00 152.12 ? 52  ALA D CB  1 
ATOM   9289  N N   . ILE D 2 53  ? 70.400  -39.641 33.164  1.00 137.57 ? 53  ILE D N   1 
ATOM   9290  C CA  . ILE D 2 53  ? 69.147  -40.140 33.721  1.00 137.92 ? 53  ILE D CA  1 
ATOM   9291  C C   . ILE D 2 53  ? 69.137  -39.881 35.220  1.00 137.83 ? 53  ILE D C   1 
ATOM   9292  O O   . ILE D 2 53  ? 70.165  -39.528 35.806  1.00 136.41 ? 53  ILE D O   1 
ATOM   9293  C CB  . ILE D 2 53  ? 68.963  -41.638 33.427  1.00 136.71 ? 53  ILE D CB  1 
ATOM   9294  C CG1 . ILE D 2 53  ? 69.998  -42.451 34.207  1.00 132.28 ? 53  ILE D CG1 1 
ATOM   9295  C CG2 . ILE D 2 53  ? 69.093  -41.906 31.940  1.00 140.01 ? 53  ILE D CG2 1 
ATOM   9296  C CD1 . ILE D 2 53  ? 69.885  -43.936 34.003  1.00 130.85 ? 53  ILE D CD1 1 
ATOM   9297  N N   . ASN D 2 54  ? 67.978  -40.061 35.854  1.00 136.80 ? 54  ASN D N   1 
ATOM   9298  C CA  . ASN D 2 54  ? 67.868  -39.958 37.300  1.00 140.33 ? 54  ASN D CA  1 
ATOM   9299  C C   . ASN D 2 54  ? 67.442  -41.254 37.969  1.00 138.49 ? 54  ASN D C   1 
ATOM   9300  O O   . ASN D 2 54  ? 67.676  -41.413 39.172  1.00 136.73 ? 54  ASN D O   1 
ATOM   9301  C CB  . ASN D 2 54  ? 66.880  -38.847 37.692  1.00 144.37 ? 54  ASN D CB  1 
ATOM   9302  C CG  . ASN D 2 54  ? 66.926  -38.523 39.171  1.00 149.90 ? 54  ASN D CG  1 
ATOM   9303  O OD1 . ASN D 2 54  ? 67.835  -37.839 39.640  1.00 149.18 ? 54  ASN D OD1 1 
ATOM   9304  N ND2 . ASN D 2 54  ? 65.948  -39.022 39.916  1.00 152.23 ? 54  ASN D ND2 1 
ATOM   9305  N N   . TYR D 2 55  ? 66.842  -42.180 37.231  1.00 136.42 ? 55  TYR D N   1 
ATOM   9306  C CA  . TYR D 2 55  ? 66.447  -43.472 37.762  1.00 136.64 ? 55  TYR D CA  1 
ATOM   9307  C C   . TYR D 2 55  ? 67.574  -44.481 37.551  1.00 136.73 ? 55  TYR D C   1 
ATOM   9308  O O   . TYR D 2 55  ? 68.647  -44.159 37.037  1.00 134.53 ? 55  TYR D O   1 
ATOM   9309  C CB  . TYR D 2 55  ? 65.144  -43.937 37.111  1.00 132.31 ? 55  TYR D CB  1 
ATOM   9310  C CG  . TYR D 2 55  ? 65.226  -44.057 35.606  1.00 131.30 ? 55  TYR D CG  1 
ATOM   9311  C CD1 . TYR D 2 55  ? 64.994  -42.956 34.792  1.00 130.56 ? 55  TYR D CD1 1 
ATOM   9312  C CD2 . TYR D 2 55  ? 65.542  -45.265 34.999  1.00 131.93 ? 55  TYR D CD2 1 
ATOM   9313  C CE1 . TYR D 2 55  ? 65.072  -43.055 33.418  1.00 128.12 ? 55  TYR D CE1 1 
ATOM   9314  C CE2 . TYR D 2 55  ? 65.623  -45.374 33.624  1.00 128.51 ? 55  TYR D CE2 1 
ATOM   9315  C CZ  . TYR D 2 55  ? 65.386  -44.264 32.838  1.00 124.81 ? 55  TYR D CZ  1 
ATOM   9316  O OH  . TYR D 2 55  ? 65.465  -44.362 31.468  1.00 120.41 ? 55  TYR D OH  1 
ATOM   9317  N N   . GLN D 2 56  ? 67.330  -45.714 37.951  1.00 144.94 ? 56  GLN D N   1 
ATOM   9318  C CA  . GLN D 2 56  ? 68.340  -46.756 37.817  1.00 146.21 ? 56  GLN D CA  1 
ATOM   9319  C C   . GLN D 2 56  ? 68.360  -47.288 36.387  1.00 147.76 ? 56  GLN D C   1 
ATOM   9320  O O   . GLN D 2 56  ? 67.307  -47.637 35.845  1.00 147.29 ? 56  GLN D O   1 
ATOM   9321  C CB  . GLN D 2 56  ? 68.083  -47.889 38.815  1.00 148.52 ? 56  GLN D CB  1 
ATOM   9322  C CG  . GLN D 2 56  ? 66.768  -48.654 38.635  1.00 156.84 ? 56  GLN D CG  1 
ATOM   9323  C CD  . GLN D 2 56  ? 65.538  -47.813 38.936  1.00 158.01 ? 56  GLN D CD  1 
ATOM   9324  O OE1 . GLN D 2 56  ? 65.614  -46.810 39.647  1.00 158.11 ? 56  GLN D OE1 1 
ATOM   9325  N NE2 . GLN D 2 56  ? 64.397  -48.217 38.389  1.00 151.83 ? 56  GLN D NE2 1 
ATOM   9326  N N   . PRO D 2 57  ? 69.527  -47.350 35.741  1.00 143.02 ? 57  PRO D N   1 
ATOM   9327  C CA  . PRO D 2 57  ? 69.589  -47.827 34.354  1.00 143.62 ? 57  PRO D CA  1 
ATOM   9328  C C   . PRO D 2 57  ? 69.481  -49.335 34.208  1.00 146.70 ? 57  PRO D C   1 
ATOM   9329  O O   . PRO D 2 57  ? 69.569  -49.836 33.081  1.00 145.32 ? 57  PRO D O   1 
ATOM   9330  C CB  . PRO D 2 57  ? 70.967  -47.336 33.893  1.00 143.10 ? 57  PRO D CB  1 
ATOM   9331  C CG  . PRO D 2 57  ? 71.788  -47.358 35.135  1.00 143.92 ? 57  PRO D CG  1 
ATOM   9332  C CD  . PRO D 2 57  ? 70.854  -46.966 36.255  1.00 142.56 ? 57  PRO D CD  1 
ATOM   9333  N N   . GLU D 2 58  ? 69.279  -50.066 35.306  1.00 150.31 ? 58  GLU D N   1 
ATOM   9334  C CA  . GLU D 2 58  ? 69.268  -51.524 35.263  1.00 152.11 ? 58  GLU D CA  1 
ATOM   9335  C C   . GLU D 2 58  ? 68.153  -52.077 34.383  1.00 155.77 ? 58  GLU D C   1 
ATOM   9336  O O   . GLU D 2 58  ? 68.238  -53.229 33.944  1.00 152.96 ? 58  GLU D O   1 
ATOM   9337  C CB  . GLU D 2 58  ? 69.138  -52.070 36.685  1.00 154.17 ? 58  GLU D CB  1 
ATOM   9338  C CG  . GLU D 2 58  ? 70.137  -51.462 37.657  1.00 154.07 ? 58  GLU D CG  1 
ATOM   9339  C CD  . GLU D 2 58  ? 69.554  -51.251 39.040  1.00 153.39 ? 58  GLU D CD  1 
ATOM   9340  O OE1 . GLU D 2 58  ? 68.366  -51.578 39.243  1.00 152.91 ? 58  GLU D OE1 1 
ATOM   9341  O OE2 . GLU D 2 58  ? 70.281  -50.752 39.923  1.00 151.87 ? 58  GLU D OE2 1 
ATOM   9342  N N   . VAL D 2 59  ? 67.116  -51.284 34.113  1.00 175.33 ? 59  VAL D N   1 
ATOM   9343  C CA  . VAL D 2 59  ? 65.977  -51.761 33.336  1.00 175.80 ? 59  VAL D CA  1 
ATOM   9344  C C   . VAL D 2 59  ? 66.156  -51.592 31.830  1.00 174.35 ? 59  VAL D C   1 
ATOM   9345  O O   . VAL D 2 59  ? 65.458  -52.261 31.057  1.00 174.26 ? 59  VAL D O   1 
ATOM   9346  C CB  . VAL D 2 59  ? 64.686  -51.052 33.782  1.00 178.26 ? 59  VAL D CB  1 
ATOM   9347  C CG1 . VAL D 2 59  ? 64.387  -51.370 35.238  1.00 176.78 ? 59  VAL D CG1 1 
ATOM   9348  C CG2 . VAL D 2 59  ? 64.809  -49.550 33.578  1.00 174.29 ? 59  VAL D CG2 1 
ATOM   9349  N N   . MET D 2 60  ? 67.066  -50.722 31.390  1.00 153.71 ? 60  MET D N   1 
ATOM   9350  C CA  . MET D 2 60  ? 67.248  -50.441 29.971  1.00 140.95 ? 60  MET D CA  1 
ATOM   9351  C C   . MET D 2 60  ? 68.633  -50.827 29.470  1.00 137.09 ? 60  MET D C   1 
ATOM   9352  O O   . MET D 2 60  ? 68.995  -50.466 28.344  1.00 136.06 ? 60  MET D O   1 
ATOM   9353  C CB  . MET D 2 60  ? 66.997  -48.957 29.680  1.00 136.89 ? 60  MET D CB  1 
ATOM   9354  C CG  . MET D 2 60  ? 67.983  -48.023 30.356  1.00 137.42 ? 60  MET D CG  1 
ATOM   9355  S SD  . MET D 2 60  ? 67.543  -46.288 30.156  1.00 127.95 ? 60  MET D SD  1 
ATOM   9356  C CE  . MET D 2 60  ? 68.990  -45.494 30.850  1.00 132.78 ? 60  MET D CE  1 
ATOM   9357  N N   . LEU D 2 61  ? 69.415  -51.549 30.275  1.00 135.46 ? 61  LEU D N   1 
ATOM   9358  C CA  . LEU D 2 61  ? 70.760  -51.931 29.856  1.00 131.66 ? 61  LEU D CA  1 
ATOM   9359  C C   . LEU D 2 61  ? 70.729  -52.828 28.624  1.00 128.75 ? 61  LEU D C   1 
ATOM   9360  O O   . LEU D 2 61  ? 71.600  -52.725 27.752  1.00 130.78 ? 61  LEU D O   1 
ATOM   9361  C CB  . LEU D 2 61  ? 71.488  -52.625 31.007  1.00 133.27 ? 61  LEU D CB  1 
ATOM   9362  C CG  . LEU D 2 61  ? 71.951  -51.723 32.153  1.00 137.75 ? 61  LEU D CG  1 
ATOM   9363  C CD1 . LEU D 2 61  ? 72.679  -52.526 33.221  1.00 141.94 ? 61  LEU D CD1 1 
ATOM   9364  C CD2 . LEU D 2 61  ? 72.830  -50.599 31.627  1.00 136.69 ? 61  LEU D CD2 1 
ATOM   9365  N N   . ASN D 2 62  ? 69.735  -53.715 28.532  1.00 126.82 ? 62  ASN D N   1 
ATOM   9366  C CA  . ASN D 2 62  ? 69.647  -54.596 27.372  1.00 122.96 ? 62  ASN D CA  1 
ATOM   9367  C C   . ASN D 2 62  ? 69.295  -53.833 26.103  1.00 125.38 ? 62  ASN D C   1 
ATOM   9368  O O   . ASN D 2 62  ? 69.746  -54.207 25.015  1.00 127.53 ? 62  ASN D O   1 
ATOM   9369  C CB  . ASN D 2 62  ? 68.623  -55.701 27.626  1.00 119.97 ? 62  ASN D CB  1 
ATOM   9370  C CG  . ASN D 2 62  ? 69.147  -56.777 28.557  1.00 116.35 ? 62  ASN D CG  1 
ATOM   9371  O OD1 . ASN D 2 62  ? 70.338  -57.090 28.559  1.00 111.76 ? 62  ASN D OD1 1 
ATOM   9372  N ND2 . ASN D 2 62  ? 68.256  -57.349 29.357  1.00 112.44 ? 62  ASN D ND2 1 
ATOM   9373  N N   . PHE D 2 63  ? 68.512  -52.759 26.214  1.00 125.70 ? 63  PHE D N   1 
ATOM   9374  C CA  . PHE D 2 63  ? 68.134  -51.997 25.027  1.00 129.38 ? 63  PHE D CA  1 
ATOM   9375  C C   . PHE D 2 63  ? 69.296  -51.150 24.526  1.00 135.40 ? 63  PHE D C   1 
ATOM   9376  O O   . PHE D 2 63  ? 69.573  -51.107 23.322  1.00 133.15 ? 63  PHE D O   1 
ATOM   9377  C CB  . PHE D 2 63  ? 66.925  -51.112 25.333  1.00 126.71 ? 63  PHE D CB  1 
ATOM   9378  C CG  . PHE D 2 63  ? 65.650  -51.874 25.545  1.00 118.61 ? 63  PHE D CG  1 
ATOM   9379  C CD1 . PHE D 2 63  ? 64.783  -52.108 24.492  1.00 110.81 ? 63  PHE D CD1 1 
ATOM   9380  C CD2 . PHE D 2 63  ? 65.319  -52.354 26.801  1.00 121.09 ? 63  PHE D CD2 1 
ATOM   9381  C CE1 . PHE D 2 63  ? 63.607  -52.808 24.688  1.00 113.23 ? 63  PHE D CE1 1 
ATOM   9382  C CE2 . PHE D 2 63  ? 64.145  -53.053 27.003  1.00 120.77 ? 63  PHE D CE2 1 
ATOM   9383  C CZ  . PHE D 2 63  ? 63.289  -53.281 25.946  1.00 118.27 ? 63  PHE D CZ  1 
ATOM   9384  N N   . LEU D 2 64  ? 69.988  -50.469 25.441  1.00 167.17 ? 64  LEU D N   1 
ATOM   9385  C CA  . LEU D 2 64  ? 71.117  -49.636 25.047  1.00 168.08 ? 64  LEU D CA  1 
ATOM   9386  C C   . LEU D 2 64  ? 72.292  -50.480 24.577  1.00 169.53 ? 64  LEU D C   1 
ATOM   9387  O O   . LEU D 2 64  ? 73.129  -50.004 23.802  1.00 169.97 ? 64  LEU D O   1 
ATOM   9388  C CB  . LEU D 2 64  ? 71.523  -48.734 26.211  1.00 169.60 ? 64  LEU D CB  1 
ATOM   9389  C CG  . LEU D 2 64  ? 70.353  -47.936 26.796  1.00 167.00 ? 64  LEU D CG  1 
ATOM   9390  C CD1 . LEU D 2 64  ? 70.807  -47.071 27.958  1.00 167.31 ? 64  LEU D CD1 1 
ATOM   9391  C CD2 . LEU D 2 64  ? 69.674  -47.097 25.722  1.00 166.65 ? 64  LEU D CD2 1 
ATOM   9392  N N   . LYS D 2 65  ? 72.370  -51.730 25.037  1.00 144.58 ? 65  LYS D N   1 
ATOM   9393  C CA  . LYS D 2 65  ? 73.437  -52.622 24.606  1.00 141.74 ? 65  LYS D CA  1 
ATOM   9394  C C   . LYS D 2 65  ? 73.205  -53.102 23.179  1.00 141.75 ? 65  LYS D C   1 
ATOM   9395  O O   . LYS D 2 65  ? 74.163  -53.441 22.474  1.00 145.43 ? 65  LYS D O   1 
ATOM   9396  C CB  . LYS D 2 65  ? 73.525  -53.812 25.562  1.00 135.15 ? 65  LYS D CB  1 
ATOM   9397  C CG  . LYS D 2 65  ? 74.857  -54.528 25.600  1.00 131.68 ? 65  LYS D CG  1 
ATOM   9398  C CD  . LYS D 2 65  ? 74.843  -55.589 26.691  1.00 126.76 ? 65  LYS D CD  1 
ATOM   9399  C CE  . LYS D 2 65  ? 74.416  -55.010 28.033  1.00 118.36 ? 65  LYS D CE  1 
ATOM   9400  N NZ  . LYS D 2 65  ? 74.301  -56.057 29.090  1.00 110.24 ? 65  LYS D NZ  1 
ATOM   9401  N N   . ASP D 2 66  ? 71.944  -53.139 22.742  1.00 136.26 ? 66  ASP D N   1 
ATOM   9402  C CA  . ASP D 2 66  ? 71.612  -53.559 21.388  1.00 135.98 ? 66  ASP D CA  1 
ATOM   9403  C C   . ASP D 2 66  ? 71.766  -52.438 20.370  1.00 135.94 ? 66  ASP D C   1 
ATOM   9404  O O   . ASP D 2 66  ? 71.797  -52.714 19.165  1.00 132.88 ? 66  ASP D O   1 
ATOM   9405  C CB  . ASP D 2 66  ? 70.178  -54.093 21.339  1.00 132.83 ? 66  ASP D CB  1 
ATOM   9406  C CG  . ASP D 2 66  ? 69.981  -55.314 22.213  1.00 134.14 ? 66  ASP D CG  1 
ATOM   9407  O OD1 . ASP D 2 66  ? 70.962  -56.058 22.427  1.00 137.36 ? 66  ASP D OD1 1 
ATOM   9408  O OD2 . ASP D 2 66  ? 68.846  -55.533 22.687  1.00 133.54 ? 66  ASP D OD2 1 
ATOM   9409  N N   . PHE D 2 67  ? 71.858  -51.189 20.820  1.00 143.13 ? 67  PHE D N   1 
ATOM   9410  C CA  . PHE D 2 67  ? 72.029  -50.063 19.914  1.00 142.05 ? 67  PHE D CA  1 
ATOM   9411  C C   . PHE D 2 67  ? 73.488  -49.692 19.706  1.00 147.21 ? 67  PHE D C   1 
ATOM   9412  O O   . PHE D 2 67  ? 73.797  -48.948 18.769  1.00 143.87 ? 67  PHE D O   1 
ATOM   9413  C CB  . PHE D 2 67  ? 71.273  -48.837 20.441  1.00 138.44 ? 67  PHE D CB  1 
ATOM   9414  C CG  . PHE D 2 67  ? 69.789  -49.040 20.564  1.00 130.70 ? 67  PHE D CG  1 
ATOM   9415  C CD1 . PHE D 2 67  ? 69.126  -49.958 19.764  1.00 128.26 ? 67  PHE D CD1 1 
ATOM   9416  C CD2 . PHE D 2 67  ? 69.060  -48.315 21.490  1.00 126.01 ? 67  PHE D CD2 1 
ATOM   9417  C CE1 . PHE D 2 67  ? 67.759  -50.141 19.885  1.00 125.98 ? 67  PHE D CE1 1 
ATOM   9418  C CE2 . PHE D 2 67  ? 67.696  -48.492 21.615  1.00 123.72 ? 67  PHE D CE2 1 
ATOM   9419  C CZ  . PHE D 2 67  ? 67.044  -49.407 20.811  1.00 121.63 ? 67  PHE D CZ  1 
ATOM   9420  N N   . GLU D 2 68  ? 74.386  -50.193 20.557  1.00 176.08 ? 68  GLU D N   1 
ATOM   9421  C CA  . GLU D 2 68  ? 75.801  -49.865 20.429  1.00 177.56 ? 68  GLU D CA  1 
ATOM   9422  C C   . GLU D 2 68  ? 76.444  -50.569 19.242  1.00 178.56 ? 68  GLU D C   1 
ATOM   9423  O O   . GLU D 2 68  ? 77.351  -50.014 18.612  1.00 179.22 ? 68  GLU D O   1 
ATOM   9424  C CB  . GLU D 2 68  ? 76.534  -50.221 21.722  1.00 178.68 ? 68  GLU D CB  1 
ATOM   9425  C CG  . GLU D 2 68  ? 76.247  -49.271 22.872  1.00 179.56 ? 68  GLU D CG  1 
ATOM   9426  C CD  . GLU D 2 68  ? 77.093  -49.564 24.091  1.00 181.85 ? 68  GLU D CD  1 
ATOM   9427  O OE1 . GLU D 2 68  ? 77.096  -50.726 24.549  1.00 181.07 ? 68  GLU D OE1 1 
ATOM   9428  O OE2 . GLU D 2 68  ? 77.761  -48.635 24.590  1.00 184.34 ? 68  GLU D OE2 1 
ATOM   9429  N N   . THR D 2 69  ? 76.000  -51.783 18.925  1.00 151.78 ? 69  THR D N   1 
ATOM   9430  C CA  . THR D 2 69  ? 76.548  -52.522 17.795  1.00 146.33 ? 69  THR D CA  1 
ATOM   9431  C C   . THR D 2 69  ? 75.829  -52.198 16.493  1.00 142.64 ? 69  THR D C   1 
ATOM   9432  O O   . THR D 2 69  ? 76.465  -52.115 15.437  1.00 138.71 ? 69  THR D O   1 
ATOM   9433  C CB  . THR D 2 69  ? 76.479  -54.028 18.063  1.00 140.48 ? 69  THR D CB  1 
ATOM   9434  O OG1 . THR D 2 69  ? 75.439  -54.298 19.011  1.00 138.04 ? 69  THR D OG1 1 
ATOM   9435  C CG2 . THR D 2 69  ? 77.808  -54.533 18.608  1.00 136.81 ? 69  THR D CG2 1 
ATOM   9436  N N   . LYS D 2 70  ? 74.508  -52.020 16.553  1.00 144.21 ? 70  LYS D N   1 
ATOM   9437  C CA  . LYS D 2 70  ? 73.745  -51.689 15.355  1.00 147.14 ? 70  LYS D CA  1 
ATOM   9438  C C   . LYS D 2 70  ? 74.138  -50.322 14.810  1.00 145.03 ? 70  LYS D C   1 
ATOM   9439  O O   . LYS D 2 70  ? 74.223  -50.131 13.591  1.00 145.85 ? 70  LYS D O   1 
ATOM   9440  C CB  . LYS D 2 70  ? 72.249  -51.737 15.668  1.00 144.87 ? 70  LYS D CB  1 
ATOM   9441  C CG  . LYS D 2 70  ? 71.347  -51.358 14.506  1.00 144.37 ? 70  LYS D CG  1 
ATOM   9442  C CD  . LYS D 2 70  ? 69.902  -51.243 14.964  1.00 145.52 ? 70  LYS D CD  1 
ATOM   9443  C CE  . LYS D 2 70  ? 69.764  -50.205 16.069  1.00 142.97 ? 70  LYS D CE  1 
ATOM   9444  N NZ  . LYS D 2 70  ? 68.366  -50.101 16.571  1.00 142.34 ? 70  LYS D NZ  1 
ATOM   9445  N N   . LEU D 2 71  ? 74.384  -49.359 15.697  1.00 141.68 ? 71  LEU D N   1 
ATOM   9446  C CA  . LEU D 2 71  ? 74.694  -47.995 15.298  1.00 136.57 ? 71  LEU D CA  1 
ATOM   9447  C C   . LEU D 2 71  ? 76.177  -47.655 15.391  1.00 136.30 ? 71  LEU D C   1 
ATOM   9448  O O   . LEU D 2 71  ? 76.570  -46.569 14.952  1.00 135.38 ? 71  LEU D O   1 
ATOM   9449  C CB  . LEU D 2 71  ? 73.889  -47.008 16.152  1.00 134.18 ? 71  LEU D CB  1 
ATOM   9450  C CG  . LEU D 2 71  ? 72.369  -47.176 16.075  1.00 137.37 ? 71  LEU D CG  1 
ATOM   9451  C CD1 . LEU D 2 71  ? 71.666  -46.215 17.019  1.00 133.10 ? 71  LEU D CD1 1 
ATOM   9452  C CD2 . LEU D 2 71  ? 71.874  -46.982 14.649  1.00 136.06 ? 71  LEU D CD2 1 
ATOM   9453  N N   . GLU D 2 72  ? 76.999  -48.549 15.938  1.00 137.38 ? 72  GLU D N   1 
ATOM   9454  C CA  . GLU D 2 72  ? 78.430  -48.310 16.133  1.00 139.09 ? 72  GLU D CA  1 
ATOM   9455  C C   . GLU D 2 72  ? 78.664  -47.025 16.930  1.00 139.39 ? 72  GLU D C   1 
ATOM   9456  O O   . GLU D 2 72  ? 79.285  -46.068 16.461  1.00 137.36 ? 72  GLU D O   1 
ATOM   9457  C CB  . GLU D 2 72  ? 79.174  -48.273 14.795  1.00 137.93 ? 72  GLU D CB  1 
ATOM   9458  C CG  . GLU D 2 72  ? 79.336  -49.627 14.130  1.00 137.35 ? 72  GLU D CG  1 
ATOM   9459  C CD  . GLU D 2 72  ? 80.189  -49.558 12.878  1.00 135.07 ? 72  GLU D CD  1 
ATOM   9460  O OE1 . GLU D 2 72  ? 80.312  -48.458 12.297  1.00 134.86 ? 72  GLU D OE1 1 
ATOM   9461  O OE2 . GLU D 2 72  ? 80.739  -50.604 12.477  1.00 132.99 ? 72  GLU D OE2 1 
ATOM   9462  N N   . ILE D 2 73  ? 78.153  -47.027 18.160  1.00 141.25 ? 73  ILE D N   1 
ATOM   9463  C CA  . ILE D 2 73  ? 78.224  -45.876 19.052  1.00 140.67 ? 73  ILE D CA  1 
ATOM   9464  C C   . ILE D 2 73  ? 78.407  -46.383 20.475  1.00 149.88 ? 73  ILE D C   1 
ATOM   9465  O O   . ILE D 2 73  ? 77.785  -47.371 20.875  1.00 158.01 ? 73  ILE D O   1 
ATOM   9466  C CB  . ILE D 2 73  ? 76.960  -44.994 18.936  1.00 141.93 ? 73  ILE D CB  1 
ATOM   9467  C CG1 . ILE D 2 73  ? 77.075  -44.050 17.740  1.00 139.55 ? 73  ILE D CG1 1 
ATOM   9468  C CG2 . ILE D 2 73  ? 76.713  -44.208 20.224  1.00 141.30 ? 73  ILE D CG2 1 
ATOM   9469  C CD1 . ILE D 2 73  ? 75.938  -43.063 17.622  1.00 131.91 ? 73  ILE D CD1 1 
ATOM   9470  N N   . LYS D 2 74  ? 79.257  -45.704 21.241  1.00 146.53 ? 74  LYS D N   1 
ATOM   9471  C CA  . LYS D 2 74  ? 79.476  -46.037 22.643  1.00 156.17 ? 74  LYS D CA  1 
ATOM   9472  C C   . LYS D 2 74  ? 78.406  -45.353 23.487  1.00 163.98 ? 74  LYS D C   1 
ATOM   9473  O O   . LYS D 2 74  ? 78.241  -44.131 23.416  1.00 154.80 ? 74  LYS D O   1 
ATOM   9474  C CB  . LYS D 2 74  ? 80.875  -45.613 23.089  1.00 151.18 ? 74  LYS D CB  1 
ATOM   9475  C CG  . LYS D 2 74  ? 81.248  -46.064 24.491  1.00 152.41 ? 74  LYS D CG  1 
ATOM   9476  C CD  . LYS D 2 74  ? 81.240  -47.581 24.598  1.00 155.65 ? 74  LYS D CD  1 
ATOM   9477  C CE  . LYS D 2 74  ? 81.715  -48.047 25.965  1.00 151.92 ? 74  LYS D CE  1 
ATOM   9478  N NZ  . LYS D 2 74  ? 83.102  -47.588 26.257  1.00 153.64 ? 74  LYS D NZ  1 
ATOM   9479  N N   . ILE D 2 75  ? 77.673  -46.138 24.270  1.00 208.33 ? 75  ILE D N   1 
ATOM   9480  C CA  . ILE D 2 75  ? 76.563  -45.635 25.072  1.00 206.77 ? 75  ILE D CA  1 
ATOM   9481  C C   . ILE D 2 75  ? 76.812  -46.005 26.527  1.00 207.65 ? 75  ILE D C   1 
ATOM   9482  O O   . ILE D 2 75  ? 76.843  -47.192 26.876  1.00 208.53 ? 75  ILE D O   1 
ATOM   9483  C CB  . ILE D 2 75  ? 75.216  -46.194 24.588  1.00 205.49 ? 75  ILE D CB  1 
ATOM   9484  C CG1 . ILE D 2 75  ? 74.977  -45.812 23.125  1.00 205.14 ? 75  ILE D CG1 1 
ATOM   9485  C CG2 . ILE D 2 75  ? 74.085  -45.683 25.467  1.00 204.22 ? 75  ILE D CG2 1 
ATOM   9486  C CD1 . ILE D 2 75  ? 73.707  -46.385 22.540  1.00 204.16 ? 75  ILE D CD1 1 
ATOM   9487  N N   . THR D 2 76  ? 76.982  -44.991 27.374  1.00 167.49 ? 76  THR D N   1 
ATOM   9488  C CA  . THR D 2 76  ? 77.159  -45.186 28.805  1.00 150.69 ? 76  THR D CA  1 
ATOM   9489  C C   . THR D 2 76  ? 76.183  -44.297 29.561  1.00 141.25 ? 76  THR D C   1 
ATOM   9490  O O   . THR D 2 76  ? 75.788  -43.232 29.080  1.00 142.13 ? 76  THR D O   1 
ATOM   9491  C CB  . THR D 2 76  ? 78.596  -44.879 29.248  1.00 140.58 ? 76  THR D CB  1 
ATOM   9492  O OG1 . THR D 2 76  ? 78.951  -43.553 28.837  1.00 140.65 ? 76  THR D OG1 1 
ATOM   9493  C CG2 . THR D 2 76  ? 79.569  -45.877 28.637  1.00 142.40 ? 76  THR D CG2 1 
ATOM   9494  N N   . CYS D 2 77  ? 75.797  -44.746 30.751  1.00 131.58 ? 77  CYS D N   1 
ATOM   9495  C CA  . CYS D 2 77  ? 74.803  -44.063 31.565  1.00 126.68 ? 77  CYS D CA  1 
ATOM   9496  C C   . CYS D 2 77  ? 75.447  -43.368 32.759  1.00 125.18 ? 77  CYS D C   1 
ATOM   9497  O O   . CYS D 2 77  ? 76.530  -43.740 33.221  1.00 125.05 ? 77  CYS D O   1 
ATOM   9498  C CB  . CYS D 2 77  ? 73.730  -45.042 32.052  1.00 125.46 ? 77  CYS D CB  1 
ATOM   9499  S SG  . CYS D 2 77  ? 72.740  -45.768 30.728  1.00 132.27 ? 77  CYS D SG  1 
ATOM   9500  N N   . SER D 2 78  ? 74.755  -42.342 33.253  1.00 125.85 ? 78  SER D N   1 
ATOM   9501  C CA  . SER D 2 78  ? 75.143  -41.643 34.473  1.00 126.44 ? 78  SER D CA  1 
ATOM   9502  C C   . SER D 2 78  ? 73.895  -41.425 35.313  1.00 130.10 ? 78  SER D C   1 
ATOM   9503  O O   . SER D 2 78  ? 72.931  -40.813 34.845  1.00 134.30 ? 78  SER D O   1 
ATOM   9504  C CB  . SER D 2 78  ? 75.822  -40.306 34.161  1.00 129.56 ? 78  SER D CB  1 
ATOM   9505  O OG  . SER D 2 78  ? 74.905  -39.387 33.591  1.00 131.80 ? 78  SER D OG  1 
ATOM   9506  N N   . GLN D 2 79  ? 73.914  -41.918 36.548  1.00 129.88 ? 79  GLN D N   1 
ATOM   9507  C CA  . GLN D 2 79  ? 72.777  -41.822 37.455  1.00 132.59 ? 79  GLN D CA  1 
ATOM   9508  C C   . GLN D 2 79  ? 73.154  -40.913 38.614  1.00 131.57 ? 79  GLN D C   1 
ATOM   9509  O O   . GLN D 2 79  ? 74.150  -41.159 39.302  1.00 131.68 ? 79  GLN D O   1 
ATOM   9510  C CB  . GLN D 2 79  ? 72.362  -43.199 37.973  1.00 134.68 ? 79  GLN D CB  1 
ATOM   9511  C CG  . GLN D 2 79  ? 71.151  -43.169 38.895  1.00 136.53 ? 79  GLN D CG  1 
ATOM   9512  C CD  . GLN D 2 79  ? 70.815  -44.533 39.469  1.00 137.75 ? 79  GLN D CD  1 
ATOM   9513  O OE1 . GLN D 2 79  ? 71.514  -45.515 39.220  1.00 139.08 ? 79  GLN D OE1 1 
ATOM   9514  N NE2 . GLN D 2 79  ? 69.741  -44.598 40.248  1.00 136.16 ? 79  GLN D NE2 1 
ATOM   9515  N N   . GLU D 2 80  ? 72.359  -39.872 38.828  1.00 131.41 ? 80  GLU D N   1 
ATOM   9516  C CA  . GLU D 2 80  ? 72.568  -38.946 39.928  1.00 133.33 ? 80  GLU D CA  1 
ATOM   9517  C C   . GLU D 2 80  ? 71.615  -39.273 41.068  1.00 133.44 ? 80  GLU D C   1 
ATOM   9518  O O   . GLU D 2 80  ? 70.488  -39.724 40.851  1.00 135.61 ? 80  GLU D O   1 
ATOM   9519  C CB  . GLU D 2 80  ? 72.358  -37.496 39.480  1.00 139.90 ? 80  GLU D CB  1 
ATOM   9520  C CG  . GLU D 2 80  ? 73.424  -36.958 38.535  1.00 141.84 ? 80  GLU D CG  1 
ATOM   9521  C CD  . GLU D 2 80  ? 73.282  -37.484 37.119  1.00 140.42 ? 80  GLU D CD  1 
ATOM   9522  O OE1 . GLU D 2 80  ? 72.279  -38.171 36.833  1.00 135.85 ? 80  GLU D OE1 1 
ATOM   9523  O OE2 . GLU D 2 80  ? 74.178  -37.217 36.291  1.00 142.07 ? 80  GLU D OE2 1 
ATOM   9524  N N   . THR D 2 81  ? 72.087  -39.044 42.295  1.00 134.80 ? 81  THR D N   1 
ATOM   9525  C CA  . THR D 2 81  ? 71.241  -39.257 43.463  1.00 134.36 ? 81  THR D CA  1 
ATOM   9526  C C   . THR D 2 81  ? 70.025  -38.339 43.424  1.00 141.17 ? 81  THR D C   1 
ATOM   9527  O O   . THR D 2 81  ? 68.890  -38.781 43.632  1.00 140.59 ? 81  THR D O   1 
ATOM   9528  C CB  . THR D 2 81  ? 72.049  -39.044 44.743  1.00 122.87 ? 81  THR D CB  1 
ATOM   9529  O OG1 . THR D 2 81  ? 72.675  -37.755 44.704  1.00 120.26 ? 81  THR D OG1 1 
ATOM   9530  C CG2 . THR D 2 81  ? 73.117  -40.118 44.886  1.00 108.57 ? 81  THR D CG2 1 
ATOM   9531  N N   . GLU D 2 82  ? 70.258  -37.116 42.946  1.00 142.71 ? 82  GLU D N   1 
ATOM   9532  C CA  . GLU D 2 82  ? 69.140  -36.160 42.735  1.00 153.33 ? 82  GLU D CA  1 
ATOM   9533  C C   . GLU D 2 82  ? 69.463  -35.399 41.443  1.00 163.74 ? 82  GLU D C   1 
ATOM   9534  O O   . GLU D 2 82  ? 70.659  -35.157 41.201  1.00 162.75 ? 82  GLU D O   1 
ATOM   9535  C CB  . GLU D 2 82  ? 69.011  -35.213 43.928  1.00 149.36 ? 82  GLU D CB  1 
ATOM   9536  C CG  . GLU D 2 82  ? 70.337  -34.766 44.510  1.00 146.36 ? 82  GLU D CG  1 
ATOM   9537  C CD  . GLU D 2 82  ? 70.316  -33.328 44.991  1.00 149.77 ? 82  GLU D CD  1 
ATOM   9538  O OE1 . GLU D 2 82  ? 69.593  -33.044 45.965  1.00 145.03 ? 82  GLU D OE1 1 
ATOM   9539  O OE2 . GLU D 2 82  ? 71.010  -32.496 44.383  1.00 155.90 ? 82  GLU D OE2 1 
ATOM   9540  N N   . PRO D 2 83  ? 68.487  -35.011 40.595  1.00 180.59 ? 83  PRO D N   1 
ATOM   9541  C CA  . PRO D 2 83  ? 68.810  -34.336 39.353  1.00 179.68 ? 83  PRO D CA  1 
ATOM   9542  C C   . PRO D 2 83  ? 69.065  -32.875 39.738  1.00 184.27 ? 83  PRO D C   1 
ATOM   9543  O O   . PRO D 2 83  ? 68.124  -32.163 40.022  1.00 185.45 ? 83  PRO D O   1 
ATOM   9544  C CB  . PRO D 2 83  ? 67.564  -34.511 38.487  1.00 179.89 ? 83  PRO D CB  1 
ATOM   9545  C CG  . PRO D 2 83  ? 66.433  -34.821 39.460  1.00 185.14 ? 83  PRO D CG  1 
ATOM   9546  C CD  . PRO D 2 83  ? 67.047  -35.100 40.821  1.00 180.01 ? 83  PRO D CD  1 
ATOM   9547  N N   . LEU D 2 84  ? 70.328  -32.456 39.731  1.00 195.57 ? 84  LEU D N   1 
ATOM   9548  C CA  . LEU D 2 84  ? 70.686  -31.091 40.205  1.00 192.74 ? 84  LEU D CA  1 
ATOM   9549  C C   . LEU D 2 84  ? 70.248  -29.986 39.235  1.00 191.66 ? 84  LEU D C   1 
ATOM   9550  O O   . LEU D 2 84  ? 71.095  -29.472 38.501  1.00 190.60 ? 84  LEU D O   1 
ATOM   9551  C CB  . LEU D 2 84  ? 72.196  -31.074 40.430  1.00 188.32 ? 84  LEU D CB  1 
ATOM   9552  C CG  . LEU D 2 84  ? 72.764  -32.335 41.076  1.00 186.88 ? 84  LEU D CG  1 
ATOM   9553  C CD1 . LEU D 2 84  ? 73.540  -33.170 40.068  1.00 183.69 ? 84  LEU D CD1 1 
ATOM   9554  C CD2 . LEU D 2 84  ? 73.649  -31.976 42.258  1.00 188.70 ? 84  LEU D CD2 1 
ATOM   9555  N N   . GLY D 2 85  ? 68.980  -29.583 39.286  1.00 179.14 ? 85  GLY D N   1 
ATOM   9556  C CA  . GLY D 2 85  ? 68.550  -28.481 38.442  1.00 170.29 ? 85  GLY D CA  1 
ATOM   9557  C C   . GLY D 2 85  ? 68.615  -28.865 36.976  1.00 167.94 ? 85  GLY D C   1 
ATOM   9558  O O   . GLY D 2 85  ? 68.181  -29.948 36.568  1.00 171.22 ? 85  GLY D O   1 
ATOM   9559  N N   . THR D 2 86  ? 69.160  -27.961 36.165  1.00 160.49 ? 86  THR D N   1 
ATOM   9560  C CA  . THR D 2 86  ? 69.325  -28.212 34.740  1.00 160.04 ? 86  THR D CA  1 
ATOM   9561  C C   . THR D 2 86  ? 70.775  -28.373 34.312  1.00 160.68 ? 86  THR D C   1 
ATOM   9562  O O   . THR D 2 86  ? 71.044  -29.092 33.347  1.00 159.39 ? 86  THR D O   1 
ATOM   9563  C CB  . THR D 2 86  ? 68.689  -27.083 33.920  1.00 158.87 ? 86  THR D CB  1 
ATOM   9564  O OG1 . THR D 2 86  ? 67.591  -26.520 34.651  1.00 160.60 ? 86  THR D OG1 1 
ATOM   9565  C CG2 . THR D 2 86  ? 68.171  -27.623 32.599  1.00 157.75 ? 86  THR D CG2 1 
ATOM   9566  N N   . ALA D 2 87  ? 71.714  -27.723 35.000  1.00 172.88 ? 87  ALA D N   1 
ATOM   9567  C CA  . ALA D 2 87  ? 73.126  -27.808 34.654  1.00 175.57 ? 87  ALA D CA  1 
ATOM   9568  C C   . ALA D 2 87  ? 73.909  -28.759 35.549  1.00 172.50 ? 87  ALA D C   1 
ATOM   9569  O O   . ALA D 2 87  ? 75.067  -29.059 35.241  1.00 172.16 ? 87  ALA D O   1 
ATOM   9570  C CB  . ALA D 2 87  ? 73.768  -26.416 34.706  1.00 177.53 ? 87  ALA D CB  1 
ATOM   9571  N N   . GLY D 2 88  ? 73.314  -29.231 36.641  1.00 172.77 ? 88  GLY D N   1 
ATOM   9572  C CA  . GLY D 2 88  ? 73.966  -30.138 37.558  1.00 172.79 ? 88  GLY D CA  1 
ATOM   9573  C C   . GLY D 2 88  ? 74.428  -31.448 36.948  1.00 169.85 ? 88  GLY D C   1 
ATOM   9574  O O   . GLY D 2 88  ? 75.590  -31.840 37.100  1.00 165.46 ? 88  GLY D O   1 
ATOM   9575  N N   . PRO D 2 89  ? 73.519  -32.176 36.264  1.00 168.09 ? 89  PRO D N   1 
ATOM   9576  C CA  . PRO D 2 89  ? 73.917  -33.443 35.630  1.00 166.62 ? 89  PRO D CA  1 
ATOM   9577  C C   . PRO D 2 89  ? 75.116  -33.315 34.699  1.00 167.64 ? 89  PRO D C   1 
ATOM   9578  O O   . PRO D 2 89  ? 75.815  -34.300 34.443  1.00 166.58 ? 89  PRO D O   1 
ATOM   9579  C CB  . PRO D 2 89  ? 72.657  -33.852 34.858  1.00 163.68 ? 89  PRO D CB  1 
ATOM   9580  C CG  . PRO D 2 89  ? 71.546  -33.283 35.658  1.00 166.55 ? 89  PRO D CG  1 
ATOM   9581  C CD  . PRO D 2 89  ? 72.059  -31.973 36.199  1.00 168.08 ? 89  PRO D CD  1 
ATOM   9582  N N   . LEU D 2 90  ? 75.364  -32.104 34.192  1.00 163.00 ? 90  LEU D N   1 
ATOM   9583  C CA  . LEU D 2 90  ? 76.528  -31.883 33.341  1.00 158.61 ? 90  LEU D CA  1 
ATOM   9584  C C   . LEU D 2 90  ? 77.821  -31.859 34.146  1.00 154.32 ? 90  LEU D C   1 
ATOM   9585  O O   . LEU D 2 90  ? 78.882  -32.215 33.621  1.00 151.71 ? 90  LEU D O   1 
ATOM   9586  C CB  . LEU D 2 90  ? 76.370  -30.575 32.562  1.00 160.38 ? 90  LEU D CB  1 
ATOM   9587  C CG  . LEU D 2 90  ? 75.355  -30.529 31.414  1.00 163.01 ? 90  LEU D CG  1 
ATOM   9588  C CD1 . LEU D 2 90  ? 73.921  -30.389 31.917  1.00 165.96 ? 90  LEU D CD1 1 
ATOM   9589  C CD2 . LEU D 2 90  ? 75.698  -29.407 30.445  1.00 165.37 ? 90  LEU D CD2 1 
ATOM   9590  N N   . ALA D 2 91  ? 77.755  -31.447 35.414  1.00 153.83 ? 91  ALA D N   1 
ATOM   9591  C CA  . ALA D 2 91  ? 78.953  -31.419 36.246  1.00 152.81 ? 91  ALA D CA  1 
ATOM   9592  C C   . ALA D 2 91  ? 79.438  -32.822 36.583  1.00 154.07 ? 91  ALA D C   1 
ATOM   9593  O O   . ALA D 2 91  ? 80.639  -33.031 36.789  1.00 150.27 ? 91  ALA D O   1 
ATOM   9594  C CB  . ALA D 2 91  ? 78.684  -30.629 37.526  1.00 149.27 ? 91  ALA D CB  1 
ATOM   9595  N N   . LEU D 2 92  ? 78.524  -33.792 36.641  1.00 152.43 ? 92  LEU D N   1 
ATOM   9596  C CA  . LEU D 2 92  ? 78.905  -35.163 36.965  1.00 150.48 ? 92  LEU D CA  1 
ATOM   9597  C C   . LEU D 2 92  ? 79.496  -35.883 35.760  1.00 151.18 ? 92  LEU D C   1 
ATOM   9598  O O   . LEU D 2 92  ? 80.435  -36.674 35.907  1.00 154.26 ? 92  LEU D O   1 
ATOM   9599  C CB  . LEU D 2 92  ? 77.690  -35.923 37.502  1.00 150.20 ? 92  LEU D CB  1 
ATOM   9600  C CG  . LEU D 2 92  ? 77.868  -37.370 37.966  1.00 148.71 ? 92  LEU D CG  1 
ATOM   9601  C CD1 . LEU D 2 92  ? 77.078  -37.612 39.242  1.00 147.99 ? 92  LEU D CD1 1 
ATOM   9602  C CD2 . LEU D 2 92  ? 77.432  -38.344 36.882  1.00 144.86 ? 92  LEU D CD2 1 
ATOM   9603  N N   . ALA D 2 93  ? 78.967  -35.623 34.566  1.00 154.02 ? 93  ALA D N   1 
ATOM   9604  C CA  . ALA D 2 93  ? 79.397  -36.300 33.351  1.00 156.78 ? 93  ALA D CA  1 
ATOM   9605  C C   . ALA D 2 93  ? 80.540  -35.587 32.638  1.00 159.72 ? 93  ALA D C   1 
ATOM   9606  O O   . ALA D 2 93  ? 80.819  -35.901 31.476  1.00 158.81 ? 93  ALA D O   1 
ATOM   9607  C CB  . ALA D 2 93  ? 78.211  -36.467 32.395  1.00 157.81 ? 93  ALA D CB  1 
ATOM   9608  N N   . ARG D 2 94  ? 81.210  -34.641 33.302  1.00 160.47 ? 94  ARG D N   1 
ATOM   9609  C CA  . ARG D 2 94  ? 82.335  -33.951 32.681  1.00 164.02 ? 94  ARG D CA  1 
ATOM   9610  C C   . ARG D 2 94  ? 83.520  -34.877 32.441  1.00 169.62 ? 94  ARG D C   1 
ATOM   9611  O O   . ARG D 2 94  ? 84.337  -34.603 31.555  1.00 165.09 ? 94  ARG D O   1 
ATOM   9612  C CB  . ARG D 2 94  ? 82.773  -32.770 33.550  1.00 163.34 ? 94  ARG D CB  1 
ATOM   9613  C CG  . ARG D 2 94  ? 83.419  -33.183 34.868  1.00 158.38 ? 94  ARG D CG  1 
ATOM   9614  C CD  . ARG D 2 94  ? 84.578  -32.270 35.249  1.00 151.32 ? 94  ARG D CD  1 
ATOM   9615  N NE  . ARG D 2 94  ? 84.143  -30.907 35.532  1.00 158.41 ? 94  ARG D NE  1 
ATOM   9616  C CZ  . ARG D 2 94  ? 84.969  -29.905 35.814  1.00 157.05 ? 94  ARG D CZ  1 
ATOM   9617  N NH1 . ARG D 2 94  ? 86.278  -30.114 35.847  1.00 145.86 ? 94  ARG D NH1 1 
ATOM   9618  N NH2 . ARG D 2 94  ? 84.489  -28.694 36.059  1.00 166.35 ? 94  ARG D NH2 1 
ATOM   9619  N N   . ASP D 2 95  ? 83.628  -35.965 33.206  1.00 203.81 ? 95  ASP D N   1 
ATOM   9620  C CA  . ASP D 2 95  ? 84.745  -36.891 33.047  1.00 205.47 ? 95  ASP D CA  1 
ATOM   9621  C C   . ASP D 2 95  ? 84.618  -37.729 31.782  1.00 205.24 ? 95  ASP D C   1 
ATOM   9622  O O   . ASP D 2 95  ? 85.635  -38.086 31.176  1.00 206.56 ? 95  ASP D O   1 
ATOM   9623  C CB  . ASP D 2 95  ? 84.848  -37.790 34.279  1.00 206.21 ? 95  ASP D CB  1 
ATOM   9624  C CG  . ASP D 2 95  ? 83.497  -38.308 34.734  1.00 204.76 ? 95  ASP D CG  1 
ATOM   9625  O OD1 . ASP D 2 95  ? 82.485  -37.995 34.070  1.00 203.19 ? 95  ASP D OD1 1 
ATOM   9626  O OD2 . ASP D 2 95  ? 83.443  -39.025 35.755  1.00 210.09 ? 95  ASP D OD2 1 
ATOM   9627  N N   . LYS D 2 96  ? 83.393  -38.053 31.372  1.00 168.86 ? 96  LYS D N   1 
ATOM   9628  C CA  . LYS D 2 96  ? 83.156  -38.825 30.160  1.00 158.53 ? 96  LYS D CA  1 
ATOM   9629  C C   . LYS D 2 96  ? 83.093  -37.954 28.915  1.00 150.66 ? 96  LYS D C   1 
ATOM   9630  O O   . LYS D 2 96  ? 82.979  -38.486 27.807  1.00 144.18 ? 96  LYS D O   1 
ATOM   9631  C CB  . LYS D 2 96  ? 81.855  -39.626 30.290  1.00 153.22 ? 96  LYS D CB  1 
ATOM   9632  C CG  . LYS D 2 96  ? 81.856  -40.660 31.403  1.00 151.05 ? 96  LYS D CG  1 
ATOM   9633  C CD  . LYS D 2 96  ? 82.907  -41.728 31.146  1.00 149.00 ? 96  LYS D CD  1 
ATOM   9634  C CE  . LYS D 2 96  ? 82.593  -42.515 29.880  1.00 136.68 ? 96  LYS D CE  1 
ATOM   9635  N NZ  . LYS D 2 96  ? 83.589  -43.595 29.622  1.00 130.47 ? 96  LYS D NZ  1 
ATOM   9636  N N   . LEU D 2 97  ? 83.174  -36.633 29.069  1.00 153.36 ? 97  LEU D N   1 
ATOM   9637  C CA  . LEU D 2 97  ? 83.101  -35.722 27.937  1.00 149.29 ? 97  LEU D CA  1 
ATOM   9638  C C   . LEU D 2 97  ? 84.458  -35.181 27.517  1.00 148.15 ? 97  LEU D C   1 
ATOM   9639  O O   . LEU D 2 97  ? 84.611  -34.762 26.365  1.00 146.53 ? 97  LEU D O   1 
ATOM   9640  C CB  . LEU D 2 97  ? 82.170  -34.548 28.265  1.00 146.05 ? 97  LEU D CB  1 
ATOM   9641  C CG  . LEU D 2 97  ? 80.682  -34.892 28.322  1.00 137.23 ? 97  LEU D CG  1 
ATOM   9642  C CD1 . LEU D 2 97  ? 79.881  -33.690 28.785  1.00 144.09 ? 97  LEU D CD1 1 
ATOM   9643  C CD2 . LEU D 2 97  ? 80.187  -35.382 26.969  1.00 139.78 ? 97  LEU D CD2 1 
ATOM   9644  N N   . LEU D 2 98  ? 85.441  -35.184 28.412  1.00 148.56 ? 98  LEU D N   1 
ATOM   9645  C CA  . LEU D 2 98  ? 86.768  -34.662 28.107  1.00 152.82 ? 98  LEU D CA  1 
ATOM   9646  C C   . LEU D 2 98  ? 87.648  -35.799 27.603  1.00 158.42 ? 98  LEU D C   1 
ATOM   9647  O O   . LEU D 2 98  ? 88.094  -36.645 28.385  1.00 154.95 ? 98  LEU D O   1 
ATOM   9648  C CB  . LEU D 2 98  ? 87.381  -33.994 29.334  1.00 153.44 ? 98  LEU D CB  1 
ATOM   9649  C CG  . LEU D 2 98  ? 86.591  -32.824 29.916  1.00 154.66 ? 98  LEU D CG  1 
ATOM   9650  C CD1 . LEU D 2 98  ? 87.380  -32.140 31.021  1.00 161.57 ? 98  LEU D CD1 1 
ATOM   9651  C CD2 . LEU D 2 98  ? 86.218  -31.831 28.825  1.00 146.71 ? 98  LEU D CD2 1 
ATOM   9652  N N   . ASP D 2 99  ? 87.900  -35.812 26.297  1.00 167.86 ? 99  ASP D N   1 
ATOM   9653  C CA  . ASP D 2 99  ? 88.812  -36.769 25.690  1.00 168.34 ? 99  ASP D CA  1 
ATOM   9654  C C   . ASP D 2 99  ? 90.239  -36.245 25.613  1.00 172.29 ? 99  ASP D C   1 
ATOM   9655  O O   . ASP D 2 99  ? 91.158  -37.028 25.349  1.00 173.72 ? 99  ASP D O   1 
ATOM   9656  C CB  . ASP D 2 99  ? 88.323  -37.154 24.288  1.00 164.96 ? 99  ASP D CB  1 
ATOM   9657  C CG  . ASP D 2 99  ? 88.106  -35.947 23.393  1.00 167.65 ? 99  ASP D CG  1 
ATOM   9658  O OD1 . ASP D 2 99  ? 87.772  -34.866 23.923  1.00 170.33 ? 99  ASP D OD1 1 
ATOM   9659  O OD2 . ASP D 2 99  ? 88.261  -36.079 22.160  1.00 168.46 ? 99  ASP D OD2 1 
ATOM   9660  N N   . GLY D 2 100 ? 90.442  -34.944 25.834  1.00 180.15 ? 100 GLY D N   1 
ATOM   9661  C CA  . GLY D 2 100 ? 91.744  -34.317 25.788  1.00 178.07 ? 100 GLY D CA  1 
ATOM   9662  C C   . GLY D 2 100 ? 91.916  -33.359 24.626  1.00 189.20 ? 100 GLY D C   1 
ATOM   9663  O O   . GLY D 2 100 ? 92.704  -32.411 24.728  1.00 181.52 ? 100 GLY D O   1 
ATOM   9664  N N   . SER D 2 101 ? 91.188  -33.583 23.529  1.00 216.94 ? 101 SER D N   1 
ATOM   9665  C CA  . SER D 2 101 ? 91.323  -32.740 22.347  1.00 217.06 ? 101 SER D CA  1 
ATOM   9666  C C   . SER D 2 101 ? 90.670  -31.375 22.514  1.00 216.11 ? 101 SER D C   1 
ATOM   9667  O O   . SER D 2 101 ? 90.952  -30.470 21.723  1.00 217.36 ? 101 SER D O   1 
ATOM   9668  C CB  . SER D 2 101 ? 90.725  -33.450 21.131  1.00 216.08 ? 101 SER D CB  1 
ATOM   9669  O OG  . SER D 2 101 ? 90.779  -32.628 19.978  1.00 215.36 ? 101 SER D OG  1 
ATOM   9670  N N   . GLY D 2 102 ? 89.815  -31.201 23.518  1.00 197.36 ? 102 GLY D N   1 
ATOM   9671  C CA  . GLY D 2 102 ? 89.158  -29.927 23.735  1.00 188.82 ? 102 GLY D CA  1 
ATOM   9672  C C   . GLY D 2 102 ? 88.206  -29.532 22.624  1.00 189.67 ? 102 GLY D C   1 
ATOM   9673  O O   . GLY D 2 102 ? 88.217  -28.385 22.164  1.00 183.02 ? 102 GLY D O   1 
ATOM   9674  N N   . GLU D 2 103 ? 87.361  -30.487 22.184  1.00 197.91 ? 103 GLU D N   1 
ATOM   9675  C CA  . GLU D 2 103 ? 86.362  -30.271 21.149  1.00 198.34 ? 103 GLU D CA  1 
ATOM   9676  C C   . GLU D 2 103 ? 84.988  -30.039 21.768  1.00 193.95 ? 103 GLU D C   1 
ATOM   9677  O O   . GLU D 2 103 ? 84.659  -30.625 22.803  1.00 193.37 ? 103 GLU D O   1 
ATOM   9678  C CB  . GLU D 2 103 ? 86.293  -31.475 20.202  1.00 204.14 ? 103 GLU D CB  1 
ATOM   9679  C CG  . GLU D 2 103 ? 87.448  -31.574 19.221  1.00 208.30 ? 103 GLU D CG  1 
ATOM   9680  C CD  . GLU D 2 103 ? 87.274  -30.664 18.021  1.00 211.11 ? 103 GLU D CD  1 
ATOM   9681  O OE1 . GLU D 2 103 ? 86.175  -30.095 17.859  1.00 207.87 ? 103 GLU D OE1 1 
ATOM   9682  O OE2 . GLU D 2 103 ? 88.236  -30.517 17.239  1.00 216.58 ? 103 GLU D OE2 1 
ATOM   9683  N N   . PRO D 2 104 ? 84.166  -29.189 21.153  1.00 183.39 ? 104 PRO D N   1 
ATOM   9684  C CA  . PRO D 2 104 ? 82.827  -28.941 21.700  1.00 179.38 ? 104 PRO D CA  1 
ATOM   9685  C C   . PRO D 2 104 ? 81.944  -30.178 21.621  1.00 178.42 ? 104 PRO D C   1 
ATOM   9686  O O   . PRO D 2 104 ? 81.985  -30.937 20.650  1.00 174.82 ? 104 PRO D O   1 
ATOM   9687  C CB  . PRO D 2 104 ? 82.285  -27.808 20.818  1.00 177.82 ? 104 PRO D CB  1 
ATOM   9688  C CG  . PRO D 2 104 ? 83.082  -27.890 19.558  1.00 184.45 ? 104 PRO D CG  1 
ATOM   9689  C CD  . PRO D 2 104 ? 84.448  -28.349 19.977  1.00 184.86 ? 104 PRO D CD  1 
ATOM   9690  N N   . PHE D 2 105 ? 81.141  -30.373 22.663  1.00 173.25 ? 105 PHE D N   1 
ATOM   9691  C CA  . PHE D 2 105 ? 80.198  -31.476 22.740  1.00 179.26 ? 105 PHE D CA  1 
ATOM   9692  C C   . PHE D 2 105 ? 78.767  -30.954 22.687  1.00 199.46 ? 105 PHE D C   1 
ATOM   9693  O O   . PHE D 2 105 ? 78.496  -29.782 22.963  1.00 191.96 ? 105 PHE D O   1 
ATOM   9694  C CB  . PHE D 2 105 ? 80.419  -32.297 24.017  1.00 165.52 ? 105 PHE D CB  1 
ATOM   9695  C CG  . PHE D 2 105 ? 80.428  -31.477 25.276  1.00 155.26 ? 105 PHE D CG  1 
ATOM   9696  C CD1 . PHE D 2 105 ? 81.612  -30.946 25.762  1.00 151.27 ? 105 PHE D CD1 1 
ATOM   9697  C CD2 . PHE D 2 105 ? 79.256  -31.241 25.977  1.00 159.28 ? 105 PHE D CD2 1 
ATOM   9698  C CE1 . PHE D 2 105 ? 81.627  -30.192 26.919  1.00 147.95 ? 105 PHE D CE1 1 
ATOM   9699  C CE2 . PHE D 2 105 ? 79.265  -30.487 27.136  1.00 151.70 ? 105 PHE D CE2 1 
ATOM   9700  C CZ  . PHE D 2 105 ? 80.453  -29.962 27.608  1.00 143.81 ? 105 PHE D CZ  1 
ATOM   9701  N N   . PHE D 2 106 ? 77.849  -31.844 22.325  1.00 267.44 ? 106 PHE D N   1 
ATOM   9702  C CA  . PHE D 2 106 ? 76.439  -31.509 22.196  1.00 265.74 ? 106 PHE D CA  1 
ATOM   9703  C C   . PHE D 2 106 ? 75.668  -31.907 23.447  1.00 264.95 ? 106 PHE D C   1 
ATOM   9704  O O   . PHE D 2 106 ? 75.978  -32.904 24.104  1.00 265.52 ? 106 PHE D O   1 
ATOM   9705  C CB  . PHE D 2 106 ? 75.821  -32.194 20.975  1.00 265.16 ? 106 PHE D CB  1 
ATOM   9706  C CG  . PHE D 2 106 ? 76.241  -31.595 19.666  1.00 265.59 ? 106 PHE D CG  1 
ATOM   9707  C CD1 . PHE D 2 106 ? 75.529  -30.545 19.112  1.00 264.65 ? 106 PHE D CD1 1 
ATOM   9708  C CD2 . PHE D 2 106 ? 77.344  -32.085 18.986  1.00 266.99 ? 106 PHE D CD2 1 
ATOM   9709  C CE1 . PHE D 2 106 ? 75.908  -29.994 17.905  1.00 265.10 ? 106 PHE D CE1 1 
ATOM   9710  C CE2 . PHE D 2 106 ? 77.729  -31.537 17.779  1.00 267.45 ? 106 PHE D CE2 1 
ATOM   9711  C CZ  . PHE D 2 106 ? 77.010  -30.490 17.239  1.00 266.50 ? 106 PHE D CZ  1 
ATOM   9712  N N   . VAL D 2 107 ? 74.652  -31.109 23.768  1.00 230.63 ? 107 VAL D N   1 
ATOM   9713  C CA  . VAL D 2 107 ? 73.746  -31.369 24.882  1.00 229.38 ? 107 VAL D CA  1 
ATOM   9714  C C   . VAL D 2 107 ? 72.322  -31.323 24.350  1.00 227.61 ? 107 VAL D C   1 
ATOM   9715  O O   . VAL D 2 107 ? 71.861  -30.269 23.895  1.00 226.96 ? 107 VAL D O   1 
ATOM   9716  C CB  . VAL D 2 107 ? 73.924  -30.357 26.026  1.00 229.35 ? 107 VAL D CB  1 
ATOM   9717  C CG1 . VAL D 2 107 ? 72.994  -30.702 27.178  1.00 228.08 ? 107 VAL D CG1 1 
ATOM   9718  C CG2 . VAL D 2 107 ? 75.373  -30.324 26.491  1.00 230.80 ? 107 VAL D CG2 1 
ATOM   9719  N N   . LEU D 2 108 ? 71.626  -32.456 24.408  1.00 196.98 ? 108 LEU D N   1 
ATOM   9720  C CA  . LEU D 2 108 ? 70.288  -32.589 23.855  1.00 178.75 ? 108 LEU D CA  1 
ATOM   9721  C C   . LEU D 2 108 ? 69.294  -32.946 24.951  1.00 170.62 ? 108 LEU D C   1 
ATOM   9722  O O   . LEU D 2 108 ? 69.640  -33.593 25.943  1.00 169.79 ? 108 LEU D O   1 
ATOM   9723  C CB  . LEU D 2 108 ? 70.246  -33.654 22.751  1.00 169.38 ? 108 LEU D CB  1 
ATOM   9724  C CG  . LEU D 2 108 ? 71.224  -33.471 21.588  1.00 168.66 ? 108 LEU D CG  1 
ATOM   9725  C CD1 . LEU D 2 108 ? 71.123  -34.630 20.609  1.00 148.36 ? 108 LEU D CD1 1 
ATOM   9726  C CD2 . LEU D 2 108 ? 70.972  -32.148 20.881  1.00 166.22 ? 108 LEU D CD2 1 
ATOM   9727  N N   . ASN D 2 109 ? 68.050  -32.516 24.759  1.00 164.88 ? 109 ASN D N   1 
ATOM   9728  C CA  . ASN D 2 109 ? 66.953  -32.842 25.659  1.00 162.25 ? 109 ASN D CA  1 
ATOM   9729  C C   . ASN D 2 109 ? 66.085  -33.922 25.025  1.00 167.21 ? 109 ASN D C   1 
ATOM   9730  O O   . ASN D 2 109 ? 65.800  -33.880 23.825  1.00 159.18 ? 109 ASN D O   1 
ATOM   9731  C CB  . ASN D 2 109 ? 66.112  -31.600 25.968  1.00 151.38 ? 109 ASN D CB  1 
ATOM   9732  C CG  . ASN D 2 109 ? 65.191  -31.795 27.161  1.00 147.80 ? 109 ASN D CG  1 
ATOM   9733  O OD1 . ASN D 2 109 ? 64.768  -32.911 27.464  1.00 152.82 ? 109 ASN D OD1 1 
ATOM   9734  N ND2 . ASN D 2 109 ? 64.872  -30.701 27.843  1.00 137.70 ? 109 ASN D ND2 1 
ATOM   9735  N N   . SER D 2 110 ? 65.668  -34.892 25.840  1.00 208.55 ? 110 SER D N   1 
ATOM   9736  C CA  . SER D 2 110 ? 64.869  -36.000 25.330  1.00 208.44 ? 110 SER D CA  1 
ATOM   9737  C C   . SER D 2 110 ? 63.435  -35.593 25.021  1.00 208.09 ? 110 SER D C   1 
ATOM   9738  O O   . SER D 2 110 ? 62.730  -36.336 24.330  1.00 207.90 ? 110 SER D O   1 
ATOM   9739  C CB  . SER D 2 110 ? 64.877  -37.157 26.332  1.00 209.26 ? 110 SER D CB  1 
ATOM   9740  O OG  . SER D 2 110 ? 64.150  -38.265 25.831  1.00 209.33 ? 110 SER D OG  1 
ATOM   9741  N N   . ASP D 2 111 ? 62.986  -34.440 25.514  1.00 159.84 ? 111 ASP D N   1 
ATOM   9742  C CA  . ASP D 2 111 ? 61.609  -34.002 25.343  1.00 144.08 ? 111 ASP D CA  1 
ATOM   9743  C C   . ASP D 2 111 ? 61.418  -33.106 24.125  1.00 132.97 ? 111 ASP D C   1 
ATOM   9744  O O   . ASP D 2 111 ? 60.404  -32.402 24.040  1.00 127.98 ? 111 ASP D O   1 
ATOM   9745  C CB  . ASP D 2 111 ? 61.129  -33.274 26.598  1.00 132.97 ? 111 ASP D CB  1 
ATOM   9746  C CG  . ASP D 2 111 ? 61.326  -34.090 27.855  1.00 137.09 ? 111 ASP D CG  1 
ATOM   9747  O OD1 . ASP D 2 111 ? 61.986  -35.148 27.787  1.00 144.05 ? 111 ASP D OD1 1 
ATOM   9748  O OD2 . ASP D 2 111 ? 60.819  -33.671 28.916  1.00 129.07 ? 111 ASP D OD2 1 
ATOM   9749  N N   . VAL D 2 112 ? 62.360  -33.111 23.184  1.00 132.08 ? 112 VAL D N   1 
ATOM   9750  C CA  . VAL D 2 112 ? 62.319  -32.228 22.025  1.00 122.15 ? 112 VAL D CA  1 
ATOM   9751  C C   . VAL D 2 112 ? 62.562  -33.043 20.763  1.00 118.29 ? 112 VAL D C   1 
ATOM   9752  O O   . VAL D 2 112 ? 63.371  -33.978 20.759  1.00 125.30 ? 112 VAL D O   1 
ATOM   9753  C CB  . VAL D 2 112 ? 63.362  -31.092 22.135  1.00 121.58 ? 112 VAL D CB  1 
ATOM   9754  C CG1 . VAL D 2 112 ? 63.178  -30.086 21.008  1.00 118.45 ? 112 VAL D CG1 1 
ATOM   9755  C CG2 . VAL D 2 112 ? 63.274  -30.401 23.487  1.00 126.54 ? 112 VAL D CG2 1 
ATOM   9756  N N   . ILE D 2 113 ? 61.858  -32.684 19.690  1.00 110.00 ? 113 ILE D N   1 
ATOM   9757  C CA  . ILE D 2 113 ? 62.079  -33.242 18.364  1.00 111.18 ? 113 ILE D CA  1 
ATOM   9758  C C   . ILE D 2 113 ? 62.279  -32.084 17.399  1.00 115.52 ? 113 ILE D C   1 
ATOM   9759  O O   . ILE D 2 113 ? 61.748  -30.987 17.598  1.00 118.79 ? 113 ILE D O   1 
ATOM   9760  C CB  . ILE D 2 113 ? 60.917  -34.147 17.896  1.00 112.41 ? 113 ILE D CB  1 
ATOM   9761  C CG1 . ILE D 2 113 ? 59.576  -33.421 18.038  1.00 116.79 ? 113 ILE D CG1 1 
ATOM   9762  C CG2 . ILE D 2 113 ? 60.919  -35.457 18.671  1.00 112.32 ? 113 ILE D CG2 1 
ATOM   9763  C CD1 . ILE D 2 113 ? 58.397  -34.186 17.464  1.00 120.52 ? 113 ILE D CD1 1 
ATOM   9764  N N   . SER D 2 114 ? 63.043  -32.333 16.346  1.00 119.22 ? 114 SER D N   1 
ATOM   9765  C CA  . SER D 2 114 ? 63.353  -31.307 15.352  1.00 123.67 ? 114 SER D CA  1 
ATOM   9766  C C   . SER D 2 114 ? 63.960  -31.999 14.137  1.00 125.59 ? 114 SER D C   1 
ATOM   9767  O O   . SER D 2 114 ? 63.973  -33.233 14.045  1.00 126.41 ? 114 SER D O   1 
ATOM   9768  C CB  . SER D 2 114 ? 64.290  -30.242 15.927  1.00 125.10 ? 114 SER D CB  1 
ATOM   9769  O OG  . SER D 2 114 ? 65.572  -30.786 16.181  1.00 124.51 ? 114 SER D OG  1 
ATOM   9770  N N   . GLU D 2 115 ? 64.451  -31.198 13.192  1.00 130.16 ? 115 GLU D N   1 
ATOM   9771  C CA  . GLU D 2 115 ? 65.106  -31.737 12.009  1.00 133.14 ? 115 GLU D CA  1 
ATOM   9772  C C   . GLU D 2 115 ? 66.580  -32.039 12.251  1.00 137.29 ? 115 GLU D C   1 
ATOM   9773  O O   . GLU D 2 115 ? 67.179  -32.791 11.473  1.00 135.12 ? 115 GLU D O   1 
ATOM   9774  C CB  . GLU D 2 115 ? 64.952  -30.756 10.845  1.00 131.52 ? 115 GLU D CB  1 
ATOM   9775  C CG  . GLU D 2 115 ? 63.522  -30.270 10.653  1.00 131.28 ? 115 GLU D CG  1 
ATOM   9776  C CD  . GLU D 2 115 ? 63.320  -29.519 9.353   1.00 135.31 ? 115 GLU D CD  1 
ATOM   9777  O OE1 . GLU D 2 115 ? 64.316  -29.020 8.788   1.00 138.06 ? 115 GLU D OE1 1 
ATOM   9778  O OE2 . GLU D 2 115 ? 62.159  -29.411 8.906   1.00 133.45 ? 115 GLU D OE2 1 
ATOM   9779  N N   . TYR D 2 116 ? 67.163  -31.479 13.315  1.00 132.29 ? 116 TYR D N   1 
ATOM   9780  C CA  . TYR D 2 116 ? 68.543  -31.695 13.741  1.00 131.55 ? 116 TYR D CA  1 
ATOM   9781  C C   . TYR D 2 116 ? 69.542  -31.458 12.612  1.00 135.91 ? 116 TYR D C   1 
ATOM   9782  O O   . TYR D 2 116 ? 70.094  -32.421 12.062  1.00 135.13 ? 116 TYR D O   1 
ATOM   9783  C CB  . TYR D 2 116 ? 68.708  -33.110 14.298  1.00 131.00 ? 116 TYR D CB  1 
ATOM   9784  C CG  . TYR D 2 116 ? 67.839  -33.410 15.500  1.00 124.87 ? 116 TYR D CG  1 
ATOM   9785  C CD1 . TYR D 2 116 ? 68.203  -32.983 16.771  1.00 123.88 ? 116 TYR D CD1 1 
ATOM   9786  C CD2 . TYR D 2 116 ? 66.655  -34.122 15.363  1.00 121.49 ? 116 TYR D CD2 1 
ATOM   9787  C CE1 . TYR D 2 116 ? 67.410  -33.257 17.872  1.00 119.03 ? 116 TYR D CE1 1 
ATOM   9788  C CE2 . TYR D 2 116 ? 65.855  -34.401 16.458  1.00 118.42 ? 116 TYR D CE2 1 
ATOM   9789  C CZ  . TYR D 2 116 ? 66.238  -33.967 17.709  1.00 115.60 ? 116 TYR D CZ  1 
ATOM   9790  O OH  . TYR D 2 116 ? 65.445  -34.244 18.800  1.00 112.33 ? 116 TYR D OH  1 
ATOM   9791  N N   . PRO D 2 117 ? 69.804  -30.202 12.233  1.00 137.69 ? 117 PRO D N   1 
ATOM   9792  C CA  . PRO D 2 117 ? 70.888  -29.913 11.267  1.00 139.48 ? 117 PRO D CA  1 
ATOM   9793  C C   . PRO D 2 117 ? 72.227  -29.713 11.972  1.00 149.15 ? 117 PRO D C   1 
ATOM   9794  O O   . PRO D 2 117 ? 72.803  -28.618 12.012  1.00 148.81 ? 117 PRO D O   1 
ATOM   9795  C CB  . PRO D 2 117 ? 70.378  -28.644 10.582  1.00 133.03 ? 117 PRO D CB  1 
ATOM   9796  C CG  . PRO D 2 117 ? 69.648  -27.929 11.675  1.00 134.13 ? 117 PRO D CG  1 
ATOM   9797  C CD  . PRO D 2 117 ? 69.021  -28.994 12.552  1.00 135.37 ? 117 PRO D CD  1 
ATOM   9798  N N   . LEU D 2 118 ? 72.740  -30.802 12.551  1.00 164.15 ? 118 LEU D N   1 
ATOM   9799  C CA  . LEU D 2 118 ? 73.945  -30.716 13.371  1.00 168.03 ? 118 LEU D CA  1 
ATOM   9800  C C   . LEU D 2 118 ? 75.199  -30.467 12.542  1.00 170.16 ? 118 LEU D C   1 
ATOM   9801  O O   . LEU D 2 118 ? 76.149  -29.850 13.036  1.00 169.53 ? 118 LEU D O   1 
ATOM   9802  C CB  . LEU D 2 118 ? 74.112  -31.998 14.187  1.00 171.03 ? 118 LEU D CB  1 
ATOM   9803  C CG  . LEU D 2 118 ? 72.975  -32.369 15.140  1.00 173.28 ? 118 LEU D CG  1 
ATOM   9804  C CD1 . LEU D 2 118 ? 73.264  -33.696 15.824  1.00 166.24 ? 118 LEU D CD1 1 
ATOM   9805  C CD2 . LEU D 2 118 ? 72.756  -31.270 16.167  1.00 179.15 ? 118 LEU D CD2 1 
ATOM   9806  N N   . LYS D 2 119 ? 75.227  -30.931 11.292  1.00 182.97 ? 119 LYS D N   1 
ATOM   9807  C CA  . LYS D 2 119 ? 76.433  -30.795 10.481  1.00 184.28 ? 119 LYS D CA  1 
ATOM   9808  C C   . LYS D 2 119 ? 76.752  -29.330 10.208  1.00 184.58 ? 119 LYS D C   1 
ATOM   9809  O O   . LYS D 2 119 ? 77.878  -28.873 10.435  1.00 185.61 ? 119 LYS D O   1 
ATOM   9810  C CB  . LYS D 2 119 ? 76.278  -31.575 9.175   1.00 189.58 ? 119 LYS D CB  1 
ATOM   9811  C CG  . LYS D 2 119 ? 76.104  -33.074 9.377   1.00 187.04 ? 119 LYS D CG  1 
ATOM   9812  C CD  . LYS D 2 119 ? 76.850  -33.875 8.324   1.00 185.93 ? 119 LYS D CD  1 
ATOM   9813  C CE  . LYS D 2 119 ? 78.342  -33.602 8.387   1.00 185.62 ? 119 LYS D CE  1 
ATOM   9814  N NZ  . LYS D 2 119 ? 78.897  -33.932 9.729   1.00 185.56 ? 119 LYS D NZ  1 
ATOM   9815  N N   . GLU D 2 120 ? 75.770  -28.578 9.714   1.00 170.03 ? 120 GLU D N   1 
ATOM   9816  C CA  . GLU D 2 120 ? 75.960  -27.176 9.366   1.00 165.66 ? 120 GLU D CA  1 
ATOM   9817  C C   . GLU D 2 120 ? 75.966  -26.251 10.580  1.00 161.42 ? 120 GLU D C   1 
ATOM   9818  O O   . GLU D 2 120 ? 75.941  -25.028 10.407  1.00 155.36 ? 120 GLU D O   1 
ATOM   9819  C CB  . GLU D 2 120 ? 74.880  -26.743 8.373   1.00 163.74 ? 120 GLU D CB  1 
ATOM   9820  C CG  . GLU D 2 120 ? 74.908  -27.537 7.075   1.00 165.77 ? 120 GLU D CG  1 
ATOM   9821  C CD  . GLU D 2 120 ? 73.849  -27.090 6.088   1.00 167.55 ? 120 GLU D CD  1 
ATOM   9822  O OE1 . GLU D 2 120 ? 73.065  -26.180 6.428   1.00 166.95 ? 120 GLU D OE1 1 
ATOM   9823  O OE2 . GLU D 2 120 ? 73.803  -27.648 4.971   1.00 170.89 ? 120 GLU D OE2 1 
ATOM   9824  N N   . MET D 2 121 ? 75.995  -26.799 11.794  1.00 164.61 ? 121 MET D N   1 
ATOM   9825  C CA  . MET D 2 121 ? 76.179  -25.988 12.990  1.00 161.16 ? 121 MET D CA  1 
ATOM   9826  C C   . MET D 2 121 ? 77.643  -25.894 13.394  1.00 171.13 ? 121 MET D C   1 
ATOM   9827  O O   . MET D 2 121 ? 78.066  -24.866 13.937  1.00 167.63 ? 121 MET D O   1 
ATOM   9828  C CB  . MET D 2 121 ? 75.357  -26.558 14.149  1.00 155.93 ? 121 MET D CB  1 
ATOM   9829  C CG  . MET D 2 121 ? 75.240  -25.628 15.344  1.00 155.19 ? 121 MET D CG  1 
ATOM   9830  S SD  . MET D 2 121 ? 74.356  -26.392 16.715  1.00 158.60 ? 121 MET D SD  1 
ATOM   9831  C CE  . MET D 2 121 ? 73.008  -27.184 15.841  1.00 148.64 ? 121 MET D CE  1 
ATOM   9832  N N   . LEU D 2 122 ? 78.422  -26.951 13.141  1.00 188.31 ? 122 LEU D N   1 
ATOM   9833  C CA  . LEU D 2 122 ? 79.861  -26.891 13.380  1.00 189.94 ? 122 LEU D CA  1 
ATOM   9834  C C   . LEU D 2 122 ? 80.515  -25.847 12.488  1.00 190.55 ? 122 LEU D C   1 
ATOM   9835  O O   . LEU D 2 122 ? 81.400  -25.104 12.931  1.00 191.54 ? 122 LEU D O   1 
ATOM   9836  C CB  . LEU D 2 122 ? 80.497  -28.262 13.139  1.00 193.25 ? 122 LEU D CB  1 
ATOM   9837  C CG  . LEU D 2 122 ? 80.459  -29.318 14.247  1.00 199.27 ? 122 LEU D CG  1 
ATOM   9838  C CD1 . LEU D 2 122 ? 79.051  -29.842 14.465  1.00 198.62 ? 122 LEU D CD1 1 
ATOM   9839  C CD2 . LEU D 2 122 ? 81.411  -30.462 13.922  1.00 198.98 ? 122 LEU D CD2 1 
ATOM   9840  N N   . GLU D 2 123 ? 80.103  -25.785 11.219  1.00 167.39 ? 123 GLU D N   1 
ATOM   9841  C CA  . GLU D 2 123 ? 80.575  -24.718 10.344  1.00 160.47 ? 123 GLU D CA  1 
ATOM   9842  C C   . GLU D 2 123 ? 80.108  -23.361 10.846  1.00 161.15 ? 123 GLU D C   1 
ATOM   9843  O O   . GLU D 2 123 ? 80.830  -22.364 10.730  1.00 162.62 ? 123 GLU D O   1 
ATOM   9844  C CB  . GLU D 2 123 ? 80.091  -24.950 8.913   1.00 152.32 ? 123 GLU D CB  1 
ATOM   9845  C CG  . GLU D 2 123 ? 80.729  -24.024 7.892   1.00 146.52 ? 123 GLU D CG  1 
ATOM   9846  C CD  . GLU D 2 123 ? 80.277  -24.320 6.477   1.00 144.31 ? 123 GLU D CD  1 
ATOM   9847  O OE1 . GLU D 2 123 ? 79.211  -24.950 6.313   1.00 142.64 ? 123 GLU D OE1 1 
ATOM   9848  O OE2 . GLU D 2 123 ? 80.984  -23.919 5.530   1.00 147.17 ? 123 GLU D OE2 1 
ATOM   9849  N N   . PHE D 2 124 ? 78.902  -23.304 11.415  1.00 161.24 ? 124 PHE D N   1 
ATOM   9850  C CA  . PHE D 2 124 ? 78.459  -22.088 12.081  1.00 157.94 ? 124 PHE D CA  1 
ATOM   9851  C C   . PHE D 2 124 ? 79.248  -21.827 13.356  1.00 165.79 ? 124 PHE D C   1 
ATOM   9852  O O   . PHE D 2 124 ? 79.210  -20.708 13.874  1.00 170.35 ? 124 PHE D O   1 
ATOM   9853  C CB  . PHE D 2 124 ? 76.961  -22.168 12.385  1.00 153.63 ? 124 PHE D CB  1 
ATOM   9854  C CG  . PHE D 2 124 ? 76.381  -20.889 12.916  1.00 152.33 ? 124 PHE D CG  1 
ATOM   9855  C CD1 . PHE D 2 124 ? 76.411  -19.730 12.158  1.00 144.08 ? 124 PHE D CD1 1 
ATOM   9856  C CD2 . PHE D 2 124 ? 75.797  -20.846 14.171  1.00 156.11 ? 124 PHE D CD2 1 
ATOM   9857  C CE1 . PHE D 2 124 ? 75.875  -18.552 12.644  1.00 143.02 ? 124 PHE D CE1 1 
ATOM   9858  C CE2 . PHE D 2 124 ? 75.260  -19.672 14.661  1.00 153.70 ? 124 PHE D CE2 1 
ATOM   9859  C CZ  . PHE D 2 124 ? 75.299  -18.524 13.898  1.00 149.67 ? 124 PHE D CZ  1 
ATOM   9860  N N   . HIS D 2 125 ? 79.959  -22.832 13.867  1.00 166.58 ? 125 HIS D N   1 
ATOM   9861  C CA  . HIS D 2 125 ? 80.841  -22.675 15.015  1.00 172.01 ? 125 HIS D CA  1 
ATOM   9862  C C   . HIS D 2 125 ? 82.287  -22.433 14.606  1.00 173.26 ? 125 HIS D C   1 
ATOM   9863  O O   . HIS D 2 125 ? 82.976  -21.622 15.231  1.00 178.64 ? 125 HIS D O   1 
ATOM   9864  C CB  . HIS D 2 125 ? 80.774  -23.912 15.919  1.00 172.87 ? 125 HIS D CB  1 
ATOM   9865  C CG  . HIS D 2 125 ? 81.495  -23.744 17.222  1.00 174.75 ? 125 HIS D CG  1 
ATOM   9866  N ND1 . HIS D 2 125 ? 80.970  -23.019 18.270  1.00 175.40 ? 125 HIS D ND1 1 
ATOM   9867  C CD2 . HIS D 2 125 ? 82.697  -24.202 17.645  1.00 172.63 ? 125 HIS D CD2 1 
ATOM   9868  C CE1 . HIS D 2 125 ? 81.816  -23.039 19.284  1.00 168.81 ? 125 HIS D CE1 1 
ATOM   9869  N NE2 . HIS D 2 125 ? 82.872  -23.749 18.931  1.00 168.14 ? 125 HIS D NE2 1 
ATOM   9870  N N   . LYS D 2 126 ? 82.759  -23.118 13.563  1.00 170.10 ? 126 LYS D N   1 
ATOM   9871  C CA  . LYS D 2 126 ? 84.128  -22.989 13.088  1.00 171.66 ? 126 LYS D CA  1 
ATOM   9872  C C   . LYS D 2 126 ? 84.304  -21.831 12.111  1.00 174.37 ? 126 LYS D C   1 
ATOM   9873  O O   . LYS D 2 126 ? 85.281  -21.814 11.353  1.00 172.78 ? 126 LYS D O   1 
ATOM   9874  C CB  . LYS D 2 126 ? 84.591  -24.292 12.431  1.00 166.83 ? 126 LYS D CB  1 
ATOM   9875  C CG  . LYS D 2 126 ? 84.745  -25.469 13.380  1.00 164.19 ? 126 LYS D CG  1 
ATOM   9876  C CD  . LYS D 2 126 ? 85.338  -26.665 12.649  1.00 158.56 ? 126 LYS D CD  1 
ATOM   9877  C CE  . LYS D 2 126 ? 85.594  -27.832 13.589  1.00 156.95 ? 126 LYS D CE  1 
ATOM   9878  N NZ  . LYS D 2 126 ? 86.248  -28.971 12.885  1.00 149.41 ? 126 LYS D NZ  1 
ATOM   9879  N N   . SER D 2 127 ? 83.381  -20.872 12.105  1.00 179.50 ? 127 SER D N   1 
ATOM   9880  C CA  . SER D 2 127 ? 83.469  -19.702 11.243  1.00 184.77 ? 127 SER D CA  1 
ATOM   9881  C C   . SER D 2 127 ? 83.830  -18.441 12.013  1.00 196.63 ? 127 SER D C   1 
ATOM   9882  O O   . SER D 2 127 ? 84.787  -17.748 11.657  1.00 195.71 ? 127 SER D O   1 
ATOM   9883  C CB  . SER D 2 127 ? 82.144  -19.491 10.496  1.00 180.61 ? 127 SER D CB  1 
ATOM   9884  O OG  . SER D 2 127 ? 82.223  -18.382 9.617   1.00 184.94 ? 127 SER D OG  1 
ATOM   9885  N N   . HIS D 2 128 ? 83.083  -18.128 13.068  1.00 219.98 ? 128 HIS D N   1 
ATOM   9886  C CA  . HIS D 2 128 ? 83.364  -16.969 13.902  1.00 220.43 ? 128 HIS D CA  1 
ATOM   9887  C C   . HIS D 2 128 ? 84.209  -17.299 15.126  1.00 221.70 ? 128 HIS D C   1 
ATOM   9888  O O   . HIS D 2 128 ? 84.721  -16.377 15.770  1.00 225.58 ? 128 HIS D O   1 
ATOM   9889  C CB  . HIS D 2 128 ? 82.051  -16.317 14.346  1.00 218.73 ? 128 HIS D CB  1 
ATOM   9890  C CG  . HIS D 2 128 ? 81.085  -17.274 14.971  1.00 217.21 ? 128 HIS D CG  1 
ATOM   9891  N ND1 . HIS D 2 128 ? 81.469  -18.504 15.459  1.00 217.46 ? 128 HIS D ND1 1 
ATOM   9892  C CD2 . HIS D 2 128 ? 79.752  -17.184 15.181  1.00 215.46 ? 128 HIS D CD2 1 
ATOM   9893  C CE1 . HIS D 2 128 ? 80.415  -19.129 15.949  1.00 216.05 ? 128 HIS D CE1 1 
ATOM   9894  N NE2 . HIS D 2 128 ? 79.360  -18.352 15.789  1.00 214.81 ? 128 HIS D NE2 1 
ATOM   9895  N N   . GLY D 2 129 ? 84.360  -18.576 15.467  1.00 202.78 ? 129 GLY D N   1 
ATOM   9896  C CA  . GLY D 2 129 ? 85.180  -18.950 16.602  1.00 190.05 ? 129 GLY D CA  1 
ATOM   9897  C C   . GLY D 2 129 ? 84.555  -18.705 17.957  1.00 179.17 ? 129 GLY D C   1 
ATOM   9898  O O   . GLY D 2 129 ? 85.275  -18.399 18.914  1.00 169.71 ? 129 GLY D O   1 
ATOM   9899  N N   . GLY D 2 130 ? 83.235  -18.823 18.071  1.00 178.45 ? 130 GLY D N   1 
ATOM   9900  C CA  . GLY D 2 130 ? 82.570  -18.638 19.342  1.00 170.96 ? 130 GLY D CA  1 
ATOM   9901  C C   . GLY D 2 130 ? 82.935  -19.724 20.339  1.00 160.04 ? 130 GLY D C   1 
ATOM   9902  O O   . GLY D 2 130 ? 83.634  -20.693 20.040  1.00 160.00 ? 130 GLY D O   1 
ATOM   9903  N N   . GLU D 2 131 ? 82.437  -19.552 21.561  1.00 156.30 ? 131 GLU D N   1 
ATOM   9904  C CA  . GLU D 2 131 ? 82.686  -20.514 22.628  1.00 147.61 ? 131 GLU D CA  1 
ATOM   9905  C C   . GLU D 2 131 ? 81.507  -21.444 22.880  1.00 154.54 ? 131 GLU D C   1 
ATOM   9906  O O   . GLU D 2 131 ? 81.703  -22.650 23.055  1.00 150.53 ? 131 GLU D O   1 
ATOM   9907  C CB  . GLU D 2 131 ? 83.035  -19.794 23.935  1.00 135.49 ? 131 GLU D CB  1 
ATOM   9908  C CG  . GLU D 2 131 ? 83.394  -20.742 25.069  1.00 133.52 ? 131 GLU D CG  1 
ATOM   9909  C CD  . GLU D 2 131 ? 83.278  -20.099 26.437  1.00 130.71 ? 131 GLU D CD  1 
ATOM   9910  O OE1 . GLU D 2 131 ? 82.855  -18.927 26.514  1.00 132.00 ? 131 GLU D OE1 1 
ATOM   9911  O OE2 . GLU D 2 131 ? 83.608  -20.770 27.437  1.00 129.36 ? 131 GLU D OE2 1 
ATOM   9912  N N   . ALA D 2 132 ? 80.287  -20.917 22.892  1.00 168.65 ? 132 ALA D N   1 
ATOM   9913  C CA  . ALA D 2 132 ? 79.100  -21.700 23.193  1.00 177.60 ? 132 ALA D CA  1 
ATOM   9914  C C   . ALA D 2 132 ? 78.028  -21.428 22.150  1.00 203.46 ? 132 ALA D C   1 
ATOM   9915  O O   . ALA D 2 132 ? 77.912  -20.315 21.632  1.00 203.69 ? 132 ALA D O   1 
ATOM   9916  C CB  . ALA D 2 132 ? 78.562  -21.385 24.594  1.00 164.93 ? 132 ALA D CB  1 
ATOM   9917  N N   . SER D 2 133 ? 77.243  -22.460 21.845  1.00 262.54 ? 133 SER D N   1 
ATOM   9918  C CA  . SER D 2 133 ? 76.204  -22.362 20.830  1.00 261.36 ? 133 SER D CA  1 
ATOM   9919  C C   . SER D 2 133 ? 74.931  -23.022 21.332  1.00 259.91 ? 133 SER D C   1 
ATOM   9920  O O   . SER D 2 133 ? 74.975  -24.120 21.894  1.00 260.02 ? 133 SER D O   1 
ATOM   9921  C CB  . SER D 2 133 ? 76.638  -23.021 19.518  1.00 261.93 ? 133 SER D CB  1 
ATOM   9922  O OG  . SER D 2 133 ? 75.644  -22.873 18.518  1.00 260.86 ? 133 SER D OG  1 
ATOM   9923  N N   . ILE D 2 134 ? 73.803  -22.344 21.131  1.00 204.48 ? 134 ILE D N   1 
ATOM   9924  C CA  . ILE D 2 134 ? 72.487  -22.908 21.385  1.00 185.32 ? 134 ILE D CA  1 
ATOM   9925  C C   . ILE D 2 134 ? 71.659  -22.758 20.117  1.00 171.79 ? 134 ILE D C   1 
ATOM   9926  O O   . ILE D 2 134 ? 72.019  -22.029 19.192  1.00 173.10 ? 134 ILE D O   1 
ATOM   9927  C CB  . ILE D 2 134 ? 71.769  -22.242 22.577  1.00 178.37 ? 134 ILE D CB  1 
ATOM   9928  C CG1 . ILE D 2 134 ? 71.387  -20.803 22.232  1.00 174.57 ? 134 ILE D CG1 1 
ATOM   9929  C CG2 . ILE D 2 134 ? 72.643  -22.280 23.818  1.00 187.74 ? 134 ILE D CG2 1 
ATOM   9930  C CD1 . ILE D 2 134 ? 70.559  -20.126 23.298  1.00 169.89 ? 134 ILE D CD1 1 
ATOM   9931  N N   . MET D 2 135 ? 70.537  -23.465 20.085  1.00 162.99 ? 135 MET D N   1 
ATOM   9932  C CA  . MET D 2 135 ? 69.594  -23.369 18.985  1.00 160.15 ? 135 MET D CA  1 
ATOM   9933  C C   . MET D 2 135 ? 68.325  -22.680 19.462  1.00 161.68 ? 135 MET D C   1 
ATOM   9934  O O   . MET D 2 135 ? 67.903  -22.838 20.610  1.00 160.23 ? 135 MET D O   1 
ATOM   9935  C CB  . MET D 2 135 ? 69.261  -24.746 18.409  1.00 152.22 ? 135 MET D CB  1 
ATOM   9936  C CG  . MET D 2 135 ? 70.414  -25.387 17.667  1.00 150.47 ? 135 MET D CG  1 
ATOM   9937  S SD  . MET D 2 135 ? 71.040  -24.324 16.351  1.00 164.98 ? 135 MET D SD  1 
ATOM   9938  C CE  . MET D 2 135 ? 69.636  -24.281 15.243  1.00 172.49 ? 135 MET D CE  1 
ATOM   9939  N N   . VAL D 2 136 ? 67.721  -21.911 18.563  1.00 163.56 ? 136 VAL D N   1 
ATOM   9940  C CA  . VAL D 2 136 ? 66.599  -21.046 18.892  1.00 161.86 ? 136 VAL D CA  1 
ATOM   9941  C C   . VAL D 2 136 ? 65.512  -21.241 17.846  1.00 165.25 ? 136 VAL D C   1 
ATOM   9942  O O   . VAL D 2 136 ? 65.800  -21.334 16.648  1.00 177.17 ? 136 VAL D O   1 
ATOM   9943  C CB  . VAL D 2 136 ? 67.040  -19.568 18.964  1.00 167.13 ? 136 VAL D CB  1 
ATOM   9944  C CG1 . VAL D 2 136 ? 65.844  -18.662 19.116  1.00 169.22 ? 136 VAL D CG1 1 
ATOM   9945  C CG2 . VAL D 2 136 ? 68.015  -19.357 20.115  1.00 165.53 ? 136 VAL D CG2 1 
ATOM   9946  N N   . THR D 2 137 ? 64.263  -21.310 18.300  1.00 162.76 ? 137 THR D N   1 
ATOM   9947  C CA  . THR D 2 137 ? 63.120  -21.468 17.414  1.00 156.76 ? 137 THR D CA  1 
ATOM   9948  C C   . THR D 2 137 ? 62.094  -20.384 17.706  1.00 155.42 ? 137 THR D C   1 
ATOM   9949  O O   . THR D 2 137 ? 61.921  -19.971 18.857  1.00 159.20 ? 137 THR D O   1 
ATOM   9950  C CB  . THR D 2 137 ? 62.477  -22.853 17.568  1.00 149.34 ? 137 THR D CB  1 
ATOM   9951  O OG1 . THR D 2 137 ? 61.279  -22.915 16.786  1.00 145.57 ? 137 THR D OG1 1 
ATOM   9952  C CG2 . THR D 2 137 ? 62.147  -23.136 19.027  1.00 147.86 ? 137 THR D CG2 1 
ATOM   9953  N N   . LYS D 2 138 ? 61.427  -19.919 16.653  1.00 146.06 ? 138 LYS D N   1 
ATOM   9954  C CA  . LYS D 2 138 ? 60.391  -18.906 16.792  1.00 148.38 ? 138 LYS D CA  1 
ATOM   9955  C C   . LYS D 2 138 ? 59.102  -19.541 17.293  1.00 147.85 ? 138 LYS D C   1 
ATOM   9956  O O   . LYS D 2 138 ? 58.741  -20.651 16.891  1.00 146.55 ? 138 LYS D O   1 
ATOM   9957  C CB  . LYS D 2 138 ? 60.130  -18.207 15.458  1.00 149.95 ? 138 LYS D CB  1 
ATOM   9958  C CG  . LYS D 2 138 ? 59.863  -19.166 14.310  1.00 148.25 ? 138 LYS D CG  1 
ATOM   9959  C CD  . LYS D 2 138 ? 59.250  -18.459 13.115  1.00 147.42 ? 138 LYS D CD  1 
ATOM   9960  C CE  . LYS D 2 138 ? 58.879  -19.458 12.035  1.00 148.04 ? 138 LYS D CE  1 
ATOM   9961  N NZ  . LYS D 2 138 ? 57.967  -20.507 12.571  1.00 152.80 ? 138 LYS D NZ  1 
ATOM   9962  N N   . VAL D 2 139 ? 58.409  -18.834 18.180  1.00 150.89 ? 139 VAL D N   1 
ATOM   9963  C CA  . VAL D 2 139 ? 57.130  -19.292 18.701  1.00 149.81 ? 139 VAL D CA  1 
ATOM   9964  C C   . VAL D 2 139 ? 56.112  -18.170 18.574  1.00 151.19 ? 139 VAL D C   1 
ATOM   9965  O O   . VAL D 2 139 ? 56.451  -16.984 18.631  1.00 151.84 ? 139 VAL D O   1 
ATOM   9966  C CB  . VAL D 2 139 ? 57.236  -19.764 20.167  1.00 155.68 ? 139 VAL D CB  1 
ATOM   9967  C CG1 . VAL D 2 139 ? 58.119  -20.995 20.263  1.00 156.00 ? 139 VAL D CG1 1 
ATOM   9968  C CG2 . VAL D 2 139 ? 57.769  -18.645 21.046  1.00 158.48 ? 139 VAL D CG2 1 
ATOM   9969  N N   . ASP D 2 140 ? 54.848  -18.558 18.389  1.00 150.22 ? 140 ASP D N   1 
ATOM   9970  C CA  . ASP D 2 140 ? 53.780  -17.570 18.318  1.00 148.25 ? 140 ASP D CA  1 
ATOM   9971  C C   . ASP D 2 140 ? 53.457  -17.008 19.695  1.00 151.66 ? 140 ASP D C   1 
ATOM   9972  O O   . ASP D 2 140 ? 52.980  -15.873 19.803  1.00 152.40 ? 140 ASP D O   1 
ATOM   9973  C CB  . ASP D 2 140 ? 52.534  -18.189 17.686  1.00 147.01 ? 140 ASP D CB  1 
ATOM   9974  C CG  . ASP D 2 140 ? 52.803  -18.773 16.313  1.00 147.18 ? 140 ASP D CG  1 
ATOM   9975  O OD1 . ASP D 2 140 ? 53.713  -18.272 15.618  1.00 143.14 ? 140 ASP D OD1 1 
ATOM   9976  O OD2 . ASP D 2 140 ? 52.107  -19.735 15.928  1.00 149.32 ? 140 ASP D OD2 1 
ATOM   9977  N N   . GLU D 2 141 ? 53.701  -17.787 20.751  1.00 159.87 ? 141 GLU D N   1 
ATOM   9978  C CA  . GLU D 2 141 ? 53.451  -17.384 22.133  1.00 164.61 ? 141 GLU D CA  1 
ATOM   9979  C C   . GLU D 2 141 ? 54.781  -17.236 22.862  1.00 167.66 ? 141 GLU D C   1 
ATOM   9980  O O   . GLU D 2 141 ? 55.284  -18.205 23.448  1.00 170.80 ? 141 GLU D O   1 
ATOM   9981  C CB  . GLU D 2 141 ? 52.560  -18.407 22.843  1.00 163.88 ? 141 GLU D CB  1 
ATOM   9982  C CG  . GLU D 2 141 ? 51.154  -18.518 22.283  1.00 163.75 ? 141 GLU D CG  1 
ATOM   9983  C CD  . GLU D 2 141 ? 50.247  -17.408 22.774  1.00 164.23 ? 141 GLU D CD  1 
ATOM   9984  O OE1 . GLU D 2 141 ? 50.642  -16.693 23.719  1.00 163.26 ? 141 GLU D OE1 1 
ATOM   9985  O OE2 . GLU D 2 141 ? 49.141  -17.249 22.217  1.00 167.85 ? 141 GLU D OE2 1 
ATOM   9986  N N   . PRO D 2 142 ? 55.393  -16.048 22.863  1.00 173.30 ? 142 PRO D N   1 
ATOM   9987  C CA  . PRO D 2 142 ? 56.649  -15.868 23.604  1.00 176.38 ? 142 PRO D CA  1 
ATOM   9988  C C   . PRO D 2 142 ? 56.462  -15.619 25.093  1.00 186.46 ? 142 PRO D C   1 
ATOM   9989  O O   . PRO D 2 142 ? 57.436  -15.748 25.848  1.00 181.80 ? 142 PRO D O   1 
ATOM   9990  C CB  . PRO D 2 142 ? 57.280  -14.649 22.921  1.00 171.68 ? 142 PRO D CB  1 
ATOM   9991  C CG  . PRO D 2 142 ? 56.113  -13.859 22.440  1.00 170.09 ? 142 PRO D CG  1 
ATOM   9992  C CD  . PRO D 2 142 ? 55.044  -14.858 22.067  1.00 167.46 ? 142 PRO D CD  1 
ATOM   9993  N N   . SER D 2 143 ? 55.251  -15.288 25.543  1.00 216.24 ? 143 SER D N   1 
ATOM   9994  C CA  . SER D 2 143 ? 55.046  -14.998 26.959  1.00 217.09 ? 143 SER D CA  1 
ATOM   9995  C C   . SER D 2 143 ? 55.091  -16.267 27.802  1.00 217.16 ? 143 SER D C   1 
ATOM   9996  O O   . SER D 2 143 ? 55.631  -16.262 28.913  1.00 217.62 ? 143 SER D O   1 
ATOM   9997  C CB  . SER D 2 143 ? 53.715  -14.272 27.158  1.00 217.62 ? 143 SER D CB  1 
ATOM   9998  O OG  . SER D 2 143 ? 52.625  -15.094 26.775  1.00 217.08 ? 143 SER D OG  1 
ATOM   9999  N N   . LYS D 2 144 ? 54.536  -17.365 27.289  1.00 191.38 ? 144 LYS D N   1 
ATOM   10000 C CA  . LYS D 2 144 ? 54.517  -18.620 28.028  1.00 187.22 ? 144 LYS D CA  1 
ATOM   10001 C C   . LYS D 2 144 ? 55.890  -19.273 28.123  1.00 184.72 ? 144 LYS D C   1 
ATOM   10002 O O   . LYS D 2 144 ? 56.041  -20.249 28.866  1.00 182.39 ? 144 LYS D O   1 
ATOM   10003 C CB  . LYS D 2 144 ? 53.521  -19.585 27.379  1.00 179.84 ? 144 LYS D CB  1 
ATOM   10004 C CG  . LYS D 2 144 ? 52.109  -19.028 27.282  1.00 172.25 ? 144 LYS D CG  1 
ATOM   10005 C CD  . LYS D 2 144 ? 51.175  -19.982 26.558  1.00 161.97 ? 144 LYS D CD  1 
ATOM   10006 C CE  . LYS D 2 144 ? 51.058  -21.308 27.287  1.00 158.17 ? 144 LYS D CE  1 
ATOM   10007 N NZ  . LYS D 2 144 ? 50.122  -22.235 26.593  1.00 154.60 ? 144 LYS D NZ  1 
ATOM   10008 N N   . TYR D 2 145 ? 56.883  -18.764 27.405  1.00 182.70 ? 145 TYR D N   1 
ATOM   10009 C CA  . TYR D 2 145 ? 58.228  -19.318 27.386  1.00 178.46 ? 145 TYR D CA  1 
ATOM   10010 C C   . TYR D 2 145 ? 59.227  -18.265 27.856  1.00 179.64 ? 145 TYR D C   1 
ATOM   10011 O O   . TYR D 2 145 ? 58.871  -17.118 28.144  1.00 178.01 ? 145 TYR D O   1 
ATOM   10012 C CB  . TYR D 2 145 ? 58.593  -19.805 25.981  1.00 177.25 ? 145 TYR D CB  1 
ATOM   10013 C CG  . TYR D 2 145 ? 57.578  -20.736 25.360  1.00 182.28 ? 145 TYR D CG  1 
ATOM   10014 C CD1 . TYR D 2 145 ? 56.993  -21.756 26.097  1.00 187.73 ? 145 TYR D CD1 1 
ATOM   10015 C CD2 . TYR D 2 145 ? 57.193  -20.581 24.035  1.00 184.15 ? 145 TYR D CD2 1 
ATOM   10016 C CE1 . TYR D 2 145 ? 56.062  -22.605 25.526  1.00 193.83 ? 145 TYR D CE1 1 
ATOM   10017 C CE2 . TYR D 2 145 ? 56.265  -21.421 23.457  1.00 190.23 ? 145 TYR D CE2 1 
ATOM   10018 C CZ  . TYR D 2 145 ? 55.702  -22.431 24.206  1.00 192.82 ? 145 TYR D CZ  1 
ATOM   10019 O OH  . TYR D 2 145 ? 54.775  -23.269 23.629  1.00 190.46 ? 145 TYR D OH  1 
ATOM   10020 N N   . GLY D 2 146 ? 60.492  -18.670 27.935  1.00 171.77 ? 146 GLY D N   1 
ATOM   10021 C CA  . GLY D 2 146 ? 61.564  -17.745 28.241  1.00 164.07 ? 146 GLY D CA  1 
ATOM   10022 C C   . GLY D 2 146 ? 62.166  -17.177 26.973  1.00 166.84 ? 146 GLY D C   1 
ATOM   10023 O O   . GLY D 2 146 ? 62.770  -17.911 26.184  1.00 171.71 ? 146 GLY D O   1 
ATOM   10024 N N   . VAL D 2 147 ? 62.011  -15.873 26.766  1.00 166.14 ? 147 VAL D N   1 
ATOM   10025 C CA  . VAL D 2 147 ? 62.421  -15.242 25.517  1.00 173.20 ? 147 VAL D CA  1 
ATOM   10026 C C   . VAL D 2 147 ? 63.912  -14.945 25.556  1.00 182.26 ? 147 VAL D C   1 
ATOM   10027 O O   . VAL D 2 147 ? 64.453  -14.502 26.577  1.00 180.58 ? 147 VAL D O   1 
ATOM   10028 C CB  . VAL D 2 147 ? 61.606  -13.963 25.262  1.00 169.04 ? 147 VAL D CB  1 
ATOM   10029 C CG1 . VAL D 2 147 ? 61.968  -13.359 23.914  1.00 177.46 ? 147 VAL D CG1 1 
ATOM   10030 C CG2 . VAL D 2 147 ? 60.125  -14.264 25.321  1.00 167.02 ? 147 VAL D CG2 1 
ATOM   10031 N N   . VAL D 2 148 ? 64.582  -15.190 24.434  1.00 214.68 ? 148 VAL D N   1 
ATOM   10032 C CA  . VAL D 2 148 ? 65.994  -14.878 24.265  1.00 214.96 ? 148 VAL D CA  1 
ATOM   10033 C C   . VAL D 2 148 ? 66.092  -13.638 23.389  1.00 215.27 ? 148 VAL D C   1 
ATOM   10034 O O   . VAL D 2 148 ? 65.653  -13.649 22.233  1.00 214.83 ? 148 VAL D O   1 
ATOM   10035 C CB  . VAL D 2 148 ? 66.759  -16.056 23.644  1.00 216.27 ? 148 VAL D CB  1 
ATOM   10036 C CG1 . VAL D 2 148 ? 68.205  -15.672 23.390  1.00 215.26 ? 148 VAL D CG1 1 
ATOM   10037 C CG2 . VAL D 2 148 ? 66.673  -17.277 24.545  1.00 214.38 ? 148 VAL D CG2 1 
ATOM   10038 N N   . VAL D 2 149 ? 66.669  -12.569 23.933  1.00 191.13 ? 149 VAL D N   1 
ATOM   10039 C CA  . VAL D 2 149 ? 66.757  -11.292 23.234  1.00 182.96 ? 149 VAL D CA  1 
ATOM   10040 C C   . VAL D 2 149 ? 68.119  -11.237 22.546  1.00 183.05 ? 149 VAL D C   1 
ATOM   10041 O O   . VAL D 2 149 ? 69.131  -10.875 23.150  1.00 190.06 ? 149 VAL D O   1 
ATOM   10042 C CB  . VAL D 2 149 ? 66.535  -10.110 24.179  1.00 174.25 ? 149 VAL D CB  1 
ATOM   10043 C CG1 . VAL D 2 149 ? 65.046  -9.899  24.404  1.00 178.09 ? 149 VAL D CG1 1 
ATOM   10044 C CG2 . VAL D 2 149 ? 67.228  -10.350 25.510  1.00 175.79 ? 149 VAL D CG2 1 
ATOM   10045 N N   . MET D 2 150 ? 68.140  -11.608 21.271  1.00 170.74 ? 150 MET D N   1 
ATOM   10046 C CA  . MET D 2 150 ? 69.335  -11.576 20.445  1.00 171.13 ? 150 MET D CA  1 
ATOM   10047 C C   . MET D 2 150 ? 69.218  -10.477 19.396  1.00 164.58 ? 150 MET D C   1 
ATOM   10048 O O   . MET D 2 150 ? 68.129  -9.973  19.112  1.00 162.69 ? 150 MET D O   1 
ATOM   10049 C CB  . MET D 2 150 ? 69.558  -12.932 19.769  1.00 175.46 ? 150 MET D CB  1 
ATOM   10050 C CG  . MET D 2 150 ? 68.352  -13.420 18.981  1.00 170.22 ? 150 MET D CG  1 
ATOM   10051 S SD  . MET D 2 150 ? 68.528  -15.104 18.367  1.00 175.18 ? 150 MET D SD  1 
ATOM   10052 C CE  . MET D 2 150 ? 69.794  -14.890 17.120  1.00 173.76 ? 150 MET D CE  1 
ATOM   10053 N N   . GLU D 2 151 ? 70.360  -10.107 18.820  1.00 161.67 ? 151 GLU D N   1 
ATOM   10054 C CA  . GLU D 2 151 ? 70.377  -9.160  17.713  1.00 157.05 ? 151 GLU D CA  1 
ATOM   10055 C C   . GLU D 2 151 ? 70.265  -9.907  16.389  1.00 157.49 ? 151 GLU D C   1 
ATOM   10056 O O   . GLU D 2 151 ? 70.787  -11.016 16.238  1.00 158.09 ? 151 GLU D O   1 
ATOM   10057 C CB  . GLU D 2 151 ? 71.642  -8.295  17.733  1.00 152.51 ? 151 GLU D CB  1 
ATOM   10058 C CG  . GLU D 2 151 ? 72.884  -8.938  17.138  1.00 154.20 ? 151 GLU D CG  1 
ATOM   10059 C CD  . GLU D 2 151 ? 73.583  -9.875  18.095  1.00 159.75 ? 151 GLU D CD  1 
ATOM   10060 O OE1 . GLU D 2 151 ? 73.558  -9.605  19.313  1.00 163.80 ? 151 GLU D OE1 1 
ATOM   10061 O OE2 . GLU D 2 151 ? 74.161  -10.879 17.628  1.00 161.02 ? 151 GLU D OE2 1 
ATOM   10062 N N   . GLU D 2 152 ? 69.554  -9.299  15.437  1.00 156.60 ? 152 GLU D N   1 
ATOM   10063 C CA  . GLU D 2 152 ? 69.304  -9.907  14.136  1.00 152.89 ? 152 GLU D CA  1 
ATOM   10064 C C   . GLU D 2 152 ? 70.424  -9.644  13.136  1.00 148.63 ? 152 GLU D C   1 
ATOM   10065 O O   . GLU D 2 152 ? 70.154  -9.492  11.936  1.00 148.25 ? 152 GLU D O   1 
ATOM   10066 C CB  . GLU D 2 152 ? 67.966  -9.416  13.580  1.00 149.90 ? 152 GLU D CB  1 
ATOM   10067 N N   . SER D 2 153 ? 71.670  -9.587  13.591  1.00 147.76 ? 153 SER D N   1 
ATOM   10068 C CA  . SER D 2 153 ? 72.801  -9.331  12.705  1.00 149.58 ? 153 SER D CA  1 
ATOM   10069 C C   . SER D 2 153 ? 73.900  -10.376 12.825  1.00 150.23 ? 153 SER D C   1 
ATOM   10070 O O   . SER D 2 153 ? 74.475  -10.771 11.806  1.00 149.26 ? 153 SER D O   1 
ATOM   10071 C CB  . SER D 2 153 ? 73.382  -7.931  12.979  1.00 149.89 ? 153 SER D CB  1 
ATOM   10072 O OG  . SER D 2 153 ? 73.883  -7.834  14.302  1.00 150.12 ? 153 SER D OG  1 
ATOM   10073 N N   . THR D 2 154 ? 74.202  -10.837 14.033  1.00 153.16 ? 154 THR D N   1 
ATOM   10074 C CA  . THR D 2 154 ? 75.251  -11.830 14.246  1.00 151.83 ? 154 THR D CA  1 
ATOM   10075 C C   . THR D 2 154 ? 74.764  -13.055 15.006  1.00 153.83 ? 154 THR D C   1 
ATOM   10076 O O   . THR D 2 154 ? 75.137  -14.177 14.652  1.00 152.38 ? 154 THR D O   1 
ATOM   10077 C CB  . THR D 2 154 ? 76.439  -11.197 14.995  1.00 145.66 ? 154 THR D CB  1 
ATOM   10078 O OG1 . THR D 2 154 ? 75.974  -10.577 16.202  1.00 146.15 ? 154 THR D OG1 1 
ATOM   10079 C CG2 . THR D 2 154 ? 77.123  -10.152 14.127  1.00 142.92 ? 154 THR D CG2 1 
ATOM   10080 N N   . GLY D 2 155 ? 73.943  -12.873 16.038  1.00 157.57 ? 155 GLY D N   1 
ATOM   10081 C CA  . GLY D 2 155 ? 73.379  -13.998 16.758  1.00 160.26 ? 155 GLY D CA  1 
ATOM   10082 C C   . GLY D 2 155 ? 73.792  -14.064 18.212  1.00 168.94 ? 155 GLY D C   1 
ATOM   10083 O O   . GLY D 2 155 ? 73.792  -15.142 18.813  1.00 175.90 ? 155 GLY D O   1 
ATOM   10084 N N   . ARG D 2 156 ? 74.134  -12.921 18.795  1.00 167.18 ? 156 ARG D N   1 
ATOM   10085 C CA  . ARG D 2 156 ? 74.561  -12.862 20.185  1.00 182.86 ? 156 ARG D CA  1 
ATOM   10086 C C   . ARG D 2 156 ? 73.381  -12.541 21.093  1.00 194.47 ? 156 ARG D C   1 
ATOM   10087 O O   . ARG D 2 156 ? 72.551  -11.684 20.779  1.00 183.29 ? 156 ARG D O   1 
ATOM   10088 C CB  . ARG D 2 156 ? 75.660  -11.813 20.362  1.00 178.79 ? 156 ARG D CB  1 
ATOM   10089 C CG  . ARG D 2 156 ? 76.358  -11.859 21.709  1.00 180.68 ? 156 ARG D CG  1 
ATOM   10090 C CD  . ARG D 2 156 ? 77.431  -10.788 21.802  1.00 172.23 ? 156 ARG D CD  1 
ATOM   10091 N NE  . ARG D 2 156 ? 78.348  -10.840 20.667  1.00 172.15 ? 156 ARG D NE  1 
ATOM   10092 C CZ  . ARG D 2 156 ? 79.316  -9.957  20.445  1.00 173.88 ? 156 ARG D CZ  1 
ATOM   10093 N NH1 . ARG D 2 156 ? 79.497  -8.944  21.282  1.00 169.05 ? 156 ARG D NH1 1 
ATOM   10094 N NH2 . ARG D 2 156 ? 80.104  -10.085 19.387  1.00 178.42 ? 156 ARG D NH2 1 
ATOM   10095 N N   . VAL D 2 157 ? 73.309  -13.239 22.219  1.00 247.62 ? 157 VAL D N   1 
ATOM   10096 C CA  . VAL D 2 157 ? 72.226  -13.066 23.170  1.00 246.45 ? 157 VAL D CA  1 
ATOM   10097 C C   . VAL D 2 157 ? 72.697  -12.127 24.272  1.00 247.13 ? 157 VAL D C   1 
ATOM   10098 O O   . VAL D 2 157 ? 73.895  -11.905 24.470  1.00 248.49 ? 157 VAL D O   1 
ATOM   10099 C CB  . VAL D 2 157 ? 71.745  -14.417 23.748  1.00 245.75 ? 157 VAL D CB  1 
ATOM   10100 C CG1 . VAL D 2 157 ? 71.741  -15.480 22.659  1.00 245.61 ? 157 VAL D CG1 1 
ATOM   10101 C CG2 . VAL D 2 157 ? 72.613  -14.842 24.917  1.00 246.65 ? 157 VAL D CG2 1 
ATOM   10102 N N   . GLU D 2 158 ? 71.739  -11.557 25.002  1.00 212.35 ? 158 GLU D N   1 
ATOM   10103 C CA  . GLU D 2 158 ? 72.070  -10.522 25.975  1.00 207.46 ? 158 GLU D CA  1 
ATOM   10104 C C   . GLU D 2 158 ? 71.455  -10.781 27.346  1.00 201.72 ? 158 GLU D C   1 
ATOM   10105 O O   . GLU D 2 158 ? 72.160  -10.735 28.360  1.00 199.69 ? 158 GLU D O   1 
ATOM   10106 C CB  . GLU D 2 158 ? 71.629  -9.151  25.454  1.00 211.20 ? 158 GLU D CB  1 
ATOM   10107 C CG  . GLU D 2 158 ? 72.272  -8.755  24.135  1.00 213.33 ? 158 GLU D CG  1 
ATOM   10108 C CD  . GLU D 2 158 ? 71.793  -7.410  23.630  1.00 223.25 ? 158 GLU D CD  1 
ATOM   10109 O OE1 . GLU D 2 158 ? 70.853  -6.847  24.228  1.00 224.47 ? 158 GLU D OE1 1 
ATOM   10110 O OE2 . GLU D 2 158 ? 72.362  -6.914  22.635  1.00 225.15 ? 158 GLU D OE2 1 
ATOM   10111 N N   . LYS D 2 159 ? 70.152  -11.056 27.393  1.00 194.19 ? 159 LYS D N   1 
ATOM   10112 C CA  . LYS D 2 159 ? 69.433  -11.167 28.655  1.00 189.77 ? 159 LYS D CA  1 
ATOM   10113 C C   . LYS D 2 159 ? 68.364  -12.244 28.532  1.00 193.69 ? 159 LYS D C   1 
ATOM   10114 O O   . LYS D 2 159 ? 68.064  -12.735 27.440  1.00 191.08 ? 159 LYS D O   1 
ATOM   10115 C CB  . LYS D 2 159 ? 68.807  -9.822  29.053  1.00 182.58 ? 159 LYS D CB  1 
ATOM   10116 C CG  . LYS D 2 159 ? 68.584  -9.626  30.547  1.00 177.20 ? 159 LYS D CG  1 
ATOM   10117 C CD  . LYS D 2 159 ? 69.904  -9.647  31.305  1.00 171.30 ? 159 LYS D CD  1 
ATOM   10118 C CE  . LYS D 2 159 ? 69.706  -9.346  32.781  1.00 159.99 ? 159 LYS D CE  1 
ATOM   10119 N NZ  . LYS D 2 159 ? 68.786  -10.317 33.429  1.00 172.36 ? 159 LYS D NZ  1 
ATOM   10120 N N   . PHE D 2 160 ? 67.790  -12.617 29.675  1.00 214.54 ? 160 PHE D N   1 
ATOM   10121 C CA  . PHE D 2 160 ? 66.718  -13.605 29.745  1.00 214.40 ? 160 PHE D CA  1 
ATOM   10122 C C   . PHE D 2 160 ? 65.462  -12.923 30.269  1.00 213.92 ? 160 PHE D C   1 
ATOM   10123 O O   . PHE D 2 160 ? 65.455  -12.398 31.387  1.00 214.49 ? 160 PHE D O   1 
ATOM   10124 C CB  . PHE D 2 160 ? 67.117  -14.798 30.623  1.00 217.76 ? 160 PHE D CB  1 
ATOM   10125 C CG  . PHE D 2 160 ? 67.457  -14.435 32.047  1.00 220.23 ? 160 PHE D CG  1 
ATOM   10126 C CD1 . PHE D 2 160 ? 66.571  -14.716 33.075  1.00 220.18 ? 160 PHE D CD1 1 
ATOM   10127 C CD2 . PHE D 2 160 ? 68.664  -13.829 32.358  1.00 216.04 ? 160 PHE D CD2 1 
ATOM   10128 C CE1 . PHE D 2 160 ? 66.879  -14.390 34.383  1.00 217.44 ? 160 PHE D CE1 1 
ATOM   10129 C CE2 . PHE D 2 160 ? 68.975  -13.500 33.663  1.00 214.99 ? 160 PHE D CE2 1 
ATOM   10130 C CZ  . PHE D 2 160 ? 68.083  -13.781 34.676  1.00 215.70 ? 160 PHE D CZ  1 
ATOM   10131 N N   . VAL D 2 161 ? 64.412  -12.911 29.452  1.00 187.87 ? 161 VAL D N   1 
ATOM   10132 C CA  . VAL D 2 161 ? 63.157  -12.244 29.782  1.00 179.07 ? 161 VAL D CA  1 
ATOM   10133 C C   . VAL D 2 161 ? 62.066  -13.306 29.793  1.00 176.06 ? 161 VAL D C   1 
ATOM   10134 O O   . VAL D 2 161 ? 61.564  -13.706 28.735  1.00 170.02 ? 161 VAL D O   1 
ATOM   10135 C CB  . VAL D 2 161 ? 62.827  -11.117 28.798  1.00 169.26 ? 161 VAL D CB  1 
ATOM   10136 C CG1 . VAL D 2 161 ? 61.549  -10.409 29.218  1.00 170.16 ? 161 VAL D CG1 1 
ATOM   10137 C CG2 . VAL D 2 161 ? 63.984  -10.135 28.704  1.00 170.86 ? 161 VAL D CG2 1 
ATOM   10138 N N   . GLU D 2 162 ? 61.697  -13.770 30.983  1.00 180.28 ? 162 GLU D N   1 
ATOM   10139 C CA  . GLU D 2 162 ? 60.624  -14.739 31.138  1.00 182.12 ? 162 GLU D CA  1 
ATOM   10140 C C   . GLU D 2 162 ? 59.301  -14.014 31.355  1.00 183.79 ? 162 GLU D C   1 
ATOM   10141 O O   . GLU D 2 162 ? 59.233  -13.026 32.094  1.00 183.03 ? 162 GLU D O   1 
ATOM   10142 C CB  . GLU D 2 162 ? 60.912  -15.689 32.304  1.00 182.29 ? 162 GLU D CB  1 
ATOM   10143 C CG  . GLU D 2 162 ? 60.833  -15.057 33.692  1.00 185.01 ? 162 GLU D CG  1 
ATOM   10144 C CD  . GLU D 2 162 ? 62.022  -14.171 34.016  1.00 188.31 ? 162 GLU D CD  1 
ATOM   10145 O OE1 . GLU D 2 162 ? 62.964  -14.102 33.198  1.00 186.56 ? 162 GLU D OE1 1 
ATOM   10146 O OE2 . GLU D 2 162 ? 62.011  -13.534 35.090  1.00 192.93 ? 162 GLU D OE2 1 
ATOM   10147 N N   . LYS D 2 163 ? 58.251  -14.509 30.696  1.00 177.71 ? 163 LYS D N   1 
ATOM   10148 C CA  . LYS D 2 163 ? 56.912  -13.924 30.726  1.00 174.24 ? 163 LYS D CA  1 
ATOM   10149 C C   . LYS D 2 163 ? 56.968  -12.416 30.493  1.00 171.81 ? 163 LYS D C   1 
ATOM   10150 O O   . LYS D 2 163 ? 56.762  -11.632 31.429  1.00 166.78 ? 163 LYS D O   1 
ATOM   10151 C CB  . LYS D 2 163 ? 56.226  -14.247 32.058  1.00 169.45 ? 163 LYS D CB  1 
ATOM   10152 C CG  . LYS D 2 163 ? 54.769  -13.802 32.165  1.00 166.09 ? 163 LYS D CG  1 
ATOM   10153 C CD  . LYS D 2 163 ? 53.942  -14.277 30.981  1.00 172.32 ? 163 LYS D CD  1 
ATOM   10154 C CE  . LYS D 2 163 ? 52.538  -13.693 31.026  1.00 164.26 ? 163 LYS D CE  1 
ATOM   10155 N NZ  . LYS D 2 163 ? 52.552  -12.204 31.006  1.00 160.78 ? 163 LYS D NZ  1 
ATOM   10156 N N   . PRO D 2 164 ? 57.270  -11.968 29.271  1.00 172.65 ? 164 PRO D N   1 
ATOM   10157 C CA  . PRO D 2 164 ? 57.275  -10.525 28.987  1.00 173.52 ? 164 PRO D CA  1 
ATOM   10158 C C   . PRO D 2 164 ? 55.857  -10.032 28.738  1.00 179.05 ? 164 PRO D C   1 
ATOM   10159 O O   . PRO D 2 164 ? 55.178  -10.501 27.822  1.00 182.32 ? 164 PRO D O   1 
ATOM   10160 C CB  . PRO D 2 164 ? 58.140  -10.413 27.722  1.00 173.40 ? 164 PRO D CB  1 
ATOM   10161 C CG  . PRO D 2 164 ? 58.708  -11.789 27.483  1.00 168.93 ? 164 PRO D CG  1 
ATOM   10162 C CD  . PRO D 2 164 ? 57.761  -12.743 28.124  1.00 173.34 ? 164 PRO D CD  1 
ATOM   10163 N N   . LYS D 2 165 ? 55.409  -9.076  29.556  1.00 184.94 ? 165 LYS D N   1 
ATOM   10164 C CA  . LYS D 2 165 ? 54.090  -8.494  29.334  1.00 188.89 ? 165 LYS D CA  1 
ATOM   10165 C C   . LYS D 2 165 ? 54.073  -7.647  28.068  1.00 191.25 ? 165 LYS D C   1 
ATOM   10166 O O   . LYS D 2 165 ? 53.083  -7.649  27.326  1.00 191.38 ? 165 LYS D O   1 
ATOM   10167 C CB  . LYS D 2 165 ? 53.662  -7.676  30.552  1.00 186.54 ? 165 LYS D CB  1 
ATOM   10168 C CG  . LYS D 2 165 ? 53.257  -8.535  31.745  1.00 181.61 ? 165 LYS D CG  1 
ATOM   10169 C CD  . LYS D 2 165 ? 52.601  -7.717  32.846  1.00 177.28 ? 165 LYS D CD  1 
ATOM   10170 C CE  . LYS D 2 165 ? 51.191  -7.301  32.463  1.00 175.02 ? 165 LYS D CE  1 
ATOM   10171 N NZ  . LYS D 2 165 ? 50.851  -5.940  32.958  1.00 167.98 ? 165 LYS D NZ  1 
ATOM   10172 N N   . LEU D 2 166 ? 55.155  -6.923  27.802  1.00 192.37 ? 166 LEU D N   1 
ATOM   10173 C CA  . LEU D 2 166 ? 55.344  -6.223  26.541  1.00 193.32 ? 166 LEU D CA  1 
ATOM   10174 C C   . LEU D 2 166 ? 56.269  -7.026  25.633  1.00 192.37 ? 166 LEU D C   1 
ATOM   10175 O O   . LEU D 2 166 ? 56.935  -7.972  26.060  1.00 187.85 ? 166 LEU D O   1 
ATOM   10176 C CB  . LEU D 2 166 ? 55.908  -4.818  26.775  1.00 195.97 ? 166 LEU D CB  1 
ATOM   10177 C CG  . LEU D 2 166 ? 55.104  -3.664  26.172  1.00 194.27 ? 166 LEU D CG  1 
ATOM   10178 C CD1 . LEU D 2 166 ? 53.820  -3.432  26.957  1.00 194.66 ? 166 LEU D CD1 1 
ATOM   10179 C CD2 . LEU D 2 166 ? 55.935  -2.390  26.099  1.00 191.08 ? 166 LEU D CD2 1 
ATOM   10180 N N   . TYR D 2 167 ? 56.308  -6.636  24.361  1.00 188.78 ? 167 TYR D N   1 
ATOM   10181 C CA  . TYR D 2 167 ? 57.052  -7.390  23.359  1.00 184.89 ? 167 TYR D CA  1 
ATOM   10182 C C   . TYR D 2 167 ? 58.525  -7.005  23.417  1.00 191.95 ? 167 TYR D C   1 
ATOM   10183 O O   . TYR D 2 167 ? 58.895  -5.871  23.096  1.00 188.66 ? 167 TYR D O   1 
ATOM   10184 C CB  . TYR D 2 167 ? 56.481  -7.148  21.965  1.00 173.13 ? 167 TYR D CB  1 
ATOM   10185 C CG  . TYR D 2 167 ? 57.258  -7.837  20.863  1.00 168.58 ? 167 TYR D CG  1 
ATOM   10186 C CD1 . TYR D 2 167 ? 57.069  -9.186  20.592  1.00 169.45 ? 167 TYR D CD1 1 
ATOM   10187 C CD2 . TYR D 2 167 ? 58.173  -7.135  20.086  1.00 164.65 ? 167 TYR D CD2 1 
ATOM   10188 C CE1 . TYR D 2 167 ? 57.773  -9.818  19.585  1.00 168.90 ? 167 TYR D CE1 1 
ATOM   10189 C CE2 . TYR D 2 167 ? 58.881  -7.760  19.076  1.00 163.46 ? 167 TYR D CE2 1 
ATOM   10190 C CZ  . TYR D 2 167 ? 58.676  -9.100  18.830  1.00 164.38 ? 167 TYR D CZ  1 
ATOM   10191 O OH  . TYR D 2 167 ? 59.377  -9.726  17.825  1.00 165.30 ? 167 TYR D OH  1 
ATOM   10192 N N   . VAL D 2 168 ? 59.364  -7.953  23.823  1.00 224.95 ? 168 VAL D N   1 
ATOM   10193 C CA  . VAL D 2 168 ? 60.811  -7.817  23.708  1.00 225.29 ? 168 VAL D CA  1 
ATOM   10194 C C   . VAL D 2 168 ? 61.409  -8.829  22.748  1.00 224.33 ? 168 VAL D C   1 
ATOM   10195 O O   . VAL D 2 168 ? 62.609  -8.741  22.446  1.00 224.56 ? 168 VAL D O   1 
ATOM   10196 C CB  . VAL D 2 168 ? 61.503  -7.925  25.083  1.00 226.05 ? 168 VAL D CB  1 
ATOM   10197 C CG1 . VAL D 2 168 ? 61.140  -6.733  25.950  1.00 227.00 ? 168 VAL D CG1 1 
ATOM   10198 C CG2 . VAL D 2 168 ? 61.120  -9.226  25.764  1.00 225.40 ? 168 VAL D CG2 1 
ATOM   10199 N N   . GLY D 2 169 ? 60.623  -9.777  22.265  1.00 191.90 ? 169 GLY D N   1 
ATOM   10200 C CA  . GLY D 2 169 ? 61.101  -10.764 21.320  1.00 186.07 ? 169 GLY D CA  1 
ATOM   10201 C C   . GLY D 2 169 ? 60.131  -11.916 21.218  1.00 187.90 ? 169 GLY D C   1 
ATOM   10202 O O   . GLY D 2 169 ? 59.146  -12.007 21.952  1.00 186.66 ? 169 GLY D O   1 
ATOM   10203 N N   . ASN D 2 170 ? 60.432  -12.809 20.278  1.00 180.54 ? 170 ASN D N   1 
ATOM   10204 C CA  . ASN D 2 170 ? 59.634  -14.003 20.058  1.00 176.56 ? 170 ASN D CA  1 
ATOM   10205 C C   . ASN D 2 170 ? 60.475  -15.268 19.974  1.00 176.32 ? 170 ASN D C   1 
ATOM   10206 O O   . ASN D 2 170 ? 59.917  -16.352 19.772  1.00 172.10 ? 170 ASN D O   1 
ATOM   10207 C CB  . ASN D 2 170 ? 58.798  -13.860 18.778  1.00 172.57 ? 170 ASN D CB  1 
ATOM   10208 C CG  . ASN D 2 170 ? 59.563  -13.186 17.652  1.00 170.90 ? 170 ASN D CG  1 
ATOM   10209 O OD1 . ASN D 2 170 ? 59.266  -12.053 17.275  1.00 167.79 ? 170 ASN D OD1 1 
ATOM   10210 N ND2 . ASN D 2 170 ? 60.561  -13.880 17.116  1.00 168.93 ? 170 ASN D ND2 1 
ATOM   10211 N N   . LYS D 2 171 ? 61.791  -15.159 20.120  1.00 179.59 ? 171 LYS D N   1 
ATOM   10212 C CA  . LYS D 2 171 ? 62.713  -16.268 19.932  1.00 178.11 ? 171 LYS D CA  1 
ATOM   10213 C C   . LYS D 2 171 ? 63.028  -16.914 21.276  1.00 185.35 ? 171 LYS D C   1 
ATOM   10214 O O   . LYS D 2 171 ? 63.453  -16.230 22.213  1.00 185.82 ? 171 LYS D O   1 
ATOM   10215 C CB  . LYS D 2 171 ? 63.994  -15.770 19.265  1.00 174.49 ? 171 LYS D CB  1 
ATOM   10216 C CG  . LYS D 2 171 ? 63.758  -15.035 17.956  1.00 172.80 ? 171 LYS D CG  1 
ATOM   10217 C CD  . LYS D 2 171 ? 64.522  -13.722 17.919  1.00 173.81 ? 171 LYS D CD  1 
ATOM   10218 C CE  . LYS D 2 171 ? 64.062  -12.790 19.031  1.00 175.60 ? 171 LYS D CE  1 
ATOM   10219 N NZ  . LYS D 2 171 ? 64.889  -11.554 19.100  1.00 173.25 ? 171 LYS D NZ  1 
ATOM   10220 N N   . ILE D 2 172 ? 62.821  -18.228 21.368  1.00 194.27 ? 172 ILE D N   1 
ATOM   10221 C CA  . ILE D 2 172 ? 63.041  -18.970 22.603  1.00 189.96 ? 172 ILE D CA  1 
ATOM   10222 C C   . ILE D 2 172 ? 64.039  -20.094 22.341  1.00 183.57 ? 172 ILE D C   1 
ATOM   10223 O O   . ILE D 2 172 ? 64.338  -20.443 21.200  1.00 179.51 ? 172 ILE D O   1 
ATOM   10224 C CB  . ILE D 2 172 ? 61.739  -19.545 23.190  1.00 187.83 ? 172 ILE D CB  1 
ATOM   10225 C CG1 . ILE D 2 172 ? 61.262  -20.724 22.341  1.00 184.00 ? 172 ILE D CG1 1 
ATOM   10226 C CG2 . ILE D 2 172 ? 60.671  -18.469 23.279  1.00 186.33 ? 172 ILE D CG2 1 
ATOM   10227 C CD1 . ILE D 2 172 ? 60.325  -21.654 23.069  1.00 177.42 ? 172 ILE D CD1 1 
ATOM   10228 N N   . ASN D 2 173 ? 64.535  -20.674 23.430  1.00 169.25 ? 173 ASN D N   1 
ATOM   10229 C CA  . ASN D 2 173 ? 65.469  -21.785 23.334  1.00 162.84 ? 173 ASN D CA  1 
ATOM   10230 C C   . ASN D 2 173 ? 64.757  -23.039 22.837  1.00 157.23 ? 173 ASN D C   1 
ATOM   10231 O O   . ASN D 2 173 ? 63.561  -23.236 23.064  1.00 154.25 ? 173 ASN D O   1 
ATOM   10232 C CB  . ASN D 2 173 ? 66.120  -22.052 24.692  1.00 162.55 ? 173 ASN D CB  1 
ATOM   10233 C CG  . ASN D 2 173 ? 67.349  -22.938 24.590  1.00 163.75 ? 173 ASN D CG  1 
ATOM   10234 O OD1 . ASN D 2 173 ? 67.342  -23.961 23.905  1.00 157.87 ? 173 ASN D OD1 1 
ATOM   10235 N ND2 . ASN D 2 173 ? 68.416  -22.543 25.274  1.00 175.11 ? 173 ASN D ND2 1 
ATOM   10236 N N   . ALA D 2 174 ? 65.512  -23.895 22.149  1.00 155.18 ? 174 ALA D N   1 
ATOM   10237 C CA  . ALA D 2 174 ? 64.978  -25.123 21.577  1.00 146.38 ? 174 ALA D CA  1 
ATOM   10238 C C   . ALA D 2 174 ? 65.453  -26.373 22.305  1.00 143.54 ? 174 ALA D C   1 
ATOM   10239 O O   . ALA D 2 174 ? 65.104  -27.483 21.891  1.00 138.96 ? 174 ALA D O   1 
ATOM   10240 C CB  . ALA D 2 174 ? 65.345  -25.217 20.090  1.00 144.46 ? 174 ALA D CB  1 
ATOM   10241 N N   . GLY D 2 175 ? 66.230  -26.225 23.376  1.00 147.82 ? 175 GLY D N   1 
ATOM   10242 C CA  . GLY D 2 175 ? 66.680  -27.362 24.155  1.00 148.18 ? 175 GLY D CA  1 
ATOM   10243 C C   . GLY D 2 175 ? 67.880  -28.100 23.607  1.00 151.54 ? 175 GLY D C   1 
ATOM   10244 O O   . GLY D 2 175 ? 68.256  -29.135 24.168  1.00 156.03 ? 175 GLY D O   1 
ATOM   10245 N N   . ILE D 2 176 ? 68.494  -27.608 22.533  1.00 151.84 ? 176 ILE D N   1 
ATOM   10246 C CA  . ILE D 2 176 ? 69.683  -28.217 21.945  1.00 154.88 ? 176 ILE D CA  1 
ATOM   10247 C C   . ILE D 2 176 ? 70.829  -27.219 22.036  1.00 160.93 ? 176 ILE D C   1 
ATOM   10248 O O   . ILE D 2 176 ? 70.666  -26.048 21.679  1.00 160.24 ? 176 ILE D O   1 
ATOM   10249 C CB  . ILE D 2 176 ? 69.429  -28.653 20.490  1.00 147.36 ? 176 ILE D CB  1 
ATOM   10250 C CG1 . ILE D 2 176 ? 70.717  -28.585 19.661  1.00 150.12 ? 176 ILE D CG1 1 
ATOM   10251 C CG2 . ILE D 2 176 ? 68.318  -27.820 19.871  1.00 145.45 ? 176 ILE D CG2 1 
ATOM   10252 C CD1 . ILE D 2 176 ? 70.545  -29.048 18.236  1.00 143.51 ? 176 ILE D CD1 1 
ATOM   10253 N N   . TYR D 2 177 ? 71.980  -27.681 22.524  1.00 170.13 ? 177 TYR D N   1 
ATOM   10254 C CA  . TYR D 2 177 ? 73.116  -26.826 22.838  1.00 176.48 ? 177 TYR D CA  1 
ATOM   10255 C C   . TYR D 2 177 ? 74.360  -27.316 22.106  1.00 184.11 ? 177 TYR D C   1 
ATOM   10256 O O   . TYR D 2 177 ? 74.385  -28.405 21.527  1.00 192.30 ? 177 TYR D O   1 
ATOM   10257 C CB  . TYR D 2 177 ? 73.376  -26.794 24.351  1.00 177.43 ? 177 TYR D CB  1 
ATOM   10258 C CG  . TYR D 2 177 ? 72.148  -26.496 25.184  1.00 175.56 ? 177 TYR D CG  1 
ATOM   10259 C CD1 . TYR D 2 177 ? 71.219  -25.545 24.780  1.00 174.64 ? 177 TYR D CD1 1 
ATOM   10260 C CD2 . TYR D 2 177 ? 71.904  -27.191 26.360  1.00 176.65 ? 177 TYR D CD2 1 
ATOM   10261 C CE1 . TYR D 2 177 ? 70.092  -25.282 25.534  1.00 174.89 ? 177 TYR D CE1 1 
ATOM   10262 C CE2 . TYR D 2 177 ? 70.780  -26.936 27.121  1.00 177.39 ? 177 TYR D CE2 1 
ATOM   10263 C CZ  . TYR D 2 177 ? 69.877  -25.980 26.703  1.00 177.26 ? 177 TYR D CZ  1 
ATOM   10264 O OH  . TYR D 2 177 ? 68.756  -25.721 27.456  1.00 182.73 ? 177 TYR D OH  1 
ATOM   10265 N N   . LEU D 2 178 ? 75.400  -26.479 22.131  1.00 185.75 ? 178 LEU D N   1 
ATOM   10266 C CA  . LEU D 2 178 ? 76.716  -26.829 21.592  1.00 183.72 ? 178 LEU D CA  1 
ATOM   10267 C C   . LEU D 2 178 ? 77.745  -26.082 22.439  1.00 172.19 ? 178 LEU D C   1 
ATOM   10268 O O   . LEU D 2 178 ? 77.906  -24.867 22.290  1.00 178.80 ? 178 LEU D O   1 
ATOM   10269 C CB  . LEU D 2 178 ? 76.824  -26.470 20.113  1.00 189.41 ? 178 LEU D CB  1 
ATOM   10270 C CG  . LEU D 2 178 ? 78.074  -26.848 19.305  1.00 182.90 ? 178 LEU D CG  1 
ATOM   10271 C CD1 . LEU D 2 178 ? 77.721  -26.989 17.835  1.00 181.91 ? 178 LEU D CD1 1 
ATOM   10272 C CD2 . LEU D 2 178 ? 79.193  -25.827 19.469  1.00 178.39 ? 178 LEU D CD2 1 
ATOM   10273 N N   . LEU D 2 179 ? 78.427  -26.808 23.322  1.00 155.73 ? 179 LEU D N   1 
ATOM   10274 C CA  . LEU D 2 179 ? 79.282  -26.211 24.340  1.00 148.49 ? 179 LEU D CA  1 
ATOM   10275 C C   . LEU D 2 179 ? 80.727  -26.665 24.184  1.00 146.69 ? 179 LEU D C   1 
ATOM   10276 O O   . LEU D 2 179 ? 80.995  -27.851 23.976  1.00 150.57 ? 179 LEU D O   1 
ATOM   10277 C CB  . LEU D 2 179 ? 78.782  -26.574 25.742  1.00 141.97 ? 179 LEU D CB  1 
ATOM   10278 C CG  . LEU D 2 179 ? 77.472  -25.925 26.189  1.00 137.99 ? 179 LEU D CG  1 
ATOM   10279 C CD1 . LEU D 2 179 ? 76.996  -26.530 27.498  1.00 133.38 ? 179 LEU D CD1 1 
ATOM   10280 C CD2 . LEU D 2 179 ? 77.651  -24.425 26.330  1.00 138.13 ? 179 LEU D CD2 1 
ATOM   10281 N N   . ASN D 2 180 ? 81.655  -25.714 24.307  1.00 143.46 ? 180 ASN D N   1 
ATOM   10282 C CA  . ASN D 2 180 ? 83.073  -26.034 24.363  1.00 143.69 ? 180 ASN D CA  1 
ATOM   10283 C C   . ASN D 2 180 ? 83.428  -26.655 25.713  1.00 144.77 ? 180 ASN D C   1 
ATOM   10284 O O   . ASN D 2 180 ? 82.710  -26.472 26.699  1.00 143.29 ? 180 ASN D O   1 
ATOM   10285 C CB  . ASN D 2 180 ? 83.917  -24.780 24.140  1.00 141.64 ? 180 ASN D CB  1 
ATOM   10286 C CG  . ASN D 2 180 ? 84.175  -24.500 22.676  1.00 147.13 ? 180 ASN D CG  1 
ATOM   10287 O OD1 . ASN D 2 180 ? 84.202  -25.413 21.853  1.00 154.09 ? 180 ASN D OD1 1 
ATOM   10288 N ND2 . ASN D 2 180 ? 84.392  -23.234 22.345  1.00 143.28 ? 180 ASN D ND2 1 
ATOM   10289 N N   . PRO D 2 181 ? 84.530  -27.409 25.780  1.00 148.79 ? 181 PRO D N   1 
ATOM   10290 C CA  . PRO D 2 181 ? 84.974  -27.938 27.081  1.00 149.23 ? 181 PRO D CA  1 
ATOM   10291 C C   . PRO D 2 181 ? 85.320  -26.859 28.094  1.00 155.84 ? 181 PRO D C   1 
ATOM   10292 O O   . PRO D 2 181 ? 85.439  -27.167 29.287  1.00 159.80 ? 181 PRO D O   1 
ATOM   10293 C CB  . PRO D 2 181 ? 86.206  -28.777 26.718  1.00 148.47 ? 181 PRO D CB  1 
ATOM   10294 C CG  . PRO D 2 181 ? 86.009  -29.131 25.288  1.00 156.43 ? 181 PRO D CG  1 
ATOM   10295 C CD  . PRO D 2 181 ? 85.335  -27.943 24.669  1.00 154.53 ? 181 PRO D CD  1 
ATOM   10296 N N   . SER D 2 182 ? 85.487  -25.611 27.663  1.00 158.94 ? 182 SER D N   1 
ATOM   10297 C CA  . SER D 2 182 ? 85.830  -24.508 28.551  1.00 158.08 ? 182 SER D CA  1 
ATOM   10298 C C   . SER D 2 182 ? 84.641  -24.000 29.361  1.00 161.69 ? 182 SER D C   1 
ATOM   10299 O O   . SER D 2 182 ? 84.773  -22.989 30.058  1.00 162.47 ? 182 SER D O   1 
ATOM   10300 C CB  . SER D 2 182 ? 86.437  -23.357 27.743  1.00 156.10 ? 182 SER D CB  1 
ATOM   10301 O OG  . SER D 2 182 ? 87.586  -23.786 27.034  1.00 159.11 ? 182 SER D OG  1 
ATOM   10302 N N   . VAL D 2 183 ? 83.491  -24.670 29.284  1.00 163.71 ? 183 VAL D N   1 
ATOM   10303 C CA  . VAL D 2 183 ? 82.315  -24.255 30.038  1.00 163.13 ? 183 VAL D CA  1 
ATOM   10304 C C   . VAL D 2 183 ? 82.050  -25.145 31.251  1.00 174.89 ? 183 VAL D C   1 
ATOM   10305 O O   . VAL D 2 183 ? 81.350  -24.711 32.180  1.00 167.18 ? 183 VAL D O   1 
ATOM   10306 C CB  . VAL D 2 183 ? 81.071  -24.215 29.124  1.00 147.80 ? 183 VAL D CB  1 
ATOM   10307 C CG1 . VAL D 2 183 ? 80.540  -25.619 28.878  1.00 151.46 ? 183 VAL D CG1 1 
ATOM   10308 C CG2 . VAL D 2 183 ? 79.995  -23.320 29.716  1.00 141.66 ? 183 VAL D CG2 1 
ATOM   10309 N N   . LEU D 2 184 ? 82.594  -26.363 31.280  1.00 221.59 ? 184 LEU D N   1 
ATOM   10310 C CA  . LEU D 2 184 ? 82.331  -27.305 32.362  1.00 221.75 ? 184 LEU D CA  1 
ATOM   10311 C C   . LEU D 2 184 ? 82.938  -26.883 33.694  1.00 222.62 ? 184 LEU D C   1 
ATOM   10312 O O   . LEU D 2 184 ? 82.739  -27.591 34.687  1.00 222.74 ? 184 LEU D O   1 
ATOM   10313 C CB  . LEU D 2 184 ? 82.845  -28.696 31.982  1.00 222.84 ? 184 LEU D CB  1 
ATOM   10314 C CG  . LEU D 2 184 ? 82.113  -29.398 30.836  1.00 221.84 ? 184 LEU D CG  1 
ATOM   10315 C CD1 . LEU D 2 184 ? 82.800  -30.706 30.474  1.00 222.54 ? 184 LEU D CD1 1 
ATOM   10316 C CD2 . LEU D 2 184 ? 80.656  -29.639 31.200  1.00 219.98 ? 184 LEU D CD2 1 
ATOM   10317 N N   . ASP D 2 185 ? 83.675  -25.774 33.753  1.00 174.84 ? 185 ASP D N   1 
ATOM   10318 C CA  . ASP D 2 185 ? 84.227  -25.304 35.015  1.00 166.73 ? 185 ASP D CA  1 
ATOM   10319 C C   . ASP D 2 185 ? 83.411  -24.186 35.647  1.00 159.01 ? 185 ASP D C   1 
ATOM   10320 O O   . ASP D 2 185 ? 83.544  -23.951 36.853  1.00 152.13 ? 185 ASP D O   1 
ATOM   10321 C CB  . ASP D 2 185 ? 85.669  -24.821 34.824  1.00 159.71 ? 185 ASP D CB  1 
ATOM   10322 C CG  . ASP D 2 185 ? 85.759  -23.601 33.933  1.00 157.86 ? 185 ASP D CG  1 
ATOM   10323 O OD1 . ASP D 2 185 ? 84.914  -23.463 33.024  1.00 162.71 ? 185 ASP D OD1 1 
ATOM   10324 O OD2 . ASP D 2 185 ? 86.672  -22.777 34.147  1.00 150.26 ? 185 ASP D OD2 1 
ATOM   10325 N N   . LYS D 2 186 ? 82.572  -23.500 34.870  1.00 154.04 ? 186 LYS D N   1 
ATOM   10326 C CA  . LYS D 2 186 ? 81.803  -22.375 35.385  1.00 149.16 ? 186 LYS D CA  1 
ATOM   10327 C C   . LYS D 2 186 ? 80.621  -22.803 36.243  1.00 147.49 ? 186 LYS D C   1 
ATOM   10328 O O   . LYS D 2 186 ? 79.965  -21.943 36.840  1.00 146.21 ? 186 LYS D O   1 
ATOM   10329 C CB  . LYS D 2 186 ? 81.295  -21.507 34.231  1.00 147.13 ? 186 LYS D CB  1 
ATOM   10330 C CG  . LYS D 2 186 ? 81.132  -20.042 34.597  1.00 147.39 ? 186 LYS D CG  1 
ATOM   10331 C CD  . LYS D 2 186 ? 80.487  -19.250 33.477  1.00 149.55 ? 186 LYS D CD  1 
ATOM   10332 C CE  . LYS D 2 186 ? 80.593  -17.761 33.748  1.00 150.31 ? 186 LYS D CE  1 
ATOM   10333 N NZ  . LYS D 2 186 ? 80.178  -17.432 35.140  1.00 144.56 ? 186 LYS D NZ  1 
ATOM   10334 N N   . ILE D 2 187 ? 80.339  -24.089 36.331  1.00 151.83 ? 187 ILE D N   1 
ATOM   10335 C CA  . ILE D 2 187 ? 79.206  -24.568 37.112  1.00 148.11 ? 187 ILE D CA  1 
ATOM   10336 C C   . ILE D 2 187 ? 79.652  -24.760 38.552  1.00 147.36 ? 187 ILE D C   1 
ATOM   10337 O O   . ILE D 2 187 ? 80.831  -24.994 38.839  1.00 143.96 ? 187 ILE D O   1 
ATOM   10338 C CB  . ILE D 2 187 ? 78.621  -25.867 36.517  1.00 147.69 ? 187 ILE D CB  1 
ATOM   10339 C CG1 . ILE D 2 187 ? 79.729  -26.744 35.921  1.00 153.11 ? 187 ILE D CG1 1 
ATOM   10340 C CG2 . ILE D 2 187 ? 77.560  -25.545 35.474  1.00 143.38 ? 187 ILE D CG2 1 
ATOM   10341 C CD1 . ILE D 2 187 ? 80.498  -27.564 36.942  1.00 149.81 ? 187 ILE D CD1 1 
ATOM   10342 N N   . GLU D 2 188 ? 78.699  -24.650 39.469  1.00 147.57 ? 188 GLU D N   1 
ATOM   10343 C CA  . GLU D 2 188 ? 78.942  -24.887 40.881  1.00 150.09 ? 188 GLU D CA  1 
ATOM   10344 C C   . GLU D 2 188 ? 78.489  -26.291 41.258  1.00 154.96 ? 188 GLU D C   1 
ATOM   10345 O O   . GLU D 2 188 ? 77.865  -27.006 40.471  1.00 155.36 ? 188 GLU D O   1 
ATOM   10346 C CB  . GLU D 2 188 ? 78.208  -23.845 41.728  1.00 148.92 ? 188 GLU D CB  1 
ATOM   10347 C CG  . GLU D 2 188 ? 76.832  -23.492 41.183  1.00 153.96 ? 188 GLU D CG  1 
ATOM   10348 C CD  . GLU D 2 188 ? 75.922  -22.881 42.228  1.00 159.62 ? 188 GLU D CD  1 
ATOM   10349 O OE1 . GLU D 2 188 ? 76.428  -22.466 43.291  1.00 155.86 ? 188 GLU D OE1 1 
ATOM   10350 O OE2 . GLU D 2 188 ? 74.700  -22.806 41.979  1.00 166.12 ? 188 GLU D OE2 1 
ATOM   10351 N N   . LEU D 2 189 ? 78.810  -26.683 42.489  1.00 162.57 ? 189 LEU D N   1 
ATOM   10352 C CA  . LEU D 2 189 ? 78.340  -27.963 42.999  1.00 165.28 ? 189 LEU D CA  1 
ATOM   10353 C C   . LEU D 2 189 ? 76.873  -27.921 43.401  1.00 165.70 ? 189 LEU D C   1 
ATOM   10354 O O   . LEU D 2 189 ? 76.242  -28.978 43.507  1.00 169.70 ? 189 LEU D O   1 
ATOM   10355 C CB  . LEU D 2 189 ? 79.207  -28.408 44.178  1.00 165.37 ? 189 LEU D CB  1 
ATOM   10356 C CG  . LEU D 2 189 ? 79.691  -27.308 45.122  1.00 164.01 ? 189 LEU D CG  1 
ATOM   10357 C CD1 . LEU D 2 189 ? 78.844  -27.265 46.382  1.00 168.15 ? 189 LEU D CD1 1 
ATOM   10358 C CD2 . LEU D 2 189 ? 81.163  -27.502 45.459  1.00 158.17 ? 189 LEU D CD2 1 
ATOM   10359 N N   . ARG D 2 190 ? 76.321  -26.733 43.620  1.00 164.23 ? 190 ARG D N   1 
ATOM   10360 C CA  . ARG D 2 190 ? 74.917  -26.617 43.981  1.00 166.64 ? 190 ARG D CA  1 
ATOM   10361 C C   . ARG D 2 190 ? 74.047  -26.736 42.730  1.00 167.97 ? 190 ARG D C   1 
ATOM   10362 O O   . ARG D 2 190 ? 74.436  -26.260 41.659  1.00 167.33 ? 190 ARG D O   1 
ATOM   10363 C CB  . ARG D 2 190 ? 74.649  -25.286 44.678  1.00 167.32 ? 190 ARG D CB  1 
ATOM   10364 C CG  . ARG D 2 190 ? 75.574  -25.004 45.854  1.00 168.41 ? 190 ARG D CG  1 
ATOM   10365 C CD  . ARG D 2 190 ? 75.431  -26.043 46.955  1.00 169.81 ? 190 ARG D CD  1 
ATOM   10366 N NE  . ARG D 2 190 ? 74.038  -26.367 47.244  1.00 175.75 ? 190 ARG D NE  1 
ATOM   10367 C CZ  . ARG D 2 190 ? 73.518  -27.583 47.125  1.00 174.57 ? 190 ARG D CZ  1 
ATOM   10368 N NH1 . ARG D 2 190 ? 74.279  -28.593 46.726  1.00 175.64 ? 190 ARG D NH1 1 
ATOM   10369 N NH2 . ARG D 2 190 ? 72.240  -27.792 47.408  1.00 169.50 ? 190 ARG D NH2 1 
ATOM   10370 N N   . PRO D 2 191 ? 72.879  -27.383 42.834  1.00 172.03 ? 191 PRO D N   1 
ATOM   10371 C CA  . PRO D 2 191 ? 71.949  -27.437 41.697  1.00 176.09 ? 191 PRO D CA  1 
ATOM   10372 C C   . PRO D 2 191 ? 71.654  -26.076 41.085  1.00 176.00 ? 191 PRO D C   1 
ATOM   10373 O O   . PRO D 2 191 ? 71.023  -25.219 41.713  1.00 172.99 ? 191 PRO D O   1 
ATOM   10374 C CB  . PRO D 2 191 ? 70.689  -28.053 42.315  1.00 176.61 ? 191 PRO D CB  1 
ATOM   10375 C CG  . PRO D 2 191 ? 71.213  -28.929 43.399  1.00 175.49 ? 191 PRO D CG  1 
ATOM   10376 C CD  . PRO D 2 191 ? 72.431  -28.230 43.954  1.00 171.92 ? 191 PRO D CD  1 
ATOM   10377 N N   . THR D 2 192 ? 72.111  -25.876 39.853  1.00 186.00 ? 192 THR D N   1 
ATOM   10378 C CA  . THR D 2 192 ? 71.903  -24.638 39.119  1.00 184.84 ? 192 THR D CA  1 
ATOM   10379 C C   . THR D 2 192 ? 71.104  -24.924 37.856  1.00 183.85 ? 192 THR D C   1 
ATOM   10380 O O   . THR D 2 192 ? 71.371  -25.900 37.147  1.00 183.75 ? 192 THR D O   1 
ATOM   10381 C CB  . THR D 2 192 ? 73.238  -23.972 38.755  1.00 185.62 ? 192 THR D CB  1 
ATOM   10382 O OG1 . THR D 2 192 ? 73.028  -23.001 37.723  1.00 184.85 ? 192 THR D OG1 1 
ATOM   10383 C CG2 . THR D 2 192 ? 74.244  -25.009 38.279  1.00 186.53 ? 192 THR D CG2 1 
ATOM   10384 N N   . SER D 2 193 ? 70.120  -24.073 37.579  1.00 163.11 ? 193 SER D N   1 
ATOM   10385 C CA  . SER D 2 193 ? 69.327  -24.191 36.363  1.00 158.19 ? 193 SER D CA  1 
ATOM   10386 C C   . SER D 2 193 ? 70.062  -23.491 35.228  1.00 160.38 ? 193 SER D C   1 
ATOM   10387 O O   . SER D 2 193 ? 70.325  -22.285 35.300  1.00 157.08 ? 193 SER D O   1 
ATOM   10388 C CB  . SER D 2 193 ? 67.935  -23.593 36.565  1.00 146.45 ? 193 SER D CB  1 
ATOM   10389 O OG  . SER D 2 193 ? 67.434  -23.888 37.859  1.00 138.45 ? 193 SER D OG  1 
ATOM   10390 N N   . ILE D 2 194 ? 70.409  -24.252 34.187  1.00 163.61 ? 194 ILE D N   1 
ATOM   10391 C CA  . ILE D 2 194 ? 71.175  -23.688 33.080  1.00 172.55 ? 194 ILE D CA  1 
ATOM   10392 C C   . ILE D 2 194 ? 70.413  -22.550 32.417  1.00 186.35 ? 194 ILE D C   1 
ATOM   10393 O O   . ILE D 2 194 ? 71.021  -21.644 31.838  1.00 198.64 ? 194 ILE D O   1 
ATOM   10394 C CB  . ILE D 2 194 ? 71.549  -24.790 32.067  1.00 177.21 ? 194 ILE D CB  1 
ATOM   10395 C CG1 . ILE D 2 194 ? 72.716  -24.336 31.191  1.00 187.81 ? 194 ILE D CG1 1 
ATOM   10396 C CG2 . ILE D 2 194 ? 70.361  -25.158 31.195  1.00 182.33 ? 194 ILE D CG2 1 
ATOM   10397 C CD1 . ILE D 2 194 ? 73.173  -25.380 30.197  1.00 183.67 ? 194 ILE D CD1 1 
ATOM   10398 N N   . GLU D 2 195 ? 69.081  -22.555 32.512  1.00 180.37 ? 195 GLU D N   1 
ATOM   10399 C CA  . GLU D 2 195 ? 68.270  -21.517 31.889  1.00 180.93 ? 195 GLU D CA  1 
ATOM   10400 C C   . GLU D 2 195 ? 68.167  -20.262 32.745  1.00 175.47 ? 195 GLU D C   1 
ATOM   10401 O O   . GLU D 2 195 ? 67.889  -19.183 32.210  1.00 180.53 ? 195 GLU D O   1 
ATOM   10402 C CB  . GLU D 2 195 ? 66.859  -22.044 31.605  1.00 181.19 ? 195 GLU D CB  1 
ATOM   10403 C CG  . GLU D 2 195 ? 66.797  -23.245 30.674  1.00 182.62 ? 195 GLU D CG  1 
ATOM   10404 C CD  . GLU D 2 195 ? 66.980  -22.872 29.216  1.00 184.41 ? 195 GLU D CD  1 
ATOM   10405 O OE1 . GLU D 2 195 ? 66.953  -21.663 28.902  1.00 187.19 ? 195 GLU D OE1 1 
ATOM   10406 O OE2 . GLU D 2 195 ? 67.151  -23.787 28.383  1.00 184.07 ? 195 GLU D OE2 1 
ATOM   10407 N N   . LYS D 2 196 ? 68.384  -20.377 34.056  1.00 157.28 ? 196 LYS D N   1 
ATOM   10408 C CA  . LYS D 2 196 ? 68.193  -19.260 34.967  1.00 151.13 ? 196 LYS D CA  1 
ATOM   10409 C C   . LYS D 2 196 ? 69.480  -18.729 35.576  1.00 149.96 ? 196 LYS D C   1 
ATOM   10410 O O   . LYS D 2 196 ? 69.513  -17.562 35.977  1.00 153.76 ? 196 LYS D O   1 
ATOM   10411 C CB  . LYS D 2 196 ? 67.241  -19.666 36.100  1.00 138.84 ? 196 LYS D CB  1 
ATOM   10412 C CG  . LYS D 2 196 ? 66.009  -20.392 35.607  1.00 133.08 ? 196 LYS D CG  1 
ATOM   10413 C CD  . LYS D 2 196 ? 65.120  -20.819 36.753  1.00 118.58 ? 196 LYS D CD  1 
ATOM   10414 C CE  . LYS D 2 196 ? 63.967  -21.667 36.250  1.00 112.40 ? 196 LYS D CE  1 
ATOM   10415 N NZ  . LYS D 2 196 ? 63.183  -20.965 35.197  1.00 106.42 ? 196 LYS D NZ  1 
ATOM   10416 N N   . GLU D 2 197 ? 70.527  -19.541 35.661  1.00 154.34 ? 197 GLU D N   1 
ATOM   10417 C CA  . GLU D 2 197 ? 71.766  -19.125 36.305  1.00 156.20 ? 197 GLU D CA  1 
ATOM   10418 C C   . GLU D 2 197 ? 72.985  -19.248 35.407  1.00 166.69 ? 197 GLU D C   1 
ATOM   10419 O O   . GLU D 2 197 ? 73.805  -18.329 35.366  1.00 167.20 ? 197 GLU D O   1 
ATOM   10420 C CB  . GLU D 2 197 ? 71.996  -19.934 37.593  1.00 149.98 ? 197 GLU D CB  1 
ATOM   10421 C CG  . GLU D 2 197 ? 71.029  -19.601 38.723  1.00 144.58 ? 197 GLU D CG  1 
ATOM   10422 C CD  . GLU D 2 197 ? 69.699  -20.315 38.588  1.00 141.86 ? 197 GLU D CD  1 
ATOM   10423 O OE1 . GLU D 2 197 ? 69.574  -21.167 37.688  1.00 145.52 ? 197 GLU D OE1 1 
ATOM   10424 O OE2 . GLU D 2 197 ? 68.779  -20.024 39.380  1.00 133.78 ? 197 GLU D OE2 1 
ATOM   10425 N N   . THR D 2 198 ? 73.135  -20.360 34.685  1.00 169.89 ? 198 THR D N   1 
ATOM   10426 C CA  . THR D 2 198 ? 74.352  -20.576 33.908  1.00 177.60 ? 198 THR D CA  1 
ATOM   10427 C C   . THR D 2 198 ? 74.339  -19.789 32.600  1.00 198.41 ? 198 THR D C   1 
ATOM   10428 O O   . THR D 2 198 ? 75.319  -19.112 32.270  1.00 192.10 ? 198 THR D O   1 
ATOM   10429 C CB  . THR D 2 198 ? 74.550  -22.067 33.635  1.00 172.19 ? 198 THR D CB  1 
ATOM   10430 O OG1 . THR D 2 198 ? 74.636  -22.770 34.880  1.00 168.16 ? 198 THR D OG1 1 
ATOM   10431 C CG2 . THR D 2 198 ? 75.832  -22.291 32.848  1.00 169.84 ? 198 THR D CG2 1 
ATOM   10432 N N   . PHE D 2 199 ? 73.251  -19.884 31.832  1.00 280.35 ? 199 PHE D N   1 
ATOM   10433 C CA  . PHE D 2 199 ? 73.171  -19.138 30.578  1.00 280.05 ? 199 PHE D CA  1 
ATOM   10434 C C   . PHE D 2 199 ? 73.319  -17.631 30.759  1.00 280.31 ? 199 PHE D C   1 
ATOM   10435 O O   . PHE D 2 199 ? 74.038  -17.014 29.954  1.00 281.00 ? 199 PHE D O   1 
ATOM   10436 C CB  . PHE D 2 199 ? 71.864  -19.467 29.843  1.00 278.66 ? 199 PHE D CB  1 
ATOM   10437 C CG  . PHE D 2 199 ? 71.902  -20.762 29.078  1.00 278.99 ? 199 PHE D CG  1 
ATOM   10438 C CD1 . PHE D 2 199 ? 73.111  -21.327 28.710  1.00 279.99 ? 199 PHE D CD1 1 
ATOM   10439 C CD2 . PHE D 2 199 ? 70.729  -21.407 28.718  1.00 277.53 ? 199 PHE D CD2 1 
ATOM   10440 C CE1 . PHE D 2 199 ? 73.152  -22.514 28.002  1.00 280.02 ? 199 PHE D CE1 1 
ATOM   10441 C CE2 . PHE D 2 199 ? 70.763  -22.595 28.010  1.00 277.52 ? 199 PHE D CE2 1 
ATOM   10442 C CZ  . PHE D 2 199 ? 71.976  -23.149 27.651  1.00 278.75 ? 199 PHE D CZ  1 
ATOM   10443 N N   . PRO D 2 200 ? 72.690  -16.978 31.745  1.00 211.00 ? 200 PRO D N   1 
ATOM   10444 C CA  . PRO D 2 200 ? 72.963  -15.545 31.943  1.00 200.87 ? 200 PRO D CA  1 
ATOM   10445 C C   . PRO D 2 200 ? 74.405  -15.252 32.319  1.00 188.62 ? 200 PRO D C   1 
ATOM   10446 O O   . PRO D 2 200 ? 74.865  -14.122 32.110  1.00 182.46 ? 200 PRO D O   1 
ATOM   10447 C CB  . PRO D 2 200 ? 71.995  -15.148 33.068  1.00 194.94 ? 200 PRO D CB  1 
ATOM   10448 C CG  . PRO D 2 200 ? 71.611  -16.428 33.721  1.00 188.83 ? 200 PRO D CG  1 
ATOM   10449 C CD  . PRO D 2 200 ? 71.605  -17.442 32.628  1.00 194.87 ? 200 PRO D CD  1 
ATOM   10450 N N   . LYS D 2 201 ? 75.132  -16.229 32.868  1.00 187.05 ? 201 LYS D N   1 
ATOM   10451 C CA  . LYS D 2 201 ? 76.533  -16.005 33.213  1.00 173.71 ? 201 LYS D CA  1 
ATOM   10452 C C   . LYS D 2 201 ? 77.395  -15.846 31.965  1.00 172.77 ? 201 LYS D C   1 
ATOM   10453 O O   . LYS D 2 201 ? 78.336  -15.045 31.954  1.00 165.71 ? 201 LYS D O   1 
ATOM   10454 C CB  . LYS D 2 201 ? 77.049  -17.155 34.078  1.00 158.84 ? 201 LYS D CB  1 
ATOM   10455 C CG  . LYS D 2 201 ? 76.637  -17.079 35.538  1.00 149.83 ? 201 LYS D CG  1 
ATOM   10456 C CD  . LYS D 2 201 ? 77.226  -18.231 36.337  1.00 138.34 ? 201 LYS D CD  1 
ATOM   10457 C CE  . LYS D 2 201 ? 76.872  -18.124 37.810  1.00 117.75 ? 201 LYS D CE  1 
ATOM   10458 N NZ  . LYS D 2 201 ? 77.489  -19.224 38.600  1.00 113.13 ? 201 LYS D NZ  1 
ATOM   10459 N N   . ILE D 2 202 ? 77.091  -16.596 30.905  1.00 177.19 ? 202 ILE D N   1 
ATOM   10460 C CA  . ILE D 2 202 ? 77.841  -16.472 29.659  1.00 172.41 ? 202 ILE D CA  1 
ATOM   10461 C C   . ILE D 2 202 ? 77.284  -15.385 28.746  1.00 173.90 ? 202 ILE D C   1 
ATOM   10462 O O   . ILE D 2 202 ? 78.029  -14.848 27.912  1.00 170.47 ? 202 ILE D O   1 
ATOM   10463 C CB  . ILE D 2 202 ? 77.877  -17.814 28.904  1.00 169.45 ? 202 ILE D CB  1 
ATOM   10464 C CG1 . ILE D 2 202 ? 78.012  -18.978 29.885  1.00 167.11 ? 202 ILE D CG1 1 
ATOM   10465 C CG2 . ILE D 2 202 ? 79.026  -17.840 27.905  1.00 160.33 ? 202 ILE D CG2 1 
ATOM   10466 C CD1 . ILE D 2 202 ? 77.986  -20.332 29.220  1.00 151.38 ? 202 ILE D CD1 1 
ATOM   10467 N N   . ALA D 2 203 ? 76.004  -15.034 28.887  1.00 177.05 ? 203 ALA D N   1 
ATOM   10468 C CA  . ALA D 2 203 ? 75.433  -13.979 28.056  1.00 178.66 ? 203 ALA D CA  1 
ATOM   10469 C C   . ALA D 2 203 ? 76.028  -12.622 28.405  1.00 172.93 ? 203 ALA D C   1 
ATOM   10470 O O   . ALA D 2 203 ? 76.324  -11.819 27.513  1.00 173.88 ? 203 ALA D O   1 
ATOM   10471 C CB  . ALA D 2 203 ? 73.912  -13.955 28.209  1.00 190.45 ? 203 ALA D CB  1 
ATOM   10472 N N   . ALA D 2 204 ? 76.211  -12.349 29.700  1.00 172.12 ? 204 ALA D N   1 
ATOM   10473 C CA  . ALA D 2 204 ? 76.842  -11.105 30.120  1.00 170.64 ? 204 ALA D CA  1 
ATOM   10474 C C   . ALA D 2 204 ? 78.308  -11.036 29.715  1.00 160.39 ? 204 ALA D C   1 
ATOM   10475 O O   . ALA D 2 204 ? 78.863  -9.936  29.632  1.00 154.65 ? 204 ALA D O   1 
ATOM   10476 C CB  . ALA D 2 204 ? 76.712  -10.932 31.635  1.00 170.88 ? 204 ALA D CB  1 
ATOM   10477 N N   . ALA D 2 205 ? 78.943  -12.180 29.460  1.00 160.84 ? 205 ALA D N   1 
ATOM   10478 C CA  . ALA D 2 205 ? 80.318  -12.192 28.984  1.00 158.29 ? 205 ALA D CA  1 
ATOM   10479 C C   . ALA D 2 205 ? 80.422  -12.001 27.477  1.00 158.84 ? 205 ALA D C   1 
ATOM   10480 O O   . ALA D 2 205 ? 81.528  -11.769 26.977  1.00 156.82 ? 205 ALA D O   1 
ATOM   10481 C CB  . ALA D 2 205 ? 81.006  -13.500 29.388  1.00 153.41 ? 205 ALA D CB  1 
ATOM   10482 N N   . GLN D 2 206 ? 79.302  -12.085 26.755  1.00 164.33 ? 206 GLN D N   1 
ATOM   10483 C CA  . GLN D 2 206 ? 79.271  -11.899 25.303  1.00 164.90 ? 206 GLN D CA  1 
ATOM   10484 C C   . GLN D 2 206 ? 80.249  -12.839 24.601  1.00 166.96 ? 206 GLN D C   1 
ATOM   10485 O O   . GLN D 2 206 ? 80.914  -12.472 23.629  1.00 165.08 ? 206 GLN D O   1 
ATOM   10486 C CB  . GLN D 2 206 ? 79.550  -10.440 24.934  1.00 163.38 ? 206 GLN D CB  1 
ATOM   10487 C CG  . GLN D 2 206 ? 78.677  -9.419  25.666  1.00 158.43 ? 206 GLN D CG  1 
ATOM   10488 C CD  . GLN D 2 206 ? 77.252  -9.344  25.132  1.00 157.25 ? 206 GLN D CD  1 
ATOM   10489 O OE1 . GLN D 2 206 ? 76.588  -10.363 24.936  1.00 166.25 ? 206 GLN D OE1 1 
ATOM   10490 N NE2 . GLN D 2 206 ? 76.777  -8.127  24.898  1.00 151.51 ? 206 GLN D NE2 1 
ATOM   10491 N N   . GLY D 2 207 ? 80.332  -14.069 25.098  0.24 167.27 ? 207 GLY D N   1 
ATOM   10492 C CA  . GLY D 2 207 ? 81.229  -15.054 24.529  0.24 168.04 ? 207 GLY D CA  1 
ATOM   10493 C C   . GLY D 2 207 ? 80.463  -16.201 23.908  0.24 173.67 ? 207 GLY D C   1 
ATOM   10494 O O   . GLY D 2 207 ? 81.012  -17.282 23.672  0.24 165.13 ? 207 GLY D O   1 
ATOM   10495 N N   . LEU D 2 208 ? 79.182  -15.967 23.640  1.00 198.64 ? 208 LEU D N   1 
ATOM   10496 C CA  . LEU D 2 208 ? 78.293  -16.952 23.045  1.00 197.85 ? 208 LEU D CA  1 
ATOM   10497 C C   . LEU D 2 208 ? 77.659  -16.396 21.775  1.00 202.88 ? 208 LEU D C   1 
ATOM   10498 O O   . LEU D 2 208 ? 77.817  -15.223 21.426  1.00 200.96 ? 208 LEU D O   1 
ATOM   10499 C CB  . LEU D 2 208 ? 77.207  -17.388 24.040  1.00 197.23 ? 208 LEU D CB  1 
ATOM   10500 C CG  . LEU D 2 208 ? 76.755  -16.400 25.122  1.00 195.42 ? 208 LEU D CG  1 
ATOM   10501 C CD1 . LEU D 2 208 ? 76.205  -15.106 24.534  1.00 198.52 ? 208 LEU D CD1 1 
ATOM   10502 C CD2 . LEU D 2 208 ? 75.721  -17.055 26.024  1.00 195.16 ? 208 LEU D CD2 1 
ATOM   10503 N N   . TYR D 2 209 ? 76.934  -17.269 21.082  1.00 203.68 ? 209 TYR D N   1 
ATOM   10504 C CA  . TYR D 2 209 ? 76.211  -16.902 19.875  1.00 200.46 ? 209 TYR D CA  1 
ATOM   10505 C C   . TYR D 2 209 ? 75.027  -17.849 19.734  1.00 198.33 ? 209 TYR D C   1 
ATOM   10506 O O   . TYR D 2 209 ? 74.959  -18.890 20.392  1.00 203.09 ? 209 TYR D O   1 
ATOM   10507 C CB  . TYR D 2 209 ? 77.114  -16.961 18.642  1.00 199.08 ? 209 TYR D CB  1 
ATOM   10508 C CG  . TYR D 2 209 ? 77.623  -18.351 18.369  1.00 204.01 ? 209 TYR D CG  1 
ATOM   10509 C CD1 . TYR D 2 209 ? 76.946  -19.192 17.501  1.00 202.13 ? 209 TYR D CD1 1 
ATOM   10510 C CD2 . TYR D 2 209 ? 78.765  -18.832 18.997  1.00 199.17 ? 209 TYR D CD2 1 
ATOM   10511 C CE1 . TYR D 2 209 ? 77.394  -20.463 17.252  1.00 200.05 ? 209 TYR D CE1 1 
ATOM   10512 C CE2 . TYR D 2 209 ? 79.220  -20.109 18.757  1.00 194.57 ? 209 TYR D CE2 1 
ATOM   10513 C CZ  . TYR D 2 209 ? 78.532  -20.915 17.879  1.00 196.70 ? 209 TYR D CZ  1 
ATOM   10514 O OH  . TYR D 2 209 ? 78.969  -22.188 17.629  1.00 191.36 ? 209 TYR D OH  1 
ATOM   10515 N N   . ALA D 2 210 ? 74.091  -17.485 18.862  1.00 183.70 ? 210 ALA D N   1 
ATOM   10516 C CA  . ALA D 2 210 ? 72.869  -18.255 18.690  1.00 175.44 ? 210 ALA D CA  1 
ATOM   10517 C C   . ALA D 2 210 ? 72.615  -18.541 17.217  1.00 170.52 ? 210 ALA D C   1 
ATOM   10518 O O   . ALA D 2 210 ? 73.027  -17.781 16.336  1.00 168.11 ? 210 ALA D O   1 
ATOM   10519 C CB  . ALA D 2 210 ? 71.657  -17.526 19.293  1.00 172.73 ? 210 ALA D CB  1 
ATOM   10520 N N   . MET D 2 211 ? 71.934  -19.659 16.966  1.00 170.75 ? 211 MET D N   1 
ATOM   10521 C CA  . MET D 2 211 ? 71.499  -20.044 15.633  1.00 178.30 ? 211 MET D CA  1 
ATOM   10522 C C   . MET D 2 211 ? 70.001  -20.312 15.661  1.00 193.33 ? 211 MET D C   1 
ATOM   10523 O O   . MET D 2 211 ? 69.451  -20.744 16.677  1.00 183.35 ? 211 MET D O   1 
ATOM   10524 C CB  . MET D 2 211 ? 72.245  -21.291 15.126  1.00 168.36 ? 211 MET D CB  1 
ATOM   10525 C CG  . MET D 2 211 ? 71.903  -21.693 13.697  1.00 164.77 ? 211 MET D CG  1 
ATOM   10526 S SD  . MET D 2 211 ? 72.609  -23.279 13.210  1.00 155.40 ? 211 MET D SD  1 
ATOM   10527 C CE  . MET D 2 211 ? 71.798  -23.540 11.635  1.00 139.89 ? 211 MET D CE  1 
ATOM   10528 N N   . VAL D 2 212 ? 69.348  -20.057 14.535  1.00 260.93 ? 212 VAL D N   1 
ATOM   10529 C CA  . VAL D 2 212 ? 67.909  -20.249 14.402  1.00 259.48 ? 212 VAL D CA  1 
ATOM   10530 C C   . VAL D 2 212 ? 67.644  -21.644 13.851  1.00 259.26 ? 212 VAL D C   1 
ATOM   10531 O O   . VAL D 2 212 ? 68.363  -22.124 12.966  1.00 260.14 ? 212 VAL D O   1 
ATOM   10532 C CB  . VAL D 2 212 ? 67.295  -19.161 13.501  1.00 259.33 ? 212 VAL D CB  1 
ATOM   10533 C CG1 . VAL D 2 212 ? 65.781  -19.304 13.438  1.00 257.75 ? 212 VAL D CG1 1 
ATOM   10534 C CG2 . VAL D 2 212 ? 67.684  -17.777 14.002  1.00 262.38 ? 212 VAL D CG2 1 
ATOM   10535 N N   . LEU D 2 213 ? 66.613  -22.303 14.382  1.00 200.21 ? 213 LEU D N   1 
ATOM   10536 C CA  . LEU D 2 213 ? 66.264  -23.654 13.957  1.00 187.46 ? 213 LEU D CA  1 
ATOM   10537 C C   . LEU D 2 213 ? 65.373  -23.590 12.724  1.00 183.24 ? 213 LEU D C   1 
ATOM   10538 O O   . LEU D 2 213 ? 64.270  -23.030 12.800  1.00 182.69 ? 213 LEU D O   1 
ATOM   10539 C CB  . LEU D 2 213 ? 65.551  -24.404 15.068  1.00 181.52 ? 213 LEU D CB  1 
ATOM   10540 C CG  . LEU D 2 213 ? 65.028  -25.794 14.701  1.00 176.14 ? 213 LEU D CG  1 
ATOM   10541 C CD1 . LEU D 2 213 ? 66.176  -26.717 14.326  1.00 173.45 ? 213 LEU D CD1 1 
ATOM   10542 C CD2 . LEU D 2 213 ? 64.214  -26.383 15.840  1.00 165.29 ? 213 LEU D CD2 1 
ATOM   10543 N N   . PRO D 2 214 ? 65.800  -24.134 11.586  1.00 166.11 ? 214 PRO D N   1 
ATOM   10544 C CA  . PRO D 2 214 ? 64.962  -24.084 10.382  1.00 156.85 ? 214 PRO D CA  1 
ATOM   10545 C C   . PRO D 2 214 ? 64.007  -25.263 10.279  1.00 152.30 ? 214 PRO D C   1 
ATOM   10546 O O   . PRO D 2 214 ? 63.800  -25.806 9.190   1.00 146.50 ? 214 PRO D O   1 
ATOM   10547 C CB  . PRO D 2 214 ? 65.996  -24.101 9.254   1.00 147.54 ? 214 PRO D CB  1 
ATOM   10548 C CG  . PRO D 2 214 ? 67.097  -24.952 9.812   1.00 146.69 ? 214 PRO D CG  1 
ATOM   10549 C CD  . PRO D 2 214 ? 67.137  -24.686 11.304  1.00 160.32 ? 214 PRO D CD  1 
ATOM   10550 N N   . GLY D 2 215 ? 63.419  -25.666 11.402  1.00 148.41 ? 215 GLY D N   1 
ATOM   10551 C CA  . GLY D 2 215 ? 62.538  -26.816 11.412  1.00 142.17 ? 215 GLY D CA  1 
ATOM   10552 C C   . GLY D 2 215 ? 61.423  -26.724 12.431  1.00 138.61 ? 215 GLY D C   1 
ATOM   10553 O O   . GLY D 2 215 ? 61.103  -25.636 12.921  1.00 138.22 ? 215 GLY D O   1 
ATOM   10554 N N   . PHE D 2 216 ? 60.821  -27.863 12.753  1.00 137.11 ? 216 PHE D N   1 
ATOM   10555 C CA  . PHE D 2 216 ? 59.707  -27.919 13.686  1.00 136.67 ? 216 PHE D CA  1 
ATOM   10556 C C   . PHE D 2 216 ? 60.213  -28.099 15.111  1.00 131.38 ? 216 PHE D C   1 
ATOM   10557 O O   . PHE D 2 216 ? 61.300  -28.633 15.343  1.00 132.79 ? 216 PHE D O   1 
ATOM   10558 C CB  . PHE D 2 216 ? 58.755  -29.061 13.321  1.00 139.17 ? 216 PHE D CB  1 
ATOM   10559 C CG  . PHE D 2 216 ? 59.381  -30.427 13.406  1.00 136.87 ? 216 PHE D CG  1 
ATOM   10560 C CD1 . PHE D 2 216 ? 60.094  -30.945 12.337  1.00 136.28 ? 216 PHE D CD1 1 
ATOM   10561 C CD2 . PHE D 2 216 ? 59.251  -31.198 14.551  1.00 132.17 ? 216 PHE D CD2 1 
ATOM   10562 C CE1 . PHE D 2 216 ? 60.670  -32.200 12.410  1.00 132.34 ? 216 PHE D CE1 1 
ATOM   10563 C CE2 . PHE D 2 216 ? 59.826  -32.454 14.628  1.00 130.75 ? 216 PHE D CE2 1 
ATOM   10564 C CZ  . PHE D 2 216 ? 60.535  -32.955 13.556  1.00 131.07 ? 216 PHE D CZ  1 
ATOM   10565 N N   . TRP D 2 217 ? 59.410  -27.642 16.068  1.00 125.68 ? 217 TRP D N   1 
ATOM   10566 C CA  . TRP D 2 217 ? 59.738  -27.767 17.480  1.00 121.33 ? 217 TRP D CA  1 
ATOM   10567 C C   . TRP D 2 217 ? 58.498  -28.189 18.253  1.00 116.97 ? 217 TRP D C   1 
ATOM   10568 O O   . TRP D 2 217 ? 57.404  -27.674 18.012  1.00 119.75 ? 217 TRP D O   1 
ATOM   10569 C CB  . TRP D 2 217 ? 60.280  -26.455 18.055  1.00 123.56 ? 217 TRP D CB  1 
ATOM   10570 C CG  . TRP D 2 217 ? 60.659  -26.568 19.495  1.00 123.70 ? 217 TRP D CG  1 
ATOM   10571 C CD1 . TRP D 2 217 ? 61.868  -26.954 19.996  1.00 123.44 ? 217 TRP D CD1 1 
ATOM   10572 C CD2 . TRP D 2 217 ? 59.812  -26.329 20.626  1.00 121.87 ? 217 TRP D CD2 1 
ATOM   10573 N NE1 . TRP D 2 217 ? 61.833  -26.949 21.371  1.00 124.86 ? 217 TRP D NE1 1 
ATOM   10574 C CE2 . TRP D 2 217 ? 60.581  -26.571 21.781  1.00 120.88 ? 217 TRP D CE2 1 
ATOM   10575 C CE3 . TRP D 2 217 ? 58.482  -25.925 20.772  1.00 119.93 ? 217 TRP D CE3 1 
ATOM   10576 C CZ2 . TRP D 2 217 ? 60.063  -26.423 23.065  1.00 116.71 ? 217 TRP D CZ2 1 
ATOM   10577 C CZ3 . TRP D 2 217 ? 57.971  -25.779 22.048  1.00 120.12 ? 217 TRP D CZ3 1 
ATOM   10578 C CH2 . TRP D 2 217 ? 58.760  -26.027 23.178  1.00 117.95 ? 217 TRP D CH2 1 
ATOM   10579 N N   . MET D 2 218 ? 58.677  -29.124 19.183  1.00 112.83 ? 218 MET D N   1 
ATOM   10580 C CA  . MET D 2 218 ? 57.570  -29.642 19.976  1.00 112.82 ? 218 MET D CA  1 
ATOM   10581 C C   . MET D 2 218 ? 58.099  -30.156 21.306  1.00 111.75 ? 218 MET D C   1 
ATOM   10582 O O   . MET D 2 218 ? 59.041  -30.953 21.329  1.00 114.43 ? 218 MET D O   1 
ATOM   10583 C CB  . MET D 2 218 ? 56.839  -30.759 19.224  1.00 120.20 ? 218 MET D CB  1 
ATOM   10584 C CG  . MET D 2 218 ? 55.755  -31.459 20.029  1.00 121.25 ? 218 MET D CG  1 
ATOM   10585 S SD  . MET D 2 218 ? 54.353  -30.389 20.397  1.00 122.81 ? 218 MET D SD  1 
ATOM   10586 C CE  . MET D 2 218 ? 53.744  -30.060 18.744  1.00 129.46 ? 218 MET D CE  1 
ATOM   10587 N N   . ASP D 2 219 ? 57.497  -29.703 22.403  1.00 112.52 ? 219 ASP D N   1 
ATOM   10588 C CA  . ASP D 2 219 ? 57.831  -30.183 23.741  1.00 111.92 ? 219 ASP D CA  1 
ATOM   10589 C C   . ASP D 2 219 ? 56.830  -31.268 24.121  1.00 116.95 ? 219 ASP D C   1 
ATOM   10590 O O   . ASP D 2 219 ? 55.674  -30.972 24.438  1.00 118.29 ? 219 ASP D O   1 
ATOM   10591 C CB  . ASP D 2 219 ? 57.815  -29.041 24.756  1.00 109.83 ? 219 ASP D CB  1 
ATOM   10592 C CG  . ASP D 2 219 ? 58.425  -29.436 26.093  1.00 109.42 ? 219 ASP D CG  1 
ATOM   10593 O OD1 . ASP D 2 219 ? 58.092  -30.522 26.616  1.00 110.43 ? 219 ASP D OD1 1 
ATOM   10594 O OD2 . ASP D 2 219 ? 59.242  -28.656 26.624  1.00 111.05 ? 219 ASP D OD2 1 
ATOM   10595 N N   . ILE D 2 220 ? 57.276  -32.521 24.094  1.00 126.75 ? 220 ILE D N   1 
ATOM   10596 C CA  . ILE D 2 220 ? 56.424  -33.663 24.410  1.00 125.81 ? 220 ILE D CA  1 
ATOM   10597 C C   . ILE D 2 220 ? 56.491  -33.883 25.918  1.00 122.91 ? 220 ILE D C   1 
ATOM   10598 O O   . ILE D 2 220 ? 57.476  -34.407 26.440  1.00 121.92 ? 220 ILE D O   1 
ATOM   10599 C CB  . ILE D 2 220 ? 56.835  -34.917 23.636  1.00 130.00 ? 220 ILE D CB  1 
ATOM   10600 C CG1 . ILE D 2 220 ? 56.746  -34.678 22.124  1.00 128.02 ? 220 ILE D CG1 1 
ATOM   10601 C CG2 . ILE D 2 220 ? 55.967  -36.098 24.048  1.00 132.93 ? 220 ILE D CG2 1 
ATOM   10602 C CD1 . ILE D 2 220 ? 58.042  -34.214 21.481  1.00 126.36 ? 220 ILE D CD1 1 
ATOM   10603 N N   . GLY D 2 221 ? 55.438  -33.473 26.620  1.00 117.13 ? 221 GLY D N   1 
ATOM   10604 C CA  . GLY D 2 221 ? 55.359  -33.668 28.053  1.00 121.88 ? 221 GLY D CA  1 
ATOM   10605 C C   . GLY D 2 221 ? 54.054  -34.307 28.482  1.00 123.82 ? 221 GLY D C   1 
ATOM   10606 O O   . GLY D 2 221 ? 53.751  -34.385 29.677  1.00 129.98 ? 221 GLY D O   1 
ATOM   10607 N N   . GLN D 2 222 ? 53.276  -34.773 27.509  1.00 117.84 ? 222 GLN D N   1 
ATOM   10608 C CA  . GLN D 2 222 ? 51.990  -35.405 27.761  1.00 113.02 ? 222 GLN D CA  1 
ATOM   10609 C C   . GLN D 2 222 ? 51.707  -36.388 26.637  1.00 113.00 ? 222 GLN D C   1 
ATOM   10610 O O   . GLN D 2 222 ? 52.115  -36.152 25.493  1.00 114.25 ? 222 GLN D O   1 
ATOM   10611 C CB  . GLN D 2 222 ? 50.864  -34.365 27.863  1.00 110.92 ? 222 GLN D CB  1 
ATOM   10612 C CG  . GLN D 2 222 ? 50.740  -33.471 26.645  1.00 112.97 ? 222 GLN D CG  1 
ATOM   10613 C CD  . GLN D 2 222 ? 49.866  -32.260 26.895  1.00 116.16 ? 222 GLN D CD  1 
ATOM   10614 O OE1 . GLN D 2 222 ? 49.636  -31.874 28.041  1.00 118.88 ? 222 GLN D OE1 1 
ATOM   10615 N NE2 . GLN D 2 222 ? 49.374  -31.650 25.822  1.00 117.14 ? 222 GLN D NE2 1 
ATOM   10616 N N   . PRO D 2 223 ? 51.029  -37.501 26.929  1.00 111.65 ? 223 PRO D N   1 
ATOM   10617 C CA  . PRO D 2 223 ? 50.813  -38.528 25.895  1.00 114.74 ? 223 PRO D CA  1 
ATOM   10618 C C   . PRO D 2 223 ? 49.971  -38.070 24.714  1.00 113.08 ? 223 PRO D C   1 
ATOM   10619 O O   . PRO D 2 223 ? 50.070  -38.677 23.641  1.00 116.24 ? 223 PRO D O   1 
ATOM   10620 C CB  . PRO D 2 223 ? 50.124  -39.663 26.666  1.00 114.91 ? 223 PRO D CB  1 
ATOM   10621 C CG  . PRO D 2 223 ? 49.551  -39.013 27.885  1.00 110.87 ? 223 PRO D CG  1 
ATOM   10622 C CD  . PRO D 2 223 ? 50.506  -37.918 28.241  1.00 108.64 ? 223 PRO D CD  1 
ATOM   10623 N N   . ARG D 2 224 ? 49.145  -37.031 24.865  1.00 111.89 ? 224 ARG D N   1 
ATOM   10624 C CA  . ARG D 2 224 ? 48.327  -36.590 23.741  1.00 113.60 ? 224 ARG D CA  1 
ATOM   10625 C C   . ARG D 2 224 ? 49.135  -35.838 22.694  1.00 115.00 ? 224 ARG D C   1 
ATOM   10626 O O   . ARG D 2 224 ? 48.650  -35.654 21.573  1.00 116.85 ? 224 ARG D O   1 
ATOM   10627 C CB  . ARG D 2 224 ? 47.177  -35.700 24.217  1.00 116.78 ? 224 ARG D CB  1 
ATOM   10628 C CG  . ARG D 2 224 ? 47.623  -34.406 24.879  1.00 117.07 ? 224 ARG D CG  1 
ATOM   10629 C CD  . ARG D 2 224 ? 46.434  -33.595 25.377  1.00 115.52 ? 224 ARG D CD  1 
ATOM   10630 N NE  . ARG D 2 224 ? 45.548  -34.367 26.242  1.00 115.87 ? 224 ARG D NE  1 
ATOM   10631 C CZ  . ARG D 2 224 ? 45.740  -34.541 27.545  1.00 119.55 ? 224 ARG D CZ  1 
ATOM   10632 N NH1 . ARG D 2 224 ? 46.793  -33.998 28.142  1.00 118.19 ? 224 ARG D NH1 1 
ATOM   10633 N NH2 . ARG D 2 224 ? 44.877  -35.258 28.252  1.00 122.28 ? 224 ARG D NH2 1 
ATOM   10634 N N   . ASP D 2 225 ? 50.347  -35.395 23.032  1.00 114.22 ? 225 ASP D N   1 
ATOM   10635 C CA  . ASP D 2 225 ? 51.190  -34.690 22.073  1.00 118.32 ? 225 ASP D CA  1 
ATOM   10636 C C   . ASP D 2 225 ? 51.801  -35.610 21.026  1.00 121.88 ? 225 ASP D C   1 
ATOM   10637 O O   . ASP D 2 225 ? 52.439  -35.115 20.089  1.00 125.50 ? 225 ASP D O   1 
ATOM   10638 C CB  . ASP D 2 225 ? 52.305  -33.943 22.809  1.00 116.52 ? 225 ASP D CB  1 
ATOM   10639 C CG  . ASP D 2 225 ? 51.792  -32.740 23.571  1.00 115.35 ? 225 ASP D CG  1 
ATOM   10640 O OD1 . ASP D 2 225 ? 50.597  -32.407 23.422  1.00 120.02 ? 225 ASP D OD1 1 
ATOM   10641 O OD2 . ASP D 2 225 ? 52.580  -32.128 24.321  1.00 113.69 ? 225 ASP D OD2 1 
ATOM   10642 N N   . TYR D 2 226 ? 51.624  -36.925 21.158  1.00 124.08 ? 226 TYR D N   1 
ATOM   10643 C CA  . TYR D 2 226 ? 52.227  -37.853 20.209  1.00 124.81 ? 226 TYR D CA  1 
ATOM   10644 C C   . TYR D 2 226 ? 51.523  -37.832 18.858  1.00 123.67 ? 226 TYR D C   1 
ATOM   10645 O O   . TYR D 2 226 ? 52.163  -38.069 17.828  1.00 119.83 ? 226 TYR D O   1 
ATOM   10646 C CB  . TYR D 2 226 ? 52.225  -39.265 20.793  1.00 128.52 ? 226 TYR D CB  1 
ATOM   10647 C CG  . TYR D 2 226 ? 53.411  -39.549 21.686  1.00 129.61 ? 226 TYR D CG  1 
ATOM   10648 C CD1 . TYR D 2 226 ? 54.670  -39.045 21.383  1.00 127.83 ? 226 TYR D CD1 1 
ATOM   10649 C CD2 . TYR D 2 226 ? 53.271  -40.313 22.837  1.00 132.79 ? 226 TYR D CD2 1 
ATOM   10650 C CE1 . TYR D 2 226 ? 55.758  -39.300 22.197  1.00 133.78 ? 226 TYR D CE1 1 
ATOM   10651 C CE2 . TYR D 2 226 ? 54.352  -40.573 23.657  1.00 134.55 ? 226 TYR D CE2 1 
ATOM   10652 C CZ  . TYR D 2 226 ? 55.592  -40.065 23.333  1.00 139.99 ? 226 TYR D CZ  1 
ATOM   10653 O OH  . TYR D 2 226 ? 56.670  -40.322 24.148  1.00 142.32 ? 226 TYR D OH  1 
ATOM   10654 N N   . ILE D 2 227 ? 50.222  -37.546 18.833  1.00 128.91 ? 227 ILE D N   1 
ATOM   10655 C CA  . ILE D 2 227 ? 49.509  -37.539 17.560  1.00 131.33 ? 227 ILE D CA  1 
ATOM   10656 C C   . ILE D 2 227 ? 49.761  -36.250 16.787  1.00 132.20 ? 227 ILE D C   1 
ATOM   10657 O O   . ILE D 2 227 ? 49.818  -36.267 15.551  1.00 131.33 ? 227 ILE D O   1 
ATOM   10658 C CB  . ILE D 2 227 ? 48.006  -37.776 17.790  1.00 135.24 ? 227 ILE D CB  1 
ATOM   10659 C CG1 . ILE D 2 227 ? 47.451  -36.763 18.796  1.00 128.40 ? 227 ILE D CG1 1 
ATOM   10660 C CG2 . ILE D 2 227 ? 47.763  -39.191 18.273  1.00 130.01 ? 227 ILE D CG2 1 
ATOM   10661 C CD1 . ILE D 2 227 ? 45.989  -36.969 19.131  1.00 126.33 ? 227 ILE D CD1 1 
ATOM   10662 N N   . THR D 2 228 ? 49.913  -35.121 17.478  1.00 129.92 ? 228 THR D N   1 
ATOM   10663 C CA  . THR D 2 228 ? 50.220  -33.866 16.804  1.00 129.17 ? 228 THR D CA  1 
ATOM   10664 C C   . THR D 2 228 ? 51.711  -33.677 16.563  1.00 130.56 ? 228 THR D C   1 
ATOM   10665 O O   . THR D 2 228 ? 52.093  -33.019 15.590  1.00 135.29 ? 228 THR D O   1 
ATOM   10666 C CB  . THR D 2 228 ? 49.670  -32.680 17.602  1.00 133.48 ? 228 THR D CB  1 
ATOM   10667 O OG1 . THR D 2 228 ? 49.980  -31.460 16.919  1.00 137.81 ? 228 THR D OG1 1 
ATOM   10668 C CG2 . THR D 2 228 ? 50.267  -32.646 19.001  1.00 127.70 ? 228 THR D CG2 1 
ATOM   10669 N N   . GLY D 2 229 ? 52.563  -34.244 17.421  1.00 129.77 ? 229 GLY D N   1 
ATOM   10670 C CA  . GLY D 2 229 ? 53.991  -34.196 17.168  1.00 128.48 ? 229 GLY D CA  1 
ATOM   10671 C C   . GLY D 2 229 ? 54.400  -35.116 16.040  1.00 129.72 ? 229 GLY D C   1 
ATOM   10672 O O   . GLY D 2 229 ? 55.408  -34.875 15.369  1.00 130.49 ? 229 GLY D O   1 
ATOM   10673 N N   . LEU D 2 230 ? 53.629  -36.182 15.818  1.00 125.10 ? 230 LEU D N   1 
ATOM   10674 C CA  . LEU D 2 230 ? 53.884  -37.061 14.686  1.00 122.16 ? 230 LEU D CA  1 
ATOM   10675 C C   . LEU D 2 230 ? 53.560  -36.366 13.371  1.00 123.72 ? 230 LEU D C   1 
ATOM   10676 O O   . LEU D 2 230 ? 54.141  -36.702 12.332  1.00 123.18 ? 230 LEU D O   1 
ATOM   10677 C CB  . LEU D 2 230 ? 53.072  -38.347 14.837  1.00 117.63 ? 230 LEU D CB  1 
ATOM   10678 C CG  . LEU D 2 230 ? 53.310  -39.477 13.840  1.00 111.79 ? 230 LEU D CG  1 
ATOM   10679 C CD1 . LEU D 2 230 ? 53.646  -40.752 14.586  1.00 104.20 ? 230 LEU D CD1 1 
ATOM   10680 C CD2 . LEU D 2 230 ? 52.083  -39.676 12.967  1.00 113.85 ? 230 LEU D CD2 1 
ATOM   10681 N N   . ARG D 2 231 ? 52.635  -35.405 13.397  1.00 126.17 ? 231 ARG D N   1 
ATOM   10682 C CA  . ARG D 2 231 ? 52.354  -34.608 12.208  1.00 131.04 ? 231 ARG D CA  1 
ATOM   10683 C C   . ARG D 2 231 ? 53.571  -33.780 11.806  1.00 134.74 ? 231 ARG D C   1 
ATOM   10684 O O   . ARG D 2 231 ? 53.985  -33.790 10.641  1.00 133.23 ? 231 ARG D O   1 
ATOM   10685 C CB  . ARG D 2 231 ? 51.136  -33.713 12.457  1.00 132.14 ? 231 ARG D CB  1 
ATOM   10686 C CG  . ARG D 2 231 ? 50.839  -32.719 11.342  1.00 134.92 ? 231 ARG D CG  1 
ATOM   10687 C CD  . ARG D 2 231 ? 50.854  -33.406 9.989   1.00 137.09 ? 231 ARG D CD  1 
ATOM   10688 N NE  . ARG D 2 231 ? 49.769  -32.987 9.110   1.00 145.82 ? 231 ARG D NE  1 
ATOM   10689 C CZ  . ARG D 2 231 ? 49.570  -33.491 7.896   1.00 146.31 ? 231 ARG D CZ  1 
ATOM   10690 N NH1 . ARG D 2 231 ? 50.382  -34.429 7.427   1.00 136.90 ? 231 ARG D NH1 1 
ATOM   10691 N NH2 . ARG D 2 231 ? 48.562  -33.059 7.151   1.00 146.68 ? 231 ARG D NH2 1 
ATOM   10692 N N   . LEU D 2 232 ? 54.161  -33.059 12.764  1.00 151.38 ? 232 LEU D N   1 
ATOM   10693 C CA  . LEU D 2 232 ? 55.340  -32.253 12.460  1.00 151.40 ? 232 LEU D CA  1 
ATOM   10694 C C   . LEU D 2 232 ? 56.498  -33.112 11.970  1.00 151.62 ? 232 LEU D C   1 
ATOM   10695 O O   . LEU D 2 232 ? 57.284  -32.671 11.123  1.00 151.59 ? 232 LEU D O   1 
ATOM   10696 C CB  . LEU D 2 232 ? 55.759  -31.451 13.691  1.00 152.92 ? 232 LEU D CB  1 
ATOM   10697 C CG  . LEU D 2 232 ? 54.730  -30.465 14.244  1.00 155.80 ? 232 LEU D CG  1 
ATOM   10698 C CD1 . LEU D 2 232 ? 55.304  -29.713 15.432  1.00 152.67 ? 232 LEU D CD1 1 
ATOM   10699 C CD2 . LEU D 2 232 ? 54.276  -29.496 13.164  1.00 162.19 ? 232 LEU D CD2 1 
ATOM   10700 N N   . TYR D 2 233 ? 56.619  -34.338 12.482  1.00 132.05 ? 233 TYR D N   1 
ATOM   10701 C CA  . TYR D 2 233 ? 57.694  -35.221 12.043  1.00 127.31 ? 233 TYR D CA  1 
ATOM   10702 C C   . TYR D 2 233 ? 57.441  -35.734 10.630  1.00 122.47 ? 233 TYR D C   1 
ATOM   10703 O O   . TYR D 2 233 ? 58.321  -35.656 9.765   1.00 119.80 ? 233 TYR D O   1 
ATOM   10704 C CB  . TYR D 2 233 ? 57.852  -36.383 13.025  1.00 121.52 ? 233 TYR D CB  1 
ATOM   10705 C CG  . TYR D 2 233 ? 58.864  -37.423 12.596  1.00 120.19 ? 233 TYR D CG  1 
ATOM   10706 C CD1 . TYR D 2 233 ? 60.228  -37.183 12.705  1.00 120.52 ? 233 TYR D CD1 1 
ATOM   10707 C CD2 . TYR D 2 233 ? 58.453  -38.649 12.091  1.00 119.32 ? 233 TYR D CD2 1 
ATOM   10708 C CE1 . TYR D 2 233 ? 61.154  -38.135 12.314  1.00 116.41 ? 233 TYR D CE1 1 
ATOM   10709 C CE2 . TYR D 2 233 ? 59.370  -39.605 11.699  1.00 118.20 ? 233 TYR D CE2 1 
ATOM   10710 C CZ  . TYR D 2 233 ? 60.719  -39.344 11.813  1.00 113.92 ? 233 TYR D CZ  1 
ATOM   10711 O OH  . TYR D 2 233 ? 61.633  -40.296 11.423  1.00 114.24 ? 233 TYR D OH  1 
ATOM   10712 N N   . LEU D 2 234 ? 56.241  -36.265 10.376  1.00 121.01 ? 234 LEU D N   1 
ATOM   10713 C CA  . LEU D 2 234 ? 55.926  -36.781 9.047   1.00 117.45 ? 234 LEU D CA  1 
ATOM   10714 C C   . LEU D 2 234 ? 55.884  -35.673 8.003   1.00 115.88 ? 234 LEU D C   1 
ATOM   10715 O O   . LEU D 2 234 ? 56.175  -35.922 6.827   1.00 110.57 ? 234 LEU D O   1 
ATOM   10716 C CB  . LEU D 2 234 ? 54.596  -37.533 9.075   1.00 120.21 ? 234 LEU D CB  1 
ATOM   10717 C CG  . LEU D 2 234 ? 54.602  -38.912 9.739   1.00 116.57 ? 234 LEU D CG  1 
ATOM   10718 C CD1 . LEU D 2 234 ? 53.288  -39.635 9.491   1.00 114.45 ? 234 LEU D CD1 1 
ATOM   10719 C CD2 . LEU D 2 234 ? 55.773  -39.747 9.242   1.00 114.36 ? 234 LEU D CD2 1 
ATOM   10720 N N   . ASP D 2 235 ? 55.523  -34.452 8.404   1.00 121.33 ? 235 ASP D N   1 
ATOM   10721 C CA  . ASP D 2 235 ? 55.560  -33.331 7.472   1.00 118.77 ? 235 ASP D CA  1 
ATOM   10722 C C   . ASP D 2 235 ? 56.991  -33.039 7.043   1.00 114.01 ? 235 ASP D C   1 
ATOM   10723 O O   . ASP D 2 235 ? 57.270  -32.845 5.854   1.00 109.36 ? 235 ASP D O   1 
ATOM   10724 C CB  . ASP D 2 235 ? 54.922  -32.094 8.104   1.00 122.74 ? 235 ASP D CB  1 
ATOM   10725 C CG  . ASP D 2 235 ? 54.779  -30.947 7.124   1.00 121.61 ? 235 ASP D CG  1 
ATOM   10726 O OD1 . ASP D 2 235 ? 54.894  -31.187 5.903   1.00 117.69 ? 235 ASP D OD1 1 
ATOM   10727 O OD2 . ASP D 2 235 ? 54.553  -29.804 7.575   1.00 128.80 ? 235 ASP D OD2 1 
ATOM   10728 N N   . SER D 2 236 ? 57.915  -33.002 8.006   1.00 115.28 ? 236 SER D N   1 
ATOM   10729 C CA  . SER D 2 236 ? 59.320  -32.819 7.667   1.00 112.58 ? 236 SER D CA  1 
ATOM   10730 C C   . SER D 2 236 ? 59.843  -33.984 6.839   1.00 110.65 ? 236 SER D C   1 
ATOM   10731 O O   . SER D 2 236 ? 60.768  -33.809 6.039   1.00 113.92 ? 236 SER D O   1 
ATOM   10732 C CB  . SER D 2 236 ? 60.150  -32.652 8.939   1.00 119.33 ? 236 SER D CB  1 
ATOM   10733 O OG  . SER D 2 236 ? 61.518  -32.448 8.631   1.00 124.72 ? 236 SER D OG  1 
ATOM   10734 N N   . LEU D 2 237 ? 59.263  -35.175 7.011   1.00 109.59 ? 237 LEU D N   1 
ATOM   10735 C CA  . LEU D 2 237 ? 59.666  -36.316 6.196   1.00 110.24 ? 237 LEU D CA  1 
ATOM   10736 C C   . LEU D 2 237 ? 59.209  -36.163 4.752   1.00 108.83 ? 237 LEU D C   1 
ATOM   10737 O O   . LEU D 2 237 ? 59.904  -36.610 3.833   1.00 110.33 ? 237 LEU D O   1 
ATOM   10738 C CB  . LEU D 2 237 ? 59.127  -37.614 6.795   1.00 110.73 ? 237 LEU D CB  1 
ATOM   10739 C CG  . LEU D 2 237 ? 60.150  -38.450 7.568   1.00 111.01 ? 237 LEU D CG  1 
ATOM   10740 C CD1 . LEU D 2 237 ? 60.754  -37.648 8.710   1.00 113.76 ? 237 LEU D CD1 1 
ATOM   10741 C CD2 . LEU D 2 237 ? 59.529  -39.740 8.085   1.00 108.15 ? 237 LEU D CD2 1 
ATOM   10742 N N   . ARG D 2 238 ? 58.045  -35.547 4.529   1.00 105.35 ? 238 ARG D N   1 
ATOM   10743 C CA  . ARG D 2 238 ? 57.620  -35.253 3.165   1.00 103.06 ? 238 ARG D CA  1 
ATOM   10744 C C   . ARG D 2 238 ? 58.593  -34.320 2.457   1.00 104.12 ? 238 ARG D C   1 
ATOM   10745 O O   . ARG D 2 238 ? 58.625  -34.294 1.222   1.00 103.76 ? 238 ARG D O   1 
ATOM   10746 C CB  . ARG D 2 238 ? 56.212  -34.655 3.167   1.00 103.56 ? 238 ARG D CB  1 
ATOM   10747 C CG  . ARG D 2 238 ? 55.231  -35.433 2.305   1.00 101.15 ? 238 ARG D CG  1 
ATOM   10748 C CD  . ARG D 2 238 ? 55.331  -36.919 2.608   1.00 101.64 ? 238 ARG D CD  1 
ATOM   10749 N NE  . ARG D 2 238 ? 55.518  -37.721 1.402   1.00 99.08  ? 238 ARG D NE  1 
ATOM   10750 C CZ  . ARG D 2 238 ? 54.709  -38.703 1.018   1.00 97.42  ? 238 ARG D CZ  1 
ATOM   10751 N NH1 . ARG D 2 238 ? 53.653  -39.024 1.753   1.00 100.64 ? 238 ARG D NH1 1 
ATOM   10752 N NH2 . ARG D 2 238 ? 54.964  -39.375 -0.096  1.00 95.85  ? 238 ARG D NH2 1 
ATOM   10753 N N   . LYS D 2 239 ? 59.382  -33.557 3.213   1.00 105.68 ? 239 LYS D N   1 
ATOM   10754 C CA  . LYS D 2 239 ? 60.386  -32.650 2.674   1.00 108.39 ? 239 LYS D CA  1 
ATOM   10755 C C   . LYS D 2 239 ? 61.763  -33.305 2.599   1.00 113.34 ? 239 LYS D C   1 
ATOM   10756 O O   . LYS D 2 239 ? 62.426  -33.242 1.559   1.00 111.47 ? 239 LYS D O   1 
ATOM   10757 C CB  . LYS D 2 239 ? 60.447  -31.381 3.530   1.00 105.48 ? 239 LYS D CB  1 
ATOM   10758 C CG  . LYS D 2 239 ? 59.092  -30.925 4.044   1.00 105.65 ? 239 LYS D CG  1 
ATOM   10759 C CD  . LYS D 2 239 ? 59.241  -29.899 5.154   1.00 109.37 ? 239 LYS D CD  1 
ATOM   10760 C CE  . LYS D 2 239 ? 57.889  -29.458 5.689   1.00 110.23 ? 239 LYS D CE  1 
ATOM   10761 N NZ  . LYS D 2 239 ? 57.910  -29.298 7.169   1.00 110.90 ? 239 LYS D NZ  1 
ATOM   10762 N N   . LYS D 2 240 ? 62.200  -33.940 3.691   1.00 116.40 ? 240 LYS D N   1 
ATOM   10763 C CA  . LYS D 2 240 ? 63.532  -34.540 3.729   1.00 116.27 ? 240 LYS D CA  1 
ATOM   10764 C C   . LYS D 2 240 ? 63.638  -35.698 2.745   1.00 120.33 ? 240 LYS D C   1 
ATOM   10765 O O   . LYS D 2 240 ? 64.415  -35.647 1.784   1.00 122.30 ? 240 LYS D O   1 
ATOM   10766 C CB  . LYS D 2 240 ? 63.853  -35.029 5.145   1.00 114.19 ? 240 LYS D CB  1 
ATOM   10767 C CG  . LYS D 2 240 ? 63.921  -33.955 6.219   1.00 110.95 ? 240 LYS D CG  1 
ATOM   10768 C CD  . LYS D 2 240 ? 64.912  -32.863 5.864   1.00 114.72 ? 240 LYS D CD  1 
ATOM   10769 C CE  . LYS D 2 240 ? 65.177  -31.981 7.070   1.00 122.45 ? 240 LYS D CE  1 
ATOM   10770 N NZ  . LYS D 2 240 ? 65.129  -32.787 8.326   1.00 120.75 ? 240 LYS D NZ  1 
ATOM   10771 N N   . SER D 2 241 ? 62.858  -36.753 2.970   1.00 140.01 ? 241 SER D N   1 
ATOM   10772 C CA  . SER D 2 241 ? 62.870  -37.939 2.116   1.00 140.60 ? 241 SER D CA  1 
ATOM   10773 C C   . SER D 2 241 ? 61.432  -38.396 1.914   1.00 139.41 ? 241 SER D C   1 
ATOM   10774 O O   . SER D 2 241 ? 60.861  -39.074 2.784   1.00 138.66 ? 241 SER D O   1 
ATOM   10775 C CB  . SER D 2 241 ? 63.719  -39.055 2.718   1.00 141.63 ? 241 SER D CB  1 
ATOM   10776 O OG  . SER D 2 241 ? 63.484  -39.174 4.111   1.00 145.72 ? 241 SER D OG  1 
ATOM   10777 N N   . PRO D 2 242 ? 60.816  -38.055 0.779   1.00 115.53 ? 242 PRO D N   1 
ATOM   10778 C CA  . PRO D 2 242 ? 59.410  -38.418 0.565   1.00 110.33 ? 242 PRO D CA  1 
ATOM   10779 C C   . PRO D 2 242 ? 59.191  -39.882 0.224   1.00 107.87 ? 242 PRO D C   1 
ATOM   10780 O O   . PRO D 2 242 ? 58.037  -40.331 0.225   1.00 106.74 ? 242 PRO D O   1 
ATOM   10781 C CB  . PRO D 2 242 ? 58.996  -37.515 -0.604  1.00 107.32 ? 242 PRO D CB  1 
ATOM   10782 C CG  . PRO D 2 242 ? 60.262  -37.293 -1.363  1.00 111.13 ? 242 PRO D CG  1 
ATOM   10783 C CD  . PRO D 2 242 ? 61.372  -37.277 -0.342  1.00 114.77 ? 242 PRO D CD  1 
ATOM   10784 N N   . ALA D 2 243 ? 60.248  -40.637 -0.070  1.00 106.49 ? 243 ALA D N   1 
ATOM   10785 C CA  . ALA D 2 243 ? 60.127  -42.054 -0.384  1.00 101.87 ? 243 ALA D CA  1 
ATOM   10786 C C   . ALA D 2 243 ? 60.141  -42.945 0.853   1.00 100.46 ? 243 ALA D C   1 
ATOM   10787 O O   . ALA D 2 243 ? 60.017  -44.166 0.717   1.00 97.06  ? 243 ALA D O   1 
ATOM   10788 C CB  . ALA D 2 243 ? 61.250  -42.481 -1.336  1.00 102.27 ? 243 ALA D CB  1 
ATOM   10789 N N   . LYS D 2 244 ? 60.279  -42.372 2.048   1.00 101.72 ? 244 LYS D N   1 
ATOM   10790 C CA  . LYS D 2 244 ? 60.221  -43.140 3.285   1.00 99.10  ? 244 LYS D CA  1 
ATOM   10791 C C   . LYS D 2 244 ? 58.806  -43.284 3.824   1.00 103.68 ? 244 LYS D C   1 
ATOM   10792 O O   . LYS D 2 244 ? 58.600  -44.017 4.798   1.00 105.47 ? 244 LYS D O   1 
ATOM   10793 C CB  . LYS D 2 244 ? 61.096  -42.491 4.362   1.00 102.11 ? 244 LYS D CB  1 
ATOM   10794 C CG  . LYS D 2 244 ? 62.555  -42.303 3.977   1.00 109.68 ? 244 LYS D CG  1 
ATOM   10795 C CD  . LYS D 2 244 ? 63.386  -43.547 4.261   1.00 101.74 ? 244 LYS D CD  1 
ATOM   10796 C CE  . LYS D 2 244 ? 63.963  -44.143 2.989   1.00 92.02  ? 244 LYS D CE  1 
ATOM   10797 N NZ  . LYS D 2 244 ? 64.650  -45.438 3.250   1.00 85.12  ? 244 LYS D NZ  1 
ATOM   10798 N N   . LEU D 2 245 ? 57.834  -42.610 3.217   1.00 104.18 ? 245 LEU D N   1 
ATOM   10799 C CA  . LEU D 2 245 ? 56.441  -42.659 3.637   1.00 99.07  ? 245 LEU D CA  1 
ATOM   10800 C C   . LEU D 2 245 ? 55.659  -43.494 2.633   1.00 98.94  ? 245 LEU D C   1 
ATOM   10801 O O   . LEU D 2 245 ? 55.741  -43.253 1.423   1.00 98.46  ? 245 LEU D O   1 
ATOM   10802 C CB  . LEU D 2 245 ? 55.848  -41.251 3.742   1.00 97.51  ? 245 LEU D CB  1 
ATOM   10803 C CG  . LEU D 2 245 ? 56.602  -40.258 4.632   1.00 100.36 ? 245 LEU D CG  1 
ATOM   10804 C CD1 . LEU D 2 245 ? 57.629  -39.469 3.829   1.00 106.77 ? 245 LEU D CD1 1 
ATOM   10805 C CD2 . LEU D 2 245 ? 55.648  -39.321 5.353   1.00 101.24 ? 245 LEU D CD2 1 
ATOM   10806 N N   . THR D 2 246 ? 54.913  -44.474 3.134   1.00 99.82  ? 246 THR D N   1 
ATOM   10807 C CA  . THR D 2 246 ? 54.203  -45.388 2.253   1.00 100.14 ? 246 THR D CA  1 
ATOM   10808 C C   . THR D 2 246 ? 53.126  -44.657 1.458   1.00 97.81  ? 246 THR D C   1 
ATOM   10809 O O   . THR D 2 246 ? 52.614  -43.610 1.866   1.00 95.65  ? 246 THR D O   1 
ATOM   10810 C CB  . THR D 2 246 ? 53.576  -46.533 3.051   1.00 98.15  ? 246 THR D CB  1 
ATOM   10811 O OG1 . THR D 2 246 ? 52.959  -47.461 2.150   1.00 95.44  ? 246 THR D OG1 1 
ATOM   10812 C CG2 . THR D 2 246 ? 52.528  -46.004 4.013   1.00 101.15 ? 246 THR D CG2 1 
ATOM   10813 N N   . SER D 2 247 ? 52.791  -45.225 0.303   1.00 97.89  ? 247 SER D N   1 
ATOM   10814 C CA  . SER D 2 247 ? 51.794  -44.655 -0.586  1.00 95.84  ? 247 SER D CA  1 
ATOM   10815 C C   . SER D 2 247 ? 50.988  -45.785 -1.209  1.00 93.89  ? 247 SER D C   1 
ATOM   10816 O O   . SER D 2 247 ? 51.410  -46.944 -1.214  1.00 93.06  ? 247 SER D O   1 
ATOM   10817 C CB  . SER D 2 247 ? 52.441  -43.791 -1.678  1.00 94.39  ? 247 SER D CB  1 
ATOM   10818 O OG  . SER D 2 247 ? 51.469  -43.297 -2.582  1.00 94.74  ? 247 SER D OG  1 
ATOM   10819 N N   . GLY D 2 248 ? 49.819  -45.435 -1.736  1.00 91.41  ? 248 GLY D N   1 
ATOM   10820 C CA  . GLY D 2 248 ? 48.961  -46.405 -2.371  1.00 89.69  ? 248 GLY D CA  1 
ATOM   10821 C C   . GLY D 2 248 ? 47.532  -45.923 -2.508  1.00 88.74  ? 248 GLY D C   1 
ATOM   10822 O O   . GLY D 2 248 ? 47.198  -44.785 -2.162  1.00 87.30  ? 248 GLY D O   1 
ATOM   10823 N N   . PRO D 2 249 ? 46.656  -46.787 -3.029  1.00 91.80  ? 249 PRO D N   1 
ATOM   10824 C CA  . PRO D 2 249 ? 45.254  -46.380 -3.191  1.00 89.11  ? 249 PRO D CA  1 
ATOM   10825 C C   . PRO D 2 249 ? 44.514  -46.284 -1.873  1.00 88.00  ? 249 PRO D C   1 
ATOM   10826 O O   . PRO D 2 249 ? 43.531  -45.540 -1.775  1.00 91.12  ? 249 PRO D O   1 
ATOM   10827 C CB  . PRO D 2 249 ? 44.672  -47.479 -4.088  1.00 93.16  ? 249 PRO D CB  1 
ATOM   10828 C CG  . PRO D 2 249 ? 45.499  -48.681 -3.771  1.00 93.87  ? 249 PRO D CG  1 
ATOM   10829 C CD  . PRO D 2 249 ? 46.889  -48.174 -3.472  1.00 95.84  ? 249 PRO D CD  1 
ATOM   10830 N N   . HIS D 2 250 ? 44.962  -47.006 -0.852  1.00 88.20  ? 250 HIS D N   1 
ATOM   10831 C CA  . HIS D 2 250 ? 44.357  -46.958 0.470   1.00 89.60  ? 250 HIS D CA  1 
ATOM   10832 C C   . HIS D 2 250 ? 45.112  -46.042 1.424   1.00 83.03  ? 250 HIS D C   1 
ATOM   10833 O O   . HIS D 2 250 ? 44.800  -46.014 2.619   1.00 85.14  ? 250 HIS D O   1 
ATOM   10834 C CB  . HIS D 2 250 ? 44.278  -48.366 1.053   1.00 91.49  ? 250 HIS D CB  1 
ATOM   10835 C CG  . HIS D 2 250 ? 45.615  -49.000 1.261   1.00 88.45  ? 250 HIS D CG  1 
ATOM   10836 N ND1 . HIS D 2 250 ? 46.404  -49.432 0.218   1.00 88.95  ? 250 HIS D ND1 1 
ATOM   10837 C CD2 . HIS D 2 250 ? 46.310  -49.260 2.393   1.00 90.40  ? 250 HIS D CD2 1 
ATOM   10838 C CE1 . HIS D 2 250 ? 47.525  -49.940 0.698   1.00 93.18  ? 250 HIS D CE1 1 
ATOM   10839 N NE2 . HIS D 2 250 ? 47.493  -49.848 2.016   1.00 91.79  ? 250 HIS D NE2 1 
ATOM   10840 N N   . ILE D 2 251 ? 46.087  -45.288 0.924   1.00 82.57  ? 251 ILE D N   1 
ATOM   10841 C CA  . ILE D 2 251 ? 46.920  -44.414 1.742   1.00 88.56  ? 251 ILE D CA  1 
ATOM   10842 C C   . ILE D 2 251 ? 46.555  -42.972 1.423   1.00 90.30  ? 251 ILE D C   1 
ATOM   10843 O O   . ILE D 2 251 ? 46.449  -42.596 0.250   1.00 88.10  ? 251 ILE D O   1 
ATOM   10844 C CB  . ILE D 2 251 ? 48.417  -44.673 1.497   1.00 91.92  ? 251 ILE D CB  1 
ATOM   10845 C CG1 . ILE D 2 251 ? 48.768  -46.124 1.833   1.00 90.83  ? 251 ILE D CG1 1 
ATOM   10846 C CG2 . ILE D 2 251 ? 49.269  -43.712 2.311   1.00 94.69  ? 251 ILE D CG2 1 
ATOM   10847 C CD1 . ILE D 2 251 ? 48.518  -46.494 3.278   1.00 92.40  ? 251 ILE D CD1 1 
ATOM   10848 N N   . VAL D 2 252 ? 46.358  -42.168 2.465   1.00 95.87  ? 252 VAL D N   1 
ATOM   10849 C CA  . VAL D 2 252 ? 46.028  -40.756 2.323   1.00 98.87  ? 252 VAL D CA  1 
ATOM   10850 C C   . VAL D 2 252 ? 46.942  -39.951 3.235   1.00 101.73 ? 252 VAL D C   1 
ATOM   10851 O O   . VAL D 2 252 ? 47.101  -40.284 4.415   1.00 102.64 ? 252 VAL D O   1 
ATOM   10852 C CB  . VAL D 2 252 ? 44.547  -40.475 2.646   1.00 98.18  ? 252 VAL D CB  1 
ATOM   10853 C CG1 . VAL D 2 252 ? 43.660  -40.933 1.499   1.00 96.41  ? 252 VAL D CG1 1 
ATOM   10854 C CG2 . VAL D 2 252 ? 44.138  -41.170 3.934   1.00 98.64  ? 252 VAL D CG2 1 
ATOM   10855 N N   . GLY D 2 253 ? 47.553  -38.906 2.686   1.00 117.17 ? 253 GLY D N   1 
ATOM   10856 C CA  . GLY D 2 253 ? 48.433  -38.058 3.463   1.00 120.40 ? 253 GLY D CA  1 
ATOM   10857 C C   . GLY D 2 253 ? 49.791  -38.676 3.717   1.00 121.65 ? 253 GLY D C   1 
ATOM   10858 O O   . GLY D 2 253 ? 50.368  -39.315 2.832   1.00 119.07 ? 253 GLY D O   1 
ATOM   10859 N N   . ASN D 2 254 ? 50.310  -38.495 4.927   1.00 115.61 ? 254 ASN D N   1 
ATOM   10860 C CA  . ASN D 2 254 ? 51.616  -39.009 5.313   1.00 113.41 ? 254 ASN D CA  1 
ATOM   10861 C C   . ASN D 2 254 ? 51.416  -40.201 6.236   1.00 113.11 ? 254 ASN D C   1 
ATOM   10862 O O   . ASN D 2 254 ? 50.830  -40.062 7.314   1.00 111.80 ? 254 ASN D O   1 
ATOM   10863 C CB  . ASN D 2 254 ? 52.443  -37.929 6.009   1.00 114.20 ? 254 ASN D CB  1 
ATOM   10864 C CG  . ASN D 2 254 ? 52.607  -36.687 5.163   1.00 111.13 ? 254 ASN D CG  1 
ATOM   10865 O OD1 . ASN D 2 254 ? 52.427  -36.724 3.946   1.00 109.97 ? 254 ASN D OD1 1 
ATOM   10866 N ND2 . ASN D 2 254 ? 52.951  -35.576 5.803   1.00 110.63 ? 254 ASN D ND2 1 
ATOM   10867 N N   . VAL D 2 255 ? 51.900  -41.365 5.817   1.00 119.33 ? 255 VAL D N   1 
ATOM   10868 C CA  . VAL D 2 255 ? 51.775  -42.592 6.593   1.00 118.43 ? 255 VAL D CA  1 
ATOM   10869 C C   . VAL D 2 255 ? 53.128  -43.286 6.610   1.00 120.70 ? 255 VAL D C   1 
ATOM   10870 O O   . VAL D 2 255 ? 53.761  -43.448 5.561   1.00 118.74 ? 255 VAL D O   1 
ATOM   10871 C CB  . VAL D 2 255 ? 50.694  -43.533 6.027   1.00 117.61 ? 255 VAL D CB  1 
ATOM   10872 C CG1 . VAL D 2 255 ? 50.627  -44.808 6.853   1.00 118.28 ? 255 VAL D CG1 1 
ATOM   10873 C CG2 . VAL D 2 255 ? 49.335  -42.846 6.003   1.00 117.34 ? 255 VAL D CG2 1 
ATOM   10874 N N   . LEU D 2 256 ? 53.571  -43.687 7.797   1.00 109.95 ? 256 LEU D N   1 
ATOM   10875 C CA  . LEU D 2 256 ? 54.849  -44.368 7.986   1.00 107.81 ? 256 LEU D CA  1 
ATOM   10876 C C   . LEU D 2 256 ? 54.556  -45.813 8.376   1.00 104.73 ? 256 LEU D C   1 
ATOM   10877 O O   . LEU D 2 256 ? 54.232  -46.102 9.532   1.00 100.44 ? 256 LEU D O   1 
ATOM   10878 C CB  . LEU D 2 256 ? 55.693  -43.665 9.047   1.00 109.64 ? 256 LEU D CB  1 
ATOM   10879 C CG  . LEU D 2 256 ? 57.038  -44.314 9.389   1.00 111.77 ? 256 LEU D CG  1 
ATOM   10880 C CD1 . LEU D 2 256 ? 57.909  -44.455 8.147   1.00 110.81 ? 256 LEU D CD1 1 
ATOM   10881 C CD2 . LEU D 2 256 ? 57.767  -43.540 10.481  1.00 109.89 ? 256 LEU D CD2 1 
ATOM   10882 N N   . VAL D 2 257 ? 54.672  -46.717 7.409   1.00 105.26 ? 257 VAL D N   1 
ATOM   10883 C CA  . VAL D 2 257 ? 54.417  -48.135 7.633   1.00 103.52 ? 257 VAL D CA  1 
ATOM   10884 C C   . VAL D 2 257 ? 55.752  -48.856 7.747   1.00 106.81 ? 257 VAL D C   1 
ATOM   10885 O O   . VAL D 2 257 ? 56.725  -48.510 7.065   1.00 109.67 ? 257 VAL D O   1 
ATOM   10886 C CB  . VAL D 2 257 ? 53.540  -48.725 6.508   1.00 101.05 ? 257 VAL D CB  1 
ATOM   10887 C CG1 . VAL D 2 257 ? 54.229  -49.890 5.801   1.00 103.71 ? 257 VAL D CG1 1 
ATOM   10888 C CG2 . VAL D 2 257 ? 52.191  -49.158 7.062   1.00 93.26  ? 257 VAL D CG2 1 
ATOM   10889 N N   . ASP D 2 258 ? 55.800  -49.855 8.621   1.00 108.30 ? 258 ASP D N   1 
ATOM   10890 C CA  . ASP D 2 258 ? 56.994  -50.656 8.823   1.00 107.04 ? 258 ASP D CA  1 
ATOM   10891 C C   . ASP D 2 258 ? 57.023  -51.819 7.842   1.00 104.89 ? 258 ASP D C   1 
ATOM   10892 O O   . ASP D 2 258 ? 55.984  -52.286 7.368   1.00 109.47 ? 258 ASP D O   1 
ATOM   10893 C CB  . ASP D 2 258 ? 57.054  -51.182 10.258  1.00 102.42 ? 258 ASP D CB  1 
ATOM   10894 C CG  . ASP D 2 258 ? 58.406  -51.768 10.609  1.00 103.94 ? 258 ASP D CG  1 
ATOM   10895 O OD1 . ASP D 2 258 ? 58.817  -52.762 9.974   1.00 103.86 ? 258 ASP D OD1 1 
ATOM   10896 O OD2 . ASP D 2 258 ? 59.063  -51.231 11.524  1.00 106.68 ? 258 ASP D OD2 1 
ATOM   10897 N N   . GLU D 2 259 ? 58.235  -52.280 7.533   1.00 104.28 ? 259 GLU D N   1 
ATOM   10898 C CA  . GLU D 2 259 ? 58.375  -53.436 6.656   1.00 104.07 ? 259 GLU D CA  1 
ATOM   10899 C C   . GLU D 2 259 ? 57.802  -54.695 7.295   1.00 103.79 ? 259 GLU D C   1 
ATOM   10900 O O   . GLU D 2 259 ? 57.373  -55.609 6.583   1.00 104.35 ? 259 GLU D O   1 
ATOM   10901 C CB  . GLU D 2 259 ? 59.846  -53.650 6.299   1.00 105.90 ? 259 GLU D CB  1 
ATOM   10902 C CG  . GLU D 2 259 ? 60.752  -53.783 7.515   1.00 110.97 ? 259 GLU D CG  1 
ATOM   10903 C CD  . GLU D 2 259 ? 62.221  -53.872 7.153   1.00 114.01 ? 259 GLU D CD  1 
ATOM   10904 O OE1 . GLU D 2 259 ? 62.541  -53.852 5.946   1.00 121.27 ? 259 GLU D OE1 1 
ATOM   10905 O OE2 . GLU D 2 259 ? 63.054  -53.971 8.079   1.00 110.63 ? 259 GLU D OE2 1 
ATOM   10906 N N   . THR D 2 260 ? 57.784  -54.761 8.629   1.00 96.24  ? 260 THR D N   1 
ATOM   10907 C CA  . THR D 2 260 ? 57.259  -55.935 9.316   1.00 93.40  ? 260 THR D CA  1 
ATOM   10908 C C   . THR D 2 260 ? 55.739  -55.917 9.417   1.00 90.88  ? 260 THR D C   1 
ATOM   10909 O O   . THR D 2 260 ? 55.109  -56.981 9.412   1.00 89.46  ? 260 THR D O   1 
ATOM   10910 C CB  . THR D 2 260 ? 57.874  -56.041 10.713  1.00 94.46  ? 260 THR D CB  1 
ATOM   10911 O OG1 . THR D 2 260 ? 59.270  -55.723 10.643  1.00 96.84  ? 260 THR D OG1 1 
ATOM   10912 C CG2 . THR D 2 260 ? 57.713  -57.450 11.262  1.00 96.16  ? 260 THR D CG2 1 
ATOM   10913 N N   . ALA D 2 261 ? 55.137  -54.733 9.509   1.00 92.52  ? 261 ALA D N   1 
ATOM   10914 C CA  . ALA D 2 261 ? 53.691  -54.633 9.649   1.00 82.76  ? 261 ALA D CA  1 
ATOM   10915 C C   . ALA D 2 261 ? 52.999  -55.084 8.371   1.00 79.04  ? 261 ALA D C   1 
ATOM   10916 O O   . ALA D 2 261 ? 53.452  -54.795 7.261   1.00 79.45  ? 261 ALA D O   1 
ATOM   10917 C CB  . ALA D 2 261 ? 53.283  -53.202 9.990   1.00 85.36  ? 261 ALA D CB  1 
ATOM   10918 N N   . THR D 2 262 ? 51.889  -55.794 8.533   1.00 78.68  ? 262 THR D N   1 
ATOM   10919 C CA  . THR D 2 262 ? 51.102  -56.288 7.413   1.00 78.72  ? 262 THR D CA  1 
ATOM   10920 C C   . THR D 2 262 ? 49.709  -55.680 7.464   1.00 81.08  ? 262 THR D C   1 
ATOM   10921 O O   . THR D 2 262 ? 49.085  -55.629 8.530   1.00 83.96  ? 262 THR D O   1 
ATOM   10922 C CB  . THR D 2 262 ? 51.014  -57.811 7.431   1.00 81.52  ? 262 THR D CB  1 
ATOM   10923 O OG1 . THR D 2 262 ? 49.997  -58.247 6.522   1.00 79.40  ? 262 THR D OG1 1 
ATOM   10924 C CG2 . THR D 2 262 ? 50.697  -58.313 8.834   1.00 83.43  ? 262 THR D CG2 1 
ATOM   10925 N N   . ILE D 2 263 ? 49.229  -55.218 6.314   1.00 79.71  ? 263 ILE D N   1 
ATOM   10926 C CA  . ILE D 2 263 ? 47.927  -54.575 6.195   1.00 77.50  ? 263 ILE D CA  1 
ATOM   10927 C C   . ILE D 2 263 ? 47.030  -55.450 5.334   1.00 81.01  ? 263 ILE D C   1 
ATOM   10928 O O   . ILE D 2 263 ? 47.451  -55.932 4.275   1.00 84.99  ? 263 ILE D O   1 
ATOM   10929 C CB  . ILE D 2 263 ? 48.054  -53.164 5.596   1.00 75.71  ? 263 ILE D CB  1 
ATOM   10930 C CG1 . ILE D 2 263 ? 48.899  -52.272 6.504   1.00 75.50  ? 263 ILE D CG1 1 
ATOM   10931 C CG2 . ILE D 2 263 ? 46.682  -52.550 5.375   1.00 79.66  ? 263 ILE D CG2 1 
ATOM   10932 C CD1 . ILE D 2 263 ? 49.011  -50.858 6.007   1.00 82.11  ? 263 ILE D CD1 1 
ATOM   10933 N N   . GLY D 2 264 ? 45.798  -55.655 5.787   1.00 85.16  ? 264 GLY D N   1 
ATOM   10934 C CA  . GLY D 2 264 ? 44.808  -56.360 5.007   1.00 101.75 ? 264 GLY D CA  1 
ATOM   10935 C C   . GLY D 2 264 ? 44.306  -55.514 3.848   1.00 103.96 ? 264 GLY D C   1 
ATOM   10936 O O   . GLY D 2 264 ? 44.765  -54.401 3.588   1.00 97.83  ? 264 GLY D O   1 
ATOM   10937 N N   . GLU D 2 265 ? 43.336  -56.070 3.131   1.00 112.59 ? 265 GLU D N   1 
ATOM   10938 C CA  . GLU D 2 265 ? 42.760  -55.402 1.976   1.00 111.73 ? 265 GLU D CA  1 
ATOM   10939 C C   . GLU D 2 265 ? 41.505  -54.633 2.377   1.00 105.09 ? 265 GLU D C   1 
ATOM   10940 O O   . GLU D 2 265 ? 40.859  -54.928 3.385   1.00 103.99 ? 265 GLU D O   1 
ATOM   10941 C CB  . GLU D 2 265 ? 42.433  -56.412 0.873   1.00 114.53 ? 265 GLU D CB  1 
ATOM   10942 C CG  . GLU D 2 265 ? 43.651  -57.163 0.350   1.00 117.91 ? 265 GLU D CG  1 
ATOM   10943 C CD  . GLU D 2 265 ? 44.580  -56.293 -0.478  1.00 117.58 ? 265 GLU D CD  1 
ATOM   10944 O OE1 . GLU D 2 265 ? 44.173  -55.178 -0.872  1.00 113.02 ? 265 GLU D OE1 1 
ATOM   10945 O OE2 . GLU D 2 265 ? 45.726  -56.725 -0.726  1.00 122.40 ? 265 GLU D OE2 1 
ATOM   10946 N N   . GLY D 2 266 ? 41.171  -53.629 1.572   1.00 101.03 ? 266 GLY D N   1 
ATOM   10947 C CA  . GLY D 2 266 ? 39.983  -52.836 1.824   1.00 98.66  ? 266 GLY D CA  1 
ATOM   10948 C C   . GLY D 2 266 ? 40.057  -51.951 3.048   1.00 96.25  ? 266 GLY D C   1 
ATOM   10949 O O   . GLY D 2 266 ? 39.027  -51.684 3.675   1.00 95.72  ? 266 GLY D O   1 
ATOM   10950 N N   . CYS D 2 267 ? 41.248  -51.485 3.404   1.00 93.87  ? 267 CYS D N   1 
ATOM   10951 C CA  . CYS D 2 267 ? 41.445  -50.592 4.536   1.00 87.77  ? 267 CYS D CA  1 
ATOM   10952 C C   . CYS D 2 267 ? 41.644  -49.163 4.045   1.00 89.31  ? 267 CYS D C   1 
ATOM   10953 O O   . CYS D 2 267 ? 41.722  -48.896 2.845   1.00 94.66  ? 267 CYS D O   1 
ATOM   10954 C CB  . CYS D 2 267 ? 42.643  -51.043 5.374   1.00 85.39  ? 267 CYS D CB  1 
ATOM   10955 S SG  . CYS D 2 267 ? 42.604  -52.782 5.854   1.00 81.70  ? 267 CYS D SG  1 
ATOM   10956 N N   . LEU D 2 268 ? 41.714  -48.235 4.995   1.00 85.03  ? 268 LEU D N   1 
ATOM   10957 C CA  . LEU D 2 268 ? 41.980  -46.836 4.671   1.00 88.11  ? 268 LEU D CA  1 
ATOM   10958 C C   . LEU D 2 268 ? 42.786  -46.243 5.817   1.00 88.93  ? 268 LEU D C   1 
ATOM   10959 O O   . LEU D 2 268 ? 42.260  -46.068 6.921   1.00 87.78  ? 268 LEU D O   1 
ATOM   10960 C CB  . LEU D 2 268 ? 40.684  -46.063 4.443   1.00 88.45  ? 268 LEU D CB  1 
ATOM   10961 C CG  . LEU D 2 268 ? 40.817  -44.711 3.741   1.00 86.71  ? 268 LEU D CG  1 
ATOM   10962 C CD1 . LEU D 2 268 ? 41.612  -44.860 2.450   1.00 90.20  ? 268 LEU D CD1 1 
ATOM   10963 C CD2 . LEU D 2 268 ? 39.450  -44.105 3.461   1.00 86.38  ? 268 LEU D CD2 1 
ATOM   10964 N N   . ILE D 2 269 ? 44.052  -45.927 5.552   1.00 88.00  ? 269 ILE D N   1 
ATOM   10965 C CA  . ILE D 2 269 ? 45.003  -45.511 6.577   1.00 88.93  ? 269 ILE D CA  1 
ATOM   10966 C C   . ILE D 2 269 ? 45.488  -44.107 6.245   1.00 89.75  ? 269 ILE D C   1 
ATOM   10967 O O   . ILE D 2 269 ? 45.892  -43.837 5.108   1.00 92.97  ? 269 ILE D O   1 
ATOM   10968 C CB  . ILE D 2 269 ? 46.193  -46.485 6.680   1.00 89.26  ? 269 ILE D CB  1 
ATOM   10969 C CG1 . ILE D 2 269 ? 45.713  -47.889 7.055   1.00 86.64  ? 269 ILE D CG1 1 
ATOM   10970 C CG2 . ILE D 2 269 ? 47.205  -45.983 7.699   1.00 94.94  ? 269 ILE D CG2 1 
ATOM   10971 C CD1 . ILE D 2 269 ? 45.506  -48.817 5.874   1.00 83.86  ? 269 ILE D CD1 1 
ATOM   10972 N N   . GLY D 2 270 ? 45.446  -43.219 7.234   1.00 95.21  ? 270 GLY D N   1 
ATOM   10973 C CA  . GLY D 2 270 ? 45.897  -41.861 7.061   1.00 100.84 ? 270 GLY D CA  1 
ATOM   10974 C C   . GLY D 2 270 ? 44.822  -40.851 7.409   1.00 107.57 ? 270 GLY D C   1 
ATOM   10975 O O   . GLY D 2 270 ? 43.639  -41.186 7.529   1.00 105.93 ? 270 GLY D O   1 
ATOM   10976 N N   . PRO D 2 271 ? 45.217  -39.580 7.587   1.00 126.16 ? 271 PRO D N   1 
ATOM   10977 C CA  . PRO D 2 271 ? 46.612  -39.135 7.507   1.00 126.21 ? 271 PRO D CA  1 
ATOM   10978 C C   . PRO D 2 271 ? 47.329  -39.239 8.848   1.00 128.06 ? 271 PRO D C   1 
ATOM   10979 O O   . PRO D 2 271 ? 46.675  -39.354 9.884   1.00 128.67 ? 271 PRO D O   1 
ATOM   10980 C CB  . PRO D 2 271 ? 46.494  -37.665 7.075   1.00 125.70 ? 271 PRO D CB  1 
ATOM   10981 C CG  . PRO D 2 271 ? 45.020  -37.424 6.815   1.00 133.74 ? 271 PRO D CG  1 
ATOM   10982 C CD  . PRO D 2 271 ? 44.295  -38.438 7.631   1.00 129.80 ? 271 PRO D CD  1 
ATOM   10983 N N   . ASP D 2 272 ? 48.664  -39.190 8.811   1.00 116.00 ? 272 ASP D N   1 
ATOM   10984 C CA  . ASP D 2 272 ? 49.512  -39.163 10.003  1.00 109.89 ? 272 ASP D CA  1 
ATOM   10985 C C   . ASP D 2 272 ? 49.228  -40.370 10.902  1.00 103.27 ? 272 ASP D C   1 
ATOM   10986 O O   . ASP D 2 272 ? 48.699  -40.263 12.011  1.00 98.04  ? 272 ASP D O   1 
ATOM   10987 C CB  . ASP D 2 272 ? 49.342  -37.843 10.762  1.00 113.82 ? 272 ASP D CB  1 
ATOM   10988 C CG  . ASP D 2 272 ? 49.621  -36.642 9.892   1.00 123.93 ? 272 ASP D CG  1 
ATOM   10989 O OD1 . ASP D 2 272 ? 48.663  -35.912 9.563   1.00 126.34 ? 272 ASP D OD1 1 
ATOM   10990 O OD2 . ASP D 2 272 ? 50.794  -36.451 9.511   1.00 126.55 ? 272 ASP D OD2 1 
ATOM   10991 N N   . VAL D 2 273 ? 49.607  -41.532 10.379  1.00 103.49 ? 273 VAL D N   1 
ATOM   10992 C CA  . VAL D 2 273 ? 49.485  -42.798 11.086  1.00 99.83  ? 273 VAL D CA  1 
ATOM   10993 C C   . VAL D 2 273 ? 50.827  -43.509 11.010  1.00 100.37 ? 273 VAL D C   1 
ATOM   10994 O O   . VAL D 2 273 ? 51.448  -43.569 9.942   1.00 104.65 ? 273 VAL D O   1 
ATOM   10995 C CB  . VAL D 2 273 ? 48.361  -43.681 10.502  1.00 97.39  ? 273 VAL D CB  1 
ATOM   10996 C CG1 . VAL D 2 273 ? 48.213  -44.954 11.317  1.00 95.85  ? 273 VAL D CG1 1 
ATOM   10997 C CG2 . VAL D 2 273 ? 47.046  -42.916 10.460  1.00 97.94  ? 273 VAL D CG2 1 
ATOM   10998 N N   . ALA D 2 274 ? 51.267  -44.061 12.139  1.00 95.07  ? 274 ALA D N   1 
ATOM   10999 C CA  . ALA D 2 274 ? 52.554  -44.744 12.230  1.00 94.59  ? 274 ALA D CA  1 
ATOM   11000 C C   . ALA D 2 274 ? 52.337  -46.110 12.863  1.00 92.94  ? 274 ALA D C   1 
ATOM   11001 O O   . ALA D 2 274 ? 51.961  -46.204 14.035  1.00 93.23  ? 274 ALA D O   1 
ATOM   11002 C CB  . ALA D 2 274 ? 53.561  -43.924 13.034  1.00 94.10  ? 274 ALA D CB  1 
ATOM   11003 N N   . ILE D 2 275 ? 52.573  -47.163 12.086  1.00 93.87  ? 275 ILE D N   1 
ATOM   11004 C CA  . ILE D 2 275 ? 52.365  -48.539 12.520  1.00 94.30  ? 275 ILE D CA  1 
ATOM   11005 C C   . ILE D 2 275 ? 53.725  -49.164 12.793  1.00 99.87  ? 275 ILE D C   1 
ATOM   11006 O O   . ILE D 2 275 ? 54.570  -49.237 11.893  1.00 100.44 ? 275 ILE D O   1 
ATOM   11007 C CB  . ILE D 2 275 ? 51.596  -49.345 11.465  1.00 93.28  ? 275 ILE D CB  1 
ATOM   11008 C CG1 . ILE D 2 275 ? 50.246  -48.685 11.181  1.00 92.02  ? 275 ILE D CG1 1 
ATOM   11009 C CG2 . ILE D 2 275 ? 51.403  -50.776 11.935  1.00 92.75  ? 275 ILE D CG2 1 
ATOM   11010 C CD1 . ILE D 2 275 ? 49.431  -49.401 10.133  1.00 95.87  ? 275 ILE D CD1 1 
ATOM   11011 N N   . GLY D 2 276 ? 53.930  -49.631 14.029  1.00 118.54 ? 276 GLY D N   1 
ATOM   11012 C CA  . GLY D 2 276 ? 55.171  -50.249 14.404  1.00 119.03 ? 276 GLY D CA  1 
ATOM   11013 C C   . GLY D 2 276 ? 55.370  -51.596 13.725  1.00 119.82 ? 276 GLY D C   1 
ATOM   11014 O O   . GLY D 2 276 ? 54.555  -52.037 12.905  1.00 120.11 ? 276 GLY D O   1 
ATOM   11015 N N   . PRO D 2 277 ? 56.480  -52.253 14.048  1.00 97.03  ? 277 PRO D N   1 
ATOM   11016 C CA  . PRO D 2 277 ? 56.751  -53.576 13.480  1.00 92.95  ? 277 PRO D CA  1 
ATOM   11017 C C   . PRO D 2 277 ? 55.986  -54.672 14.208  1.00 88.55  ? 277 PRO D C   1 
ATOM   11018 O O   . PRO D 2 277 ? 55.514  -54.504 15.334  1.00 90.64  ? 277 PRO D O   1 
ATOM   11019 C CB  . PRO D 2 277 ? 58.261  -53.738 13.678  1.00 98.32  ? 277 PRO D CB  1 
ATOM   11020 C CG  . PRO D 2 277 ? 58.549  -52.939 14.903  1.00 99.28  ? 277 PRO D CG  1 
ATOM   11021 C CD  . PRO D 2 277 ? 57.603  -51.763 14.868  1.00 99.27  ? 277 PRO D CD  1 
ATOM   11022 N N   . GLY D 2 278 ? 55.872  -55.815 13.534  1.00 85.43  ? 278 GLY D N   1 
ATOM   11023 C CA  . GLY D 2 278 ? 55.200  -56.966 14.105  1.00 88.16  ? 278 GLY D CA  1 
ATOM   11024 C C   . GLY D 2 278 ? 53.704  -56.837 14.279  1.00 86.29  ? 278 GLY D C   1 
ATOM   11025 O O   . GLY D 2 278 ? 53.096  -57.702 14.917  1.00 87.50  ? 278 GLY D O   1 
ATOM   11026 N N   . CYS D 2 279 ? 53.088  -55.794 13.732  1.00 83.89  ? 279 CYS D N   1 
ATOM   11027 C CA  . CYS D 2 279 ? 51.656  -55.588 13.867  1.00 79.04  ? 279 CYS D CA  1 
ATOM   11028 C C   . CYS D 2 279 ? 50.886  -56.447 12.871  1.00 82.20  ? 279 CYS D C   1 
ATOM   11029 O O   . CYS D 2 279 ? 51.427  -56.936 11.875  1.00 85.06  ? 279 CYS D O   1 
ATOM   11030 C CB  . CYS D 2 279 ? 51.299  -54.121 13.656  1.00 78.04  ? 279 CYS D CB  1 
ATOM   11031 S SG  . CYS D 2 279 ? 52.266  -52.999 14.661  1.00 76.45  ? 279 CYS D SG  1 
ATOM   11032 N N   . ILE D 2 280 ? 49.599  -56.623 13.155  1.00 80.20  ? 280 ILE D N   1 
ATOM   11033 C CA  . ILE D 2 280 ? 48.702  -57.417 12.325  1.00 80.67  ? 280 ILE D CA  1 
ATOM   11034 C C   . ILE D 2 280 ? 47.442  -56.585 12.121  1.00 87.34  ? 280 ILE D C   1 
ATOM   11035 O O   . ILE D 2 280 ? 46.583  -56.519 13.007  1.00 89.72  ? 280 ILE D O   1 
ATOM   11036 C CB  . ILE D 2 280 ? 48.372  -58.769 12.963  1.00 85.23  ? 280 ILE D CB  1 
ATOM   11037 C CG1 . ILE D 2 280 ? 49.658  -59.485 13.391  1.00 90.60  ? 280 ILE D CG1 1 
ATOM   11038 C CG2 . ILE D 2 280 ? 47.560  -59.621 12.002  1.00 95.10  ? 280 ILE D CG2 1 
ATOM   11039 C CD1 . ILE D 2 280 ? 49.432  -60.808 14.072  1.00 91.17  ? 280 ILE D CD1 1 
ATOM   11040 N N   . VAL D 2 281 ? 47.322  -55.954 10.956  1.00 91.19  ? 281 VAL D N   1 
ATOM   11041 C CA  . VAL D 2 281 ? 46.172  -55.120 10.625  1.00 87.93  ? 281 VAL D CA  1 
ATOM   11042 C C   . VAL D 2 281 ? 45.205  -55.938 9.780   1.00 91.65  ? 281 VAL D C   1 
ATOM   11043 O O   . VAL D 2 281 ? 45.578  -56.450 8.717   1.00 95.77  ? 281 VAL D O   1 
ATOM   11044 C CB  . VAL D 2 281 ? 46.600  -53.845 9.884   1.00 84.59  ? 281 VAL D CB  1 
ATOM   11045 C CG1 . VAL D 2 281 ? 45.383  -53.125 9.335   1.00 85.13  ? 281 VAL D CG1 1 
ATOM   11046 C CG2 . VAL D 2 281 ? 47.396  -52.938 10.810  1.00 85.90  ? 281 VAL D CG2 1 
ATOM   11047 N N   . GLU D 2 282 ? 43.967  -56.066 10.250  1.00 92.01  ? 282 GLU D N   1 
ATOM   11048 C CA  . GLU D 2 282 ? 42.955  -56.820 9.529   1.00 94.41  ? 282 GLU D CA  1 
ATOM   11049 C C   . GLU D 2 282 ? 42.212  -55.897 8.557   1.00 89.24  ? 282 GLU D C   1 
ATOM   11050 O O   . GLU D 2 282 ? 42.548  -54.721 8.398   1.00 83.83  ? 282 GLU D O   1 
ATOM   11051 C CB  . GLU D 2 282 ? 42.032  -57.522 10.524  1.00 93.24  ? 282 GLU D CB  1 
ATOM   11052 C CG  . GLU D 2 282 ? 42.800  -58.491 11.428  1.00 98.65  ? 282 GLU D CG  1 
ATOM   11053 C CD  . GLU D 2 282 ? 41.909  -59.449 12.194  1.00 101.57 ? 282 GLU D CD  1 
ATOM   11054 O OE1 . GLU D 2 282 ? 40.672  -59.292 12.145  1.00 98.94  ? 282 GLU D OE1 1 
ATOM   11055 O OE2 . GLU D 2 282 ? 42.455  -60.353 12.863  1.00 105.53 ? 282 GLU D OE2 1 
ATOM   11056 N N   . SER D 2 283 ? 41.181  -56.429 7.902   1.00 92.15  ? 283 SER D N   1 
ATOM   11057 C CA  . SER D 2 283 ? 40.523  -55.737 6.799   1.00 96.17  ? 283 SER D CA  1 
ATOM   11058 C C   . SER D 2 283 ? 39.376  -54.848 7.264   1.00 87.37  ? 283 SER D C   1 
ATOM   11059 O O   . SER D 2 283 ? 38.765  -55.073 8.311   1.00 83.31  ? 283 SER D O   1 
ATOM   11060 C CB  . SER D 2 283 ? 40.000  -56.737 5.769   1.00 104.43 ? 283 SER D CB  1 
ATOM   11061 O OG  . SER D 2 283 ? 41.062  -57.226 4.968   1.00 113.55 ? 283 SER D OG  1 
ATOM   11062 N N   . GLY D 2 284 ? 39.091  -53.824 6.462   1.00 85.56  ? 284 GLY D N   1 
ATOM   11063 C CA  . GLY D 2 284 ? 37.976  -52.940 6.719   1.00 79.29  ? 284 GLY D CA  1 
ATOM   11064 C C   . GLY D 2 284 ? 38.240  -51.875 7.755   1.00 81.36  ? 284 GLY D C   1 
ATOM   11065 O O   . GLY D 2 284 ? 37.290  -51.231 8.213   1.00 83.62  ? 284 GLY D O   1 
ATOM   11066 N N   . VAL D 2 285 ? 39.496  -51.661 8.131   1.00 81.14  ? 285 VAL D N   1 
ATOM   11067 C CA  . VAL D 2 285 ? 39.830  -50.739 9.205   1.00 83.35  ? 285 VAL D CA  1 
ATOM   11068 C C   . VAL D 2 285 ? 39.974  -49.330 8.643   1.00 83.79  ? 285 VAL D C   1 
ATOM   11069 O O   . VAL D 2 285 ? 40.168  -49.123 7.442   1.00 82.94  ? 285 VAL D O   1 
ATOM   11070 C CB  . VAL D 2 285 ? 41.109  -51.184 9.944   1.00 82.69  ? 285 VAL D CB  1 
ATOM   11071 C CG1 . VAL D 2 285 ? 40.959  -52.612 10.456  1.00 79.51  ? 285 VAL D CG1 1 
ATOM   11072 C CG2 . VAL D 2 285 ? 42.317  -51.068 9.033   1.00 84.89  ? 285 VAL D CG2 1 
ATOM   11073 N N   . ARG D 2 286 ? 39.877  -48.344 9.535   1.00 86.33  ? 286 ARG D N   1 
ATOM   11074 C CA  . ARG D 2 286 ? 39.946  -46.930 9.165   1.00 86.08  ? 286 ARG D CA  1 
ATOM   11075 C C   . ARG D 2 286 ? 40.779  -46.217 10.227  1.00 89.07  ? 286 ARG D C   1 
ATOM   11076 O O   . ARG D 2 286 ? 40.271  -45.881 11.302  1.00 87.33  ? 286 ARG D O   1 
ATOM   11077 C CB  . ARG D 2 286 ? 38.548  -46.330 9.048   1.00 84.44  ? 286 ARG D CB  1 
ATOM   11078 C CG  . ARG D 2 286 ? 38.495  -44.825 8.857   1.00 87.56  ? 286 ARG D CG  1 
ATOM   11079 C CD  . ARG D 2 286 ? 39.406  -44.357 7.737   1.00 87.78  ? 286 ARG D CD  1 
ATOM   11080 N NE  . ARG D 2 286 ? 39.231  -42.933 7.475   1.00 94.46  ? 286 ARG D NE  1 
ATOM   11081 C CZ  . ARG D 2 286 ? 40.157  -42.154 6.928   1.00 93.66  ? 286 ARG D CZ  1 
ATOM   11082 N NH1 . ARG D 2 286 ? 41.334  -42.662 6.591   1.00 90.96  ? 286 ARG D NH1 1 
ATOM   11083 N NH2 . ARG D 2 286 ? 39.909  -40.868 6.726   1.00 98.54  ? 286 ARG D NH2 1 
ATOM   11084 N N   . LEU D 2 287 ? 42.058  -46.006 9.931   1.00 99.30  ? 287 LEU D N   1 
ATOM   11085 C CA  . LEU D 2 287 ? 42.978  -45.348 10.846  1.00 98.85  ? 287 LEU D CA  1 
ATOM   11086 C C   . LEU D 2 287 ? 43.214  -43.911 10.405  1.00 100.59 ? 287 LEU D C   1 
ATOM   11087 O O   . LEU D 2 287 ? 43.328  -43.626 9.209   1.00 104.83 ? 287 LEU D O   1 
ATOM   11088 C CB  . LEU D 2 287 ? 44.308  -46.100 10.922  1.00 99.29  ? 287 LEU D CB  1 
ATOM   11089 C CG  . LEU D 2 287 ? 44.207  -47.571 11.331  1.00 100.78 ? 287 LEU D CG  1 
ATOM   11090 C CD1 . LEU D 2 287 ? 45.586  -48.201 11.416  1.00 103.17 ? 287 LEU D CD1 1 
ATOM   11091 C CD2 . LEU D 2 287 ? 43.468  -47.708 12.652  1.00 101.38 ? 287 LEU D CD2 1 
ATOM   11092 N N   . SER D 2 288 ? 43.284  -43.006 11.378  1.00 93.00  ? 288 SER D N   1 
ATOM   11093 C CA  . SER D 2 288 ? 43.447  -41.590 11.080  1.00 93.32  ? 288 SER D CA  1 
ATOM   11094 C C   . SER D 2 288 ? 44.032  -40.892 12.296  1.00 94.42  ? 288 SER D C   1 
ATOM   11095 O O   . SER D 2 288 ? 43.502  -41.025 13.402  1.00 96.93  ? 288 SER D O   1 
ATOM   11096 C CB  . SER D 2 288 ? 42.106  -40.958 10.685  1.00 97.37  ? 288 SER D CB  1 
ATOM   11097 O OG  . SER D 2 288 ? 41.093  -41.283 11.621  1.00 91.28  ? 288 SER D OG  1 
ATOM   11098 N N   . ARG D 2 289 ? 45.125  -40.161 12.086  1.00 94.56  ? 289 ARG D N   1 
ATOM   11099 C CA  . ARG D 2 289 ? 45.744  -39.320 13.108  1.00 102.19 ? 289 ARG D CA  1 
ATOM   11100 C C   . ARG D 2 289 ? 46.191  -40.115 14.335  1.00 100.67 ? 289 ARG D C   1 
ATOM   11101 O O   . ARG D 2 289 ? 46.431  -39.538 15.400  1.00 101.79 ? 289 ARG D O   1 
ATOM   11102 C CB  . ARG D 2 289 ? 44.801  -38.178 13.522  1.00 108.94 ? 289 ARG D CB  1 
ATOM   11103 C CG  . ARG D 2 289 ? 45.495  -36.952 14.116  1.00 116.07 ? 289 ARG D CG  1 
ATOM   11104 C CD  . ARG D 2 289 ? 44.486  -35.927 14.625  1.00 118.76 ? 289 ARG D CD  1 
ATOM   11105 N NE  . ARG D 2 289 ? 45.087  -34.998 15.579  1.00 125.81 ? 289 ARG D NE  1 
ATOM   11106 C CZ  . ARG D 2 289 ? 45.706  -33.871 15.239  1.00 129.10 ? 289 ARG D CZ  1 
ATOM   11107 N NH1 . ARG D 2 289 ? 45.810  -33.527 13.963  1.00 132.97 ? 289 ARG D NH1 1 
ATOM   11108 N NH2 . ARG D 2 289 ? 46.223  -33.088 16.176  1.00 129.48 ? 289 ARG D NH2 1 
ATOM   11109 N N   . CYS D 2 290 ? 46.313  -41.431 14.219  1.00 94.61  ? 290 CYS D N   1 
ATOM   11110 C CA  . CYS D 2 290 ? 46.701  -42.267 15.342  1.00 90.68  ? 290 CYS D CA  1 
ATOM   11111 C C   . CYS D 2 290 ? 48.105  -42.814 15.125  1.00 94.19  ? 290 CYS D C   1 
ATOM   11112 O O   . CYS D 2 290 ? 48.722  -42.620 14.077  1.00 96.83  ? 290 CYS D O   1 
ATOM   11113 C CB  . CYS D 2 290 ? 45.704  -43.413 15.536  1.00 86.61  ? 290 CYS D CB  1 
ATOM   11114 S SG  . CYS D 2 290 ? 45.434  -44.391 14.045  1.00 86.17  ? 290 CYS D SG  1 
ATOM   11115 N N   . THR D 2 291 ? 48.616  -43.490 16.150  1.00 92.58  ? 291 THR D N   1 
ATOM   11116 C CA  . THR D 2 291 ? 49.908  -44.159 16.072  1.00 85.42  ? 291 THR D CA  1 
ATOM   11117 C C   . THR D 2 291 ? 49.761  -45.543 16.678  1.00 84.66  ? 291 THR D C   1 
ATOM   11118 O O   . THR D 2 291 ? 49.233  -45.688 17.784  1.00 92.87  ? 291 THR D O   1 
ATOM   11119 C CB  . THR D 2 291 ? 51.013  -43.390 16.810  1.00 91.36  ? 291 THR D CB  1 
ATOM   11120 O OG1 . THR D 2 291 ? 50.968  -43.716 18.205  1.00 98.13  ? 291 THR D OG1 1 
ATOM   11121 C CG2 . THR D 2 291 ? 50.852  -41.884 16.638  1.00 96.66  ? 291 THR D CG2 1 
ATOM   11122 N N   . VAL D 2 292 ? 50.231  -46.552 15.952  1.00 85.34  ? 292 VAL D N   1 
ATOM   11123 C CA  . VAL D 2 292 ? 50.141  -47.947 16.364  1.00 85.02  ? 292 VAL D CA  1 
ATOM   11124 C C   . VAL D 2 292 ? 51.543  -48.441 16.691  1.00 89.36  ? 292 VAL D C   1 
ATOM   11125 O O   . VAL D 2 292 ? 52.463  -48.306 15.875  1.00 94.12  ? 292 VAL D O   1 
ATOM   11126 C CB  . VAL D 2 292 ? 49.484  -48.804 15.269  1.00 84.32  ? 292 VAL D CB  1 
ATOM   11127 C CG1 . VAL D 2 292 ? 49.693  -50.276 15.545  1.00 82.59  ? 292 VAL D CG1 1 
ATOM   11128 C CG2 . VAL D 2 292 ? 47.999  -48.476 15.172  1.00 86.08  ? 292 VAL D CG2 1 
ATOM   11129 N N   . MET D 2 293 ? 51.705  -49.018 17.879  1.00 85.29  ? 293 MET D N   1 
ATOM   11130 C CA  . MET D 2 293 ? 52.990  -49.522 18.328  1.00 90.10  ? 293 MET D CA  1 
ATOM   11131 C C   . MET D 2 293 ? 53.110  -51.013 18.012  1.00 92.97  ? 293 MET D C   1 
ATOM   11132 O O   . MET D 2 293 ? 52.286  -51.586 17.297  1.00 94.15  ? 293 MET D O   1 
ATOM   11133 C CB  . MET D 2 293 ? 53.176  -49.211 19.814  1.00 94.75  ? 293 MET D CB  1 
ATOM   11134 C CG  . MET D 2 293 ? 53.323  -47.721 20.084  1.00 93.30  ? 293 MET D CG  1 
ATOM   11135 S SD  . MET D 2 293 ? 53.824  -47.331 21.764  1.00 102.15 ? 293 MET D SD  1 
ATOM   11136 C CE  . MET D 2 293 ? 53.762  -45.542 21.716  1.00 101.08 ? 293 MET D CE  1 
ATOM   11137 N N   . ARG D 2 294 ? 54.143  -51.650 18.555  1.00 92.95  ? 294 ARG D N   1 
ATOM   11138 C CA  . ARG D 2 294 ? 54.546  -52.978 18.110  1.00 86.39  ? 294 ARG D CA  1 
ATOM   11139 C C   . ARG D 2 294 ? 53.541  -54.054 18.507  1.00 88.24  ? 294 ARG D C   1 
ATOM   11140 O O   . ARG D 2 294 ? 52.881  -53.975 19.546  1.00 94.07  ? 294 ARG D O   1 
ATOM   11141 C CB  . ARG D 2 294 ? 55.916  -53.328 18.689  1.00 89.52  ? 294 ARG D CB  1 
ATOM   11142 C CG  . ARG D 2 294 ? 57.002  -52.326 18.350  1.00 93.86  ? 294 ARG D CG  1 
ATOM   11143 C CD  . ARG D 2 294 ? 58.330  -52.736 18.957  1.00 90.83  ? 294 ARG D CD  1 
ATOM   11144 N NE  . ARG D 2 294 ? 58.662  -54.121 18.637  1.00 87.38  ? 294 ARG D NE  1 
ATOM   11145 C CZ  . ARG D 2 294 ? 59.799  -54.717 18.979  1.00 86.26  ? 294 ARG D CZ  1 
ATOM   11146 N NH1 . ARG D 2 294 ? 60.725  -54.048 19.653  1.00 88.79  ? 294 ARG D NH1 1 
ATOM   11147 N NH2 . ARG D 2 294 ? 60.014  -55.980 18.639  1.00 87.82  ? 294 ARG D NH2 1 
ATOM   11148 N N   . GLY D 2 295 ? 53.440  -55.077 17.657  1.00 86.65  ? 295 GLY D N   1 
ATOM   11149 C CA  . GLY D 2 295 ? 52.799  -56.336 17.985  1.00 88.41  ? 295 GLY D CA  1 
ATOM   11150 C C   . GLY D 2 295 ? 51.298  -56.317 18.163  1.00 85.57  ? 295 GLY D C   1 
ATOM   11151 O O   . GLY D 2 295 ? 50.695  -57.393 18.257  1.00 86.09  ? 295 GLY D O   1 
ATOM   11152 N N   . VAL D 2 296 ? 50.664  -55.153 18.205  1.00 85.22  ? 296 VAL D N   1 
ATOM   11153 C CA  . VAL D 2 296 ? 49.226  -55.093 18.440  1.00 88.14  ? 296 VAL D CA  1 
ATOM   11154 C C   . VAL D 2 296 ? 48.485  -55.431 17.155  1.00 83.22  ? 296 VAL D C   1 
ATOM   11155 O O   . VAL D 2 296 ? 48.834  -54.955 16.068  1.00 80.88  ? 296 VAL D O   1 
ATOM   11156 C CB  . VAL D 2 296 ? 48.823  -53.708 18.981  1.00 88.78  ? 296 VAL D CB  1 
ATOM   11157 C CG1 . VAL D 2 296 ? 49.500  -52.614 18.196  1.00 85.28  ? 296 VAL D CG1 1 
ATOM   11158 C CG2 . VAL D 2 296 ? 47.314  -53.535 18.927  1.00 88.83  ? 296 VAL D CG2 1 
ATOM   11159 N N   . ARG D 2 297 ? 47.456  -56.264 17.277  1.00 82.12  ? 297 ARG D N   1 
ATOM   11160 C CA  . ARG D 2 297 ? 46.608  -56.641 16.157  1.00 82.30  ? 297 ARG D CA  1 
ATOM   11161 C C   . ARG D 2 297 ? 45.261  -55.944 16.291  1.00 86.36  ? 297 ARG D C   1 
ATOM   11162 O O   . ARG D 2 297 ? 44.618  -56.020 17.343  1.00 84.88  ? 297 ARG D O   1 
ATOM   11163 C CB  . ARG D 2 297 ? 46.417  -58.158 16.088  1.00 83.99  ? 297 ARG D CB  1 
ATOM   11164 C CG  . ARG D 2 297 ? 45.283  -58.588 15.169  1.00 85.32  ? 297 ARG D CG  1 
ATOM   11165 C CD  . ARG D 2 297 ? 44.948  -60.063 15.316  1.00 85.50  ? 297 ARG D CD  1 
ATOM   11166 N NE  . ARG D 2 297 ? 46.092  -60.930 15.047  1.00 92.00  ? 297 ARG D NE  1 
ATOM   11167 C CZ  . ARG D 2 297 ? 46.005  -62.248 14.900  1.00 92.89  ? 297 ARG D CZ  1 
ATOM   11168 N NH1 . ARG D 2 297 ? 44.825  -62.847 14.993  1.00 98.77  ? 297 ARG D NH1 1 
ATOM   11169 N NH2 . ARG D 2 297 ? 47.091  -62.969 14.660  1.00 90.55  ? 297 ARG D NH2 1 
ATOM   11170 N N   . ILE D 2 298 ? 44.840  -55.268 15.226  1.00 95.14  ? 298 ILE D N   1 
ATOM   11171 C CA  . ILE D 2 298 ? 43.538  -54.613 15.162  1.00 95.57  ? 298 ILE D CA  1 
ATOM   11172 C C   . ILE D 2 298 ? 42.642  -55.442 14.255  1.00 95.20  ? 298 ILE D C   1 
ATOM   11173 O O   . ILE D 2 298 ? 42.977  -55.681 13.089  1.00 95.90  ? 298 ILE D O   1 
ATOM   11174 C CB  . ILE D 2 298 ? 43.652  -53.166 14.660  1.00 95.72  ? 298 ILE D CB  1 
ATOM   11175 C CG1 . ILE D 2 298 ? 44.504  -52.337 15.624  1.00 98.21  ? 298 ILE D CG1 1 
ATOM   11176 C CG2 . ILE D 2 298 ? 42.273  -52.546 14.499  1.00 94.18  ? 298 ILE D CG2 1 
ATOM   11177 C CD1 . ILE D 2 298 ? 44.665  -50.906 15.197  1.00 100.18 ? 298 ILE D CD1 1 
ATOM   11178 N N   . LYS D 2 299 ? 41.507  -55.884 14.790  1.00 88.94  ? 299 LYS D N   1 
ATOM   11179 C CA  . LYS D 2 299 ? 40.637  -56.790 14.062  1.00 85.28  ? 299 LYS D CA  1 
ATOM   11180 C C   . LYS D 2 299 ? 39.842  -56.035 12.997  1.00 82.82  ? 299 LYS D C   1 
ATOM   11181 O O   . LYS D 2 299 ? 40.033  -54.837 12.761  1.00 83.48  ? 299 LYS D O   1 
ATOM   11182 C CB  . LYS D 2 299 ? 39.716  -57.531 15.027  1.00 88.19  ? 299 LYS D CB  1 
ATOM   11183 C CG  . LYS D 2 299 ? 40.444  -58.492 15.958  1.00 89.01  ? 299 LYS D CG  1 
ATOM   11184 C CD  . LYS D 2 299 ? 39.471  -59.248 16.850  1.00 91.34  ? 299 LYS D CD  1 
ATOM   11185 C CE  . LYS D 2 299 ? 40.204  -60.194 17.791  1.00 96.27  ? 299 LYS D CE  1 
ATOM   11186 N NZ  . LYS D 2 299 ? 39.272  -60.947 18.678  1.00 96.98  ? 299 LYS D NZ  1 
ATOM   11187 N N   . LYS D 2 300 ? 38.938  -56.755 12.342  1.00 83.83  ? 300 LYS D N   1 
ATOM   11188 C CA  . LYS D 2 300 ? 38.273  -56.242 11.154  1.00 77.19  ? 300 LYS D CA  1 
ATOM   11189 C C   . LYS D 2 300 ? 37.217  -55.196 11.499  1.00 74.41  ? 300 LYS D C   1 
ATOM   11190 O O   . LYS D 2 300 ? 36.585  -55.239 12.558  1.00 75.09  ? 300 LYS D O   1 
ATOM   11191 C CB  . LYS D 2 300 ? 37.642  -57.393 10.369  1.00 77.72  ? 300 LYS D CB  1 
ATOM   11192 C CG  . LYS D 2 300 ? 38.659  -58.248 9.627   1.00 82.60  ? 300 LYS D CG  1 
ATOM   11193 C CD  . LYS D 2 300 ? 38.024  -59.422 8.896   1.00 79.81  ? 300 LYS D CD  1 
ATOM   11194 C CE  . LYS D 2 300 ? 37.827  -60.615 9.817   1.00 90.82  ? 300 LYS D CE  1 
ATOM   11195 N NZ  . LYS D 2 300 ? 37.416  -61.845 9.080   1.00 84.40  ? 300 LYS D NZ  1 
ATOM   11196 N N   . HIS D 2 301 ? 37.041  -54.245 10.578  1.00 76.65  ? 301 HIS D N   1 
ATOM   11197 C CA  . HIS D 2 301 ? 35.967  -53.251 10.616  1.00 77.04  ? 301 HIS D CA  1 
ATOM   11198 C C   . HIS D 2 301 ? 36.088  -52.293 11.799  1.00 72.46  ? 301 HIS D C   1 
ATOM   11199 O O   . HIS D 2 301 ? 35.085  -51.759 12.274  1.00 72.30  ? 301 HIS D O   1 
ATOM   11200 C CB  . HIS D 2 301 ? 34.590  -53.925 10.623  1.00 74.30  ? 301 HIS D CB  1 
ATOM   11201 C CG  . HIS D 2 301 ? 34.424  -54.969 9.563   1.00 71.34  ? 301 HIS D CG  1 
ATOM   11202 N ND1 . HIS D 2 301 ? 33.685  -56.116 9.757   1.00 70.16  ? 301 HIS D ND1 1 
ATOM   11203 C CD2 . HIS D 2 301 ? 34.902  -55.039 8.299   1.00 73.26  ? 301 HIS D CD2 1 
ATOM   11204 C CE1 . HIS D 2 301 ? 33.715  -56.848 8.658   1.00 70.79  ? 301 HIS D CE1 1 
ATOM   11205 N NE2 . HIS D 2 301 ? 34.446  -56.215 7.758   1.00 71.17  ? 301 HIS D NE2 1 
ATOM   11206 N N   . ALA D 2 302 ? 37.304  -52.059 12.279  1.00 70.27  ? 302 ALA D N   1 
ATOM   11207 C CA  . ALA D 2 302 ? 37.537  -51.123 13.369  1.00 73.20  ? 302 ALA D CA  1 
ATOM   11208 C C   . ALA D 2 302 ? 37.800  -49.722 12.827  1.00 73.86  ? 302 ALA D C   1 
ATOM   11209 O O   . ALA D 2 302 ? 38.348  -49.551 11.736  1.00 78.15  ? 302 ALA D O   1 
ATOM   11210 C CB  . ALA D 2 302 ? 38.712  -51.580 14.235  1.00 74.77  ? 302 ALA D CB  1 
ATOM   11211 N N   . CYS D 2 303 ? 37.397  -48.715 13.601  1.00 74.56  ? 303 CYS D N   1 
ATOM   11212 C CA  . CYS D 2 303 ? 37.578  -47.314 13.231  1.00 75.12  ? 303 CYS D CA  1 
ATOM   11213 C C   . CYS D 2 303 ? 38.300  -46.597 14.366  1.00 77.05  ? 303 CYS D C   1 
ATOM   11214 O O   . CYS D 2 303 ? 37.700  -46.313 15.409  1.00 78.31  ? 303 CYS D O   1 
ATOM   11215 C CB  . CYS D 2 303 ? 36.240  -46.638 12.929  1.00 75.67  ? 303 CYS D CB  1 
ATOM   11216 S SG  . CYS D 2 303 ? 36.377  -44.879 12.527  1.00 74.27  ? 303 CYS D SG  1 
ATOM   11217 N N   . ILE D 2 304 ? 39.584  -46.308 14.168  1.00 82.74  ? 304 ILE D N   1 
ATOM   11218 C CA  . ILE D 2 304 ? 40.405  -45.635 15.166  1.00 77.85  ? 304 ILE D CA  1 
ATOM   11219 C C   . ILE D 2 304 ? 40.820  -44.283 14.611  1.00 78.69  ? 304 ILE D C   1 
ATOM   11220 O O   . ILE D 2 304 ? 41.364  -44.200 13.505  1.00 82.13  ? 304 ILE D O   1 
ATOM   11221 C CB  . ILE D 2 304 ? 41.638  -46.469 15.556  1.00 77.93  ? 304 ILE D CB  1 
ATOM   11222 C CG1 . ILE D 2 304 ? 41.204  -47.833 16.091  1.00 83.20  ? 304 ILE D CG1 1 
ATOM   11223 C CG2 . ILE D 2 304 ? 42.477  -45.720 16.582  1.00 83.33  ? 304 ILE D CG2 1 
ATOM   11224 C CD1 . ILE D 2 304 ? 42.312  -48.597 16.750  1.00 89.55  ? 304 ILE D CD1 1 
ATOM   11225 N N   . SER D 2 305 ? 40.555  -43.226 15.371  1.00 79.80  ? 305 SER D N   1 
ATOM   11226 C CA  . SER D 2 305 ? 40.906  -41.873 14.964  1.00 81.63  ? 305 SER D CA  1 
ATOM   11227 C C   . SER D 2 305 ? 41.542  -41.148 16.134  1.00 84.65  ? 305 SER D C   1 
ATOM   11228 O O   . SER D 2 305 ? 40.968  -41.123 17.225  1.00 89.87  ? 305 SER D O   1 
ATOM   11229 C CB  . SER D 2 305 ? 39.679  -41.095 14.487  1.00 86.58  ? 305 SER D CB  1 
ATOM   11230 O OG  . SER D 2 305 ? 38.545  -41.406 15.278  1.00 86.23  ? 305 SER D OG  1 
ATOM   11231 N N   . SER D 2 306 ? 42.693  -40.523 15.888  1.00 87.62  ? 306 SER D N   1 
ATOM   11232 C CA  . SER D 2 306 ? 43.398  -39.671 16.853  1.00 93.58  ? 306 SER D CA  1 
ATOM   11233 C C   . SER D 2 306 ? 43.508  -40.338 18.225  1.00 94.57  ? 306 SER D C   1 
ATOM   11234 O O   . SER D 2 306 ? 42.983  -39.858 19.231  1.00 93.82  ? 306 SER D O   1 
ATOM   11235 C CB  . SER D 2 306 ? 42.732  -38.294 16.966  1.00 94.66  ? 306 SER D CB  1 
ATOM   11236 O OG  . SER D 2 306 ? 41.375  -38.401 17.352  1.00 100.79 ? 306 SER D OG  1 
ATOM   11237 N N   . SER D 2 307 ? 44.217  -41.463 18.248  1.00 96.80  ? 307 SER D N   1 
ATOM   11238 C CA  . SER D 2 307 ? 44.390  -42.246 19.461  1.00 95.55  ? 307 SER D CA  1 
ATOM   11239 C C   . SER D 2 307 ? 45.795  -42.834 19.479  1.00 103.80 ? 307 SER D C   1 
ATOM   11240 O O   . SER D 2 307 ? 46.568  -42.684 18.529  1.00 99.26  ? 307 SER D O   1 
ATOM   11241 C CB  . SER D 2 307 ? 43.324  -43.340 19.565  1.00 92.65  ? 307 SER D CB  1 
ATOM   11242 O OG  . SER D 2 307 ? 42.035  -42.772 19.721  1.00 93.21  ? 307 SER D OG  1 
ATOM   11243 N N   . ILE D 2 308 ? 46.119  -43.520 20.572  1.00 127.03 ? 308 ILE D N   1 
ATOM   11244 C CA  . ILE D 2 308 ? 47.435  -44.110 20.783  1.00 127.47 ? 308 ILE D CA  1 
ATOM   11245 C C   . ILE D 2 308 ? 47.240  -45.553 21.223  1.00 128.85 ? 308 ILE D C   1 
ATOM   11246 O O   . ILE D 2 308 ? 46.569  -45.813 22.229  1.00 129.82 ? 308 ILE D O   1 
ATOM   11247 C CB  . ILE D 2 308 ? 48.257  -43.338 21.826  1.00 127.55 ? 308 ILE D CB  1 
ATOM   11248 C CG1 . ILE D 2 308 ? 48.443  -41.884 21.390  1.00 126.51 ? 308 ILE D CG1 1 
ATOM   11249 C CG2 . ILE D 2 308 ? 49.604  -44.009 22.027  1.00 128.28 ? 308 ILE D CG2 1 
ATOM   11250 C CD1 . ILE D 2 308 ? 49.348  -41.726 20.196  1.00 125.69 ? 308 ILE D CD1 1 
ATOM   11251 N N   . ILE D 2 309 ? 47.827  -46.487 20.478  1.00 106.39 ? 309 ILE D N   1 
ATOM   11252 C CA  . ILE D 2 309 ? 47.679  -47.917 20.723  1.00 100.83 ? 309 ILE D CA  1 
ATOM   11253 C C   . ILE D 2 309 ? 48.971  -48.444 21.332  1.00 100.60 ? 309 ILE D C   1 
ATOM   11254 O O   . ILE D 2 309 ? 50.060  -48.204 20.796  1.00 99.17  ? 309 ILE D O   1 
ATOM   11255 C CB  . ILE D 2 309 ? 47.338  -48.673 19.428  1.00 96.70  ? 309 ILE D CB  1 
ATOM   11256 C CG1 . ILE D 2 309 ? 46.253  -47.931 18.645  1.00 97.95  ? 309 ILE D CG1 1 
ATOM   11257 C CG2 . ILE D 2 309 ? 46.874  -50.076 19.751  1.00 97.50  ? 309 ILE D CG2 1 
ATOM   11258 C CD1 . ILE D 2 309 ? 44.953  -47.765 19.398  1.00 99.13  ? 309 ILE D CD1 1 
ATOM   11259 N N   . GLY D 2 310 ? 48.849  -49.166 22.447  1.00 100.37 ? 310 GLY D N   1 
ATOM   11260 C CA  . GLY D 2 310 ? 50.002  -49.704 23.137  1.00 101.22 ? 310 GLY D CA  1 
ATOM   11261 C C   . GLY D 2 310 ? 50.573  -50.944 22.472  1.00 105.45 ? 310 GLY D C   1 
ATOM   11262 O O   . GLY D 2 310 ? 50.143  -51.380 21.404  1.00 104.11 ? 310 GLY D O   1 
ATOM   11263 N N   . TRP D 2 311 ? 51.573  -51.520 23.136  1.00 122.34 ? 311 TRP D N   1 
ATOM   11264 C CA  . TRP D 2 311 ? 52.254  -52.698 22.617  1.00 123.01 ? 311 TRP D CA  1 
ATOM   11265 C C   . TRP D 2 311 ? 51.433  -53.958 22.863  1.00 124.43 ? 311 TRP D C   1 
ATOM   11266 O O   . TRP D 2 311 ? 50.870  -54.148 23.946  1.00 125.59 ? 311 TRP D O   1 
ATOM   11267 C CB  . TRP D 2 311 ? 53.633  -52.844 23.264  1.00 123.43 ? 311 TRP D CB  1 
ATOM   11268 C CG  . TRP D 2 311 ? 54.537  -51.668 23.032  1.00 125.00 ? 311 TRP D CG  1 
ATOM   11269 C CD1 . TRP D 2 311 ? 55.220  -51.369 21.889  1.00 121.05 ? 311 TRP D CD1 1 
ATOM   11270 C CD2 . TRP D 2 311 ? 54.865  -50.640 23.975  1.00 132.04 ? 311 TRP D CD2 1 
ATOM   11271 N NE1 . TRP D 2 311 ? 55.947  -50.216 22.059  1.00 122.01 ? 311 TRP D NE1 1 
ATOM   11272 C CE2 . TRP D 2 311 ? 55.747  -49.749 23.332  1.00 129.86 ? 311 TRP D CE2 1 
ATOM   11273 C CE3 . TRP D 2 311 ? 54.496  -50.385 25.300  1.00 129.03 ? 311 TRP D CE3 1 
ATOM   11274 C CZ2 . TRP D 2 311 ? 56.265  -48.623 23.967  1.00 127.28 ? 311 TRP D CZ2 1 
ATOM   11275 C CZ3 . TRP D 2 311 ? 55.012  -49.266 25.929  1.00 131.44 ? 311 TRP D CZ3 1 
ATOM   11276 C CH2 . TRP D 2 311 ? 55.887  -48.400 25.262  1.00 130.42 ? 311 TRP D CH2 1 
ATOM   11277 N N   . HIS D 2 312 ? 51.382  -54.824 21.847  1.00 105.50 ? 312 HIS D N   1 
ATOM   11278 C CA  . HIS D 2 312 ? 50.799  -56.165 21.962  1.00 100.61 ? 312 HIS D CA  1 
ATOM   11279 C C   . HIS D 2 312 ? 49.367  -56.117 22.494  1.00 97.35  ? 312 HIS D C   1 
ATOM   11280 O O   . HIS D 2 312 ? 48.935  -56.981 23.260  1.00 92.81  ? 312 HIS D O   1 
ATOM   11281 C CB  . HIS D 2 312 ? 51.674  -57.076 22.826  1.00 104.91 ? 312 HIS D CB  1 
ATOM   11282 C CG  . HIS D 2 312 ? 53.087  -57.194 22.342  1.00 107.00 ? 312 HIS D CG  1 
ATOM   11283 N ND1 . HIS D 2 312 ? 54.101  -56.373 22.787  1.00 110.31 ? 312 HIS D ND1 1 
ATOM   11284 C CD2 . HIS D 2 312 ? 53.655  -58.043 21.452  1.00 105.88 ? 312 HIS D CD2 1 
ATOM   11285 C CE1 . HIS D 2 312 ? 55.232  -56.710 22.192  1.00 110.59 ? 312 HIS D CE1 1 
ATOM   11286 N NE2 . HIS D 2 312 ? 54.989  -57.721 21.377  1.00 107.75 ? 312 HIS D NE2 1 
ATOM   11287 N N   . SER D 2 313 ? 48.625  -55.095 22.084  1.00 96.14  ? 313 SER D N   1 
ATOM   11288 C CA  . SER D 2 313 ? 47.226  -54.966 22.457  1.00 89.29  ? 313 SER D CA  1 
ATOM   11289 C C   . SER D 2 313 ? 46.366  -55.655 21.401  1.00 87.35  ? 313 SER D C   1 
ATOM   11290 O O   . SER D 2 313 ? 46.872  -56.313 20.488  1.00 88.62  ? 313 SER D O   1 
ATOM   11291 C CB  . SER D 2 313 ? 46.860  -53.494 22.632  1.00 89.18  ? 313 SER D CB  1 
ATOM   11292 O OG  . SER D 2 313 ? 47.585  -52.919 23.704  1.00 94.79  ? 313 SER D OG  1 
ATOM   11293 N N   . THR D 2 314 ? 45.048  -55.520 21.517  1.00 85.86  ? 314 THR D N   1 
ATOM   11294 C CA  . THR D 2 314 ? 44.141  -56.165 20.575  1.00 84.47  ? 314 THR D CA  1 
ATOM   11295 C C   . THR D 2 314 ? 42.838  -55.386 20.528  1.00 84.12  ? 314 THR D C   1 
ATOM   11296 O O   . THR D 2 314 ? 42.134  -55.290 21.538  1.00 81.10  ? 314 THR D O   1 
ATOM   11297 C CB  . THR D 2 314 ? 43.879  -57.621 20.963  1.00 86.74  ? 314 THR D CB  1 
ATOM   11298 O OG1 . THR D 2 314 ? 45.086  -58.381 20.824  1.00 85.53  ? 314 THR D OG1 1 
ATOM   11299 C CG2 . THR D 2 314 ? 42.802  -58.218 20.071  1.00 90.01  ? 314 THR D CG2 1 
ATOM   11300 N N   . VAL D 2 315 ? 42.523  -54.836 19.360  1.00 84.83  ? 315 VAL D N   1 
ATOM   11301 C CA  . VAL D 2 315 ? 41.268  -54.131 19.130  1.00 87.06  ? 315 VAL D CA  1 
ATOM   11302 C C   . VAL D 2 315 ? 40.310  -55.091 18.443  1.00 89.02  ? 315 VAL D C   1 
ATOM   11303 O O   . VAL D 2 315 ? 40.598  -55.590 17.349  1.00 91.58  ? 315 VAL D O   1 
ATOM   11304 C CB  . VAL D 2 315 ? 41.477  -52.867 18.283  1.00 88.23  ? 315 VAL D CB  1 
ATOM   11305 C CG1 . VAL D 2 315 ? 40.135  -52.228 17.967  1.00 84.12  ? 315 VAL D CG1 1 
ATOM   11306 C CG2 . VAL D 2 315 ? 42.386  -51.887 19.006  1.00 93.61  ? 315 VAL D CG2 1 
ATOM   11307 N N   . GLY D 2 316 ? 39.172  -55.348 19.079  1.00 95.75  ? 316 GLY D N   1 
ATOM   11308 C CA  . GLY D 2 316 ? 38.191  -56.262 18.539  1.00 96.45  ? 316 GLY D CA  1 
ATOM   11309 C C   . GLY D 2 316 ? 37.540  -55.741 17.267  1.00 94.81  ? 316 GLY D C   1 
ATOM   11310 O O   . GLY D 2 316 ? 37.762  -54.616 16.816  1.00 92.90  ? 316 GLY D O   1 
ATOM   11311 N N   . GLN D 2 317 ? 36.715  -56.601 16.674  1.00 82.68  ? 317 GLN D N   1 
ATOM   11312 C CA  . GLN D 2 317 ? 36.018  -56.237 15.449  1.00 79.39  ? 317 GLN D CA  1 
ATOM   11313 C C   . GLN D 2 317 ? 34.944  -55.191 15.725  1.00 78.96  ? 317 GLN D C   1 
ATOM   11314 O O   . GLN D 2 317 ? 34.334  -55.156 16.798  1.00 79.51  ? 317 GLN D O   1 
ATOM   11315 C CB  . GLN D 2 317 ? 35.390  -57.468 14.790  1.00 77.55  ? 317 GLN D CB  1 
ATOM   11316 C CG  . GLN D 2 317 ? 36.387  -58.510 14.310  1.00 82.96  ? 317 GLN D CG  1 
ATOM   11317 C CD  . GLN D 2 317 ? 35.717  -59.723 13.693  1.00 84.71  ? 317 GLN D CD  1 
ATOM   11318 O OE1 . GLN D 2 317 ? 34.492  -59.785 13.589  1.00 79.80  ? 317 GLN D OE1 1 
ATOM   11319 N NE2 . GLN D 2 317 ? 36.520  -60.694 13.276  1.00 95.10  ? 317 GLN D NE2 1 
ATOM   11320 N N   . TRP D 2 318 ? 34.721  -54.326 14.734  1.00 75.21  ? 318 TRP D N   1 
ATOM   11321 C CA  . TRP D 2 318 ? 33.700  -53.280 14.769  1.00 73.16  ? 318 TRP D CA  1 
ATOM   11322 C C   . TRP D 2 318 ? 33.872  -52.320 15.945  1.00 71.39  ? 318 TRP D C   1 
ATOM   11323 O O   . TRP D 2 318 ? 32.936  -51.592 16.295  1.00 74.74  ? 318 TRP D O   1 
ATOM   11324 C CB  . TRP D 2 318 ? 32.287  -53.879 14.785  1.00 72.87  ? 318 TRP D CB  1 
ATOM   11325 C CG  . TRP D 2 318 ? 31.883  -54.527 13.490  1.00 69.37  ? 318 TRP D CG  1 
ATOM   11326 C CD1 . TRP D 2 318 ? 31.527  -53.893 12.335  1.00 69.90  ? 318 TRP D CD1 1 
ATOM   11327 C CD2 . TRP D 2 318 ? 31.754  -55.932 13.231  1.00 69.25  ? 318 TRP D CD2 1 
ATOM   11328 N NE1 . TRP D 2 318 ? 31.206  -54.814 11.367  1.00 68.77  ? 318 TRP D NE1 1 
ATOM   11329 C CE2 . TRP D 2 318 ? 31.334  -56.072 11.893  1.00 69.18  ? 318 TRP D CE2 1 
ATOM   11330 C CE3 . TRP D 2 318 ? 31.959  -57.083 13.998  1.00 69.90  ? 318 TRP D CE3 1 
ATOM   11331 C CZ2 . TRP D 2 318 ? 31.117  -57.318 11.305  1.00 69.92  ? 318 TRP D CZ2 1 
ATOM   11332 C CZ3 . TRP D 2 318 ? 31.743  -58.318 13.411  1.00 71.06  ? 318 TRP D CZ3 1 
ATOM   11333 C CH2 . TRP D 2 318 ? 31.327  -58.426 12.079  1.00 70.54  ? 318 TRP D CH2 1 
ATOM   11334 N N   . ALA D 2 319 ? 35.044  -52.302 16.574  1.00 72.65  ? 319 ALA D N   1 
ATOM   11335 C CA  . ALA D 2 319 ? 35.293  -51.400 17.690  1.00 74.66  ? 319 ALA D CA  1 
ATOM   11336 C C   . ALA D 2 319 ? 35.681  -50.015 17.187  1.00 74.19  ? 319 ALA D C   1 
ATOM   11337 O O   . ALA D 2 319 ? 36.431  -49.879 16.217  1.00 73.30  ? 319 ALA D O   1 
ATOM   11338 C CB  . ALA D 2 319 ? 36.394  -51.961 18.590  1.00 74.35  ? 319 ALA D CB  1 
ATOM   11339 N N   . ARG D 2 320 ? 35.167  -48.983 17.852  1.00 80.90  ? 320 ARG D N   1 
ATOM   11340 C CA  . ARG D 2 320 ? 35.438  -47.597 17.493  1.00 82.25  ? 320 ARG D CA  1 
ATOM   11341 C C   . ARG D 2 320 ? 36.278  -46.929 18.573  1.00 82.46  ? 320 ARG D C   1 
ATOM   11342 O O   . ARG D 2 320 ? 35.908  -46.940 19.751  1.00 81.82  ? 320 ARG D O   1 
ATOM   11343 C CB  . ARG D 2 320 ? 34.142  -46.811 17.277  1.00 83.70  ? 320 ARG D CB  1 
ATOM   11344 C CG  . ARG D 2 320 ? 34.373  -45.355 16.884  1.00 86.62  ? 320 ARG D CG  1 
ATOM   11345 C CD  . ARG D 2 320 ? 33.064  -44.603 16.701  1.00 84.03  ? 320 ARG D CD  1 
ATOM   11346 N NE  . ARG D 2 320 ? 33.274  -43.208 16.321  1.00 86.15  ? 320 ARG D NE  1 
ATOM   11347 C CZ  . ARG D 2 320 ? 33.298  -42.770 15.066  1.00 88.13  ? 320 ARG D CZ  1 
ATOM   11348 N NH1 . ARG D 2 320 ? 33.123  -43.617 14.062  1.00 87.13  ? 320 ARG D NH1 1 
ATOM   11349 N NH2 . ARG D 2 320 ? 33.495  -41.482 14.816  1.00 91.81  ? 320 ARG D NH2 1 
ATOM   11350 N N   . ILE D 2 321 ? 37.400  -46.343 18.162  1.00 79.77  ? 321 ILE D N   1 
ATOM   11351 C CA  . ILE D 2 321 ? 38.336  -45.675 19.058  1.00 81.88  ? 321 ILE D CA  1 
ATOM   11352 C C   . ILE D 2 321 ? 38.532  -44.254 18.549  1.00 83.13  ? 321 ILE D C   1 
ATOM   11353 O O   . ILE D 2 321 ? 38.855  -44.052 17.373  1.00 84.49  ? 321 ILE D O   1 
ATOM   11354 C CB  . ILE D 2 321 ? 39.681  -46.422 19.137  1.00 82.80  ? 321 ILE D CB  1 
ATOM   11355 C CG1 . ILE D 2 321 ? 39.469  -47.885 19.523  1.00 81.49  ? 321 ILE D CG1 1 
ATOM   11356 C CG2 . ILE D 2 321 ? 40.611  -45.735 20.119  1.00 83.59  ? 321 ILE D CG2 1 
ATOM   11357 C CD1 . ILE D 2 321 ? 38.852  -48.067 20.897  1.00 83.82  ? 321 ILE D CD1 1 
ATOM   11358 N N   . GLU D 2 322 ? 38.326  -43.271 19.422  1.00 87.66  ? 322 GLU D N   1 
ATOM   11359 C CA  . GLU D 2 322 ? 38.444  -41.878 19.010  1.00 89.41  ? 322 GLU D CA  1 
ATOM   11360 C C   . GLU D 2 322 ? 38.731  -41.005 20.224  1.00 95.73  ? 322 GLU D C   1 
ATOM   11361 O O   . GLU D 2 322 ? 38.671  -41.455 21.372  1.00 95.06  ? 322 GLU D O   1 
ATOM   11362 C CB  . GLU D 2 322 ? 37.177  -41.412 18.289  1.00 92.99  ? 322 GLU D CB  1 
ATOM   11363 C CG  . GLU D 2 322 ? 35.948  -41.360 19.182  1.00 91.79  ? 322 GLU D CG  1 
ATOM   11364 C CD  . GLU D 2 322 ? 34.721  -40.835 18.464  1.00 94.87  ? 322 GLU D CD  1 
ATOM   11365 O OE1 . GLU D 2 322 ? 34.797  -40.597 17.240  1.00 98.34  ? 322 GLU D OE1 1 
ATOM   11366 O OE2 . GLU D 2 322 ? 33.680  -40.647 19.127  1.00 91.32  ? 322 GLU D OE2 1 
ATOM   11367 N N   . ASN D 2 323 ? 39.062  -39.743 19.941  1.00 113.03 ? 323 ASN D N   1 
ATOM   11368 C CA  . ASN D 2 323 ? 39.152  -38.681 20.945  1.00 113.34 ? 323 ASN D CA  1 
ATOM   11369 C C   . ASN D 2 323 ? 40.238  -38.974 21.983  1.00 113.95 ? 323 ASN D C   1 
ATOM   11370 O O   . ASN D 2 323 ? 39.981  -39.059 23.183  1.00 114.95 ? 323 ASN D O   1 
ATOM   11371 C CB  . ASN D 2 323 ? 37.791  -38.465 21.616  1.00 113.65 ? 323 ASN D CB  1 
ATOM   11372 C CG  . ASN D 2 323 ? 37.769  -37.245 22.519  1.00 113.80 ? 323 ASN D CG  1 
ATOM   11373 O OD1 . ASN D 2 323 ? 38.603  -36.349 22.395  1.00 118.25 ? 323 ASN D OD1 1 
ATOM   11374 N ND2 . ASN D 2 323 ? 36.815  -37.212 23.443  1.00 114.37 ? 323 ASN D ND2 1 
ATOM   11375 N N   . MET D 2 324 ? 41.473  -39.089 21.495  1.00 96.38  ? 324 MET D N   1 
ATOM   11376 C CA  . MET D 2 324 ? 42.653  -39.211 22.350  1.00 92.05  ? 324 MET D CA  1 
ATOM   11377 C C   . MET D 2 324 ? 42.499  -40.355 23.347  1.00 87.92  ? 324 MET D C   1 
ATOM   11378 O O   . MET D 2 324 ? 42.764  -40.215 24.543  1.00 86.01  ? 324 MET D O   1 
ATOM   11379 C CB  . MET D 2 324 ? 42.942  -37.901 23.082  1.00 94.46  ? 324 MET D CB  1 
ATOM   11380 C CG  . MET D 2 324 ? 43.167  -36.712 22.182  1.00 98.01  ? 324 MET D CG  1 
ATOM   11381 S SD  . MET D 2 324 ? 43.247  -35.188 23.141  1.00 99.95  ? 324 MET D SD  1 
ATOM   11382 C CE  . MET D 2 324 ? 41.644  -35.198 23.947  1.00 101.88 ? 324 MET D CE  1 
ATOM   11383 N N   . THR D 2 325 ? 42.065  -41.504 22.843  1.00 85.59  ? 325 THR D N   1 
ATOM   11384 C CA  . THR D 2 325 ? 41.946  -42.683 23.686  1.00 79.86  ? 325 THR D CA  1 
ATOM   11385 C C   . THR D 2 325 ? 43.327  -43.297 23.848  1.00 85.15  ? 325 THR D C   1 
ATOM   11386 O O   . THR D 2 325 ? 43.977  -43.646 22.858  1.00 90.31  ? 325 THR D O   1 
ATOM   11387 C CB  . THR D 2 325 ? 40.973  -43.688 23.076  1.00 76.94  ? 325 THR D CB  1 
ATOM   11388 O OG1 . THR D 2 325 ? 39.717  -43.048 22.821  1.00 83.34  ? 325 THR D OG1 1 
ATOM   11389 C CG2 . THR D 2 325 ? 40.759  -44.854 24.022  1.00 73.65  ? 325 THR D CG2 1 
ATOM   11390 N N   . ILE D 2 326 ? 43.764  -43.446 25.094  1.00 88.57  ? 326 ILE D N   1 
ATOM   11391 C CA  . ILE D 2 326 ? 45.117  -43.884 25.413  1.00 89.69  ? 326 ILE D CA  1 
ATOM   11392 C C   . ILE D 2 326 ? 45.035  -45.284 26.002  1.00 92.49  ? 326 ILE D C   1 
ATOM   11393 O O   . ILE D 2 326 ? 44.402  -45.492 27.044  1.00 89.11  ? 326 ILE D O   1 
ATOM   11394 C CB  . ILE D 2 326 ? 45.806  -42.917 26.386  1.00 83.83  ? 326 ILE D CB  1 
ATOM   11395 C CG1 . ILE D 2 326 ? 45.693  -41.480 25.869  1.00 85.57  ? 326 ILE D CG1 1 
ATOM   11396 C CG2 . ILE D 2 326 ? 47.262  -43.307 26.581  1.00 89.87  ? 326 ILE D CG2 1 
ATOM   11397 C CD1 . ILE D 2 326 ? 46.347  -41.268 24.526  1.00 91.84  ? 326 ILE D CD1 1 
ATOM   11398 N N   . LEU D 2 327 ? 45.682  -46.240 25.343  1.00 104.00 ? 327 LEU D N   1 
ATOM   11399 C CA  . LEU D 2 327 ? 45.677  -47.630 25.773  1.00 106.62 ? 327 LEU D CA  1 
ATOM   11400 C C   . LEU D 2 327 ? 47.073  -48.047 26.218  1.00 107.01 ? 327 LEU D C   1 
ATOM   11401 O O   . LEU D 2 327 ? 48.072  -47.664 25.601  1.00 105.02 ? 327 LEU D O   1 
ATOM   11402 C CB  . LEU D 2 327 ? 45.194  -48.550 24.647  1.00 105.51 ? 327 LEU D CB  1 
ATOM   11403 C CG  . LEU D 2 327 ? 43.773  -48.317 24.124  1.00 105.16 ? 327 LEU D CG  1 
ATOM   11404 C CD1 . LEU D 2 327 ? 43.378  -49.408 23.141  1.00 105.44 ? 327 LEU D CD1 1 
ATOM   11405 C CD2 . LEU D 2 327 ? 42.778  -48.235 25.268  1.00 106.39 ? 327 LEU D CD2 1 
ATOM   11406 N N   . GLY D 2 328 ? 47.133  -48.826 27.294  1.00 95.21  ? 328 GLY D N   1 
ATOM   11407 C CA  . GLY D 2 328 ? 48.383  -49.361 27.787  1.00 91.65  ? 328 GLY D CA  1 
ATOM   11408 C C   . GLY D 2 328 ? 48.789  -50.630 27.058  1.00 90.45  ? 328 GLY D C   1 
ATOM   11409 O O   . GLY D 2 328 ? 48.171  -51.063 26.084  1.00 92.54  ? 328 GLY D O   1 
ATOM   11410 N N   . GLU D 2 329 ? 49.867  -51.231 27.553  1.00 91.66  ? 329 GLU D N   1 
ATOM   11411 C CA  . GLU D 2 329 ? 50.367  -52.472 26.978  1.00 92.60  ? 329 GLU D CA  1 
ATOM   11412 C C   . GLU D 2 329 ? 49.434  -53.631 27.303  1.00 85.59  ? 329 GLU D C   1 
ATOM   11413 O O   . GLU D 2 329 ? 48.969  -53.774 28.435  1.00 85.87  ? 329 GLU D O   1 
ATOM   11414 C CB  . GLU D 2 329 ? 51.770  -52.766 27.508  1.00 98.85  ? 329 GLU D CB  1 
ATOM   11415 C CG  . GLU D 2 329 ? 52.330  -54.112 27.089  1.00 99.74  ? 329 GLU D CG  1 
ATOM   11416 C CD  . GLU D 2 329 ? 53.664  -54.409 27.741  1.00 95.89  ? 329 GLU D CD  1 
ATOM   11417 O OE1 . GLU D 2 329 ? 54.208  -53.511 28.417  1.00 103.43 ? 329 GLU D OE1 1 
ATOM   11418 O OE2 . GLU D 2 329 ? 54.163  -55.543 27.586  1.00 93.38  ? 329 GLU D OE2 1 
ATOM   11419 N N   . ASP D 2 330 ? 49.167  -54.466 26.299  1.00 86.64  ? 330 ASP D N   1 
ATOM   11420 C CA  . ASP D 2 330 ? 48.353  -55.671 26.464  1.00 86.22  ? 330 ASP D CA  1 
ATOM   11421 C C   . ASP D 2 330 ? 46.962  -55.327 27.007  1.00 84.29  ? 330 ASP D C   1 
ATOM   11422 O O   . ASP D 2 330 ? 46.559  -55.747 28.092  1.00 84.02  ? 330 ASP D O   1 
ATOM   11423 C CB  . ASP D 2 330 ? 49.068  -56.689 27.362  1.00 85.07  ? 330 ASP D CB  1 
ATOM   11424 C CG  . ASP D 2 330 ? 48.276  -57.971 27.543  1.00 87.26  ? 330 ASP D CG  1 
ATOM   11425 O OD1 . ASP D 2 330 ? 48.123  -58.722 26.558  1.00 95.72  ? 330 ASP D OD1 1 
ATOM   11426 O OD2 . ASP D 2 330 ? 47.807  -58.225 28.674  1.00 83.82  ? 330 ASP D OD2 1 
ATOM   11427 N N   . VAL D 2 331 ? 46.227  -54.547 26.221  1.00 84.24  ? 331 VAL D N   1 
ATOM   11428 C CA  . VAL D 2 331 ? 44.849  -54.194 26.533  1.00 82.98  ? 331 VAL D CA  1 
ATOM   11429 C C   . VAL D 2 331 ? 43.960  -54.791 25.455  1.00 83.91  ? 331 VAL D C   1 
ATOM   11430 O O   . VAL D 2 331 ? 44.171  -54.546 24.262  1.00 85.00  ? 331 VAL D O   1 
ATOM   11431 C CB  . VAL D 2 331 ? 44.650  -52.670 26.630  1.00 83.16  ? 331 VAL D CB  1 
ATOM   11432 C CG1 . VAL D 2 331 ? 43.181  -52.341 26.860  1.00 80.16  ? 331 VAL D CG1 1 
ATOM   11433 C CG2 . VAL D 2 331 ? 45.503  -52.094 27.748  1.00 87.29  ? 331 VAL D CG2 1 
ATOM   11434 N N   . HIS D 2 332 ? 42.968  -55.570 25.874  1.00 82.85  ? 332 HIS D N   1 
ATOM   11435 C CA  . HIS D 2 332 ? 42.110  -56.312 24.959  1.00 84.84  ? 332 HIS D CA  1 
ATOM   11436 C C   . HIS D 2 332 ? 40.738  -55.655 24.935  1.00 83.01  ? 332 HIS D C   1 
ATOM   11437 O O   . HIS D 2 332 ? 39.953  -55.796 25.880  1.00 79.97  ? 332 HIS D O   1 
ATOM   11438 C CB  . HIS D 2 332 ? 42.024  -57.780 25.363  1.00 87.02  ? 332 HIS D CB  1 
ATOM   11439 C CG  . HIS D 2 332 ? 43.336  -58.493 25.294  1.00 86.29  ? 332 HIS D CG  1 
ATOM   11440 N ND1 . HIS D 2 332 ? 43.684  -59.313 24.242  1.00 89.09  ? 332 HIS D ND1 1 
ATOM   11441 C CD2 . HIS D 2 332 ? 44.397  -58.490 26.135  1.00 86.99  ? 332 HIS D CD2 1 
ATOM   11442 C CE1 . HIS D 2 332 ? 44.897  -59.795 24.445  1.00 89.46  ? 332 HIS D CE1 1 
ATOM   11443 N NE2 . HIS D 2 332 ? 45.352  -59.310 25.587  1.00 90.31  ? 332 HIS D NE2 1 
ATOM   11444 N N   . VAL D 2 333 ? 40.458  -54.943 23.849  1.00 80.61  ? 333 VAL D N   1 
ATOM   11445 C CA  . VAL D 2 333 ? 39.169  -54.301 23.641  1.00 79.48  ? 333 VAL D CA  1 
ATOM   11446 C C   . VAL D 2 333 ? 38.256  -55.306 22.955  1.00 80.58  ? 333 VAL D C   1 
ATOM   11447 O O   . VAL D 2 333 ? 38.591  -55.835 21.889  1.00 83.00  ? 333 VAL D O   1 
ATOM   11448 C CB  . VAL D 2 333 ? 39.312  -53.024 22.799  1.00 77.89  ? 333 VAL D CB  1 
ATOM   11449 C CG1 . VAL D 2 333 ? 37.959  -52.360 22.615  1.00 78.64  ? 333 VAL D CG1 1 
ATOM   11450 C CG2 . VAL D 2 333 ? 40.310  -52.072 23.436  1.00 81.05  ? 333 VAL D CG2 1 
ATOM   11451 N N   . SER D 2 334 ? 37.109  -55.580 23.568  1.00 79.67  ? 334 SER D N   1 
ATOM   11452 C CA  . SER D 2 334 ? 36.166  -56.512 22.978  1.00 84.11  ? 334 SER D CA  1 
ATOM   11453 C C   . SER D 2 334 ? 35.595  -55.939 21.683  1.00 81.69  ? 334 SER D C   1 
ATOM   11454 O O   . SER D 2 334 ? 35.832  -54.784 21.317  1.00 77.97  ? 334 SER D O   1 
ATOM   11455 C CB  . SER D 2 334 ? 35.036  -56.828 23.957  1.00 87.62  ? 334 SER D CB  1 
ATOM   11456 O OG  . SER D 2 334 ? 35.541  -57.425 25.135  1.00 87.18  ? 334 SER D OG  1 
ATOM   11457 N N   . ASP D 2 335 ? 34.825  -56.764 20.984  1.00 82.38  ? 335 ASP D N   1 
ATOM   11458 C CA  . ASP D 2 335 ? 34.170  -56.294 19.777  1.00 75.30  ? 335 ASP D CA  1 
ATOM   11459 C C   . ASP D 2 335 ? 33.073  -55.304 20.142  1.00 74.20  ? 335 ASP D C   1 
ATOM   11460 O O   . ASP D 2 335 ? 32.518  -55.336 21.245  1.00 76.22  ? 335 ASP D O   1 
ATOM   11461 C CB  . ASP D 2 335 ? 33.574  -57.460 18.986  1.00 79.06  ? 335 ASP D CB  1 
ATOM   11462 C CG  . ASP D 2 335 ? 34.596  -58.530 18.663  1.00 84.98  ? 335 ASP D CG  1 
ATOM   11463 O OD1 . ASP D 2 335 ? 35.797  -58.209 18.601  1.00 88.35  ? 335 ASP D OD1 1 
ATOM   11464 O OD2 . ASP D 2 335 ? 34.192  -59.695 18.460  1.00 88.81  ? 335 ASP D OD2 1 
ATOM   11465 N N   . GLU D 2 336 ? 32.775  -54.404 19.204  1.00 73.53  ? 336 GLU D N   1 
ATOM   11466 C CA  . GLU D 2 336 ? 31.642  -53.481 19.301  1.00 71.98  ? 336 GLU D CA  1 
ATOM   11467 C C   . GLU D 2 336 ? 31.758  -52.520 20.483  1.00 72.22  ? 336 GLU D C   1 
ATOM   11468 O O   . GLU D 2 336 ? 30.746  -52.020 20.979  1.00 72.06  ? 336 GLU D O   1 
ATOM   11469 C CB  . GLU D 2 336 ? 30.323  -54.260 19.389  1.00 69.01  ? 336 GLU D CB  1 
ATOM   11470 C CG  . GLU D 2 336 ? 30.234  -55.445 18.431  1.00 68.18  ? 336 GLU D CG  1 
ATOM   11471 C CD  . GLU D 2 336 ? 29.171  -56.453 18.831  1.00 68.55  ? 336 GLU D CD  1 
ATOM   11472 O OE1 . GLU D 2 336 ? 28.234  -56.083 19.571  1.00 69.62  ? 336 GLU D OE1 1 
ATOM   11473 O OE2 . GLU D 2 336 ? 29.285  -57.626 18.417  1.00 69.27  ? 336 GLU D OE2 1 
ATOM   11474 N N   . ILE D 2 337 ? 32.978  -52.255 20.953  1.00 71.34  ? 337 ILE D N   1 
ATOM   11475 C CA  . ILE D 2 337 ? 33.210  -51.387 22.103  1.00 70.90  ? 337 ILE D CA  1 
ATOM   11476 C C   . ILE D 2 337 ? 33.604  -50.000 21.616  1.00 70.98  ? 337 ILE D C   1 
ATOM   11477 O O   . ILE D 2 337 ? 34.427  -49.858 20.704  1.00 72.93  ? 337 ILE D O   1 
ATOM   11478 C CB  . ILE D 2 337 ? 34.284  -51.983 23.032  1.00 72.04  ? 337 ILE D CB  1 
ATOM   11479 C CG1 . ILE D 2 337 ? 33.838  -53.356 23.533  1.00 68.62  ? 337 ILE D CG1 1 
ATOM   11480 C CG2 . ILE D 2 337 ? 34.564  -51.057 24.201  1.00 70.76  ? 337 ILE D CG2 1 
ATOM   11481 C CD1 . ILE D 2 337 ? 32.617  -53.306 24.421  1.00 69.80  ? 337 ILE D CD1 1 
ATOM   11482 N N   . TYR D 2 338 ? 33.017  -48.973 22.227  1.00 72.77  ? 338 TYR D N   1 
ATOM   11483 C CA  . TYR D 2 338 ? 33.262  -47.582 21.867  1.00 74.42  ? 338 TYR D CA  1 
ATOM   11484 C C   . TYR D 2 338 ? 34.027  -46.895 22.993  1.00 74.01  ? 338 TYR D C   1 
ATOM   11485 O O   . TYR D 2 338 ? 33.685  -47.056 24.169  1.00 70.95  ? 338 TYR D O   1 
ATOM   11486 C CB  . TYR D 2 338 ? 31.940  -46.860 21.590  1.00 72.45  ? 338 TYR D CB  1 
ATOM   11487 C CG  . TYR D 2 338 ? 32.051  -45.362 21.420  1.00 72.17  ? 338 TYR D CG  1 
ATOM   11488 C CD1 . TYR D 2 338 ? 32.559  -44.815 20.249  1.00 74.58  ? 338 TYR D CD1 1 
ATOM   11489 C CD2 . TYR D 2 338 ? 31.640  -44.495 22.423  1.00 70.81  ? 338 TYR D CD2 1 
ATOM   11490 C CE1 . TYR D 2 338 ? 32.659  -43.446 20.084  1.00 75.03  ? 338 TYR D CE1 1 
ATOM   11491 C CE2 . TYR D 2 338 ? 31.737  -43.125 22.268  1.00 70.66  ? 338 TYR D CE2 1 
ATOM   11492 C CZ  . TYR D 2 338 ? 32.248  -42.606 21.096  1.00 73.70  ? 338 TYR D CZ  1 
ATOM   11493 O OH  . TYR D 2 338 ? 32.348  -41.243 20.933  1.00 77.11  ? 338 TYR D OH  1 
ATOM   11494 N N   . SER D 2 339 ? 35.059  -46.135 22.634  1.00 72.05  ? 339 SER D N   1 
ATOM   11495 C CA  . SER D 2 339 ? 35.887  -45.422 23.602  1.00 71.62  ? 339 SER D CA  1 
ATOM   11496 C C   . SER D 2 339 ? 35.987  -43.961 23.188  1.00 72.34  ? 339 SER D C   1 
ATOM   11497 O O   . SER D 2 339 ? 36.383  -43.659 22.057  1.00 77.19  ? 339 SER D O   1 
ATOM   11498 C CB  . SER D 2 339 ? 37.281  -46.049 23.713  1.00 77.74  ? 339 SER D CB  1 
ATOM   11499 O OG  . SER D 2 339 ? 37.212  -47.346 24.289  1.00 79.78  ? 339 SER D OG  1 
ATOM   11500 N N   . ASN D 2 340 ? 35.624  -43.061 24.103  1.00 80.91  ? 340 ASN D N   1 
ATOM   11501 C CA  . ASN D 2 340 ? 35.682  -41.624 23.858  1.00 84.76  ? 340 ASN D CA  1 
ATOM   11502 C C   . ASN D 2 340 ? 36.699  -40.967 24.779  1.00 88.69  ? 340 ASN D C   1 
ATOM   11503 O O   . ASN D 2 340 ? 36.345  -40.120 25.603  1.00 85.90  ? 340 ASN D O   1 
ATOM   11504 C CB  . ASN D 2 340 ? 34.301  -40.996 24.060  1.00 82.41  ? 340 ASN D CB  1 
ATOM   11505 C CG  . ASN D 2 340 ? 34.221  -39.566 23.559  1.00 86.33  ? 340 ASN D CG  1 
ATOM   11506 O OD1 . ASN D 2 340 ? 34.897  -39.191 22.602  1.00 92.74  ? 340 ASN D OD1 1 
ATOM   11507 N ND2 . ASN D 2 340 ? 33.399  -38.756 24.215  1.00 84.36  ? 340 ASN D ND2 1 
ATOM   11508 N N   . GLY D 2 341 ? 37.964  -41.350 24.648  1.00 84.98  ? 341 GLY D N   1 
ATOM   11509 C CA  . GLY D 2 341 ? 39.006  -40.763 25.467  1.00 88.38  ? 341 GLY D CA  1 
ATOM   11510 C C   . GLY D 2 341 ? 39.307  -41.569 26.712  1.00 81.24  ? 341 GLY D C   1 
ATOM   11511 O O   . GLY D 2 341 ? 39.508  -41.003 27.791  1.00 79.03  ? 341 GLY D O   1 
ATOM   11512 N N   . GLY D 2 342 ? 39.355  -42.890 26.574  1.00 74.67  ? 342 GLY D N   1 
ATOM   11513 C CA  . GLY D 2 342 ? 39.624  -43.730 27.718  1.00 75.83  ? 342 GLY D CA  1 
ATOM   11514 C C   . GLY D 2 342 ? 41.100  -44.014 27.892  1.00 78.56  ? 342 GLY D C   1 
ATOM   11515 O O   . GLY D 2 342 ? 41.693  -44.760 27.107  1.00 79.08  ? 342 GLY D O   1 
ATOM   11516 N N   . VAL D 2 343 ? 41.703  -43.425 28.923  1.00 77.51  ? 343 VAL D N   1 
ATOM   11517 C CA  . VAL D 2 343 ? 43.107  -43.651 29.245  1.00 77.07  ? 343 VAL D CA  1 
ATOM   11518 C C   . VAL D 2 343 ? 43.154  -44.906 30.110  1.00 76.16  ? 343 VAL D C   1 
ATOM   11519 O O   . VAL D 2 343 ? 42.896  -44.857 31.313  1.00 80.02  ? 343 VAL D O   1 
ATOM   11520 C CB  . VAL D 2 343 ? 43.731  -42.444 29.949  1.00 78.26  ? 343 VAL D CB  1 
ATOM   11521 C CG1 . VAL D 2 343 ? 45.235  -42.628 30.094  1.00 78.56  ? 343 VAL D CG1 1 
ATOM   11522 C CG2 . VAL D 2 343 ? 43.415  -41.162 29.188  1.00 82.05  ? 343 VAL D CG2 1 
ATOM   11523 N N   . VAL D 2 344 ? 43.487  -46.035 29.490  1.00 78.43  ? 344 VAL D N   1 
ATOM   11524 C CA  . VAL D 2 344 ? 43.382  -47.344 30.123  1.00 79.24  ? 344 VAL D CA  1 
ATOM   11525 C C   . VAL D 2 344 ? 44.759  -47.809 30.579  1.00 86.89  ? 344 VAL D C   1 
ATOM   11526 O O   . VAL D 2 344 ? 45.780  -47.545 29.932  1.00 88.12  ? 344 VAL D O   1 
ATOM   11527 C CB  . VAL D 2 344 ? 42.733  -48.360 29.158  1.00 79.29  ? 344 VAL D CB  1 
ATOM   11528 C CG1 . VAL D 2 344 ? 42.473  -49.689 29.854  1.00 77.43  ? 344 VAL D CG1 1 
ATOM   11529 C CG2 . VAL D 2 344 ? 41.437  -47.792 28.597  1.00 81.23  ? 344 VAL D CG2 1 
ATOM   11530 N N   . LEU D 2 345 ? 44.784  -48.508 31.711  1.00 84.77  ? 345 LEU D N   1 
ATOM   11531 C CA  . LEU D 2 345 ? 45.996  -49.105 32.244  1.00 82.94  ? 345 LEU D CA  1 
ATOM   11532 C C   . LEU D 2 345 ? 46.335  -50.395 31.503  1.00 84.89  ? 345 LEU D C   1 
ATOM   11533 O O   . LEU D 2 345 ? 45.462  -51.027 30.902  1.00 86.57  ? 345 LEU D O   1 
ATOM   11534 C CB  . LEU D 2 345 ? 45.833  -49.388 33.734  1.00 82.78  ? 345 LEU D CB  1 
ATOM   11535 C CG  . LEU D 2 345 ? 46.329  -48.311 34.700  1.00 82.53  ? 345 LEU D CG  1 
ATOM   11536 C CD1 . LEU D 2 345 ? 45.579  -47.010 34.494  1.00 86.51  ? 345 LEU D CD1 1 
ATOM   11537 C CD2 . LEU D 2 345 ? 46.193  -48.794 36.133  1.00 88.01  ? 345 LEU D CD2 1 
ATOM   11538 N N   . PRO D 2 346 ? 47.602  -50.800 31.519  1.00 88.85  ? 346 PRO D N   1 
ATOM   11539 C CA  . PRO D 2 346 ? 47.992  -52.041 30.843  1.00 86.38  ? 346 PRO D CA  1 
ATOM   11540 C C   . PRO D 2 346 ? 47.390  -53.275 31.502  1.00 85.18  ? 346 PRO D C   1 
ATOM   11541 O O   . PRO D 2 346 ? 46.972  -53.258 32.661  1.00 87.79  ? 346 PRO D O   1 
ATOM   11542 C CB  . PRO D 2 346 ? 49.522  -52.042 30.960  1.00 90.57  ? 346 PRO D CB  1 
ATOM   11543 C CG  . PRO D 2 346 ? 49.816  -51.164 32.126  1.00 92.08  ? 346 PRO D CG  1 
ATOM   11544 C CD  . PRO D 2 346 ? 48.767  -50.096 32.086  1.00 93.33  ? 346 PRO D CD  1 
ATOM   11545 N N   . HIS D 2 347 ? 47.349  -54.358 30.723  1.00 84.06  ? 347 HIS D N   1 
ATOM   11546 C CA  . HIS D 2 347 ? 46.826  -55.654 31.161  1.00 81.46  ? 347 HIS D CA  1 
ATOM   11547 C C   . HIS D 2 347 ? 45.382  -55.530 31.653  1.00 80.77  ? 347 HIS D C   1 
ATOM   11548 O O   . HIS D 2 347 ? 45.054  -55.833 32.802  1.00 83.53  ? 347 HIS D O   1 
ATOM   11549 C CB  . HIS D 2 347 ? 47.731  -56.274 32.231  1.00 79.48  ? 347 HIS D CB  1 
ATOM   11550 C CG  . HIS D 2 347 ? 49.168  -56.362 31.823  1.00 79.62  ? 347 HIS D CG  1 
ATOM   11551 N ND1 . HIS D 2 347 ? 49.599  -57.167 30.791  1.00 83.13  ? 347 HIS D ND1 1 
ATOM   11552 C CD2 . HIS D 2 347 ? 50.272  -55.746 32.307  1.00 80.66  ? 347 HIS D CD2 1 
ATOM   11553 C CE1 . HIS D 2 347 ? 50.908  -57.042 30.656  1.00 86.13  ? 347 HIS D CE1 1 
ATOM   11554 N NE2 . HIS D 2 347 ? 51.340  -56.187 31.565  1.00 84.22  ? 347 HIS D NE2 1 
ATOM   11555 N N   . LYS D 2 348 ? 44.516  -55.078 30.747  1.00 78.71  ? 348 LYS D N   1 
ATOM   11556 C CA  . LYS D 2 348 ? 43.115  -54.847 31.060  1.00 74.64  ? 348 LYS D CA  1 
ATOM   11557 C C   . LYS D 2 348 ? 42.256  -55.300 29.889  1.00 74.81  ? 348 LYS D C   1 
ATOM   11558 O O   . LYS D 2 348 ? 42.567  -55.002 28.732  1.00 78.98  ? 348 LYS D O   1 
ATOM   11559 C CB  . LYS D 2 348 ? 42.856  -53.363 31.355  1.00 74.33  ? 348 LYS D CB  1 
ATOM   11560 C CG  . LYS D 2 348 ? 41.486  -53.067 31.937  1.00 77.02  ? 348 LYS D CG  1 
ATOM   11561 C CD  . LYS D 2 348 ? 41.344  -53.720 33.304  1.00 81.21  ? 348 LYS D CD  1 
ATOM   11562 C CE  . LYS D 2 348 ? 39.996  -53.424 33.941  1.00 89.89  ? 348 LYS D CE  1 
ATOM   11563 N NZ  . LYS D 2 348 ? 39.894  -53.995 35.316  1.00 96.55  ? 348 LYS D NZ  1 
ATOM   11564 N N   . GLU D 2 349 ? 41.175  -56.015 30.189  1.00 73.50  ? 349 GLU D N   1 
ATOM   11565 C CA  . GLU D 2 349 ? 40.217  -56.435 29.175  1.00 73.13  ? 349 GLU D CA  1 
ATOM   11566 C C   . GLU D 2 349 ? 39.040  -55.470 29.194  1.00 72.10  ? 349 GLU D C   1 
ATOM   11567 O O   . GLU D 2 349 ? 38.345  -55.351 30.210  1.00 72.02  ? 349 GLU D O   1 
ATOM   11568 C CB  . GLU D 2 349 ? 39.732  -57.865 29.406  1.00 75.70  ? 349 GLU D CB  1 
ATOM   11569 C CG  . GLU D 2 349 ? 40.790  -58.936 29.227  1.00 77.90  ? 349 GLU D CG  1 
ATOM   11570 C CD  . GLU D 2 349 ? 40.213  -60.334 29.334  1.00 79.29  ? 349 GLU D CD  1 
ATOM   11571 O OE1 . GLU D 2 349 ? 39.153  -60.491 29.975  1.00 79.41  ? 349 GLU D OE1 1 
ATOM   11572 O OE2 . GLU D 2 349 ? 40.815  -61.272 28.771  1.00 86.58  ? 349 GLU D OE2 1 
ATOM   11573 N N   . ILE D 2 350 ? 38.822  -54.788 28.076  1.00 71.38  ? 350 ILE D N   1 
ATOM   11574 C CA  . ILE D 2 350 ? 37.748  -53.813 27.955  1.00 70.41  ? 350 ILE D CA  1 
ATOM   11575 C C   . ILE D 2 350 ? 36.564  -54.518 27.313  1.00 71.49  ? 350 ILE D C   1 
ATOM   11576 O O   . ILE D 2 350 ? 36.595  -54.850 26.124  1.00 76.87  ? 350 ILE D O   1 
ATOM   11577 C CB  . ILE D 2 350 ? 38.182  -52.589 27.137  1.00 69.73  ? 350 ILE D CB  1 
ATOM   11578 C CG1 . ILE D 2 350 ? 39.419  -51.946 27.762  1.00 69.96  ? 350 ILE D CG1 1 
ATOM   11579 C CG2 . ILE D 2 350 ? 37.045  -51.583 27.045  1.00 71.69  ? 350 ILE D CG2 1 
ATOM   11580 C CD1 . ILE D 2 350 ? 39.220  -51.544 29.205  1.00 70.83  ? 350 ILE D CD1 1 
ATOM   11581 N N   . LYS D 2 351 ? 35.519  -54.745 28.105  1.00 70.23  ? 351 LYS D N   1 
ATOM   11582 C CA  . LYS D 2 351 ? 34.296  -55.359 27.621  1.00 70.13  ? 351 LYS D CA  1 
ATOM   11583 C C   . LYS D 2 351 ? 33.110  -54.413 27.702  1.00 69.27  ? 351 LYS D C   1 
ATOM   11584 O O   . LYS D 2 351 ? 31.982  -54.830 27.413  1.00 69.16  ? 351 LYS D O   1 
ATOM   11585 C CB  . LYS D 2 351 ? 33.996  -56.646 28.403  1.00 74.22  ? 351 LYS D CB  1 
ATOM   11586 C CG  . LYS D 2 351 ? 35.102  -57.693 28.325  1.00 75.19  ? 351 LYS D CG  1 
ATOM   11587 C CD  . LYS D 2 351 ? 34.672  -59.017 28.944  1.00 74.77  ? 351 LYS D CD  1 
ATOM   11588 C CE  . LYS D 2 351 ? 35.752  -60.076 28.769  1.00 75.93  ? 351 LYS D CE  1 
ATOM   11589 N NZ  . LYS D 2 351 ? 35.336  -61.412 29.280  1.00 74.69  ? 351 LYS D NZ  1 
ATOM   11590 N N   . SER D 2 352 ? 33.330  -53.160 28.093  1.00 68.70  ? 352 SER D N   1 
ATOM   11591 C CA  . SER D 2 352 ? 32.281  -52.158 28.181  1.00 68.42  ? 352 SER D CA  1 
ATOM   11592 C C   . SER D 2 352 ? 32.734  -50.903 27.447  1.00 67.90  ? 352 SER D C   1 
ATOM   11593 O O   . SER D 2 352 ? 33.931  -50.666 27.261  1.00 68.96  ? 352 SER D O   1 
ATOM   11594 C CB  . SER D 2 352 ? 31.940  -51.829 29.640  1.00 75.44  ? 352 SER D CB  1 
ATOM   11595 O OG  . SER D 2 352 ? 31.552  -52.992 30.353  1.00 83.69  ? 352 SER D OG  1 
ATOM   11596 N N   . ASN D 2 353 ? 31.759  -50.096 27.032  1.00 70.53  ? 353 ASN D N   1 
ATOM   11597 C CA  . ASN D 2 353 ? 32.041  -48.881 26.279  1.00 72.59  ? 353 ASN D CA  1 
ATOM   11598 C C   . ASN D 2 353 ? 32.553  -47.768 27.190  1.00 67.92  ? 353 ASN D C   1 
ATOM   11599 O O   . ASN D 2 353 ? 32.026  -47.545 28.283  1.00 66.74  ? 353 ASN D O   1 
ATOM   11600 C CB  . ASN D 2 353 ? 30.784  -48.406 25.542  1.00 78.29  ? 353 ASN D CB  1 
ATOM   11601 C CG  . ASN D 2 353 ? 30.240  -49.444 24.570  1.00 75.17  ? 353 ASN D CG  1 
ATOM   11602 O OD1 . ASN D 2 353 ? 30.980  -50.287 24.065  1.00 75.10  ? 353 ASN D OD1 1 
ATOM   11603 N ND2 . ASN D 2 353 ? 28.939  -49.381 24.303  1.00 72.87  ? 353 ASN D ND2 1 
ATOM   11604 N N   . ILE D 2 354 ? 33.595  -47.070 26.732  1.00 74.13  ? 354 ILE D N   1 
ATOM   11605 C CA  . ILE D 2 354 ? 34.067  -45.857 27.395  1.00 70.57  ? 354 ILE D CA  1 
ATOM   11606 C C   . ILE D 2 354 ? 33.488  -44.670 26.638  1.00 79.28  ? 354 ILE D C   1 
ATOM   11607 O O   . ILE D 2 354 ? 34.208  -43.958 25.929  1.00 75.77  ? 354 ILE D O   1 
ATOM   11608 C CB  . ILE D 2 354 ? 35.607  -45.794 27.451  1.00 74.71  ? 354 ILE D CB  1 
ATOM   11609 C CG1 . ILE D 2 354 ? 36.178  -47.115 27.963  1.00 71.27  ? 354 ILE D CG1 1 
ATOM   11610 C CG2 . ILE D 2 354 ? 36.068  -44.669 28.369  1.00 77.73  ? 354 ILE D CG2 1 
ATOM   11611 C CD1 . ILE D 2 354 ? 37.686  -47.131 28.050  1.00 67.02  ? 354 ILE D CD1 1 
ATOM   11612 N N   . LEU D 2 355 ? 32.176  -44.462 26.766  1.00 73.88  ? 355 LEU D N   1 
ATOM   11613 C CA  . LEU D 2 355 ? 31.483  -43.468 25.954  1.00 82.36  ? 355 LEU D CA  1 
ATOM   11614 C C   . LEU D 2 355 ? 31.889  -42.035 26.275  1.00 85.40  ? 355 LEU D C   1 
ATOM   11615 O O   . LEU D 2 355 ? 31.516  -41.125 25.527  1.00 85.35  ? 355 LEU D O   1 
ATOM   11616 C CB  . LEU D 2 355 ? 29.966  -43.633 26.100  1.00 78.17  ? 355 LEU D CB  1 
ATOM   11617 C CG  . LEU D 2 355 ? 29.407  -44.129 27.435  1.00 77.34  ? 355 LEU D CG  1 
ATOM   11618 C CD1 . LEU D 2 355 ? 29.437  -43.028 28.483  1.00 86.71  ? 355 LEU D CD1 1 
ATOM   11619 C CD2 . LEU D 2 355 ? 27.995  -44.673 27.256  1.00 72.95  ? 355 LEU D CD2 1 
ATOM   11620 N N   . LYS D 2 356 ? 32.627  -41.810 27.351  1.00 94.19  ? 356 LYS D N   1 
ATOM   11621 C CA  . LYS D 2 356 ? 33.088  -40.485 27.732  1.00 94.29  ? 356 LYS D CA  1 
ATOM   11622 C C   . LYS D 2 356 ? 34.486  -40.616 28.314  1.00 95.12  ? 356 LYS D C   1 
ATOM   11623 O O   . LYS D 2 356 ? 34.882  -41.704 28.746  1.00 96.46  ? 356 LYS D O   1 
ATOM   11624 C CB  . LYS D 2 356 ? 32.130  -39.834 28.741  1.00 95.29  ? 356 LYS D CB  1 
ATOM   11625 C CG  . LYS D 2 356 ? 30.805  -39.389 28.128  1.00 95.20  ? 356 LYS D CG  1 
ATOM   11626 C CD  . LYS D 2 356 ? 29.852  -38.840 29.175  1.00 104.58 ? 356 LYS D CD  1 
ATOM   11627 C CE  . LYS D 2 356 ? 30.422  -37.597 29.836  1.00 115.42 ? 356 LYS D CE  1 
ATOM   11628 N NZ  . LYS D 2 356 ? 30.644  -36.501 28.849  1.00 113.01 ? 356 LYS D NZ  1 
ATOM   11629 N N   . PRO D 2 357 ? 35.267  -39.534 28.318  1.00 86.66  ? 357 PRO D N   1 
ATOM   11630 C CA  . PRO D 2 357 ? 36.636  -39.612 28.846  1.00 83.74  ? 357 PRO D CA  1 
ATOM   11631 C C   . PRO D 2 357 ? 36.667  -40.153 30.268  1.00 86.89  ? 357 PRO D C   1 
ATOM   11632 O O   . PRO D 2 357 ? 35.976  -39.653 31.160  1.00 86.52  ? 357 PRO D O   1 
ATOM   11633 C CB  . PRO D 2 357 ? 37.117  -38.159 28.783  1.00 82.81  ? 357 PRO D CB  1 
ATOM   11634 C CG  . PRO D 2 357 ? 36.335  -37.561 27.674  1.00 85.33  ? 357 PRO D CG  1 
ATOM   11635 C CD  . PRO D 2 357 ? 34.980  -38.210 27.737  1.00 89.31  ? 357 PRO D CD  1 
ATOM   11636 N N   . GLU D 2 358 ? 37.490  -41.178 30.476  1.00 86.55  ? 358 GLU D N   1 
ATOM   11637 C CA  . GLU D 2 358 ? 37.505  -41.908 31.733  1.00 84.20  ? 358 GLU D CA  1 
ATOM   11638 C C   . GLU D 2 358 ? 38.814  -42.678 31.844  1.00 84.63  ? 358 GLU D C   1 
ATOM   11639 O O   . GLU D 2 358 ? 39.318  -43.204 30.849  1.00 81.87  ? 358 GLU D O   1 
ATOM   11640 C CB  . GLU D 2 358 ? 36.307  -42.862 31.820  1.00 85.87  ? 358 GLU D CB  1 
ATOM   11641 C CG  . GLU D 2 358 ? 36.281  -43.750 33.050  1.00 83.23  ? 358 GLU D CG  1 
ATOM   11642 C CD  . GLU D 2 358 ? 35.157  -44.766 33.000  1.00 86.48  ? 358 GLU D CD  1 
ATOM   11643 O OE1 . GLU D 2 358 ? 34.253  -44.614 32.150  1.00 87.04  ? 358 GLU D OE1 1 
ATOM   11644 O OE2 . GLU D 2 358 ? 35.177  -45.716 33.810  1.00 90.13  ? 358 GLU D OE2 1 
ATOM   11645 N N   . ILE D 2 359 ? 39.353  -42.735 33.057  1.00 85.62  ? 359 ILE D N   1 
ATOM   11646 C CA  . ILE D 2 359 ? 40.586  -43.457 33.349  1.00 81.84  ? 359 ILE D CA  1 
ATOM   11647 C C   . ILE D 2 359 ? 40.216  -44.832 33.888  1.00 81.22  ? 359 ILE D C   1 
ATOM   11648 O O   . ILE D 2 359 ? 39.583  -44.944 34.944  1.00 86.49  ? 359 ILE D O   1 
ATOM   11649 C CB  . ILE D 2 359 ? 41.463  -42.684 34.346  1.00 82.54  ? 359 ILE D CB  1 
ATOM   11650 C CG1 . ILE D 2 359 ? 41.920  -41.362 33.728  1.00 86.52  ? 359 ILE D CG1 1 
ATOM   11651 C CG2 . ILE D 2 359 ? 42.653  -43.526 34.771  1.00 83.90  ? 359 ILE D CG2 1 
ATOM   11652 C CD1 . ILE D 2 359 ? 42.704  -40.482 34.666  1.00 94.56  ? 359 ILE D CD1 1 
ATOM   11653 N N   . VAL D 2 360 ? 40.608  -45.878 33.164  1.00 80.26  ? 360 VAL D N   1 
ATOM   11654 C CA  . VAL D 2 360 ? 40.284  -47.255 33.516  1.00 80.18  ? 360 VAL D CA  1 
ATOM   11655 C C   . VAL D 2 360 ? 41.522  -47.937 34.077  1.00 81.27  ? 360 VAL D C   1 
ATOM   11656 O O   . VAL D 2 360 ? 42.623  -47.787 33.538  1.00 79.22  ? 360 VAL D O   1 
ATOM   11657 C CB  . VAL D 2 360 ? 39.749  -48.020 32.289  1.00 78.51  ? 360 VAL D CB  1 
ATOM   11658 C CG1 . VAL D 2 360 ? 39.330  -49.429 32.675  1.00 81.36  ? 360 VAL D CG1 1 
ATOM   11659 C CG2 . VAL D 2 360 ? 38.599  -47.262 31.647  1.00 79.93  ? 360 VAL D CG2 1 
ATOM   11660 N N   . MET D 2 361 ? 41.338  -48.697 35.153  1.00 81.68  ? 361 MET D N   1 
ATOM   11661 C CA  . MET D 2 361 ? 42.433  -49.448 35.763  1.00 82.92  ? 361 MET D CA  1 
ATOM   11662 C C   . MET D 2 361 ? 42.162  -50.943 35.705  1.00 89.51  ? 361 MET D C   1 
ATOM   11663 O O   . MET D 2 361 ? 42.992  -51.718 35.229  1.00 91.64  ? 361 MET D O   1 
ATOM   11664 C CB  . MET D 2 361 ? 42.662  -49.023 37.213  1.00 87.66  ? 361 MET D CB  1 
ATOM   11665 C CG  . MET D 2 361 ? 42.423  -47.557 37.493  1.00 87.32  ? 361 MET D CG  1 
ATOM   11666 S SD  . MET D 2 361 ? 42.830  -47.167 39.204  1.00 81.76  ? 361 MET D SD  1 
ATOM   11667 C CE  . MET D 2 361 ? 44.517  -47.757 39.300  1.00 94.09  ? 361 MET D CE  1 
ATOM   11668 O OXT . MET D 2 361 ? 41.112  -51.405 36.152  1.00 94.84  ? 361 MET D OXT 1 
ATOM   11669 N N   . MET E 2 1   ? -5.741  -24.192 87.208  1.00 177.61 ? 1   MET E N   1 
ATOM   11670 C CA  . MET E 2 1   ? -5.051  -25.184 86.392  1.00 182.06 ? 1   MET E CA  1 
ATOM   11671 C C   . MET E 2 1   ? -3.852  -24.559 85.687  1.00 179.89 ? 1   MET E C   1 
ATOM   11672 O O   . MET E 2 1   ? -3.907  -23.407 85.253  1.00 177.61 ? 1   MET E O   1 
ATOM   11673 C CB  . MET E 2 1   ? -6.011  -25.801 85.372  1.00 184.09 ? 1   MET E CB  1 
ATOM   11674 C CG  . MET E 2 1   ? -5.442  -26.997 84.626  1.00 183.43 ? 1   MET E CG  1 
ATOM   11675 S SD  . MET E 2 1   ? -6.674  -27.846 83.622  1.00 187.74 ? 1   MET E SD  1 
ATOM   11676 C CE  . MET E 2 1   ? -7.811  -28.399 84.890  1.00 186.71 ? 1   MET E CE  1 
ATOM   11677 N N   . LYS E 2 2   ? -2.770  -25.323 85.577  1.00 172.05 ? 2   LYS E N   1 
ATOM   11678 C CA  . LYS E 2 2   ? -1.513  -24.855 85.011  1.00 165.75 ? 2   LYS E CA  1 
ATOM   11679 C C   . LYS E 2 2   ? -1.242  -25.550 83.678  1.00 169.84 ? 2   LYS E C   1 
ATOM   11680 O O   . LYS E 2 2   ? -1.977  -26.446 83.253  1.00 176.88 ? 2   LYS E O   1 
ATOM   11681 C CB  . LYS E 2 2   ? -0.367  -25.089 85.997  1.00 158.08 ? 2   LYS E CB  1 
ATOM   11682 C CG  . LYS E 2 2   ? -0.537  -24.364 87.322  1.00 156.52 ? 2   LYS E CG  1 
ATOM   11683 C CD  . LYS E 2 2   ? -0.374  -22.864 87.159  1.00 151.03 ? 2   LYS E CD  1 
ATOM   11684 C CE  . LYS E 2 2   ? -0.417  -22.160 88.504  1.00 146.58 ? 2   LYS E CE  1 
ATOM   11685 N NZ  . LYS E 2 2   ? -0.086  -20.714 88.382  1.00 134.16 ? 2   LYS E NZ  1 
ATOM   11686 N N   . ALA E 2 3   ? -0.163  -25.126 83.022  1.00 168.79 ? 3   ALA E N   1 
ATOM   11687 C CA  . ALA E 2 3   ? 0.242   -25.689 81.741  1.00 166.76 ? 3   ALA E CA  1 
ATOM   11688 C C   . ALA E 2 3   ? 1.678   -25.279 81.448  1.00 165.58 ? 3   ALA E C   1 
ATOM   11689 O O   . ALA E 2 3   ? 2.154   -24.247 81.927  1.00 168.97 ? 3   ALA E O   1 
ATOM   11690 C CB  . ALA E 2 3   ? -0.685  -25.239 80.605  1.00 162.27 ? 3   ALA E CB  1 
ATOM   11691 N N   . LEU E 2 4   ? 2.360   -26.102 80.653  1.00 168.26 ? 4   LEU E N   1 
ATOM   11692 C CA  . LEU E 2 4   ? 3.743   -25.867 80.259  1.00 172.39 ? 4   LEU E CA  1 
ATOM   11693 C C   . LEU E 2 4   ? 3.910   -26.221 78.788  1.00 172.28 ? 4   LEU E C   1 
ATOM   11694 O O   . LEU E 2 4   ? 3.352   -27.215 78.318  1.00 175.36 ? 4   LEU E O   1 
ATOM   11695 C CB  . LEU E 2 4   ? 4.712   -26.693 81.120  1.00 170.92 ? 4   LEU E CB  1 
ATOM   11696 C CG  . LEU E 2 4   ? 6.198   -26.694 80.753  1.00 165.77 ? 4   LEU E CG  1 
ATOM   11697 C CD1 . LEU E 2 4   ? 6.806   -25.315 80.938  1.00 174.56 ? 4   LEU E CD1 1 
ATOM   11698 C CD2 . LEU E 2 4   ? 6.946   -27.723 81.584  1.00 159.75 ? 4   LEU E CD2 1 
ATOM   11699 N N   . ILE E 2 5   ? 4.661   -25.400 78.057  1.00 170.93 ? 5   ILE E N   1 
ATOM   11700 C CA  . ILE E 2 5   ? 4.880   -25.599 76.628  1.00 167.10 ? 5   ILE E CA  1 
ATOM   11701 C C   . ILE E 2 5   ? 6.377   -25.716 76.372  1.00 160.15 ? 5   ILE E C   1 
ATOM   11702 O O   . ILE E 2 5   ? 7.147   -24.818 76.736  1.00 159.13 ? 5   ILE E O   1 
ATOM   11703 C CB  . ILE E 2 5   ? 4.267   -24.466 75.792  1.00 167.27 ? 5   ILE E CB  1 
ATOM   11704 C CG1 . ILE E 2 5   ? 2.748   -24.423 75.987  1.00 174.09 ? 5   ILE E CG1 1 
ATOM   11705 C CG2 . ILE E 2 5   ? 4.616   -24.643 74.322  1.00 161.23 ? 5   ILE E CG2 1 
ATOM   11706 C CD1 . ILE E 2 5   ? 2.056   -23.344 75.187  1.00 188.90 ? 5   ILE E CD1 1 
ATOM   11707 N N   . LEU E 2 6   ? 6.787   -26.819 75.748  1.00 146.71 ? 6   LEU E N   1 
ATOM   11708 C CA  . LEU E 2 6   ? 8.179   -27.023 75.362  1.00 137.61 ? 6   LEU E CA  1 
ATOM   11709 C C   . LEU E 2 6   ? 8.444   -26.339 74.025  1.00 135.08 ? 6   LEU E C   1 
ATOM   11710 O O   . LEU E 2 6   ? 7.873   -26.724 73.000  1.00 136.98 ? 6   LEU E O   1 
ATOM   11711 C CB  . LEU E 2 6   ? 8.500   -28.512 75.274  1.00 131.46 ? 6   LEU E CB  1 
ATOM   11712 C CG  . LEU E 2 6   ? 8.424   -29.338 76.556  1.00 137.81 ? 6   LEU E CG  1 
ATOM   11713 C CD1 . LEU E 2 6   ? 8.629   -30.805 76.234  1.00 135.04 ? 6   LEU E CD1 1 
ATOM   11714 C CD2 . LEU E 2 6   ? 9.459   -28.869 77.564  1.00 144.73 ? 6   LEU E CD2 1 
ATOM   11715 N N   . VAL E 2 7   ? 9.309   -25.328 74.033  1.00 133.13 ? 7   VAL E N   1 
ATOM   11716 C CA  . VAL E 2 7   ? 9.673   -24.618 72.812  1.00 128.77 ? 7   VAL E CA  1 
ATOM   11717 C C   . VAL E 2 7   ? 10.978  -25.178 72.265  1.00 126.30 ? 7   VAL E C   1 
ATOM   11718 O O   . VAL E 2 7   ? 11.048  -25.606 71.111  1.00 126.38 ? 7   VAL E O   1 
ATOM   11719 C CB  . VAL E 2 7   ? 9.795   -23.103 73.061  1.00 132.36 ? 7   VAL E CB  1 
ATOM   11720 C CG1 . VAL E 2 7   ? 10.166  -22.386 71.773  1.00 129.50 ? 7   VAL E CG1 1 
ATOM   11721 C CG2 . VAL E 2 7   ? 8.505   -22.551 73.641  1.00 143.68 ? 7   VAL E CG2 1 
ATOM   11722 N N   . GLY E 2 8   ? 12.013  -25.178 73.087  1.00 131.22 ? 8   GLY E N   1 
ATOM   11723 C CA  . GLY E 2 8   ? 13.330  -25.625 72.664  1.00 140.63 ? 8   GLY E CA  1 
ATOM   11724 C C   . GLY E 2 8   ? 14.268  -24.445 72.446  1.00 150.66 ? 8   GLY E C   1 
ATOM   11725 O O   . GLY E 2 8   ? 14.424  -23.598 73.322  1.00 147.62 ? 8   GLY E O   1 
ATOM   11726 N N   . GLY E 2 9   ? 14.891  -24.398 71.276  1.00 187.12 ? 9   GLY E N   1 
ATOM   11727 C CA  . GLY E 2 9   ? 15.799  -23.330 70.919  1.00 187.14 ? 9   GLY E CA  1 
ATOM   11728 C C   . GLY E 2 9   ? 15.123  -22.222 70.142  1.00 186.72 ? 9   GLY E C   1 
ATOM   11729 O O   . GLY E 2 9   ? 13.926  -21.959 70.293  1.00 186.81 ? 9   GLY E O   1 
ATOM   11730 N N   . PHE E 2 10  ? 15.906  -21.564 69.290  1.00 158.98 ? 10  PHE E N   1 
ATOM   11731 C CA  . PHE E 2 10  ? 15.434  -20.427 68.512  1.00 152.04 ? 10  PHE E CA  1 
ATOM   11732 C C   . PHE E 2 10  ? 14.769  -20.835 67.206  1.00 146.24 ? 10  PHE E C   1 
ATOM   11733 O O   . PHE E 2 10  ? 14.088  -20.008 66.590  1.00 145.71 ? 10  PHE E O   1 
ATOM   11734 C CB  . PHE E 2 10  ? 16.603  -19.482 68.210  1.00 152.44 ? 10  PHE E CB  1 
ATOM   11735 C CG  . PHE E 2 10  ? 16.230  -18.028 68.214  1.00 151.37 ? 10  PHE E CG  1 
ATOM   11736 C CD1 . PHE E 2 10  ? 16.126  -17.324 69.402  1.00 153.26 ? 10  PHE E CD1 1 
ATOM   11737 C CD2 . PHE E 2 10  ? 15.995  -17.360 67.024  1.00 148.94 ? 10  PHE E CD2 1 
ATOM   11738 C CE1 . PHE E 2 10  ? 15.786  -15.983 69.402  1.00 152.58 ? 10  PHE E CE1 1 
ATOM   11739 C CE2 . PHE E 2 10  ? 15.658  -16.022 67.017  1.00 147.94 ? 10  PHE E CE2 1 
ATOM   11740 C CZ  . PHE E 2 10  ? 15.551  -15.332 68.206  1.00 149.08 ? 10  PHE E CZ  1 
ATOM   11741 N N   . GLY E 2 11  ? 14.941  -22.080 66.776  1.00 139.11 ? 11  GLY E N   1 
ATOM   11742 C CA  . GLY E 2 11  ? 14.444  -22.507 65.485  1.00 132.53 ? 11  GLY E CA  1 
ATOM   11743 C C   . GLY E 2 11  ? 15.518  -22.413 64.425  1.00 127.36 ? 11  GLY E C   1 
ATOM   11744 O O   . GLY E 2 11  ? 15.325  -21.774 63.386  1.00 125.43 ? 11  GLY E O   1 
ATOM   11745 N N   . THR E 2 12  ? 16.664  -23.047 64.683  1.00 126.14 ? 12  THR E N   1 
ATOM   11746 C CA  . THR E 2 12  ? 17.782  -22.972 63.749  1.00 123.07 ? 12  THR E CA  1 
ATOM   11747 C C   . THR E 2 12  ? 17.427  -23.591 62.405  1.00 123.72 ? 12  THR E C   1 
ATOM   11748 O O   . THR E 2 12  ? 17.890  -23.122 61.360  1.00 123.92 ? 12  THR E O   1 
ATOM   11749 C CB  . THR E 2 12  ? 19.011  -23.662 64.340  1.00 122.52 ? 12  THR E CB  1 
ATOM   11750 O OG1 . THR E 2 12  ? 18.705  -25.036 64.608  1.00 127.02 ? 12  THR E OG1 1 
ATOM   11751 C CG2 . THR E 2 12  ? 19.430  -22.981 65.635  1.00 120.12 ? 12  THR E CG2 1 
ATOM   11752 N N   . ARG E 2 13  ? 16.610  -24.639 62.415  1.00 135.43 ? 13  ARG E N   1 
ATOM   11753 C CA  . ARG E 2 13  ? 16.196  -25.340 61.209  1.00 134.83 ? 13  ARG E CA  1 
ATOM   11754 C C   . ARG E 2 13  ? 15.040  -24.650 60.493  1.00 134.83 ? 13  ARG E C   1 
ATOM   11755 O O   . ARG E 2 13  ? 14.511  -25.206 59.523  1.00 133.93 ? 13  ARG E O   1 
ATOM   11756 C CB  . ARG E 2 13  ? 15.812  -26.777 61.565  1.00 136.99 ? 13  ARG E CB  1 
ATOM   11757 C CG  . ARG E 2 13  ? 15.112  -26.893 62.912  1.00 140.38 ? 13  ARG E CG  1 
ATOM   11758 C CD  . ARG E 2 13  ? 15.229  -28.289 63.499  1.00 143.92 ? 13  ARG E CD  1 
ATOM   11759 N NE  . ARG E 2 13  ? 16.620  -28.707 63.624  1.00 147.45 ? 13  ARG E NE  1 
ATOM   11760 C CZ  . ARG E 2 13  ? 17.163  -29.708 62.940  1.00 152.09 ? 13  ARG E CZ  1 
ATOM   11761 N NH1 . ARG E 2 13  ? 16.427  -30.398 62.079  1.00 152.71 ? 13  ARG E NH1 1 
ATOM   11762 N NH2 . ARG E 2 13  ? 18.439  -30.021 63.119  1.00 153.77 ? 13  ARG E NH2 1 
ATOM   11763 N N   . LEU E 2 14  ? 14.638  -23.461 60.943  1.00 127.21 ? 14  LEU E N   1 
ATOM   11764 C CA  . LEU E 2 14  ? 13.560  -22.704 60.321  1.00 124.42 ? 14  LEU E CA  1 
ATOM   11765 C C   . LEU E 2 14  ? 14.046  -21.392 59.718  1.00 120.62 ? 14  LEU E C   1 
ATOM   11766 O O   . LEU E 2 14  ? 13.222  -20.547 59.353  1.00 118.41 ? 14  LEU E O   1 
ATOM   11767 C CB  . LEU E 2 14  ? 12.444  -22.425 61.333  1.00 127.25 ? 14  LEU E CB  1 
ATOM   11768 C CG  . LEU E 2 14  ? 11.559  -23.569 61.841  1.00 126.70 ? 14  LEU E CG  1 
ATOM   11769 C CD1 . LEU E 2 14  ? 12.275  -24.421 62.883  1.00 125.84 ? 14  LEU E CD1 1 
ATOM   11770 C CD2 . LEU E 2 14  ? 10.256  -23.019 62.402  1.00 132.11 ? 14  LEU E CD2 1 
ATOM   11771 N N   . ARG E 2 15  ? 15.362  -21.203 59.606  1.00 114.92 ? 15  ARG E N   1 
ATOM   11772 C CA  . ARG E 2 15  ? 15.903  -20.002 58.995  1.00 110.85 ? 15  ARG E CA  1 
ATOM   11773 C C   . ARG E 2 15  ? 15.510  -19.945 57.519  1.00 109.42 ? 15  ARG E C   1 
ATOM   11774 O O   . ARG E 2 15  ? 15.245  -20.979 56.899  1.00 110.91 ? 15  ARG E O   1 
ATOM   11775 C CB  . ARG E 2 15  ? 17.425  -19.975 59.151  1.00 110.91 ? 15  ARG E CB  1 
ATOM   11776 C CG  . ARG E 2 15  ? 17.895  -19.806 60.590  1.00 112.08 ? 15  ARG E CG  1 
ATOM   11777 C CD  . ARG E 2 15  ? 19.389  -19.519 60.657  1.00 113.69 ? 15  ARG E CD  1 
ATOM   11778 N NE  . ARG E 2 15  ? 19.834  -19.210 62.015  1.00 111.57 ? 15  ARG E NE  1 
ATOM   11779 C CZ  . ARG E 2 15  ? 20.416  -20.082 62.832  1.00 113.87 ? 15  ARG E CZ  1 
ATOM   11780 N NH1 . ARG E 2 15  ? 20.631  -21.329 62.434  1.00 117.77 ? 15  ARG E NH1 1 
ATOM   11781 N NH2 . ARG E 2 15  ? 20.785  -19.707 64.049  1.00 110.18 ? 15  ARG E NH2 1 
ATOM   11782 N N   . PRO E 2 16  ? 15.472  -18.740 56.920  1.00 106.48 ? 16  PRO E N   1 
ATOM   11783 C CA  . PRO E 2 16  ? 15.811  -17.422 57.473  1.00 106.37 ? 16  PRO E CA  1 
ATOM   11784 C C   . PRO E 2 16  ? 14.674  -16.741 58.228  1.00 105.86 ? 16  PRO E C   1 
ATOM   11785 O O   . PRO E 2 16  ? 14.802  -15.573 58.599  1.00 105.18 ? 16  PRO E O   1 
ATOM   11786 C CB  . PRO E 2 16  ? 16.166  -16.616 56.225  1.00 102.82 ? 16  PRO E CB  1 
ATOM   11787 C CG  . PRO E 2 16  ? 15.263  -17.175 55.184  1.00 95.32  ? 16  PRO E CG  1 
ATOM   11788 C CD  . PRO E 2 16  ? 15.126  -18.649 55.490  1.00 101.03 ? 16  PRO E CD  1 
ATOM   11789 N N   . LEU E 2 17  ? 13.572  -17.460 58.450  1.00 105.17 ? 17  LEU E N   1 
ATOM   11790 C CA  . LEU E 2 17  ? 12.445  -16.859 59.152  1.00 104.58 ? 17  LEU E CA  1 
ATOM   11791 C C   . LEU E 2 17  ? 12.739  -16.671 60.634  1.00 107.23 ? 17  LEU E C   1 
ATOM   11792 O O   . LEU E 2 17  ? 12.171  -15.774 61.269  1.00 106.47 ? 17  LEU E O   1 
ATOM   11793 C CB  . LEU E 2 17  ? 11.191  -17.710 58.957  1.00 104.42 ? 17  LEU E CB  1 
ATOM   11794 C CG  . LEU E 2 17  ? 10.761  -17.901 57.502  1.00 98.00  ? 17  LEU E CG  1 
ATOM   11795 C CD1 . LEU E 2 17  ? 9.519   -18.773 57.424  1.00 103.60 ? 17  LEU E CD1 1 
ATOM   11796 C CD2 . LEU E 2 17  ? 10.526  -16.555 56.833  1.00 96.29  ? 17  LEU E CD2 1 
ATOM   11797 N N   . THR E 2 18  ? 13.617  -17.496 61.201  1.00 107.95 ? 18  THR E N   1 
ATOM   11798 C CA  . THR E 2 18  ? 13.968  -17.403 62.611  1.00 113.24 ? 18  THR E CA  1 
ATOM   11799 C C   . THR E 2 18  ? 15.289  -16.682 62.852  1.00 116.14 ? 18  THR E C   1 
ATOM   11800 O O   . THR E 2 18  ? 15.823  -16.748 63.964  1.00 119.68 ? 18  THR E O   1 
ATOM   11801 C CB  . THR E 2 18  ? 14.007  -18.795 63.244  1.00 115.30 ? 18  THR E CB  1 
ATOM   11802 O OG1 . THR E 2 18  ? 14.844  -19.656 62.462  1.00 116.05 ? 18  THR E OG1 1 
ATOM   11803 C CG2 . THR E 2 18  ? 12.605  -19.379 63.325  1.00 112.59 ? 18  THR E CG2 1 
ATOM   11804 N N   . LEU E 2 19  ? 15.832  -16.000 61.840  1.00 113.78 ? 19  LEU E N   1 
ATOM   11805 C CA  . LEU E 2 19  ? 17.032  -15.199 62.063  1.00 115.15 ? 19  LEU E CA  1 
ATOM   11806 C C   . LEU E 2 19  ? 16.728  -13.960 62.894  1.00 119.02 ? 19  LEU E C   1 
ATOM   11807 O O   . LEU E 2 19  ? 17.610  -13.455 63.599  1.00 114.30 ? 19  LEU E O   1 
ATOM   11808 C CB  . LEU E 2 19  ? 17.659  -14.800 60.726  1.00 114.92 ? 19  LEU E CB  1 
ATOM   11809 C CG  . LEU E 2 19  ? 18.709  -15.747 60.142  1.00 106.54 ? 19  LEU E CG  1 
ATOM   11810 C CD1 . LEU E 2 19  ? 19.238  -15.211 58.821  1.00 96.88  ? 19  LEU E CD1 1 
ATOM   11811 C CD2 . LEU E 2 19  ? 19.844  -15.948 61.132  1.00 106.62 ? 19  LEU E CD2 1 
ATOM   11812 N N   . SER E 2 20  ? 15.494  -13.462 62.829  1.00 137.13 ? 20  SER E N   1 
ATOM   11813 C CA  . SER E 2 20  ? 15.073  -12.294 63.591  1.00 138.35 ? 20  SER E CA  1 
ATOM   11814 C C   . SER E 2 20  ? 14.052  -12.664 64.660  1.00 138.29 ? 20  SER E C   1 
ATOM   11815 O O   . SER E 2 20  ? 14.318  -12.505 65.854  1.00 139.02 ? 20  SER E O   1 
ATOM   11816 C CB  . SER E 2 20  ? 14.503  -11.226 62.646  1.00 144.59 ? 20  SER E CB  1 
ATOM   11817 O OG  . SER E 2 20  ? 15.467  -10.830 61.683  1.00 138.62 ? 20  SER E OG  1 
ATOM   11818 N N   . PHE E 2 21  ? 12.881  -13.156 64.259  1.00 123.58 ? 21  PHE E N   1 
ATOM   11819 C CA  . PHE E 2 21  ? 11.912  -13.587 65.258  1.00 119.39 ? 21  PHE E CA  1 
ATOM   11820 C C   . PHE E 2 21  ? 12.142  -15.056 65.602  1.00 116.73 ? 21  PHE E C   1 
ATOM   11821 O O   . PHE E 2 21  ? 12.419  -15.863 64.712  1.00 115.06 ? 21  PHE E O   1 
ATOM   11822 C CB  . PHE E 2 21  ? 10.485  -13.401 64.746  1.00 117.21 ? 21  PHE E CB  1 
ATOM   11823 C CG  . PHE E 2 21  ? 10.085  -11.962 64.568  1.00 121.63 ? 21  PHE E CG  1 
ATOM   11824 C CD1 . PHE E 2 21  ? 10.661  -10.969 65.343  1.00 125.06 ? 21  PHE E CD1 1 
ATOM   11825 C CD2 . PHE E 2 21  ? 9.137   -11.603 63.622  1.00 124.10 ? 21  PHE E CD2 1 
ATOM   11826 C CE1 . PHE E 2 21  ? 10.298  -9.645  65.180  1.00 127.96 ? 21  PHE E CE1 1 
ATOM   11827 C CE2 . PHE E 2 21  ? 8.770   -10.279 63.455  1.00 127.66 ? 21  PHE E CE2 1 
ATOM   11828 C CZ  . PHE E 2 21  ? 9.352   -9.300  64.235  1.00 128.06 ? 21  PHE E CZ  1 
ATOM   11829 N N   . PRO E 2 22  ? 12.021  -15.443 66.867  1.00 116.49 ? 22  PRO E N   1 
ATOM   11830 C CA  . PRO E 2 22  ? 12.270  -16.840 67.242  1.00 116.82 ? 22  PRO E CA  1 
ATOM   11831 C C   . PRO E 2 22  ? 11.200  -17.767 66.685  1.00 110.59 ? 22  PRO E C   1 
ATOM   11832 O O   . PRO E 2 22  ? 10.209  -17.343 66.085  1.00 108.05 ? 22  PRO E O   1 
ATOM   11833 C CB  . PRO E 2 22  ? 12.262  -16.824 68.773  1.00 122.80 ? 22  PRO E CB  1 
ATOM   11834 C CG  . PRO E 2 22  ? 11.640  -15.526 69.175  1.00 123.87 ? 22  PRO E CG  1 
ATOM   11835 C CD  . PRO E 2 22  ? 11.456  -14.651 67.971  1.00 120.48 ? 22  PRO E CD  1 
ATOM   11836 N N   . LYS E 2 23  ? 11.434  -19.065 66.882  1.00 112.09 ? 23  LYS E N   1 
ATOM   11837 C CA  . LYS E 2 23  ? 10.553  -20.096 66.334  1.00 112.10 ? 23  LYS E CA  1 
ATOM   11838 C C   . LYS E 2 23  ? 9.081   -19.892 66.675  1.00 103.94 ? 23  LYS E C   1 
ATOM   11839 O O   . LYS E 2 23  ? 8.248   -19.963 65.758  1.00 102.46 ? 23  LYS E O   1 
ATOM   11840 C CB  . LYS E 2 23  ? 11.029  -21.480 66.801  1.00 117.46 ? 23  LYS E CB  1 
ATOM   11841 C CG  . LYS E 2 23  ? 10.125  -22.618 66.349  1.00 112.00 ? 23  LYS E CG  1 
ATOM   11842 C CD  . LYS E 2 23  ? 10.729  -23.978 66.666  1.00 113.16 ? 23  LYS E CD  1 
ATOM   11843 C CE  . LYS E 2 23  ? 11.032  -24.120 68.151  1.00 117.17 ? 23  LYS E CE  1 
ATOM   11844 N NZ  . LYS E 2 23  ? 11.572  -25.468 68.488  1.00 114.98 ? 23  LYS E NZ  1 
ATOM   11845 N N   . PRO E 2 24  ? 8.684   -19.644 67.929  1.00 105.76 ? 24  PRO E N   1 
ATOM   11846 C CA  . PRO E 2 24  ? 7.249   -19.520 68.220  1.00 109.81 ? 24  PRO E CA  1 
ATOM   11847 C C   . PRO E 2 24  ? 6.639   -18.201 67.779  1.00 112.70 ? 24  PRO E C   1 
ATOM   11848 O O   . PRO E 2 24  ? 5.410   -18.060 67.840  1.00 118.19 ? 24  PRO E O   1 
ATOM   11849 C CB  . PRO E 2 24  ? 7.194   -19.664 69.746  1.00 119.70 ? 24  PRO E CB  1 
ATOM   11850 C CG  . PRO E 2 24  ? 8.487   -19.114 70.201  1.00 109.37 ? 24  PRO E CG  1 
ATOM   11851 C CD  . PRO E 2 24  ? 9.490   -19.524 69.159  1.00 107.72 ? 24  PRO E CD  1 
ATOM   11852 N N   . LEU E 2 25  ? 7.441   -17.239 67.330  1.00 103.77 ? 25  LEU E N   1 
ATOM   11853 C CA  . LEU E 2 25  ? 6.931   -15.943 66.908  1.00 103.72 ? 25  LEU E CA  1 
ATOM   11854 C C   . LEU E 2 25  ? 6.734   -15.863 65.400  1.00 103.29 ? 25  LEU E C   1 
ATOM   11855 O O   . LEU E 2 25  ? 6.431   -14.785 64.879  1.00 103.80 ? 25  LEU E O   1 
ATOM   11856 C CB  . LEU E 2 25  ? 7.855   -14.819 67.386  1.00 107.85 ? 25  LEU E CB  1 
ATOM   11857 C CG  . LEU E 2 25  ? 7.816   -14.544 68.892  1.00 109.94 ? 25  LEU E CG  1 
ATOM   11858 C CD1 . LEU E 2 25  ? 8.527   -13.243 69.242  1.00 120.38 ? 25  LEU E CD1 1 
ATOM   11859 C CD2 . LEU E 2 25  ? 6.386   -14.533 69.418  1.00 116.16 ? 25  LEU E CD2 1 
ATOM   11860 N N   . VAL E 2 26  ? 6.904   -16.974 64.690  1.00 101.80 ? 26  VAL E N   1 
ATOM   11861 C CA  . VAL E 2 26  ? 6.674   -17.007 63.250  1.00 100.99 ? 26  VAL E CA  1 
ATOM   11862 C C   . VAL E 2 26  ? 5.175   -17.074 62.995  1.00 105.86 ? 26  VAL E C   1 
ATOM   11863 O O   . VAL E 2 26  ? 4.480   -17.945 63.532  1.00 108.89 ? 26  VAL E O   1 
ATOM   11864 C CB  . VAL E 2 26  ? 7.399   -18.200 62.608  1.00 99.79  ? 26  VAL E CB  1 
ATOM   11865 C CG1 . VAL E 2 26  ? 7.054   -18.295 61.131  1.00 106.51 ? 26  VAL E CG1 1 
ATOM   11866 C CG2 . VAL E 2 26  ? 8.902   -18.075 62.806  1.00 98.03  ? 26  VAL E CG2 1 
ATOM   11867 N N   . ASP E 2 27  ? 4.669   -16.147 62.185  1.00 106.40 ? 27  ASP E N   1 
ATOM   11868 C CA  . ASP E 2 27  ? 3.249   -16.126 61.857  1.00 108.61 ? 27  ASP E CA  1 
ATOM   11869 C C   . ASP E 2 27  ? 2.887   -17.347 61.022  1.00 107.39 ? 27  ASP E C   1 
ATOM   11870 O O   . ASP E 2 27  ? 3.370   -17.499 59.896  1.00 105.17 ? 27  ASP E O   1 
ATOM   11871 C CB  . ASP E 2 27  ? 2.903   -14.845 61.102  1.00 109.81 ? 27  ASP E CB  1 
ATOM   11872 C CG  . ASP E 2 27  ? 2.937   -13.621 61.988  1.00 113.81 ? 27  ASP E CG  1 
ATOM   11873 O OD1 . ASP E 2 27  ? 3.481   -13.710 63.108  1.00 114.39 ? 27  ASP E OD1 1 
ATOM   11874 O OD2 . ASP E 2 27  ? 2.421   -12.568 61.562  1.00 116.50 ? 27  ASP E OD2 1 
ATOM   11875 N N   . PHE E 2 28  ? 2.040   -18.215 61.569  1.00 113.87 ? 28  PHE E N   1 
ATOM   11876 C CA  . PHE E 2 28  ? 1.503   -19.356 60.837  1.00 117.02 ? 28  PHE E CA  1 
ATOM   11877 C C   . PHE E 2 28  ? 0.001   -19.174 60.672  1.00 120.81 ? 28  PHE E C   1 
ATOM   11878 O O   . PHE E 2 28  ? -0.738  -19.187 61.661  1.00 121.10 ? 28  PHE E O   1 
ATOM   11879 C CB  . PHE E 2 28  ? 1.804   -20.669 61.556  1.00 119.04 ? 28  PHE E CB  1 
ATOM   11880 C CG  . PHE E 2 28  ? 1.135   -21.861 60.934  1.00 118.62 ? 28  PHE E CG  1 
ATOM   11881 C CD1 . PHE E 2 28  ? 0.053   -22.471 61.548  1.00 120.76 ? 28  PHE E CD1 1 
ATOM   11882 C CD2 . PHE E 2 28  ? 1.577   -22.355 59.720  1.00 121.71 ? 28  PHE E CD2 1 
ATOM   11883 C CE1 . PHE E 2 28  ? -0.565  -23.563 60.965  1.00 120.41 ? 28  PHE E CE1 1 
ATOM   11884 C CE2 . PHE E 2 28  ? 0.965   -23.445 59.134  1.00 125.92 ? 28  PHE E CE2 1 
ATOM   11885 C CZ  . PHE E 2 28  ? -0.108  -24.050 59.758  1.00 122.87 ? 28  PHE E CZ  1 
ATOM   11886 N N   . ALA E 2 29  ? -0.446  -19.043 59.425  1.00 133.43 ? 29  ALA E N   1 
ATOM   11887 C CA  . ALA E 2 29  ? -1.844  -18.754 59.112  1.00 132.06 ? 29  ALA E CA  1 
ATOM   11888 C C   . ALA E 2 29  ? -2.329  -17.531 59.893  1.00 132.71 ? 29  ALA E C   1 
ATOM   11889 O O   . ALA E 2 29  ? -3.220  -17.613 60.741  1.00 133.12 ? 29  ALA E O   1 
ATOM   11890 C CB  . ALA E 2 29  ? -2.732  -19.973 59.380  1.00 131.08 ? 29  ALA E CB  1 
ATOM   11891 N N   . ASN E 2 30  ? -1.676  -16.397 59.614  1.00 114.13 ? 30  ASN E N   1 
ATOM   11892 C CA  . ASN E 2 30  ? -1.975  -15.089 60.196  1.00 110.72 ? 30  ASN E CA  1 
ATOM   11893 C C   . ASN E 2 30  ? -1.464  -14.975 61.625  1.00 112.27 ? 30  ASN E C   1 
ATOM   11894 O O   . ASN E 2 30  ? -0.846  -13.970 61.993  1.00 109.38 ? 30  ASN E O   1 
ATOM   11895 C CB  . ASN E 2 30  ? -3.477  -14.788 60.159  1.00 113.50 ? 30  ASN E CB  1 
ATOM   11896 C CG  . ASN E 2 30  ? -3.970  -14.438 58.773  1.00 115.17 ? 30  ASN E CG  1 
ATOM   11897 O OD1 . ASN E 2 30  ? -4.155  -13.266 58.452  1.00 114.89 ? 30  ASN E OD1 1 
ATOM   11898 N ND2 . ASN E 2 30  ? -4.182  -15.450 57.942  1.00 116.29 ? 30  ASN E ND2 1 
ATOM   11899 N N   . LYS E 2 31  ? -1.709  -15.979 62.420  1.00 115.89 ? 31  LYS E N   1 
ATOM   11900 C CA  . LYS E 2 31  ? -1.385  -15.926 63.834  1.00 117.57 ? 31  LYS E CA  1 
ATOM   11901 C C   . LYS E 2 31  ? -0.026  -16.559 64.104  1.00 117.08 ? 31  LYS E C   1 
ATOM   11902 O O   . LYS E 2 31  ? 0.374   -17.504 63.419  1.00 115.84 ? 31  LYS E O   1 
ATOM   11903 C CB  . LYS E 2 31  ? -2.464  -16.649 64.645  1.00 119.45 ? 31  LYS E CB  1 
ATOM   11904 C CG  . LYS E 2 31  ? -3.779  -15.889 64.681  1.00 116.04 ? 31  LYS E CG  1 
ATOM   11905 C CD  . LYS E 2 31  ? -4.960  -16.817 64.893  1.00 114.23 ? 31  LYS E CD  1 
ATOM   11906 C CE  . LYS E 2 31  ? -6.263  -16.118 64.532  1.00 114.34 ? 31  LYS E CE  1 
ATOM   11907 N NZ  . LYS E 2 31  ? -7.323  -17.077 64.117  1.00 118.10 ? 31  LYS E NZ  1 
ATOM   11908 N N   . PRO E 2 32  ? 0.715   -16.038 65.080  1.00 118.42 ? 32  PRO E N   1 
ATOM   11909 C CA  . PRO E 2 32  ? 1.977   -16.676 65.466  1.00 120.10 ? 32  PRO E CA  1 
ATOM   11910 C C   . PRO E 2 32  ? 1.757   -18.116 65.904  1.00 133.07 ? 32  PRO E C   1 
ATOM   11911 O O   . PRO E 2 32  ? 0.669   -18.507 66.332  1.00 141.41 ? 32  PRO E O   1 
ATOM   11912 C CB  . PRO E 2 32  ? 2.476   -15.807 66.626  1.00 122.00 ? 32  PRO E CB  1 
ATOM   11913 C CG  . PRO E 2 32  ? 1.835   -14.478 66.398  1.00 119.37 ? 32  PRO E CG  1 
ATOM   11914 C CD  . PRO E 2 32  ? 0.484   -14.779 65.809  1.00 122.62 ? 32  PRO E CD  1 
ATOM   11915 N N   . MET E 2 33  ? 2.820   -18.914 65.782  1.00 130.10 ? 33  MET E N   1 
ATOM   11916 C CA  . MET E 2 33  ? 2.714   -20.338 66.079  1.00 136.20 ? 33  MET E CA  1 
ATOM   11917 C C   . MET E 2 33  ? 2.351   -20.594 67.535  1.00 157.71 ? 33  MET E C   1 
ATOM   11918 O O   . MET E 2 33  ? 1.767   -21.636 67.853  1.00 168.04 ? 33  MET E O   1 
ATOM   11919 C CB  . MET E 2 33  ? 4.025   -21.045 65.737  1.00 126.03 ? 33  MET E CB  1 
ATOM   11920 C CG  . MET E 2 33  ? 3.989   -21.841 64.447  1.00 127.09 ? 33  MET E CG  1 
ATOM   11921 S SD  . MET E 2 33  ? 2.628   -23.019 64.460  1.00 127.70 ? 33  MET E SD  1 
ATOM   11922 C CE  . MET E 2 33  ? 3.078   -24.044 65.859  1.00 131.75 ? 33  MET E CE  1 
ATOM   11923 N N   . ILE E 2 34  ? 2.689   -19.667 68.430  1.00 184.29 ? 34  ILE E N   1 
ATOM   11924 C CA  . ILE E 2 34  ? 2.426   -19.886 69.848  1.00 187.67 ? 34  ILE E CA  1 
ATOM   11925 C C   . ILE E 2 34  ? 0.944   -19.705 70.185  1.00 195.78 ? 34  ILE E C   1 
ATOM   11926 O O   . ILE E 2 34  ? 0.447   -20.305 71.144  1.00 212.90 ? 34  ILE E O   1 
ATOM   11927 C CB  . ILE E 2 34  ? 3.318   -18.962 70.695  1.00 189.22 ? 34  ILE E CB  1 
ATOM   11928 C CG1 . ILE E 2 34  ? 3.336   -19.421 72.155  1.00 202.90 ? 34  ILE E CG1 1 
ATOM   11929 C CG2 . ILE E 2 34  ? 2.852   -17.517 70.591  1.00 187.71 ? 34  ILE E CG2 1 
ATOM   11930 C CD1 . ILE E 2 34  ? 4.004   -20.765 72.366  1.00 209.16 ? 34  ILE E CD1 1 
ATOM   11931 N N   . LEU E 2 35  ? 0.213   -18.893 69.418  1.00 179.53 ? 35  LEU E N   1 
ATOM   11932 C CA  . LEU E 2 35  ? -1.188  -18.622 69.727  1.00 185.56 ? 35  LEU E CA  1 
ATOM   11933 C C   . LEU E 2 35  ? -2.126  -19.760 69.348  1.00 192.33 ? 35  LEU E C   1 
ATOM   11934 O O   . LEU E 2 35  ? -3.304  -19.717 69.723  1.00 196.43 ? 35  LEU E O   1 
ATOM   11935 C CB  . LEU E 2 35  ? -1.648  -17.340 69.026  1.00 181.01 ? 35  LEU E CB  1 
ATOM   11936 C CG  . LEU E 2 35  ? -0.967  -16.038 69.446  1.00 182.04 ? 35  LEU E CG  1 
ATOM   11937 C CD1 . LEU E 2 35  ? -1.682  -14.842 68.836  1.00 181.34 ? 35  LEU E CD1 1 
ATOM   11938 C CD2 . LEU E 2 35  ? -0.930  -15.922 70.962  1.00 192.80 ? 35  LEU E CD2 1 
ATOM   11939 N N   . HIS E 2 36  ? -1.648  -20.767 68.616  1.00 193.62 ? 36  HIS E N   1 
ATOM   11940 C CA  . HIS E 2 36  ? -2.539  -21.835 68.176  1.00 196.44 ? 36  HIS E CA  1 
ATOM   11941 C C   . HIS E 2 36  ? -2.934  -22.760 69.321  1.00 223.15 ? 36  HIS E C   1 
ATOM   11942 O O   . HIS E 2 36  ? -4.009  -23.366 69.275  1.00 217.46 ? 36  HIS E O   1 
ATOM   11943 C CB  . HIS E 2 36  ? -1.887  -22.616 67.037  1.00 178.01 ? 36  HIS E CB  1 
ATOM   11944 C CG  . HIS E 2 36  ? -1.736  -21.820 65.778  1.00 154.63 ? 36  HIS E CG  1 
ATOM   11945 N ND1 . HIS E 2 36  ? -0.687  -20.950 65.571  1.00 144.43 ? 36  HIS E ND1 1 
ATOM   11946 C CD2 . HIS E 2 36  ? -2.507  -21.752 64.666  1.00 139.24 ? 36  HIS E CD2 1 
ATOM   11947 C CE1 . HIS E 2 36  ? -0.815  -20.385 64.384  1.00 133.37 ? 36  HIS E CE1 1 
ATOM   11948 N NE2 . HIS E 2 36  ? -1.910  -20.854 63.814  1.00 133.23 ? 36  HIS E NE2 1 
ATOM   11949 N N   . GLN E 2 37  ? -2.090  -22.900 70.344  1.00 289.28 ? 37  GLN E N   1 
ATOM   11950 C CA  . GLN E 2 37  ? -2.420  -23.751 71.477  1.00 290.29 ? 37  GLN E CA  1 
ATOM   11951 C C   . GLN E 2 37  ? -2.622  -22.993 72.783  1.00 290.94 ? 37  GLN E C   1 
ATOM   11952 O O   . GLN E 2 37  ? -3.107  -23.590 73.751  1.00 291.40 ? 37  GLN E O   1 
ATOM   11953 C CB  . GLN E 2 37  ? -1.342  -24.829 71.679  1.00 291.57 ? 37  GLN E CB  1 
ATOM   11954 C CG  . GLN E 2 37  ? -0.043  -24.347 72.302  1.00 292.67 ? 37  GLN E CG  1 
ATOM   11955 C CD  . GLN E 2 37  ? 0.769   -23.478 71.365  1.00 292.22 ? 37  GLN E CD  1 
ATOM   11956 O OE1 . GLN E 2 37  ? 1.031   -23.852 70.222  1.00 291.06 ? 37  GLN E OE1 1 
ATOM   11957 N NE2 . GLN E 2 37  ? 1.190   -22.320 71.853  1.00 292.92 ? 37  GLN E NE2 1 
ATOM   11958 N N   . ILE E 2 38  ? -2.281  -21.704 72.842  1.00 236.25 ? 38  ILE E N   1 
ATOM   11959 C CA  . ILE E 2 38  ? -2.583  -20.929 74.043  1.00 221.61 ? 38  ILE E CA  1 
ATOM   11960 C C   . ILE E 2 38  ? -4.078  -20.653 74.135  1.00 209.51 ? 38  ILE E C   1 
ATOM   11961 O O   . ILE E 2 38  ? -4.683  -20.790 75.206  1.00 202.06 ? 38  ILE E O   1 
ATOM   11962 C CB  . ILE E 2 38  ? -1.759  -19.629 74.072  1.00 208.74 ? 38  ILE E CB  1 
ATOM   11963 C CG1 . ILE E 2 38  ? -0.304  -19.931 74.423  1.00 207.07 ? 38  ILE E CG1 1 
ATOM   11964 C CG2 . ILE E 2 38  ? -2.349  -18.641 75.068  1.00 191.92 ? 38  ILE E CG2 1 
ATOM   11965 C CD1 . ILE E 2 38  ? 0.550   -18.694 74.583  1.00 194.47 ? 38  ILE E CD1 1 
ATOM   11966 N N   . GLU E 2 39  ? -4.700  -20.269 73.017  1.00 204.96 ? 39  GLU E N   1 
ATOM   11967 C CA  . GLU E 2 39  ? -6.149  -20.103 73.007  1.00 198.97 ? 39  GLU E CA  1 
ATOM   11968 C C   . GLU E 2 39  ? -6.854  -21.432 73.237  1.00 197.36 ? 39  GLU E C   1 
ATOM   11969 O O   . GLU E 2 39  ? -7.953  -21.465 73.804  1.00 189.48 ? 39  GLU E O   1 
ATOM   11970 C CB  . GLU E 2 39  ? -6.596  -19.470 71.686  1.00 200.15 ? 39  GLU E CB  1 
ATOM   11971 C CG  . GLU E 2 39  ? -8.040  -18.985 71.669  1.00 201.83 ? 39  GLU E CG  1 
ATOM   11972 C CD  . GLU E 2 39  ? -9.026  -20.072 71.282  1.00 204.02 ? 39  GLU E CD  1 
ATOM   11973 O OE1 . GLU E 2 39  ? -8.587  -21.127 70.776  1.00 204.27 ? 39  GLU E OE1 1 
ATOM   11974 O OE2 . GLU E 2 39  ? -10.242 -19.873 71.486  1.00 204.70 ? 39  GLU E OE2 1 
ATOM   11975 N N   . ALA E 2 40  ? -6.236  -22.538 72.814  1.00 203.45 ? 40  ALA E N   1 
ATOM   11976 C CA  . ALA E 2 40  ? -6.791  -23.852 73.114  1.00 200.62 ? 40  ALA E CA  1 
ATOM   11977 C C   . ALA E 2 40  ? -6.691  -24.165 74.601  1.00 193.35 ? 40  ALA E C   1 
ATOM   11978 O O   . ALA E 2 40  ? -7.544  -24.879 75.142  1.00 185.13 ? 40  ALA E O   1 
ATOM   11979 C CB  . ALA E 2 40  ? -6.079  -24.927 72.294  1.00 204.97 ? 40  ALA E CB  1 
ATOM   11980 N N   . LEU E 2 41  ? -5.662  -23.643 75.274  1.00 202.61 ? 41  LEU E N   1 
ATOM   11981 C CA  . LEU E 2 41  ? -5.578  -23.771 76.723  1.00 200.30 ? 41  LEU E CA  1 
ATOM   11982 C C   . LEU E 2 41  ? -6.587  -22.877 77.429  1.00 198.08 ? 41  LEU E C   1 
ATOM   11983 O O   . LEU E 2 41  ? -6.916  -23.131 78.592  1.00 197.56 ? 41  LEU E O   1 
ATOM   11984 C CB  . LEU E 2 41  ? -4.160  -23.451 77.205  1.00 202.17 ? 41  LEU E CB  1 
ATOM   11985 C CG  . LEU E 2 41  ? -3.089  -24.493 76.871  1.00 202.61 ? 41  LEU E CG  1 
ATOM   11986 C CD1 . LEU E 2 41  ? -1.706  -23.976 77.230  1.00 201.57 ? 41  LEU E CD1 1 
ATOM   11987 C CD2 . LEU E 2 41  ? -3.375  -25.805 77.586  1.00 202.74 ? 41  LEU E CD2 1 
ATOM   11988 N N   . LYS E 2 42  ? -7.084  -21.840 76.752  1.00 179.72 ? 42  LYS E N   1 
ATOM   11989 C CA  . LYS E 2 42  ? -8.172  -21.040 77.293  1.00 169.14 ? 42  LYS E CA  1 
ATOM   11990 C C   . LYS E 2 42  ? -9.516  -21.739 77.149  1.00 166.74 ? 42  LYS E C   1 
ATOM   11991 O O   . LYS E 2 42  ? -10.459 -21.399 77.870  1.00 163.21 ? 42  LYS E O   1 
ATOM   11992 C CB  . LYS E 2 42  ? -8.223  -19.678 76.595  1.00 167.13 ? 42  LYS E CB  1 
ATOM   11993 C CG  . LYS E 2 42  ? -8.090  -18.489 77.532  1.00 157.50 ? 42  LYS E CG  1 
ATOM   11994 C CD  . LYS E 2 42  ? -9.226  -18.443 78.538  1.00 155.59 ? 42  LYS E CD  1 
ATOM   11995 C CE  . LYS E 2 42  ? -9.034  -17.314 79.537  1.00 152.90 ? 42  LYS E CE  1 
ATOM   11996 N NZ  . LYS E 2 42  ? -7.814  -17.506 80.368  1.00 153.12 ? 42  LYS E NZ  1 
ATOM   11997 N N   . ALA E 2 43  ? -9.623  -22.701 76.230  1.00 168.24 ? 43  ALA E N   1 
ATOM   11998 C CA  . ALA E 2 43  ? -10.851 -23.478 76.109  1.00 162.56 ? 43  ALA E CA  1 
ATOM   11999 C C   . ALA E 2 43  ? -11.056 -24.390 77.313  1.00 164.59 ? 43  ALA E C   1 
ATOM   12000 O O   . ALA E 2 43  ? -12.199 -24.745 77.631  1.00 163.88 ? 43  ALA E O   1 
ATOM   12001 C CB  . ALA E 2 43  ? -10.835 -24.298 74.817  1.00 158.74 ? 43  ALA E CB  1 
ATOM   12002 N N   . VAL E 2 44  ? -9.973  -24.783 77.986  1.00 166.21 ? 44  VAL E N   1 
ATOM   12003 C CA  . VAL E 2 44  ? -10.061 -25.587 79.201  1.00 167.07 ? 44  VAL E CA  1 
ATOM   12004 C C   . VAL E 2 44  ? -9.819  -24.758 80.459  1.00 165.64 ? 44  VAL E C   1 
ATOM   12005 O O   . VAL E 2 44  ? -9.681  -25.321 81.551  1.00 165.42 ? 44  VAL E O   1 
ATOM   12006 C CB  . VAL E 2 44  ? -9.102  -26.783 79.141  1.00 165.58 ? 44  VAL E CB  1 
ATOM   12007 C CG1 . VAL E 2 44  ? -9.583  -27.780 78.112  1.00 164.91 ? 44  VAL E CG1 1 
ATOM   12008 C CG2 . VAL E 2 44  ? -7.690  -26.315 78.814  1.00 167.62 ? 44  VAL E CG2 1 
ATOM   12009 N N   . GLY E 2 45  ? -9.763  -23.435 80.335  1.00 168.09 ? 45  GLY E N   1 
ATOM   12010 C CA  . GLY E 2 45  ? -9.645  -22.575 81.495  1.00 165.73 ? 45  GLY E CA  1 
ATOM   12011 C C   . GLY E 2 45  ? -8.315  -22.663 82.215  1.00 163.31 ? 45  GLY E C   1 
ATOM   12012 O O   . GLY E 2 45  ? -8.272  -22.805 83.441  1.00 159.69 ? 45  GLY E O   1 
ATOM   12013 N N   . VAL E 2 46  ? -7.221  -22.586 81.466  1.00 165.90 ? 46  VAL E N   1 
ATOM   12014 C CA  . VAL E 2 46  ? -5.885  -22.552 82.047  1.00 166.00 ? 46  VAL E CA  1 
ATOM   12015 C C   . VAL E 2 46  ? -5.467  -21.097 82.203  1.00 165.25 ? 46  VAL E C   1 
ATOM   12016 O O   . VAL E 2 46  ? -5.491  -20.325 81.237  1.00 165.44 ? 46  VAL E O   1 
ATOM   12017 C CB  . VAL E 2 46  ? -4.883  -23.329 81.179  1.00 169.26 ? 46  VAL E CB  1 
ATOM   12018 C CG1 . VAL E 2 46  ? -3.472  -23.134 81.708  1.00 165.71 ? 46  VAL E CG1 1 
ATOM   12019 C CG2 . VAL E 2 46  ? -5.243  -24.806 81.153  1.00 171.99 ? 46  VAL E CG2 1 
ATOM   12020 N N   . ASP E 2 47  ? -5.083  -20.723 83.422  1.00 165.33 ? 47  ASP E N   1 
ATOM   12021 C CA  . ASP E 2 47  ? -4.757  -19.337 83.731  1.00 168.53 ? 47  ASP E CA  1 
ATOM   12022 C C   . ASP E 2 47  ? -3.291  -19.003 83.471  1.00 169.42 ? 47  ASP E C   1 
ATOM   12023 O O   . ASP E 2 47  ? -2.991  -17.954 82.893  1.00 171.95 ? 47  ASP E O   1 
ATOM   12024 C CB  . ASP E 2 47  ? -5.111  -19.031 85.189  1.00 171.98 ? 47  ASP E CB  1 
ATOM   12025 C CG  . ASP E 2 47  ? -5.600  -20.257 85.944  1.00 171.39 ? 47  ASP E CG  1 
ATOM   12026 O OD1 . ASP E 2 47  ? -6.300  -21.097 85.340  1.00 169.99 ? 47  ASP E OD1 1 
ATOM   12027 O OD2 . ASP E 2 47  ? -5.281  -20.379 87.146  1.00 168.88 ? 47  ASP E OD2 1 
ATOM   12028 N N   . GLU E 2 48  ? -2.371  -19.871 83.883  1.00 169.50 ? 48  GLU E N   1 
ATOM   12029 C CA  . GLU E 2 48  ? -0.943  -19.609 83.780  1.00 169.81 ? 48  GLU E CA  1 
ATOM   12030 C C   . GLU E 2 48  ? -0.300  -20.613 82.834  1.00 166.38 ? 48  GLU E C   1 
ATOM   12031 O O   . GLU E 2 48  ? -0.645  -21.799 82.844  1.00 166.57 ? 48  GLU E O   1 
ATOM   12032 C CB  . GLU E 2 48  ? -0.267  -19.675 85.154  1.00 165.07 ? 48  GLU E CB  1 
ATOM   12033 N N   . VAL E 2 49  ? 0.638   -20.133 82.019  1.00 175.19 ? 49  VAL E N   1 
ATOM   12034 C CA  . VAL E 2 49  ? 1.352   -20.962 81.052  1.00 176.63 ? 49  VAL E CA  1 
ATOM   12035 C C   . VAL E 2 49  ? 2.831   -20.606 81.108  1.00 186.31 ? 49  VAL E C   1 
ATOM   12036 O O   . VAL E 2 49  ? 3.193   -19.425 81.073  1.00 181.40 ? 49  VAL E O   1 
ATOM   12037 C CB  . VAL E 2 49  ? 0.812   -20.781 79.619  1.00 169.58 ? 49  VAL E CB  1 
ATOM   12038 C CG1 . VAL E 2 49  ? 1.614   -21.628 78.646  1.00 175.50 ? 49  VAL E CG1 1 
ATOM   12039 C CG2 . VAL E 2 49  ? -0.665  -21.144 79.549  1.00 165.82 ? 49  VAL E CG2 1 
ATOM   12040 N N   . VAL E 2 50  ? 3.683   -21.626 81.198  1.00 219.29 ? 50  VAL E N   1 
ATOM   12041 C CA  . VAL E 2 50  ? 5.129   -21.449 81.269  1.00 219.80 ? 50  VAL E CA  1 
ATOM   12042 C C   . VAL E 2 50  ? 5.751   -21.979 79.983  1.00 219.56 ? 50  VAL E C   1 
ATOM   12043 O O   . VAL E 2 50  ? 5.268   -22.950 79.388  1.00 219.14 ? 50  VAL E O   1 
ATOM   12044 C CB  . VAL E 2 50  ? 5.723   -22.150 82.508  1.00 220.37 ? 50  VAL E CB  1 
ATOM   12045 C CG1 . VAL E 2 50  ? 7.199   -21.810 82.670  1.00 220.59 ? 50  VAL E CG1 1 
ATOM   12046 C CG2 . VAL E 2 50  ? 4.939   -21.770 83.756  1.00 220.77 ? 50  VAL E CG2 1 
ATOM   12047 N N   . LEU E 2 51  ? 6.826   -21.323 79.546  1.00 206.36 ? 51  LEU E N   1 
ATOM   12048 C CA  . LEU E 2 51  ? 7.527   -21.672 78.316  1.00 206.13 ? 51  LEU E CA  1 
ATOM   12049 C C   . LEU E 2 51  ? 8.909   -22.213 78.657  1.00 206.20 ? 51  LEU E C   1 
ATOM   12050 O O   . LEU E 2 51  ? 9.713   -21.520 79.291  1.00 206.61 ? 51  LEU E O   1 
ATOM   12051 C CB  . LEU E 2 51  ? 7.639   -20.463 77.387  1.00 205.73 ? 51  LEU E CB  1 
ATOM   12052 C CG  . LEU E 2 51  ? 6.321   -19.830 76.942  1.00 205.61 ? 51  LEU E CG  1 
ATOM   12053 C CD1 . LEU E 2 51  ? 6.592   -18.632 76.051  1.00 205.14 ? 51  LEU E CD1 1 
ATOM   12054 C CD2 . LEU E 2 51  ? 5.458   -20.856 76.224  1.00 204.73 ? 51  LEU E CD2 1 
ATOM   12055 N N   . ALA E 2 52  ? 9.178   -23.449 78.238  1.00 174.26 ? 52  ALA E N   1 
ATOM   12056 C CA  . ALA E 2 52  ? 10.475  -24.088 78.468  1.00 163.65 ? 52  ALA E CA  1 
ATOM   12057 C C   . ALA E 2 52  ? 11.408  -23.801 77.289  1.00 150.06 ? 52  ALA E C   1 
ATOM   12058 O O   . ALA E 2 52  ? 11.716  -24.659 76.460  1.00 145.02 ? 52  ALA E O   1 
ATOM   12059 C CB  . ALA E 2 52  ? 10.297  -25.581 78.699  1.00 165.42 ? 52  ALA E CB  1 
ATOM   12060 N N   . ILE E 2 53  ? 11.857  -22.549 77.231  1.00 148.73 ? 53  ILE E N   1 
ATOM   12061 C CA  . ILE E 2 53  ? 12.756  -22.083 76.181  1.00 144.75 ? 53  ILE E CA  1 
ATOM   12062 C C   . ILE E 2 53  ? 14.192  -22.371 76.591  1.00 142.77 ? 53  ILE E C   1 
ATOM   12063 O O   . ILE E 2 53  ? 14.461  -22.729 77.741  1.00 149.34 ? 53  ILE E O   1 
ATOM   12064 C CB  . ILE E 2 53  ? 12.565  -20.580 75.917  1.00 146.36 ? 53  ILE E CB  1 
ATOM   12065 C CG1 . ILE E 2 53  ? 13.044  -19.784 77.133  1.00 147.68 ? 53  ILE E CG1 1 
ATOM   12066 C CG2 . ILE E 2 53  ? 11.109  -20.278 75.613  1.00 153.07 ? 53  ILE E CG2 1 
ATOM   12067 C CD1 . ILE E 2 53  ? 12.928  -18.291 76.986  1.00 152.23 ? 53  ILE E CD1 1 
ATOM   12068 N N   . ASN E 2 54  ? 15.128  -22.212 75.656  1.00 142.90 ? 54  ASN E N   1 
ATOM   12069 C CA  . ASN E 2 54  ? 16.545  -22.337 75.960  1.00 142.00 ? 54  ASN E CA  1 
ATOM   12070 C C   . ASN E 2 54  ? 17.328  -21.055 75.728  1.00 142.41 ? 54  ASN E C   1 
ATOM   12071 O O   . ASN E 2 54  ? 18.419  -20.909 76.289  1.00 143.40 ? 54  ASN E O   1 
ATOM   12072 C CB  . ASN E 2 54  ? 17.178  -23.466 75.131  1.00 142.03 ? 54  ASN E CB  1 
ATOM   12073 C CG  . ASN E 2 54  ? 18.575  -23.814 75.597  1.00 142.50 ? 54  ASN E CG  1 
ATOM   12074 O OD1 . ASN E 2 54  ? 18.751  -24.490 76.610  1.00 147.78 ? 54  ASN E OD1 1 
ATOM   12075 N ND2 . ASN E 2 54  ? 19.578  -23.352 74.860  1.00 138.34 ? 54  ASN E ND2 1 
ATOM   12076 N N   . TYR E 2 55  ? 16.800  -20.127 74.938  1.00 141.66 ? 55  TYR E N   1 
ATOM   12077 C CA  . TYR E 2 55  ? 17.430  -18.847 74.667  1.00 144.11 ? 55  TYR E CA  1 
ATOM   12078 C C   . TYR E 2 55  ? 16.943  -17.797 75.664  1.00 147.23 ? 55  TYR E C   1 
ATOM   12079 O O   . TYR E 2 55  ? 16.147  -18.076 76.563  1.00 148.76 ? 55  TYR E O   1 
ATOM   12080 C CB  . TYR E 2 55  ? 17.129  -18.418 73.232  1.00 144.41 ? 55  TYR E CB  1 
ATOM   12081 C CG  . TYR E 2 55  ? 15.648  -18.272 72.965  1.00 147.50 ? 55  TYR E CG  1 
ATOM   12082 C CD1 . TYR E 2 55  ? 14.876  -19.368 72.599  1.00 147.40 ? 55  TYR E CD1 1 
ATOM   12083 C CD2 . TYR E 2 55  ? 15.019  -17.042 73.087  1.00 150.06 ? 55  TYR E CD2 1 
ATOM   12084 C CE1 . TYR E 2 55  ? 13.521  -19.241 72.363  1.00 148.22 ? 55  TYR E CE1 1 
ATOM   12085 C CE2 . TYR E 2 55  ? 13.665  -16.904 72.853  1.00 148.99 ? 55  TYR E CE2 1 
ATOM   12086 C CZ  . TYR E 2 55  ? 12.920  -18.006 72.490  1.00 146.90 ? 55  TYR E CZ  1 
ATOM   12087 O OH  . TYR E 2 55  ? 11.571  -17.873 72.254  1.00 141.35 ? 55  TYR E OH  1 
ATOM   12088 N N   . GLN E 2 56  ? 17.431  -16.571 75.506  1.00 150.78 ? 56  GLN E N   1 
ATOM   12089 C CA  . GLN E 2 56  ? 17.029  -15.483 76.392  1.00 155.84 ? 56  GLN E CA  1 
ATOM   12090 C C   . GLN E 2 56  ? 15.696  -14.897 75.930  1.00 160.98 ? 56  GLN E C   1 
ATOM   12091 O O   . GLN E 2 56  ? 15.543  -14.567 74.750  1.00 157.65 ? 56  GLN E O   1 
ATOM   12092 C CB  . GLN E 2 56  ? 18.103  -14.390 76.448  1.00 157.58 ? 56  GLN E CB  1 
ATOM   12093 C CG  . GLN E 2 56  ? 18.373  -13.635 75.142  1.00 158.89 ? 56  GLN E CG  1 
ATOM   12094 C CD  . GLN E 2 56  ? 19.000  -14.497 74.062  1.00 152.17 ? 56  GLN E CD  1 
ATOM   12095 O OE1 . GLN E 2 56  ? 19.609  -15.528 74.348  1.00 151.85 ? 56  GLN E OE1 1 
ATOM   12096 N NE2 . GLN E 2 56  ? 18.849  -14.077 72.811  1.00 144.81 ? 56  GLN E NE2 1 
ATOM   12097 N N   . PRO E 2 57  ? 14.708  -14.769 76.819  1.00 180.01 ? 57  PRO E N   1 
ATOM   12098 C CA  . PRO E 2 57  ? 13.406  -14.219 76.421  1.00 179.94 ? 57  PRO E CA  1 
ATOM   12099 C C   . PRO E 2 57  ? 13.380  -12.705 76.272  1.00 180.35 ? 57  PRO E C   1 
ATOM   12100 O O   . PRO E 2 57  ? 12.304  -12.150 76.021  1.00 180.14 ? 57  PRO E O   1 
ATOM   12101 C CB  . PRO E 2 57  ? 12.488  -14.673 77.564  1.00 180.24 ? 57  PRO E CB  1 
ATOM   12102 C CG  . PRO E 2 57  ? 13.384  -14.718 78.748  1.00 183.17 ? 57  PRO E CG  1 
ATOM   12103 C CD  . PRO E 2 57  ? 14.728  -15.178 78.235  1.00 180.70 ? 57  PRO E CD  1 
ATOM   12104 N N   . GLU E 2 58  ? 14.522  -12.026 76.416  1.00 174.46 ? 58  GLU E N   1 
ATOM   12105 C CA  . GLU E 2 58  ? 14.542  -10.566 76.385  1.00 173.60 ? 58  GLU E CA  1 
ATOM   12106 C C   . GLU E 2 58  ? 14.043  -10.009 75.059  1.00 172.72 ? 58  GLU E C   1 
ATOM   12107 O O   . GLU E 2 58  ? 13.643  -8.842  74.998  1.00 173.10 ? 58  GLU E O   1 
ATOM   12108 C CB  . GLU E 2 58  ? 15.959  -10.053 76.640  1.00 177.58 ? 58  GLU E CB  1 
ATOM   12109 C CG  . GLU E 2 58  ? 16.645  -10.652 77.852  1.00 183.17 ? 58  GLU E CG  1 
ATOM   12110 C CD  . GLU E 2 58  ? 18.130  -10.853 77.620  1.00 189.80 ? 58  GLU E CD  1 
ATOM   12111 O OE1 . GLU E 2 58  ? 18.606  -10.525 76.513  1.00 187.56 ? 58  GLU E OE1 1 
ATOM   12112 O OE2 . GLU E 2 58  ? 18.822  -11.339 78.539  1.00 194.81 ? 58  GLU E OE2 1 
ATOM   12113 N N   . VAL E 2 59  ? 14.056  -10.816 74.000  1.00 153.30 ? 59  VAL E N   1 
ATOM   12114 C CA  . VAL E 2 59  ? 13.642  -10.342 72.687  1.00 149.25 ? 59  VAL E CA  1 
ATOM   12115 C C   . VAL E 2 59  ? 12.140  -10.468 72.476  1.00 148.48 ? 59  VAL E C   1 
ATOM   12116 O O   . VAL E 2 59  ? 11.593  -9.815  71.577  1.00 148.69 ? 59  VAL E O   1 
ATOM   12117 C CB  . VAL E 2 59  ? 14.384  -11.103 71.576  1.00 145.72 ? 59  VAL E CB  1 
ATOM   12118 C CG1 . VAL E 2 59  ? 15.878  -10.865 71.687  1.00 142.87 ? 59  VAL E CG1 1 
ATOM   12119 C CG2 . VAL E 2 59  ? 14.067  -12.589 71.649  1.00 144.83 ? 59  VAL E CG2 1 
ATOM   12120 N N   . MET E 2 60  ? 11.459  -11.291 73.272  1.00 143.97 ? 60  MET E N   1 
ATOM   12121 C CA  . MET E 2 60  ? 10.038  -11.553 73.091  1.00 143.41 ? 60  MET E CA  1 
ATOM   12122 C C   . MET E 2 60  ? 9.192   -11.120 74.283  1.00 142.34 ? 60  MET E C   1 
ATOM   12123 O O   . MET E 2 60  ? 8.005   -11.457 74.337  1.00 141.42 ? 60  MET E O   1 
ATOM   12124 C CB  . MET E 2 60  ? 9.823   -13.041 72.800  1.00 143.26 ? 60  MET E CB  1 
ATOM   12125 C CG  . MET E 2 60  ? 10.251  -13.953 73.933  1.00 147.84 ? 60  MET E CG  1 
ATOM   12126 S SD  . MET E 2 60  ? 10.208  -15.696 73.479  1.00 150.57 ? 60  MET E SD  1 
ATOM   12127 C CE  . MET E 2 60  ? 10.532  -16.460 75.063  1.00 160.24 ? 60  MET E CE  1 
ATOM   12128 N N   . LEU E 2 61  ? 9.766   -10.387 75.240  1.00 142.61 ? 61  LEU E N   1 
ATOM   12129 C CA  . LEU E 2 61  ? 8.986   -9.944  76.391  1.00 142.57 ? 61  LEU E CA  1 
ATOM   12130 C C   . LEU E 2 61  ? 7.859   -9.008  75.972  1.00 147.29 ? 61  LEU E C   1 
ATOM   12131 O O   . LEU E 2 61  ? 6.765   -9.043  76.549  1.00 154.81 ? 61  LEU E O   1 
ATOM   12132 C CB  . LEU E 2 61  ? 9.896   -9.269  77.417  1.00 140.53 ? 61  LEU E CB  1 
ATOM   12133 C CG  . LEU E 2 61  ? 10.798  -10.201 78.227  1.00 145.92 ? 61  LEU E CG  1 
ATOM   12134 C CD1 . LEU E 2 61  ? 11.624  -9.403  79.217  1.00 146.28 ? 61  LEU E CD1 1 
ATOM   12135 C CD2 . LEU E 2 61  ? 9.971   -11.259 78.946  1.00 145.30 ? 61  LEU E CD2 1 
ATOM   12136 N N   . ASN E 2 62  ? 8.105   -8.162  74.969  1.00 141.30 ? 62  ASN E N   1 
ATOM   12137 C CA  . ASN E 2 62  ? 7.071   -7.243  74.505  1.00 142.25 ? 62  ASN E CA  1 
ATOM   12138 C C   . ASN E 2 62  ? 5.926   -7.977  73.819  1.00 145.48 ? 62  ASN E C   1 
ATOM   12139 O O   . ASN E 2 62  ? 4.777   -7.527  73.888  1.00 147.01 ? 62  ASN E O   1 
ATOM   12140 C CB  . ASN E 2 62  ? 7.679   -6.200  73.570  1.00 143.95 ? 62  ASN E CB  1 
ATOM   12141 C CG  . ASN E 2 62  ? 8.471   -5.145  74.317  1.00 141.85 ? 62  ASN E CG  1 
ATOM   12142 O OD1 . ASN E 2 62  ? 8.134   -4.782  75.444  1.00 142.23 ? 62  ASN E OD1 1 
ATOM   12143 N ND2 . ASN E 2 62  ? 9.537   -4.655  73.697  1.00 138.79 ? 62  ASN E ND2 1 
ATOM   12144 N N   . PHE E 2 63  ? 6.214   -9.099  73.157  1.00 147.94 ? 63  PHE E N   1 
ATOM   12145 C CA  . PHE E 2 63  ? 5.156   -9.856  72.493  1.00 153.51 ? 63  PHE E CA  1 
ATOM   12146 C C   . PHE E 2 63  ? 4.311   -10.626 73.500  1.00 154.96 ? 63  PHE E C   1 
ATOM   12147 O O   . PHE E 2 63  ? 3.079   -10.639 73.405  1.00 159.88 ? 63  PHE E O   1 
ATOM   12148 C CB  . PHE E 2 63  ? 5.754   -10.816 71.464  1.00 152.02 ? 63  PHE E CB  1 
ATOM   12149 C CG  . PHE E 2 63  ? 6.309   -10.140 70.238  1.00 153.75 ? 63  PHE E CG  1 
ATOM   12150 C CD1 . PHE E 2 63  ? 5.522   -9.979  69.109  1.00 151.80 ? 63  PHE E CD1 1 
ATOM   12151 C CD2 . PHE E 2 63  ? 7.615   -9.678  70.209  1.00 155.12 ? 63  PHE E CD2 1 
ATOM   12152 C CE1 . PHE E 2 63  ? 6.024   -9.365  67.976  1.00 151.06 ? 63  PHE E CE1 1 
ATOM   12153 C CE2 . PHE E 2 63  ? 8.124   -9.062  69.077  1.00 153.96 ? 63  PHE E CE2 1 
ATOM   12154 C CZ  . PHE E 2 63  ? 7.327   -8.906  67.960  1.00 149.46 ? 63  PHE E CZ  1 
ATOM   12155 N N   . LEU E 2 64  ? 4.955   -11.279 74.468  1.00 154.22 ? 64  LEU E N   1 
ATOM   12156 C CA  . LEU E 2 64  ? 4.219   -12.054 75.460  1.00 161.36 ? 64  LEU E CA  1 
ATOM   12157 C C   . LEU E 2 64  ? 3.441   -11.161 76.419  1.00 170.36 ? 64  LEU E C   1 
ATOM   12158 O O   . LEU E 2 64  ? 2.431   -11.594 76.985  1.00 173.44 ? 64  LEU E O   1 
ATOM   12159 C CB  . LEU E 2 64  ? 5.185   -12.952 76.231  1.00 157.04 ? 64  LEU E CB  1 
ATOM   12160 C CG  . LEU E 2 64  ? 6.077   -13.830 75.344  1.00 151.65 ? 64  LEU E CG  1 
ATOM   12161 C CD1 . LEU E 2 64  ? 7.019   -14.662 76.188  1.00 148.94 ? 64  LEU E CD1 1 
ATOM   12162 C CD2 . LEU E 2 64  ? 5.244   -14.721 74.437  1.00 155.69 ? 64  LEU E CD2 1 
ATOM   12163 N N   . LYS E 2 65  ? 3.886   -9.917  76.613  1.00 190.76 ? 65  LYS E N   1 
ATOM   12164 C CA  . LYS E 2 65  ? 3.176   -9.018  77.517  1.00 191.74 ? 65  LYS E CA  1 
ATOM   12165 C C   . LYS E 2 65  ? 1.877   -8.508  76.902  1.00 190.64 ? 65  LYS E C   1 
ATOM   12166 O O   . LYS E 2 65  ? 0.935   -8.176  77.632  1.00 190.72 ? 65  LYS E O   1 
ATOM   12167 C CB  . LYS E 2 65  ? 4.079   -7.847  77.904  1.00 193.01 ? 65  LYS E CB  1 
ATOM   12168 C CG  . LYS E 2 65  ? 3.687   -7.153  79.194  1.00 195.65 ? 65  LYS E CG  1 
ATOM   12169 C CD  . LYS E 2 65  ? 4.731   -6.121  79.576  1.00 194.81 ? 65  LYS E CD  1 
ATOM   12170 C CE  . LYS E 2 65  ? 6.118   -6.745  79.609  1.00 194.95 ? 65  LYS E CE  1 
ATOM   12171 N NZ  . LYS E 2 65  ? 7.187   -5.748  79.885  1.00 195.97 ? 65  LYS E NZ  1 
ATOM   12172 N N   . ASP E 2 66  ? 1.802   -8.445  75.572  1.00 169.08 ? 66  ASP E N   1 
ATOM   12173 C CA  . ASP E 2 66  ? 0.593   -7.986  74.901  1.00 165.03 ? 66  ASP E CA  1 
ATOM   12174 C C   . ASP E 2 66  ? -0.458  -9.078  74.768  1.00 170.44 ? 66  ASP E C   1 
ATOM   12175 O O   . ASP E 2 66  ? -1.618  -8.769  74.474  1.00 167.48 ? 66  ASP E O   1 
ATOM   12176 C CB  . ASP E 2 66  ? 0.938   -7.437  73.516  1.00 154.63 ? 66  ASP E CB  1 
ATOM   12177 C CG  . ASP E 2 66  ? 1.853   -6.233  73.580  1.00 143.50 ? 66  ASP E CG  1 
ATOM   12178 O OD1 . ASP E 2 66  ? 1.809   -5.506  74.595  1.00 144.64 ? 66  ASP E OD1 1 
ATOM   12179 O OD2 . ASP E 2 66  ? 2.621   -6.016  72.621  1.00 138.62 ? 66  ASP E OD2 1 
ATOM   12180 N N   . PHE E 2 67  ? -0.082  -10.338 74.977  1.00 183.49 ? 67  PHE E N   1 
ATOM   12181 C CA  . PHE E 2 67  ? -1.018  -11.449 74.896  1.00 182.84 ? 67  PHE E CA  1 
ATOM   12182 C C   . PHE E 2 67  ? -1.621  -11.801 76.246  1.00 183.38 ? 67  PHE E C   1 
ATOM   12183 O O   . PHE E 2 67  ? -2.620  -12.526 76.294  1.00 182.63 ? 67  PHE E O   1 
ATOM   12184 C CB  . PHE E 2 67  ? -0.317  -12.681 74.318  1.00 183.57 ? 67  PHE E CB  1 
ATOM   12185 C CG  . PHE E 2 67  ? 0.228   -12.476 72.933  1.00 189.93 ? 67  PHE E CG  1 
ATOM   12186 C CD1 . PHE E 2 67  ? -0.339  -11.547 72.075  1.00 191.43 ? 67  PHE E CD1 1 
ATOM   12187 C CD2 . PHE E 2 67  ? 1.326   -13.199 72.498  1.00 190.02 ? 67  PHE E CD2 1 
ATOM   12188 C CE1 . PHE E 2 67  ? 0.171   -11.356 70.803  1.00 192.02 ? 67  PHE E CE1 1 
ATOM   12189 C CE2 . PHE E 2 67  ? 1.841   -13.012 71.231  1.00 189.23 ? 67  PHE E CE2 1 
ATOM   12190 C CZ  . PHE E 2 67  ? 1.262   -12.089 70.382  1.00 190.85 ? 67  PHE E CZ  1 
ATOM   12191 N N   . GLU E 2 68  ? -1.034  -11.305 77.338  1.00 171.00 ? 68  GLU E N   1 
ATOM   12192 C CA  . GLU E 2 68  ? -1.566  -11.596 78.663  1.00 168.69 ? 68  GLU E CA  1 
ATOM   12193 C C   . GLU E 2 68  ? -2.863  -10.841 78.918  1.00 163.22 ? 68  GLU E C   1 
ATOM   12194 O O   . GLU E 2 68  ? -3.739  -11.340 79.632  1.00 161.14 ? 68  GLU E O   1 
ATOM   12195 C CB  . GLU E 2 68  ? -0.528  -11.257 79.733  1.00 168.47 ? 68  GLU E CB  1 
ATOM   12196 C CG  . GLU E 2 68  ? 0.629   -12.243 79.806  1.00 171.30 ? 68  GLU E CG  1 
ATOM   12197 C CD  . GLU E 2 68  ? 1.555   -11.968 80.973  1.00 169.78 ? 68  GLU E CD  1 
ATOM   12198 O OE1 . GLU E 2 68  ? 2.023   -10.819 81.105  1.00 168.07 ? 68  GLU E OE1 1 
ATOM   12199 O OE2 . GLU E 2 68  ? 1.813   -12.903 81.759  1.00 176.62 ? 68  GLU E OE2 1 
ATOM   12200 N N   . THR E 2 69  ? -2.998  -9.642  78.357  1.00 159.07 ? 69  THR E N   1 
ATOM   12201 C CA  . THR E 2 69  ? -4.213  -8.855  78.527  1.00 155.56 ? 69  THR E CA  1 
ATOM   12202 C C   . THR E 2 69  ? -5.264  -9.172  77.470  1.00 158.92 ? 69  THR E C   1 
ATOM   12203 O O   . THR E 2 69  ? -6.460  -9.201  77.780  1.00 157.69 ? 69  THR E O   1 
ATOM   12204 C CB  . THR E 2 69  ? -3.883  -7.360  78.497  1.00 148.32 ? 69  THR E CB  1 
ATOM   12205 O OG1 . THR E 2 69  ? -2.676  -7.150  77.753  1.00 148.64 ? 69  THR E OG1 1 
ATOM   12206 C CG2 . THR E 2 69  ? -3.706  -6.828  79.910  1.00 141.59 ? 69  THR E CG2 1 
ATOM   12207 N N   . LYS E 2 70  ? -4.843  -9.398  76.222  1.00 156.37 ? 70  LYS E N   1 
ATOM   12208 C CA  . LYS E 2 70  ? -5.801  -9.721  75.168  1.00 157.18 ? 70  LYS E CA  1 
ATOM   12209 C C   . LYS E 2 70  ? -6.471  -11.066 75.420  1.00 158.01 ? 70  LYS E C   1 
ATOM   12210 O O   . LYS E 2 70  ? -7.676  -11.219 75.186  1.00 153.11 ? 70  LYS E O   1 
ATOM   12211 C CB  . LYS E 2 70  ? -5.110  -9.716  73.804  1.00 157.20 ? 70  LYS E CB  1 
ATOM   12212 C CG  . LYS E 2 70  ? -6.039  -10.078 72.654  1.00 160.78 ? 70  LYS E CG  1 
ATOM   12213 C CD  . LYS E 2 70  ? -5.288  -10.255 71.343  1.00 164.28 ? 70  LYS E CD  1 
ATOM   12214 C CE  . LYS E 2 70  ? -4.231  -11.344 71.446  1.00 168.31 ? 70  LYS E CE  1 
ATOM   12215 N NZ  . LYS E 2 70  ? -3.466  -11.500 70.175  1.00 171.09 ? 70  LYS E NZ  1 
ATOM   12216 N N   . LEU E 2 71  ? -5.713  -12.049 75.905  1.00 157.99 ? 71  LEU E N   1 
ATOM   12217 C CA  . LEU E 2 71  ? -6.236  -13.390 76.122  1.00 158.52 ? 71  LEU E CA  1 
ATOM   12218 C C   . LEU E 2 71  ? -6.561  -13.681 77.580  1.00 157.24 ? 71  LEU E C   1 
ATOM   12219 O O   . LEU E 2 71  ? -7.131  -14.740 77.867  1.00 157.20 ? 71  LEU E O   1 
ATOM   12220 C CB  . LEU E 2 71  ? -5.244  -14.439 75.604  1.00 157.54 ? 71  LEU E CB  1 
ATOM   12221 C CG  . LEU E 2 71  ? -4.888  -14.368 74.119  1.00 161.39 ? 71  LEU E CG  1 
ATOM   12222 C CD1 . LEU E 2 71  ? -3.842  -15.414 73.775  1.00 168.50 ? 71  LEU E CD1 1 
ATOM   12223 C CD2 . LEU E 2 71  ? -6.133  -14.552 73.264  1.00 160.97 ? 71  LEU E CD2 1 
ATOM   12224 N N   . GLU E 2 72  ? -6.222  -12.774 78.495  1.00 156.95 ? 72  GLU E N   1 
ATOM   12225 C CA  . GLU E 2 72  ? -6.447  -12.956 79.929  1.00 155.25 ? 72  GLU E CA  1 
ATOM   12226 C C   . GLU E 2 72  ? -5.807  -14.256 80.418  1.00 157.02 ? 72  GLU E C   1 
ATOM   12227 O O   . GLU E 2 72  ? -6.471  -15.164 80.921  1.00 155.77 ? 72  GLU E O   1 
ATOM   12228 C CB  . GLU E 2 72  ? -7.944  -12.914 80.248  1.00 155.09 ? 72  GLU E CB  1 
ATOM   12229 C CG  . GLU E 2 72  ? -8.562  -11.529 80.136  1.00 156.40 ? 72  GLU E CG  1 
ATOM   12230 C CD  . GLU E 2 72  ? -10.021 -11.506 80.551  1.00 157.95 ? 72  GLU E CD  1 
ATOM   12231 O OE1 . GLU E 2 72  ? -10.661 -12.580 80.536  1.00 153.09 ? 72  GLU E OE1 1 
ATOM   12232 O OE2 . GLU E 2 72  ? -10.531 -10.415 80.879  1.00 161.25 ? 72  GLU E OE2 1 
ATOM   12233 N N   . ILE E 2 73  ? -4.487  -14.322 80.267  1.00 166.57 ? 73  ILE E N   1 
ATOM   12234 C CA  . ILE E 2 73  ? -3.705  -15.502 80.617  1.00 173.49 ? 73  ILE E CA  1 
ATOM   12235 C C   . ILE E 2 73  ? -2.369  -15.038 81.175  1.00 184.25 ? 73  ILE E C   1 
ATOM   12236 O O   . ILE E 2 73  ? -1.768  -14.092 80.658  1.00 177.39 ? 73  ILE E O   1 
ATOM   12237 C CB  . ILE E 2 73  ? -3.505  -16.426 79.393  1.00 168.21 ? 73  ILE E CB  1 
ATOM   12238 C CG1 . ILE E 2 73  ? -4.722  -17.327 79.187  1.00 162.89 ? 73  ILE E CG1 1 
ATOM   12239 C CG2 . ILE E 2 73  ? -2.236  -17.260 79.529  1.00 168.44 ? 73  ILE E CG2 1 
ATOM   12240 C CD1 . ILE E 2 73  ? -4.543  -18.348 78.084  1.00 159.22 ? 73  ILE E CD1 1 
ATOM   12241 N N   . LYS E 2 74  ? -1.901  -15.704 82.227  1.00 229.61 ? 74  LYS E N   1 
ATOM   12242 C CA  . LYS E 2 74  ? -0.602  -15.399 82.813  1.00 230.70 ? 74  LYS E CA  1 
ATOM   12243 C C   . LYS E 2 74  ? 0.474   -16.148 82.038  1.00 230.16 ? 74  LYS E C   1 
ATOM   12244 O O   . LYS E 2 74  ? 0.415   -17.376 81.912  1.00 229.73 ? 74  LYS E O   1 
ATOM   12245 C CB  . LYS E 2 74  ? -0.569  -15.779 84.292  1.00 231.44 ? 74  LYS E CB  1 
ATOM   12246 C CG  . LYS E 2 74  ? 0.693   -15.341 85.011  1.00 232.64 ? 74  LYS E CG  1 
ATOM   12247 C CD  . LYS E 2 74  ? 0.836   -13.829 84.970  1.00 233.36 ? 74  LYS E CD  1 
ATOM   12248 C CE  . LYS E 2 74  ? 2.031   -13.357 85.779  1.00 234.70 ? 74  LYS E CE  1 
ATOM   12249 N NZ  . LYS E 2 74  ? 1.913   -13.758 87.208  1.00 241.21 ? 74  LYS E NZ  1 
ATOM   12250 N N   . ILE E 2 75  ? 1.451   -15.411 81.517  1.00 185.50 ? 75  ILE E N   1 
ATOM   12251 C CA  . ILE E 2 75  ? 2.507   -15.972 80.683  1.00 174.51 ? 75  ILE E CA  1 
ATOM   12252 C C   . ILE E 2 75  ? 3.849   -15.628 81.311  1.00 170.00 ? 75  ILE E C   1 
ATOM   12253 O O   . ILE E 2 75  ? 4.213   -14.448 81.405  1.00 170.20 ? 75  ILE E O   1 
ATOM   12254 C CB  . ILE E 2 75  ? 2.431   -15.451 79.240  1.00 171.34 ? 75  ILE E CB  1 
ATOM   12255 C CG1 . ILE E 2 75  ? 1.078   -15.802 78.616  1.00 175.40 ? 75  ILE E CG1 1 
ATOM   12256 C CG2 . ILE E 2 75  ? 3.569   -16.026 78.409  1.00 167.87 ? 75  ILE E CG2 1 
ATOM   12257 C CD1 . ILE E 2 75  ? 0.888   -15.259 77.219  1.00 174.49 ? 75  ILE E CD1 1 
ATOM   12258 N N   . THR E 2 76  ? 4.583   -16.654 81.734  1.00 167.90 ? 76  THR E N   1 
ATOM   12259 C CA  . THR E 2 76  ? 5.914   -16.491 82.299  1.00 160.91 ? 76  THR E CA  1 
ATOM   12260 C C   . THR E 2 76  ? 6.884   -17.423 81.590  1.00 158.88 ? 76  THR E C   1 
ATOM   12261 O O   . THR E 2 76  ? 6.497   -18.480 81.082  1.00 166.44 ? 76  THR E O   1 
ATOM   12262 C CB  . THR E 2 76  ? 5.933   -16.774 83.809  1.00 162.29 ? 76  THR E CB  1 
ATOM   12263 O OG1 . THR E 2 76  ? 5.407   -18.083 84.061  1.00 170.54 ? 76  THR E OG1 1 
ATOM   12264 C CG2 . THR E 2 76  ? 5.101   -15.744 84.558  1.00 167.62 ? 76  THR E CG2 1 
ATOM   12265 N N   . CYS E 2 77  ? 8.150   -17.022 81.561  1.00 147.57 ? 77  CYS E N   1 
ATOM   12266 C CA  . CYS E 2 77  ? 9.185   -17.756 80.852  1.00 154.93 ? 77  CYS E CA  1 
ATOM   12267 C C   . CYS E 2 77  ? 10.090  -18.496 81.827  1.00 148.70 ? 77  CYS E C   1 
ATOM   12268 O O   . CYS E 2 77  ? 10.232  -18.121 82.994  1.00 150.86 ? 77  CYS E O   1 
ATOM   12269 C CB  . CYS E 2 77  ? 10.025  -16.817 79.979  1.00 158.55 ? 77  CYS E CB  1 
ATOM   12270 S SG  . CYS E 2 77  ? 9.117   -16.023 78.641  1.00 170.43 ? 77  CYS E SG  1 
ATOM   12271 N N   . SER E 2 78  ? 10.703  -19.562 81.321  1.00 159.88 ? 78  SER E N   1 
ATOM   12272 C CA  . SER E 2 78  ? 11.712  -20.313 82.056  1.00 160.20 ? 78  SER E CA  1 
ATOM   12273 C C   . SER E 2 78  ? 12.858  -20.599 81.103  1.00 162.93 ? 78  SER E C   1 
ATOM   12274 O O   . SER E 2 78  ? 12.651  -21.216 80.054  1.00 164.60 ? 78  SER E O   1 
ATOM   12275 C CB  . SER E 2 78  ? 11.138  -21.615 82.622  1.00 163.87 ? 78  SER E CB  1 
ATOM   12276 O OG  . SER E 2 78  ? 10.809  -22.519 81.581  1.00 168.45 ? 78  SER E OG  1 
ATOM   12277 N N   . GLN E 2 79  ? 14.057  -20.159 81.465  1.00 157.70 ? 79  GLN E N   1 
ATOM   12278 C CA  . GLN E 2 79  ? 15.239  -20.321 80.630  1.00 157.22 ? 79  GLN E CA  1 
ATOM   12279 C C   . GLN E 2 79  ? 16.194  -21.275 81.324  1.00 160.10 ? 79  GLN E C   1 
ATOM   12280 O O   . GLN E 2 79  ? 16.583  -21.043 82.473  1.00 162.25 ? 79  GLN E O   1 
ATOM   12281 C CB  . GLN E 2 79  ? 15.932  -18.984 80.367  1.00 158.39 ? 79  GLN E CB  1 
ATOM   12282 C CG  . GLN E 2 79  ? 17.155  -19.107 79.469  1.00 156.33 ? 79  GLN E CG  1 
ATOM   12283 C CD  . GLN E 2 79  ? 17.891  -17.793 79.286  1.00 157.69 ? 79  GLN E CD  1 
ATOM   12284 O OE1 . GLN E 2 79  ? 17.523  -16.774 79.870  1.00 161.83 ? 79  GLN E OE1 1 
ATOM   12285 N NE2 . GLN E 2 79  ? 18.939  -17.811 78.470  1.00 157.38 ? 79  GLN E NE2 1 
ATOM   12286 N N   . GLU E 2 80  ? 16.564  -22.341 80.628  1.00 174.85 ? 80  GLU E N   1 
ATOM   12287 C CA  . GLU E 2 80  ? 17.518  -23.309 81.137  1.00 175.22 ? 80  GLU E CA  1 
ATOM   12288 C C   . GLU E 2 80  ? 18.886  -23.043 80.529  1.00 173.78 ? 80  GLU E C   1 
ATOM   12289 O O   . GLU E 2 80  ? 19.001  -22.594 79.385  1.00 173.65 ? 80  GLU E O   1 
ATOM   12290 C CB  . GLU E 2 80  ? 17.077  -24.742 80.825  1.00 176.68 ? 80  GLU E CB  1 
ATOM   12291 C CG  . GLU E 2 80  ? 15.863  -25.222 81.612  1.00 187.98 ? 80  GLU E CG  1 
ATOM   12292 C CD  . GLU E 2 80  ? 14.559  -24.633 81.111  1.00 187.27 ? 80  GLU E CD  1 
ATOM   12293 O OE1 . GLU E 2 80  ? 14.575  -23.943 80.073  1.00 178.99 ? 80  GLU E OE1 1 
ATOM   12294 O OE2 . GLU E 2 80  ? 13.516  -24.854 81.761  1.00 188.47 ? 80  GLU E OE2 1 
ATOM   12295 N N   . THR E 2 81  ? 19.926  -23.316 81.315  1.00 155.86 ? 81  THR E N   1 
ATOM   12296 C CA  . THR E 2 81  ? 21.285  -23.154 80.815  1.00 152.79 ? 81  THR E CA  1 
ATOM   12297 C C   . THR E 2 81  ? 21.528  -24.071 79.623  1.00 150.30 ? 81  THR E C   1 
ATOM   12298 O O   . THR E 2 81  ? 22.028  -23.635 78.579  1.00 147.65 ? 81  THR E O   1 
ATOM   12299 C CB  . THR E 2 81  ? 22.293  -23.432 81.932  1.00 150.08 ? 81  THR E CB  1 
ATOM   12300 O OG1 . THR E 2 81  ? 22.034  -24.721 82.503  1.00 149.28 ? 81  THR E OG1 1 
ATOM   12301 C CG2 . THR E 2 81  ? 22.199  -22.380 83.018  1.00 145.54 ? 81  THR E CG2 1 
ATOM   12302 N N   . GLU E 2 82  ? 21.173  -25.344 79.758  1.00 149.45 ? 82  GLU E N   1 
ATOM   12303 C CA  . GLU E 2 82  ? 21.336  -26.325 78.699  1.00 149.18 ? 82  GLU E CA  1 
ATOM   12304 C C   . GLU E 2 82  ? 20.014  -27.014 78.413  1.00 152.14 ? 82  GLU E C   1 
ATOM   12305 O O   . GLU E 2 82  ? 19.161  -27.125 79.299  1.00 151.76 ? 82  GLU E O   1 
ATOM   12306 C CB  . GLU E 2 82  ? 22.378  -27.391 79.069  1.00 144.94 ? 82  GLU E CB  1 
ATOM   12307 C CG  . GLU E 2 82  ? 23.777  -26.854 79.163  1.00 142.56 ? 82  GLU E CG  1 
ATOM   12308 C CD  . GLU E 2 82  ? 23.957  -25.997 80.388  1.00 141.84 ? 82  GLU E CD  1 
ATOM   12309 O OE1 . GLU E 2 82  ? 23.460  -26.383 81.467  1.00 145.84 ? 82  GLU E OE1 1 
ATOM   12310 O OE2 . GLU E 2 82  ? 24.560  -24.912 80.266  1.00 138.77 ? 82  GLU E OE2 1 
ATOM   12311 N N   . PRO E 2 83  ? 19.811  -27.472 77.179  1.00 158.08 ? 83  PRO E N   1 
ATOM   12312 C CA  . PRO E 2 83  ? 18.693  -28.386 76.919  1.00 158.18 ? 83  PRO E CA  1 
ATOM   12313 C C   . PRO E 2 83  ? 18.904  -29.663 77.715  1.00 159.90 ? 83  PRO E C   1 
ATOM   12314 O O   . PRO E 2 83  ? 19.897  -30.372 77.535  1.00 158.32 ? 83  PRO E O   1 
ATOM   12315 C CB  . PRO E 2 83  ? 18.775  -28.628 75.408  1.00 154.94 ? 83  PRO E CB  1 
ATOM   12316 C CG  . PRO E 2 83  ? 19.545  -27.460 74.873  1.00 154.35 ? 83  PRO E CG  1 
ATOM   12317 C CD  . PRO E 2 83  ? 20.530  -27.110 75.947  1.00 156.15 ? 83  PRO E CD  1 
ATOM   12318 N N   . LEU E 2 84  ? 17.964  -29.951 78.606  1.00 164.12 ? 84  LEU E N   1 
ATOM   12319 C CA  . LEU E 2 84  ? 18.102  -31.076 79.528  1.00 162.42 ? 84  LEU E CA  1 
ATOM   12320 C C   . LEU E 2 84  ? 17.306  -32.278 79.025  1.00 165.44 ? 84  LEU E C   1 
ATOM   12321 O O   . LEU E 2 84  ? 16.415  -32.806 79.690  1.00 166.86 ? 84  LEU E O   1 
ATOM   12322 C CB  . LEU E 2 84  ? 17.677  -30.665 80.934  1.00 160.16 ? 84  LEU E CB  1 
ATOM   12323 C CG  . LEU E 2 84  ? 18.334  -29.395 81.478  1.00 152.37 ? 84  LEU E CG  1 
ATOM   12324 C CD1 . LEU E 2 84  ? 17.739  -29.011 82.825  1.00 139.92 ? 84  LEU E CD1 1 
ATOM   12325 C CD2 . LEU E 2 84  ? 19.842  -29.563 81.574  1.00 149.85 ? 84  LEU E CD2 1 
ATOM   12326 N N   . GLY E 2 85  ? 17.660  -32.710 77.819  1.00 158.54 ? 85  GLY E N   1 
ATOM   12327 C CA  . GLY E 2 85  ? 16.944  -33.810 77.199  1.00 160.82 ? 85  GLY E CA  1 
ATOM   12328 C C   . GLY E 2 85  ? 15.552  -33.358 76.812  1.00 155.03 ? 85  GLY E C   1 
ATOM   12329 O O   . GLY E 2 85  ? 15.363  -32.277 76.242  1.00 152.09 ? 85  GLY E O   1 
ATOM   12330 N N   . THR E 2 86  ? 14.558  -34.189 77.114  1.00 165.67 ? 86  THR E N   1 
ATOM   12331 C CA  . THR E 2 86  ? 13.171  -33.851 76.830  1.00 161.00 ? 86  THR E CA  1 
ATOM   12332 C C   . THR E 2 86  ? 12.339  -33.592 78.078  1.00 158.42 ? 86  THR E C   1 
ATOM   12333 O O   . THR E 2 86  ? 11.391  -32.807 78.018  1.00 154.27 ? 86  THR E O   1 
ATOM   12334 C CB  . THR E 2 86  ? 12.506  -34.963 76.008  1.00 158.24 ? 86  THR E CB  1 
ATOM   12335 O OG1 . THR E 2 86  ? 13.488  -35.600 75.180  1.00 162.00 ? 86  THR E OG1 1 
ATOM   12336 C CG2 . THR E 2 86  ? 11.418  -34.382 75.121  1.00 143.40 ? 86  THR E CG2 1 
ATOM   12337 N N   . ALA E 2 87  ? 12.671  -34.227 79.203  1.00 162.26 ? 87  ALA E N   1 
ATOM   12338 C CA  . ALA E 2 87  ? 11.926  -34.061 80.444  1.00 162.09 ? 87  ALA E CA  1 
ATOM   12339 C C   . ALA E 2 87  ? 12.598  -33.116 81.432  1.00 158.63 ? 87  ALA E C   1 
ATOM   12340 O O   . ALA E 2 87  ? 11.977  -32.758 82.438  1.00 151.69 ? 87  ALA E O   1 
ATOM   12341 C CB  . ALA E 2 87  ? 11.708  -35.422 81.116  1.00 179.61 ? 87  ALA E CB  1 
ATOM   12342 N N   . GLY E 2 88  ? 13.839  -32.714 81.176  1.00 168.69 ? 88  GLY E N   1 
ATOM   12343 C CA  . GLY E 2 88  ? 14.567  -31.822 82.050  1.00 168.44 ? 88  GLY E CA  1 
ATOM   12344 C C   . GLY E 2 88  ? 13.902  -30.479 82.288  1.00 171.76 ? 88  GLY E C   1 
ATOM   12345 O O   . GLY E 2 88  ? 13.733  -30.050 83.435  1.00 170.05 ? 88  GLY E O   1 
ATOM   12346 N N   . PRO E 2 89  ? 13.537  -29.764 81.204  1.00 197.89 ? 89  PRO E N   1 
ATOM   12347 C CA  . PRO E 2 89  ? 12.865  -28.465 81.367  1.00 198.38 ? 89  PRO E CA  1 
ATOM   12348 C C   . PRO E 2 89  ? 11.628  -28.516 82.254  1.00 198.48 ? 89  PRO E C   1 
ATOM   12349 O O   . PRO E 2 89  ? 11.221  -27.493 82.814  1.00 198.85 ? 89  PRO E O   1 
ATOM   12350 C CB  . PRO E 2 89  ? 12.504  -28.084 79.927  1.00 198.18 ? 89  PRO E CB  1 
ATOM   12351 C CG  . PRO E 2 89  ? 13.568  -28.717 79.111  1.00 197.61 ? 89  PRO E CG  1 
ATOM   12352 C CD  . PRO E 2 89  ? 13.890  -30.019 79.794  1.00 197.35 ? 89  PRO E CD  1 
ATOM   12353 N N   . LEU E 2 90  ? 11.021  -29.697 82.386  1.00 172.26 ? 90  LEU E N   1 
ATOM   12354 C CA  . LEU E 2 90  ? 9.878   -29.846 83.279  1.00 166.11 ? 90  LEU E CA  1 
ATOM   12355 C C   . LEU E 2 90  ? 10.296  -29.857 84.743  1.00 168.61 ? 90  LEU E C   1 
ATOM   12356 O O   . LEU E 2 90  ? 9.513   -29.451 85.608  1.00 167.71 ? 90  LEU E O   1 
ATOM   12357 C CB  . LEU E 2 90  ? 9.108   -31.127 82.950  1.00 158.16 ? 90  LEU E CB  1 
ATOM   12358 C CG  . LEU E 2 90  ? 8.278   -31.163 81.664  1.00 154.31 ? 90  LEU E CG  1 
ATOM   12359 C CD1 . LEU E 2 90  ? 9.149   -31.386 80.433  1.00 154.87 ? 90  LEU E CD1 1 
ATOM   12360 C CD2 . LEU E 2 90  ? 7.194   -32.224 81.763  1.00 157.43 ? 90  LEU E CD2 1 
ATOM   12361 N N   . ALA E 2 91  ? 11.516  -30.316 85.039  1.00 169.71 ? 91  ALA E N   1 
ATOM   12362 C CA  . ALA E 2 91  ? 11.988  -30.335 86.419  1.00 169.21 ? 91  ALA E CA  1 
ATOM   12363 C C   . ALA E 2 91  ? 12.245  -28.932 86.948  1.00 181.45 ? 91  ALA E C   1 
ATOM   12364 O O   . ALA E 2 91  ? 12.133  -28.696 88.156  1.00 179.26 ? 91  ALA E O   1 
ATOM   12365 C CB  . ALA E 2 91  ? 13.255  -31.181 86.530  1.00 161.59 ? 91  ALA E CB  1 
ATOM   12366 N N   . LEU E 2 92  ? 12.593  -27.993 86.067  1.00 214.55 ? 92  LEU E N   1 
ATOM   12367 C CA  . LEU E 2 92  ? 12.848  -26.625 86.500  1.00 215.18 ? 92  LEU E CA  1 
ATOM   12368 C C   . LEU E 2 92  ? 11.548  -25.864 86.725  1.00 215.56 ? 92  LEU E C   1 
ATOM   12369 O O   . LEU E 2 92  ? 11.458  -25.043 87.644  1.00 216.10 ? 92  LEU E O   1 
ATOM   12370 C CB  . LEU E 2 92  ? 13.722  -25.905 85.470  1.00 214.96 ? 92  LEU E CB  1 
ATOM   12371 C CG  . LEU E 2 92  ? 14.154  -24.468 85.767  1.00 216.79 ? 92  LEU E CG  1 
ATOM   12372 C CD1 . LEU E 2 92  ? 15.606  -24.263 85.367  1.00 215.13 ? 92  LEU E CD1 1 
ATOM   12373 C CD2 . LEU E 2 92  ? 13.260  -23.474 85.042  1.00 214.73 ? 92  LEU E CD2 1 
ATOM   12374 N N   . ALA E 2 93  ? 10.537  -26.123 85.899  1.00 186.31 ? 93  ALA E N   1 
ATOM   12375 C CA  . ALA E 2 93  ? 9.266   -25.419 85.975  1.00 178.73 ? 93  ALA E CA  1 
ATOM   12376 C C   . ALA E 2 93  ? 8.270   -26.097 86.906  1.00 168.20 ? 93  ALA E C   1 
ATOM   12377 O O   . ALA E 2 93  ? 7.084   -25.757 86.873  1.00 160.45 ? 93  ALA E O   1 
ATOM   12378 C CB  . ALA E 2 93  ? 8.656   -25.279 84.578  1.00 177.26 ? 93  ALA E CB  1 
ATOM   12379 N N   . ARG E 2 94  ? 8.723   -27.039 87.738  1.00 173.38 ? 94  ARG E N   1 
ATOM   12380 C CA  . ARG E 2 94  ? 7.809   -27.691 88.670  1.00 172.35 ? 94  ARG E CA  1 
ATOM   12381 C C   . ARG E 2 94  ? 7.303   -26.720 89.728  1.00 169.32 ? 94  ARG E C   1 
ATOM   12382 O O   . ARG E 2 94  ? 6.222   -26.927 90.291  1.00 167.97 ? 94  ARG E O   1 
ATOM   12383 C CB  . ARG E 2 94  ? 8.492   -28.884 89.340  1.00 174.19 ? 94  ARG E CB  1 
ATOM   12384 C CG  . ARG E 2 94  ? 9.600   -28.498 90.308  1.00 173.48 ? 94  ARG E CG  1 
ATOM   12385 C CD  . ARG E 2 94  ? 9.605   -29.407 91.525  1.00 177.74 ? 94  ARG E CD  1 
ATOM   12386 N NE  . ARG E 2 94  ? 9.932   -30.786 91.179  1.00 179.47 ? 94  ARG E NE  1 
ATOM   12387 C CZ  . ARG E 2 94  ? 9.919   -31.795 92.043  1.00 174.64 ? 94  ARG E CZ  1 
ATOM   12388 N NH1 . ARG E 2 94  ? 9.589   -31.583 93.310  1.00 177.38 ? 94  ARG E NH1 1 
ATOM   12389 N NH2 . ARG E 2 94  ? 10.232  -33.019 91.640  1.00 171.07 ? 94  ARG E NH2 1 
ATOM   12390 N N   . ASP E 2 95  ? 8.064   -25.660 90.009  1.00 163.48 ? 95  ASP E N   1 
ATOM   12391 C CA  . ASP E 2 95  ? 7.637   -24.688 91.006  1.00 158.67 ? 95  ASP E CA  1 
ATOM   12392 C C   . ASP E 2 95  ? 6.489   -23.831 90.493  1.00 156.98 ? 95  ASP E C   1 
ATOM   12393 O O   . ASP E 2 95  ? 5.629   -23.414 91.276  1.00 156.90 ? 95  ASP E O   1 
ATOM   12394 C CB  . ASP E 2 95  ? 8.821   -23.812 91.419  1.00 161.91 ? 95  ASP E CB  1 
ATOM   12395 C CG  . ASP E 2 95  ? 9.645   -23.346 90.232  1.00 164.33 ? 95  ASP E CG  1 
ATOM   12396 O OD1 . ASP E 2 95  ? 9.281   -23.676 89.083  1.00 162.39 ? 95  ASP E OD1 1 
ATOM   12397 O OD2 . ASP E 2 95  ? 10.660  -22.651 90.448  1.00 169.87 ? 95  ASP E OD2 1 
ATOM   12398 N N   . LYS E 2 96  ? 6.458   -23.559 89.190  1.00 154.38 ? 96  LYS E N   1 
ATOM   12399 C CA  . LYS E 2 96  ? 5.392   -22.775 88.584  1.00 145.95 ? 96  LYS E CA  1 
ATOM   12400 C C   . LYS E 2 96  ? 4.202   -23.625 88.158  1.00 145.28 ? 96  LYS E C   1 
ATOM   12401 O O   . LYS E 2 96  ? 3.196   -23.073 87.703  1.00 141.44 ? 96  LYS E O   1 
ATOM   12402 C CB  . LYS E 2 96  ? 5.932   -22.001 87.378  1.00 144.67 ? 96  LYS E CB  1 
ATOM   12403 C CG  . LYS E 2 96  ? 7.047   -21.032 87.727  1.00 138.44 ? 96  LYS E CG  1 
ATOM   12404 C CD  . LYS E 2 96  ? 6.568   -19.973 88.704  1.00 134.42 ? 96  LYS E CD  1 
ATOM   12405 C CE  . LYS E 2 96  ? 5.481   -19.099 88.106  1.00 129.95 ? 96  LYS E CE  1 
ATOM   12406 N NZ  . LYS E 2 96  ? 5.052   -18.045 89.068  1.00 121.69 ? 96  LYS E NZ  1 
ATOM   12407 N N   . LEU E 2 97  ? 4.290   -24.947 88.298  1.00 151.60 ? 97  LEU E N   1 
ATOM   12408 C CA  . LEU E 2 97  ? 3.215   -25.845 87.896  1.00 155.71 ? 97  LEU E CA  1 
ATOM   12409 C C   . LEU E 2 97  ? 2.382   -26.345 89.066  1.00 159.91 ? 97  LEU E C   1 
ATOM   12410 O O   . LEU E 2 97  ? 1.234   -26.753 88.860  1.00 162.15 ? 97  LEU E O   1 
ATOM   12411 C CB  . LEU E 2 97  ? 3.784   -27.054 87.140  1.00 164.55 ? 97  LEU E CB  1 
ATOM   12412 C CG  . LEU E 2 97  ? 4.301   -26.804 85.723  1.00 164.46 ? 97  LEU E CG  1 
ATOM   12413 C CD1 . LEU E 2 97  ? 4.958   -28.057 85.167  1.00 169.67 ? 97  LEU E CD1 1 
ATOM   12414 C CD2 . LEU E 2 97  ? 3.171   -26.345 84.816  1.00 167.25 ? 97  LEU E CD2 1 
ATOM   12415 N N   . LEU E 2 98  ? 2.925   -26.321 90.279  1.00 155.28 ? 98  LEU E N   1 
ATOM   12416 C CA  . LEU E 2 98  ? 2.216   -26.803 91.458  1.00 162.38 ? 98  LEU E CA  1 
ATOM   12417 C C   . LEU E 2 98  ? 1.472   -25.633 92.089  1.00 172.10 ? 98  LEU E C   1 
ATOM   12418 O O   . LEU E 2 98  ? 2.082   -24.767 92.724  1.00 171.43 ? 98  LEU E O   1 
ATOM   12419 C CB  . LEU E 2 98  ? 3.189   -27.440 92.446  1.00 158.56 ? 98  LEU E CB  1 
ATOM   12420 C CG  . LEU E 2 98  ? 3.990   -28.618 91.892  1.00 154.40 ? 98  LEU E CG  1 
ATOM   12421 C CD1 . LEU E 2 98  ? 4.803   -29.288 92.989  1.00 158.10 ? 98  LEU E CD1 1 
ATOM   12422 C CD2 . LEU E 2 98  ? 3.073   -29.619 91.207  1.00 154.43 ? 98  LEU E CD2 1 
ATOM   12423 N N   . ASP E 2 99  ? 0.152   -25.613 91.916  1.00 182.89 ? 99  ASP E N   1 
ATOM   12424 C CA  . ASP E 2 99  ? -0.701  -24.605 92.527  1.00 184.34 ? 99  ASP E CA  1 
ATOM   12425 C C   . ASP E 2 99  ? -1.233  -25.024 93.890  1.00 196.14 ? 99  ASP E C   1 
ATOM   12426 O O   . ASP E 2 99  ? -1.756  -24.177 94.622  1.00 199.46 ? 99  ASP E O   1 
ATOM   12427 C CB  . ASP E 2 99  ? -1.868  -24.269 91.591  1.00 184.00 ? 99  ASP E CB  1 
ATOM   12428 C CG  . ASP E 2 99  ? -2.654  -25.499 91.172  1.00 189.66 ? 99  ASP E CG  1 
ATOM   12429 O OD1 . ASP E 2 99  ? -2.053  -26.592 91.092  1.00 186.39 ? 99  ASP E OD1 1 
ATOM   12430 O OD2 . ASP E 2 99  ? -3.870  -25.372 90.916  1.00 196.22 ? 99  ASP E OD2 1 
ATOM   12431 N N   . GLY E 2 100 ? -1.118  -26.306 94.246  1.00 197.64 ? 100 GLY E N   1 
ATOM   12432 C CA  . GLY E 2 100 ? -1.581  -26.828 95.513  1.00 204.15 ? 100 GLY E CA  1 
ATOM   12433 C C   . GLY E 2 100 ? -2.769  -27.759 95.387  1.00 214.17 ? 100 GLY E C   1 
ATOM   12434 O O   . GLY E 2 100 ? -2.935  -28.655 96.223  1.00 218.56 ? 100 GLY E O   1 
ATOM   12435 N N   . SER E 2 101 ? -3.593  -27.570 94.356  1.00 228.24 ? 101 SER E N   1 
ATOM   12436 C CA  . SER E 2 101 ? -4.775  -28.400 94.165  1.00 229.64 ? 101 SER E CA  1 
ATOM   12437 C C   . SER E 2 101 ? -4.439  -29.792 93.653  1.00 228.12 ? 101 SER E C   1 
ATOM   12438 O O   . SER E 2 101 ? -5.301  -30.676 93.707  1.00 231.63 ? 101 SER E O   1 
ATOM   12439 C CB  . SER E 2 101 ? -5.743  -27.719 93.199  1.00 226.84 ? 101 SER E CB  1 
ATOM   12440 O OG  . SER E 2 101 ? -6.871  -28.536 92.941  1.00 226.01 ? 101 SER E OG  1 
ATOM   12441 N N   . GLY E 2 102 ? -3.222  -30.010 93.164  1.00 209.17 ? 102 GLY E N   1 
ATOM   12442 C CA  . GLY E 2 102 ? -2.840  -31.306 92.643  1.00 196.84 ? 102 GLY E CA  1 
ATOM   12443 C C   . GLY E 2 102 ? -3.638  -31.663 91.409  1.00 193.20 ? 102 GLY E C   1 
ATOM   12444 O O   . GLY E 2 102 ? -4.111  -32.795 91.264  1.00 187.78 ? 102 GLY E O   1 
ATOM   12445 N N   . GLU E 2 103 ? -3.779  -30.704 90.505  1.00 190.51 ? 103 GLU E N   1 
ATOM   12446 C CA  . GLU E 2 103 ? -4.509  -30.935 89.274  1.00 189.97 ? 103 GLU E CA  1 
ATOM   12447 C C   . GLU E 2 103 ? -3.546  -31.224 88.131  1.00 186.22 ? 103 GLU E C   1 
ATOM   12448 O O   . GLU E 2 103 ? -2.439  -30.678 88.088  1.00 186.02 ? 103 GLU E O   1 
ATOM   12449 C CB  . GLU E 2 103 ? -5.372  -29.721 88.915  1.00 193.00 ? 103 GLU E CB  1 
ATOM   12450 C CG  . GLU E 2 103 ? -6.621  -29.573 89.765  1.00 194.28 ? 103 GLU E CG  1 
ATOM   12451 C CD  . GLU E 2 103 ? -7.746  -30.481 89.308  1.00 189.76 ? 103 GLU E CD  1 
ATOM   12452 O OE1 . GLU E 2 103 ? -7.623  -31.085 88.222  1.00 186.69 ? 103 GLU E OE1 1 
ATOM   12453 O OE2 . GLU E 2 103 ? -8.752  -30.598 90.038  1.00 192.39 ? 103 GLU E OE2 1 
ATOM   12454 N N   . PRO E 2 104 ? -3.939  -32.085 87.194  1.00 189.68 ? 104 PRO E N   1 
ATOM   12455 C CA  . PRO E 2 104 ? -3.054  -32.384 86.065  1.00 192.18 ? 104 PRO E CA  1 
ATOM   12456 C C   . PRO E 2 104 ? -2.848  -31.161 85.188  1.00 199.51 ? 104 PRO E C   1 
ATOM   12457 O O   . PRO E 2 104 ? -3.775  -30.388 84.934  1.00 195.67 ? 104 PRO E O   1 
ATOM   12458 C CB  . PRO E 2 104 ? -3.794  -33.498 85.315  1.00 191.05 ? 104 PRO E CB  1 
ATOM   12459 C CG  . PRO E 2 104 ? -5.223  -33.351 85.727  1.00 189.23 ? 104 PRO E CG  1 
ATOM   12460 C CD  . PRO E 2 104 ? -5.181  -32.874 87.148  1.00 187.71 ? 104 PRO E CD  1 
ATOM   12461 N N   . PHE E 2 105 ? -1.615  -30.995 84.725  1.00 223.78 ? 105 PHE E N   1 
ATOM   12462 C CA  . PHE E 2 105 ? -1.238  -29.905 83.841  1.00 223.53 ? 105 PHE E CA  1 
ATOM   12463 C C   . PHE E 2 105 ? -0.879  -30.449 82.464  1.00 223.41 ? 105 PHE E C   1 
ATOM   12464 O O   . PHE E 2 105 ? -0.563  -31.631 82.300  1.00 223.90 ? 105 PHE E O   1 
ATOM   12465 C CB  . PHE E 2 105 ? -0.067  -29.105 84.426  1.00 223.96 ? 105 PHE E CB  1 
ATOM   12466 C CG  . PHE E 2 105 ? 1.114   -29.950 84.812  1.00 224.55 ? 105 PHE E CG  1 
ATOM   12467 C CD1 . PHE E 2 105 ? 1.218   -30.478 86.090  1.00 224.97 ? 105 PHE E CD1 1 
ATOM   12468 C CD2 . PHE E 2 105 ? 2.123   -30.214 83.901  1.00 224.53 ? 105 PHE E CD2 1 
ATOM   12469 C CE1 . PHE E 2 105 ? 2.302   -31.255 86.448  1.00 225.25 ? 105 PHE E CE1 1 
ATOM   12470 C CE2 . PHE E 2 105 ? 3.210   -30.991 84.253  1.00 224.78 ? 105 PHE E CE2 1 
ATOM   12471 C CZ  . PHE E 2 105 ? 3.299   -31.511 85.529  1.00 225.15 ? 105 PHE E CZ  1 
ATOM   12472 N N   . PHE E 2 106 ? -0.927  -29.568 81.471  0.62 204.93 ? 106 PHE E N   1 
ATOM   12473 C CA  . PHE E 2 106 ? -0.648  -29.936 80.093  0.62 196.62 ? 106 PHE E CA  1 
ATOM   12474 C C   . PHE E 2 106 ? 0.791   -29.595 79.723  0.62 196.85 ? 106 PHE E C   1 
ATOM   12475 O O   . PHE E 2 106 ? 1.355   -28.602 80.191  0.62 191.61 ? 106 PHE E O   1 
ATOM   12476 C CB  . PHE E 2 106 ? -1.613  -29.228 79.140  0.62 178.40 ? 106 PHE E CB  1 
ATOM   12477 N N   . VAL E 2 107 ? 1.379   -30.436 78.874  1.00 201.39 ? 107 VAL E N   1 
ATOM   12478 C CA  . VAL E 2 107 ? 2.727   -30.236 78.348  1.00 201.31 ? 107 VAL E CA  1 
ATOM   12479 C C   . VAL E 2 107 ? 2.653   -30.320 76.829  1.00 200.47 ? 107 VAL E C   1 
ATOM   12480 O O   . VAL E 2 107 ? 2.313   -31.374 76.279  1.00 207.44 ? 107 VAL E O   1 
ATOM   12481 C CB  . VAL E 2 107 ? 3.726   -31.265 78.901  1.00 202.63 ? 107 VAL E CB  1 
ATOM   12482 C CG1 . VAL E 2 107 ? 5.120   -30.985 78.362  1.00 202.10 ? 107 VAL E CG1 1 
ATOM   12483 C CG2 . VAL E 2 107 ? 3.727   -31.240 80.424  1.00 202.78 ? 107 VAL E CG2 1 
ATOM   12484 N N   . LEU E 2 108 ? 2.963   -29.214 76.154  1.00 177.35 ? 108 LEU E N   1 
ATOM   12485 C CA  . LEU E 2 108 ? 2.819   -29.110 74.709  1.00 167.16 ? 108 LEU E CA  1 
ATOM   12486 C C   . LEU E 2 108 ? 4.159   -28.816 74.044  1.00 156.06 ? 108 LEU E C   1 
ATOM   12487 O O   . LEU E 2 108 ? 5.040   -28.184 74.634  1.00 152.26 ? 108 LEU E O   1 
ATOM   12488 C CB  . LEU E 2 108 ? 1.806   -28.019 74.351  1.00 164.33 ? 108 LEU E CB  1 
ATOM   12489 C CG  . LEU E 2 108 ? 0.443   -28.194 75.027  1.00 167.07 ? 108 LEU E CG  1 
ATOM   12490 C CD1 . LEU E 2 108 ? -0.493  -27.047 74.682  1.00 182.87 ? 108 LEU E CD1 1 
ATOM   12491 C CD2 . LEU E 2 108 ? -0.180  -29.533 74.658  1.00 178.94 ? 108 LEU E CD2 1 
ATOM   12492 N N   . ASN E 2 109 ? 4.306   -29.287 72.807  1.00 147.93 ? 109 ASN E N   1 
ATOM   12493 C CA  . ASN E 2 109 ? 5.481   -29.019 71.986  1.00 136.37 ? 109 ASN E CA  1 
ATOM   12494 C C   . ASN E 2 109 ? 5.151   -27.985 70.916  1.00 131.76 ? 109 ASN E C   1 
ATOM   12495 O O   . ASN E 2 109 ? 4.075   -28.018 70.312  1.00 129.89 ? 109 ASN E O   1 
ATOM   12496 C CB  . ASN E 2 109 ? 6.003   -30.298 71.327  1.00 133.39 ? 109 ASN E CB  1 
ATOM   12497 C CG  . ASN E 2 109 ? 7.404   -30.134 70.752  1.00 124.68 ? 109 ASN E CG  1 
ATOM   12498 O OD1 . ASN E 2 109 ? 7.810   -29.037 70.366  1.00 122.91 ? 109 ASN E OD1 1 
ATOM   12499 N ND2 . ASN E 2 109 ? 8.148   -31.232 70.690  1.00 121.93 ? 109 ASN E ND2 1 
ATOM   12500 N N   . SER E 2 110 ? 6.088   -27.064 70.689  1.00 137.61 ? 110 SER E N   1 
ATOM   12501 C CA  . SER E 2 110 ? 5.881   -26.000 69.714  1.00 138.14 ? 110 SER E CA  1 
ATOM   12502 C C   . SER E 2 110 ? 5.997   -26.483 68.272  1.00 135.57 ? 110 SER E C   1 
ATOM   12503 O O   . SER E 2 110 ? 5.564   -25.770 67.360  1.00 134.99 ? 110 SER E O   1 
ATOM   12504 C CB  . SER E 2 110 ? 6.882   -24.867 69.960  1.00 139.42 ? 110 SER E CB  1 
ATOM   12505 O OG  . SER E 2 110 ? 6.673   -23.796 69.055  1.00 142.19 ? 110 SER E OG  1 
ATOM   12506 N N   . ASP E 2 111 ? 6.565   -27.665 68.037  1.00 124.19 ? 111 ASP E N   1 
ATOM   12507 C CA  . ASP E 2 111 ? 6.803   -28.145 66.683  1.00 118.54 ? 111 ASP E CA  1 
ATOM   12508 C C   . ASP E 2 111 ? 5.674   -29.024 66.151  1.00 115.73 ? 111 ASP E C   1 
ATOM   12509 O O   . ASP E 2 111 ? 5.874   -29.742 65.164  1.00 113.26 ? 111 ASP E O   1 
ATOM   12510 C CB  . ASP E 2 111 ? 8.126   -28.909 66.625  1.00 116.45 ? 111 ASP E CB  1 
ATOM   12511 C CG  . ASP E 2 111 ? 9.287   -28.107 67.174  1.00 114.81 ? 111 ASP E CG  1 
ATOM   12512 O OD1 . ASP E 2 111 ? 9.047   -27.029 67.757  1.00 118.32 ? 111 ASP E OD1 1 
ATOM   12513 O OD2 . ASP E 2 111 ? 10.443  -28.554 67.023  1.00 106.25 ? 111 ASP E OD2 1 
ATOM   12514 N N   . VAL E 2 112 ? 4.497   -28.982 66.773  1.00 117.70 ? 112 VAL E N   1 
ATOM   12515 C CA  . VAL E 2 112 ? 3.375   -29.839 66.405  1.00 119.48 ? 112 VAL E CA  1 
ATOM   12516 C C   . VAL E 2 112 ? 2.113   -28.993 66.286  1.00 118.99 ? 112 VAL E C   1 
ATOM   12517 O O   . VAL E 2 112 ? 1.919   -28.039 67.048  1.00 122.22 ? 112 VAL E O   1 
ATOM   12518 C CB  . VAL E 2 112 ? 3.167   -30.979 67.428  1.00 126.68 ? 112 VAL E CB  1 
ATOM   12519 C CG1 . VAL E 2 112 ? 2.111   -31.954 66.935  1.00 132.65 ? 112 VAL E CG1 1 
ATOM   12520 C CG2 . VAL E 2 112 ? 4.475   -31.710 67.694  1.00 131.21 ? 112 VAL E CG2 1 
ATOM   12521 N N   . ILE E 2 113 ? 1.258   -29.345 65.326  1.00 116.88 ? 113 ILE E N   1 
ATOM   12522 C CA  . ILE E 2 113 ? -0.054  -28.733 65.163  1.00 123.22 ? 113 ILE E CA  1 
ATOM   12523 C C   . ILE E 2 113 ? -1.101  -29.837 65.140  1.00 126.84 ? 113 ILE E C   1 
ATOM   12524 O O   . ILE E 2 113 ? -0.831  -30.967 64.721  1.00 125.81 ? 113 ILE E O   1 
ATOM   12525 C CB  . ILE E 2 113 ? -0.140  -27.872 63.883  1.00 118.99 ? 113 ILE E CB  1 
ATOM   12526 C CG1 . ILE E 2 113 ? 0.328   -28.672 62.665  1.00 116.83 ? 113 ILE E CG1 1 
ATOM   12527 C CG2 . ILE E 2 113 ? 0.678   -26.603 64.043  1.00 118.70 ? 113 ILE E CG2 1 
ATOM   12528 C CD1 . ILE E 2 113 ? 0.150   -27.946 61.346  1.00 115.24 ? 113 ILE E CD1 1 
ATOM   12529 N N   . SER E 2 114 ? -2.305  -29.502 65.584  1.00 132.88 ? 114 SER E N   1 
ATOM   12530 C CA  . SER E 2 114 ? -3.399  -30.468 65.656  1.00 140.12 ? 114 SER E CA  1 
ATOM   12531 C C   . SER E 2 114 ? -4.698  -29.701 65.880  1.00 149.20 ? 114 SER E C   1 
ATOM   12532 O O   . SER E 2 114 ? -4.732  -28.466 65.809  1.00 152.60 ? 114 SER E O   1 
ATOM   12533 C CB  . SER E 2 114 ? -3.153  -31.502 66.756  1.00 153.37 ? 114 SER E CB  1 
ATOM   12534 O OG  . SER E 2 114 ? -3.222  -30.898 68.035  1.00 160.41 ? 114 SER E OG  1 
ATOM   12535 N N   . GLU E 2 115 ? -5.779  -30.444 66.124  1.00 147.45 ? 115 GLU E N   1 
ATOM   12536 C CA  . GLU E 2 115 ? -7.083  -29.858 66.406  1.00 153.76 ? 115 GLU E CA  1 
ATOM   12537 C C   . GLU E 2 115 ? -7.281  -29.518 67.880  1.00 172.33 ? 115 GLU E C   1 
ATOM   12538 O O   . GLU E 2 115 ? -8.190  -28.745 68.203  1.00 176.00 ? 115 GLU E O   1 
ATOM   12539 C CB  . GLU E 2 115 ? -8.186  -30.806 65.926  1.00 146.58 ? 115 GLU E CB  1 
ATOM   12540 C CG  . GLU E 2 115 ? -7.970  -31.303 64.499  1.00 140.46 ? 115 GLU E CG  1 
ATOM   12541 C CD  . GLU E 2 115 ? -9.182  -32.006 63.920  1.00 142.78 ? 115 GLU E CD  1 
ATOM   12542 O OE1 . GLU E 2 115 ? -10.035 -32.472 64.704  1.00 149.33 ? 115 GLU E OE1 1 
ATOM   12543 O OE2 . GLU E 2 115 ? -9.275  -32.104 62.678  1.00 135.09 ? 115 GLU E OE2 1 
ATOM   12544 N N   . TYR E 2 116 ? -6.455  -30.076 68.770  1.00 183.90 ? 116 TYR E N   1 
ATOM   12545 C CA  . TYR E 2 116 ? -6.435  -29.813 70.207  1.00 188.88 ? 116 TYR E CA  1 
ATOM   12546 C C   . TYR E 2 116 ? -7.793  -29.988 70.884  1.00 197.13 ? 116 TYR E C   1 
ATOM   12547 O O   . TYR E 2 116 ? -8.446  -28.994 71.230  1.00 194.53 ? 116 TYR E O   1 
ATOM   12548 C CB  . TYR E 2 116 ? -5.910  -28.399 70.460  1.00 184.63 ? 116 TYR E CB  1 
ATOM   12549 C CG  . TYR E 2 116 ? -4.516  -28.170 69.924  1.00 182.49 ? 116 TYR E CG  1 
ATOM   12550 C CD1 . TYR E 2 116 ? -3.400  -28.608 70.623  1.00 183.99 ? 116 TYR E CD1 1 
ATOM   12551 C CD2 . TYR E 2 116 ? -4.317  -27.519 68.714  1.00 180.25 ? 116 TYR E CD2 1 
ATOM   12552 C CE1 . TYR E 2 116 ? -2.123  -28.403 70.132  1.00 180.46 ? 116 TYR E CE1 1 
ATOM   12553 C CE2 . TYR E 2 116 ? -3.045  -27.308 68.215  1.00 178.69 ? 116 TYR E CE2 1 
ATOM   12554 C CZ  . TYR E 2 116 ? -1.952  -27.752 68.928  1.00 173.79 ? 116 TYR E CZ  1 
ATOM   12555 O OH  . TYR E 2 116 ? -0.684  -27.543 68.434  1.00 171.54 ? 116 TYR E OH  1 
ATOM   12556 N N   . PRO E 2 117 ? -8.255  -31.228 71.094  1.00 229.74 ? 117 PRO E N   1 
ATOM   12557 C CA  . PRO E 2 117 ? -9.478  -31.467 71.896  1.00 229.51 ? 117 PRO E CA  1 
ATOM   12558 C C   . PRO E 2 117 ? -9.174  -31.628 73.384  1.00 230.61 ? 117 PRO E C   1 
ATOM   12559 O O   . PRO E 2 117 ? -9.321  -32.703 73.981  1.00 231.15 ? 117 PRO E O   1 
ATOM   12560 C CB  . PRO E 2 117 ? -10.027 -32.748 71.267  1.00 229.47 ? 117 PRO E CB  1 
ATOM   12561 C CG  . PRO E 2 117 ? -8.794  -33.500 70.880  1.00 230.65 ? 117 PRO E CG  1 
ATOM   12562 C CD  . PRO E 2 117 ? -7.763  -32.468 70.470  1.00 230.22 ? 117 PRO E CD  1 
ATOM   12563 N N   . LEU E 2 118 ? -8.736  -30.536 74.013  1.00 193.51 ? 118 LEU E N   1 
ATOM   12564 C CA  . LEU E 2 118 ? -8.316  -30.611 75.409  1.00 180.48 ? 118 LEU E CA  1 
ATOM   12565 C C   . LEU E 2 118 ? -9.498  -30.805 76.352  1.00 178.75 ? 118 LEU E C   1 
ATOM   12566 O O   . LEU E 2 118 ? -9.334  -31.377 77.436  1.00 178.69 ? 118 LEU E O   1 
ATOM   12567 C CB  . LEU E 2 118 ? -7.534  -29.353 75.785  1.00 168.91 ? 118 LEU E CB  1 
ATOM   12568 C CG  . LEU E 2 118 ? -6.274  -29.064 74.971  1.00 169.42 ? 118 LEU E CG  1 
ATOM   12569 C CD1 . LEU E 2 118 ? -5.643  -27.757 75.418  1.00 170.65 ? 118 LEU E CD1 1 
ATOM   12570 C CD2 . LEU E 2 118 ? -5.284  -30.210 75.092  1.00 165.60 ? 118 LEU E CD2 1 
ATOM   12571 N N   . LYS E 2 119 ? -10.687 -30.334 75.967  1.00 173.22 ? 119 LYS E N   1 
ATOM   12572 C CA  . LYS E 2 119 ? -11.850 -30.425 76.846  1.00 171.27 ? 119 LYS E CA  1 
ATOM   12573 C C   . LYS E 2 119 ? -12.243 -31.876 77.102  1.00 176.30 ? 119 LYS E C   1 
ATOM   12574 O O   . LYS E 2 119 ? -12.376 -32.302 78.255  1.00 175.67 ? 119 LYS E O   1 
ATOM   12575 C CB  . LYS E 2 119 ? -13.023 -29.651 76.241  1.00 163.68 ? 119 LYS E CB  1 
ATOM   12576 C CG  . LYS E 2 119 ? -12.780 -28.157 76.101  1.00 157.33 ? 119 LYS E CG  1 
ATOM   12577 C CD  . LYS E 2 119 ? -14.037 -27.356 76.405  1.00 150.15 ? 119 LYS E CD  1 
ATOM   12578 C CE  . LYS E 2 119 ? -14.515 -27.605 77.823  1.00 147.79 ? 119 LYS E CE  1 
ATOM   12579 N NZ  . LYS E 2 119 ? -13.473 -27.261 78.829  1.00 152.82 ? 119 LYS E NZ  1 
ATOM   12580 N N   . GLU E 2 120 ? -12.441 -32.650 76.037  1.00 183.28 ? 120 GLU E N   1 
ATOM   12581 C CA  . GLU E 2 120 ? -12.866 -34.039 76.158  1.00 186.99 ? 120 GLU E CA  1 
ATOM   12582 C C   . GLU E 2 120 ? -11.729 -34.982 76.537  1.00 187.02 ? 120 GLU E C   1 
ATOM   12583 O O   . GLU E 2 120 ? -11.919 -36.203 76.498  1.00 187.49 ? 120 GLU E O   1 
ATOM   12584 C CB  . GLU E 2 120 ? -13.523 -34.503 74.855  1.00 188.01 ? 120 GLU E CB  1 
ATOM   12585 C CG  . GLU E 2 120 ? -14.764 -33.705 74.478  1.00 188.54 ? 120 GLU E CG  1 
ATOM   12586 C CD  . GLU E 2 120 ? -15.414 -34.198 73.200  1.00 195.00 ? 120 GLU E CD  1 
ATOM   12587 O OE1 . GLU E 2 120 ? -14.881 -35.146 72.587  1.00 193.74 ? 120 GLU E OE1 1 
ATOM   12588 O OE2 . GLU E 2 120 ? -16.460 -33.638 72.809  1.00 198.95 ? 120 GLU E OE2 1 
ATOM   12589 N N   . MET E 2 121 ? -10.560 -34.452 76.899  1.00 183.74 ? 121 MET E N   1 
ATOM   12590 C CA  . MET E 2 121 ? -9.483  -35.278 77.426  1.00 184.59 ? 121 MET E CA  1 
ATOM   12591 C C   . MET E 2 121 ? -9.502  -35.352 78.946  1.00 186.66 ? 121 MET E C   1 
ATOM   12592 O O   . MET E 2 121 ? -9.139  -36.390 79.514  1.00 188.59 ? 121 MET E O   1 
ATOM   12593 C CB  . MET E 2 121 ? -8.128  -34.741 76.958  1.00 183.22 ? 121 MET E CB  1 
ATOM   12594 C CG  . MET E 2 121 ? -6.965  -35.685 77.209  1.00 188.07 ? 121 MET E CG  1 
ATOM   12595 S SD  . MET E 2 121 ? -5.383  -34.960 76.743  1.00 191.17 ? 121 MET E SD  1 
ATOM   12596 C CE  . MET E 2 121 ? -5.812  -34.198 75.181  1.00 190.02 ? 121 MET E CE  1 
ATOM   12597 N N   . LEU E 2 122 ? -9.918  -34.274 79.617  1.00 184.42 ? 122 LEU E N   1 
ATOM   12598 C CA  . LEU E 2 122 ? -10.075 -34.320 81.067  1.00 185.14 ? 122 LEU E CA  1 
ATOM   12599 C C   . LEU E 2 122 ? -11.149 -35.320 81.465  1.00 189.54 ? 122 LEU E C   1 
ATOM   12600 O O   . LEU E 2 122 ? -10.996 -36.050 82.452  1.00 193.39 ? 122 LEU E O   1 
ATOM   12601 C CB  . LEU E 2 122 ? -10.410 -32.932 81.615  1.00 181.58 ? 122 LEU E CB  1 
ATOM   12602 C CG  . LEU E 2 122 ? -9.258  -31.956 81.865  1.00 176.65 ? 122 LEU E CG  1 
ATOM   12603 C CD1 . LEU E 2 122 ? -8.654  -31.475 80.563  1.00 173.18 ? 122 LEU E CD1 1 
ATOM   12604 C CD2 . LEU E 2 122 ? -9.729  -30.781 82.705  1.00 175.67 ? 122 LEU E CD2 1 
ATOM   12605 N N   . GLU E 2 123 ? -12.255 -35.356 80.717  1.00 193.36 ? 123 GLU E N   1 
ATOM   12606 C CA  . GLU E 2 123 ? -13.263 -36.382 80.953  1.00 200.50 ? 123 GLU E CA  1 
ATOM   12607 C C   . GLU E 2 123 ? -12.701 -37.771 80.686  1.00 201.51 ? 123 GLU E C   1 
ATOM   12608 O O   . GLU E 2 123 ? -13.066 -38.731 81.373  1.00 205.64 ? 123 GLU E O   1 
ATOM   12609 C CB  . GLU E 2 123 ? -14.493 -36.123 80.084  1.00 203.84 ? 123 GLU E CB  1 
ATOM   12610 C CG  . GLU E 2 123 ? -15.692 -36.987 80.435  1.00 209.91 ? 123 GLU E CG  1 
ATOM   12611 C CD  . GLU E 2 123 ? -16.916 -36.645 79.610  1.00 213.53 ? 123 GLU E CD  1 
ATOM   12612 O OE1 . GLU E 2 123 ? -16.755 -36.043 78.528  1.00 213.35 ? 123 GLU E OE1 1 
ATOM   12613 O OE2 . GLU E 2 123 ? -18.039 -36.976 80.046  1.00 214.27 ? 123 GLU E OE2 1 
ATOM   12614 N N   . PHE E 2 124 ? -11.813 -37.899 79.697  1.00 192.77 ? 124 PHE E N   1 
ATOM   12615 C CA  . PHE E 2 124 ? -11.091 -39.150 79.507  1.00 192.63 ? 124 PHE E CA  1 
ATOM   12616 C C   . PHE E 2 124 ? -10.089 -39.401 80.626  1.00 195.32 ? 124 PHE E C   1 
ATOM   12617 O O   . PHE E 2 124 ? -9.609  -40.529 80.768  1.00 195.90 ? 124 PHE E O   1 
ATOM   12618 C CB  . PHE E 2 124 ? -10.385 -39.154 78.149  1.00 189.62 ? 124 PHE E CB  1 
ATOM   12619 C CG  . PHE E 2 124 ? -9.770  -40.478 77.789  1.00 188.89 ? 124 PHE E CG  1 
ATOM   12620 C CD1 . PHE E 2 124 ? -10.561 -41.608 77.653  1.00 188.56 ? 124 PHE E CD1 1 
ATOM   12621 C CD2 . PHE E 2 124 ? -8.406  -40.593 77.580  1.00 186.98 ? 124 PHE E CD2 1 
ATOM   12622 C CE1 . PHE E 2 124 ? -10.002 -42.828 77.321  1.00 187.24 ? 124 PHE E CE1 1 
ATOM   12623 C CE2 . PHE E 2 124 ? -7.843  -41.810 77.245  1.00 187.43 ? 124 PHE E CE2 1 
ATOM   12624 C CZ  . PHE E 2 124 ? -8.641  -42.928 77.116  1.00 186.54 ? 124 PHE E CZ  1 
ATOM   12625 N N   . HIS E 2 125 ? -9.767  -38.377 81.420  1.00 192.89 ? 125 HIS E N   1 
ATOM   12626 C CA  . HIS E 2 125 ? -8.894  -38.519 82.579  1.00 194.40 ? 125 HIS E CA  1 
ATOM   12627 C C   . HIS E 2 125 ? -9.676  -38.739 83.866  1.00 197.68 ? 125 HIS E C   1 
ATOM   12628 O O   . HIS E 2 125 ? -9.273  -39.552 84.705  1.00 196.50 ? 125 HIS E O   1 
ATOM   12629 C CB  . HIS E 2 125 ? -8.012  -37.275 82.735  1.00 191.47 ? 125 HIS E CB  1 
ATOM   12630 C CG  . HIS E 2 125 ? -6.984  -37.395 83.818  1.00 191.63 ? 125 HIS E CG  1 
ATOM   12631 N ND1 . HIS E 2 125 ? -5.825  -38.126 83.669  1.00 190.74 ? 125 HIS E ND1 1 
ATOM   12632 C CD2 . HIS E 2 125 ? -6.942  -36.878 85.068  1.00 189.73 ? 125 HIS E CD2 1 
ATOM   12633 C CE1 . HIS E 2 125 ? -5.114  -38.054 84.779  1.00 188.80 ? 125 HIS E CE1 1 
ATOM   12634 N NE2 . HIS E 2 125 ? -5.770  -37.302 85.645  1.00 188.00 ? 125 HIS E NE2 1 
ATOM   12635 N N   . LYS E 2 126 ? -10.789 -38.027 84.035  1.00 201.24 ? 126 LYS E N   1 
ATOM   12636 C CA  . LYS E 2 126 ? -11.609 -38.115 85.233  1.00 205.01 ? 126 LYS E CA  1 
ATOM   12637 C C   . LYS E 2 126 ? -12.639 -39.237 85.159  1.00 220.74 ? 126 LYS E C   1 
ATOM   12638 O O   . LYS E 2 126 ? -13.622 -39.214 85.909  1.00 223.49 ? 126 LYS E O   1 
ATOM   12639 C CB  . LYS E 2 126 ? -12.305 -36.776 85.488  1.00 197.23 ? 126 LYS E CB  1 
ATOM   12640 C CG  . LYS E 2 126 ? -11.357 -35.642 85.849  1.00 188.75 ? 126 LYS E CG  1 
ATOM   12641 C CD  . LYS E 2 126 ? -12.124 -34.380 86.209  1.00 184.29 ? 126 LYS E CD  1 
ATOM   12642 C CE  . LYS E 2 126 ? -11.189 -33.266 86.652  1.00 180.53 ? 126 LYS E CE  1 
ATOM   12643 N NZ  . LYS E 2 126 ? -11.938 -32.052 87.079  1.00 186.82 ? 126 LYS E NZ  1 
ATOM   12644 N N   . SER E 2 127 ? -12.437 -40.217 84.280  1.00 255.42 ? 127 SER E N   1 
ATOM   12645 C CA  . SER E 2 127 ? -13.345 -41.347 84.136  1.00 255.88 ? 127 SER E CA  1 
ATOM   12646 C C   . SER E 2 127 ? -12.778 -42.629 84.725  1.00 257.01 ? 127 SER E C   1 
ATOM   12647 O O   . SER E 2 127 ? -13.433 -43.278 85.547  1.00 258.37 ? 127 SER E O   1 
ATOM   12648 C CB  . SER E 2 127 ? -13.686 -41.567 82.654  1.00 254.78 ? 127 SER E CB  1 
ATOM   12649 O OG  . SER E 2 127 ? -14.602 -42.634 82.494  1.00 258.25 ? 127 SER E OG  1 
ATOM   12650 N N   . HIS E 2 128 ? -11.569 -43.010 84.324  1.00 226.33 ? 128 HIS E N   1 
ATOM   12651 C CA  . HIS E 2 128 ? -10.902 -44.187 84.861  1.00 220.16 ? 128 HIS E CA  1 
ATOM   12652 C C   . HIS E 2 128 ? -9.975  -43.859 86.023  1.00 214.28 ? 128 HIS E C   1 
ATOM   12653 O O   . HIS E 2 128 ? -9.526  -44.778 86.717  1.00 212.07 ? 128 HIS E O   1 
ATOM   12654 C CB  . HIS E 2 128 ? -10.110 -44.889 83.753  1.00 211.96 ? 128 HIS E CB  1 
ATOM   12655 C CG  . HIS E 2 128 ? -9.218  -43.972 82.978  1.00 203.85 ? 128 HIS E CG  1 
ATOM   12656 N ND1 . HIS E 2 128 ? -8.818  -42.745 83.461  1.00 201.38 ? 128 HIS E ND1 1 
ATOM   12657 C CD2 . HIS E 2 128 ? -8.658  -44.096 81.753  1.00 196.10 ? 128 HIS E CD2 1 
ATOM   12658 C CE1 . HIS E 2 128 ? -8.045  -42.155 82.569  1.00 195.50 ? 128 HIS E CE1 1 
ATOM   12659 N NE2 . HIS E 2 128 ? -7.933  -42.953 81.523  1.00 192.76 ? 128 HIS E NE2 1 
ATOM   12660 N N   . GLY E 2 129 ? -9.672  -42.582 86.243  1.00 209.64 ? 129 GLY E N   1 
ATOM   12661 C CA  . GLY E 2 129 ? -8.817  -42.195 87.346  1.00 206.59 ? 129 GLY E CA  1 
ATOM   12662 C C   . GLY E 2 129 ? -7.348  -42.466 87.128  1.00 205.00 ? 129 GLY E C   1 
ATOM   12663 O O   . GLY E 2 129 ? -6.627  -42.747 88.092  1.00 206.77 ? 129 GLY E O   1 
ATOM   12664 N N   . GLY E 2 130 ? -6.877  -42.393 85.885  1.00 202.74 ? 130 GLY E N   1 
ATOM   12665 C CA  . GLY E 2 130 ? -5.473  -42.604 85.610  1.00 198.79 ? 130 GLY E CA  1 
ATOM   12666 C C   . GLY E 2 130 ? -4.608  -41.505 86.193  1.00 196.68 ? 130 GLY E C   1 
ATOM   12667 O O   . GLY E 2 130 ? -5.081  -40.500 86.726  1.00 193.36 ? 130 GLY E O   1 
ATOM   12668 N N   . GLU E 2 131 ? -3.297  -41.702 86.080  1.00 200.21 ? 131 GLU E N   1 
ATOM   12669 C CA  . GLU E 2 131 ? -2.334  -40.731 86.583  1.00 200.87 ? 131 GLU E CA  1 
ATOM   12670 C C   . GLU E 2 131 ? -1.727  -39.872 85.482  1.00 199.34 ? 131 GLU E C   1 
ATOM   12671 O O   . GLU E 2 131 ? -1.567  -38.662 85.664  1.00 194.93 ? 131 GLU E O   1 
ATOM   12672 C CB  . GLU E 2 131 ? -1.214  -41.437 87.356  1.00 202.56 ? 131 GLU E CB  1 
ATOM   12673 C CG  . GLU E 2 131 ? -0.225  -40.483 88.006  1.00 200.10 ? 131 GLU E CG  1 
ATOM   12674 C CD  . GLU E 2 131 ? 1.088   -41.149 88.366  1.00 197.73 ? 131 GLU E CD  1 
ATOM   12675 O OE1 . GLU E 2 131 ? 1.257   -42.347 88.056  1.00 207.03 ? 131 GLU E OE1 1 
ATOM   12676 O OE2 . GLU E 2 131 ? 1.953   -40.472 88.958  1.00 192.76 ? 131 GLU E OE2 1 
ATOM   12677 N N   . ALA E 2 132 ? -1.391  -40.466 84.340  1.00 195.53 ? 132 ALA E N   1 
ATOM   12678 C CA  . ALA E 2 132 ? -0.744  -39.753 83.250  1.00 189.02 ? 132 ALA E CA  1 
ATOM   12679 C C   . ALA E 2 132 ? -1.463  -40.052 81.943  1.00 185.68 ? 132 ALA E C   1 
ATOM   12680 O O   . ALA E 2 132 ? -1.961  -41.160 81.729  1.00 187.22 ? 132 ALA E O   1 
ATOM   12681 C CB  . ALA E 2 132 ? 0.737   -40.133 83.131  1.00 185.57 ? 132 ALA E CB  1 
ATOM   12682 N N   . SER E 2 133 ? -1.501  -39.052 81.065  1.00 190.39 ? 133 SER E N   1 
ATOM   12683 C CA  . SER E 2 133 ? -2.202  -39.164 79.793  1.00 192.17 ? 133 SER E CA  1 
ATOM   12684 C C   . SER E 2 133 ? -1.339  -38.596 78.681  1.00 197.19 ? 133 SER E C   1 
ATOM   12685 O O   . SER E 2 133 ? -0.762  -37.514 78.828  1.00 207.82 ? 133 SER E O   1 
ATOM   12686 C CB  . SER E 2 133 ? -3.540  -38.420 79.829  1.00 193.86 ? 133 SER E CB  1 
ATOM   12687 O OG  . SER E 2 133 ? -4.243  -38.576 78.608  1.00 191.36 ? 133 SER E OG  1 
ATOM   12688 N N   . ILE E 2 134 ? -1.256  -39.328 77.571  1.00 186.53 ? 134 ILE E N   1 
ATOM   12689 C CA  . ILE E 2 134 ? -0.614  -38.851 76.357  1.00 195.39 ? 134 ILE E CA  1 
ATOM   12690 C C   . ILE E 2 134 ? -1.600  -38.995 75.205  1.00 197.22 ? 134 ILE E C   1 
ATOM   12691 O O   . ILE E 2 134 ? -2.616  -39.684 75.307  1.00 193.58 ? 134 ILE E O   1 
ATOM   12692 C CB  . ILE E 2 134 ? 0.699   -39.601 76.047  1.00 199.56 ? 134 ILE E CB  1 
ATOM   12693 C CG1 . ILE E 2 134 ? 0.408   -41.054 75.666  1.00 196.78 ? 134 ILE E CG1 1 
ATOM   12694 C CG2 . ILE E 2 134 ? 1.647   -39.535 77.234  1.00 203.79 ? 134 ILE E CG2 1 
ATOM   12695 C CD1 . ILE E 2 134 ? 1.632   -41.821 75.221  1.00 200.47 ? 134 ILE E CD1 1 
ATOM   12696 N N   . MET E 2 135 ? -1.286  -38.331 74.099  1.00 203.24 ? 135 MET E N   1 
ATOM   12697 C CA  . MET E 2 135 ? -2.084  -38.413 72.887  1.00 203.85 ? 135 MET E CA  1 
ATOM   12698 C C   . MET E 2 135 ? -1.302  -39.145 71.804  1.00 204.77 ? 135 MET E C   1 
ATOM   12699 O O   . MET E 2 135 ? -0.075  -39.040 71.721  1.00 207.78 ? 135 MET E O   1 
ATOM   12700 C CB  . MET E 2 135 ? -2.491  -37.022 72.396  1.00 212.23 ? 135 MET E CB  1 
ATOM   12701 C CG  . MET E 2 135 ? -3.477  -36.318 73.312  1.00 210.52 ? 135 MET E CG  1 
ATOM   12702 S SD  . MET E 2 135 ? -4.960  -37.293 73.630  1.00 197.09 ? 135 MET E SD  1 
ATOM   12703 C CE  . MET E 2 135 ? -5.688  -37.350 71.996  1.00 208.33 ? 135 MET E CE  1 
ATOM   12704 N N   . VAL E 2 136 ? -2.025  -39.891 70.973  1.00 207.49 ? 136 VAL E N   1 
ATOM   12705 C CA  . VAL E 2 136 ? -1.427  -40.786 69.992  1.00 205.62 ? 136 VAL E CA  1 
ATOM   12706 C C   . VAL E 2 136 ? -2.111  -40.578 68.648  1.00 202.59 ? 136 VAL E C   1 
ATOM   12707 O O   . VAL E 2 136 ? -3.337  -40.437 68.580  1.00 205.83 ? 136 VAL E O   1 
ATOM   12708 C CB  . VAL E 2 136 ? -1.539  -42.260 70.440  1.00 200.32 ? 136 VAL E CB  1 
ATOM   12709 C CG1 . VAL E 2 136 ? -1.090  -43.191 69.337  1.00 211.22 ? 136 VAL E CG1 1 
ATOM   12710 C CG2 . VAL E 2 136 ? -0.723  -42.499 71.702  1.00 199.32 ? 136 VAL E CG2 1 
ATOM   12711 N N   . THR E 2 137 ? -1.317  -40.553 67.578  1.00 198.16 ? 137 THR E N   1 
ATOM   12712 C CA  . THR E 2 137 ? -1.827  -40.409 66.223  1.00 191.32 ? 137 THR E CA  1 
ATOM   12713 C C   . THR E 2 137 ? -1.278  -41.529 65.352  1.00 194.46 ? 137 THR E C   1 
ATOM   12714 O O   . THR E 2 137 ? -0.139  -41.970 65.534  1.00 209.24 ? 137 THR E O   1 
ATOM   12715 C CB  . THR E 2 137 ? -1.459  -39.047 65.613  1.00 190.27 ? 137 THR E CB  1 
ATOM   12716 O OG1 . THR E 2 137 ? -1.862  -39.012 64.238  1.00 183.68 ? 137 THR E OG1 1 
ATOM   12717 C CG2 . THR E 2 137 ? 0.041   -38.801 65.704  1.00 196.78 ? 137 THR E CG2 1 
ATOM   12718 N N   . LYS E 2 138 ? -2.102  -41.992 64.417  1.00 181.89 ? 138 LYS E N   1 
ATOM   12719 C CA  . LYS E 2 138 ? -1.700  -43.039 63.490  1.00 180.16 ? 138 LYS E CA  1 
ATOM   12720 C C   . LYS E 2 138 ? -0.827  -42.474 62.378  1.00 173.93 ? 138 LYS E C   1 
ATOM   12721 O O   . LYS E 2 138 ? -1.074  -41.376 61.869  1.00 174.29 ? 138 LYS E O   1 
ATOM   12722 C CB  . LYS E 2 138 ? -2.934  -43.712 62.892  1.00 177.01 ? 138 LYS E CB  1 
ATOM   12723 C CG  . LYS E 2 138 ? -3.947  -42.720 62.346  1.00 171.43 ? 138 LYS E CG  1 
ATOM   12724 C CD  . LYS E 2 138 ? -4.971  -43.381 61.448  1.00 166.89 ? 138 LYS E CD  1 
ATOM   12725 C CE  . LYS E 2 138 ? -5.903  -42.344 60.848  1.00 160.63 ? 138 LYS E CE  1 
ATOM   12726 N NZ  . LYS E 2 138 ? -5.157  -41.283 60.117  1.00 164.01 ? 138 LYS E NZ  1 
ATOM   12727 N N   . VAL E 2 139 ? 0.202   -43.230 62.004  1.00 176.65 ? 139 VAL E N   1 
ATOM   12728 C CA  . VAL E 2 139 ? 1.091   -42.857 60.913  1.00 176.61 ? 139 VAL E CA  1 
ATOM   12729 C C   . VAL E 2 139 ? 1.225   -44.039 59.965  1.00 175.81 ? 139 VAL E C   1 
ATOM   12730 O O   . VAL E 2 139 ? 1.142   -45.201 60.373  1.00 176.19 ? 139 VAL E O   1 
ATOM   12731 C CB  . VAL E 2 139 ? 2.480   -42.403 61.415  1.00 190.22 ? 139 VAL E CB  1 
ATOM   12732 C CG1 . VAL E 2 139 ? 2.361   -41.119 62.221  1.00 192.87 ? 139 VAL E CG1 1 
ATOM   12733 C CG2 . VAL E 2 139 ? 3.132   -43.501 62.240  1.00 197.76 ? 139 VAL E CG2 1 
ATOM   12734 N N   . ASP E 2 140 ? 1.432   -43.730 58.684  1.00 168.00 ? 140 ASP E N   1 
ATOM   12735 C CA  . ASP E 2 140 ? 1.615   -44.785 57.695  1.00 167.04 ? 140 ASP E CA  1 
ATOM   12736 C C   . ASP E 2 140 ? 2.991   -45.424 57.810  1.00 178.65 ? 140 ASP E C   1 
ATOM   12737 O O   . ASP E 2 140 ? 3.164   -46.593 57.446  1.00 175.51 ? 140 ASP E O   1 
ATOM   12738 C CB  . ASP E 2 140 ? 1.409   -44.225 56.290  1.00 160.08 ? 140 ASP E CB  1 
ATOM   12739 C CG  . ASP E 2 140 ? 0.060   -43.562 56.123  1.00 156.04 ? 140 ASP E CG  1 
ATOM   12740 O OD1 . ASP E 2 140 ? -0.892  -43.969 56.820  1.00 156.64 ? 140 ASP E OD1 1 
ATOM   12741 O OD2 . ASP E 2 140 ? -0.047  -42.629 55.300  1.00 152.44 ? 140 ASP E OD2 1 
ATOM   12742 N N   . GLU E 2 141 ? 3.978   -44.675 58.304  1.00 217.43 ? 141 GLU E N   1 
ATOM   12743 C CA  . GLU E 2 141 ? 5.350   -45.149 58.456  1.00 219.05 ? 141 GLU E CA  1 
ATOM   12744 C C   . GLU E 2 141 ? 5.687   -45.264 59.937  1.00 219.93 ? 141 GLU E C   1 
ATOM   12745 O O   . GLU E 2 141 ? 6.150   -44.291 60.551  1.00 219.73 ? 141 GLU E O   1 
ATOM   12746 C CB  . GLU E 2 141 ? 6.326   -44.202 57.753  1.00 218.45 ? 141 GLU E CB  1 
ATOM   12747 N N   . PRO E 2 142 ? 5.479   -46.427 60.562  1.00 196.76 ? 142 PRO E N   1 
ATOM   12748 C CA  . PRO E 2 142 ? 5.842   -46.572 61.978  1.00 195.36 ? 142 PRO E CA  1 
ATOM   12749 C C   . PRO E 2 142 ? 7.320   -46.839 62.211  1.00 191.92 ? 142 PRO E C   1 
ATOM   12750 O O   . PRO E 2 142 ? 7.785   -46.680 63.347  1.00 189.00 ? 142 PRO E O   1 
ATOM   12751 C CB  . PRO E 2 142 ? 4.997   -47.768 62.428  1.00 190.52 ? 142 PRO E CB  1 
ATOM   12752 C CG  . PRO E 2 142 ? 4.844   -48.590 61.196  1.00 186.92 ? 142 PRO E CG  1 
ATOM   12753 C CD  . PRO E 2 142 ? 4.791   -47.621 60.040  1.00 189.88 ? 142 PRO E CD  1 
ATOM   12754 N N   . SER E 2 143 ? 8.076   -47.217 61.180  1.00 192.92 ? 143 SER E N   1 
ATOM   12755 C CA  . SER E 2 143 ? 9.490   -47.514 61.381  1.00 188.70 ? 143 SER E CA  1 
ATOM   12756 C C   . SER E 2 143 ? 10.303  -46.242 61.588  1.00 189.28 ? 143 SER E C   1 
ATOM   12757 O O   . SER E 2 143 ? 11.219  -46.214 62.418  1.00 185.46 ? 143 SER E O   1 
ATOM   12758 C CB  . SER E 2 143 ? 10.033  -48.311 60.194  1.00 185.57 ? 143 SER E CB  1 
ATOM   12759 O OG  . SER E 2 143 ? 9.964   -47.555 58.997  1.00 189.96 ? 143 SER E OG  1 
ATOM   12760 N N   . LYS E 2 144 ? 9.980   -45.172 60.858  1.00 189.70 ? 144 LYS E N   1 
ATOM   12761 C CA  . LYS E 2 144 ? 10.726  -43.927 61.006  1.00 190.70 ? 144 LYS E CA  1 
ATOM   12762 C C   . LYS E 2 144 ? 10.439  -43.216 62.321  1.00 192.53 ? 144 LYS E C   1 
ATOM   12763 O O   . LYS E 2 144 ? 11.135  -42.248 62.645  1.00 192.35 ? 144 LYS E O   1 
ATOM   12764 C CB  . LYS E 2 144 ? 10.432  -42.984 59.837  1.00 191.13 ? 144 LYS E CB  1 
ATOM   12765 C CG  . LYS E 2 144 ? 10.754  -43.562 58.470  1.00 185.40 ? 144 LYS E CG  1 
ATOM   12766 C CD  . LYS E 2 144 ? 10.385  -42.584 57.370  1.00 177.78 ? 144 LYS E CD  1 
ATOM   12767 C CE  . LYS E 2 144 ? 11.172  -41.289 57.513  1.00 174.03 ? 144 LYS E CE  1 
ATOM   12768 N NZ  . LYS E 2 144 ? 10.854  -40.313 56.434  1.00 167.52 ? 144 LYS E NZ  1 
ATOM   12769 N N   . TYR E 2 145 ? 9.451   -43.669 63.081  1.00 192.60 ? 145 TYR E N   1 
ATOM   12770 C CA  . TYR E 2 145 ? 9.066   -43.073 64.351  1.00 196.98 ? 145 TYR E CA  1 
ATOM   12771 C C   . TYR E 2 145 ? 9.208   -44.110 65.462  1.00 192.00 ? 145 TYR E C   1 
ATOM   12772 O O   . TYR E 2 145 ? 9.544   -45.273 65.223  1.00 185.04 ? 145 TYR E O   1 
ATOM   12773 C CB  . TYR E 2 145 ? 7.631   -42.541 64.294  1.00 207.88 ? 145 TYR E CB  1 
ATOM   12774 C CG  . TYR E 2 145 ? 7.338   -41.597 63.147  1.00 209.11 ? 145 TYR E CG  1 
ATOM   12775 C CD1 . TYR E 2 145 ? 8.231   -40.593 62.796  1.00 204.55 ? 145 TYR E CD1 1 
ATOM   12776 C CD2 . TYR E 2 145 ? 6.165   -41.716 62.412  1.00 209.04 ? 145 TYR E CD2 1 
ATOM   12777 C CE1 . TYR E 2 145 ? 7.956   -39.728 61.750  1.00 202.36 ? 145 TYR E CE1 1 
ATOM   12778 C CE2 . TYR E 2 145 ? 5.883   -40.859 61.367  1.00 201.92 ? 145 TYR E CE2 1 
ATOM   12779 C CZ  . TYR E 2 145 ? 6.782   -39.867 61.039  1.00 200.88 ? 145 TYR E CZ  1 
ATOM   12780 O OH  . TYR E 2 145 ? 6.502   -39.014 59.996  1.00 197.14 ? 145 TYR E OH  1 
ATOM   12781 N N   . GLY E 2 146 ? 8.945   -43.674 66.692  1.00 195.77 ? 146 GLY E N   1 
ATOM   12782 C CA  . GLY E 2 146 ? 8.929   -44.577 67.826  1.00 187.08 ? 146 GLY E CA  1 
ATOM   12783 C C   . GLY E 2 146 ? 7.539   -45.126 68.076  1.00 204.16 ? 146 GLY E C   1 
ATOM   12784 O O   . GLY E 2 146 ? 6.623   -44.372 68.420  1.00 222.12 ? 146 GLY E O   1 
ATOM   12785 N N   . VAL E 2 147 ? 7.368   -46.435 67.914  1.00 194.78 ? 147 VAL E N   1 
ATOM   12786 C CA  . VAL E 2 147 ? 6.045   -47.045 67.985  1.00 212.84 ? 147 VAL E CA  1 
ATOM   12787 C C   . VAL E 2 147 ? 5.657   -47.283 69.437  1.00 226.76 ? 147 VAL E C   1 
ATOM   12788 O O   . VAL E 2 147 ? 6.471   -47.729 70.256  1.00 206.44 ? 147 VAL E O   1 
ATOM   12789 C CB  . VAL E 2 147 ? 6.013   -48.355 67.179  1.00 197.39 ? 147 VAL E CB  1 
ATOM   12790 C CG1 . VAL E 2 147 ? 4.616   -48.950 67.188  1.00 213.83 ? 147 VAL E CG1 1 
ATOM   12791 C CG2 . VAL E 2 147 ? 6.451   -48.099 65.758  1.00 186.82 ? 147 VAL E CG2 1 
ATOM   12792 N N   . VAL E 2 148 ? 4.401   -46.981 69.755  1.00 288.58 ? 148 VAL E N   1 
ATOM   12793 C CA  . VAL E 2 148 ? 3.817   -47.219 71.071  1.00 289.03 ? 148 VAL E CA  1 
ATOM   12794 C C   . VAL E 2 148 ? 2.876   -48.411 70.954  1.00 289.22 ? 148 VAL E C   1 
ATOM   12795 O O   . VAL E 2 148 ? 1.898   -48.367 70.198  1.00 288.63 ? 148 VAL E O   1 
ATOM   12796 C CB  . VAL E 2 148 ? 3.078   -45.977 71.591  1.00 288.48 ? 148 VAL E CB  1 
ATOM   12797 C CG1 . VAL E 2 148 ? 2.400   -46.275 72.918  1.00 288.72 ? 148 VAL E CG1 1 
ATOM   12798 C CG2 . VAL E 2 148 ? 4.042   -44.806 71.724  1.00 288.41 ? 148 VAL E CG2 1 
ATOM   12799 N N   . VAL E 2 149 ? 3.170   -49.473 71.698  1.00 254.63 ? 149 VAL E N   1 
ATOM   12800 C CA  . VAL E 2 149 ? 2.411   -50.718 71.637  1.00 250.38 ? 149 VAL E CA  1 
ATOM   12801 C C   . VAL E 2 149 ? 1.382   -50.700 72.763  1.00 241.24 ? 149 VAL E C   1 
ATOM   12802 O O   . VAL E 2 149 ? 1.686   -51.022 73.916  1.00 229.00 ? 149 VAL E O   1 
ATOM   12803 C CB  . VAL E 2 149 ? 3.324   -51.945 71.710  1.00 242.72 ? 149 VAL E CB  1 
ATOM   12804 C CG1 . VAL E 2 149 ? 3.918   -52.230 70.341  1.00 231.38 ? 149 VAL E CG1 1 
ATOM   12805 C CG2 . VAL E 2 149 ? 4.438   -51.724 72.718  1.00 232.48 ? 149 VAL E CG2 1 
ATOM   12806 N N   . MET E 2 150 ? 0.160   -50.305 72.429  1.00 250.87 ? 150 MET E N   1 
ATOM   12807 C CA  . MET E 2 150 ? -0.958  -50.301 73.358  1.00 249.16 ? 150 MET E CA  1 
ATOM   12808 C C   . MET E 2 150 ? -1.952  -51.389 72.974  1.00 249.10 ? 150 MET E C   1 
ATOM   12809 O O   . MET E 2 150 ? -1.932  -51.913 71.858  1.00 249.20 ? 150 MET E O   1 
ATOM   12810 C CB  . MET E 2 150 ? -1.660  -48.939 73.371  1.00 248.29 ? 150 MET E CB  1 
ATOM   12811 C CG  . MET E 2 150 ? -2.101  -48.472 71.993  1.00 247.55 ? 150 MET E CG  1 
ATOM   12812 S SD  . MET E 2 150 ? -2.757  -46.793 71.968  1.00 252.35 ? 150 MET E SD  1 
ATOM   12813 C CE  . MET E 2 150 ? -4.298  -47.014 72.845  1.00 245.46 ? 150 MET E CE  1 
ATOM   12814 N N   . GLU E 2 151 ? -2.829  -51.724 73.915  1.00 194.38 ? 151 GLU E N   1 
ATOM   12815 C CA  . GLU E 2 151 ? -3.925  -52.639 73.637  1.00 174.88 ? 151 GLU E CA  1 
ATOM   12816 C C   . GLU E 2 151 ? -5.129  -51.846 73.146  1.00 168.42 ? 151 GLU E C   1 
ATOM   12817 O O   . GLU E 2 151 ? -5.369  -50.717 73.586  1.00 170.07 ? 151 GLU E O   1 
ATOM   12818 C CB  . GLU E 2 151 ? -4.296  -53.462 74.874  1.00 160.51 ? 151 GLU E CB  1 
ATOM   12819 C CG  . GLU E 2 151 ? -5.193  -52.747 75.869  1.00 156.87 ? 151 GLU E CG  1 
ATOM   12820 C CD  . GLU E 2 151 ? -4.432  -51.803 76.775  1.00 164.88 ? 151 GLU E CD  1 
ATOM   12821 O OE1 . GLU E 2 151 ? -3.267  -52.109 77.108  1.00 171.26 ? 151 GLU E OE1 1 
ATOM   12822 O OE2 . GLU E 2 151 ? -4.997  -50.755 77.154  1.00 164.91 ? 151 GLU E OE2 1 
ATOM   12823 N N   . GLU E 2 152 ? -5.867  -52.432 72.208  1.00 151.91 ? 152 GLU E N   1 
ATOM   12824 C CA  . GLU E 2 152 ? -7.011  -51.776 71.575  1.00 145.34 ? 152 GLU E CA  1 
ATOM   12825 C C   . GLU E 2 152 ? -8.303  -51.947 72.366  1.00 140.82 ? 152 GLU E C   1 
ATOM   12826 O O   . GLU E 2 152 ? -9.376  -52.053 71.773  1.00 141.66 ? 152 GLU E O   1 
ATOM   12827 C CB  . GLU E 2 152 ? -7.173  -52.296 70.150  1.00 142.69 ? 152 GLU E CB  1 
ATOM   12828 N N   . SER E 2 153 ? -8.235  -51.964 73.693  1.00 141.17 ? 153 SER E N   1 
ATOM   12829 C CA  . SER E 2 153 ? -9.430  -52.137 74.515  1.00 140.06 ? 153 SER E CA  1 
ATOM   12830 C C   . SER E 2 153 ? -9.600  -51.047 75.563  1.00 138.72 ? 153 SER E C   1 
ATOM   12831 O O   . SER E 2 153 ? -10.723 -50.594 75.791  1.00 134.37 ? 153 SER E O   1 
ATOM   12832 C CB  . SER E 2 153 ? -9.405  -53.512 75.201  1.00 134.64 ? 153 SER E CB  1 
ATOM   12833 O OG  . SER E 2 153 ? -8.298  -53.623 76.078  1.00 135.63 ? 153 SER E OG  1 
ATOM   12834 N N   . THR E 2 154 ? -8.522  -50.610 76.194  1.00 142.53 ? 154 THR E N   1 
ATOM   12835 C CA  . THR E 2 154 ? -8.593  -49.586 77.232  1.00 142.89 ? 154 THR E CA  1 
ATOM   12836 C C   . THR E 2 154 ? -7.687  -48.397 76.955  1.00 150.83 ? 154 THR E C   1 
ATOM   12837 O O   . THR E 2 154 ? -8.096  -47.256 77.181  1.00 150.66 ? 154 THR E O   1 
ATOM   12838 C CB  . THR E 2 154 ? -8.235  -50.191 78.599  1.00 138.03 ? 154 THR E CB  1 
ATOM   12839 O OG1 . THR E 2 154 ? -6.962  -50.844 78.517  1.00 142.79 ? 154 THR E OG1 1 
ATOM   12840 C CG2 . THR E 2 154 ? -9.287  -51.200 79.029  1.00 134.18 ? 154 THR E CG2 1 
ATOM   12841 N N   . GLY E 2 155 ? -6.469  -48.633 76.474  1.00 167.00 ? 155 GLY E N   1 
ATOM   12842 C CA  . GLY E 2 155 ? -5.574  -47.551 76.117  1.00 176.41 ? 155 GLY E CA  1 
ATOM   12843 C C   . GLY E 2 155 ? -4.293  -47.514 76.924  1.00 183.40 ? 155 GLY E C   1 
ATOM   12844 O O   . GLY E 2 155 ? -3.672  -46.458 77.063  1.00 191.10 ? 155 GLY E O   1 
ATOM   12845 N N   . ARG E 2 156 ? -3.875  -48.663 77.445  1.00 177.81 ? 156 ARG E N   1 
ATOM   12846 C CA  . ARG E 2 156 ? -2.662  -48.749 78.246  1.00 185.70 ? 156 ARG E CA  1 
ATOM   12847 C C   . ARG E 2 156 ? -1.480  -49.143 77.370  1.00 197.28 ? 156 ARG E C   1 
ATOM   12848 O O   . ARG E 2 156 ? -1.591  -50.021 76.511  1.00 194.49 ? 156 ARG E O   1 
ATOM   12849 C CB  . ARG E 2 156 ? -2.846  -49.755 79.383  1.00 180.15 ? 156 ARG E CB  1 
ATOM   12850 C CG  . ARG E 2 156 ? -1.756  -49.722 80.440  1.00 184.10 ? 156 ARG E CG  1 
ATOM   12851 C CD  . ARG E 2 156 ? -2.032  -50.740 81.535  1.00 185.90 ? 156 ARG E CD  1 
ATOM   12852 N NE  . ARG E 2 156 ? -3.382  -50.599 82.078  1.00 179.88 ? 156 ARG E NE  1 
ATOM   12853 C CZ  . ARG E 2 156 ? -3.917  -51.417 82.979  1.00 172.35 ? 156 ARG E CZ  1 
ATOM   12854 N NH1 . ARG E 2 156 ? -3.218  -52.442 83.445  1.00 176.22 ? 156 ARG E NH1 1 
ATOM   12855 N NH2 . ARG E 2 156 ? -5.153  -51.211 83.415  1.00 166.13 ? 156 ARG E NH2 1 
ATOM   12856 N N   . VAL E 2 157 ? -0.349  -48.485 77.590  1.00 229.10 ? 157 VAL E N   1 
ATOM   12857 C CA  . VAL E 2 157 ? 0.847   -48.717 76.798  1.00 229.28 ? 157 VAL E CA  1 
ATOM   12858 C C   . VAL E 2 157 ? 1.746   -49.695 77.543  1.00 230.32 ? 157 VAL E C   1 
ATOM   12859 O O   . VAL E 2 157 ? 1.607   -49.917 78.750  1.00 230.83 ? 157 VAL E O   1 
ATOM   12860 C CB  . VAL E 2 157 ? 1.589   -47.400 76.481  1.00 234.56 ? 157 VAL E CB  1 
ATOM   12861 C CG1 . VAL E 2 157 ? 0.589   -46.307 76.134  1.00 230.04 ? 157 VAL E CG1 1 
ATOM   12862 C CG2 . VAL E 2 157 ? 2.465   -46.986 77.647  1.00 238.25 ? 157 VAL E CG2 1 
ATOM   12863 N N   . GLU E 2 158 ? 2.682   -50.302 76.810  1.00 211.20 ? 158 GLU E N   1 
ATOM   12864 C CA  . GLU E 2 158 ? 3.486   -51.380 77.372  1.00 201.69 ? 158 GLU E CA  1 
ATOM   12865 C C   . GLU E 2 158 ? 4.986   -51.197 77.151  1.00 195.88 ? 158 GLU E C   1 
ATOM   12866 O O   . GLU E 2 158 ? 5.764   -51.282 78.106  1.00 197.27 ? 158 GLU E O   1 
ATOM   12867 C CB  . GLU E 2 158 ? 3.025   -52.720 76.790  1.00 192.49 ? 158 GLU E CB  1 
ATOM   12868 C CG  . GLU E 2 158 ? 1.559   -53.027 77.067  1.00 187.03 ? 158 GLU E CG  1 
ATOM   12869 C CD  . GLU E 2 158 ? 1.096   -54.331 76.452  1.00 170.16 ? 158 GLU E CD  1 
ATOM   12870 O OE1 . GLU E 2 158 ? 1.869   -54.939 75.685  1.00 165.30 ? 158 GLU E OE1 1 
ATOM   12871 O OE2 . GLU E 2 158 ? -0.047  -54.747 76.736  1.00 166.25 ? 158 GLU E OE2 1 
ATOM   12872 N N   . LYS E 2 159 ? 5.409   -50.941 75.915  1.00 187.06 ? 159 LYS E N   1 
ATOM   12873 C CA  . LYS E 2 159 ? 6.831   -50.895 75.596  1.00 174.96 ? 159 LYS E CA  1 
ATOM   12874 C C   . LYS E 2 159 ? 7.071   -49.837 74.527  1.00 173.67 ? 159 LYS E C   1 
ATOM   12875 O O   . LYS E 2 159 ? 6.135   -49.316 73.918  1.00 188.22 ? 159 LYS E O   1 
ATOM   12876 C CB  . LYS E 2 159 ? 7.340   -52.265 75.128  1.00 171.13 ? 159 LYS E CB  1 
ATOM   12877 C CG  . LYS E 2 159 ? 8.828   -52.511 75.339  1.00 164.61 ? 159 LYS E CG  1 
ATOM   12878 C CD  . LYS E 2 159 ? 9.194   -52.482 76.813  1.00 164.07 ? 159 LYS E CD  1 
ATOM   12879 C CE  . LYS E 2 159 ? 10.659  -52.827 77.019  1.00 159.24 ? 159 LYS E CE  1 
ATOM   12880 N NZ  . LYS E 2 159 ? 11.555  -51.889 76.290  1.00 160.62 ? 159 LYS E NZ  1 
ATOM   12881 N N   . PHE E 2 160 ? 8.345   -49.512 74.311  1.00 165.13 ? 160 PHE E N   1 
ATOM   12882 C CA  . PHE E 2 160 ? 8.745   -48.567 73.274  1.00 157.20 ? 160 PHE E CA  1 
ATOM   12883 C C   . PHE E 2 160 ? 9.600   -49.307 72.255  1.00 153.25 ? 160 PHE E C   1 
ATOM   12884 O O   . PHE E 2 160 ? 10.662  -49.838 72.596  1.00 152.17 ? 160 PHE E O   1 
ATOM   12885 C CB  . PHE E 2 160 ? 9.490   -47.359 73.858  1.00 158.28 ? 160 PHE E CB  1 
ATOM   12886 C CG  . PHE E 2 160 ? 10.765  -47.699 74.585  1.00 161.82 ? 160 PHE E CG  1 
ATOM   12887 C CD1 . PHE E 2 160 ? 11.995  -47.438 74.001  1.00 159.94 ? 160 PHE E CD1 1 
ATOM   12888 C CD2 . PHE E 2 160 ? 10.737  -48.260 75.852  1.00 167.65 ? 160 PHE E CD2 1 
ATOM   12889 C CE1 . PHE E 2 160 ? 13.172  -47.739 74.660  1.00 159.92 ? 160 PHE E CE1 1 
ATOM   12890 C CE2 . PHE E 2 160 ? 11.911  -48.564 76.517  1.00 169.88 ? 160 PHE E CE2 1 
ATOM   12891 C CZ  . PHE E 2 160 ? 13.130  -48.303 75.919  1.00 165.84 ? 160 PHE E CZ  1 
ATOM   12892 N N   . VAL E 2 161 ? 9.125   -49.363 71.014  1.00 160.07 ? 161 VAL E N   1 
ATOM   12893 C CA  . VAL E 2 161 ? 9.802   -50.075 69.936  1.00 160.01 ? 161 VAL E CA  1 
ATOM   12894 C C   . VAL E 2 161 ? 10.131  -49.044 68.865  1.00 165.63 ? 161 VAL E C   1 
ATOM   12895 O O   . VAL E 2 161 ? 9.267   -48.675 68.059  1.00 166.81 ? 161 VAL E O   1 
ATOM   12896 C CB  . VAL E 2 161 ? 8.952   -51.216 69.368  1.00 154.16 ? 161 VAL E CB  1 
ATOM   12897 C CG1 . VAL E 2 161 ? 9.728   -51.967 68.297  1.00 153.16 ? 161 VAL E CG1 1 
ATOM   12898 C CG2 . VAL E 2 161 ? 8.506   -52.157 70.477  1.00 152.21 ? 161 VAL E CG2 1 
ATOM   12899 N N   . GLU E 2 162 ? 11.376  -48.577 68.848  1.00 164.60 ? 162 GLU E N   1 
ATOM   12900 C CA  . GLU E 2 162 ? 11.829  -47.629 67.842  1.00 169.56 ? 162 GLU E CA  1 
ATOM   12901 C C   . GLU E 2 162 ? 12.408  -48.381 66.651  1.00 170.92 ? 162 GLU E C   1 
ATOM   12902 O O   . GLU E 2 162 ? 13.137  -49.365 66.816  1.00 169.95 ? 162 GLU E O   1 
ATOM   12903 C CB  . GLU E 2 162 ? 12.867  -46.664 68.427  1.00 169.54 ? 162 GLU E CB  1 
ATOM   12904 C CG  . GLU E 2 162 ? 14.222  -47.282 68.772  1.00 168.96 ? 162 GLU E CG  1 
ATOM   12905 C CD  . GLU E 2 162 ? 14.190  -48.118 70.038  1.00 169.07 ? 162 GLU E CD  1 
ATOM   12906 O OE1 . GLU E 2 162 ? 13.134  -48.159 70.703  1.00 165.03 ? 162 GLU E OE1 1 
ATOM   12907 O OE2 . GLU E 2 162 ? 15.222  -48.740 70.366  1.00 170.01 ? 162 GLU E OE2 1 
ATOM   12908 N N   . LYS E 2 163 ? 12.072  -47.909 65.449  1.00 168.74 ? 163 LYS E N   1 
ATOM   12909 C CA  . LYS E 2 163 ? 12.462  -48.537 64.190  1.00 165.22 ? 163 LYS E CA  1 
ATOM   12910 C C   . LYS E 2 163 ? 12.186  -50.037 64.229  1.00 161.49 ? 163 LYS E C   1 
ATOM   12911 O O   . LYS E 2 163 ? 13.122  -50.842 64.322  1.00 158.39 ? 163 LYS E O   1 
ATOM   12912 C CB  . LYS E 2 163 ? 13.940  -48.258 63.891  1.00 164.37 ? 163 LYS E CB  1 
ATOM   12913 C CG  . LYS E 2 163 ? 14.438  -48.774 62.540  1.00 164.11 ? 163 LYS E CG  1 
ATOM   12914 C CD  . LYS E 2 163 ? 13.543  -48.339 61.393  1.00 166.82 ? 163 LYS E CD  1 
ATOM   12915 C CE  . LYS E 2 163 ? 13.971  -49.000 60.092  1.00 162.10 ? 163 LYS E CE  1 
ATOM   12916 N NZ  . LYS E 2 163 ? 13.924  -50.486 60.182  1.00 148.46 ? 163 LYS E NZ  1 
ATOM   12917 N N   . PRO E 2 164 ? 10.918  -50.455 64.192  1.00 162.54 ? 164 PRO E N   1 
ATOM   12918 C CA  . PRO E 2 164 ? 10.620  -51.894 64.157  1.00 155.72 ? 164 PRO E CA  1 
ATOM   12919 C C   . PRO E 2 164 ? 10.776  -52.416 62.736  1.00 155.68 ? 164 PRO E C   1 
ATOM   12920 O O   . PRO E 2 164 ? 10.095  -51.955 61.816  1.00 158.10 ? 164 PRO E O   1 
ATOM   12921 C CB  . PRO E 2 164 ? 9.161   -51.969 64.631  1.00 151.61 ? 164 PRO E CB  1 
ATOM   12922 C CG  . PRO E 2 164 ? 8.797   -50.580 65.073  1.00 156.02 ? 164 PRO E CG  1 
ATOM   12923 C CD  . PRO E 2 164 ? 9.692   -49.656 64.323  1.00 163.37 ? 164 PRO E CD  1 
ATOM   12924 N N   . LYS E 2 165 ? 11.675  -53.386 62.557  1.00 147.91 ? 165 LYS E N   1 
ATOM   12925 C CA  . LYS E 2 165 ? 11.838  -53.988 61.239  1.00 146.44 ? 165 LYS E CA  1 
ATOM   12926 C C   . LYS E 2 165 ? 10.613  -54.809 60.862  1.00 146.84 ? 165 LYS E C   1 
ATOM   12927 O O   . LYS E 2 165 ? 10.194  -54.811 59.698  1.00 147.10 ? 165 LYS E O   1 
ATOM   12928 C CB  . LYS E 2 165 ? 13.102  -54.847 61.201  1.00 143.06 ? 165 LYS E CB  1 
ATOM   12929 C CG  . LYS E 2 165 ? 14.392  -54.043 61.150  1.00 138.49 ? 165 LYS E CG  1 
ATOM   12930 C CD  . LYS E 2 165 ? 15.574  -54.943 60.851  1.00 132.21 ? 165 LYS E CD  1 
ATOM   12931 C CE  . LYS E 2 165 ? 15.554  -55.381 59.397  1.00 132.29 ? 165 LYS E CE  1 
ATOM   12932 N NZ  . LYS E 2 165 ? 16.012  -56.786 59.234  1.00 129.33 ? 165 LYS E NZ  1 
ATOM   12933 N N   . LEU E 2 166 ? 10.027  -55.505 61.828  1.00 148.72 ? 166 LEU E N   1 
ATOM   12934 C CA  . LEU E 2 166 ? 8.746   -56.167 61.650  1.00 152.92 ? 166 LEU E CA  1 
ATOM   12935 C C   . LEU E 2 166 ? 7.642   -55.314 62.263  1.00 155.59 ? 166 LEU E C   1 
ATOM   12936 O O   . LEU E 2 166 ? 7.895   -54.365 63.009  1.00 155.45 ? 166 LEU E O   1 
ATOM   12937 C CB  . LEU E 2 166 ? 8.758   -57.564 62.275  1.00 154.21 ? 166 LEU E CB  1 
ATOM   12938 C CG  . LEU E 2 166 ? 8.271   -58.676 61.345  1.00 150.79 ? 166 LEU E CG  1 
ATOM   12939 C CD1 . LEU E 2 166 ? 9.337   -59.014 60.310  1.00 150.06 ? 166 LEU E CD1 1 
ATOM   12940 C CD2 . LEU E 2 166 ? 7.856   -59.913 62.128  1.00 148.74 ? 166 LEU E CD2 1 
ATOM   12941 N N   . TYR E 2 167 ? 6.400   -55.665 61.943  1.00 159.44 ? 167 TYR E N   1 
ATOM   12942 C CA  . TYR E 2 167 ? 5.260   -54.858 62.362  1.00 165.20 ? 167 TYR E CA  1 
ATOM   12943 C C   . TYR E 2 167 ? 4.902   -55.202 63.803  1.00 169.75 ? 167 TYR E C   1 
ATOM   12944 O O   . TYR E 2 167 ? 4.463   -56.319 64.095  1.00 169.83 ? 167 TYR E O   1 
ATOM   12945 C CB  . TYR E 2 167 ? 4.066   -55.081 61.439  1.00 167.46 ? 167 TYR E CB  1 
ATOM   12946 C CG  . TYR E 2 167 ? 2.830   -54.326 61.878  1.00 175.76 ? 167 TYR E CG  1 
ATOM   12947 C CD1 . TYR E 2 167 ? 2.673   -52.979 61.581  1.00 180.50 ? 167 TYR E CD1 1 
ATOM   12948 C CD2 . TYR E 2 167 ? 1.826   -54.959 62.603  1.00 173.63 ? 167 TYR E CD2 1 
ATOM   12949 C CE1 . TYR E 2 167 ? 1.548   -52.285 61.986  1.00 185.29 ? 167 TYR E CE1 1 
ATOM   12950 C CE2 . TYR E 2 167 ? 0.699   -54.274 63.012  1.00 175.89 ? 167 TYR E CE2 1 
ATOM   12951 C CZ  . TYR E 2 167 ? 0.566   -52.938 62.701  1.00 183.15 ? 167 TYR E CZ  1 
ATOM   12952 O OH  . TYR E 2 167 ? -0.556  -52.256 63.107  1.00 184.42 ? 167 TYR E OH  1 
ATOM   12953 N N   . VAL E 2 168 ? 5.090   -54.239 64.702  1.00 173.17 ? 168 VAL E N   1 
ATOM   12954 C CA  . VAL E 2 168 ? 4.585   -54.335 66.067  1.00 178.25 ? 168 VAL E CA  1 
ATOM   12955 C C   . VAL E 2 168 ? 3.523   -53.292 66.357  1.00 188.20 ? 168 VAL E C   1 
ATOM   12956 O O   . VAL E 2 168 ? 2.895   -53.348 67.428  1.00 190.87 ? 168 VAL E O   1 
ATOM   12957 C CB  . VAL E 2 168 ? 5.723   -54.226 67.103  1.00 170.72 ? 168 VAL E CB  1 
ATOM   12958 C CG1 . VAL E 2 168 ? 6.642   -55.432 67.008  1.00 166.09 ? 168 VAL E CG1 1 
ATOM   12959 C CG2 . VAL E 2 168 ? 6.496   -52.934 66.908  1.00 168.83 ? 168 VAL E CG2 1 
ATOM   12960 N N   . GLY E 2 169 ? 3.302   -52.354 65.451  1.00 211.47 ? 169 GLY E N   1 
ATOM   12961 C CA  . GLY E 2 169 ? 2.291   -51.334 65.630  1.00 211.63 ? 169 GLY E CA  1 
ATOM   12962 C C   . GLY E 2 169 ? 2.500   -50.203 64.651  1.00 213.59 ? 169 GLY E C   1 
ATOM   12963 O O   . GLY E 2 169 ? 3.477   -50.160 63.903  1.00 210.68 ? 169 GLY E O   1 
ATOM   12964 N N   . ASN E 2 170 ? 1.544   -49.275 64.665  1.00 208.83 ? 170 ASN E N   1 
ATOM   12965 C CA  . ASN E 2 170 ? 1.597   -48.093 63.821  1.00 208.54 ? 170 ASN E CA  1 
ATOM   12966 C C   . ASN E 2 170 ? 1.317   -46.802 64.578  1.00 218.62 ? 170 ASN E C   1 
ATOM   12967 O O   . ASN E 2 170 ? 1.318   -45.731 63.962  1.00 214.43 ? 170 ASN E O   1 
ATOM   12968 C CB  . ASN E 2 170 ? 0.605   -48.226 62.656  1.00 203.27 ? 170 ASN E CB  1 
ATOM   12969 C CG  . ASN E 2 170 ? -0.695  -48.893 63.069  1.00 203.66 ? 170 ASN E CG  1 
ATOM   12970 O OD1 . ASN E 2 170 ? -0.931  -50.062 62.763  1.00 200.23 ? 170 ASN E OD1 1 
ATOM   12971 N ND2 . ASN E 2 170 ? -1.543  -48.152 63.772  1.00 205.50 ? 170 ASN E ND2 1 
ATOM   12972 N N   . LYS E 2 171 ? 1.079   -46.873 65.884  1.00 230.89 ? 171 LYS E N   1 
ATOM   12973 C CA  . LYS E 2 171 ? 0.670   -45.731 66.690  1.00 237.79 ? 171 LYS E CA  1 
ATOM   12974 C C   . LYS E 2 171 ? 1.882   -45.100 67.366  1.00 257.88 ? 171 LYS E C   1 
ATOM   12975 O O   . LYS E 2 171 ? 2.644   -45.792 68.050  1.00 255.04 ? 171 LYS E O   1 
ATOM   12976 C CB  . LYS E 2 171 ? -0.360  -46.176 67.727  1.00 226.30 ? 171 LYS E CB  1 
ATOM   12977 C CG  . LYS E 2 171 ? -1.569  -46.869 67.114  1.00 221.68 ? 171 LYS E CG  1 
ATOM   12978 C CD  . LYS E 2 171 ? -1.895  -48.174 67.822  1.00 221.12 ? 171 LYS E CD  1 
ATOM   12979 C CE  . LYS E 2 171 ? -0.746  -49.166 67.707  1.00 221.77 ? 171 LYS E CE  1 
ATOM   12980 N NZ  . LYS E 2 171 ? -0.990  -50.401 68.502  1.00 226.06 ? 171 LYS E NZ  1 
ATOM   12981 N N   . ILE E 2 172 ? 2.060   -43.792 67.170  1.00 309.83 ? 172 ILE E N   1 
ATOM   12982 C CA  . ILE E 2 172 ? 3.202   -43.063 67.707  1.00 310.37 ? 172 ILE E CA  1 
ATOM   12983 C C   . ILE E 2 172 ? 2.711   -41.898 68.566  1.00 309.91 ? 172 ILE E C   1 
ATOM   12984 O O   . ILE E 2 172 ? 1.537   -41.529 68.549  1.00 309.12 ? 172 ILE E O   1 
ATOM   12985 C CB  . ILE E 2 172 ? 4.143   -42.548 66.603  1.00 310.04 ? 172 ILE E CB  1 
ATOM   12986 C CG1 . ILE E 2 172 ? 3.492   -41.375 65.866  1.00 308.76 ? 172 ILE E CG1 1 
ATOM   12987 C CG2 . ILE E 2 172 ? 4.497   -43.670 65.641  1.00 310.30 ? 172 ILE E CG2 1 
ATOM   12988 C CD1 . ILE E 2 172 ? 4.473   -40.488 65.137  1.00 308.31 ? 172 ILE E CD1 1 
ATOM   12989 N N   . ASN E 2 173 ? 3.646   -41.316 69.314  1.00 258.82 ? 173 ASN E N   1 
ATOM   12990 C CA  . ASN E 2 173 ? 3.354   -40.169 70.162  1.00 237.99 ? 173 ASN E CA  1 
ATOM   12991 C C   . ASN E 2 173 ? 3.109   -38.918 69.321  1.00 237.55 ? 173 ASN E C   1 
ATOM   12992 O O   . ASN E 2 173 ? 3.658   -38.759 68.227  1.00 237.86 ? 173 ASN E O   1 
ATOM   12993 C CB  . ASN E 2 173 ? 4.511   -39.929 71.135  1.00 222.36 ? 173 ASN E CB  1 
ATOM   12994 C CG  . ASN E 2 173 ? 4.142   -38.993 72.271  1.00 216.62 ? 173 ASN E CG  1 
ATOM   12995 O OD1 . ASN E 2 173 ? 3.529   -37.946 72.060  1.00 218.81 ? 173 ASN E OD1 1 
ATOM   12996 N ND2 . ASN E 2 173 ? 4.520   -39.367 73.488  1.00 212.72 ? 173 ASN E ND2 1 
ATOM   12997 N N   . ALA E 2 174 ? 2.270   -38.021 69.846  1.00 240.59 ? 174 ALA E N   1 
ATOM   12998 C CA  . ALA E 2 174 ? 1.904   -36.789 69.157  1.00 236.34 ? 174 ALA E CA  1 
ATOM   12999 C C   . ALA E 2 174 ? 2.477   -35.533 69.803  1.00 234.37 ? 174 ALA E C   1 
ATOM   13000 O O   . ALA E 2 174 ? 2.212   -34.429 69.315  1.00 232.87 ? 174 ALA E O   1 
ATOM   13001 C CB  . ALA E 2 174 ? 0.378   -36.668 69.067  1.00 233.30 ? 174 ALA E CB  1 
ATOM   13002 N N   . GLY E 2 175 ? 3.256   -35.664 70.876  1.00 228.59 ? 175 GLY E N   1 
ATOM   13003 C CA  . GLY E 2 175 ? 3.884   -34.517 71.504  1.00 220.54 ? 175 GLY E CA  1 
ATOM   13004 C C   . GLY E 2 175 ? 3.028   -33.716 72.462  1.00 225.45 ? 175 GLY E C   1 
ATOM   13005 O O   . GLY E 2 175 ? 3.486   -32.672 72.941  1.00 212.43 ? 175 GLY E O   1 
ATOM   13006 N N   . ILE E 2 176 ? 1.805   -34.155 72.755  1.00 242.57 ? 176 ILE E N   1 
ATOM   13007 C CA  . ILE E 2 176 ? 0.926   -33.483 73.709  1.00 242.36 ? 176 ILE E CA  1 
ATOM   13008 C C   . ILE E 2 176 ? 0.650   -34.440 74.861  1.00 243.08 ? 176 ILE E C   1 
ATOM   13009 O O   . ILE E 2 176 ? 0.298   -35.603 74.636  1.00 242.92 ? 176 ILE E O   1 
ATOM   13010 C CB  . ILE E 2 176 ? -0.385  -33.015 73.048  1.00 243.41 ? 176 ILE E CB  1 
ATOM   13011 C CG1 . ILE E 2 176 ? -1.518  -32.936 74.080  1.00 242.26 ? 176 ILE E CG1 1 
ATOM   13012 C CG2 . ILE E 2 176 ? -0.754  -33.919 71.885  1.00 247.25 ? 176 ILE E CG2 1 
ATOM   13013 C CD1 . ILE E 2 176 ? -2.854  -32.531 73.497  1.00 242.25 ? 176 ILE E CD1 1 
ATOM   13014 N N   . TYR E 2 177 ? 0.816   -33.953 76.089  1.00 237.82 ? 177 TYR E N   1 
ATOM   13015 C CA  . TYR E 2 177 ? 0.757   -34.778 77.287  1.00 238.42 ? 177 TYR E CA  1 
ATOM   13016 C C   . TYR E 2 177 ? -0.274  -34.224 78.264  1.00 238.50 ? 177 TYR E C   1 
ATOM   13017 O O   . TYR E 2 177 ? -0.776  -33.106 78.117  1.00 237.63 ? 177 TYR E O   1 
ATOM   13018 C CB  . TYR E 2 177 ? 2.132   -34.854 77.967  1.00 239.27 ? 177 TYR E CB  1 
ATOM   13019 C CG  . TYR E 2 177 ? 3.275   -35.217 77.040  1.00 240.11 ? 177 TYR E CG  1 
ATOM   13020 C CD1 . TYR E 2 177 ? 3.120   -36.182 76.051  1.00 239.87 ? 177 TYR E CD1 1 
ATOM   13021 C CD2 . TYR E 2 177 ? 4.505   -34.582 77.146  1.00 241.77 ? 177 TYR E CD2 1 
ATOM   13022 C CE1 . TYR E 2 177 ? 4.162   -36.507 75.199  1.00 240.56 ? 177 TYR E CE1 1 
ATOM   13023 C CE2 . TYR E 2 177 ? 5.552   -34.901 76.299  1.00 241.86 ? 177 TYR E CE2 1 
ATOM   13024 C CZ  . TYR E 2 177 ? 5.375   -35.864 75.327  1.00 240.08 ? 177 TYR E CZ  1 
ATOM   13025 O OH  . TYR E 2 177 ? 6.411   -36.188 74.480  1.00 238.57 ? 177 TYR E OH  1 
ATOM   13026 N N   . LEU E 2 178 ? -0.584  -35.035 79.277  1.00 224.04 ? 178 LEU E N   1 
ATOM   13027 C CA  . LEU E 2 178 ? -1.461  -34.626 80.374  1.00 219.43 ? 178 LEU E CA  1 
ATOM   13028 C C   . LEU E 2 178 ? -0.978  -35.375 81.615  1.00 216.40 ? 178 LEU E C   1 
ATOM   13029 O O   . LEU E 2 178 ? -1.216  -36.580 81.748  1.00 213.71 ? 178 LEU E O   1 
ATOM   13030 C CB  . LEU E 2 178 ? -2.923  -34.924 80.061  1.00 218.17 ? 178 LEU E CB  1 
ATOM   13031 C CG  . LEU E 2 178 ? -4.013  -34.461 81.035  1.00 213.36 ? 178 LEU E CG  1 
ATOM   13032 C CD1 . LEU E 2 178 ? -5.320  -34.257 80.292  1.00 209.34 ? 178 LEU E CD1 1 
ATOM   13033 C CD2 . LEU E 2 178 ? -4.216  -35.454 82.171  1.00 208.46 ? 178 LEU E CD2 1 
ATOM   13034 N N   . LEU E 2 179 ? -0.294  -34.662 82.507  1.00 208.49 ? 179 LEU E N   1 
ATOM   13035 C CA  . LEU E 2 179 ? 0.404   -35.266 83.632  1.00 202.51 ? 179 LEU E CA  1 
ATOM   13036 C C   . LEU E 2 179 ? -0.145  -34.747 84.953  1.00 199.71 ? 179 LEU E C   1 
ATOM   13037 O O   . LEU E 2 179 ? -0.345  -33.540 85.121  1.00 201.99 ? 179 LEU E O   1 
ATOM   13038 C CB  . LEU E 2 179 ? 1.906   -34.972 83.564  1.00 201.25 ? 179 LEU E CB  1 
ATOM   13039 C CG  . LEU E 2 179 ? 2.731   -35.663 82.479  1.00 202.49 ? 179 LEU E CG  1 
ATOM   13040 C CD1 . LEU E 2 179 ? 4.139   -35.092 82.441  1.00 204.89 ? 179 LEU E CD1 1 
ATOM   13041 C CD2 . LEU E 2 179 ? 2.771   -37.159 82.722  1.00 202.65 ? 179 LEU E CD2 1 
ATOM   13042 N N   . ASN E 2 180 ? -0.356  -35.662 85.896  1.00 183.19 ? 180 ASN E N   1 
ATOM   13043 C CA  . ASN E 2 180 ? -0.680  -35.277 87.257  1.00 174.67 ? 180 ASN E CA  1 
ATOM   13044 C C   . ASN E 2 180 ? 0.563   -34.719 87.944  1.00 165.92 ? 180 ASN E C   1 
ATOM   13045 O O   . ASN E 2 180 ? 1.690   -34.999 87.529  1.00 161.51 ? 180 ASN E O   1 
ATOM   13046 C CB  . ASN E 2 180 ? -1.214  -36.473 88.043  1.00 172.55 ? 180 ASN E CB  1 
ATOM   13047 C CG  . ASN E 2 180 ? -2.706  -36.666 87.877  1.00 179.21 ? 180 ASN E CG  1 
ATOM   13048 O OD1 . ASN E 2 180 ? -3.445  -35.712 87.639  1.00 179.16 ? 180 ASN E OD1 1 
ATOM   13049 N ND2 . ASN E 2 180 ? -3.160  -37.905 88.015  1.00 181.77 ? 180 ASN E ND2 1 
ATOM   13050 N N   . PRO E 2 181 ? 0.385   -33.914 88.995  1.00 164.87 ? 181 PRO E N   1 
ATOM   13051 C CA  . PRO E 2 181 ? 1.550   -33.439 89.761  1.00 158.97 ? 181 PRO E CA  1 
ATOM   13052 C C   . PRO E 2 181 ? 2.362   -34.557 90.396  1.00 150.69 ? 181 PRO E C   1 
ATOM   13053 O O   . PRO E 2 181 ? 3.492   -34.304 90.833  1.00 148.44 ? 181 PRO E O   1 
ATOM   13054 C CB  . PRO E 2 181 ? 0.924   -32.528 90.826  1.00 153.90 ? 181 PRO E CB  1 
ATOM   13055 C CG  . PRO E 2 181 ? -0.372  -32.098 90.230  1.00 164.38 ? 181 PRO E CG  1 
ATOM   13056 C CD  . PRO E 2 181 ? -0.864  -33.276 89.445  1.00 169.83 ? 181 PRO E CD  1 
ATOM   13057 N N   . SER E 2 182 ? 1.830   -35.777 90.457  1.00 149.43 ? 182 SER E N   1 
ATOM   13058 C CA  . SER E 2 182 ? 2.529   -36.904 91.059  1.00 144.02 ? 182 SER E CA  1 
ATOM   13059 C C   . SER E 2 182 ? 3.618   -37.479 90.164  1.00 144.75 ? 182 SER E C   1 
ATOM   13060 O O   . SER E 2 182 ? 4.202   -38.511 90.512  1.00 142.59 ? 182 SER E O   1 
ATOM   13061 C CB  . SER E 2 182 ? 1.527   -38.004 91.416  1.00 143.99 ? 182 SER E CB  1 
ATOM   13062 O OG  . SER E 2 182 ? 0.531   -37.511 92.292  1.00 136.12 ? 182 SER E OG  1 
ATOM   13063 N N   . VAL E 2 183 ? 3.898   -36.853 89.022  1.00 150.02 ? 183 VAL E N   1 
ATOM   13064 C CA  . VAL E 2 183 ? 4.951   -37.326 88.133  1.00 152.86 ? 183 VAL E CA  1 
ATOM   13065 C C   . VAL E 2 183 ? 6.202   -36.454 88.200  1.00 157.28 ? 183 VAL E C   1 
ATOM   13066 O O   . VAL E 2 183 ? 7.288   -36.920 87.820  1.00 155.29 ? 183 VAL E O   1 
ATOM   13067 C CB  . VAL E 2 183 ? 4.444   -37.422 86.679  1.00 155.72 ? 183 VAL E CB  1 
ATOM   13068 C CG1 . VAL E 2 183 ? 4.386   -36.043 86.041  1.00 165.93 ? 183 VAL E CG1 1 
ATOM   13069 C CG2 . VAL E 2 183 ? 5.323   -38.359 85.869  1.00 148.00 ? 183 VAL E CG2 1 
ATOM   13070 N N   . LEU E 2 184 ? 6.089   -35.214 88.681  1.00 176.40 ? 184 LEU E N   1 
ATOM   13071 C CA  . LEU E 2 184 ? 7.220   -34.295 88.720  1.00 176.70 ? 184 LEU E CA  1 
ATOM   13072 C C   . LEU E 2 184 ? 8.296   -34.724 89.707  1.00 177.11 ? 184 LEU E C   1 
ATOM   13073 O O   . LEU E 2 184 ? 9.326   -34.049 89.803  1.00 177.19 ? 184 LEU E O   1 
ATOM   13074 C CB  . LEU E 2 184 ? 6.733   -32.885 89.060  1.00 178.74 ? 184 LEU E CB  1 
ATOM   13075 C CG  . LEU E 2 184 ? 5.860   -32.202 88.005  1.00 184.96 ? 184 LEU E CG  1 
ATOM   13076 C CD1 . LEU E 2 184 ? 5.334   -30.871 88.519  1.00 187.76 ? 184 LEU E CD1 1 
ATOM   13077 C CD2 . LEU E 2 184 ? 6.632   -32.008 86.706  1.00 184.21 ? 184 LEU E CD2 1 
ATOM   13078 N N   . ASP E 2 185 ? 8.084   -35.815 90.441  1.00 156.11 ? 185 ASP E N   1 
ATOM   13079 C CA  . ASP E 2 185 ? 9.077   -36.331 91.370  1.00 151.81 ? 185 ASP E CA  1 
ATOM   13080 C C   . ASP E 2 185 ? 9.884   -37.490 90.804  1.00 149.33 ? 185 ASP E C   1 
ATOM   13081 O O   . ASP E 2 185 ? 10.972  -37.772 91.315  1.00 145.22 ? 185 ASP E O   1 
ATOM   13082 C CB  . ASP E 2 185 ? 8.393   -36.784 92.662  1.00 147.30 ? 185 ASP E CB  1 
ATOM   13083 C CG  . ASP E 2 185 ? 7.446   -37.943 92.436  1.00 148.43 ? 185 ASP E CG  1 
ATOM   13084 O OD1 . ASP E 2 185 ? 6.866   -38.025 91.332  1.00 147.11 ? 185 ASP E OD1 1 
ATOM   13085 O OD2 . ASP E 2 185 ? 7.283   -38.770 93.355  1.00 154.42 ? 185 ASP E OD2 1 
ATOM   13086 N N   . LYS E 2 186 ? 9.383   -38.160 89.766  1.00 149.79 ? 186 LYS E N   1 
ATOM   13087 C CA  . LYS E 2 186 ? 10.067  -39.318 89.205  1.00 148.14 ? 186 LYS E CA  1 
ATOM   13088 C C   . LYS E 2 186 ? 11.261  -38.936 88.341  1.00 148.88 ? 186 LYS E C   1 
ATOM   13089 O O   . LYS E 2 186 ? 11.997  -39.825 87.898  1.00 147.59 ? 186 LYS E O   1 
ATOM   13090 C CB  . LYS E 2 186 ? 9.087   -40.158 88.383  1.00 149.09 ? 186 LYS E CB  1 
ATOM   13091 C CG  . LYS E 2 186 ? 9.407   -41.641 88.381  1.00 157.64 ? 186 LYS E CG  1 
ATOM   13092 C CD  . LYS E 2 186 ? 8.494   -42.412 87.449  1.00 179.19 ? 186 LYS E CD  1 
ATOM   13093 C CE  . LYS E 2 186 ? 8.626   -43.906 87.689  1.00 189.46 ? 186 LYS E CE  1 
ATOM   13094 N NZ  . LYS E 2 186 ? 10.050  -44.337 87.745  1.00 189.31 ? 186 LYS E NZ  1 
ATOM   13095 N N   . ILE E 2 187 ? 11.470  -37.651 88.093  1.00 155.99 ? 187 ILE E N   1 
ATOM   13096 C CA  . ILE E 2 187 ? 12.565  -37.181 87.255  1.00 168.65 ? 187 ILE E CA  1 
ATOM   13097 C C   . ILE E 2 187 ? 13.807  -36.978 88.109  1.00 186.79 ? 187 ILE E C   1 
ATOM   13098 O O   . ILE E 2 187 ? 13.732  -36.733 89.318  1.00 181.77 ? 187 ILE E O   1 
ATOM   13099 C CB  . ILE E 2 187 ? 12.175  -35.888 86.508  1.00 165.42 ? 187 ILE E CB  1 
ATOM   13100 C CG1 . ILE E 2 187 ? 11.347  -34.966 87.412  1.00 157.70 ? 187 ILE E CG1 1 
ATOM   13101 C CG2 . ILE E 2 187 ? 11.414  -36.218 85.235  1.00 167.85 ? 187 ILE E CG2 1 
ATOM   13102 C CD1 . ILE E 2 187 ? 12.170  -34.100 88.348  1.00 158.51 ? 187 ILE E CD1 1 
ATOM   13103 N N   . GLU E 2 188 ? 14.964  -37.092 87.469  1.00 247.44 ? 188 GLU E N   1 
ATOM   13104 C CA  . GLU E 2 188 ? 16.250  -36.832 88.096  1.00 247.16 ? 188 GLU E CA  1 
ATOM   13105 C C   . GLU E 2 188 ? 16.747  -35.440 87.719  1.00 246.94 ? 188 GLU E C   1 
ATOM   13106 O O   . GLU E 2 188 ? 16.149  -34.734 86.904  1.00 246.83 ? 188 GLU E O   1 
ATOM   13107 C CB  . GLU E 2 188 ? 17.271  -37.900 87.692  1.00 247.31 ? 188 GLU E CB  1 
ATOM   13108 C CG  . GLU E 2 188 ? 17.164  -38.344 86.241  1.00 247.02 ? 188 GLU E CG  1 
ATOM   13109 C CD  . GLU E 2 188 ? 18.435  -38.996 85.733  1.00 246.76 ? 188 GLU E CD  1 
ATOM   13110 O OE1 . GLU E 2 188 ? 19.291  -39.363 86.565  1.00 246.47 ? 188 GLU E OE1 1 
ATOM   13111 O OE2 . GLU E 2 188 ? 18.575  -39.147 84.501  1.00 246.45 ? 188 GLU E OE2 1 
ATOM   13112 N N   . LEU E 2 189 ? 17.866  -35.051 88.329  1.00 210.13 ? 189 LEU E N   1 
ATOM   13113 C CA  . LEU E 2 189 ? 18.495  -33.781 87.992  1.00 192.53 ? 189 LEU E CA  1 
ATOM   13114 C C   . LEU E 2 189 ? 19.206  -33.832 86.646  1.00 201.32 ? 189 LEU E C   1 
ATOM   13115 O O   . LEU E 2 189 ? 19.506  -32.777 86.076  1.00 194.50 ? 189 LEU E O   1 
ATOM   13116 C CB  . LEU E 2 189 ? 19.476  -33.381 89.095  1.00 171.37 ? 189 LEU E CB  1 
ATOM   13117 C CG  . LEU E 2 189 ? 20.222  -34.540 89.761  1.00 168.38 ? 189 LEU E CG  1 
ATOM   13118 C CD1 . LEU E 2 189 ? 21.721  -34.439 89.526  1.00 155.73 ? 189 LEU E CD1 1 
ATOM   13119 C CD2 . LEU E 2 189 ? 19.910  -34.598 91.251  1.00 139.32 ? 189 LEU E CD2 1 
ATOM   13120 N N   . ARG E 2 190 ? 19.482  -35.024 86.135  1.00 223.50 ? 190 ARG E N   1 
ATOM   13121 C CA  . ARG E 2 190 ? 20.166  -35.218 84.864  1.00 223.16 ? 190 ARG E CA  1 
ATOM   13122 C C   . ARG E 2 190 ? 19.210  -35.054 83.681  1.00 222.68 ? 190 ARG E C   1 
ATOM   13123 O O   . ARG E 2 190 ? 18.040  -35.438 83.769  1.00 222.95 ? 190 ARG E O   1 
ATOM   13124 C CB  . ARG E 2 190 ? 20.800  -36.606 84.812  1.00 224.82 ? 190 ARG E CB  1 
ATOM   13125 C CG  . ARG E 2 190 ? 21.727  -36.926 85.973  1.00 223.12 ? 190 ARG E CG  1 
ATOM   13126 C CD  . ARG E 2 190 ? 22.905  -35.976 85.978  1.00 222.66 ? 190 ARG E CD  1 
ATOM   13127 N NE  . ARG E 2 190 ? 23.408  -35.780 84.623  1.00 222.11 ? 190 ARG E NE  1 
ATOM   13128 C CZ  . ARG E 2 190 ? 23.472  -34.598 84.021  1.00 221.71 ? 190 ARG E CZ  1 
ATOM   13129 N NH1 . ARG E 2 190 ? 23.082  -33.506 84.662  1.00 221.98 ? 190 ARG E NH1 1 
ATOM   13130 N NH2 . ARG E 2 190 ? 23.933  -34.506 82.780  1.00 221.02 ? 190 ARG E NH2 1 
ATOM   13131 N N   . PRO E 2 191 ? 19.686  -34.463 82.569  1.00 197.13 ? 191 PRO E N   1 
ATOM   13132 C CA  . PRO E 2 191 ? 18.906  -34.446 81.327  1.00 192.30 ? 191 PRO E CA  1 
ATOM   13133 C C   . PRO E 2 191 ? 18.400  -35.817 80.918  1.00 202.34 ? 191 PRO E C   1 
ATOM   13134 O O   . PRO E 2 191 ? 19.186  -36.703 80.567  1.00 202.69 ? 191 PRO E O   1 
ATOM   13135 C CB  . PRO E 2 191 ? 19.913  -33.910 80.304  1.00 181.04 ? 191 PRO E CB  1 
ATOM   13136 C CG  . PRO E 2 191 ? 20.763  -33.002 81.092  1.00 181.63 ? 191 PRO E CG  1 
ATOM   13137 C CD  . PRO E 2 191 ? 20.877  -33.607 82.464  1.00 194.38 ? 191 PRO E CD  1 
ATOM   13138 N N   . THR E 2 192 ? 17.087  -35.996 80.959  1.00 224.70 ? 192 THR E N   1 
ATOM   13139 C CA  . THR E 2 192 ? 16.449  -37.244 80.577  1.00 225.08 ? 192 THR E CA  1 
ATOM   13140 C C   . THR E 2 192 ? 15.514  -36.999 79.404  1.00 223.32 ? 192 THR E C   1 
ATOM   13141 O O   . THR E 2 192 ? 14.771  -36.012 79.385  1.00 222.66 ? 192 THR E O   1 
ATOM   13142 C CB  . THR E 2 192 ? 15.669  -37.852 81.745  1.00 232.52 ? 192 THR E CB  1 
ATOM   13143 O OG1 . THR E 2 192 ? 14.698  -38.779 81.242  1.00 243.50 ? 192 THR E OG1 1 
ATOM   13144 C CG2 . THR E 2 192 ? 14.964  -36.762 82.540  1.00 226.75 ? 192 THR E CG2 1 
ATOM   13145 N N   . SER E 2 193 ? 15.556  -37.899 78.427  1.00 203.45 ? 193 SER E N   1 
ATOM   13146 C CA  . SER E 2 193 ? 14.640  -37.826 77.298  1.00 190.04 ? 193 SER E CA  1 
ATOM   13147 C C   . SER E 2 193 ? 13.335  -38.496 77.706  1.00 199.06 ? 193 SER E C   1 
ATOM   13148 O O   . SER E 2 193 ? 13.312  -39.694 78.016  1.00 213.77 ? 193 SER E O   1 
ATOM   13149 C CB  . SER E 2 193 ? 15.240  -38.493 76.063  1.00 180.49 ? 193 SER E CB  1 
ATOM   13150 O OG  . SER E 2 193 ? 16.627  -38.218 75.963  1.00 176.51 ? 193 SER E OG  1 
ATOM   13151 N N   . ILE E 2 194 ? 12.253  -37.717 77.721  1.00 190.66 ? 194 ILE E N   1 
ATOM   13152 C CA  . ILE E 2 194 ? 10.973  -38.238 78.186  1.00 198.81 ? 194 ILE E CA  1 
ATOM   13153 C C   . ILE E 2 194 ? 10.517  -39.401 77.318  1.00 203.36 ? 194 ILE E C   1 
ATOM   13154 O O   . ILE E 2 194 ? 9.783   -40.282 77.780  1.00 217.05 ? 194 ILE E O   1 
ATOM   13155 C CB  . ILE E 2 194 ? 9.925   -37.109 78.230  1.00 186.18 ? 194 ILE E CB  1 
ATOM   13156 C CG1 . ILE E 2 194 ? 8.766   -37.500 79.146  1.00 208.38 ? 194 ILE E CG1 1 
ATOM   13157 C CG2 . ILE E 2 194 ? 9.404   -36.795 76.832  1.00 178.47 ? 194 ILE E CG2 1 
ATOM   13158 C CD1 . ILE E 2 194 ? 7.728   -36.416 79.285  1.00 203.68 ? 194 ILE E CD1 1 
ATOM   13159 N N   . GLU E 2 195 ? 10.974  -39.452 76.066  0.26 184.46 ? 195 GLU E N   1 
ATOM   13160 C CA  . GLU E 2 195 ? 10.557  -40.507 75.151  0.26 180.91 ? 195 GLU E CA  1 
ATOM   13161 C C   . GLU E 2 195 ? 11.364  -41.788 75.317  0.26 183.43 ? 195 GLU E C   1 
ATOM   13162 O O   . GLU E 2 195 ? 10.888  -42.860 74.928  0.26 179.25 ? 195 GLU E O   1 
ATOM   13163 C CB  . GLU E 2 195 ? 10.666  -40.015 73.706  0.26 163.79 ? 195 GLU E CB  1 
ATOM   13164 N N   . LYS E 2 196 ? 12.570  -41.707 75.881  1.00 191.29 ? 196 LYS E N   1 
ATOM   13165 C CA  . LYS E 2 196 ? 13.448  -42.864 75.974  1.00 197.65 ? 196 LYS E CA  1 
ATOM   13166 C C   . LYS E 2 196 ? 13.653  -43.389 77.387  1.00 219.58 ? 196 LYS E C   1 
ATOM   13167 O O   . LYS E 2 196 ? 13.962  -44.575 77.542  1.00 215.07 ? 196 LYS E O   1 
ATOM   13168 C CB  . LYS E 2 196 ? 14.823  -42.531 75.373  1.00 186.17 ? 196 LYS E CB  1 
ATOM   13169 C CG  . LYS E 2 196 ? 14.755  -41.820 74.040  1.00 170.07 ? 196 LYS E CG  1 
ATOM   13170 C CD  . LYS E 2 196 ? 16.143  -41.481 73.537  1.00 157.64 ? 196 LYS E CD  1 
ATOM   13171 C CE  . LYS E 2 196 ? 16.080  -40.651 72.268  1.00 129.39 ? 196 LYS E CE  1 
ATOM   13172 N NZ  . LYS E 2 196 ? 15.288  -41.321 71.200  1.00 124.97 ? 196 LYS E NZ  1 
ATOM   13173 N N   . GLU E 2 197 ? 13.488  -42.552 78.408  1.00 263.87 ? 197 GLU E N   1 
ATOM   13174 C CA  . GLU E 2 197 ? 13.755  -42.942 79.791  1.00 270.56 ? 197 GLU E CA  1 
ATOM   13175 C C   . GLU E 2 197 ? 12.573  -42.743 80.724  1.00 283.64 ? 197 GLU E C   1 
ATOM   13176 O O   . GLU E 2 197 ? 12.288  -43.621 81.539  1.00 280.73 ? 197 GLU E O   1 
ATOM   13177 C CB  . GLU E 2 197 ? 14.967  -42.163 80.336  1.00 268.73 ? 197 GLU E CB  1 
ATOM   13178 C CG  . GLU E 2 197 ? 16.299  -42.569 79.717  1.00 264.48 ? 197 GLU E CG  1 
ATOM   13179 C CD  . GLU E 2 197 ? 16.553  -41.891 78.390  1.00 259.60 ? 197 GLU E CD  1 
ATOM   13180 O OE1 . GLU E 2 197 ? 15.759  -41.002 78.018  1.00 259.49 ? 197 GLU E OE1 1 
ATOM   13181 O OE2 . GLU E 2 197 ? 17.540  -42.246 77.717  1.00 258.80 ? 197 GLU E OE2 1 
ATOM   13182 N N   . THR E 2 198 ? 11.879  -41.607 80.641  1.00 368.01 ? 198 THR E N   1 
ATOM   13183 C CA  . THR E 2 198 ? 10.819  -41.312 81.602  1.00 368.09 ? 198 THR E CA  1 
ATOM   13184 C C   . THR E 2 198 ? 9.543   -42.085 81.288  1.00 367.82 ? 198 THR E C   1 
ATOM   13185 O O   . THR E 2 198 ? 8.951   -42.706 82.179  1.00 367.89 ? 198 THR E O   1 
ATOM   13186 C CB  . THR E 2 198 ? 10.538  -39.807 81.639  1.00 367.80 ? 198 THR E CB  1 
ATOM   13187 O OG1 . THR E 2 198 ? 11.738  -39.109 81.997  1.00 368.11 ? 198 THR E OG1 1 
ATOM   13188 C CG2 . THR E 2 198 ? 9.449   -39.484 82.654  1.00 367.73 ? 198 THR E CG2 1 
ATOM   13189 N N   . PHE E 2 199 ? 9.101   -42.047 80.032  1.00 283.61 ? 199 PHE E N   1 
ATOM   13190 C CA  . PHE E 2 199 ? 7.892   -42.773 79.650  1.00 264.82 ? 199 PHE E CA  1 
ATOM   13191 C C   . PHE E 2 199 ? 7.974   -44.274 79.922  1.00 260.96 ? 199 PHE E C   1 
ATOM   13192 O O   . PHE E 2 199 ? 6.980   -44.831 80.421  1.00 253.65 ? 199 PHE E O   1 
ATOM   13193 C CB  . PHE E 2 199 ? 7.570   -42.507 78.172  1.00 242.26 ? 199 PHE E CB  1 
ATOM   13194 C CG  . PHE E 2 199 ? 6.914   -41.178 77.923  1.00 233.71 ? 199 PHE E CG  1 
ATOM   13195 C CD1 . PHE E 2 199 ? 6.266   -40.507 78.946  1.00 237.74 ? 199 PHE E CD1 1 
ATOM   13196 C CD2 . PHE E 2 199 ? 6.942   -40.603 76.663  1.00 218.88 ? 199 PHE E CD2 1 
ATOM   13197 C CE1 . PHE E 2 199 ? 5.660   -39.285 78.717  1.00 224.07 ? 199 PHE E CE1 1 
ATOM   13198 C CE2 . PHE E 2 199 ? 6.338   -39.381 76.429  1.00 217.72 ? 199 PHE E CE2 1 
ATOM   13199 C CZ  . PHE E 2 199 ? 5.696   -38.722 77.457  1.00 220.43 ? 199 PHE E CZ  1 
ATOM   13200 N N   . PRO E 2 200 ? 9.072   -44.981 79.627  1.00 259.24 ? 200 PRO E N   1 
ATOM   13201 C CA  . PRO E 2 200 ? 9.131   -46.406 80.001  1.00 249.97 ? 200 PRO E CA  1 
ATOM   13202 C C   . PRO E 2 200 ? 9.084   -46.654 81.500  1.00 252.71 ? 200 PRO E C   1 
ATOM   13203 O O   . PRO E 2 200 ? 8.707   -47.759 81.911  1.00 245.76 ? 200 PRO E O   1 
ATOM   13204 C CB  . PRO E 2 200 ? 10.461  -46.880 79.396  1.00 234.27 ? 200 PRO E CB  1 
ATOM   13205 C CG  . PRO E 2 200 ? 11.247  -45.641 79.159  1.00 245.78 ? 200 PRO E CG  1 
ATOM   13206 C CD  . PRO E 2 200 ? 10.239  -44.596 78.813  1.00 247.08 ? 200 PRO E CD  1 
ATOM   13207 N N   . LYS E 2 201 ? 9.459   -45.677 82.329  1.00 256.60 ? 201 LYS E N   1 
ATOM   13208 C CA  . LYS E 2 201 ? 9.397   -45.880 83.774  1.00 249.97 ? 201 LYS E CA  1 
ATOM   13209 C C   . LYS E 2 201 ? 7.957   -45.965 84.267  1.00 243.36 ? 201 LYS E C   1 
ATOM   13210 O O   . LYS E 2 201 ? 7.656   -46.730 85.190  1.00 233.08 ? 201 LYS E O   1 
ATOM   13211 C CB  . LYS E 2 201 ? 10.148  -44.767 84.505  1.00 249.39 ? 201 LYS E CB  1 
ATOM   13212 C CG  . LYS E 2 201 ? 11.658  -44.941 84.534  1.00 246.04 ? 201 LYS E CG  1 
ATOM   13213 C CD  . LYS E 2 201 ? 12.320  -43.842 85.349  1.00 232.73 ? 201 LYS E CD  1 
ATOM   13214 C CE  . LYS E 2 201 ? 13.821  -44.055 85.454  1.00 227.85 ? 201 LYS E CE  1 
ATOM   13215 N NZ  . LYS E 2 201 ? 14.466  -43.014 86.301  1.00 220.14 ? 201 LYS E NZ  1 
ATOM   13216 N N   . ILE E 2 202 ? 7.051   -45.191 83.666  1.00 250.86 ? 202 ILE E N   1 
ATOM   13217 C CA  . ILE E 2 202 ? 5.647   -45.246 84.057  1.00 245.74 ? 202 ILE E CA  1 
ATOM   13218 C C   . ILE E 2 202 ? 4.880   -46.336 83.317  1.00 241.86 ? 202 ILE E C   1 
ATOM   13219 O O   . ILE E 2 202 ? 3.853   -46.812 83.824  1.00 232.56 ? 202 ILE E O   1 
ATOM   13220 C CB  . ILE E 2 202 ? 4.965   -43.884 83.830  1.00 245.40 ? 202 ILE E CB  1 
ATOM   13221 C CG1 . ILE E 2 202 ? 5.921   -42.741 84.171  1.00 246.18 ? 202 ILE E CG1 1 
ATOM   13222 C CG2 . ILE E 2 202 ? 3.699   -43.770 84.670  1.00 234.24 ? 202 ILE E CG2 1 
ATOM   13223 C CD1 . ILE E 2 202 ? 5.345   -41.375 83.903  1.00 244.72 ? 202 ILE E CD1 1 
ATOM   13224 N N   . ALA E 2 203 ? 5.353   -46.755 82.141  1.00 260.81 ? 203 ALA E N   1 
ATOM   13225 C CA  . ALA E 2 203 ? 4.676   -47.816 81.403  1.00 259.80 ? 203 ALA E CA  1 
ATOM   13226 C C   . ALA E 2 203 ? 4.803   -49.154 82.119  1.00 260.32 ? 203 ALA E C   1 
ATOM   13227 O O   . ALA E 2 203 ? 3.838   -49.925 82.181  1.00 260.25 ? 203 ALA E O   1 
ATOM   13228 C CB  . ALA E 2 203 ? 5.236   -47.909 79.983  1.00 259.75 ? 203 ALA E CB  1 
ATOM   13229 N N   . ALA E 2 204 ? 5.986   -49.448 82.666  1.00 236.66 ? 204 ALA E N   1 
ATOM   13230 C CA  . ALA E 2 204 ? 6.174   -50.681 83.419  1.00 228.94 ? 204 ALA E CA  1 
ATOM   13231 C C   . ALA E 2 204 ? 5.364   -50.703 84.708  1.00 218.34 ? 204 ALA E C   1 
ATOM   13232 O O   . ALA E 2 204 ? 5.099   -51.786 85.241  1.00 216.57 ? 204 ALA E O   1 
ATOM   13233 C CB  . ALA E 2 204 ? 7.658   -50.886 83.732  1.00 231.35 ? 204 ALA E CB  1 
ATOM   13234 N N   . ALA E 2 205 ? 4.965   -49.538 85.219  1.00 222.23 ? 205 ALA E N   1 
ATOM   13235 C CA  . ALA E 2 205 ? 4.113   -49.472 86.398  1.00 210.28 ? 205 ALA E CA  1 
ATOM   13236 C C   . ALA E 2 205 ? 2.636   -49.634 86.070  1.00 212.29 ? 205 ALA E C   1 
ATOM   13237 O O   . ALA E 2 205 ? 1.832   -49.805 86.993  1.00 203.07 ? 205 ALA E O   1 
ATOM   13238 C CB  . ALA E 2 205 ? 4.333   -48.148 87.136  1.00 200.74 ? 205 ALA E CB  1 
ATOM   13239 N N   . GLN E 2 206 ? 2.269   -49.587 84.786  1.00 208.58 ? 206 GLN E N   1 
ATOM   13240 C CA  . GLN E 2 206 ? 0.883   -49.745 84.340  1.00 205.58 ? 206 GLN E CA  1 
ATOM   13241 C C   . GLN E 2 206 ? -0.046  -48.738 85.018  1.00 208.06 ? 206 GLN E C   1 
ATOM   13242 O O   . GLN E 2 206 ? -1.178  -49.058 85.386  1.00 203.56 ? 206 GLN E O   1 
ATOM   13243 C CB  . GLN E 2 206 ? 0.392   -51.178 84.568  1.00 202.14 ? 206 GLN E CB  1 
ATOM   13244 C CG  . GLN E 2 206 ? 1.303   -52.261 83.993  1.00 205.18 ? 206 GLN E CG  1 
ATOM   13245 C CD  . GLN E 2 206 ? 1.195   -52.405 82.482  1.00 208.71 ? 206 GLN E CD  1 
ATOM   13246 O OE1 . GLN E 2 206 ? 1.231   -51.422 81.741  1.00 208.20 ? 206 GLN E OE1 1 
ATOM   13247 N NE2 . GLN E 2 206 ? 1.065   -53.642 82.020  1.00 209.32 ? 206 GLN E NE2 1 
ATOM   13248 N N   . GLY E 2 207 ? 0.437   -47.510 85.182  1.00 238.61 ? 207 GLY E N   1 
ATOM   13249 C CA  . GLY E 2 207 ? -0.348  -46.467 85.812  1.00 238.50 ? 207 GLY E CA  1 
ATOM   13250 C C   . GLY E 2 207 ? -0.676  -45.337 84.860  1.00 236.65 ? 207 GLY E C   1 
ATOM   13251 O O   . GLY E 2 207 ? -1.042  -44.237 85.286  1.00 235.95 ? 207 GLY E O   1 
ATOM   13252 N N   . LEU E 2 208 ? -0.551  -45.602 83.563  1.00 211.03 ? 208 LEU E N   1 
ATOM   13253 C CA  . LEU E 2 208 ? -0.820  -44.623 82.522  1.00 198.99 ? 208 LEU E CA  1 
ATOM   13254 C C   . LEU E 2 208 ? -1.858  -45.157 81.542  1.00 196.66 ? 208 LEU E C   1 
ATOM   13255 O O   . LEU E 2 208 ? -2.283  -46.314 81.609  1.00 195.94 ? 208 LEU E O   1 
ATOM   13256 C CB  . LEU E 2 208 ? 0.468   -44.235 81.782  1.00 197.60 ? 208 LEU E CB  1 
ATOM   13257 C CG  . LEU E 2 208 ? 1.589   -45.272 81.667  1.00 209.60 ? 208 LEU E CG  1 
ATOM   13258 C CD1 . LEU E 2 208 ? 1.133   -46.536 80.949  1.00 213.28 ? 208 LEU E CD1 1 
ATOM   13259 C CD2 . LEU E 2 208 ? 2.782   -44.657 80.959  1.00 210.36 ? 208 LEU E CD2 1 
ATOM   13260 N N   . TYR E 2 209 ? -2.268  -44.282 80.628  1.00 191.27 ? 209 TYR E N   1 
ATOM   13261 C CA  . TYR E 2 209 ? -3.227  -44.624 79.588  1.00 186.75 ? 209 TYR E CA  1 
ATOM   13262 C C   . TYR E 2 209 ? -2.996  -43.717 78.387  1.00 184.42 ? 209 TYR E C   1 
ATOM   13263 O O   . TYR E 2 209 ? -2.319  -42.691 78.483  1.00 182.24 ? 209 TYR E O   1 
ATOM   13264 C CB  . TYR E 2 209 ? -4.664  -44.497 80.100  1.00 189.45 ? 209 TYR E CB  1 
ATOM   13265 C CG  . TYR E 2 209 ? -5.000  -43.093 80.529  1.00 190.17 ? 209 TYR E CG  1 
ATOM   13266 C CD1 . TYR E 2 209 ? -5.601  -42.205 79.652  1.00 188.57 ? 209 TYR E CD1 1 
ATOM   13267 C CD2 . TYR E 2 209 ? -4.699  -42.650 81.810  1.00 186.75 ? 209 TYR E CD2 1 
ATOM   13268 C CE1 . TYR E 2 209 ? -5.905  -40.922 80.039  1.00 187.77 ? 209 TYR E CE1 1 
ATOM   13269 C CE2 . TYR E 2 209 ? -4.991  -41.366 82.205  1.00 186.33 ? 209 TYR E CE2 1 
ATOM   13270 C CZ  . TYR E 2 209 ? -5.599  -40.509 81.317  1.00 187.81 ? 209 TYR E CZ  1 
ATOM   13271 O OH  . TYR E 2 209 ? -5.896  -39.228 81.703  1.00 185.98 ? 209 TYR E OH  1 
ATOM   13272 N N   . VAL E 2 212 ? -6.372  -41.618 71.402  1.00 197.72 ? 212 VAL E N   1 
ATOM   13273 C CA  . VAL E 2 212 ? -6.101  -41.485 69.974  1.00 202.84 ? 212 VAL E CA  1 
ATOM   13274 C C   . VAL E 2 212 ? -6.510  -40.097 69.498  1.00 210.61 ? 212 VAL E C   1 
ATOM   13275 O O   . VAL E 2 212 ? -7.543  -39.559 69.914  1.00 210.05 ? 212 VAL E O   1 
ATOM   13276 C CB  . VAL E 2 212 ? -6.832  -42.585 69.180  1.00 204.36 ? 212 VAL E CB  1 
ATOM   13277 C CG1 . VAL E 2 212 ? -6.477  -42.507 67.704  1.00 205.51 ? 212 VAL E CG1 1 
ATOM   13278 C CG2 . VAL E 2 212 ? -6.497  -43.958 69.745  1.00 205.20 ? 212 VAL E CG2 1 
ATOM   13279 N N   . LEU E 2 213 ? -5.689  -39.511 68.623  1.00 231.61 ? 213 LEU E N   1 
ATOM   13280 C CA  . LEU E 2 213 ? -5.951  -38.180 68.085  1.00 229.25 ? 213 LEU E CA  1 
ATOM   13281 C C   . LEU E 2 213 ? -6.870  -38.278 66.874  1.00 227.68 ? 213 LEU E C   1 
ATOM   13282 O O   . LEU E 2 213 ? -6.489  -38.900 65.873  1.00 227.44 ? 213 LEU E O   1 
ATOM   13283 C CB  . LEU E 2 213 ? -4.654  -37.495 67.687  1.00 229.40 ? 213 LEU E CB  1 
ATOM   13284 C CG  . LEU E 2 213 ? -4.805  -36.142 66.984  1.00 228.01 ? 213 LEU E CG  1 
ATOM   13285 C CD1 . LEU E 2 213 ? -5.472  -35.127 67.899  1.00 228.18 ? 213 LEU E CD1 1 
ATOM   13286 C CD2 . LEU E 2 213 ? -3.460  -35.626 66.490  1.00 227.89 ? 213 LEU E CD2 1 
ATOM   13287 N N   . PRO E 2 214 ? -8.069  -37.694 66.916  1.00 207.24 ? 214 PRO E N   1 
ATOM   13288 C CA  . PRO E 2 214 ? -8.964  -37.761 65.755  1.00 196.37 ? 214 PRO E CA  1 
ATOM   13289 C C   . PRO E 2 214 ? -8.749  -36.612 64.783  1.00 187.42 ? 214 PRO E C   1 
ATOM   13290 O O   . PRO E 2 214 ? -9.712  -36.074 64.228  1.00 184.79 ? 214 PRO E O   1 
ATOM   13291 C CB  . PRO E 2 214 ? -10.352 -37.696 66.396  1.00 195.98 ? 214 PRO E CB  1 
ATOM   13292 C CG  . PRO E 2 214 ? -10.137 -36.810 67.585  1.00 202.32 ? 214 PRO E CG  1 
ATOM   13293 C CD  . PRO E 2 214 ? -8.732  -37.089 68.084  1.00 207.75 ? 214 PRO E CD  1 
ATOM   13294 N N   . GLY E 2 215 ? -7.494  -36.232 64.559  1.00 187.44 ? 215 GLY E N   1 
ATOM   13295 C CA  . GLY E 2 215 ? -7.209  -35.105 63.695  1.00 164.47 ? 215 GLY E CA  1 
ATOM   13296 C C   . GLY E 2 215 ? -5.903  -35.236 62.942  1.00 147.24 ? 215 GLY E C   1 
ATOM   13297 O O   . GLY E 2 215 ? -5.349  -36.334 62.824  1.00 149.02 ? 215 GLY E O   1 
ATOM   13298 N N   . PHE E 2 216 ? -5.399  -34.117 62.433  1.00 132.47 ? 216 PHE E N   1 
ATOM   13299 C CA  . PHE E 2 216 ? -4.178  -34.106 61.645  1.00 129.32 ? 216 PHE E CA  1 
ATOM   13300 C C   . PHE E 2 216 ? -2.965  -33.932 62.546  1.00 132.06 ? 216 PHE E C   1 
ATOM   13301 O O   . PHE E 2 216 ? -3.052  -33.369 63.641  1.00 129.67 ? 216 PHE E O   1 
ATOM   13302 C CB  . PHE E 2 216 ? -4.210  -32.984 60.603  1.00 123.48 ? 216 PHE E CB  1 
ATOM   13303 C CG  . PHE E 2 216 ? -4.265  -31.599 61.198  1.00 121.98 ? 216 PHE E CG  1 
ATOM   13304 C CD1 . PHE E 2 216 ? -5.476  -31.030 61.552  1.00 122.76 ? 216 PHE E CD1 1 
ATOM   13305 C CD2 . PHE E 2 216 ? -3.106  -30.861 61.392  1.00 121.40 ? 216 PHE E CD2 1 
ATOM   13306 C CE1 . PHE E 2 216 ? -5.531  -29.759 62.096  1.00 120.96 ? 216 PHE E CE1 1 
ATOM   13307 C CE2 . PHE E 2 216 ? -3.157  -29.587 61.936  1.00 118.83 ? 216 PHE E CE2 1 
ATOM   13308 C CZ  . PHE E 2 216 ? -4.372  -29.037 62.286  1.00 117.25 ? 216 PHE E CZ  1 
ATOM   13309 N N   . TRP E 2 217 ? -1.825  -34.421 62.069  1.00 140.93 ? 217 TRP E N   1 
ATOM   13310 C CA  . TRP E 2 217 ? -0.563  -34.300 62.781  1.00 141.16 ? 217 TRP E CA  1 
ATOM   13311 C C   . TRP E 2 217 ? 0.528   -33.910 61.799  1.00 137.19 ? 217 TRP E C   1 
ATOM   13312 O O   . TRP E 2 217 ? 0.595   -34.439 60.686  1.00 136.68 ? 217 TRP E O   1 
ATOM   13313 C CB  . TRP E 2 217 ? -0.173  -35.598 63.492  1.00 147.17 ? 217 TRP E CB  1 
ATOM   13314 C CG  . TRP E 2 217 ? 1.121   -35.476 64.238  1.00 148.96 ? 217 TRP E CG  1 
ATOM   13315 C CD1 . TRP E 2 217 ? 1.292   -35.036 65.518  1.00 154.62 ? 217 TRP E CD1 1 
ATOM   13316 C CD2 . TRP E 2 217 ? 2.429   -35.786 63.741  1.00 150.94 ? 217 TRP E CD2 1 
ATOM   13317 N NE1 . TRP E 2 217 ? 2.626   -35.058 65.851  1.00 158.49 ? 217 TRP E NE1 1 
ATOM   13318 C CE2 . TRP E 2 217 ? 3.345   -35.514 64.777  1.00 151.29 ? 217 TRP E CE2 1 
ATOM   13319 C CE3 . TRP E 2 217 ? 2.913   -36.269 62.522  1.00 150.64 ? 217 TRP E CE3 1 
ATOM   13320 C CZ2 . TRP E 2 217 ? 4.717   -35.711 64.631  1.00 149.69 ? 217 TRP E CZ2 1 
ATOM   13321 C CZ3 . TRP E 2 217 ? 4.275   -36.464 62.379  1.00 152.21 ? 217 TRP E CZ3 1 
ATOM   13322 C CH2 . TRP E 2 217 ? 5.161   -36.186 63.428  1.00 150.91 ? 217 TRP E CH2 1 
ATOM   13323 N N   . MET E 2 218 ? 1.379   -32.981 62.223  1.00 131.96 ? 218 MET E N   1 
ATOM   13324 C CA  . MET E 2 218 ? 2.459   -32.479 61.387  1.00 128.38 ? 218 MET E CA  1 
ATOM   13325 C C   . MET E 2 218 ? 3.590   -31.998 62.281  1.00 126.77 ? 218 MET E C   1 
ATOM   13326 O O   . MET E 2 218 ? 3.365   -31.189 63.186  1.00 124.12 ? 218 MET E O   1 
ATOM   13327 C CB  . MET E 2 218 ? 1.970   -31.335 60.491  1.00 122.65 ? 218 MET E CB  1 
ATOM   13328 C CG  . MET E 2 218 ? 3.076   -30.635 59.714  1.00 116.25 ? 218 MET E CG  1 
ATOM   13329 S SD  . MET E 2 218 ? 3.852   -31.681 58.474  1.00 114.36 ? 218 MET E SD  1 
ATOM   13330 C CE  . MET E 2 218 ? 2.472   -31.977 57.372  1.00 114.15 ? 218 MET E CE  1 
ATOM   13331 N N   . ASP E 2 219 ? 4.797   -32.494 62.026  1.00 123.22 ? 219 ASP E N   1 
ATOM   13332 C CA  . ASP E 2 219 ? 5.991   -32.038 62.725  1.00 118.83 ? 219 ASP E CA  1 
ATOM   13333 C C   . ASP E 2 219 ? 6.659   -30.996 61.837  1.00 118.42 ? 219 ASP E C   1 
ATOM   13334 O O   . ASP E 2 219 ? 7.277   -31.338 60.823  1.00 116.59 ? 219 ASP E O   1 
ATOM   13335 C CB  . ASP E 2 219 ? 6.936   -33.198 63.032  1.00 119.43 ? 219 ASP E CB  1 
ATOM   13336 C CG  . ASP E 2 219 ? 8.038   -32.814 64.005  1.00 119.47 ? 219 ASP E CG  1 
ATOM   13337 O OD1 . ASP E 2 219 ? 8.663   -31.746 63.823  1.00 118.29 ? 219 ASP E OD1 1 
ATOM   13338 O OD2 . ASP E 2 219 ? 8.277   -33.580 64.962  1.00 123.02 ? 219 ASP E OD2 1 
ATOM   13339 N N   . ILE E 2 220 ? 6.528   -29.727 62.214  1.00 119.87 ? 220 ILE E N   1 
ATOM   13340 C CA  . ILE E 2 220 ? 7.086   -28.625 61.441  1.00 117.75 ? 220 ILE E CA  1 
ATOM   13341 C C   . ILE E 2 220 ? 8.521   -28.435 61.920  1.00 116.71 ? 220 ILE E C   1 
ATOM   13342 O O   . ILE E 2 220 ? 8.765   -27.873 62.990  1.00 115.74 ? 220 ILE E O   1 
ATOM   13343 C CB  . ILE E 2 220 ? 6.260   -27.346 61.591  1.00 118.44 ? 220 ILE E CB  1 
ATOM   13344 C CG1 . ILE E 2 220 ? 4.817   -27.575 61.130  1.00 118.20 ? 220 ILE E CG1 1 
ATOM   13345 C CG2 . ILE E 2 220 ? 6.895   -26.211 60.801  1.00 121.20 ? 220 ILE E CG2 1 
ATOM   13346 C CD1 . ILE E 2 220 ? 3.868   -27.975 62.245  1.00 116.59 ? 220 ILE E CD1 1 
ATOM   13347 N N   . GLY E 2 221 ? 9.474   -28.911 61.125  1.00 118.52 ? 221 GLY E N   1 
ATOM   13348 C CA  . GLY E 2 221 ? 10.876  -28.766 61.457  1.00 121.96 ? 221 GLY E CA  1 
ATOM   13349 C C   . GLY E 2 221 ? 11.687  -28.184 60.320  1.00 123.86 ? 221 GLY E C   1 
ATOM   13350 O O   . GLY E 2 221 ? 12.920  -28.163 60.369  1.00 127.29 ? 221 GLY E O   1 
ATOM   13351 N N   . GLN E 2 222 ? 11.000  -27.709 59.287  1.00 120.10 ? 222 GLN E N   1 
ATOM   13352 C CA  . GLN E 2 222 ? 11.636  -27.120 58.120  1.00 120.86 ? 222 GLN E CA  1 
ATOM   13353 C C   . GLN E 2 222 ? 10.673  -26.116 57.510  1.00 122.02 ? 222 GLN E C   1 
ATOM   13354 O O   . GLN E 2 222 ? 9.454   -26.306 57.591  1.00 122.96 ? 222 GLN E O   1 
ATOM   13355 C CB  . GLN E 2 222 ? 12.033  -28.189 57.090  1.00 124.47 ? 222 GLN E CB  1 
ATOM   13356 C CG  . GLN E 2 222 ? 10.887  -29.073 56.638  1.00 127.08 ? 222 GLN E CG  1 
ATOM   13357 C CD  . GLN E 2 222 ? 11.356  -30.302 55.879  1.00 129.31 ? 222 GLN E CD  1 
ATOM   13358 O OE1 . GLN E 2 222 ? 12.517  -30.698 55.973  1.00 131.07 ? 222 GLN E OE1 1 
ATOM   13359 N NE2 . GLN E 2 222 ? 10.449  -30.916 55.127  1.00 131.12 ? 222 GLN E NE2 1 
ATOM   13360 N N   . PRO E 2 223 ? 11.181  -25.033 56.915  1.00 122.16 ? 223 PRO E N   1 
ATOM   13361 C CA  . PRO E 2 223 ? 10.278  -23.993 56.395  1.00 122.00 ? 223 PRO E CA  1 
ATOM   13362 C C   . PRO E 2 223 ? 9.355   -24.479 55.293  1.00 121.55 ? 223 PRO E C   1 
ATOM   13363 O O   . PRO E 2 223 ? 8.305   -23.863 55.073  1.00 122.37 ? 223 PRO E O   1 
ATOM   13364 C CB  . PRO E 2 223 ? 11.241  -22.912 55.884  1.00 118.01 ? 223 PRO E CB  1 
ATOM   13365 C CG  . PRO E 2 223 ? 12.540  -23.619 55.671  1.00 121.93 ? 223 PRO E CG  1 
ATOM   13366 C CD  . PRO E 2 223 ? 12.598  -24.679 56.728  1.00 122.29 ? 223 PRO E CD  1 
ATOM   13367 N N   . ARG E 2 224 ? 9.702   -25.560 54.593  1.00 125.94 ? 224 ARG E N   1 
ATOM   13368 C CA  . ARG E 2 224 ? 8.835   -26.071 53.541  1.00 124.83 ? 224 ARG E CA  1 
ATOM   13369 C C   . ARG E 2 224 ? 7.622   -26.802 54.101  1.00 123.87 ? 224 ARG E C   1 
ATOM   13370 O O   . ARG E 2 224 ? 6.667   -27.047 53.356  1.00 122.70 ? 224 ARG E O   1 
ATOM   13371 C CB  . ARG E 2 224 ? 9.618   -26.994 52.609  1.00 126.34 ? 224 ARG E CB  1 
ATOM   13372 C CG  . ARG E 2 224 ? 10.149  -28.236 53.285  1.00 128.34 ? 224 ARG E CG  1 
ATOM   13373 C CD  . ARG E 2 224 ? 11.026  -29.044 52.352  1.00 129.05 ? 224 ARG E CD  1 
ATOM   13374 N NE  . ARG E 2 224 ? 12.091  -28.220 51.791  1.00 136.41 ? 224 ARG E NE  1 
ATOM   13375 C CZ  . ARG E 2 224 ? 13.238  -27.960 52.412  1.00 139.89 ? 224 ARG E CZ  1 
ATOM   13376 N NH1 . ARG E 2 224 ? 13.469  -28.455 53.621  1.00 135.44 ? 224 ARG E NH1 1 
ATOM   13377 N NH2 . ARG E 2 224 ? 14.152  -27.199 51.826  1.00 147.82 ? 224 ARG E NH2 1 
ATOM   13378 N N   . ASP E 2 225 ? 7.640   -27.165 55.387  1.00 125.23 ? 225 ASP E N   1 
ATOM   13379 C CA  . ASP E 2 225 ? 6.477   -27.797 56.000  1.00 125.40 ? 225 ASP E CA  1 
ATOM   13380 C C   . ASP E 2 225 ? 5.347   -26.812 56.252  1.00 126.40 ? 225 ASP E C   1 
ATOM   13381 O O   . ASP E 2 225 ? 4.250   -27.238 56.629  1.00 125.90 ? 225 ASP E O   1 
ATOM   13382 C CB  . ASP E 2 225 ? 6.859   -28.470 57.322  1.00 122.28 ? 225 ASP E CB  1 
ATOM   13383 C CG  . ASP E 2 225 ? 7.663   -29.735 57.121  1.00 123.26 ? 225 ASP E CG  1 
ATOM   13384 O OD1 . ASP E 2 225 ? 7.811   -30.162 55.957  1.00 126.99 ? 225 ASP E OD1 1 
ATOM   13385 O OD2 . ASP E 2 225 ? 8.139   -30.308 58.124  1.00 119.92 ? 225 ASP E OD2 1 
ATOM   13386 N N   . TYR E 2 226 ? 5.584   -25.516 56.043  1.00 130.39 ? 226 TYR E N   1 
ATOM   13387 C CA  . TYR E 2 226 ? 4.544   -24.525 56.285  1.00 129.86 ? 226 TYR E CA  1 
ATOM   13388 C C   . TYR E 2 226 ? 3.466   -24.570 55.211  1.00 131.55 ? 226 TYR E C   1 
ATOM   13389 O O   . TYR E 2 226 ? 2.300   -24.281 55.496  1.00 133.60 ? 226 TYR E O   1 
ATOM   13390 C CB  . TYR E 2 226 ? 5.161   -23.129 56.367  1.00 131.01 ? 226 TYR E CB  1 
ATOM   13391 C CG  . TYR E 2 226 ? 5.692   -22.765 57.738  1.00 136.44 ? 226 TYR E CG  1 
ATOM   13392 C CD1 . TYR E 2 226 ? 5.029   -23.164 58.892  1.00 140.62 ? 226 TYR E CD1 1 
ATOM   13393 C CD2 . TYR E 2 226 ? 6.859   -22.026 57.877  1.00 138.32 ? 226 TYR E CD2 1 
ATOM   13394 C CE1 . TYR E 2 226 ? 5.513   -22.833 60.146  1.00 141.41 ? 226 TYR E CE1 1 
ATOM   13395 C CE2 . TYR E 2 226 ? 7.350   -21.691 59.124  1.00 139.61 ? 226 TYR E CE2 1 
ATOM   13396 C CZ  . TYR E 2 226 ? 6.674   -22.096 60.255  1.00 140.32 ? 226 TYR E CZ  1 
ATOM   13397 O OH  . TYR E 2 226 ? 7.162   -21.763 61.498  1.00 136.89 ? 226 TYR E OH  1 
ATOM   13398 N N   . ILE E 2 227 ? 3.829   -24.928 53.978  1.00 146.04 ? 227 ILE E N   1 
ATOM   13399 C CA  . ILE E 2 227 ? 2.829   -24.988 52.916  1.00 144.04 ? 227 ILE E CA  1 
ATOM   13400 C C   . ILE E 2 227 ? 2.035   -26.287 52.985  1.00 144.12 ? 227 ILE E C   1 
ATOM   13401 O O   . ILE E 2 227 ? 0.843   -26.306 52.657  1.00 144.77 ? 227 ILE E O   1 
ATOM   13402 C CB  . ILE E 2 227 ? 3.481   -24.802 51.534  1.00 142.12 ? 227 ILE E CB  1 
ATOM   13403 C CG1 . ILE E 2 227 ? 4.611   -25.813 51.320  1.00 143.77 ? 227 ILE E CG1 1 
ATOM   13404 C CG2 . ILE E 2 227 ? 3.988   -23.381 51.376  1.00 141.02 ? 227 ILE E CG2 1 
ATOM   13405 C CD1 . ILE E 2 227 ? 5.340   -25.650 50.000  1.00 142.05 ? 227 ILE E CD1 1 
ATOM   13406 N N   . THR E 2 228 ? 2.665   -27.385 53.404  1.00 131.21 ? 228 THR E N   1 
ATOM   13407 C CA  . THR E 2 228 ? 1.935   -28.640 53.539  1.00 127.05 ? 228 THR E CA  1 
ATOM   13408 C C   . THR E 2 228 ? 1.216   -28.738 54.878  1.00 125.01 ? 228 THR E C   1 
ATOM   13409 O O   . THR E 2 228 ? 0.182   -29.408 54.971  1.00 124.01 ? 228 THR E O   1 
ATOM   13410 C CB  . THR E 2 228 ? 2.881   -29.829 53.356  1.00 121.11 ? 228 THR E CB  1 
ATOM   13411 O OG1 . THR E 2 228 ? 2.146   -31.053 53.485  1.00 120.92 ? 228 THR E OG1 1 
ATOM   13412 C CG2 . THR E 2 228 ? 3.989   -29.800 54.393  1.00 118.43 ? 228 THR E CG2 1 
ATOM   13413 N N   . GLY E 2 229 ? 1.742   -28.089 55.919  1.00 125.64 ? 229 GLY E N   1 
ATOM   13414 C CA  . GLY E 2 229 ? 1.042   -28.058 57.190  1.00 127.51 ? 229 GLY E CA  1 
ATOM   13415 C C   . GLY E 2 229 ? -0.158  -27.134 57.190  1.00 130.74 ? 229 GLY E C   1 
ATOM   13416 O O   . GLY E 2 229 ? -1.112  -27.351 57.943  1.00 127.15 ? 229 GLY E O   1 
ATOM   13417 N N   . LEU E 2 230 ? -0.130  -26.094 56.352  1.00 143.00 ? 230 LEU E N   1 
ATOM   13418 C CA  . LEU E 2 230 ? -1.272  -25.193 56.250  1.00 141.91 ? 230 LEU E CA  1 
ATOM   13419 C C   . LEU E 2 230 ? -2.463  -25.861 55.574  1.00 140.51 ? 230 LEU E C   1 
ATOM   13420 O O   . LEU E 2 230 ? -3.613  -25.497 55.850  1.00 140.91 ? 230 LEU E O   1 
ATOM   13421 C CB  . LEU E 2 230 ? -0.870  -23.927 55.495  1.00 140.80 ? 230 LEU E CB  1 
ATOM   13422 C CG  . LEU E 2 230 ? -1.897  -22.799 55.437  1.00 141.27 ? 230 LEU E CG  1 
ATOM   13423 C CD1 . LEU E 2 230 ? -1.281  -21.509 55.946  1.00 140.93 ? 230 LEU E CD1 1 
ATOM   13424 C CD2 . LEU E 2 230 ? -2.419  -22.627 54.021  1.00 143.25 ? 230 LEU E CD2 1 
ATOM   13425 N N   . ARG E 2 231 ? -2.214  -26.833 54.694  1.00 127.57 ? 231 ARG E N   1 
ATOM   13426 C CA  . ARG E 2 231 ? -3.310  -27.589 54.093  1.00 126.04 ? 231 ARG E CA  1 
ATOM   13427 C C   . ARG E 2 231 ? -4.078  -28.362 55.157  1.00 122.71 ? 231 ARG E C   1 
ATOM   13428 O O   . ARG E 2 231 ? -5.313  -28.317 55.206  1.00 120.06 ? 231 ARG E O   1 
ATOM   13429 C CB  . ARG E 2 231 ? -2.768  -28.532 53.016  1.00 128.19 ? 231 ARG E CB  1 
ATOM   13430 C CG  . ARG E 2 231 ? -3.796  -29.502 52.435  1.00 133.76 ? 231 ARG E CG  1 
ATOM   13431 C CD  . ARG E 2 231 ? -5.086  -28.800 52.029  1.00 144.17 ? 231 ARG E CD  1 
ATOM   13432 N NE  . ARG E 2 231 ? -5.609  -29.267 50.749  1.00 153.99 ? 231 ARG E NE  1 
ATOM   13433 C CZ  . ARG E 2 231 ? -6.705  -28.784 50.170  1.00 155.70 ? 231 ARG E CZ  1 
ATOM   13434 N NH1 . ARG E 2 231 ? -7.397  -27.817 50.757  1.00 152.79 ? 231 ARG E NH1 1 
ATOM   13435 N NH2 . ARG E 2 231 ? -7.111  -29.268 49.003  1.00 152.73 ? 231 ARG E NH2 1 
ATOM   13436 N N   . LEU E 2 232 ? -3.357  -29.084 56.018  1.00 120.42 ? 232 LEU E N   1 
ATOM   13437 C CA  . LEU E 2 232 ? -4.004  -29.832 57.088  1.00 116.67 ? 232 LEU E CA  1 
ATOM   13438 C C   . LEU E 2 232 ? -4.769  -28.910 58.028  1.00 116.91 ? 232 LEU E C   1 
ATOM   13439 O O   . LEU E 2 232 ? -5.810  -29.298 58.570  1.00 116.25 ? 232 LEU E O   1 
ATOM   13440 C CB  . LEU E 2 232 ? -2.958  -30.632 57.864  1.00 114.17 ? 232 LEU E CB  1 
ATOM   13441 C CG  . LEU E 2 232 ? -2.145  -31.648 57.059  1.00 112.81 ? 232 LEU E CG  1 
ATOM   13442 C CD1 . LEU E 2 232 ? -1.179  -32.405 57.960  1.00 114.82 ? 232 LEU E CD1 1 
ATOM   13443 C CD2 . LEU E 2 232 ? -3.057  -32.608 56.312  1.00 116.41 ? 232 LEU E CD2 1 
ATOM   13444 N N   . TYR E 2 233 ? -4.270  -27.689 58.229  1.00 116.62 ? 233 TYR E N   1 
ATOM   13445 C CA  . TYR E 2 233 ? -4.946  -26.737 59.104  1.00 116.22 ? 233 TYR E CA  1 
ATOM   13446 C C   . TYR E 2 233 ? -6.222  -26.206 58.460  1.00 116.26 ? 233 TYR E C   1 
ATOM   13447 O O   . TYR E 2 233 ? -7.293  -26.218 59.078  1.00 114.65 ? 233 TYR E O   1 
ATOM   13448 C CB  . TYR E 2 233 ? -3.994  -25.592 59.455  1.00 116.00 ? 233 TYR E CB  1 
ATOM   13449 C CG  . TYR E 2 233 ? -4.620  -24.491 60.280  1.00 115.52 ? 233 TYR E CG  1 
ATOM   13450 C CD1 . TYR E 2 233 ? -4.849  -24.661 61.640  1.00 118.00 ? 233 TYR E CD1 1 
ATOM   13451 C CD2 . TYR E 2 233 ? -4.979  -23.281 59.702  1.00 115.06 ? 233 TYR E CD2 1 
ATOM   13452 C CE1 . TYR E 2 233 ? -5.420  -23.656 62.398  1.00 118.46 ? 233 TYR E CE1 1 
ATOM   13453 C CE2 . TYR E 2 233 ? -5.551  -22.271 60.452  1.00 114.58 ? 233 TYR E CE2 1 
ATOM   13454 C CZ  . TYR E 2 233 ? -5.769  -22.465 61.800  1.00 116.90 ? 233 TYR E CZ  1 
ATOM   13455 O OH  . TYR E 2 233 ? -6.338  -21.463 62.553  1.00 118.46 ? 233 TYR E OH  1 
ATOM   13456 N N   . LEU E 2 234 ? -6.127  -25.734 57.214  1.00 117.59 ? 234 LEU E N   1 
ATOM   13457 C CA  . LEU E 2 234 ? -7.306  -25.212 56.530  1.00 119.47 ? 234 LEU E CA  1 
ATOM   13458 C C   . LEU E 2 234 ? -8.332  -26.304 56.256  1.00 119.42 ? 234 LEU E C   1 
ATOM   13459 O O   . LEU E 2 234 ? -9.534  -26.021 56.194  1.00 122.72 ? 234 LEU E O   1 
ATOM   13460 C CB  . LEU E 2 234 ? -6.897  -24.521 55.230  1.00 125.27 ? 234 LEU E CB  1 
ATOM   13461 C CG  . LEU E 2 234 ? -6.215  -23.162 55.406  1.00 126.61 ? 234 LEU E CG  1 
ATOM   13462 C CD1 . LEU E 2 234 ? -6.063  -22.465 54.068  1.00 143.53 ? 234 LEU E CD1 1 
ATOM   13463 C CD2 . LEU E 2 234 ? -6.983  -22.285 56.387  1.00 124.41 ? 234 LEU E CD2 1 
ATOM   13464 N N   . ASP E 2 235 ? -7.883  -27.549 56.085  1.00 119.47 ? 235 ASP E N   1 
ATOM   13465 C CA  . ASP E 2 235 ? -8.822  -28.655 55.918  1.00 118.95 ? 235 ASP E CA  1 
ATOM   13466 C C   . ASP E 2 235 ? -9.643  -28.865 57.184  1.00 114.96 ? 235 ASP E C   1 
ATOM   13467 O O   . ASP E 2 235 ? -10.868 -29.027 57.123  1.00 112.60 ? 235 ASP E O   1 
ATOM   13468 C CB  . ASP E 2 235 ? -8.070  -29.932 55.542  1.00 122.54 ? 235 ASP E CB  1 
ATOM   13469 C CG  . ASP E 2 235 ? -9.001  -31.078 55.192  1.00 129.23 ? 235 ASP E CG  1 
ATOM   13470 O OD1 . ASP E 2 235 ? -10.202 -30.823 54.951  1.00 131.69 ? 235 ASP E OD1 1 
ATOM   13471 O OD2 . ASP E 2 235 ? -8.534  -32.235 55.162  1.00 134.45 ? 235 ASP E OD2 1 
ATOM   13472 N N   . SER E 2 236 ? -8.982  -28.870 58.345  1.00 114.04 ? 236 SER E N   1 
ATOM   13473 C CA  . SER E 2 236 ? -9.705  -28.988 59.607  1.00 113.64 ? 236 SER E CA  1 
ATOM   13474 C C   . SER E 2 236 ? -10.621 -27.796 59.842  1.00 112.80 ? 236 SER E C   1 
ATOM   13475 O O   . SER E 2 236 ? -11.652 -27.930 60.510  1.00 114.50 ? 236 SER E O   1 
ATOM   13476 C CB  . SER E 2 236 ? -8.719  -29.133 60.766  1.00 115.42 ? 236 SER E CB  1 
ATOM   13477 O OG  . SER E 2 236 ? -9.398  -29.269 62.002  1.00 118.94 ? 236 SER E OG  1 
ATOM   13478 N N   . LEU E 2 237 ? -10.269 -26.628 59.301  1.00 112.52 ? 237 LEU E N   1 
ATOM   13479 C CA  . LEU E 2 237 ? -11.138 -25.465 59.439  1.00 114.07 ? 237 LEU E CA  1 
ATOM   13480 C C   . LEU E 2 237 ? -12.406 -25.612 58.610  1.00 115.14 ? 237 LEU E C   1 
ATOM   13481 O O   . LEU E 2 237 ? -13.468 -25.129 59.018  1.00 114.76 ? 237 LEU E O   1 
ATOM   13482 C CB  . LEU E 2 237 ? -10.384 -24.193 59.053  1.00 119.00 ? 237 LEU E CB  1 
ATOM   13483 C CG  . LEU E 2 237 ? -9.898  -23.351 60.236  1.00 116.76 ? 237 LEU E CG  1 
ATOM   13484 C CD1 . LEU E 2 237 ? -8.982  -24.160 61.146  1.00 114.73 ? 237 LEU E CD1 1 
ATOM   13485 C CD2 . LEU E 2 237 ? -9.201  -22.084 59.760  1.00 118.85 ? 237 LEU E CD2 1 
ATOM   13486 N N   . ARG E 2 238 ? -12.319 -26.265 57.449  1.00 112.67 ? 238 ARG E N   1 
ATOM   13487 C CA  . ARG E 2 238 ? -13.515 -26.553 56.665  1.00 112.65 ? 238 ARG E CA  1 
ATOM   13488 C C   . ARG E 2 238 ? -14.500 -27.433 57.423  1.00 112.60 ? 238 ARG E C   1 
ATOM   13489 O O   . ARG E 2 238 ? -15.696 -27.422 57.110  1.00 111.87 ? 238 ARG E O   1 
ATOM   13490 C CB  . ARG E 2 238 ? -13.125 -27.219 55.345  1.00 113.87 ? 238 ARG E CB  1 
ATOM   13491 C CG  . ARG E 2 238 ? -13.486 -26.406 54.116  1.00 123.53 ? 238 ARG E CG  1 
ATOM   13492 C CD  . ARG E 2 238 ? -13.186 -24.934 54.336  1.00 132.97 ? 238 ARG E CD  1 
ATOM   13493 N NE  . ARG E 2 238 ? -14.395 -24.116 54.293  1.00 139.27 ? 238 ARG E NE  1 
ATOM   13494 C CZ  . ARG E 2 238 ? -14.668 -23.235 53.336  1.00 143.74 ? 238 ARG E CZ  1 
ATOM   13495 N NH1 . ARG E 2 238 ? -13.809 -23.043 52.343  1.00 140.15 ? 238 ARG E NH1 1 
ATOM   13496 N NH2 . ARG E 2 238 ? -15.794 -22.536 53.375  1.00 147.77 ? 238 ARG E NH2 1 
ATOM   13497 N N   . LYS E 2 239 ? -14.024 -28.188 58.411  1.00 108.95 ? 239 LYS E N   1 
ATOM   13498 C CA  . LYS E 2 239 ? -14.862 -29.048 59.233  1.00 109.17 ? 239 LYS E CA  1 
ATOM   13499 C C   . LYS E 2 239 ? -15.303 -28.348 60.514  1.00 113.67 ? 239 LYS E C   1 
ATOM   13500 O O   . LYS E 2 239 ? -16.490 -28.359 60.855  1.00 117.49 ? 239 LYS E O   1 
ATOM   13501 C CB  . LYS E 2 239 ? -14.103 -30.336 59.563  1.00 107.46 ? 239 LYS E CB  1 
ATOM   13502 C CG  . LYS E 2 239 ? -13.236 -30.827 58.419  1.00 108.55 ? 239 LYS E CG  1 
ATOM   13503 C CD  . LYS E 2 239 ? -12.242 -31.875 58.882  1.00 111.18 ? 239 LYS E CD  1 
ATOM   13504 C CE  . LYS E 2 239 ? -11.363 -32.339 57.733  1.00 110.33 ? 239 LYS E CE  1 
ATOM   13505 N NZ  . LYS E 2 239 ? -9.951  -32.538 58.160  1.00 116.22 ? 239 LYS E NZ  1 
ATOM   13506 N N   . LYS E 2 240 ? -14.356 -27.737 61.229  1.00 113.82 ? 240 LYS E N   1 
ATOM   13507 C CA  . LYS E 2 240 ? -14.673 -27.096 62.501  1.00 114.22 ? 240 LYS E CA  1 
ATOM   13508 C C   . LYS E 2 240 ? -15.586 -25.896 62.292  1.00 115.57 ? 240 LYS E C   1 
ATOM   13509 O O   . LYS E 2 240 ? -16.727 -25.874 62.769  1.00 118.85 ? 240 LYS E O   1 
ATOM   13510 C CB  . LYS E 2 240 ? -13.384 -26.673 63.209  1.00 114.67 ? 240 LYS E CB  1 
ATOM   13511 C CG  . LYS E 2 240 ? -12.467 -27.829 63.559  1.00 117.40 ? 240 LYS E CG  1 
ATOM   13512 C CD  . LYS E 2 240 ? -13.193 -28.879 64.380  1.00 123.55 ? 240 LYS E CD  1 
ATOM   13513 C CE  . LYS E 2 240 ? -12.210 -29.883 64.950  1.00 130.12 ? 240 LYS E CE  1 
ATOM   13514 N NZ  . LYS E 2 240 ? -10.914 -29.222 65.275  1.00 137.55 ? 240 LYS E NZ  1 
ATOM   13515 N N   . SER E 2 241 ? -15.097 -24.882 61.580  1.00 119.26 ? 241 SER E N   1 
ATOM   13516 C CA  . SER E 2 241 ? -15.874 -23.677 61.300  1.00 124.51 ? 241 SER E CA  1 
ATOM   13517 C C   . SER E 2 241 ? -15.622 -23.269 59.856  1.00 125.75 ? 241 SER E C   1 
ATOM   13518 O O   . SER E 2 241 ? -14.618 -22.602 59.558  1.00 127.09 ? 241 SER E O   1 
ATOM   13519 C CB  . SER E 2 241 ? -15.513 -22.547 62.259  1.00 132.10 ? 241 SER E CB  1 
ATOM   13520 O OG  . SER E 2 241 ? -14.110 -22.476 62.444  1.00 135.26 ? 241 SER E OG  1 
ATOM   13521 N N   . PRO E 2 242 ? -16.515 -23.638 58.934  1.00 124.96 ? 242 PRO E N   1 
ATOM   13522 C CA  . PRO E 2 242 ? -16.299 -23.305 57.520  1.00 123.94 ? 242 PRO E CA  1 
ATOM   13523 C C   . PRO E 2 242 ? -16.589 -21.855 57.182  1.00 130.90 ? 242 PRO E C   1 
ATOM   13524 O O   . PRO E 2 242 ? -16.250 -21.417 56.074  1.00 134.69 ? 242 PRO E O   1 
ATOM   13525 C CB  . PRO E 2 242 ? -17.270 -24.245 56.794  1.00 123.79 ? 242 PRO E CB  1 
ATOM   13526 C CG  . PRO E 2 242 ? -18.371 -24.467 57.777  1.00 124.83 ? 242 PRO E CG  1 
ATOM   13527 C CD  . PRO E 2 242 ? -17.733 -24.440 59.142  1.00 123.84 ? 242 PRO E CD  1 
ATOM   13528 N N   . ALA E 2 243 ? -17.204 -21.102 58.090  1.00 138.85 ? 243 ALA E N   1 
ATOM   13529 C CA  . ALA E 2 243 ? -17.489 -19.693 57.863  1.00 142.89 ? 243 ALA E CA  1 
ATOM   13530 C C   . ALA E 2 243 ? -16.319 -18.792 58.230  1.00 155.74 ? 243 ALA E C   1 
ATOM   13531 O O   . ALA E 2 243 ? -16.422 -17.572 58.073  1.00 154.26 ? 243 ALA E O   1 
ATOM   13532 C CB  . ALA E 2 243 ? -18.734 -19.271 58.652  1.00 133.94 ? 243 ALA E CB  1 
ATOM   13533 N N   . LYS E 2 244 ? -15.215 -19.360 58.714  1.00 180.98 ? 244 LYS E N   1 
ATOM   13534 C CA  . LYS E 2 244 ? -14.011 -18.594 59.006  1.00 182.32 ? 244 LYS E CA  1 
ATOM   13535 C C   . LYS E 2 244 ? -13.083 -18.475 57.807  1.00 181.56 ? 244 LYS E C   1 
ATOM   13536 O O   . LYS E 2 244 ? -12.086 -17.749 57.883  1.00 181.76 ? 244 LYS E O   1 
ATOM   13537 C CB  . LYS E 2 244 ? -13.246 -19.230 60.172  1.00 184.06 ? 244 LYS E CB  1 
ATOM   13538 C CG  . LYS E 2 244 ? -14.063 -19.381 61.442  1.00 184.79 ? 244 LYS E CG  1 
ATOM   13539 C CD  . LYS E 2 244 ? -14.040 -18.108 62.272  1.00 189.78 ? 244 LYS E CD  1 
ATOM   13540 C CE  . LYS E 2 244 ? -15.428 -17.501 62.394  1.00 195.67 ? 244 LYS E CE  1 
ATOM   13541 N NZ  . LYS E 2 244 ? -15.401 -16.175 63.074  1.00 203.60 ? 244 LYS E NZ  1 
ATOM   13542 N N   . LEU E 2 245 ? -13.384 -19.165 56.712  1.00 175.69 ? 245 LEU E N   1 
ATOM   13543 C CA  . LEU E 2 245 ? -12.575 -19.135 55.503  1.00 173.58 ? 245 LEU E CA  1 
ATOM   13544 C C   . LEU E 2 245 ? -13.298 -18.320 54.439  1.00 170.25 ? 245 LEU E C   1 
ATOM   13545 O O   . LEU E 2 245 ? -14.473 -18.570 54.150  1.00 170.87 ? 245 LEU E O   1 
ATOM   13546 C CB  . LEU E 2 245 ? -12.294 -20.554 54.999  1.00 173.15 ? 245 LEU E CB  1 
ATOM   13547 C CG  . LEU E 2 245 ? -11.650 -21.518 56.002  1.00 172.97 ? 245 LEU E CG  1 
ATOM   13548 C CD1 . LEU E 2 245 ? -12.697 -22.305 56.787  1.00 173.65 ? 245 LEU E CD1 1 
ATOM   13549 C CD2 . LEU E 2 245 ? -10.678 -22.457 55.304  1.00 172.58 ? 245 LEU E CD2 1 
ATOM   13550 N N   . THR E 2 246 ? -12.595 -17.346 53.867  1.00 161.53 ? 246 THR E N   1 
ATOM   13551 C CA  . THR E 2 246 ? -13.193 -16.440 52.899  1.00 152.68 ? 246 THR E CA  1 
ATOM   13552 C C   . THR E 2 246 ? -13.597 -17.181 51.625  1.00 148.52 ? 246 THR E C   1 
ATOM   13553 O O   . THR E 2 246 ? -13.062 -18.242 51.289  1.00 152.24 ? 246 THR E O   1 
ATOM   13554 C CB  . THR E 2 246 ? -12.229 -15.302 52.565  1.00 148.90 ? 246 THR E CB  1 
ATOM   13555 O OG1 . THR E 2 246 ? -12.866 -14.379 51.673  1.00 142.24 ? 246 THR E OG1 1 
ATOM   13556 C CG2 . THR E 2 246 ? -10.969 -15.848 51.915  1.00 157.69 ? 246 THR E CG2 1 
ATOM   13557 N N   . SER E 2 247 ? -14.564 -16.601 50.915  1.00 146.66 ? 247 SER E N   1 
ATOM   13558 C CA  . SER E 2 247 ? -15.104 -17.188 49.697  1.00 144.96 ? 247 SER E CA  1 
ATOM   13559 C C   . SER E 2 247 ? -15.410 -16.089 48.688  1.00 142.29 ? 247 SER E C   1 
ATOM   13560 O O   . SER E 2 247 ? -15.473 -14.905 49.027  1.00 143.31 ? 247 SER E O   1 
ATOM   13561 C CB  . SER E 2 247 ? -16.371 -18.005 49.985  1.00 147.37 ? 247 SER E CB  1 
ATOM   13562 O OG  . SER E 2 247 ? -16.937 -18.511 48.789  1.00 150.04 ? 247 SER E OG  1 
ATOM   13563 N N   . GLY E 2 248 ? -15.593 -16.497 47.432  1.00 117.34 ? 248 GLY E N   1 
ATOM   13564 C CA  . GLY E 2 248 ? -15.927 -15.570 46.378  1.00 104.50 ? 248 GLY E CA  1 
ATOM   13565 C C   . GLY E 2 248 ? -15.705 -16.125 44.985  1.00 97.06  ? 248 GLY E C   1 
ATOM   13566 O O   . GLY E 2 248 ? -15.313 -17.282 44.801  1.00 98.60  ? 248 GLY E O   1 
ATOM   13567 N N   . PRO E 2 249 ? -15.958 -15.296 43.967  1.00 89.95  ? 249 PRO E N   1 
ATOM   13568 C CA  . PRO E 2 249 ? -15.787 -15.767 42.583  1.00 86.58  ? 249 PRO E CA  1 
ATOM   13569 C C   . PRO E 2 249 ? -14.333 -15.924 42.186  1.00 88.88  ? 249 PRO E C   1 
ATOM   13570 O O   . PRO E 2 249 ? -14.026 -16.701 41.274  1.00 89.19  ? 249 PRO E O   1 
ATOM   13571 C CB  . PRO E 2 249 ? -16.475 -14.673 41.758  1.00 86.62  ? 249 PRO E CB  1 
ATOM   13572 C CG  . PRO E 2 249 ? -16.314 -13.440 42.587  1.00 85.85  ? 249 PRO E CG  1 
ATOM   13573 C CD  . PRO E 2 249 ? -16.377 -13.884 44.027  1.00 87.75  ? 249 PRO E CD  1 
ATOM   13574 N N   . HIS E 2 250 ? -13.433 -15.202 42.846  1.00 93.12  ? 250 HIS E N   1 
ATOM   13575 C CA  . HIS E 2 250 ? -12.001 -15.266 42.601  1.00 90.56  ? 250 HIS E CA  1 
ATOM   13576 C C   . HIS E 2 250 ? -11.283 -16.172 43.590  1.00 89.98  ? 250 HIS E C   1 
ATOM   13577 O O   . HIS E 2 250 ? -10.048 -16.197 43.614  1.00 88.72  ? 250 HIS E O   1 
ATOM   13578 C CB  . HIS E 2 250 ? -11.414 -13.860 42.672  1.00 89.47  ? 250 HIS E CB  1 
ATOM   13579 C CG  . HIS E 2 250 ? -11.580 -13.222 44.015  1.00 95.18  ? 250 HIS E CG  1 
ATOM   13580 N ND1 . HIS E 2 250 ? -12.803 -12.791 44.483  1.00 97.12  ? 250 HIS E ND1 1 
ATOM   13581 C CD2 . HIS E 2 250 ? -10.687 -12.967 45.000  1.00 97.36  ? 250 HIS E CD2 1 
ATOM   13582 C CE1 . HIS E 2 250 ? -12.654 -12.285 45.694  1.00 99.38  ? 250 HIS E CE1 1 
ATOM   13583 N NE2 . HIS E 2 250 ? -11.380 -12.380 46.031  1.00 100.62 ? 250 HIS E NE2 1 
ATOM   13584 N N   . ILE E 2 251 ? -12.029 -16.910 44.408  1.00 95.65  ? 251 ILE E N   1 
ATOM   13585 C CA  . ILE E 2 251 ? -11.473 -17.758 45.455  1.00 90.12  ? 251 ILE E CA  1 
ATOM   13586 C C   . ILE E 2 251 ? -11.679 -19.214 45.068  1.00 88.71  ? 251 ILE E C   1 
ATOM   13587 O O   . ILE E 2 251 ? -12.775 -19.603 44.645  1.00 84.42  ? 251 ILE E O   1 
ATOM   13588 C CB  . ILE E 2 251 ? -12.120 -17.454 46.817  1.00 99.45  ? 251 ILE E CB  1 
ATOM   13589 C CG1 . ILE E 2 251 ? -11.893 -15.989 47.187  1.00 103.28 ? 251 ILE E CG1 1 
ATOM   13590 C CG2 . ILE E 2 251 ? -11.566 -18.373 47.892  1.00 114.39 ? 251 ILE E CG2 1 
ATOM   13591 C CD1 . ILE E 2 251 ? -10.437 -15.618 47.314  1.00 104.42 ? 251 ILE E CD1 1 
ATOM   13592 N N   . VAL E 2 252 ? -10.626 -20.016 45.212  1.00 94.30  ? 252 VAL E N   1 
ATOM   13593 C CA  . VAL E 2 252 ? -10.665 -21.446 44.930  1.00 95.07  ? 252 VAL E CA  1 
ATOM   13594 C C   . VAL E 2 252 ? -10.053 -22.186 46.112  1.00 104.01 ? 252 VAL E C   1 
ATOM   13595 O O   . VAL E 2 252 ? -8.972  -21.823 46.587  1.00 107.13 ? 252 VAL E O   1 
ATOM   13596 C CB  . VAL E 2 252 ? -9.928  -21.798 43.623  1.00 89.74  ? 252 VAL E CB  1 
ATOM   13597 C CG1 . VAL E 2 252 ? -10.773 -21.415 42.419  1.00 89.42  ? 252 VAL E CG1 1 
ATOM   13598 C CG2 . VAL E 2 252 ? -8.588  -21.093 43.560  1.00 91.50  ? 252 VAL E CG2 1 
ATOM   13599 N N   . GLY E 2 253 ? -10.751 -23.214 46.589  1.00 116.50 ? 253 GLY E N   1 
ATOM   13600 C CA  . GLY E 2 253 ? -10.297 -24.018 47.707  1.00 123.35 ? 253 GLY E CA  1 
ATOM   13601 C C   . GLY E 2 253 ? -10.496 -23.370 49.062  1.00 133.51 ? 253 GLY E C   1 
ATOM   13602 O O   . GLY E 2 253 ? -11.510 -22.707 49.297  1.00 135.35 ? 253 GLY E O   1 
ATOM   13603 N N   . ASN E 2 254 ? -9.533  -23.552 49.961  1.00 144.01 ? 254 ASN E N   1 
ATOM   13604 C CA  . ASN E 2 254 ? -9.589  -23.016 51.316  1.00 158.52 ? 254 ASN E CA  1 
ATOM   13605 C C   . ASN E 2 254 ? -8.612  -21.854 51.416  1.00 174.92 ? 254 ASN E C   1 
ATOM   13606 O O   . ASN E 2 254 ? -7.414  -22.030 51.182  1.00 167.13 ? 254 ASN E O   1 
ATOM   13607 C CB  . ASN E 2 254 ? -9.249  -24.091 52.349  1.00 146.54 ? 254 ASN E CB  1 
ATOM   13608 C CG  . ASN E 2 254 ? -10.146 -25.307 52.243  1.00 140.70 ? 254 ASN E CG  1 
ATOM   13609 O OD1 . ASN E 2 254 ? -11.233 -25.242 51.671  1.00 140.82 ? 254 ASN E OD1 1 
ATOM   13610 N ND2 . ASN E 2 254 ? -9.692  -26.426 52.796  1.00 132.74 ? 254 ASN E ND2 1 
ATOM   13611 N N   . VAL E 2 255 ? -9.121  -20.672 51.751  1.00 246.29 ? 255 VAL E N   1 
ATOM   13612 C CA  . VAL E 2 255 ? -8.304  -19.468 51.852  1.00 246.54 ? 255 VAL E CA  1 
ATOM   13613 C C   . VAL E 2 255 ? -8.641  -18.747 53.150  1.00 247.77 ? 255 VAL E C   1 
ATOM   13614 O O   . VAL E 2 255 ? -9.819  -18.535 53.458  1.00 247.86 ? 255 VAL E O   1 
ATOM   13615 C CB  . VAL E 2 255 ? -8.514  -18.529 50.648  1.00 244.88 ? 255 VAL E CB  1 
ATOM   13616 C CG1 . VAL E 2 255 ? -7.680  -17.271 50.811  1.00 245.47 ? 255 VAL E CG1 1 
ATOM   13617 C CG2 . VAL E 2 255 ? -8.165  -19.235 49.345  1.00 242.79 ? 255 VAL E CG2 1 
ATOM   13618 N N   . LEU E 2 256 ? -7.610  -18.379 53.909  1.00 172.72 ? 256 LEU E N   1 
ATOM   13619 C CA  . LEU E 2 256 ? -7.756  -17.661 55.174  1.00 153.66 ? 256 LEU E CA  1 
ATOM   13620 C C   . LEU E 2 256 ? -7.201  -16.252 54.987  1.00 140.91 ? 256 LEU E C   1 
ATOM   13621 O O   . LEU E 2 256 ? -5.985  -16.042 55.016  1.00 131.43 ? 256 LEU E O   1 
ATOM   13622 C CB  . LEU E 2 256 ? -7.044  -18.389 56.309  1.00 138.55 ? 256 LEU E CB  1 
ATOM   13623 C CG  . LEU E 2 256 ? -7.081  -17.692 57.673  1.00 129.06 ? 256 LEU E CG  1 
ATOM   13624 C CD1 . LEU E 2 256 ? -8.516  -17.438 58.118  1.00 130.72 ? 256 LEU E CD1 1 
ATOM   13625 C CD2 . LEU E 2 256 ? -6.323  -18.496 58.720  1.00 122.30 ? 256 LEU E CD2 1 
ATOM   13626 N N   . VAL E 2 257 ? -8.094  -15.293 54.796  1.00 143.02 ? 257 VAL E N   1 
ATOM   13627 C CA  . VAL E 2 257 ? -7.719  -13.900 54.595  1.00 136.29 ? 257 VAL E CA  1 
ATOM   13628 C C   . VAL E 2 257 ? -7.981  -13.127 55.879  1.00 137.67 ? 257 VAL E C   1 
ATOM   13629 O O   . VAL E 2 257 ? -8.924  -13.414 56.627  1.00 138.36 ? 257 VAL E O   1 
ATOM   13630 C CB  . VAL E 2 257 ? -8.476  -13.294 53.393  1.00 138.09 ? 257 VAL E CB  1 
ATOM   13631 C CG1 . VAL E 2 257 ? -9.330  -12.104 53.813  1.00 143.43 ? 257 VAL E CG1 1 
ATOM   13632 C CG2 . VAL E 2 257 ? -7.498  -12.902 52.297  1.00 133.47 ? 257 VAL E CG2 1 
ATOM   13633 N N   . ASP E 2 258 ? -7.128  -12.145 56.146  1.00 116.65 ? 258 ASP E N   1 
ATOM   13634 C CA  . ASP E 2 258 ? -7.277  -11.297 57.316  1.00 107.52 ? 258 ASP E CA  1 
ATOM   13635 C C   . ASP E 2 258 ? -8.211  -10.134 57.006  1.00 105.58 ? 258 ASP E C   1 
ATOM   13636 O O   . ASP E 2 258 ? -8.340  -9.704  55.857  1.00 107.39 ? 258 ASP E O   1 
ATOM   13637 C CB  . ASP E 2 258 ? -5.919  -10.769 57.775  1.00 101.91 ? 258 ASP E CB  1 
ATOM   13638 C CG  . ASP E 2 258 ? -5.976  -10.125 59.143  1.00 98.31  ? 258 ASP E CG  1 
ATOM   13639 O OD1 . ASP E 2 258 ? -6.694  -9.116  59.299  1.00 96.94  ? 258 ASP E OD1 1 
ATOM   13640 O OD2 . ASP E 2 258 ? -5.307  -10.632 60.067  1.00 101.72 ? 258 ASP E OD2 1 
ATOM   13641 N N   . GLU E 2 259 ? -8.867  -9.627  58.053  1.00 100.70 ? 259 GLU E N   1 
ATOM   13642 C CA  . GLU E 2 259 ? -9.750  -8.478  57.882  1.00 98.04  ? 259 GLU E CA  1 
ATOM   13643 C C   . GLU E 2 259 ? -8.975  -7.237  57.462  1.00 96.78  ? 259 GLU E C   1 
ATOM   13644 O O   . GLU E 2 259 ? -9.536  -6.340  56.822  1.00 96.32  ? 259 GLU E O   1 
ATOM   13645 C CB  . GLU E 2 259 ? -10.519 -8.215  59.176  1.00 94.01  ? 259 GLU E CB  1 
ATOM   13646 C CG  . GLU E 2 259 ? -9.623  -8.033  60.390  1.00 95.95  ? 259 GLU E CG  1 
ATOM   13647 C CD  . GLU E 2 259 ? -10.403 -7.914  61.683  1.00 97.64  ? 259 GLU E CD  1 
ATOM   13648 O OE1 . GLU E 2 259 ? -11.651 -7.945  61.634  1.00 105.38 ? 259 GLU E OE1 1 
ATOM   13649 O OE2 . GLU E 2 259 ? -9.766  -7.791  62.750  1.00 97.41  ? 259 GLU E OE2 1 
ATOM   13650 N N   . THR E 2 260 ? -7.690  -7.167  57.813  1.00 94.90  ? 260 THR E N   1 
ATOM   13651 C CA  . THR E 2 260 ? -6.861  -6.023  57.456  1.00 93.41  ? 260 THR E CA  1 
ATOM   13652 C C   . THR E 2 260 ? -6.343  -6.107  56.024  1.00 99.76  ? 260 THR E C   1 
ATOM   13653 O O   . THR E 2 260 ? -6.125  -5.070  55.388  1.00 104.99 ? 260 THR E O   1 
ATOM   13654 C CB  . THR E 2 260 ? -5.687  -5.911  58.430  1.00 94.66  ? 260 THR E CB  1 
ATOM   13655 O OG1 . THR E 2 260 ? -6.147  -6.180  59.760  1.00 97.78  ? 260 THR E OG1 1 
ATOM   13656 C CG2 . THR E 2 260 ? -5.087  -4.515  58.387  1.00 95.21  ? 260 THR E CG2 1 
ATOM   13657 N N   . ALA E 2 261 ? -6.141  -7.316  55.506  1.00 102.66 ? 261 ALA E N   1 
ATOM   13658 C CA  . ALA E 2 261 ? -5.581  -7.486  54.171  1.00 108.95 ? 261 ALA E CA  1 
ATOM   13659 C C   . ALA E 2 261 ? -6.546  -7.000  53.095  1.00 119.96 ? 261 ALA E C   1 
ATOM   13660 O O   . ALA E 2 261 ? -7.760  -7.204  53.185  1.00 118.82 ? 261 ALA E O   1 
ATOM   13661 C CB  . ALA E 2 261 ? -5.224  -8.952  53.932  1.00 104.21 ? 261 ALA E CB  1 
ATOM   13662 N N   . THR E 2 262 ? -5.993  -6.354  52.069  1.00 149.41 ? 262 THR E N   1 
ATOM   13663 C CA  . THR E 2 262 ? -6.757  -5.836  50.941  1.00 147.66 ? 262 THR E CA  1 
ATOM   13664 C C   . THR E 2 262 ? -6.298  -6.501  49.649  1.00 145.65 ? 262 THR E C   1 
ATOM   13665 O O   . THR E 2 262 ? -5.093  -6.631  49.405  1.00 145.75 ? 262 THR E O   1 
ATOM   13666 C CB  . THR E 2 262 ? -6.615  -4.313  50.832  1.00 148.54 ? 262 THR E CB  1 
ATOM   13667 O OG1 . THR E 2 262 ? -7.094  -3.874  49.554  1.00 146.65 ? 262 THR E OG1 1 
ATOM   13668 C CG2 . THR E 2 262 ? -5.163  -3.888  51.006  1.00 149.89 ? 262 THR E CG2 1 
ATOM   13669 N N   . ILE E 2 263 ? -7.262  -6.929  48.834  1.00 114.71 ? 263 ILE E N   1 
ATOM   13670 C CA  . ILE E 2 263 ? -7.010  -7.606  47.568  1.00 97.44  ? 263 ILE E CA  1 
ATOM   13671 C C   . ILE E 2 263 ? -7.536  -6.740  46.432  1.00 93.37  ? 263 ILE E C   1 
ATOM   13672 O O   . ILE E 2 263 ? -8.638  -6.189  46.522  1.00 99.83  ? 263 ILE E O   1 
ATOM   13673 C CB  . ILE E 2 263 ? -7.663  -9.003  47.530  1.00 89.89  ? 263 ILE E CB  1 
ATOM   13674 C CG1 . ILE E 2 263 ? -7.073  -9.896  48.621  1.00 94.78  ? 263 ILE E CG1 1 
ATOM   13675 C CG2 . ILE E 2 263 ? -7.481  -9.649  46.163  1.00 90.78  ? 263 ILE E CG2 1 
ATOM   13676 C CD1 . ILE E 2 263 ? -7.620  -11.302 48.603  1.00 90.26  ? 263 ILE E CD1 1 
ATOM   13677 N N   . GLY E 2 264 ? -6.745  -6.615  45.370  1.00 85.66  ? 264 GLY E N   1 
ATOM   13678 C CA  . GLY E 2 264 ? -7.184  -5.919  44.179  1.00 80.09  ? 264 GLY E CA  1 
ATOM   13679 C C   . GLY E 2 264 ? -8.221  -6.715  43.402  1.00 80.29  ? 264 GLY E C   1 
ATOM   13680 O O   . GLY E 2 264 ? -8.665  -7.794  43.798  1.00 82.56  ? 264 GLY E O   1 
ATOM   13681 N N   . GLU E 2 265 ? -8.612  -6.160  42.260  1.00 75.82  ? 265 GLU E N   1 
ATOM   13682 C CA  . GLU E 2 265 ? -9.617  -6.783  41.412  1.00 75.61  ? 265 GLU E CA  1 
ATOM   13683 C C   . GLU E 2 265 ? -8.964  -7.651  40.343  1.00 73.94  ? 265 GLU E C   1 
ATOM   13684 O O   . GLU E 2 265 ? -7.807  -7.459  39.965  1.00 75.69  ? 265 GLU E O   1 
ATOM   13685 C CB  . GLU E 2 265 ? -10.504 -5.726  40.749  1.00 79.49  ? 265 GLU E CB  1 
ATOM   13686 C CG  . GLU E 2 265 ? -11.334 -4.895  41.717  1.00 87.61  ? 265 GLU E CG  1 
ATOM   13687 C CD  . GLU E 2 265 ? -12.487 -5.678  42.327  1.00 91.53  ? 265 GLU E CD  1 
ATOM   13688 O OE1 . GLU E 2 265 ? -12.801 -6.778  41.822  1.00 90.78  ? 265 GLU E OE1 1 
ATOM   13689 O OE2 . GLU E 2 265 ? -13.082 -5.188  43.312  1.00 95.48  ? 265 GLU E OE2 1 
ATOM   13690 N N   . GLY E 2 266 ? -9.732  -8.622  39.855  1.00 77.80  ? 266 GLY E N   1 
ATOM   13691 C CA  . GLY E 2 266 ? -9.236  -9.496  38.809  1.00 79.28  ? 266 GLY E CA  1 
ATOM   13692 C C   . GLY E 2 266 ? -8.127  -10.427 39.243  1.00 81.99  ? 266 GLY E C   1 
ATOM   13693 O O   . GLY E 2 266 ? -7.266  -10.773 38.429  1.00 84.12  ? 266 GLY E O   1 
ATOM   13694 N N   . CYS E 2 267 ? -8.123  -10.846 40.503  1.00 89.28  ? 267 CYS E N   1 
ATOM   13695 C CA  . CYS E 2 267 ? -7.111  -11.753 41.021  1.00 85.76  ? 267 CYS E CA  1 
ATOM   13696 C C   . CYS E 2 267 ? -7.668  -13.170 41.105  1.00 88.85  ? 267 CYS E C   1 
ATOM   13697 O O   . CYS E 2 267 ? -8.854  -13.415 40.880  1.00 92.83  ? 267 CYS E O   1 
ATOM   13698 C CB  . CYS E 2 267 ? -6.626  -11.288 42.397  1.00 87.57  ? 267 CYS E CB  1 
ATOM   13699 S SG  . CYS E 2 267 ? -6.118  -9.556  42.477  1.00 88.95  ? 267 CYS E SG  1 
ATOM   13700 N N   . LEU E 2 268 ? -6.790  -14.112 41.435  1.00 83.39  ? 268 LEU E N   1 
ATOM   13701 C CA  . LEU E 2 268 ? -7.204  -15.501 41.619  1.00 86.15  ? 268 LEU E CA  1 
ATOM   13702 C C   . LEU E 2 268 ? -6.341  -16.100 42.717  1.00 79.86  ? 268 LEU E C   1 
ATOM   13703 O O   . LEU E 2 268 ? -5.131  -16.264 42.542  1.00 80.65  ? 268 LEU E O   1 
ATOM   13704 C CB  . LEU E 2 268 ? -7.083  -16.301 40.329  1.00 92.30  ? 268 LEU E CB  1 
ATOM   13705 C CG  . LEU E 2 268 ? -7.831  -17.635 40.362  1.00 93.44  ? 268 LEU E CG  1 
ATOM   13706 C CD1 . LEU E 2 268 ? -9.278  -17.437 40.798  1.00 92.88  ? 268 LEU E CD1 1 
ATOM   13707 C CD2 . LEU E 2 268 ? -7.771  -18.312 39.007  1.00 99.33  ? 268 LEU E CD2 1 
ATOM   13708 N N   . ILE E 2 269 ? -6.962  -16.412 43.847  1.00 81.91  ? 269 ILE E N   1 
ATOM   13709 C CA  . ILE E 2 269 ? -6.256  -16.835 45.047  1.00 83.35  ? 269 ILE E CA  1 
ATOM   13710 C C   . ILE E 2 269 ? -6.738  -18.227 45.428  1.00 86.60  ? 269 ILE E C   1 
ATOM   13711 O O   . ILE E 2 269 ? -7.947  -18.479 45.483  1.00 88.89  ? 269 ILE E O   1 
ATOM   13712 C CB  . ILE E 2 269 ? -6.469  -15.841 46.202  1.00 86.89  ? 269 ILE E CB  1 
ATOM   13713 C CG1 . ILE E 2 269 ? -5.928  -14.457 45.820  1.00 78.40  ? 269 ILE E CG1 1 
ATOM   13714 C CG2 . ILE E 2 269 ? -5.810  -16.352 47.468  1.00 98.43  ? 269 ILE E CG2 1 
ATOM   13715 C CD1 . ILE E 2 269 ? -6.975  -13.500 45.265  1.00 81.12  ? 269 ILE E CD1 1 
ATOM   13716 N N   . GLY E 2 270 ? -5.793  -19.129 45.681  1.00 88.41  ? 270 GLY E N   1 
ATOM   13717 C CA  . GLY E 2 270 ? -6.120  -20.476 46.077  1.00 90.72  ? 270 GLY E CA  1 
ATOM   13718 C C   . GLY E 2 270 ? -5.493  -21.522 45.179  1.00 92.29  ? 270 GLY E C   1 
ATOM   13719 O O   . GLY E 2 270 ? -5.015  -21.227 44.079  1.00 87.22  ? 270 GLY E O   1 
ATOM   13720 N N   . PRO E 2 271 ? -5.486  -22.784 45.636  1.00 93.30  ? 271 PRO E N   1 
ATOM   13721 C CA  . PRO E 2 271 ? -6.023  -23.171 46.944  1.00 109.11 ? 271 PRO E CA  1 
ATOM   13722 C C   . PRO E 2 271 ? -4.986  -23.053 48.056  1.00 117.14 ? 271 PRO E C   1 
ATOM   13723 O O   . PRO E 2 271 ? -3.792  -22.969 47.770  1.00 112.93 ? 271 PRO E O   1 
ATOM   13724 C CB  . PRO E 2 271 ? -6.432  -24.640 46.741  1.00 111.67 ? 271 PRO E CB  1 
ATOM   13725 C CG  . PRO E 2 271 ? -6.209  -24.936 45.267  1.00 104.80 ? 271 PRO E CG  1 
ATOM   13726 C CD  . PRO E 2 271 ? -5.176  -23.961 44.814  1.00 95.44  ? 271 PRO E CD  1 
ATOM   13727 N N   . ASP E 2 272 ? -5.455  -23.052 49.306  1.00 144.72 ? 272 ASP E N   1 
ATOM   13728 C CA  . ASP E 2 272 ? -4.603  -23.057 50.497  1.00 147.01 ? 272 ASP E CA  1 
ATOM   13729 C C   . ASP E 2 272 ? -3.645  -21.860 50.496  1.00 147.06 ? 272 ASP E C   1 
ATOM   13730 O O   . ASP E 2 272 ? -2.433  -21.984 50.310  1.00 147.28 ? 272 ASP E O   1 
ATOM   13731 C CB  . ASP E 2 272 ? -3.851  -24.386 50.619  1.00 148.10 ? 272 ASP E CB  1 
ATOM   13732 C CG  . ASP E 2 272 ? -4.787  -25.576 50.646  1.00 151.36 ? 272 ASP E CG  1 
ATOM   13733 O OD1 . ASP E 2 272 ? -4.816  -26.336 49.656  1.00 155.02 ? 272 ASP E OD1 1 
ATOM   13734 O OD2 . ASP E 2 272 ? -5.521  -25.729 51.644  1.00 150.91 ? 272 ASP E OD2 1 
ATOM   13735 N N   . VAL E 2 273 ? -4.239  -20.686 50.710  1.00 139.04 ? 273 VAL E N   1 
ATOM   13736 C CA  . VAL E 2 273 ? -3.510  -19.427 50.794  1.00 129.64 ? 273 VAL E CA  1 
ATOM   13737 C C   . VAL E 2 273 ? -3.930  -18.702 52.067  1.00 134.22 ? 273 VAL E C   1 
ATOM   13738 O O   . VAL E 2 273 ? -5.121  -18.643 52.395  1.00 149.66 ? 273 VAL E O   1 
ATOM   13739 C CB  . VAL E 2 273 ? -3.762  -18.536 49.558  1.00 122.45 ? 273 VAL E CB  1 
ATOM   13740 C CG1 . VAL E 2 273 ? -2.932  -17.264 49.639  1.00 115.62 ? 273 VAL E CG1 1 
ATOM   13741 C CG2 . VAL E 2 273 ? -3.460  -19.293 48.272  1.00 109.09 ? 273 VAL E CG2 1 
ATOM   13742 N N   . ALA E 2 274 ? -2.948  -18.153 52.784  1.00 117.78 ? 274 ALA E N   1 
ATOM   13743 C CA  . ALA E 2 274 ? -3.177  -17.431 54.033  1.00 114.08 ? 274 ALA E CA  1 
ATOM   13744 C C   . ALA E 2 274 ? -2.453  -16.093 53.970  1.00 104.58 ? 274 ALA E C   1 
ATOM   13745 O O   . ALA E 2 274 ? -1.218  -16.053 53.926  1.00 101.52 ? 274 ALA E O   1 
ATOM   13746 C CB  . ALA E 2 274 ? -2.708  -18.244 55.240  1.00 117.43 ? 274 ALA E CB  1 
ATOM   13747 N N   . ILE E 2 275 ? -3.216  -15.002 53.963  1.00 104.78 ? 275 ILE E N   1 
ATOM   13748 C CA  . ILE E 2 275 ? -2.674  -13.651 53.868  1.00 101.69 ? 275 ILE E CA  1 
ATOM   13749 C C   . ILE E 2 275 ? -2.763  -12.995 55.239  1.00 100.48 ? 275 ILE E C   1 
ATOM   13750 O O   . ILE E 2 275 ? -3.856  -12.872 55.803  1.00 104.86 ? 275 ILE E O   1 
ATOM   13751 C CB  . ILE E 2 275 ? -3.425  -12.817 52.819  1.00 101.91 ? 275 ILE E CB  1 
ATOM   13752 C CG1 . ILE E 2 275 ? -3.342  -13.477 51.442  1.00 108.04 ? 275 ILE E CG1 1 
ATOM   13753 C CG2 . ILE E 2 275 ? -2.860  -11.408 52.763  1.00 102.03 ? 275 ILE E CG2 1 
ATOM   13754 C CD1 . ILE E 2 275 ? -4.075  -12.709 50.370  1.00 112.87 ? 275 ILE E CD1 1 
ATOM   13755 N N   . GLY E 2 276 ? -1.616  -12.561 55.771  1.00 94.30  ? 276 GLY E N   1 
ATOM   13756 C CA  . GLY E 2 276 ? -1.579  -11.910 57.050  1.00 95.48  ? 276 GLY E CA  1 
ATOM   13757 C C   . GLY E 2 276 ? -2.235  -10.537 57.014  1.00 95.41  ? 276 GLY E C   1 
ATOM   13758 O O   . GLY E 2 276 ? -2.775  -10.102 55.988  1.00 98.60  ? 276 GLY E O   1 
ATOM   13759 N N   . PRO E 2 277 ? -2.211  -9.849  58.151  1.00 92.57  ? 277 PRO E N   1 
ATOM   13760 C CA  . PRO E 2 277 ? -2.787  -8.504  58.218  1.00 91.72  ? 277 PRO E CA  1 
ATOM   13761 C C   . PRO E 2 277 ? -1.841  -7.450  57.661  1.00 91.43  ? 277 PRO E C   1 
ATOM   13762 O O   . PRO E 2 277 ? -0.634  -7.656  57.525  1.00 92.93  ? 277 PRO E O   1 
ATOM   13763 C CB  . PRO E 2 277 ? -3.011  -8.294  59.718  1.00 98.22  ? 277 PRO E CB  1 
ATOM   13764 C CG  . PRO E 2 277 ? -1.936  -9.106  60.353  1.00 101.71 ? 277 PRO E CG  1 
ATOM   13765 C CD  . PRO E 2 277 ? -1.740  -10.313 59.468  1.00 97.74  ? 277 PRO E CD  1 
ATOM   13766 N N   . GLY E 2 278 ? -2.424  -6.298  57.338  1.00 91.26  ? 278 GLY E N   1 
ATOM   13767 C CA  . GLY E 2 278 ? -1.657  -5.183  56.821  1.00 92.47  ? 278 GLY E CA  1 
ATOM   13768 C C   . GLY E 2 278 ? -1.076  -5.377  55.440  1.00 90.34  ? 278 GLY E C   1 
ATOM   13769 O O   . GLY E 2 278 ? -0.278  -4.544  55.000  1.00 89.77  ? 278 GLY E O   1 
ATOM   13770 N N   . CYS E 2 279 ? -1.450  -6.442  54.738  1.00 91.48  ? 279 CYS E N   1 
ATOM   13771 C CA  . CYS E 2 279 ? -0.922  -6.695  53.407  1.00 98.79  ? 279 CYS E CA  1 
ATOM   13772 C C   . CYS E 2 279 ? -1.669  -5.871  52.365  1.00 109.90 ? 279 CYS E C   1 
ATOM   13773 O O   . CYS E 2 279 ? -2.790  -5.406  52.586  1.00 112.05 ? 279 CYS E O   1 
ATOM   13774 C CB  . CYS E 2 279 ? -1.024  -8.177  53.062  1.00 94.00  ? 279 CYS E CB  1 
ATOM   13775 S SG  . CYS E 2 279 ? -0.334  -9.253  54.321  1.00 87.71  ? 279 CYS E SG  1 
ATOM   13776 N N   . ILE E 2 280 ? -1.032  -5.704  51.208  1.00 124.13 ? 280 ILE E N   1 
ATOM   13777 C CA  . ILE E 2 280 ? -1.597  -4.945  50.097  1.00 122.55 ? 280 ILE E CA  1 
ATOM   13778 C C   . ILE E 2 280 ? -1.401  -5.783  48.840  1.00 120.49 ? 280 ILE E C   1 
ATOM   13779 O O   . ILE E 2 280 ? -0.303  -5.822  48.274  1.00 120.27 ? 280 ILE E O   1 
ATOM   13780 C CB  . ILE E 2 280 ? -0.950  -3.565  49.943  1.00 123.97 ? 280 ILE E CB  1 
ATOM   13781 C CG1 . ILE E 2 280 ? -0.944  -2.822  51.282  1.00 126.72 ? 280 ILE E CG1 1 
ATOM   13782 C CG2 . ILE E 2 280 ? -1.687  -2.756  48.888  1.00 125.50 ? 280 ILE E CG2 1 
ATOM   13783 C CD1 . ILE E 2 280 ? -0.291  -1.463  51.225  1.00 132.84 ? 280 ILE E CD1 1 
ATOM   13784 N N   . VAL E 2 281 ? -2.461  -6.449  48.396  1.00 105.90 ? 281 VAL E N   1 
ATOM   13785 C CA  . VAL E 2 281 ? -2.427  -7.278  47.198  1.00 93.55  ? 281 VAL E CA  1 
ATOM   13786 C C   . VAL E 2 281 ? -2.995  -6.466  46.042  1.00 91.81  ? 281 VAL E C   1 
ATOM   13787 O O   . VAL E 2 281 ? -4.128  -5.972  46.114  1.00 98.05  ? 281 VAL E O   1 
ATOM   13788 C CB  . VAL E 2 281 ? -3.208  -8.583  47.396  1.00 89.95  ? 281 VAL E CB  1 
ATOM   13789 C CG1 . VAL E 2 281 ? -3.374  -9.296  46.072  1.00 83.42  ? 281 VAL E CG1 1 
ATOM   13790 C CG2 . VAL E 2 281 ? -2.486  -9.472  48.393  1.00 92.68  ? 281 VAL E CG2 1 
ATOM   13791 N N   . GLU E 2 282 ? -2.210  -6.321  44.979  1.00 79.10  ? 282 GLU E N   1 
ATOM   13792 C CA  . GLU E 2 282 ? -2.624  -5.553  43.818  1.00 73.83  ? 282 GLU E CA  1 
ATOM   13793 C C   . GLU E 2 282 ? -3.411  -6.455  42.865  1.00 72.40  ? 282 GLU E C   1 
ATOM   13794 O O   . GLU E 2 282 ? -3.716  -7.610  43.175  1.00 73.62  ? 282 GLU E O   1 
ATOM   13795 C CB  . GLU E 2 282 ? -1.404  -4.916  43.155  1.00 74.38  ? 282 GLU E CB  1 
ATOM   13796 C CG  . GLU E 2 282 ? -0.640  -3.952  44.064  1.00 77.04  ? 282 GLU E CG  1 
ATOM   13797 C CD  . GLU E 2 282 ? 0.354   -3.090  43.307  1.00 72.87  ? 282 GLU E CD  1 
ATOM   13798 O OE1 . GLU E 2 282 ? 0.555   -3.332  42.100  1.00 69.81  ? 282 GLU E OE1 1 
ATOM   13799 O OE2 . GLU E 2 282 ? 0.949   -2.181  43.923  1.00 76.78  ? 282 GLU E OE2 1 
ATOM   13800 N N   . SER E 2 283 ? -3.742  -5.932  41.690  1.00 71.96  ? 283 SER E N   1 
ATOM   13801 C CA  . SER E 2 283 ? -4.647  -6.594  40.762  1.00 69.20  ? 283 SER E CA  1 
ATOM   13802 C C   . SER E 2 283 ? -3.897  -7.536  39.831  1.00 66.95  ? 283 SER E C   1 
ATOM   13803 O O   . SER E 2 283 ? -2.714  -7.347  39.544  1.00 66.70  ? 283 SER E O   1 
ATOM   13804 C CB  . SER E 2 283 ? -5.407  -5.557  39.932  1.00 68.65  ? 283 SER E CB  1 
ATOM   13805 O OG  . SER E 2 283 ? -6.437  -4.947  40.691  1.00 77.09  ? 283 SER E OG  1 
ATOM   13806 N N   . GLY E 2 284 ? -4.603  -8.559  39.359  1.00 68.24  ? 284 GLY E N   1 
ATOM   13807 C CA  . GLY E 2 284 ? -4.049  -9.474  38.382  1.00 73.43  ? 284 GLY E CA  1 
ATOM   13808 C C   . GLY E 2 284 ? -3.138  -10.550 38.929  1.00 77.31  ? 284 GLY E C   1 
ATOM   13809 O O   . GLY E 2 284 ? -2.438  -11.199 38.144  1.00 80.84  ? 284 GLY E O   1 
ATOM   13810 N N   . VAL E 2 285 ? -3.116  -10.763 40.244  1.00 72.59  ? 285 VAL E N   1 
ATOM   13811 C CA  . VAL E 2 285 ? -2.192  -11.714 40.847  1.00 74.73  ? 285 VAL E CA  1 
ATOM   13812 C C   . VAL E 2 285 ? -2.818  -13.104 40.855  1.00 83.72  ? 285 VAL E C   1 
ATOM   13813 O O   . VAL E 2 285 ? -4.033  -13.272 40.723  1.00 90.80  ? 285 VAL E O   1 
ATOM   13814 C CB  . VAL E 2 285 ? -1.777  -11.288 42.271  1.00 70.32  ? 285 VAL E CB  1 
ATOM   13815 C CG1 . VAL E 2 285 ? -1.193  -9.884  42.264  1.00 68.44  ? 285 VAL E CG1 1 
ATOM   13816 C CG2 . VAL E 2 285 ? -2.957  -11.383 43.218  1.00 79.57  ? 285 VAL E CG2 1 
ATOM   13817 N N   . ARG E 2 286 ? -1.969  -14.121 41.018  1.00 81.04  ? 286 ARG E N   1 
ATOM   13818 C CA  . ARG E 2 286 ? -2.405  -15.520 41.029  1.00 85.40  ? 286 ARG E CA  1 
ATOM   13819 C C   . ARG E 2 286 ? -1.650  -16.226 42.151  1.00 77.73  ? 286 ARG E C   1 
ATOM   13820 O O   . ARG E 2 286 ? -0.485  -16.604 41.989  1.00 74.77  ? 286 ARG E O   1 
ATOM   13821 C CB  . ARG E 2 286 ? -2.171  -16.205 39.686  1.00 97.24  ? 286 ARG E CB  1 
ATOM   13822 C CG  . ARG E 2 286 ? -2.432  -17.710 39.706  1.00 97.68  ? 286 ARG E CG  1 
ATOM   13823 C CD  . ARG E 2 286 ? -3.782  -18.031 40.338  1.00 91.76  ? 286 ARG E CD  1 
ATOM   13824 N NE  . ARG E 2 286 ? -4.114  -19.450 40.277  1.00 87.35  ? 286 ARG E NE  1 
ATOM   13825 C CZ  . ARG E 2 286 ? -4.937  -20.052 41.130  1.00 86.87  ? 286 ARG E CZ  1 
ATOM   13826 N NH1 . ARG E 2 286 ? -5.499  -19.355 42.108  1.00 86.17  ? 286 ARG E NH1 1 
ATOM   13827 N NH2 . ARG E 2 286 ? -5.191  -21.348 41.013  1.00 87.92  ? 286 ARG E NH2 1 
ATOM   13828 N N   . LEU E 2 287 ? -2.314  -16.387 43.290  1.00 76.05  ? 287 LEU E N   1 
ATOM   13829 C CA  . LEU E 2 287 ? -1.725  -17.018 44.460  1.00 76.14  ? 287 LEU E CA  1 
ATOM   13830 C C   . LEU E 2 287 ? -2.248  -18.442 44.596  1.00 78.35  ? 287 LEU E C   1 
ATOM   13831 O O   . LEU E 2 287 ? -3.436  -18.702 44.383  1.00 80.13  ? 287 LEU E O   1 
ATOM   13832 C CB  . LEU E 2 287 ? -2.043  -16.204 45.711  1.00 78.46  ? 287 LEU E CB  1 
ATOM   13833 C CG  . LEU E 2 287 ? -1.599  -14.746 45.553  1.00 73.27  ? 287 LEU E CG  1 
ATOM   13834 C CD1 . LEU E 2 287 ? -1.874  -13.939 46.808  1.00 81.03  ? 287 LEU E CD1 1 
ATOM   13835 C CD2 . LEU E 2 287 ? -0.131  -14.661 45.158  1.00 71.80  ? 287 LEU E CD2 1 
ATOM   13836 N N   . SER E 2 288 ? -1.354  -19.364 44.949  1.00 79.61  ? 288 SER E N   1 
ATOM   13837 C CA  . SER E 2 288 ? -1.719  -20.772 45.038  1.00 83.23  ? 288 SER E CA  1 
ATOM   13838 C C   . SER E 2 288 ? -0.721  -21.493 45.928  1.00 86.38  ? 288 SER E C   1 
ATOM   13839 O O   . SER E 2 288 ? 0.489   -21.379 45.718  1.00 89.30  ? 288 SER E O   1 
ATOM   13840 C CB  . SER E 2 288 ? -1.758  -21.413 43.649  1.00 86.66  ? 288 SER E CB  1 
ATOM   13841 O OG  . SER E 2 288 ? -0.571  -21.125 42.931  1.00 82.93  ? 288 SER E OG  1 
ATOM   13842 N N   . ARG E 2 289 ? -1.231  -22.219 46.921  1.00 95.72  ? 289 ARG E N   1 
ATOM   13843 C CA  . ARG E 2 289 ? -0.429  -23.077 47.793  1.00 100.92 ? 289 ARG E CA  1 
ATOM   13844 C C   . ARG E 2 289 ? 0.647   -22.295 48.549  1.00 101.97 ? 289 ARG E C   1 
ATOM   13845 O O   . ARG E 2 289 ? 1.599   -22.885 49.072  1.00 106.56 ? 289 ARG E O   1 
ATOM   13846 C CB  . ARG E 2 289 ? 0.199   -24.233 46.997  1.00 103.24 ? 289 ARG E CB  1 
ATOM   13847 C CG  . ARG E 2 289 ? 0.554   -25.459 47.832  1.00 114.85 ? 289 ARG E CG  1 
ATOM   13848 C CD  . ARG E 2 289 ? 1.289   -26.508 47.012  1.00 116.24 ? 289 ARG E CD  1 
ATOM   13849 N NE  . ARG E 2 289 ? 2.021   -27.447 47.859  1.00 131.56 ? 289 ARG E NE  1 
ATOM   13850 C CZ  . ARG E 2 289 ? 1.496   -28.553 48.376  1.00 140.55 ? 289 ARG E CZ  1 
ATOM   13851 N NH1 . ARG E 2 289 ? 0.229   -28.862 48.137  1.00 144.55 ? 289 ARG E NH1 1 
ATOM   13852 N NH2 . ARG E 2 289 ? 2.236   -29.350 49.134  1.00 137.57 ? 289 ARG E NH2 1 
ATOM   13853 N N   . CYS E 2 290 ? 0.510   -20.974 48.620  1.00 93.06  ? 290 CYS E N   1 
ATOM   13854 C CA  . CYS E 2 290 ? 1.485   -20.103 49.258  1.00 88.77  ? 290 CYS E CA  1 
ATOM   13855 C C   . CYS E 2 290 ? 0.923   -19.508 50.544  1.00 90.71  ? 290 CYS E C   1 
ATOM   13856 O O   . CYS E 2 290 ? -0.254  -19.669 50.874  1.00 101.07 ? 290 CYS E O   1 
ATOM   13857 C CB  . CYS E 2 290 ? 1.912   -18.990 48.295  1.00 88.22  ? 290 CYS E CB  1 
ATOM   13858 S SG  . CYS E 2 290 ? 0.530   -18.067 47.582  1.00 81.79  ? 290 CYS E SG  1 
ATOM   13859 N N   . THR E 2 291 ? 1.795   -18.809 51.275  1.00 85.90  ? 291 THR E N   1 
ATOM   13860 C CA  . THR E 2 291 ? 1.424   -18.110 52.502  1.00 91.37  ? 291 THR E CA  1 
ATOM   13861 C C   . THR E 2 291 ? 2.056   -16.726 52.508  1.00 89.96  ? 291 THR E C   1 
ATOM   13862 O O   . THR E 2 291 ? 3.249   -16.585 52.220  1.00 88.85  ? 291 THR E O   1 
ATOM   13863 C CB  . THR E 2 291 ? 1.865   -18.867 53.764  1.00 93.63  ? 291 THR E CB  1 
ATOM   13864 O OG1 . THR E 2 291 ? 3.236   -18.559 54.051  1.00 91.32  ? 291 THR E OG1 1 
ATOM   13865 C CG2 . THR E 2 291 ? 1.707   -20.372 53.597  1.00 100.66 ? 291 THR E CG2 1 
ATOM   13866 N N   . VAL E 2 292 ? 1.254   -15.714 52.827  1.00 92.90  ? 292 VAL E N   1 
ATOM   13867 C CA  . VAL E 2 292 ? 1.690   -14.322 52.870  1.00 93.02  ? 292 VAL E CA  1 
ATOM   13868 C C   . VAL E 2 292 ? 1.689   -13.853 54.321  1.00 93.12  ? 292 VAL E C   1 
ATOM   13869 O O   . VAL E 2 292 ? 0.689   -14.013 55.031  1.00 96.76  ? 292 VAL E O   1 
ATOM   13870 C CB  . VAL E 2 292 ? 0.788   -13.429 52.000  1.00 93.61  ? 292 VAL E CB  1 
ATOM   13871 C CG1 . VAL E 2 292 ? 1.023   -11.966 52.315  1.00 91.49  ? 292 VAL E CG1 1 
ATOM   13872 C CG2 . VAL E 2 292 ? 1.043   -13.705 50.527  1.00 92.18  ? 292 VAL E CG2 1 
ATOM   13873 N N   . MET E 2 293 ? 2.808   -13.278 54.760  1.00 91.89  ? 293 MET E N   1 
ATOM   13874 C CA  . MET E 2 293 ? 2.930   -12.770 56.118  1.00 95.72  ? 293 MET E CA  1 
ATOM   13875 C C   . MET E 2 293 ? 2.596   -11.279 56.139  1.00 97.33  ? 293 MET E C   1 
ATOM   13876 O O   . MET E 2 293 ? 2.111   -10.716 55.157  1.00 97.95  ? 293 MET E O   1 
ATOM   13877 C CB  . MET E 2 293 ? 4.325   -13.053 56.673  1.00 102.70 ? 293 MET E CB  1 
ATOM   13878 C CG  . MET E 2 293 ? 4.613   -14.528 56.918  1.00 105.23 ? 293 MET E CG  1 
ATOM   13879 S SD  . MET E 2 293 ? 6.151   -14.785 57.830  1.00 109.31 ? 293 MET E SD  1 
ATOM   13880 C CE  . MET E 2 293 ? 6.270   -16.572 57.831  1.00 100.37 ? 293 MET E CE  1 
ATOM   13881 N N   . ARG E 2 294 ? 2.859   -10.624 57.265  1.00 103.91 ? 294 ARG E N   1 
ATOM   13882 C CA  . ARG E 2 294 ? 2.356   -9.278  57.503  1.00 103.47 ? 294 ARG E CA  1 
ATOM   13883 C C   . ARG E 2 294 ? 3.045   -8.242  56.623  1.00 103.17 ? 294 ARG E C   1 
ATOM   13884 O O   . ARG E 2 294 ? 4.219   -8.369  56.268  1.00 103.80 ? 294 ARG E O   1 
ATOM   13885 C CB  . ARG E 2 294 ? 2.547   -8.895  58.967  1.00 107.02 ? 294 ARG E CB  1 
ATOM   13886 C CG  . ARG E 2 294 ? 1.895   -9.840  59.949  1.00 112.90 ? 294 ARG E CG  1 
ATOM   13887 C CD  . ARG E 2 294 ? 2.148   -9.370  61.364  1.00 121.01 ? 294 ARG E CD  1 
ATOM   13888 N NE  . ARG E 2 294 ? 1.806   -7.960  61.521  1.00 123.69 ? 294 ARG E NE  1 
ATOM   13889 C CZ  . ARG E 2 294 ? 1.866   -7.299  62.672  1.00 129.44 ? 294 ARG E CZ  1 
ATOM   13890 N NH1 . ARG E 2 294 ? 2.255   -7.919  63.778  1.00 134.98 ? 294 ARG E NH1 1 
ATOM   13891 N NH2 . ARG E 2 294 ? 1.531   -6.017  62.717  1.00 132.27 ? 294 ARG E NH2 1 
ATOM   13892 N N   . GLY E 2 295 ? 2.288   -7.199  56.278  1.00 99.70  ? 295 GLY E N   1 
ATOM   13893 C CA  . GLY E 2 295 ? 2.823   -5.969  55.729  1.00 101.93 ? 295 GLY E CA  1 
ATOM   13894 C C   . GLY E 2 295 ? 3.401   -6.039  54.334  1.00 97.03  ? 295 GLY E C   1 
ATOM   13895 O O   . GLY E 2 295 ? 3.699   -4.986  53.758  1.00 98.95  ? 295 GLY E O   1 
ATOM   13896 N N   . VAL E 2 296 ? 3.568   -7.222  53.764  1.00 93.79  ? 296 VAL E N   1 
ATOM   13897 C CA  . VAL E 2 296 ? 4.172   -7.336  52.443  1.00 96.91  ? 296 VAL E CA  1 
ATOM   13898 C C   . VAL E 2 296 ? 3.136   -6.991  51.383  1.00 95.98  ? 296 VAL E C   1 
ATOM   13899 O O   . VAL E 2 296 ? 1.978   -7.422  51.452  1.00 92.85  ? 296 VAL E O   1 
ATOM   13900 C CB  . VAL E 2 296 ? 4.750   -8.747  52.235  1.00 98.25  ? 296 VAL E CB  1 
ATOM   13901 C CG1 . VAL E 2 296 ? 3.780   -9.784  52.728  1.00 98.09  ? 296 VAL E CG1 1 
ATOM   13902 C CG2 . VAL E 2 296 ? 5.068   -8.980  50.768  1.00 99.39  ? 296 VAL E CG2 1 
ATOM   13903 N N   . ARG E 2 297 ? 3.554   -6.206  50.395  1.00 103.12 ? 297 ARG E N   1 
ATOM   13904 C CA  . ARG E 2 297 ? 2.707   -5.824  49.275  1.00 102.10 ? 297 ARG E CA  1 
ATOM   13905 C C   . ARG E 2 297 ? 3.134   -6.592  48.031  1.00 98.29  ? 297 ARG E C   1 
ATOM   13906 O O   . ARG E 2 297 ? 4.322   -6.620  47.688  1.00 98.21  ? 297 ARG E O   1 
ATOM   13907 C CB  . ARG E 2 297 ? 2.773   -4.319  49.010  1.00 106.89 ? 297 ARG E CB  1 
ATOM   13908 C CG  . ARG E 2 297 ? 2.199   -3.919  47.657  1.00 105.72 ? 297 ARG E CG  1 
ATOM   13909 C CD  . ARG E 2 297 ? 2.505   -2.474  47.303  1.00 110.62 ? 297 ARG E CD  1 
ATOM   13910 N NE  . ARG E 2 297 ? 1.996   -1.539  48.303  1.00 125.58 ? 297 ARG E NE  1 
ATOM   13911 C CZ  . ARG E 2 297 ? 1.938   -0.223  48.127  1.00 129.92 ? 297 ARG E CZ  1 
ATOM   13912 N NH1 . ARG E 2 297 ? 2.353   0.312   46.987  1.00 135.04 ? 297 ARG E NH1 1 
ATOM   13913 N NH2 . ARG E 2 297 ? 1.466   0.559   49.089  1.00 127.77 ? 297 ARG E NH2 1 
ATOM   13914 N N   . ILE E 2 298 ? 2.166   -7.216  47.366  1.00 87.08  ? 298 ILE E N   1 
ATOM   13915 C CA  . ILE E 2 298 ? 2.395   -7.927  46.115  1.00 80.47  ? 298 ILE E CA  1 
ATOM   13916 C C   . ILE E 2 298 ? 1.845   -7.070  44.987  1.00 77.83  ? 298 ILE E C   1 
ATOM   13917 O O   . ILE E 2 298 ? 0.655   -6.733  44.975  1.00 79.33  ? 298 ILE E O   1 
ATOM   13918 C CB  . ILE E 2 298 ? 1.733   -9.312  46.123  1.00 78.76  ? 298 ILE E CB  1 
ATOM   13919 C CG1 . ILE E 2 298 ? 2.328   -10.181 47.234  1.00 76.98  ? 298 ILE E CG1 1 
ATOM   13920 C CG2 . ILE E 2 298 ? 1.880   -9.977  44.760  1.00 73.68  ? 298 ILE E CG2 1 
ATOM   13921 C CD1 . ILE E 2 298 ? 1.716   -11.554 47.321  1.00 73.99  ? 298 ILE E CD1 1 
ATOM   13922 N N   . LYS E 2 299 ? 2.710   -6.716  44.041  1.00 71.55  ? 299 LYS E N   1 
ATOM   13923 C CA  . LYS E 2 299 ? 2.337   -5.799  42.974  1.00 67.28  ? 299 LYS E CA  1 
ATOM   13924 C C   . LYS E 2 299 ? 1.498   -6.520  41.920  1.00 74.01  ? 299 LYS E C   1 
ATOM   13925 O O   . LYS E 2 299 ? 1.141   -7.694  42.058  1.00 65.95  ? 299 LYS E O   1 
ATOM   13926 C CB  . LYS E 2 299 ? 3.580   -5.153  42.368  1.00 66.74  ? 299 LYS E CB  1 
ATOM   13927 C CG  . LYS E 2 299 ? 4.310   -4.206  43.309  1.00 69.05  ? 299 LYS E CG  1 
ATOM   13928 C CD  . LYS E 2 299 ? 5.489   -3.539  42.612  1.00 69.15  ? 299 LYS E CD  1 
ATOM   13929 C CE  . LYS E 2 299 ? 6.226   -2.589  43.546  1.00 69.33  ? 299 LYS E CE  1 
ATOM   13930 N NZ  . LYS E 2 299 ? 7.381   -1.924  42.875  1.00 75.73  ? 299 LYS E NZ  1 
ATOM   13931 N N   . LYS E 2 300 ? 1.181   -5.808  40.843  1.00 65.79  ? 300 LYS E N   1 
ATOM   13932 C CA  . LYS E 2 300 ? 0.217   -6.298  39.873  1.00 65.62  ? 300 LYS E CA  1 
ATOM   13933 C C   . LYS E 2 300 ? 0.804   -7.414  39.020  1.00 64.85  ? 300 LYS E C   1 
ATOM   13934 O O   . LYS E 2 300 ? 2.007   -7.457  38.747  1.00 64.35  ? 300 LYS E O   1 
ATOM   13935 C CB  . LYS E 2 300 ? -0.257  -5.161  38.965  1.00 66.22  ? 300 LYS E CB  1 
ATOM   13936 C CG  . LYS E 2 300 ? -1.208  -4.178  39.624  1.00 71.48  ? 300 LYS E CG  1 
ATOM   13937 C CD  . LYS E 2 300 ? -1.595  -3.050  38.676  1.00 76.89  ? 300 LYS E CD  1 
ATOM   13938 C CE  . LYS E 2 300 ? -0.555  -1.938  38.670  1.00 79.56  ? 300 LYS E CE  1 
ATOM   13939 N NZ  . LYS E 2 300 ? -1.009  -0.730  37.920  1.00 83.35  ? 300 LYS E NZ  1 
ATOM   13940 N N   . HIS E 2 301 ? -0.073  -8.333  38.612  1.00 67.90  ? 301 HIS E N   1 
ATOM   13941 C CA  . HIS E 2 301 ? 0.237   -9.357  37.617  1.00 67.33  ? 301 HIS E CA  1 
ATOM   13942 C C   . HIS E 2 301 ? 1.304   -10.336 38.102  1.00 63.84  ? 301 HIS E C   1 
ATOM   13943 O O   . HIS E 2 301 ? 2.046   -10.905 37.299  1.00 63.23  ? 301 HIS E O   1 
ATOM   13944 C CB  . HIS E 2 301 ? 0.656   -8.712  36.294  1.00 66.70  ? 301 HIS E CB  1 
ATOM   13945 C CG  . HIS E 2 301 ? -0.275  -7.632  35.835  1.00 67.45  ? 301 HIS E CG  1 
ATOM   13946 N ND1 . HIS E 2 301 ? 0.162   -6.499  35.187  1.00 72.21  ? 301 HIS E ND1 1 
ATOM   13947 C CD2 . HIS E 2 301 ? -1.619  -7.511  35.937  1.00 69.13  ? 301 HIS E CD2 1 
ATOM   13948 C CE1 . HIS E 2 301 ? -0.872  -5.726  34.905  1.00 71.27  ? 301 HIS E CE1 1 
ATOM   13949 N NE2 . HIS E 2 301 ? -1.966  -6.319  35.347  1.00 70.00  ? 301 HIS E NE2 1 
ATOM   13950 N N   . ALA E 2 302 ? 1.390   -10.544 39.411  1.00 64.28  ? 302 ALA E N   1 
ATOM   13951 C CA  . ALA E 2 302 ? 2.334   -11.501 39.963  1.00 64.08  ? 302 ALA E CA  1 
ATOM   13952 C C   . ALA E 2 302 ? 1.691   -12.879 40.041  1.00 64.16  ? 302 ALA E C   1 
ATOM   13953 O O   . ALA E 2 302 ? 0.487   -13.014 40.263  1.00 73.22  ? 302 ALA E O   1 
ATOM   13954 C CB  . ALA E 2 302 ? 2.811   -11.066 41.348  1.00 64.57  ? 302 ALA E CB  1 
ATOM   13955 N N   . CYS E 2 303 ? 2.510   -13.908 39.850  1.00 63.73  ? 303 CYS E N   1 
ATOM   13956 C CA  . CYS E 2 303 ? 2.051   -15.294 39.880  1.00 63.78  ? 303 CYS E CA  1 
ATOM   13957 C C   . CYS E 2 303 ? 2.923   -16.056 40.869  1.00 65.69  ? 303 CYS E C   1 
ATOM   13958 O O   . CYS E 2 303 ? 4.078   -16.375 40.569  1.00 70.51  ? 303 CYS E O   1 
ATOM   13959 C CB  . CYS E 2 303 ? 2.107   -15.919 38.486  1.00 71.07  ? 303 CYS E CB  1 
ATOM   13960 S SG  . CYS E 2 303 ? 1.608   -17.649 38.431  1.00 82.80  ? 303 CYS E SG  1 
ATOM   13961 N N   . ILE E 2 304 ? 2.372   -16.343 42.046  1.00 65.58  ? 304 ILE E N   1 
ATOM   13962 C CA  . ILE E 2 304 ? 3.092   -17.010 43.124  1.00 74.25  ? 304 ILE E CA  1 
ATOM   13963 C C   . ILE E 2 304 ? 2.441   -18.357 43.395  1.00 76.64  ? 304 ILE E C   1 
ATOM   13964 O O   . ILE E 2 304 ? 1.221   -18.435 43.580  1.00 77.81  ? 304 ILE E O   1 
ATOM   13965 C CB  . ILE E 2 304 ? 3.115   -16.150 44.398  1.00 68.99  ? 304 ILE E CB  1 
ATOM   13966 C CG1 . ILE E 2 304 ? 3.743   -14.788 44.104  1.00 69.06  ? 304 ILE E CG1 1 
ATOM   13967 C CG2 . ILE E 2 304 ? 3.863   -16.872 45.506  1.00 74.61  ? 304 ILE E CG2 1 
ATOM   13968 C CD1 . ILE E 2 304 ? 4.035   -13.986 45.333  1.00 75.10  ? 304 ILE E CD1 1 
ATOM   13969 N N   . SER E 2 305 ? 3.250   -19.414 43.401  1.00 88.02  ? 305 SER E N   1 
ATOM   13970 C CA  . SER E 2 305 ? 2.774   -20.763 43.677  1.00 88.70  ? 305 SER E CA  1 
ATOM   13971 C C   . SER E 2 305 ? 3.720   -21.439 44.654  1.00 91.18  ? 305 SER E C   1 
ATOM   13972 O O   . SER E 2 305 ? 4.931   -21.454 44.425  1.00 92.22  ? 305 SER E O   1 
ATOM   13973 C CB  . SER E 2 305 ? 2.677   -21.597 42.397  1.00 86.55  ? 305 SER E CB  1 
ATOM   13974 O OG  . SER E 2 305 ? 3.752   -21.305 41.520  1.00 85.51  ? 305 SER E OG  1 
ATOM   13975 N N   . SER E 2 306 ? 3.157   -22.022 45.713  1.00 88.90  ? 306 SER E N   1 
ATOM   13976 C CA  . SER E 2 306 ? 3.873   -22.847 46.694  1.00 89.79  ? 306 SER E CA  1 
ATOM   13977 C C   . SER E 2 306 ? 5.171   -22.194 47.176  1.00 81.16  ? 306 SER E C   1 
ATOM   13978 O O   . SER E 2 306 ? 6.272   -22.702 46.963  1.00 80.11  ? 306 SER E O   1 
ATOM   13979 C CB  . SER E 2 306 ? 4.148   -24.249 46.135  1.00 91.78  ? 306 SER E CB  1 
ATOM   13980 O OG  . SER E 2 306 ? 4.901   -24.196 44.938  1.00 88.66  ? 306 SER E OG  1 
ATOM   13981 N N   . SER E 2 307 ? 5.025   -21.050 47.843  1.00 81.66  ? 307 SER E N   1 
ATOM   13982 C CA  . SER E 2 307 ? 6.167   -20.299 48.345  1.00 76.76  ? 307 SER E CA  1 
ATOM   13983 C C   . SER E 2 307 ? 5.809   -19.670 49.686  1.00 80.04  ? 307 SER E C   1 
ATOM   13984 O O   . SER E 2 307 ? 4.669   -19.754 50.152  1.00 92.44  ? 307 SER E O   1 
ATOM   13985 C CB  . SER E 2 307 ? 6.616   -19.243 47.332  1.00 78.45  ? 307 SER E CB  1 
ATOM   13986 O OG  . SER E 2 307 ? 7.124   -19.858 46.162  1.00 89.91  ? 307 SER E OG  1 
ATOM   13987 N N   . ILE E 2 308 ? 6.795   -19.019 50.302  1.00 79.33  ? 308 ILE E N   1 
ATOM   13988 C CA  . ILE E 2 308 ? 6.647   -18.407 51.619  1.00 85.24  ? 308 ILE E CA  1 
ATOM   13989 C C   . ILE E 2 308 ? 7.193   -16.987 51.558  1.00 90.27  ? 308 ILE E C   1 
ATOM   13990 O O   . ILE E 2 308 ? 8.364   -16.784 51.213  1.00 85.47  ? 308 ILE E O   1 
ATOM   13991 C CB  . ILE E 2 308 ? 7.371   -19.209 52.712  1.00 85.32  ? 308 ILE E CB  1 
ATOM   13992 C CG1 . ILE E 2 308 ? 6.832   -20.640 52.792  1.00 92.84  ? 308 ILE E CG1 1 
ATOM   13993 C CG2 . ILE E 2 308 ? 7.234   -18.505 54.051  1.00 92.25  ? 308 ILE E CG2 1 
ATOM   13994 C CD1 . ILE E 2 308 ? 5.428   -20.738 53.335  1.00 103.68 ? 308 ILE E CD1 1 
ATOM   13995 N N   . ILE E 2 309 ? 6.352   -16.011 51.889  1.00 111.17 ? 309 ILE E N   1 
ATOM   13996 C CA  . ILE E 2 309 ? 6.707   -14.596 51.843  1.00 111.71 ? 309 ILE E CA  1 
ATOM   13997 C C   . ILE E 2 309 ? 6.866   -14.077 53.266  1.00 114.52 ? 309 ILE E C   1 
ATOM   13998 O O   . ILE E 2 309 ? 5.981   -14.273 54.107  1.00 115.18 ? 309 ILE E O   1 
ATOM   13999 C CB  . ILE E 2 309 ? 5.655   -13.776 51.080  1.00 109.89 ? 309 ILE E CB  1 
ATOM   14000 C CG1 . ILE E 2 309 ? 5.272   -14.484 49.781  1.00 109.92 ? 309 ILE E CG1 1 
ATOM   14001 C CG2 . ILE E 2 309 ? 6.191   -12.390 50.784  1.00 110.07 ? 309 ILE E CG2 1 
ATOM   14002 C CD1 . ILE E 2 309 ? 6.434   -14.695 48.839  1.00 106.36 ? 309 ILE E CD1 1 
ATOM   14003 N N   . GLY E 2 310 ? 7.991   -13.414 53.530  1.00 101.70 ? 310 GLY E N   1 
ATOM   14004 C CA  . GLY E 2 310 ? 8.290   -12.866 54.837  1.00 100.40 ? 310 GLY E CA  1 
ATOM   14005 C C   . GLY E 2 310 ? 7.555   -11.565 55.114  1.00 103.23 ? 310 GLY E C   1 
ATOM   14006 O O   . GLY E 2 310 ? 6.687   -11.122 54.361  1.00 106.85 ? 310 GLY E O   1 
ATOM   14007 N N   . TRP E 2 311 ? 7.920   -10.948 56.237  1.00 107.79 ? 311 TRP E N   1 
ATOM   14008 C CA  . TRP E 2 311 ? 7.298   -9.699  56.655  1.00 108.21 ? 311 TRP E CA  1 
ATOM   14009 C C   . TRP E 2 311 ? 7.817   -8.518  55.848  1.00 107.91 ? 311 TRP E C   1 
ATOM   14010 O O   . TRP E 2 311 ? 9.013   -8.421  55.556  1.00 108.70 ? 311 TRP E O   1 
ATOM   14011 C CB  . TRP E 2 311 ? 7.553   -9.407  58.136  1.00 112.23 ? 311 TRP E CB  1 
ATOM   14012 C CG  . TRP E 2 311 ? 7.002   -10.378 59.126  1.00 118.11 ? 311 TRP E CG  1 
ATOM   14013 C CD1 . TRP E 2 311 ? 6.923   -11.733 59.008  1.00 117.43 ? 311 TRP E CD1 1 
ATOM   14014 C CD2 . TRP E 2 311 ? 6.442   -10.052 60.404  1.00 125.04 ? 311 TRP E CD2 1 
ATOM   14015 N NE1 . TRP E 2 311 ? 6.352   -12.273 60.136  1.00 122.63 ? 311 TRP E NE1 1 
ATOM   14016 C CE2 . TRP E 2 311 ? 6.048   -11.261 61.008  1.00 125.47 ? 311 TRP E CE2 1 
ATOM   14017 C CE3 . TRP E 2 311 ? 6.238   -8.853  61.098  1.00 122.37 ? 311 TRP E CE3 1 
ATOM   14018 C CZ2 . TRP E 2 311 ? 5.461   -11.308 62.271  1.00 122.02 ? 311 TRP E CZ2 1 
ATOM   14019 C CZ3 . TRP E 2 311 ? 5.656   -8.902  62.352  1.00 119.32 ? 311 TRP E CZ3 1 
ATOM   14020 C CH2 . TRP E 2 311 ? 5.274   -10.121 62.925  1.00 120.25 ? 311 TRP E CH2 1 
ATOM   14021 N N   . HIS E 2 312 ? 6.897   -7.619  55.498  1.00 119.76 ? 312 HIS E N   1 
ATOM   14022 C CA  . HIS E 2 312 ? 7.223   -6.311  54.931  1.00 119.59 ? 312 HIS E CA  1 
ATOM   14023 C C   . HIS E 2 312 ? 8.095   -6.430  53.685  1.00 117.84 ? 312 HIS E C   1 
ATOM   14024 O O   . HIS E 2 312 ? 8.973   -5.601  53.436  1.00 118.25 ? 312 HIS E O   1 
ATOM   14025 C CB  . HIS E 2 312 ? 7.901   -5.425  55.979  1.00 123.34 ? 312 HIS E CB  1 
ATOM   14026 C CG  . HIS E 2 312 ? 7.127   -5.309  57.256  1.00 124.46 ? 312 HIS E CG  1 
ATOM   14027 N ND1 . HIS E 2 312 ? 7.336   -6.150  58.327  1.00 125.43 ? 312 HIS E ND1 1 
ATOM   14028 C CD2 . HIS E 2 312 ? 6.140   -4.461  57.630  1.00 126.20 ? 312 HIS E CD2 1 
ATOM   14029 C CE1 . HIS E 2 312 ? 6.515   -5.822  59.309  1.00 126.18 ? 312 HIS E CE1 1 
ATOM   14030 N NE2 . HIS E 2 312 ? 5.779   -4.800  58.911  1.00 128.23 ? 312 HIS E NE2 1 
ATOM   14031 N N   . SER E 2 313 ? 7.853   -7.466  52.892  1.00 103.38 ? 313 SER E N   1 
ATOM   14032 C CA  . SER E 2 313 ? 8.572   -7.625  51.642  1.00 99.23  ? 313 SER E CA  1 
ATOM   14033 C C   . SER E 2 313 ? 7.796   -6.934  50.527  1.00 92.01  ? 313 SER E C   1 
ATOM   14034 O O   . SER E 2 313 ? 6.782   -6.272  50.756  1.00 96.52  ? 313 SER E O   1 
ATOM   14035 C CB  . SER E 2 313 ? 8.796   -9.104  51.333  1.00 97.65  ? 313 SER E CB  1 
ATOM   14036 O OG  . SER E 2 313 ? 9.633   -9.701  52.303  1.00 96.63  ? 313 SER E OG  1 
ATOM   14037 N N   . THR E 2 314 ? 8.280   -7.085  49.299  1.00 88.63  ? 314 THR E N   1 
ATOM   14038 C CA  . THR E 2 314 ? 7.628   -6.441  48.165  1.00 80.52  ? 314 THR E CA  1 
ATOM   14039 C C   . THR E 2 314 ? 7.958   -7.226  46.909  1.00 83.76  ? 314 THR E C   1 
ATOM   14040 O O   . THR E 2 314 ? 9.128   -7.312  46.521  1.00 89.64  ? 314 THR E O   1 
ATOM   14041 C CB  . THR E 2 314 ? 8.072   -4.990  48.027  1.00 88.70  ? 314 THR E CB  1 
ATOM   14042 O OG1 . THR E 2 314 ? 7.610   -4.242  49.158  1.00 94.07  ? 314 THR E OG1 1 
ATOM   14043 C CG2 . THR E 2 314 ? 7.489   -4.387  46.763  1.00 84.84  ? 314 THR E CG2 1 
ATOM   14044 N N   . VAL E 2 315 ? 6.934   -7.781  46.273  1.00 76.63  ? 315 VAL E N   1 
ATOM   14045 C CA  . VAL E 2 315 ? 7.077   -8.516  45.022  1.00 76.60  ? 315 VAL E CA  1 
ATOM   14046 C C   . VAL E 2 315 ? 6.734   -7.574  43.880  1.00 73.14  ? 315 VAL E C   1 
ATOM   14047 O O   . VAL E 2 315 ? 5.625   -7.031  43.829  1.00 76.05  ? 315 VAL E O   1 
ATOM   14048 C CB  . VAL E 2 315 ? 6.176   -9.759  44.991  1.00 73.96  ? 315 VAL E CB  1 
ATOM   14049 C CG1 . VAL E 2 315 ? 6.262   -10.426 43.631  1.00 72.93  ? 315 VAL E CG1 1 
ATOM   14050 C CG2 . VAL E 2 315 ? 6.563   -10.725 46.097  1.00 73.84  ? 315 VAL E CG2 1 
ATOM   14051 N N   . GLY E 2 316 ? 7.680   -7.378  42.967  1.00 74.24  ? 316 GLY E N   1 
ATOM   14052 C CA  . GLY E 2 316 ? 7.456   -6.486  41.851  1.00 66.22  ? 316 GLY E CA  1 
ATOM   14053 C C   . GLY E 2 316 ? 6.383   -6.997  40.904  1.00 69.07  ? 316 GLY E C   1 
ATOM   14054 O O   . GLY E 2 316 ? 5.862   -8.106  41.026  1.00 64.05  ? 316 GLY E O   1 
ATOM   14055 N N   . GLN E 2 317 ? 6.052   -6.153  39.930  1.00 63.95  ? 317 GLN E N   1 
ATOM   14056 C CA  . GLN E 2 317 ? 5.027   -6.493  38.954  1.00 63.75  ? 317 GLN E CA  1 
ATOM   14057 C C   . GLN E 2 317 ? 5.513   -7.590  38.013  1.00 63.06  ? 317 GLN E C   1 
ATOM   14058 O O   . GLN E 2 317 ? 6.700   -7.689  37.697  1.00 64.28  ? 317 GLN E O   1 
ATOM   14059 C CB  . GLN E 2 317 ? 4.624   -5.255  38.152  1.00 63.84  ? 317 GLN E CB  1 
ATOM   14060 C CG  . GLN E 2 317 ? 3.999   -4.147  38.983  1.00 64.58  ? 317 GLN E CG  1 
ATOM   14061 C CD  . GLN E 2 317 ? 3.649   -2.923  38.160  1.00 64.71  ? 317 GLN E CD  1 
ATOM   14062 O OE1 . GLN E 2 317 ? 3.840   -2.901  36.944  1.00 66.88  ? 317 GLN E OE1 1 
ATOM   14063 N NE2 . GLN E 2 317 ? 3.133   -1.896  38.822  1.00 73.42  ? 317 GLN E NE2 1 
ATOM   14064 N N   . TRP E 2 318 ? 4.571   -8.425  37.567  1.00 62.99  ? 318 TRP E N   1 
ATOM   14065 C CA  . TRP E 2 318 ? 4.828   -9.510  36.619  1.00 62.41  ? 318 TRP E CA  1 
ATOM   14066 C C   . TRP E 2 318 ? 5.886   -10.496 37.112  1.00 62.16  ? 318 TRP E C   1 
ATOM   14067 O O   . TRP E 2 318 ? 6.429   -11.270 36.320  1.00 62.65  ? 318 TRP E O   1 
ATOM   14068 C CB  . TRP E 2 318 ? 5.236   -8.972  35.242  1.00 64.72  ? 318 TRP E CB  1 
ATOM   14069 C CG  . TRP E 2 318 ? 4.124   -8.329  34.471  1.00 67.62  ? 318 TRP E CG  1 
ATOM   14070 C CD1 . TRP E 2 318 ? 3.111   -8.964  33.809  1.00 68.11  ? 318 TRP E CD1 1 
ATOM   14071 C CD2 . TRP E 2 318 ? 3.918   -6.928  34.268  1.00 63.39  ? 318 TRP E CD2 1 
ATOM   14072 N NE1 . TRP E 2 318 ? 2.286   -8.043  33.211  1.00 68.04  ? 318 TRP E NE1 1 
ATOM   14073 C CE2 . TRP E 2 318 ? 2.760   -6.785  33.477  1.00 69.58  ? 318 TRP E CE2 1 
ATOM   14074 C CE3 . TRP E 2 318 ? 4.599   -5.779  34.678  1.00 66.74  ? 318 TRP E CE3 1 
ATOM   14075 C CZ2 . TRP E 2 318 ? 2.269   -5.540  33.090  1.00 67.97  ? 318 TRP E CZ2 1 
ATOM   14076 C CZ3 . TRP E 2 318 ? 4.109   -4.545  34.295  1.00 67.98  ? 318 TRP E CZ3 1 
ATOM   14077 C CH2 . TRP E 2 318 ? 2.955   -4.435  33.512  1.00 69.29  ? 318 TRP E CH2 1 
ATOM   14078 N N   . ALA E 2 319 ? 6.193   -10.498 38.405  1.00 62.55  ? 319 ALA E N   1 
ATOM   14079 C CA  . ALA E 2 319 ? 7.197   -11.412 38.926  1.00 62.39  ? 319 ALA E CA  1 
ATOM   14080 C C   . ALA E 2 319 ? 6.599   -12.794 39.149  1.00 62.45  ? 319 ALA E C   1 
ATOM   14081 O O   . ALA E 2 319 ? 5.467   -12.929 39.622  1.00 62.89  ? 319 ALA E O   1 
ATOM   14082 C CB  . ALA E 2 319 ? 7.784   -10.877 40.230  1.00 62.85  ? 319 ALA E CB  1 
ATOM   14083 N N   . ARG E 2 320 ? 7.369   -13.824 38.806  1.00 62.04  ? 320 ARG E N   1 
ATOM   14084 C CA  . ARG E 2 320 ? 6.943   -15.207 38.963  1.00 62.09  ? 320 ARG E CA  1 
ATOM   14085 C C   . ARG E 2 320 ? 7.765   -15.877 40.053  1.00 63.30  ? 320 ARG E C   1 
ATOM   14086 O O   . ARG E 2 320 ? 9.000   -15.887 39.997  1.00 75.08  ? 320 ARG E O   1 
ATOM   14087 C CB  . ARG E 2 320 ? 7.071   -15.999 37.661  1.00 61.52  ? 320 ARG E CB  1 
ATOM   14088 C CG  . ARG E 2 320 ? 6.619   -17.434 37.850  1.00 63.71  ? 320 ARG E CG  1 
ATOM   14089 C CD  . ARG E 2 320 ? 6.713   -18.289 36.607  1.00 71.26  ? 320 ARG E CD  1 
ATOM   14090 N NE  . ARG E 2 320 ? 6.241   -19.637 36.905  1.00 80.96  ? 320 ARG E NE  1 
ATOM   14091 C CZ  . ARG E 2 320 ? 4.986   -20.040 36.733  1.00 85.91  ? 320 ARG E CZ  1 
ATOM   14092 N NH1 . ARG E 2 320 ? 4.077   -19.197 36.260  1.00 86.38  ? 320 ARG E NH1 1 
ATOM   14093 N NH2 . ARG E 2 320 ? 4.640   -21.283 37.036  1.00 86.06  ? 320 ARG E NH2 1 
ATOM   14094 N N   . ILE E 2 321 ? 7.068   -16.439 41.036  1.00 76.69  ? 321 ILE E N   1 
ATOM   14095 C CA  . ILE E 2 321 ? 7.669   -17.096 42.188  1.00 78.58  ? 321 ILE E CA  1 
ATOM   14096 C C   . ILE E 2 321 ? 7.070   -18.493 42.279  1.00 79.70  ? 321 ILE E C   1 
ATOM   14097 O O   . ILE E 2 321 ? 5.843   -18.642 42.289  1.00 81.73  ? 321 ILE E O   1 
ATOM   14098 C CB  . ILE E 2 321 ? 7.406   -16.306 43.485  1.00 80.26  ? 321 ILE E CB  1 
ATOM   14099 C CG1 . ILE E 2 321 ? 7.829   -14.845 43.321  1.00 80.09  ? 321 ILE E CG1 1 
ATOM   14100 C CG2 . ILE E 2 321 ? 8.133   -16.939 44.653  1.00 83.33  ? 321 ILE E CG2 1 
ATOM   14101 C CD1 . ILE E 2 321 ? 9.300   -14.657 43.048  1.00 80.87  ? 321 ILE E CD1 1 
ATOM   14102 N N   . GLU E 2 322 ? 7.923   -19.514 42.338  1.00 91.77  ? 322 GLU E N   1 
ATOM   14103 C CA  . GLU E 2 322 ? 7.427   -20.883 42.401  1.00 92.07  ? 322 GLU E CA  1 
ATOM   14104 C C   . GLU E 2 322 ? 8.471   -21.775 43.055  1.00 94.13  ? 322 GLU E C   1 
ATOM   14105 O O   . GLU E 2 322 ? 9.611   -21.368 43.296  1.00 94.89  ? 322 GLU E O   1 
ATOM   14106 C CB  . GLU E 2 322 ? 7.076   -21.429 41.014  1.00 90.22  ? 322 GLU E CB  1 
ATOM   14107 C CG  . GLU E 2 322 ? 8.278   -21.632 40.104  1.00 88.60  ? 322 GLU E CG  1 
ATOM   14108 C CD  . GLU E 2 322 ? 7.897   -22.266 38.781  1.00 87.74  ? 322 GLU E CD  1 
ATOM   14109 O OE1 . GLU E 2 322 ? 6.687   -22.465 38.547  1.00 85.38  ? 322 GLU E OE1 1 
ATOM   14110 O OE2 . GLU E 2 322 ? 8.805   -22.576 37.981  1.00 91.83  ? 322 GLU E OE2 1 
ATOM   14111 N N   . ASN E 2 323 ? 8.045   -23.005 43.346  1.00 84.72  ? 323 ASN E N   1 
ATOM   14112 C CA  . ASN E 2 323 ? 8.920   -24.100 43.761  1.00 84.06  ? 323 ASN E CA  1 
ATOM   14113 C C   . ASN E 2 323 ? 9.617   -23.790 45.089  1.00 79.93  ? 323 ASN E C   1 
ATOM   14114 O O   . ASN E 2 323 ? 10.845  -23.761 45.190  1.00 78.03  ? 323 ASN E O   1 
ATOM   14115 C CB  . ASN E 2 323 ? 9.933   -24.426 42.657  1.00 80.17  ? 323 ASN E CB  1 
ATOM   14116 C CG  . ASN E 2 323 ? 10.700  -25.706 42.930  1.00 81.45  ? 323 ASN E CG  1 
ATOM   14117 O OD1 . ASN E 2 323 ? 10.268  -26.544 43.721  1.00 87.25  ? 323 ASN E OD1 1 
ATOM   14118 N ND2 . ASN E 2 323 ? 11.842  -25.865 42.271  1.00 79.44  ? 323 ASN E ND2 1 
ATOM   14119 N N   . MET E 2 324 ? 8.793   -23.593 46.121  1.00 82.81  ? 324 MET E N   1 
ATOM   14120 C CA  . MET E 2 324 ? 9.256   -23.464 47.504  1.00 85.05  ? 324 MET E CA  1 
ATOM   14121 C C   . MET E 2 324 ? 10.301  -22.357 47.654  1.00 84.91  ? 324 MET E C   1 
ATOM   14122 O O   . MET E 2 324 ? 11.358  -22.542 48.260  1.00 87.02  ? 324 MET E O   1 
ATOM   14123 C CB  . MET E 2 324 ? 9.789   -24.804 48.014  1.00 95.81  ? 324 MET E CB  1 
ATOM   14124 C CG  . MET E 2 324 ? 8.757   -25.921 47.954  1.00 101.68 ? 324 MET E CG  1 
ATOM   14125 S SD  . MET E 2 324 ? 9.453   -27.550 48.273  1.00 119.78 ? 324 MET E SD  1 
ATOM   14126 C CE  . MET E 2 324 ? 10.671  -27.647 46.960  1.00 103.33 ? 324 MET E CE  1 
ATOM   14127 N N   . THR E 2 325 ? 9.992   -21.193 47.092  1.00 82.66  ? 325 THR E N   1 
ATOM   14128 C CA  . THR E 2 325 ? 10.864  -20.032 47.217  1.00 73.22  ? 325 THR E CA  1 
ATOM   14129 C C   . THR E 2 325 ? 10.638  -19.370 48.571  1.00 70.16  ? 325 THR E C   1 
ATOM   14130 O O   . THR E 2 325 ? 9.507   -19.006 48.910  1.00 80.46  ? 325 THR E O   1 
ATOM   14131 C CB  . THR E 2 325 ? 10.603  -19.044 46.085  1.00 73.72  ? 325 THR E CB  1 
ATOM   14132 O OG1 . THR E 2 325 ? 10.735  -19.713 44.825  1.00 76.63  ? 325 THR E OG1 1 
ATOM   14133 C CG2 . THR E 2 325 ? 11.589  -17.893 46.146  1.00 71.75  ? 325 THR E CG2 1 
ATOM   14134 N N   . ILE E 2 326 ? 11.712  -19.210 49.338  1.00 73.37  ? 326 ILE E N   1 
ATOM   14135 C CA  . ILE E 2 326 ? 11.646  -18.709 50.706  1.00 71.51  ? 326 ILE E CA  1 
ATOM   14136 C C   . ILE E 2 326 ? 12.283  -17.326 50.747  1.00 69.71  ? 326 ILE E C   1 
ATOM   14137 O O   . ILE E 2 326 ? 13.457  -17.164 50.394  1.00 71.51  ? 326 ILE E O   1 
ATOM   14138 C CB  . ILE E 2 326 ? 12.335  -19.664 51.692  1.00 73.72  ? 326 ILE E CB  1 
ATOM   14139 C CG1 . ILE E 2 326 ? 11.813  -21.094 51.510  1.00 75.27  ? 326 ILE E CG1 1 
ATOM   14140 C CG2 . ILE E 2 326 ? 12.119  -19.195 53.126  1.00 75.20  ? 326 ILE E CG2 1 
ATOM   14141 C CD1 . ILE E 2 326 ? 10.328  -21.247 51.765  1.00 79.22  ? 326 ILE E CD1 1 
ATOM   14142 N N   . LEU E 2 327 ? 11.508  -16.332 51.171  1.00 68.89  ? 327 LEU E N   1 
ATOM   14143 C CA  . LEU E 2 327 ? 11.971  -14.956 51.270  1.00 73.22  ? 327 LEU E CA  1 
ATOM   14144 C C   . LEU E 2 327 ? 12.024  -14.529 52.730  1.00 75.69  ? 327 LEU E C   1 
ATOM   14145 O O   . LEU E 2 327 ? 11.146  -14.879 53.524  1.00 77.74  ? 327 LEU E O   1 
ATOM   14146 C CB  . LEU E 2 327 ? 11.063  -14.011 50.480  1.00 79.77  ? 327 LEU E CB  1 
ATOM   14147 C CG  . LEU E 2 327 ? 10.990  -14.278 48.975  1.00 80.06  ? 327 LEU E CG  1 
ATOM   14148 C CD1 . LEU E 2 327 ? 10.198  -13.185 48.280  1.00 86.30  ? 327 LEU E CD1 1 
ATOM   14149 C CD2 . LEU E 2 327 ? 12.386  -14.389 48.387  1.00 74.01  ? 327 LEU E CD2 1 
ATOM   14150 N N   . GLY E 2 328 ? 13.065  -13.780 53.079  1.00 80.26  ? 328 GLY E N   1 
ATOM   14151 C CA  . GLY E 2 328 ? 13.215  -13.245 54.413  1.00 81.85  ? 328 GLY E CA  1 
ATOM   14152 C C   . GLY E 2 328 ? 12.423  -11.965 54.598  1.00 84.89  ? 328 GLY E C   1 
ATOM   14153 O O   . GLY E 2 328 ? 11.642  -11.541 53.743  1.00 85.75  ? 328 GLY E O   1 
ATOM   14154 N N   . GLU E 2 329 ? 12.628  -11.347 55.756  1.00 88.20  ? 329 GLU E N   1 
ATOM   14155 C CA  . GLU E 2 329 ? 11.953  -10.095 56.058  1.00 93.06  ? 329 GLU E CA  1 
ATOM   14156 C C   . GLU E 2 329 ? 12.511  -8.965  55.203  1.00 92.43  ? 329 GLU E C   1 
ATOM   14157 O O   . GLU E 2 329 ? 13.727  -8.829  55.045  1.00 93.06  ? 329 GLU E O   1 
ATOM   14158 C CB  . GLU E 2 329 ? 12.116  -9.747  57.536  1.00 96.21  ? 329 GLU E CB  1 
ATOM   14159 C CG  . GLU E 2 329 ? 11.575  -8.378  57.904  1.00 98.02  ? 329 GLU E CG  1 
ATOM   14160 C CD  . GLU E 2 329 ? 11.869  -8.001  59.340  1.00 95.99  ? 329 GLU E CD  1 
ATOM   14161 O OE1 . GLU E 2 329 ? 12.384  -8.858  60.090  1.00 101.59 ? 329 GLU E OE1 1 
ATOM   14162 O OE2 . GLU E 2 329 ? 11.595  -6.843  59.717  1.00 96.15  ? 329 GLU E OE2 1 
ATOM   14163 N N   . ASP E 2 330 ? 11.610  -8.148  54.656  1.00 95.80  ? 330 ASP E N   1 
ATOM   14164 C CA  . ASP E 2 330 ? 11.985  -6.965  53.883  1.00 97.63  ? 330 ASP E CA  1 
ATOM   14165 C C   . ASP E 2 330 ? 12.886  -7.349  52.707  1.00 97.62  ? 330 ASP E C   1 
ATOM   14166 O O   . ASP E 2 330 ? 14.049  -6.953  52.614  1.00 100.94 ? 330 ASP E O   1 
ATOM   14167 C CB  . ASP E 2 330 ? 12.647  -5.917  54.789  1.00 97.49  ? 330 ASP E CB  1 
ATOM   14168 C CG  . ASP E 2 330 ? 13.023  -4.647  54.047  1.00 101.37 ? 330 ASP E CG  1 
ATOM   14169 O OD1 . ASP E 2 330 ? 12.112  -3.908  53.620  1.00 103.68 ? 330 ASP E OD1 1 
ATOM   14170 O OD2 . ASP E 2 330 ? 14.236  -4.388  53.900  1.00 101.78 ? 330 ASP E OD2 1 
ATOM   14171 N N   . VAL E 2 331 ? 12.323  -8.144  51.803  1.00 99.31  ? 331 VAL E N   1 
ATOM   14172 C CA  . VAL E 2 331 ? 13.003  -8.555  50.581  1.00 97.63  ? 331 VAL E CA  1 
ATOM   14173 C C   . VAL E 2 331 ? 12.256  -7.935  49.413  1.00 104.22 ? 331 VAL E C   1 
ATOM   14174 O O   . VAL E 2 331 ? 11.045  -8.133  49.264  1.00 102.65 ? 331 VAL E O   1 
ATOM   14175 C CB  . VAL E 2 331 ? 13.070  -10.084 50.448  1.00 92.37  ? 331 VAL E CB  1 
ATOM   14176 C CG1 . VAL E 2 331 ? 13.691  -10.471 49.117  1.00 95.79  ? 331 VAL E CG1 1 
ATOM   14177 C CG2 . VAL E 2 331 ? 13.867  -10.681 51.594  1.00 90.38  ? 331 VAL E CG2 1 
ATOM   14178 N N   . HIS E 2 332 ? 12.976  -7.191  48.584  1.00 121.00 ? 332 HIS E N   1 
ATOM   14179 C CA  . HIS E 2 332 ? 12.378  -6.420  47.501  1.00 118.48 ? 332 HIS E CA  1 
ATOM   14180 C C   . HIS E 2 332 ? 12.737  -7.097  46.185  1.00 115.56 ? 332 HIS E C   1 
ATOM   14181 O O   . HIS E 2 332 ? 13.868  -6.984  45.702  1.00 116.11 ? 332 HIS E O   1 
ATOM   14182 C CB  . HIS E 2 332 ? 12.860  -4.976  47.549  1.00 120.44 ? 332 HIS E CB  1 
ATOM   14183 C CG  . HIS E 2 332 ? 12.495  -4.268  48.815  1.00 123.18 ? 332 HIS E CG  1 
ATOM   14184 N ND1 . HIS E 2 332 ? 11.431  -3.397  48.905  1.00 123.73 ? 332 HIS E ND1 1 
ATOM   14185 C CD2 . HIS E 2 332 ? 13.045  -4.318  50.051  1.00 126.12 ? 332 HIS E CD2 1 
ATOM   14186 C CE1 . HIS E 2 332 ? 11.348  -2.933  50.139  1.00 126.98 ? 332 HIS E CE1 1 
ATOM   14187 N NE2 . HIS E 2 332 ? 12.315  -3.477  50.855  1.00 128.10 ? 332 HIS E NE2 1 
ATOM   14188 N N   . VAL E 2 333 ? 11.765  -7.798  45.612  1.00 97.29  ? 333 VAL E N   1 
ATOM   14189 C CA  . VAL E 2 333 ? 11.929  -8.462  44.326  1.00 94.32  ? 333 VAL E CA  1 
ATOM   14190 C C   . VAL E 2 333 ? 11.527  -7.489  43.228  1.00 92.26  ? 333 VAL E C   1 
ATOM   14191 O O   . VAL E 2 333 ? 10.414  -6.952  43.241  1.00 92.23  ? 333 VAL E O   1 
ATOM   14192 C CB  . VAL E 2 333 ? 11.096  -9.749  44.254  1.00 97.16  ? 333 VAL E CB  1 
ATOM   14193 C CG1 . VAL E 2 333 ? 11.297  -10.428 42.912  1.00 94.31  ? 333 VAL E CG1 1 
ATOM   14194 C CG2 . VAL E 2 333 ? 11.471  -10.682 45.395  1.00 101.20 ? 333 VAL E CG2 1 
ATOM   14195 N N   . SER E 2 334 ? 12.434  -7.256  42.283  1.00 84.03  ? 334 SER E N   1 
ATOM   14196 C CA  . SER E 2 334 ? 12.146  -6.357  41.179  1.00 75.20  ? 334 SER E CA  1 
ATOM   14197 C C   . SER E 2 334 ? 11.038  -6.930  40.299  1.00 70.84  ? 334 SER E C   1 
ATOM   14198 O O   . SER E 2 334 ? 10.569  -8.057  40.486  1.00 69.47  ? 334 SER E O   1 
ATOM   14199 C CB  . SER E 2 334 ? 13.404  -6.104  40.348  1.00 72.34  ? 334 SER E CB  1 
ATOM   14200 O OG  . SER E 2 334 ? 14.417  -5.505  41.132  1.00 76.99  ? 334 SER E OG  1 
ATOM   14201 N N   . ASP E 2 335 ? 10.614  -6.130  39.326  1.00 67.00  ? 335 ASP E N   1 
ATOM   14202 C CA  . ASP E 2 335 ? 9.599   -6.578  38.388  1.00 62.83  ? 335 ASP E CA  1 
ATOM   14203 C C   . ASP E 2 335 ? 10.167  -7.647  37.463  1.00 61.90  ? 335 ASP E C   1 
ATOM   14204 O O   . ASP E 2 335 ? 11.368  -7.683  37.183  1.00 61.62  ? 335 ASP E O   1 
ATOM   14205 C CB  . ASP E 2 335 ? 9.084   -5.406  37.553  1.00 62.60  ? 335 ASP E CB  1 
ATOM   14206 C CG  . ASP E 2 335 ? 8.602   -4.249  38.404  1.00 64.95  ? 335 ASP E CG  1 
ATOM   14207 O OD1 . ASP E 2 335 ? 8.207   -4.483  39.565  1.00 66.72  ? 335 ASP E OD1 1 
ATOM   14208 O OD2 . ASP E 2 335 ? 8.626   -3.103  37.908  1.00 65.88  ? 335 ASP E OD2 1 
ATOM   14209 N N   . GLU E 2 336 ? 9.282   -8.528  36.991  1.00 61.73  ? 336 GLU E N   1 
ATOM   14210 C CA  . GLU E 2 336 ? 9.607   -9.510  35.954  1.00 61.16  ? 336 GLU E CA  1 
ATOM   14211 C C   . GLU E 2 336 ? 10.710  -10.477 36.381  1.00 60.97  ? 336 GLU E C   1 
ATOM   14212 O O   . GLU E 2 336 ? 11.429  -11.020 35.538  1.00 63.55  ? 336 GLU E O   1 
ATOM   14213 C CB  . GLU E 2 336 ? 9.987   -8.817  34.642  1.00 67.92  ? 336 GLU E CB  1 
ATOM   14214 C CG  . GLU E 2 336 ? 9.077   -7.655  34.283  1.00 65.65  ? 336 GLU E CG  1 
ATOM   14215 C CD  . GLU E 2 336 ? 9.690   -6.730  33.255  1.00 70.38  ? 336 GLU E CD  1 
ATOM   14216 O OE1 . GLU E 2 336 ? 10.597  -7.172  32.519  1.00 71.32  ? 336 GLU E OE1 1 
ATOM   14217 O OE2 . GLU E 2 336 ? 9.270   -5.555  33.192  1.00 67.36  ? 336 GLU E OE2 1 
ATOM   14218 N N   . ILE E 2 337 ? 10.861  -10.704 37.683  1.00 63.55  ? 337 ILE E N   1 
ATOM   14219 C CA  . ILE E 2 337 ? 11.911  -11.571 38.208  1.00 62.62  ? 337 ILE E CA  1 
ATOM   14220 C C   . ILE E 2 337 ? 11.331  -12.955 38.464  1.00 61.28  ? 337 ILE E C   1 
ATOM   14221 O O   . ILE E 2 337 ? 10.220  -13.091 38.995  1.00 61.64  ? 337 ILE E O   1 
ATOM   14222 C CB  . ILE E 2 337 ? 12.537  -10.983 39.488  1.00 61.75  ? 337 ILE E CB  1 
ATOM   14223 C CG1 . ILE E 2 337 ? 13.160  -9.613  39.205  1.00 61.78  ? 337 ILE E CG1 1 
ATOM   14224 C CG2 . ILE E 2 337 ? 13.582  -11.933 40.058  1.00 61.74  ? 337 ILE E CG2 1 
ATOM   14225 C CD1 . ILE E 2 337 ? 14.356  -9.658  38.270  1.00 61.31  ? 337 ILE E CD1 1 
ATOM   14226 N N   . TYR E 2 338 ? 12.082  -13.986 38.081  1.00 60.94  ? 338 TYR E N   1 
ATOM   14227 C CA  . TYR E 2 338 ? 11.663  -15.375 38.218  1.00 60.94  ? 338 TYR E CA  1 
ATOM   14228 C C   . TYR E 2 338 ? 12.473  -16.074 39.303  1.00 61.21  ? 338 TYR E C   1 
ATOM   14229 O O   . TYR E 2 338 ? 13.698  -15.921 39.375  1.00 61.11  ? 338 TYR E O   1 
ATOM   14230 C CB  . TYR E 2 338 ? 11.816  -16.132 36.895  1.00 60.41  ? 338 TYR E CB  1 
ATOM   14231 C CG  . TYR E 2 338 ? 11.652  -17.629 37.034  1.00 61.09  ? 338 TYR E CG  1 
ATOM   14232 C CD1 . TYR E 2 338 ? 10.397  -18.200 37.199  1.00 66.10  ? 338 TYR E CD1 1 
ATOM   14233 C CD2 . TYR E 2 338 ? 12.753  -18.473 36.996  1.00 60.25  ? 338 TYR E CD2 1 
ATOM   14234 C CE1 . TYR E 2 338 ? 10.245  -19.572 37.329  1.00 68.62  ? 338 TYR E CE1 1 
ATOM   14235 C CE2 . TYR E 2 338 ? 12.611  -19.843 37.123  1.00 64.88  ? 338 TYR E CE2 1 
ATOM   14236 C CZ  . TYR E 2 338 ? 11.356  -20.387 37.290  1.00 67.93  ? 338 TYR E CZ  1 
ATOM   14237 O OH  . TYR E 2 338 ? 11.216  -21.750 37.415  1.00 72.27  ? 338 TYR E OH  1 
ATOM   14238 N N   . SER E 2 339 ? 11.778  -16.842 40.143  1.00 63.13  ? 339 SER E N   1 
ATOM   14239 C CA  . SER E 2 339 ? 12.398  -17.567 41.246  1.00 61.98  ? 339 SER E CA  1 
ATOM   14240 C C   . SER E 2 339 ? 11.982  -19.029 41.197  1.00 86.30  ? 339 SER E C   1 
ATOM   14241 O O   . SER E 2 339 ? 10.785  -19.337 41.219  1.00 63.78  ? 339 SER E O   1 
ATOM   14242 C CB  . SER E 2 339 ? 12.004  -16.956 42.593  1.00 66.65  ? 339 SER E CB  1 
ATOM   14243 O OG  . SER E 2 339 ? 12.553  -15.660 42.743  1.00 69.53  ? 339 SER E OG  1 
ATOM   14244 N N   . ASN E 2 340 ? 12.969  -19.922 41.136  1.00 62.24  ? 340 ASN E N   1 
ATOM   14245 C CA  . ASN E 2 340 ? 12.714  -21.357 41.145  1.00 69.27  ? 340 ASN E CA  1 
ATOM   14246 C C   . ASN E 2 340 ? 13.349  -21.995 42.375  1.00 69.39  ? 340 ASN E C   1 
ATOM   14247 O O   . ASN E 2 340 ? 14.232  -22.850 42.250  1.00 70.17  ? 340 ASN E O   1 
ATOM   14248 C CB  . ASN E 2 340 ? 13.251  -22.009 39.870  1.00 65.87  ? 340 ASN E CB  1 
ATOM   14249 C CG  . ASN E 2 340 ? 12.752  -23.423 39.687  1.00 68.83  ? 340 ASN E CG  1 
ATOM   14250 O OD1 . ASN E 2 340 ? 11.644  -23.760 40.104  1.00 73.39  ? 340 ASN E OD1 1 
ATOM   14251 N ND2 . ASN E 2 340 ? 13.573  -24.265 39.070  1.00 69.33  ? 340 ASN E ND2 1 
ATOM   14252 N N   . GLY E 2 341 ? 12.914  -21.589 43.564  1.00 69.16  ? 341 GLY E N   1 
ATOM   14253 C CA  . GLY E 2 341 ? 13.439  -22.158 44.789  1.00 70.25  ? 341 GLY E CA  1 
ATOM   14254 C C   . GLY E 2 341 ? 14.579  -21.367 45.397  1.00 69.85  ? 341 GLY E C   1 
ATOM   14255 O O   . GLY E 2 341 ? 15.558  -21.948 45.877  1.00 71.68  ? 341 GLY E O   1 
ATOM   14256 N N   . GLY E 2 342 ? 14.458  -20.042 45.394  1.00 68.34  ? 342 GLY E N   1 
ATOM   14257 C CA  . GLY E 2 342 ? 15.497  -19.188 45.939  1.00 69.94  ? 342 GLY E CA  1 
ATOM   14258 C C   . GLY E 2 342 ? 15.290  -18.838 47.398  1.00 73.23  ? 342 GLY E C   1 
ATOM   14259 O O   . GLY E 2 342 ? 14.376  -18.081 47.737  1.00 74.98  ? 342 GLY E O   1 
ATOM   14260 N N   . VAL E 2 343 ? 16.132  -19.383 48.273  1.00 69.67  ? 343 VAL E N   1 
ATOM   14261 C CA  . VAL E 2 343 ? 16.070  -19.094 49.702  1.00 68.75  ? 343 VAL E CA  1 
ATOM   14262 C C   . VAL E 2 343 ? 16.896  -17.834 49.944  1.00 72.40  ? 343 VAL E C   1 
ATOM   14263 O O   . VAL E 2 343 ? 18.128  -17.879 49.990  1.00 71.32  ? 343 VAL E O   1 
ATOM   14264 C CB  . VAL E 2 343 ? 16.563  -20.272 50.541  1.00 68.13  ? 343 VAL E CB  1 
ATOM   14265 C CG1 . VAL E 2 343 ? 16.300  -20.013 52.015  1.00 78.66  ? 343 VAL E CG1 1 
ATOM   14266 C CG2 . VAL E 2 343 ? 15.886  -21.556 50.090  1.00 72.56  ? 343 VAL E CG2 1 
ATOM   14267 N N   . VAL E 2 344 ? 16.214  -16.703 50.084  1.00 72.79  ? 344 VAL E N   1 
ATOM   14268 C CA  . VAL E 2 344 ? 16.859  -15.396 50.147  1.00 72.25  ? 344 VAL E CA  1 
ATOM   14269 C C   . VAL E 2 344 ? 16.924  -14.935 51.595  1.00 75.47  ? 344 VAL E C   1 
ATOM   14270 O O   . VAL E 2 344 ? 16.026  -15.204 52.402  1.00 76.10  ? 344 VAL E O   1 
ATOM   14271 C CB  . VAL E 2 344 ? 16.119  -14.370 49.263  1.00 75.30  ? 344 VAL E CB  1 
ATOM   14272 C CG1 . VAL E 2 344 ? 16.880  -13.056 49.209  1.00 79.49  ? 344 VAL E CG1 1 
ATOM   14273 C CG2 . VAL E 2 344 ? 15.921  -14.930 47.861  1.00 73.09  ? 344 VAL E CG2 1 
ATOM   14274 N N   . LEU E 2 345 ? 18.007  -14.239 51.930  1.00 77.06  ? 345 LEU E N   1 
ATOM   14275 C CA  . LEU E 2 345 ? 18.168  -13.653 53.248  1.00 79.95  ? 345 LEU E CA  1 
ATOM   14276 C C   . LEU E 2 345 ? 17.344  -12.376 53.370  1.00 81.07  ? 345 LEU E C   1 
ATOM   14277 O O   . LEU E 2 345 ? 17.020  -11.734 52.367  1.00 88.48  ? 345 LEU E O   1 
ATOM   14278 C CB  . LEU E 2 345 ? 19.639  -13.342 53.514  1.00 82.07  ? 345 LEU E CB  1 
ATOM   14279 C CG  . LEU E 2 345 ? 20.488  -14.386 54.249  1.00 77.83  ? 345 LEU E CG  1 
ATOM   14280 C CD1 . LEU E 2 345 ? 20.591  -15.692 53.474  1.00 77.49  ? 345 LEU E CD1 1 
ATOM   14281 C CD2 . LEU E 2 345 ? 21.868  -13.827 54.572  1.00 79.76  ? 345 LEU E CD2 1 
ATOM   14282 N N   . PRO E 2 346 ? 16.985  -11.988 54.592  1.00 82.62  ? 346 PRO E N   1 
ATOM   14283 C CA  . PRO E 2 346 ? 16.238  -10.742 54.774  1.00 84.69  ? 346 PRO E CA  1 
ATOM   14284 C C   . PRO E 2 346 ? 17.082  -9.537  54.394  1.00 87.62  ? 346 PRO E C   1 
ATOM   14285 O O   . PRO E 2 346 ? 18.314  -9.581  54.384  1.00 86.73  ? 346 PRO E O   1 
ATOM   14286 C CB  . PRO E 2 346 ? 15.907  -10.740 56.271  1.00 88.84  ? 346 PRO E CB  1 
ATOM   14287 C CG  . PRO E 2 346 ? 16.929  -11.634 56.885  1.00 88.31  ? 346 PRO E CG  1 
ATOM   14288 C CD  . PRO E 2 346 ? 17.179  -12.701 55.865  1.00 84.53  ? 346 PRO E CD  1 
ATOM   14289 N N   . HIS E 2 347 ? 16.386  -8.441  54.087  1.00 88.89  ? 347 HIS E N   1 
ATOM   14290 C CA  . HIS E 2 347 ? 17.012  -7.184  53.679  1.00 90.70  ? 347 HIS E CA  1 
ATOM   14291 C C   . HIS E 2 347 ? 17.921  -7.401  52.467  1.00 94.18  ? 347 HIS E C   1 
ATOM   14292 O O   . HIS E 2 347 ? 19.126  -7.137  52.493  1.00 94.37  ? 347 HIS E O   1 
ATOM   14293 C CB  . HIS E 2 347 ? 17.767  -6.540  54.846  1.00 94.64  ? 347 HIS E CB  1 
ATOM   14294 C CG  . HIS E 2 347 ? 16.927  -6.347  56.071  1.00 98.17  ? 347 HIS E CG  1 
ATOM   14295 N ND1 . HIS E 2 347 ? 15.853  -5.482  56.107  1.00 98.66  ? 347 HIS E ND1 1 
ATOM   14296 C CD2 . HIS E 2 347 ? 17.000  -6.908  57.301  1.00 96.81  ? 347 HIS E CD2 1 
ATOM   14297 C CE1 . HIS E 2 347 ? 15.302  -5.518  57.306  1.00 95.76  ? 347 HIS E CE1 1 
ATOM   14298 N NE2 . HIS E 2 347 ? 15.979  -6.375  58.050  1.00 96.50  ? 347 HIS E NE2 1 
ATOM   14299 N N   . LYS E 2 348 ? 17.308  -7.895  51.393  1.00 99.65  ? 348 LYS E N   1 
ATOM   14300 C CA  . LYS E 2 348 ? 18.007  -8.198  50.152  1.00 105.87 ? 348 LYS E CA  1 
ATOM   14301 C C   . LYS E 2 348 ? 17.133  -7.774  48.985  1.00 115.78 ? 348 LYS E C   1 
ATOM   14302 O O   . LYS E 2 348 ? 15.934  -8.065  48.968  1.00 113.96 ? 348 LYS E O   1 
ATOM   14303 C CB  . LYS E 2 348 ? 18.338  -9.692  50.048  1.00 99.65  ? 348 LYS E CB  1 
ATOM   14304 C CG  . LYS E 2 348 ? 19.240  -10.045 48.876  1.00 105.57 ? 348 LYS E CG  1 
ATOM   14305 C CD  . LYS E 2 348 ? 20.607  -9.396  49.013  1.00 106.43 ? 348 LYS E CD  1 
ATOM   14306 C CE  . LYS E 2 348 ? 21.512  -9.764  47.849  1.00 103.24 ? 348 LYS E CE  1 
ATOM   14307 N NZ  . LYS E 2 348 ? 22.883  -9.204  48.013  1.00 101.18 ? 348 LYS E NZ  1 
ATOM   14308 N N   . GLU E 2 349 ? 17.734  -7.093  48.015  1.00 156.53 ? 349 GLU E N   1 
ATOM   14309 C CA  . GLU E 2 349 ? 17.046  -6.675  46.801  1.00 153.82 ? 349 GLU E CA  1 
ATOM   14310 C C   . GLU E 2 349 ? 17.395  -7.649  45.684  1.00 150.83 ? 349 GLU E C   1 
ATOM   14311 O O   . GLU E 2 349 ? 18.569  -7.791  45.324  1.00 150.17 ? 349 GLU E O   1 
ATOM   14312 C CB  . GLU E 2 349 ? 17.427  -5.247  46.414  1.00 154.04 ? 349 GLU E CB  1 
ATOM   14313 C CG  . GLU E 2 349 ? 16.971  -4.192  47.407  1.00 157.05 ? 349 GLU E CG  1 
ATOM   14314 C CD  . GLU E 2 349 ? 17.257  -2.783  46.930  1.00 162.38 ? 349 GLU E CD  1 
ATOM   14315 O OE1 . GLU E 2 349 ? 18.172  -2.613  46.097  1.00 165.17 ? 349 GLU E OE1 1 
ATOM   14316 O OE2 . GLU E 2 349 ? 16.571  -1.847  47.391  1.00 165.50 ? 349 GLU E OE2 1 
ATOM   14317 N N   . ILE E 2 350 ? 16.381  -8.313  45.142  1.00 114.75 ? 350 ILE E N   1 
ATOM   14318 C CA  . ILE E 2 350 ? 16.563  -9.309  44.095  1.00 103.86 ? 350 ILE E CA  1 
ATOM   14319 C C   . ILE E 2 350 ? 16.334  -8.624  42.755  1.00 91.66  ? 350 ILE E C   1 
ATOM   14320 O O   . ILE E 2 350 ? 15.206  -8.242  42.423  1.00 89.42  ? 350 ILE E O   1 
ATOM   14321 C CB  . ILE E 2 350 ? 15.619  -10.503 44.281  1.00 96.63  ? 350 ILE E CB  1 
ATOM   14322 C CG1 . ILE E 2 350 ? 15.827  -11.134 45.658  1.00 98.99  ? 350 ILE E CG1 1 
ATOM   14323 C CG2 . ILE E 2 350 ? 15.840  -11.532 43.184  1.00 88.37  ? 350 ILE E CG2 1 
ATOM   14324 C CD1 . ILE E 2 350 ? 17.251  -11.573 45.911  1.00 102.37 ? 350 ILE E CD1 1 
ATOM   14325 N N   . LYS E 2 351 ? 17.409  -8.469  41.981  1.00 89.70  ? 351 LYS E N   1 
ATOM   14326 C CA  . LYS E 2 351 ? 17.340  -7.874  40.653  1.00 81.44  ? 351 LYS E CA  1 
ATOM   14327 C C   . LYS E 2 351 ? 17.712  -8.864  39.557  1.00 72.89  ? 351 LYS E C   1 
ATOM   14328 O O   . LYS E 2 351 ? 17.804  -8.474  38.387  1.00 65.30  ? 351 LYS E O   1 
ATOM   14329 C CB  . LYS E 2 351 ? 18.232  -6.631  40.581  1.00 85.57  ? 351 LYS E CB  1 
ATOM   14330 C CG  . LYS E 2 351 ? 17.843  -5.547  41.575  1.00 88.70  ? 351 LYS E CG  1 
ATOM   14331 C CD  . LYS E 2 351 ? 18.603  -4.255  41.325  1.00 85.97  ? 351 LYS E CD  1 
ATOM   14332 C CE  . LYS E 2 351 ? 18.118  -3.149  42.249  1.00 93.74  ? 351 LYS E CE  1 
ATOM   14333 N NZ  . LYS E 2 351 ? 18.770  -1.841  41.960  1.00 95.31  ? 351 LYS E NZ  1 
ATOM   14334 N N   . SER E 2 352 ? 17.938  -10.128 39.906  1.00 72.27  ? 352 SER E N   1 
ATOM   14335 C CA  . SER E 2 352 ? 18.251  -11.168 38.942  1.00 68.37  ? 352 SER E CA  1 
ATOM   14336 C C   . SER E 2 352 ? 17.330  -12.354 39.186  1.00 61.10  ? 352 SER E C   1 
ATOM   14337 O O   . SER E 2 352 ? 16.812  -12.545 40.287  1.00 62.35  ? 352 SER E O   1 
ATOM   14338 C CB  . SER E 2 352 ? 19.719  -11.609 39.038  1.00 78.67  ? 352 SER E CB  1 
ATOM   14339 O OG  . SER E 2 352 ? 20.597  -10.515 38.845  1.00 84.60  ? 352 SER E OG  1 
ATOM   14340 N N   . ASN E 2 353 ? 17.137  -13.160 38.146  1.00 60.64  ? 353 ASN E N   1 
ATOM   14341 C CA  . ASN E 2 353 ? 16.263  -14.319 38.254  1.00 60.60  ? 353 ASN E CA  1 
ATOM   14342 C C   . ASN E 2 353 ? 16.949  -15.442 39.017  1.00 60.78  ? 353 ASN E C   1 
ATOM   14343 O O   . ASN E 2 353 ? 18.129  -15.731 38.803  1.00 60.65  ? 353 ASN E O   1 
ATOM   14344 C CB  . ASN E 2 353 ? 15.837  -14.816 36.872  1.00 60.10  ? 353 ASN E CB  1 
ATOM   14345 C CG  . ASN E 2 353 ? 15.075  -13.770 36.088  1.00 59.98  ? 353 ASN E CG  1 
ATOM   14346 O OD1 . ASN E 2 353 ? 14.450  -12.883 36.666  1.00 60.31  ? 353 ASN E OD1 1 
ATOM   14347 N ND2 . ASN E 2 353 ? 15.099  -13.885 34.766  1.00 59.57  ? 353 ASN E ND2 1 
ATOM   14348 N N   . ILE E 2 354 ? 16.196  -16.074 39.916  1.00 61.13  ? 354 ILE E N   1 
ATOM   14349 C CA  . ILE E 2 354 ? 16.665  -17.274 40.597  1.00 66.80  ? 354 ILE E CA  1 
ATOM   14350 C C   . ILE E 2 354 ? 16.091  -18.474 39.859  1.00 61.50  ? 354 ILE E C   1 
ATOM   14351 O O   . ILE E 2 354 ? 15.181  -19.153 40.350  1.00 75.09  ? 354 ILE E O   1 
ATOM   14352 C CB  . ILE E 2 354 ? 16.269  -17.284 42.082  1.00 62.36  ? 354 ILE E CB  1 
ATOM   14353 C CG1 . ILE E 2 354 ? 16.640  -15.953 42.735  1.00 63.58  ? 354 ILE E CG1 1 
ATOM   14354 C CG2 . ILE E 2 354 ? 16.970  -18.425 42.800  1.00 62.85  ? 354 ILE E CG2 1 
ATOM   14355 C CD1 . ILE E 2 354 ? 16.293  -15.882 44.198  1.00 71.65  ? 354 ILE E CD1 1 
ATOM   14356 N N   . LEU E 2 355 ? 16.617  -18.724 38.661  1.00 62.16  ? 355 LEU E N   1 
ATOM   14357 C CA  . LEU E 2 355 ? 16.073  -19.725 37.754  1.00 65.01  ? 355 LEU E CA  1 
ATOM   14358 C C   . LEU E 2 355 ? 16.239  -21.156 38.254  1.00 67.99  ? 355 LEU E C   1 
ATOM   14359 O O   . LEU E 2 355 ? 15.613  -22.062 37.693  1.00 71.09  ? 355 LEU E O   1 
ATOM   14360 C CB  . LEU E 2 355 ? 16.733  -19.562 36.385  1.00 64.22  ? 355 LEU E CB  1 
ATOM   14361 C CG  . LEU E 2 355 ? 18.130  -18.931 36.434  1.00 65.15  ? 355 LEU E CG  1 
ATOM   14362 C CD1 . LEU E 2 355 ? 19.182  -19.942 36.875  1.00 70.10  ? 355 LEU E CD1 1 
ATOM   14363 C CD2 . LEU E 2 355 ? 18.501  -18.304 35.098  1.00 70.37  ? 355 LEU E CD2 1 
ATOM   14364 N N   . LYS E 2 356 ? 17.051  -21.381 39.279  1.00 69.08  ? 356 LYS E N   1 
ATOM   14365 C CA  . LYS E 2 356 ? 17.267  -22.696 39.860  1.00 68.83  ? 356 LYS E CA  1 
ATOM   14366 C C   . LYS E 2 356 ? 17.448  -22.532 41.361  1.00 68.98  ? 356 LYS E C   1 
ATOM   14367 O O   . LYS E 2 356 ? 17.795  -21.443 41.831  1.00 68.01  ? 356 LYS E O   1 
ATOM   14368 C CB  . LYS E 2 356 ? 18.489  -23.387 39.240  1.00 70.81  ? 356 LYS E CB  1 
ATOM   14369 C CG  . LYS E 2 356 ? 18.255  -23.880 37.817  1.00 77.34  ? 356 LYS E CG  1 
ATOM   14370 C CD  . LYS E 2 356 ? 19.516  -24.466 37.207  1.00 92.10  ? 356 LYS E CD  1 
ATOM   14371 C CE  . LYS E 2 356 ? 19.992  -25.681 37.984  1.00 100.63 ? 356 LYS E CE  1 
ATOM   14372 N NZ  . LYS E 2 356 ? 18.982  -26.780 37.989  1.00 98.21  ? 356 LYS E NZ  1 
ATOM   14373 N N   . PRO E 2 357 ? 17.201  -23.587 42.140  1.00 68.15  ? 357 PRO E N   1 
ATOM   14374 C CA  . PRO E 2 357 ? 17.345  -23.473 43.599  1.00 69.81  ? 357 PRO E CA  1 
ATOM   14375 C C   . PRO E 2 357 ? 18.737  -22.996 43.997  1.00 70.78  ? 357 PRO E C   1 
ATOM   14376 O O   . PRO E 2 357 ? 19.751  -23.569 43.591  1.00 73.16  ? 357 PRO E O   1 
ATOM   14377 C CB  . PRO E 2 357 ? 17.066  -24.897 44.092  1.00 71.23  ? 357 PRO E CB  1 
ATOM   14378 C CG  . PRO E 2 357 ? 16.164  -25.473 43.050  1.00 67.83  ? 357 PRO E CG  1 
ATOM   14379 C CD  . PRO E 2 357 ? 16.634  -24.890 41.745  1.00 68.81  ? 357 PRO E CD  1 
ATOM   14380 N N   . GLU E 2 358 ? 18.773  -21.939 44.806  1.00 69.62  ? 358 GLU E N   1 
ATOM   14381 C CA  . GLU E 2 358 ? 20.016  -21.266 45.153  1.00 67.07  ? 358 GLU E CA  1 
ATOM   14382 C C   . GLU E 2 358 ? 19.776  -20.423 46.397  1.00 68.32  ? 358 GLU E C   1 
ATOM   14383 O O   . GLU E 2 358 ? 18.699  -19.843 46.558  1.00 70.41  ? 358 GLU E O   1 
ATOM   14384 C CB  . GLU E 2 358 ? 20.512  -20.393 43.993  1.00 70.66  ? 358 GLU E CB  1 
ATOM   14385 C CG  . GLU E 2 358 ? 21.754  -19.565 44.290  1.00 69.68  ? 358 GLU E CG  1 
ATOM   14386 C CD  . GLU E 2 358 ? 22.100  -18.623 43.151  1.00 74.42  ? 358 GLU E CD  1 
ATOM   14387 O OE1 . GLU E 2 358 ? 21.543  -18.798 42.045  1.00 76.29  ? 358 GLU E OE1 1 
ATOM   14388 O OE2 . GLU E 2 358 ? 22.921  -17.707 43.361  1.00 78.58  ? 358 GLU E OE2 1 
ATOM   14389 N N   . ILE E 2 359 ? 20.776  -20.362 47.271  1.00 68.93  ? 359 ILE E N   1 
ATOM   14390 C CA  . ILE E 2 359 ? 20.699  -19.575 48.497  1.00 71.68  ? 359 ILE E CA  1 
ATOM   14391 C C   . ILE E 2 359 ? 21.357  -18.224 48.249  1.00 72.36  ? 359 ILE E C   1 
ATOM   14392 O O   . ILE E 2 359 ? 22.561  -18.149 47.972  1.00 75.20  ? 359 ILE E O   1 
ATOM   14393 C CB  . ILE E 2 359 ? 21.358  -20.303 49.679  1.00 74.09  ? 359 ILE E CB  1 
ATOM   14394 C CG1 . ILE E 2 359 ? 20.604  -21.595 50.000  1.00 72.79  ? 359 ILE E CG1 1 
ATOM   14395 C CG2 . ILE E 2 359 ? 21.399  -19.398 50.899  1.00 80.06  ? 359 ILE E CG2 1 
ATOM   14396 C CD1 . ILE E 2 359 ? 21.240  -22.425 51.097  1.00 75.40  ? 359 ILE E CD1 1 
ATOM   14397 N N   . VAL E 2 360 ? 20.566  -17.159 48.344  1.00 75.16  ? 360 VAL E N   1 
ATOM   14398 C CA  . VAL E 2 360 ? 21.028  -15.795 48.118  1.00 73.51  ? 360 VAL E CA  1 
ATOM   14399 C C   . VAL E 2 360 ? 21.140  -15.101 49.468  1.00 76.96  ? 360 VAL E C   1 
ATOM   14400 O O   . VAL E 2 360 ? 20.271  -15.264 50.333  1.00 77.50  ? 360 VAL E O   1 
ATOM   14401 C CB  . VAL E 2 360 ? 20.079  -15.028 47.175  1.00 73.53  ? 360 VAL E CB  1 
ATOM   14402 C CG1 . VAL E 2 360 ? 20.623  -13.638 46.881  1.00 80.55  ? 360 VAL E CG1 1 
ATOM   14403 C CG2 . VAL E 2 360 ? 19.861  -15.808 45.889  1.00 70.87  ? 360 VAL E CG2 1 
ATOM   14404 N N   . MET E 2 361 ? 22.201  -14.318 49.645  1.00 78.39  ? 361 MET E N   1 
ATOM   14405 C CA  . MET E 2 361 ? 22.420  -13.607 50.901  1.00 84.69  ? 361 MET E CA  1 
ATOM   14406 C C   . MET E 2 361 ? 22.340  -12.098 50.720  1.00 89.90  ? 361 MET E C   1 
ATOM   14407 O O   . MET E 2 361 ? 21.571  -11.419 51.405  1.00 91.03  ? 361 MET E O   1 
ATOM   14408 C CB  . MET E 2 361 ? 23.782  -13.967 51.501  1.00 89.36  ? 361 MET E CB  1 
ATOM   14409 C CG  . MET E 2 361 ? 24.241  -15.394 51.271  1.00 88.38  ? 361 MET E CG  1 
ATOM   14410 S SD  . MET E 2 361 ? 25.810  -15.701 52.114  1.00 81.16  ? 361 MET E SD  1 
ATOM   14411 C CE  . MET E 2 361 ? 25.383  -15.227 53.788  1.00 88.22  ? 361 MET E CE  1 
ATOM   14412 O OXT . MET E 2 361 ? 23.043  -11.527 49.888  1.00 93.55  ? 361 MET E OXT 1 
ATOM   14413 N N   . MET F 2 1   ? 40.119  21.663  60.486  1.00 175.74 ? 1   MET F N   1 
ATOM   14414 C CA  . MET F 2 1   ? 39.930  20.972  59.217  1.00 175.22 ? 1   MET F CA  1 
ATOM   14415 C C   . MET F 2 1   ? 38.894  19.860  59.371  1.00 172.87 ? 1   MET F C   1 
ATOM   14416 O O   . MET F 2 1   ? 38.845  19.184  60.400  1.00 168.49 ? 1   MET F O   1 
ATOM   14417 C CB  . MET F 2 1   ? 41.263  20.412  58.714  1.00 173.09 ? 1   MET F CB  1 
ATOM   14418 C CG  . MET F 2 1   ? 41.229  19.869  57.296  1.00 173.55 ? 1   MET F CG  1 
ATOM   14419 S SD  . MET F 2 1   ? 42.876  19.464  56.681  1.00 178.53 ? 1   MET F SD  1 
ATOM   14420 C CE  . MET F 2 1   ? 43.656  21.077  56.704  1.00 178.04 ? 1   MET F CE  1 
ATOM   14421 N N   . LYS F 2 2   ? 38.071  19.675  58.344  1.00 176.99 ? 2   LYS F N   1 
ATOM   14422 C CA  . LYS F 2 2   ? 36.968  18.724  58.356  1.00 180.29 ? 2   LYS F CA  1 
ATOM   14423 C C   . LYS F 2 2   ? 37.254  17.569  57.400  1.00 179.30 ? 2   LYS F C   1 
ATOM   14424 O O   . LYS F 2 2   ? 38.252  17.559  56.673  1.00 176.76 ? 2   LYS F O   1 
ATOM   14425 C CB  . LYS F 2 2   ? 35.656  19.423  57.993  1.00 182.70 ? 2   LYS F CB  1 
ATOM   14426 C CG  . LYS F 2 2   ? 35.247  20.532  58.949  1.00 186.46 ? 2   LYS F CG  1 
ATOM   14427 C CD  . LYS F 2 2   ? 34.804  19.975  60.292  1.00 188.30 ? 2   LYS F CD  1 
ATOM   14428 C CE  . LYS F 2 2   ? 34.270  21.077  61.193  1.00 188.47 ? 2   LYS F CE  1 
ATOM   14429 N NZ  . LYS F 2 2   ? 33.668  20.537  62.443  1.00 182.18 ? 2   LYS F NZ  1 
ATOM   14430 N N   . ALA F 2 3   ? 36.351  16.590  57.403  1.00 175.67 ? 3   ALA F N   1 
ATOM   14431 C CA  . ALA F 2 3   ? 36.476  15.417  56.550  1.00 171.51 ? 3   ALA F CA  1 
ATOM   14432 C C   . ALA F 2 3   ? 35.140  14.688  56.501  1.00 177.89 ? 3   ALA F C   1 
ATOM   14433 O O   . ALA F 2 3   ? 34.325  14.794  57.421  1.00 188.27 ? 3   ALA F O   1 
ATOM   14434 C CB  . ALA F 2 3   ? 37.581  14.476  57.043  1.00 168.07 ? 3   ALA F CB  1 
ATOM   14435 N N   . LEU F 2 4   ? 34.927  13.953  55.411  1.00 173.70 ? 4   LEU F N   1 
ATOM   14436 C CA  . LEU F 2 4   ? 33.716  13.172  55.200  1.00 176.49 ? 4   LEU F CA  1 
ATOM   14437 C C   . LEU F 2 4   ? 34.081  11.823  54.596  1.00 169.88 ? 4   LEU F C   1 
ATOM   14438 O O   . LEU F 2 4   ? 34.944  11.743  53.718  1.00 166.32 ? 4   LEU F O   1 
ATOM   14439 C CB  . LEU F 2 4   ? 32.727  13.908  54.282  1.00 173.69 ? 4   LEU F CB  1 
ATOM   14440 C CG  . LEU F 2 4   ? 31.485  13.127  53.849  1.00 170.64 ? 4   LEU F CG  1 
ATOM   14441 C CD1 . LEU F 2 4   ? 30.605  12.817  55.045  1.00 182.52 ? 4   LEU F CD1 1 
ATOM   14442 C CD2 . LEU F 2 4   ? 30.708  13.902  52.806  1.00 182.01 ? 4   LEU F CD2 1 
ATOM   14443 N N   . ILE F 2 5   ? 33.428  10.766  55.072  1.00 165.99 ? 5   ILE F N   1 
ATOM   14444 C CA  . ILE F 2 5   ? 33.688  9.405   54.616  1.00 150.24 ? 5   ILE F CA  1 
ATOM   14445 C C   . ILE F 2 5   ? 32.390  8.819   54.077  1.00 147.28 ? 5   ILE F C   1 
ATOM   14446 O O   . ILE F 2 5   ? 31.377  8.778   54.787  1.00 152.28 ? 5   ILE F O   1 
ATOM   14447 C CB  . ILE F 2 5   ? 34.261  8.529   55.740  1.00 144.23 ? 5   ILE F CB  1 
ATOM   14448 C CG1 . ILE F 2 5   ? 35.606  9.086   56.213  1.00 148.93 ? 5   ILE F CG1 1 
ATOM   14449 C CG2 . ILE F 2 5   ? 34.412  7.091   55.271  1.00 142.49 ? 5   ILE F CG2 1 
ATOM   14450 C CD1 . ILE F 2 5   ? 36.248  8.274   57.309  1.00 144.70 ? 5   ILE F CD1 1 
ATOM   14451 N N   . LEU F 2 6   ? 32.421  8.371   52.823  1.00 140.23 ? 6   LEU F N   1 
ATOM   14452 C CA  . LEU F 2 6   ? 31.276  7.712   52.203  1.00 135.24 ? 6   LEU F CA  1 
ATOM   14453 C C   . LEU F 2 6   ? 31.296  6.234   52.577  1.00 142.04 ? 6   LEU F C   1 
ATOM   14454 O O   . LEU F 2 6   ? 32.213  5.500   52.189  1.00 143.03 ? 6   LEU F O   1 
ATOM   14455 C CB  . LEU F 2 6   ? 31.313  7.902   50.690  1.00 124.10 ? 6   LEU F CB  1 
ATOM   14456 C CG  . LEU F 2 6   ? 31.191  9.353   50.220  1.00 127.62 ? 6   LEU F CG  1 
ATOM   14457 C CD1 . LEU F 2 6   ? 31.379  9.441   48.718  1.00 129.68 ? 6   LEU F CD1 1 
ATOM   14458 C CD2 . LEU F 2 6   ? 29.850  9.934   50.632  1.00 139.98 ? 6   LEU F CD2 1 
ATOM   14459 N N   . VAL F 2 7   ? 30.287  5.792   53.329  1.00 155.64 ? 7   VAL F N   1 
ATOM   14460 C CA  . VAL F 2 7   ? 30.185  4.393   53.735  1.00 157.01 ? 7   VAL F CA  1 
ATOM   14461 C C   . VAL F 2 7   ? 29.234  3.646   52.810  1.00 153.32 ? 7   VAL F C   1 
ATOM   14462 O O   . VAL F 2 7   ? 29.603  2.640   52.199  1.00 151.72 ? 7   VAL F O   1 
ATOM   14463 C CB  . VAL F 2 7   ? 29.716  4.270   55.196  1.00 159.97 ? 7   VAL F CB  1 
ATOM   14464 C CG1 . VAL F 2 7   ? 29.622  2.807   55.604  1.00 155.67 ? 7   VAL F CG1 1 
ATOM   14465 C CG2 . VAL F 2 7   ? 30.651  5.033   56.123  1.00 165.06 ? 7   VAL F CG2 1 
ATOM   14466 N N   . GLY F 2 8   ? 28.005  4.138   52.694  1.00 148.97 ? 8   GLY F N   1 
ATOM   14467 C CA  . GLY F 2 8   ? 26.995  3.461   51.906  1.00 155.10 ? 8   GLY F CA  1 
ATOM   14468 C C   . GLY F 2 8   ? 25.983  2.746   52.779  1.00 160.36 ? 8   GLY F C   1 
ATOM   14469 O O   . GLY F 2 8   ? 25.416  3.349   53.693  1.00 158.27 ? 8   GLY F O   1 
ATOM   14470 N N   . GLY F 2 9   ? 25.750  1.467   52.515  1.00 173.73 ? 9   GLY F N   1 
ATOM   14471 C CA  . GLY F 2 9   ? 24.818  0.669   53.272  1.00 175.05 ? 9   GLY F CA  1 
ATOM   14472 C C   . GLY F 2 9   ? 25.475  -0.127  54.380  1.00 175.89 ? 9   GLY F C   1 
ATOM   14473 O O   . GLY F 2 9   ? 26.509  0.263   54.937  1.00 176.22 ? 9   GLY F O   1 
ATOM   14474 N N   . PHE F 2 10  ? 24.866  -1.270  54.700  1.00 153.42 ? 10  PHE F N   1 
ATOM   14475 C CA  . PHE F 2 10  ? 25.318  -2.142  55.777  1.00 144.90 ? 10  PHE F CA  1 
ATOM   14476 C C   . PHE F 2 10  ? 26.385  -3.135  55.332  1.00 140.04 ? 10  PHE F C   1 
ATOM   14477 O O   . PHE F 2 10  ? 27.030  -3.752  56.187  1.00 133.90 ? 10  PHE F O   1 
ATOM   14478 C CB  . PHE F 2 10  ? 24.124  -2.905  56.366  1.00 144.89 ? 10  PHE F CB  1 
ATOM   14479 C CG  . PHE F 2 10  ? 24.209  -3.129  57.851  1.00 140.71 ? 10  PHE F CG  1 
ATOM   14480 C CD1 . PHE F 2 10  ? 23.866  -2.124  58.740  1.00 143.51 ? 10  PHE F CD1 1 
ATOM   14481 C CD2 . PHE F 2 10  ? 24.602  -4.356  58.356  1.00 134.22 ? 10  PHE F CD2 1 
ATOM   14482 C CE1 . PHE F 2 10  ? 23.933  -2.335  60.106  1.00 141.02 ? 10  PHE F CE1 1 
ATOM   14483 C CE2 . PHE F 2 10  ? 24.668  -4.574  59.720  1.00 133.94 ? 10  PHE F CE2 1 
ATOM   14484 C CZ  . PHE F 2 10  ? 24.336  -3.562  60.595  1.00 134.99 ? 10  PHE F CZ  1 
ATOM   14485 N N   . GLY F 2 11  ? 26.589  -3.299  54.027  1.00 147.78 ? 11  GLY F N   1 
ATOM   14486 C CA  . GLY F 2 11  ? 27.505  -4.302  53.522  1.00 144.53 ? 11  GLY F CA  1 
ATOM   14487 C C   . GLY F 2 11  ? 26.821  -5.592  53.117  1.00 141.72 ? 11  GLY F C   1 
ATOM   14488 O O   . GLY F 2 11  ? 27.178  -6.670  53.600  1.00 141.46 ? 11  GLY F O   1 
ATOM   14489 N N   . THR F 2 12  ? 25.832  -5.489  52.225  1.00 130.43 ? 12  THR F N   1 
ATOM   14490 C CA  . THR F 2 12  ? 25.073  -6.669  51.816  1.00 121.56 ? 12  THR F CA  1 
ATOM   14491 C C   . THR F 2 12  ? 25.963  -7.684  51.109  1.00 114.73 ? 12  THR F C   1 
ATOM   14492 O O   . THR F 2 12  ? 25.775  -8.898  51.259  1.00 109.99 ? 12  THR F O   1 
ATOM   14493 C CB  . THR F 2 12  ? 23.913  -6.260  50.909  1.00 122.93 ? 12  THR F CB  1 
ATOM   14494 O OG1 . THR F 2 12  ? 24.425  -5.599  49.745  1.00 130.25 ? 12  THR F OG1 1 
ATOM   14495 C CG2 . THR F 2 12  ? 22.974  -5.317  51.644  1.00 122.20 ? 12  THR F CG2 1 
ATOM   14496 N N   . ARG F 2 13  ? 26.936  -7.209  50.338  1.00 119.37 ? 13  ARG F N   1 
ATOM   14497 C CA  . ARG F 2 13  ? 27.842  -8.082  49.608  1.00 120.77 ? 13  ARG F CA  1 
ATOM   14498 C C   . ARG F 2 13  ? 28.983  -8.600  50.470  1.00 116.87 ? 13  ARG F C   1 
ATOM   14499 O O   . ARG F 2 13  ? 29.886  -9.263  49.949  1.00 115.96 ? 13  ARG F O   1 
ATOM   14500 C CB  . ARG F 2 13  ? 28.404  -7.348  48.390  1.00 126.86 ? 13  ARG F CB  1 
ATOM   14501 C CG  . ARG F 2 13  ? 28.653  -5.867  48.618  1.00 131.72 ? 13  ARG F CG  1 
ATOM   14502 C CD  . ARG F 2 13  ? 28.686  -5.130  47.295  1.00 139.09 ? 13  ARG F CD  1 
ATOM   14503 N NE  . ARG F 2 13  ? 27.468  -5.367  46.529  1.00 144.11 ? 13  ARG F NE  1 
ATOM   14504 C CZ  . ARG F 2 13  ? 27.431  -6.032  45.379  1.00 146.98 ? 13  ARG F CZ  1 
ATOM   14505 N NH1 . ARG F 2 13  ? 28.548  -6.526  44.863  1.00 147.72 ? 13  ARG F NH1 1 
ATOM   14506 N NH2 . ARG F 2 13  ? 26.278  -6.202  44.746  1.00 146.00 ? 13  ARG F NH2 1 
ATOM   14507 N N   . LEU F 2 14  ? 28.963  -8.315  51.770  1.00 118.06 ? 14  LEU F N   1 
ATOM   14508 C CA  . LEU F 2 14  ? 29.989  -8.790  52.686  1.00 117.51 ? 14  LEU F CA  1 
ATOM   14509 C C   . LEU F 2 14  ? 29.422  -9.746  53.728  1.00 114.91 ? 14  LEU F C   1 
ATOM   14510 O O   . LEU F 2 14  ? 30.105  -10.052 54.711  1.00 119.25 ? 14  LEU F O   1 
ATOM   14511 C CB  . LEU F 2 14  ? 30.697  -7.609  53.363  1.00 120.89 ? 14  LEU F CB  1 
ATOM   14512 C CG  . LEU F 2 14  ? 31.621  -6.724  52.512  1.00 125.09 ? 14  LEU F CG  1 
ATOM   14513 C CD1 . LEU F 2 14  ? 30.843  -5.759  51.625  1.00 127.45 ? 14  LEU F CD1 1 
ATOM   14514 C CD2 . LEU F 2 14  ? 32.596  -5.960  53.395  1.00 136.35 ? 14  LEU F CD2 1 
ATOM   14515 N N   . ARG F 2 15  ? 28.187  -10.219 53.541  1.00 108.61 ? 15  ARG F N   1 
ATOM   14516 C CA  . ARG F 2 15  ? 27.608  -11.198 54.442  1.00 107.25 ? 15  ARG F CA  1 
ATOM   14517 C C   . ARG F 2 15  ? 28.404  -12.501 54.367  1.00 107.16 ? 15  ARG F C   1 
ATOM   14518 O O   . ARG F 2 15  ? 29.057  -12.779 53.359  1.00 109.38 ? 15  ARG F O   1 
ATOM   14519 C CB  . ARG F 2 15  ? 26.142  -11.450 54.086  1.00 102.45 ? 15  ARG F CB  1 
ATOM   14520 C CG  . ARG F 2 15  ? 25.202  -10.281 54.344  1.00 101.61 ? 15  ARG F CG  1 
ATOM   14521 C CD  . ARG F 2 15  ? 23.757  -10.747 54.223  1.00 95.99  ? 15  ARG F CD  1 
ATOM   14522 N NE  . ARG F 2 15  ? 22.783  -9.728  54.606  1.00 92.19  ? 15  ARG F NE  1 
ATOM   14523 C CZ  . ARG F 2 15  ? 22.116  -8.964  53.748  1.00 94.20  ? 15  ARG F CZ  1 
ATOM   14524 N NH1 . ARG F 2 15  ? 22.311  -9.097  52.443  1.00 98.46  ? 15  ARG F NH1 1 
ATOM   14525 N NH2 . ARG F 2 15  ? 21.247  -8.068  54.195  1.00 92.22  ? 15  ARG F NH2 1 
ATOM   14526 N N   . PRO F 2 16  ? 28.365  -13.328 55.428  1.00 107.11 ? 16  PRO F N   1 
ATOM   14527 C CA  . PRO F 2 16  ? 27.610  -13.178 56.678  1.00 110.52 ? 16  PRO F CA  1 
ATOM   14528 C C   . PRO F 2 16  ? 28.314  -12.339 57.742  1.00 118.02 ? 16  PRO F C   1 
ATOM   14529 O O   . PRO F 2 16  ? 27.838  -12.280 58.877  1.00 118.41 ? 16  PRO F O   1 
ATOM   14530 C CB  . PRO F 2 16  ? 27.457  -14.621 57.153  1.00 111.04 ? 16  PRO F CB  1 
ATOM   14531 C CG  . PRO F 2 16  ? 28.711  -15.274 56.693  1.00 115.93 ? 16  PRO F CG  1 
ATOM   14532 C CD  . PRO F 2 16  ? 29.066  -14.624 55.375  1.00 110.96 ? 16  PRO F CD  1 
ATOM   14533 N N   . LEU F 2 17  ? 29.431  -11.700 57.385  1.00 133.12 ? 17  LEU F N   1 
ATOM   14534 C CA  . LEU F 2 17  ? 30.152  -10.889 58.362  1.00 134.02 ? 17  LEU F CA  1 
ATOM   14535 C C   . LEU F 2 17  ? 29.405  -9.602  58.686  1.00 136.05 ? 17  LEU F C   1 
ATOM   14536 O O   . LEU F 2 17  ? 29.564  -9.054  59.783  1.00 137.91 ? 17  LEU F O   1 
ATOM   14537 C CB  . LEU F 2 17  ? 31.560  -10.576 57.856  1.00 134.92 ? 17  LEU F CB  1 
ATOM   14538 C CG  . LEU F 2 17  ? 32.448  -11.789 57.568  1.00 139.55 ? 17  LEU F CG  1 
ATOM   14539 C CD1 . LEU F 2 17  ? 33.816  -11.358 57.057  1.00 153.68 ? 17  LEU F CD1 1 
ATOM   14540 C CD2 . LEU F 2 17  ? 32.581  -12.659 58.809  1.00 149.32 ? 17  LEU F CD2 1 
ATOM   14541 N N   . THR F 2 18  ? 28.591  -9.107  57.756  1.00 121.25 ? 18  THR F N   1 
ATOM   14542 C CA  . THR F 2 18  ? 27.823  -7.888  57.965  1.00 120.54 ? 18  THR F CA  1 
ATOM   14543 C C   . THR F 2 18  ? 26.379  -8.168  58.355  1.00 119.41 ? 18  THR F C   1 
ATOM   14544 O O   . THR F 2 18  ? 25.550  -7.254  58.320  1.00 121.55 ? 18  THR F O   1 
ATOM   14545 C CB  . THR F 2 18  ? 27.865  -7.012  56.714  1.00 120.71 ? 18  THR F CB  1 
ATOM   14546 O OG1 . THR F 2 18  ? 27.479  -7.788  55.573  1.00 118.16 ? 18  THR F OG1 1 
ATOM   14547 C CG2 . THR F 2 18  ? 29.264  -6.459  56.503  1.00 121.63 ? 18  THR F CG2 1 
ATOM   14548 N N   . LEU F 2 19  ? 26.058  -9.411  58.718  1.00 116.57 ? 19  LEU F N   1 
ATOM   14549 C CA  . LEU F 2 19  ? 24.716  -9.711  59.200  1.00 116.95 ? 19  LEU F CA  1 
ATOM   14550 C C   . LEU F 2 19  ? 24.469  -9.129  60.586  1.00 125.28 ? 19  LEU F C   1 
ATOM   14551 O O   . LEU F 2 19  ? 23.323  -8.822  60.933  1.00 126.19 ? 19  LEU F O   1 
ATOM   14552 C CB  . LEU F 2 19  ? 24.492  -11.222 59.207  1.00 111.64 ? 19  LEU F CB  1 
ATOM   14553 C CG  . LEU F 2 19  ? 23.906  -11.807 57.923  1.00 104.67 ? 19  LEU F CG  1 
ATOM   14554 C CD1 . LEU F 2 19  ? 23.739  -13.309 58.050  1.00 103.51 ? 19  LEU F CD1 1 
ATOM   14555 C CD2 . LEU F 2 19  ? 22.573  -11.145 57.615  1.00 100.69 ? 19  LEU F CD2 1 
ATOM   14556 N N   . SER F 2 20  ? 25.521  -8.965  61.388  1.00 132.55 ? 20  SER F N   1 
ATOM   14557 C CA  . SER F 2 20  ? 25.403  -8.406  62.728  1.00 135.97 ? 20  SER F CA  1 
ATOM   14558 C C   . SER F 2 20  ? 26.075  -7.043  62.831  1.00 133.45 ? 20  SER F C   1 
ATOM   14559 O O   . SER F 2 20  ? 25.407  -6.039  63.098  1.00 134.89 ? 20  SER F O   1 
ATOM   14560 C CB  . SER F 2 20  ? 25.993  -9.377  63.759  1.00 142.23 ? 20  SER F CB  1 
ATOM   14561 O OG  . SER F 2 20  ? 25.323  -10.626 63.722  1.00 145.37 ? 20  SER F OG  1 
ATOM   14562 N N   . PHE F 2 21  ? 27.387  -6.983  62.624  1.00 141.03 ? 21  PHE F N   1 
ATOM   14563 C CA  . PHE F 2 21  ? 28.073  -5.699  62.651  1.00 141.24 ? 21  PHE F CA  1 
ATOM   14564 C C   . PHE F 2 21  ? 28.046  -5.073  61.260  1.00 140.20 ? 21  PHE F C   1 
ATOM   14565 O O   . PHE F 2 21  ? 28.197  -5.781  60.261  1.00 138.75 ? 21  PHE F O   1 
ATOM   14566 C CB  . PHE F 2 21  ? 29.522  -5.866  63.105  1.00 140.18 ? 21  PHE F CB  1 
ATOM   14567 C CG  . PHE F 2 21  ? 29.667  -6.287  64.541  1.00 144.48 ? 21  PHE F CG  1 
ATOM   14568 C CD1 . PHE F 2 21  ? 28.701  -5.956  65.476  1.00 148.16 ? 21  PHE F CD1 1 
ATOM   14569 C CD2 . PHE F 2 21  ? 30.771  -7.017  64.957  1.00 140.54 ? 21  PHE F CD2 1 
ATOM   14570 C CE1 . PHE F 2 21  ? 28.830  -6.345  66.797  1.00 146.48 ? 21  PHE F CE1 1 
ATOM   14571 C CE2 . PHE F 2 21  ? 30.906  -7.409  66.277  1.00 140.62 ? 21  PHE F CE2 1 
ATOM   14572 C CZ  . PHE F 2 21  ? 29.934  -7.072  67.198  1.00 142.35 ? 21  PHE F CZ  1 
ATOM   14573 N N   . PRO F 2 22  ? 27.863  -3.761  61.158  1.00 135.16 ? 22  PRO F N   1 
ATOM   14574 C CA  . PRO F 2 22  ? 27.798  -3.129  59.836  1.00 134.34 ? 22  PRO F CA  1 
ATOM   14575 C C   . PRO F 2 22  ? 29.150  -3.175  59.142  1.00 130.09 ? 22  PRO F C   1 
ATOM   14576 O O   . PRO F 2 22  ? 30.164  -3.583  59.709  1.00 128.04 ? 22  PRO F O   1 
ATOM   14577 C CB  . PRO F 2 22  ? 27.363  -1.691  60.133  1.00 138.63 ? 22  PRO F CB  1 
ATOM   14578 C CG  . PRO F 2 22  ? 27.588  -1.480  61.597  1.00 139.10 ? 22  PRO F CG  1 
ATOM   14579 C CD  . PRO F 2 22  ? 27.941  -2.781  62.253  1.00 138.43 ? 22  PRO F CD  1 
ATOM   14580 N N   . LYS F 2 23  ? 29.142  -2.756  57.878  1.00 130.88 ? 23  LYS F N   1 
ATOM   14581 C CA  . LYS F 2 23  ? 30.344  -2.814  57.047  1.00 127.83 ? 23  LYS F CA  1 
ATOM   14582 C C   . LYS F 2 23  ? 31.561  -2.142  57.679  1.00 127.25 ? 23  LYS F C   1 
ATOM   14583 O O   . LYS F 2 23  ? 32.638  -2.759  57.683  1.00 125.67 ? 23  LYS F O   1 
ATOM   14584 C CB  . LYS F 2 23  ? 30.037  -2.219  55.664  1.00 130.27 ? 23  LYS F CB  1 
ATOM   14585 C CG  . LYS F 2 23  ? 31.247  -2.152  54.739  1.00 130.96 ? 23  LYS F CG  1 
ATOM   14586 C CD  . LYS F 2 23  ? 30.862  -1.765  53.316  1.00 132.69 ? 23  LYS F CD  1 
ATOM   14587 C CE  . LYS F 2 23  ? 30.117  -0.442  53.263  1.00 138.91 ? 23  LYS F CE  1 
ATOM   14588 N NZ  . LYS F 2 23  ? 29.803  -0.053  51.859  1.00 138.11 ? 23  LYS F NZ  1 
ATOM   14589 N N   . PRO F 2 24  ? 31.484  -0.916  58.213  1.00 129.33 ? 24  PRO F N   1 
ATOM   14590 C CA  . PRO F 2 24  ? 32.702  -0.276  58.732  1.00 125.93 ? 24  PRO F CA  1 
ATOM   14591 C C   . PRO F 2 24  ? 33.178  -0.803  60.078  1.00 123.19 ? 24  PRO F C   1 
ATOM   14592 O O   . PRO F 2 24  ? 34.278  -0.429  60.506  1.00 121.61 ? 24  PRO F O   1 
ATOM   14593 C CB  . PRO F 2 24  ? 32.294  1.198   58.841  1.00 126.96 ? 24  PRO F CB  1 
ATOM   14594 C CG  . PRO F 2 24  ? 30.845  1.149   59.118  1.00 127.21 ? 24  PRO F CG  1 
ATOM   14595 C CD  . PRO F 2 24  ? 30.321  -0.013  58.317  1.00 130.21 ? 24  PRO F CD  1 
ATOM   14596 N N   . LEU F 2 25  ? 32.413  -1.657  60.755  1.00 125.56 ? 25  LEU F N   1 
ATOM   14597 C CA  . LEU F 2 25  ? 32.798  -2.168  62.065  1.00 122.48 ? 25  LEU F CA  1 
ATOM   14598 C C   . LEU F 2 25  ? 33.459  -3.538  61.993  1.00 122.49 ? 25  LEU F C   1 
ATOM   14599 O O   . LEU F 2 25  ? 33.738  -4.136  63.038  1.00 120.63 ? 25  LEU F O   1 
ATOM   14600 C CB  . LEU F 2 25  ? 31.586  -2.222  62.997  1.00 123.29 ? 25  LEU F CB  1 
ATOM   14601 C CG  . LEU F 2 25  ? 31.082  -0.875  63.508  1.00 123.58 ? 25  LEU F CG  1 
ATOM   14602 C CD1 . LEU F 2 25  ? 30.068  -1.083  64.615  1.00 126.31 ? 25  LEU F CD1 1 
ATOM   14603 C CD2 . LEU F 2 25  ? 32.243  -0.023  64.000  1.00 124.01 ? 25  LEU F CD2 1 
ATOM   14604 N N   . VAL F 2 26  ? 33.716  -4.045  60.792  1.00 124.25 ? 26  VAL F N   1 
ATOM   14605 C CA  . VAL F 2 26  ? 34.385  -5.330  60.626  1.00 124.91 ? 26  VAL F CA  1 
ATOM   14606 C C   . VAL F 2 26  ? 35.882  -5.150  60.845  1.00 124.26 ? 26  VAL F C   1 
ATOM   14607 O O   . VAL F 2 26  ? 36.515  -4.288  60.224  1.00 122.28 ? 26  VAL F O   1 
ATOM   14608 C CB  . VAL F 2 26  ? 34.096  -5.920  59.238  1.00 132.93 ? 26  VAL F CB  1 
ATOM   14609 C CG1 . VAL F 2 26  ? 34.898  -7.193  59.027  1.00 138.71 ? 26  VAL F CG1 1 
ATOM   14610 C CG2 . VAL F 2 26  ? 32.607  -6.190  59.079  1.00 132.00 ? 26  VAL F CG2 1 
ATOM   14611 N N   . ASP F 2 27  ? 36.448  -5.957  61.740  1.00 132.22 ? 27  ASP F N   1 
ATOM   14612 C CA  . ASP F 2 27  ? 37.879  -5.905  62.014  1.00 127.06 ? 27  ASP F CA  1 
ATOM   14613 C C   . ASP F 2 27  ? 38.663  -6.385  60.797  1.00 125.94 ? 27  ASP F C   1 
ATOM   14614 O O   . ASP F 2 27  ? 38.545  -7.546  60.393  1.00 129.44 ? 27  ASP F O   1 
ATOM   14615 C CB  . ASP F 2 27  ? 38.211  -6.759  63.238  1.00 125.67 ? 27  ASP F CB  1 
ATOM   14616 C CG  . ASP F 2 27  ? 37.718  -6.142  64.537  1.00 126.95 ? 27  ASP F CG  1 
ATOM   14617 O OD1 . ASP F 2 27  ? 36.895  -5.203  64.483  1.00 129.97 ? 27  ASP F OD1 1 
ATOM   14618 O OD2 . ASP F 2 27  ? 38.146  -6.603  65.617  1.00 123.22 ? 27  ASP F OD2 1 
ATOM   14619 N N   . PHE F 2 28  ? 39.463  -5.497  60.214  1.00 121.47 ? 28  PHE F N   1 
ATOM   14620 C CA  . PHE F 2 28  ? 40.373  -5.846  59.130  1.00 123.78 ? 28  PHE F CA  1 
ATOM   14621 C C   . PHE F 2 28  ? 41.803  -5.708  59.631  1.00 125.63 ? 28  PHE F C   1 
ATOM   14622 O O   . PHE F 2 28  ? 42.239  -4.603  59.969  1.00 126.24 ? 28  PHE F O   1 
ATOM   14623 C CB  . PHE F 2 28  ? 40.149  -4.961  57.904  1.00 128.63 ? 28  PHE F CB  1 
ATOM   14624 C CG  . PHE F 2 28  ? 41.193  -5.138  56.838  1.00 131.85 ? 28  PHE F CG  1 
ATOM   14625 C CD1 . PHE F 2 28  ? 42.146  -4.158  56.611  1.00 128.94 ? 28  PHE F CD1 1 
ATOM   14626 C CD2 . PHE F 2 28  ? 41.234  -6.294  56.078  1.00 143.05 ? 28  PHE F CD2 1 
ATOM   14627 C CE1 . PHE F 2 28  ? 43.112  -4.322  55.637  1.00 134.81 ? 28  PHE F CE1 1 
ATOM   14628 C CE2 . PHE F 2 28  ? 42.198  -6.466  55.104  1.00 153.34 ? 28  PHE F CE2 1 
ATOM   14629 C CZ  . PHE F 2 28  ? 43.139  -5.478  54.883  1.00 143.00 ? 28  PHE F CZ  1 
ATOM   14630 N N   . ALA F 2 29  ? 42.527  -6.825  59.663  1.00 124.76 ? 29  ALA F N   1 
ATOM   14631 C CA  . ALA F 2 29  ? 43.875  -6.877  60.224  1.00 123.65 ? 29  ALA F CA  1 
ATOM   14632 C C   . ALA F 2 29  ? 43.887  -6.279  61.632  1.00 124.06 ? 29  ALA F C   1 
ATOM   14633 O O   . ALA F 2 29  ? 44.515  -5.251  61.897  1.00 125.56 ? 29  ALA F O   1 
ATOM   14634 C CB  . ALA F 2 29  ? 44.885  -6.178  59.308  1.00 127.62 ? 29  ALA F CB  1 
ATOM   14635 N N   . ASN F 2 30  ? 43.127  -6.932  62.518  1.00 126.77 ? 30  ASN F N   1 
ATOM   14636 C CA  . ASN F 2 30  ? 42.989  -6.596  63.936  1.00 126.00 ? 30  ASN F CA  1 
ATOM   14637 C C   . ASN F 2 30  ? 42.068  -5.402  64.168  1.00 130.43 ? 30  ASN F C   1 
ATOM   14638 O O   . ASN F 2 30  ? 41.202  -5.447  65.049  1.00 132.96 ? 30  ASN F O   1 
ATOM   14639 C CB  . ASN F 2 30  ? 44.356  -6.328  64.571  1.00 127.66 ? 30  ASN F CB  1 
ATOM   14640 C CG  . ASN F 2 30  ? 45.156  -7.592  64.785  1.00 127.98 ? 30  ASN F CG  1 
ATOM   14641 O OD1 . ASN F 2 30  ? 45.217  -8.113  65.895  1.00 127.64 ? 30  ASN F OD1 1 
ATOM   14642 N ND2 . ASN F 2 30  ? 45.762  -8.102  63.719  1.00 126.04 ? 30  ASN F ND2 1 
ATOM   14643 N N   . LYS F 2 31  ? 42.240  -4.329  63.385  1.00 127.77 ? 31  LYS F N   1 
ATOM   14644 C CA  . LYS F 2 31  ? 41.509  -3.088  63.594  1.00 125.32 ? 31  LYS F CA  1 
ATOM   14645 C C   . LYS F 2 31  ? 40.268  -3.016  62.710  1.00 124.75 ? 31  LYS F C   1 
ATOM   14646 O O   . LYS F 2 31  ? 40.254  -3.554  61.599  1.00 125.36 ? 31  LYS F O   1 
ATOM   14647 C CB  . LYS F 2 31  ? 42.408  -1.882  63.313  1.00 122.60 ? 31  LYS F CB  1 
ATOM   14648 C CG  . LYS F 2 31  ? 43.466  -1.662  64.380  1.00 129.20 ? 31  LYS F CG  1 
ATOM   14649 C CD  . LYS F 2 31  ? 44.675  -0.924  63.836  1.00 134.68 ? 31  LYS F CD  1 
ATOM   14650 C CE  . LYS F 2 31  ? 45.859  -1.050  64.783  1.00 140.27 ? 31  LYS F CE  1 
ATOM   14651 N NZ  . LYS F 2 31  ? 47.164  -0.916  64.081  1.00 140.57 ? 31  LYS F NZ  1 
ATOM   14652 N N   . PRO F 2 32  ? 39.204  -2.373  63.196  1.00 122.95 ? 32  PRO F N   1 
ATOM   14653 C CA  . PRO F 2 32  ? 38.022  -2.166  62.352  1.00 121.11 ? 32  PRO F CA  1 
ATOM   14654 C C   . PRO F 2 32  ? 38.374  -1.395  61.090  1.00 122.32 ? 32  PRO F C   1 
ATOM   14655 O O   . PRO F 2 32  ? 39.341  -0.630  61.049  1.00 126.05 ? 32  PRO F O   1 
ATOM   14656 C CB  . PRO F 2 32  ? 37.078  -1.362  63.253  1.00 122.07 ? 32  PRO F CB  1 
ATOM   14657 C CG  . PRO F 2 32  ? 37.504  -1.704  64.641  1.00 121.99 ? 32  PRO F CG  1 
ATOM   14658 C CD  . PRO F 2 32  ? 38.995  -1.886  64.570  1.00 124.12 ? 32  PRO F CD  1 
ATOM   14659 N N   . MET F 2 33  ? 37.568  -1.608  60.047  1.00 120.99 ? 33  MET F N   1 
ATOM   14660 C CA  . MET F 2 33  ? 37.856  -1.003  58.752  1.00 121.74 ? 33  MET F CA  1 
ATOM   14661 C C   . MET F 2 33  ? 37.778  0.518   58.805  1.00 125.06 ? 33  MET F C   1 
ATOM   14662 O O   . MET F 2 33  ? 38.426  1.200   58.002  1.00 127.86 ? 33  MET F O   1 
ATOM   14663 C CB  . MET F 2 33  ? 36.894  -1.547  57.695  1.00 121.45 ? 33  MET F CB  1 
ATOM   14664 C CG  . MET F 2 33  ? 37.489  -2.621  56.795  1.00 126.74 ? 33  MET F CG  1 
ATOM   14665 S SD  . MET F 2 33  ? 39.017  -2.098  55.999  1.00 116.02 ? 33  MET F SD  1 
ATOM   14666 C CE  . MET F 2 33  ? 38.442  -0.709  55.027  1.00 127.87 ? 33  MET F CE  1 
ATOM   14667 N N   . ILE F 2 34  ? 36.988  1.068   59.729  1.00 125.71 ? 34  ILE F N   1 
ATOM   14668 C CA  . ILE F 2 34  ? 36.825  2.517   59.798  1.00 125.49 ? 34  ILE F CA  1 
ATOM   14669 C C   . ILE F 2 34  ? 38.055  3.190   60.404  1.00 132.49 ? 34  ILE F C   1 
ATOM   14670 O O   . ILE F 2 34  ? 38.349  4.349   60.090  1.00 137.36 ? 34  ILE F O   1 
ATOM   14671 C CB  . ILE F 2 34  ? 35.543  2.872   60.575  1.00 124.41 ? 34  ILE F CB  1 
ATOM   14672 C CG1 . ILE F 2 34  ? 35.175  4.342   60.362  1.00 128.36 ? 34  ILE F CG1 1 
ATOM   14673 C CG2 . ILE F 2 34  ? 35.693  2.559   62.060  1.00 128.37 ? 34  ILE F CG2 1 
ATOM   14674 C CD1 . ILE F 2 34  ? 34.780  4.674   58.943  1.00 130.08 ? 34  ILE F CD1 1 
ATOM   14675 N N   . LEU F 2 35  ? 38.799  2.489   61.260  1.00 133.12 ? 35  LEU F N   1 
ATOM   14676 C CA  . LEU F 2 35  ? 39.950  3.088   61.922  1.00 137.43 ? 35  LEU F CA  1 
ATOM   14677 C C   . LEU F 2 35  ? 41.168  3.207   61.014  1.00 143.93 ? 35  LEU F C   1 
ATOM   14678 O O   . LEU F 2 35  ? 42.142  3.865   61.396  1.00 152.31 ? 35  LEU F O   1 
ATOM   14679 C CB  . LEU F 2 35  ? 40.312  2.283   63.173  1.00 131.84 ? 35  LEU F CB  1 
ATOM   14680 C CG  . LEU F 2 35  ? 39.236  2.257   64.260  1.00 135.91 ? 35  LEU F CG  1 
ATOM   14681 C CD1 . LEU F 2 35  ? 39.771  1.640   65.544  1.00 134.68 ? 35  LEU F CD1 1 
ATOM   14682 C CD2 . LEU F 2 35  ? 38.699  3.657   64.517  1.00 147.33 ? 35  LEU F CD2 1 
ATOM   14683 N N   . HIS F 2 36  ? 41.141  2.588   59.831  1.00 142.84 ? 36  HIS F N   1 
ATOM   14684 C CA  . HIS F 2 36  ? 42.294  2.649   58.938  1.00 143.91 ? 36  HIS F CA  1 
ATOM   14685 C C   . HIS F 2 36  ? 42.439  4.026   58.303  1.00 152.92 ? 36  HIS F C   1 
ATOM   14686 O O   . HIS F 2 36  ? 43.552  4.424   57.940  1.00 155.65 ? 36  HIS F O   1 
ATOM   14687 C CB  . HIS F 2 36  ? 42.189  1.566   57.863  1.00 144.86 ? 36  HIS F CB  1 
ATOM   14688 C CG  . HIS F 2 36  ? 42.327  0.173   58.395  1.00 142.35 ? 36  HIS F CG  1 
ATOM   14689 N ND1 . HIS F 2 36  ? 41.277  -0.513  58.964  1.00 142.60 ? 36  HIS F ND1 1 
ATOM   14690 C CD2 . HIS F 2 36  ? 43.390  -0.666  58.436  1.00 141.00 ? 36  HIS F CD2 1 
ATOM   14691 C CE1 . HIS F 2 36  ? 41.687  -1.712  59.339  1.00 140.28 ? 36  HIS F CE1 1 
ATOM   14692 N NE2 . HIS F 2 36  ? 42.965  -1.830  59.029  1.00 138.88 ? 36  HIS F NE2 1 
ATOM   14693 N N   . GLN F 2 37  ? 41.337  4.762   58.155  1.00 155.19 ? 37  GLN F N   1 
ATOM   14694 C CA  . GLN F 2 37  ? 41.377  6.094   57.572  1.00 159.83 ? 37  GLN F CA  1 
ATOM   14695 C C   . GLN F 2 37  ? 41.076  7.199   58.572  1.00 167.71 ? 37  GLN F C   1 
ATOM   14696 O O   . GLN F 2 37  ? 41.307  8.372   58.258  1.00 171.72 ? 37  GLN F O   1 
ATOM   14697 C CB  . GLN F 2 37  ? 40.382  6.199   56.403  1.00 154.20 ? 37  GLN F CB  1 
ATOM   14698 C CG  . GLN F 2 37  ? 40.642  5.241   55.251  1.00 151.79 ? 37  GLN F CG  1 
ATOM   14699 C CD  . GLN F 2 37  ? 39.965  3.897   55.433  1.00 143.85 ? 37  GLN F CD  1 
ATOM   14700 O OE1 . GLN F 2 37  ? 39.203  3.691   56.378  1.00 137.98 ? 37  GLN F OE1 1 
ATOM   14701 N NE2 . GLN F 2 37  ? 40.238  2.972   54.520  1.00 143.73 ? 37  GLN F NE2 1 
ATOM   14702 N N   . ILE F 2 38  ? 40.583  6.866   59.766  1.00 178.09 ? 38  ILE F N   1 
ATOM   14703 C CA  . ILE F 2 38  ? 40.402  7.886   60.794  1.00 181.71 ? 38  ILE F CA  1 
ATOM   14704 C C   . ILE F 2 38  ? 41.748  8.297   61.376  1.00 186.25 ? 38  ILE F C   1 
ATOM   14705 O O   . ILE F 2 38  ? 42.025  9.490   61.554  1.00 187.98 ? 38  ILE F O   1 
ATOM   14706 C CB  . ILE F 2 38  ? 39.437  7.383   61.883  1.00 181.42 ? 38  ILE F CB  1 
ATOM   14707 C CG1 . ILE F 2 38  ? 38.003  7.369   61.352  1.00 183.42 ? 38  ILE F CG1 1 
ATOM   14708 C CG2 . ILE F 2 38  ? 39.527  8.262   63.121  1.00 184.27 ? 38  ILE F CG2 1 
ATOM   14709 C CD1 . ILE F 2 38  ? 36.969  6.978   62.385  1.00 185.08 ? 38  ILE F CD1 1 
ATOM   14710 N N   . GLU F 2 39  ? 42.609  7.319   61.672  1.00 201.12 ? 39  GLU F N   1 
ATOM   14711 C CA  . GLU F 2 39  ? 43.953  7.629   62.145  1.00 200.92 ? 39  GLU F CA  1 
ATOM   14712 C C   . GLU F 2 39  ? 44.776  8.326   61.069  1.00 201.34 ? 39  GLU F C   1 
ATOM   14713 O O   . GLU F 2 39  ? 45.649  9.141   61.389  1.00 203.38 ? 39  GLU F O   1 
ATOM   14714 C CB  . GLU F 2 39  ? 44.645  6.345   62.614  1.00 199.77 ? 39  GLU F CB  1 
ATOM   14715 C CG  . GLU F 2 39  ? 45.931  6.558   63.403  1.00 207.26 ? 39  GLU F CG  1 
ATOM   14716 C CD  . GLU F 2 39  ? 47.159  6.686   62.520  1.00 209.71 ? 39  GLU F CD  1 
ATOM   14717 O OE1 . GLU F 2 39  ? 47.072  6.357   61.318  1.00 213.97 ? 39  GLU F OE1 1 
ATOM   14718 O OE2 . GLU F 2 39  ? 48.214  7.116   63.030  1.00 208.55 ? 39  GLU F OE2 1 
ATOM   14719 N N   . ALA F 2 40  ? 44.512  8.027   59.795  1.00 188.64 ? 40  ALA F N   1 
ATOM   14720 C CA  . ALA F 2 40  ? 45.186  8.747   58.721  1.00 183.24 ? 40  ALA F CA  1 
ATOM   14721 C C   . ALA F 2 40  ? 44.712  10.192  58.636  1.00 181.31 ? 40  ALA F C   1 
ATOM   14722 O O   . ALA F 2 40  ? 45.487  11.075  58.252  1.00 182.97 ? 40  ALA F O   1 
ATOM   14723 C CB  . ALA F 2 40  ? 44.969  8.033   57.387  1.00 170.83 ? 40  ALA F CB  1 
ATOM   14724 N N   . LEU F 2 41  ? 43.450  10.453  58.989  1.00 180.59 ? 41  LEU F N   1 
ATOM   14725 C CA  . LEU F 2 41  ? 42.965  11.826  59.056  1.00 179.06 ? 41  LEU F CA  1 
ATOM   14726 C C   . LEU F 2 41  ? 43.514  12.573  60.263  1.00 180.57 ? 41  LEU F C   1 
ATOM   14727 O O   . LEU F 2 41  ? 43.541  13.807  60.252  1.00 181.56 ? 41  LEU F O   1 
ATOM   14728 C CB  . LEU F 2 41  ? 41.434  11.843  59.075  1.00 174.75 ? 41  LEU F CB  1 
ATOM   14729 C CG  . LEU F 2 41  ? 40.760  11.463  57.753  1.00 170.75 ? 41  LEU F CG  1 
ATOM   14730 C CD1 . LEU F 2 41  ? 39.257  11.318  57.930  1.00 163.94 ? 41  LEU F CD1 1 
ATOM   14731 C CD2 . LEU F 2 41  ? 41.079  12.484  56.672  1.00 169.26 ? 41  LEU F CD2 1 
ATOM   14732 N N   . LYS F 2 42  ? 43.960  11.858  61.298  1.00 179.11 ? 42  LYS F N   1 
ATOM   14733 C CA  . LYS F 2 42  ? 44.644  12.506  62.408  1.00 176.21 ? 42  LYS F CA  1 
ATOM   14734 C C   . LYS F 2 42  ? 46.086  12.850  62.067  1.00 184.77 ? 42  LYS F C   1 
ATOM   14735 O O   . LYS F 2 42  ? 46.678  13.710  62.727  1.00 185.35 ? 42  LYS F O   1 
ATOM   14736 C CB  . LYS F 2 42  ? 44.605  11.617  63.654  1.00 172.03 ? 42  LYS F CB  1 
ATOM   14737 C CG  . LYS F 2 42  ? 43.938  12.265  64.864  1.00 164.95 ? 42  LYS F CG  1 
ATOM   14738 C CD  . LYS F 2 42  ? 44.646  13.543  65.287  1.00 161.53 ? 42  LYS F CD  1 
ATOM   14739 C CE  . LYS F 2 42  ? 43.953  14.195  66.476  1.00 151.35 ? 42  LYS F CE  1 
ATOM   14740 N NZ  . LYS F 2 42  ? 42.577  14.662  66.146  1.00 150.93 ? 42  LYS F NZ  1 
ATOM   14741 N N   . ALA F 2 43  ? 46.659  12.200  61.050  1.00 190.17 ? 43  ALA F N   1 
ATOM   14742 C CA  . ALA F 2 43  ? 48.002  12.556  60.606  1.00 193.60 ? 43  ALA F CA  1 
ATOM   14743 C C   . ALA F 2 43  ? 48.031  13.943  59.980  1.00 209.95 ? 43  ALA F C   1 
ATOM   14744 O O   . ALA F 2 43  ? 49.079  14.598  59.977  1.00 213.39 ? 43  ALA F O   1 
ATOM   14745 C CB  . ALA F 2 43  ? 48.526  11.514  59.618  1.00 184.55 ? 43  ALA F CB  1 
ATOM   14746 N N   . VAL F 2 44  ? 46.900  14.402  59.444  1.00 246.16 ? 44  VAL F N   1 
ATOM   14747 C CA  . VAL F 2 44  ? 46.779  15.755  58.917  1.00 247.05 ? 44  VAL F CA  1 
ATOM   14748 C C   . VAL F 2 44  ? 46.015  16.668  59.871  1.00 249.45 ? 44  VAL F C   1 
ATOM   14749 O O   . VAL F 2 44  ? 45.660  17.790  59.500  1.00 250.82 ? 44  VAL F O   1 
ATOM   14750 C CB  . VAL F 2 44  ? 46.131  15.756  57.523  1.00 246.11 ? 44  VAL F CB  1 
ATOM   14751 C CG1 . VAL F 2 44  ? 47.074  15.140  56.507  1.00 243.54 ? 44  VAL F CG1 1 
ATOM   14752 C CG2 . VAL F 2 44  ? 44.812  15.007  57.551  1.00 246.34 ? 44  VAL F CG2 1 
ATOM   14753 N N   . GLY F 2 45  ? 45.754  16.210  61.094  1.00 208.60 ? 45  GLY F N   1 
ATOM   14754 C CA  . GLY F 2 45  ? 45.127  17.036  62.106  1.00 191.09 ? 45  GLY F CA  1 
ATOM   14755 C C   . GLY F 2 45  ? 43.672  17.366  61.842  1.00 178.83 ? 45  GLY F C   1 
ATOM   14756 O O   . GLY F 2 45  ? 43.270  18.530  61.927  1.00 171.24 ? 45  GLY F O   1 
ATOM   14757 N N   . VAL F 2 46  ? 42.872  16.355  61.526  1.00 176.56 ? 46  VAL F N   1 
ATOM   14758 C CA  . VAL F 2 46  ? 41.438  16.534  61.334  1.00 170.17 ? 46  VAL F CA  1 
ATOM   14759 C C   . VAL F 2 46  ? 40.729  16.243  62.649  1.00 166.44 ? 46  VAL F C   1 
ATOM   14760 O O   . VAL F 2 46  ? 40.903  15.170  63.240  1.00 163.53 ? 46  VAL F O   1 
ATOM   14761 C CB  . VAL F 2 46  ? 40.913  15.630  60.208  1.00 169.94 ? 46  VAL F CB  1 
ATOM   14762 C CG1 . VAL F 2 46  ? 39.398  15.699  60.142  1.00 166.61 ? 46  VAL F CG1 1 
ATOM   14763 C CG2 . VAL F 2 46  ? 41.524  16.039  58.878  1.00 176.06 ? 46  VAL F CG2 1 
ATOM   14764 N N   . ASP F 2 47  ? 39.926  17.202  63.107  1.00 171.65 ? 47  ASP F N   1 
ATOM   14765 C CA  . ASP F 2 47  ? 39.245  17.108  64.392  1.00 170.19 ? 47  ASP F CA  1 
ATOM   14766 C C   . ASP F 2 47  ? 37.886  16.425  64.289  1.00 165.97 ? 47  ASP F C   1 
ATOM   14767 O O   . ASP F 2 47  ? 37.546  15.599  65.141  1.00 165.76 ? 47  ASP F O   1 
ATOM   14768 C CB  . ASP F 2 47  ? 39.081  18.502  64.999  1.00 170.83 ? 47  ASP F CB  1 
ATOM   14769 C CG  . ASP F 2 47  ? 39.458  19.605  64.031  1.00 172.53 ? 47  ASP F CG  1 
ATOM   14770 O OD1 . ASP F 2 47  ? 40.496  19.468  63.350  1.00 172.60 ? 47  ASP F OD1 1 
ATOM   14771 O OD2 . ASP F 2 47  ? 38.712  20.603  63.945  1.00 173.37 ? 47  ASP F OD2 1 
ATOM   14772 N N   . GLU F 2 48  ? 37.094  16.761  63.275  1.00 165.38 ? 48  GLU F N   1 
ATOM   14773 C CA  . GLU F 2 48  ? 35.738  16.250  63.139  1.00 166.08 ? 48  GLU F CA  1 
ATOM   14774 C C   . GLU F 2 48  ? 35.631  15.389  61.889  1.00 171.66 ? 48  GLU F C   1 
ATOM   14775 O O   . GLU F 2 48  ? 36.209  15.714  60.847  1.00 174.02 ? 48  GLU F O   1 
ATOM   14776 C CB  . GLU F 2 48  ? 34.716  17.391  63.081  1.00 163.11 ? 48  GLU F CB  1 
ATOM   14777 N N   . VAL F 2 49  ? 34.888  14.290  62.000  1.00 171.62 ? 49  VAL F N   1 
ATOM   14778 C CA  . VAL F 2 49  ? 34.681  13.358  60.896  1.00 184.05 ? 49  VAL F CA  1 
ATOM   14779 C C   . VAL F 2 49  ? 33.206  12.986  60.848  1.00 201.58 ? 49  VAL F C   1 
ATOM   14780 O O   . VAL F 2 49  ? 32.619  12.613  61.869  1.00 187.54 ? 49  VAL F O   1 
ATOM   14781 C CB  . VAL F 2 49  ? 35.545  12.089  61.040  1.00 176.57 ? 49  VAL F CB  1 
ATOM   14782 C CG1 . VAL F 2 49  ? 35.268  11.130  59.895  1.00 182.02 ? 49  VAL F CG1 1 
ATOM   14783 C CG2 . VAL F 2 49  ? 37.024  12.449  61.091  1.00 167.21 ? 49  VAL F CG2 1 
ATOM   14784 N N   . VAL F 2 50  ? 32.612  13.081  59.661  1.00 280.97 ? 50  VAL F N   1 
ATOM   14785 C CA  . VAL F 2 50  ? 31.204  12.771  59.449  1.00 281.85 ? 50  VAL F CA  1 
ATOM   14786 C C   . VAL F 2 50  ? 31.097  11.522  58.586  1.00 279.57 ? 50  VAL F C   1 
ATOM   14787 O O   . VAL F 2 50  ? 31.928  11.278  57.703  1.00 277.40 ? 50  VAL F O   1 
ATOM   14788 C CB  . VAL F 2 50  ? 30.457  13.957  58.803  1.00 283.18 ? 50  VAL F CB  1 
ATOM   14789 C CG1 . VAL F 2 50  ? 28.961  13.685  58.752  1.00 284.34 ? 50  VAL F CG1 1 
ATOM   14790 C CG2 . VAL F 2 50  ? 30.745  15.237  59.569  1.00 285.16 ? 50  VAL F CG2 1 
ATOM   14791 N N   . LEU F 2 51  ? 30.067  10.722  58.851  1.00 203.10 ? 51  LEU F N   1 
ATOM   14792 C CA  . LEU F 2 51  ? 29.836  9.468   58.145  1.00 179.47 ? 51  LEU F CA  1 
ATOM   14793 C C   . LEU F 2 51  ? 28.568  9.588   57.307  1.00 169.12 ? 51  LEU F C   1 
ATOM   14794 O O   . LEU F 2 51  ? 27.482  9.823   57.848  1.00 164.61 ? 51  LEU F O   1 
ATOM   14795 C CB  . LEU F 2 51  ? 29.724  8.311   59.137  1.00 167.54 ? 51  LEU F CB  1 
ATOM   14796 C CG  . LEU F 2 51  ? 30.952  8.129   60.035  1.00 166.28 ? 51  LEU F CG  1 
ATOM   14797 C CD1 . LEU F 2 51  ? 30.752  6.979   61.009  1.00 153.62 ? 51  LEU F CD1 1 
ATOM   14798 C CD2 . LEU F 2 51  ? 32.207  7.920   59.199  1.00 165.45 ? 51  LEU F CD2 1 
ATOM   14799 N N   . ALA F 2 52  ? 28.712  9.428   55.989  1.00 159.98 ? 52  ALA F N   1 
ATOM   14800 C CA  . ALA F 2 52  ? 27.576  9.479   55.066  1.00 153.50 ? 52  ALA F CA  1 
ATOM   14801 C C   . ALA F 2 52  ? 27.010  8.070   54.880  1.00 148.51 ? 52  ALA F C   1 
ATOM   14802 O O   . ALA F 2 52  ? 27.149  7.428   53.836  1.00 146.84 ? 52  ALA F O   1 
ATOM   14803 C CB  . ALA F 2 52  ? 27.993  10.102  53.741  1.00 152.85 ? 52  ALA F CB  1 
ATOM   14804 N N   . ILE F 2 53  ? 26.351  7.597   55.936  1.00 142.97 ? 53  ILE F N   1 
ATOM   14805 C CA  . ILE F 2 53  ? 25.759  6.264   55.971  1.00 143.73 ? 53  ILE F CA  1 
ATOM   14806 C C   . ILE F 2 53  ? 24.353  6.294   55.388  1.00 145.81 ? 53  ILE F C   1 
ATOM   14807 O O   . ILE F 2 53  ? 23.790  7.367   55.148  1.00 151.60 ? 53  ILE F O   1 
ATOM   14808 C CB  . ILE F 2 53  ? 25.738  5.711   57.406  1.00 146.49 ? 53  ILE F CB  1 
ATOM   14809 C CG1 . ILE F 2 53  ? 24.766  6.524   58.267  1.00 148.27 ? 53  ILE F CG1 1 
ATOM   14810 C CG2 . ILE F 2 53  ? 27.134  5.736   58.003  1.00 147.47 ? 53  ILE F CG2 1 
ATOM   14811 C CD1 . ILE F 2 53  ? 24.661  6.045   59.694  1.00 147.79 ? 53  ILE F CD1 1 
ATOM   14812 N N   . ASN F 2 54  ? 23.776  5.113   55.161  1.00 150.94 ? 54  ASN F N   1 
ATOM   14813 C CA  . ASN F 2 54  ? 22.398  4.994   54.712  1.00 151.78 ? 54  ASN F CA  1 
ATOM   14814 C C   . ASN F 2 54  ? 21.494  4.272   55.700  1.00 153.43 ? 54  ASN F C   1 
ATOM   14815 O O   . ASN F 2 54  ? 20.273  4.448   55.630  1.00 152.36 ? 54  ASN F O   1 
ATOM   14816 C CB  . ASN F 2 54  ? 22.336  4.267   53.358  1.00 150.48 ? 54  ASN F CB  1 
ATOM   14817 C CG  . ASN F 2 54  ? 20.965  4.341   52.718  1.00 158.28 ? 54  ASN F CG  1 
ATOM   14818 O OD1 . ASN F 2 54  ? 20.587  5.366   52.151  1.00 173.02 ? 54  ASN F OD1 1 
ATOM   14819 N ND2 . ASN F 2 54  ? 20.213  3.250   52.804  1.00 153.19 ? 54  ASN F ND2 1 
ATOM   14820 N N   . TYR F 2 55  ? 22.049  3.482   56.617  1.00 157.99 ? 55  TYR F N   1 
ATOM   14821 C CA  . TYR F 2 55  ? 21.270  2.797   57.634  1.00 161.60 ? 55  TYR F CA  1 
ATOM   14822 C C   . TYR F 2 55  ? 21.205  3.649   58.902  1.00 162.03 ? 55  TYR F C   1 
ATOM   14823 O O   . TYR F 2 55  ? 21.733  4.761   58.965  1.00 160.69 ? 55  TYR F O   1 
ATOM   14824 C CB  . TYR F 2 55  ? 21.859  1.415   57.921  1.00 160.42 ? 55  TYR F CB  1 
ATOM   14825 C CG  . TYR F 2 55  ? 23.284  1.438   58.433  1.00 158.78 ? 55  TYR F CG  1 
ATOM   14826 C CD1 . TYR F 2 55  ? 24.359  1.484   57.557  1.00 156.45 ? 55  TYR F CD1 1 
ATOM   14827 C CD2 . TYR F 2 55  ? 23.552  1.398   59.794  1.00 159.62 ? 55  TYR F CD2 1 
ATOM   14828 C CE1 . TYR F 2 55  ? 25.662  1.503   58.024  1.00 153.28 ? 55  TYR F CE1 1 
ATOM   14829 C CE2 . TYR F 2 55  ? 24.850  1.417   60.271  1.00 154.46 ? 55  TYR F CE2 1 
ATOM   14830 C CZ  . TYR F 2 55  ? 25.901  1.469   59.382  1.00 150.03 ? 55  TYR F CZ  1 
ATOM   14831 O OH  . TYR F 2 55  ? 27.195  1.487   59.852  1.00 146.17 ? 55  TYR F OH  1 
ATOM   14832 N N   . GLN F 2 56  ? 20.549  3.119   59.929  1.00 168.90 ? 56  GLN F N   1 
ATOM   14833 C CA  . GLN F 2 56  ? 20.421  3.840   61.193  1.00 170.11 ? 56  GLN F CA  1 
ATOM   14834 C C   . GLN F 2 56  ? 21.694  3.676   62.020  1.00 169.45 ? 56  GLN F C   1 
ATOM   14835 O O   . GLN F 2 56  ? 22.170  2.551   62.199  1.00 168.23 ? 56  GLN F O   1 
ATOM   14836 C CB  . GLN F 2 56  ? 19.199  3.356   61.984  1.00 169.96 ? 56  GLN F CB  1 
ATOM   14837 C CG  . GLN F 2 56  ? 19.222  1.900   62.458  1.00 172.32 ? 56  GLN F CG  1 
ATOM   14838 C CD  . GLN F 2 56  ? 19.141  0.896   61.324  1.00 181.07 ? 56  GLN F CD  1 
ATOM   14839 O OE1 . GLN F 2 56  ? 18.679  1.215   60.228  1.00 180.12 ? 56  GLN F OE1 1 
ATOM   14840 N NE2 . GLN F 2 56  ? 19.587  -0.327  61.584  1.00 180.26 ? 56  GLN F NE2 1 
ATOM   14841 N N   . PRO F 2 57  ? 22.277  4.765   62.526  1.00 155.27 ? 57  PRO F N   1 
ATOM   14842 C CA  . PRO F 2 57  ? 23.520  4.655   63.300  1.00 150.09 ? 57  PRO F CA  1 
ATOM   14843 C C   . PRO F 2 57  ? 23.329  4.138   64.716  1.00 143.85 ? 57  PRO F C   1 
ATOM   14844 O O   . PRO F 2 57  ? 24.313  4.048   65.459  1.00 141.21 ? 57  PRO F O   1 
ATOM   14845 C CB  . PRO F 2 57  ? 24.032  6.101   63.314  1.00 147.17 ? 57  PRO F CB  1 
ATOM   14846 C CG  . PRO F 2 57  ? 22.788  6.920   63.280  1.00 147.58 ? 57  PRO F CG  1 
ATOM   14847 C CD  . PRO F 2 57  ? 21.815  6.160   62.412  1.00 155.02 ? 57  PRO F CD  1 
ATOM   14848 N N   . GLU F 2 58  ? 22.102  3.775   65.096  1.00 143.97 ? 58  GLU F N   1 
ATOM   14849 C CA  . GLU F 2 58  ? 21.809  3.374   66.468  1.00 142.22 ? 58  GLU F CA  1 
ATOM   14850 C C   . GLU F 2 58  ? 22.583  2.134   66.894  1.00 143.05 ? 58  GLU F C   1 
ATOM   14851 O O   . GLU F 2 58  ? 22.748  1.900   68.096  1.00 140.39 ? 58  GLU F O   1 
ATOM   14852 C CB  . GLU F 2 58  ? 20.309  3.121   66.610  1.00 140.17 ? 58  GLU F CB  1 
ATOM   14853 C CG  . GLU F 2 58  ? 19.448  4.244   66.060  1.00 142.33 ? 58  GLU F CG  1 
ATOM   14854 C CD  . GLU F 2 58  ? 18.186  3.730   65.397  1.00 145.06 ? 58  GLU F CD  1 
ATOM   14855 O OE1 . GLU F 2 58  ? 17.986  2.497   65.374  1.00 145.41 ? 58  GLU F OE1 1 
ATOM   14856 O OE2 . GLU F 2 58  ? 17.399  4.556   64.890  1.00 144.45 ? 58  GLU F OE2 1 
ATOM   14857 N N   . VAL F 2 59  ? 23.063  1.337   65.939  1.00 146.91 ? 59  VAL F N   1 
ATOM   14858 C CA  . VAL F 2 59  ? 23.756  0.097   66.268  1.00 146.36 ? 59  VAL F CA  1 
ATOM   14859 C C   . VAL F 2 59  ? 25.248  0.296   66.498  1.00 143.51 ? 59  VAL F C   1 
ATOM   14860 O O   . VAL F 2 59  ? 25.886  -0.557  67.131  1.00 143.67 ? 59  VAL F O   1 
ATOM   14861 C CB  . VAL F 2 59  ? 23.543  -0.950  65.161  1.00 145.66 ? 59  VAL F CB  1 
ATOM   14862 C CG1 . VAL F 2 59  ? 22.067  -1.283  65.029  1.00 150.21 ? 59  VAL F CG1 1 
ATOM   14863 C CG2 . VAL F 2 59  ? 24.104  -0.447  63.840  1.00 143.63 ? 59  VAL F CG2 1 
ATOM   14864 N N   . MET F 2 60  ? 25.824  1.394   66.010  1.00 140.72 ? 60  MET F N   1 
ATOM   14865 C CA  . MET F 2 60  ? 27.257  1.632   66.116  1.00 138.90 ? 60  MET F CA  1 
ATOM   14866 C C   . MET F 2 60  ? 27.579  2.867   66.942  1.00 138.66 ? 60  MET F C   1 
ATOM   14867 O O   . MET F 2 60  ? 28.742  3.286   66.978  1.00 138.06 ? 60  MET F O   1 
ATOM   14868 C CB  . MET F 2 60  ? 27.874  1.774   64.722  1.00 139.34 ? 60  MET F CB  1 
ATOM   14869 C CG  . MET F 2 60  ? 27.349  2.969   63.954  1.00 141.61 ? 60  MET F CG  1 
ATOM   14870 S SD  . MET F 2 60  ? 27.920  3.013   62.249  1.00 142.23 ? 60  MET F SD  1 
ATOM   14871 C CE  . MET F 2 60  ? 27.305  4.614   61.734  1.00 147.07 ? 60  MET F CE  1 
ATOM   14872 N N   . LEU F 2 61  ? 26.586  3.456   67.610  1.00 138.94 ? 61  LEU F N   1 
ATOM   14873 C CA  . LEU F 2 61  ? 26.847  4.642   68.417  1.00 141.44 ? 61  LEU F CA  1 
ATOM   14874 C C   . LEU F 2 61  ? 27.816  4.329   69.548  1.00 145.45 ? 61  LEU F C   1 
ATOM   14875 O O   . LEU F 2 61  ? 28.648  5.168   69.911  1.00 149.58 ? 61  LEU F O   1 
ATOM   14876 C CB  . LEU F 2 61  ? 25.538  5.214   68.959  1.00 139.23 ? 61  LEU F CB  1 
ATOM   14877 C CG  . LEU F 2 61  ? 24.677  5.932   67.917  1.00 138.80 ? 61  LEU F CG  1 
ATOM   14878 C CD1 . LEU F 2 61  ? 23.412  6.503   68.541  1.00 134.40 ? 61  LEU F CD1 1 
ATOM   14879 C CD2 . LEU F 2 61  ? 25.475  7.020   67.206  1.00 138.68 ? 61  LEU F CD2 1 
ATOM   14880 N N   . ASN F 2 62  ? 27.727  3.125   70.117  1.00 144.51 ? 62  ASN F N   1 
ATOM   14881 C CA  . ASN F 2 62  ? 28.668  2.750   71.164  1.00 146.78 ? 62  ASN F CA  1 
ATOM   14882 C C   . ASN F 2 62  ? 30.076  2.607   70.613  1.00 148.84 ? 62  ASN F C   1 
ATOM   14883 O O   . ASN F 2 62  ? 31.047  2.914   71.309  1.00 149.36 ? 62  ASN F O   1 
ATOM   14884 C CB  . ASN F 2 62  ? 28.234  1.445   71.826  1.00 147.54 ? 62  ASN F CB  1 
ATOM   14885 C CG  . ASN F 2 62  ? 27.074  1.635   72.772  1.00 152.97 ? 62  ASN F CG  1 
ATOM   14886 O OD1 . ASN F 2 62  ? 26.951  2.675   73.418  1.00 157.03 ? 62  ASN F OD1 1 
ATOM   14887 N ND2 . ASN F 2 62  ? 26.211  0.632   72.857  1.00 153.30 ? 62  ASN F ND2 1 
ATOM   14888 N N   . PHE F 2 63  ? 30.204  2.166   69.362  1.00 147.82 ? 63  PHE F N   1 
ATOM   14889 C CA  . PHE F 2 63  ? 31.522  2.017   68.759  1.00 147.58 ? 63  PHE F CA  1 
ATOM   14890 C C   . PHE F 2 63  ? 32.108  3.366   68.365  1.00 151.44 ? 63  PHE F C   1 
ATOM   14891 O O   . PHE F 2 63  ? 33.294  3.622   68.597  1.00 153.96 ? 63  PHE F O   1 
ATOM   14892 C CB  . PHE F 2 63  ? 31.439  1.089   67.548  1.00 142.13 ? 63  PHE F CB  1 
ATOM   14893 C CG  . PHE F 2 63  ? 31.175  -0.346  67.906  1.00 137.66 ? 63  PHE F CG  1 
ATOM   14894 C CD1 . PHE F 2 63  ? 32.223  -1.233  68.091  1.00 133.51 ? 63  PHE F CD1 1 
ATOM   14895 C CD2 . PHE F 2 63  ? 29.877  -0.806  68.063  1.00 136.92 ? 63  PHE F CD2 1 
ATOM   14896 C CE1 . PHE F 2 63  ? 31.980  -2.553  68.422  1.00 128.05 ? 63  PHE F CE1 1 
ATOM   14897 C CE2 . PHE F 2 63  ? 29.629  -2.124  68.392  1.00 137.16 ? 63  PHE F CE2 1 
ATOM   14898 C CZ  . PHE F 2 63  ? 30.681  -2.997  68.572  1.00 133.23 ? 63  PHE F CZ  1 
ATOM   14899 N N   . LEU F 2 64  ? 31.297  4.236   67.759  1.00 152.98 ? 64  LEU F N   1 
ATOM   14900 C CA  . LEU F 2 64  ? 31.792  5.549   67.363  1.00 156.62 ? 64  LEU F CA  1 
ATOM   14901 C C   . LEU F 2 64  ? 32.055  6.440   68.570  1.00 157.26 ? 64  LEU F C   1 
ATOM   14902 O O   . LEU F 2 64  ? 32.898  7.341   68.501  1.00 158.04 ? 64  LEU F O   1 
ATOM   14903 C CB  . LEU F 2 64  ? 30.796  6.213   66.415  1.00 156.99 ? 64  LEU F CB  1 
ATOM   14904 C CG  . LEU F 2 64  ? 30.408  5.352   65.212  1.00 154.71 ? 64  LEU F CG  1 
ATOM   14905 C CD1 . LEU F 2 64  ? 29.403  6.073   64.351  1.00 151.70 ? 64  LEU F CD1 1 
ATOM   14906 C CD2 . LEU F 2 64  ? 31.638  4.979   64.400  1.00 155.52 ? 64  LEU F CD2 1 
ATOM   14907 N N   . LYS F 2 65  ? 31.346  6.209   69.678  1.00 170.38 ? 65  LYS F N   1 
ATOM   14908 C CA  . LYS F 2 65  ? 31.572  6.999   70.883  1.00 171.19 ? 65  LYS F CA  1 
ATOM   14909 C C   . LYS F 2 65  ? 32.844  6.582   71.609  1.00 169.98 ? 65  LYS F C   1 
ATOM   14910 O O   . LYS F 2 65  ? 33.449  7.402   72.308  1.00 170.18 ? 65  LYS F O   1 
ATOM   14911 C CB  . LYS F 2 65  ? 30.370  6.885   71.821  1.00 174.45 ? 65  LYS F CB  1 
ATOM   14912 C CG  . LYS F 2 65  ? 30.238  8.023   72.819  1.00 178.85 ? 65  LYS F CG  1 
ATOM   14913 C CD  . LYS F 2 65  ? 28.939  7.906   73.597  1.00 184.71 ? 65  LYS F CD  1 
ATOM   14914 C CE  . LYS F 2 65  ? 27.748  7.782   72.658  1.00 185.80 ? 65  LYS F CE  1 
ATOM   14915 N NZ  . LYS F 2 65  ? 26.472  7.572   73.394  1.00 188.90 ? 65  LYS F NZ  1 
ATOM   14916 N N   . ASP F 2 66  ? 33.268  5.325   71.453  1.00 160.67 ? 66  ASP F N   1 
ATOM   14917 C CA  . ASP F 2 66  ? 34.486  4.862   72.105  1.00 161.53 ? 66  ASP F CA  1 
ATOM   14918 C C   . ASP F 2 66  ? 35.738  5.256   71.338  1.00 162.72 ? 66  ASP F C   1 
ATOM   14919 O O   . ASP F 2 66  ? 36.839  5.186   71.896  1.00 163.84 ? 66  ASP F O   1 
ATOM   14920 C CB  . ASP F 2 66  ? 34.458  3.339   72.279  1.00 160.24 ? 66  ASP F CB  1 
ATOM   14921 C CG  . ASP F 2 66  ? 33.328  2.872   73.177  1.00 158.08 ? 66  ASP F CG  1 
ATOM   14922 O OD1 . ASP F 2 66  ? 32.905  3.648   74.059  1.00 159.99 ? 66  ASP F OD1 1 
ATOM   14923 O OD2 . ASP F 2 66  ? 32.867  1.722   73.006  1.00 153.48 ? 66  ASP F OD2 1 
ATOM   14924 N N   . PHE F 2 67  ? 35.598  5.658   70.077  1.00 168.90 ? 67  PHE F N   1 
ATOM   14925 C CA  . PHE F 2 67  ? 36.728  6.088   69.268  1.00 167.64 ? 67  PHE F CA  1 
ATOM   14926 C C   . PHE F 2 67  ? 36.933  7.598   69.280  1.00 168.00 ? 67  PHE F C   1 
ATOM   14927 O O   . PHE F 2 67  ? 37.991  8.063   68.843  1.00 167.17 ? 67  PHE F O   1 
ATOM   14928 C CB  . PHE F 2 67  ? 36.561  5.588   67.827  1.00 169.35 ? 67  PHE F CB  1 
ATOM   14929 C CG  . PHE F 2 67  ? 36.528  4.088   67.711  1.00 169.31 ? 67  PHE F CG  1 
ATOM   14930 C CD1 . PHE F 2 67  ? 37.152  3.293   68.661  1.00 167.06 ? 67  PHE F CD1 1 
ATOM   14931 C CD2 . PHE F 2 67  ? 35.869  3.473   66.660  1.00 165.56 ? 67  PHE F CD2 1 
ATOM   14932 C CE1 . PHE F 2 67  ? 37.121  1.914   68.562  1.00 165.90 ? 67  PHE F CE1 1 
ATOM   14933 C CE2 . PHE F 2 67  ? 35.836  2.093   66.555  1.00 163.31 ? 67  PHE F CE2 1 
ATOM   14934 C CZ  . PHE F 2 67  ? 36.464  1.313   67.508  1.00 164.34 ? 67  PHE F CZ  1 
ATOM   14935 N N   . GLU F 2 68  ? 35.955  8.370   69.764  1.00 161.28 ? 68  GLU F N   1 
ATOM   14936 C CA  . GLU F 2 68  ? 36.112  9.821   69.796  1.00 156.08 ? 68  GLU F CA  1 
ATOM   14937 C C   . GLU F 2 68  ? 37.102  10.263  70.866  1.00 158.28 ? 68  GLU F C   1 
ATOM   14938 O O   . GLU F 2 68  ? 37.824  11.247  70.670  1.00 158.56 ? 68  GLU F O   1 
ATOM   14939 C CB  . GLU F 2 68  ? 34.763  10.499  70.035  1.00 152.25 ? 68  GLU F CB  1 
ATOM   14940 C CG  . GLU F 2 68  ? 33.829  10.503  68.841  1.00 149.63 ? 68  GLU F CG  1 
ATOM   14941 C CD  . GLU F 2 68  ? 32.582  11.325  69.097  1.00 143.16 ? 68  GLU F CD  1 
ATOM   14942 O OE1 . GLU F 2 68  ? 31.903  11.078  70.115  1.00 142.44 ? 68  GLU F OE1 1 
ATOM   14943 O OE2 . GLU F 2 68  ? 32.289  12.229  68.287  1.00 142.77 ? 68  GLU F OE2 1 
ATOM   14944 N N   . THR F 2 69  ? 37.156  9.556   71.993  1.00 156.86 ? 69  THR F N   1 
ATOM   14945 C CA  . THR F 2 69  ? 38.075  9.905   73.069  1.00 155.10 ? 69  THR F CA  1 
ATOM   14946 C C   . THR F 2 69  ? 39.440  9.253   72.898  1.00 153.20 ? 69  THR F C   1 
ATOM   14947 O O   . THR F 2 69  ? 40.465  9.871   73.209  1.00 152.85 ? 69  THR F O   1 
ATOM   14948 C CB  . THR F 2 69  ? 37.481  9.514   74.425  1.00 153.67 ? 69  THR F CB  1 
ATOM   14949 O OG1 . THR F 2 69  ? 36.406  8.587   74.229  1.00 155.06 ? 69  THR F OG1 1 
ATOM   14950 C CG2 . THR F 2 69  ? 36.962  10.746  75.154  1.00 156.95 ? 69  THR F CG2 1 
ATOM   14951 N N   . LYS F 2 70  ? 39.472  8.010   72.415  1.00 152.74 ? 70  LYS F N   1 
ATOM   14952 C CA  . LYS F 2 70  ? 40.743  7.325   72.210  1.00 151.86 ? 70  LYS F CA  1 
ATOM   14953 C C   . LYS F 2 70  ? 41.582  8.025   71.148  1.00 151.67 ? 70  LYS F C   1 
ATOM   14954 O O   . LYS F 2 70  ? 42.807  8.124   71.278  1.00 151.73 ? 70  LYS F O   1 
ATOM   14955 C CB  . LYS F 2 70  ? 40.492  5.868   71.818  1.00 154.24 ? 70  LYS F CB  1 
ATOM   14956 C CG  . LYS F 2 70  ? 41.754  5.072   71.532  1.00 156.16 ? 70  LYS F CG  1 
ATOM   14957 C CD  . LYS F 2 70  ? 41.429  3.702   70.955  1.00 156.68 ? 70  LYS F CD  1 
ATOM   14958 C CE  . LYS F 2 70  ? 40.632  3.818   69.663  1.00 151.55 ? 70  LYS F CE  1 
ATOM   14959 N NZ  . LYS F 2 70  ? 40.275  2.482   69.108  1.00 147.64 ? 70  LYS F NZ  1 
ATOM   14960 N N   . LEU F 2 71  ? 40.939  8.520   70.092  1.00 153.21 ? 71  LEU F N   1 
ATOM   14961 C CA  . LEU F 2 71  ? 41.639  9.136   68.975  1.00 150.75 ? 71  LEU F CA  1 
ATOM   14962 C C   . LEU F 2 71  ? 41.590  10.659  68.996  1.00 153.91 ? 71  LEU F C   1 
ATOM   14963 O O   . LEU F 2 71  ? 42.263  11.292  68.174  1.00 155.31 ? 71  LEU F O   1 
ATOM   14964 C CB  . LEU F 2 71  ? 41.054  8.623   67.656  1.00 150.56 ? 71  LEU F CB  1 
ATOM   14965 C CG  . LEU F 2 71  ? 41.126  7.102   67.510  1.00 150.28 ? 71  LEU F CG  1 
ATOM   14966 C CD1 . LEU F 2 71  ? 40.461  6.645   66.225  1.00 152.54 ? 71  LEU F CD1 1 
ATOM   14967 C CD2 . LEU F 2 71  ? 42.567  6.622   67.576  1.00 148.86 ? 71  LEU F CD2 1 
ATOM   14968 N N   . GLU F 2 72  ? 40.826  11.252  69.912  1.00 158.74 ? 72  GLU F N   1 
ATOM   14969 C CA  . GLU F 2 72  ? 40.646  12.701  70.002  1.00 159.30 ? 72  GLU F CA  1 
ATOM   14970 C C   . GLU F 2 72  ? 40.165  13.271  68.666  1.00 160.49 ? 72  GLU F C   1 
ATOM   14971 O O   . GLU F 2 72  ? 40.811  14.112  68.038  1.00 160.47 ? 72  GLU F O   1 
ATOM   14972 C CB  . GLU F 2 72  ? 41.932  13.386  70.476  1.00 154.36 ? 72  GLU F CB  1 
ATOM   14973 C CG  . GLU F 2 72  ? 42.238  13.163  71.951  1.00 157.53 ? 72  GLU F CG  1 
ATOM   14974 C CD  . GLU F 2 72  ? 43.451  13.942  72.425  1.00 168.44 ? 72  GLU F CD  1 
ATOM   14975 O OE1 . GLU F 2 72  ? 44.286  14.319  71.576  1.00 171.88 ? 72  GLU F OE1 1 
ATOM   14976 O OE2 . GLU F 2 72  ? 43.570  14.173  73.647  1.00 170.21 ? 72  GLU F OE2 1 
ATOM   14977 N N   . ILE F 2 73  ? 38.997  12.791  68.248  1.00 153.17 ? 73  ILE F N   1 
ATOM   14978 C CA  . ILE F 2 73  ? 38.383  13.175  66.982  1.00 151.79 ? 73  ILE F CA  1 
ATOM   14979 C C   . ILE F 2 73  ? 36.876  13.213  67.185  1.00 151.32 ? 73  ILE F C   1 
ATOM   14980 O O   . ILE F 2 73  ? 36.309  12.354  67.864  1.00 149.45 ? 73  ILE F O   1 
ATOM   14981 C CB  . ILE F 2 73  ? 38.775  12.205  65.841  1.00 150.51 ? 73  ILE F CB  1 
ATOM   14982 C CG1 . ILE F 2 73  ? 40.130  12.586  65.245  1.00 152.39 ? 73  ILE F CG1 1 
ATOM   14983 C CG2 . ILE F 2 73  ? 37.709  12.165  64.754  1.00 151.02 ? 73  ILE F CG2 1 
ATOM   14984 C CD1 . ILE F 2 73  ? 40.506  11.764  64.032  1.00 156.36 ? 73  ILE F CD1 1 
ATOM   14985 N N   . LYS F 2 74  ? 36.227  14.213  66.594  1.00 151.46 ? 74  LYS F N   1 
ATOM   14986 C CA  . LYS F 2 74  ? 34.776  14.329  66.653  1.00 149.96 ? 74  LYS F CA  1 
ATOM   14987 C C   . LYS F 2 74  ? 34.162  13.474  65.551  1.00 149.47 ? 74  LYS F C   1 
ATOM   14988 O O   . LYS F 2 74  ? 34.496  13.636  64.373  1.00 150.38 ? 74  LYS F O   1 
ATOM   14989 C CB  . LYS F 2 74  ? 34.341  15.787  66.512  1.00 148.46 ? 74  LYS F CB  1 
ATOM   14990 C CG  . LYS F 2 74  ? 32.852  16.002  66.714  1.00 147.24 ? 74  LYS F CG  1 
ATOM   14991 C CD  . LYS F 2 74  ? 32.432  15.577  68.111  1.00 145.39 ? 74  LYS F CD  1 
ATOM   14992 C CE  . LYS F 2 74  ? 30.967  15.879  68.368  1.00 147.13 ? 74  LYS F CE  1 
ATOM   14993 N NZ  . LYS F 2 74  ? 30.675  17.331  68.233  1.00 149.83 ? 74  LYS F NZ  1 
ATOM   14994 N N   . ILE F 2 75  ? 33.278  12.558  65.935  1.00 151.02 ? 75  ILE F N   1 
ATOM   14995 C CA  . ILE F 2 75  ? 32.646  11.629  65.004  1.00 151.90 ? 75  ILE F CA  1 
ATOM   14996 C C   . ILE F 2 75  ? 31.139  11.795  65.122  1.00 152.62 ? 75  ILE F C   1 
ATOM   14997 O O   . ILE F 2 75  ? 30.556  11.510  66.176  1.00 149.12 ? 75  ILE F O   1 
ATOM   14998 C CB  . ILE F 2 75  ? 33.062  10.174  65.273  1.00 145.42 ? 75  ILE F CB  1 
ATOM   14999 C CG1 . ILE F 2 75  ? 34.578  10.014  65.139  1.00 146.22 ? 75  ILE F CG1 1 
ATOM   15000 C CG2 . ILE F 2 75  ? 32.337  9.230   64.323  1.00 145.95 ? 75  ILE F CG2 1 
ATOM   15001 C CD1 . ILE F 2 75  ? 35.076  8.622   65.453  1.00 146.94 ? 75  ILE F CD1 1 
ATOM   15002 N N   . THR F 2 76  ? 30.511  12.249  64.040  1.00 157.35 ? 76  THR F N   1 
ATOM   15003 C CA  . THR F 2 76  ? 29.068  12.416  63.968  1.00 159.26 ? 76  THR F CA  1 
ATOM   15004 C C   . THR F 2 76  ? 28.546  11.728  62.715  1.00 171.01 ? 76  THR F C   1 
ATOM   15005 O O   . THR F 2 76  ? 29.269  11.569  61.728  1.00 178.21 ? 76  THR F O   1 
ATOM   15006 C CB  . THR F 2 76  ? 28.662  13.895  63.958  1.00 163.68 ? 76  THR F CB  1 
ATOM   15007 O OG1 . THR F 2 76  ? 29.335  14.569  62.888  1.00 180.59 ? 76  THR F OG1 1 
ATOM   15008 C CG2 . THR F 2 76  ? 29.022  14.558  65.282  1.00 157.11 ? 76  THR F CG2 1 
ATOM   15009 N N   . CYS F 2 77  ? 27.285  11.315  62.764  1.00 165.69 ? 77  CYS F N   1 
ATOM   15010 C CA  . CYS F 2 77  ? 26.677  10.553  61.685  1.00 162.25 ? 77  CYS F CA  1 
ATOM   15011 C C   . CYS F 2 77  ? 25.722  11.410  60.862  1.00 158.82 ? 77  CYS F C   1 
ATOM   15012 O O   . CYS F 2 77  ? 25.176  12.412  61.333  1.00 155.15 ? 77  CYS F O   1 
ATOM   15013 C CB  . CYS F 2 77  ? 25.925  9.341   62.238  1.00 159.51 ? 77  CYS F CB  1 
ATOM   15014 S SG  . CYS F 2 77  ? 26.970  8.131   63.066  1.00 167.07 ? 77  CYS F SG  1 
ATOM   15015 N N   . SER F 2 78  ? 25.529  10.992  59.612  1.00 163.09 ? 78  SER F N   1 
ATOM   15016 C CA  . SER F 2 78  ? 24.545  11.597  58.723  1.00 162.87 ? 78  SER F CA  1 
ATOM   15017 C C   . SER F 2 78  ? 23.804  10.475  58.014  1.00 160.85 ? 78  SER F C   1 
ATOM   15018 O O   . SER F 2 78  ? 24.424  9.660   57.324  1.00 157.48 ? 78  SER F O   1 
ATOM   15019 C CB  . SER F 2 78  ? 25.211  12.534  57.713  1.00 163.02 ? 78  SER F CB  1 
ATOM   15020 O OG  . SER F 2 78  ? 26.019  11.807  56.805  1.00 159.40 ? 78  SER F OG  1 
ATOM   15021 N N   . GLN F 2 79  ? 22.484  10.437  58.177  1.00 162.98 ? 79  GLN F N   1 
ATOM   15022 C CA  . GLN F 2 79  ? 21.646  9.387   57.611  1.00 165.61 ? 79  GLN F CA  1 
ATOM   15023 C C   . GLN F 2 79  ? 20.708  9.993   56.579  1.00 173.96 ? 79  GLN F C   1 
ATOM   15024 O O   . GLN F 2 79  ? 19.959  10.926  56.889  1.00 176.08 ? 79  GLN F O   1 
ATOM   15025 C CB  . GLN F 2 79  ? 20.854  8.674   58.709  1.00 161.44 ? 79  GLN F CB  1 
ATOM   15026 C CG  . GLN F 2 79  ? 19.990  7.528   58.218  1.00 161.05 ? 79  GLN F CG  1 
ATOM   15027 C CD  . GLN F 2 79  ? 19.170  6.904   59.331  1.00 158.12 ? 79  GLN F CD  1 
ATOM   15028 O OE1 . GLN F 2 79  ? 19.207  7.357   60.476  1.00 154.74 ? 79  GLN F OE1 1 
ATOM   15029 N NE2 . GLN F 2 79  ? 18.427  5.854   59.001  1.00 158.56 ? 79  GLN F NE2 1 
ATOM   15030 N N   . GLU F 2 80  ? 20.750  9.467   55.359  1.00 190.84 ? 80  GLU F N   1 
ATOM   15031 C CA  . GLU F 2 80  ? 19.877  9.905   54.280  1.00 192.89 ? 80  GLU F CA  1 
ATOM   15032 C C   . GLU F 2 80  ? 18.726  8.923   54.094  1.00 195.81 ? 80  GLU F C   1 
ATOM   15033 O O   . GLU F 2 80  ? 18.876  7.716   54.298  1.00 191.80 ? 80  GLU F O   1 
ATOM   15034 C CB  . GLU F 2 80  ? 20.653  10.053  52.968  1.00 192.25 ? 80  GLU F CB  1 
ATOM   15035 C CG  . GLU F 2 80  ? 21.625  11.226  52.934  1.00 193.63 ? 80  GLU F CG  1 
ATOM   15036 C CD  . GLU F 2 80  ? 22.885  10.981  53.742  1.00 196.69 ? 80  GLU F CD  1 
ATOM   15037 O OE1 . GLU F 2 80  ? 23.072  9.849   54.234  1.00 190.43 ? 80  GLU F OE1 1 
ATOM   15038 O OE2 . GLU F 2 80  ? 23.686  11.926  53.893  1.00 199.18 ? 80  GLU F OE2 1 
ATOM   15039 N N   . THR F 2 81  ? 17.567  9.461   53.706  1.00 198.05 ? 81  THR F N   1 
ATOM   15040 C CA  . THR F 2 81  ? 16.405  8.618   53.444  1.00 203.36 ? 81  THR F CA  1 
ATOM   15041 C C   . THR F 2 81  ? 16.665  7.664   52.284  1.00 207.10 ? 81  THR F C   1 
ATOM   15042 O O   . THR F 2 81  ? 16.421  6.457   52.390  1.00 207.16 ? 81  THR F O   1 
ATOM   15043 C CB  . THR F 2 81  ? 15.178  9.487   53.162  1.00 203.54 ? 81  THR F CB  1 
ATOM   15044 O OG1 . THR F 2 81  ? 15.474  10.405  52.103  1.00 202.16 ? 81  THR F OG1 1 
ATOM   15045 C CG2 . THR F 2 81  ? 14.775  10.264  54.404  1.00 199.85 ? 81  THR F CG2 1 
ATOM   15046 N N   . GLU F 2 82  ? 17.153  8.189   51.162  1.00 211.67 ? 82  GLU F N   1 
ATOM   15047 C CA  . GLU F 2 82  ? 17.464  7.378   49.997  1.00 211.78 ? 82  GLU F CA  1 
ATOM   15048 C C   . GLU F 2 82  ? 18.911  7.594   49.571  1.00 210.55 ? 82  GLU F C   1 
ATOM   15049 O O   . GLU F 2 82  ? 19.471  8.675   49.785  1.00 207.10 ? 82  GLU F O   1 
ATOM   15050 C CB  . GLU F 2 82  ? 16.542  7.699   48.811  1.00 210.03 ? 82  GLU F CB  1 
ATOM   15051 C CG  . GLU F 2 82  ? 15.088  7.278   48.985  1.00 212.26 ? 82  GLU F CG  1 
ATOM   15052 C CD  . GLU F 2 82  ? 14.329  8.143   49.971  1.00 211.77 ? 82  GLU F CD  1 
ATOM   15053 O OE1 . GLU F 2 82  ? 14.520  9.377   49.952  1.00 210.20 ? 82  GLU F OE1 1 
ATOM   15054 O OE2 . GLU F 2 82  ? 13.540  7.588   50.764  1.00 213.53 ? 82  GLU F OE2 1 
ATOM   15055 N N   . PRO F 2 83  ? 19.545  6.586   48.974  1.00 218.05 ? 83  PRO F N   1 
ATOM   15056 C CA  . PRO F 2 83  ? 20.852  6.810   48.340  1.00 217.06 ? 83  PRO F CA  1 
ATOM   15057 C C   . PRO F 2 83  ? 20.726  7.799   47.193  1.00 215.67 ? 83  PRO F C   1 
ATOM   15058 O O   . PRO F 2 83  ? 20.007  7.563   46.219  1.00 213.36 ? 83  PRO F O   1 
ATOM   15059 C CB  . PRO F 2 83  ? 21.251  5.414   47.848  1.00 217.67 ? 83  PRO F CB  1 
ATOM   15060 C CG  . PRO F 2 83  ? 20.456  4.468   48.690  1.00 215.93 ? 83  PRO F CG  1 
ATOM   15061 C CD  . PRO F 2 83  ? 19.155  5.166   48.953  1.00 216.35 ? 83  PRO F CD  1 
ATOM   15062 N N   . LEU F 2 84  ? 21.434  8.915   47.314  1.00 195.31 ? 84  LEU F N   1 
ATOM   15063 C CA  . LEU F 2 84  ? 21.336  9.998   46.338  1.00 185.54 ? 84  LEU F CA  1 
ATOM   15064 C C   . LEU F 2 84  ? 22.525  9.957   45.380  1.00 188.65 ? 84  LEU F C   1 
ATOM   15065 O O   . LEU F 2 84  ? 23.277  10.918  45.224  1.00 193.17 ? 84  LEU F O   1 
ATOM   15066 C CB  . LEU F 2 84  ? 21.241  11.341  47.054  1.00 177.55 ? 84  LEU F CB  1 
ATOM   15067 C CG  . LEU F 2 84  ? 20.169  11.452  48.138  1.00 172.39 ? 84  LEU F CG  1 
ATOM   15068 C CD1 . LEU F 2 84  ? 20.293  12.780  48.863  1.00 159.93 ? 84  LEU F CD1 1 
ATOM   15069 C CD2 . LEU F 2 84  ? 18.783  11.289  47.536  1.00 168.27 ? 84  LEU F CD2 1 
ATOM   15070 N N   . GLY F 2 85  ? 22.677  8.808   44.726  1.00 197.47 ? 85  GLY F N   1 
ATOM   15071 C CA  . GLY F 2 85  ? 23.803  8.626   43.825  1.00 196.47 ? 85  GLY F CA  1 
ATOM   15072 C C   . GLY F 2 85  ? 25.109  8.548   44.593  1.00 201.12 ? 85  GLY F C   1 
ATOM   15073 O O   . GLY F 2 85  ? 25.224  7.857   45.611  1.00 202.39 ? 85  GLY F O   1 
ATOM   15074 N N   . THR F 2 86  ? 26.115  9.264   44.094  1.00 198.10 ? 86  THR F N   1 
ATOM   15075 C CA  . THR F 2 86  ? 27.420  9.324   44.738  1.00 199.17 ? 86  THR F CA  1 
ATOM   15076 C C   . THR F 2 86  ? 27.731  10.680  45.352  1.00 217.69 ? 86  THR F C   1 
ATOM   15077 O O   . THR F 2 86  ? 28.477  10.743  46.331  1.00 207.76 ? 86  THR F O   1 
ATOM   15078 C CB  . THR F 2 86  ? 28.530  8.964   43.741  1.00 187.42 ? 86  THR F CB  1 
ATOM   15079 O OG1 . THR F 2 86  ? 28.025  8.034   42.776  1.00 184.17 ? 86  THR F OG1 1 
ATOM   15080 C CG2 . THR F 2 86  ? 29.706  8.328   44.468  1.00 178.91 ? 86  THR F CG2 1 
ATOM   15081 N N   . ALA F 2 87  ? 27.179  11.764  44.804  1.00 318.65 ? 87  ALA F N   1 
ATOM   15082 C CA  . ALA F 2 87  ? 27.430  13.107  45.307  1.00 320.95 ? 87  ALA F CA  1 
ATOM   15083 C C   . ALA F 2 87  ? 26.310  13.638  46.191  1.00 323.41 ? 87  ALA F C   1 
ATOM   15084 O O   . ALA F 2 87  ? 26.485  14.686  46.820  1.00 325.69 ? 87  ALA F O   1 
ATOM   15085 C CB  . ALA F 2 87  ? 27.656  14.076  44.139  1.00 320.03 ? 87  ALA F CB  1 
ATOM   15086 N N   . GLY F 2 88  ? 25.170  12.953  46.243  1.00 231.60 ? 88  GLY F N   1 
ATOM   15087 C CA  . GLY F 2 88  ? 24.051  13.371  47.054  1.00 210.53 ? 88  GLY F CA  1 
ATOM   15088 C C   . GLY F 2 88  ? 24.341  13.474  48.540  1.00 208.31 ? 88  GLY F C   1 
ATOM   15089 O O   . GLY F 2 88  ? 24.078  14.506  49.165  1.00 209.22 ? 88  GLY F O   1 
ATOM   15090 N N   . PRO F 2 89  ? 24.869  12.391  49.151  1.00 200.40 ? 89  PRO F N   1 
ATOM   15091 C CA  . PRO F 2 89  ? 25.192  12.440  50.586  1.00 200.29 ? 89  PRO F CA  1 
ATOM   15092 C C   . PRO F 2 89  ? 26.101  13.595  50.981  1.00 215.68 ? 89  PRO F C   1 
ATOM   15093 O O   . PRO F 2 89  ? 26.098  14.017  52.143  1.00 211.13 ? 89  PRO F O   1 
ATOM   15094 C CB  . PRO F 2 89  ? 25.873  11.088  50.831  1.00 181.03 ? 89  PRO F CB  1 
ATOM   15095 C CG  . PRO F 2 89  ? 25.236  10.185  49.843  1.00 178.47 ? 89  PRO F CG  1 
ATOM   15096 C CD  . PRO F 2 89  ? 24.993  11.023  48.614  1.00 193.68 ? 89  PRO F CD  1 
ATOM   15097 N N   . LEU F 2 90  ? 26.885  14.115  50.034  1.00 255.82 ? 90  LEU F N   1 
ATOM   15098 C CA  . LEU F 2 90  ? 27.709  15.282  50.327  1.00 257.23 ? 90  LEU F CA  1 
ATOM   15099 C C   . LEU F 2 90  ? 26.881  16.559  50.384  1.00 259.10 ? 90  LEU F C   1 
ATOM   15100 O O   . LEU F 2 90  ? 27.253  17.502  51.092  1.00 261.22 ? 90  LEU F O   1 
ATOM   15101 C CB  . LEU F 2 90  ? 28.831  15.428  49.295  1.00 255.36 ? 90  LEU F CB  1 
ATOM   15102 C CG  . LEU F 2 90  ? 30.002  14.439  49.357  1.00 253.05 ? 90  LEU F CG  1 
ATOM   15103 C CD1 . LEU F 2 90  ? 29.644  13.087  48.755  1.00 251.04 ? 90  LEU F CD1 1 
ATOM   15104 C CD2 . LEU F 2 90  ? 31.240  15.023  48.692  1.00 251.95 ? 90  LEU F CD2 1 
ATOM   15105 N N   . ALA F 2 91  ? 25.764  16.611  49.653  1.00 223.43 ? 91  ALA F N   1 
ATOM   15106 C CA  . ALA F 2 91  ? 24.913  17.796  49.690  1.00 207.68 ? 91  ALA F CA  1 
ATOM   15107 C C   . ALA F 2 91  ? 24.222  17.941  51.040  1.00 204.54 ? 91  ALA F C   1 
ATOM   15108 O O   . ALA F 2 91  ? 23.904  19.061  51.456  1.00 198.94 ? 91  ALA F O   1 
ATOM   15109 C CB  . ALA F 2 91  ? 23.880  17.739  48.565  1.00 193.94 ? 91  ALA F CB  1 
ATOM   15110 N N   . LEU F 2 92  ? 23.982  16.826  51.732  1.00 206.00 ? 92  LEU F N   1 
ATOM   15111 C CA  . LEU F 2 92  ? 23.339  16.874  53.039  1.00 204.90 ? 92  LEU F CA  1 
ATOM   15112 C C   . LEU F 2 92  ? 24.324  17.271  54.132  1.00 204.20 ? 92  LEU F C   1 
ATOM   15113 O O   . LEU F 2 92  ? 23.958  17.988  55.071  1.00 199.50 ? 92  LEU F O   1 
ATOM   15114 C CB  . LEU F 2 92  ? 22.703  15.519  53.357  1.00 202.54 ? 92  LEU F CB  1 
ATOM   15115 C CG  . LEU F 2 92  ? 21.922  15.359  54.663  1.00 200.53 ? 92  LEU F CG  1 
ATOM   15116 C CD1 . LEU F 2 92  ? 20.659  14.549  54.422  1.00 202.31 ? 92  LEU F CD1 1 
ATOM   15117 C CD2 . LEU F 2 92  ? 22.780  14.693  55.729  1.00 194.03 ? 92  LEU F CD2 1 
ATOM   15118 N N   . ALA F 2 93  ? 25.571  16.818  54.028  1.00 204.09 ? 93  ALA F N   1 
ATOM   15119 C CA  . ALA F 2 93  ? 26.586  17.065  55.043  1.00 196.94 ? 93  ALA F CA  1 
ATOM   15120 C C   . ALA F 2 93  ? 27.368  18.351  54.806  1.00 190.03 ? 93  ALA F C   1 
ATOM   15121 O O   . ALA F 2 93  ? 28.421  18.540  55.423  1.00 186.94 ? 93  ALA F O   1 
ATOM   15122 C CB  . ALA F 2 93  ? 27.551  15.879  55.121  1.00 197.31 ? 93  ALA F CB  1 
ATOM   15123 N N   . ARG F 2 94  ? 26.885  19.236  53.930  1.00 188.04 ? 94  ARG F N   1 
ATOM   15124 C CA  . ARG F 2 94  ? 27.587  20.490  53.685  1.00 182.08 ? 94  ARG F CA  1 
ATOM   15125 C C   . ARG F 2 94  ? 27.566  21.414  54.896  1.00 174.25 ? 94  ARG F C   1 
ATOM   15126 O O   . ARG F 2 94  ? 28.455  22.263  55.028  1.00 169.06 ? 94  ARG F O   1 
ATOM   15127 C CB  . ARG F 2 94  ? 26.982  21.209  52.477  1.00 181.37 ? 94  ARG F CB  1 
ATOM   15128 C CG  . ARG F 2 94  ? 25.583  21.752  52.713  1.00 176.19 ? 94  ARG F CG  1 
ATOM   15129 C CD  . ARG F 2 94  ? 25.389  23.090  52.019  1.00 173.03 ? 94  ARG F CD  1 
ATOM   15130 N NE  . ARG F 2 94  ? 25.457  22.967  50.566  1.00 177.46 ? 94  ARG F NE  1 
ATOM   15131 C CZ  . ARG F 2 94  ? 25.399  23.996  49.728  1.00 183.12 ? 94  ARG F CZ  1 
ATOM   15132 N NH1 . ARG F 2 94  ? 25.274  25.229  50.199  1.00 178.06 ? 94  ARG F NH1 1 
ATOM   15133 N NH2 . ARG F 2 94  ? 25.468  23.794  48.419  1.00 190.12 ? 94  ARG F NH2 1 
ATOM   15134 N N   . ASP F 2 95  ? 26.577  21.270  55.781  1.00 176.11 ? 95  ASP F N   1 
ATOM   15135 C CA  . ASP F 2 95  ? 26.499  22.134  56.954  1.00 175.16 ? 95  ASP F CA  1 
ATOM   15136 C C   . ASP F 2 95  ? 27.566  21.788  57.985  1.00 179.87 ? 95  ASP F C   1 
ATOM   15137 O O   . ASP F 2 95  ? 28.054  22.678  58.692  1.00 174.19 ? 95  ASP F O   1 
ATOM   15138 C CB  . ASP F 2 95  ? 25.104  22.042  57.576  1.00 173.63 ? 95  ASP F CB  1 
ATOM   15139 C CG  . ASP F 2 95  ? 24.603  20.614  57.676  1.00 178.15 ? 95  ASP F CG  1 
ATOM   15140 O OD1 . ASP F 2 95  ? 25.353  19.692  57.291  1.00 183.42 ? 95  ASP F OD1 1 
ATOM   15141 O OD2 . ASP F 2 95  ? 23.460  20.414  58.136  1.00 170.47 ? 95  ASP F OD2 1 
ATOM   15142 N N   . LYS F 2 96  ? 27.939  20.515  58.086  1.00 193.98 ? 96  LYS F N   1 
ATOM   15143 C CA  . LYS F 2 96  ? 28.963  20.070  59.023  1.00 194.21 ? 96  LYS F CA  1 
ATOM   15144 C C   . LYS F 2 96  ? 30.375  20.167  58.456  1.00 190.43 ? 96  LYS F C   1 
ATOM   15145 O O   . LYS F 2 96  ? 31.336  19.890  59.180  1.00 190.98 ? 96  LYS F O   1 
ATOM   15146 C CB  . LYS F 2 96  ? 28.684  18.625  59.457  1.00 199.44 ? 96  LYS F CB  1 
ATOM   15147 C CG  . LYS F 2 96  ? 27.361  18.427  60.187  1.00 197.21 ? 96  LYS F CG  1 
ATOM   15148 C CD  . LYS F 2 96  ? 27.326  19.190  61.499  1.00 197.17 ? 96  LYS F CD  1 
ATOM   15149 C CE  . LYS F 2 96  ? 28.372  18.659  62.468  1.00 200.76 ? 96  LYS F CE  1 
ATOM   15150 N NZ  . LYS F 2 96  ? 28.329  19.365  63.778  1.00 204.79 ? 96  LYS F NZ  1 
ATOM   15151 N N   . LEU F 2 97  ? 30.527  20.557  57.190  1.00 173.16 ? 97  LEU F N   1 
ATOM   15152 C CA  . LEU F 2 97  ? 31.840  20.643  56.564  1.00 168.95 ? 97  LEU F CA  1 
ATOM   15153 C C   . LEU F 2 97  ? 32.376  22.064  56.471  1.00 159.55 ? 97  LEU F C   1 
ATOM   15154 O O   . LEU F 2 97  ? 33.595  22.244  56.373  1.00 158.75 ? 97  LEU F O   1 
ATOM   15155 C CB  . LEU F 2 97  ? 31.800  20.037  55.153  1.00 169.47 ? 97  LEU F CB  1 
ATOM   15156 C CG  . LEU F 2 97  ? 31.692  18.514  55.051  1.00 170.47 ? 97  LEU F CG  1 
ATOM   15157 C CD1 . LEU F 2 97  ? 31.524  18.082  53.602  1.00 173.60 ? 97  LEU F CD1 1 
ATOM   15158 C CD2 . LEU F 2 97  ? 32.915  17.853  55.668  1.00 171.85 ? 97  LEU F CD2 1 
ATOM   15159 N N   . LEU F 2 98  ? 31.508  23.070  56.502  1.00 158.81 ? 98  LEU F N   1 
ATOM   15160 C CA  . LEU F 2 98  ? 31.926  24.463  56.394  1.00 152.56 ? 98  LEU F CA  1 
ATOM   15161 C C   . LEU F 2 98  ? 32.139  25.018  57.797  1.00 156.07 ? 98  LEU F C   1 
ATOM   15162 O O   . LEU F 2 98  ? 31.175  25.278  58.523  1.00 152.79 ? 98  LEU F O   1 
ATOM   15163 C CB  . LEU F 2 98  ? 30.888  25.279  55.629  1.00 146.93 ? 98  LEU F CB  1 
ATOM   15164 C CG  . LEU F 2 98  ? 30.589  24.791  54.212  1.00 143.98 ? 98  LEU F CG  1 
ATOM   15165 C CD1 . LEU F 2 98  ? 29.685  25.768  53.474  1.00 127.11 ? 98  LEU F CD1 1 
ATOM   15166 C CD2 . LEU F 2 98  ? 31.874  24.551  53.443  1.00 152.37 ? 98  LEU F CD2 1 
ATOM   15167 N N   . ASP F 2 99  ? 33.401  25.206  58.176  1.00 160.54 ? 99  ASP F N   1 
ATOM   15168 C CA  . ASP F 2 99  ? 33.734  25.805  59.460  1.00 161.84 ? 99  ASP F CA  1 
ATOM   15169 C C   . ASP F 2 99  ? 33.875  27.318  59.385  1.00 161.29 ? 99  ASP F C   1 
ATOM   15170 O O   . ASP F 2 99  ? 33.897  27.975  60.431  1.00 164.73 ? 99  ASP F O   1 
ATOM   15171 C CB  . ASP F 2 99  ? 35.037  25.210  60.005  1.00 166.22 ? 99  ASP F CB  1 
ATOM   15172 C CG  . ASP F 2 99  ? 36.196  25.361  59.036  1.00 167.54 ? 99  ASP F CG  1 
ATOM   15173 O OD1 . ASP F 2 99  ? 35.953  25.375  57.811  1.00 168.35 ? 99  ASP F OD1 1 
ATOM   15174 O OD2 . ASP F 2 99  ? 37.351  25.471  59.501  1.00 166.74 ? 99  ASP F OD2 1 
ATOM   15175 N N   . GLY F 2 100 ? 33.971  27.881  58.179  1.00 154.91 ? 100 GLY F N   1 
ATOM   15176 C CA  . GLY F 2 100 ? 34.126  29.303  57.972  1.00 153.61 ? 100 GLY F CA  1 
ATOM   15177 C C   . GLY F 2 100 ? 35.482  29.685  57.416  1.00 153.56 ? 100 GLY F C   1 
ATOM   15178 O O   . GLY F 2 100 ? 35.596  30.710  56.732  1.00 152.25 ? 100 GLY F O   1 
ATOM   15179 N N   . SER F 2 101 ? 36.513  28.884  57.696  1.00 160.84 ? 101 SER F N   1 
ATOM   15180 C CA  . SER F 2 101 ? 37.853  29.190  57.215  1.00 160.40 ? 101 SER F CA  1 
ATOM   15181 C C   . SER F 2 101 ? 38.016  28.904  55.729  1.00 168.45 ? 101 SER F C   1 
ATOM   15182 O O   . SER F 2 101 ? 38.986  29.373  55.125  1.00 167.50 ? 101 SER F O   1 
ATOM   15183 C CB  . SER F 2 101 ? 38.891  28.398  58.009  1.00 156.36 ? 101 SER F CB  1 
ATOM   15184 O OG  . SER F 2 101 ? 40.199  28.629  57.515  1.00 153.55 ? 101 SER F OG  1 
ATOM   15185 N N   . GLY F 2 102 ? 37.096  28.154  55.131  1.00 178.97 ? 102 GLY F N   1 
ATOM   15186 C CA  . GLY F 2 102 ? 37.173  27.832  53.720  1.00 183.67 ? 102 GLY F CA  1 
ATOM   15187 C C   . GLY F 2 102 ? 38.363  26.966  53.360  1.00 197.12 ? 102 GLY F C   1 
ATOM   15188 O O   . GLY F 2 102 ? 39.059  27.233  52.374  1.00 201.66 ? 102 GLY F O   1 
ATOM   15189 N N   . GLU F 2 103 ? 38.606  25.915  54.153  1.00 203.20 ? 103 GLU F N   1 
ATOM   15190 C CA  . GLU F 2 103 ? 39.703  24.999  53.884  1.00 202.95 ? 103 GLU F CA  1 
ATOM   15191 C C   . GLU F 2 103 ? 39.195  23.740  53.190  1.00 201.74 ? 103 GLU F C   1 
ATOM   15192 O O   . GLU F 2 103 ? 38.075  23.289  53.449  1.00 202.50 ? 103 GLU F O   1 
ATOM   15193 C CB  . GLU F 2 103 ? 40.420  24.614  55.183  1.00 200.91 ? 103 GLU F CB  1 
ATOM   15194 C CG  . GLU F 2 103 ? 41.306  25.713  55.748  1.00 199.32 ? 103 GLU F CG  1 
ATOM   15195 C CD  . GLU F 2 103 ? 42.654  25.798  55.055  1.00 199.08 ? 103 GLU F CD  1 
ATOM   15196 O OE1 . GLU F 2 103 ? 42.982  24.888  54.266  1.00 198.26 ? 103 GLU F OE1 1 
ATOM   15197 O OE2 . GLU F 2 103 ? 43.384  26.782  55.296  1.00 198.26 ? 103 GLU F OE2 1 
ATOM   15198 N N   . PRO F 2 104 ? 39.997  23.154  52.301  1.00 191.71 ? 104 PRO F N   1 
ATOM   15199 C CA  . PRO F 2 104 ? 39.558  21.939  51.602  1.00 182.35 ? 104 PRO F CA  1 
ATOM   15200 C C   . PRO F 2 104 ? 39.389  20.763  52.551  1.00 176.58 ? 104 PRO F C   1 
ATOM   15201 O O   . PRO F 2 104 ? 40.168  20.577  53.489  1.00 178.68 ? 104 PRO F O   1 
ATOM   15202 C CB  . PRO F 2 104 ? 40.684  21.682  50.593  1.00 180.62 ? 104 PRO F CB  1 
ATOM   15203 C CG  . PRO F 2 104 ? 41.872  22.391  51.157  1.00 185.37 ? 104 PRO F CG  1 
ATOM   15204 C CD  . PRO F 2 104 ? 41.325  23.604  51.847  1.00 191.60 ? 104 PRO F CD  1 
ATOM   15205 N N   . PHE F 2 105 ? 38.356  19.965  52.294  1.00 173.38 ? 105 PHE F N   1 
ATOM   15206 C CA  . PHE F 2 105 ? 38.070  18.771  53.074  1.00 168.05 ? 105 PHE F CA  1 
ATOM   15207 C C   . PHE F 2 105 ? 38.283  17.518  52.233  1.00 162.70 ? 105 PHE F C   1 
ATOM   15208 O O   . PHE F 2 105 ? 38.285  17.558  51.000  1.00 163.62 ? 105 PHE F O   1 
ATOM   15209 C CB  . PHE F 2 105 ? 36.637  18.799  53.624  1.00 168.42 ? 105 PHE F CB  1 
ATOM   15210 C CG  . PHE F 2 105 ? 35.580  19.020  52.576  1.00 167.78 ? 105 PHE F CG  1 
ATOM   15211 C CD1 . PHE F 2 105 ? 35.172  20.302  52.241  1.00 175.52 ? 105 PHE F CD1 1 
ATOM   15212 C CD2 . PHE F 2 105 ? 34.982  17.945  51.938  1.00 166.93 ? 105 PHE F CD2 1 
ATOM   15213 C CE1 . PHE F 2 105 ? 34.196  20.506  51.281  1.00 178.46 ? 105 PHE F CE1 1 
ATOM   15214 C CE2 . PHE F 2 105 ? 34.006  18.143  50.978  1.00 170.67 ? 105 PHE F CE2 1 
ATOM   15215 C CZ  . PHE F 2 105 ? 33.613  19.425  50.650  1.00 173.43 ? 105 PHE F CZ  1 
ATOM   15216 N N   . PHE F 2 106 ? 38.462  16.397  52.925  1.00 160.98 ? 106 PHE F N   1 
ATOM   15217 C CA  . PHE F 2 106 ? 38.695  15.104  52.300  1.00 162.07 ? 106 PHE F CA  1 
ATOM   15218 C C   . PHE F 2 106 ? 37.397  14.310  52.218  1.00 165.20 ? 106 PHE F C   1 
ATOM   15219 O O   . PHE F 2 106 ? 36.534  14.402  53.095  1.00 167.95 ? 106 PHE F O   1 
ATOM   15220 C CB  . PHE F 2 106 ? 39.730  14.293  53.084  1.00 162.17 ? 106 PHE F CB  1 
ATOM   15221 C CG  . PHE F 2 106 ? 41.139  14.790  52.940  1.00 160.03 ? 106 PHE F CG  1 
ATOM   15222 C CD1 . PHE F 2 106 ? 41.948  14.327  51.916  1.00 158.41 ? 106 PHE F CD1 1 
ATOM   15223 C CD2 . PHE F 2 106 ? 41.661  15.707  53.838  1.00 161.70 ? 106 PHE F CD2 1 
ATOM   15224 C CE1 . PHE F 2 106 ? 43.246  14.773  51.785  1.00 156.56 ? 106 PHE F CE1 1 
ATOM   15225 C CE2 . PHE F 2 106 ? 42.958  16.159  53.711  1.00 161.27 ? 106 PHE F CE2 1 
ATOM   15226 C CZ  . PHE F 2 106 ? 43.751  15.691  52.683  1.00 156.64 ? 106 PHE F CZ  1 
ATOM   15227 N N   . VAL F 2 107 ? 37.265  13.529  51.147  1.00 169.65 ? 107 VAL F N   1 
ATOM   15228 C CA  . VAL F 2 107 ? 36.140  12.618  50.963  1.00 168.88 ? 107 VAL F CA  1 
ATOM   15229 C C   . VAL F 2 107 ? 36.709  11.239  50.662  1.00 167.55 ? 107 VAL F C   1 
ATOM   15230 O O   . VAL F 2 107 ? 37.362  11.045  49.629  1.00 172.01 ? 107 VAL F O   1 
ATOM   15231 C CB  . VAL F 2 107 ? 35.191  13.073  49.843  1.00 172.09 ? 107 VAL F CB  1 
ATOM   15232 C CG1 . VAL F 2 107 ? 34.018  12.112  49.729  1.00 171.42 ? 107 VAL F CG1 1 
ATOM   15233 C CG2 . VAL F 2 107 ? 34.694  14.487  50.111  1.00 174.49 ? 107 VAL F CG2 1 
ATOM   15234 N N   . LEU F 2 108 ? 36.465  10.285  51.558  1.00 151.65 ? 108 LEU F N   1 
ATOM   15235 C CA  . LEU F 2 108 ? 37.035  8.951   51.462  1.00 143.88 ? 108 LEU F CA  1 
ATOM   15236 C C   . LEU F 2 108 ? 35.930  7.910   51.335  1.00 139.91 ? 108 LEU F C   1 
ATOM   15237 O O   . LEU F 2 108 ? 34.816  8.097   51.832  1.00 142.25 ? 108 LEU F O   1 
ATOM   15238 C CB  . LEU F 2 108 ? 37.906  8.629   52.684  1.00 145.43 ? 108 LEU F CB  1 
ATOM   15239 C CG  . LEU F 2 108 ? 39.042  9.603   53.006  1.00 150.56 ? 108 LEU F CG  1 
ATOM   15240 C CD1 . LEU F 2 108 ? 39.762  9.179   54.277  1.00 147.23 ? 108 LEU F CD1 1 
ATOM   15241 C CD2 . LEU F 2 108 ? 40.015  9.698   51.843  1.00 149.60 ? 108 LEU F CD2 1 
ATOM   15242 N N   . ASN F 2 109 ? 36.252  6.810   50.661  1.00 139.65 ? 109 ASN F N   1 
ATOM   15243 C CA  . ASN F 2 109 ? 35.349  5.677   50.521  1.00 140.11 ? 109 ASN F CA  1 
ATOM   15244 C C   . ASN F 2 109 ? 35.789  4.558   51.457  1.00 143.02 ? 109 ASN F C   1 
ATOM   15245 O O   . ASN F 2 109 ? 36.984  4.275   51.587  1.00 139.50 ? 109 ASN F O   1 
ATOM   15246 C CB  . ASN F 2 109 ? 35.320  5.176   49.073  1.00 136.83 ? 109 ASN F CB  1 
ATOM   15247 C CG  . ASN F 2 109 ? 34.151  4.243   48.794  1.00 132.73 ? 109 ASN F CG  1 
ATOM   15248 O OD1 . ASN F 2 109 ? 33.655  3.556   49.687  1.00 136.33 ? 109 ASN F OD1 1 
ATOM   15249 N ND2 . ASN F 2 109 ? 33.710  4.212   47.541  1.00 126.26 ? 109 ASN F ND2 1 
ATOM   15250 N N   . SER F 2 110 ? 34.813  3.925   52.111  1.00 166.28 ? 110 SER F N   1 
ATOM   15251 C CA  . SER F 2 110 ? 35.116  2.862   53.062  1.00 166.30 ? 110 SER F CA  1 
ATOM   15252 C C   . SER F 2 110 ? 35.531  1.564   52.382  1.00 164.16 ? 110 SER F C   1 
ATOM   15253 O O   . SER F 2 110 ? 36.080  0.680   53.048  1.00 164.15 ? 110 SER F O   1 
ATOM   15254 C CB  . SER F 2 110 ? 33.907  2.611   53.965  1.00 167.95 ? 110 SER F CB  1 
ATOM   15255 O OG  . SER F 2 110 ? 34.190  1.614   54.930  1.00 167.75 ? 110 SER F OG  1 
ATOM   15256 N N   . ASP F 2 111 ? 35.281  1.425   51.080  1.00 144.11 ? 111 ASP F N   1 
ATOM   15257 C CA  . ASP F 2 111 ? 35.558  0.193   50.355  1.00 140.64 ? 111 ASP F CA  1 
ATOM   15258 C C   . ASP F 2 111 ? 36.927  0.195   49.680  1.00 145.44 ? 111 ASP F C   1 
ATOM   15259 O O   . ASP F 2 111 ? 37.162  -0.619  48.779  1.00 152.38 ? 111 ASP F O   1 
ATOM   15260 C CB  . ASP F 2 111 ? 34.465  -0.056  49.313  1.00 139.11 ? 111 ASP F CB  1 
ATOM   15261 C CG  . ASP F 2 111 ? 33.072  -0.011  49.907  1.00 134.96 ? 111 ASP F CG  1 
ATOM   15262 O OD1 . ASP F 2 111 ? 32.938  0.380   51.086  1.00 136.51 ? 111 ASP F OD1 1 
ATOM   15263 O OD2 . ASP F 2 111 ? 32.108  -0.359  49.193  1.00 129.05 ? 111 ASP F OD2 1 
ATOM   15264 N N   . VAL F 2 112 ? 37.831  1.083   50.091  1.00 145.84 ? 112 VAL F N   1 
ATOM   15265 C CA  . VAL F 2 112 ? 39.136  1.235   49.457  1.00 150.45 ? 112 VAL F CA  1 
ATOM   15266 C C   . VAL F 2 112 ? 40.213  1.236   50.534  1.00 152.87 ? 112 VAL F C   1 
ATOM   15267 O O   . VAL F 2 112 ? 40.007  1.765   51.631  1.00 151.71 ? 112 VAL F O   1 
ATOM   15268 C CB  . VAL F 2 112 ? 39.214  2.526   48.610  1.00 150.89 ? 112 VAL F CB  1 
ATOM   15269 C CG1 . VAL F 2 112 ? 40.510  2.571   47.820  1.00 164.22 ? 112 VAL F CG1 1 
ATOM   15270 C CG2 . VAL F 2 112 ? 38.017  2.632   47.674  1.00 148.89 ? 112 VAL F CG2 1 
ATOM   15271 N N   . ILE F 2 113 ? 41.362  0.634   50.218  1.00 161.96 ? 113 ILE F N   1 
ATOM   15272 C CA  . ILE F 2 113 ? 42.533  0.656   51.084  1.00 165.31 ? 113 ILE F CA  1 
ATOM   15273 C C   . ILE F 2 113 ? 43.728  1.158   50.287  1.00 166.78 ? 113 ILE F C   1 
ATOM   15274 O O   . ILE F 2 113 ? 43.820  0.955   49.072  1.00 170.54 ? 113 ILE F O   1 
ATOM   15275 C CB  . ILE F 2 113 ? 42.828  -0.736  51.684  1.00 168.47 ? 113 ILE F CB  1 
ATOM   15276 C CG1 . ILE F 2 113 ? 42.886  -1.791  50.577  1.00 166.71 ? 113 ILE F CG1 1 
ATOM   15277 C CG2 . ILE F 2 113 ? 41.777  -1.103  52.720  1.00 171.57 ? 113 ILE F CG2 1 
ATOM   15278 C CD1 . ILE F 2 113 ? 43.309  -3.163  51.053  1.00 167.26 ? 113 ILE F CD1 1 
ATOM   15279 N N   . SER F 2 114 ? 44.654  1.806   50.983  1.00 155.34 ? 114 SER F N   1 
ATOM   15280 C CA  . SER F 2 114 ? 45.860  2.377   50.380  1.00 154.84 ? 114 SER F CA  1 
ATOM   15281 C C   . SER F 2 114 ? 46.814  2.759   51.510  1.00 151.82 ? 114 SER F C   1 
ATOM   15282 O O   . SER F 2 114 ? 46.576  2.439   52.681  1.00 152.18 ? 114 SER F O   1 
ATOM   15283 C CB  . SER F 2 114 ? 45.521  3.569   49.482  1.00 159.30 ? 114 SER F CB  1 
ATOM   15284 O OG  . SER F 2 114 ? 45.043  4.661   50.248  1.00 160.60 ? 114 SER F OG  1 
ATOM   15285 N N   . GLU F 2 115 ? 47.910  3.434   51.152  1.00 145.67 ? 115 GLU F N   1 
ATOM   15286 C CA  . GLU F 2 115 ? 48.880  3.914   52.128  1.00 143.89 ? 115 GLU F CA  1 
ATOM   15287 C C   . GLU F 2 115 ? 48.515  5.271   52.716  1.00 146.08 ? 115 GLU F C   1 
ATOM   15288 O O   . GLU F 2 115 ? 49.053  5.641   53.767  1.00 146.95 ? 115 GLU F O   1 
ATOM   15289 C CB  . GLU F 2 115 ? 50.272  3.983   51.495  1.00 145.31 ? 115 GLU F CB  1 
ATOM   15290 C CG  . GLU F 2 115 ? 50.680  2.712   50.761  1.00 150.05 ? 115 GLU F CG  1 
ATOM   15291 C CD  . GLU F 2 115 ? 52.149  2.694   50.390  1.00 153.32 ? 115 GLU F CD  1 
ATOM   15292 O OE1 . GLU F 2 115 ? 52.759  3.780   50.318  1.00 153.91 ? 115 GLU F OE1 1 
ATOM   15293 O OE2 . GLU F 2 115 ? 52.691  1.592   50.165  1.00 151.49 ? 115 GLU F OE2 1 
ATOM   15294 N N   . TYR F 2 116 ? 47.613  6.010   52.067  1.00 146.13 ? 116 TYR F N   1 
ATOM   15295 C CA  . TYR F 2 116 ? 47.095  7.299   52.516  1.00 146.86 ? 116 TYR F CA  1 
ATOM   15296 C C   . TYR F 2 116 ? 48.193  8.305   52.845  1.00 147.16 ? 116 TYR F C   1 
ATOM   15297 O O   . TYR F 2 116 ? 48.466  8.570   54.023  1.00 147.92 ? 116 TYR F O   1 
ATOM   15298 C CB  . TYR F 2 116 ? 46.175  7.093   53.718  1.00 149.00 ? 116 TYR F CB  1 
ATOM   15299 C CG  . TYR F 2 116 ? 44.979  6.234   53.388  1.00 152.07 ? 116 TYR F CG  1 
ATOM   15300 C CD1 . TYR F 2 116 ? 43.875  6.776   52.745  1.00 152.71 ? 116 TYR F CD1 1 
ATOM   15301 C CD2 . TYR F 2 116 ? 44.963  4.880   53.690  1.00 151.90 ? 116 TYR F CD2 1 
ATOM   15302 C CE1 . TYR F 2 116 ? 42.779  5.999   52.432  1.00 148.90 ? 116 TYR F CE1 1 
ATOM   15303 C CE2 . TYR F 2 116 ? 43.869  4.090   53.378  1.00 149.28 ? 116 TYR F CE2 1 
ATOM   15304 C CZ  . TYR F 2 116 ? 42.781  4.657   52.747  1.00 148.39 ? 116 TYR F CZ  1 
ATOM   15305 O OH  . TYR F 2 116 ? 41.687  3.883   52.434  1.00 146.42 ? 116 TYR F OH  1 
ATOM   15306 N N   . PRO F 2 117 ? 48.845  8.880   51.836  1.00 146.93 ? 117 PRO F N   1 
ATOM   15307 C CA  . PRO F 2 117 ? 49.790  9.990   52.073  1.00 151.69 ? 117 PRO F CA  1 
ATOM   15308 C C   . PRO F 2 117 ? 49.074  11.338  52.052  1.00 157.18 ? 117 PRO F C   1 
ATOM   15309 O O   . PRO F 2 117 ? 49.258  12.178  51.162  1.00 162.55 ? 117 PRO F O   1 
ATOM   15310 C CB  . PRO F 2 117 ? 50.779  9.822   50.919  1.00 152.76 ? 117 PRO F CB  1 
ATOM   15311 C CG  . PRO F 2 117 ? 49.921  9.317   49.800  1.00 156.44 ? 117 PRO F CG  1 
ATOM   15312 C CD  . PRO F 2 117 ? 48.854  8.446   50.428  1.00 148.50 ? 117 PRO F CD  1 
ATOM   15313 N N   . LEU F 2 118 ? 48.224  11.556  53.059  1.00 161.44 ? 118 LEU F N   1 
ATOM   15314 C CA  . LEU F 2 118 ? 47.396  12.757  53.082  1.00 167.83 ? 118 LEU F CA  1 
ATOM   15315 C C   . LEU F 2 118 ? 48.215  14.010  53.365  1.00 181.00 ? 118 LEU F C   1 
ATOM   15316 O O   . LEU F 2 118 ? 47.834  15.105  52.937  1.00 179.11 ? 118 LEU F O   1 
ATOM   15317 C CB  . LEU F 2 118 ? 46.282  12.601  54.118  1.00 168.66 ? 118 LEU F CB  1 
ATOM   15318 C CG  . LEU F 2 118 ? 45.336  11.417  53.910  1.00 159.54 ? 118 LEU F CG  1 
ATOM   15319 C CD1 . LEU F 2 118 ? 44.319  11.338  55.036  1.00 164.58 ? 118 LEU F CD1 1 
ATOM   15320 C CD2 . LEU F 2 118 ? 44.641  11.512  52.560  1.00 152.17 ? 118 LEU F CD2 1 
ATOM   15321 N N   . LYS F 2 119 ? 49.333  13.876  54.084  1.00 192.40 ? 119 LYS F N   1 
ATOM   15322 C CA  . LYS F 2 119 ? 50.134  15.044  54.441  1.00 196.23 ? 119 LYS F CA  1 
ATOM   15323 C C   . LYS F 2 119 ? 50.717  15.718  53.206  1.00 195.22 ? 119 LYS F C   1 
ATOM   15324 O O   . LYS F 2 119 ? 50.548  16.926  53.004  1.00 190.41 ? 119 LYS F O   1 
ATOM   15325 C CB  . LYS F 2 119 ? 51.252  14.639  55.402  1.00 201.71 ? 119 LYS F CB  1 
ATOM   15326 C CG  . LYS F 2 119 ? 50.769  14.128  56.742  1.00 206.49 ? 119 LYS F CG  1 
ATOM   15327 C CD  . LYS F 2 119 ? 51.682  14.612  57.854  1.00 209.63 ? 119 LYS F CD  1 
ATOM   15328 C CE  . LYS F 2 119 ? 51.719  16.130  57.893  1.00 214.36 ? 119 LYS F CE  1 
ATOM   15329 N NZ  . LYS F 2 119 ? 50.366  16.718  58.081  1.00 222.93 ? 119 LYS F NZ  1 
ATOM   15330 N N   . GLU F 2 120 ? 51.409  14.952  52.370  1.00 223.30 ? 120 GLU F N   1 
ATOM   15331 C CA  . GLU F 2 120 ? 52.064  15.490  51.185  1.00 222.35 ? 120 GLU F CA  1 
ATOM   15332 C C   . GLU F 2 120 ? 51.094  15.749  50.038  1.00 221.78 ? 120 GLU F C   1 
ATOM   15333 O O   . GLU F 2 120 ? 51.538  16.035  48.921  1.00 220.58 ? 120 GLU F O   1 
ATOM   15334 C CB  . GLU F 2 120 ? 53.183  14.543  50.745  1.00 228.09 ? 120 GLU F CB  1 
ATOM   15335 C CG  . GLU F 2 120 ? 54.249  14.353  51.818  1.00 230.86 ? 120 GLU F CG  1 
ATOM   15336 C CD  . GLU F 2 120 ? 55.371  13.433  51.385  1.00 237.82 ? 120 GLU F CD  1 
ATOM   15337 O OE1 . GLU F 2 120 ? 55.311  12.912  50.252  1.00 241.80 ? 120 GLU F OE1 1 
ATOM   15338 O OE2 . GLU F 2 120 ? 56.313  13.229  52.180  1.00 236.98 ? 120 GLU F OE2 1 
ATOM   15339 N N   . MET F 2 121 ? 49.788  15.658  50.290  1.00 188.45 ? 121 MET F N   1 
ATOM   15340 C CA  . MET F 2 121 ? 48.786  16.051  49.310  1.00 176.52 ? 121 MET F CA  1 
ATOM   15341 C C   . MET F 2 121 ? 48.349  17.499  49.483  1.00 175.25 ? 121 MET F C   1 
ATOM   15342 O O   . MET F 2 121 ? 48.027  18.164  48.492  1.00 171.19 ? 121 MET F O   1 
ATOM   15343 C CB  . MET F 2 121 ? 47.568  15.128  49.404  1.00 169.82 ? 121 MET F CB  1 
ATOM   15344 C CG  . MET F 2 121 ? 46.592  15.269  48.250  1.00 163.85 ? 121 MET F CG  1 
ATOM   15345 S SD  . MET F 2 121 ? 45.121  14.245  48.451  1.00 148.27 ? 121 MET F SD  1 
ATOM   15346 C CE  . MET F 2 121 ? 45.844  12.708  49.018  1.00 149.60 ? 121 MET F CE  1 
ATOM   15347 N N   . LEU F 2 122 ? 48.328  17.999  50.723  1.00 174.21 ? 122 LEU F N   1 
ATOM   15348 C CA  . LEU F 2 122 ? 48.042  19.412  50.947  1.00 170.37 ? 122 LEU F CA  1 
ATOM   15349 C C   . LEU F 2 122 ? 49.113  20.289  50.316  1.00 172.80 ? 122 LEU F C   1 
ATOM   15350 O O   . LEU F 2 122 ? 48.807  21.332  49.726  1.00 171.55 ? 122 LEU F O   1 
ATOM   15351 C CB  . LEU F 2 122 ? 47.931  19.706  52.444  1.00 166.09 ? 122 LEU F CB  1 
ATOM   15352 C CG  . LEU F 2 122 ? 46.605  19.431  53.156  1.00 163.44 ? 122 LEU F CG  1 
ATOM   15353 C CD1 . LEU F 2 122 ? 46.332  17.942  53.274  1.00 167.15 ? 122 LEU F CD1 1 
ATOM   15354 C CD2 . LEU F 2 122 ? 46.597  20.090  54.526  1.00 163.07 ? 122 LEU F CD2 1 
ATOM   15355 N N   . GLU F 2 123 ? 50.381  19.889  50.445  1.00 176.09 ? 123 GLU F N   1 
ATOM   15356 C CA  . GLU F 2 123 ? 51.452  20.599  49.757  1.00 174.68 ? 123 GLU F CA  1 
ATOM   15357 C C   . GLU F 2 123 ? 51.298  20.496  48.246  1.00 172.44 ? 123 GLU F C   1 
ATOM   15358 O O   . GLU F 2 123 ? 51.635  21.439  47.521  1.00 173.38 ? 123 GLU F O   1 
ATOM   15359 C CB  . GLU F 2 123 ? 52.811  20.056  50.201  1.00 177.62 ? 123 GLU F CB  1 
ATOM   15360 C CG  . GLU F 2 123 ? 53.996  20.887  49.740  1.00 177.69 ? 123 GLU F CG  1 
ATOM   15361 C CD  . GLU F 2 123 ? 55.315  20.366  50.274  1.00 179.58 ? 123 GLU F CD  1 
ATOM   15362 O OE1 . GLU F 2 123 ? 55.375  19.179  50.660  1.00 178.96 ? 123 GLU F OE1 1 
ATOM   15363 O OE2 . GLU F 2 123 ? 56.293  21.143  50.311  1.00 185.58 ? 123 GLU F OE2 1 
ATOM   15364 N N   . PHE F 2 124 ? 50.793  19.363  47.752  1.00 172.79 ? 124 PHE F N   1 
ATOM   15365 C CA  . PHE F 2 124 ? 50.445  19.259  46.340  1.00 169.63 ? 124 PHE F CA  1 
ATOM   15366 C C   . PHE F 2 124 ? 49.242  20.125  45.989  1.00 169.19 ? 124 PHE F C   1 
ATOM   15367 O O   . PHE F 2 124 ? 48.996  20.378  44.806  1.00 168.50 ? 124 PHE F O   1 
ATOM   15368 C CB  . PHE F 2 124 ? 50.175  17.797  45.972  1.00 166.21 ? 124 PHE F CB  1 
ATOM   15369 C CG  . PHE F 2 124 ? 49.985  17.562  44.499  1.00 162.66 ? 124 PHE F CG  1 
ATOM   15370 C CD1 . PHE F 2 124 ? 51.000  17.849  43.600  1.00 161.82 ? 124 PHE F CD1 1 
ATOM   15371 C CD2 . PHE F 2 124 ? 48.795  17.046  44.016  1.00 161.49 ? 124 PHE F CD2 1 
ATOM   15372 C CE1 . PHE F 2 124 ? 50.826  17.629  42.245  1.00 160.52 ? 124 PHE F CE1 1 
ATOM   15373 C CE2 . PHE F 2 124 ? 48.618  16.824  42.664  1.00 157.52 ? 124 PHE F CE2 1 
ATOM   15374 C CZ  . PHE F 2 124 ? 49.633  17.116  41.777  1.00 155.55 ? 124 PHE F CZ  1 
ATOM   15375 N N   . HIS F 2 125 ? 48.494  20.585  46.991  1.00 171.14 ? 125 HIS F N   1 
ATOM   15376 C CA  . HIS F 2 125 ? 47.373  21.495  46.798  1.00 172.52 ? 125 HIS F CA  1 
ATOM   15377 C C   . HIS F 2 125 ? 47.753  22.957  46.990  1.00 169.91 ? 125 HIS F C   1 
ATOM   15378 O O   . HIS F 2 125 ? 47.288  23.819  46.238  1.00 167.70 ? 125 HIS F O   1 
ATOM   15379 C CB  . HIS F 2 125 ? 46.239  21.141  47.764  1.00 175.99 ? 125 HIS F CB  1 
ATOM   15380 C CG  . HIS F 2 125 ? 44.987  21.930  47.534  1.00 177.48 ? 125 HIS F CG  1 
ATOM   15381 N ND1 . HIS F 2 125 ? 44.115  21.659  46.502  1.00 175.34 ? 125 HIS F ND1 1 
ATOM   15382 C CD2 . HIS F 2 125 ? 44.464  22.985  48.202  1.00 178.00 ? 125 HIS F CD2 1 
ATOM   15383 C CE1 . HIS F 2 125 ? 43.106  22.511  46.546  1.00 176.89 ? 125 HIS F CE1 1 
ATOM   15384 N NE2 . HIS F 2 125 ? 43.294  23.326  47.568  1.00 178.87 ? 125 HIS F NE2 1 
ATOM   15385 N N   . LYS F 2 126 ? 48.591  23.256  47.982  1.00 171.65 ? 126 LYS F N   1 
ATOM   15386 C CA  . LYS F 2 126 ? 48.990  24.620  48.293  1.00 172.05 ? 126 LYS F CA  1 
ATOM   15387 C C   . LYS F 2 126 ? 50.183  25.089  47.468  1.00 168.98 ? 126 LYS F C   1 
ATOM   15388 O O   . LYS F 2 126 ? 50.851  26.056  47.853  1.00 167.34 ? 126 LYS F O   1 
ATOM   15389 C CB  . LYS F 2 126 ? 49.302  24.742  49.787  1.00 170.83 ? 126 LYS F CB  1 
ATOM   15390 C CG  . LYS F 2 126 ? 48.087  24.557  50.685  1.00 168.84 ? 126 LYS F CG  1 
ATOM   15391 C CD  . LYS F 2 126 ? 48.430  24.806  52.146  1.00 164.80 ? 126 LYS F CD  1 
ATOM   15392 C CE  . LYS F 2 126 ? 47.196  24.702  53.028  1.00 164.38 ? 126 LYS F CE  1 
ATOM   15393 N NZ  . LYS F 2 126 ? 47.500  25.015  54.452  1.00 169.61 ? 126 LYS F NZ  1 
ATOM   15394 N N   . SER F 2 127 ? 50.463  24.433  46.345  1.00 167.53 ? 127 SER F N   1 
ATOM   15395 C CA  . SER F 2 127 ? 51.568  24.805  45.472  1.00 169.33 ? 127 SER F CA  1 
ATOM   15396 C C   . SER F 2 127 ? 51.105  25.471  44.186  1.00 168.81 ? 127 SER F C   1 
ATOM   15397 O O   . SER F 2 127 ? 51.570  26.565  43.853  1.00 168.51 ? 127 SER F O   1 
ATOM   15398 C CB  . SER F 2 127 ? 52.416  23.568  45.139  1.00 169.44 ? 127 SER F CB  1 
ATOM   15399 O OG  . SER F 2 127 ? 53.525  23.914  44.329  1.00 169.16 ? 127 SER F OG  1 
ATOM   15400 N N   . HIS F 2 128 ? 50.198  24.833  43.449  1.00 168.13 ? 128 HIS F N   1 
ATOM   15401 C CA  . HIS F 2 128 ? 49.656  25.398  42.220  1.00 172.20 ? 128 HIS F CA  1 
ATOM   15402 C C   . HIS F 2 128 ? 48.348  26.150  42.430  1.00 174.34 ? 128 HIS F C   1 
ATOM   15403 O O   . HIS F 2 128 ? 47.917  26.873  41.525  1.00 174.22 ? 128 HIS F O   1 
ATOM   15404 C CB  . HIS F 2 128 ? 49.452  24.292  41.177  1.00 173.95 ? 128 HIS F CB  1 
ATOM   15405 C CG  . HIS F 2 128 ? 48.637  23.135  41.667  1.00 171.68 ? 128 HIS F CG  1 
ATOM   15406 N ND1 . HIS F 2 128 ? 47.908  23.176  42.836  1.00 171.97 ? 128 HIS F ND1 1 
ATOM   15407 C CD2 . HIS F 2 128 ? 48.438  21.903  41.144  1.00 169.30 ? 128 HIS F CD2 1 
ATOM   15408 C CE1 . HIS F 2 128 ? 47.295  22.021  43.011  1.00 171.00 ? 128 HIS F CE1 1 
ATOM   15409 N NE2 . HIS F 2 128 ? 47.601  21.230  41.999  1.00 171.14 ? 128 HIS F NE2 1 
ATOM   15410 N N   . GLY F 2 129 ? 47.707  25.994  43.586  1.00 173.39 ? 129 GLY F N   1 
ATOM   15411 C CA  . GLY F 2 129 ? 46.476  26.708  43.861  1.00 172.36 ? 129 GLY F CA  1 
ATOM   15412 C C   . GLY F 2 129 ? 45.240  26.168  43.174  1.00 169.81 ? 129 GLY F C   1 
ATOM   15413 O O   . GLY F 2 129 ? 44.345  26.945  42.834  1.00 170.28 ? 129 GLY F O   1 
ATOM   15414 N N   . GLY F 2 130 ? 45.162  24.858  42.956  1.00 168.40 ? 130 GLY F N   1 
ATOM   15415 C CA  . GLY F 2 130 ? 43.991  24.274  42.334  1.00 169.84 ? 130 GLY F CA  1 
ATOM   15416 C C   . GLY F 2 130 ? 42.755  24.372  43.214  1.00 174.53 ? 130 GLY F C   1 
ATOM   15417 O O   . GLY F 2 130 ? 42.796  24.802  44.370  1.00 176.53 ? 130 GLY F O   1 
ATOM   15418 N N   . GLU F 2 131 ? 41.624  23.954  42.645  1.00 176.21 ? 131 GLU F N   1 
ATOM   15419 C CA  . GLU F 2 131 ? 40.348  23.960  43.352  1.00 173.37 ? 131 GLU F CA  1 
ATOM   15420 C C   . GLU F 2 131 ? 39.931  22.583  43.851  1.00 176.08 ? 131 GLU F C   1 
ATOM   15421 O O   . GLU F 2 131 ? 39.471  22.458  44.990  1.00 177.91 ? 131 GLU F O   1 
ATOM   15422 C CB  . GLU F 2 131 ? 39.238  24.515  42.454  1.00 165.32 ? 131 GLU F CB  1 
ATOM   15423 C CG  . GLU F 2 131 ? 37.887  24.621  43.142  1.00 158.67 ? 131 GLU F CG  1 
ATOM   15424 C CD  . GLU F 2 131 ? 36.736  24.702  42.159  1.00 152.07 ? 131 GLU F CD  1 
ATOM   15425 O OE1 . GLU F 2 131 ? 36.986  24.612  40.938  1.00 153.29 ? 131 GLU F OE1 1 
ATOM   15426 O OE2 . GLU F 2 131 ? 35.581  24.850  42.608  1.00 152.46 ? 131 GLU F OE2 1 
ATOM   15427 N N   . ALA F 2 132 ? 40.088  21.542  43.035  1.00 174.61 ? 132 ALA F N   1 
ATOM   15428 C CA  . ALA F 2 132 ? 39.659  20.198  43.391  1.00 184.00 ? 132 ALA F CA  1 
ATOM   15429 C C   . ALA F 2 132 ? 40.779  19.210  43.103  1.00 196.56 ? 132 ALA F C   1 
ATOM   15430 O O   . ALA F 2 132 ? 41.540  19.370  42.145  1.00 188.45 ? 132 ALA F O   1 
ATOM   15431 C CB  . ALA F 2 132 ? 38.395  19.787  42.625  1.00 173.27 ? 132 ALA F CB  1 
ATOM   15432 N N   . SER F 2 133 ? 40.869  18.181  43.946  1.00 252.38 ? 133 SER F N   1 
ATOM   15433 C CA  . SER F 2 133 ? 41.924  17.183  43.841  1.00 250.53 ? 133 SER F CA  1 
ATOM   15434 C C   . SER F 2 133 ? 41.345  15.792  44.034  1.00 249.40 ? 133 SER F C   1 
ATOM   15435 O O   . SER F 2 133 ? 40.542  15.571  44.946  1.00 250.66 ? 133 SER F O   1 
ATOM   15436 C CB  . SER F 2 133 ? 43.026  17.434  44.874  1.00 251.49 ? 133 SER F CB  1 
ATOM   15437 O OG  . SER F 2 133 ? 44.078  16.493  44.731  1.00 249.71 ? 133 SER F OG  1 
ATOM   15438 N N   . ILE F 2 134 ? 41.755  14.859  43.174  1.00 267.64 ? 134 ILE F N   1 
ATOM   15439 C CA  . ILE F 2 134 ? 41.437  13.446  43.322  1.00 266.55 ? 134 ILE F CA  1 
ATOM   15440 C C   . ILE F 2 134 ? 42.739  12.654  43.283  1.00 264.34 ? 134 ILE F C   1 
ATOM   15441 O O   . ILE F 2 134 ? 43.793  13.162  42.896  1.00 263.57 ? 134 ILE F O   1 
ATOM   15442 C CB  . ILE F 2 134 ? 40.463  12.937  42.236  1.00 264.04 ? 134 ILE F CB  1 
ATOM   15443 C CG1 . ILE F 2 134 ? 41.144  12.935  40.865  1.00 261.74 ? 134 ILE F CG1 1 
ATOM   15444 C CG2 . ILE F 2 134 ? 39.199  13.780  42.211  1.00 264.88 ? 134 ILE F CG2 1 
ATOM   15445 C CD1 . ILE F 2 134 ? 40.300  12.323  39.770  1.00 258.59 ? 134 ILE F CD1 1 
ATOM   15446 N N   . MET F 2 135 ? 42.651  11.392  43.691  1.00 208.38 ? 135 MET F N   1 
ATOM   15447 C CA  . MET F 2 135 ? 43.772  10.465  43.647  1.00 181.17 ? 135 MET F CA  1 
ATOM   15448 C C   . MET F 2 135 ? 43.517  9.408   42.583  1.00 170.08 ? 135 MET F C   1 
ATOM   15449 O O   . MET F 2 135 ? 42.374  8.990   42.369  1.00 170.39 ? 135 MET F O   1 
ATOM   15450 C CB  . MET F 2 135 ? 43.997  9.797   45.005  1.00 168.81 ? 135 MET F CB  1 
ATOM   15451 C CG  . MET F 2 135 ? 44.544  10.721  46.078  1.00 163.90 ? 135 MET F CG  1 
ATOM   15452 S SD  . MET F 2 135 ? 46.095  11.491  45.581  1.00 162.98 ? 135 MET F SD  1 
ATOM   15453 C CE  . MET F 2 135 ? 47.164  10.058  45.499  1.00 169.22 ? 135 MET F CE  1 
ATOM   15454 N N   . VAL F 2 136 ? 44.587  8.979   41.922  1.00 163.40 ? 136 VAL F N   1 
ATOM   15455 C CA  . VAL F 2 136 ? 44.504  8.094   40.769  1.00 154.79 ? 136 VAL F CA  1 
ATOM   15456 C C   . VAL F 2 136 ? 45.531  6.982   40.930  1.00 156.90 ? 136 VAL F C   1 
ATOM   15457 O O   . VAL F 2 136 ? 46.669  7.230   41.341  1.00 164.61 ? 136 VAL F O   1 
ATOM   15458 C CB  . VAL F 2 136 ? 44.732  8.871   39.454  1.00 150.87 ? 136 VAL F CB  1 
ATOM   15459 C CG1 . VAL F 2 136 ? 44.838  7.924   38.284  1.00 150.20 ? 136 VAL F CG1 1 
ATOM   15460 C CG2 . VAL F 2 136 ? 43.605  9.869   39.224  1.00 163.93 ? 136 VAL F CG2 1 
ATOM   15461 N N   . THR F 2 137 ? 45.129  5.756   40.603  1.00 157.94 ? 137 THR F N   1 
ATOM   15462 C CA  . THR F 2 137 ? 46.007  4.598   40.674  1.00 162.91 ? 137 THR F CA  1 
ATOM   15463 C C   . THR F 2 137 ? 45.996  3.869   39.340  1.00 170.54 ? 137 THR F C   1 
ATOM   15464 O O   . THR F 2 137 ? 44.970  3.823   38.656  1.00 166.64 ? 137 THR F O   1 
ATOM   15465 C CB  . THR F 2 137 ? 45.590  3.639   41.795  1.00 169.54 ? 137 THR F CB  1 
ATOM   15466 O OG1 . THR F 2 137 ? 46.389  2.451   41.730  1.00 167.85 ? 137 THR F OG1 1 
ATOM   15467 C CG2 . THR F 2 137 ? 44.120  3.268   41.664  1.00 178.85 ? 137 THR F CG2 1 
ATOM   15468 N N   . LYS F 2 138 ? 47.147  3.314   38.970  1.00 193.30 ? 138 LYS F N   1 
ATOM   15469 C CA  . LYS F 2 138 ? 47.262  2.560   37.730  1.00 192.29 ? 138 LYS F CA  1 
ATOM   15470 C C   . LYS F 2 138 ? 46.682  1.161   37.896  1.00 192.09 ? 138 LYS F C   1 
ATOM   15471 O O   . LYS F 2 138 ? 46.862  0.515   38.933  1.00 194.56 ? 138 LYS F O   1 
ATOM   15472 C CB  . LYS F 2 138 ? 48.725  2.481   37.288  1.00 193.11 ? 138 LYS F CB  1 
ATOM   15473 C CG  . LYS F 2 138 ? 49.694  2.032   38.374  1.00 194.53 ? 138 LYS F CG  1 
ATOM   15474 C CD  . LYS F 2 138 ? 51.043  1.639   37.786  1.00 197.04 ? 138 LYS F CD  1 
ATOM   15475 C CE  . LYS F 2 138 ? 51.983  1.102   38.855  1.00 202.40 ? 138 LYS F CE  1 
ATOM   15476 N NZ  . LYS F 2 138 ? 51.397  -0.047  39.598  1.00 205.01 ? 138 LYS F NZ  1 
ATOM   15477 N N   . VAL F 2 139 ? 45.978  0.697   36.864  1.00 173.62 ? 139 VAL F N   1 
ATOM   15478 C CA  . VAL F 2 139 ? 45.382  -0.631  36.848  1.00 164.27 ? 139 VAL F CA  1 
ATOM   15479 C C   . VAL F 2 139 ? 45.767  -1.336  35.556  1.00 160.55 ? 139 VAL F C   1 
ATOM   15480 O O   . VAL F 2 139 ? 45.972  -0.703  34.516  1.00 165.62 ? 139 VAL F O   1 
ATOM   15481 C CB  . VAL F 2 139 ? 43.846  -0.575  36.994  1.00 164.07 ? 139 VAL F CB  1 
ATOM   15482 C CG1 . VAL F 2 139 ? 43.461  -0.025  38.359  1.00 165.78 ? 139 VAL F CG1 1 
ATOM   15483 C CG2 . VAL F 2 139 ? 43.243  0.270   35.884  1.00 166.81 ? 139 VAL F CG2 1 
ATOM   15484 N N   . ASP F 2 140 ? 45.869  -2.665  35.630  1.00 153.87 ? 140 ASP F N   1 
ATOM   15485 C CA  . ASP F 2 140 ? 46.194  -3.448  34.443  1.00 151.81 ? 140 ASP F CA  1 
ATOM   15486 C C   . ASP F 2 140 ? 45.006  -3.566  33.496  1.00 162.13 ? 140 ASP F C   1 
ATOM   15487 O O   . ASP F 2 140 ? 45.198  -3.741  32.288  1.00 161.25 ? 140 ASP F O   1 
ATOM   15488 C CB  . ASP F 2 140 ? 46.688  -4.835  34.850  1.00 146.32 ? 140 ASP F CB  1 
ATOM   15489 C CG  . ASP F 2 140 ? 47.882  -4.778  35.779  1.00 136.82 ? 140 ASP F CG  1 
ATOM   15490 O OD1 . ASP F 2 140 ? 48.654  -3.799  35.697  1.00 134.30 ? 140 ASP F OD1 1 
ATOM   15491 O OD2 . ASP F 2 140 ? 48.049  -5.709  36.593  1.00 129.14 ? 140 ASP F OD2 1 
ATOM   15492 N N   . GLU F 2 141 ? 43.782  -3.485  34.020  1.00 177.16 ? 141 GLU F N   1 
ATOM   15493 C CA  . GLU F 2 141 ? 42.564  -3.594  33.221  1.00 175.24 ? 141 GLU F CA  1 
ATOM   15494 C C   . GLU F 2 141 ? 41.853  -2.247  33.193  1.00 172.36 ? 141 GLU F C   1 
ATOM   15495 O O   . GLU F 2 141 ? 41.018  -1.962  34.065  1.00 170.08 ? 141 GLU F O   1 
ATOM   15496 C CB  . GLU F 2 141 ? 41.641  -4.679  33.782  1.00 174.97 ? 141 GLU F CB  1 
ATOM   15497 C CG  . GLU F 2 141 ? 42.220  -6.079  33.706  1.00 178.71 ? 141 GLU F CG  1 
ATOM   15498 C CD  . GLU F 2 141 ? 42.098  -6.684  32.322  1.00 183.55 ? 141 GLU F CD  1 
ATOM   15499 O OE1 . GLU F 2 141 ? 41.365  -6.114  31.486  1.00 180.57 ? 141 GLU F OE1 1 
ATOM   15500 O OE2 . GLU F 2 141 ? 42.739  -7.725  32.068  1.00 186.80 ? 141 GLU F OE2 1 
ATOM   15501 N N   . PRO F 2 142 ? 42.135  -1.385  32.211  1.00 163.86 ? 142 PRO F N   1 
ATOM   15502 C CA  . PRO F 2 142 ? 41.431  -0.098  32.150  1.00 167.10 ? 142 PRO F CA  1 
ATOM   15503 C C   . PRO F 2 142 ? 40.049  -0.179  31.528  1.00 164.52 ? 142 PRO F C   1 
ATOM   15504 O O   . PRO F 2 142 ? 39.253  0.750   31.715  1.00 164.89 ? 142 PRO F O   1 
ATOM   15505 C CB  . PRO F 2 142 ? 42.363  0.765   31.292  1.00 172.43 ? 142 PRO F CB  1 
ATOM   15506 C CG  . PRO F 2 142 ? 43.035  -0.217  30.392  1.00 167.41 ? 142 PRO F CG  1 
ATOM   15507 C CD  . PRO F 2 142 ? 43.188  -1.492  31.187  1.00 161.51 ? 142 PRO F CD  1 
ATOM   15508 N N   . SER F 2 143 ? 39.725  -1.259  30.817  1.00 168.40 ? 143 SER F N   1 
ATOM   15509 C CA  . SER F 2 143 ? 38.403  -1.353  30.210  1.00 161.05 ? 143 SER F CA  1 
ATOM   15510 C C   . SER F 2 143 ? 37.341  -1.640  31.264  1.00 166.64 ? 143 SER F C   1 
ATOM   15511 O O   . SER F 2 143 ? 36.237  -1.089  31.208  1.00 163.65 ? 143 SER F O   1 
ATOM   15512 C CB  . SER F 2 143 ? 38.396  -2.426  29.121  1.00 152.72 ? 143 SER F CB  1 
ATOM   15513 O OG  . SER F 2 143 ? 38.653  -3.708  29.665  1.00 159.25 ? 143 SER F OG  1 
ATOM   15514 N N   . LYS F 2 144 ? 37.665  -2.481  32.247  1.00 187.81 ? 144 LYS F N   1 
ATOM   15515 C CA  . LYS F 2 144 ? 36.706  -2.812  33.293  1.00 189.44 ? 144 LYS F CA  1 
ATOM   15516 C C   . LYS F 2 144 ? 36.457  -1.664  34.262  1.00 191.63 ? 144 LYS F C   1 
ATOM   15517 O O   . LYS F 2 144 ? 35.525  -1.754  35.067  1.00 195.52 ? 144 LYS F O   1 
ATOM   15518 C CB  . LYS F 2 144 ? 37.187  -4.032  34.080  1.00 191.10 ? 144 LYS F CB  1 
ATOM   15519 C CG  . LYS F 2 144 ? 37.421  -5.279  33.251  1.00 195.36 ? 144 LYS F CG  1 
ATOM   15520 C CD  . LYS F 2 144 ? 37.971  -6.385  34.130  1.00 198.27 ? 144 LYS F CD  1 
ATOM   15521 C CE  . LYS F 2 144 ? 36.995  -6.729  35.242  1.00 202.43 ? 144 LYS F CE  1 
ATOM   15522 N NZ  . LYS F 2 144 ? 37.501  -7.824  36.113  1.00 205.82 ? 144 LYS F NZ  1 
ATOM   15523 N N   . TYR F 2 145 ? 37.248  -0.598  34.205  1.00 169.53 ? 145 TYR F N   1 
ATOM   15524 C CA  . TYR F 2 145 ? 37.112  0.536   35.108  1.00 162.72 ? 145 TYR F CA  1 
ATOM   15525 C C   . TYR F 2 145 ? 36.858  1.809   34.303  1.00 160.05 ? 145 TYR F C   1 
ATOM   15526 O O   . TYR F 2 145 ? 36.852  1.804   33.068  1.00 157.35 ? 145 TYR F O   1 
ATOM   15527 C CB  . TYR F 2 145 ? 38.359  0.691   35.983  1.00 160.80 ? 145 TYR F CB  1 
ATOM   15528 C CG  . TYR F 2 145 ? 38.776  -0.567  36.715  1.00 163.94 ? 145 TYR F CG  1 
ATOM   15529 C CD1 . TYR F 2 145 ? 37.838  -1.387  37.325  1.00 168.04 ? 145 TYR F CD1 1 
ATOM   15530 C CD2 . TYR F 2 145 ? 40.114  -0.931  36.799  1.00 163.04 ? 145 TYR F CD2 1 
ATOM   15531 C CE1 . TYR F 2 145 ? 38.220  -2.536  37.995  1.00 169.22 ? 145 TYR F CE1 1 
ATOM   15532 C CE2 . TYR F 2 145 ? 40.507  -2.077  37.466  1.00 165.84 ? 145 TYR F CE2 1 
ATOM   15533 C CZ  . TYR F 2 145 ? 39.556  -2.875  38.062  1.00 167.91 ? 145 TYR F CZ  1 
ATOM   15534 O OH  . TYR F 2 145 ? 39.941  -4.017  38.728  1.00 163.88 ? 145 TYR F OH  1 
ATOM   15535 N N   . GLY F 2 146 ? 36.650  2.910   35.022  1.00 166.57 ? 146 GLY F N   1 
ATOM   15536 C CA  . GLY F 2 146 ? 36.502  4.205   34.389  1.00 171.50 ? 146 GLY F CA  1 
ATOM   15537 C C   . GLY F 2 146 ? 37.826  4.929   34.276  1.00 185.19 ? 146 GLY F C   1 
ATOM   15538 O O   . GLY F 2 146 ? 38.423  5.314   35.286  1.00 180.09 ? 146 GLY F O   1 
ATOM   15539 N N   . VAL F 2 147 ? 38.288  5.129   33.048  1.00 220.23 ? 147 VAL F N   1 
ATOM   15540 C CA  . VAL F 2 147 ? 39.613  5.687   32.810  1.00 220.21 ? 147 VAL F CA  1 
ATOM   15541 C C   . VAL F 2 147 ? 39.560  7.205   32.895  1.00 221.88 ? 147 VAL F C   1 
ATOM   15542 O O   . VAL F 2 147 ? 38.629  7.844   32.391  1.00 222.82 ? 147 VAL F O   1 
ATOM   15543 C CB  . VAL F 2 147 ? 40.153  5.224   31.446  1.00 218.39 ? 147 VAL F CB  1 
ATOM   15544 C CG1 . VAL F 2 147 ? 41.566  5.733   31.240  1.00 218.54 ? 147 VAL F CG1 1 
ATOM   15545 C CG2 . VAL F 2 147 ? 40.122  3.715   31.355  1.00 216.67 ? 147 VAL F CG2 1 
ATOM   15546 N N   . VAL F 2 148 ? 40.571  7.785   33.537  1.00 192.72 ? 148 VAL F N   1 
ATOM   15547 C CA  . VAL F 2 148 ? 40.741  9.230   33.627  1.00 190.36 ? 148 VAL F CA  1 
ATOM   15548 C C   . VAL F 2 148 ? 41.873  9.614   32.683  1.00 191.19 ? 148 VAL F C   1 
ATOM   15549 O O   . VAL F 2 148 ? 43.014  9.166   32.858  1.00 187.72 ? 148 VAL F O   1 
ATOM   15550 C CB  . VAL F 2 148 ? 41.040  9.676   35.066  1.00 179.16 ? 148 VAL F CB  1 
ATOM   15551 C CG1 . VAL F 2 148 ? 41.296  11.173  35.116  1.00 178.90 ? 148 VAL F CG1 1 
ATOM   15552 C CG2 . VAL F 2 148 ? 39.899  9.286   35.996  1.00 173.38 ? 148 VAL F CG2 1 
ATOM   15553 N N   . VAL F 2 149 ? 41.562  10.440  31.685  1.00 200.21 ? 149 VAL F N   1 
ATOM   15554 C CA  . VAL F 2 149 ? 42.521  10.836  30.658  1.00 196.84 ? 149 VAL F CA  1 
ATOM   15555 C C   . VAL F 2 149 ? 43.130  12.168  31.084  1.00 197.57 ? 149 VAL F C   1 
ATOM   15556 O O   . VAL F 2 149 ? 42.560  13.239  30.852  1.00 196.15 ? 149 VAL F O   1 
ATOM   15557 C CB  . VAL F 2 149 ? 41.878  10.915  29.269  1.00 198.14 ? 149 VAL F CB  1 
ATOM   15558 C CG1 . VAL F 2 149 ? 41.774  9.527   28.656  1.00 193.98 ? 149 VAL F CG1 1 
ATOM   15559 C CG2 . VAL F 2 149 ? 40.502  11.558  29.338  1.00 193.30 ? 149 VAL F CG2 1 
ATOM   15560 N N   . MET F 2 150 ? 44.291  12.099  31.724  1.00 190.53 ? 150 MET F N   1 
ATOM   15561 C CA  . MET F 2 150 ? 45.047  13.264  32.154  1.00 181.90 ? 150 MET F CA  1 
ATOM   15562 C C   . MET F 2 150 ? 46.313  13.401  31.319  1.00 178.38 ? 150 MET F C   1 
ATOM   15563 O O   . MET F 2 150 ? 46.747  12.459  30.650  1.00 178.36 ? 150 MET F O   1 
ATOM   15564 C CB  . MET F 2 150 ? 45.414  13.158  33.638  1.00 176.85 ? 150 MET F CB  1 
ATOM   15565 C CG  . MET F 2 150 ? 46.153  11.873  33.991  1.00 176.66 ? 150 MET F CG  1 
ATOM   15566 S SD  . MET F 2 150 ? 46.419  11.647  35.761  1.00 168.39 ? 150 MET F SD  1 
ATOM   15567 C CE  . MET F 2 150 ? 47.617  12.935  36.089  1.00 177.86 ? 150 MET F CE  1 
ATOM   15568 N N   . ARG F 2 156 ? 46.101  17.595  35.035  1.00 138.39 ? 156 ARG F N   1 
ATOM   15569 C CA  . ARG F 2 156 ? 44.745  18.053  34.768  1.00 147.11 ? 156 ARG F CA  1 
ATOM   15570 C C   . ARG F 2 156 ? 43.989  17.011  33.951  1.00 153.37 ? 156 ARG F C   1 
ATOM   15571 O O   . ARG F 2 156 ? 44.536  16.423  33.015  1.00 157.15 ? 156 ARG F O   1 
ATOM   15572 C CB  . ARG F 2 156 ? 44.774  19.391  34.027  1.00 153.32 ? 156 ARG F CB  1 
ATOM   15573 C CG  . ARG F 2 156 ? 43.438  20.107  33.946  1.00 168.31 ? 156 ARG F CG  1 
ATOM   15574 C CD  . ARG F 2 156 ? 43.584  21.418  33.191  1.00 177.75 ? 156 ARG F CD  1 
ATOM   15575 N NE  . ARG F 2 156 ? 44.670  22.235  33.728  1.00 172.26 ? 156 ARG F NE  1 
ATOM   15576 C CZ  . ARG F 2 156 ? 45.079  23.381  33.194  1.00 166.91 ? 156 ARG F CZ  1 
ATOM   15577 N NH1 . ARG F 2 156 ? 44.495  23.851  32.101  1.00 177.04 ? 156 ARG F NH1 1 
ATOM   15578 N NH2 . ARG F 2 156 ? 46.075  24.056  33.751  1.00 158.42 ? 156 ARG F NH2 1 
ATOM   15579 N N   . VAL F 2 157 ? 42.731  16.780  34.316  1.00 156.90 ? 157 VAL F N   1 
ATOM   15580 C CA  . VAL F 2 157 ? 41.906  15.777  33.657  1.00 159.21 ? 157 VAL F CA  1 
ATOM   15581 C C   . VAL F 2 157 ? 41.041  16.461  32.605  1.00 159.93 ? 157 VAL F C   1 
ATOM   15582 O O   . VAL F 2 157 ? 40.833  17.678  32.626  1.00 160.62 ? 157 VAL F O   1 
ATOM   15583 C CB  . VAL F 2 157 ? 41.042  14.989  34.670  1.00 153.66 ? 157 VAL F CB  1 
ATOM   15584 C CG1 . VAL F 2 157 ? 41.852  14.673  35.921  1.00 157.65 ? 157 VAL F CG1 1 
ATOM   15585 C CG2 . VAL F 2 157 ? 39.786  15.758  35.024  1.00 148.74 ? 157 VAL F CG2 1 
ATOM   15586 N N   . GLU F 2 158 ? 40.531  15.668  31.660  1.00 163.94 ? 158 GLU F N   1 
ATOM   15587 C CA  . GLU F 2 158 ? 39.828  16.234  30.514  1.00 165.21 ? 158 GLU F CA  1 
ATOM   15588 C C   . GLU F 2 158 ? 38.473  15.584  30.249  1.00 166.03 ? 158 GLU F C   1 
ATOM   15589 O O   . GLU F 2 158 ? 37.466  16.287  30.114  1.00 167.87 ? 158 GLU F O   1 
ATOM   15590 C CB  . GLU F 2 158 ? 40.702  16.131  29.260  1.00 166.79 ? 158 GLU F CB  1 
ATOM   15591 C CG  . GLU F 2 158 ? 42.039  16.849  29.370  1.00 167.36 ? 158 GLU F CG  1 
ATOM   15592 C CD  . GLU F 2 158 ? 42.894  16.690  28.128  1.00 166.83 ? 158 GLU F CD  1 
ATOM   15593 O OE1 . GLU F 2 158 ? 42.511  15.905  27.237  1.00 170.78 ? 158 GLU F OE1 1 
ATOM   15594 O OE2 . GLU F 2 158 ? 43.952  17.349  28.043  1.00 164.94 ? 158 GLU F OE2 1 
ATOM   15595 N N   . LYS F 2 159 ? 38.424  14.256  30.172  1.00 166.36 ? 159 LYS F N   1 
ATOM   15596 C CA  . LYS F 2 159 ? 37.199  13.573  29.778  1.00 159.42 ? 159 LYS F CA  1 
ATOM   15597 C C   . LYS F 2 159 ? 37.091  12.259  30.541  1.00 162.82 ? 159 LYS F C   1 
ATOM   15598 O O   . LYS F 2 159 ? 38.036  11.817  31.198  1.00 172.30 ? 159 LYS F O   1 
ATOM   15599 C CB  . LYS F 2 159 ? 37.161  13.335  28.262  1.00 150.03 ? 159 LYS F CB  1 
ATOM   15600 C CG  . LYS F 2 159 ? 35.762  13.213  27.675  1.00 143.02 ? 159 LYS F CG  1 
ATOM   15601 C CD  . LYS F 2 159 ? 34.971  14.498  27.866  1.00 138.26 ? 159 LYS F CD  1 
ATOM   15602 C CE  . LYS F 2 159 ? 33.604  14.412  27.205  1.00 127.63 ? 159 LYS F CE  1 
ATOM   15603 N NZ  . LYS F 2 159 ? 32.791  13.288  27.746  1.00 126.99 ? 159 LYS F NZ  1 
ATOM   15604 N N   . PHE F 2 160 ? 35.911  11.647  30.469  0.53 154.47 ? 160 PHE F N   1 
ATOM   15605 C CA  . PHE F 2 160 ? 35.652  10.358  31.100  0.53 155.75 ? 160 PHE F CA  1 
ATOM   15606 C C   . PHE F 2 160 ? 35.312  9.335   30.025  0.53 154.95 ? 160 PHE F C   1 
ATOM   15607 O O   . PHE F 2 160 ? 34.335  9.502   29.287  0.53 153.68 ? 160 PHE F O   1 
ATOM   15608 C CB  . PHE F 2 160 ? 34.533  10.460  32.145  0.53 159.36 ? 160 PHE F CB  1 
ATOM   15609 N N   . VAL F 2 161 ? 36.134  8.294   29.920  1.00 158.11 ? 161 VAL F N   1 
ATOM   15610 C CA  . VAL F 2 161 ? 35.963  7.239   28.927  1.00 153.56 ? 161 VAL F CA  1 
ATOM   15611 C C   . VAL F 2 161 ? 35.775  5.939   29.699  1.00 154.96 ? 161 VAL F C   1 
ATOM   15612 O O   . VAL F 2 161 ? 36.749  5.334   30.162  1.00 160.50 ? 161 VAL F O   1 
ATOM   15613 C CB  . VAL F 2 161 ? 37.149  7.146   27.961  1.00 150.66 ? 161 VAL F CB  1 
ATOM   15614 C CG1 . VAL F 2 161 ? 36.892  6.072   26.914  1.00 147.56 ? 161 VAL F CG1 1 
ATOM   15615 C CG2 . VAL F 2 161 ? 37.408  8.491   27.302  1.00 149.28 ? 161 VAL F CG2 1 
ATOM   15616 N N   . GLU F 2 162 ? 34.527  5.503   29.839  1.00 148.73 ? 162 GLU F N   1 
ATOM   15617 C CA  . GLU F 2 162 ? 34.221  4.254   30.518  1.00 144.96 ? 162 GLU F CA  1 
ATOM   15618 C C   . GLU F 2 162 ? 34.210  3.117   29.505  1.00 143.68 ? 162 GLU F C   1 
ATOM   15619 O O   . GLU F 2 162 ? 33.692  3.264   28.393  1.00 141.93 ? 162 GLU F O   1 
ATOM   15620 C CB  . GLU F 2 162 ? 32.875  4.344   31.244  1.00 143.75 ? 162 GLU F CB  1 
ATOM   15621 C CG  . GLU F 2 162 ? 31.648  4.393   30.336  1.00 146.47 ? 162 GLU F CG  1 
ATOM   15622 C CD  . GLU F 2 162 ? 31.457  5.736   29.651  1.00 151.08 ? 162 GLU F CD  1 
ATOM   15623 O OE1 . GLU F 2 162 ? 32.227  6.677   29.939  1.00 154.52 ? 162 GLU F OE1 1 
ATOM   15624 O OE2 . GLU F 2 162 ? 30.541  5.844   28.810  1.00 147.73 ? 162 GLU F OE2 1 
ATOM   15625 N N   . LYS F 2 163 ? 34.795  1.984   29.897  1.00 143.41 ? 163 LYS F N   1 
ATOM   15626 C CA  . LYS F 2 163 ? 34.955  0.819   29.033  1.00 144.09 ? 163 LYS F CA  1 
ATOM   15627 C C   . LYS F 2 163 ? 35.517  1.245   27.680  1.00 143.92 ? 163 LYS F C   1 
ATOM   15628 O O   . LYS F 2 163 ? 34.790  1.252   26.676  1.00 140.23 ? 163 LYS F O   1 
ATOM   15629 C CB  . LYS F 2 163 ? 33.622  0.081   28.866  1.00 143.34 ? 163 LYS F CB  1 
ATOM   15630 C CG  . LYS F 2 163 ? 33.716  -1.219  28.071  1.00 141.50 ? 163 LYS F CG  1 
ATOM   15631 C CD  . LYS F 2 163 ? 34.810  -2.123  28.609  1.00 142.78 ? 163 LYS F CD  1 
ATOM   15632 C CE  . LYS F 2 163 ? 35.028  -3.328  27.711  1.00 141.23 ? 163 LYS F CE  1 
ATOM   15633 N NZ  . LYS F 2 163 ? 35.420  -2.923  26.332  1.00 141.52 ? 163 LYS F NZ  1 
ATOM   15634 N N   . PRO F 2 164 ? 36.792  1.635   27.610  1.00 145.45 ? 164 PRO F N   1 
ATOM   15635 C CA  . PRO F 2 164 ? 37.376  1.998   26.313  1.00 148.02 ? 164 PRO F CA  1 
ATOM   15636 C C   . PRO F 2 164 ? 37.765  0.742   25.549  1.00 151.94 ? 164 PRO F C   1 
ATOM   15637 O O   . PRO F 2 164 ? 38.589  -0.051  26.013  1.00 150.55 ? 164 PRO F O   1 
ATOM   15638 C CB  . PRO F 2 164 ? 38.608  2.833   26.697  1.00 146.61 ? 164 PRO F CB  1 
ATOM   15639 C CG  . PRO F 2 164 ? 38.526  3.033   28.191  1.00 147.78 ? 164 PRO F CG  1 
ATOM   15640 C CD  . PRO F 2 164 ? 37.726  1.891   28.714  1.00 148.78 ? 164 PRO F CD  1 
ATOM   15641 N N   . LYS F 2 165 ? 37.170  0.562   24.368  1.00 156.43 ? 165 LYS F N   1 
ATOM   15642 C CA  . LYS F 2 165 ? 37.541  -0.574  23.532  1.00 156.99 ? 165 LYS F CA  1 
ATOM   15643 C C   . LYS F 2 165 ? 38.951  -0.407  22.988  1.00 156.76 ? 165 LYS F C   1 
ATOM   15644 O O   . LYS F 2 165 ? 39.711  -1.379  22.905  1.00 156.11 ? 165 LYS F O   1 
ATOM   15645 C CB  . LYS F 2 165 ? 36.538  -0.740  22.392  1.00 157.72 ? 165 LYS F CB  1 
ATOM   15646 C CG  . LYS F 2 165 ? 35.202  -1.316  22.822  1.00 156.75 ? 165 LYS F CG  1 
ATOM   15647 C CD  . LYS F 2 165 ? 34.356  -1.685  21.617  1.00 164.40 ? 165 LYS F CD  1 
ATOM   15648 C CE  . LYS F 2 165 ? 34.894  -2.934  20.937  1.00 168.10 ? 165 LYS F CE  1 
ATOM   15649 N NZ  . LYS F 2 165 ? 34.767  -2.873  19.455  1.00 172.89 ? 165 LYS F NZ  1 
ATOM   15650 N N   . LEU F 2 166 ? 39.319  0.815   22.621  1.00 155.42 ? 166 LEU F N   1 
ATOM   15651 C CA  . LEU F 2 166 ? 40.690  1.149   22.275  1.00 160.56 ? 166 LEU F CA  1 
ATOM   15652 C C   . LEU F 2 166 ? 41.357  1.826   23.465  1.00 163.43 ? 166 LEU F C   1 
ATOM   15653 O O   . LEU F 2 166 ? 40.701  2.259   24.415  1.00 159.21 ? 166 LEU F O   1 
ATOM   15654 C CB  . LEU F 2 166 ? 40.738  2.055   21.042  1.00 160.83 ? 166 LEU F CB  1 
ATOM   15655 C CG  . LEU F 2 166 ? 41.578  1.560   19.863  1.00 163.34 ? 166 LEU F CG  1 
ATOM   15656 C CD1 . LEU F 2 166 ? 40.862  0.443   19.117  1.00 164.61 ? 166 LEU F CD1 1 
ATOM   15657 C CD2 . LEU F 2 166 ? 41.933  2.703   18.920  1.00 161.17 ? 166 LEU F CD2 1 
ATOM   15658 N N   . TYR F 2 167 ? 42.681  1.922   23.406  1.00 171.95 ? 167 TYR F N   1 
ATOM   15659 C CA  . TYR F 2 167 ? 43.441  2.433   24.540  1.00 166.70 ? 167 TYR F CA  1 
ATOM   15660 C C   . TYR F 2 167 ? 43.438  3.955   24.514  1.00 164.31 ? 167 TYR F C   1 
ATOM   15661 O O   . TYR F 2 167 ? 44.013  4.573   23.612  1.00 161.22 ? 167 TYR F O   1 
ATOM   15662 C CB  . TYR F 2 167 ? 44.869  1.896   24.535  1.00 167.55 ? 167 TYR F CB  1 
ATOM   15663 C CG  . TYR F 2 167 ? 45.702  2.454   25.669  1.00 172.10 ? 167 TYR F CG  1 
ATOM   15664 C CD1 . TYR F 2 167 ? 45.607  1.922   26.948  1.00 176.59 ? 167 TYR F CD1 1 
ATOM   15665 C CD2 . TYR F 2 167 ? 46.573  3.517   25.464  1.00 174.12 ? 167 TYR F CD2 1 
ATOM   15666 C CE1 . TYR F 2 167 ? 46.360  2.427   27.988  1.00 183.44 ? 167 TYR F CE1 1 
ATOM   15667 C CE2 . TYR F 2 167 ? 47.330  4.030   26.500  1.00 179.98 ? 167 TYR F CE2 1 
ATOM   15668 C CZ  . TYR F 2 167 ? 47.219  3.481   27.759  1.00 187.42 ? 167 TYR F CZ  1 
ATOM   15669 O OH  . TYR F 2 167 ? 47.970  3.986   28.793  1.00 194.95 ? 167 TYR F OH  1 
ATOM   15670 N N   . VAL F 2 168 ? 42.793  4.557   25.510  1.00 170.27 ? 168 VAL F N   1 
ATOM   15671 C CA  . VAL F 2 168 ? 42.910  5.988   25.765  1.00 168.43 ? 168 VAL F CA  1 
ATOM   15672 C C   . VAL F 2 168 ? 43.597  6.270   27.087  1.00 173.02 ? 168 VAL F C   1 
ATOM   15673 O O   . VAL F 2 168 ? 43.898  7.439   27.377  1.00 168.53 ? 168 VAL F O   1 
ATOM   15674 C CB  . VAL F 2 168 ? 41.535  6.689   25.725  1.00 159.93 ? 168 VAL F CB  1 
ATOM   15675 C CG1 . VAL F 2 168 ? 40.965  6.664   24.315  1.00 151.08 ? 168 VAL F CG1 1 
ATOM   15676 C CG2 . VAL F 2 168 ? 40.580  6.034   26.706  1.00 158.01 ? 168 VAL F CG2 1 
ATOM   15677 N N   . GLY F 2 169 ? 43.854  5.250   27.889  1.00 182.70 ? 169 GLY F N   1 
ATOM   15678 C CA  . GLY F 2 169 ? 44.539  5.408   29.155  1.00 186.39 ? 169 GLY F CA  1 
ATOM   15679 C C   . GLY F 2 169 ? 44.365  4.178   30.014  1.00 192.20 ? 169 GLY F C   1 
ATOM   15680 O O   . GLY F 2 169 ? 43.634  3.246   29.677  1.00 189.21 ? 169 GLY F O   1 
ATOM   15681 N N   . ASN F 2 170 ? 45.062  4.191   31.147  1.00 210.50 ? 170 ASN F N   1 
ATOM   15682 C CA  . ASN F 2 170 ? 44.981  3.114   32.121  1.00 210.22 ? 170 ASN F CA  1 
ATOM   15683 C C   . ASN F 2 170 ? 44.754  3.625   33.535  1.00 212.08 ? 170 ASN F C   1 
ATOM   15684 O O   . ASN F 2 170 ? 44.690  2.816   34.467  1.00 212.22 ? 170 ASN F O   1 
ATOM   15685 C CB  . ASN F 2 170 ? 46.251  2.254   32.084  1.00 209.28 ? 170 ASN F CB  1 
ATOM   15686 C CG  . ASN F 2 170 ? 47.505  3.082   31.896  1.00 209.99 ? 170 ASN F CG  1 
ATOM   15687 O OD1 . ASN F 2 170 ? 48.109  3.079   30.823  1.00 215.19 ? 170 ASN F OD1 1 
ATOM   15688 N ND2 . ASN F 2 170 ? 47.899  3.804   32.937  1.00 211.34 ? 170 ASN F ND2 1 
ATOM   15689 N N   . LYS F 2 171 ? 44.632  4.936   33.717  1.00 190.08 ? 171 LYS F N   1 
ATOM   15690 C CA  . LYS F 2 171 ? 44.542  5.546   35.034  1.00 178.26 ? 171 LYS F CA  1 
ATOM   15691 C C   . LYS F 2 171 ? 43.080  5.748   35.412  1.00 176.91 ? 171 LYS F C   1 
ATOM   15692 O O   . LYS F 2 171 ? 42.316  6.359   34.658  1.00 183.31 ? 171 LYS F O   1 
ATOM   15693 C CB  . LYS F 2 171 ? 45.288  6.879   35.041  1.00 171.25 ? 171 LYS F CB  1 
ATOM   15694 C CG  . LYS F 2 171 ? 46.736  6.774   34.595  1.00 167.48 ? 171 LYS F CG  1 
ATOM   15695 C CD  . LYS F 2 171 ? 47.078  7.848   33.576  1.00 162.13 ? 171 LYS F CD  1 
ATOM   15696 C CE  . LYS F 2 171 ? 46.232  7.710   32.320  1.00 170.00 ? 171 LYS F CE  1 
ATOM   15697 N NZ  . LYS F 2 171 ? 46.460  8.835   31.370  1.00 167.12 ? 171 LYS F NZ  1 
ATOM   15698 N N   . ILE F 2 172 ? 42.697  5.232   36.579  1.00 161.89 ? 172 ILE F N   1 
ATOM   15699 C CA  . ILE F 2 172 ? 41.322  5.292   37.052  1.00 159.33 ? 172 ILE F CA  1 
ATOM   15700 C C   . ILE F 2 172 ? 41.295  5.986   38.410  1.00 152.33 ? 172 ILE F C   1 
ATOM   15701 O O   . ILE F 2 172 ? 42.322  6.175   39.060  1.00 150.81 ? 172 ILE F O   1 
ATOM   15702 C CB  . ILE F 2 172 ? 40.676  3.897   37.146  1.00 156.73 ? 172 ILE F CB  1 
ATOM   15703 C CG1 . ILE F 2 172 ? 41.253  3.125   38.333  1.00 152.38 ? 172 ILE F CG1 1 
ATOM   15704 C CG2 . ILE F 2 172 ? 40.903  3.130   35.857  1.00 162.16 ? 172 ILE F CG2 1 
ATOM   15705 C CD1 . ILE F 2 172 ? 40.377  1.985   38.805  1.00 157.92 ? 172 ILE F CD1 1 
ATOM   15706 N N   . ASN F 2 173 ? 40.090  6.352   38.837  1.00 158.05 ? 173 ASN F N   1 
ATOM   15707 C CA  . ASN F 2 173 ? 39.920  6.999   40.129  1.00 153.86 ? 173 ASN F CA  1 
ATOM   15708 C C   . ASN F 2 173 ? 40.172  6.001   41.255  1.00 155.63 ? 173 ASN F C   1 
ATOM   15709 O O   . ASN F 2 173 ? 39.940  4.798   41.113  1.00 158.23 ? 173 ASN F O   1 
ATOM   15710 C CB  . ASN F 2 173 ? 38.516  7.593   40.244  1.00 143.86 ? 173 ASN F CB  1 
ATOM   15711 C CG  . ASN F 2 173 ? 38.393  8.584   41.385  1.00 147.65 ? 173 ASN F CG  1 
ATOM   15712 O OD1 . ASN F 2 173 ? 38.853  8.333   42.499  1.00 148.68 ? 173 ASN F OD1 1 
ATOM   15713 N ND2 . ASN F 2 173 ? 37.771  9.724   41.109  1.00 152.41 ? 173 ASN F ND2 1 
ATOM   15714 N N   . ALA F 2 174 ? 40.649  6.516   42.387  1.00 167.76 ? 174 ALA F N   1 
ATOM   15715 C CA  . ALA F 2 174 ? 40.996  5.685   43.532  1.00 175.34 ? 174 ALA F CA  1 
ATOM   15716 C C   . ALA F 2 174 ? 40.028  5.828   44.698  1.00 177.41 ? 174 ALA F C   1 
ATOM   15717 O O   . ALA F 2 174 ? 40.240  5.197   45.739  1.00 180.46 ? 174 ALA F O   1 
ATOM   15718 C CB  . ALA F 2 174 ? 42.421  6.005   44.002  1.00 179.46 ? 174 ALA F CB  1 
ATOM   15719 N N   . GLY F 2 175 ? 38.975  6.629   44.555  0.05 157.73 ? 175 GLY F N   1 
ATOM   15720 C CA  . GLY F 2 175 ? 37.972  6.772   45.591  0.05 151.76 ? 175 GLY F CA  1 
ATOM   15721 C C   . GLY F 2 175 ? 38.317  7.716   46.722  0.05 151.94 ? 175 GLY F C   1 
ATOM   15722 O O   . GLY F 2 175 ? 37.539  7.812   47.680  0.05 150.25 ? 175 GLY F O   1 
ATOM   15723 N N   . ILE F 2 176 ? 39.449  8.411   46.653  0.20 161.29 ? 176 ILE F N   1 
ATOM   15724 C CA  . ILE F 2 176 ? 39.846  9.386   47.663  0.20 163.43 ? 176 ILE F CA  1 
ATOM   15725 C C   . ILE F 2 176 ? 39.938  10.752  46.995  0.20 172.60 ? 176 ILE F C   1 
ATOM   15726 O O   . ILE F 2 176 ? 40.566  10.890  45.939  0.20 182.99 ? 176 ILE F O   1 
ATOM   15727 C CB  . ILE F 2 176 ? 41.176  8.997   48.336  0.20 154.62 ? 176 ILE F CB  1 
ATOM   15728 N N   . TYR F 2 177 ? 39.307  11.752  47.606  1.00 172.79 ? 177 TYR F N   1 
ATOM   15729 C CA  . TYR F 2 177 ? 39.155  13.077  47.023  1.00 178.60 ? 177 TYR F CA  1 
ATOM   15730 C C   . TYR F 2 177 ? 39.705  14.139  47.970  1.00 174.66 ? 177 TYR F C   1 
ATOM   15731 O O   . TYR F 2 177 ? 40.003  13.878  49.138  1.00 170.86 ? 177 TYR F O   1 
ATOM   15732 C CB  . TYR F 2 177 ? 37.682  13.375  46.703  1.00 177.99 ? 177 TYR F CB  1 
ATOM   15733 C CG  . TYR F 2 177 ? 36.969  12.302  45.901  1.00 172.46 ? 177 TYR F CG  1 
ATOM   15734 C CD1 . TYR F 2 177 ? 37.600  11.650  44.847  1.00 172.36 ? 177 TYR F CD1 1 
ATOM   15735 C CD2 . TYR F 2 177 ? 35.659  11.948  46.197  1.00 167.17 ? 177 TYR F CD2 1 
ATOM   15736 C CE1 . TYR F 2 177 ? 36.945  10.671  44.116  1.00 168.37 ? 177 TYR F CE1 1 
ATOM   15737 C CE2 . TYR F 2 177 ? 34.997  10.973  45.472  1.00 164.81 ? 177 TYR F CE2 1 
ATOM   15738 C CZ  . TYR F 2 177 ? 35.644  10.338  44.433  1.00 163.81 ? 177 TYR F CZ  1 
ATOM   15739 O OH  . TYR F 2 177 ? 34.984  9.368   43.712  1.00 158.15 ? 177 TYR F OH  1 
ATOM   15740 N N   . LEU F 2 178 ? 39.836  15.357  47.440  1.00 184.48 ? 178 LEU F N   1 
ATOM   15741 C CA  . LEU F 2 178 ? 40.235  16.525  48.229  1.00 181.51 ? 178 LEU F CA  1 
ATOM   15742 C C   . LEU F 2 178 ? 39.546  17.733  47.597  1.00 181.76 ? 178 LEU F C   1 
ATOM   15743 O O   . LEU F 2 178 ? 39.959  18.194  46.528  1.00 187.29 ? 178 LEU F O   1 
ATOM   15744 C CB  . LEU F 2 178 ? 41.752  16.685  48.259  1.00 181.62 ? 178 LEU F CB  1 
ATOM   15745 C CG  . LEU F 2 178 ? 42.378  17.777  49.138  1.00 170.45 ? 178 LEU F CG  1 
ATOM   15746 C CD1 . LEU F 2 178 ? 43.787  17.385  49.538  1.00 166.07 ? 178 LEU F CD1 1 
ATOM   15747 C CD2 . LEU F 2 178 ? 42.402  19.132  48.442  1.00 179.19 ? 178 LEU F CD2 1 
ATOM   15748 N N   . LEU F 2 179 ? 38.499  18.230  48.252  1.00 172.97 ? 179 LEU F N   1 
ATOM   15749 C CA  . LEU F 2 179 ? 37.617  19.235  47.674  1.00 173.11 ? 179 LEU F CA  1 
ATOM   15750 C C   . LEU F 2 179 ? 37.614  20.512  48.504  1.00 176.17 ? 179 LEU F C   1 
ATOM   15751 O O   . LEU F 2 179 ? 37.525  20.464  49.735  1.00 174.64 ? 179 LEU F O   1 
ATOM   15752 C CB  . LEU F 2 179 ? 36.190  18.695  47.558  1.00 172.39 ? 179 LEU F CB  1 
ATOM   15753 C CG  . LEU F 2 179 ? 35.986  17.605  46.505  1.00 169.69 ? 179 LEU F CG  1 
ATOM   15754 C CD1 . LEU F 2 179 ? 34.593  17.011  46.615  1.00 166.16 ? 179 LEU F CD1 1 
ATOM   15755 C CD2 . LEU F 2 179 ? 36.230  18.161  45.113  1.00 173.71 ? 179 LEU F CD2 1 
ATOM   15756 N N   . ASN F 2 180 ? 37.687  21.652  47.816  1.00 178.63 ? 180 ASN F N   1 
ATOM   15757 C CA  . ASN F 2 180 ? 37.515  22.949  48.449  1.00 185.10 ? 180 ASN F CA  1 
ATOM   15758 C C   . ASN F 2 180 ? 36.047  23.184  48.801  1.00 189.91 ? 180 ASN F C   1 
ATOM   15759 O O   . ASN F 2 180 ? 35.153  22.563  48.223  1.00 188.19 ? 180 ASN F O   1 
ATOM   15760 C CB  . ASN F 2 180 ? 38.008  24.062  47.527  1.00 182.10 ? 180 ASN F CB  1 
ATOM   15761 C CG  . ASN F 2 180 ? 39.489  24.341  47.682  1.00 180.64 ? 180 ASN F CG  1 
ATOM   15762 O OD1 . ASN F 2 180 ? 40.061  24.140  48.752  1.00 182.80 ? 180 ASN F OD1 1 
ATOM   15763 N ND2 . ASN F 2 180 ? 40.118  24.815  46.613  1.00 176.47 ? 180 ASN F ND2 1 
ATOM   15764 N N   . PRO F 2 181 ? 35.775  24.071  49.762  1.00 207.86 ? 181 PRO F N   1 
ATOM   15765 C CA  . PRO F 2 181 ? 34.375  24.414  50.063  1.00 209.62 ? 181 PRO F CA  1 
ATOM   15766 C C   . PRO F 2 181 ? 33.635  25.045  48.894  1.00 209.43 ? 181 PRO F C   1 
ATOM   15767 O O   . PRO F 2 181 ? 32.400  25.116  48.930  1.00 210.54 ? 181 PRO F O   1 
ATOM   15768 C CB  . PRO F 2 181 ? 34.499  25.392  51.240  1.00 212.27 ? 181 PRO F CB  1 
ATOM   15769 C CG  . PRO F 2 181 ? 35.811  25.063  51.866  1.00 212.79 ? 181 PRO F CG  1 
ATOM   15770 C CD  . PRO F 2 181 ? 36.707  24.681  50.726  1.00 209.97 ? 181 PRO F CD  1 
ATOM   15771 N N   . SER F 2 182 ? 34.341  25.501  47.863  1.00 194.91 ? 182 SER F N   1 
ATOM   15772 C CA  . SER F 2 182 ? 33.716  26.131  46.706  1.00 190.18 ? 182 SER F CA  1 
ATOM   15773 C C   . SER F 2 182 ? 33.081  25.128  45.748  1.00 193.91 ? 182 SER F C   1 
ATOM   15774 O O   . SER F 2 182 ? 32.625  25.528  44.670  1.00 192.88 ? 182 SER F O   1 
ATOM   15775 C CB  . SER F 2 182 ? 34.743  26.982  45.956  1.00 178.51 ? 182 SER F CB  1 
ATOM   15776 O OG  . SER F 2 182 ? 35.295  27.968  46.808  1.00 171.13 ? 182 SER F OG  1 
ATOM   15777 N N   . VAL F 2 183 ? 33.043  23.846  46.107  1.00 191.60 ? 183 VAL F N   1 
ATOM   15778 C CA  . VAL F 2 183 ? 32.442  22.832  45.249  1.00 194.69 ? 183 VAL F CA  1 
ATOM   15779 C C   . VAL F 2 183 ? 31.069  22.378  45.745  1.00 203.41 ? 183 VAL F C   1 
ATOM   15780 O O   . VAL F 2 183 ? 30.289  21.829  44.951  1.00 201.97 ? 183 VAL F O   1 
ATOM   15781 C CB  . VAL F 2 183 ? 33.385  21.620  45.098  1.00 185.36 ? 183 VAL F CB  1 
ATOM   15782 C CG1 . VAL F 2 183 ? 33.331  20.740  46.339  1.00 187.02 ? 183 VAL F CG1 1 
ATOM   15783 C CG2 . VAL F 2 183 ? 33.045  20.825  43.847  1.00 180.46 ? 183 VAL F CG2 1 
ATOM   15784 N N   . LEU F 2 184 ? 30.747  22.599  47.021  1.00 213.54 ? 184 LEU F N   1 
ATOM   15785 C CA  . LEU F 2 184 ? 29.492  22.130  47.602  1.00 215.61 ? 184 LEU F CA  1 
ATOM   15786 C C   . LEU F 2 184 ? 28.264  22.845  47.053  1.00 216.47 ? 184 LEU F C   1 
ATOM   15787 O O   . LEU F 2 184 ? 27.146  22.484  47.437  1.00 211.73 ? 184 LEU F O   1 
ATOM   15788 C CB  . LEU F 2 184 ? 29.531  22.287  49.124  1.00 212.17 ? 184 LEU F CB  1 
ATOM   15789 C CG  . LEU F 2 184 ? 30.512  21.407  49.898  1.00 204.52 ? 184 LEU F CG  1 
ATOM   15790 C CD1 . LEU F 2 184 ? 30.516  21.783  51.372  1.00 204.81 ? 184 LEU F CD1 1 
ATOM   15791 C CD2 . LEU F 2 184 ? 30.166  19.937  49.722  1.00 204.19 ? 184 LEU F CD2 1 
ATOM   15792 N N   . ASP F 2 185 ? 28.428  23.836  46.178  1.00 238.30 ? 185 ASP F N   1 
ATOM   15793 C CA  . ASP F 2 185 ? 27.296  24.543  45.595  1.00 238.64 ? 185 ASP F CA  1 
ATOM   15794 C C   . ASP F 2 185 ? 26.932  24.061  44.198  1.00 235.29 ? 185 ASP F C   1 
ATOM   15795 O O   . ASP F 2 185 ? 25.806  24.306  43.752  1.00 234.97 ? 185 ASP F O   1 
ATOM   15796 C CB  . ASP F 2 185 ? 27.588  26.046  45.538  1.00 241.09 ? 185 ASP F CB  1 
ATOM   15797 C CG  . ASP F 2 185 ? 28.743  26.380  44.614  1.00 240.16 ? 185 ASP F CG  1 
ATOM   15798 O OD1 . ASP F 2 185 ? 29.666  25.548  44.486  1.00 238.06 ? 185 ASP F OD1 1 
ATOM   15799 O OD2 . ASP F 2 185 ? 28.725  27.473  44.011  1.00 247.00 ? 185 ASP F OD2 1 
ATOM   15800 N N   . LYS F 2 186 ? 27.847  23.384  43.507  1.00 200.04 ? 186 LYS F N   1 
ATOM   15801 C CA  . LYS F 2 186 ? 27.614  22.957  42.134  1.00 183.73 ? 186 LYS F CA  1 
ATOM   15802 C C   . LYS F 2 186 ? 26.688  21.751  42.036  1.00 172.38 ? 186 LYS F C   1 
ATOM   15803 O O   . LYS F 2 186 ? 26.325  21.358  40.923  1.00 165.88 ? 186 LYS F O   1 
ATOM   15804 C CB  . LYS F 2 186 ? 28.953  22.641  41.460  1.00 174.41 ? 186 LYS F CB  1 
ATOM   15805 C CG  . LYS F 2 186 ? 28.995  22.907  39.963  1.00 154.19 ? 186 LYS F CG  1 
ATOM   15806 C CD  . LYS F 2 186 ? 30.314  22.443  39.362  1.00 144.64 ? 186 LYS F CD  1 
ATOM   15807 C CE  . LYS F 2 186 ? 30.498  22.969  37.947  1.00 141.24 ? 186 LYS F CE  1 
ATOM   15808 N NZ  . LYS F 2 186 ? 29.290  22.756  37.102  1.00 141.25 ? 186 LYS F NZ  1 
ATOM   15809 N N   . ILE F 2 187 ? 26.293  21.163  43.161  1.00 174.51 ? 187 ILE F N   1 
ATOM   15810 C CA  . ILE F 2 187 ? 25.444  19.978  43.168  1.00 165.06 ? 187 ILE F CA  1 
ATOM   15811 C C   . ILE F 2 187 ? 23.980  20.389  43.137  1.00 161.37 ? 187 ILE F C   1 
ATOM   15812 O O   . ILE F 2 187 ? 23.602  21.485  43.567  1.00 160.68 ? 187 ILE F O   1 
ATOM   15813 C CB  . ILE F 2 187 ? 25.750  19.081  44.387  1.00 161.58 ? 187 ILE F CB  1 
ATOM   15814 C CG1 . ILE F 2 187 ? 26.084  19.928  45.620  1.00 172.59 ? 187 ILE F CG1 1 
ATOM   15815 C CG2 . ILE F 2 187 ? 26.884  18.120  44.072  1.00 168.57 ? 187 ILE F CG2 1 
ATOM   15816 C CD1 . ILE F 2 187 ? 24.873  20.465  46.358  1.00 170.18 ? 187 ILE F CD1 1 
ATOM   15817 N N   . GLU F 2 188 ? 23.152  19.498  42.607  1.00 154.03 ? 188 GLU F N   1 
ATOM   15818 C CA  . GLU F 2 188 ? 21.707  19.657  42.582  1.00 154.53 ? 188 GLU F CA  1 
ATOM   15819 C C   . GLU F 2 188 ? 21.074  18.847  43.709  1.00 154.80 ? 188 GLU F C   1 
ATOM   15820 O O   . GLU F 2 188 ? 21.735  18.072  44.403  1.00 154.64 ? 188 GLU F O   1 
ATOM   15821 C CB  . GLU F 2 188 ? 21.152  19.213  41.228  1.00 152.43 ? 188 GLU F CB  1 
ATOM   15822 C CG  . GLU F 2 188 ? 21.862  17.988  40.673  1.00 152.65 ? 188 GLU F CG  1 
ATOM   15823 C CD  . GLU F 2 188 ? 21.044  17.242  39.642  1.00 152.85 ? 188 GLU F CD  1 
ATOM   15824 O OE1 . GLU F 2 188 ? 20.054  17.811  39.137  1.00 151.26 ? 188 GLU F OE1 1 
ATOM   15825 O OE2 . GLU F 2 188 ? 21.395  16.083  39.335  1.00 155.64 ? 188 GLU F OE2 1 
ATOM   15826 N N   . LEU F 2 189 ? 19.766  19.038  43.887  1.00 156.33 ? 189 LEU F N   1 
ATOM   15827 C CA  . LEU F 2 189 ? 19.021  18.247  44.859  1.00 157.55 ? 189 LEU F CA  1 
ATOM   15828 C C   . LEU F 2 189 ? 18.708  16.842  44.361  1.00 158.87 ? 189 LEU F C   1 
ATOM   15829 O O   . LEU F 2 189 ? 18.408  15.963  45.177  1.00 159.65 ? 189 LEU F O   1 
ATOM   15830 C CB  . LEU F 2 189 ? 17.729  18.971  45.246  1.00 159.69 ? 189 LEU F CB  1 
ATOM   15831 C CG  . LEU F 2 189 ? 16.984  19.701  44.129  1.00 157.70 ? 189 LEU F CG  1 
ATOM   15832 C CD1 . LEU F 2 189 ? 15.824  18.869  43.605  1.00 156.03 ? 189 LEU F CD1 1 
ATOM   15833 C CD2 . LEU F 2 189 ? 16.506  21.064  44.609  1.00 151.83 ? 189 LEU F CD2 1 
ATOM   15834 N N   . ARG F 2 190 ? 18.776  16.608  43.052  1.00 160.14 ? 190 ARG F N   1 
ATOM   15835 C CA  . ARG F 2 190 ? 18.507  15.284  42.510  1.00 160.12 ? 190 ARG F CA  1 
ATOM   15836 C C   . ARG F 2 190 ? 19.729  14.386  42.701  1.00 162.32 ? 190 ARG F C   1 
ATOM   15837 O O   . ARG F 2 190 ? 20.865  14.864  42.634  1.00 162.02 ? 190 ARG F O   1 
ATOM   15838 C CB  . ARG F 2 190 ? 18.151  15.367  41.026  1.00 159.99 ? 190 ARG F CB  1 
ATOM   15839 C CG  . ARG F 2 190 ? 17.022  16.337  40.698  1.00 163.18 ? 190 ARG F CG  1 
ATOM   15840 C CD  . ARG F 2 190 ? 15.702  15.940  41.350  1.00 167.53 ? 190 ARG F CD  1 
ATOM   15841 N NE  . ARG F 2 190 ? 15.414  14.513  41.229  1.00 169.32 ? 190 ARG F NE  1 
ATOM   15842 C CZ  . ARG F 2 190 ? 15.239  13.697  42.264  1.00 168.34 ? 190 ARG F CZ  1 
ATOM   15843 N NH1 . ARG F 2 190 ? 15.313  14.167  43.501  1.00 166.68 ? 190 ARG F NH1 1 
ATOM   15844 N NH2 . ARG F 2 190 ? 14.980  12.412  42.061  1.00 167.02 ? 190 ARG F NH2 1 
ATOM   15845 N N   . PRO F 2 191 ? 19.522  13.088  42.971  1.00 163.63 ? 191 PRO F N   1 
ATOM   15846 C CA  . PRO F 2 191 ? 20.653  12.154  43.065  1.00 165.48 ? 191 PRO F CA  1 
ATOM   15847 C C   . PRO F 2 191 ? 21.604  12.237  41.880  1.00 164.30 ? 191 PRO F C   1 
ATOM   15848 O O   . PRO F 2 191 ? 21.249  11.870  40.755  1.00 161.02 ? 191 PRO F O   1 
ATOM   15849 C CB  . PRO F 2 191 ? 19.962  10.788  43.127  1.00 164.95 ? 191 PRO F CB  1 
ATOM   15850 C CG  . PRO F 2 191 ? 18.661  11.072  43.798  1.00 163.17 ? 191 PRO F CG  1 
ATOM   15851 C CD  . PRO F 2 191 ? 18.245  12.450  43.340  1.00 162.59 ? 191 PRO F CD  1 
ATOM   15852 N N   . THR F 2 192 ? 22.820  12.717  42.132  1.00 171.64 ? 192 THR F N   1 
ATOM   15853 C CA  . THR F 2 192 ? 23.845  12.859  41.109  1.00 171.98 ? 192 THR F CA  1 
ATOM   15854 C C   . THR F 2 192 ? 25.057  12.006  41.464  1.00 185.25 ? 192 THR F C   1 
ATOM   15855 O O   . THR F 2 192 ? 25.506  11.994  42.615  1.00 192.54 ? 192 THR F O   1 
ATOM   15856 C CB  . THR F 2 192 ? 24.260  14.327  40.947  1.00 171.15 ? 192 THR F CB  1 
ATOM   15857 O OG1 . THR F 2 192 ? 25.508  14.404  40.248  1.00 174.18 ? 192 THR F OG1 1 
ATOM   15858 C CG2 . THR F 2 192 ? 24.392  15.002  42.305  1.00 179.00 ? 192 THR F CG2 1 
ATOM   15859 N N   . SER F 2 193 ? 25.577  11.292  40.467  1.00 183.40 ? 193 SER F N   1 
ATOM   15860 C CA  . SER F 2 193 ? 26.770  10.465  40.619  1.00 181.61 ? 193 SER F CA  1 
ATOM   15861 C C   . SER F 2 193 ? 28.020  11.309  40.390  1.00 175.70 ? 193 SER F C   1 
ATOM   15862 O O   . SER F 2 193 ? 28.195  11.891  39.312  1.00 171.25 ? 193 SER F O   1 
ATOM   15863 C CB  . SER F 2 193 ? 26.733  9.283   39.652  1.00 171.49 ? 193 SER F CB  1 
ATOM   15864 O OG  . SER F 2 193 ? 25.420  8.758   39.543  1.00 175.48 ? 193 SER F OG  1 
ATOM   15865 N N   . ILE F 2 194 ? 28.881  11.387  41.409  1.00 176.04 ? 194 ILE F N   1 
ATOM   15866 C CA  . ILE F 2 194 ? 30.083  12.212  41.312  1.00 164.20 ? 194 ILE F CA  1 
ATOM   15867 C C   . ILE F 2 194 ? 30.998  11.736  40.190  1.00 147.66 ? 194 ILE F C   1 
ATOM   15868 O O   . ILE F 2 194 ? 31.759  12.530  39.623  1.00 149.16 ? 194 ILE F O   1 
ATOM   15869 C CB  . ILE F 2 194 ? 30.825  12.241  42.664  1.00 160.08 ? 194 ILE F CB  1 
ATOM   15870 C CG1 . ILE F 2 194 ? 31.787  13.427  42.716  1.00 146.99 ? 194 ILE F CG1 1 
ATOM   15871 C CG2 . ILE F 2 194 ? 31.585  10.944  42.902  1.00 151.62 ? 194 ILE F CG2 1 
ATOM   15872 C CD1 . ILE F 2 194 ? 32.525  13.546  44.024  1.00 146.55 ? 194 ILE F CD1 1 
ATOM   15873 N N   . GLU F 2 195 ? 30.937  10.450  39.836  1.00 140.30 ? 195 GLU F N   1 
ATOM   15874 C CA  . GLU F 2 195 ? 31.819  9.914   38.805  1.00 134.09 ? 195 GLU F CA  1 
ATOM   15875 C C   . GLU F 2 195 ? 31.294  10.138  37.392  1.00 136.49 ? 195 GLU F C   1 
ATOM   15876 O O   . GLU F 2 195 ? 32.085  10.109  36.443  1.00 134.67 ? 195 GLU F O   1 
ATOM   15877 C CB  . GLU F 2 195 ? 32.058  8.420   39.039  1.00 129.53 ? 195 GLU F CB  1 
ATOM   15878 C CG  . GLU F 2 195 ? 32.713  8.101   40.375  1.00 126.05 ? 195 GLU F CG  1 
ATOM   15879 C CD  . GLU F 2 195 ? 34.202  8.397   40.384  1.00 127.17 ? 195 GLU F CD  1 
ATOM   15880 O OE1 . GLU F 2 195 ? 34.768  8.653   39.300  1.00 126.21 ? 195 GLU F OE1 1 
ATOM   15881 O OE2 . GLU F 2 195 ? 34.808  8.378   41.477  1.00 129.26 ? 195 GLU F OE2 1 
ATOM   15882 N N   . LYS F 2 196 ? 29.987  10.353  37.226  1.00 142.80 ? 196 LYS F N   1 
ATOM   15883 C CA  . LYS F 2 196 ? 29.396  10.478  35.901  1.00 145.88 ? 196 LYS F CA  1 
ATOM   15884 C C   . LYS F 2 196 ? 28.896  11.876  35.567  1.00 151.09 ? 196 LYS F C   1 
ATOM   15885 O O   . LYS F 2 196 ? 28.807  12.209  34.382  1.00 153.39 ? 196 LYS F O   1 
ATOM   15886 C CB  . LYS F 2 196 ? 28.234  9.486   35.737  1.00 141.72 ? 196 LYS F CB  1 
ATOM   15887 C CG  . LYS F 2 196 ? 28.553  8.066   36.185  1.00 133.47 ? 196 LYS F CG  1 
ATOM   15888 C CD  . LYS F 2 196 ? 27.346  7.152   36.029  1.00 122.09 ? 196 LYS F CD  1 
ATOM   15889 C CE  . LYS F 2 196 ? 27.618  5.766   36.594  1.00 113.09 ? 196 LYS F CE  1 
ATOM   15890 N NZ  . LYS F 2 196 ? 28.822  5.139   35.982  1.00 104.86 ? 196 LYS F NZ  1 
ATOM   15891 N N   . GLU F 2 197 ? 28.574  12.697  36.563  1.00 151.03 ? 197 GLU F N   1 
ATOM   15892 C CA  . GLU F 2 197 ? 28.014  14.022  36.319  1.00 157.17 ? 197 GLU F CA  1 
ATOM   15893 C C   . GLU F 2 197 ? 28.815  15.147  36.952  1.00 162.45 ? 197 GLU F C   1 
ATOM   15894 O O   . GLU F 2 197 ? 29.039  16.174  36.307  1.00 163.96 ? 197 GLU F O   1 
ATOM   15895 C CB  . GLU F 2 197 ? 26.563  14.104  36.829  1.00 159.14 ? 197 GLU F CB  1 
ATOM   15896 C CG  . GLU F 2 197 ? 25.547  13.298  36.031  1.00 154.88 ? 197 GLU F CG  1 
ATOM   15897 C CD  . GLU F 2 197 ? 25.509  11.837  36.431  1.00 155.65 ? 197 GLU F CD  1 
ATOM   15898 O OE1 . GLU F 2 197 ? 26.187  11.472  37.413  1.00 157.62 ? 197 GLU F OE1 1 
ATOM   15899 O OE2 . GLU F 2 197 ? 24.793  11.055  35.771  1.00 153.13 ? 197 GLU F OE2 1 
ATOM   15900 N N   . THR F 2 198 ? 29.252  14.987  38.201  1.00 169.65 ? 198 THR F N   1 
ATOM   15901 C CA  . THR F 2 198 ? 29.892  16.091  38.908  1.00 171.18 ? 198 THR F CA  1 
ATOM   15902 C C   . THR F 2 198 ? 31.330  16.300  38.447  1.00 171.67 ? 198 THR F C   1 
ATOM   15903 O O   . THR F 2 198 ? 31.736  17.430  38.155  1.00 172.16 ? 198 THR F O   1 
ATOM   15904 C CB  . THR F 2 198 ? 29.843  15.847  40.415  1.00 172.80 ? 198 THR F CB  1 
ATOM   15905 O OG1 . THR F 2 198 ? 28.479  15.718  40.832  1.00 176.96 ? 198 THR F OG1 1 
ATOM   15906 C CG2 . THR F 2 198 ? 30.487  17.004  41.159  1.00 173.66 ? 198 THR F CG2 1 
ATOM   15907 N N   . PHE F 2 199 ? 32.117  15.226  38.394  1.00 161.30 ? 199 PHE F N   1 
ATOM   15908 C CA  . PHE F 2 199 ? 33.501  15.349  37.943  1.00 155.64 ? 199 PHE F CA  1 
ATOM   15909 C C   . PHE F 2 199 ? 33.636  15.922  36.534  1.00 162.59 ? 199 PHE F C   1 
ATOM   15910 O O   . PHE F 2 199 ? 34.518  16.776  36.334  1.00 159.89 ? 199 PHE F O   1 
ATOM   15911 C CB  . PHE F 2 199 ? 34.205  13.989  38.047  1.00 146.07 ? 199 PHE F CB  1 
ATOM   15912 C CG  . PHE F 2 199 ? 34.656  13.643  39.437  1.00 137.73 ? 199 PHE F CG  1 
ATOM   15913 C CD1 . PHE F 2 199 ? 34.831  14.632  40.391  1.00 136.74 ? 199 PHE F CD1 1 
ATOM   15914 C CD2 . PHE F 2 199 ? 34.910  12.327  39.787  1.00 132.27 ? 199 PHE F CD2 1 
ATOM   15915 C CE1 . PHE F 2 199 ? 35.249  14.315  41.670  1.00 137.13 ? 199 PHE F CE1 1 
ATOM   15916 C CE2 . PHE F 2 199 ? 35.327  12.003  41.064  1.00 138.99 ? 199 PHE F CE2 1 
ATOM   15917 C CZ  . PHE F 2 199 ? 35.498  12.999  42.006  1.00 143.97 ? 199 PHE F CZ  1 
ATOM   15918 N N   . PRO F 2 200 ? 32.843  15.518  35.533  1.00 180.38 ? 200 PRO F N   1 
ATOM   15919 C CA  . PRO F 2 200 ? 32.952  16.176  34.219  1.00 181.79 ? 200 PRO F CA  1 
ATOM   15920 C C   . PRO F 2 200 ? 32.584  17.650  34.236  1.00 181.37 ? 200 PRO F C   1 
ATOM   15921 O O   . PRO F 2 200 ? 33.026  18.389  33.349  1.00 181.29 ? 200 PRO F O   1 
ATOM   15922 C CB  . PRO F 2 200 ? 31.988  15.369  33.334  1.00 180.93 ? 200 PRO F CB  1 
ATOM   15923 C CG  . PRO F 2 200 ? 31.089  14.661  34.284  1.00 178.45 ? 200 PRO F CG  1 
ATOM   15924 C CD  . PRO F 2 200 ? 31.931  14.362  35.478  1.00 179.15 ? 200 PRO F CD  1 
ATOM   15925 N N   . LYS F 2 201 ? 31.788  18.102  35.208  1.00 159.79 ? 201 LYS F N   1 
ATOM   15926 C CA  . LYS F 2 201 ? 31.444  19.519  35.271  1.00 151.65 ? 201 LYS F CA  1 
ATOM   15927 C C   . LYS F 2 201 ? 32.655  20.367  35.642  1.00 148.56 ? 201 LYS F C   1 
ATOM   15928 O O   . LYS F 2 201 ? 32.813  21.487  35.142  1.00 144.91 ? 201 LYS F O   1 
ATOM   15929 C CB  . LYS F 2 201 ? 30.302  19.742  36.261  1.00 151.42 ? 201 LYS F CB  1 
ATOM   15930 C CG  . LYS F 2 201 ? 28.932  19.393  35.706  1.00 151.94 ? 201 LYS F CG  1 
ATOM   15931 C CD  . LYS F 2 201 ? 27.830  19.698  36.707  1.00 149.80 ? 201 LYS F CD  1 
ATOM   15932 C CE  . LYS F 2 201 ? 26.458  19.411  36.116  1.00 146.29 ? 201 LYS F CE  1 
ATOM   15933 N NZ  . LYS F 2 201 ? 25.358  19.752  37.061  1.00 144.49 ? 201 LYS F NZ  1 
ATOM   15934 N N   . ILE F 2 202 ? 33.523  19.853  36.515  1.00 150.59 ? 202 ILE F N   1 
ATOM   15935 C CA  . ILE F 2 202 ? 34.735  20.581  36.870  1.00 146.63 ? 202 ILE F CA  1 
ATOM   15936 C C   . ILE F 2 202 ? 35.877  20.294  35.905  1.00 153.34 ? 202 ILE F C   1 
ATOM   15937 O O   . ILE F 2 202 ? 36.785  21.127  35.768  1.00 157.58 ? 202 ILE F O   1 
ATOM   15938 C CB  . ILE F 2 202 ? 35.176  20.245  38.305  1.00 139.67 ? 202 ILE F CB  1 
ATOM   15939 C CG1 . ILE F 2 202 ? 33.959  20.079  39.210  1.00 140.99 ? 202 ILE F CG1 1 
ATOM   15940 C CG2 . ILE F 2 202 ? 36.087  21.334  38.850  1.00 145.62 ? 202 ILE F CG2 1 
ATOM   15941 C CD1 . ILE F 2 202 ? 34.313  19.679  40.614  1.00 139.27 ? 202 ILE F CD1 1 
ATOM   15942 N N   . ALA F 2 203 ? 35.853  19.146  35.224  1.00 155.29 ? 203 ALA F N   1 
ATOM   15943 C CA  . ALA F 2 203 ? 36.901  18.833  34.260  1.00 158.11 ? 203 ALA F CA  1 
ATOM   15944 C C   . ALA F 2 203 ? 36.818  19.745  33.045  1.00 165.77 ? 203 ALA F C   1 
ATOM   15945 O O   . ALA F 2 203 ? 37.844  20.227  32.552  1.00 177.45 ? 203 ALA F O   1 
ATOM   15946 C CB  . ALA F 2 203 ? 36.806  17.367  33.842  1.00 155.79 ? 203 ALA F CB  1 
ATOM   15947 N N   . ALA F 2 204 ? 35.604  19.995  32.549  1.00 155.46 ? 204 ALA F N   1 
ATOM   15948 C CA  . ALA F 2 204 ? 35.434  20.931  31.446  1.00 156.47 ? 204 ALA F CA  1 
ATOM   15949 C C   . ALA F 2 204 ? 35.760  22.357  31.860  1.00 164.49 ? 204 ALA F C   1 
ATOM   15950 O O   . ALA F 2 204 ? 36.044  23.193  30.995  1.00 170.58 ? 204 ALA F O   1 
ATOM   15951 C CB  . ALA F 2 204 ? 34.007  20.854  30.899  1.00 156.24 ? 204 ALA F CB  1 
ATOM   15952 N N   . ALA F 2 205 ? 35.723  22.651  33.160  1.00 172.38 ? 205 ALA F N   1 
ATOM   15953 C CA  . ALA F 2 205 ? 36.111  23.957  33.670  1.00 177.29 ? 205 ALA F CA  1 
ATOM   15954 C C   . ALA F 2 205 ? 37.614  24.090  33.860  1.00 197.19 ? 205 ALA F C   1 
ATOM   15955 O O   . ALA F 2 205 ? 38.093  25.208  34.082  1.00 197.41 ? 205 ALA F O   1 
ATOM   15956 C CB  . ALA F 2 205 ? 35.401  24.235  34.998  1.00 163.29 ? 205 ALA F CB  1 
ATOM   15957 N N   . GLN F 2 206 ? 38.357  22.984  33.776  1.00 247.63 ? 206 GLN F N   1 
ATOM   15958 C CA  . GLN F 2 206 ? 39.812  22.988  33.930  1.00 247.49 ? 206 GLN F CA  1 
ATOM   15959 C C   . GLN F 2 206 ? 40.224  23.631  35.252  1.00 249.47 ? 206 GLN F C   1 
ATOM   15960 O O   . GLN F 2 206 ? 41.217  24.357  35.336  1.00 250.27 ? 206 GLN F O   1 
ATOM   15961 C CB  . GLN F 2 206 ? 40.489  23.683  32.746  1.00 247.31 ? 206 GLN F CB  1 
ATOM   15962 C CG  . GLN F 2 206 ? 40.072  23.160  31.372  1.00 245.97 ? 206 GLN F CG  1 
ATOM   15963 C CD  . GLN F 2 206 ? 40.706  21.823  31.016  1.00 243.98 ? 206 GLN F CD  1 
ATOM   15964 O OE1 . GLN F 2 206 ? 40.709  20.884  31.813  1.00 243.16 ? 206 GLN F OE1 1 
ATOM   15965 N NE2 . GLN F 2 206 ? 41.250  21.737  29.808  1.00 243.57 ? 206 GLN F NE2 1 
ATOM   15966 N N   . GLY F 2 207 ? 39.451  23.357  36.299  1.00 192.49 ? 207 GLY F N   1 
ATOM   15967 C CA  . GLY F 2 207 ? 39.728  23.910  37.608  1.00 185.58 ? 207 GLY F CA  1 
ATOM   15968 C C   . GLY F 2 207 ? 40.096  22.829  38.599  1.00 183.23 ? 207 GLY F C   1 
ATOM   15969 O O   . GLY F 2 207 ? 40.039  23.035  39.814  1.00 181.45 ? 207 GLY F O   1 
ATOM   15970 N N   . LEU F 2 208 ? 40.471  21.662  38.082  1.00 175.80 ? 208 LEU F N   1 
ATOM   15971 C CA  . LEU F 2 208 ? 40.856  20.522  38.898  1.00 166.22 ? 208 LEU F CA  1 
ATOM   15972 C C   . LEU F 2 208 ? 42.245  20.036  38.498  1.00 162.40 ? 208 LEU F C   1 
ATOM   15973 O O   . LEU F 2 208 ? 42.839  20.497  37.520  1.00 164.18 ? 208 LEU F O   1 
ATOM   15974 C CB  . LEU F 2 208 ? 39.832  19.383  38.781  1.00 158.96 ? 208 LEU F CB  1 
ATOM   15975 C CG  . LEU F 2 208 ? 39.023  19.249  37.486  1.00 149.67 ? 208 LEU F CG  1 
ATOM   15976 C CD1 . LEU F 2 208 ? 39.921  19.101  36.265  1.00 158.61 ? 208 LEU F CD1 1 
ATOM   15977 C CD2 . LEU F 2 208 ? 38.073  18.069  37.593  1.00 140.64 ? 208 LEU F CD2 1 
ATOM   15978 N N   . TYR F 2 209 ? 42.759  19.091  39.281  1.00 163.73 ? 209 TYR F N   1 
ATOM   15979 C CA  . TYR F 2 209 ? 44.044  18.466  39.010  1.00 158.59 ? 209 TYR F CA  1 
ATOM   15980 C C   . TYR F 2 209 ? 44.032  17.074  39.630  1.00 164.78 ? 209 TYR F C   1 
ATOM   15981 O O   . TYR F 2 209 ? 43.173  16.746  40.451  1.00 185.16 ? 209 TYR F O   1 
ATOM   15982 C CB  . TYR F 2 209 ? 45.205  19.309  39.545  1.00 161.05 ? 209 TYR F CB  1 
ATOM   15983 C CG  . TYR F 2 209 ? 45.175  19.477  41.040  1.00 171.65 ? 209 TYR F CG  1 
ATOM   15984 C CD1 . TYR F 2 209 ? 45.888  18.622  41.865  1.00 172.78 ? 209 TYR F CD1 1 
ATOM   15985 C CD2 . TYR F 2 209 ? 44.423  20.484  41.629  1.00 174.93 ? 209 TYR F CD2 1 
ATOM   15986 C CE1 . TYR F 2 209 ? 45.861  18.767  43.233  1.00 175.83 ? 209 TYR F CE1 1 
ATOM   15987 C CE2 . TYR F 2 209 ? 44.384  20.634  42.999  1.00 179.11 ? 209 TYR F CE2 1 
ATOM   15988 C CZ  . TYR F 2 209 ? 45.110  19.775  43.795  1.00 179.27 ? 209 TYR F CZ  1 
ATOM   15989 O OH  . TYR F 2 209 ? 45.078  19.917  45.160  1.00 179.70 ? 209 TYR F OH  1 
ATOM   15990 N N   . MET F 2 211 ? 46.498  13.582  41.128  1.00 159.15 ? 211 MET F N   1 
ATOM   15991 C CA  . MET F 2 211 ? 47.739  13.078  41.697  1.00 156.10 ? 211 MET F CA  1 
ATOM   15992 C C   . MET F 2 211 ? 47.782  11.563  41.549  1.00 159.05 ? 211 MET F C   1 
ATOM   15993 O O   . MET F 2 211 ? 46.745  10.895  41.546  1.00 160.78 ? 211 MET F O   1 
ATOM   15994 C CB  . MET F 2 211 ? 47.871  13.476  43.178  1.00 153.95 ? 211 MET F CB  1 
ATOM   15995 C CG  . MET F 2 211 ? 49.186  13.084  43.836  1.00 150.39 ? 211 MET F CG  1 
ATOM   15996 S SD  . MET F 2 211 ? 49.185  13.387  45.614  1.00 150.37 ? 211 MET F SD  1 
ATOM   15997 C CE  . MET F 2 211 ? 50.716  12.594  46.101  1.00 153.57 ? 211 MET F CE  1 
ATOM   15998 N N   . VAL F 2 212 ? 48.994  11.025  41.428  1.00 164.74 ? 212 VAL F N   1 
ATOM   15999 C CA  . VAL F 2 212 ? 49.198  9.590   41.263  1.00 171.11 ? 212 VAL F CA  1 
ATOM   16000 C C   . VAL F 2 212 ? 49.404  8.960   42.633  1.00 190.30 ? 212 VAL F C   1 
ATOM   16001 O O   . VAL F 2 212 ? 50.103  9.514   43.489  1.00 190.28 ? 212 VAL F O   1 
ATOM   16002 C CB  . VAL F 2 212 ? 50.396  9.313   40.334  1.00 164.08 ? 212 VAL F CB  1 
ATOM   16003 C CG1 . VAL F 2 212 ? 50.551  7.820   40.088  1.00 168.32 ? 212 VAL F CG1 1 
ATOM   16004 C CG2 . VAL F 2 212 ? 50.237  10.066  39.021  1.00 154.12 ? 212 VAL F CG2 1 
ATOM   16005 N N   . LEU F 2 213 ? 48.790  7.796   42.845  1.00 242.32 ? 213 LEU F N   1 
ATOM   16006 C CA  . LEU F 2 213 ? 48.889  7.099   44.123  1.00 244.15 ? 213 LEU F CA  1 
ATOM   16007 C C   . LEU F 2 213 ? 50.127  6.213   44.138  1.00 243.83 ? 213 LEU F C   1 
ATOM   16008 O O   . LEU F 2 213 ? 50.216  5.279   43.329  1.00 242.07 ? 213 LEU F O   1 
ATOM   16009 C CB  . LEU F 2 213 ? 47.648  6.260   44.377  1.00 243.47 ? 213 LEU F CB  1 
ATOM   16010 C CG  . LEU F 2 213 ? 47.687  5.397   45.638  1.00 244.33 ? 213 LEU F CG  1 
ATOM   16011 C CD1 . LEU F 2 213 ? 47.797  6.273   46.876  1.00 245.79 ? 213 LEU F CD1 1 
ATOM   16012 C CD2 . LEU F 2 213 ? 46.463  4.500   45.719  1.00 243.28 ? 213 LEU F CD2 1 
ATOM   16013 N N   . PRO F 2 214 ? 51.093  6.456   45.027  1.00 247.45 ? 214 PRO F N   1 
ATOM   16014 C CA  . PRO F 2 214 ? 52.292  5.609   45.066  1.00 246.40 ? 214 PRO F CA  1 
ATOM   16015 C C   . PRO F 2 214 ? 52.142  4.404   45.984  1.00 241.84 ? 214 PRO F C   1 
ATOM   16016 O O   . PRO F 2 214 ? 53.085  4.047   46.696  1.00 240.88 ? 214 PRO F O   1 
ATOM   16017 C CB  . PRO F 2 214 ? 53.366  6.572   45.580  1.00 246.10 ? 214 PRO F CB  1 
ATOM   16018 C CG  . PRO F 2 214 ? 52.607  7.469   46.508  1.00 243.80 ? 214 PRO F CG  1 
ATOM   16019 C CD  . PRO F 2 214 ? 51.216  7.621   45.921  1.00 242.95 ? 214 PRO F CD  1 
ATOM   16020 N N   . GLY F 2 215 ? 50.970  3.770   45.980  1.00 236.38 ? 215 GLY F N   1 
ATOM   16021 C CA  . GLY F 2 215 ? 50.730  2.646   46.865  1.00 232.02 ? 215 GLY F CA  1 
ATOM   16022 C C   . GLY F 2 215 ? 49.789  1.602   46.299  1.00 230.58 ? 215 GLY F C   1 
ATOM   16023 O O   . GLY F 2 215 ? 49.547  1.564   45.089  1.00 232.57 ? 215 GLY F O   1 
ATOM   16024 N N   . PHE F 2 216 ? 49.253  0.746   47.164  1.00 190.37 ? 216 PHE F N   1 
ATOM   16025 C CA  . PHE F 2 216 ? 48.374  -0.330  46.736  1.00 184.20 ? 216 PHE F CA  1 
ATOM   16026 C C   . PHE F 2 216 ? 46.924  0.135   46.724  1.00 195.26 ? 216 PHE F C   1 
ATOM   16027 O O   . PHE F 2 216 ? 46.536  1.053   47.451  1.00 188.10 ? 216 PHE F O   1 
ATOM   16028 C CB  . PHE F 2 216 ? 48.530  -1.553  47.644  1.00 163.60 ? 216 PHE F CB  1 
ATOM   16029 C CG  . PHE F 2 216 ? 48.135  -1.307  49.074  1.00 158.78 ? 216 PHE F CG  1 
ATOM   16030 C CD1 . PHE F 2 216 ? 49.040  -0.769  49.974  1.00 155.42 ? 216 PHE F CD1 1 
ATOM   16031 C CD2 . PHE F 2 216 ? 46.864  -1.628  49.523  1.00 161.97 ? 216 PHE F CD2 1 
ATOM   16032 C CE1 . PHE F 2 216 ? 48.681  -0.545  51.290  1.00 151.89 ? 216 PHE F CE1 1 
ATOM   16033 C CE2 . PHE F 2 216 ? 46.501  -1.406  50.838  1.00 157.68 ? 216 PHE F CE2 1 
ATOM   16034 C CZ  . PHE F 2 216 ? 47.411  -0.865  51.722  1.00 153.74 ? 216 PHE F CZ  1 
ATOM   16035 N N   . TRP F 2 217 ? 46.123  -0.511  45.881  1.00 242.90 ? 217 TRP F N   1 
ATOM   16036 C CA  . TRP F 2 217 ? 44.704  -0.210  45.764  1.00 243.79 ? 217 TRP F CA  1 
ATOM   16037 C C   . TRP F 2 217 ? 43.927  -1.513  45.683  1.00 243.08 ? 217 TRP F C   1 
ATOM   16038 O O   . TRP F 2 217 ? 44.338  -2.447  44.990  1.00 241.68 ? 217 TRP F O   1 
ATOM   16039 C CB  . TRP F 2 217 ? 44.412  0.657   44.532  1.00 243.28 ? 217 TRP F CB  1 
ATOM   16040 C CG  . TRP F 2 217 ? 42.965  1.035   44.374  1.00 243.71 ? 217 TRP F CG  1 
ATOM   16041 C CD1 . TRP F 2 217 ? 42.334  2.111   44.927  1.00 245.56 ? 217 TRP F CD1 1 
ATOM   16042 C CD2 . TRP F 2 217 ? 41.976  0.346   43.598  1.00 243.21 ? 217 TRP F CD2 1 
ATOM   16043 N NE1 . TRP F 2 217 ? 41.012  2.131   44.550  1.00 246.26 ? 217 TRP F NE1 1 
ATOM   16044 C CE2 . TRP F 2 217 ? 40.767  1.058   43.733  1.00 244.34 ? 217 TRP F CE2 1 
ATOM   16045 C CE3 . TRP F 2 217 ? 41.995  -0.805  42.804  1.00 242.14 ? 217 TRP F CE3 1 
ATOM   16046 C CZ2 . TRP F 2 217 ? 39.589  0.657   43.105  1.00 243.69 ? 217 TRP F CZ2 1 
ATOM   16047 C CZ3 . TRP F 2 217 ? 40.824  -1.202  42.181  1.00 240.40 ? 217 TRP F CZ3 1 
ATOM   16048 C CH2 . TRP F 2 217 ? 39.638  -0.472  42.335  1.00 241.84 ? 217 TRP F CH2 1 
ATOM   16049 N N   . MET F 2 218 ? 42.810  -1.571  46.402  1.00 203.20 ? 218 MET F N   1 
ATOM   16050 C CA  . MET F 2 218 ? 41.979  -2.765  46.434  1.00 188.04 ? 218 MET F CA  1 
ATOM   16051 C C   . MET F 2 218 ? 40.549  -2.350  46.737  1.00 181.77 ? 218 MET F C   1 
ATOM   16052 O O   . MET F 2 218 ? 40.304  -1.638  47.715  1.00 170.80 ? 218 MET F O   1 
ATOM   16053 C CB  . MET F 2 218 ? 42.484  -3.765  47.481  1.00 169.93 ? 218 MET F CB  1 
ATOM   16054 C CG  . MET F 2 218 ? 41.576  -4.969  47.681  1.00 165.16 ? 218 MET F CG  1 
ATOM   16055 S SD  . MET F 2 218 ? 41.499  -6.044  46.236  1.00 160.40 ? 218 MET F SD  1 
ATOM   16056 C CE  . MET F 2 218 ? 43.197  -6.604  46.137  1.00 147.46 ? 218 MET F CE  1 
ATOM   16057 N N   . ASP F 2 219 ? 39.616  -2.796  45.903  1.00 176.86 ? 219 ASP F N   1 
ATOM   16058 C CA  . ASP F 2 219 ? 38.193  -2.547  46.103  1.00 172.66 ? 219 ASP F CA  1 
ATOM   16059 C C   . ASP F 2 219 ? 37.602  -3.760  46.810  1.00 169.16 ? 219 ASP F C   1 
ATOM   16060 O O   . ASP F 2 219 ? 37.402  -4.811  46.193  1.00 169.52 ? 219 ASP F O   1 
ATOM   16061 C CB  . ASP F 2 219 ? 37.495  -2.282  44.770  1.00 178.90 ? 219 ASP F CB  1 
ATOM   16062 C CG  . ASP F 2 219 ? 36.088  -1.734  44.941  1.00 173.41 ? 219 ASP F CG  1 
ATOM   16063 O OD1 . ASP F 2 219 ? 35.317  -2.279  45.760  1.00 161.94 ? 219 ASP F OD1 1 
ATOM   16064 O OD2 . ASP F 2 219 ? 35.751  -0.749  44.251  1.00 182.64 ? 219 ASP F OD2 1 
ATOM   16065 N N   . ILE F 2 220 ? 37.324  -3.612  48.103  1.00 159.38 ? 220 ILE F N   1 
ATOM   16066 C CA  . ILE F 2 220 ? 36.789  -4.696  48.918  1.00 157.51 ? 220 ILE F CA  1 
ATOM   16067 C C   . ILE F 2 220 ? 35.269  -4.649  48.792  1.00 152.89 ? 220 ILE F C   1 
ATOM   16068 O O   . ILE F 2 220 ? 34.604  -3.819  49.414  1.00 146.49 ? 220 ILE F O   1 
ATOM   16069 C CB  . ILE F 2 220 ? 37.242  -4.591  50.375  1.00 156.48 ? 220 ILE F CB  1 
ATOM   16070 C CG1 . ILE F 2 220 ? 38.771  -4.631  50.475  1.00 159.11 ? 220 ILE F CG1 1 
ATOM   16071 C CG2 . ILE F 2 220 ? 36.629  -5.710  51.204  1.00 170.33 ? 220 ILE F CG2 1 
ATOM   16072 C CD1 . ILE F 2 220 ? 39.433  -3.264  50.477  1.00 154.60 ? 220 ILE F CD1 1 
ATOM   16073 N N   . GLY F 2 221 ? 34.718  -5.548  47.981  1.00 149.44 ? 221 GLY F N   1 
ATOM   16074 C CA  . GLY F 2 221 ? 33.282  -5.638  47.812  1.00 146.83 ? 221 GLY F CA  1 
ATOM   16075 C C   . GLY F 2 221 ? 32.770  -7.053  47.974  1.00 140.01 ? 221 GLY F C   1 
ATOM   16076 O O   . GLY F 2 221 ? 31.601  -7.337  47.697  1.00 140.31 ? 221 GLY F O   1 
ATOM   16077 N N   . GLN F 2 222 ? 33.640  -7.950  48.430  1.00 138.70 ? 222 GLN F N   1 
ATOM   16078 C CA  . GLN F 2 222 ? 33.300  -9.352  48.618  1.00 138.33 ? 222 GLN F CA  1 
ATOM   16079 C C   . GLN F 2 222 ? 34.171  -9.916  49.728  1.00 140.68 ? 222 GLN F C   1 
ATOM   16080 O O   . GLN F 2 222 ? 35.312  -9.473  49.901  1.00 144.11 ? 222 GLN F O   1 
ATOM   16081 C CB  . GLN F 2 222 ? 33.497  -10.158 47.325  1.00 143.04 ? 222 GLN F CB  1 
ATOM   16082 C CG  . GLN F 2 222 ? 34.898  -10.070 46.747  1.00 147.10 ? 222 GLN F CG  1 
ATOM   16083 C CD  . GLN F 2 222 ? 34.978  -10.605 45.331  1.00 149.03 ? 222 GLN F CD  1 
ATOM   16084 O OE1 . GLN F 2 222 ? 33.966  -10.714 44.639  1.00 149.16 ? 222 GLN F OE1 1 
ATOM   16085 N NE2 . GLN F 2 222 ? 36.185  -10.948 44.894  1.00 150.84 ? 222 GLN F NE2 1 
ATOM   16086 N N   . PRO F 2 223 ? 33.659  -10.873 50.507  1.00 140.38 ? 223 PRO F N   1 
ATOM   16087 C CA  . PRO F 2 223 ? 34.436  -11.381 51.651  1.00 148.35 ? 223 PRO F CA  1 
ATOM   16088 C C   . PRO F 2 223 ? 35.737  -12.071 51.271  1.00 156.56 ? 223 PRO F C   1 
ATOM   16089 O O   . PRO F 2 223 ? 36.639  -12.152 52.113  1.00 167.82 ? 223 PRO F O   1 
ATOM   16090 C CB  . PRO F 2 223 ? 33.465  -12.358 52.330  1.00 140.90 ? 223 PRO F CB  1 
ATOM   16091 C CG  . PRO F 2 223 ? 32.472  -12.717 51.271  1.00 133.92 ? 223 PRO F CG  1 
ATOM   16092 C CD  . PRO F 2 223 ? 32.324  -11.488 50.430  1.00 134.43 ? 223 PRO F CD  1 
ATOM   16093 N N   . ARG F 2 224 ? 35.871  -12.572 50.041  1.00 149.22 ? 224 ARG F N   1 
ATOM   16094 C CA  . ARG F 2 224 ? 37.099  -13.253 49.649  1.00 152.26 ? 224 ARG F CA  1 
ATOM   16095 C C   . ARG F 2 224 ? 38.253  -12.296 49.376  1.00 164.96 ? 224 ARG F C   1 
ATOM   16096 O O   . ARG F 2 224 ? 39.405  -12.739 49.333  1.00 174.68 ? 224 ARG F O   1 
ATOM   16097 C CB  . ARG F 2 224 ? 36.850  -14.130 48.420  1.00 147.69 ? 224 ARG F CB  1 
ATOM   16098 C CG  . ARG F 2 224 ? 36.409  -13.374 47.179  1.00 149.58 ? 224 ARG F CG  1 
ATOM   16099 C CD  . ARG F 2 224 ? 36.090  -14.334 46.042  1.00 147.27 ? 224 ARG F CD  1 
ATOM   16100 N NE  . ARG F 2 224 ? 35.130  -15.357 46.444  1.00 146.09 ? 224 ARG F NE  1 
ATOM   16101 C CZ  . ARG F 2 224 ? 33.811  -15.191 46.443  1.00 150.84 ? 224 ARG F CZ  1 
ATOM   16102 N NH1 . ARG F 2 224 ? 33.286  -14.035 46.059  1.00 153.46 ? 224 ARG F NH1 1 
ATOM   16103 N NH2 . ARG F 2 224 ? 33.016  -16.181 46.826  1.00 149.59 ? 224 ARG F NH2 1 
ATOM   16104 N N   . ASP F 2 225 ? 37.982  -11.003 49.191  1.00 169.27 ? 225 ASP F N   1 
ATOM   16105 C CA  . ASP F 2 225 ? 39.064  -10.047 48.979  1.00 176.33 ? 225 ASP F CA  1 
ATOM   16106 C C   . ASP F 2 225 ? 39.828  -9.715  50.255  1.00 195.60 ? 225 ASP F C   1 
ATOM   16107 O O   . ASP F 2 225 ? 40.829  -8.995  50.179  1.00 191.45 ? 225 ASP F O   1 
ATOM   16108 C CB  . ASP F 2 225 ? 38.526  -8.757  48.356  1.00 164.60 ? 225 ASP F CB  1 
ATOM   16109 C CG  . ASP F 2 225 ? 38.158  -8.927  46.898  1.00 159.66 ? 225 ASP F CG  1 
ATOM   16110 O OD1 . ASP F 2 225 ? 38.448  -10.004 46.333  1.00 158.34 ? 225 ASP F OD1 1 
ATOM   16111 O OD2 . ASP F 2 225 ? 37.586  -7.983  46.317  1.00 154.62 ? 225 ASP F OD2 1 
ATOM   16112 N N   . TYR F 2 226 ? 39.388  -10.210 51.414  1.00 260.35 ? 226 TYR F N   1 
ATOM   16113 C CA  . TYR F 2 226 ? 40.073  -9.880  52.660  1.00 262.04 ? 226 TYR F CA  1 
ATOM   16114 C C   . TYR F 2 226 ? 41.421  -10.580 52.773  1.00 260.95 ? 226 TYR F C   1 
ATOM   16115 O O   . TYR F 2 226 ? 42.345  -10.037 53.389  1.00 260.98 ? 226 TYR F O   1 
ATOM   16116 C CB  . TYR F 2 226 ? 39.194  -10.235 53.861  1.00 264.43 ? 226 TYR F CB  1 
ATOM   16117 C CG  . TYR F 2 226 ? 38.214  -9.151  54.259  1.00 266.28 ? 226 TYR F CG  1 
ATOM   16118 C CD1 . TYR F 2 226 ? 38.566  -7.808  54.188  1.00 266.54 ? 226 TYR F CD1 1 
ATOM   16119 C CD2 . TYR F 2 226 ? 36.939  -9.470  54.709  1.00 267.72 ? 226 TYR F CD2 1 
ATOM   16120 C CE1 . TYR F 2 226 ? 37.676  -6.814  54.552  1.00 268.09 ? 226 TYR F CE1 1 
ATOM   16121 C CE2 . TYR F 2 226 ? 36.041  -8.482  55.074  1.00 269.20 ? 226 TYR F CE2 1 
ATOM   16122 C CZ  . TYR F 2 226 ? 36.415  -7.156  54.994  1.00 269.23 ? 226 TYR F CZ  1 
ATOM   16123 O OH  . TYR F 2 226 ? 35.528  -6.168  55.356  1.00 270.73 ? 226 TYR F OH  1 
ATOM   16124 N N   . ILE F 2 227 ? 41.561  -11.773 52.195  1.00 224.73 ? 227 ILE F N   1 
ATOM   16125 C CA  . ILE F 2 227 ? 42.837  -12.475 52.294  1.00 220.85 ? 227 ILE F CA  1 
ATOM   16126 C C   . ILE F 2 227 ? 43.839  -11.931 51.283  1.00 217.24 ? 227 ILE F C   1 
ATOM   16127 O O   . ILE F 2 227 ? 45.042  -11.887 51.561  1.00 213.67 ? 227 ILE F O   1 
ATOM   16128 C CB  . ILE F 2 227 ? 42.643  -13.992 52.128  1.00 216.72 ? 227 ILE F CB  1 
ATOM   16129 C CG1 . ILE F 2 227 ? 41.928  -14.311 50.812  1.00 214.63 ? 227 ILE F CG1 1 
ATOM   16130 C CG2 . ILE F 2 227 ? 41.855  -14.550 53.300  1.00 212.16 ? 227 ILE F CG2 1 
ATOM   16131 C CD1 . ILE F 2 227 ? 41.660  -15.789 50.603  1.00 208.11 ? 227 ILE F CD1 1 
ATOM   16132 N N   . THR F 2 228 ? 43.374  -11.508 50.106  1.00 196.30 ? 228 THR F N   1 
ATOM   16133 C CA  . THR F 2 228 ? 44.278  -10.923 49.123  1.00 184.42 ? 228 THR F CA  1 
ATOM   16134 C C   . THR F 2 228 ? 44.513  -9.442  49.389  1.00 177.12 ? 228 THR F C   1 
ATOM   16135 O O   . THR F 2 228 ? 45.576  -8.916  49.043  1.00 169.14 ? 228 THR F O   1 
ATOM   16136 C CB  . THR F 2 228 ? 43.737  -11.134 47.705  1.00 174.71 ? 228 THR F CB  1 
ATOM   16137 O OG1 . THR F 2 228 ? 44.639  -10.553 46.756  1.00 169.14 ? 228 THR F OG1 1 
ATOM   16138 C CG2 . THR F 2 228 ? 42.363  -10.501 47.548  1.00 171.72 ? 228 THR F CG2 1 
ATOM   16139 N N   . GLY F 2 229 ? 43.541  -8.756  49.993  1.00 182.49 ? 229 GLY F N   1 
ATOM   16140 C CA  . GLY F 2 229 ? 43.755  -7.376  50.387  1.00 171.43 ? 229 GLY F CA  1 
ATOM   16141 C C   . GLY F 2 229 ? 44.648  -7.240  51.602  1.00 170.31 ? 229 GLY F C   1 
ATOM   16142 O O   . GLY F 2 229 ? 45.324  -6.219  51.767  1.00 164.32 ? 229 GLY F O   1 
ATOM   16143 N N   . LEU F 2 230 ? 44.668  -8.259  52.465  1.00 176.56 ? 230 LEU F N   1 
ATOM   16144 C CA  . LEU F 2 230 ? 45.565  -8.235  53.615  1.00 169.91 ? 230 LEU F CA  1 
ATOM   16145 C C   . LEU F 2 230 ? 47.019  -8.387  53.191  1.00 171.53 ? 230 LEU F C   1 
ATOM   16146 O O   . LEU F 2 230 ? 47.920  -7.897  53.884  1.00 164.27 ? 230 LEU F O   1 
ATOM   16147 C CB  . LEU F 2 230 ? 45.176  -9.332  54.609  1.00 165.68 ? 230 LEU F CB  1 
ATOM   16148 C CG  . LEU F 2 230 ? 45.908  -9.365  55.954  1.00 143.98 ? 230 LEU F CG  1 
ATOM   16149 C CD1 . LEU F 2 230 ? 44.911  -9.329  57.096  1.00 137.03 ? 230 LEU F CD1 1 
ATOM   16150 C CD2 . LEU F 2 230 ? 46.781  -10.604 56.055  1.00 135.92 ? 230 LEU F CD2 1 
ATOM   16151 N N   . ARG F 2 231 ? 47.267  -9.057  52.064  1.00 202.40 ? 231 ARG F N   1 
ATOM   16152 C CA  . ARG F 2 231 ? 48.624  -9.142  51.535  1.00 200.70 ? 231 ARG F CA  1 
ATOM   16153 C C   . ARG F 2 231 ? 49.139  -7.763  51.142  1.00 200.55 ? 231 ARG F C   1 
ATOM   16154 O O   . ARG F 2 231 ? 50.246  -7.370  51.524  1.00 200.29 ? 231 ARG F O   1 
ATOM   16155 C CB  . ARG F 2 231 ? 48.664  -10.101 50.342  1.00 199.04 ? 231 ARG F CB  1 
ATOM   16156 C CG  . ARG F 2 231 ? 50.005  -10.155 49.616  1.00 197.71 ? 231 ARG F CG  1 
ATOM   16157 C CD  . ARG F 2 231 ? 51.149  -10.329 50.601  1.00 203.58 ? 231 ARG F CD  1 
ATOM   16158 N NE  . ARG F 2 231 ? 52.147  -11.298 50.162  1.00 210.82 ? 231 ARG F NE  1 
ATOM   16159 C CZ  . ARG F 2 231 ? 53.210  -11.646 50.881  1.00 204.87 ? 231 ARG F CZ  1 
ATOM   16160 N NH1 . ARG F 2 231 ? 53.410  -11.105 52.076  1.00 197.82 ? 231 ARG F NH1 1 
ATOM   16161 N NH2 . ARG F 2 231 ? 54.071  -12.538 50.412  1.00 204.51 ? 231 ARG F NH2 1 
ATOM   16162 N N   . LEU F 2 232 ? 48.341  -7.012  50.379  1.00 175.10 ? 232 LEU F N   1 
ATOM   16163 C CA  . LEU F 2 232 ? 48.752  -5.670  49.981  1.00 164.29 ? 232 LEU F CA  1 
ATOM   16164 C C   . LEU F 2 232 ? 48.973  -4.775  51.192  1.00 165.13 ? 232 LEU F C   1 
ATOM   16165 O O   . LEU F 2 232 ? 49.839  -3.893  51.164  1.00 164.02 ? 232 LEU F O   1 
ATOM   16166 C CB  . LEU F 2 232 ? 47.709  -5.056  49.048  1.00 150.51 ? 232 LEU F CB  1 
ATOM   16167 C CG  . LEU F 2 232 ? 47.442  -5.803  47.741  1.00 139.71 ? 232 LEU F CG  1 
ATOM   16168 C CD1 . LEU F 2 232 ? 46.425  -5.051  46.900  1.00 143.00 ? 232 LEU F CD1 1 
ATOM   16169 C CD2 . LEU F 2 232 ? 48.733  -6.012  46.966  1.00 132.40 ? 232 LEU F CD2 1 
ATOM   16170 N N   . TYR F 2 233 ? 48.199  -4.980  52.260  1.00 172.04 ? 233 TYR F N   1 
ATOM   16171 C CA  . TYR F 2 233 ? 48.387  -4.187  53.470  1.00 174.50 ? 233 TYR F CA  1 
ATOM   16172 C C   . TYR F 2 233 ? 49.657  -4.597  54.205  1.00 173.99 ? 233 TYR F C   1 
ATOM   16173 O O   . TYR F 2 233 ? 50.483  -3.746  54.557  1.00 172.92 ? 233 TYR F O   1 
ATOM   16174 C CB  . TYR F 2 233 ? 47.171  -4.322  54.387  1.00 177.09 ? 233 TYR F CB  1 
ATOM   16175 C CG  . TYR F 2 233 ? 47.351  -3.626  55.716  1.00 181.36 ? 233 TYR F CG  1 
ATOM   16176 C CD1 . TYR F 2 233 ? 47.248  -2.245  55.818  1.00 184.40 ? 233 TYR F CD1 1 
ATOM   16177 C CD2 . TYR F 2 233 ? 47.634  -4.349  56.868  1.00 178.33 ? 233 TYR F CD2 1 
ATOM   16178 C CE1 . TYR F 2 233 ? 47.418  -1.604  57.031  1.00 182.77 ? 233 TYR F CE1 1 
ATOM   16179 C CE2 . TYR F 2 233 ? 47.805  -3.717  58.085  1.00 177.23 ? 233 TYR F CE2 1 
ATOM   16180 C CZ  . TYR F 2 233 ? 47.695  -2.345  58.160  1.00 177.88 ? 233 TYR F CZ  1 
ATOM   16181 O OH  . TYR F 2 233 ? 47.865  -1.712  59.370  1.00 177.08 ? 233 TYR F OH  1 
ATOM   16182 N N   . LEU F 2 234 ? 49.828  -5.899  54.454  1.00 171.60 ? 234 LEU F N   1 
ATOM   16183 C CA  . LEU F 2 234 ? 51.022  -6.363  55.155  1.00 166.50 ? 234 LEU F CA  1 
ATOM   16184 C C   . LEU F 2 234 ? 52.283  -6.140  54.332  1.00 170.92 ? 234 LEU F C   1 
ATOM   16185 O O   . LEU F 2 234 ? 53.368  -5.965  54.899  1.00 167.20 ? 234 LEU F O   1 
ATOM   16186 C CB  . LEU F 2 234 ? 50.884  -7.841  55.525  1.00 153.44 ? 234 LEU F CB  1 
ATOM   16187 C CG  . LEU F 2 234 ? 49.944  -8.180  56.684  1.00 142.45 ? 234 LEU F CG  1 
ATOM   16188 C CD1 . LEU F 2 234 ? 50.099  -9.638  57.085  1.00 133.11 ? 234 LEU F CD1 1 
ATOM   16189 C CD2 . LEU F 2 234 ? 50.196  -7.266  57.874  1.00 141.62 ? 234 LEU F CD2 1 
ATOM   16190 N N   . ASP F 2 235 ? 52.168  -6.150  53.002  1.00 184.68 ? 235 ASP F N   1 
ATOM   16191 C CA  . ASP F 2 235 ? 53.321  -5.849  52.160  1.00 183.93 ? 235 ASP F CA  1 
ATOM   16192 C C   . ASP F 2 235 ? 53.772  -4.406  52.351  1.00 183.82 ? 235 ASP F C   1 
ATOM   16193 O O   . ASP F 2 235 ? 54.968  -4.134  52.505  1.00 183.26 ? 235 ASP F O   1 
ATOM   16194 C CB  . ASP F 2 235 ? 52.984  -6.119  50.693  1.00 187.42 ? 235 ASP F CB  1 
ATOM   16195 C CG  . ASP F 2 235 ? 54.186  -5.987  49.783  1.00 193.79 ? 235 ASP F CG  1 
ATOM   16196 O OD1 . ASP F 2 235 ? 55.326  -5.977  50.295  1.00 190.15 ? 235 ASP F OD1 1 
ATOM   16197 O OD2 . ASP F 2 235 ? 53.990  -5.887  48.554  1.00 199.42 ? 235 ASP F OD2 1 
ATOM   16198 N N   . SER F 2 236 ? 52.822  -3.467  52.344  1.00 174.36 ? 236 SER F N   1 
ATOM   16199 C CA  . SER F 2 236 ? 53.159  -2.068  52.588  1.00 167.01 ? 236 SER F CA  1 
ATOM   16200 C C   . SER F 2 236 ? 53.708  -1.857  53.993  1.00 164.12 ? 236 SER F C   1 
ATOM   16201 O O   . SER F 2 236 ? 54.491  -0.926  54.218  1.00 158.96 ? 236 SER F O   1 
ATOM   16202 C CB  . SER F 2 236 ? 51.932  -1.186  52.360  1.00 161.40 ? 236 SER F CB  1 
ATOM   16203 O OG  . SER F 2 236 ? 52.239  0.182   52.569  1.00 151.06 ? 236 SER F OG  1 
ATOM   16204 N N   . LEU F 2 237 ? 53.314  -2.702  54.949  1.00 171.14 ? 237 LEU F N   1 
ATOM   16205 C CA  . LEU F 2 237 ? 53.850  -2.585  56.302  1.00 169.64 ? 237 LEU F CA  1 
ATOM   16206 C C   . LEU F 2 237 ? 55.317  -2.986  56.364  1.00 167.67 ? 237 LEU F C   1 
ATOM   16207 O O   . LEU F 2 237 ? 56.079  -2.418  57.154  1.00 167.43 ? 237 LEU F O   1 
ATOM   16208 C CB  . LEU F 2 237 ? 53.029  -3.430  57.275  1.00 170.83 ? 237 LEU F CB  1 
ATOM   16209 C CG  . LEU F 2 237 ? 52.038  -2.664  58.153  1.00 174.31 ? 237 LEU F CG  1 
ATOM   16210 C CD1 . LEU F 2 237 ? 51.042  -1.892  57.302  1.00 179.06 ? 237 LEU F CD1 1 
ATOM   16211 C CD2 . LEU F 2 237 ? 51.318  -3.607  59.106  1.00 175.60 ? 237 LEU F CD2 1 
ATOM   16212 N N   . ARG F 2 238 ? 55.730  -3.961  55.551  1.00 158.56 ? 238 ARG F N   1 
ATOM   16213 C CA  . ARG F 2 238 ? 57.144  -4.312  55.471  1.00 151.12 ? 238 ARG F CA  1 
ATOM   16214 C C   . ARG F 2 238 ? 57.998  -3.143  54.996  1.00 151.85 ? 238 ARG F C   1 
ATOM   16215 O O   . ARG F 2 238 ? 59.207  -3.129  55.251  1.00 145.32 ? 238 ARG F O   1 
ATOM   16216 C CB  . ARG F 2 238 ? 57.336  -5.519  54.551  1.00 146.41 ? 238 ARG F CB  1 
ATOM   16217 C CG  . ARG F 2 238 ? 58.015  -6.699  55.228  1.00 135.08 ? 238 ARG F CG  1 
ATOM   16218 C CD  . ARG F 2 238 ? 57.363  -6.991  56.570  1.00 136.41 ? 238 ARG F CD  1 
ATOM   16219 N NE  . ARG F 2 238 ? 58.329  -7.017  57.666  1.00 131.73 ? 238 ARG F NE  1 
ATOM   16220 C CZ  . ARG F 2 238 ? 58.565  -8.077  58.433  1.00 124.08 ? 238 ARG F CZ  1 
ATOM   16221 N NH1 . ARG F 2 238 ? 57.896  -9.206  58.235  1.00 122.58 ? 238 ARG F NH1 1 
ATOM   16222 N NH2 . ARG F 2 238 ? 59.463  -8.006  59.405  1.00 119.51 ? 238 ARG F NH2 1 
ATOM   16223 N N   . LYS F 2 239 ? 57.398  -2.168  54.314  1.00 157.97 ? 239 LYS F N   1 
ATOM   16224 C CA  . LYS F 2 239 ? 58.108  -0.989  53.835  1.00 154.82 ? 239 LYS F CA  1 
ATOM   16225 C C   . LYS F 2 239 ? 58.018  0.172   54.821  1.00 154.98 ? 239 LYS F C   1 
ATOM   16226 O O   . LYS F 2 239 ? 59.036  0.784   55.157  1.00 155.79 ? 239 LYS F O   1 
ATOM   16227 C CB  . LYS F 2 239 ? 57.547  -0.561  52.475  1.00 154.13 ? 239 LYS F CB  1 
ATOM   16228 C CG  . LYS F 2 239 ? 57.137  -1.716  51.578  1.00 158.49 ? 239 LYS F CG  1 
ATOM   16229 C CD  . LYS F 2 239 ? 56.277  -1.230  50.423  1.00 164.67 ? 239 LYS F CD  1 
ATOM   16230 C CE  . LYS F 2 239 ? 55.830  -2.382  49.538  1.00 173.59 ? 239 LYS F CE  1 
ATOM   16231 N NZ  . LYS F 2 239 ? 54.420  -2.215  49.086  1.00 174.02 ? 239 LYS F NZ  1 
ATOM   16232 N N   . LYS F 2 240 ? 56.807  0.486   55.289  1.00 153.77 ? 240 LYS F N   1 
ATOM   16233 C CA  . LYS F 2 240 ? 56.618  1.639   56.166  1.00 149.83 ? 240 LYS F CA  1 
ATOM   16234 C C   . LYS F 2 240 ? 57.302  1.431   57.513  1.00 150.92 ? 240 LYS F C   1 
ATOM   16235 O O   . LYS F 2 240 ? 58.233  2.163   57.871  1.00 144.23 ? 240 LYS F O   1 
ATOM   16236 C CB  . LYS F 2 240 ? 55.123  1.909   56.355  1.00 144.77 ? 240 LYS F CB  1 
ATOM   16237 C CG  . LYS F 2 240 ? 54.391  2.269   55.069  1.00 138.80 ? 240 LYS F CG  1 
ATOM   16238 C CD  . LYS F 2 240 ? 55.052  3.449   54.373  1.00 132.88 ? 240 LYS F CD  1 
ATOM   16239 C CE  . LYS F 2 240 ? 54.176  3.980   53.252  1.00 130.39 ? 240 LYS F CE  1 
ATOM   16240 N NZ  . LYS F 2 240 ? 52.732  3.849   53.597  1.00 131.57 ? 240 LYS F NZ  1 
ATOM   16241 N N   . SER F 2 241 ? 56.854  0.434   58.273  1.00 156.91 ? 241 SER F N   1 
ATOM   16242 C CA  . SER F 2 241 ? 57.418  0.132   59.587  1.00 152.23 ? 241 SER F CA  1 
ATOM   16243 C C   . SER F 2 241 ? 57.533  -1.382  59.710  1.00 154.31 ? 241 SER F C   1 
ATOM   16244 O O   . SER F 2 241 ? 56.539  -2.066  60.004  1.00 160.51 ? 241 SER F O   1 
ATOM   16245 C CB  . SER F 2 241 ? 56.565  0.714   60.712  1.00 156.54 ? 241 SER F CB  1 
ATOM   16246 O OG  . SER F 2 241 ? 55.185  0.517   60.457  1.00 166.13 ? 241 SER F OG  1 
ATOM   16247 N N   . PRO F 2 242 ? 58.727  -1.941  59.495  1.00 144.22 ? 242 PRO F N   1 
ATOM   16248 C CA  . PRO F 2 242 ? 58.878  -3.404  59.517  1.00 140.67 ? 242 PRO F CA  1 
ATOM   16249 C C   . PRO F 2 242 ? 58.877  -4.019  60.906  1.00 141.21 ? 242 PRO F C   1 
ATOM   16250 O O   . PRO F 2 242 ? 58.781  -5.250  61.012  1.00 139.23 ? 242 PRO F O   1 
ATOM   16251 C CB  . PRO F 2 242 ? 60.231  -3.619  58.827  1.00 136.26 ? 242 PRO F CB  1 
ATOM   16252 C CG  . PRO F 2 242 ? 60.998  -2.373  59.121  1.00 136.97 ? 242 PRO F CG  1 
ATOM   16253 C CD  . PRO F 2 242 ? 59.987  -1.253  59.162  1.00 142.16 ? 242 PRO F CD  1 
ATOM   16254 N N   . ALA F 2 243 ? 58.977  -3.218  61.964  1.00 145.84 ? 243 ALA F N   1 
ATOM   16255 C CA  . ALA F 2 243 ? 58.964  -3.727  63.328  1.00 146.25 ? 243 ALA F CA  1 
ATOM   16256 C C   . ALA F 2 243 ? 57.557  -3.919  63.871  1.00 156.38 ? 243 ALA F C   1 
ATOM   16257 O O   . ALA F 2 243 ? 57.402  -4.356  65.016  1.00 152.26 ? 243 ALA F O   1 
ATOM   16258 C CB  . ALA F 2 243 ? 59.746  -2.785  64.250  1.00 138.63 ? 243 ALA F CB  1 
ATOM   16259 N N   . LYS F 2 244 ? 56.532  -3.609  63.080  1.00 180.24 ? 244 LYS F N   1 
ATOM   16260 C CA  . LYS F 2 244 ? 55.152  -3.826  63.486  1.00 181.46 ? 244 LYS F CA  1 
ATOM   16261 C C   . LYS F 2 244 ? 54.645  -5.217  63.135  1.00 180.75 ? 244 LYS F C   1 
ATOM   16262 O O   . LYS F 2 244 ? 53.532  -5.573  63.534  1.00 181.61 ? 244 LYS F O   1 
ATOM   16263 C CB  . LYS F 2 244 ? 54.241  -2.780  62.836  1.00 182.27 ? 244 LYS F CB  1 
ATOM   16264 C CG  . LYS F 2 244 ? 54.656  -1.346  63.111  1.00 183.08 ? 244 LYS F CG  1 
ATOM   16265 C CD  . LYS F 2 244 ? 54.117  -0.848  64.439  1.00 185.11 ? 244 LYS F CD  1 
ATOM   16266 C CE  . LYS F 2 244 ? 55.248  -0.523  65.400  1.00 188.50 ? 244 LYS F CE  1 
ATOM   16267 N NZ  . LYS F 2 244 ? 54.747  -0.180  66.759  1.00 192.31 ? 244 LYS F NZ  1 
ATOM   16268 N N   . LEU F 2 245 ? 55.427  -6.003  62.404  1.00 161.15 ? 245 LEU F N   1 
ATOM   16269 C CA  . LEU F 2 245 ? 55.055  -7.355  62.014  1.00 154.65 ? 245 LEU F CA  1 
ATOM   16270 C C   . LEU F 2 245 ? 55.878  -8.346  62.825  1.00 156.51 ? 245 LEU F C   1 
ATOM   16271 O O   . LEU F 2 245 ? 57.108  -8.235  62.883  1.00 153.86 ? 245 LEU F O   1 
ATOM   16272 C CB  . LEU F 2 245 ? 55.277  -7.574  60.515  1.00 145.31 ? 245 LEU F CB  1 
ATOM   16273 C CG  . LEU F 2 245 ? 54.595  -6.575  59.577  1.00 146.35 ? 245 LEU F CG  1 
ATOM   16274 C CD1 . LEU F 2 245 ? 55.508  -5.396  59.257  1.00 149.88 ? 245 LEU F CD1 1 
ATOM   16275 C CD2 . LEU F 2 245 ? 54.140  -7.263  58.308  1.00 141.40 ? 245 LEU F CD2 1 
ATOM   16276 N N   . THR F 2 246 ? 55.202  -9.303  63.455  1.00 158.95 ? 246 THR F N   1 
ATOM   16277 C CA  . THR F 2 246 ? 55.892  -10.248 64.320  1.00 157.95 ? 246 THR F CA  1 
ATOM   16278 C C   . THR F 2 246 ? 56.843  -11.129 63.516  1.00 160.87 ? 246 THR F C   1 
ATOM   16279 O O   . THR F 2 246 ? 56.663  -11.352 62.315  1.00 158.43 ? 246 THR F O   1 
ATOM   16280 C CB  . THR F 2 246 ? 54.892  -11.124 65.076  1.00 154.18 ? 246 THR F CB  1 
ATOM   16281 O OG1 . THR F 2 246 ? 55.595  -11.984 65.981  1.00 156.09 ? 246 THR F OG1 1 
ATOM   16282 C CG2 . THR F 2 246 ? 54.092  -11.977 64.110  1.00 151.73 ? 246 THR F CG2 1 
ATOM   16283 N N   . SER F 2 247 ? 57.870  -11.627 64.199  1.00 169.72 ? 247 SER F N   1 
ATOM   16284 C CA  . SER F 2 247 ? 58.875  -12.480 63.587  1.00 167.06 ? 247 SER F CA  1 
ATOM   16285 C C   . SER F 2 247 ? 59.284  -13.547 64.590  1.00 167.04 ? 247 SER F C   1 
ATOM   16286 O O   . SER F 2 247 ? 59.057  -13.416 65.795  1.00 167.91 ? 247 SER F O   1 
ATOM   16287 C CB  . SER F 2 247 ? 60.098  -11.677 63.128  1.00 166.54 ? 247 SER F CB  1 
ATOM   16288 O OG  . SER F 2 247 ? 61.099  -12.530 62.599  1.00 166.24 ? 247 SER F OG  1 
ATOM   16289 N N   . GLY F 2 248 ? 59.893  -14.612 64.079  1.00 147.92 ? 248 GLY F N   1 
ATOM   16290 C CA  . GLY F 2 248 ? 60.346  -15.688 64.924  1.00 140.51 ? 248 GLY F CA  1 
ATOM   16291 C C   . GLY F 2 248 ? 60.590  -16.971 64.160  1.00 135.91 ? 248 GLY F C   1 
ATOM   16292 O O   . GLY F 2 248 ? 60.470  -17.027 62.932  1.00 136.73 ? 248 GLY F O   1 
ATOM   16293 N N   . PRO F 2 249 ? 60.941  -18.036 64.884  1.00 134.03 ? 249 PRO F N   1 
ATOM   16294 C CA  . PRO F 2 249 ? 61.194  -19.321 64.217  1.00 134.41 ? 249 PRO F CA  1 
ATOM   16295 C C   . PRO F 2 249 ? 59.936  -19.986 63.688  1.00 140.27 ? 249 PRO F C   1 
ATOM   16296 O O   . PRO F 2 249 ? 60.030  -20.786 62.749  1.00 140.52 ? 249 PRO F O   1 
ATOM   16297 C CB  . PRO F 2 249 ? 61.855  -20.160 65.316  1.00 132.25 ? 249 PRO F CB  1 
ATOM   16298 C CG  . PRO F 2 249 ? 61.316  -19.590 66.587  1.00 137.16 ? 249 PRO F CG  1 
ATOM   16299 C CD  . PRO F 2 249 ? 61.122  -18.118 66.344  1.00 134.51 ? 249 PRO F CD  1 
ATOM   16300 N N   . HIS F 2 250 ? 58.767  -19.685 64.252  1.00 152.19 ? 250 HIS F N   1 
ATOM   16301 C CA  . HIS F 2 250 ? 57.507  -20.227 63.766  1.00 152.41 ? 250 HIS F CA  1 
ATOM   16302 C C   . HIS F 2 250 ? 56.771  -19.246 62.864  1.00 152.09 ? 250 HIS F C   1 
ATOM   16303 O O   . HIS F 2 250 ? 55.630  -19.513 62.472  1.00 152.29 ? 250 HIS F O   1 
ATOM   16304 C CB  . HIS F 2 250 ? 56.603  -20.611 64.938  1.00 153.84 ? 250 HIS F CB  1 
ATOM   16305 C CG  . HIS F 2 250 ? 56.174  -19.445 65.772  1.00 155.03 ? 250 HIS F CG  1 
ATOM   16306 N ND1 . HIS F 2 250 ? 57.033  -18.766 66.608  1.00 155.18 ? 250 HIS F ND1 1 
ATOM   16307 C CD2 . HIS F 2 250 ? 54.973  -18.830 65.888  1.00 156.08 ? 250 HIS F CD2 1 
ATOM   16308 C CE1 . HIS F 2 250 ? 56.379  -17.787 67.208  1.00 156.47 ? 250 HIS F CE1 1 
ATOM   16309 N NE2 . HIS F 2 250 ? 55.127  -17.804 66.788  1.00 156.95 ? 250 HIS F NE2 1 
ATOM   16310 N N   . ILE F 2 251 ? 57.400  -18.125 62.521  1.00 138.71 ? 251 ILE F N   1 
ATOM   16311 C CA  . ILE F 2 251 ? 56.787  -17.079 61.714  1.00 128.54 ? 251 ILE F CA  1 
ATOM   16312 C C   . ILE F 2 251 ? 57.462  -17.071 60.352  1.00 118.42 ? 251 ILE F C   1 
ATOM   16313 O O   . ILE F 2 251 ? 58.696  -17.089 60.262  1.00 116.95 ? 251 ILE F O   1 
ATOM   16314 C CB  . ILE F 2 251 ? 56.898  -15.703 62.396  1.00 135.92 ? 251 ILE F CB  1 
ATOM   16315 C CG1 . ILE F 2 251 ? 56.192  -15.721 63.755  1.00 139.98 ? 251 ILE F CG1 1 
ATOM   16316 C CG2 . ILE F 2 251 ? 56.324  -14.613 61.506  1.00 133.11 ? 251 ILE F CG2 1 
ATOM   16317 C CD1 . ILE F 2 251 ? 54.708  -16.012 63.669  1.00 130.98 ? 251 ILE F CD1 1 
ATOM   16318 N N   . VAL F 2 252 ? 56.656  -17.039 59.295  1.00 113.29 ? 252 VAL F N   1 
ATOM   16319 C CA  . VAL F 2 252 ? 57.147  -17.006 57.925  1.00 106.73 ? 252 VAL F CA  1 
ATOM   16320 C C   . VAL F 2 252 ? 56.416  -15.896 57.185  1.00 103.55 ? 252 VAL F C   1 
ATOM   16321 O O   . VAL F 2 252 ? 55.186  -15.800 57.257  1.00 105.22 ? 252 VAL F O   1 
ATOM   16322 C CB  . VAL F 2 252 ? 56.956  -18.359 57.212  1.00 104.00 ? 252 VAL F CB  1 
ATOM   16323 C CG1 . VAL F 2 252 ? 57.987  -19.360 57.703  1.00 104.72 ? 252 VAL F CG1 1 
ATOM   16324 C CG2 . VAL F 2 252 ? 55.551  -18.894 57.446  1.00 106.75 ? 252 VAL F CG2 1 
ATOM   16325 N N   . GLY F 2 253 ? 57.172  -15.052 56.492  1.00 101.70 ? 253 GLY F N   1 
ATOM   16326 C CA  . GLY F 2 253 ? 56.571  -13.965 55.750  1.00 105.64 ? 253 GLY F CA  1 
ATOM   16327 C C   . GLY F 2 253 ? 56.137  -12.822 56.641  1.00 111.68 ? 253 GLY F C   1 
ATOM   16328 O O   . GLY F 2 253 ? 56.842  -12.451 57.584  1.00 110.81 ? 253 GLY F O   1 
ATOM   16329 N N   . ASN F 2 254 ? 54.973  -12.255 56.343  1.00 119.20 ? 254 ASN F N   1 
ATOM   16330 C CA  . ASN F 2 254 ? 54.420  -11.124 57.076  1.00 120.41 ? 254 ASN F CA  1 
ATOM   16331 C C   . ASN F 2 254 ? 53.252  -11.605 57.925  1.00 120.83 ? 254 ASN F C   1 
ATOM   16332 O O   . ASN F 2 254 ? 52.272  -12.131 57.391  1.00 115.69 ? 254 ASN F O   1 
ATOM   16333 C CB  . ASN F 2 254 ? 53.966  -10.029 56.111  1.00 128.78 ? 254 ASN F CB  1 
ATOM   16334 C CG  . ASN F 2 254 ? 55.076  -9.573  55.186  1.00 130.67 ? 254 ASN F CG  1 
ATOM   16335 O OD1 . ASN F 2 254 ? 56.257  -9.788  55.461  1.00 126.08 ? 254 ASN F OD1 1 
ATOM   16336 N ND2 . ASN F 2 254 ? 54.701  -8.937  54.082  1.00 144.01 ? 254 ASN F ND2 1 
ATOM   16337 N N   . VAL F 2 255 ? 53.356  -11.430 59.241  1.00 133.59 ? 255 VAL F N   1 
ATOM   16338 C CA  . VAL F 2 255 ? 52.319  -11.849 60.179  1.00 137.01 ? 255 VAL F CA  1 
ATOM   16339 C C   . VAL F 2 255 ? 52.067  -10.712 61.161  1.00 138.54 ? 255 VAL F C   1 
ATOM   16340 O O   . VAL F 2 255 ? 53.013  -10.158 61.730  1.00 136.41 ? 255 VAL F O   1 
ATOM   16341 C CB  . VAL F 2 255 ? 52.711  -13.136 60.933  1.00 132.41 ? 255 VAL F CB  1 
ATOM   16342 C CG1 . VAL F 2 255 ? 51.626  -13.517 61.927  1.00 131.69 ? 255 VAL F CG1 1 
ATOM   16343 C CG2 . VAL F 2 255 ? 52.970  -14.278 59.958  1.00 126.57 ? 255 VAL F CG2 1 
ATOM   16344 N N   . LEU F 2 256 ? 50.794  -10.361 61.350  1.00 134.36 ? 256 LEU F N   1 
ATOM   16345 C CA  . LEU F 2 256 ? 50.379  -9.290  62.258  1.00 130.22 ? 256 LEU F CA  1 
ATOM   16346 C C   . LEU F 2 256 ? 49.610  -9.905  63.426  1.00 130.91 ? 256 LEU F C   1 
ATOM   16347 O O   . LEU F 2 256 ? 48.428  -10.235 63.298  1.00 128.86 ? 256 LEU F O   1 
ATOM   16348 C CB  . LEU F 2 256 ? 49.533  -8.257  61.520  1.00 124.80 ? 256 LEU F CB  1 
ATOM   16349 C CG  . LEU F 2 256 ? 48.985  -7.103  62.359  1.00 122.09 ? 256 LEU F CG  1 
ATOM   16350 C CD1 . LEU F 2 256 ? 50.123  -6.370  63.049  1.00 127.27 ? 256 LEU F CD1 1 
ATOM   16351 C CD2 . LEU F 2 256 ? 48.186  -6.153  61.486  1.00 129.20 ? 256 LEU F CD2 1 
ATOM   16352 N N   . VAL F 2 257 ? 50.281  -10.052 64.567  1.00 138.63 ? 257 VAL F N   1 
ATOM   16353 C CA  . VAL F 2 257 ? 49.684  -10.635 65.764  1.00 136.13 ? 257 VAL F CA  1 
ATOM   16354 C C   . VAL F 2 257 ? 49.357  -9.530  66.761  1.00 137.62 ? 257 VAL F C   1 
ATOM   16355 O O   . VAL F 2 257 ? 50.061  -8.517  66.856  1.00 143.64 ? 257 VAL F O   1 
ATOM   16356 C CB  . VAL F 2 257 ? 50.618  -11.703 66.379  1.00 134.25 ? 257 VAL F CB  1 
ATOM   16357 C CG1 . VAL F 2 257 ? 50.921  -11.407 67.842  1.00 134.13 ? 257 VAL F CG1 1 
ATOM   16358 C CG2 . VAL F 2 257 ? 50.007  -13.086 66.225  1.00 134.11 ? 257 VAL F CG2 1 
ATOM   16359 N N   . ASP F 2 258 ? 48.266  -9.719  67.504  1.00 128.73 ? 258 ASP F N   1 
ATOM   16360 C CA  . ASP F 2 258 ? 47.854  -8.774  68.531  1.00 123.08 ? 258 ASP F CA  1 
ATOM   16361 C C   . ASP F 2 258 ? 48.551  -9.089  69.850  1.00 120.93 ? 258 ASP F C   1 
ATOM   16362 O O   . ASP F 2 258 ? 48.899  -10.239 70.130  1.00 124.17 ? 258 ASP F O   1 
ATOM   16363 C CB  . ASP F 2 258 ? 46.335  -8.816  68.719  1.00 118.62 ? 258 ASP F CB  1 
ATOM   16364 C CG  . ASP F 2 258 ? 45.812  -7.663  69.557  1.00 113.10 ? 258 ASP F CG  1 
ATOM   16365 O OD1 . ASP F 2 258 ? 46.182  -7.561  70.744  1.00 112.34 ? 258 ASP F OD1 1 
ATOM   16366 O OD2 . ASP F 2 258 ? 45.027  -6.853  69.022  1.00 112.83 ? 258 ASP F OD2 1 
ATOM   16367 N N   . GLU F 2 259 ? 48.750  -8.047  70.664  1.00 115.94 ? 259 GLU F N   1 
ATOM   16368 C CA  . GLU F 2 259 ? 49.370  -8.239  71.973  1.00 111.94 ? 259 GLU F CA  1 
ATOM   16369 C C   . GLU F 2 259 ? 48.484  -9.054  72.905  1.00 111.33 ? 259 GLU F C   1 
ATOM   16370 O O   . GLU F 2 259 ? 48.991  -9.713  73.820  1.00 108.75 ? 259 GLU F O   1 
ATOM   16371 C CB  . GLU F 2 259 ? 49.707  -6.892  72.614  1.00 111.44 ? 259 GLU F CB  1 
ATOM   16372 C CG  . GLU F 2 259 ? 48.532  -5.936  72.748  1.00 117.16 ? 259 GLU F CG  1 
ATOM   16373 C CD  . GLU F 2 259 ? 48.953  -4.576  73.275  1.00 119.01 ? 259 GLU F CD  1 
ATOM   16374 O OE1 . GLU F 2 259 ? 50.157  -4.395  73.556  1.00 117.31 ? 259 GLU F OE1 1 
ATOM   16375 O OE2 . GLU F 2 259 ? 48.082  -3.691  73.411  1.00 122.74 ? 259 GLU F OE2 1 
ATOM   16376 N N   . THR F 2 260 ? 47.168  -9.022  72.696  1.00 113.71 ? 260 THR F N   1 
ATOM   16377 C CA  . THR F 2 260 ? 46.268  -9.792  73.544  1.00 109.93 ? 260 THR F CA  1 
ATOM   16378 C C   . THR F 2 260 ? 46.242  -11.258 73.136  1.00 112.71 ? 260 THR F C   1 
ATOM   16379 O O   . THR F 2 260 ? 46.020  -12.131 73.983  1.00 114.04 ? 260 THR F O   1 
ATOM   16380 C CB  . THR F 2 260 ? 44.856  -9.207  73.491  1.00 107.04 ? 260 THR F CB  1 
ATOM   16381 O OG1 . THR F 2 260 ? 44.930  -7.776  73.518  1.00 106.07 ? 260 THR F OG1 1 
ATOM   16382 C CG2 . THR F 2 260 ? 44.042  -9.683  74.684  1.00 110.03 ? 260 THR F CG2 1 
ATOM   16383 N N   . ALA F 2 261 ? 46.462  -11.541 71.856  1.00 119.40 ? 261 ALA F N   1 
ATOM   16384 C CA  . ALA F 2 261 ? 46.432  -12.911 71.366  1.00 119.96 ? 261 ALA F CA  1 
ATOM   16385 C C   . ALA F 2 261 ? 47.608  -13.708 71.919  1.00 117.74 ? 261 ALA F C   1 
ATOM   16386 O O   . ALA F 2 261 ? 48.729  -13.202 72.032  1.00 113.87 ? 261 ALA F O   1 
ATOM   16387 C CB  . ALA F 2 261 ? 46.457  -12.927 69.838  1.00 121.56 ? 261 ALA F CB  1 
ATOM   16388 N N   . THR F 2 262 ? 47.342  -14.964 72.269  1.00 114.38 ? 262 THR F N   1 
ATOM   16389 C CA  . THR F 2 262 ? 48.349  -15.890 72.769  1.00 112.79 ? 262 THR F CA  1 
ATOM   16390 C C   . THR F 2 262 ? 48.448  -17.069 71.810  1.00 113.72 ? 262 THR F C   1 
ATOM   16391 O O   . THR F 2 262 ? 47.425  -17.614 71.384  1.00 120.07 ? 262 THR F O   1 
ATOM   16392 C CB  . THR F 2 262 ? 48.013  -16.363 74.192  1.00 111.77 ? 262 THR F CB  1 
ATOM   16393 O OG1 . THR F 2 262 ? 48.810  -17.507 74.532  1.00 107.01 ? 262 THR F OG1 1 
ATOM   16394 C CG2 . THR F 2 262 ? 46.538  -16.703 74.326  1.00 115.69 ? 262 THR F CG2 1 
ATOM   16395 N N   . ILE F 2 263 ? 49.676  -17.455 71.471  1.00 107.80 ? 263 ILE F N   1 
ATOM   16396 C CA  . ILE F 2 263 ? 49.943  -18.527 70.516  1.00 109.07 ? 263 ILE F CA  1 
ATOM   16397 C C   . ILE F 2 263 ? 50.599  -19.682 71.257  1.00 109.31 ? 263 ILE F C   1 
ATOM   16398 O O   . ILE F 2 263 ? 51.516  -19.471 72.060  1.00 113.81 ? 263 ILE F O   1 
ATOM   16399 C CB  . ILE F 2 263 ? 50.836  -18.039 69.363  1.00 108.78 ? 263 ILE F CB  1 
ATOM   16400 C CG1 . ILE F 2 263 ? 50.140  -16.917 68.587  1.00 112.02 ? 263 ILE F CG1 1 
ATOM   16401 C CG2 . ILE F 2 263 ? 51.197  -19.197 68.432  1.00 111.31 ? 263 ILE F CG2 1 
ATOM   16402 C CD1 . ILE F 2 263 ? 50.930  -16.419 67.403  1.00 112.63 ? 263 ILE F CD1 1 
ATOM   16403 N N   . GLY F 2 264 ? 50.128  -20.896 70.994  1.00 112.52 ? 264 GLY F N   1 
ATOM   16404 C CA  . GLY F 2 264 ? 50.737  -22.083 71.552  1.00 112.17 ? 264 GLY F CA  1 
ATOM   16405 C C   . GLY F 2 264 ? 52.071  -22.409 70.903  1.00 114.67 ? 264 GLY F C   1 
ATOM   16406 O O   . GLY F 2 264 ? 52.588  -21.698 70.041  1.00 115.99 ? 264 GLY F O   1 
ATOM   16407 N N   . GLU F 2 265 ? 52.635  -23.528 71.340  1.00 116.06 ? 265 GLU F N   1 
ATOM   16408 C CA  . GLU F 2 265 ? 53.918  -24.002 70.848  1.00 119.45 ? 265 GLU F CA  1 
ATOM   16409 C C   . GLU F 2 265 ? 53.714  -25.000 69.712  1.00 121.10 ? 265 GLU F C   1 
ATOM   16410 O O   . GLU F 2 265 ? 52.653  -25.607 69.567  1.00 122.41 ? 265 GLU F O   1 
ATOM   16411 C CB  . GLU F 2 265 ? 54.728  -24.641 71.980  1.00 125.17 ? 265 GLU F CB  1 
ATOM   16412 C CG  . GLU F 2 265 ? 55.076  -23.686 73.117  1.00 129.86 ? 265 GLU F CG  1 
ATOM   16413 C CD  . GLU F 2 265 ? 56.124  -22.658 72.731  1.00 135.83 ? 265 GLU F CD  1 
ATOM   16414 O OE1 . GLU F 2 265 ? 56.766  -22.823 71.672  1.00 138.79 ? 265 GLU F OE1 1 
ATOM   16415 O OE2 . GLU F 2 265 ? 56.307  -21.683 73.491  1.00 139.88 ? 265 GLU F OE2 1 
ATOM   16416 N N   . GLY F 2 266 ? 54.749  -25.157 68.894  1.00 124.96 ? 266 GLY F N   1 
ATOM   16417 C CA  . GLY F 2 266 ? 54.683  -26.092 67.786  1.00 128.58 ? 266 GLY F CA  1 
ATOM   16418 C C   . GLY F 2 266 ? 53.751  -25.658 66.685  1.00 129.17 ? 266 GLY F C   1 
ATOM   16419 O O   . GLY F 2 266 ? 53.172  -26.504 65.996  1.00 130.06 ? 266 GLY F O   1 
ATOM   16420 N N   . CYS F 2 267 ? 53.596  -24.356 66.498  1.00 126.57 ? 267 CYS F N   1 
ATOM   16421 C CA  . CYS F 2 267 ? 52.744  -23.807 65.461  1.00 122.90 ? 267 CYS F CA  1 
ATOM   16422 C C   . CYS F 2 267 ? 53.591  -23.313 64.296  1.00 119.93 ? 267 CYS F C   1 
ATOM   16423 O O   . CYS F 2 267 ? 54.820  -23.257 64.361  1.00 120.36 ? 267 CYS F O   1 
ATOM   16424 C CB  . CYS F 2 267 ? 51.897  -22.667 66.029  1.00 119.06 ? 267 CYS F CB  1 
ATOM   16425 S SG  . CYS F 2 267 ? 51.020  -23.086 67.552  1.00 117.87 ? 267 CYS F SG  1 
ATOM   16426 N N   . LEU F 2 268 ? 52.909  -22.949 63.217  1.00 117.93 ? 268 LEU F N   1 
ATOM   16427 C CA  . LEU F 2 268 ? 53.565  -22.363 62.054  1.00 115.72 ? 268 LEU F CA  1 
ATOM   16428 C C   . LEU F 2 268 ? 52.572  -21.391 61.439  1.00 112.56 ? 268 LEU F C   1 
ATOM   16429 O O   . LEU F 2 268 ? 51.550  -21.814 60.894  1.00 114.49 ? 268 LEU F O   1 
ATOM   16430 C CB  . LEU F 2 268 ? 53.994  -23.429 61.053  1.00 116.44 ? 268 LEU F CB  1 
ATOM   16431 C CG  . LEU F 2 268 ? 54.993  -22.952 59.999  1.00 114.63 ? 268 LEU F CG  1 
ATOM   16432 C CD1 . LEU F 2 268 ? 56.184  -22.267 60.659  1.00 118.44 ? 268 LEU F CD1 1 
ATOM   16433 C CD2 . LEU F 2 268 ? 55.451  -24.109 59.131  1.00 118.71 ? 268 LEU F CD2 1 
ATOM   16434 N N   . ILE F 2 269 ? 52.870  -20.100 61.522  1.00 111.84 ? 269 ILE F N   1 
ATOM   16435 C CA  . ILE F 2 269 ? 51.936  -19.053 61.131  1.00 112.00 ? 269 ILE F CA  1 
ATOM   16436 C C   . ILE F 2 269 ? 52.558  -18.262 59.993  1.00 108.86 ? 269 ILE F C   1 
ATOM   16437 O O   . ILE F 2 269 ? 53.710  -17.825 60.088  1.00 109.85 ? 269 ILE F O   1 
ATOM   16438 C CB  . ILE F 2 269 ? 51.581  -18.132 62.313  1.00 113.40 ? 269 ILE F CB  1 
ATOM   16439 C CG1 . ILE F 2 269 ? 50.913  -18.931 63.432  1.00 113.30 ? 269 ILE F CG1 1 
ATOM   16440 C CG2 . ILE F 2 269 ? 50.663  -17.015 61.854  1.00 115.68 ? 269 ILE F CG2 1 
ATOM   16441 C CD1 . ILE F 2 269 ? 51.856  -19.387 64.520  1.00 118.92 ? 269 ILE F CD1 1 
ATOM   16442 N N   . GLY F 2 270 ? 51.794  -18.081 58.923  1.00 105.87 ? 270 GLY F N   1 
ATOM   16443 C CA  . GLY F 2 270 ? 52.255  -17.346 57.776  1.00 104.94 ? 270 GLY F CA  1 
ATOM   16444 C C   . GLY F 2 270 ? 52.159  -18.162 56.504  1.00 104.59 ? 270 GLY F C   1 
ATOM   16445 O O   . GLY F 2 270 ? 51.997  -19.387 56.529  1.00 105.94 ? 270 GLY F O   1 
ATOM   16446 N N   . PRO F 2 271 ? 52.256  -17.486 55.351  1.00 101.41 ? 271 PRO F N   1 
ATOM   16447 C CA  . PRO F 2 271 ? 52.413  -16.031 55.328  1.00 106.00 ? 271 PRO F CA  1 
ATOM   16448 C C   . PRO F 2 271 ? 51.077  -15.298 55.345  1.00 112.58 ? 271 PRO F C   1 
ATOM   16449 O O   . PRO F 2 271 ? 50.040  -15.897 55.059  1.00 117.43 ? 271 PRO F O   1 
ATOM   16450 C CB  . PRO F 2 271 ? 53.145  -15.773 54.000  1.00 107.15 ? 271 PRO F CB  1 
ATOM   16451 C CG  . PRO F 2 271 ? 53.467  -17.143 53.429  1.00 104.44 ? 271 PRO F CG  1 
ATOM   16452 C CD  . PRO F 2 271 ? 52.465  -18.073 54.022  1.00 100.94 ? 271 PRO F CD  1 
ATOM   16453 N N   . ASP F 2 272 ? 51.127  -14.007 55.680  1.00 115.59 ? 272 ASP F N   1 
ATOM   16454 C CA  . ASP F 2 272 ? 49.982  -13.099 55.615  1.00 119.80 ? 272 ASP F CA  1 
ATOM   16455 C C   . ASP F 2 272 ? 48.815  -13.608 56.468  1.00 118.93 ? 272 ASP F C   1 
ATOM   16456 O O   . ASP F 2 272 ? 47.766  -14.027 55.974  1.00 117.38 ? 272 ASP F O   1 
ATOM   16457 C CB  . ASP F 2 272 ? 49.573  -12.886 54.155  1.00 131.39 ? 272 ASP F CB  1 
ATOM   16458 C CG  . ASP F 2 272 ? 50.731  -12.419 53.304  1.00 142.28 ? 272 ASP F CG  1 
ATOM   16459 O OD1 . ASP F 2 272 ? 51.209  -13.212 52.464  1.00 144.82 ? 272 ASP F OD1 1 
ATOM   16460 O OD2 . ASP F 2 272 ? 51.192  -11.278 53.508  1.00 147.27 ? 272 ASP F OD2 1 
ATOM   16461 N N   . VAL F 2 273 ? 49.038  -13.555 57.780  1.00 118.22 ? 273 VAL F N   1 
ATOM   16462 C CA  . VAL F 2 273 ? 48.042  -13.932 58.774  1.00 116.14 ? 273 VAL F CA  1 
ATOM   16463 C C   . VAL F 2 273 ? 47.943  -12.816 59.804  1.00 118.78 ? 273 VAL F C   1 
ATOM   16464 O O   . VAL F 2 273 ? 48.962  -12.277 60.251  1.00 122.15 ? 273 VAL F O   1 
ATOM   16465 C CB  . VAL F 2 273 ? 48.386  -15.274 59.457  1.00 112.39 ? 273 VAL F CB  1 
ATOM   16466 C CG1 . VAL F 2 273 ? 47.289  -15.670 60.432  1.00 114.07 ? 273 VAL F CG1 1 
ATOM   16467 C CG2 . VAL F 2 273 ? 48.596  -16.367 58.418  1.00 113.08 ? 273 VAL F CG2 1 
ATOM   16468 N N   . ALA F 2 274 ? 46.714  -12.469 60.182  1.00 117.32 ? 274 ALA F N   1 
ATOM   16469 C CA  . ALA F 2 274 ? 46.456  -11.408 61.152  1.00 118.28 ? 274 ALA F CA  1 
ATOM   16470 C C   . ALA F 2 274 ? 45.518  -11.949 62.222  1.00 117.65 ? 274 ALA F C   1 
ATOM   16471 O O   . ALA F 2 274 ? 44.358  -12.262 61.935  1.00 116.08 ? 274 ALA F O   1 
ATOM   16472 C CB  . ALA F 2 274 ? 45.863  -10.170 60.478  1.00 120.70 ? 274 ALA F CB  1 
ATOM   16473 N N   . ILE F 2 275 ? 46.018  -12.056 63.450  1.00 125.11 ? 275 ILE F N   1 
ATOM   16474 C CA  . ILE F 2 275 ? 45.264  -12.609 64.571  1.00 127.44 ? 275 ILE F CA  1 
ATOM   16475 C C   . ILE F 2 275 ? 44.814  -11.463 65.466  1.00 127.83 ? 275 ILE F C   1 
ATOM   16476 O O   . ILE F 2 275 ? 45.646  -10.720 65.999  1.00 126.24 ? 275 ILE F O   1 
ATOM   16477 C CB  . ILE F 2 275 ? 46.102  -13.624 65.362  1.00 125.61 ? 275 ILE F CB  1 
ATOM   16478 C CG1 . ILE F 2 275 ? 46.552  -14.769 64.449  1.00 123.34 ? 275 ILE F CG1 1 
ATOM   16479 C CG2 . ILE F 2 275 ? 45.306  -14.147 66.549  1.00 124.30 ? 275 ILE F CG2 1 
ATOM   16480 C CD1 . ILE F 2 275 ? 47.402  -15.807 65.145  1.00 125.67 ? 275 ILE F CD1 1 
ATOM   16481 N N   . GLY F 2 276 ? 43.495  -11.343 65.657  1.00 139.70 ? 276 GLY F N   1 
ATOM   16482 C CA  . GLY F 2 276 ? 42.934  -10.291 66.458  1.00 141.15 ? 276 GLY F CA  1 
ATOM   16483 C C   . GLY F 2 276 ? 43.246  -10.446 67.939  1.00 141.86 ? 276 GLY F C   1 
ATOM   16484 O O   . GLY F 2 276 ? 43.958  -11.367 68.363  1.00 141.31 ? 276 GLY F O   1 
ATOM   16485 N N   . PRO F 2 277 ? 42.716  -9.525  68.741  1.00 118.58 ? 277 PRO F N   1 
ATOM   16486 C CA  . PRO F 2 277 ? 42.932  -9.583  70.188  1.00 114.13 ? 277 PRO F CA  1 
ATOM   16487 C C   . PRO F 2 277 ? 42.015  -10.590 70.866  1.00 109.39 ? 277 PRO F C   1 
ATOM   16488 O O   . PRO F 2 277 ? 40.993  -11.019 70.328  1.00 107.33 ? 277 PRO F O   1 
ATOM   16489 C CB  . PRO F 2 277 ? 42.607  -8.159  70.648  1.00 114.71 ? 277 PRO F CB  1 
ATOM   16490 C CG  . PRO F 2 277 ? 41.598  -7.687  69.665  1.00 112.26 ? 277 PRO F CG  1 
ATOM   16491 C CD  . PRO F 2 277 ? 41.974  -8.317  68.343  1.00 119.35 ? 277 PRO F CD  1 
ATOM   16492 N N   . GLY F 2 278 ? 42.415  -10.964 72.079  1.00 108.34 ? 278 GLY F N   1 
ATOM   16493 C CA  . GLY F 2 278 ? 41.663  -11.899 72.888  1.00 106.47 ? 278 GLY F CA  1 
ATOM   16494 C C   . GLY F 2 278 ? 41.633  -13.313 72.365  1.00 105.08 ? 278 GLY F C   1 
ATOM   16495 O O   . GLY F 2 278 ? 40.900  -14.145 72.910  1.00 104.03 ? 278 GLY F O   1 
ATOM   16496 N N   . CYS F 2 279 ? 42.402  -13.612 71.323  1.00 110.07 ? 279 CYS F N   1 
ATOM   16497 C CA  . CYS F 2 279 ? 42.436  -14.953 70.769  1.00 114.18 ? 279 CYS F CA  1 
ATOM   16498 C C   . CYS F 2 279 ? 43.406  -15.830 71.553  1.00 119.81 ? 279 CYS F C   1 
ATOM   16499 O O   . CYS F 2 279 ? 44.332  -15.347 72.212  1.00 118.42 ? 279 CYS F O   1 
ATOM   16500 C CB  . CYS F 2 279 ? 42.850  -14.906 69.300  1.00 114.32 ? 279 CYS F CB  1 
ATOM   16501 S SG  . CYS F 2 279 ? 41.900  -13.717 68.335  1.00 111.80 ? 279 CYS F SG  1 
ATOM   16502 N N   . ILE F 2 280 ? 43.186  -17.141 71.461  1.00 131.23 ? 280 ILE F N   1 
ATOM   16503 C CA  . ILE F 2 280 ? 44.026  -18.148 72.100  1.00 134.25 ? 280 ILE F CA  1 
ATOM   16504 C C   . ILE F 2 280 ? 44.251  -19.263 71.082  1.00 136.76 ? 280 ILE F C   1 
ATOM   16505 O O   . ILE F 2 280 ? 43.344  -20.063 70.821  1.00 149.06 ? 280 ILE F O   1 
ATOM   16506 C CB  . ILE F 2 280 ? 43.419  -18.703 73.396  1.00 139.04 ? 280 ILE F CB  1 
ATOM   16507 C CG1 . ILE F 2 280 ? 43.007  -17.559 74.327  1.00 130.71 ? 280 ILE F CG1 1 
ATOM   16508 C CG2 . ILE F 2 280 ? 44.428  -19.621 74.092  1.00 141.95 ? 280 ILE F CG2 1 
ATOM   16509 C CD1 . ILE F 2 280 ? 42.385  -18.013 75.617  1.00 136.53 ? 280 ILE F CD1 1 
ATOM   16510 N N   . VAL F 2 281 ? 45.448  -19.311 70.504  1.00 137.90 ? 281 VAL F N   1 
ATOM   16511 C CA  . VAL F 2 281 ? 45.814  -20.298 69.494  1.00 135.10 ? 281 VAL F CA  1 
ATOM   16512 C C   . VAL F 2 281 ? 46.522  -21.457 70.184  1.00 134.64 ? 281 VAL F C   1 
ATOM   16513 O O   . VAL F 2 281 ? 47.508  -21.250 70.902  1.00 136.03 ? 281 VAL F O   1 
ATOM   16514 C CB  . VAL F 2 281 ? 46.714  -19.677 68.413  1.00 132.56 ? 281 VAL F CB  1 
ATOM   16515 C CG1 . VAL F 2 281 ? 47.288  -20.751 67.518  1.00 131.13 ? 281 VAL F CG1 1 
ATOM   16516 C CG2 . VAL F 2 281 ? 45.936  -18.648 67.603  1.00 132.66 ? 281 VAL F CG2 1 
ATOM   16517 N N   . GLU F 2 282 ? 46.017  -22.672 69.977  1.00 127.51 ? 282 GLU F N   1 
ATOM   16518 C CA  . GLU F 2 282 ? 46.582  -23.864 70.593  1.00 123.43 ? 282 GLU F CA  1 
ATOM   16519 C C   . GLU F 2 282 ? 47.738  -24.409 69.750  1.00 119.13 ? 282 GLU F C   1 
ATOM   16520 O O   . GLU F 2 282 ? 48.164  -23.808 68.760  1.00 121.79 ? 282 GLU F O   1 
ATOM   16521 C CB  . GLU F 2 282 ? 45.502  -24.923 70.809  1.00 121.96 ? 282 GLU F CB  1 
ATOM   16522 C CG  . GLU F 2 282 ? 44.385  -24.509 71.759  1.00 136.03 ? 282 GLU F CG  1 
ATOM   16523 C CD  . GLU F 2 282 ? 43.529  -25.687 72.195  1.00 137.74 ? 282 GLU F CD  1 
ATOM   16524 O OE1 . GLU F 2 282 ? 43.700  -26.788 71.633  1.00 125.20 ? 282 GLU F OE1 1 
ATOM   16525 O OE2 . GLU F 2 282 ? 42.691  -25.516 73.104  1.00 160.54 ? 282 GLU F OE2 1 
ATOM   16526 N N   . SER F 2 283 ? 48.245  -25.575 70.139  1.00 118.59 ? 283 SER F N   1 
ATOM   16527 C CA  . SER F 2 283 ? 49.477  -26.123 69.596  1.00 119.65 ? 283 SER F CA  1 
ATOM   16528 C C   . SER F 2 283 ? 49.226  -26.964 68.352  1.00 125.80 ? 283 SER F C   1 
ATOM   16529 O O   . SER F 2 283 ? 48.149  -27.530 68.163  1.00 122.09 ? 283 SER F O   1 
ATOM   16530 C CB  . SER F 2 283 ? 50.180  -26.971 70.656  1.00 120.44 ? 283 SER F CB  1 
ATOM   16531 O OG  . SER F 2 283 ? 50.811  -26.144 71.619  1.00 121.25 ? 283 SER F OG  1 
ATOM   16532 N N   . GLY F 2 284 ? 50.245  -27.039 67.500  1.00 166.91 ? 284 GLY F N   1 
ATOM   16533 C CA  . GLY F 2 284 ? 50.187  -27.874 66.320  1.00 166.18 ? 284 GLY F CA  1 
ATOM   16534 C C   . GLY F 2 284 ? 49.442  -27.282 65.147  1.00 165.69 ? 284 GLY F C   1 
ATOM   16535 O O   . GLY F 2 284 ? 49.131  -28.014 64.202  1.00 165.19 ? 284 GLY F O   1 
ATOM   16536 N N   . VAL F 2 285 ? 49.143  -25.988 65.175  1.00 131.71 ? 285 VAL F N   1 
ATOM   16537 C CA  . VAL F 2 285 ? 48.341  -25.363 64.136  1.00 126.98 ? 285 VAL F CA  1 
ATOM   16538 C C   . VAL F 2 285 ? 49.245  -24.896 63.002  1.00 126.28 ? 285 VAL F C   1 
ATOM   16539 O O   . VAL F 2 285 ? 50.460  -24.747 63.155  1.00 125.01 ? 285 VAL F O   1 
ATOM   16540 C CB  . VAL F 2 285 ? 47.514  -24.191 64.698  1.00 122.26 ? 285 VAL F CB  1 
ATOM   16541 C CG1 . VAL F 2 285 ? 46.666  -24.652 65.877  1.00 122.29 ? 285 VAL F CG1 1 
ATOM   16542 C CG2 . VAL F 2 285 ? 48.426  -23.052 65.091  1.00 117.81 ? 285 VAL F CG2 1 
ATOM   16543 N N   . ARG F 2 286 ? 48.632  -24.666 61.839  1.00 124.63 ? 286 ARG F N   1 
ATOM   16544 C CA  . ARG F 2 286 ? 49.336  -24.230 60.631  1.00 117.45 ? 286 ARG F CA  1 
ATOM   16545 C C   . ARG F 2 286 ? 48.463  -23.190 59.933  1.00 114.68 ? 286 ARG F C   1 
ATOM   16546 O O   . ARG F 2 286 ? 47.514  -23.546 59.227  1.00 120.03 ? 286 ARG F O   1 
ATOM   16547 C CB  . ARG F 2 286 ? 49.642  -25.414 59.720  1.00 121.44 ? 286 ARG F CB  1 
ATOM   16548 C CG  . ARG F 2 286 ? 50.190  -25.048 58.355  1.00 118.87 ? 286 ARG F CG  1 
ATOM   16549 C CD  . ARG F 2 286 ? 51.345  -24.071 58.453  1.00 115.87 ? 286 ARG F CD  1 
ATOM   16550 N NE  . ARG F 2 286 ? 51.951  -23.830 57.149  1.00 115.33 ? 286 ARG F NE  1 
ATOM   16551 C CZ  . ARG F 2 286 ? 52.619  -22.728 56.830  1.00 112.46 ? 286 ARG F CZ  1 
ATOM   16552 N NH1 . ARG F 2 286 ? 52.762  -21.756 57.721  1.00 109.11 ? 286 ARG F NH1 1 
ATOM   16553 N NH2 . ARG F 2 286 ? 53.138  -22.594 55.618  1.00 113.80 ? 286 ARG F NH2 1 
ATOM   16554 N N   . LEU F 2 287 ? 48.775  -21.913 60.139  1.00 111.83 ? 287 LEU F N   1 
ATOM   16555 C CA  . LEU F 2 287 ? 48.014  -20.814 59.557  1.00 110.78 ? 287 LEU F CA  1 
ATOM   16556 C C   . LEU F 2 287 ? 48.747  -20.222 58.360  1.00 112.74 ? 287 LEU F C   1 
ATOM   16557 O O   . LEU F 2 287 ? 49.971  -20.065 58.382  1.00 112.43 ? 287 LEU F O   1 
ATOM   16558 C CB  . LEU F 2 287 ? 47.750  -19.722 60.596  1.00 110.16 ? 287 LEU F CB  1 
ATOM   16559 C CG  . LEU F 2 287 ? 47.021  -20.157 61.869  1.00 110.43 ? 287 LEU F CG  1 
ATOM   16560 C CD1 . LEU F 2 287 ? 46.799  -18.969 62.790  1.00 112.28 ? 287 LEU F CD1 1 
ATOM   16561 C CD2 . LEU F 2 287 ? 45.697  -20.822 61.522  1.00 111.33 ? 287 LEU F CD2 1 
ATOM   16562 N N   . SER F 2 288 ? 47.987  -19.893 57.316  1.00 125.43 ? 288 SER F N   1 
ATOM   16563 C CA  . SER F 2 288 ? 48.564  -19.369 56.084  1.00 124.13 ? 288 SER F CA  1 
ATOM   16564 C C   . SER F 2 288 ? 47.489  -18.631 55.300  1.00 124.25 ? 288 SER F C   1 
ATOM   16565 O O   . SER F 2 288 ? 46.402  -19.174 55.077  1.00 125.64 ? 288 SER F O   1 
ATOM   16566 C CB  . SER F 2 288 ? 49.166  -20.497 55.238  1.00 124.69 ? 288 SER F CB  1 
ATOM   16567 O OG  . SER F 2 288 ? 48.246  -21.562 55.088  1.00 124.89 ? 288 SER F OG  1 
ATOM   16568 N N   . ARG F 2 289 ? 47.790  -17.395 54.899  1.00 115.20 ? 289 ARG F N   1 
ATOM   16569 C CA  . ARG F 2 289 ? 46.931  -16.595 54.023  1.00 116.67 ? 289 ARG F CA  1 
ATOM   16570 C C   . ARG F 2 289 ? 45.551  -16.338 54.626  1.00 119.54 ? 289 ARG F C   1 
ATOM   16571 O O   . ARG F 2 289 ? 44.618  -15.965 53.911  1.00 133.06 ? 289 ARG F O   1 
ATOM   16572 C CB  . ARG F 2 289 ? 46.793  -17.253 52.639  1.00 122.67 ? 289 ARG F CB  1 
ATOM   16573 C CG  . ARG F 2 289 ? 46.404  -16.310 51.497  1.00 140.95 ? 289 ARG F CG  1 
ATOM   16574 C CD  . ARG F 2 289 ? 46.146  -17.080 50.202  1.00 148.92 ? 289 ARG F CD  1 
ATOM   16575 N NE  . ARG F 2 289 ? 45.337  -16.323 49.244  1.00 165.09 ? 289 ARG F NE  1 
ATOM   16576 C CZ  . ARG F 2 289 ? 45.827  -15.481 48.338  1.00 167.33 ? 289 ARG F CZ  1 
ATOM   16577 N NH1 . ARG F 2 289 ? 47.134  -15.275 48.253  1.00 163.26 ? 289 ARG F NH1 1 
ATOM   16578 N NH2 . ARG F 2 289 ? 45.005  -14.844 47.514  1.00 164.59 ? 289 ARG F NH2 1 
ATOM   16579 N N   . CYS F 2 290 ? 45.390  -16.524 55.930  1.00 115.99 ? 290 CYS F N   1 
ATOM   16580 C CA  . CYS F 2 290 ? 44.101  -16.350 56.579  1.00 115.07 ? 290 CYS F CA  1 
ATOM   16581 C C   . CYS F 2 290 ? 44.118  -15.118 57.476  1.00 113.28 ? 290 CYS F C   1 
ATOM   16582 O O   . CYS F 2 290 ? 45.149  -14.473 57.676  1.00 112.04 ? 290 CYS F O   1 
ATOM   16583 C CB  . CYS F 2 290 ? 43.733  -17.600 57.383  1.00 112.64 ? 290 CYS F CB  1 
ATOM   16584 S SG  . CYS F 2 290 ? 45.013  -18.124 58.545  1.00 109.66 ? 290 CYS F SG  1 
ATOM   16585 N N   . THR F 2 291 ? 42.942  -14.790 58.010  1.00 111.90 ? 291 THR F N   1 
ATOM   16586 C CA  . THR F 2 291 ? 42.792  -13.699 58.966  1.00 108.45 ? 291 THR F CA  1 
ATOM   16587 C C   . THR F 2 291 ? 41.902  -14.179 60.101  1.00 109.41 ? 291 THR F C   1 
ATOM   16588 O O   . THR F 2 291 ? 40.823  -14.728 59.857  1.00 109.93 ? 291 THR F O   1 
ATOM   16589 C CB  . THR F 2 291 ? 42.178  -12.442 58.334  1.00 108.83 ? 291 THR F CB  1 
ATOM   16590 O OG1 . THR F 2 291 ? 40.750  -12.568 58.310  1.00 108.78 ? 291 THR F OG1 1 
ATOM   16591 C CG2 . THR F 2 291 ? 42.691  -12.222 56.918  1.00 125.55 ? 291 THR F CG2 1 
ATOM   16592 N N   . VAL F 2 292 ? 42.353  -13.963 61.334  1.00 110.86 ? 292 VAL F N   1 
ATOM   16593 C CA  . VAL F 2 292 ? 41.648  -14.398 62.535  1.00 109.36 ? 292 VAL F CA  1 
ATOM   16594 C C   . VAL F 2 292 ? 41.128  -13.172 63.273  1.00 110.39 ? 292 VAL F C   1 
ATOM   16595 O O   . VAL F 2 292 ? 41.888  -12.232 63.540  1.00 115.65 ? 292 VAL F O   1 
ATOM   16596 C CB  . VAL F 2 292 ? 42.563  -15.243 63.437  1.00 110.83 ? 292 VAL F CB  1 
ATOM   16597 C CG1 . VAL F 2 292 ? 41.956  -15.397 64.813  1.00 113.19 ? 292 VAL F CG1 1 
ATOM   16598 C CG2 . VAL F 2 292 ? 42.811  -16.605 62.805  1.00 108.79 ? 292 VAL F CG2 1 
ATOM   16599 N N   . MET F 2 293 ? 39.837  -13.182 63.607  1.00 108.25 ? 293 MET F N   1 
ATOM   16600 C CA  . MET F 2 293 ? 39.217  -12.076 64.321  1.00 106.21 ? 293 MET F CA  1 
ATOM   16601 C C   . MET F 2 293 ? 39.224  -12.360 65.823  1.00 106.27 ? 293 MET F C   1 
ATOM   16602 O O   . MET F 2 293 ? 39.841  -13.317 66.294  1.00 110.15 ? 293 MET F O   1 
ATOM   16603 C CB  . MET F 2 293 ? 37.807  -11.824 63.790  1.00 106.06 ? 293 MET F CB  1 
ATOM   16604 C CG  . MET F 2 293 ? 37.776  -11.295 62.364  1.00 108.18 ? 293 MET F CG  1 
ATOM   16605 S SD  . MET F 2 293 ? 36.143  -10.731 61.859  1.00 119.02 ? 293 MET F SD  1 
ATOM   16606 C CE  . MET F 2 293 ? 36.446  -10.327 60.138  1.00 121.90 ? 293 MET F CE  1 
ATOM   16607 N N   . ARG F 2 294 ? 38.517  -11.532 66.589  1.00 104.61 ? 294 ARG F N   1 
ATOM   16608 C CA  . ARG F 2 294 ? 38.658  -11.516 68.039  1.00 102.21 ? 294 ARG F CA  1 
ATOM   16609 C C   . ARG F 2 294 ? 38.075  -12.767 68.689  1.00 100.85 ? 294 ARG F C   1 
ATOM   16610 O O   . ARG F 2 294 ? 37.103  -13.354 68.208  1.00 105.02 ? 294 ARG F O   1 
ATOM   16611 C CB  . ARG F 2 294 ? 37.970  -10.279 68.611  1.00 103.48 ? 294 ARG F CB  1 
ATOM   16612 C CG  . ARG F 2 294 ? 38.478  -8.973  68.028  1.00 110.68 ? 294 ARG F CG  1 
ATOM   16613 C CD  . ARG F 2 294 ? 37.746  -7.788  68.624  1.00 111.99 ? 294 ARG F CD  1 
ATOM   16614 N NE  . ARG F 2 294 ? 37.739  -7.832  70.082  1.00 107.76 ? 294 ARG F NE  1 
ATOM   16615 C CZ  . ARG F 2 294 ? 37.219  -6.887  70.857  1.00 109.96 ? 294 ARG F CZ  1 
ATOM   16616 N NH1 . ARG F 2 294 ? 36.658  -5.812  70.317  1.00 112.69 ? 294 ARG F NH1 1 
ATOM   16617 N NH2 . ARG F 2 294 ? 37.265  -7.014  72.175  1.00 110.92 ? 294 ARG F NH2 1 
ATOM   16618 N N   . GLY F 2 295 ? 38.689  -13.171 69.802  1.00 102.54 ? 295 GLY F N   1 
ATOM   16619 C CA  . GLY F 2 295 ? 38.101  -14.113 70.736  1.00 111.80 ? 295 GLY F CA  1 
ATOM   16620 C C   . GLY F 2 295 ? 37.947  -15.542 70.269  1.00 118.70 ? 295 GLY F C   1 
ATOM   16621 O O   . GLY F 2 295 ? 37.606  -16.402 71.088  1.00 126.46 ? 295 GLY F O   1 
ATOM   16622 N N   . VAL F 2 296 ? 38.185  -15.839 69.001  1.00 122.18 ? 296 VAL F N   1 
ATOM   16623 C CA  . VAL F 2 296 ? 37.975  -17.189 68.493  1.00 137.46 ? 296 VAL F CA  1 
ATOM   16624 C C   . VAL F 2 296 ? 39.131  -18.083 68.919  1.00 159.79 ? 296 VAL F C   1 
ATOM   16625 O O   . VAL F 2 296 ? 40.303  -17.692 68.854  1.00 148.08 ? 296 VAL F O   1 
ATOM   16626 C CB  . VAL F 2 296 ? 37.807  -17.171 66.964  1.00 126.77 ? 296 VAL F CB  1 
ATOM   16627 C CG1 . VAL F 2 296 ? 38.865  -16.303 66.331  1.00 118.38 ? 296 VAL F CG1 1 
ATOM   16628 C CG2 . VAL F 2 296 ? 37.882  -18.581 66.411  1.00 134.94 ? 296 VAL F CG2 1 
ATOM   16629 N N   . ARG F 2 297 ? 38.799  -19.298 69.348  1.00 236.24 ? 297 ARG F N   1 
ATOM   16630 C CA  . ARG F 2 297 ? 39.774  -20.298 69.759  1.00 235.31 ? 297 ARG F CA  1 
ATOM   16631 C C   . ARG F 2 297 ? 39.915  -21.358 68.676  1.00 234.16 ? 297 ARG F C   1 
ATOM   16632 O O   . ARG F 2 297 ? 38.917  -21.937 68.234  1.00 234.67 ? 297 ARG F O   1 
ATOM   16633 C CB  . ARG F 2 297 ? 39.352  -20.968 71.069  1.00 236.32 ? 297 ARG F CB  1 
ATOM   16634 C CG  . ARG F 2 297 ? 40.103  -22.261 71.354  1.00 235.79 ? 297 ARG F CG  1 
ATOM   16635 C CD  . ARG F 2 297 ? 39.463  -23.063 72.477  1.00 237.19 ? 297 ARG F CD  1 
ATOM   16636 N NE  . ARG F 2 297 ? 39.373  -22.324 73.731  1.00 239.03 ? 297 ARG F NE  1 
ATOM   16637 C CZ  . ARG F 2 297 ? 39.043  -22.880 74.893  1.00 240.21 ? 297 ARG F CZ  1 
ATOM   16638 N NH1 . ARG F 2 297 ? 38.775  -24.177 74.951  1.00 240.08 ? 297 ARG F NH1 1 
ATOM   16639 N NH2 . ARG F 2 297 ? 38.981  -22.146 75.994  1.00 240.88 ? 297 ARG F NH2 1 
ATOM   16640 N N   . ILE F 2 298 ? 41.152  -21.608 68.254  1.00 163.89 ? 298 ILE F N   1 
ATOM   16641 C CA  . ILE F 2 298 ? 41.471  -22.669 67.305  1.00 143.67 ? 298 ILE F CA  1 
ATOM   16642 C C   . ILE F 2 298 ? 42.180  -23.778 68.070  1.00 135.76 ? 298 ILE F C   1 
ATOM   16643 O O   . ILE F 2 298 ? 43.220  -23.542 68.697  1.00 137.50 ? 298 ILE F O   1 
ATOM   16644 C CB  . ILE F 2 298 ? 42.331  -22.154 66.142  1.00 136.49 ? 298 ILE F CB  1 
ATOM   16645 C CG1 . ILE F 2 298 ? 41.573  -21.071 65.367  1.00 138.81 ? 298 ILE F CG1 1 
ATOM   16646 C CG2 . ILE F 2 298 ? 42.713  -23.305 65.221  1.00 124.45 ? 298 ILE F CG2 1 
ATOM   16647 C CD1 . ILE F 2 298 ? 42.346  -20.492 64.208  1.00 127.56 ? 298 ILE F CD1 1 
ATOM   16648 N N   . LYS F 2 299 ? 41.616  -24.983 68.029  1.00 124.81 ? 299 LYS F N   1 
ATOM   16649 C CA  . LYS F 2 299 ? 42.133  -26.089 68.820  1.00 114.78 ? 299 LYS F CA  1 
ATOM   16650 C C   . LYS F 2 299 ? 43.382  -26.688 68.172  1.00 111.54 ? 299 LYS F C   1 
ATOM   16651 O O   . LYS F 2 299 ? 43.890  -26.203 67.157  1.00 113.27 ? 299 LYS F O   1 
ATOM   16652 C CB  . LYS F 2 299 ? 41.039  -27.132 69.029  1.00 111.45 ? 299 LYS F CB  1 
ATOM   16653 C CG  . LYS F 2 299 ? 39.890  -26.641 69.900  1.00 116.73 ? 299 LYS F CG  1 
ATOM   16654 C CD  . LYS F 2 299 ? 38.852  -27.725 70.144  1.00 112.41 ? 299 LYS F CD  1 
ATOM   16655 C CE  . LYS F 2 299 ? 37.714  -27.204 71.009  1.00 120.56 ? 299 LYS F CE  1 
ATOM   16656 N NZ  . LYS F 2 299 ? 36.678  -28.242 71.264  1.00 126.74 ? 299 LYS F NZ  1 
ATOM   16657 N N   . LYS F 2 300 ? 43.881  -27.767 68.770  1.00 108.90 ? 300 LYS F N   1 
ATOM   16658 C CA  . LYS F 2 300 ? 45.184  -28.310 68.413  1.00 109.89 ? 300 LYS F CA  1 
ATOM   16659 C C   . LYS F 2 300 ? 45.156  -29.058 67.085  1.00 109.30 ? 300 LYS F C   1 
ATOM   16660 O O   . LYS F 2 300 ? 44.148  -29.658 66.702  1.00 109.00 ? 300 LYS F O   1 
ATOM   16661 C CB  . LYS F 2 300 ? 45.695  -29.238 69.515  1.00 110.51 ? 300 LYS F CB  1 
ATOM   16662 C CG  . LYS F 2 300 ? 46.186  -28.511 70.753  1.00 109.91 ? 300 LYS F CG  1 
ATOM   16663 C CD  . LYS F 2 300 ? 46.623  -29.475 71.840  1.00 106.89 ? 300 LYS F CD  1 
ATOM   16664 C CE  . LYS F 2 300 ? 45.439  -29.941 72.668  1.00 106.38 ? 300 LYS F CE  1 
ATOM   16665 N NZ  . LYS F 2 300 ? 45.865  -30.714 73.867  1.00 94.55  ? 300 LYS F NZ  1 
ATOM   16666 N N   . HIS F 2 301 ? 46.291  -29.003 66.381  1.00 115.16 ? 301 HIS F N   1 
ATOM   16667 C CA  . HIS F 2 301 ? 46.546  -29.804 65.182  1.00 116.68 ? 301 HIS F CA  1 
ATOM   16668 C C   . HIS F 2 301 ? 45.598  -29.451 64.041  1.00 116.53 ? 301 HIS F C   1 
ATOM   16669 O O   . HIS F 2 301 ? 45.310  -30.285 63.180  1.00 114.01 ? 301 HIS F O   1 
ATOM   16670 C CB  . HIS F 2 301 ? 46.476  -31.300 65.492  1.00 116.20 ? 301 HIS F CB  1 
ATOM   16671 C CG  . HIS F 2 301 ? 47.277  -31.699 66.689  1.00 118.05 ? 301 HIS F CG  1 
ATOM   16672 N ND1 . HIS F 2 301 ? 46.878  -32.693 67.556  1.00 120.37 ? 301 HIS F ND1 1 
ATOM   16673 C CD2 . HIS F 2 301 ? 48.451  -31.228 67.171  1.00 121.79 ? 301 HIS F CD2 1 
ATOM   16674 C CE1 . HIS F 2 301 ? 47.775  -32.822 68.517  1.00 120.45 ? 301 HIS F CE1 1 
ATOM   16675 N NE2 . HIS F 2 301 ? 48.740  -31.945 68.306  1.00 120.80 ? 301 HIS F NE2 1 
ATOM   16676 N N   . ALA F 2 302 ? 45.114  -28.216 64.025  1.00 117.54 ? 302 ALA F N   1 
ATOM   16677 C CA  . ALA F 2 302 ? 44.238  -27.741 62.967  1.00 117.24 ? 302 ALA F CA  1 
ATOM   16678 C C   . ALA F 2 302 ? 45.059  -27.134 61.836  1.00 126.68 ? 302 ALA F C   1 
ATOM   16679 O O   . ALA F 2 302 ? 46.128  -26.560 62.057  1.00 126.02 ? 302 ALA F O   1 
ATOM   16680 C CB  . ALA F 2 302 ? 43.247  -26.712 63.511  1.00 115.09 ? 302 ALA F CB  1 
ATOM   16681 N N   . CYS F 2 303 ? 44.546  -27.263 60.613  1.00 143.68 ? 303 CYS F N   1 
ATOM   16682 C CA  . CYS F 2 303 ? 45.215  -26.746 59.418  1.00 141.97 ? 303 CYS F CA  1 
ATOM   16683 C C   . CYS F 2 303 ? 44.240  -25.837 58.675  1.00 141.30 ? 303 CYS F C   1 
ATOM   16684 O O   . CYS F 2 303 ? 43.314  -26.315 58.013  1.00 141.18 ? 303 CYS F O   1 
ATOM   16685 C CB  . CYS F 2 303 ? 45.703  -27.885 58.525  1.00 140.96 ? 303 CYS F CB  1 
ATOM   16686 S SG  . CYS F 2 303 ? 46.495  -27.362 56.985  1.00 138.20 ? 303 CYS F SG  1 
ATOM   16687 N N   . ILE F 2 304 ? 44.453  -24.527 58.785  1.00 122.07 ? 304 ILE F N   1 
ATOM   16688 C CA  . ILE F 2 304 ? 43.599  -23.525 58.158  1.00 115.62 ? 304 ILE F CA  1 
ATOM   16689 C C   . ILE F 2 304 ? 44.425  -22.766 57.130  1.00 113.16 ? 304 ILE F C   1 
ATOM   16690 O O   . ILE F 2 304 ? 45.506  -22.257 57.449  1.00 113.83 ? 304 ILE F O   1 
ATOM   16691 C CB  . ILE F 2 304 ? 42.991  -22.563 59.195  1.00 113.75 ? 304 ILE F CB  1 
ATOM   16692 C CG1 . ILE F 2 304 ? 42.196  -23.350 60.241  1.00 116.13 ? 304 ILE F CG1 1 
ATOM   16693 C CG2 . ILE F 2 304 ? 42.112  -21.527 58.504  1.00 112.85 ? 304 ILE F CG2 1 
ATOM   16694 C CD1 . ILE F 2 304 ? 41.349  -22.493 61.149  1.00 118.62 ? 304 ILE F CD1 1 
ATOM   16695 N N   . SER F 2 305 ? 43.921  -22.700 55.898  1.00 114.61 ? 305 SER F N   1 
ATOM   16696 C CA  . SER F 2 305 ? 44.598  -22.010 54.809  1.00 113.66 ? 305 SER F CA  1 
ATOM   16697 C C   . SER F 2 305 ? 43.601  -21.163 54.033  1.00 110.07 ? 305 SER F C   1 
ATOM   16698 O O   . SER F 2 305 ? 42.538  -21.656 53.644  1.00 109.37 ? 305 SER F O   1 
ATOM   16699 C CB  . SER F 2 305 ? 45.289  -23.011 53.878  1.00 116.34 ? 305 SER F CB  1 
ATOM   16700 O OG  . SER F 2 305 ? 44.480  -24.154 53.670  1.00 116.12 ? 305 SER F OG  1 
ATOM   16701 N N   . SER F 2 306 ? 43.964  -19.901 53.794  1.00 113.19 ? 306 SER F N   1 
ATOM   16702 C CA  . SER F 2 306 ? 43.197  -18.972 52.960  1.00 114.60 ? 306 SER F CA  1 
ATOM   16703 C C   . SER F 2 306 ? 41.713  -18.988 53.327  1.00 108.21 ? 306 SER F C   1 
ATOM   16704 O O   . SER F 2 306 ? 40.851  -19.353 52.529  1.00 105.71 ? 306 SER F O   1 
ATOM   16705 C CB  . SER F 2 306 ? 43.397  -19.280 51.472  1.00 114.93 ? 306 SER F CB  1 
ATOM   16706 O OG  . SER F 2 306 ? 43.017  -20.610 51.154  1.00 106.59 ? 306 SER F OG  1 
ATOM   16707 N N   . SER F 2 307 ? 41.427  -18.586 54.563  1.00 108.88 ? 307 SER F N   1 
ATOM   16708 C CA  . SER F 2 307 ? 40.067  -18.596 55.079  1.00 108.90 ? 307 SER F CA  1 
ATOM   16709 C C   . SER F 2 307 ? 39.861  -17.373 55.964  1.00 111.11 ? 307 SER F C   1 
ATOM   16710 O O   . SER F 2 307 ? 40.787  -16.595 56.211  1.00 111.94 ? 307 SER F O   1 
ATOM   16711 C CB  . SER F 2 307 ? 39.778  -19.891 55.848  1.00 109.42 ? 307 SER F CB  1 
ATOM   16712 O OG  . SER F 2 307 ? 39.804  -21.014 54.984  1.00 104.10 ? 307 SER F OG  1 
ATOM   16713 N N   . ILE F 2 308 ? 38.629  -17.208 56.439  0.18 118.35 ? 308 ILE F N   1 
ATOM   16714 C CA  . ILE F 2 308 ? 38.236  -16.079 57.274  0.18 121.74 ? 308 ILE F CA  1 
ATOM   16715 C C   . ILE F 2 308 ? 37.486  -16.630 58.476  0.18 132.71 ? 308 ILE F C   1 
ATOM   16716 O O   . ILE F 2 308 ? 36.472  -17.320 58.316  0.18 150.84 ? 308 ILE F O   1 
ATOM   16717 C CB  . ILE F 2 308 ? 37.363  -15.066 56.516  0.18 121.85 ? 308 ILE F CB  1 
ATOM   16718 N N   . ILE F 2 309 ? 37.982  -16.333 59.672  1.00 120.78 ? 309 ILE F N   1 
ATOM   16719 C CA  . ILE F 2 309 ? 37.406  -16.832 60.914  1.00 126.05 ? 309 ILE F CA  1 
ATOM   16720 C C   . ILE F 2 309 ? 36.681  -15.684 61.603  1.00 125.92 ? 309 ILE F C   1 
ATOM   16721 O O   . ILE F 2 309 ? 37.256  -14.605 61.797  1.00 121.91 ? 309 ILE F O   1 
ATOM   16722 C CB  . ILE F 2 309 ? 38.483  -17.438 61.828  1.00 123.33 ? 309 ILE F CB  1 
ATOM   16723 C CG1 . ILE F 2 309 ? 39.419  -18.346 61.025  1.00 121.32 ? 309 ILE F CG1 1 
ATOM   16724 C CG2 . ILE F 2 309 ? 37.835  -18.243 62.928  1.00 127.74 ? 309 ILE F CG2 1 
ATOM   16725 C CD1 . ILE F 2 309 ? 38.724  -19.515 60.353  1.00 127.75 ? 309 ILE F CD1 1 
ATOM   16726 N N   . GLY F 2 310 ? 35.426  -15.919 61.976  1.00 131.08 ? 310 GLY F N   1 
ATOM   16727 C CA  . GLY F 2 310 ? 34.610  -14.904 62.607  1.00 120.62 ? 310 GLY F CA  1 
ATOM   16728 C C   . GLY F 2 310 ? 34.955  -14.703 64.070  1.00 111.50 ? 310 GLY F C   1 
ATOM   16729 O O   . GLY F 2 310 ? 35.903  -15.272 64.613  1.00 112.56 ? 310 GLY F O   1 
ATOM   16730 N N   . TRP F 2 311 ? 34.149  -13.864 64.717  1.00 108.98 ? 311 TRP F N   1 
ATOM   16731 C CA  . TRP F 2 311 ? 34.359  -13.537 66.118  1.00 104.63 ? 311 TRP F CA  1 
ATOM   16732 C C   . TRP F 2 311 ? 33.860  -14.670 67.006  1.00 108.61 ? 311 TRP F C   1 
ATOM   16733 O O   . TRP F 2 311 ? 32.786  -15.231 66.773  1.00 111.16 ? 311 TRP F O   1 
ATOM   16734 C CB  . TRP F 2 311 ? 33.626  -12.245 66.482  1.00 106.39 ? 311 TRP F CB  1 
ATOM   16735 C CG  . TRP F 2 311 ? 34.030  -11.054 65.672  1.00 108.61 ? 311 TRP F CG  1 
ATOM   16736 C CD1 . TRP F 2 311 ? 35.169  -10.314 65.807  1.00 109.66 ? 311 TRP F CD1 1 
ATOM   16737 C CD2 . TRP F 2 311 ? 33.283  -10.450 64.608  1.00 110.90 ? 311 TRP F CD2 1 
ATOM   16738 N NE1 . TRP F 2 311 ? 35.180  -9.292  64.888  1.00 114.54 ? 311 TRP F NE1 1 
ATOM   16739 C CE2 . TRP F 2 311 ? 34.033  -9.353  64.141  1.00 113.65 ? 311 TRP F CE2 1 
ATOM   16740 C CE3 . TRP F 2 311 ? 32.053  -10.733 64.004  1.00 109.66 ? 311 TRP F CE3 1 
ATOM   16741 C CZ2 . TRP F 2 311 ? 33.595  -8.539  63.097  1.00 116.08 ? 311 TRP F CZ2 1 
ATOM   16742 C CZ3 . TRP F 2 311 ? 31.621  -9.923  62.968  1.00 111.75 ? 311 TRP F CZ3 1 
ATOM   16743 C CH2 . TRP F 2 311 ? 32.389  -8.841  62.525  1.00 113.97 ? 311 TRP F CH2 1 
ATOM   16744 N N   . HIS F 2 312 ? 34.648  -14.994 68.034  1.00 111.20 ? 312 HIS F N   1 
ATOM   16745 C CA  . HIS F 2 312 ? 34.237  -15.915 69.098  1.00 114.95 ? 312 HIS F CA  1 
ATOM   16746 C C   . HIS F 2 312 ? 33.777  -17.263 68.543  1.00 118.36 ? 312 HIS F C   1 
ATOM   16747 O O   . HIS F 2 312 ? 32.852  -17.889 69.067  1.00 116.30 ? 312 HIS F O   1 
ATOM   16748 C CB  . HIS F 2 312 ? 33.146  -15.285 69.967  1.00 112.02 ? 312 HIS F CB  1 
ATOM   16749 C CG  . HIS F 2 312 ? 33.519  -13.946 70.525  1.00 113.07 ? 312 HIS F CG  1 
ATOM   16750 N ND1 . HIS F 2 312 ? 33.219  -12.763 69.883  1.00 113.94 ? 312 HIS F ND1 1 
ATOM   16751 C CD2 . HIS F 2 312 ? 34.171  -13.603 71.661  1.00 111.81 ? 312 HIS F CD2 1 
ATOM   16752 C CE1 . HIS F 2 312 ? 33.668  -11.749 70.602  1.00 113.01 ? 312 HIS F CE1 1 
ATOM   16753 N NE2 . HIS F 2 312 ? 34.249  -12.232 71.686  1.00 111.36 ? 312 HIS F NE2 1 
ATOM   16754 N N   . SER F 2 313 ? 34.429  -17.717 67.476  1.00 118.33 ? 313 SER F N   1 
ATOM   16755 C CA  . SER F 2 313 ? 34.131  -19.011 66.880  1.00 115.61 ? 313 SER F CA  1 
ATOM   16756 C C   . SER F 2 313 ? 35.015  -20.080 67.522  1.00 122.67 ? 313 SER F C   1 
ATOM   16757 O O   . SER F 2 313 ? 35.732  -19.821 68.492  1.00 131.72 ? 313 SER F O   1 
ATOM   16758 C CB  . SER F 2 313 ? 34.304  -18.946 65.364  1.00 109.22 ? 313 SER F CB  1 
ATOM   16759 O OG  . SER F 2 313 ? 33.365  -18.056 64.785  1.00 106.84 ? 313 SER F OG  1 
ATOM   16760 N N   . THR F 2 314 ? 34.966  -21.301 66.994  1.00 119.03 ? 314 THR F N   1 
ATOM   16761 C CA  . THR F 2 314 ? 35.735  -22.401 67.568  1.00 120.69 ? 314 THR F CA  1 
ATOM   16762 C C   . THR F 2 314 ? 36.022  -23.438 66.496  1.00 114.52 ? 314 THR F C   1 
ATOM   16763 O O   . THR F 2 314 ? 35.095  -24.042 65.949  1.00 110.77 ? 314 THR F O   1 
ATOM   16764 C CB  . THR F 2 314 ? 34.990  -23.044 68.740  1.00 121.56 ? 314 THR F CB  1 
ATOM   16765 O OG1 . THR F 2 314 ? 34.896  -22.110 69.823  1.00 131.76 ? 314 THR F OG1 1 
ATOM   16766 C CG2 . THR F 2 314 ? 35.719  -24.295 69.213  1.00 118.20 ? 314 THR F CG2 1 
ATOM   16767 N N   . VAL F 2 315 ? 37.303  -23.637 66.200  1.00 116.90 ? 315 VAL F N   1 
ATOM   16768 C CA  . VAL F 2 315 ? 37.756  -24.669 65.276  1.00 113.58 ? 315 VAL F CA  1 
ATOM   16769 C C   . VAL F 2 315 ? 38.223  -25.857 66.103  1.00 113.98 ? 315 VAL F C   1 
ATOM   16770 O O   . VAL F 2 315 ? 39.140  -25.727 66.922  1.00 121.06 ? 315 VAL F O   1 
ATOM   16771 C CB  . VAL F 2 315 ? 38.880  -24.158 64.362  1.00 117.38 ? 315 VAL F CB  1 
ATOM   16772 C CG1 . VAL F 2 315 ? 39.403  -25.292 63.494  1.00 112.54 ? 315 VAL F CG1 1 
ATOM   16773 C CG2 . VAL F 2 315 ? 38.384  -23.005 63.505  1.00 122.16 ? 315 VAL F CG2 1 
ATOM   16774 N N   . GLY F 2 316 ? 37.599  -27.011 65.893  1.00 109.43 ? 316 GLY F N   1 
ATOM   16775 C CA  . GLY F 2 316 ? 37.952  -28.193 66.648  1.00 112.69 ? 316 GLY F CA  1 
ATOM   16776 C C   . GLY F 2 316 ? 39.345  -28.705 66.329  1.00 112.01 ? 316 GLY F C   1 
ATOM   16777 O O   . GLY F 2 316 ? 40.041  -28.223 65.435  1.00 109.49 ? 316 GLY F O   1 
ATOM   16778 N N   . GLN F 2 317 ? 39.757  -29.716 67.091  1.00 113.88 ? 317 GLN F N   1 
ATOM   16779 C CA  . GLN F 2 317 ? 41.070  -30.308 66.886  1.00 112.26 ? 317 GLN F CA  1 
ATOM   16780 C C   . GLN F 2 317 ? 41.098  -31.095 65.580  1.00 114.90 ? 317 GLN F C   1 
ATOM   16781 O O   . GLN F 2 317 ? 40.098  -31.683 65.160  1.00 116.17 ? 317 GLN F O   1 
ATOM   16782 C CB  . GLN F 2 317 ? 41.445  -31.213 68.063  1.00 113.40 ? 317 GLN F CB  1 
ATOM   16783 C CG  . GLN F 2 317 ? 41.585  -30.480 69.389  1.00 111.14 ? 317 GLN F CG  1 
ATOM   16784 C CD  . GLN F 2 317 ? 41.923  -31.395 70.549  1.00 105.60 ? 317 GLN F CD  1 
ATOM   16785 O OE1 . GLN F 2 317 ? 42.096  -32.600 70.376  1.00 110.28 ? 317 GLN F OE1 1 
ATOM   16786 N NE2 . GLN F 2 317 ? 42.017  -30.822 71.745  1.00 97.78  ? 317 GLN F NE2 1 
ATOM   16787 N N   . TRP F 2 318 ? 42.265  -31.099 64.937  1.00 116.70 ? 318 TRP F N   1 
ATOM   16788 C CA  . TRP F 2 318 ? 42.505  -31.822 63.687  1.00 116.44 ? 318 TRP F CA  1 
ATOM   16789 C C   . TRP F 2 318 ? 41.554  -31.407 62.568  1.00 115.25 ? 318 TRP F C   1 
ATOM   16790 O O   . TRP F 2 318 ? 41.424  -32.119 61.568  1.00 114.99 ? 318 TRP F O   1 
ATOM   16791 C CB  . TRP F 2 318 ? 42.425  -33.340 63.887  1.00 118.12 ? 318 TRP F CB  1 
ATOM   16792 C CG  . TRP F 2 318 ? 43.563  -33.921 64.659  1.00 121.39 ? 318 TRP F CG  1 
ATOM   16793 C CD1 . TRP F 2 318 ? 44.834  -34.134 64.210  1.00 122.14 ? 318 TRP F CD1 1 
ATOM   16794 C CD2 . TRP F 2 318 ? 43.530  -34.396 66.009  1.00 124.19 ? 318 TRP F CD2 1 
ATOM   16795 N NE1 . TRP F 2 318 ? 45.599  -34.697 65.202  1.00 123.77 ? 318 TRP F NE1 1 
ATOM   16796 C CE2 . TRP F 2 318 ? 44.821  -34.870 66.316  1.00 123.81 ? 318 TRP F CE2 1 
ATOM   16797 C CE3 . TRP F 2 318 ? 42.537  -34.460 66.991  1.00 123.33 ? 318 TRP F CE3 1 
ATOM   16798 C CZ2 . TRP F 2 318 ? 45.144  -35.401 67.563  1.00 122.72 ? 318 TRP F CZ2 1 
ATOM   16799 C CZ3 . TRP F 2 318 ? 42.859  -34.987 68.227  1.00 124.51 ? 318 TRP F CZ3 1 
ATOM   16800 C CH2 . TRP F 2 318 ? 44.152  -35.450 68.503  1.00 126.62 ? 318 TRP F CH2 1 
ATOM   16801 N N   . ALA F 2 319 ? 40.875  -30.271 62.704  1.00 112.67 ? 319 ALA F N   1 
ATOM   16802 C CA  . ALA F 2 319 ? 39.978  -29.815 61.654  1.00 109.33 ? 319 ALA F CA  1 
ATOM   16803 C C   . ALA F 2 319 ? 40.773  -29.102 60.570  1.00 109.03 ? 319 ALA F C   1 
ATOM   16804 O O   . ALA F 2 319 ? 41.678  -28.316 60.862  1.00 111.32 ? 319 ALA F O   1 
ATOM   16805 C CB  . ALA F 2 319 ? 38.910  -28.883 62.225  1.00 111.05 ? 319 ALA F CB  1 
ATOM   16806 N N   . ARG F 2 320 ? 40.426  -29.365 59.314  1.00 111.11 ? 320 ARG F N   1 
ATOM   16807 C CA  . ARG F 2 320 ? 41.108  -28.754 58.183  1.00 111.58 ? 320 ARG F CA  1 
ATOM   16808 C C   . ARG F 2 320 ? 40.172  -27.779 57.489  1.00 104.69 ? 320 ARG F C   1 
ATOM   16809 O O   . ARG F 2 320 ? 39.057  -28.143 57.102  1.00 99.45  ? 320 ARG F O   1 
ATOM   16810 C CB  . ARG F 2 320 ? 41.608  -29.791 57.175  1.00 109.04 ? 320 ARG F CB  1 
ATOM   16811 C CG  . ARG F 2 320 ? 42.355  -29.139 56.016  1.00 108.84 ? 320 ARG F CG  1 
ATOM   16812 C CD  . ARG F 2 320 ? 42.842  -30.141 54.991  1.00 109.18 ? 320 ARG F CD  1 
ATOM   16813 N NE  . ARG F 2 320 ? 43.580  -29.504 53.906  1.00 113.63 ? 320 ARG F NE  1 
ATOM   16814 C CZ  . ARG F 2 320 ? 44.901  -29.365 53.890  1.00 115.46 ? 320 ARG F CZ  1 
ATOM   16815 N NH1 . ARG F 2 320 ? 45.628  -29.820 54.902  1.00 118.54 ? 320 ARG F NH1 1 
ATOM   16816 N NH2 . ARG F 2 320 ? 45.496  -28.772 52.864  1.00 113.42 ? 320 ARG F NH2 1 
ATOM   16817 N N   . ILE F 2 321 ? 40.636  -26.545 57.333  1.00 105.88 ? 321 ILE F N   1 
ATOM   16818 C CA  . ILE F 2 321 ? 39.873  -25.469 56.719  1.00 100.79 ? 321 ILE F CA  1 
ATOM   16819 C C   . ILE F 2 321 ? 40.713  -24.911 55.579  1.00 102.67 ? 321 ILE F C   1 
ATOM   16820 O O   . ILE F 2 321 ? 41.883  -24.571 55.778  1.00 106.38 ? 321 ILE F O   1 
ATOM   16821 C CB  . ILE F 2 321 ? 39.526  -24.363 57.733  1.00 102.08 ? 321 ILE F CB  1 
ATOM   16822 C CG1 . ILE F 2 321 ? 38.830  -24.956 58.960  1.00 107.77 ? 321 ILE F CG1 1 
ATOM   16823 C CG2 . ILE F 2 321 ? 38.660  -23.303 57.085  1.00 101.93 ? 321 ILE F CG2 1 
ATOM   16824 C CD1 . ILE F 2 321 ? 37.513  -25.626 58.647  1.00 108.41 ? 321 ILE F CD1 1 
ATOM   16825 N N   . GLU F 2 322 ? 40.133  -24.834 54.384  1.00 101.91 ? 322 GLU F N   1 
ATOM   16826 C CA  . GLU F 2 322 ? 40.873  -24.336 53.232  1.00 99.43  ? 322 GLU F CA  1 
ATOM   16827 C C   . GLU F 2 322 ? 39.908  -23.776 52.197  1.00 93.43  ? 322 GLU F C   1 
ATOM   16828 O O   . GLU F 2 322 ? 38.690  -23.949 52.286  1.00 95.35  ? 322 GLU F O   1 
ATOM   16829 C CB  . GLU F 2 322 ? 41.735  -25.432 52.594  1.00 99.36  ? 322 GLU F CB  1 
ATOM   16830 C CG  . GLU F 2 322 ? 40.932  -26.542 51.930  1.00 94.60  ? 322 GLU F CG  1 
ATOM   16831 C CD  . GLU F 2 322 ? 41.805  -27.562 51.221  1.00 98.50  ? 322 GLU F CD  1 
ATOM   16832 O OE1 . GLU F 2 322 ? 43.046  -27.459 51.314  1.00 103.94 ? 322 GLU F OE1 1 
ATOM   16833 O OE2 . GLU F 2 322 ? 41.247  -28.463 50.560  1.00 99.90  ? 322 GLU F OE2 1 
ATOM   16834 N N   . ASN F 2 323 ? 40.485  -23.091 51.208  1.00 90.05  ? 323 ASN F N   1 
ATOM   16835 C CA  . ASN F 2 323 ? 39.790  -22.672 49.990  1.00 90.53  ? 323 ASN F CA  1 
ATOM   16836 C C   . ASN F 2 323 ? 38.644  -21.702 50.298  1.00 91.69  ? 323 ASN F C   1 
ATOM   16837 O O   . ASN F 2 323 ? 37.471  -21.975 50.025  1.00 93.56  ? 323 ASN F O   1 
ATOM   16838 C CB  . ASN F 2 323 ? 39.296  -23.893 49.204  1.00 91.59  ? 323 ASN F CB  1 
ATOM   16839 C CG  . ASN F 2 323 ? 38.787  -23.531 47.816  1.00 86.60  ? 323 ASN F CG  1 
ATOM   16840 O OD1 . ASN F 2 323 ? 39.110  -22.469 47.281  1.00 83.17  ? 323 ASN F OD1 1 
ATOM   16841 N ND2 . ASN F 2 323 ? 37.995  -24.419 47.224  1.00 88.95  ? 323 ASN F ND2 1 
ATOM   16842 N N   . MET F 2 324 ? 39.010  -20.552 50.864  1.00 92.68  ? 324 MET F N   1 
ATOM   16843 C CA  . MET F 2 324 ? 38.095  -19.423 51.059  1.00 95.58  ? 324 MET F CA  1 
ATOM   16844 C C   . MET F 2 324 ? 36.844  -19.817 51.846  1.00 100.96 ? 324 MET F C   1 
ATOM   16845 O O   . MET F 2 324 ? 35.714  -19.497 51.469  1.00 107.84 ? 324 MET F O   1 
ATOM   16846 C CB  . MET F 2 324 ? 37.723  -18.808 49.709  1.00 92.60  ? 324 MET F CB  1 
ATOM   16847 C CG  . MET F 2 324 ? 38.926  -18.328 48.908  1.00 97.68  ? 324 MET F CG  1 
ATOM   16848 S SD  . MET F 2 324 ? 38.520  -17.865 47.212  1.00 105.79 ? 324 MET F SD  1 
ATOM   16849 C CE  . MET F 2 324 ? 37.839  -19.405 46.604  1.00 87.88  ? 324 MET F CE  1 
ATOM   16850 N N   . THR F 2 325 ? 37.054  -20.519 52.957  1.00 106.94 ? 325 THR F N   1 
ATOM   16851 C CA  . THR F 2 325 ? 35.957  -20.874 53.849  1.00 113.96 ? 325 THR F CA  1 
ATOM   16852 C C   . THR F 2 325 ? 35.630  -19.691 54.753  1.00 135.59 ? 325 THR F C   1 
ATOM   16853 O O   . THR F 2 325 ? 36.508  -19.170 55.449  1.00 134.78 ? 325 THR F O   1 
ATOM   16854 C CB  . THR F 2 325 ? 36.319  -22.100 54.687  1.00 108.97 ? 325 THR F CB  1 
ATOM   16855 O OG1 . THR F 2 325 ? 36.718  -23.171 53.824  1.00 105.92 ? 325 THR F OG1 1 
ATOM   16856 C CG2 . THR F 2 325 ? 35.131  -22.548 55.522  1.00 123.41 ? 325 THR F CG2 1 
ATOM   16857 N N   . ILE F 2 326 ? 34.367  -19.272 54.746  1.00 180.75 ? 326 ILE F N   1 
ATOM   16858 C CA  . ILE F 2 326 ? 33.921  -18.074 55.450  1.00 182.63 ? 326 ILE F CA  1 
ATOM   16859 C C   . ILE F 2 326 ? 33.048  -18.502 56.621  1.00 186.84 ? 326 ILE F C   1 
ATOM   16860 O O   . ILE F 2 326 ? 32.021  -19.165 56.429  1.00 186.41 ? 326 ILE F O   1 
ATOM   16861 C CB  . ILE F 2 326 ? 33.158  -17.123 54.516  1.00 182.33 ? 326 ILE F CB  1 
ATOM   16862 C CG1 . ILE F 2 326 ? 33.970  -16.868 53.244  1.00 180.19 ? 326 ILE F CG1 1 
ATOM   16863 C CG2 . ILE F 2 326 ? 32.847  -15.813 55.226  1.00 183.91 ? 326 ILE F CG2 1 
ATOM   16864 C CD1 . ILE F 2 326 ? 35.311  -16.225 53.500  1.00 179.74 ? 326 ILE F CD1 1 
ATOM   16865 N N   . LEU F 2 327 ? 33.458  -18.129 57.831  1.00 239.08 ? 327 LEU F N   1 
ATOM   16866 C CA  . LEU F 2 327 ? 32.740  -18.468 59.051  1.00 241.19 ? 327 LEU F CA  1 
ATOM   16867 C C   . LEU F 2 327 ? 32.180  -17.211 59.703  1.00 242.31 ? 327 LEU F C   1 
ATOM   16868 O O   . LEU F 2 327 ? 32.840  -16.168 59.732  1.00 241.80 ? 327 LEU F O   1 
ATOM   16869 C CB  . LEU F 2 327 ? 33.654  -19.198 60.041  1.00 241.39 ? 327 LEU F CB  1 
ATOM   16870 C CG  . LEU F 2 327 ? 34.247  -20.533 59.583  1.00 240.29 ? 327 LEU F CG  1 
ATOM   16871 C CD1 . LEU F 2 327 ? 34.989  -21.213 60.725  1.00 241.62 ? 327 LEU F CD1 1 
ATOM   16872 C CD2 . LEU F 2 327 ? 33.162  -21.440 59.027  1.00 240.46 ? 327 LEU F CD2 1 
ATOM   16873 N N   . GLY F 2 328 ? 30.959  -17.316 60.220  1.00 167.31 ? 328 GLY F N   1 
ATOM   16874 C CA  . GLY F 2 328 ? 30.335  -16.228 60.939  1.00 141.00 ? 328 GLY F CA  1 
ATOM   16875 C C   . GLY F 2 328 ? 30.754  -16.189 62.398  1.00 126.74 ? 328 GLY F C   1 
ATOM   16876 O O   . GLY F 2 328 ? 31.620  -16.935 62.858  1.00 127.59 ? 328 GLY F O   1 
ATOM   16877 N N   . GLU F 2 329 ? 30.119  -15.281 63.134  1.00 116.53 ? 329 GLU F N   1 
ATOM   16878 C CA  . GLU F 2 329 ? 30.386  -15.153 64.559  1.00 106.23 ? 329 GLU F CA  1 
ATOM   16879 C C   . GLU F 2 329 ? 29.801  -16.339 65.315  1.00 101.63 ? 329 GLU F C   1 
ATOM   16880 O O   . GLU F 2 329 ? 28.678  -16.774 65.046  1.00 104.48 ? 329 GLU F O   1 
ATOM   16881 C CB  . GLU F 2 329 ? 29.803  -13.846 65.099  1.00 106.88 ? 329 GLU F CB  1 
ATOM   16882 C CG  . GLU F 2 329 ? 29.920  -13.691 66.608  1.00 103.49 ? 329 GLU F CG  1 
ATOM   16883 C CD  . GLU F 2 329 ? 29.237  -12.443 67.130  1.00 104.42 ? 329 GLU F CD  1 
ATOM   16884 O OE1 . GLU F 2 329 ? 28.773  -11.624 66.309  1.00 105.42 ? 329 GLU F OE1 1 
ATOM   16885 O OE2 . GLU F 2 329 ? 29.169  -12.280 68.366  1.00 110.59 ? 329 GLU F OE2 1 
ATOM   16886 N N   . ASP F 2 330 ? 30.577  -16.861 66.266  1.00 101.08 ? 330 ASP F N   1 
ATOM   16887 C CA  . ASP F 2 330 ? 30.147  -17.958 67.132  1.00 102.01 ? 330 ASP F CA  1 
ATOM   16888 C C   . ASP F 2 330 ? 29.757  -19.185 66.303  1.00 102.92 ? 330 ASP F C   1 
ATOM   16889 O O   . ASP F 2 330 ? 28.616  -19.651 66.309  1.00 102.36 ? 330 ASP F O   1 
ATOM   16890 C CB  . ASP F 2 330 ? 29.001  -17.505 68.046  1.00 99.02  ? 330 ASP F CB  1 
ATOM   16891 C CG  . ASP F 2 330 ? 28.539  -18.596 68.989  1.00 102.19 ? 330 ASP F CG  1 
ATOM   16892 O OD1 . ASP F 2 330 ? 29.314  -18.969 69.893  1.00 108.93 ? 330 ASP F OD1 1 
ATOM   16893 O OD2 . ASP F 2 330 ? 27.397  -19.076 68.823  1.00 99.57  ? 330 ASP F OD2 1 
ATOM   16894 N N   . VAL F 2 331 ? 30.743  -19.702 65.577  1.00 104.99 ? 331 VAL F N   1 
ATOM   16895 C CA  . VAL F 2 331 ? 30.596  -20.919 64.791  1.00 107.11 ? 331 VAL F CA  1 
ATOM   16896 C C   . VAL F 2 331 ? 31.527  -21.968 65.374  1.00 111.19 ? 331 VAL F C   1 
ATOM   16897 O O   . VAL F 2 331 ? 32.735  -21.735 65.496  1.00 111.68 ? 331 VAL F O   1 
ATOM   16898 C CB  . VAL F 2 331 ? 30.899  -20.683 63.301  1.00 116.40 ? 331 VAL F CB  1 
ATOM   16899 C CG1 . VAL F 2 331 ? 30.830  -21.996 62.540  1.00 125.67 ? 331 VAL F CG1 1 
ATOM   16900 C CG2 . VAL F 2 331 ? 29.925  -19.677 62.717  1.00 117.90 ? 331 VAL F CG2 1 
ATOM   16901 N N   . HIS F 2 332 ? 30.968  -23.119 65.725  1.00 113.51 ? 332 HIS F N   1 
ATOM   16902 C CA  . HIS F 2 332 ? 31.696  -24.169 66.425  1.00 115.36 ? 332 HIS F CA  1 
ATOM   16903 C C   . HIS F 2 332 ? 31.923  -25.339 65.477  1.00 113.85 ? 332 HIS F C   1 
ATOM   16904 O O   . HIS F 2 332 ? 30.996  -26.105 65.188  1.00 116.96 ? 332 HIS F O   1 
ATOM   16905 C CB  . HIS F 2 332 ? 30.935  -24.590 67.677  1.00 116.98 ? 332 HIS F CB  1 
ATOM   16906 C CG  . HIS F 2 332 ? 30.766  -23.480 68.666  1.00 118.08 ? 332 HIS F CG  1 
ATOM   16907 N ND1 . HIS F 2 332 ? 31.562  -23.351 69.784  1.00 128.12 ? 332 HIS F ND1 1 
ATOM   16908 C CD2 . HIS F 2 332 ? 29.912  -22.430 68.689  1.00 117.31 ? 332 HIS F CD2 1 
ATOM   16909 C CE1 . HIS F 2 332 ? 31.194  -22.278 70.462  1.00 128.93 ? 332 HIS F CE1 1 
ATOM   16910 N NE2 . HIS F 2 332 ? 30.195  -21.701 69.818  1.00 124.43 ? 332 HIS F NE2 1 
ATOM   16911 N N   . VAL F 2 333 ? 33.157  -25.472 65.004  1.00 110.54 ? 333 VAL F N   1 
ATOM   16912 C CA  . VAL F 2 333 ? 33.553  -26.569 64.129  1.00 113.14 ? 333 VAL F CA  1 
ATOM   16913 C C   . VAL F 2 333 ? 34.024  -27.728 64.995  1.00 110.57 ? 333 VAL F C   1 
ATOM   16914 O O   . VAL F 2 333 ? 34.919  -27.566 65.832  1.00 109.20 ? 333 VAL F O   1 
ATOM   16915 C CB  . VAL F 2 333 ? 34.655  -26.128 63.155  1.00 114.06 ? 333 VAL F CB  1 
ATOM   16916 C CG1 . VAL F 2 333 ? 35.038  -27.277 62.236  1.00 113.82 ? 333 VAL F CG1 1 
ATOM   16917 C CG2 . VAL F 2 333 ? 34.200  -24.917 62.360  1.00 120.43 ? 333 VAL F CG2 1 
ATOM   16918 N N   . SER F 2 334 ? 33.416  -28.895 64.805  1.00 111.76 ? 334 SER F N   1 
ATOM   16919 C CA  . SER F 2 334 ? 33.813  -30.066 65.568  1.00 114.25 ? 334 SER F CA  1 
ATOM   16920 C C   . SER F 2 334 ? 35.230  -30.494 65.192  1.00 115.21 ? 334 SER F C   1 
ATOM   16921 O O   . SER F 2 334 ? 35.853  -29.959 64.270  1.00 115.03 ? 334 SER F O   1 
ATOM   16922 C CB  . SER F 2 334 ? 32.837  -31.217 65.333  1.00 116.99 ? 334 SER F CB  1 
ATOM   16923 O OG  . SER F 2 334 ? 31.532  -30.861 65.744  1.00 118.35 ? 334 SER F OG  1 
ATOM   16924 N N   . ASP F 2 335 ? 35.741  -31.475 65.928  1.00 120.21 ? 335 ASP F N   1 
ATOM   16925 C CA  . ASP F 2 335 ? 37.055  -32.014 65.626  1.00 120.75 ? 335 ASP F CA  1 
ATOM   16926 C C   . ASP F 2 335 ? 37.012  -32.820 64.333  1.00 125.40 ? 335 ASP F C   1 
ATOM   16927 O O   . ASP F 2 335 ? 35.976  -33.377 63.954  1.00 124.82 ? 335 ASP F O   1 
ATOM   16928 C CB  . ASP F 2 335 ? 37.559  -32.892 66.773  1.00 127.05 ? 335 ASP F CB  1 
ATOM   16929 C CG  . ASP F 2 335 ? 37.567  -32.168 68.108  1.00 129.82 ? 335 ASP F CG  1 
ATOM   16930 O OD1 . ASP F 2 335 ? 37.659  -30.924 68.116  1.00 126.82 ? 335 ASP F OD1 1 
ATOM   16931 O OD2 . ASP F 2 335 ? 37.492  -32.849 69.153  1.00 133.85 ? 335 ASP F OD2 1 
ATOM   16932 N N   . GLU F 2 336 ? 38.158  -32.872 63.650  1.00 128.33 ? 336 GLU F N   1 
ATOM   16933 C CA  . GLU F 2 336 ? 38.361  -33.708 62.466  1.00 127.87 ? 336 GLU F CA  1 
ATOM   16934 C C   . GLU F 2 336 ? 37.423  -33.337 61.319  1.00 127.53 ? 336 GLU F C   1 
ATOM   16935 O O   . GLU F 2 336 ? 37.114  -34.177 60.468  1.00 127.34 ? 336 GLU F O   1 
ATOM   16936 C CB  . GLU F 2 336 ? 38.214  -35.198 62.805  1.00 128.81 ? 336 GLU F CB  1 
ATOM   16937 C CG  . GLU F 2 336 ? 38.898  -35.621 64.098  1.00 129.46 ? 336 GLU F CG  1 
ATOM   16938 C CD  . GLU F 2 336 ? 38.390  -36.953 64.616  1.00 130.31 ? 336 GLU F CD  1 
ATOM   16939 O OE1 . GLU F 2 336 ? 37.839  -37.734 63.812  1.00 130.42 ? 336 GLU F OE1 1 
ATOM   16940 O OE2 . GLU F 2 336 ? 38.535  -37.215 65.828  1.00 130.50 ? 336 GLU F OE2 1 
ATOM   16941 N N   . ILE F 2 337 ? 36.957  -32.089 61.280  1.00 118.45 ? 337 ILE F N   1 
ATOM   16942 C CA  . ILE F 2 337 ? 36.009  -31.634 60.269  1.00 115.06 ? 337 ILE F CA  1 
ATOM   16943 C C   . ILE F 2 337 ? 36.757  -30.913 59.158  1.00 115.23 ? 337 ILE F C   1 
ATOM   16944 O O   . ILE F 2 337 ? 37.647  -30.093 59.418  1.00 115.22 ? 337 ILE F O   1 
ATOM   16945 C CB  . ILE F 2 337 ? 34.933  -30.722 60.891  1.00 116.65 ? 337 ILE F CB  1 
ATOM   16946 C CG1 . ILE F 2 337 ? 34.160  -31.476 61.973  1.00 121.35 ? 337 ILE F CG1 1 
ATOM   16947 C CG2 . ILE F 2 337 ? 33.989  -30.194 59.822  1.00 120.83 ? 337 ILE F CG2 1 
ATOM   16948 C CD1 . ILE F 2 337 ? 33.340  -32.632 61.448  1.00 119.94 ? 337 ILE F CD1 1 
ATOM   16949 N N   . TYR F 2 338 ? 36.393  -31.221 57.917  1.00 116.04 ? 338 TYR F N   1 
ATOM   16950 C CA  . TYR F 2 338 ? 37.002  -30.638 56.729  1.00 109.33 ? 338 TYR F CA  1 
ATOM   16951 C C   . TYR F 2 338 ? 36.003  -29.724 56.034  1.00 110.67 ? 338 TYR F C   1 
ATOM   16952 O O   . TYR F 2 338 ? 34.835  -30.091 55.861  1.00 114.06 ? 338 TYR F O   1 
ATOM   16953 C CB  . TYR F 2 338 ? 37.475  -31.731 55.770  1.00 106.67 ? 338 TYR F CB  1 
ATOM   16954 C CG  . TYR F 2 338 ? 37.878  -31.220 54.408  1.00 105.86 ? 338 TYR F CG  1 
ATOM   16955 C CD1 . TYR F 2 338 ? 39.087  -30.562 54.219  1.00 106.42 ? 338 TYR F CD1 1 
ATOM   16956 C CD2 . TYR F 2 338 ? 37.049  -31.396 53.309  1.00 104.56 ? 338 TYR F CD2 1 
ATOM   16957 C CE1 . TYR F 2 338 ? 39.457  -30.094 52.970  1.00 104.37 ? 338 TYR F CE1 1 
ATOM   16958 C CE2 . TYR F 2 338 ? 37.409  -30.932 52.060  1.00 99.13  ? 338 TYR F CE2 1 
ATOM   16959 C CZ  . TYR F 2 338 ? 38.614  -30.282 51.896  1.00 97.59  ? 338 TYR F CZ  1 
ATOM   16960 O OH  . TYR F 2 338 ? 38.977  -29.819 50.653  1.00 95.71  ? 338 TYR F OH  1 
ATOM   16961 N N   . SER F 2 339 ? 36.464  -28.537 55.637  1.00 108.37 ? 339 SER F N   1 
ATOM   16962 C CA  . SER F 2 339 ? 35.634  -27.546 54.959  1.00 104.91 ? 339 SER F CA  1 
ATOM   16963 C C   . SER F 2 339 ? 36.344  -27.075 53.699  1.00 102.89 ? 339 SER F C   1 
ATOM   16964 O O   . SER F 2 339 ? 37.486  -26.609 53.765  1.00 101.80 ? 339 SER F O   1 
ATOM   16965 C CB  . SER F 2 339 ? 35.334  -26.358 55.874  1.00 103.90 ? 339 SER F CB  1 
ATOM   16966 O OG  . SER F 2 339 ? 34.514  -26.752 56.960  1.00 116.15 ? 339 SER F OG  1 
ATOM   16967 N N   . ASN F 2 340 ? 35.667  -27.188 52.558  1.00 102.40 ? 340 ASN F N   1 
ATOM   16968 C CA  . ASN F 2 340 ? 36.228  -26.754 51.284  1.00 95.82  ? 340 ASN F CA  1 
ATOM   16969 C C   . ASN F 2 340 ? 35.434  -25.606 50.670  1.00 92.23  ? 340 ASN F C   1 
ATOM   16970 O O   . ASN F 2 340 ? 34.839  -25.762 49.599  1.00 95.01  ? 340 ASN F O   1 
ATOM   16971 C CB  . ASN F 2 340 ? 36.286  -27.925 50.306  1.00 95.22  ? 340 ASN F CB  1 
ATOM   16972 C CG  . ASN F 2 340 ? 37.094  -27.608 49.071  1.00 94.56  ? 340 ASN F CG  1 
ATOM   16973 O OD1 . ASN F 2 340 ? 38.050  -26.835 49.119  1.00 92.34  ? 340 ASN F OD1 1 
ATOM   16974 N ND2 . ASN F 2 340 ? 36.695  -28.184 47.945  1.00 100.34 ? 340 ASN F ND2 1 
ATOM   16975 N N   . GLY F 2 341 ? 35.400  -24.459 51.339  1.00 94.90  ? 341 GLY F N   1 
ATOM   16976 C CA  . GLY F 2 341 ? 34.703  -23.309 50.799  1.00 92.05  ? 341 GLY F CA  1 
ATOM   16977 C C   . GLY F 2 341 ? 33.279  -23.197 51.298  1.00 96.77  ? 341 GLY F C   1 
ATOM   16978 O O   . GLY F 2 341 ? 32.365  -22.862 50.536  1.00 97.00  ? 341 GLY F O   1 
ATOM   16979 N N   . GLY F 2 342 ? 33.081  -23.466 52.584  1.00 100.86 ? 342 GLY F N   1 
ATOM   16980 C CA  . GLY F 2 342 ? 31.758  -23.399 53.167  1.00 103.91 ? 342 GLY F CA  1 
ATOM   16981 C C   . GLY F 2 342 ? 31.453  -22.038 53.759  1.00 115.85 ? 342 GLY F C   1 
ATOM   16982 O O   . GLY F 2 342 ? 32.035  -21.664 54.782  1.00 127.71 ? 342 GLY F O   1 
ATOM   16983 N N   . VAL F 2 343 ? 30.548  -21.289 53.132  1.00 110.64 ? 343 VAL F N   1 
ATOM   16984 C CA  . VAL F 2 343 ? 30.137  -19.978 53.628  1.00 119.06 ? 343 VAL F CA  1 
ATOM   16985 C C   . VAL F 2 343 ? 29.027  -20.223 54.646  1.00 118.34 ? 343 VAL F C   1 
ATOM   16986 O O   . VAL F 2 343 ? 27.868  -20.440 54.285  1.00 114.79 ? 343 VAL F O   1 
ATOM   16987 C CB  . VAL F 2 343 ? 29.683  -19.059 52.492  1.00 111.37 ? 343 VAL F CB  1 
ATOM   16988 C CG1 . VAL F 2 343 ? 29.457  -17.646 53.011  1.00 114.23 ? 343 VAL F CG1 1 
ATOM   16989 C CG2 . VAL F 2 343 ? 30.705  -19.067 51.361  1.00 108.84 ? 343 VAL F CG2 1 
ATOM   16990 N N   . VAL F 2 344 ? 29.389  -20.191 55.932  1.00 125.80 ? 344 VAL F N   1 
ATOM   16991 C CA  . VAL F 2 344 ? 28.507  -20.613 57.017  1.00 124.74 ? 344 VAL F CA  1 
ATOM   16992 C C   . VAL F 2 344 ? 27.917  -19.399 57.722  1.00 128.50 ? 344 VAL F C   1 
ATOM   16993 O O   . VAL F 2 344 ? 28.561  -18.354 57.864  1.00 132.61 ? 344 VAL F O   1 
ATOM   16994 C CB  . VAL F 2 344 ? 29.262  -21.529 58.004  1.00 127.06 ? 344 VAL F CB  1 
ATOM   16995 C CG1 . VAL F 2 344 ? 28.312  -22.115 59.046  1.00 129.07 ? 344 VAL F CG1 1 
ATOM   16996 C CG2 . VAL F 2 344 ? 29.975  -22.633 57.242  1.00 122.74 ? 344 VAL F CG2 1 
ATOM   16997 N N   . LEU F 2 345 ? 26.668  -19.541 58.158  1.00 134.69 ? 345 LEU F N   1 
ATOM   16998 C CA  . LEU F 2 345 ? 25.980  -18.514 58.921  1.00 133.00 ? 345 LEU F CA  1 
ATOM   16999 C C   . LEU F 2 345 ? 26.411  -18.536 60.387  1.00 133.83 ? 345 LEU F C   1 
ATOM   17000 O O   . LEU F 2 345 ? 26.887  -19.556 60.892  1.00 134.95 ? 345 LEU F O   1 
ATOM   17001 C CB  . LEU F 2 345 ? 24.471  -18.706 58.799  1.00 136.50 ? 345 LEU F CB  1 
ATOM   17002 C CG  . LEU F 2 345 ? 23.766  -17.926 57.683  1.00 131.67 ? 345 LEU F CG  1 
ATOM   17003 C CD1 . LEU F 2 345 ? 24.288  -18.311 56.301  1.00 126.99 ? 345 LEU F CD1 1 
ATOM   17004 C CD2 . LEU F 2 345 ? 22.266  -18.152 57.769  1.00 134.77 ? 345 LEU F CD2 1 
ATOM   17005 N N   . PRO F 2 346 ? 26.262  -17.413 61.089  1.00 117.27 ? 346 PRO F N   1 
ATOM   17006 C CA  . PRO F 2 346 ? 26.639  -17.367 62.505  1.00 111.50 ? 346 PRO F CA  1 
ATOM   17007 C C   . PRO F 2 346 ? 25.750  -18.247 63.368  1.00 106.04 ? 346 PRO F C   1 
ATOM   17008 O O   . PRO F 2 346 ? 24.629  -18.608 63.001  1.00 107.90 ? 346 PRO F O   1 
ATOM   17009 C CB  . PRO F 2 346 ? 26.462  -15.890 62.873  1.00 109.52 ? 346 PRO F CB  1 
ATOM   17010 C CG  . PRO F 2 346 ? 25.497  -15.365 61.873  1.00 110.66 ? 346 PRO F CG  1 
ATOM   17011 C CD  . PRO F 2 346 ? 25.808  -16.099 60.605  1.00 115.40 ? 346 PRO F CD  1 
ATOM   17012 N N   . HIS F 2 347 ? 26.280  -18.579 64.547  1.00 103.03 ? 347 HIS F N   1 
ATOM   17013 C CA  . HIS F 2 347 ? 25.591  -19.398 65.541  1.00 99.06  ? 347 HIS F CA  1 
ATOM   17014 C C   . HIS F 2 347 ? 25.180  -20.744 64.943  1.00 99.75  ? 347 HIS F C   1 
ATOM   17015 O O   . HIS F 2 347 ? 24.005  -21.114 64.899  1.00 97.75  ? 347 HIS F O   1 
ATOM   17016 C CB  . HIS F 2 347 ? 24.395  -18.641 66.126  1.00 96.44  ? 347 HIS F CB  1 
ATOM   17017 C CG  . HIS F 2 347 ? 24.750  -17.287 66.658  1.00 96.38  ? 347 HIS F CG  1 
ATOM   17018 N ND1 . HIS F 2 347 ? 25.578  -17.111 67.746  1.00 98.02  ? 347 HIS F ND1 1 
ATOM   17019 C CD2 . HIS F 2 347 ? 24.402  -16.046 66.244  1.00 97.72  ? 347 HIS F CD2 1 
ATOM   17020 C CE1 . HIS F 2 347 ? 25.721  -15.819 67.983  1.00 101.57 ? 347 HIS F CE1 1 
ATOM   17021 N NE2 . HIS F 2 347 ? 25.018  -15.151 67.086  1.00 102.32 ? 347 HIS F NE2 1 
ATOM   17022 N N   . LYS F 2 348 ? 26.191  -21.480 64.488  1.00 101.03 ? 348 LYS F N   1 
ATOM   17023 C CA  . LYS F 2 348 ? 25.992  -22.768 63.842  1.00 108.26 ? 348 LYS F CA  1 
ATOM   17024 C C   . LYS F 2 348 ? 27.055  -23.741 64.321  1.00 111.04 ? 348 LYS F C   1 
ATOM   17025 O O   . LYS F 2 348 ? 28.236  -23.390 64.391  1.00 109.96 ? 348 LYS F O   1 
ATOM   17026 C CB  . LYS F 2 348 ? 26.042  -22.638 62.316  1.00 113.29 ? 348 LYS F CB  1 
ATOM   17027 C CG  . LYS F 2 348 ? 25.650  -23.910 61.595  1.00 116.54 ? 348 LYS F CG  1 
ATOM   17028 C CD  . LYS F 2 348 ? 24.215  -24.276 61.907  1.00 119.24 ? 348 LYS F CD  1 
ATOM   17029 C CE  . LYS F 2 348 ? 23.799  -25.540 61.186  1.00 120.96 ? 348 LYS F CE  1 
ATOM   17030 N NZ  . LYS F 2 348 ? 22.367  -25.844 61.447  1.00 124.91 ? 348 LYS F NZ  1 
ATOM   17031 N N   . GLU F 2 349 ? 26.628  -24.955 64.651  1.00 112.23 ? 349 GLU F N   1 
ATOM   17032 C CA  . GLU F 2 349 ? 27.524  -26.021 65.077  1.00 117.07 ? 349 GLU F CA  1 
ATOM   17033 C C   . GLU F 2 349 ? 27.775  -26.943 63.892  1.00 121.91 ? 349 GLU F C   1 
ATOM   17034 O O   . GLU F 2 349 ? 26.843  -27.576 63.385  1.00 120.94 ? 349 GLU F O   1 
ATOM   17035 C CB  . GLU F 2 349 ? 26.917  -26.790 66.250  1.00 120.68 ? 349 GLU F CB  1 
ATOM   17036 C CG  . GLU F 2 349 ? 26.751  -25.949 67.509  1.00 125.34 ? 349 GLU F CG  1 
ATOM   17037 C CD  . GLU F 2 349 ? 26.240  -26.747 68.692  1.00 128.81 ? 349 GLU F CD  1 
ATOM   17038 O OE1 . GLU F 2 349 ? 25.597  -27.796 68.474  1.00 126.51 ? 349 GLU F OE1 1 
ATOM   17039 O OE2 . GLU F 2 349 ? 26.467  -26.315 69.842  1.00 131.59 ? 349 GLU F OE2 1 
ATOM   17040 N N   . ILE F 2 350 ? 29.028  -27.019 63.458  1.00 144.92 ? 350 ILE F N   1 
ATOM   17041 C CA  . ILE F 2 350 ? 29.415  -27.824 62.306  1.00 143.95 ? 350 ILE F CA  1 
ATOM   17042 C C   . ILE F 2 350 ? 29.963  -29.151 62.813  1.00 144.06 ? 350 ILE F C   1 
ATOM   17043 O O   . ILE F 2 350 ? 31.042  -29.201 63.415  1.00 143.44 ? 350 ILE F O   1 
ATOM   17044 C CB  . ILE F 2 350 ? 30.437  -27.095 61.426  1.00 142.42 ? 350 ILE F CB  1 
ATOM   17045 C CG1 . ILE F 2 350 ? 29.875  -25.745 60.977  1.00 142.61 ? 350 ILE F CG1 1 
ATOM   17046 C CG2 . ILE F 2 350 ? 30.802  -27.950 60.224  1.00 141.13 ? 350 ILE F CG2 1 
ATOM   17047 C CD1 . ILE F 2 350 ? 28.555  -25.852 60.242  1.00 143.02 ? 350 ILE F CD1 1 
ATOM   17048 N N   . LYS F 2 351 ? 29.218  -30.229 62.571  1.00 129.16 ? 351 LYS F N   1 
ATOM   17049 C CA  . LYS F 2 351 ? 29.637  -31.569 62.949  1.00 123.75 ? 351 LYS F CA  1 
ATOM   17050 C C   . LYS F 2 351 ? 29.853  -32.481 61.750  1.00 122.11 ? 351 LYS F C   1 
ATOM   17051 O O   . LYS F 2 351 ? 30.134  -33.671 61.940  1.00 120.22 ? 351 LYS F O   1 
ATOM   17052 C CB  . LYS F 2 351 ? 28.603  -32.200 63.891  1.00 121.77 ? 351 LYS F CB  1 
ATOM   17053 C CG  . LYS F 2 351 ? 28.372  -31.413 65.168  1.00 118.77 ? 351 LYS F CG  1 
ATOM   17054 C CD  . LYS F 2 351 ? 27.498  -32.183 66.142  1.00 111.95 ? 351 LYS F CD  1 
ATOM   17055 C CE  . LYS F 2 351 ? 27.360  -31.434 67.457  1.00 114.42 ? 351 LYS F CE  1 
ATOM   17056 N NZ  . LYS F 2 351 ? 26.588  -32.202 68.473  1.00 113.89 ? 351 LYS F NZ  1 
ATOM   17057 N N   . SER F 2 352 ? 29.726  -31.963 60.529  1.00 124.74 ? 352 SER F N   1 
ATOM   17058 C CA  . SER F 2 352 ? 29.916  -32.741 59.316  1.00 125.25 ? 352 SER F CA  1 
ATOM   17059 C C   . SER F 2 352 ? 30.862  -32.002 58.381  1.00 124.79 ? 352 SER F C   1 
ATOM   17060 O O   . SER F 2 352 ? 31.041  -30.785 58.477  1.00 124.22 ? 352 SER F O   1 
ATOM   17061 C CB  . SER F 2 352 ? 28.582  -33.014 58.609  1.00 127.73 ? 352 SER F CB  1 
ATOM   17062 O OG  . SER F 2 352 ? 27.678  -33.690 59.465  1.00 130.17 ? 352 SER F OG  1 
ATOM   17063 N N   . ASN F 2 353 ? 31.470  -32.756 57.469  1.00 133.54 ? 353 ASN F N   1 
ATOM   17064 C CA  . ASN F 2 353 ? 32.423  -32.180 56.531  1.00 131.40 ? 353 ASN F CA  1 
ATOM   17065 C C   . ASN F 2 353 ? 31.705  -31.404 55.434  1.00 130.72 ? 353 ASN F C   1 
ATOM   17066 O O   . ASN F 2 353 ? 30.706  -31.867 54.875  1.00 132.38 ? 353 ASN F O   1 
ATOM   17067 C CB  . ASN F 2 353 ? 33.283  -33.277 55.901  1.00 130.11 ? 353 ASN F CB  1 
ATOM   17068 C CG  . ASN F 2 353 ? 34.061  -34.073 56.928  1.00 131.40 ? 353 ASN F CG  1 
ATOM   17069 O OD1 . ASN F 2 353 ? 34.370  -33.575 58.011  1.00 135.30 ? 353 ASN F OD1 1 
ATOM   17070 N ND2 . ASN F 2 353 ? 34.386  -35.316 56.592  1.00 130.72 ? 353 ASN F ND2 1 
ATOM   17071 N N   . ILE F 2 354 ? 32.223  -30.213 55.131  1.00 129.51 ? 354 ILE F N   1 
ATOM   17072 C CA  . ILE F 2 354 ? 31.783  -29.444 53.974  1.00 125.62 ? 354 ILE F CA  1 
ATOM   17073 C C   . ILE F 2 354 ? 32.796  -29.693 52.867  1.00 120.07 ? 354 ILE F C   1 
ATOM   17074 O O   . ILE F 2 354 ? 33.609  -28.822 52.538  1.00 117.53 ? 354 ILE F O   1 
ATOM   17075 C CB  . ILE F 2 354 ? 31.647  -27.945 54.289  1.00 122.38 ? 354 ILE F CB  1 
ATOM   17076 C CG1 . ILE F 2 354 ? 30.836  -27.744 55.566  1.00 129.25 ? 354 ILE F CG1 1 
ATOM   17077 C CG2 . ILE F 2 354 ? 30.973  -27.222 53.132  1.00 114.90 ? 354 ILE F CG2 1 
ATOM   17078 C CD1 . ILE F 2 354 ? 30.655  -26.297 55.939  1.00 133.22 ? 354 ILE F CD1 1 
ATOM   17079 N N   . LEU F 2 355 ? 32.760  -30.899 52.302  1.00 113.35 ? 355 LEU F N   1 
ATOM   17080 C CA  . LEU F 2 355 ? 33.778  -31.358 51.366  1.00 107.50 ? 355 LEU F CA  1 
ATOM   17081 C C   . LEU F 2 355 ? 33.796  -30.581 50.056  1.00 103.91 ? 355 LEU F C   1 
ATOM   17082 O O   . LEU F 2 355 ? 34.747  -30.736 49.282  1.00 105.76 ? 355 LEU F O   1 
ATOM   17083 C CB  . LEU F 2 355 ? 33.573  -32.850 51.092  1.00 106.97 ? 355 LEU F CB  1 
ATOM   17084 C CG  . LEU F 2 355 ? 32.155  -33.379 51.340  1.00 107.44 ? 355 LEU F CG  1 
ATOM   17085 C CD1 . LEU F 2 355 ? 31.210  -32.982 50.213  1.00 105.20 ? 355 LEU F CD1 1 
ATOM   17086 C CD2 . LEU F 2 355 ? 32.160  -34.889 51.540  1.00 105.54 ? 355 LEU F CD2 1 
ATOM   17087 N N   . LYS F 2 356 ? 32.791  -29.759 49.789  1.00 101.86 ? 356 LYS F N   1 
ATOM   17088 C CA  . LYS F 2 356 ? 32.727  -28.953 48.582  1.00 98.93  ? 356 LYS F CA  1 
ATOM   17089 C C   . LYS F 2 356 ? 32.102  -27.612 48.928  1.00 96.00  ? 356 LYS F C   1 
ATOM   17090 O O   . LYS F 2 356 ? 31.419  -27.486 49.951  1.00 96.21  ? 356 LYS F O   1 
ATOM   17091 C CB  . LYS F 2 356 ? 31.925  -29.656 47.477  1.00 102.43 ? 356 LYS F CB  1 
ATOM   17092 C CG  . LYS F 2 356 ? 32.651  -30.831 46.833  1.00 110.91 ? 356 LYS F CG  1 
ATOM   17093 C CD  . LYS F 2 356 ? 31.774  -31.529 45.810  1.00 116.96 ? 356 LYS F CD  1 
ATOM   17094 C CE  . LYS F 2 356 ? 31.414  -30.582 44.679  1.00 115.37 ? 356 LYS F CE  1 
ATOM   17095 N NZ  . LYS F 2 356 ? 32.624  -30.097 43.955  1.00 110.31 ? 356 LYS F NZ  1 
ATOM   17096 N N   . PRO F 2 357 ? 32.339  -26.583 48.112  1.00 93.49  ? 357 PRO F N   1 
ATOM   17097 C CA  . PRO F 2 357 ? 31.776  -25.258 48.403  1.00 93.03  ? 357 PRO F CA  1 
ATOM   17098 C C   . PRO F 2 357 ? 30.265  -25.306 48.578  1.00 96.58  ? 357 PRO F C   1 
ATOM   17099 O O   . PRO F 2 357 ? 29.535  -25.827 47.731  1.00 96.50  ? 357 PRO F O   1 
ATOM   17100 C CB  . PRO F 2 357 ? 32.179  -24.432 47.178  1.00 91.04  ? 357 PRO F CB  1 
ATOM   17101 C CG  . PRO F 2 357 ? 33.428  -25.082 46.695  1.00 92.25  ? 357 PRO F CG  1 
ATOM   17102 C CD  . PRO F 2 357 ? 33.242  -26.550 46.946  1.00 95.88  ? 357 PRO F CD  1 
ATOM   17103 N N   . GLU F 2 358 ? 29.798  -24.750 49.694  1.00 98.85  ? 358 GLU F N   1 
ATOM   17104 C CA  . GLU F 2 358 ? 28.403  -24.874 50.086  1.00 99.69  ? 358 GLU F CA  1 
ATOM   17105 C C   . GLU F 2 358 ? 28.085  -23.802 51.116  1.00 97.55  ? 358 GLU F C   1 
ATOM   17106 O O   . GLU F 2 358 ? 28.918  -23.492 51.969  1.00 99.20  ? 358 GLU F O   1 
ATOM   17107 C CB  . GLU F 2 358 ? 28.133  -26.270 50.660  1.00 103.60 ? 358 GLU F CB  1 
ATOM   17108 C CG  . GLU F 2 358 ? 26.737  -26.490 51.209  1.00 105.71 ? 358 GLU F CG  1 
ATOM   17109 C CD  . GLU F 2 358 ? 26.603  -27.837 51.893  1.00 107.07 ? 358 GLU F CD  1 
ATOM   17110 O OE1 . GLU F 2 358 ? 27.502  -28.686 51.714  1.00 108.11 ? 358 GLU F OE1 1 
ATOM   17111 O OE2 . GLU F 2 358 ? 25.605  -28.046 52.612  1.00 112.26 ? 358 GLU F OE2 1 
ATOM   17112 N N   . ILE F 2 359 ? 26.882  -23.244 51.034  1.00 94.88  ? 359 ILE F N   1 
ATOM   17113 C CA  . ILE F 2 359 ? 26.423  -22.245 51.990  1.00 97.44  ? 359 ILE F CA  1 
ATOM   17114 C C   . ILE F 2 359 ? 25.595  -22.956 53.050  1.00 102.67 ? 359 ILE F C   1 
ATOM   17115 O O   . ILE F 2 359 ? 24.536  -23.520 52.749  1.00 105.66 ? 359 ILE F O   1 
ATOM   17116 C CB  . ILE F 2 359 ? 25.614  -21.133 51.304  1.00 93.25  ? 359 ILE F CB  1 
ATOM   17117 C CG1 . ILE F 2 359 ? 26.499  -20.354 50.329  1.00 94.59  ? 359 ILE F CG1 1 
ATOM   17118 C CG2 . ILE F 2 359 ? 25.014  -20.201 52.345  1.00 96.69  ? 359 ILE F CG2 1 
ATOM   17119 C CD1 . ILE F 2 359 ? 25.759  -19.301 49.536  1.00 83.05  ? 359 ILE F CD1 1 
ATOM   17120 N N   . VAL F 2 360 ? 26.075  -22.926 54.291  1.00 108.45 ? 360 VAL F N   1 
ATOM   17121 C CA  . VAL F 2 360 ? 25.433  -23.597 55.415  1.00 118.46 ? 360 VAL F CA  1 
ATOM   17122 C C   . VAL F 2 360 ? 24.748  -22.550 56.280  1.00 130.44 ? 360 VAL F C   1 
ATOM   17123 O O   . VAL F 2 360 ? 25.302  -21.472 56.524  1.00 127.62 ? 360 VAL F O   1 
ATOM   17124 C CB  . VAL F 2 360 ? 26.450  -24.416 56.234  1.00 121.28 ? 360 VAL F CB  1 
ATOM   17125 C CG1 . VAL F 2 360 ? 25.753  -25.170 57.357  1.00 128.15 ? 360 VAL F CG1 1 
ATOM   17126 C CG2 . VAL F 2 360 ? 27.198  -25.378 55.329  1.00 114.92 ? 360 VAL F CG2 1 
ATOM   17127 N N   . MET F 2 361 ? 23.549  -22.872 56.752  1.00 162.87 ? 361 MET F N   1 
ATOM   17128 C CA  . MET F 2 361 ? 22.775  -21.948 57.572  1.00 164.88 ? 361 MET F CA  1 
ATOM   17129 C C   . MET F 2 361 ? 22.554  -22.477 58.986  1.00 166.92 ? 361 MET F C   1 
ATOM   17130 O O   . MET F 2 361 ? 22.859  -21.796 59.969  1.00 167.61 ? 361 MET F O   1 
ATOM   17131 C CB  . MET F 2 361 ? 21.429  -21.664 56.902  1.00 165.16 ? 361 MET F CB  1 
ATOM   17132 C CG  . MET F 2 361 ? 21.499  -21.669 55.382  1.00 163.12 ? 361 MET F CG  1 
ATOM   17133 S SD  . MET F 2 361 ? 19.938  -21.228 54.601  1.00 166.04 ? 361 MET F SD  1 
ATOM   17134 C CE  . MET F 2 361 ? 19.631  -19.636 55.361  1.00 166.28 ? 361 MET F CE  1 
ATOM   17135 O OXT . MET F 2 361 ? 22.062  -23.588 59.181  1.00 167.78 ? 361 MET F OXT 1 
HETATM 17136 S S   . SO4 G 3 .   ? -10.482 -42.589 27.403  1.00 196.72 ? 501 SO4 A S   1 
HETATM 17137 O O1  . SO4 G 3 .   ? -9.447  -42.749 26.385  1.00 192.83 ? 501 SO4 A O1  1 
HETATM 17138 O O2  . SO4 G 3 .   ? -11.586 -41.807 26.852  1.00 192.05 ? 501 SO4 A O2  1 
HETATM 17139 O O3  . SO4 G 3 .   ? -10.974 -43.901 27.810  1.00 195.44 ? 501 SO4 A O3  1 
HETATM 17140 O O4  . SO4 G 3 .   ? -9.920  -41.902 28.562  1.00 194.13 ? 501 SO4 A O4  1 
HETATM 17141 S S   . SO4 H 3 .   ? 0.395   -39.786 23.634  0.96 164.05 ? 502 SO4 A S   1 
HETATM 17142 O O1  . SO4 H 3 .   ? 0.893   -40.823 22.734  0.96 153.98 ? 502 SO4 A O1  1 
HETATM 17143 O O2  . SO4 H 3 .   ? 0.652   -38.473 23.049  0.96 152.31 ? 502 SO4 A O2  1 
HETATM 17144 O O3  . SO4 H 3 .   ? 1.080   -39.890 24.919  0.96 158.43 ? 502 SO4 A O3  1 
HETATM 17145 O O4  . SO4 H 3 .   ? -1.042  -39.956 23.831  0.96 155.56 ? 502 SO4 A O4  1 
HETATM 17146 S S   . SO4 I 3 .   ? 19.412  -31.276 25.391  1.00 145.60 ? 503 SO4 A S   1 
HETATM 17147 O O1  . SO4 I 3 .   ? 19.697  -30.616 24.121  1.00 129.93 ? 503 SO4 A O1  1 
HETATM 17148 O O2  . SO4 I 3 .   ? 18.158  -32.014 25.269  1.00 130.08 ? 503 SO4 A O2  1 
HETATM 17149 O O3  . SO4 I 3 .   ? 20.499  -32.195 25.721  1.00 134.29 ? 503 SO4 A O3  1 
HETATM 17150 O O4  . SO4 I 3 .   ? 19.293  -30.275 26.449  1.00 136.24 ? 503 SO4 A O4  1 
HETATM 17151 S S   . SO4 J 3 .   ? -2.584  -9.837  -5.099  0.56 78.62  ? 501 SO4 B S   1 
HETATM 17152 O O1  . SO4 J 3 .   ? -1.962  -9.434  -6.357  0.56 83.61  ? 501 SO4 B O1  1 
HETATM 17153 O O2  . SO4 J 3 .   ? -2.704  -11.292 -5.066  0.56 78.21  ? 501 SO4 B O2  1 
HETATM 17154 O O3  . SO4 J 3 .   ? -3.909  -9.233  -4.986  0.56 77.67  ? 501 SO4 B O3  1 
HETATM 17155 O O4  . SO4 J 3 .   ? -1.755  -9.387  -3.985  0.56 88.41  ? 501 SO4 B O4  1 
HETATM 17156 S S   . SO4 K 3 .   ? 59.743  -37.104 34.918  1.00 158.68 ? 401 SO4 D S   1 
HETATM 17157 O O1  . SO4 K 3 .   ? 58.624  -36.991 33.987  1.00 147.80 ? 401 SO4 D O1  1 
HETATM 17158 O O2  . SO4 K 3 .   ? 60.989  -36.831 34.207  1.00 156.15 ? 401 SO4 D O2  1 
HETATM 17159 O O3  . SO4 K 3 .   ? 59.781  -38.453 35.474  1.00 146.64 ? 401 SO4 D O3  1 
HETATM 17160 O O4  . SO4 K 3 .   ? 59.579  -36.138 36.000  1.00 150.41 ? 401 SO4 D O4  1 
HETATM 17161 S S   . SO4 L 3 .   ? 35.133  -60.563 23.492  1.00 137.31 ? 402 SO4 D S   1 
HETATM 17162 O O1  . SO4 L 3 .   ? 35.768  -59.954 22.327  1.00 131.26 ? 402 SO4 D O1  1 
HETATM 17163 O O2  . SO4 L 3 .   ? 33.685  -60.392 23.410  1.00 141.41 ? 402 SO4 D O2  1 
HETATM 17164 O O3  . SO4 L 3 .   ? 35.450  -61.988 23.524  1.00 139.68 ? 402 SO4 D O3  1 
HETATM 17165 O O4  . SO4 L 3 .   ? 35.625  -59.924 24.709  1.00 134.57 ? 402 SO4 D O4  1 
HETATM 17166 S S   . SO4 M 3 .   ? 38.899  -63.436 13.650  0.93 150.45 ? 403 SO4 D S   1 
HETATM 17167 O O1  . SO4 M 3 .   ? 40.108  -63.406 12.834  0.93 141.85 ? 403 SO4 D O1  1 
HETATM 17168 O O2  . SO4 M 3 .   ? 37.721  -63.444 12.786  0.93 143.48 ? 403 SO4 D O2  1 
HETATM 17169 O O3  . SO4 M 3 .   ? 38.897  -64.639 14.476  0.93 152.93 ? 403 SO4 D O3  1 
HETATM 17170 O O4  . SO4 M 3 .   ? 38.870  -62.254 14.508  0.93 142.32 ? 403 SO4 D O4  1 
HETATM 17171 S S   . SO4 N 3 .   ? 40.312  -48.754 -0.264  1.00 151.49 ? 404 SO4 D S   1 
HETATM 17172 O O1  . SO4 N 3 .   ? 40.335  -48.643 -1.720  1.00 148.86 ? 404 SO4 D O1  1 
HETATM 17173 O O2  . SO4 N 3 .   ? 41.237  -49.803 0.157   1.00 140.20 ? 404 SO4 D O2  1 
HETATM 17174 O O3  . SO4 N 3 .   ? 38.962  -49.092 0.178   1.00 139.35 ? 404 SO4 D O3  1 
HETATM 17175 O O4  . SO4 N 3 .   ? 40.718  -47.482 0.327   1.00 137.61 ? 404 SO4 D O4  1 
HETATM 17176 S S   . SO4 O 3 .   ? 16.221  -25.862 67.375  1.00 130.09 ? 401 SO4 E S   1 
HETATM 17177 O O1  . SO4 O 3 .   ? 17.427  -26.683 67.309  1.00 128.88 ? 401 SO4 E O1  1 
HETATM 17178 O O2  . SO4 O 3 .   ? 15.465  -26.016 66.136  1.00 124.71 ? 401 SO4 E O2  1 
HETATM 17179 O O3  . SO4 O 3 .   ? 15.401  -26.284 68.507  1.00 133.62 ? 401 SO4 E O3  1 
HETATM 17180 O O4  . SO4 O 3 .   ? 16.594  -24.460 67.545  1.00 135.14 ? 401 SO4 E O4  1 
HETATM 17181 S S   . SO4 P 3 .   ? 21.065  -9.450  43.210  1.00 150.27 ? 402 SO4 E S   1 
HETATM 17182 O O1  . SO4 P 3 .   ? 22.258  -9.118  42.436  1.00 152.31 ? 402 SO4 E O1  1 
HETATM 17183 O O2  . SO4 P 3 .   ? 19.900  -8.785  42.633  1.00 148.69 ? 402 SO4 E O2  1 
HETATM 17184 O O3  . SO4 P 3 .   ? 20.858  -10.895 43.181  1.00 149.67 ? 402 SO4 E O3  1 
HETATM 17185 O O4  . SO4 P 3 .   ? 21.244  -9.008  44.589  1.00 153.01 ? 402 SO4 E O4  1 
HETATM 17186 S S   . SO4 Q 3 .   ? 26.389  -2.202  50.503  1.00 163.52 ? 401 SO4 F S   1 
HETATM 17187 O O1  . SO4 Q 3 .   ? 27.252  -3.367  50.328  1.00 151.69 ? 401 SO4 F O1  1 
HETATM 17188 O O2  . SO4 Q 3 .   ? 25.929  -1.728  49.201  1.00 170.54 ? 401 SO4 F O2  1 
HETATM 17189 O O3  . SO4 Q 3 .   ? 25.232  -2.571  51.313  1.00 160.52 ? 401 SO4 F O3  1 
HETATM 17190 O O4  . SO4 Q 3 .   ? 27.141  -1.143  51.170  1.00 159.58 ? 401 SO4 F O4  1 
HETATM 17191 S S   . SO4 R 3 .   ? 24.517  -11.047 67.317  1.00 162.98 ? 402 SO4 F S   1 
HETATM 17192 O O1  . SO4 R 3 .   ? 25.181  -12.147 66.623  1.00 153.98 ? 402 SO4 F O1  1 
HETATM 17193 O O2  . SO4 R 3 .   ? 23.220  -10.796 66.694  1.00 162.58 ? 402 SO4 F O2  1 
HETATM 17194 O O3  . SO4 R 3 .   ? 24.331  -11.400 68.722  1.00 165.14 ? 402 SO4 F O3  1 
HETATM 17195 O O4  . SO4 R 3 .   ? 25.340  -9.843  67.229  1.00 158.62 ? 402 SO4 F O4  1 
HETATM 17196 O O   . HOH S 4 .   ? 1.659   -37.682 7.189   1.00 76.30  ? 601 HOH A O   1 
HETATM 17197 O O   . HOH T 4 .   ? 27.093  -14.445 25.926  1.00 75.04  ? 601 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . GLU A 4   ? 0.6445 1.2772 1.5390 -0.2488 0.0753  -0.1079 4   GLU A N   
2     C CA  . GLU A 4   ? 0.6300 1.2726 1.5120 -0.2401 0.0793  -0.1004 4   GLU A CA  
3     C C   . GLU A 4   ? 0.6137 1.2695 1.4855 -0.2287 0.0681  -0.1058 4   GLU A C   
4     O O   . GLU A 4   ? 0.6134 1.2725 1.4883 -0.2277 0.0574  -0.1157 4   GLU A O   
5     C CB  . GLU A 4   ? 0.6811 1.2994 1.5403 -0.2378 0.0885  -0.0882 4   GLU A CB  
6     C CG  . GLU A 4   ? 0.7672 1.3724 1.6327 -0.2480 0.1014  -0.0806 4   GLU A CG  
7     C CD  . GLU A 4   ? 0.8313 1.4129 1.6717 -0.2447 0.1097  -0.0685 4   GLU A CD  
8     O OE1 . GLU A 4   ? 0.8037 1.3778 1.6228 -0.2348 0.1044  -0.0670 4   GLU A OE1 
9     O OE2 . GLU A 4   ? 0.8932 1.4642 1.7351 -0.2520 0.1214  -0.0607 4   GLU A OE2 
10    N N   . LYS A 5   ? 0.6355 1.2985 1.4945 -0.2204 0.0710  -0.0990 5   LYS A N   
11    C CA  . LYS A 5   ? 0.6560 1.3298 1.5026 -0.2093 0.0618  -0.1021 5   LYS A CA  
12    C C   . LYS A 5   ? 0.7342 1.3984 1.5579 -0.2013 0.0675  -0.0915 5   LYS A C   
13    O O   . LYS A 5   ? 0.7544 1.4169 1.5780 -0.2033 0.0780  -0.0829 5   LYS A O   
14    C CB  . LYS A 5   ? 0.6900 1.3944 1.5533 -0.2075 0.0563  -0.1081 5   LYS A CB  
15    C CG  . LYS A 5   ? 0.6934 1.4085 1.5507 -0.1998 0.0433  -0.1165 5   LYS A CG  
16    C CD  . LYS A 5   ? 0.8335 1.5783 1.7058 -0.1977 0.0379  -0.1214 5   LYS A CD  
17    C CE  . LYS A 5   ? 0.8991 1.6538 1.7678 -0.1922 0.0246  -0.1313 5   LYS A CE  
18    N NZ  . LYS A 5   ? 0.8819 1.6237 1.7539 -0.1978 0.0195  -0.1399 5   LYS A NZ  
19    N N   . VAL A 6   ? 0.7432 1.4013 1.5481 -0.1923 0.0607  -0.0924 6   VAL A N   
20    C CA  . VAL A 6   ? 0.6648 1.3121 1.4469 -0.1844 0.0646  -0.0832 6   VAL A CA  
21    C C   . VAL A 6   ? 0.6464 1.3109 1.4212 -0.1743 0.0572  -0.0855 6   VAL A C   
22    O O   . VAL A 6   ? 0.7024 1.3753 1.4793 -0.1715 0.0471  -0.0943 6   VAL A O   
23    C CB  . VAL A 6   ? 0.6292 1.2483 1.3932 -0.1834 0.0643  -0.0805 6   VAL A CB  
24    C CG1 . VAL A 6   ? 0.6691 1.2778 1.4099 -0.1753 0.0680  -0.0712 6   VAL A CG1 
25    C CG2 . VAL A 6   ? 0.7067 1.3077 1.4775 -0.1938 0.0716  -0.0778 6   VAL A CG2 
26    N N   . VAL A 7   ? 0.6079 1.2773 1.3739 -0.1688 0.0623  -0.0778 7   VAL A N   
27    C CA  . VAL A 7   ? 0.5887 1.2719 1.3457 -0.1589 0.0564  -0.0781 7   VAL A CA  
28    C C   . VAL A 7   ? 0.5869 1.2533 1.3199 -0.1521 0.0597  -0.0698 7   VAL A C   
29    O O   . VAL A 7   ? 0.6003 1.2490 1.3256 -0.1549 0.0681  -0.0624 7   VAL A O   
30    C CB  . VAL A 7   ? 0.5464 1.2540 1.3169 -0.1580 0.0582  -0.0773 7   VAL A CB  
31    C CG1 . VAL A 7   ? 0.5583 1.2609 1.3240 -0.1578 0.0697  -0.0671 7   VAL A CG1 
32    C CG2 . VAL A 7   ? 0.5674 1.2920 1.3331 -0.1491 0.0493  -0.0806 7   VAL A CG2 
33    N N   . ALA A 8   ? 0.5597 1.2317 1.2808 -0.1433 0.0528  -0.0711 8   ALA A N   
34    C CA  . ALA A 8   ? 0.5191 1.1767 1.2180 -0.1363 0.0543  -0.0644 8   ALA A CA  
35    C C   . ALA A 8   ? 0.5204 1.1937 1.2137 -0.1282 0.0527  -0.0617 8   ALA A C   
36    O O   . ALA A 8   ? 0.5684 1.2604 1.2685 -0.1252 0.0454  -0.0675 8   ALA A O   
37    C CB  . ALA A 8   ? 0.6115 1.2555 1.2991 -0.1334 0.0471  -0.0688 8   ALA A CB  
38    N N   . VAL A 9   ? 0.5453 1.2105 1.2259 -0.1248 0.0592  -0.0528 9   VAL A N   
39    C CA  . VAL A 9   ? 0.5628 1.2398 1.2366 -0.1170 0.0585  -0.0492 9   VAL A CA  
40    C C   . VAL A 9   ? 0.6597 1.3197 1.3113 -0.1110 0.0590  -0.0436 9   VAL A C   
41    O O   . VAL A 9   ? 0.6628 1.3042 1.3052 -0.1131 0.0656  -0.0376 9   VAL A O   
42    C CB  . VAL A 9   ? 0.5292 1.2165 1.2121 -0.1187 0.0665  -0.0442 9   VAL A CB  
43    C CG1 . VAL A 9   ? 0.5441 1.2415 1.2189 -0.1103 0.0655  -0.0403 9   VAL A CG1 
44    C CG2 . VAL A 9   ? 0.6009 1.3065 1.3074 -0.1246 0.0655  -0.0501 9   VAL A CG2 
45    N N   . ILE A 10  ? 0.7144 1.3805 1.3573 -0.1036 0.0519  -0.0454 10  ILE A N   
46    C CA  . ILE A 10  ? 0.7115 1.3636 1.3346 -0.0974 0.0511  -0.0410 10  ILE A CA  
47    C C   . ILE A 10  ? 0.6895 1.3513 1.3065 -0.0911 0.0526  -0.0358 10  ILE A C   
48    O O   . ILE A 10  ? 0.6680 1.3493 1.2926 -0.0883 0.0486  -0.0385 10  ILE A O   
49    C CB  . ILE A 10  ? 0.7345 1.3846 1.3519 -0.0940 0.0422  -0.0472 10  ILE A CB  
50    C CG1 . ILE A 10  ? 0.7719 1.4123 1.3964 -0.1001 0.0404  -0.0531 10  ILE A CG1 
51    C CG2 . ILE A 10  ? 0.7282 1.3646 1.3264 -0.0875 0.0413  -0.0427 10  ILE A CG2 
52    C CD1 . ILE A 10  ? 0.7300 1.3682 1.3498 -0.0967 0.0319  -0.0600 10  ILE A CD1 
53    N N   . MET A 11  ? 0.6471 1.2949 1.2501 -0.0887 0.0580  -0.0283 11  MET A N   
54    C CA  . MET A 11  ? 0.6445 1.2985 1.2395 -0.0823 0.0589  -0.0234 11  MET A CA  
55    C C   . MET A 11  ? 0.6644 1.3192 1.2487 -0.0755 0.0512  -0.0253 11  MET A C   
56    O O   . MET A 11  ? 0.6387 1.2813 1.2154 -0.0750 0.0476  -0.0274 11  MET A O   
57    C CB  . MET A 11  ? 0.6926 1.3308 1.2759 -0.0822 0.0672  -0.0153 11  MET A CB  
58    C CG  . MET A 11  ? 0.6616 1.3022 1.2552 -0.0879 0.0762  -0.0126 11  MET A CG  
59    S SD  . MET A 11  ? 0.4633 1.1295 1.0716 -0.0856 0.0773  -0.0130 11  MET A SD  
60    C CE  . MET A 11  ? 0.7003 1.3652 1.3203 -0.0932 0.0887  -0.0102 11  MET A CE  
61    N N   . VAL A 12  ? 0.7163 1.3859 1.3006 -0.0702 0.0487  -0.0244 12  VAL A N   
62    C CA  . VAL A 12  ? 0.6998 1.3735 1.2756 -0.0640 0.0417  -0.0261 12  VAL A CA  
63    C C   . VAL A 12  ? 0.8254 1.4956 1.3887 -0.0581 0.0437  -0.0194 12  VAL A C   
64    O O   . VAL A 12  ? 0.8567 1.5177 1.4073 -0.0541 0.0410  -0.0182 12  VAL A O   
65    C CB  . VAL A 12  ? 0.6222 1.3174 1.2090 -0.0629 0.0353  -0.0320 12  VAL A CB  
66    C CG1 . VAL A 12  ? 0.6777 1.3788 1.2551 -0.0561 0.0296  -0.0322 12  VAL A CG1 
67    C CG2 . VAL A 12  ? 0.5586 1.2550 1.1547 -0.0678 0.0314  -0.0399 12  VAL A CG2 
68    N N   . GLY A 13  ? 1.1996 1.8771 1.7669 -0.0576 0.0485  -0.0152 13  GLY A N   
69    C CA  . GLY A 13  ? 1.1921 1.8681 1.7491 -0.0521 0.0502  -0.0094 13  GLY A CA  
70    C C   . GLY A 13  ? 1.1676 1.8599 1.7260 -0.0469 0.0441  -0.0107 13  GLY A C   
71    O O   . GLY A 13  ? 1.1546 1.8581 1.7193 -0.0470 0.0380  -0.0162 13  GLY A O   
72    N N   . GLY A 14  ? 0.7997 1.4931 1.3517 -0.0422 0.0458  -0.0055 14  GLY A N   
73    C CA  . GLY A 14  ? 0.7039 1.4117 1.2566 -0.0373 0.0408  -0.0055 14  GLY A CA  
74    C C   . GLY A 14  ? 0.7042 1.4048 1.2426 -0.0323 0.0378  -0.0031 14  GLY A C   
75    O O   . GLY A 14  ? 0.6418 1.3266 1.1700 -0.0325 0.0384  -0.0024 14  GLY A O   
76    N N   . PRO A 15  ? 0.5204 1.2326 1.0582 -0.0278 0.0344  -0.0016 15  PRO A N   
77    C CA  . PRO A 15  ? 0.6342 1.3413 1.1598 -0.0232 0.0314  0.0005  15  PRO A CA  
78    C C   . PRO A 15  ? 0.6180 1.3103 1.1329 -0.0214 0.0360  0.0062  15  PRO A C   
79    O O   . PRO A 15  ? 0.6397 1.3262 1.1445 -0.0180 0.0337  0.0080  15  PRO A O   
80    C CB  . PRO A 15  ? 0.6022 1.3265 1.1316 -0.0196 0.0275  0.0012  15  PRO A CB  
81    C CG  . PRO A 15  ? 0.4496 1.1839 0.9908 -0.0210 0.0304  0.0021  15  PRO A CG  
82    C CD  . PRO A 15  ? 0.5395 1.2701 1.0882 -0.0267 0.0329  -0.0017 15  PRO A CD  
83    N N   . THR A 16  ? 0.5426 1.2291 1.0595 -0.0235 0.0423  0.0090  16  THR A N   
84    C CA  . THR A 16  ? 0.5612 1.2327 1.0671 -0.0220 0.0470  0.0140  16  THR A CA  
85    C C   . THR A 16  ? 0.6357 1.2891 1.1335 -0.0249 0.0490  0.0137  16  THR A C   
86    O O   . THR A 16  ? 0.6223 1.2617 1.1086 -0.0236 0.0518  0.0175  16  THR A O   
87    C CB  . THR A 16  ? 0.5732 1.2479 1.0846 -0.0224 0.0533  0.0173  16  THR A CB  
88    O OG1 . THR A 16  ? 0.6095 1.2870 1.1315 -0.0275 0.0569  0.0148  16  THR A OG1 
89    C CG2 . THR A 16  ? 0.5422 1.2332 1.0606 -0.0187 0.0509  0.0184  16  THR A CG2 
90    N N   . LYS A 17  ? 0.6420 1.2951 1.1453 -0.0289 0.0476  0.0093  17  LYS A N   
91    C CA  . LYS A 17  ? 0.7631 1.3987 1.2589 -0.0316 0.0486  0.0089  17  LYS A CA  
92    C C   . LYS A 17  ? 0.8141 1.4450 1.3029 -0.0291 0.0421  0.0063  17  LYS A C   
93    O O   . LYS A 17  ? 0.8204 1.4353 1.2978 -0.0281 0.0420  0.0083  17  LYS A O   
94    C CB  . LYS A 17  ? 0.7796 1.4159 1.2857 -0.0376 0.0509  0.0055  17  LYS A CB  
95    C CG  . LYS A 17  ? 0.7427 1.3880 1.2594 -0.0402 0.0568  0.0069  17  LYS A CG  
96    C CD  . LYS A 17  ? 0.7473 1.3814 1.2554 -0.0396 0.0640  0.0129  17  LYS A CD  
97    C CE  . LYS A 17  ? 0.7098 1.3543 1.2298 -0.0418 0.0702  0.0139  17  LYS A CE  
98    N NZ  . LYS A 17  ? 0.6805 1.3278 1.2127 -0.0482 0.0726  0.0106  17  LYS A NZ  
99    N N   . GLY A 18  ? 0.8640 1.5087 1.3595 -0.0279 0.0365  0.0017  18  GLY A N   
100   C CA  . GLY A 18  ? 0.8486 1.4913 1.3385 -0.0251 0.0306  -0.0012 18  GLY A CA  
101   C C   . GLY A 18  ? 0.8508 1.4942 1.3325 -0.0200 0.0289  0.0025  18  GLY A C   
102   O O   . GLY A 18  ? 0.8724 1.5213 1.3525 -0.0171 0.0240  0.0001  18  GLY A O   
103   N N   . THR A 19  ? 0.7584 1.3964 1.2350 -0.0189 0.0332  0.0080  19  THR A N   
104   C CA  . THR A 19  ? 0.7605 1.3972 1.2290 -0.0144 0.0320  0.0118  19  THR A CA  
105   C C   . THR A 19  ? 0.7252 1.3455 1.1819 -0.0128 0.0303  0.0128  19  THR A C   
106   O O   . THR A 19  ? 0.7333 1.3505 1.1828 -0.0093 0.0294  0.0159  19  THR A O   
107   C CB  . THR A 19  ? 0.7025 1.3396 1.1702 -0.0136 0.0371  0.0168  19  THR A CB  
108   O OG1 . THR A 19  ? 0.6323 1.2696 1.0936 -0.0093 0.0354  0.0200  19  THR A OG1 
109   C CG2 . THR A 19  ? 0.8060 1.4268 1.2674 -0.0160 0.0427  0.0195  19  THR A CG2 
110   N N   . ARG A 20  ? 0.7188 1.3281 1.1736 -0.0152 0.0298  0.0105  20  ARG A N   
111   C CA  . ARG A 20  ? 0.7259 1.3207 1.1708 -0.0133 0.0268  0.0107  20  ARG A CA  
112   C C   . ARG A 20  ? 0.7498 1.3497 1.1980 -0.0119 0.0209  0.0053  20  ARG A C   
113   O O   . ARG A 20  ? 0.8047 1.3976 1.2464 -0.0090 0.0173  0.0052  20  ARG A O   
114   C CB  . ARG A 20  ? 0.7957 1.3725 1.2348 -0.0164 0.0300  0.0123  20  ARG A CB  
115   C CG  . ARG A 20  ? 0.9533 1.5310 1.3972 -0.0206 0.0365  0.0140  20  ARG A CG  
116   C CD  . ARG A 20  ? 1.1112 1.6712 1.5439 -0.0217 0.0415  0.0190  20  ARG A CD  
117   N NE  . ARG A 20  ? 1.1231 1.6658 1.5458 -0.0211 0.0384  0.0193  20  ARG A NE  
118   C CZ  . ARG A 20  ? 1.1024 1.6274 1.5132 -0.0220 0.0415  0.0235  20  ARG A CZ  
119   N NH1 . ARG A 20  ? 1.1775 1.6998 1.5850 -0.0236 0.0483  0.0275  20  ARG A NH1 
120   N NH2 . ARG A 20  ? 1.0402 1.5501 1.4424 -0.0210 0.0377  0.0236  20  ARG A NH2 
121   N N   . PHE A 21  ? 0.7721 1.3841 1.2304 -0.0139 0.0197  0.0004  21  PHE A N   
122   C CA  . PHE A 21  ? 0.8140 1.4330 1.2763 -0.0126 0.0144  -0.0055 21  PHE A CA  
123   C C   . PHE A 21  ? 0.9288 1.5647 1.3937 -0.0095 0.0119  -0.0062 21  PHE A C   
124   O O   . PHE A 21  ? 1.0078 1.6544 1.4780 -0.0092 0.0086  -0.0115 21  PHE A O   
125   C CB  . PHE A 21  ? 0.7122 1.3350 1.1835 -0.0166 0.0142  -0.0109 21  PHE A CB  
126   C CG  . PHE A 21  ? 0.6772 1.2827 1.1463 -0.0199 0.0161  -0.0109 21  PHE A CG  
127   C CD1 . PHE A 21  ? 0.6797 1.2788 1.1500 -0.0203 0.0125  -0.0161 21  PHE A CD1 
128   C CD2 . PHE A 21  ? 0.7142 1.3097 1.1799 -0.0226 0.0215  -0.0058 21  PHE A CD2 
129   C CE1 . PHE A 21  ? 0.6371 1.2195 1.1051 -0.0234 0.0139  -0.0157 21  PHE A CE1 
130   C CE2 . PHE A 21  ? 0.7084 1.2877 1.1714 -0.0258 0.0234  -0.0053 21  PHE A CE2 
131   C CZ  . PHE A 21  ? 0.6572 1.2296 1.1213 -0.0263 0.0195  -0.0100 21  PHE A CZ  
132   N N   . ARG A 22  ? 0.9084 1.5464 1.3693 -0.0073 0.0136  -0.0008 22  ARG A N   
133   C CA  . ARG A 22  ? 0.9782 1.6316 1.4415 -0.0048 0.0122  0.0002  22  ARG A CA  
134   C C   . ARG A 22  ? 1.1509 1.8140 1.6160 -0.0028 0.0076  -0.0045 22  ARG A C   
135   O O   . ARG A 22  ? 1.0701 1.7485 1.5410 -0.0030 0.0064  -0.0069 22  ARG A O   
136   C CB  . ARG A 22  ? 0.8683 1.5167 1.3244 -0.0022 0.0138  0.0064  22  ARG A CB  
137   C CG  . ARG A 22  ? 0.8290 1.4704 1.2835 -0.0037 0.0188  0.0109  22  ARG A CG  
138   C CD  . ARG A 22  ? 0.8475 1.5022 1.3112 -0.0055 0.0210  0.0108  22  ARG A CD  
139   N NE  . ARG A 22  ? 0.8006 1.4679 1.2663 -0.0029 0.0202  0.0134  22  ARG A NE  
140   C CZ  . ARG A 22  ? 0.7805 1.4480 1.2457 -0.0019 0.0235  0.0182  22  ARG A CZ  
141   N NH1 . ARG A 22  ? 0.7912 1.4476 1.2538 -0.0033 0.0282  0.0206  22  ARG A NH1 
142   N NH2 . ARG A 22  ? 0.7800 1.4586 1.2473 0.0006  0.0223  0.0206  22  ARG A NH2 
143   N N   . PRO A 23  ? 1.6675 2.3229 2.1278 -0.0007 0.0050  -0.0061 23  PRO A N   
144   C CA  . PRO A 23  ? 1.6492 2.3151 2.1117 0.0013  0.0012  -0.0108 23  PRO A CA  
145   C C   . PRO A 23  ? 1.6431 2.3182 2.1127 -0.0007 -0.0003 -0.0174 23  PRO A C   
146   O O   . PRO A 23  ? 1.6250 2.3149 2.0975 0.0003  -0.0021 -0.0203 23  PRO A O   
147   C CB  . PRO A 23  ? 1.6575 2.3109 2.1151 0.0034  -0.0011 -0.0119 23  PRO A CB  
148   C CG  . PRO A 23  ? 1.6839 2.3199 2.1373 0.0017  0.0009  -0.0093 23  PRO A CG  
149   C CD  . PRO A 23  ? 1.6843 2.3215 2.1373 -0.0001 0.0050  -0.0040 23  PRO A CD  
150   N N   . LEU A 24  ? 1.1613 1.8276 1.6333 -0.0036 0.0004  -0.0201 24  LEU A N   
151   C CA  . LEU A 24  ? 0.9409 1.6148 1.4201 -0.0061 -0.0010 -0.0267 24  LEU A CA  
152   C C   . LEU A 24  ? 0.7977 1.4811 1.2829 -0.0090 0.0012  -0.0253 24  LEU A C   
153   O O   . LEU A 24  ? 0.7533 1.4496 1.2445 -0.0101 -0.0008 -0.0302 24  LEU A O   
154   C CB  . LEU A 24  ? 0.8867 1.5462 1.3666 -0.0082 -0.0016 -0.0304 24  LEU A CB  
155   C CG  . LEU A 24  ? 0.8704 1.5152 1.3439 -0.0056 -0.0032 -0.0299 24  LEU A CG  
156   C CD1 . LEU A 24  ? 0.7683 1.3958 1.2413 -0.0082 -0.0025 -0.0307 24  LEU A CD1 
157   C CD2 . LEU A 24  ? 0.7813 1.4334 1.2561 -0.0024 -0.0071 -0.0359 24  LEU A CD2 
158   N N   . SER A 25  ? 0.8361 1.5136 1.3197 -0.0101 0.0050  -0.0191 25  SER A N   
159   C CA  . SER A 25  ? 0.7286 1.4152 1.2190 -0.0126 0.0073  -0.0178 25  SER A CA  
160   C C   . SER A 25  ? 0.7248 1.4295 1.2177 -0.0105 0.0055  -0.0172 25  SER A C   
161   O O   . SER A 25  ? 0.6564 1.3727 1.1567 -0.0123 0.0053  -0.0187 25  SER A O   
162   C CB  . SER A 25  ? 0.7298 1.4063 1.2174 -0.0136 0.0123  -0.0112 25  SER A CB  
163   O OG  . SER A 25  ? 0.7215 1.3864 1.2109 -0.0174 0.0148  -0.0123 25  SER A OG  
164   N N   . PHE A 26  ? 0.7357 1.4430 1.2226 -0.0068 0.0040  -0.0149 26  PHE A N   
165   C CA  . PHE A 26  ? 0.7087 1.4324 1.1969 -0.0048 0.0023  -0.0138 26  PHE A CA  
166   C C   . PHE A 26  ? 0.5991 1.3355 1.0917 -0.0055 -0.0014 -0.0209 26  PHE A C   
167   O O   . PHE A 26  ? 0.5320 1.2829 1.0281 -0.0053 -0.0028 -0.0208 26  PHE A O   
168   C CB  . PHE A 26  ? 0.7460 1.4685 1.2270 -0.0011 0.0018  -0.0100 26  PHE A CB  
169   C CG  . PHE A 26  ? 0.7583 1.4718 1.2352 -0.0001 0.0050  -0.0027 26  PHE A CG  
170   C CD1 . PHE A 26  ? 0.8330 1.5373 1.3030 0.0022  0.0050  0.0000  26  PHE A CD1 
171   C CD2 . PHE A 26  ? 0.7843 1.4985 1.2647 -0.0013 0.0080  0.0009  26  PHE A CD2 
172   C CE1 . PHE A 26  ? 0.8003 1.4959 1.2660 0.0031  0.0077  0.0062  26  PHE A CE1 
173   C CE2 . PHE A 26  ? 0.8071 1.5128 1.2834 -0.0002 0.0111  0.0070  26  PHE A CE2 
174   C CZ  . PHE A 26  ? 0.7609 1.4569 1.2294 0.0020  0.0109  0.0096  26  PHE A CZ  
175   N N   . ASN A 27  ? 0.5811 1.3123 1.0736 -0.0062 -0.0032 -0.0271 27  ASN A N   
176   C CA  . ASN A 27  ? 0.4953 1.2374 0.9918 -0.0071 -0.0067 -0.0348 27  ASN A CA  
177   C C   . ASN A 27  ? 0.5057 1.2467 1.0102 -0.0113 -0.0066 -0.0390 27  ASN A C   
178   O O   . ASN A 27  ? 0.5156 1.2697 1.0255 -0.0127 -0.0087 -0.0422 27  ASN A O   
179   C CB  . ASN A 27  ? 0.4629 1.2008 0.9558 -0.0053 -0.0087 -0.0401 27  ASN A CB  
180   C CG  . ASN A 27  ? 0.4561 1.2055 0.9521 -0.0057 -0.0122 -0.0486 27  ASN A CG  
181   O OD1 . ASN A 27  ? 0.4729 1.2364 0.9672 -0.0040 -0.0138 -0.0492 27  ASN A OD1 
182   N ND2 . ASN A 27  ? 0.4486 1.1918 0.9490 -0.0082 -0.0133 -0.0551 27  ASN A ND2 
183   N N   . THR A 28  ? 0.5113 1.2368 1.0164 -0.0136 -0.0045 -0.0388 28  THR A N   
184   C CA  . THR A 28  ? 0.4830 1.2057 0.9959 -0.0181 -0.0040 -0.0427 28  THR A CA  
185   C C   . THR A 28  ? 0.5274 1.2372 1.0405 -0.0205 0.0008  -0.0369 28  THR A C   
186   O O   . THR A 28  ? 0.5533 1.2487 1.0593 -0.0191 0.0027  -0.0331 28  THR A O   
187   C CB  . THR A 28  ? 0.4776 1.1932 0.9912 -0.0191 -0.0066 -0.0505 28  THR A CB  
188   O OG1 . THR A 28  ? 0.4473 1.1769 0.9620 -0.0177 -0.0108 -0.0571 28  THR A OG1 
189   C CG2 . THR A 28  ? 0.4406 1.1488 0.9615 -0.0242 -0.0054 -0.0534 28  THR A CG2 
190   N N   . PRO A 29  ? 0.5377 1.2523 1.0588 -0.0239 0.0029  -0.0361 29  PRO A N   
191   C CA  . PRO A 29  ? 0.5287 1.2316 1.0501 -0.0263 0.0082  -0.0307 29  PRO A CA  
192   C C   . PRO A 29  ? 0.5319 1.2164 1.0506 -0.0288 0.0096  -0.0321 29  PRO A C   
193   O O   . PRO A 29  ? 0.5237 1.2052 1.0431 -0.0294 0.0063  -0.0382 29  PRO A O   
194   C CB  . PRO A 29  ? 0.5605 1.2748 1.0936 -0.0300 0.0093  -0.0319 29  PRO A CB  
195   C CG  . PRO A 29  ? 0.5856 1.3187 1.1217 -0.0278 0.0046  -0.0349 29  PRO A CG  
196   C CD  . PRO A 29  ? 0.5815 1.3135 1.1115 -0.0254 0.0004  -0.0398 29  PRO A CD  
197   N N   . LYS A 30  ? 0.5086 1.1803 1.0237 -0.0301 0.0147  -0.0263 30  LYS A N   
198   C CA  . LYS A 30  ? 0.4294 1.0816 0.9399 -0.0322 0.0165  -0.0259 30  LYS A CA  
199   C C   . LYS A 30  ? 0.4345 1.0841 0.9531 -0.0369 0.0153  -0.0322 30  LYS A C   
200   O O   . LYS A 30  ? 0.4348 1.0736 0.9500 -0.0366 0.0127  -0.0355 30  LYS A O   
201   C CB  . LYS A 30  ? 0.4837 1.1252 0.9901 -0.0337 0.0228  -0.0186 30  LYS A CB  
202   C CG  . LYS A 30  ? 0.5107 1.1311 1.0106 -0.0359 0.0252  -0.0169 30  LYS A CG  
203   C CD  . LYS A 30  ? 0.5439 1.1578 1.0456 -0.0402 0.0321  -0.0125 30  LYS A CD  
204   C CE  . LYS A 30  ? 0.5994 1.1935 1.0880 -0.0395 0.0356  -0.0064 30  LYS A CE  
205   N NZ  . LYS A 30  ? 0.7221 1.3179 1.2023 -0.0348 0.0363  -0.0014 30  LYS A NZ  
206   N N   . PRO A 31  ? 0.5141 1.1728 1.0440 -0.0413 0.0168  -0.0344 31  PRO A N   
207   C CA  . PRO A 31  ? 0.4988 1.1529 1.0365 -0.0464 0.0159  -0.0402 31  PRO A CA  
208   C C   . PRO A 31  ? 0.5105 1.1705 1.0504 -0.0450 0.0094  -0.0486 31  PRO A C   
209   O O   . PRO A 31  ? 0.5351 1.1872 1.0789 -0.0483 0.0080  -0.0537 31  PRO A O   
210   C CB  . PRO A 31  ? 0.5254 1.1914 1.0756 -0.0509 0.0187  -0.0406 31  PRO A CB  
211   C CG  . PRO A 31  ? 0.5000 1.1709 1.0472 -0.0485 0.0226  -0.0334 31  PRO A CG  
212   C CD  . PRO A 31  ? 0.5403 1.2133 1.0772 -0.0421 0.0193  -0.0317 31  PRO A CD  
213   N N   . LEU A 32  ? 0.4575 1.1310 0.9949 -0.0405 0.0056  -0.0502 32  LEU A N   
214   C CA  . LEU A 32  ? 0.4807 1.1621 1.0201 -0.0391 -0.0001 -0.0586 32  LEU A CA  
215   C C   . LEU A 32  ? 0.4286 1.1016 0.9585 -0.0344 -0.0025 -0.0595 32  LEU A C   
216   O O   . LEU A 32  ? 0.4363 1.1160 0.9667 -0.0324 -0.0069 -0.0663 32  LEU A O   
217   C CB  . LEU A 32  ? 0.5119 1.2150 1.0552 -0.0374 -0.0028 -0.0603 32  LEU A CB  
218   C CG  . LEU A 32  ? 0.4700 1.1831 1.0224 -0.0407 -0.0004 -0.0577 32  LEU A CG  
219   C CD1 . LEU A 32  ? 0.5244 1.2582 1.0790 -0.0381 -0.0038 -0.0587 32  LEU A CD1 
220   C CD2 . LEU A 32  ? 0.5153 1.2259 1.0787 -0.0470 0.0000  -0.0627 32  LEU A CD2 
221   N N   . ILE A 33  ? 0.4645 1.1233 0.9859 -0.0325 0.0002  -0.0530 33  ILE A N   
222   C CA  . ILE A 33  ? 0.4773 1.1280 0.9904 -0.0279 -0.0023 -0.0536 33  ILE A CA  
223   C C   . ILE A 33  ? 0.4973 1.1347 1.0121 -0.0295 -0.0044 -0.0593 33  ILE A C   
224   O O   . ILE A 33  ? 0.5996 1.2233 1.1156 -0.0335 -0.0018 -0.0573 33  ILE A O   
225   C CB  . ILE A 33  ? 0.4312 1.0709 0.9348 -0.0255 0.0007  -0.0450 33  ILE A CB  
226   C CG1 . ILE A 33  ? 0.4206 1.0735 0.9226 -0.0234 0.0023  -0.0398 33  ILE A CG1 
227   C CG2 . ILE A 33  ? 0.4575 1.0875 0.9538 -0.0212 -0.0022 -0.0458 33  ILE A CG2 
228   C CD1 . ILE A 33  ? 0.4724 1.1152 0.9652 -0.0211 0.0053  -0.0317 33  ILE A CD1 
229   N N   . PRO A 34  ? 0.4465 1.0872 0.9615 -0.0266 -0.0089 -0.0663 34  PRO A N   
230   C CA  . PRO A 34  ? 0.5622 1.1916 1.0804 -0.0281 -0.0113 -0.0729 34  PRO A CA  
231   C C   . PRO A 34  ? 0.6275 1.2352 1.1392 -0.0270 -0.0105 -0.0687 34  PRO A C   
232   O O   . PRO A 34  ? 0.6268 1.2304 1.1314 -0.0222 -0.0118 -0.0663 34  PRO A O   
233   C CB  . PRO A 34  ? 0.5576 1.1982 1.0766 -0.0240 -0.0159 -0.0810 34  PRO A CB  
234   C CG  . PRO A 34  ? 0.5400 1.2003 1.0582 -0.0223 -0.0156 -0.0792 34  PRO A CG  
235   C CD  . PRO A 34  ? 0.5046 1.1610 1.0176 -0.0221 -0.0116 -0.0689 34  PRO A CD  
236   N N   . LEU A 35  ? 0.8271 1.4208 1.3413 -0.0318 -0.0085 -0.0676 35  LEU A N   
237   C CA  . LEU A 35  ? 0.8567 1.4282 1.3649 -0.0313 -0.0083 -0.0642 35  LEU A CA  
238   C C   . LEU A 35  ? 0.8783 1.4417 1.3917 -0.0321 -0.0121 -0.0724 35  LEU A C   
239   O O   . LEU A 35  ? 0.8877 1.4529 1.4097 -0.0370 -0.0119 -0.0771 35  LEU A O   
240   C CB  . LEU A 35  ? 0.8768 1.4365 1.3827 -0.0361 -0.0029 -0.0565 35  LEU A CB  
241   C CG  . LEU A 35  ? 0.8596 1.4231 1.3586 -0.0348 0.0010  -0.0479 35  LEU A CG  
242   C CD1 . LEU A 35  ? 0.9282 1.4779 1.4239 -0.0393 0.0067  -0.0407 35  LEU A CD1 
243   C CD2 . LEU A 35  ? 0.8553 1.4153 1.3446 -0.0284 -0.0015 -0.0452 35  LEU A CD2 
244   N N   . ALA A 36  ? 0.7346 1.2888 1.2435 -0.0271 -0.0157 -0.0742 36  ALA A N   
245   C CA  . ALA A 36  ? 0.7026 1.2490 1.2163 -0.0266 -0.0198 -0.0825 36  ALA A CA  
246   C C   . ALA A 36  ? 0.6861 1.2503 1.2088 -0.0272 -0.0222 -0.0926 36  ALA A C   
247   O O   . ALA A 36  ? 0.7284 1.2881 1.2580 -0.0299 -0.0242 -0.0998 36  ALA A O   
248   C CB  . ALA A 36  ? 0.7701 1.2964 1.2853 -0.0316 -0.0185 -0.0807 36  ALA A CB  
249   N N   . GLY A 37  ? 0.6489 1.2327 1.1709 -0.0248 -0.0221 -0.0931 37  GLY A N   
250   C CA  . GLY A 37  ? 0.6594 1.2615 1.1878 -0.0250 -0.0245 -0.1019 37  GLY A CA  
251   C C   . GLY A 37  ? 0.6648 1.2793 1.1990 -0.0303 -0.0223 -0.1015 37  GLY A C   
252   O O   . GLY A 37  ? 0.6595 1.2928 1.1961 -0.0296 -0.0238 -0.1057 37  GLY A O   
253   N N   . GLN A 38  ? 0.6668 1.2715 1.2033 -0.0356 -0.0190 -0.0963 38  GLN A N   
254   C CA  . GLN A 38  ? 0.6276 1.2437 1.1713 -0.0409 -0.0169 -0.0960 38  GLN A CA  
255   C C   . GLN A 38  ? 0.5767 1.1949 1.1161 -0.0415 -0.0121 -0.0856 38  GLN A C   
256   O O   . GLN A 38  ? 0.6210 1.2256 1.1526 -0.0399 -0.0096 -0.0783 38  GLN A O   
257   C CB  . GLN A 38  ? 0.5970 1.2021 1.1490 -0.0475 -0.0163 -0.0992 38  GLN A CB  
258   C CG  . GLN A 38  ? 0.5870 1.1864 1.1432 -0.0471 -0.0210 -0.1094 38  GLN A CG  
259   C CD  . GLN A 38  ? 0.5756 1.1945 1.1358 -0.0452 -0.0252 -0.1191 38  GLN A CD  
260   O OE1 . GLN A 38  ? 0.5513 1.1880 1.1141 -0.0463 -0.0249 -0.1188 38  GLN A OE1 
261   N NE2 . GLN A 38  ? 0.6688 1.2843 1.2293 -0.0421 -0.0293 -0.1276 38  GLN A NE2 
262   N N   . PRO A 39  ? 0.7023 1.3374 1.2467 -0.0435 -0.0109 -0.0849 39  PRO A N   
263   C CA  . PRO A 39  ? 0.5290 1.1668 1.0701 -0.0437 -0.0062 -0.0754 39  PRO A CA  
264   C C   . PRO A 39  ? 0.5914 1.2115 1.1313 -0.0477 -0.0012 -0.0689 39  PRO A C   
265   O O   . PRO A 39  ? 0.5370 1.1440 1.0804 -0.0515 -0.0011 -0.0715 39  PRO A O   
266   C CB  . PRO A 39  ? 0.5136 1.1714 1.0635 -0.0462 -0.0066 -0.0778 39  PRO A CB  
267   C CG  . PRO A 39  ? 0.5171 1.1862 1.0697 -0.0443 -0.0123 -0.0875 39  PRO A CG  
268   C CD  . PRO A 39  ? 0.5209 1.1743 1.0732 -0.0447 -0.0144 -0.0929 39  PRO A CD  
269   N N   . MET A 40  ? 0.4851 1.1046 1.0196 -0.0468 0.0031  -0.0603 40  MET A N   
270   C CA  . MET A 40  ? 0.5942 1.1967 1.1249 -0.0499 0.0084  -0.0532 40  MET A CA  
271   C C   . MET A 40  ? 0.6818 1.2827 1.2233 -0.0573 0.0114  -0.0549 40  MET A C   
272   O O   . MET A 40  ? 0.6945 1.2782 1.2354 -0.0608 0.0131  -0.0541 40  MET A O   
273   C CB  . MET A 40  ? 0.5549 1.1602 1.0789 -0.0477 0.0126  -0.0446 40  MET A CB  
274   C CG  . MET A 40  ? 0.5743 1.1627 1.0924 -0.0504 0.0186  -0.0370 40  MET A CG  
275   S SD  . MET A 40  ? 0.6063 1.1978 1.1155 -0.0467 0.0228  -0.0281 40  MET A SD  
276   C CE  . MET A 40  ? 0.6186 1.2092 1.1174 -0.0391 0.0171  -0.0286 40  MET A CE  
277   N N   . ILE A 41  ? 0.8643 1.4831 1.4160 -0.0597 0.0118  -0.0572 41  ILE A N   
278   C CA  . ILE A 41  ? 0.8635 1.4836 1.4275 -0.0670 0.0144  -0.0593 41  ILE A CA  
279   C C   . ILE A 41  ? 0.8682 1.4885 1.4406 -0.0699 0.0095  -0.0689 41  ILE A C   
280   O O   . ILE A 41  ? 0.8743 1.4950 1.4579 -0.0763 0.0111  -0.0716 41  ILE A O   
281   C CB  . ILE A 41  ? 0.8287 1.4684 1.4013 -0.0682 0.0164  -0.0580 41  ILE A CB  
282   C CG1 . ILE A 41  ? 0.7983 1.4575 1.3724 -0.0638 0.0104  -0.0631 41  ILE A CG1 
283   C CG2 . ILE A 41  ? 0.8259 1.4625 1.3918 -0.0668 0.0226  -0.0484 41  ILE A CG2 
284   C CD1 . ILE A 41  ? 0.7707 1.4493 1.3527 -0.0642 0.0113  -0.0616 41  ILE A CD1 
285   N N   . HIS A 42  ? 0.6837 1.3039 1.2516 -0.0654 0.0038  -0.0745 42  HIS A N   
286   C CA  . HIS A 42  ? 0.6032 1.2237 1.1788 -0.0676 -0.0011 -0.0845 42  HIS A CA  
287   C C   . HIS A 42  ? 0.6427 1.2417 1.2197 -0.0721 0.0004  -0.0849 42  HIS A C   
288   O O   . HIS A 42  ? 0.6651 1.2632 1.2509 -0.0757 -0.0026 -0.0928 42  HIS A O   
289   C CB  . HIS A 42  ? 0.5830 1.2085 1.1527 -0.0612 -0.0069 -0.0903 42  HIS A CB  
290   C CG  . HIS A 42  ? 0.5734 1.2054 1.1512 -0.0626 -0.0123 -0.1017 42  HIS A CG  
291   N ND1 . HIS A 42  ? 0.5673 1.2201 1.1516 -0.0629 -0.0155 -0.1075 42  HIS A ND1 
292   C CD2 . HIS A 42  ? 0.5850 1.2049 1.1650 -0.0637 -0.0152 -0.1085 42  HIS A CD2 
293   C CE1 . HIS A 42  ? 0.6374 1.2910 1.2272 -0.0642 -0.0201 -0.1178 42  HIS A CE1 
294   N NE2 . HIS A 42  ? 0.6288 1.2625 1.2165 -0.0648 -0.0200 -0.1187 42  HIS A NE2 
295   N N   . HIS A 43  ? 0.6723 1.2538 1.2405 -0.0719 0.0048  -0.0765 43  HIS A N   
296   C CA  . HIS A 43  ? 0.6902 1.2498 1.2582 -0.0761 0.0064  -0.0756 43  HIS A CA  
297   C C   . HIS A 43  ? 0.6701 1.2265 1.2463 -0.0842 0.0126  -0.0718 43  HIS A C   
298   O O   . HIS A 43  ? 0.6923 1.2390 1.2760 -0.0898 0.0126  -0.0753 43  HIS A O   
299   C CB  . HIS A 43  ? 0.7291 1.2701 1.2825 -0.0715 0.0072  -0.0688 43  HIS A CB  
300   C CG  . HIS A 43  ? 0.7748 1.3183 1.3215 -0.0638 0.0013  -0.0727 43  HIS A CG  
301   N ND1 . HIS A 43  ? 0.7315 1.2927 1.2756 -0.0587 -0.0004 -0.0731 43  HIS A ND1 
302   C CD2 . HIS A 43  ? 0.8698 1.4007 1.4128 -0.0605 -0.0031 -0.0765 43  HIS A CD2 
303   C CE1 . HIS A 43  ? 0.7337 1.2935 1.2727 -0.0528 -0.0052 -0.0770 43  HIS A CE1 
304   N NE2 . HIS A 43  ? 0.8144 1.3562 1.3530 -0.0535 -0.0070 -0.0793 43  HIS A NE2 
305   N N   . PRO A 44  ? 0.7063 1.2702 1.2819 -0.0851 0.0182  -0.0648 44  PRO A N   
306   C CA  . PRO A 44  ? 0.6523 1.2170 1.2384 -0.0931 0.0241  -0.0626 44  PRO A CA  
307   C C   . PRO A 44  ? 0.6308 1.2104 1.2339 -0.0978 0.0208  -0.0718 44  PRO A C   
308   O O   . PRO A 44  ? 0.6469 1.2197 1.2597 -0.1051 0.0230  -0.0736 44  PRO A O   
309   C CB  . PRO A 44  ? 0.6933 1.2678 1.2759 -0.0913 0.0295  -0.0550 44  PRO A CB  
310   C CG  . PRO A 44  ? 0.7378 1.3045 1.3040 -0.0840 0.0283  -0.0502 44  PRO A CG  
311   C CD  . PRO A 44  ? 0.7229 1.2911 1.2874 -0.0794 0.0202  -0.0577 44  PRO A CD  
312   N N   . ILE A 45  ? 0.6265 1.2263 1.2331 -0.0939 0.0156  -0.0775 45  ILE A N   
313   C CA  . ILE A 45  ? 0.6092 1.2239 1.2308 -0.0978 0.0114  -0.0868 45  ILE A CA  
314   C C   . ILE A 45  ? 0.6632 1.2657 1.2881 -0.1003 0.0071  -0.0946 45  ILE A C   
315   O O   . ILE A 45  ? 0.7065 1.3122 1.3449 -0.1066 0.0059  -0.1008 45  ILE A O   
316   C CB  . ILE A 45  ? 0.5975 1.2346 1.2190 -0.0922 0.0061  -0.0908 45  ILE A CB  
317   C CG1 . ILE A 45  ? 0.5763 1.2241 1.1948 -0.0896 0.0104  -0.0827 45  ILE A CG1 
318   C CG2 . ILE A 45  ? 0.7762 1.4295 1.4126 -0.0961 0.0013  -0.1005 45  ILE A CG2 
319   C CD1 . ILE A 45  ? 0.6514 1.3194 1.2681 -0.0838 0.0055  -0.0852 45  ILE A CD1 
320   N N   . SER A 46  ? 0.6021 1.1905 1.2153 -0.0953 0.0045  -0.0948 46  SER A N   
321   C CA  . SER A 46  ? 0.6298 1.2050 1.2457 -0.0969 0.0003  -0.1021 46  SER A CA  
322   C C   . SER A 46  ? 0.6415 1.1987 1.2631 -0.1048 0.0049  -0.0992 46  SER A C   
323   O O   . SER A 46  ? 0.6861 1.2368 1.3163 -0.1091 0.0020  -0.1065 46  SER A O   
324   C CB  . SER A 46  ? 0.6437 1.2071 1.2460 -0.0894 -0.0029 -0.1018 46  SER A CB  
325   O OG  . SER A 46  ? 0.6856 1.2655 1.2852 -0.0831 -0.0082 -0.1075 46  SER A OG  
326   N N   . ALA A 47  ? 0.6318 1.1804 1.2485 -0.1069 0.0122  -0.0887 47  ALA A N   
327   C CA  . ALA A 47  ? 0.7157 1.2472 1.3367 -0.1147 0.0177  -0.0847 47  ALA A CA  
328   C C   . ALA A 47  ? 0.8087 1.3531 1.4467 -0.1229 0.0209  -0.0869 47  ALA A C   
329   O O   . ALA A 47  ? 0.8888 1.4210 1.5339 -0.1306 0.0249  -0.0856 47  ALA A O   
330   C CB  . ALA A 47  ? 0.7632 1.2795 1.3704 -0.1135 0.0245  -0.0725 47  ALA A CB  
331   N N   . CYS A 48  ? 0.7377 1.3064 1.3828 -0.1215 0.0193  -0.0899 48  CYS A N   
332   C CA  . CYS A 48  ? 0.7457 1.3287 1.4081 -0.1287 0.0217  -0.0923 48  CYS A CA  
333   C C   . CYS A 48  ? 0.8183 1.4045 1.4949 -0.1337 0.0160  -0.1036 48  CYS A C   
334   O O   . CYS A 48  ? 0.8670 1.4575 1.5590 -0.1418 0.0185  -0.1055 48  CYS A O   
335   C CB  . CYS A 48  ? 0.7314 1.3391 1.3964 -0.1249 0.0212  -0.0917 48  CYS A CB  
336   S SG  . CYS A 48  ? 0.6409 1.2467 1.2922 -0.1202 0.0287  -0.0787 48  CYS A SG  
337   N N   . LYS A 49  ? 0.8466 1.4311 1.5189 -0.1292 0.0083  -0.1115 49  LYS A N   
338   C CA  . LYS A 49  ? 0.9739 1.5614 1.6591 -0.1336 0.0024  -0.1231 49  LYS A CA  
339   C C   . LYS A 49  ? 1.0047 1.5696 1.6949 -0.1408 0.0049  -0.1231 49  LYS A C   
340   O O   . LYS A 49  ? 1.0126 1.5799 1.7175 -0.1474 0.0024  -0.1310 49  LYS A O   
341   C CB  . LYS A 49  ? 1.0404 1.6328 1.7189 -0.1263 -0.0061 -0.1319 49  LYS A CB  
342   C CG  . LYS A 49  ? 1.1209 1.7213 1.8125 -0.1300 -0.0129 -0.1450 49  LYS A CG  
343   C CD  . LYS A 49  ? 1.1844 1.8044 1.8921 -0.1362 -0.0124 -0.1474 49  LYS A CD  
344   C CE  . LYS A 49  ? 1.1690 1.7933 1.8912 -0.1417 -0.0186 -0.1601 49  LYS A CE  
345   N NZ  . LYS A 49  ? 1.2233 1.8743 1.9555 -0.1423 -0.0231 -0.1662 49  LYS A NZ  
346   N N   . LYS A 50  ? 1.1986 1.7414 1.8769 -0.1399 0.0097  -0.1143 50  LYS A N   
347   C CA  . LYS A 50  ? 1.2382 1.7580 1.9200 -0.1466 0.0122  -0.1133 50  LYS A CA  
348   C C   . LYS A 50  ? 1.2405 1.7615 1.9360 -0.1569 0.0194  -0.1096 50  LYS A C   
349   O O   . LYS A 50  ? 1.2721 1.7764 1.9740 -0.1640 0.0213  -0.1100 50  LYS A O   
350   C CB  . LYS A 50  ? 1.2690 1.7649 1.9332 -0.1425 0.0151  -0.1043 50  LYS A CB  
351   C CG  . LYS A 50  ? 1.2810 1.7704 1.9384 -0.1447 0.0245  -0.0914 50  LYS A CG  
352   C CD  . LYS A 50  ? 1.3249 1.7866 1.9668 -0.1427 0.0267  -0.0835 50  LYS A CD  
353   C CE  . LYS A 50  ? 1.3222 1.7810 1.9500 -0.1398 0.0336  -0.0714 50  LYS A CE  
354   N NZ  . LYS A 50  ? 1.2856 1.7630 1.9067 -0.1313 0.0307  -0.0719 50  LYS A NZ  
355   N N   . ILE A 51  ? 1.0342 1.5744 1.7351 -0.1578 0.0233  -0.1062 51  ILE A N   
356   C CA  . ILE A 51  ? 0.9478 1.4931 1.6644 -0.1674 0.0299  -0.1038 51  ILE A CA  
357   C C   . ILE A 51  ? 0.8789 1.4443 1.6147 -0.1714 0.0239  -0.1155 51  ILE A C   
358   O O   . ILE A 51  ? 0.8215 1.4098 1.5603 -0.1672 0.0200  -0.1191 51  ILE A O   
359   C CB  . ILE A 51  ? 0.8913 1.4464 1.6043 -0.1662 0.0378  -0.0940 51  ILE A CB  
360   C CG1 . ILE A 51  ? 0.9467 1.4816 1.6394 -0.1620 0.0432  -0.0829 51  ILE A CG1 
361   C CG2 . ILE A 51  ? 0.8508 1.4121 1.5815 -0.1763 0.0449  -0.0922 51  ILE A CG2 
362   C CD1 . ILE A 51  ? 1.0033 1.5438 1.6799 -0.1511 0.0392  -0.0813 51  ILE A CD1 
363   N N   . SER A 52  ? 0.8405 1.3970 1.5891 -0.1795 0.0227  -0.1214 52  SER A N   
364   C CA  . SER A 52  ? 0.8220 1.3959 1.5887 -0.1835 0.0160  -0.1334 52  SER A CA  
365   C C   . SER A 52  ? 0.7987 1.3946 1.5816 -0.1886 0.0198  -0.1323 52  SER A C   
366   O O   . SER A 52  ? 0.7929 1.4103 1.5877 -0.1888 0.0134  -0.1411 52  SER A O   
367   C CB  . SER A 52  ? 0.8372 1.3944 1.6139 -0.1913 0.0140  -0.1399 52  SER A CB  
368   O OG  . SER A 52  ? 0.8887 1.4317 1.6715 -0.2002 0.0232  -0.1320 52  SER A OG  
369   N N   . ASN A 53  ? 0.7906 1.3819 1.5742 -0.1926 0.0300  -0.1218 53  ASN A N   
370   C CA  . ASN A 53  ? 0.7496 1.3612 1.5489 -0.1971 0.0347  -0.1199 53  ASN A CA  
371   C C   . ASN A 53  ? 0.7642 1.3915 1.5542 -0.1889 0.0364  -0.1139 53  ASN A C   
372   O O   . ASN A 53  ? 0.7422 1.3827 1.5419 -0.1917 0.0425  -0.1095 53  ASN A O   
373   C CB  . ASN A 53  ? 0.7353 1.3340 1.5424 -0.2069 0.0456  -0.1124 53  ASN A CB  
374   C CG  . ASN A 53  ? 0.7470 1.3191 1.5342 -0.2049 0.0523  -0.1018 53  ASN A CG  
375   O OD1 . ASN A 53  ? 0.7965 1.3514 1.5700 -0.2007 0.0476  -0.1031 53  ASN A OD1 
376   N ND2 . ASN A 53  ? 0.6698 1.2383 1.4551 -0.2079 0.0631  -0.0914 53  ASN A ND2 
377   N N   . LEU A 54  ? 0.7847 1.4109 1.5570 -0.1790 0.0313  -0.1138 54  LEU A N   
378   C CA  . LEU A 54  ? 0.7901 1.4310 1.5534 -0.1708 0.0318  -0.1090 54  LEU A CA  
379   C C   . LEU A 54  ? 0.7953 1.4610 1.5662 -0.1671 0.0224  -0.1182 54  LEU A C   
380   O O   . LEU A 54  ? 0.7805 1.4472 1.5541 -0.1670 0.0141  -0.1280 54  LEU A O   
381   C CB  . LEU A 54  ? 0.7835 1.4091 1.5229 -0.1623 0.0319  -0.1029 54  LEU A CB  
382   C CG  . LEU A 54  ? 0.7278 1.3610 1.4560 -0.1554 0.0362  -0.0941 54  LEU A CG  
383   C CD1 . LEU A 54  ? 0.6678 1.2776 1.3767 -0.1525 0.0418  -0.0846 54  LEU A CD1 
384   C CD2 . LEU A 54  ? 0.7393 1.3901 1.4621 -0.1467 0.0282  -0.0985 54  LEU A CD2 
385   N N   . ALA A 55  ? 0.9484 1.6337 1.7224 -0.1638 0.0237  -0.1149 55  ALA A N   
386   C CA  . ALA A 55  ? 0.9196 1.6294 1.7010 -0.1604 0.0151  -0.1225 55  ALA A CA  
387   C C   . ALA A 55  ? 0.9244 1.6439 1.6915 -0.1504 0.0138  -0.1175 55  ALA A C   
388   O O   . ALA A 55  ? 1.0735 1.7861 1.8241 -0.1436 0.0098  -0.1181 55  ALA A O   
389   C CB  . ALA A 55  ? 0.9495 1.6776 1.7541 -0.1673 0.0165  -0.1249 55  ALA A CB  
390   N N   . GLN A 56  ? 0.7836 1.5190 1.5574 -0.1494 0.0173  -0.1127 56  GLN A N   
391   C CA  . GLN A 56  ? 0.7133 1.4595 1.4754 -0.1402 0.0157  -0.1083 56  GLN A CA  
392   C C   . GLN A 56  ? 0.6741 1.4019 1.4161 -0.1353 0.0217  -0.0990 56  GLN A C   
393   O O   . GLN A 56  ? 0.6338 1.3443 1.3733 -0.1394 0.0296  -0.0932 56  GLN A O   
394   C CB  . GLN A 56  ? 0.6415 1.4080 1.4171 -0.1406 0.0184  -0.1053 56  GLN A CB  
395   N N   . ILE A 57  ? 0.7188 1.4505 1.4461 -0.1265 0.0176  -0.0975 57  ILE A N   
396   C CA  . ILE A 57  ? 0.6789 1.3965 1.3872 -0.1208 0.0221  -0.0890 57  ILE A CA  
397   C C   . ILE A 57  ? 0.6346 1.3677 1.3391 -0.1143 0.0223  -0.0840 57  ILE A C   
398   O O   . ILE A 57  ? 0.6911 1.4427 1.3998 -0.1110 0.0155  -0.0886 57  ILE A O   
399   C CB  . ILE A 57  ? 0.7139 1.4185 1.4068 -0.1163 0.0168  -0.0922 57  ILE A CB  
400   C CG1 . ILE A 57  ? 0.8240 1.5150 1.5226 -0.1226 0.0152  -0.0985 57  ILE A CG1 
401   C CG2 . ILE A 57  ? 0.6185 1.3076 1.2929 -0.1110 0.0215  -0.0833 57  ILE A CG2 
402   C CD1 . ILE A 57  ? 0.9169 1.5901 1.6003 -0.1186 0.0123  -0.0998 57  ILE A CD1 
403   N N   . PHE A 58  ? 0.5728 1.2977 1.2689 -0.1122 0.0300  -0.0747 58  PHE A N   
404   C CA  . PHE A 58  ? 0.5495 1.2875 1.2438 -0.1068 0.0316  -0.0692 58  PHE A CA  
405   C C   . PHE A 58  ? 0.4973 1.2226 1.1712 -0.1001 0.0337  -0.0623 58  PHE A C   
406   O O   . PHE A 58  ? 0.5525 1.2593 1.2178 -0.1016 0.0402  -0.0569 58  PHE A O   
407   C CB  . PHE A 58  ? 0.5565 1.2999 1.2639 -0.1113 0.0398  -0.0648 58  PHE A CB  
408   C CG  . PHE A 58  ? 0.5811 1.3416 1.3108 -0.1171 0.0372  -0.0713 58  PHE A CG  
409   C CD1 . PHE A 58  ? 0.6279 1.4112 1.3671 -0.1139 0.0322  -0.0736 58  PHE A CD1 
410   C CD2 . PHE A 58  ? 0.6128 1.3664 1.3542 -0.1258 0.0397  -0.0749 58  PHE A CD2 
411   C CE1 . PHE A 58  ? 0.7129 1.5125 1.4731 -0.1191 0.0293  -0.0798 58  PHE A CE1 
412   C CE2 . PHE A 58  ? 0.6260 1.3958 1.3888 -0.1314 0.0371  -0.0812 58  PHE A CE2 
413   C CZ  . PHE A 58  ? 0.6755 1.4685 1.4478 -0.1279 0.0318  -0.0838 58  PHE A CZ  
414   N N   . LEU A 59  ? 0.4947 1.2297 1.1606 -0.0929 0.0282  -0.0625 59  LEU A N   
415   C CA  . LEU A 59  ? 0.5400 1.2663 1.1882 -0.0863 0.0299  -0.0559 59  LEU A CA  
416   C C   . LEU A 59  ? 0.5013 1.2406 1.1517 -0.0826 0.0326  -0.0504 59  LEU A C   
417   O O   . LEU A 59  ? 0.5457 1.3037 1.2029 -0.0800 0.0274  -0.0531 59  LEU A O   
418   C CB  . LEU A 59  ? 0.5897 1.3165 1.2270 -0.0808 0.0221  -0.0599 59  LEU A CB  
419   C CG  . LEU A 59  ? 0.5485 1.2671 1.1859 -0.0836 0.0175  -0.0675 59  LEU A CG  
420   C CD1 . LEU A 59  ? 0.5375 1.2607 1.1651 -0.0775 0.0102  -0.0715 59  LEU A CD1 
421   C CD2 . LEU A 59  ? 0.5327 1.2277 1.1631 -0.0865 0.0224  -0.0644 59  LEU A CD2 
422   N N   . ILE A 60  ? 0.4934 1.2225 1.1378 -0.0821 0.0405  -0.0428 60  ILE A N   
423   C CA  . ILE A 60  ? 0.4967 1.2363 1.1436 -0.0788 0.0441  -0.0375 60  ILE A CA  
424   C C   . ILE A 60  ? 0.5479 1.2771 1.1767 -0.0725 0.0459  -0.0309 60  ILE A C   
425   O O   . ILE A 60  ? 0.5675 1.2781 1.1836 -0.0726 0.0482  -0.0285 60  ILE A O   
426   C CB  . ILE A 60  ? 0.4826 1.2225 1.1416 -0.0843 0.0527  -0.0348 60  ILE A CB  
427   C CG1 . ILE A 60  ? 0.5379 1.2553 1.1870 -0.0876 0.0604  -0.0303 60  ILE A CG1 
428   C CG2 . ILE A 60  ? 0.5502 1.3028 1.2291 -0.0905 0.0504  -0.0415 60  ILE A CG2 
429   C CD1 . ILE A 60  ? 0.6395 1.3566 1.2992 -0.0931 0.0698  -0.0273 60  ILE A CD1 
430   N N   . GLY A 61  ? 0.5469 1.2882 1.1749 -0.0670 0.0444  -0.0281 61  GLY A N   
431   C CA  . GLY A 61  ? 0.6152 1.3492 1.2278 -0.0608 0.0457  -0.0222 61  GLY A CA  
432   C C   . GLY A 61  ? 0.5720 1.3228 1.1863 -0.0551 0.0411  -0.0213 61  GLY A C   
433   O O   . GLY A 61  ? 0.5799 1.3459 1.2028 -0.0550 0.0347  -0.0262 61  GLY A O   
434   N N   . PHE A 62  ? 0.5882 1.3361 1.1940 -0.0502 0.0441  -0.0151 62  PHE A N   
435   C CA  . PHE A 62  ? 0.5839 1.3467 1.1918 -0.0448 0.0406  -0.0132 62  PHE A CA  
436   C C   . PHE A 62  ? 0.6063 1.3706 1.2031 -0.0401 0.0336  -0.0139 62  PHE A C   
437   O O   . PHE A 62  ? 0.5659 1.3353 1.1579 -0.0348 0.0321  -0.0100 62  PHE A O   
438   C CB  . PHE A 62  ? 0.6415 1.4011 1.2468 -0.0419 0.0472  -0.0065 62  PHE A CB  
439   C CG  . PHE A 62  ? 0.6513 1.3914 1.2400 -0.0403 0.0514  -0.0019 62  PHE A CG  
440   C CD1 . PHE A 62  ? 0.6913 1.4157 1.2762 -0.0447 0.0576  -0.0011 62  PHE A CD1 
441   C CD2 . PHE A 62  ? 0.6350 1.3723 1.2116 -0.0345 0.0491  0.0018  62  PHE A CD2 
442   C CE1 . PHE A 62  ? 0.6858 1.3922 1.2547 -0.0430 0.0608  0.0031  62  PHE A CE1 
443   C CE2 . PHE A 62  ? 0.6252 1.3449 1.1869 -0.0330 0.0524  0.0057  62  PHE A CE2 
444   C CZ  . PHE A 62  ? 0.6536 1.3580 1.2112 -0.0371 0.0581  0.0063  62  PHE A CZ  
445   N N   . TYR A 63  ? 0.7191 1.4789 1.3119 -0.0418 0.0294  -0.0188 63  TYR A N   
446   C CA  . TYR A 63  ? 0.7250 1.4906 1.3108 -0.0380 0.0222  -0.0212 63  TYR A CA  
447   C C   . TYR A 63  ? 0.7310 1.5172 1.3275 -0.0374 0.0165  -0.0248 63  TYR A C   
448   O O   . TYR A 63  ? 0.7287 1.5245 1.3388 -0.0401 0.0176  -0.0259 63  TYR A O   
449   C CB  . TYR A 63  ? 0.7501 1.5055 1.3302 -0.0402 0.0196  -0.0263 63  TYR A CB  
450   C CG  . TYR A 63  ? 0.7359 1.4744 1.3009 -0.0376 0.0212  -0.0231 63  TYR A CG  
451   C CD1 . TYR A 63  ? 0.7363 1.4748 1.2915 -0.0322 0.0206  -0.0183 63  TYR A CD1 
452   C CD2 . TYR A 63  ? 0.7543 1.4768 1.3151 -0.0406 0.0227  -0.0251 63  TYR A CD2 
453   C CE1 . TYR A 63  ? 0.7966 1.5205 1.3390 -0.0299 0.0215  -0.0157 63  TYR A CE1 
454   C CE2 . TYR A 63  ? 0.7767 1.4841 1.3242 -0.0380 0.0235  -0.0223 63  TYR A CE2 
455   C CZ  . TYR A 63  ? 0.8049 1.5134 1.3435 -0.0327 0.0228  -0.0178 63  TYR A CZ  
456   O OH  . TYR A 63  ? 0.7518 1.4460 1.2780 -0.0302 0.0231  -0.0153 63  TYR A OH  
457   N N   . GLU A 64  ? 0.7709 1.5644 1.3612 -0.0339 0.0102  -0.0267 64  GLU A N   
458   C CA  . GLU A 64  ? 0.8017 1.6141 1.3998 -0.0332 0.0039  -0.0304 64  GLU A CA  
459   C C   . GLU A 64  ? 0.7901 1.6051 1.3933 -0.0375 -0.0004 -0.0391 64  GLU A C   
460   O O   . GLU A 64  ? 0.7891 1.5940 1.3844 -0.0381 -0.0012 -0.0424 64  GLU A O   
461   C CB  . GLU A 64  ? 0.8684 1.6879 1.4567 -0.0275 -0.0005 -0.0278 64  GLU A CB  
462   C CG  . GLU A 64  ? 0.8829 1.7037 1.4690 -0.0232 0.0023  -0.0196 64  GLU A CG  
463   C CD  . GLU A 64  ? 0.9202 1.7536 1.5204 -0.0236 0.0027  -0.0183 64  GLU A CD  
464   O OE1 . GLU A 64  ? 0.9596 1.8053 1.5704 -0.0261 -0.0015 -0.0237 64  GLU A OE1 
465   O OE2 . GLU A 64  ? 0.9283 1.7595 1.5295 -0.0214 0.0070  -0.0122 64  GLU A OE2 
466   N N   . GLU A 65  ? 0.8793 1.7080 1.4964 -0.0403 -0.0032 -0.0432 65  GLU A N   
467   C CA  . GLU A 65  ? 0.8831 1.7150 1.5067 -0.0448 -0.0074 -0.0521 65  GLU A CA  
468   C C   . GLU A 65  ? 0.8684 1.7051 1.4827 -0.0421 -0.0142 -0.0570 65  GLU A C   
469   O O   . GLU A 65  ? 0.8675 1.7013 1.4827 -0.0451 -0.0169 -0.0645 65  GLU A O   
470   C CB  . GLU A 65  ? 0.9003 1.7480 1.5412 -0.0478 -0.0098 -0.0552 65  GLU A CB  
471   C CG  . GLU A 65  ? 0.9096 1.7599 1.5596 -0.0535 -0.0136 -0.0646 65  GLU A CG  
472   C CD  . GLU A 65  ? 0.9929 1.8585 1.6613 -0.0569 -0.0156 -0.0675 65  GLU A CD  
473   O OE1 . GLU A 65  ? 0.9776 1.8515 1.6521 -0.0547 -0.0137 -0.0620 65  GLU A OE1 
474   O OE2 . GLU A 65  ? 1.0381 1.9077 1.7155 -0.0617 -0.0194 -0.0755 65  GLU A OE2 
475   N N   . ARG A 66  ? 0.8456 1.6890 1.4509 -0.0365 -0.0166 -0.0529 66  ARG A N   
476   C CA  . ARG A 66  ? 0.8807 1.7301 1.4768 -0.0338 -0.0226 -0.0573 66  ARG A CA  
477   C C   . ARG A 66  ? 0.8973 1.7320 1.4838 -0.0341 -0.0213 -0.0604 66  ARG A C   
478   O O   . ARG A 66  ? 0.8510 1.6888 1.4347 -0.0344 -0.0258 -0.0677 66  ARG A O   
479   C CB  . ARG A 66  ? 0.9352 1.7925 1.5229 -0.0279 -0.0241 -0.0508 66  ARG A CB  
480   C CG  . ARG A 66  ? 0.9837 1.8537 1.5803 -0.0266 -0.0250 -0.0463 66  ARG A CG  
481   C CD  . ARG A 66  ? 1.0562 1.9282 1.6435 -0.0209 -0.0245 -0.0381 66  ARG A CD  
482   N NE  . ARG A 66  ? 1.1065 1.9622 1.6863 -0.0197 -0.0180 -0.0324 66  ARG A NE  
483   C CZ  . ARG A 66  ? 1.1513 2.0047 1.7226 -0.0153 -0.0164 -0.0251 66  ARG A CZ  
484   N NH1 . ARG A 66  ? 1.1665 2.0324 1.7356 -0.0116 -0.0205 -0.0221 66  ARG A NH1 
485   N NH2 . ARG A 66  ? 1.1536 1.9920 1.7184 -0.0146 -0.0109 -0.0208 66  ARG A NH2 
486   N N   . GLU A 67  ? 1.1176 1.9363 1.6991 -0.0339 -0.0153 -0.0553 67  GLU A N   
487   C CA  . GLU A 67  ? 1.1392 1.9436 1.7118 -0.0337 -0.0144 -0.0578 67  GLU A CA  
488   C C   . GLU A 67  ? 1.1459 1.9428 1.7256 -0.0391 -0.0146 -0.0650 67  GLU A C   
489   O O   . GLU A 67  ? 1.1554 1.9476 1.7309 -0.0391 -0.0172 -0.0712 67  GLU A O   
490   C CB  . GLU A 67  ? 1.1607 1.9501 1.7252 -0.0317 -0.0087 -0.0501 67  GLU A CB  
491   C CG  . GLU A 67  ? 1.1446 1.9384 1.6998 -0.0261 -0.0089 -0.0438 67  GLU A CG  
492   C CD  . GLU A 67  ? 1.1497 1.9289 1.6979 -0.0245 -0.0035 -0.0364 67  GLU A CD  
493   O OE1 . GLU A 67  ? 1.1336 1.9076 1.6867 -0.0264 0.0011  -0.0325 67  GLU A OE1 
494   O OE2 . GLU A 67  ? 1.1343 1.9074 1.6723 -0.0213 -0.0037 -0.0348 67  GLU A OE2 
495   N N   . PHE A 68  ? 0.8420 1.6377 1.4330 -0.0436 -0.0117 -0.0645 68  PHE A N   
496   C CA  . PHE A 68  ? 0.7517 1.5385 1.3500 -0.0493 -0.0110 -0.0703 68  PHE A CA  
497   C C   . PHE A 68  ? 0.7245 1.5240 1.3324 -0.0524 -0.0171 -0.0796 68  PHE A C   
498   O O   . PHE A 68  ? 0.7216 1.5137 1.3330 -0.0562 -0.0182 -0.0863 68  PHE A O   
499   C CB  . PHE A 68  ? 0.7091 1.4881 1.3152 -0.0535 -0.0044 -0.0655 68  PHE A CB  
500   C CG  . PHE A 68  ? 0.6448 1.4067 1.2409 -0.0518 0.0017  -0.0580 68  PHE A CG  
501   C CD1 . PHE A 68  ? 0.6161 1.3597 1.2101 -0.0551 0.0051  -0.0584 68  PHE A CD1 
502   C CD2 . PHE A 68  ? 0.6692 1.4328 1.2575 -0.0468 0.0036  -0.0507 68  PHE A CD2 
503   C CE1 . PHE A 68  ? 0.6363 1.3640 1.2200 -0.0534 0.0101  -0.0516 68  PHE A CE1 
504   C CE2 . PHE A 68  ? 0.6461 1.3940 1.2248 -0.0452 0.0088  -0.0443 68  PHE A CE2 
505   C CZ  . PHE A 68  ? 0.6361 1.3662 1.2122 -0.0484 0.0119  -0.0448 68  PHE A CZ  
506   N N   . ALA A 69  ? 0.7211 1.5392 1.3333 -0.0507 -0.0212 -0.0802 69  ALA A N   
507   C CA  . ALA A 69  ? 0.7116 1.5427 1.3329 -0.0536 -0.0276 -0.0891 69  ALA A CA  
508   C C   . ALA A 69  ? 0.6967 1.5256 1.3106 -0.0527 -0.0322 -0.0974 69  ALA A C   
509   O O   . ALA A 69  ? 0.7796 1.6093 1.4007 -0.0568 -0.0356 -0.1061 69  ALA A O   
510   C CB  . ALA A 69  ? 0.7445 1.5956 1.3692 -0.0509 -0.0318 -0.0874 69  ALA A CB  
511   N N   . LEU A 70  ? 0.6513 1.4775 1.2512 -0.0473 -0.0324 -0.0951 70  LEU A N   
512   C CA  . LEU A 70  ? 0.7103 1.5346 1.3028 -0.0460 -0.0363 -0.1030 70  LEU A CA  
513   C C   . LEU A 70  ? 0.7196 1.5252 1.3129 -0.0489 -0.0337 -0.1066 70  LEU A C   
514   O O   . LEU A 70  ? 0.6877 1.4920 1.2819 -0.0503 -0.0374 -0.1158 70  LEU A O   
515   C CB  . LEU A 70  ? 0.7436 1.5702 1.3219 -0.0396 -0.0365 -0.0992 70  LEU A CB  
516   C CG  . LEU A 70  ? 0.7262 1.5714 1.3002 -0.0360 -0.0406 -0.0978 70  LEU A CG  
517   C CD1 . LEU A 70  ? 0.6924 1.5445 1.2711 -0.0353 -0.0387 -0.0890 70  LEU A CD1 
518   C CD2 . LEU A 70  ? 0.6393 1.4845 1.1992 -0.0307 -0.0407 -0.0965 70  LEU A CD2 
519   N N   . TYR A 71  ? 0.6980 1.4889 1.2907 -0.0498 -0.0276 -0.0995 71  TYR A N   
520   C CA  . TYR A 71  ? 0.6991 1.4708 1.2913 -0.0523 -0.0251 -0.1015 71  TYR A CA  
521   C C   . TYR A 71  ? 0.7498 1.5184 1.3555 -0.0593 -0.0252 -0.1067 71  TYR A C   
522   O O   . TYR A 71  ? 0.8327 1.5921 1.4401 -0.0616 -0.0270 -0.1138 71  TYR A O   
523   C CB  . TYR A 71  ? 0.6926 1.4496 1.2782 -0.0507 -0.0188 -0.0917 71  TYR A CB  
524   C CG  . TYR A 71  ? 0.7557 1.4920 1.3412 -0.0538 -0.0158 -0.0923 71  TYR A CG  
525   C CD1 . TYR A 71  ? 0.7840 1.5114 1.3654 -0.0527 -0.0186 -0.0987 71  TYR A CD1 
526   C CD2 . TYR A 71  ? 0.7551 1.4805 1.3443 -0.0575 -0.0100 -0.0861 71  TYR A CD2 
527   C CE1 . TYR A 71  ? 0.7620 1.4697 1.3432 -0.0552 -0.0162 -0.0988 71  TYR A CE1 
528   C CE2 . TYR A 71  ? 0.7564 1.4622 1.3445 -0.0603 -0.0073 -0.0859 71  TYR A CE2 
529   C CZ  . TYR A 71  ? 0.7395 1.4362 1.3236 -0.0591 -0.0107 -0.0921 71  TYR A CZ  
530   O OH  . TYR A 71  ? 0.7268 1.4032 1.3097 -0.0616 -0.0084 -0.0915 71  TYR A OH  
531   N N   . VAL A 72  ? 0.7996 1.5754 1.4154 -0.0627 -0.0231 -0.1032 72  VAL A N   
532   C CA  . VAL A 72  ? 0.8228 1.5966 1.4528 -0.0699 -0.0227 -0.1077 72  VAL A CA  
533   C C   . VAL A 72  ? 0.9219 1.7055 1.5580 -0.0719 -0.0299 -0.1192 72  VAL A C   
534   O O   . VAL A 72  ? 0.9936 1.7703 1.6384 -0.0774 -0.0306 -0.1254 72  VAL A O   
535   C CB  . VAL A 72  ? 0.7965 1.5794 1.4371 -0.0725 -0.0192 -0.1019 72  VAL A CB  
536   C CG1 . VAL A 72  ? 0.8303 1.6142 1.4874 -0.0802 -0.0192 -0.1071 72  VAL A CG1 
537   C CG2 . VAL A 72  ? 0.8056 1.5763 1.4402 -0.0712 -0.0115 -0.0913 72  VAL A CG2 
538   N N   . SER A 73  ? 1.0478 1.8468 1.6786 -0.0674 -0.0354 -0.1224 73  SER A N   
539   C CA  . SER A 73  ? 1.0457 1.8549 1.6805 -0.0689 -0.0426 -0.1337 73  SER A CA  
540   C C   . SER A 73  ? 1.0806 1.8762 1.7112 -0.0693 -0.0441 -0.1414 73  SER A C   
541   O O   . SER A 73  ? 1.1100 1.9090 1.7469 -0.0724 -0.0490 -0.1516 73  SER A O   
542   C CB  . SER A 73  ? 1.0239 1.8512 1.6510 -0.0634 -0.0477 -0.1344 73  SER A CB  
543   O OG  . SER A 73  ? 1.0557 1.8957 1.6875 -0.0627 -0.0470 -0.1275 73  SER A OG  
544   N N   . SER A 74  ? 0.9870 1.7672 1.6073 -0.0660 -0.0402 -0.1371 74  SER A N   
545   C CA  . SER A 74  ? 0.9811 1.7483 1.5969 -0.0654 -0.0417 -0.1440 74  SER A CA  
546   C C   . SER A 74  ? 1.0363 1.7840 1.6589 -0.0707 -0.0382 -0.1441 74  SER A C   
547   O O   . SER A 74  ? 0.9968 1.7351 1.6204 -0.0720 -0.0407 -0.1522 74  SER A O   
548   C CB  . SER A 74  ? 0.9804 1.7424 1.5815 -0.0585 -0.0401 -0.1399 74  SER A CB  
549   O OG  . SER A 74  ? 0.8624 1.6417 1.4566 -0.0537 -0.0426 -0.1388 74  SER A OG  
550   N N   . ILE A 75  ? 1.2391 1.9800 1.8660 -0.0738 -0.0325 -0.1354 75  ILE A N   
551   C CA  . ILE A 75  ? 1.2685 1.9897 1.9003 -0.0790 -0.0286 -0.1342 75  ILE A CA  
552   C C   . ILE A 75  ? 1.2839 2.0071 1.9302 -0.0861 -0.0315 -0.1429 75  ILE A C   
553   O O   . ILE A 75  ? 1.3223 2.0317 1.9711 -0.0888 -0.0326 -0.1487 75  ILE A O   
554   C CB  . ILE A 75  ? 1.2674 1.9818 1.8991 -0.0805 -0.0212 -0.1224 75  ILE A CB  
555   C CG1 . ILE A 75  ? 1.2467 1.9657 1.8661 -0.0736 -0.0193 -0.1143 75  ILE A CG1 
556   C CG2 . ILE A 75  ? 1.2879 1.9786 1.9185 -0.0837 -0.0167 -0.1194 75  ILE A CG2 
557   C CD1 . ILE A 75  ? 1.2362 1.9524 1.8560 -0.0747 -0.0126 -0.1036 75  ILE A CD1 
558   N N   . SER A 76  ? 1.2010 1.9414 1.8579 -0.0892 -0.0331 -0.1441 76  SER A N   
559   C CA  . SER A 76  ? 1.2720 2.0162 1.9443 -0.0963 -0.0361 -0.1524 76  SER A CA  
560   C C   . SER A 76  ? 1.1827 1.9298 1.8545 -0.0956 -0.0435 -0.1651 76  SER A C   
561   O O   . SER A 76  ? 1.1810 1.9268 1.8646 -0.1017 -0.0463 -0.1732 76  SER A O   
562   C CB  . SER A 76  ? 1.2621 2.0263 1.9455 -0.0988 -0.0370 -0.1510 76  SER A CB  
563   O OG  . SER A 76  ? 1.2792 2.0405 1.9646 -0.0998 -0.0296 -0.1400 76  SER A OG  
564   N N   . ASN A 77  ? 1.1300 1.8810 1.7886 -0.0885 -0.0467 -0.1674 77  ASN A N   
565   C CA  . ASN A 77  ? 1.0310 1.7824 1.6875 -0.0872 -0.0528 -0.1795 77  ASN A CA  
566   C C   . ASN A 77  ? 1.0222 1.7507 1.6768 -0.0881 -0.0512 -0.1822 77  ASN A C   
567   O O   . ASN A 77  ? 1.0270 1.7527 1.6838 -0.0889 -0.0559 -0.1932 77  ASN A O   
568   C CB  . ASN A 77  ? 0.9601 1.7237 1.6030 -0.0793 -0.0559 -0.1807 77  ASN A CB  
569   C CG  . ASN A 77  ? 0.9030 1.6893 1.5470 -0.0782 -0.0587 -0.1788 77  ASN A CG  
570   O OD1 . ASN A 77  ? 0.9049 1.7010 1.5613 -0.0832 -0.0611 -0.1816 77  ASN A OD1 
571   N ND2 . ASN A 77  ? 0.8599 1.6546 1.4916 -0.0715 -0.0585 -0.1739 77  ASN A ND2 
572   N N   . GLU A 78  ? 1.0309 1.7429 1.6812 -0.0877 -0.0449 -0.1725 78  GLU A N   
573   C CA  . GLU A 78  ? 1.0618 1.7509 1.7095 -0.0881 -0.0434 -0.1736 78  GLU A CA  
574   C C   . GLU A 78  ? 1.1612 1.8365 1.8210 -0.0965 -0.0404 -0.1726 78  GLU A C   
575   O O   . GLU A 78  ? 1.1961 1.8615 1.8621 -0.1000 -0.0431 -0.1809 78  GLU A O   
576   C CB  . GLU A 78  ? 1.0099 1.6882 1.6443 -0.0822 -0.0389 -0.1636 78  GLU A CB  
577   C CG  . GLU A 78  ? 1.0110 1.7000 1.6334 -0.0739 -0.0415 -0.1647 78  GLU A CG  
578   C CD  . GLU A 78  ? 0.8968 1.5739 1.5072 -0.0685 -0.0376 -0.1558 78  GLU A CD  
579   O OE1 . GLU A 78  ? 0.8217 1.4823 1.4322 -0.0710 -0.0330 -0.1483 78  GLU A OE1 
580   O OE2 . GLU A 78  ? 0.9031 1.5874 1.5040 -0.0619 -0.0391 -0.1562 78  GLU A OE2 
581   N N   . LEU A 79  ? 1.1811 1.8556 1.8444 -0.0999 -0.0345 -0.1626 79  LEU A N   
582   C CA  . LEU A 79  ? 1.3305 1.9913 2.0043 -0.1080 -0.0302 -0.1600 79  LEU A CA  
583   C C   . LEU A 79  ? 1.4561 2.1314 2.1466 -0.1152 -0.0312 -0.1637 79  LEU A C   
584   O O   . LEU A 79  ? 1.5081 2.1735 2.2094 -0.1229 -0.0280 -0.1630 79  LEU A O   
585   C CB  . LEU A 79  ? 1.3519 2.0006 2.0190 -0.1077 -0.0222 -0.1464 79  LEU A CB  
586   C CG  . LEU A 79  ? 1.2363 1.8642 1.8895 -0.1029 -0.0204 -0.1417 79  LEU A CG  
587   C CD1 . LEU A 79  ? 1.2209 1.8326 1.8766 -0.1047 -0.0239 -0.1499 79  LEU A CD1 
588   C CD2 . LEU A 79  ? 1.1649 1.8010 1.8045 -0.0936 -0.0224 -0.1400 79  LEU A CD2 
589   N N   . LYS A 80  ? 1.4092 2.1075 2.1021 -0.1131 -0.0356 -0.1676 80  LYS A N   
590   C CA  . LYS A 80  ? 1.5289 2.2433 2.2381 -0.1192 -0.0380 -0.1721 80  LYS A CA  
591   C C   . LYS A 80  ? 1.7271 2.4400 2.4455 -0.1247 -0.0305 -0.1627 80  LYS A C   
592   O O   . LYS A 80  ? 1.7197 2.4287 2.4527 -0.1329 -0.0288 -0.1648 80  LYS A O   
593   C CB  . LYS A 80  ? 1.4407 2.1511 2.1608 -0.1249 -0.0432 -0.1845 80  LYS A CB  
594   C CG  . LYS A 80  ? 1.3847 2.0969 2.0966 -0.1198 -0.0506 -0.1953 80  LYS A CG  
595   C CD  . LYS A 80  ? 1.4121 2.1008 2.1148 -0.1173 -0.0490 -0.1955 80  LYS A CD  
596   C CE  . LYS A 80  ? 1.4384 2.1073 2.1513 -0.1253 -0.0453 -0.1945 80  LYS A CE  
597   N NZ  . LYS A 80  ? 1.4021 2.0467 2.1052 -0.1226 -0.0431 -0.1923 80  LYS A NZ  
598   N N   . ILE A 81  ? 2.5443 3.2607 3.2543 -0.1201 -0.0257 -0.1522 81  ILE A N   
599   C CA  . ILE A 81  ? 2.5397 3.2559 3.2567 -0.1242 -0.0180 -0.1429 81  ILE A CA  
600   C C   . ILE A 81  ? 2.5084 3.2454 3.2250 -0.1199 -0.0182 -0.1383 81  ILE A C   
601   O O   . ILE A 81  ? 2.4964 3.2381 3.1994 -0.1121 -0.0201 -0.1358 81  ILE A O   
602   C CB  . ILE A 81  ? 2.5612 3.2546 3.2674 -0.1236 -0.0103 -0.1331 81  ILE A CB  
603   C CG1 . ILE A 81  ? 2.5657 3.2509 3.2532 -0.1151 -0.0125 -0.1319 81  ILE A CG1 
604   C CG2 . ILE A 81  ? 2.5917 3.2663 3.3056 -0.1315 -0.0074 -0.1349 81  ILE A CG2 
605   C CD1 . ILE A 81  ? 2.5895 3.2518 3.2657 -0.1142 -0.0061 -0.1230 81  ILE A CD1 
606   N N   . PRO A 82  ? 1.5354 2.2852 2.2671 -0.1246 -0.0162 -0.1369 82  PRO A N   
607   C CA  . PRO A 82  ? 1.2373 2.0071 1.9697 -0.1203 -0.0167 -0.1326 82  PRO A CA  
608   C C   . PRO A 82  ? 1.0785 1.8413 1.7991 -0.1157 -0.0093 -0.1206 82  PRO A C   
609   O O   . PRO A 82  ? 1.0168 1.7752 1.7435 -0.1194 -0.0017 -0.1138 82  PRO A O   
610   C CB  . PRO A 82  ? 1.1565 1.9392 1.9105 -0.1275 -0.0160 -0.1347 82  PRO A CB  
611   C CG  . PRO A 82  ? 1.1842 1.9575 1.9485 -0.1352 -0.0179 -0.1431 82  PRO A CG  
612   C CD  . PRO A 82  ? 1.3964 2.1449 2.1468 -0.1342 -0.0144 -0.1405 82  PRO A CD  
613   N N   . VAL A 83  ? 1.0402 1.8022 1.7443 -0.1077 -0.0114 -0.1182 83  VAL A N   
614   C CA  . VAL A 83  ? 0.9149 1.6710 1.6068 -0.1027 -0.0055 -0.1075 83  VAL A CA  
615   C C   . VAL A 83  ? 0.8241 1.6009 1.5179 -0.0983 -0.0072 -0.1045 83  VAL A C   
616   O O   . VAL A 83  ? 0.8105 1.6030 1.5055 -0.0957 -0.0147 -0.1103 83  VAL A O   
617   C CB  . VAL A 83  ? 0.9125 1.6548 1.5858 -0.0968 -0.0066 -0.1063 83  VAL A CB  
618   C CG1 . VAL A 83  ? 0.7845 1.5185 1.4459 -0.0925 -0.0001 -0.0953 83  VAL A CG1 
619   C CG2 . VAL A 83  ? 1.1271 1.8506 1.7998 -0.1007 -0.0067 -0.1110 83  VAL A CG2 
620   N N   . ARG A 84  ? 0.7668 1.5434 1.4605 -0.0973 -0.0004 -0.0954 84  ARG A N   
621   C CA  . ARG A 84  ? 0.7352 1.5301 1.4316 -0.0931 -0.0015 -0.0917 84  ARG A CA  
622   C C   . ARG A 84  ? 0.6516 1.4386 1.3364 -0.0885 0.0052  -0.0813 84  ARG A C   
623   O O   . ARG A 84  ? 0.6458 1.4170 1.3282 -0.0912 0.0127  -0.0762 84  ARG A O   
624   C CB  . ARG A 84  ? 0.7468 1.5561 1.4638 -0.0985 -0.0007 -0.0935 84  ARG A CB  
625   C CG  . ARG A 84  ? 0.7559 1.5845 1.4774 -0.0941 -0.0022 -0.0899 84  ARG A CG  
626   C CD  . ARG A 84  ? 0.8358 1.6782 1.5792 -0.0996 -0.0012 -0.0919 84  ARG A CD  
627   N NE  . ARG A 84  ? 0.9823 1.8338 1.7375 -0.1043 -0.0087 -0.1022 84  ARG A NE  
628   C CZ  . ARG A 84  ? 0.9894 1.8595 1.7487 -0.1017 -0.0178 -0.1075 84  ARG A CZ  
629   N NH1 . ARG A 84  ? 1.0382 1.9196 1.7909 -0.0945 -0.0204 -0.1030 84  ARG A NH1 
630   N NH2 . ARG A 84  ? 0.9476 1.8247 1.7175 -0.1063 -0.0244 -0.1173 84  ARG A NH2 
631   N N   . TYR A 85  ? 0.5660 1.3634 1.2433 -0.0817 0.0024  -0.0781 85  TYR A N   
632   C CA  . TYR A 85  ? 0.5585 1.3504 1.2255 -0.0770 0.0079  -0.0687 85  TYR A CA  
633   C C   . TYR A 85  ? 0.5755 1.3824 1.2537 -0.0763 0.0102  -0.0647 85  TYR A C   
634   O O   . TYR A 85  ? 0.6376 1.4630 1.3244 -0.0752 0.0043  -0.0682 85  TYR A O   
635   C CB  . TYR A 85  ? 0.5879 1.3794 1.2384 -0.0696 0.0039  -0.0671 85  TYR A CB  
636   C CG  . TYR A 85  ? 0.5593 1.3463 1.2000 -0.0646 0.0089  -0.0578 85  TYR A CG  
637   C CD1 . TYR A 85  ? 0.5527 1.3203 1.1833 -0.0647 0.0151  -0.0525 85  TYR A CD1 
638   C CD2 . TYR A 85  ? 0.5749 1.3765 1.2161 -0.0598 0.0070  -0.0542 85  TYR A CD2 
639   C CE1 . TYR A 85  ? 0.5335 1.2968 1.1551 -0.0603 0.0194  -0.0446 85  TYR A CE1 
640   C CE2 . TYR A 85  ? 0.5748 1.3716 1.2073 -0.0554 0.0114  -0.0461 85  TYR A CE2 
641   C CZ  . TYR A 85  ? 0.5514 1.3293 1.1742 -0.0557 0.0176  -0.0415 85  TYR A CZ  
642   O OH  . TYR A 85  ? 0.5736 1.3464 1.1876 -0.0514 0.0218  -0.0339 85  TYR A OH  
643   N N   . LEU A 86  ? 0.5432 1.3421 1.2208 -0.0768 0.0186  -0.0574 86  LEU A N   
644   C CA  . LEU A 86  ? 0.5274 1.3386 1.2151 -0.0756 0.0220  -0.0531 86  LEU A CA  
645   C C   . LEU A 86  ? 0.5336 1.3373 1.2077 -0.0698 0.0267  -0.0446 86  LEU A C   
646   O O   . LEU A 86  ? 0.5507 1.3363 1.2141 -0.0704 0.0326  -0.0406 86  LEU A O   
647   C CB  . LEU A 86  ? 0.6058 1.4159 1.3091 -0.0828 0.0288  -0.0533 86  LEU A CB  
648   C CG  . LEU A 86  ? 0.6029 1.4187 1.3213 -0.0899 0.0252  -0.0616 86  LEU A CG  
649   C CD1 . LEU A 86  ? 0.6501 1.4642 1.3839 -0.0971 0.0332  -0.0606 86  LEU A CD1 
650   C CD2 . LEU A 86  ? 0.6239 1.4617 1.3522 -0.0879 0.0158  -0.0673 86  LEU A CD2 
651   N N   . LYS A 87  ? 0.5611 1.3783 1.2355 -0.0642 0.0238  -0.0419 87  LYS A N   
652   C CA  . LYS A 87  ? 0.6313 1.4426 1.2939 -0.0584 0.0276  -0.0341 87  LYS A CA  
653   C C   . LYS A 87  ? 0.6969 1.5113 1.3696 -0.0593 0.0352  -0.0296 87  LYS A C   
654   O O   . LYS A 87  ? 0.7653 1.5966 1.4514 -0.0583 0.0334  -0.0302 87  LYS A O   
655   C CB  . LYS A 87  ? 0.6311 1.4541 1.2876 -0.0517 0.0205  -0.0332 87  LYS A CB  
656   C CG  . LYS A 87  ? 0.6836 1.5039 1.3317 -0.0458 0.0241  -0.0254 87  LYS A CG  
657   C CD  . LYS A 87  ? 0.6165 1.4482 1.2591 -0.0397 0.0170  -0.0243 87  LYS A CD  
658   C CE  . LYS A 87  ? 0.6381 1.4692 1.2762 -0.0343 0.0204  -0.0166 87  LYS A CE  
659   N NZ  . LYS A 87  ? 0.6633 1.4752 1.2901 -0.0342 0.0278  -0.0121 87  LYS A NZ  
660   N N   . GLU A 88  ? 0.6771 1.4752 1.3433 -0.0610 0.0437  -0.0252 88  GLU A N   
661   C CA  . GLU A 88  ? 0.8288 1.6284 1.5023 -0.0612 0.0519  -0.0206 88  GLU A CA  
662   C C   . GLU A 88  ? 0.9622 1.7673 1.6298 -0.0536 0.0510  -0.0156 88  GLU A C   
663   O O   . GLU A 88  ? 0.9142 1.7071 1.5652 -0.0497 0.0522  -0.0113 88  GLU A O   
664   C CB  . GLU A 88  ? 0.8245 1.6042 1.4902 -0.0650 0.0612  -0.0172 88  GLU A CB  
665   C CG  . GLU A 88  ? 0.7969 1.5575 1.4410 -0.0623 0.0611  -0.0143 88  GLU A CG  
666   C CD  . GLU A 88  ? 0.8826 1.6245 1.5184 -0.0651 0.0705  -0.0098 88  GLU A CD  
667   O OE1 . GLU A 88  ? 0.9773 1.7216 1.6226 -0.0680 0.0781  -0.0080 88  GLU A OE1 
668   O OE2 . GLU A 88  ? 0.9357 1.6606 1.5552 -0.0642 0.0704  -0.0080 88  GLU A OE2 
669   N N   . ASP A 89  ? 1.3182 2.1418 1.9998 -0.0515 0.0485  -0.0161 89  ASP A N   
670   C CA  . ASP A 89  ? 1.3104 2.1399 1.9880 -0.0443 0.0473  -0.0112 89  ASP A CA  
671   C C   . ASP A 89  ? 1.3254 2.1424 1.9959 -0.0426 0.0567  -0.0052 89  ASP A C   
672   O O   . ASP A 89  ? 1.3157 2.1271 1.9737 -0.0369 0.0565  -0.0007 89  ASP A O   
673   C CB  . ASP A 89  ? 1.3717 2.2229 2.0675 -0.0427 0.0433  -0.0129 89  ASP A CB  
674   C CG  . ASP A 89  ? 1.3902 2.2539 2.0965 -0.0463 0.0355  -0.0199 89  ASP A CG  
675   O OD1 . ASP A 89  ? 1.3421 2.2104 2.0636 -0.0523 0.0380  -0.0238 89  ASP A OD1 
676   O OD2 . ASP A 89  ? 1.3888 2.2576 2.0881 -0.0434 0.0270  -0.0217 89  ASP A OD2 
677   N N   . LYS A 90  ? 1.1293 1.9418 1.8076 -0.0475 0.0651  -0.0052 90  LYS A N   
678   C CA  . LYS A 90  ? 1.1244 1.9239 1.7951 -0.0467 0.0748  -0.0001 90  LYS A CA  
679   C C   . LYS A 90  ? 1.1387 1.9181 1.7968 -0.0514 0.0793  0.0002  90  LYS A C   
680   O O   . LYS A 90  ? 1.1271 1.9039 1.7933 -0.0580 0.0843  -0.0018 90  LYS A O   
681   C CB  . LYS A 90  ? 1.1404 1.9499 1.8289 -0.0484 0.0820  0.0002  90  LYS A CB  
682   N N   . PRO A 91  ? 1.1129 1.8775 1.7515 -0.0484 0.0776  0.0028  91  PRO A N   
683   C CA  . PRO A 91  ? 1.1337 1.8788 1.7600 -0.0525 0.0810  0.0032  91  PRO A CA  
684   C C   . PRO A 91  ? 1.2508 1.9842 1.8736 -0.0548 0.0920  0.0072  91  PRO A C   
685   O O   . PRO A 91  ? 1.2273 1.9580 1.8440 -0.0504 0.0960  0.0113  91  PRO A O   
686   C CB  . PRO A 91  ? 1.0081 1.7432 1.6157 -0.0475 0.0756  0.0050  91  PRO A CB  
687   C CG  . PRO A 91  ? 0.9726 1.7241 1.5847 -0.0421 0.0682  0.0044  91  PRO A CG  
688   C CD  . PRO A 91  ? 1.0630 1.8287 1.6907 -0.0414 0.0717  0.0051  91  PRO A CD  
689   N N   . HIS A 92  ? 1.5381 2.2641 2.1646 -0.0617 0.0970  0.0058  92  HIS A N   
690   C CA  . HIS A 92  ? 1.5595 2.2740 2.1823 -0.0646 0.1081  0.0096  92  HIS A CA  
691   C C   . HIS A 92  ? 1.5905 2.2830 2.1976 -0.0683 0.1102  0.0112  92  HIS A C   
692   O O   . HIS A 92  ? 1.6103 2.2954 2.2203 -0.0745 0.1173  0.0117  92  HIS A O   
693   C CB  . HIS A 92  ? 1.5556 2.2821 2.1993 -0.0702 0.1141  0.0075  92  HIS A CB  
694   C CG  . HIS A 92  ? 1.5278 2.2775 2.1898 -0.0672 0.1104  0.0050  92  HIS A CG  
695   N ND1 . HIS A 92  ? 1.5132 2.2788 2.1955 -0.0714 0.1072  -0.0001 92  HIS A ND1 
696   C CD2 . HIS A 92  ? 1.5534 2.3127 2.2166 -0.0604 0.1090  0.0069  92  HIS A CD2 
697   C CE1 . HIS A 92  ? 1.5005 2.2848 2.1955 -0.0671 0.1038  -0.0010 92  HIS A CE1 
698   N NE2 . HIS A 92  ? 1.5745 2.3550 2.2582 -0.0603 0.1049  0.0033  92  HIS A NE2 
699   N N   . GLY A 93  ? 1.4132 2.0951 2.0038 -0.0643 0.1042  0.0121  93  GLY A N   
700   C CA  . GLY A 93  ? 1.3696 2.0308 1.9452 -0.0670 0.1050  0.0135  93  GLY A CA  
701   C C   . GLY A 93  ? 1.2538 1.9142 1.8384 -0.0736 0.1029  0.0092  93  GLY A C   
702   O O   . GLY A 93  ? 1.1104 1.7779 1.6995 -0.0730 0.0943  0.0046  93  GLY A O   
703   N N   . SER A 94  ? 1.2534 1.9051 1.8406 -0.0801 0.1109  0.0106  94  SER A N   
704   C CA  . SER A 94  ? 1.1746 1.8233 1.7702 -0.0871 0.1098  0.0070  94  SER A CA  
705   C C   . SER A 94  ? 1.0720 1.7320 1.6877 -0.0936 0.1164  0.0053  94  SER A C   
706   O O   . SER A 94  ? 0.9864 1.6599 1.6187 -0.0966 0.1117  -0.0003 94  SER A O   
707   C CB  . SER A 94  ? 1.2196 1.8435 1.7982 -0.0897 0.1124  0.0103  94  SER A CB  
708   O OG  . SER A 94  ? 1.3249 1.9391 1.8865 -0.0837 0.1057  0.0113  94  SER A OG  
709   N N   . ALA A 95  ? 1.0902 1.7455 1.7050 -0.0959 0.1272  0.0098  95  ALA A N   
710   C CA  . ALA A 95  ? 1.0612 1.7257 1.6951 -0.1029 0.1345  0.0084  95  ALA A CA  
711   C C   . ALA A 95  ? 1.0212 1.7117 1.6764 -0.1011 0.1312  0.0041  95  ALA A C   
712   O O   . ALA A 95  ? 0.9682 1.6705 1.6423 -0.1063 0.1292  -0.0008 95  ALA A O   
713   C CB  . ALA A 95  ? 1.1323 1.7868 1.7593 -0.1049 0.1473  0.0142  95  ALA A CB  
714   N N   . GLY A 96  ? 1.1302 1.8294 1.7828 -0.0939 0.1303  0.0058  96  GLY A N   
715   C CA  . GLY A 96  ? 1.1591 1.8824 1.8307 -0.0912 0.1259  0.0021  96  GLY A CA  
716   C C   . GLY A 96  ? 1.0676 1.8007 1.7440 -0.0896 0.1134  -0.0033 96  GLY A C   
717   O O   . GLY A 96  ? 1.0345 1.7877 1.7292 -0.0895 0.1092  -0.0074 96  GLY A O   
718   N N   . ALA A 97  ? 1.0525 1.7722 1.7128 -0.0880 0.1074  -0.0035 97  ALA A N   
719   C CA  . ALA A 97  ? 0.9657 1.6940 1.6289 -0.0864 0.0960  -0.0088 97  ALA A CA  
720   C C   . ALA A 97  ? 0.8417 1.5783 1.5230 -0.0936 0.0938  -0.0150 97  ALA A C   
721   O O   . ALA A 97  ? 0.8119 1.5661 1.5060 -0.0928 0.0863  -0.0201 97  ALA A O   
722   C CB  . ALA A 97  ? 0.9686 1.6797 1.6113 -0.0836 0.0912  -0.0079 97  ALA A CB  
723   N N   . LEU A 98  ? 0.8376 1.5614 1.5200 -0.1009 0.1001  -0.0145 98  LEU A N   
724   C CA  . LEU A 98  ? 0.8231 1.5528 1.5224 -0.1084 0.0981  -0.0204 98  LEU A CA  
725   C C   . LEU A 98  ? 0.8662 1.6115 1.5879 -0.1131 0.1042  -0.0215 98  LEU A C   
726   O O   . LEU A 98  ? 0.8719 1.6294 1.6117 -0.1179 0.1003  -0.0275 98  LEU A O   
727   C CB  . LEU A 98  ? 0.7897 1.4977 1.4804 -0.1144 0.1011  -0.0198 98  LEU A CB  
728   C CG  . LEU A 98  ? 0.8421 1.5371 1.5320 -0.1205 0.1134  -0.0146 98  LEU A CG  
729   C CD1 . LEU A 98  ? 0.7891 1.4722 1.4833 -0.1289 0.1141  -0.0171 98  LEU A CD1 
730   C CD2 . LEU A 98  ? 0.8924 1.5691 1.5589 -0.1160 0.1183  -0.0073 98  LEU A CD2 
731   N N   . TYR A 99  ? 0.8886 1.6342 1.6100 -0.1119 0.1136  -0.0162 99  TYR A N   
732   C CA  . TYR A 99  ? 0.8434 1.6069 1.5876 -0.1152 0.1188  -0.0176 99  TYR A CA  
733   C C   . TYR A 99  ? 0.8496 1.6367 1.6073 -0.1101 0.1098  -0.0218 99  TYR A C   
734   O O   . TYR A 99  ? 0.8187 1.6231 1.5988 -0.1139 0.1083  -0.0264 99  TYR A O   
735   C CB  . TYR A 99  ? 0.8816 1.6404 1.6218 -0.1141 0.1309  -0.0113 99  TYR A CB  
736   C CG  . TYR A 99  ? 0.9308 1.7095 1.6954 -0.1166 0.1363  -0.0129 99  TYR A CG  
737   C CD1 . TYR A 99  ? 0.9523 1.7374 1.7368 -0.1255 0.1396  -0.0165 99  TYR A CD1 
738   C CD2 . TYR A 99  ? 1.0262 1.8176 1.7949 -0.1099 0.1380  -0.0110 99  TYR A CD2 
739   C CE1 . TYR A 99  ? 0.9821 1.7863 1.7904 -0.1278 0.1444  -0.0183 99  TYR A CE1 
740   C CE2 . TYR A 99  ? 1.0714 1.8817 1.8637 -0.1117 0.1427  -0.0128 99  TYR A CE2 
741   C CZ  . TYR A 99  ? 1.0460 1.8630 1.8583 -0.1207 0.1459  -0.0165 99  TYR A CZ  
742   O OH  . TYR A 99  ? 1.0372 1.8738 1.8742 -0.1227 0.1506  -0.0185 99  TYR A OH  
743   N N   . TYR A 100 ? 0.8758 1.6638 1.6201 -0.1015 0.1038  -0.0200 100 TYR A N   
744   C CA  . TYR A 100 ? 0.8316 1.6389 1.5843 -0.0965 0.0931  -0.0240 100 TYR A CA  
745   C C   . TYR A 100 ? 0.8231 1.6354 1.5842 -0.1012 0.0846  -0.0312 100 TYR A C   
746   O O   . TYR A 100 ? 0.8419 1.6388 1.5922 -0.1042 0.0831  -0.0325 100 TYR A O   
747   C CB  . TYR A 100 ? 0.8376 1.6395 1.5704 -0.0877 0.0880  -0.0206 100 TYR A CB  
748   C CG  . TYR A 100 ? 0.8009 1.6221 1.5400 -0.0809 0.0799  -0.0218 100 TYR A CG  
749   C CD1 . TYR A 100 ? 0.8652 1.6830 1.5884 -0.0729 0.0767  -0.0179 100 TYR A CD1 
750   C CD2 . TYR A 100 ? 0.7784 1.6206 1.5390 -0.0826 0.0752  -0.0267 100 TYR A CD2 
751   C CE1 . TYR A 100 ? 0.9013 1.7355 1.6293 -0.0668 0.0694  -0.0184 100 TYR A CE1 
752   C CE2 . TYR A 100 ? 0.8080 1.6671 1.5733 -0.0761 0.0674  -0.0274 100 TYR A CE2 
753   C CZ  . TYR A 100 ? 0.8407 1.6953 1.5893 -0.0683 0.0647  -0.0229 100 TYR A CZ  
754   O OH  . TYR A 100 ? 0.8386 1.7091 1.5913 -0.0621 0.0570  -0.0230 100 TYR A OH  
755   N N   . PHE A 101 ? 0.8004 1.6343 1.5810 -0.1015 0.0786  -0.0362 101 PHE A N   
756   C CA  . PHE A 101 ? 0.8253 1.6673 1.6178 -0.1065 0.0706  -0.0441 101 PHE A CA  
757   C C   . PHE A 101 ? 0.8265 1.6531 1.6199 -0.1154 0.0755  -0.0458 101 PHE A C   
758   O O   . PHE A 101 ? 0.8161 1.6340 1.6025 -0.1175 0.0698  -0.0498 101 PHE A O   
759   C CB  . PHE A 101 ? 0.8443 1.6892 1.6256 -0.1011 0.0586  -0.0474 101 PHE A CB  
760   C CG  . PHE A 101 ? 0.8304 1.6570 1.5863 -0.0961 0.0586  -0.0431 101 PHE A CG  
761   C CD1 . PHE A 101 ? 0.7956 1.6240 1.5399 -0.0878 0.0576  -0.0380 101 PHE A CD1 
762   C CD2 . PHE A 101 ? 0.7579 1.5660 1.5022 -0.0996 0.0589  -0.0443 101 PHE A CD2 
763   C CE1 . PHE A 101 ? 0.7243 1.5367 1.4464 -0.0835 0.0573  -0.0343 101 PHE A CE1 
764   C CE2 . PHE A 101 ? 0.6769 1.4691 1.3990 -0.0949 0.0584  -0.0405 101 PHE A CE2 
765   C CZ  . PHE A 101 ? 0.6768 1.4715 1.3880 -0.0869 0.0576  -0.0357 101 PHE A CZ  
766   N N   . ARG A 102 ? 0.8315 1.6547 1.6339 -0.1208 0.0866  -0.0428 102 ARG A N   
767   C CA  . ARG A 102 ? 0.8387 1.6499 1.6462 -0.1304 0.0917  -0.0445 102 ARG A CA  
768   C C   . ARG A 102 ? 0.8175 1.6434 1.6470 -0.1366 0.0852  -0.0530 102 ARG A C   
769   O O   . ARG A 102 ? 0.8207 1.6362 1.6531 -0.1441 0.0858  -0.0560 102 ARG A O   
770   C CB  . ARG A 102 ? 0.8851 1.6909 1.6977 -0.1348 0.1057  -0.0390 102 ARG A CB  
771   C CG  . ARG A 102 ? 0.8988 1.7271 1.7348 -0.1353 0.1091  -0.0400 102 ARG A CG  
772   C CD  . ARG A 102 ? 0.9031 1.7262 1.7469 -0.1417 0.1234  -0.0360 102 ARG A CD  
773   N NE  . ARG A 102 ? 0.9145 1.7310 1.7686 -0.1523 0.1264  -0.0390 102 ARG A NE  
774   C CZ  . ARG A 102 ? 0.9205 1.7330 1.7840 -0.1599 0.1385  -0.0364 102 ARG A CZ  
775   N NH1 . ARG A 102 ? 0.9196 1.7343 1.7832 -0.1577 0.1490  -0.0311 102 ARG A NH1 
776   N NH2 . ARG A 102 ? 0.9156 1.7216 1.7884 -0.1697 0.1403  -0.0392 102 ARG A NH2 
777   N N   . ASP A 103 ? 0.7881 1.6374 1.6330 -0.1335 0.0785  -0.0568 103 ASP A N   
778   C CA  . ASP A 103 ? 0.8039 1.6685 1.6697 -0.1389 0.0711  -0.0654 103 ASP A CA  
779   C C   . ASP A 103 ? 0.8438 1.7028 1.6997 -0.1385 0.0603  -0.0713 103 ASP A C   
780   O O   . ASP A 103 ? 0.8495 1.7075 1.7158 -0.1457 0.0574  -0.0777 103 ASP A O   
781   C CB  . ASP A 103 ? 0.8437 1.7346 1.7267 -0.1346 0.0662  -0.0674 103 ASP A CB  
782   C CG  . ASP A 103 ? 0.8748 1.7694 1.7421 -0.1237 0.0609  -0.0637 103 ASP A CG  
783   O OD1 . ASP A 103 ? 0.8488 1.7270 1.6928 -0.1197 0.0601  -0.0606 103 ASP A OD1 
784   O OD2 . ASP A 103 ? 0.9571 1.8710 1.8358 -0.1191 0.0575  -0.0638 103 ASP A OD2 
785   N N   . ARG A 104 ? 0.9351 1.7905 1.7714 -0.1301 0.0543  -0.0697 104 ARG A N   
786   C CA  . ARG A 104 ? 0.9351 1.7864 1.7615 -0.1289 0.0441  -0.0756 104 ARG A CA  
787   C C   . ARG A 104 ? 0.9466 1.7749 1.7635 -0.1344 0.0474  -0.0761 104 ARG A C   
788   O O   . ARG A 104 ? 0.9607 1.7869 1.7792 -0.1375 0.0404  -0.0834 104 ARG A O   
789   C CB  . ARG A 104 ? 0.9086 1.7601 1.7155 -0.1188 0.0386  -0.0726 104 ARG A CB  
790   C CG  . ARG A 104 ? 0.9255 1.7971 1.7390 -0.1125 0.0359  -0.0704 104 ARG A CG  
791   C CD  . ARG A 104 ? 0.9052 1.7742 1.6981 -0.1030 0.0318  -0.0664 104 ARG A CD  
792   N NE  . ARG A 104 ? 1.0269 1.9000 1.8126 -0.1005 0.0207  -0.0724 104 ARG A NE  
793   C CZ  . ARG A 104 ? 1.0324 1.9237 1.8215 -0.0958 0.0118  -0.0749 104 ARG A CZ  
794   N NH1 . ARG A 104 ? 1.0275 1.9344 1.8278 -0.0928 0.0123  -0.0720 104 ARG A NH1 
795   N NH2 . ARG A 104 ? 0.9819 1.8757 1.7629 -0.0939 0.0025  -0.0805 104 ARG A NH2 
796   N N   . ILE A 105 ? 0.8636 1.6740 1.6704 -0.1356 0.0578  -0.0687 105 ILE A N   
797   C CA  . ILE A 105 ? 0.8387 1.6258 1.6353 -0.1404 0.0610  -0.0683 105 ILE A CA  
798   C C   . ILE A 105 ? 0.8652 1.6516 1.6809 -0.1511 0.0647  -0.0722 105 ILE A C   
799   O O   . ILE A 105 ? 0.8640 1.6412 1.6805 -0.1558 0.0608  -0.0776 105 ILE A O   
800   C CB  . ILE A 105 ? 0.7857 1.5536 1.5632 -0.1376 0.0702  -0.0588 105 ILE A CB  
801   C CG1 . ILE A 105 ? 0.7396 1.5101 1.5004 -0.1272 0.0666  -0.0551 105 ILE A CG1 
802   C CG2 . ILE A 105 ? 0.7296 1.4727 1.4945 -0.1414 0.0721  -0.0581 105 ILE A CG2 
803   C CD1 . ILE A 105 ? 0.7084 1.4618 1.4510 -0.1240 0.0750  -0.0461 105 ILE A CD1 
804   N N   . MET A 106 ? 0.8572 1.6533 1.6893 -0.1552 0.0726  -0.0697 106 MET A N   
805   C CA  . MET A 106 ? 0.8381 1.6362 1.6912 -0.1658 0.0768  -0.0731 106 MET A CA  
806   C C   . MET A 106 ? 0.8780 1.6995 1.7539 -0.1683 0.0678  -0.0823 106 MET A C   
807   O O   . MET A 106 ? 0.8679 1.6997 1.7663 -0.1756 0.0718  -0.0845 106 MET A O   
808   C CB  . MET A 106 ? 0.8573 1.6545 1.7176 -0.1695 0.0903  -0.0661 106 MET A CB  
809   C CG  . MET A 106 ? 0.8946 1.6656 1.7349 -0.1705 0.1002  -0.0579 106 MET A CG  
810   S SD  . MET A 106 ? 0.8755 1.6242 1.7158 -0.1810 0.1023  -0.0600 106 MET A SD  
811   C CE  . MET A 106 ? 0.8829 1.6020 1.6901 -0.1760 0.1061  -0.0516 106 MET A CE  
812   N N   . GLU A 107 ? 1.0617 1.8921 1.9323 -0.1623 0.0558  -0.0878 107 GLU A N   
813   C CA  . GLU A 107 ? 1.0646 1.9178 1.9550 -0.1639 0.0463  -0.0966 107 GLU A CA  
814   C C   . GLU A 107 ? 1.0668 1.9160 1.9699 -0.1732 0.0430  -0.1048 107 GLU A C   
815   O O   . GLU A 107 ? 1.0538 1.9203 1.9799 -0.1783 0.0393  -0.1112 107 GLU A O   
816   C CB  . GLU A 107 ? 1.0934 1.9565 1.9721 -0.1545 0.0348  -0.0995 107 GLU A CB  
817   C CG  . GLU A 107 ? 1.2440 2.1322 2.1410 -0.1546 0.0245  -0.1075 107 GLU A CG  
818   C CD  . GLU A 107 ? 1.3253 2.2237 2.2094 -0.1447 0.0146  -0.1085 107 GLU A CD  
819   O OE1 . GLU A 107 ? 1.3226 2.2230 2.1968 -0.1374 0.0175  -0.1012 107 GLU A OE1 
820   O OE2 . GLU A 107 ? 1.3188 2.2230 2.2023 -0.1444 0.0040  -0.1166 107 GLU A OE2 
821   N N   . GLU A 108 ? 0.9962 1.8226 1.8853 -0.1756 0.0439  -0.1049 108 GLU A N   
822   C CA  . GLU A 108 ? 0.9795 1.7989 1.8793 -0.1845 0.0411  -0.1124 108 GLU A CA  
823   C C   . GLU A 108 ? 0.9715 1.7751 1.8778 -0.1938 0.0531  -0.1077 108 GLU A C   
824   O O   . GLU A 108 ? 0.9858 1.7761 1.8955 -0.2010 0.0525  -0.1118 108 GLU A O   
825   C CB  . GLU A 108 ? 1.0473 1.8519 1.9285 -0.1811 0.0334  -0.1166 108 GLU A CB  
826   C CG  . GLU A 108 ? 1.0927 1.9120 1.9666 -0.1726 0.0216  -0.1219 108 GLU A CG  
827   C CD  . GLU A 108 ? 1.0680 1.8730 1.9246 -0.1695 0.0148  -0.1265 108 GLU A CD  
828   O OE1 . GLU A 108 ? 1.0550 1.8370 1.8975 -0.1699 0.0202  -0.1220 108 GLU A OE1 
829   O OE2 . GLU A 108 ? 1.0929 1.9096 1.9499 -0.1665 0.0041  -0.1348 108 GLU A OE2 
830   N N   . LYS A 109 ? 0.8595 1.6646 1.7679 -0.1939 0.0639  -0.0993 109 LYS A N   
831   C CA  . LYS A 109 ? 0.7690 1.5586 1.6806 -0.2020 0.0767  -0.0933 109 LYS A CA  
832   C C   . LYS A 109 ? 0.8005 1.5610 1.6925 -0.2036 0.0784  -0.0908 109 LYS A C   
833   O O   . LYS A 109 ? 0.8094 1.5583 1.7097 -0.2127 0.0805  -0.0932 109 LYS A O   
834   C CB  . LYS A 109 ? 0.6947 1.4957 1.6355 -0.2129 0.0789  -0.0985 109 LYS A CB  
835   C CG  . LYS A 109 ? 0.6275 1.4540 1.5889 -0.2127 0.0819  -0.0981 109 LYS A CG  
836   C CD  . LYS A 109 ? 0.5498 1.3882 1.5413 -0.2238 0.0828  -0.1044 109 LYS A CD  
837   C CE  . LYS A 109 ? 0.5483 1.3660 1.5419 -0.2343 0.0940  -0.1006 109 LYS A CE  
838   N NZ  . LYS A 109 ? 0.5507 1.3621 1.5392 -0.2346 0.1089  -0.0900 109 LYS A NZ  
839   N N   . PRO A 110 ? 0.7830 1.5308 1.6497 -0.1950 0.0773  -0.0858 110 PRO A N   
840   C CA  . PRO A 110 ? 0.7627 1.4828 1.6110 -0.1960 0.0787  -0.0831 110 PRO A CA  
841   C C   . PRO A 110 ? 0.8196 1.5224 1.6642 -0.2018 0.0923  -0.0739 110 PRO A C   
842   O O   . PRO A 110 ? 0.8047 1.5124 1.6483 -0.2001 0.1009  -0.0670 110 PRO A O   
843   C CB  . PRO A 110 ? 0.7230 1.4386 1.5472 -0.1845 0.0737  -0.0803 110 PRO A CB  
844   C CG  . PRO A 110 ? 0.7577 1.4993 1.5890 -0.1782 0.0675  -0.0835 110 PRO A CG  
845   C CD  . PRO A 110 ? 0.8067 1.5647 1.6606 -0.1839 0.0739  -0.0830 110 PRO A CD  
846   N N   . SER A 111 ? 1.0186 1.7003 1.8607 -0.2086 0.0943  -0.0740 111 SER A N   
847   C CA  . SER A 111 ? 1.0459 1.7092 1.8834 -0.2148 0.1071  -0.0651 111 SER A CA  
848   C C   . SER A 111 ? 1.0602 1.7084 1.8709 -0.2071 0.1119  -0.0555 111 SER A C   
849   O O   . SER A 111 ? 1.0587 1.7058 1.8661 -0.2076 0.1226  -0.0476 111 SER A O   
850   C CB  . SER A 111 ? 1.0760 1.7190 1.9160 -0.2234 0.1071  -0.0673 111 SER A CB  
851   O OG  . SER A 111 ? 1.1176 1.7397 1.9485 -0.2284 0.1190  -0.0577 111 SER A OG  
852   N N   . HIS A 112 ? 0.8878 1.5245 1.6793 -0.1998 0.1041  -0.0563 112 HIS A N   
853   C CA  . HIS A 112 ? 0.8325 1.4544 1.5984 -0.1922 0.1071  -0.0479 112 HIS A CA  
854   C C   . HIS A 112 ? 0.7538 1.3872 1.5098 -0.1812 0.0976  -0.0509 112 HIS A C   
855   O O   . HIS A 112 ? 0.7413 1.3848 1.5038 -0.1792 0.0872  -0.0596 112 HIS A O   
856   C CB  . HIS A 112 ? 0.8745 1.4668 1.6241 -0.1942 0.1079  -0.0445 112 HIS A CB  
857   C CG  . HIS A 112 ? 0.9177 1.4971 1.6769 -0.2056 0.1162  -0.0420 112 HIS A CG  
858   N ND1 . HIS A 112 ? 0.9541 1.5299 1.7137 -0.2104 0.1291  -0.0337 112 HIS A ND1 
859   C CD2 . HIS A 112 ? 0.9183 1.4877 1.6874 -0.2133 0.1137  -0.0466 112 HIS A CD2 
860   C CE1 . HIS A 112 ? 0.9858 1.5498 1.7548 -0.2208 0.1344  -0.0330 112 HIS A CE1 
861   N NE2 . HIS A 112 ? 0.9373 1.4969 1.7124 -0.2228 0.1251  -0.0407 112 HIS A NE2 
862   N N   . VAL A 113 ? 0.7476 1.3792 1.4876 -0.1741 0.1014  -0.0438 113 VAL A N   
863   C CA  . VAL A 113 ? 0.6875 1.3288 1.4169 -0.1636 0.0937  -0.0451 113 VAL A CA  
864   C C   . VAL A 113 ? 0.6539 1.2736 1.3574 -0.1577 0.0938  -0.0391 113 VAL A C   
865   O O   . VAL A 113 ? 0.6646 1.2702 1.3566 -0.1584 0.1026  -0.0307 113 VAL A O   
866   C CB  . VAL A 113 ? 0.6653 1.3275 1.4014 -0.1598 0.0971  -0.0428 113 VAL A CB  
867   C CG1 . VAL A 113 ? 0.7570 1.4123 1.4913 -0.1633 0.1103  -0.0343 113 VAL A CG1 
868   C CG2 . VAL A 113 ? 0.6358 1.3027 1.3564 -0.1489 0.0910  -0.0416 113 VAL A CG2 
869   N N   . PHE A 114 ? 0.6340 1.2513 1.3284 -0.1518 0.0839  -0.0435 114 PHE A N   
870   C CA  . PHE A 114 ? 0.6527 1.2518 1.3238 -0.1453 0.0824  -0.0388 114 PHE A CA  
871   C C   . PHE A 114 ? 0.6508 1.2602 1.3118 -0.1365 0.0819  -0.0351 114 PHE A C   
872   O O   . PHE A 114 ? 0.6398 1.2701 1.3090 -0.1328 0.0768  -0.0395 114 PHE A O   
873   C CB  . PHE A 114 ? 0.6755 1.2680 1.3427 -0.1430 0.0723  -0.0457 114 PHE A CB  
874   C CG  . PHE A 114 ? 0.6853 1.2594 1.3557 -0.1503 0.0731  -0.0474 114 PHE A CG  
875   C CD1 . PHE A 114 ? 0.6925 1.2525 1.3635 -0.1575 0.0827  -0.0409 114 PHE A CD1 
876   C CD2 . PHE A 114 ? 0.7676 1.3385 1.4406 -0.1501 0.0642  -0.0556 114 PHE A CD2 
877   C CE1 . PHE A 114 ? 0.7247 1.2671 1.3988 -0.1644 0.0833  -0.0421 114 PHE A CE1 
878   C CE2 . PHE A 114 ? 0.8011 1.3544 1.4776 -0.1567 0.0647  -0.0573 114 PHE A CE2 
879   C CZ  . PHE A 114 ? 0.7781 1.3169 1.4552 -0.1640 0.0741  -0.0504 114 PHE A CZ  
880   N N   . LEU A 115 ? 0.6704 1.2644 1.3131 -0.1332 0.0871  -0.0269 115 LEU A N   
881   C CA  . LEU A 115 ? 0.6804 1.2806 1.3114 -0.1248 0.0868  -0.0229 115 LEU A CA  
882   C C   . LEU A 115 ? 0.7090 1.2886 1.3175 -0.1196 0.0848  -0.0186 115 LEU A C   
883   O O   . LEU A 115 ? 0.7343 1.2948 1.3316 -0.1219 0.0912  -0.0122 115 LEU A O   
884   C CB  . LEU A 115 ? 0.6921 1.2983 1.3260 -0.1261 0.0968  -0.0169 115 LEU A CB  
885   C CG  . LEU A 115 ? 0.7010 1.3158 1.3256 -0.1179 0.0968  -0.0132 115 LEU A CG  
886   C CD1 . LEU A 115 ? 0.8130 1.4469 1.4526 -0.1192 0.1024  -0.0127 115 LEU A CD1 
887   C CD2 . LEU A 115 ? 0.7603 1.3549 1.3627 -0.1145 0.1014  -0.0054 115 LEU A CD2 
888   N N   . LEU A 116 ? 0.7049 1.2886 1.3069 -0.1127 0.0760  -0.0222 116 LEU A N   
889   C CA  . LEU A 116 ? 0.7182 1.2851 1.3004 -0.1070 0.0730  -0.0189 116 LEU A CA  
890   C C   . LEU A 116 ? 0.6948 1.2738 1.2701 -0.0985 0.0688  -0.0185 116 LEU A C   
891   O O   . LEU A 116 ? 0.6471 1.2469 1.2331 -0.0968 0.0658  -0.0225 116 LEU A O   
892   C CB  . LEU A 116 ? 0.7678 1.3237 1.3486 -0.1075 0.0659  -0.0243 116 LEU A CB  
893   C CG  . LEU A 116 ? 0.7513 1.3235 1.3460 -0.1075 0.0578  -0.0342 116 LEU A CG  
894   C CD1 . LEU A 116 ? 0.7246 1.3052 1.3116 -0.0989 0.0501  -0.0371 116 LEU A CD1 
895   C CD2 . LEU A 116 ? 0.7642 1.3244 1.3645 -0.1128 0.0551  -0.0394 116 LEU A CD2 
896   N N   . ASN A 117 ? 0.6929 1.2582 1.2501 -0.0932 0.0685  -0.0136 117 ASN A N   
897   C CA  . ASN A 117 ? 0.6684 1.2428 1.2178 -0.0855 0.0652  -0.0122 117 ASN A CA  
898   C C   . ASN A 117 ? 0.6671 1.2439 1.2136 -0.0805 0.0556  -0.0178 117 ASN A C   
899   O O   . ASN A 117 ? 0.6603 1.2275 1.2069 -0.0822 0.0518  -0.0217 117 ASN A O   
900   C CB  . ASN A 117 ? 0.7025 1.2619 1.2343 -0.0824 0.0700  -0.0041 117 ASN A CB  
901   C CG  . ASN A 117 ? 0.7063 1.2766 1.2326 -0.0755 0.0687  -0.0019 117 ASN A CG  
902   O OD1 . ASN A 117 ? 0.6880 1.2780 1.2247 -0.0738 0.0660  -0.0053 117 ASN A OD1 
903   N ND2 . ASN A 117 ? 0.7110 1.2681 1.2206 -0.0716 0.0703  0.0038  117 ASN A ND2 
904   N N   . CYS A 118 ? 0.6657 1.2556 1.2096 -0.0743 0.0520  -0.0181 118 CYS A N   
905   C CA  . CYS A 118 ? 0.6256 1.2202 1.1667 -0.0694 0.0436  -0.0232 118 CYS A CA  
906   C C   . CYS A 118 ? 0.6412 1.2169 1.1667 -0.0656 0.0415  -0.0206 118 CYS A C   
907   O O   . CYS A 118 ? 0.6887 1.2577 1.2135 -0.0652 0.0363  -0.0252 118 CYS A O   
908   C CB  . CYS A 118 ? 0.5964 1.2102 1.1391 -0.0643 0.0411  -0.0235 118 CYS A CB  
909   S SG  . CYS A 118 ? 0.4684 1.0868 1.0040 -0.0573 0.0323  -0.0276 118 CYS A SG  
910   N N   . ASP A 119 ? 0.6818 1.2488 1.1949 -0.0628 0.0451  -0.0135 119 ASP A N   
911   C CA  . ASP A 119 ? 0.7269 1.2775 1.2248 -0.0585 0.0424  -0.0107 119 ASP A CA  
912   C C   . ASP A 119 ? 0.7948 1.3231 1.2863 -0.0625 0.0459  -0.0072 119 ASP A C   
913   O O   . ASP A 119 ? 0.8498 1.3652 1.3300 -0.0625 0.0506  -0.0004 119 ASP A O   
914   C CB  . ASP A 119 ? 0.7264 1.2785 1.2139 -0.0533 0.0439  -0.0051 119 ASP A CB  
915   C CG  . ASP A 119 ? 0.6932 1.2476 1.1816 -0.0559 0.0519  0.0002  119 ASP A CG  
916   O OD1 . ASP A 119 ? 0.6693 1.2245 1.1668 -0.0619 0.0566  -0.0003 119 ASP A OD1 
917   O OD2 . ASP A 119 ? 0.6886 1.2441 1.1691 -0.0521 0.0537  0.0046  119 ASP A OD2 
918   N N   . VAL A 120 ? 0.9270 1.4505 1.4256 -0.0662 0.0433  -0.0122 120 VAL A N   
919   C CA  . VAL A 120 ? 0.9742 1.4763 1.4681 -0.0704 0.0458  -0.0096 120 VAL A CA  
920   C C   . VAL A 120 ? 0.9853 1.4802 1.4807 -0.0692 0.0386  -0.0155 120 VAL A C   
921   O O   . VAL A 120 ? 0.9644 1.4728 1.4708 -0.0690 0.0340  -0.0232 120 VAL A O   
922   C CB  . VAL A 120 ? 0.9761 1.4796 1.4809 -0.0786 0.0527  -0.0089 120 VAL A CB  
923   C CG1 . VAL A 120 ? 1.0185 1.5010 1.5209 -0.0836 0.0541  -0.0077 120 VAL A CG1 
924   C CG2 . VAL A 120 ? 0.9691 1.4758 1.4705 -0.0797 0.0609  -0.0022 120 VAL A CG2 
925   N N   . CYS A 121 ? 0.9169 1.3902 1.4006 -0.0680 0.0374  -0.0121 121 CYS A N   
926   C CA  . CYS A 121 ? 0.9488 1.4129 1.4329 -0.0661 0.0304  -0.0174 121 CYS A CA  
927   C C   . CYS A 121 ? 0.9542 1.3952 1.4346 -0.0708 0.0327  -0.0141 121 CYS A C   
928   O O   . CYS A 121 ? 0.9307 1.3532 1.3979 -0.0681 0.0314  -0.0093 121 CYS A O   
929   C CB  . CYS A 121 ? 0.9594 1.4212 1.4330 -0.0579 0.0247  -0.0170 121 CYS A CB  
930   S SG  . CYS A 121 ? 1.0137 1.5021 1.4931 -0.0525 0.0209  -0.0221 121 CYS A SG  
931   N N   . CYS A 122 ? 0.9733 1.4155 1.4658 -0.0780 0.0357  -0.0169 122 CYS A N   
932   C CA  . CYS A 122 ? 0.9586 1.3798 1.4499 -0.0835 0.0379  -0.0145 122 CYS A CA  
933   C C   . CYS A 122 ? 0.9597 1.3820 1.4642 -0.0858 0.0327  -0.0236 122 CYS A C   
934   O O   . CYS A 122 ? 0.9519 1.3905 1.4646 -0.0826 0.0272  -0.0317 122 CYS A O   
935   C CB  . CYS A 122 ? 0.9264 1.3457 1.4200 -0.0911 0.0476  -0.0086 122 CYS A CB  
936   S SG  . CYS A 122 ? 0.9022 1.3488 1.4162 -0.0962 0.0510  -0.0142 122 CYS A SG  
937   N N   . SER A 123 ? 0.9402 1.3443 1.4462 -0.0914 0.0344  -0.0223 123 SER A N   
938   C CA  . SER A 123 ? 0.9830 1.3855 1.5013 -0.0942 0.0297  -0.0310 123 SER A CA  
939   C C   . SER A 123 ? 1.0687 1.4885 1.6050 -0.1010 0.0323  -0.0367 123 SER A C   
940   O O   . SER A 123 ? 1.0960 1.5201 1.6439 -0.1024 0.0274  -0.0458 123 SER A O   
941   C CB  . SER A 123 ? 1.0396 1.4146 1.5526 -0.0976 0.0302  -0.0271 123 SER A CB  
942   O OG  . SER A 123 ? 1.1035 1.4699 1.6149 -0.1051 0.0391  -0.0193 123 SER A OG  
943   N N   . PHE A 124 ? 1.1131 1.5428 1.6521 -0.1050 0.0396  -0.0320 124 PHE A N   
944   C CA  . PHE A 124 ? 1.1606 1.6079 1.7171 -0.1115 0.0425  -0.0367 124 PHE A CA  
945   C C   . PHE A 124 ? 1.3161 1.7528 1.8840 -0.1196 0.0430  -0.0404 124 PHE A C   
946   O O   . PHE A 124 ? 1.2564 1.7012 1.8364 -0.1205 0.0372  -0.0501 124 PHE A O   
947   C CB  . PHE A 124 ? 1.0769 1.5487 1.6422 -0.1071 0.0363  -0.0455 124 PHE A CB  
948   C CG  . PHE A 124 ? 0.9738 1.4588 1.5307 -0.1004 0.0365  -0.0420 124 PHE A CG  
949   C CD1 . PHE A 124 ? 0.8898 1.3885 1.4504 -0.1024 0.0426  -0.0379 124 PHE A CD1 
950   C CD2 . PHE A 124 ? 0.9444 1.4283 1.4906 -0.0920 0.0307  -0.0429 124 PHE A CD2 
951   C CE1 . PHE A 124 ? 0.8205 1.3306 1.3737 -0.0962 0.0427  -0.0347 124 PHE A CE1 
952   C CE2 . PHE A 124 ? 0.8983 1.3940 1.4373 -0.0862 0.0310  -0.0396 124 PHE A CE2 
953   C CZ  . PHE A 124 ? 0.8387 1.3470 1.3809 -0.0882 0.0369  -0.0355 124 PHE A CZ  
954   N N   . PRO A 125 ? 1.8090 2.2273 2.3732 -0.1257 0.0497  -0.0330 125 PRO A N   
955   C CA  . PRO A 125 ? 1.8292 2.2378 2.4056 -0.1345 0.0512  -0.0358 125 PRO A CA  
956   C C   . PRO A 125 ? 1.8031 2.2281 2.3961 -0.1426 0.0575  -0.0370 125 PRO A C   
957   O O   . PRO A 125 ? 1.8188 2.2348 2.4136 -0.1500 0.0658  -0.0308 125 PRO A O   
958   C CB  . PRO A 125 ? 1.8765 2.2566 2.4384 -0.1365 0.0556  -0.0260 125 PRO A CB  
959   C CG  . PRO A 125 ? 1.8746 2.2526 2.4176 -0.1295 0.0578  -0.0177 125 PRO A CG  
960   C CD  . PRO A 125 ? 1.8267 2.2316 2.3748 -0.1250 0.0565  -0.0215 125 PRO A CD  
961   N N   . LEU A 126 ? 1.4054 1.8554 2.0109 -0.1410 0.0536  -0.0450 126 LEU A N   
962   C CA  . LEU A 126 ? 1.2572 1.7263 1.8783 -0.1471 0.0589  -0.0460 126 LEU A CA  
963   C C   . LEU A 126 ? 1.1776 1.6400 1.8138 -0.1578 0.0623  -0.0481 126 LEU A C   
964   O O   . LEU A 126 ? 1.1251 1.5928 1.7699 -0.1646 0.0705  -0.0442 126 LEU A O   
965   C CB  . LEU A 126 ? 1.1499 1.6457 1.7810 -0.1430 0.0523  -0.0548 126 LEU A CB  
966   C CG  . LEU A 126 ? 1.0966 1.6022 1.7150 -0.1328 0.0488  -0.0534 126 LEU A CG  
967   C CD1 . LEU A 126 ? 0.9750 1.5075 1.6047 -0.1303 0.0434  -0.0615 126 LEU A CD1 
968   C CD2 . LEU A 126 ? 1.0594 1.5621 1.6663 -0.1311 0.0567  -0.0427 126 LEU A CD2 
969   N N   . GLN A 127 ? 1.1813 1.6322 1.8217 -0.1596 0.0564  -0.0545 127 GLN A N   
970   C CA  . GLN A 127 ? 1.1638 1.6076 1.8193 -0.1701 0.0592  -0.0571 127 GLN A CA  
971   C C   . GLN A 127 ? 1.1417 1.5606 1.7888 -0.1758 0.0676  -0.0466 127 GLN A C   
972   O O   . GLN A 127 ? 1.0680 1.4839 1.7276 -0.1856 0.0735  -0.0456 127 GLN A O   
973   C CB  . GLN A 127 ? 1.2000 1.6396 1.8630 -0.1700 0.0498  -0.0679 127 GLN A CB  
974   C CG  . GLN A 127 ? 1.1750 1.6141 1.8580 -0.1807 0.0508  -0.0736 127 GLN A CG  
975   C CD  . GLN A 127 ? 1.2942 1.7334 1.9855 -0.1799 0.0408  -0.0861 127 GLN A CD  
976   O OE1 . GLN A 127 ? 1.2835 1.7272 1.9670 -0.1711 0.0332  -0.0912 127 GLN A OE1 
977   N NE2 . GLN A 127 ? 1.4234 1.8577 2.1307 -0.1891 0.0409  -0.0912 127 GLN A NE2 
978   N N   . GLY A 128 ? 1.2271 1.6284 1.8532 -0.1699 0.0684  -0.0386 128 GLY A N   
979   C CA  . GLY A 128 ? 1.2108 1.5878 1.8261 -0.1746 0.0762  -0.0279 128 GLY A CA  
980   C C   . GLY A 128 ? 1.2183 1.6020 1.8304 -0.1775 0.0871  -0.0191 128 GLY A C   
981   O O   . GLY A 128 ? 1.1796 1.5517 1.7931 -0.1857 0.0959  -0.0127 128 GLY A O   
982   N N   . ILE A 129 ? 1.3558 1.7581 1.9638 -0.1707 0.0868  -0.0188 129 ILE A N   
983   C CA  . ILE A 129 ? 1.3446 1.7550 1.9505 -0.1727 0.0970  -0.0114 129 ILE A CA  
984   C C   . ILE A 129 ? 1.3139 1.7441 1.9432 -0.1809 0.1018  -0.0157 129 ILE A C   
985   O O   . ILE A 129 ? 1.3112 1.7420 1.9433 -0.1868 0.1123  -0.0095 129 ILE A O   
986   C CB  . ILE A 129 ? 1.3231 1.7455 1.9168 -0.1626 0.0947  -0.0097 129 ILE A CB  
987   C CG1 . ILE A 129 ? 1.3110 1.7417 1.9023 -0.1641 0.1052  -0.0025 129 ILE A CG1 
988   C CG2 . ILE A 129 ? 1.3088 1.7548 1.9139 -0.1576 0.0858  -0.0199 129 ILE A CG2 
989   C CD1 . ILE A 129 ? 1.3469 1.7561 1.9269 -0.1696 0.1153  0.0077  129 ILE A CD1 
990   N N   . LEU A 130 ? 1.1706 1.6174 1.8172 -0.1813 0.0942  -0.0265 130 LEU A N   
991   C CA  . LEU A 130 ? 1.0575 1.5230 1.7279 -0.1893 0.0975  -0.0314 130 LEU A CA  
992   C C   . LEU A 130 ? 1.0416 1.4911 1.7199 -0.2007 0.1048  -0.0281 130 LEU A C   
993   O O   . LEU A 130 ? 1.0246 1.4817 1.7139 -0.2078 0.1141  -0.0249 130 LEU A O   
994   C CB  . LEU A 130 ? 0.9933 1.4761 1.6784 -0.1876 0.0867  -0.0439 130 LEU A CB  
995   C CG  . LEU A 130 ? 0.8647 1.3759 1.5725 -0.1912 0.0863  -0.0507 130 LEU A CG  
996   C CD1 . LEU A 130 ? 0.8591 1.3840 1.5745 -0.1871 0.0742  -0.0625 130 LEU A CD1 
997   C CD2 . LEU A 130 ? 0.9696 1.4800 1.6961 -0.2033 0.0933  -0.0509 130 LEU A CD2 
998   N N   . ASP A 131 ? 1.0427 1.4698 1.7159 -0.2025 0.1008  -0.0289 131 ASP A N   
999   C CA  . ASP A 131 ? 0.9872 1.3970 1.6672 -0.2134 0.1074  -0.0256 131 ASP A CA  
1000  C C   . ASP A 131 ? 1.0729 1.4655 1.7370 -0.2158 0.1188  -0.0124 131 ASP A C   
1001  O O   . ASP A 131 ? 1.0834 1.4704 1.7559 -0.2258 0.1282  -0.0081 131 ASP A O   
1002  C CB  . ASP A 131 ? 0.9777 1.3673 1.6558 -0.2139 0.0994  -0.0300 131 ASP A CB  
1003  C CG  . ASP A 131 ? 0.9873 1.3927 1.6786 -0.2107 0.0879  -0.0435 131 ASP A CG  
1004  O OD1 . ASP A 131 ? 0.9585 1.3899 1.6661 -0.2120 0.0871  -0.0497 131 ASP A OD1 
1005  O OD2 . ASP A 131 ? 1.0278 1.4199 1.7129 -0.2067 0.0796  -0.0478 131 ASP A OD2 
1006  N N   . ALA A 132 ? 1.1256 1.5095 1.7666 -0.2070 0.1183  -0.0059 132 ALA A N   
1007  C CA  . ALA A 132 ? 1.1322 1.5015 1.7567 -0.2085 0.1291  0.0064  132 ALA A CA  
1008  C C   . ALA A 132 ? 1.1401 1.5295 1.7737 -0.2118 0.1391  0.0089  132 ALA A C   
1009  O O   . ALA A 132 ? 1.1633 1.5434 1.7932 -0.2182 0.1506  0.0172  132 ALA A O   
1010  C CB  . ALA A 132 ? 1.1587 1.5159 1.7571 -0.1979 0.1251  0.0117  132 ALA A CB  
1011  N N   . HIS A 133 ? 1.2295 1.6463 1.8752 -0.2076 0.1352  0.0019  133 HIS A N   
1012  C CA  . HIS A 133 ? 1.2011 1.6384 1.8574 -0.2101 0.1440  0.0036  133 HIS A CA  
1013  C C   . HIS A 133 ? 1.1874 1.6332 1.8689 -0.2219 0.1498  0.0003  133 HIS A C   
1014  O O   . HIS A 133 ? 1.1792 1.6301 1.8664 -0.2275 0.1613  0.0054  133 HIS A O   
1015  C CB  . HIS A 133 ? 1.1750 1.6382 1.8362 -0.2015 0.1373  -0.0026 133 HIS A CB  
1016  C CG  . HIS A 133 ? 1.1499 1.6355 1.8240 -0.2034 0.1453  -0.0018 133 HIS A CG  
1017  N ND1 . HIS A 133 ? 1.1677 1.6480 1.8346 -0.2062 0.1578  0.0071  133 HIS A ND1 
1018  C CD2 . HIS A 133 ? 1.1128 1.6261 1.8063 -0.2025 0.1423  -0.0090 133 HIS A CD2 
1019  C CE1 . HIS A 133 ? 1.1478 1.6519 1.8301 -0.2069 0.1625  0.0052  133 HIS A CE1 
1020  N NE2 . HIS A 133 ? 1.1154 1.6397 1.8141 -0.2047 0.1530  -0.0043 133 HIS A NE2 
1021  N N   . ARG A 134 ? 1.1143 1.5622 1.8115 -0.2257 0.1419  -0.0085 134 ARG A N   
1022  C CA  . ARG A 134 ? 1.0427 1.4974 1.7644 -0.2374 0.1466  -0.0120 134 ARG A CA  
1023  C C   . ARG A 134 ? 1.0669 1.4985 1.7833 -0.2466 0.1580  -0.0026 134 ARG A C   
1024  O O   . ARG A 134 ? 1.0570 1.4958 1.7896 -0.2560 0.1676  -0.0011 134 ARG A O   
1025  C CB  . ARG A 134 ? 0.9983 1.4557 1.7348 -0.2393 0.1352  -0.0232 134 ARG A CB  
1026  C CG  . ARG A 134 ? 0.9283 1.4137 1.6771 -0.2332 0.1256  -0.0335 134 ARG A CG  
1027  C CD  . ARG A 134 ? 0.8985 1.3833 1.6575 -0.2342 0.1140  -0.0445 134 ARG A CD  
1028  N NE  . ARG A 134 ? 0.9075 1.4204 1.6807 -0.2303 0.1056  -0.0547 134 ARG A NE  
1029  C CZ  . ARG A 134 ? 0.9298 1.4471 1.7098 -0.2286 0.0942  -0.0654 134 ARG A CZ  
1030  N NH1 . ARG A 134 ? 0.9610 1.4567 1.7358 -0.2303 0.0898  -0.0676 134 ARG A NH1 
1031  N NH2 . ARG A 134 ? 0.8847 1.4280 1.6763 -0.2250 0.0871  -0.0738 134 ARG A NH2 
1032  N N   . ARG A 135 ? 1.2416 1.6452 1.9354 -0.2441 0.1571  0.0038  135 ARG A N   
1033  C CA  . ARG A 135 ? 1.2769 1.6566 1.9620 -0.2522 0.1678  0.0140  135 ARG A CA  
1034  C C   . ARG A 135 ? 1.2765 1.6571 1.9482 -0.2510 0.1799  0.0239  135 ARG A C   
1035  O O   . ARG A 135 ? 1.2815 1.6591 1.9588 -0.2602 0.1923  0.0297  135 ARG A O   
1036  C CB  . ARG A 135 ? 1.3286 1.6778 1.9939 -0.2494 0.1620  0.0176  135 ARG A CB  
1037  C CG  . ARG A 135 ? 1.4422 1.7642 2.0930 -0.2561 0.1726  0.0296  135 ARG A CG  
1038  C CD  . ARG A 135 ? 1.5571 1.8491 2.1905 -0.2534 0.1655  0.0325  135 ARG A CD  
1039  N NE  . ARG A 135 ? 1.6747 1.9400 2.2889 -0.2577 0.1751  0.0455  135 ARG A NE  
1040  C CZ  . ARG A 135 ? 1.6645 1.9166 2.2516 -0.2505 0.1768  0.0543  135 ARG A CZ  
1041  N NH1 . ARG A 135 ? 1.6409 1.9041 2.2178 -0.2389 0.1696  0.0515  135 ARG A NH1 
1042  N NH2 . ARG A 135 ? 1.7116 1.9392 2.2816 -0.2552 0.1855  0.0659  135 ARG A NH2 
1043  N N   . TYR A 136 ? 1.1628 1.5475 1.8167 -0.2399 0.1767  0.0259  136 TYR A N   
1044  C CA  . TYR A 136 ? 1.1206 1.5070 1.7613 -0.2379 0.1875  0.0344  136 TYR A CA  
1045  C C   . TYR A 136 ? 1.0697 1.4835 1.7324 -0.2422 0.1954  0.0315  136 TYR A C   
1046  O O   . TYR A 136 ? 1.0560 1.4685 1.7174 -0.2475 0.2086  0.0385  136 TYR A O   
1047  C CB  . TYR A 136 ? 1.1370 1.5237 1.7562 -0.2250 0.1811  0.0358  136 TYR A CB  
1048  C CG  . TYR A 136 ? 1.1628 1.5218 1.7573 -0.2200 0.1750  0.0405  136 TYR A CG  
1049  C CD1 . TYR A 136 ? 1.2335 1.5654 1.8183 -0.2266 0.1798  0.0477  136 TYR A CD1 
1050  C CD2 . TYR A 136 ? 1.1449 1.5048 1.7260 -0.2086 0.1645  0.0380  136 TYR A CD2 
1051  C CE1 . TYR A 136 ? 1.3107 1.6172 1.8731 -0.2216 0.1737  0.0521  136 TYR A CE1 
1052  C CE2 . TYR A 136 ? 1.2056 1.5412 1.7653 -0.2037 0.1586  0.0421  136 TYR A CE2 
1053  C CZ  . TYR A 136 ? 1.2912 1.6001 1.8416 -0.2100 0.1630  0.0491  136 TYR A CZ  
1054  O OH  . TYR A 136 ? 1.3766 1.6611 1.9061 -0.2048 0.1566  0.0532  136 TYR A OH  
1055  N N   . GLY A 137 ? 1.0762 1.5151 1.7591 -0.2398 0.1875  0.0213  137 GLY A N   
1056  C CA  . GLY A 137 ? 1.0399 1.5062 1.7430 -0.2420 0.1935  0.0184  137 GLY A CA  
1057  C C   . GLY A 137 ? 1.0229 1.4989 1.7121 -0.2326 0.1962  0.0220  137 GLY A C   
1058  O O   . GLY A 137 ? 1.0818 1.5508 1.7512 -0.2229 0.1890  0.0231  137 GLY A O   
1059  N N   . GLY A 138 ? 0.9679 1.4601 1.6685 -0.2356 0.2067  0.0238  138 GLY A N   
1060  C CA  . GLY A 138 ? 0.9522 1.4550 1.6423 -0.2270 0.2097  0.0266  138 GLY A CA  
1061  C C   . GLY A 138 ? 0.9398 1.4642 1.6373 -0.2179 0.1975  0.0185  138 GLY A C   
1062  O O   . GLY A 138 ? 0.9496 1.4848 1.6635 -0.2189 0.1879  0.0101  138 GLY A O   
1063  N N   . ILE A 139 ? 0.9552 1.4855 1.6395 -0.2088 0.1981  0.0212  139 ILE A N   
1064  C CA  . ILE A 139 ? 0.9216 1.4725 1.6115 -0.1999 0.1878  0.0146  139 ILE A CA  
1065  C C   . ILE A 139 ? 0.9474 1.4865 1.6219 -0.1932 0.1749  0.0123  139 ILE A C   
1066  O O   . ILE A 139 ? 0.9626 1.5100 1.6491 -0.1931 0.1646  0.0045  139 ILE A O   
1067  C CB  . ILE A 139 ? 0.8963 1.4577 1.5787 -0.1928 0.1932  0.0183  139 ILE A CB  
1068  C CG1 . ILE A 139 ? 0.8728 1.4459 1.5712 -0.1994 0.2068  0.0204  139 ILE A CG1 
1069  C CG2 . ILE A 139 ? 0.8775 1.4604 1.5669 -0.1840 0.1824  0.0118  139 ILE A CG2 
1070  C CD1 . ILE A 139 ? 0.8899 1.4888 1.6203 -0.2039 0.2046  0.0124  139 ILE A CD1 
1071  N N   . GLY A 140 ? 0.9824 1.5022 1.6303 -0.1875 0.1753  0.0189  140 GLY A N   
1072  C CA  . GLY A 140 ? 0.9848 1.4944 1.6174 -0.1802 0.1635  0.0170  140 GLY A CA  
1073  C C   . GLY A 140 ? 1.0754 1.5554 1.6899 -0.1825 0.1635  0.0221  140 GLY A C   
1074  O O   . GLY A 140 ? 1.1053 1.5719 1.7198 -0.1908 0.1725  0.0270  140 GLY A O   
1075  N N   . THR A 141 ? 1.0724 1.5419 1.6717 -0.1753 0.1535  0.0211  141 THR A N   
1076  C CA  . THR A 141 ? 1.1157 1.5570 1.6977 -0.1762 0.1518  0.0256  141 THR A CA  
1077  C C   . THR A 141 ? 1.1581 1.5890 1.7172 -0.1660 0.1446  0.0280  141 THR A C   
1078  O O   . THR A 141 ? 1.2223 1.6291 1.7640 -0.1654 0.1434  0.0329  141 THR A O   
1079  C CB  . THR A 141 ? 1.1147 1.5517 1.7099 -0.1813 0.1450  0.0192  141 THR A CB  
1080  O OG1 . THR A 141 ? 1.0841 1.5464 1.7010 -0.1808 0.1388  0.0095  141 THR A OG1 
1081  C CG2 . THR A 141 ? 1.1500 1.5749 1.7528 -0.1927 0.1542  0.0229  141 THR A CG2 
1082  N N   . MET A 142 ? 1.0150 1.4635 1.5745 -0.1579 0.1394  0.0244  142 MET A N   
1083  C CA  . MET A 142 ? 1.0409 1.4820 1.5800 -0.1482 0.1331  0.0266  142 MET A CA  
1084  C C   . MET A 142 ? 1.0678 1.4922 1.5989 -0.1459 0.1234  0.0245  142 MET A C   
1085  O O   . MET A 142 ? 1.0542 1.4794 1.5990 -0.1500 0.1190  0.0186  142 MET A O   
1086  C CB  . MET A 142 ? 1.1007 1.5273 1.6188 -0.1467 0.1414  0.0362  142 MET A CB  
1087  C CG  . MET A 142 ? 1.0943 1.5360 1.6083 -0.1403 0.1436  0.0372  142 MET A CG  
1088  S SD  . MET A 142 ? 1.1514 1.5726 1.6355 -0.1359 0.1491  0.0472  142 MET A SD  
1089  C CE  . MET A 142 ? 1.2113 1.6107 1.6781 -0.1309 0.1376  0.0477  142 MET A CE  
1090  N N   . LEU A 143 ? 1.0918 1.5015 1.6014 -0.1391 0.1200  0.0290  143 LEU A N   
1091  C CA  . LEU A 143 ? 1.1239 1.5141 1.6227 -0.1363 0.1120  0.0287  143 LEU A CA  
1092  C C   . LEU A 143 ? 1.1710 1.5446 1.6447 -0.1302 0.1121  0.0363  143 LEU A C   
1093  O O   . LEU A 143 ? 1.1878 1.5711 1.6547 -0.1246 0.1130  0.0378  143 LEU A O   
1094  C CB  . LEU A 143 ? 1.0837 1.4863 1.5917 -0.1310 0.1003  0.0194  143 LEU A CB  
1095  C CG  . LEU A 143 ? 1.0979 1.4820 1.6010 -0.1299 0.0924  0.0173  143 LEU A CG  
1096  C CD1 . LEU A 143 ? 1.1808 1.5666 1.7028 -0.1374 0.0914  0.0111  143 LEU A CD1 
1097  C CD2 . LEU A 143 ? 1.0267 1.4158 1.5244 -0.1203 0.0818  0.0126  143 LEU A CD2 
1098  N N   . VAL A 144 ? 1.2207 1.5692 1.6809 -0.1311 0.1106  0.0409  144 VAL A N   
1099  C CA  . VAL A 144 ? 1.2674 1.5975 1.7030 -0.1260 0.1106  0.0486  144 VAL A CA  
1100  C C   . VAL A 144 ? 1.3243 1.6378 1.7514 -0.1214 0.1002  0.0474  144 VAL A C   
1101  O O   . VAL A 144 ? 1.2901 1.6026 1.7293 -0.1234 0.0948  0.0417  144 VAL A O   
1102  C CB  . VAL A 144 ? 1.2611 1.5741 1.6847 -0.1323 0.1218  0.0581  144 VAL A CB  
1103  C CG1 . VAL A 144 ? 1.2489 1.5783 1.6775 -0.1348 0.1321  0.0598  144 VAL A CG1 
1104  C CG2 . VAL A 144 ? 1.2430 1.5432 1.6752 -0.1413 0.1246  0.0587  144 VAL A CG2 
1105  N N   . ILE A 145 ? 1.3893 1.6897 1.7956 -0.1149 0.0971  0.0526  145 ILE A N   
1106  C CA  . ILE A 145 ? 1.3844 1.6681 1.7810 -0.1096 0.0873  0.0523  145 ILE A CA  
1107  C C   . ILE A 145 ? 1.4903 1.7538 1.8616 -0.1061 0.0884  0.0615  145 ILE A C   
1108  O O   . ILE A 145 ? 1.4485 1.7183 1.8101 -0.1029 0.0918  0.0646  145 ILE A O   
1109  C CB  . ILE A 145 ? 1.3474 1.6473 1.7519 -0.1018 0.0769  0.0438  145 ILE A CB  
1110  C CG1 . ILE A 145 ? 1.3783 1.6612 1.7732 -0.0959 0.0669  0.0434  145 ILE A CG1 
1111  C CG2 . ILE A 145 ? 1.3353 1.6521 1.7356 -0.0963 0.0779  0.0440  145 ILE A CG2 
1112  C CD1 . ILE A 145 ? 1.3030 1.6013 1.7076 -0.0891 0.0571  0.0343  145 ILE A CD1 
1113  N N   . LYS A 146 ? 1.6956 1.9344 2.0560 -0.1068 0.0854  0.0659  146 LYS A N   
1114  C CA  . LYS A 146 ? 1.7396 1.9570 2.0748 -0.1039 0.0860  0.0751  146 LYS A CA  
1115  C C   . LYS A 146 ? 1.7356 1.9560 2.0611 -0.0936 0.0766  0.0733  146 LYS A C   
1116  O O   . LYS A 146 ? 1.7371 1.9575 2.0680 -0.0886 0.0665  0.0680  146 LYS A O   
1117  C CB  . LYS A 146 ? 1.8267 2.0168 2.1538 -0.1072 0.0845  0.0802  146 LYS A CB  
1118  C CG  . LYS A 146 ? 1.8816 2.0658 2.2167 -0.1180 0.0943  0.0831  146 LYS A CG  
1119  C CD  . LYS A 146 ? 2.0408 2.1960 2.3660 -0.1208 0.0923  0.0889  146 LYS A CD  
1120  C CE  . LYS A 146 ? 2.1453 2.2938 2.4782 -0.1322 0.1026  0.0924  146 LYS A CE  
1121  N NZ  . LYS A 146 ? 2.1484 2.2672 2.4711 -0.1351 0.1008  0.0987  146 LYS A NZ  
1122  N N   . VAL A 147 ? 1.5960 1.8191 1.9078 -0.0904 0.0800  0.0775  147 VAL A N   
1123  C CA  . VAL A 147 ? 1.5424 1.7677 1.8439 -0.0812 0.0718  0.0766  147 VAL A CA  
1124  C C   . VAL A 147 ? 1.5661 1.7701 1.8414 -0.0794 0.0734  0.0860  147 VAL A C   
1125  O O   . VAL A 147 ? 1.6038 1.7952 1.8694 -0.0853 0.0823  0.0929  147 VAL A O   
1126  C CB  . VAL A 147 ? 1.4755 1.7270 1.7861 -0.0780 0.0730  0.0716  147 VAL A CB  
1127  C CG1 . VAL A 147 ? 1.4829 1.7557 1.8185 -0.0804 0.0721  0.0628  147 VAL A CG1 
1128  C CG2 . VAL A 147 ? 1.4723 1.7267 1.7745 -0.0811 0.0839  0.0769  147 VAL A CG2 
1129  N N   . SER A 148 ? 1.5239 1.7240 1.7879 -0.0712 0.0647  0.0860  148 SER A N   
1130  C CA  . SER A 148 ? 1.4986 1.6795 1.7370 -0.0687 0.0648  0.0942  148 SER A CA  
1131  C C   . SER A 148 ? 1.5103 1.6996 1.7408 -0.0702 0.0744  0.0972  148 SER A C   
1132  O O   . SER A 148 ? 1.5014 1.7133 1.7449 -0.0696 0.0770  0.0921  148 SER A O   
1133  C CB  . SER A 148 ? 1.4552 1.6319 1.6855 -0.0595 0.0525  0.0927  148 SER A CB  
1134  O OG  . SER A 148 ? 1.4358 1.6347 1.6747 -0.0546 0.0498  0.0867  148 SER A OG  
1135  N N   . ALA A 149 ? 1.5438 1.7142 1.7524 -0.0721 0.0796  0.1058  149 ALA A N   
1136  C CA  . ALA A 149 ? 1.5007 1.6769 1.6996 -0.0732 0.0889  0.1088  149 ALA A CA  
1137  C C   . ALA A 149 ? 1.5665 1.7531 1.7604 -0.0652 0.0828  0.1057  149 ALA A C   
1138  O O   . ALA A 149 ? 1.5998 1.7999 1.7945 -0.0651 0.0891  0.1047  149 ALA A O   
1139  C CB  . ALA A 149 ? 1.4261 1.5785 1.6009 -0.0767 0.0955  0.1185  149 ALA A CB  
1140  N N   . GLU A 150 ? 1.5528 1.7332 1.7419 -0.0584 0.0705  0.1042  150 GLU A N   
1141  C CA  . GLU A 150 ? 1.5623 1.7537 1.7493 -0.0510 0.0640  0.1006  150 GLU A CA  
1142  C C   . GLU A 150 ? 1.5734 1.7925 1.7837 -0.0504 0.0646  0.0926  150 GLU A C   
1143  O O   . GLU A 150 ? 1.5781 1.8100 1.7881 -0.0469 0.0649  0.0906  150 GLU A O   
1144  C CB  . GLU A 150 ? 1.5595 1.7399 1.7402 -0.0442 0.0506  0.1001  150 GLU A CB  
1145  C CG  . GLU A 150 ? 1.6301 1.8040 1.7917 -0.0379 0.0454  0.1025  150 GLU A CG  
1146  C CD  . GLU A 150 ? 1.6201 1.8161 1.7908 -0.0341 0.0444  0.0968  150 GLU A CD  
1147  O OE1 . GLU A 150 ? 1.5556 1.7702 1.7474 -0.0332 0.0417  0.0901  150 GLU A OE1 
1148  O OE2 . GLU A 150 ? 1.6719 1.8664 1.8285 -0.0320 0.0463  0.0992  150 GLU A OE2 
1149  N N   . ALA A 151 ? 1.6386 1.8668 1.8689 -0.0539 0.0647  0.0881  151 ALA A N   
1150  C CA  . ALA A 151 ? 1.6954 1.9497 1.9478 -0.0541 0.0659  0.0808  151 ALA A CA  
1151  C C   . ALA A 151 ? 1.7334 1.9969 1.9915 -0.0606 0.0785  0.0822  151 ALA A C   
1152  O O   . ALA A 151 ? 1.7114 1.9814 1.9847 -0.0664 0.0832  0.0801  151 ALA A O   
1153  C CB  . ALA A 151 ? 1.6460 1.9058 1.9166 -0.0547 0.0599  0.0749  151 ALA A CB  
1154  N N   . ALA A 152 ? 1.7897 2.0539 2.0356 -0.0593 0.0838  0.0854  152 ALA A N   
1155  C CA  . ALA A 152 ? 1.7908 2.0635 2.0406 -0.0646 0.0961  0.0869  152 ALA A CA  
1156  C C   . ALA A 152 ? 1.8379 2.1296 2.0926 -0.0611 0.0982  0.0838  152 ALA A C   
1157  O O   . ALA A 152 ? 1.8078 2.1121 2.0724 -0.0650 0.1073  0.0831  152 ALA A O   
1158  C CB  . ALA A 152 ? 1.7949 2.0468 2.0234 -0.0681 0.1041  0.0951  152 ALA A CB  
1159  N N   . SER A 153 ? 1.8791 2.1733 2.1278 -0.0540 0.0901  0.0821  153 SER A N   
1160  C CA  . SER A 153 ? 1.8669 2.1789 2.1210 -0.0506 0.0915  0.0791  153 SER A CA  
1161  C C   . SER A 153 ? 1.8623 2.1980 2.1413 -0.0511 0.0902  0.0725  153 SER A C   
1162  O O   . SER A 153 ? 1.8229 2.1750 2.1105 -0.0507 0.0947  0.0705  153 SER A O   
1163  C CB  . SER A 153 ? 1.8319 2.1394 2.0733 -0.0433 0.0828  0.0790  153 SER A CB  
1164  O OG  . SER A 153 ? 1.8042 2.1124 2.0519 -0.0399 0.0719  0.0755  153 SER A OG  
1165  N N   . GLN A 154 ? 2.0833 2.4208 2.3737 -0.0517 0.0839  0.0690  154 GLN A N   
1166  C CA  . GLN A 154 ? 2.0482 2.4076 2.3611 -0.0521 0.0819  0.0625  154 GLN A CA  
1167  C C   . GLN A 154 ? 2.0104 2.3815 2.3364 -0.0582 0.0918  0.0620  154 GLN A C   
1168  O O   . GLN A 154 ? 1.9652 2.3566 2.3056 -0.0574 0.0929  0.0581  154 GLN A O   
1169  C CB  . GLN A 154 ? 2.0649 2.4215 2.3858 -0.0521 0.0739  0.0588  154 GLN A CB  
1170  C CG  . GLN A 154 ? 2.0919 2.4260 2.4028 -0.0556 0.0745  0.0630  154 GLN A CG  
1171  C CD  . GLN A 154 ? 2.1350 2.4506 2.4272 -0.0505 0.0672  0.0663  154 GLN A CD  
1172  O OE1 . GLN A 154 ? 2.1574 2.4621 2.4318 -0.0490 0.0697  0.0714  154 GLN A OE1 
1173  N NE2 . GLN A 154 ? 2.1785 2.4908 2.4747 -0.0476 0.0579  0.0630  154 GLN A NE2 
1174  N N   . PHE A 155 ? 1.7368 2.0954 2.0586 -0.0643 0.0991  0.0659  155 PHE A N   
1175  C CA  . PHE A 155 ? 1.6167 1.9859 1.9515 -0.0705 0.1091  0.0657  155 PHE A CA  
1176  C C   . PHE A 155 ? 1.6124 1.9720 1.9329 -0.0727 0.1195  0.0717  155 PHE A C   
1177  O O   . PHE A 155 ? 1.5816 1.9517 1.9022 -0.0705 0.1239  0.0716  155 PHE A O   
1178  C CB  . PHE A 155 ? 1.5904 1.9559 1.9366 -0.0770 0.1098  0.0643  155 PHE A CB  
1179  C CG  . PHE A 155 ? 1.5362 1.9059 1.8912 -0.0845 0.1213  0.0660  155 PHE A CG  
1180  C CD1 . PHE A 155 ? 1.4988 1.8905 1.8704 -0.0856 0.1261  0.0626  155 PHE A CD1 
1181  C CD2 . PHE A 155 ? 1.5138 1.8652 1.8606 -0.0906 0.1275  0.0712  155 PHE A CD2 
1182  C CE1 . PHE A 155 ? 1.4780 1.8741 1.8588 -0.0925 0.1368  0.0639  155 PHE A CE1 
1183  C CE2 . PHE A 155 ? 1.4905 1.8459 1.8459 -0.0979 0.1385  0.0728  155 PHE A CE2 
1184  C CZ  . PHE A 155 ? 1.4835 1.8616 1.8563 -0.0988 0.1432  0.0690  155 PHE A CZ  
1185  N N   . GLY A 156 ? 1.6639 2.0035 1.9718 -0.0769 0.1236  0.0771  156 GLY A N   
1186  C CA  . GLY A 156 ? 1.6735 2.0038 1.9686 -0.0803 0.1348  0.0828  156 GLY A CA  
1187  C C   . GLY A 156 ? 1.6672 1.9815 1.9591 -0.0878 0.1403  0.0872  156 GLY A C   
1188  O O   . GLY A 156 ? 1.6646 1.9643 1.9512 -0.0879 0.1336  0.0883  156 GLY A O   
1189  N N   . GLU A 157 ? 1.6911 2.0087 1.9875 -0.0940 0.1526  0.0894  157 GLU A N   
1190  C CA  . GLU A 157 ? 1.6820 1.9840 1.9740 -0.1018 0.1600  0.0945  157 GLU A CA  
1191  C C   . GLU A 157 ? 1.4916 1.8076 1.8094 -0.1088 0.1639  0.0906  157 GLU A C   
1192  O O   . GLU A 157 ? 1.4651 1.8038 1.8017 -0.1089 0.1664  0.0856  157 GLU A O   
1193  C CB  . GLU A 157 ? 1.7920 2.0846 2.0670 -0.1043 0.1722  0.1008  157 GLU A CB  
1194  N N   . LEU A 158 ? 1.4371 1.7393 1.7558 -0.1147 0.1642  0.0929  158 LEU A N   
1195  C CA  . LEU A 158 ? 1.4025 1.7149 1.7445 -0.1225 0.1685  0.0898  158 LEU A CA  
1196  C C   . LEU A 158 ? 1.4116 1.7013 1.7446 -0.1299 0.1737  0.0962  158 LEU A C   
1197  O O   . LEU A 158 ? 1.4473 1.7177 1.7677 -0.1282 0.1663  0.0987  158 LEU A O   
1198  C CB  . LEU A 158 ? 1.3770 1.7028 1.7383 -0.1203 0.1573  0.0817  158 LEU A CB  
1199  C CG  . LEU A 158 ? 1.3324 1.6763 1.7214 -0.1268 0.1604  0.0761  158 LEU A CG  
1200  C CD1 . LEU A 158 ? 1.3367 1.6994 1.7422 -0.1220 0.1496  0.0675  158 LEU A CD1 
1201  C CD2 . LEU A 158 ? 1.3003 1.6295 1.6934 -0.1352 0.1629  0.0783  158 LEU A CD2 
1202  N N   . ILE A 159 ? 1.4096 1.7019 1.7499 -0.1380 0.1863  0.0987  159 ILE A N   
1203  C CA  . ILE A 159 ? 1.4138 1.6850 1.7451 -0.1459 0.1936  0.1058  159 ILE A CA  
1204  C C   . ILE A 159 ? 1.3542 1.6338 1.7112 -0.1544 0.1959  0.1020  159 ILE A C   
1205  O O   . ILE A 159 ? 1.3421 1.6447 1.7211 -0.1571 0.2005  0.0968  159 ILE A O   
1206  C CB  . ILE A 159 ? 1.4482 1.7134 1.7647 -0.1491 0.2077  0.1127  159 ILE A CB  
1207  C CG1 . ILE A 159 ? 1.4842 1.7450 1.7778 -0.1403 0.2053  0.1149  159 ILE A CG1 
1208  C CG2 . ILE A 159 ? 1.4125 1.6527 1.7155 -0.1567 0.2145  0.1211  159 ILE A CG2 
1209  C CD1 . ILE A 159 ? 1.5240 1.7599 1.7924 -0.1357 0.1964  0.1198  159 ILE A CD1 
1210  N N   . ALA A 160 ? 1.3755 1.6365 1.7300 -0.1585 0.1923  0.1043  160 ALA A N   
1211  C CA  . ALA A 160 ? 1.3562 1.6221 1.7338 -0.1670 0.1940  0.1009  160 ALA A CA  
1212  C C   . ALA A 160 ? 1.3857 1.6244 1.7517 -0.1740 0.1980  0.1087  160 ALA A C   
1213  O O   . ALA A 160 ? 1.3781 1.5952 1.7255 -0.1702 0.1906  0.1125  160 ALA A O   
1214  C CB  . ALA A 160 ? 1.3300 1.6072 1.7248 -0.1632 0.1805  0.0917  160 ALA A CB  
1215  N N   . ASP A 161 ? 1.3903 1.6301 1.7678 -0.1844 0.2097  0.1110  161 ASP A N   
1216  C CA  . ASP A 161 ? 1.3747 1.5893 1.7428 -0.1924 0.2151  0.1188  161 ASP A CA  
1217  C C   . ASP A 161 ? 1.3572 1.5648 1.7388 -0.1949 0.2055  0.1145  161 ASP A C   
1218  O O   . ASP A 161 ? 1.3309 1.5551 1.7392 -0.1999 0.2054  0.1074  161 ASP A O   
1219  C CB  . ASP A 161 ? 1.3278 1.5476 1.7054 -0.2029 0.2316  0.1224  161 ASP A CB  
1220  N N   . PRO A 162 ? 1.3014 1.4844 1.6653 -0.1915 0.1971  0.1185  162 PRO A N   
1221  C CA  . PRO A 162 ? 1.2617 1.4391 1.6384 -0.1921 0.1862  0.1131  162 PRO A CA  
1222  C C   . PRO A 162 ? 1.2221 1.3936 1.6155 -0.2040 0.1925  0.1138  162 PRO A C   
1223  O O   . PRO A 162 ? 1.2012 1.3719 1.6097 -0.2052 0.1842  0.1076  162 PRO A O   
1224  C CB  . PRO A 162 ? 1.2591 1.4096 1.6100 -0.1855 0.1775  0.1190  162 PRO A CB  
1225  C CG  . PRO A 162 ? 1.2751 1.4098 1.6006 -0.1872 0.1878  0.1302  162 PRO A CG  
1226  C CD  . PRO A 162 ? 1.2989 1.4576 1.6305 -0.1873 0.1973  0.1282  162 PRO A CD  
1227  N N   . ASP A 163 ? 1.2070 1.3743 1.5984 -0.2129 0.2070  0.1208  163 ASP A N   
1228  C CA  . ASP A 163 ? 1.1923 1.3546 1.6008 -0.2249 0.2136  0.1214  163 ASP A CA  
1229  C C   . ASP A 163 ? 1.1833 1.3754 1.6251 -0.2291 0.2146  0.1109  163 ASP A C   
1230  O O   . ASP A 163 ? 1.1126 1.3062 1.5738 -0.2334 0.2091  0.1048  163 ASP A O   
1231  C CB  . ASP A 163 ? 1.1854 1.3335 1.5805 -0.2332 0.2293  0.1327  163 ASP A CB  
1232  C CG  . ASP A 163 ? 1.2006 1.3136 1.5741 -0.2358 0.2284  0.1426  163 ASP A CG  
1233  O OD1 . ASP A 163 ? 1.1826 1.2830 1.5558 -0.2323 0.2160  0.1400  163 ASP A OD1 
1234  O OD2 . ASP A 163 ? 1.2871 1.3851 1.6437 -0.2412 0.2403  0.1530  163 ASP A OD2 
1235  N N   . THR A 164 ? 1.1911 1.4070 1.6397 -0.2276 0.2211  0.1085  164 THR A N   
1236  C CA  . THR A 164 ? 1.2063 1.4522 1.6854 -0.2302 0.2212  0.0985  164 THR A CA  
1237  C C   . THR A 164 ? 1.2417 1.5072 1.7261 -0.2193 0.2089  0.0894  164 THR A C   
1238  O O   . THR A 164 ? 1.2235 1.5144 1.7324 -0.2202 0.2069  0.0806  164 THR A O   
1239  C CB  . THR A 164 ? 1.1894 1.4510 1.6761 -0.2357 0.2365  0.1011  164 THR A CB  
1240  O OG1 . THR A 164 ? 1.1538 1.4176 1.6200 -0.2277 0.2394  0.1051  164 THR A OG1 
1241  C CG2 . THR A 164 ? 1.1198 1.3639 1.6038 -0.2475 0.2496  0.1097  164 THR A CG2 
1242  N N   . LYS A 165 ? 1.3541 1.6084 1.8162 -0.2093 0.2005  0.0915  165 LYS A N   
1243  C CA  . LYS A 165 ? 1.3296 1.6007 1.7941 -0.1987 0.1890  0.0838  165 LYS A CA  
1244  C C   . LYS A 165 ? 1.3163 1.6159 1.7930 -0.1969 0.1943  0.0798  165 LYS A C   
1245  O O   . LYS A 165 ? 1.3251 1.6468 1.8188 -0.1932 0.1872  0.0709  165 LYS A O   
1246  C CB  . LYS A 165 ? 1.3219 1.5975 1.8036 -0.1981 0.1769  0.0745  165 LYS A CB  
1247  C CG  . LYS A 165 ? 1.3631 1.6106 1.8357 -0.2004 0.1719  0.0778  165 LYS A CG  
1248  C CD  . LYS A 165 ? 1.3910 1.6222 1.8392 -0.1901 0.1627  0.0809  165 LYS A CD  
1249  C CE  . LYS A 165 ? 1.3733 1.6193 1.8298 -0.1813 0.1493  0.0709  165 LYS A CE  
1250  N NZ  . LYS A 165 ? 1.3828 1.6214 1.8513 -0.1833 0.1406  0.0649  165 LYS A NZ  
1251  N N   . GLU A 166 ? 1.2558 1.5546 1.7230 -0.1993 0.2067  0.0867  166 GLU A N   
1252  C CA  . GLU A 166 ? 1.2114 1.5356 1.6901 -0.1983 0.2135  0.0838  166 GLU A CA  
1253  C C   . GLU A 166 ? 1.2142 1.5380 1.6713 -0.1885 0.2128  0.0869  166 GLU A C   
1254  O O   . GLU A 166 ? 1.2469 1.5489 1.6781 -0.1868 0.2153  0.0950  166 GLU A O   
1255  C CB  . GLU A 166 ? 1.1946 1.5203 1.6815 -0.2088 0.2294  0.0884  166 GLU A CB  
1256  C CG  . GLU A 166 ? 1.1788 1.5347 1.6900 -0.2106 0.2355  0.0827  166 GLU A CG  
1257  C CD  . GLU A 166 ? 1.1750 1.5381 1.6741 -0.2058 0.2439  0.0863  166 GLU A CD  
1258  O OE1 . GLU A 166 ? 1.1215 1.4686 1.6027 -0.2089 0.2547  0.0948  166 GLU A OE1 
1259  O OE2 . GLU A 166 ? 1.1951 1.5795 1.7026 -0.1989 0.2397  0.0807  166 GLU A OE2 
1260  N N   . LEU A 167 ? 1.2149 1.5627 1.6823 -0.1822 0.2090  0.0806  167 LEU A N   
1261  C CA  . LEU A 167 ? 1.2561 1.6053 1.7052 -0.1728 0.2078  0.0826  167 LEU A CA  
1262  C C   . LEU A 167 ? 1.2444 1.5918 1.6840 -0.1758 0.2225  0.0892  167 LEU A C   
1263  O O   . LEU A 167 ? 1.2176 1.5845 1.6746 -0.1791 0.2308  0.0866  167 LEU A O   
1264  C CB  . LEU A 167 ? 1.2760 1.6513 1.7400 -0.1658 0.2001  0.0743  167 LEU A CB  
1265  C CG  . LEU A 167 ? 1.2470 1.6246 1.6936 -0.1562 0.1986  0.0760  167 LEU A CG  
1266  C CD1 . LEU A 167 ? 1.2520 1.6361 1.6984 -0.1474 0.1841  0.0703  167 LEU A CD1 
1267  C CD2 . LEU A 167 ? 1.2523 1.6503 1.7090 -0.1562 0.2080  0.0749  167 LEU A CD2 
1268  N N   . LEU A 168 ? 1.2566 1.5804 1.6682 -0.1745 0.2258  0.0974  168 LEU A N   
1269  C CA  . LEU A 168 ? 1.2597 1.5793 1.6593 -0.1774 0.2401  0.1039  168 LEU A CA  
1270  C C   . LEU A 168 ? 1.2957 1.6271 1.6869 -0.1689 0.2409  0.1027  168 LEU A C   
1271  O O   . LEU A 168 ? 1.2388 1.5758 1.6283 -0.1710 0.2533  0.1052  168 LEU A O   
1272  C CB  . LEU A 168 ? 1.2825 1.5710 1.6546 -0.1800 0.2436  0.1136  168 LEU A CB  
1273  C CG  . LEU A 168 ? 1.2174 1.4970 1.5956 -0.1920 0.2556  0.1185  168 LEU A CG  
1274  C CD1 . LEU A 168 ? 1.1223 1.4157 1.5073 -0.1963 0.2714  0.1198  168 LEU A CD1 
1275  C CD2 . LEU A 168 ? 1.1942 1.4815 1.5994 -0.1980 0.2505  0.1127  168 LEU A CD2 
1276  N N   . HIS A 169 ? 1.5647 1.8995 1.9504 -0.1595 0.2284  0.0989  169 HIS A N   
1277  C CA  . HIS A 169 ? 1.5496 1.8937 1.9263 -0.1511 0.2281  0.0978  169 HIS A CA  
1278  C C   . HIS A 169 ? 1.5335 1.8865 1.9142 -0.1426 0.2130  0.0917  169 HIS A C   
1279  O O   . HIS A 169 ? 1.5487 1.8919 1.9276 -0.1416 0.2028  0.0907  169 HIS A O   
1280  C CB  . HIS A 169 ? 1.5949 1.9172 1.9397 -0.1486 0.2329  0.1057  169 HIS A CB  
1281  C CG  . HIS A 169 ? 1.6637 1.9909 1.9959 -0.1388 0.2285  0.1043  169 HIS A CG  
1282  N ND1 . HIS A 169 ? 1.7169 2.0329 2.0326 -0.1313 0.2162  0.1045  169 HIS A ND1 
1283  C CD2 . HIS A 169 ? 1.6386 1.9805 1.9730 -0.1354 0.2347  0.1025  169 HIS A CD2 
1284  C CE1 . HIS A 169 ? 1.7136 2.0372 2.0219 -0.1240 0.2151  0.1029  169 HIS A CE1 
1285  N NE2 . HIS A 169 ? 1.6609 1.9998 1.9800 -0.1262 0.2261  0.1017  169 HIS A NE2 
1286  N N   . TYR A 170 ? 1.4677 1.8391 1.8539 -0.1363 0.2118  0.0877  170 TYR A N   
1287  C CA  . TYR A 170 ? 1.4034 1.7853 1.7944 -0.1284 0.1984  0.0820  170 TYR A CA  
1288  C C   . TYR A 170 ? 1.4143 1.8053 1.7977 -0.1207 0.1990  0.0814  170 TYR A C   
1289  O O   . TYR A 170 ? 1.3708 1.7783 1.7661 -0.1214 0.2068  0.0797  170 TYR A O   
1290  C CB  . TYR A 170 ? 1.3017 1.7052 1.7219 -0.1306 0.1939  0.0744  170 TYR A CB  
1291  C CG  . TYR A 170 ? 1.3218 1.7396 1.7476 -0.1224 0.1820  0.0686  170 TYR A CG  
1292  C CD1 . TYR A 170 ? 1.3764 1.7827 1.7894 -0.1169 0.1706  0.0682  170 TYR A CD1 
1293  C CD2 . TYR A 170 ? 1.3146 1.7570 1.7580 -0.1198 0.1824  0.0636  170 TYR A CD2 
1294  C CE1 . TYR A 170 ? 1.3705 1.7898 1.7884 -0.1097 0.1605  0.0631  170 TYR A CE1 
1295  C CE2 . TYR A 170 ? 1.3609 1.8156 1.8083 -0.1124 0.1718  0.0588  170 TYR A CE2 
1296  C CZ  . TYR A 170 ? 1.3610 1.8040 1.7954 -0.1076 0.1612  0.0587  170 TYR A CZ  
1297  O OH  . TYR A 170 ? 1.3360 1.7909 1.7740 -0.1006 0.1512  0.0541  170 TYR A OH  
1298  N N   . THR A 171 ? 1.4446 1.8250 1.8092 -0.1134 0.1905  0.0825  171 THR A N   
1299  C CA  . THR A 171 ? 1.4665 1.8552 1.8246 -0.1054 0.1883  0.0811  171 THR A CA  
1300  C C   . THR A 171 ? 1.4736 1.8676 1.8344 -0.0987 0.1739  0.0766  171 THR A C   
1301  O O   . THR A 171 ? 1.4949 1.8740 1.8454 -0.0975 0.1659  0.0778  171 THR A O   
1302  C CB  . THR A 171 ? 1.5442 1.9141 1.8743 -0.1029 0.1929  0.0872  171 THR A CB  
1303  O OG1 . THR A 171 ? 1.6064 1.9521 1.9185 -0.1047 0.1895  0.0921  171 THR A OG1 
1304  C CG2 . THR A 171 ? 1.5688 1.9409 1.8983 -0.1073 0.2081  0.0901  171 THR A CG2 
1305  N N   . GLU A 172 ? 1.5615 1.9767 1.9365 -0.0943 0.1708  0.0716  172 GLU A N   
1306  C CA  . GLU A 172 ? 1.5826 2.0059 1.9631 -0.0886 0.1579  0.0669  172 GLU A CA  
1307  C C   . GLU A 172 ? 1.6188 2.0269 1.9769 -0.0820 0.1507  0.0694  172 GLU A C   
1308  O O   . GLU A 172 ? 1.6065 2.0036 1.9584 -0.0809 0.1423  0.0693  172 GLU A O   
1309  C CB  . GLU A 172 ? 1.5557 2.0042 1.9545 -0.0853 0.1571  0.0619  172 GLU A CB  
1310  C CG  . GLU A 172 ? 1.5848 2.0420 1.9879 -0.0867 0.1688  0.0632  172 GLU A CG  
1311  C CD  . GLU A 172 ? 1.6065 2.0537 1.9887 -0.0818 0.1720  0.0669  172 GLU A CD  
1312  O OE1 . GLU A 172 ? 1.5936 2.0400 1.9675 -0.0750 0.1637  0.0660  172 GLU A OE1 
1313  O OE2 . GLU A 172 ? 1.5760 2.0159 1.9502 -0.0848 0.1830  0.0707  172 GLU A OE2 
1314  N N   . LYS A 173 ? 1.6067 2.0140 1.9528 -0.0776 0.1538  0.0713  173 LYS A N   
1315  C CA  . LYS A 173 ? 1.5905 1.9859 1.9172 -0.0710 0.1462  0.0729  173 LYS A CA  
1316  C C   . LYS A 173 ? 1.6561 2.0303 1.9579 -0.0714 0.1521  0.0791  173 LYS A C   
1317  O O   . LYS A 173 ? 1.6940 2.0501 1.9788 -0.0696 0.1459  0.0819  173 LYS A O   
1318  C CB  . LYS A 173 ? 1.5316 1.9428 1.8636 -0.0644 0.1422  0.0694  173 LYS A CB  
1319  C CG  . LYS A 173 ? 1.4700 1.8833 1.8023 -0.0590 0.1292  0.0664  173 LYS A CG  
1320  C CD  . LYS A 173 ? 1.4283 1.8489 1.7773 -0.0619 0.1239  0.0626  173 LYS A CD  
1321  C CE  . LYS A 173 ? 1.3993 1.8154 1.7439 -0.0573 0.1118  0.0606  173 LYS A CE  
1322  N NZ  . LYS A 173 ? 1.5569 1.9492 1.8801 -0.0565 0.1094  0.0651  173 LYS A NZ  
1323  N N   . PRO A 174 ? 1.6647 2.0397 1.9628 -0.0736 0.1637  0.0814  174 PRO A N   
1324  C CA  . PRO A 174 ? 1.7529 2.1065 2.0257 -0.0744 0.1695  0.0874  174 PRO A CA  
1325  C C   . PRO A 174 ? 1.8803 2.2169 2.1467 -0.0808 0.1719  0.0918  174 PRO A C   
1326  O O   . PRO A 174 ? 1.8489 2.1876 2.1236 -0.0877 0.1818  0.0932  174 PRO A O   
1327  C CB  . PRO A 174 ? 1.6777 2.0397 1.9528 -0.0759 0.1824  0.0878  174 PRO A CB  
1328  C CG  . PRO A 174 ? 1.6364 2.0232 1.9344 -0.0731 0.1803  0.0819  174 PRO A CG  
1329  C CD  . PRO A 174 ? 1.6276 2.0226 1.9430 -0.0747 0.1718  0.0786  174 PRO A CD  
1330  N N   . GLU A 175 ? 2.1677 2.4872 2.4196 -0.0786 0.1627  0.0939  175 GLU A N   
1331  C CA  . GLU A 175 ? 2.2106 2.5136 2.4578 -0.0841 0.1630  0.0979  175 GLU A CA  
1332  C C   . GLU A 175 ? 2.2888 2.5744 2.5166 -0.0886 0.1743  0.1049  175 GLU A C   
1333  O O   . GLU A 175 ? 2.2902 2.5754 2.5254 -0.0961 0.1838  0.1069  175 GLU A O   
1334  C CB  . GLU A 175 ? 2.2406 2.5304 2.4779 -0.0797 0.1496  0.0981  175 GLU A CB  
1335  C CG  . GLU A 175 ? 2.3008 2.5806 2.5165 -0.0725 0.1437  0.0998  175 GLU A CG  
1336  C CD  . GLU A 175 ? 2.2797 2.5478 2.4881 -0.0682 0.1303  0.0997  175 GLU A CD  
1337  O OE1 . GLU A 175 ? 2.2693 2.5337 2.4866 -0.0712 0.1268  0.0993  175 GLU A OE1 
1338  O OE2 . GLU A 175 ? 2.2639 2.5267 2.4585 -0.0618 0.1234  0.0999  175 GLU A OE2 
1339  N N   . THR A 176 ? 2.5950 2.8665 2.7979 -0.0843 0.1737  0.1085  176 THR A N   
1340  C CA  . THR A 176 ? 2.6318 2.8841 2.8118 -0.0878 0.1832  0.1155  176 THR A CA  
1341  C C   . THR A 176 ? 2.6615 2.8978 2.8389 -0.0946 0.1849  0.1205  176 THR A C   
1342  O O   . THR A 176 ? 2.6590 2.8969 2.8444 -0.1021 0.1960  0.1225  176 THR A O   
1343  C CB  . THR A 176 ? 2.6100 2.8736 2.7944 -0.0907 0.1976  0.1152  176 THR A CB  
1344  O OG1 . THR A 176 ? 2.5662 2.8511 2.7649 -0.0854 0.1951  0.1089  176 THR A OG1 
1345  C CG2 . THR A 176 ? 2.6424 2.8879 2.7976 -0.0904 0.2049  0.1210  176 THR A CG2 
1346  N N   . PHE A 177 ? 2.3162 2.5371 2.4832 -0.0917 0.1734  0.1222  177 PHE A N   
1347  C CA  . PHE A 177 ? 2.1273 2.3313 2.2916 -0.0967 0.1718  0.1265  177 PHE A CA  
1348  C C   . PHE A 177 ? 2.0946 2.3133 2.2880 -0.1008 0.1700  0.1214  177 PHE A C   
1349  O O   . PHE A 177 ? 2.1116 2.3490 2.3246 -0.1047 0.1780  0.1180  177 PHE A O   
1350  C CB  . PHE A 177 ? 2.0268 2.2139 2.1745 -0.1036 0.1845  0.1345  177 PHE A CB  
1351  C CG  . PHE A 177 ? 1.9541 2.1261 2.1034 -0.1102 0.1849  0.1389  177 PHE A CG  
1352  C CD1 . PHE A 177 ? 1.9026 2.0525 2.0355 -0.1077 0.1750  0.1431  177 PHE A CD1 
1353  C CD2 . PHE A 177 ? 1.9282 2.1080 2.0960 -0.1188 0.1949  0.1387  177 PHE A CD2 
1354  C CE1 . PHE A 177 ? 1.8551 1.9902 1.9896 -0.1136 0.1752  0.1472  177 PHE A CE1 
1355  C CE2 . PHE A 177 ? 1.8455 2.0108 2.0153 -0.1252 0.1953  0.1427  177 PHE A CE2 
1356  C CZ  . PHE A 177 ? 1.8278 1.9703 1.9807 -0.1226 0.1855  0.1470  177 PHE A CZ  
1357  N N   . VAL A 178 ? 2.0775 2.2879 2.2741 -0.0998 0.1594  0.1207  178 VAL A N   
1358  C CA  . VAL A 178 ? 1.9860 2.2100 2.2092 -0.1026 0.1557  0.1148  178 VAL A CA  
1359  C C   . VAL A 178 ? 1.9586 2.1652 2.1813 -0.1096 0.1576  0.1192  178 VAL A C   
1360  O O   . VAL A 178 ? 2.0139 2.2000 2.2170 -0.1130 0.1637  0.1271  178 VAL A O   
1361  C CB  . VAL A 178 ? 1.9519 2.1840 2.1827 -0.0950 0.1412  0.1086  178 VAL A CB  
1362  C CG1 . VAL A 178 ? 2.0040 2.2517 2.2343 -0.0883 0.1394  0.1049  178 VAL A CG1 
1363  C CG2 . VAL A 178 ? 1.9306 2.1397 2.1433 -0.0912 0.1311  0.1123  178 VAL A CG2 
1364  N N   . SER A 179 ? 1.8136 2.0278 2.0576 -0.1118 0.1524  0.1140  179 SER A N   
1365  C CA  . SER A 179 ? 1.8324 2.0304 2.0783 -0.1182 0.1529  0.1173  179 SER A CA  
1366  C C   . SER A 179 ? 1.7856 1.9826 2.0418 -0.1148 0.1396  0.1121  179 SER A C   
1367  O O   . SER A 179 ? 1.8119 2.0020 2.0782 -0.1203 0.1393  0.1119  179 SER A O   
1368  C CB  . SER A 179 ? 1.8074 2.0158 2.0725 -0.1279 0.1644  0.1164  179 SER A CB  
1369  O OG  . SER A 179 ? 1.8116 2.0011 2.0751 -0.1349 0.1667  0.1211  179 SER A OG  
1370  N N   . ASP A 180 ? 1.6643 1.8691 1.9197 -0.1061 0.1290  0.1075  180 ASP A N   
1371  C CA  . ASP A 180 ? 1.6266 1.8322 1.8907 -0.1013 0.1159  0.1019  180 ASP A CA  
1372  C C   . ASP A 180 ? 1.5858 1.8135 1.8784 -0.1041 0.1150  0.0932  180 ASP A C   
1373  O O   . ASP A 180 ? 1.5840 1.8161 1.8868 -0.1003 0.1049  0.0872  180 ASP A O   
1374  C CB  . ASP A 180 ? 1.6452 1.8240 1.8973 -0.1020 0.1106  0.1068  180 ASP A CB  
1375  C CG  . ASP A 180 ? 1.6976 1.8753 1.9684 -0.1080 0.1098  0.1035  180 ASP A CG  
1376  O OD1 . ASP A 180 ? 1.6838 1.8683 1.9676 -0.1043 0.1000  0.0965  180 ASP A OD1 
1377  O OD2 . ASP A 180 ? 1.7304 1.8997 2.0024 -0.1165 0.1190  0.1079  180 ASP A OD2 
1378  N N   . LEU A 181 ? 1.5246 1.7675 1.8308 -0.1101 0.1252  0.0919  181 LEU A N   
1379  C CA  . LEU A 181 ? 1.4616 1.7261 1.7947 -0.1131 0.1247  0.0838  181 LEU A CA  
1380  C C   . LEU A 181 ? 1.4373 1.7272 1.7796 -0.1085 0.1247  0.0787  181 LEU A C   
1381  O O   . LEU A 181 ? 1.4099 1.7022 1.7415 -0.1066 0.1304  0.0822  181 LEU A O   
1382  C CB  . LEU A 181 ? 1.4519 1.7166 1.7965 -0.1234 0.1356  0.0857  181 LEU A CB  
1383  C CG  . LEU A 181 ? 1.4789 1.7224 1.8221 -0.1291 0.1347  0.0887  181 LEU A CG  
1384  C CD1 . LEU A 181 ? 1.4448 1.6921 1.8030 -0.1398 0.1456  0.0894  181 LEU A CD1 
1385  C CD2 . LEU A 181 ? 1.5021 1.7463 1.8556 -0.1254 0.1221  0.0817  181 LEU A CD2 
1386  N N   . ILE A 182 ? 1.4409 1.7494 1.8030 -0.1068 0.1182  0.0704  182 ILE A N   
1387  C CA  . ILE A 182 ? 1.4014 1.7340 1.7732 -0.1021 0.1164  0.0651  182 ILE A CA  
1388  C C   . ILE A 182 ? 1.3606 1.7136 1.7584 -0.1057 0.1155  0.0574  182 ILE A C   
1389  O O   . ILE A 182 ? 1.3106 1.6587 1.7179 -0.1099 0.1129  0.0547  182 ILE A O   
1390  C CB  . ILE A 182 ? 1.3619 1.6950 1.7249 -0.0926 0.1054  0.0628  182 ILE A CB  
1391  C CG1 . ILE A 182 ? 1.3200 1.6446 1.6862 -0.0910 0.0953  0.0592  182 ILE A CG1 
1392  C CG2 . ILE A 182 ? 1.4105 1.7280 1.7490 -0.0884 0.1064  0.0697  182 ILE A CG2 
1393  C CD1 . ILE A 182 ? 1.3003 1.6377 1.6712 -0.0833 0.0850  0.0530  182 ILE A CD1 
1394  N N   . ASN A 183 ? 1.4823 1.8581 1.8915 -0.1040 0.1174  0.0537  183 ASN A N   
1395  C CA  . ASN A 183 ? 1.4192 1.8163 1.8524 -0.1063 0.1152  0.0461  183 ASN A CA  
1396  C C   . ASN A 183 ? 1.4012 1.8020 1.8391 -0.1014 0.1031  0.0396  183 ASN A C   
1397  O O   . ASN A 183 ? 1.4159 1.8087 1.8404 -0.0948 0.0963  0.0405  183 ASN A O   
1398  C CB  . ASN A 183 ? 1.4238 1.8439 1.8666 -0.1045 0.1192  0.0441  183 ASN A CB  
1399  C CG  . ASN A 183 ? 1.4575 1.8757 1.8965 -0.1087 0.1317  0.0498  183 ASN A CG  
1400  O OD1 . ASN A 183 ? 1.5384 1.9443 1.9584 -0.1060 0.1352  0.0558  183 ASN A OD1 
1401  N ND2 . ASN A 183 ? 1.3570 1.7877 1.8143 -0.1153 0.1383  0.0478  183 ASN A ND2 
1402  N N   . CYS A 184 ? 1.1938 1.6073 1.6514 -0.1049 0.1004  0.0327  184 CYS A N   
1403  C CA  . CYS A 184 ? 1.0977 1.5185 1.5622 -0.1006 0.0896  0.0254  184 CYS A CA  
1404  C C   . CYS A 184 ? 1.0384 1.4862 1.5193 -0.0987 0.0870  0.0187  184 CYS A C   
1405  O O   . CYS A 184 ? 1.0148 1.4705 1.4986 -0.0937 0.0783  0.0131  184 CYS A O   
1406  C CB  . CYS A 184 ? 1.1016 1.5116 1.5735 -0.1055 0.0865  0.0220  184 CYS A CB  
1407  S SG  . CYS A 184 ? 1.1416 1.5192 1.5931 -0.1046 0.0842  0.0283  184 CYS A SG  
1408  N N   . GLY A 185 ? 1.0992 1.5613 1.5909 -0.1025 0.0942  0.0191  185 GLY A N   
1409  C CA  . GLY A 185 ? 1.1264 1.6140 1.6337 -0.1008 0.0918  0.0133  185 GLY A CA  
1410  C C   . GLY A 185 ? 1.0416 1.5409 1.5694 -0.1063 0.0897  0.0062  185 GLY A C   
1411  O O   . GLY A 185 ? 1.0372 1.5579 1.5794 -0.1065 0.0895  0.0021  185 GLY A O   
1412  N N   . VAL A 186 ? 0.9117 1.3972 1.4412 -0.1107 0.0878  0.0044  186 VAL A N   
1413  C CA  . VAL A 186 ? 0.8539 1.3486 1.4028 -0.1166 0.0857  -0.0028 186 VAL A CA  
1414  C C   . VAL A 186 ? 0.8768 1.3680 1.4342 -0.1257 0.0956  0.0006  186 VAL A C   
1415  O O   . VAL A 186 ? 0.8775 1.3478 1.4262 -0.1298 0.1002  0.0059  186 VAL A O   
1416  C CB  . VAL A 186 ? 0.8044 1.2867 1.3518 -0.1162 0.0778  -0.0074 186 VAL A CB  
1417  C CG1 . VAL A 186 ? 0.8895 1.3451 1.4177 -0.1148 0.0787  -0.0007 186 VAL A CG1 
1418  C CG2 . VAL A 186 ? 0.8421 1.3266 1.4073 -0.1243 0.0779  -0.0131 186 VAL A CG2 
1419  N N   . TYR A 187 ? 0.7989 1.3106 1.3732 -0.1288 0.0991  -0.0021 187 TYR A N   
1420  C CA  . TYR A 187 ? 0.7879 1.3001 1.3725 -0.1373 0.1092  0.0008  187 TYR A CA  
1421  C C   . TYR A 187 ? 0.7294 1.2569 1.3380 -0.1434 0.1068  -0.0071 187 TYR A C   
1422  O O   . TYR A 187 ? 0.6991 1.2424 1.3168 -0.1401 0.0984  -0.0146 187 TYR A O   
1423  C CB  . TYR A 187 ? 0.7895 1.3126 1.3728 -0.1354 0.1171  0.0057  187 TYR A CB  
1424  C CG  . TYR A 187 ? 0.8704 1.3805 1.4305 -0.1290 0.1193  0.0129  187 TYR A CG  
1425  C CD1 . TYR A 187 ? 0.8979 1.4200 1.4551 -0.1240 0.1224  0.0153  187 TYR A CD1 
1426  C CD2 . TYR A 187 ? 0.9735 1.4594 1.5148 -0.1278 0.1177  0.0172  187 TYR A CD2 
1427  C CE1 . TYR A 187 ? 1.0319 1.5422 1.5681 -0.1183 0.1240  0.0214  187 TYR A CE1 
1428  C CE2 . TYR A 187 ? 1.0380 1.5124 1.5582 -0.1219 0.1189  0.0234  187 TYR A CE2 
1429  C CZ  . TYR A 187 ? 1.0779 1.5646 1.5956 -0.1174 0.1221  0.0253  187 TYR A CZ  
1430  O OH  . TYR A 187 ? 1.0939 1.5689 1.5907 -0.1118 0.1231  0.0311  187 TYR A OH  
1431  N N   . VAL A 188 ? 0.7496 1.2724 1.3683 -0.1526 0.1145  -0.0055 188 VAL A N   
1432  C CA  . VAL A 188 ? 0.7379 1.2752 1.3808 -0.1596 0.1136  -0.0126 188 VAL A CA  
1433  C C   . VAL A 188 ? 0.8081 1.3504 1.4621 -0.1671 0.1255  -0.0085 188 VAL A C   
1434  O O   . VAL A 188 ? 0.9098 1.4339 1.5547 -0.1716 0.1341  -0.0013 188 VAL A O   
1435  C CB  . VAL A 188 ? 0.7629 1.2859 1.4095 -0.1647 0.1087  -0.0169 188 VAL A CB  
1436  C CG1 . VAL A 188 ? 0.9294 1.4234 1.5575 -0.1661 0.1128  -0.0092 188 VAL A CG1 
1437  C CG2 . VAL A 188 ? 0.7985 1.3312 1.4691 -0.1746 0.1116  -0.0216 188 VAL A CG2 
1438  N N   . PHE A 189 ? 0.7949 1.3619 1.4682 -0.1682 0.1260  -0.0128 189 PHE A N   
1439  C CA  . PHE A 189 ? 0.8389 1.4143 1.5260 -0.1750 0.1370  -0.0100 189 PHE A CA  
1440  C C   . PHE A 189 ? 0.8817 1.4692 1.5948 -0.1836 0.1357  -0.0172 189 PHE A C   
1441  O O   . PHE A 189 ? 0.8642 1.4524 1.5836 -0.1844 0.1263  -0.0244 189 PHE A O   
1442  C CB  . PHE A 189 ? 0.8241 1.4185 1.5132 -0.1691 0.1399  -0.0084 189 PHE A CB  
1443  C CG  . PHE A 189 ? 0.8115 1.3946 1.4760 -0.1611 0.1418  -0.0015 189 PHE A CG  
1444  C CD1 . PHE A 189 ? 0.8190 1.3899 1.4724 -0.1631 0.1534  0.0067  189 PHE A CD1 
1445  C CD2 . PHE A 189 ? 0.8134 1.3982 1.4660 -0.1518 0.1322  -0.0033 189 PHE A CD2 
1446  C CE1 . PHE A 189 ? 0.8152 1.3755 1.4459 -0.1559 0.1548  0.0127  189 PHE A CE1 
1447  C CE2 . PHE A 189 ? 0.8619 1.4364 1.4928 -0.1448 0.1337  0.0028  189 PHE A CE2 
1448  C CZ  . PHE A 189 ? 0.8941 1.4563 1.5141 -0.1468 0.1448  0.0106  189 PHE A CZ  
1449  N N   . THR A 190 ? 0.9796 1.5771 1.7083 -0.1901 0.1454  -0.0155 190 THR A N   
1450  C CA  . THR A 190 ? 0.9815 1.5956 1.7379 -0.1979 0.1450  -0.0222 190 THR A CA  
1451  C C   . THR A 190 ? 0.9991 1.6422 1.7707 -0.1936 0.1429  -0.0261 190 THR A C   
1452  O O   . THR A 190 ? 0.9674 1.6163 1.7277 -0.1848 0.1418  -0.0234 190 THR A O   
1453  C CB  . THR A 190 ? 1.0359 1.6410 1.8008 -0.2089 0.1576  -0.0176 190 THR A CB  
1454  O OG1 . THR A 190 ? 1.1016 1.7232 1.8950 -0.2169 0.1566  -0.0248 190 THR A OG1 
1455  C CG2 . THR A 190 ? 0.9957 1.6040 1.7557 -0.2077 0.1700  -0.0099 190 THR A CG2 
1456  N N   . SER A 191 ? 0.9382 1.5996 1.7362 -0.1999 0.1419  -0.0325 191 SER A N   
1457  C CA  . SER A 191 ? 0.8775 1.5670 1.6917 -0.1960 0.1395  -0.0363 191 SER A CA  
1458  C C   . SER A 191 ? 0.8861 1.5814 1.7002 -0.1947 0.1513  -0.0294 191 SER A C   
1459  O O   . SER A 191 ? 0.8926 1.6091 1.7160 -0.1894 0.1495  -0.0311 191 SER A O   
1460  C CB  . SER A 191 ? 0.8965 1.6041 1.7399 -0.2036 0.1357  -0.0448 191 SER A CB  
1461  O OG  . SER A 191 ? 0.9773 1.7121 1.8365 -0.1995 0.1327  -0.0483 191 SER A OG  
1462  N N   . ASP A 192 ? 0.9091 1.5862 1.7128 -0.1991 0.1632  -0.0217 192 ASP A N   
1463  C CA  . ASP A 192 ? 0.9070 1.5881 1.7105 -0.1988 0.1759  -0.0154 192 ASP A CA  
1464  C C   . ASP A 192 ? 0.9160 1.5917 1.6959 -0.1881 0.1760  -0.0100 192 ASP A C   
1465  O O   . ASP A 192 ? 0.9310 1.6101 1.7090 -0.1866 0.1860  -0.0051 192 ASP A O   
1466  C CB  . ASP A 192 ? 0.8671 1.5300 1.6680 -0.2084 0.1889  -0.0093 192 ASP A CB  
1467  C CG  . ASP A 192 ? 0.8692 1.5415 1.6787 -0.2109 0.2030  -0.0049 192 ASP A CG  
1468  O OD1 . ASP A 192 ? 0.9315 1.6269 1.7549 -0.2064 0.2021  -0.0079 192 ASP A OD1 
1469  O OD2 . ASP A 192 ? 0.8070 1.4631 1.6089 -0.2171 0.2149  0.0016  192 ASP A OD2 
1470  N N   . ILE A 193 ? 0.9370 1.6045 1.6993 -0.1808 0.1655  -0.0110 193 ILE A N   
1471  C CA  . ILE A 193 ? 0.9894 1.6499 1.7288 -0.1712 0.1657  -0.0057 193 ILE A CA  
1472  C C   . ILE A 193 ? 1.0624 1.7465 1.8113 -0.1643 0.1642  -0.0074 193 ILE A C   
1473  O O   . ILE A 193 ? 1.0776 1.7596 1.8144 -0.1588 0.1698  -0.0022 193 ILE A O   
1474  C CB  . ILE A 193 ? 0.9206 1.5666 1.6401 -0.1655 0.1548  -0.0066 193 ILE A CB  
1475  C CG1 . ILE A 193 ? 0.8804 1.5190 1.5767 -0.1560 0.1549  -0.0011 193 ILE A CG1 
1476  C CG2 . ILE A 193 ? 0.9546 1.6168 1.6867 -0.1631 0.1417  -0.0153 193 ILE A CG2 
1477  C CD1 . ILE A 193 ? 0.9103 1.5326 1.5917 -0.1576 0.1674  0.0073  193 ILE A CD1 
1478  N N   . PHE A 194 ? 1.1606 1.8669 1.9311 -0.1645 0.1566  -0.0147 194 PHE A N   
1479  C CA  . PHE A 194 ? 1.1424 1.8713 1.9229 -0.1578 0.1545  -0.0163 194 PHE A CA  
1480  C C   . PHE A 194 ? 1.1471 1.8846 1.9393 -0.1604 0.1674  -0.0129 194 PHE A C   
1481  O O   . PHE A 194 ? 1.1532 1.9017 1.9453 -0.1536 0.1689  -0.0112 194 PHE A O   
1482  C CB  . PHE A 194 ? 1.0987 1.8490 1.9000 -0.1581 0.1433  -0.0249 194 PHE A CB  
1483  C CG  . PHE A 194 ? 1.0952 1.8403 1.8852 -0.1541 0.1304  -0.0288 194 PHE A CG  
1484  C CD1 . PHE A 194 ? 1.0672 1.8137 1.8418 -0.1441 0.1237  -0.0276 194 PHE A CD1 
1485  C CD2 . PHE A 194 ? 1.0931 1.8320 1.8881 -0.1603 0.1252  -0.0339 194 PHE A CD2 
1486  C CE1 . PHE A 194 ? 1.0475 1.7899 1.8120 -0.1405 0.1124  -0.0314 194 PHE A CE1 
1487  C CE2 . PHE A 194 ? 1.0865 1.8210 1.8712 -0.1564 0.1137  -0.0380 194 PHE A CE2 
1488  C CZ  . PHE A 194 ? 1.0610 1.7976 1.8304 -0.1464 0.1075  -0.0367 194 PHE A CZ  
1489  N N   . ASN A 195 ? 1.0463 1.7788 1.8488 -0.1703 0.1769  -0.0119 195 ASN A N   
1490  C CA  . ASN A 195 ? 1.0575 1.7974 1.8706 -0.1732 0.1904  -0.0085 195 ASN A CA  
1491  C C   . ASN A 195 ? 1.1211 1.8430 1.9092 -0.1692 0.1998  -0.0004 195 ASN A C   
1492  O O   . ASN A 195 ? 1.1286 1.8586 1.9204 -0.1670 0.2088  0.0022  195 ASN A O   
1493  C CB  . ASN A 195 ? 1.0012 1.7407 1.8326 -0.1854 0.1982  -0.0097 195 ASN A CB  
1494  C CG  . ASN A 195 ? 0.9443 1.7005 1.8003 -0.1898 0.1884  -0.0183 195 ASN A CG  
1495  O OD1 . ASN A 195 ? 0.9392 1.7152 1.8063 -0.1841 0.1789  -0.0234 195 ASN A OD1 
1496  N ND2 . ASN A 195 ? 0.8920 1.6399 1.7566 -0.2001 0.1906  -0.0198 195 ASN A ND2 
1497  N N   . ALA A 196 ? 1.2720 1.9696 2.0347 -0.1683 0.1978  0.0035  196 ALA A N   
1498  C CA  . ALA A 196 ? 1.3320 2.0116 2.0692 -0.1643 0.2055  0.0110  196 ALA A CA  
1499  C C   . ALA A 196 ? 1.3492 2.0363 2.0767 -0.1530 0.2009  0.0116  196 ALA A C   
1500  O O   . ALA A 196 ? 1.3510 2.0323 2.0660 -0.1495 0.2093  0.0165  196 ALA A O   
1501  C CB  . ALA A 196 ? 1.3332 1.9853 2.0467 -0.1659 0.2031  0.0147  196 ALA A CB  
1502  N N   . ILE A 197 ? 1.1994 1.8989 1.9322 -0.1473 0.1879  0.0065  197 ILE A N   
1503  C CA  . ILE A 197 ? 1.1924 1.8993 1.9169 -0.1369 0.1833  0.0072  197 ILE A CA  
1504  C C   . ILE A 197 ? 1.2175 1.9466 1.9617 -0.1349 0.1885  0.0059  197 ILE A C   
1505  O O   . ILE A 197 ? 1.3131 2.0438 2.0490 -0.1278 0.1914  0.0087  197 ILE A O   
1506  C CB  . ILE A 197 ? 1.1364 1.8486 1.8589 -0.1316 0.1680  0.0027  197 ILE A CB  
1507  C CG1 . ILE A 197 ? 1.0562 1.7471 1.7615 -0.1338 0.1631  0.0033  197 ILE A CG1 
1508  C CG2 . ILE A 197 ? 1.1728 1.8896 1.8842 -0.1210 0.1635  0.0043  197 ILE A CG2 
1509  C CD1 . ILE A 197 ? 0.9249 1.6198 1.6265 -0.1284 0.1488  -0.0011 197 ILE A CD1 
1510  N N   . GLU A 198 ? 1.1411 1.8875 1.9121 -0.1410 0.1898  0.0014  198 GLU A N   
1511  C CA  . GLU A 198 ? 1.1548 1.9229 1.9466 -0.1394 0.1951  -0.0001 198 GLU A CA  
1512  C C   . GLU A 198 ? 1.2315 1.9922 2.0177 -0.1409 0.2107  0.0053  198 GLU A C   
1513  O O   . GLU A 198 ? 1.2671 2.0401 2.0601 -0.1358 0.2153  0.0058  198 GLU A O   
1514  C CB  . GLU A 198 ? 1.0765 1.8639 1.8988 -0.1465 0.1931  -0.0062 198 GLU A CB  
1515  C CG  . GLU A 198 ? 1.0860 1.8840 1.9155 -0.1444 0.1774  -0.0123 198 GLU A CG  
1516  C CD  . GLU A 198 ? 1.0681 1.8867 1.9284 -0.1509 0.1747  -0.0188 198 GLU A CD  
1517  O OE1 . GLU A 198 ? 1.0723 1.8953 1.9486 -0.1581 0.1854  -0.0185 198 GLU A OE1 
1518  O OE2 . GLU A 198 ? 1.0408 1.8712 1.9092 -0.1488 0.1619  -0.0244 198 GLU A OE2 
1519  N N   . GLU A 199 ? 1.2115 1.9520 1.9851 -0.1477 0.2192  0.0093  199 GLU A N   
1520  C CA  . GLU A 199 ? 1.2501 1.9815 2.0150 -0.1493 0.2344  0.0148  199 GLU A CA  
1521  C C   . GLU A 199 ? 1.3513 2.0670 2.0873 -0.1410 0.2350  0.0197  199 GLU A C   
1522  O O   . GLU A 199 ? 1.4002 2.1076 2.1261 -0.1411 0.2472  0.0241  199 GLU A O   
1523  C CB  . GLU A 199 ? 1.2308 1.9461 1.9926 -0.1602 0.2434  0.0177  199 GLU A CB  
1524  C CG  . GLU A 199 ? 1.1981 1.9295 1.9904 -0.1693 0.2452  0.0130  199 GLU A CG  
1525  C CD  . GLU A 199 ? 1.1966 1.9542 2.0150 -0.1680 0.2504  0.0098  199 GLU A CD  
1526  O OE1 . GLU A 199 ? 1.2892 2.0466 2.1033 -0.1659 0.2621  0.0133  199 GLU A OE1 
1527  O OE2 . GLU A 199 ? 1.1008 1.8792 1.9438 -0.1687 0.2424  0.0035  199 GLU A OE2 
1528  N N   . VAL A 200 ? 1.3770 2.0885 2.0997 -0.1339 0.2225  0.0190  200 VAL A N   
1529  C CA  . VAL A 200 ? 1.4304 2.1302 2.1287 -0.1253 0.2217  0.0228  200 VAL A CA  
1530  C C   . VAL A 200 ? 1.5226 2.2389 2.2269 -0.1159 0.2125  0.0199  200 VAL A C   
1531  O O   . VAL A 200 ? 1.5516 2.2637 2.2421 -0.1087 0.2143  0.0226  200 VAL A O   
1532  C CB  . VAL A 200 ? 1.4144 2.0895 2.0860 -0.1251 0.2162  0.0260  200 VAL A CB  
1533  C CG1 . VAL A 200 ? 1.4058 2.0856 2.0789 -0.1216 0.2007  0.0219  200 VAL A CG1 
1534  C CG2 . VAL A 200 ? 1.5065 2.1656 2.1517 -0.1188 0.2202  0.0312  200 VAL A CG2 
1535  N N   . TYR A 201 ? 1.8629 2.5975 2.5869 -0.1156 0.2027  0.0146  201 TYR A N   
1536  C CA  . TYR A 201 ? 1.8362 2.5875 2.5673 -0.1070 0.1939  0.0121  201 TYR A CA  
1537  C C   . TYR A 201 ? 1.8140 2.5877 2.5699 -0.1062 0.1993  0.0098  201 TYR A C   
1538  O O   . TYR A 201 ? 1.8008 2.5831 2.5572 -0.0982 0.1978  0.0102  201 TYR A O   
1539  C CB  . TYR A 201 ? 1.8223 2.5807 2.5589 -0.1065 0.1794  0.0076  201 TYR A CB  
1540  C CG  . TYR A 201 ? 1.8227 2.5728 2.5390 -0.0986 0.1696  0.0090  201 TYR A CG  
1541  C CD1 . TYR A 201 ? 1.8167 2.5675 2.5237 -0.0902 0.1700  0.0117  201 TYR A CD1 
1542  C CD2 . TYR A 201 ? 1.8293 2.5707 2.5362 -0.0996 0.1601  0.0073  201 TYR A CD2 
1543  C CE1 . TYR A 201 ? 1.8348 2.5783 2.5242 -0.0834 0.1613  0.0130  201 TYR A CE1 
1544  C CE2 . TYR A 201 ? 1.8283 2.5628 2.5176 -0.0926 0.1515  0.0085  201 TYR A CE2 
1545  C CZ  . TYR A 201 ? 1.8250 2.5606 2.5057 -0.0847 0.1522  0.0114  201 TYR A CZ  
1546  O OH  . TYR A 201 ? 1.8183 2.5473 2.4822 -0.0782 0.1439  0.0126  201 TYR A OH  
1547  N N   . SER A 202 ? 1.4868 2.2705 2.2642 -0.1142 0.2051  0.0073  202 SER A N   
1548  C CA  . SER A 202 ? 1.4124 2.2180 2.2155 -0.1141 0.2110  0.0049  202 SER A CA  
1549  C C   . SER A 202 ? 1.3842 2.1839 2.1855 -0.1169 0.2277  0.0084  202 SER A C   
1550  O O   . SER A 202 ? 1.3664 2.1784 2.1776 -0.1121 0.2331  0.0081  202 SER A O   
1551  C CB  . SER A 202 ? 1.3503 2.1731 2.1811 -0.1213 0.2073  -0.0007 202 SER A CB  
1552  O OG  . SER A 202 ? 1.3338 2.1612 2.1653 -0.1194 0.1921  -0.0043 202 SER A OG  
1553  N N   . GLN A 203 ? 1.4450 2.2261 2.2337 -0.1243 0.2360  0.0116  203 GLN A N   
1554  C CA  . GLN A 203 ? 1.4703 2.2455 2.2567 -0.1278 0.2526  0.0150  203 GLN A CA  
1555  C C   . GLN A 203 ? 1.4450 2.2031 2.2032 -0.1209 0.2571  0.0199  203 GLN A C   
1556  O O   . GLN A 203 ? 1.3956 2.1585 2.1559 -0.1177 0.2668  0.0208  203 GLN A O   
1557  C CB  . GLN A 203 ? 1.5100 2.2724 2.2950 -0.1392 0.2600  0.0168  203 GLN A CB  
1558  C CG  . GLN A 203 ? 1.6168 2.3717 2.3976 -0.1438 0.2779  0.0208  203 GLN A CG  
1559  C CD  . GLN A 203 ? 1.6296 2.3557 2.3820 -0.1483 0.2831  0.0268  203 GLN A CD  
1560  O OE1 . GLN A 203 ? 1.6001 2.3155 2.3482 -0.1539 0.2775  0.0270  203 GLN A OE1 
1561  N NE2 . GLN A 203 ? 1.6468 2.3600 2.3792 -0.1457 0.2936  0.0314  203 GLN A NE2 
1562  N N   . ILE A 204 ? 1.4743 2.2127 2.2066 -0.1185 0.2499  0.0227  204 ILE A N   
1563  C CA  . ILE A 204 ? 1.5215 2.2419 2.2257 -0.1125 0.2531  0.0272  204 ILE A CA  
1564  C C   . ILE A 204 ? 1.5215 2.2482 2.2213 -0.1020 0.2418  0.0258  204 ILE A C   
1565  O O   . ILE A 204 ? 1.4839 2.2051 2.1701 -0.0953 0.2449  0.0280  204 ILE A O   
1566  C CB  . ILE A 204 ? 1.5549 2.2486 2.2326 -0.1164 0.2530  0.0316  204 ILE A CB  
1567  C CG1 . ILE A 204 ? 1.5580 2.2456 2.2413 -0.1275 0.2635  0.0332  204 ILE A CG1 
1568  C CG2 . ILE A 204 ? 1.5353 2.2106 2.1843 -0.1107 0.2572  0.0362  204 ILE A CG2 
1569  C CD1 . ILE A 204 ? 1.5902 2.2509 2.2481 -0.1316 0.2635  0.0379  204 ILE A CD1 
1570  N N   . ARG A 205 ? 1.4856 2.2236 2.1967 -0.1007 0.2286  0.0222  205 ARG A N   
1571  C CA  . ARG A 205 ? 1.4669 2.2123 2.1758 -0.0913 0.2171  0.0209  205 ARG A CA  
1572  C C   . ARG A 205 ? 1.4457 2.1703 2.1243 -0.0858 0.2138  0.0248  205 ARG A C   
1573  O O   . ARG A 205 ? 1.4222 2.1383 2.0893 -0.0852 0.2038  0.0249  205 ARG A O   
1574  C CB  . ARG A 205 ? 1.3916 2.1560 2.1176 -0.0856 0.2207  0.0192  205 ARG A CB  
1575  C CG  . ARG A 205 ? 1.3124 2.1000 2.0706 -0.0900 0.2224  0.0149  205 ARG A CG  
1576  C CD  . ARG A 205 ? 1.2139 2.0125 1.9857 -0.0883 0.2345  0.0147  205 ARG A CD  
1577  N NE  . ARG A 205 ? 1.2085 1.9928 1.9698 -0.0940 0.2494  0.0178  205 ARG A NE  
1578  C CZ  . ARG A 205 ? 1.1738 1.9423 1.9129 -0.0903 0.2569  0.0216  205 ARG A CZ  
1579  N NH1 . ARG A 205 ? 1.0710 1.8358 1.7969 -0.0810 0.2507  0.0225  205 ARG A NH1 
1580  N NH2 . ARG A 205 ? 1.2110 1.9671 1.9409 -0.0960 0.2705  0.0244  205 ARG A NH2 
1581  N N   . PHE A 222 ? 1.6592 2.3641 2.2824 -0.0661 0.1396  0.0194  222 PHE A N   
1582  C CA  . PHE A 222 ? 1.7059 2.3913 2.3072 -0.0638 0.1448  0.0242  222 PHE A CA  
1583  C C   . PHE A 222 ? 1.7039 2.3732 2.2980 -0.0709 0.1535  0.0262  222 PHE A C   
1584  O O   . PHE A 222 ? 1.6940 2.3460 2.2695 -0.0700 0.1588  0.0302  222 PHE A O   
1585  C CB  . PHE A 222 ? 1.6789 2.3692 2.2806 -0.0585 0.1506  0.0264  222 PHE A CB  
1586  C CG  . PHE A 222 ? 1.6728 2.3760 2.2937 -0.0616 0.1595  0.0253  222 PHE A CG  
1587  C CD1 . PHE A 222 ? 1.6715 2.3647 2.2884 -0.0661 0.1716  0.0276  222 PHE A CD1 
1588  C CD2 . PHE A 222 ? 1.7037 2.4293 2.3468 -0.0600 0.1559  0.0220  222 PHE A CD2 
1589  C CE1 . PHE A 222 ? 1.6900 2.3959 2.3255 -0.0691 0.1804  0.0263  222 PHE A CE1 
1590  C CE2 . PHE A 222 ? 1.6980 2.4363 2.3603 -0.0628 0.1640  0.0207  222 PHE A CE2 
1591  C CZ  . PHE A 222 ? 1.6722 2.4010 2.3312 -0.0674 0.1765  0.0227  222 PHE A CZ  
1592  N N   . VAL A 223 ? 1.6361 2.3110 2.2450 -0.0779 0.1548  0.0234  223 VAL A N   
1593  C CA  . VAL A 223 ? 1.5540 2.2141 2.1579 -0.0854 0.1627  0.0253  223 VAL A CA  
1594  C C   . VAL A 223 ? 1.5256 2.1693 2.1147 -0.0867 0.1558  0.0255  223 VAL A C   
1595  O O   . VAL A 223 ? 1.4994 2.1498 2.0960 -0.0872 0.1465  0.0214  223 VAL A O   
1596  C CB  . VAL A 223 ? 1.5267 2.2002 2.1544 -0.0928 0.1675  0.0222  223 VAL A CB  
1597  C CG1 . VAL A 223 ? 1.4591 2.1161 2.0813 -0.1011 0.1738  0.0241  223 VAL A CG1 
1598  C CG2 . VAL A 223 ? 1.5728 2.2598 2.2136 -0.0918 0.1764  0.0226  223 VAL A CG2 
1599  N N   . ARG A 224 ? 1.5127 2.1347 2.0805 -0.0870 0.1600  0.0301  224 ARG A N   
1600  C CA  . ARG A 224 ? 1.5153 2.1199 2.0677 -0.0877 0.1537  0.0309  224 ARG A CA  
1601  C C   . ARG A 224 ? 1.4440 2.0392 2.0002 -0.0965 0.1584  0.0311  224 ARG A C   
1602  O O   . ARG A 224 ? 1.4394 2.0283 1.9945 -0.1011 0.1693  0.0344  224 ARG A O   
1603  C CB  . ARG A 224 ? 1.5131 2.0988 2.0400 -0.0831 0.1547  0.0358  224 ARG A CB  
1604  C CG  . ARG A 224 ? 1.5155 2.1080 2.0370 -0.0745 0.1503  0.0360  224 ARG A CG  
1605  C CD  . ARG A 224 ? 1.4945 2.0949 2.0206 -0.0728 0.1594  0.0376  224 ARG A CD  
1606  N NE  . ARG A 224 ? 1.5285 2.1156 2.0463 -0.0775 0.1710  0.0414  224 ARG A NE  
1607  C CZ  . ARG A 224 ? 1.5146 2.1097 2.0425 -0.0798 0.1815  0.0418  224 ARG A CZ  
1608  N NH1 . ARG A 224 ? 1.5154 2.1318 2.0630 -0.0776 0.1813  0.0386  224 ARG A NH1 
1609  N NH2 . ARG A 224 ? 1.4902 2.0720 2.0086 -0.0843 0.1922  0.0454  224 ARG A NH2 
1610  N N   . LEU A 225 ? 1.3728 1.9663 1.9328 -0.0988 0.1503  0.0277  225 LEU A N   
1611  C CA  . LEU A 225 ? 1.2893 1.8743 1.8548 -0.1074 0.1538  0.0274  225 LEU A CA  
1612  C C   . LEU A 225 ? 1.3127 1.8725 1.8573 -0.1098 0.1604  0.0337  225 LEU A C   
1613  O O   . LEU A 225 ? 1.2862 1.8398 1.8338 -0.1169 0.1698  0.0362  225 LEU A O   
1614  C CB  . LEU A 225 ? 1.2489 1.8355 1.8204 -0.1083 0.1429  0.0221  225 LEU A CB  
1615  C CG  . LEU A 225 ? 1.1874 1.7767 1.7760 -0.1170 0.1439  0.0185  225 LEU A CG  
1616  C CD1 . LEU A 225 ? 1.1136 1.7141 1.7131 -0.1158 0.1322  0.0114  225 LEU A CD1 
1617  C CD2 . LEU A 225 ? 1.1498 1.7149 1.7260 -0.1226 0.1484  0.0226  225 LEU A CD2 
1618  N N   . ASP A 226 ? 1.4024 1.9477 1.9257 -0.1041 0.1556  0.0365  226 ASP A N   
1619  C CA  . ASP A 226 ? 1.4332 1.9533 1.9347 -0.1058 0.1598  0.0425  226 ASP A CA  
1620  C C   . ASP A 226 ? 1.4711 1.9849 1.9580 -0.1031 0.1684  0.0477  226 ASP A C   
1621  O O   . ASP A 226 ? 1.5358 2.0319 2.0004 -0.0996 0.1673  0.0518  226 ASP A O   
1622  C CB  . ASP A 226 ? 1.4324 1.9393 1.9194 -0.1015 0.1491  0.0422  226 ASP A CB  
1623  C CG  . ASP A 226 ? 1.4584 1.9772 1.9451 -0.0932 0.1401  0.0391  226 ASP A CG  
1624  O OD1 . ASP A 226 ? 1.4558 1.9781 1.9357 -0.0883 0.1429  0.0413  226 ASP A OD1 
1625  O OD2 . ASP A 226 ? 1.5210 2.0455 2.0141 -0.0915 0.1306  0.0345  226 ASP A OD2 
1626  N N   . GLN A 227 ? 1.4282 1.9561 1.9271 -0.1043 0.1769  0.0474  227 GLN A N   
1627  C CA  . GLN A 227 ? 1.4652 1.9878 1.9510 -0.1017 0.1858  0.0518  227 GLN A CA  
1628  C C   . GLN A 227 ? 1.5152 2.0466 2.0145 -0.1075 0.1987  0.0524  227 GLN A C   
1629  O O   . GLN A 227 ? 1.4460 1.9650 1.9327 -0.1100 0.2090  0.0572  227 GLN A O   
1630  C CB  . GLN A 227 ? 1.5152 2.0483 1.9988 -0.0928 0.1806  0.0501  227 GLN A CB  
1631  C CG  . GLN A 227 ? 1.5415 2.0583 2.0012 -0.0867 0.1739  0.0527  227 GLN A CG  
1632  C CD  . GLN A 227 ? 1.5258 2.0516 1.9897 -0.0810 0.1610  0.0488  227 GLN A CD  
1633  O OE1 . GLN A 227 ? 1.5165 2.0513 1.9801 -0.0747 0.1580  0.0478  227 GLN A OE1 
1634  N NE2 . GLN A 227 ? 1.5117 2.0346 1.9792 -0.0832 0.1535  0.0465  227 GLN A NE2 
1635  N N   . ASP A 228 ? 1.9234 2.4765 2.4486 -0.1097 0.1982  0.0476  228 ASP A N   
1636  C CA  . ASP A 228 ? 1.9130 2.4777 2.4548 -0.1150 0.2098  0.0473  228 ASP A CA  
1637  C C   . ASP A 228 ? 1.9059 2.4775 2.4683 -0.1236 0.2102  0.0444  228 ASP A C   
1638  O O   . ASP A 228 ? 1.8933 2.4786 2.4748 -0.1283 0.2184  0.0429  228 ASP A O   
1639  C CB  . ASP A 228 ? 1.8816 2.4682 2.4374 -0.1094 0.2103  0.0443  228 ASP A CB  
1640  C CG  . ASP A 228 ? 1.8583 2.4621 2.4286 -0.1052 0.1976  0.0388  228 ASP A CG  
1641  O OD1 . ASP A 228 ? 1.8555 2.4611 2.4347 -0.1090 0.1909  0.0358  228 ASP A OD1 
1642  O OD2 . ASP A 228 ? 1.8591 2.4740 2.4312 -0.0979 0.1942  0.0375  228 ASP A OD2 
1643  N N   . ILE A 229 ? 1.4444 2.0070 2.0040 -0.1256 0.2015  0.0431  229 ILE A N   
1644  C CA  . ILE A 229 ? 1.3190 1.8855 1.8966 -0.1339 0.2011  0.0401  229 ILE A CA  
1645  C C   . ILE A 229 ? 1.2063 1.7477 1.7678 -0.1387 0.2013  0.0440  229 ILE A C   
1646  O O   . ILE A 229 ? 1.1610 1.6965 1.7289 -0.1474 0.2087  0.0456  229 ILE A O   
1647  C CB  . ILE A 229 ? 1.2643 1.8487 1.8596 -0.1317 0.1887  0.0328  229 ILE A CB  
1648  C CG1 . ILE A 229 ? 1.2966 1.9064 1.9097 -0.1276 0.1890  0.0293  229 ILE A CG1 
1649  C CG2 . ILE A 229 ? 1.1232 1.7087 1.7347 -0.1403 0.1872  0.0293  229 ILE A CG2 
1650  C CD1 . ILE A 229 ? 1.2110 1.8391 1.8405 -0.1251 0.1769  0.0225  229 ILE A CD1 
1651  N N   . LEU A 230 ? 1.2097 1.7359 1.7505 -0.1331 0.1931  0.0457  230 LEU A N   
1652  C CA  . LEU A 230 ? 1.1387 1.6400 1.6630 -0.1367 0.1923  0.0497  230 LEU A CA  
1653  C C   . LEU A 230 ? 1.1353 1.6180 1.6396 -0.1388 0.2037  0.0575  230 LEU A C   
1654  O O   . LEU A 230 ? 1.0950 1.5629 1.5956 -0.1462 0.2098  0.0613  230 LEU A O   
1655  C CB  . LEU A 230 ? 1.1782 1.6706 1.6887 -0.1298 0.1793  0.0484  230 LEU A CB  
1656  C CG  . LEU A 230 ? 1.1857 1.6919 1.7129 -0.1286 0.1677  0.0409  230 LEU A CG  
1657  C CD1 . LEU A 230 ? 1.2265 1.7209 1.7384 -0.1225 0.1563  0.0403  230 LEU A CD1 
1658  C CD2 . LEU A 230 ? 1.1828 1.6908 1.7280 -0.1378 0.1694  0.0380  230 LEU A CD2 
1659  N N   . SER A 231 ? 1.1633 1.6461 1.6541 -0.1324 0.2066  0.0600  231 SER A N   
1660  C CA  . SER A 231 ? 1.1253 1.5908 1.5955 -0.1339 0.2174  0.0671  231 SER A CA  
1661  C C   . SER A 231 ? 1.1045 1.5750 1.5867 -0.1422 0.2318  0.0690  231 SER A C   
1662  O O   . SER A 231 ? 1.1273 1.5792 1.5963 -0.1478 0.2397  0.0748  231 SER A O   
1663  C CB  . SER A 231 ? 1.1437 1.6101 1.5987 -0.1250 0.2170  0.0683  231 SER A CB  
1664  O OG  . SER A 231 ? 1.2026 1.6645 1.6473 -0.1178 0.2039  0.0668  231 SER A OG  
1665  N N   . PRO A 232 ? 1.1271 1.6216 1.6335 -0.1434 0.2360  0.0645  232 PRO A N   
1666  C CA  . PRO A 232 ? 1.1138 1.6131 1.6322 -0.1516 0.2505  0.0663  232 PRO A CA  
1667  C C   . PRO A 232 ? 1.1196 1.6107 1.6466 -0.1618 0.2528  0.0673  232 PRO A C   
1668  O O   . PRO A 232 ? 1.0933 1.5755 1.6171 -0.1690 0.2653  0.0721  232 PRO A O   
1669  C CB  . PRO A 232 ? 1.1184 1.6470 1.6637 -0.1497 0.2509  0.0601  232 PRO A CB  
1670  C CG  . PRO A 232 ? 1.2133 1.7478 1.7512 -0.1391 0.2408  0.0577  232 PRO A CG  
1671  C CD  . PRO A 232 ? 1.2075 1.7254 1.7296 -0.1367 0.2290  0.0584  232 PRO A CD  
1672  N N   . LEU A 233 ? 1.2449 1.7384 1.7827 -0.1628 0.2415  0.0629  233 LEU A N   
1673  C CA  . LEU A 233 ? 1.2528 1.7380 1.7997 -0.1725 0.2429  0.0633  233 LEU A CA  
1674  C C   . LEU A 233 ? 1.3083 1.7632 1.8285 -0.1735 0.2417  0.0699  233 LEU A C   
1675  O O   . LEU A 233 ? 1.3773 1.8220 1.8928 -0.1722 0.2308  0.0685  233 LEU A O   
1676  C CB  . LEU A 233 ? 1.2906 1.7907 1.8599 -0.1731 0.2313  0.0554  233 LEU A CB  
1677  C CG  . LEU A 233 ? 1.3209 1.8344 1.9183 -0.1830 0.2370  0.0520  233 LEU A CG  
1678  C CD1 . LEU A 233 ? 1.3382 1.8734 1.9518 -0.1834 0.2469  0.0508  233 LEU A CD1 
1679  C CD2 . LEU A 233 ? 1.3428 1.8680 1.9594 -0.1836 0.2245  0.0440  233 LEU A CD2 
1680  N N   . ALA A 234 ? 1.1201 1.5604 1.6221 -0.1757 0.2533  0.0773  234 ALA A N   
1681  C CA  . ALA A 234 ? 1.1150 1.5258 1.5895 -0.1766 0.2535  0.0847  234 ALA A CA  
1682  C C   . ALA A 234 ? 1.0706 1.4687 1.5472 -0.1879 0.2644  0.0897  234 ALA A C   
1683  O O   . ALA A 234 ? 1.0902 1.4764 1.5692 -0.1927 0.2593  0.0900  234 ALA A O   
1684  C CB  . ALA A 234 ? 1.1159 1.5168 1.5636 -0.1696 0.2572  0.0897  234 ALA A CB  
1685  N N   . GLY A 235 ? 1.0493 1.4493 1.5251 -0.1926 0.2795  0.0938  235 GLY A N   
1686  C CA  . GLY A 235 ? 1.0077 1.3955 1.4851 -0.2038 0.2909  0.0992  235 GLY A CA  
1687  C C   . GLY A 235 ? 1.0053 1.4075 1.5147 -0.2122 0.2906  0.0938  235 GLY A C   
1688  O O   . GLY A 235 ? 1.0178 1.4055 1.5287 -0.2207 0.2928  0.0969  235 GLY A O   
1689  N N   . LYS A 236 ? 0.9994 1.4296 1.5347 -0.2101 0.2876  0.0857  236 LYS A N   
1690  C CA  . LYS A 236 ? 0.9523 1.3982 1.5191 -0.2177 0.2866  0.0797  236 LYS A CA  
1691  C C   . LYS A 236 ? 0.9878 1.4238 1.5565 -0.2183 0.2728  0.0767  236 LYS A C   
1692  O O   . LYS A 236 ? 1.0083 1.4454 1.5704 -0.2096 0.2595  0.0730  236 LYS A O   
1693  C CB  . LYS A 236 ? 0.9345 1.4124 1.5265 -0.2138 0.2847  0.0717  236 LYS A CB  
1694  C CG  . LYS A 236 ? 0.9725 1.4575 1.5517 -0.2018 0.2799  0.0706  236 LYS A CG  
1695  C CD  . LYS A 236 ? 0.8817 1.3837 1.4689 -0.2009 0.2921  0.0707  236 LYS A CD  
1696  C CE  . LYS A 236 ? 0.8412 1.3245 1.4036 -0.2025 0.3056  0.0793  236 LYS A CE  
1697  N NZ  . LYS A 236 ? 0.9534 1.4192 1.4841 -0.1933 0.2995  0.0830  236 LYS A NZ  
1698  N N   . LYS A 237 ? 0.9991 1.4256 1.5772 -0.2286 0.2761  0.0780  237 LYS A N   
1699  C CA  . LYS A 237 ? 1.0321 1.4459 1.6112 -0.2302 0.2644  0.0756  237 LYS A CA  
1700  C C   . LYS A 237 ? 1.0531 1.4907 1.6589 -0.2284 0.2531  0.0647  237 LYS A C   
1701  O O   . LYS A 237 ? 1.0287 1.4757 1.6591 -0.2365 0.2536  0.0601  237 LYS A O   
1702  C CB  . LYS A 237 ? 1.1143 1.5107 1.6962 -0.2423 0.2723  0.0806  237 LYS A CB  
1703  C CG  . LYS A 237 ? 1.1552 1.5240 1.7076 -0.2442 0.2818  0.0920  237 LYS A CG  
1704  C CD  . LYS A 237 ? 1.2290 1.5714 1.7578 -0.2396 0.2708  0.0953  237 LYS A CD  
1705  C CE  . LYS A 237 ? 1.1883 1.5275 1.7335 -0.2440 0.2608  0.0898  237 LYS A CE  
1706  N NZ  . LYS A 237 ? 1.1495 1.4764 1.7033 -0.2569 0.2701  0.0941  237 LYS A NZ  
1707  N N   . GLN A 238 ? 1.1153 1.5630 1.7159 -0.2175 0.2427  0.0604  238 GLN A N   
1708  C CA  . GLN A 238 ? 1.1263 1.5947 1.7475 -0.2143 0.2305  0.0504  238 GLN A CA  
1709  C C   . GLN A 238 ? 1.1952 1.6571 1.8014 -0.2044 0.2160  0.0478  238 GLN A C   
1710  O O   . GLN A 238 ? 1.1521 1.6213 1.7712 -0.2038 0.2050  0.0404  238 GLN A O   
1711  C CB  . GLN A 238 ? 1.0826 1.5805 1.7221 -0.2114 0.2336  0.0459  238 GLN A CB  
1712  C CG  . GLN A 238 ? 1.0360 1.5481 1.7008 -0.2215 0.2448  0.0448  238 GLN A CG  
1713  C CD  . GLN A 238 ? 1.0121 1.5256 1.6706 -0.2223 0.2600  0.0511  238 GLN A CD  
1714  O OE1 . GLN A 238 ? 0.9583 1.4850 1.6142 -0.2147 0.2608  0.0503  238 GLN A OE1 
1715  N NE2 . GLN A 238 ? 1.0417 1.5411 1.6973 -0.2317 0.2723  0.0573  238 GLN A NE2 
1716  N N   . LEU A 239 ? 1.5384 1.9872 2.1183 -0.1967 0.2154  0.0533  239 LEU A N   
1717  C CA  . LEU A 239 ? 1.5447 1.9869 2.1098 -0.1874 0.2023  0.0513  239 LEU A CA  
1718  C C   . LEU A 239 ? 1.5881 2.0013 2.1356 -0.1893 0.1990  0.0559  239 LEU A C   
1719  O O   . LEU A 239 ? 1.6196 2.0129 2.1494 -0.1922 0.2074  0.0643  239 LEU A O   
1720  C CB  . LEU A 239 ? 1.5426 1.9875 2.0901 -0.1778 0.2027  0.0543  239 LEU A CB  
1721  C CG  . LEU A 239 ? 1.5315 1.9917 2.0819 -0.1682 0.1903  0.0478  239 LEU A CG  
1722  C CD1 . LEU A 239 ? 1.5377 1.9831 2.0770 -0.1644 0.1781  0.0462  239 LEU A CD1 
1723  C CD2 . LEU A 239 ? 1.4740 1.9616 2.0535 -0.1703 0.1878  0.0396  239 LEU A CD2 
1724  N N   . TYR A 240 ? 1.3096 1.7203 1.8615 -0.1874 0.1870  0.0503  240 TYR A N   
1725  C CA  . TYR A 240 ? 1.2694 1.6533 1.8075 -0.1892 0.1830  0.0537  240 TYR A CA  
1726  C C   . TYR A 240 ? 1.2477 1.6247 1.7701 -0.1788 0.1703  0.0520  240 TYR A C   
1727  O O   . TYR A 240 ? 1.2610 1.6519 1.7805 -0.1706 0.1659  0.0494  240 TYR A O   
1728  C CB  . TYR A 240 ? 1.2230 1.6067 1.7818 -0.1981 0.1813  0.0489  240 TYR A CB  
1729  C CG  . TYR A 240 ? 1.2367 1.6211 1.8076 -0.2093 0.1947  0.0525  240 TYR A CG  
1730  C CD1 . TYR A 240 ? 1.2470 1.6064 1.8040 -0.2156 0.2029  0.0614  240 TYR A CD1 
1731  C CD2 . TYR A 240 ? 1.2066 1.6168 1.8026 -0.2135 0.1992  0.0472  240 TYR A CD2 
1732  C CE1 . TYR A 240 ? 1.2173 1.5774 1.7853 -0.2262 0.2159  0.0650  240 TYR A CE1 
1733  C CE2 . TYR A 240 ? 1.1750 1.5868 1.7832 -0.2239 0.2119  0.0504  240 TYR A CE2 
1734  C CZ  . TYR A 240 ? 1.1644 1.5512 1.7586 -0.2304 0.2205  0.0593  240 TYR A CZ  
1735  O OH  . TYR A 240 ? 1.1597 1.5481 1.7661 -0.2411 0.2338  0.0626  240 TYR A OH  
1736  N N   . THR A 241 ? 1.2236 1.5784 1.7361 -0.1793 0.1646  0.0536  241 THR A N   
1737  C CA  . THR A 241 ? 1.1985 1.5437 1.6954 -0.1699 0.1530  0.0525  241 THR A CA  
1738  C C   . THR A 241 ? 1.2014 1.5339 1.7037 -0.1721 0.1446  0.0486  241 THR A C   
1739  O O   . THR A 241 ? 1.2385 1.5611 1.7490 -0.1810 0.1489  0.0498  241 THR A O   
1740  C CB  . THR A 241 ? 1.2543 1.5785 1.7225 -0.1656 0.1558  0.0621  241 THR A CB  
1741  O OG1 . THR A 241 ? 1.2998 1.6051 1.7607 -0.1739 0.1661  0.0702  241 THR A OG1 
1742  C CG2 . THR A 241 ? 1.2528 1.5908 1.7136 -0.1597 0.1596  0.0637  241 THR A CG2 
1743  N N   . TYR A 242 ? 1.1776 1.5105 1.6755 -0.1638 0.1327  0.0437  242 TYR A N   
1744  C CA  . TYR A 242 ? 1.2120 1.5330 1.7139 -0.1641 0.1236  0.0391  242 TYR A CA  
1745  C C   . TYR A 242 ? 1.2693 1.5829 1.7553 -0.1535 0.1132  0.0385  242 TYR A C   
1746  O O   . TYR A 242 ? 1.2806 1.6119 1.7676 -0.1463 0.1084  0.0341  242 TYR A O   
1747  C CB  . TYR A 242 ? 1.1813 1.5224 1.7093 -0.1675 0.1193  0.0283  242 TYR A CB  
1748  C CG  . TYR A 242 ? 1.1788 1.5117 1.7116 -0.1659 0.1085  0.0214  242 TYR A CG  
1749  C CD1 . TYR A 242 ? 1.1859 1.4985 1.7212 -0.1728 0.1092  0.0228  242 TYR A CD1 
1750  C CD2 . TYR A 242 ? 1.1880 1.5337 1.7233 -0.1577 0.0979  0.0135  242 TYR A CD2 
1751  C CE1 . TYR A 242 ? 1.1906 1.4955 1.7307 -0.1711 0.0993  0.0160  242 TYR A CE1 
1752  C CE2 . TYR A 242 ? 1.2211 1.5598 1.7610 -0.1560 0.0885  0.0066  242 TYR A CE2 
1753  C CZ  . TYR A 242 ? 1.1906 1.5089 1.7330 -0.1626 0.0891  0.0077  242 TYR A CZ  
1754  O OH  . TYR A 242 ? 1.2461 1.5571 1.7935 -0.1606 0.0796  0.0004  242 TYR A OH  
1755  N N   . GLU A 243 ? 1.4110 1.6988 1.8828 -0.1526 0.1098  0.0428  243 GLU A N   
1756  C CA  . GLU A 243 ? 1.4255 1.7041 1.8808 -0.1427 0.1006  0.0434  243 GLU A CA  
1757  C C   . GLU A 243 ? 1.4027 1.6946 1.8704 -0.1372 0.0893  0.0326  243 GLU A C   
1758  O O   . GLU A 243 ? 1.3933 1.6914 1.8790 -0.1416 0.0869  0.0253  243 GLU A O   
1759  C CB  . GLU A 243 ? 1.4761 1.7233 1.9145 -0.1433 0.0995  0.0508  243 GLU A CB  
1760  N N   . ASN A 244 ? 1.2014 1.4977 1.6589 -0.1275 0.0825  0.0314  244 ASN A N   
1761  C CA  . ASN A 244 ? 1.1135 1.4216 1.5799 -0.1213 0.0719  0.0217  244 ASN A CA  
1762  C C   . ASN A 244 ? 1.0837 1.3713 1.5471 -0.1198 0.0643  0.0200  244 ASN A C   
1763  O O   . ASN A 244 ? 1.0535 1.3454 1.5319 -0.1217 0.0596  0.0117  244 ASN A O   
1764  C CB  . ASN A 244 ? 1.1093 1.4287 1.5659 -0.1119 0.0678  0.0217  244 ASN A CB  
1765  C CG  . ASN A 244 ? 1.0291 1.3666 1.4970 -0.1062 0.0588  0.0114  244 ASN A CG  
1766  O OD1 . ASN A 244 ? 1.0534 1.3897 1.5322 -0.1075 0.0535  0.0044  244 ASN A OD1 
1767  N ND2 . ASN A 244 ? 0.9902 1.3441 1.4551 -0.1000 0.0571  0.0104  244 ASN A ND2 
1768  N N   . LYS A 245 ? 1.0665 1.3321 1.5104 -0.1159 0.0626  0.0274  245 LYS A N   
1769  C CA  . LYS A 245 ? 0.9779 1.2223 1.4168 -0.1131 0.0549  0.0268  245 LYS A CA  
1770  C C   . LYS A 245 ? 0.9124 1.1675 1.3574 -0.1048 0.0441  0.0174  245 LYS A C   
1771  O O   . LYS A 245 ? 0.8400 1.0851 1.2901 -0.1037 0.0375  0.0125  245 LYS A O   
1772  C CB  . LYS A 245 ? 1.0223 1.2531 1.4713 -0.1219 0.0572  0.0261  245 LYS A CB  
1773  N N   . ASP A 246 ? 0.9551 1.2304 1.3996 -0.0989 0.0424  0.0147  246 ASP A N   
1774  C CA  . ASP A 246 ? 0.9202 1.2067 1.3692 -0.0909 0.0330  0.0064  246 ASP A CA  
1775  C C   . ASP A 246 ? 0.8771 1.1735 1.3149 -0.0832 0.0315  0.0089  246 ASP A C   
1776  O O   . ASP A 246 ? 0.8543 1.1358 1.2749 -0.0801 0.0317  0.0169  246 ASP A O   
1777  C CB  . ASP A 246 ? 0.9251 1.2333 1.3947 -0.0934 0.0315  -0.0044 246 ASP A CB  
1778  C CG  . ASP A 246 ? 0.8612 1.1589 1.3418 -0.0972 0.0279  -0.0104 246 ASP A CG  
1779  O OD1 . ASP A 246 ? 0.8747 1.1590 1.3510 -0.0920 0.0206  -0.0125 246 ASP A OD1 
1780  O OD2 . ASP A 246 ? 0.8506 1.1530 1.3444 -0.1052 0.0321  -0.0131 246 ASP A OD2 
1781  N N   . PHE A 247 ? 0.8927 1.2140 1.3400 -0.0803 0.0298  0.0024  247 PHE A N   
1782  C CA  . PHE A 247 ? 0.9314 1.2634 1.3701 -0.0731 0.0278  0.0039  247 PHE A CA  
1783  C C   . PHE A 247 ? 1.0229 1.3755 1.4664 -0.0756 0.0344  0.0047  247 PHE A C   
1784  O O   . PHE A 247 ? 1.0412 1.4053 1.4985 -0.0816 0.0384  0.0012  247 PHE A O   
1785  C CB  . PHE A 247 ? 0.9186 1.2613 1.3627 -0.0657 0.0187  -0.0045 247 PHE A CB  
1786  C CG  . PHE A 247 ? 0.9143 1.2748 1.3769 -0.0680 0.0168  -0.0148 247 PHE A CG  
1787  C CD1 . PHE A 247 ? 0.9265 1.2781 1.3980 -0.0709 0.0137  -0.0203 247 PHE A CD1 
1788  C CD2 . PHE A 247 ? 0.9036 1.2891 1.3742 -0.0671 0.0178  -0.0189 247 PHE A CD2 
1789  C CE1 . PHE A 247 ? 0.9034 1.2712 1.3912 -0.0729 0.0117  -0.0302 247 PHE A CE1 
1790  C CE2 . PHE A 247 ? 0.9139 1.3157 1.4002 -0.0691 0.0157  -0.0282 247 PHE A CE2 
1791  C CZ  . PHE A 247 ? 0.9290 1.3221 1.4238 -0.0720 0.0126  -0.0341 247 PHE A CZ  
1792  N N   . TRP A 248 ? 1.1206 1.4776 1.5531 -0.0708 0.0352  0.0091  248 TRP A N   
1793  C CA  . TRP A 248 ? 1.0807 1.4579 1.5173 -0.0715 0.0404  0.0096  248 TRP A CA  
1794  C C   . TRP A 248 ? 1.0728 1.4541 1.4977 -0.0641 0.0378  0.0123  248 TRP A C   
1795  O O   . TRP A 248 ? 1.1056 1.4699 1.5148 -0.0610 0.0366  0.0181  248 TRP A O   
1796  C CB  . TRP A 248 ? 1.0900 1.4631 1.5251 -0.0787 0.0506  0.0160  248 TRP A CB  
1797  C CG  . TRP A 248 ? 1.0667 1.4618 1.5087 -0.0792 0.0555  0.0153  248 TRP A CG  
1798  C CD1 . TRP A 248 ? 1.0587 1.4747 1.5185 -0.0819 0.0561  0.0090  248 TRP A CD1 
1799  C CD2 . TRP A 248 ? 1.0486 1.4468 1.4801 -0.0766 0.0600  0.0211  248 TRP A CD2 
1800  N NE1 . TRP A 248 ? 1.0041 1.4358 1.4652 -0.0811 0.0606  0.0108  248 TRP A NE1 
1801  C CE2 . TRP A 248 ? 1.0398 1.4608 1.4838 -0.0778 0.0633  0.0181  248 TRP A CE2 
1802  C CE3 . TRP A 248 ? 1.0685 1.4520 1.4809 -0.0733 0.0612  0.0284  248 TRP A CE3 
1803  C CZ2 . TRP A 248 ? 1.0940 1.5232 1.5327 -0.0757 0.0680  0.0221  248 TRP A CZ2 
1804  C CZ3 . TRP A 248 ? 1.1111 1.5028 1.5177 -0.0715 0.0660  0.0320  248 TRP A CZ3 
1805  C CH2 . TRP A 248 ? 1.1311 1.5453 1.5511 -0.0726 0.0695  0.0289  248 TRP A CH2 
1806  N N   . GLU A 249 ? 1.0417 1.4454 1.4744 -0.0613 0.0367  0.0081  249 GLU A N   
1807  C CA  . GLU A 249 ? 1.0692 1.4788 1.4928 -0.0546 0.0344  0.0102  249 GLU A CA  
1808  C C   . GLU A 249 ? 1.0698 1.5028 1.5023 -0.0547 0.0375  0.0082  249 GLU A C   
1809  O O   . GLU A 249 ? 1.0265 1.4763 1.4727 -0.0551 0.0349  0.0013  249 GLU A O   
1810  C CB  . GLU A 249 ? 1.0576 1.4668 1.4802 -0.0479 0.0251  0.0055  249 GLU A CB  
1811  N N   . GLN A 250 ? 1.2676 1.7016 1.6920 -0.0544 0.0429  0.0141  250 GLN A N   
1812  C CA  . GLN A 250 ? 1.2234 1.6785 1.6553 -0.0537 0.0457  0.0130  250 GLN A CA  
1813  C C   . GLN A 250 ? 1.1933 1.6607 1.6256 -0.0469 0.0388  0.0093  250 GLN A C   
1814  O O   . GLN A 250 ? 1.2055 1.6638 1.6264 -0.0420 0.0348  0.0115  250 GLN A O   
1815  C CB  . GLN A 250 ? 1.2296 1.6807 1.6518 -0.0546 0.0532  0.0202  250 GLN A CB  
1816  C CG  . GLN A 250 ? 1.2101 1.6748 1.6437 -0.0595 0.0607  0.0202  250 GLN A CG  
1817  C CD  . GLN A 250 ? 1.1709 1.6542 1.6080 -0.0558 0.0612  0.0197  250 GLN A CD  
1818  O OE1 . GLN A 250 ? 1.1645 1.6472 1.5954 -0.0556 0.0670  0.0245  250 GLN A OE1 
1819  N NE2 . GLN A 250 ? 1.1374 1.6370 1.5842 -0.0529 0.0552  0.0140  250 GLN A NE2 
1820  N N   . ILE A 251 ? 0.9789 1.4671 1.4244 -0.0468 0.0373  0.0039  251 ILE A N   
1821  C CA  . ILE A 251 ? 0.8931 1.3938 1.3402 -0.0409 0.0310  0.0000  251 ILE A CA  
1822  C C   . ILE A 251 ? 0.8272 1.3463 1.2781 -0.0394 0.0333  0.0009  251 ILE A C   
1823  O O   . ILE A 251 ? 0.7686 1.3057 1.2307 -0.0393 0.0313  -0.0040 251 ILE A O   
1824  C CB  . ILE A 251 ? 0.8519 1.3600 1.3100 -0.0412 0.0255  -0.0082 251 ILE A CB  
1825  C CG1 . ILE A 251 ? 0.8516 1.3680 1.3231 -0.0475 0.0288  -0.0116 251 ILE A CG1 
1826  C CG2 . ILE A 251 ? 0.9422 1.4324 1.3947 -0.0399 0.0211  -0.0094 251 ILE A CG2 
1827  C CD1 . ILE A 251 ? 0.7844 1.3184 1.2683 -0.0469 0.0240  -0.0199 251 ILE A CD1 
1828  N N   . LYS A 252 ? 0.8217 1.3362 1.2629 -0.0379 0.0371  0.0071  252 LYS A N   
1829  C CA  . LYS A 252 ? 0.8272 1.3570 1.2704 -0.0352 0.0384  0.0084  252 LYS A CA  
1830  C C   . LYS A 252 ? 0.8217 1.3543 1.2587 -0.0290 0.0328  0.0082  252 LYS A C   
1831  O O   . LYS A 252 ? 0.8470 1.3938 1.2871 -0.0264 0.0325  0.0083  252 LYS A O   
1832  C CB  . LYS A 252 ? 0.9585 1.4826 1.3951 -0.0367 0.0458  0.0148  252 LYS A CB  
1833  C CG  . LYS A 252 ? 0.9930 1.4976 1.4126 -0.0345 0.0462  0.0200  252 LYS A CG  
1834  C CD  . LYS A 252 ? 1.0240 1.5110 1.4379 -0.0393 0.0510  0.0232  252 LYS A CD  
1835  C CE  . LYS A 252 ? 1.0168 1.4830 1.4147 -0.0369 0.0479  0.0265  252 LYS A CE  
1836  N NZ  . LYS A 252 ? 1.0359 1.4991 1.4364 -0.0349 0.0400  0.0220  252 LYS A NZ  
1837  N N   . THR A 253 ? 0.8372 1.3565 1.2662 -0.0265 0.0282  0.0079  253 THR A N   
1838  C CA  . THR A 253 ? 0.8358 1.3559 1.2595 -0.0208 0.0225  0.0073  253 THR A CA  
1839  C C   . THR A 253 ? 0.8129 1.3438 1.2459 -0.0193 0.0168  0.0002  253 THR A C   
1840  O O   . THR A 253 ? 0.7698 1.2970 1.2080 -0.0217 0.0155  -0.0038 253 THR A O   
1841  C CB  . THR A 253 ? 0.8456 1.3450 1.2561 -0.0189 0.0204  0.0107  253 THR A CB  
1842  O OG1 . THR A 253 ? 0.9217 1.4072 1.3247 -0.0226 0.0263  0.0159  253 THR A OG1 
1843  C CG2 . THR A 253 ? 0.8156 1.3153 1.2181 -0.0138 0.0174  0.0131  253 THR A CG2 
1844  N N   . PRO A 254 ? 0.8691 1.4134 1.3042 -0.0153 0.0135  -0.0015 254 PRO A N   
1845  C CA  . PRO A 254 ? 0.8122 1.3655 1.2542 -0.0133 0.0082  -0.0082 254 PRO A CA  
1846  C C   . PRO A 254 ? 0.7810 1.3202 1.2182 -0.0108 0.0035  -0.0099 254 PRO A C   
1847  O O   . PRO A 254 ? 0.7674 1.3103 1.2108 -0.0100 -0.0003 -0.0162 254 PRO A O   
1848  C CB  . PRO A 254 ? 0.7936 1.3626 1.2368 -0.0097 0.0068  -0.0080 254 PRO A CB  
1849  C CG  . PRO A 254 ? 0.8388 1.4007 1.2727 -0.0084 0.0094  -0.0011 254 PRO A CG  
1850  C CD  . PRO A 254 ? 0.8716 1.4232 1.3030 -0.0127 0.0149  0.0025  254 PRO A CD  
1851  N N   . GLY A 255 ? 0.7314 1.2544 1.1575 -0.0093 0.0035  -0.0048 255 GLY A N   
1852  C CA  . GLY A 255 ? 0.7245 1.2329 1.1459 -0.0068 -0.0013 -0.0059 255 GLY A CA  
1853  C C   . GLY A 255 ? 0.7293 1.2249 1.1522 -0.0105 -0.0008 -0.0074 255 GLY A C   
1854  O O   . GLY A 255 ? 0.7398 1.2294 1.1649 -0.0088 -0.0054 -0.0116 255 GLY A O   
1855  N N   . LYS A 256 ? 0.7144 1.2057 1.1366 -0.0155 0.0050  -0.0041 256 LYS A N   
1856  C CA  . LYS A 256 ? 0.7565 1.2361 1.1810 -0.0198 0.0063  -0.0052 256 LYS A CA  
1857  C C   . LYS A 256 ? 0.7012 1.1914 1.1389 -0.0212 0.0038  -0.0133 256 LYS A C   
1858  O O   . LYS A 256 ? 0.7251 1.2051 1.1658 -0.0242 0.0035  -0.0155 256 LYS A O   
1859  C CB  . LYS A 256 ? 0.8302 1.3057 1.2528 -0.0253 0.0138  -0.0002 256 LYS A CB  
1860  C CG  . LYS A 256 ? 0.8903 1.3479 1.2980 -0.0252 0.0165  0.0076  256 LYS A CG  
1861  C CD  . LYS A 256 ? 0.9293 1.3654 1.3298 -0.0251 0.0134  0.0088  256 LYS A CD  
1862  C CE  . LYS A 256 ? 0.9692 1.3868 1.3554 -0.0272 0.0180  0.0168  256 LYS A CE  
1863  N NZ  . LYS A 256 ? 0.9615 1.3816 1.3512 -0.0335 0.0265  0.0192  256 LYS A NZ  
1864  N N   . SER A 257 ? 0.6648 1.1748 1.1101 -0.0191 0.0021  -0.0179 257 SER A N   
1865  C CA  . SER A 257 ? 0.6656 1.1868 1.1225 -0.0201 -0.0004 -0.0261 257 SER A CA  
1866  C C   . SER A 257 ? 0.6739 1.1859 1.1317 -0.0174 -0.0060 -0.0313 257 SER A C   
1867  O O   . SER A 257 ? 0.7451 1.2632 1.2120 -0.0186 -0.0080 -0.0386 257 SER A O   
1868  C CB  . SER A 257 ? 0.6730 1.2167 1.1354 -0.0178 -0.0013 -0.0292 257 SER A CB  
1869  O OG  . SER A 257 ? 0.6958 1.2478 1.1576 -0.0197 0.0034  -0.0243 257 SER A OG  
1870  N N   . LEU A 258 ? 0.6869 1.1846 1.1358 -0.0136 -0.0088 -0.0281 258 LEU A N   
1871  C CA  . LEU A 258 ? 0.7186 1.2060 1.1684 -0.0106 -0.0143 -0.0326 258 LEU A CA  
1872  C C   . LEU A 258 ? 0.7209 1.1857 1.1662 -0.0134 -0.0139 -0.0296 258 LEU A C   
1873  O O   . LEU A 258 ? 0.7047 1.1637 1.1561 -0.0144 -0.0163 -0.0350 258 LEU A O   
1874  C CB  . LEU A 258 ? 0.7196 1.2062 1.1637 -0.0040 -0.0186 -0.0315 258 LEU A CB  
1875  C CG  . LEU A 258 ? 0.6735 1.1811 1.1237 -0.0005 -0.0205 -0.0364 258 LEU A CG  
1876  C CD1 . LEU A 258 ? 0.6426 1.1483 1.0875 0.0053  -0.0243 -0.0346 258 LEU A CD1 
1877  C CD2 . LEU A 258 ? 0.7116 1.2274 1.1724 -0.0003 -0.0231 -0.0460 258 LEU A CD2 
1878  N N   . LYS A 259 ? 0.7745 1.2259 1.2088 -0.0147 -0.0109 -0.0212 259 LYS A N   
1879  C CA  . LYS A 259 ? 0.8151 1.2440 1.2434 -0.0176 -0.0100 -0.0173 259 LYS A CA  
1880  C C   . LYS A 259 ? 0.7881 1.2170 1.2254 -0.0242 -0.0065 -0.0202 259 LYS A C   
1881  O O   . LYS A 259 ? 0.8056 1.2200 1.2443 -0.0258 -0.0083 -0.0218 259 LYS A O   
1882  C CB  . LYS A 259 ? 0.8697 1.2869 1.2842 -0.0185 -0.0061 -0.0077 259 LYS A CB  
1883  C CG  . LYS A 259 ? 0.8969 1.2893 1.3023 -0.0209 -0.0056 -0.0025 259 LYS A CG  
1884  C CD  . LYS A 259 ? 0.9517 1.3336 1.3421 -0.0215 -0.0015 0.0066  259 LYS A CD  
1885  C CE  . LYS A 259 ? 0.9458 1.3019 1.3251 -0.0231 -0.0017 0.0123  259 LYS A CE  
1886  N NZ  . LYS A 259 ? 0.9719 1.3161 1.3478 -0.0174 -0.0102 0.0107  259 LYS A NZ  
1887  N N   . CYS A 260 ? 0.8206 1.2660 1.2648 -0.0280 -0.0018 -0.0212 260 CYS A N   
1888  C CA  . CYS A 260 ? 0.8346 1.2826 1.2892 -0.0343 0.0012  -0.0247 260 CYS A CA  
1889  C C   . CYS A 260 ? 0.7928 1.2505 1.2592 -0.0332 -0.0037 -0.0349 260 CYS A C   
1890  O O   . CYS A 260 ? 0.8926 1.3450 1.3663 -0.0375 -0.0036 -0.0388 260 CYS A O   
1891  C CB  . CYS A 260 ? 0.7936 1.2566 1.2523 -0.0384 0.0074  -0.0225 260 CYS A CB  
1892  S SG  . CYS A 260 ? 0.7714 1.2627 1.2377 -0.0347 0.0054  -0.0278 260 CYS A SG  
1893  N N   . SER A 261 ? 0.7277 1.1998 1.1961 -0.0277 -0.0077 -0.0393 261 SER A N   
1894  C CA  . SER A 261 ? 0.7035 1.1853 1.1820 -0.0262 -0.0122 -0.0493 261 SER A CA  
1895  C C   . SER A 261 ? 0.8474 1.3111 1.3260 -0.0248 -0.0166 -0.0526 261 SER A C   
1896  O O   . SER A 261 ? 0.7977 1.2634 1.2856 -0.0262 -0.0188 -0.0606 261 SER A O   
1897  C CB  . SER A 261 ? 0.6406 1.1394 1.1193 -0.0202 -0.0152 -0.0525 261 SER A CB  
1898  O OG  . SER A 261 ? 0.6262 1.1344 1.1137 -0.0185 -0.0192 -0.0624 261 SER A OG  
1899  N N   . ALA A 262 ? 0.7286 1.1746 1.1971 -0.0218 -0.0181 -0.0467 262 ALA A N   
1900  C CA  . ALA A 262 ? 0.7967 1.2239 1.2648 -0.0201 -0.0226 -0.0489 262 ALA A CA  
1901  C C   . ALA A 262 ? 0.8964 1.3095 1.3673 -0.0270 -0.0197 -0.0480 262 ALA A C   
1902  O O   . ALA A 262 ? 0.9580 1.3621 1.4348 -0.0273 -0.0230 -0.0536 262 ALA A O   
1903  C CB  . ALA A 262 ? 0.7991 1.2107 1.2549 -0.0152 -0.0252 -0.0421 262 ALA A CB  
1904  N N   . LEU A 263 ? 0.8976 1.3085 1.3648 -0.0327 -0.0133 -0.0410 263 LEU A N   
1905  C CA  . LEU A 263 ? 0.9465 1.3443 1.4166 -0.0399 -0.0097 -0.0393 263 LEU A CA  
1906  C C   . LEU A 263 ? 1.0272 1.4379 1.5126 -0.0443 -0.0097 -0.0484 263 LEU A C   
1907  O O   . LEU A 263 ? 1.0560 1.4548 1.5470 -0.0480 -0.0106 -0.0516 263 LEU A O   
1908  C CB  . LEU A 263 ? 0.9375 1.3317 1.4003 -0.0448 -0.0023 -0.0298 263 LEU A CB  
1909  C CG  . LEU A 263 ? 0.9202 1.3013 1.3666 -0.0411 -0.0019 -0.0206 263 LEU A CG  
1910  C CD1 . LEU A 263 ? 0.8932 1.2736 1.3333 -0.0460 0.0062  -0.0124 263 LEU A CD1 
1911  C CD2 . LEU A 263 ? 0.9446 1.3005 1.3836 -0.0395 -0.0058 -0.0180 263 LEU A CD2 
1912  N N   . TYR A 264 ? 1.2454 1.6797 1.7373 -0.0439 -0.0089 -0.0526 264 TYR A N   
1913  C CA  . TYR A 264 ? 1.2263 1.6741 1.7321 -0.0475 -0.0097 -0.0618 264 TYR A CA  
1914  C C   . TYR A 264 ? 1.2313 1.6767 1.7424 -0.0437 -0.0163 -0.0713 264 TYR A C   
1915  O O   . TYR A 264 ? 1.2419 1.6850 1.7626 -0.0477 -0.0175 -0.0780 264 TYR A O   
1916  C CB  . TYR A 264 ? 1.2090 1.6824 1.7190 -0.0471 -0.0081 -0.0636 264 TYR A CB  
1917  C CG  . TYR A 264 ? 1.2196 1.6977 1.7299 -0.0527 -0.0012 -0.0570 264 TYR A CG  
1918  C CD1 . TYR A 264 ? 1.2393 1.7051 1.7527 -0.0599 0.0031  -0.0540 264 TYR A CD1 
1919  C CD2 . TYR A 264 ? 1.1421 1.6368 1.6502 -0.0509 0.0012  -0.0537 264 TYR A CD2 
1920  C CE1 . TYR A 264 ? 1.1946 1.6654 1.7091 -0.0649 0.0098  -0.0482 264 TYR A CE1 
1921  C CE2 . TYR A 264 ? 1.1451 1.6443 1.6543 -0.0556 0.0075  -0.0481 264 TYR A CE2 
1922  C CZ  . TYR A 264 ? 1.1560 1.6437 1.6687 -0.0625 0.0119  -0.0455 264 TYR A CZ  
1923  O OH  . TYR A 264 ? 1.1448 1.6376 1.6593 -0.0671 0.0187  -0.0401 264 TYR A OH  
1924  N N   . LEU A 265 ? 1.0463 1.4927 1.5522 -0.0361 -0.0206 -0.0725 265 LEU A N   
1925  C CA  . LEU A 265 ? 1.0142 1.4570 1.5248 -0.0318 -0.0267 -0.0815 265 LEU A CA  
1926  C C   . LEU A 265 ? 1.0062 1.4233 1.5158 -0.0334 -0.0283 -0.0801 265 LEU A C   
1927  O O   . LEU A 265 ? 1.0429 1.4554 1.5606 -0.0340 -0.0316 -0.0883 265 LEU A O   
1928  C CB  . LEU A 265 ? 0.9503 1.3994 1.4557 -0.0234 -0.0304 -0.0822 265 LEU A CB  
1929  C CG  . LEU A 265 ? 0.8544 1.3292 1.3617 -0.0213 -0.0295 -0.0847 265 LEU A CG  
1930  C CD1 . LEU A 265 ? 0.8583 1.3375 1.3606 -0.0134 -0.0328 -0.0848 265 LEU A CD1 
1931  C CD2 . LEU A 265 ? 0.9244 1.4146 1.4427 -0.0233 -0.0307 -0.0954 265 LEU A CD2 
1932  N N   . SER A 266 ? 0.9927 1.3923 1.4917 -0.0341 -0.0262 -0.0698 266 SER A N   
1933  C CA  . SER A 266 ? 1.0007 1.3748 1.4976 -0.0366 -0.0269 -0.0669 266 SER A CA  
1934  C C   . SER A 266 ? 1.0562 1.4283 1.5626 -0.0454 -0.0234 -0.0695 266 SER A C   
1935  O O   . SER A 266 ? 1.1037 1.4602 1.6146 -0.0474 -0.0257 -0.0728 266 SER A O   
1936  C CB  . SER A 266 ? 0.9874 1.3446 1.4699 -0.0364 -0.0245 -0.0546 266 SER A CB  
1937  O OG  . SER A 266 ? 0.9868 1.3191 1.4665 -0.0397 -0.0245 -0.0509 266 SER A OG  
1938  N N   . GLN A 267 ? 1.0687 1.4565 1.5788 -0.0506 -0.0180 -0.0682 267 GLN A N   
1939  C CA  . GLN A 267 ? 1.0790 1.4685 1.6002 -0.0590 -0.0150 -0.0717 267 GLN A CA  
1940  C C   . GLN A 267 ? 1.1422 1.5426 1.6761 -0.0584 -0.0199 -0.0848 267 GLN A C   
1941  O O   . GLN A 267 ? 1.1600 1.5532 1.7030 -0.0639 -0.0201 -0.0894 267 GLN A O   
1942  C CB  . GLN A 267 ? 1.0538 1.4594 1.5767 -0.0639 -0.0085 -0.0674 267 GLN A CB  
1943  C CG  . GLN A 267 ? 1.0339 1.4403 1.5680 -0.0733 -0.0044 -0.0691 267 GLN A CG  
1944  C CD  . GLN A 267 ? 1.0831 1.5083 1.6206 -0.0772 0.0013  -0.0661 267 GLN A CD  
1945  O OE1 . GLN A 267 ? 1.1180 1.5616 1.6538 -0.0727 0.0006  -0.0669 267 GLN A OE1 
1946  N NE2 . GLN A 267 ? 1.0589 1.4796 1.6017 -0.0855 0.0071  -0.0625 267 GLN A NE2 
1947  N N   . PHE A 268 ? 1.2988 1.7162 1.8334 -0.0519 -0.0237 -0.0909 268 PHE A N   
1948  C CA  . PHE A 268 ? 1.2889 1.7163 1.8337 -0.0502 -0.0285 -0.1037 268 PHE A CA  
1949  C C   . PHE A 268 ? 1.3261 1.7377 1.8700 -0.0447 -0.0342 -0.1083 268 PHE A C   
1950  O O   . PHE A 268 ? 1.3645 1.7819 1.9166 -0.0428 -0.0384 -0.1195 268 PHE A O   
1951  C CB  . PHE A 268 ? 1.2687 1.7223 1.8144 -0.0459 -0.0295 -0.1083 268 PHE A CB  
1952  C CG  . PHE A 268 ? 1.2564 1.7268 1.8034 -0.0504 -0.0246 -0.1041 268 PHE A CG  
1953  C CD1 . PHE A 268 ? 1.2978 1.7653 1.8509 -0.0588 -0.0206 -0.1019 268 PHE A CD1 
1954  C CD2 . PHE A 268 ? 1.2508 1.7400 1.7936 -0.0462 -0.0241 -0.1024 268 PHE A CD2 
1955  C CE1 . PHE A 268 ? 1.2856 1.7691 1.8409 -0.0625 -0.0162 -0.0983 268 PHE A CE1 
1956  C CE2 . PHE A 268 ? 1.2331 1.7373 1.7774 -0.0499 -0.0199 -0.0986 268 PHE A CE2 
1957  C CZ  . PHE A 268 ? 1.2925 1.7942 1.8433 -0.0578 -0.0160 -0.0966 268 PHE A CZ  
1958  N N   . ARG A 269 ? 1.1773 1.5693 1.7116 -0.0417 -0.0347 -0.1002 269 ARG A N   
1959  C CA  . ARG A 269 ? 1.1984 1.5724 1.7323 -0.0368 -0.0402 -0.1036 269 ARG A CA  
1960  C C   . ARG A 269 ? 1.2653 1.6148 1.8009 -0.0426 -0.0396 -0.1009 269 ARG A C   
1961  O O   . ARG A 269 ? 1.2724 1.6089 1.8126 -0.0404 -0.0443 -0.1070 269 ARG A O   
1962  C CB  . ARG A 269 ? 1.1408 1.5082 1.6632 -0.0292 -0.0423 -0.0967 269 ARG A CB  
1963  C CG  . ARG A 269 ? 1.0592 1.4218 1.5838 -0.0210 -0.0491 -0.1040 269 ARG A CG  
1964  C CD  . ARG A 269 ? 1.0272 1.4108 1.5621 -0.0187 -0.0513 -0.1170 269 ARG A CD  
1965  N NE  . ARG A 269 ? 0.9917 1.3894 1.5242 -0.0105 -0.0537 -0.1194 269 ARG A NE  
1966  C CZ  . ARG A 269 ? 1.0395 1.4516 1.5792 -0.0061 -0.0566 -0.1307 269 ARG A CZ  
1967  N NH1 . ARG A 269 ? 1.0790 1.4929 1.6282 -0.0090 -0.0579 -0.1409 269 ARG A NH1 
1968  N NH2 . ARG A 269 ? 1.0505 1.4751 1.5878 0.0009  -0.0582 -0.1319 269 ARG A NH2 
1969  N N   . GLU A 270 ? 1.3837 1.7264 1.9157 -0.0498 -0.0337 -0.0917 270 GLU A N   
1970  C CA  . GLU A 270 ? 1.4150 1.7377 1.9507 -0.0570 -0.0320 -0.0898 270 GLU A CA  
1971  C C   . GLU A 270 ? 1.3991 1.7325 1.9499 -0.0631 -0.0318 -0.1002 270 GLU A C   
1972  O O   . GLU A 270 ? 1.4237 1.7455 1.9822 -0.0642 -0.0355 -0.1072 270 GLU A O   
1973  C CB  . GLU A 270 ? 1.4266 1.7401 1.9535 -0.0630 -0.0249 -0.0769 270 GLU A CB  
1974  N N   . THR A 271 ? 1.2482 1.6038 1.8038 -0.0670 -0.0281 -0.1015 271 THR A N   
1975  C CA  . THR A 271 ? 1.2401 1.6086 1.8101 -0.0726 -0.0283 -0.1114 271 THR A CA  
1976  C C   . THR A 271 ? 1.2734 1.6634 1.8478 -0.0665 -0.0331 -0.1227 271 THR A C   
1977  O O   . THR A 271 ? 1.2588 1.6646 1.8271 -0.0614 -0.0328 -0.1206 271 THR A O   
1978  C CB  . THR A 271 ? 1.1541 1.5347 1.7277 -0.0805 -0.0216 -0.1065 271 THR A CB  
1979  O OG1 . THR A 271 ? 1.1337 1.5394 1.7057 -0.0770 -0.0210 -0.1074 271 THR A OG1 
1980  C CG2 . THR A 271 ? 1.1266 1.4901 1.6907 -0.0842 -0.0156 -0.0928 271 THR A CG2 
1981  N N   . SER A 272 ? 1.3067 1.6971 1.8916 -0.0675 -0.0374 -0.1346 272 SER A N   
1982  C CA  . SER A 272 ? 1.2794 1.6886 1.8691 -0.0623 -0.0421 -0.1469 272 SER A CA  
1983  C C   . SER A 272 ? 1.3264 1.7410 1.9065 -0.0524 -0.0443 -0.1454 272 SER A C   
1984  O O   . SER A 272 ? 1.2971 1.7318 1.8735 -0.0499 -0.0427 -0.1437 272 SER A O   
1985  C CB  . SER A 272 ? 1.1560 1.5905 1.7522 -0.0666 -0.0402 -0.1509 272 SER A CB  
1986  O OG  . SER A 272 ? 1.0765 1.5228 1.6653 -0.0660 -0.0358 -0.1413 272 SER A OG  
1987  N N   . PRO A 273 ? 1.4009 1.7982 1.9773 -0.0465 -0.0479 -0.1457 273 PRO A N   
1988  C CA  . PRO A 273 ? 1.3726 1.7755 1.9411 -0.0371 -0.0501 -0.1444 273 PRO A CA  
1989  C C   . PRO A 273 ? 1.3265 1.7490 1.8997 -0.0317 -0.0536 -0.1566 273 PRO A C   
1990  O O   . PRO A 273 ? 1.2799 1.7135 1.8475 -0.0249 -0.0543 -0.1556 273 PRO A O   
1991  C CB  . PRO A 273 ? 1.4335 1.8099 1.9982 -0.0334 -0.0532 -0.1410 273 PRO A CB  
1992  C CG  . PRO A 273 ? 1.5201 1.8829 2.0944 -0.0383 -0.0551 -0.1481 273 PRO A CG  
1993  C CD  . PRO A 273 ? 1.4668 1.8386 2.0467 -0.0481 -0.0504 -0.1472 273 PRO A CD  
1994  N N   . HIS A 274 ? 1.4790 1.9060 2.0622 -0.0345 -0.0558 -0.1682 274 HIS A N   
1995  C CA  . HIS A 274 ? 1.4631 1.9090 2.0502 -0.0298 -0.0588 -0.1805 274 HIS A CA  
1996  C C   . HIS A 274 ? 1.4207 1.8932 2.0049 -0.0300 -0.0561 -0.1793 274 HIS A C   
1997  O O   . HIS A 274 ? 1.3992 1.8882 1.9826 -0.0245 -0.0578 -0.1863 274 HIS A O   
1998  C CB  . HIS A 274 ? 1.4779 1.9213 2.0758 -0.0338 -0.0616 -0.1930 274 HIS A CB  
1999  C CG  . HIS A 274 ? 1.5144 1.9523 2.1178 -0.0439 -0.0590 -0.1898 274 HIS A CG  
2000  N ND1 . HIS A 274 ? 1.5428 1.9561 2.1486 -0.0485 -0.0586 -0.1854 274 HIS A ND1 
2001  C CD2 . HIS A 274 ? 1.5266 1.9809 2.1338 -0.0504 -0.0565 -0.1901 274 HIS A CD2 
2002  C CE1 . HIS A 274 ? 1.5602 1.9752 2.1716 -0.0577 -0.0556 -0.1834 274 HIS A CE1 
2003  N NE2 . HIS A 274 ? 1.5414 1.9814 2.1542 -0.0589 -0.0544 -0.1863 274 HIS A NE2 
2004  N N   . ILE A 275 ? 1.2712 1.7478 1.8534 -0.0360 -0.0518 -0.1704 275 ILE A N   
2005  C CA  . ILE A 275 ? 1.1987 1.6989 1.7775 -0.0357 -0.0493 -0.1676 275 ILE A CA  
2006  C C   . ILE A 275 ? 1.1083 1.6119 1.6772 -0.0285 -0.0486 -0.1607 275 ILE A C   
2007  O O   . ILE A 275 ? 1.0277 1.5515 1.5936 -0.0259 -0.0476 -0.1607 275 ILE A O   
2008  C CB  . ILE A 275 ? 1.1434 1.6465 1.7236 -0.0437 -0.0448 -0.1598 275 ILE A CB  
2009  C CG1 . ILE A 275 ? 1.1033 1.5926 1.6751 -0.0439 -0.0409 -0.1458 275 ILE A CG1 
2010  C CG2 . ILE A 275 ? 1.1770 1.6710 1.7674 -0.0514 -0.0454 -0.1650 275 ILE A CG2 
2011  C CD1 . ILE A 275 ? 1.0586 1.5563 1.6297 -0.0496 -0.0357 -0.1374 275 ILE A CD1 
2012  N N   . LEU A 276 ? 1.1155 1.5997 1.6795 -0.0253 -0.0492 -0.1547 276 LEU A N   
2013  C CA  . LEU A 276 ? 1.0628 1.5488 1.6183 -0.0183 -0.0492 -0.1488 276 LEU A CA  
2014  C C   . LEU A 276 ? 1.0183 1.5063 1.5762 -0.0107 -0.0536 -0.1583 276 LEU A C   
2015  O O   . LEU A 276 ? 1.0422 1.5176 1.6057 -0.0100 -0.0569 -0.1656 276 LEU A O   
2016  C CB  . LEU A 276 ? 1.0900 1.5544 1.6384 -0.0185 -0.0480 -0.1371 276 LEU A CB  
2017  C CG  . LEU A 276 ? 1.0872 1.5498 1.6307 -0.0246 -0.0427 -0.1258 276 LEU A CG  
2018  C CD1 . LEU A 276 ? 1.0572 1.5041 1.5902 -0.0220 -0.0419 -0.1144 276 LEU A CD1 
2019  C CD2 . LEU A 276 ? 1.1140 1.6013 1.6574 -0.0259 -0.0398 -0.1252 276 LEU A CD2 
2020  N N   . ALA A 277 ? 0.9893 1.4932 1.5433 -0.0051 -0.0535 -0.1583 277 ALA A N   
2021  C CA  . ALA A 277 ? 0.9529 1.4600 1.5091 0.0025  -0.0569 -0.1668 277 ALA A CA  
2022  C C   . ALA A 277 ? 0.9646 1.4492 1.5196 0.0068  -0.0599 -0.1637 277 ALA A C   
2023  O O   . ALA A 277 ? 0.9717 1.4466 1.5196 0.0075  -0.0590 -0.1528 277 ALA A O   
2024  C CB  . ALA A 277 ? 0.9935 1.5214 1.5454 0.0071  -0.0555 -0.1656 277 ALA A CB  
2025  N N   . SER A 278 ? 0.9617 1.4374 1.5234 0.0097  -0.0637 -0.1735 278 SER A N   
2026  C CA  . SER A 278 ? 0.9899 1.4442 1.5516 0.0145  -0.0674 -0.1719 278 SER A CA  
2027  C C   . SER A 278 ? 1.0462 1.5064 1.6147 0.0218  -0.0709 -0.1844 278 SER A C   
2028  O O   . SER A 278 ? 1.0995 1.5488 1.6748 0.0226  -0.0740 -0.1930 278 SER A O   
2029  C CB  . SER A 278 ? 0.9430 1.3734 1.5067 0.0092  -0.0684 -0.1696 278 SER A CB  
2030  O OG  . SER A 278 ? 0.9226 1.3580 1.4932 0.0031  -0.0675 -0.1775 278 SER A OG  
2031  N N   . GLY A 279 ? 1.0388 1.5166 1.6055 0.0273  -0.0703 -0.1855 279 GLY A N   
2032  C CA  . GLY A 279 ? 1.0836 1.5692 1.6565 0.0346  -0.0727 -0.1969 279 GLY A CA  
2033  C C   . GLY A 279 ? 1.1774 1.6439 1.7530 0.0410  -0.0772 -0.1966 279 GLY A C   
2034  O O   . GLY A 279 ? 1.2265 1.6827 1.8093 0.0434  -0.0805 -0.2058 279 GLY A O   
2035  N N   . ASP A 280 ? 1.3489 1.8101 1.9186 0.0440  -0.0777 -0.1862 280 ASP A N   
2036  C CA  . ASP A 280 ? 1.3800 1.8220 1.9510 0.0501  -0.0826 -0.1839 280 ASP A CA  
2037  C C   . ASP A 280 ? 1.3941 1.8406 1.9749 0.0579  -0.0858 -0.1967 280 ASP A C   
2038  O O   . ASP A 280 ? 1.4110 1.8404 1.9976 0.0608  -0.0899 -0.2018 280 ASP A O   
2039  C CB  . ASP A 280 ? 1.4216 1.8367 1.9909 0.0458  -0.0846 -0.1787 280 ASP A CB  
2040  C CG  . ASP A 280 ? 1.4224 1.8318 1.9816 0.0389  -0.0812 -0.1652 280 ASP A CG  
2041  O OD1 . ASP A 280 ? 1.4056 1.8269 1.9634 0.0322  -0.0768 -0.1648 280 ASP A OD1 
2042  O OD2 . ASP A 280 ? 1.4385 1.8317 1.9910 0.0403  -0.0831 -0.1551 280 ASP A OD2 
2043  N N   . GLY A 281 ? 1.1821 1.6521 1.7648 0.0615  -0.0836 -0.2018 281 GLY A N   
2044  C CA  . GLY A 281 ? 1.0562 1.5342 1.6483 0.0688  -0.0854 -0.2146 281 GLY A CA  
2045  C C   . GLY A 281 ? 0.9761 1.4825 1.5681 0.0703  -0.0812 -0.2188 281 GLY A C   
2046  O O   . GLY A 281 ? 0.9897 1.5072 1.5744 0.0671  -0.0778 -0.2101 281 GLY A O   
2047  N N   . THR A 282 ? 0.9754 1.4928 1.5752 0.0752  -0.0813 -0.2321 282 THR A N   
2048  C CA  . THR A 282 ? 0.9749 1.5193 1.5747 0.0771  -0.0770 -0.2372 282 THR A CA  
2049  C C   . THR A 282 ? 0.9147 1.4684 1.5205 0.0783  -0.0762 -0.2530 282 THR A C   
2050  O O   . THR A 282 ? 0.8810 1.4421 1.4940 0.0851  -0.0765 -0.2629 282 THR A O   
2051  C CB  . THR A 282 ? 0.9677 1.5193 1.5709 0.0845  -0.0775 -0.2353 282 THR A CB  
2052  O OG1 . THR A 282 ? 1.0143 1.5477 1.6250 0.0908  -0.0829 -0.2379 282 THR A OG1 
2053  C CG2 . THR A 282 ? 0.8782 1.4318 1.4732 0.0819  -0.0761 -0.2207 282 THR A CG2 
2054  N N   . ASN A 283 ? 0.9037 1.4573 1.5066 0.0715  -0.0751 -0.2557 283 ASN A N   
2055  C CA  . ASN A 283 ? 0.8973 1.4625 1.5037 0.0715  -0.0740 -0.2702 283 ASN A CA  
2056  C C   . ASN A 283 ? 0.8706 1.4586 1.4695 0.0666  -0.0693 -0.2691 283 ASN A C   
2057  O O   . ASN A 283 ? 0.8479 1.4383 1.4447 0.0607  -0.0690 -0.2727 283 ASN A O   
2058  C CB  . ASN A 283 ? 0.9682 1.5154 1.5783 0.0677  -0.0773 -0.2761 283 ASN A CB  
2059  C CG  . ASN A 283 ? 1.0485 1.5686 1.6626 0.0698  -0.0819 -0.2712 283 ASN A CG  
2060  O OD1 . ASN A 283 ? 0.9662 1.4814 1.5839 0.0768  -0.0839 -0.2696 283 ASN A OD1 
2061  N ND2 . ASN A 283 ? 1.2020 1.7042 1.8157 0.0637  -0.0838 -0.2686 283 ASN A ND2 
2062  N N   . ARG A 284 ? 0.8845 1.4893 1.4798 0.0690  -0.0660 -0.2639 284 ARG A N   
2063  C CA  . ARG A 284 ? 0.8680 1.4921 1.4549 0.0646  -0.0617 -0.2582 284 ARG A CA  
2064  C C   . ARG A 284 ? 0.8753 1.4904 1.4558 0.0580  -0.0617 -0.2442 284 ARG A C   
2065  O O   . ARG A 284 ? 0.8231 1.4522 1.3968 0.0542  -0.0585 -0.2377 284 ARG A O   
2066  C CB  . ARG A 284 ? 0.8206 1.4606 1.4054 0.0617  -0.0598 -0.2687 284 ARG A CB  
2067  C CG  . ARG A 284 ? 0.8252 1.4885 1.4087 0.0660  -0.0559 -0.2754 284 ARG A CG  
2068  C CD  . ARG A 284 ? 0.9147 1.5942 1.4928 0.0621  -0.0540 -0.2827 284 ARG A CD  
2069  N NE  . ARG A 284 ? 0.9123 1.6150 1.4865 0.0652  -0.0495 -0.2864 284 ARG A NE  
2070  C CZ  . ARG A 284 ? 0.8823 1.6016 1.4478 0.0618  -0.0462 -0.2798 284 ARG A CZ  
2071  N NH1 . ARG A 284 ? 0.8370 1.5529 1.3975 0.0554  -0.0469 -0.2697 284 ARG A NH1 
2072  N NH2 . ARG A 284 ? 0.8521 1.5915 1.4142 0.0647  -0.0419 -0.2834 284 ARG A NH2 
2073  N N   . LYS A 285 ? 0.9373 1.5292 1.5199 0.0565  -0.0651 -0.2393 285 LYS A N   
2074  C CA  . LYS A 285 ? 0.9445 1.5253 1.5214 0.0508  -0.0650 -0.2260 285 LYS A CA  
2075  C C   . LYS A 285 ? 0.9460 1.5178 1.5212 0.0545  -0.0660 -0.2156 285 LYS A C   
2076  O O   . LYS A 285 ? 0.9997 1.5596 1.5803 0.0603  -0.0693 -0.2186 285 LYS A O   
2077  C CB  . LYS A 285 ? 0.9944 1.5548 1.5740 0.0462  -0.0678 -0.2273 285 LYS A CB  
2078  N N   . PRO A 286 ? 0.8293 1.4060 1.3972 0.0518  -0.0635 -0.2038 286 PRO A N   
2079  C CA  . PRO A 286 ? 0.8469 1.4160 1.4127 0.0554  -0.0647 -0.1943 286 PRO A CA  
2080  C C   . PRO A 286 ? 0.8566 1.3991 1.4221 0.0548  -0.0685 -0.1886 286 PRO A C   
2081  O O   . PRO A 286 ? 0.8914 1.4208 1.4581 0.0509  -0.0697 -0.1908 286 PRO A O   
2082  C CB  . PRO A 286 ? 0.7957 1.3766 1.3533 0.0513  -0.0609 -0.1838 286 PRO A CB  
2083  C CG  . PRO A 286 ? 0.8080 1.4084 1.3649 0.0479  -0.0576 -0.1899 286 PRO A CG  
2084  C CD  . PRO A 286 ? 0.8518 1.4442 1.4136 0.0460  -0.0596 -0.1996 286 PRO A CD  
2085  N N   . THR A 287 ? 0.8309 1.3654 1.3945 0.0587  -0.0705 -0.1809 287 THR A N   
2086  C CA  . THR A 287 ? 0.8361 1.3451 1.3976 0.0588  -0.0744 -0.1741 287 THR A CA  
2087  C C   . THR A 287 ? 0.7909 1.2931 1.3431 0.0515  -0.0718 -0.1625 287 THR A C   
2088  O O   . THR A 287 ? 0.7470 1.2535 1.2925 0.0509  -0.0702 -0.1532 287 THR A O   
2089  C CB  . THR A 287 ? 0.7682 1.2719 1.3307 0.0659  -0.0780 -0.1704 287 THR A CB  
2090  O OG1 . THR A 287 ? 0.7150 1.2394 1.2764 0.0677  -0.0751 -0.1686 287 THR A OG1 
2091  C CG2 . THR A 287 ? 0.7920 1.2893 1.3646 0.0729  -0.0824 -0.1807 287 THR A CG2 
2092  N N   . ILE A 288 ? 0.9151 1.4065 1.4672 0.0458  -0.0714 -0.1634 288 ILE A N   
2093  C CA  . ILE A 288 ? 0.9188 1.4029 1.4633 0.0386  -0.0686 -0.1533 288 ILE A CA  
2094  C C   . ILE A 288 ? 0.9913 1.4489 1.5319 0.0388  -0.0717 -0.1456 288 ILE A C   
2095  O O   . ILE A 288 ? 1.0499 1.4917 1.5953 0.0406  -0.0754 -0.1504 288 ILE A O   
2096  C CB  . ILE A 288 ? 0.9570 1.4455 1.5045 0.0318  -0.0662 -0.1585 288 ILE A CB  
2097  C CG1 . ILE A 288 ? 0.9170 1.4324 1.4654 0.0308  -0.0628 -0.1633 288 ILE A CG1 
2098  C CG2 . ILE A 288 ? 0.9876 1.4633 1.5294 0.0244  -0.0639 -0.1488 288 ILE A CG2 
2099  C CD1 . ILE A 288 ? 1.0056 1.5282 1.5596 0.0269  -0.0622 -0.1733 288 ILE A CD1 
2100  N N   . ILE A 289 ? 0.9825 1.4347 1.5138 0.0370  -0.0703 -0.1336 289 ILE A N   
2101  C CA  . ILE A 289 ? 1.0151 1.4427 1.5405 0.0379  -0.0734 -0.1254 289 ILE A CA  
2102  C C   . ILE A 289 ? 1.1100 1.5257 1.6288 0.0298  -0.0699 -0.1173 289 ILE A C   
2103  O O   . ILE A 289 ? 1.0218 1.4271 1.5309 0.0284  -0.0691 -0.1065 289 ILE A O   
2104  C CB  . ILE A 289 ? 0.9438 1.3721 1.4631 0.0430  -0.0752 -0.1181 289 ILE A CB  
2105  C CG1 . ILE A 289 ? 0.8498 1.2995 1.3759 0.0489  -0.0759 -0.1255 289 ILE A CG1 
2106  C CG2 . ILE A 289 ? 0.9297 1.3339 1.4462 0.0471  -0.0809 -0.1139 289 ILE A CG2 
2107  C CD1 . ILE A 289 ? 0.8761 1.3232 1.4123 0.0554  -0.0805 -0.1359 289 ILE A CD1 
2108  N N   . GLY A 290 ? 1.6118 2.0290 2.1360 0.0243  -0.0677 -0.1228 290 GLY A N   
2109  C CA  . GLY A 290 ? 1.6354 2.0406 2.1555 0.0163  -0.0644 -0.1162 290 GLY A CA  
2110  C C   . GLY A 290 ? 1.6124 2.0301 2.1264 0.0113  -0.0587 -0.1087 290 GLY A C   
2111  O O   . GLY A 290 ? 1.5889 2.0165 2.0974 0.0144  -0.0580 -0.1041 290 GLY A O   
2112  N N   . ASP A 291 ? 1.1709 1.5881 1.6863 0.0035  -0.0547 -0.1077 291 ASP A N   
2113  C CA  . ASP A 291 ? 1.0086 1.4365 1.5193 -0.0018 -0.0491 -0.1007 291 ASP A CA  
2114  C C   . ASP A 291 ? 0.9318 1.3858 1.4441 0.0008  -0.0479 -0.1041 291 ASP A C   
2115  O O   . ASP A 291 ? 0.8407 1.3017 1.3462 0.0023  -0.0460 -0.0972 291 ASP A O   
2116  C CB  . ASP A 291 ? 0.9718 1.3849 1.4706 -0.0023 -0.0474 -0.0880 291 ASP A CB  
2117  C CG  . ASP A 291 ? 1.0239 1.4203 1.5202 -0.0097 -0.0440 -0.0821 291 ASP A CG  
2118  O OD1 . ASP A 291 ? 1.0561 1.4474 1.5604 -0.0136 -0.0443 -0.0879 291 ASP A OD1 
2119  O OD2 . ASP A 291 ? 0.9926 1.3808 1.4790 -0.0118 -0.0408 -0.0717 291 ASP A OD2 
2120  N N   . VAL A 292 ? 0.9668 1.4348 1.4880 0.0013  -0.0491 -0.1150 292 VAL A N   
2121  C CA  . VAL A 292 ? 0.9539 1.4469 1.4769 0.0035  -0.0481 -0.1193 292 VAL A CA  
2122  C C   . VAL A 292 ? 1.0303 1.5362 1.5601 -0.0019 -0.0463 -0.1260 292 VAL A C   
2123  O O   . VAL A 292 ? 1.0438 1.5439 1.5804 -0.0035 -0.0484 -0.1341 292 VAL A O   
2124  C CB  . VAL A 292 ? 0.9601 1.4593 1.4864 0.0112  -0.0520 -0.1271 292 VAL A CB  
2125  C CG1 . VAL A 292 ? 0.9130 1.4378 1.4400 0.0131  -0.0502 -0.1303 292 VAL A CG1 
2126  C CG2 . VAL A 292 ? 0.9710 1.4561 1.4921 0.0166  -0.0547 -0.1211 292 VAL A CG2 
2127  N N   . TYR A 293 ? 1.2098 1.7329 1.7378 -0.0046 -0.0428 -0.1229 293 TYR A N   
2128  C CA  . TYR A 293 ? 1.2116 1.7504 1.7458 -0.0088 -0.0418 -0.1295 293 TYR A CA  
2129  C C   . TYR A 293 ? 1.1594 1.7205 1.6938 -0.0044 -0.0424 -0.1350 293 TYR A C   
2130  O O   . TYR A 293 ? 1.1430 1.7143 1.6720 -0.0024 -0.0405 -0.1288 293 TYR A O   
2131  C CB  . TYR A 293 ? 1.2100 1.7523 1.7431 -0.0154 -0.0375 -0.1220 293 TYR A CB  
2132  C CG  . TYR A 293 ? 1.2323 1.7939 1.7714 -0.0190 -0.0369 -0.1282 293 TYR A CG  
2133  C CD1 . TYR A 293 ? 1.1914 1.7732 1.7279 -0.0180 -0.0352 -0.1260 293 TYR A CD1 
2134  C CD2 . TYR A 293 ? 1.2323 1.7917 1.7797 -0.0233 -0.0385 -0.1363 293 TYR A CD2 
2135  C CE1 . TYR A 293 ? 1.1407 1.7400 1.6822 -0.0210 -0.0353 -0.1315 293 TYR A CE1 
2136  C CE2 . TYR A 293 ? 1.1914 1.7687 1.7442 -0.0266 -0.0386 -0.1423 293 TYR A CE2 
2137  C CZ  . TYR A 293 ? 1.1379 1.7352 1.6875 -0.0252 -0.0372 -0.1397 293 TYR A CZ  
2138  O OH  . TYR A 293 ? 1.1127 1.7276 1.6671 -0.0281 -0.0379 -0.1454 293 TYR A OH  
2139  N N   . ILE A 294 ? 1.3562 1.9243 1.8966 -0.0031 -0.0451 -0.1466 294 ILE A N   
2140  C CA  . ILE A 294 ? 1.3403 1.9292 1.8807 0.0010  -0.0455 -0.1530 294 ILE A CA  
2141  C C   . ILE A 294 ? 1.3309 1.9351 1.8752 -0.0034 -0.0453 -0.1594 294 ILE A C   
2142  O O   . ILE A 294 ? 1.3530 1.9519 1.9035 -0.0065 -0.0472 -0.1670 294 ILE A O   
2143  C CB  . ILE A 294 ? 1.3895 1.9750 1.9328 0.0073  -0.0488 -0.1619 294 ILE A CB  
2144  C CG1 . ILE A 294 ? 1.3722 1.9480 1.9114 0.0126  -0.0493 -0.1551 294 ILE A CG1 
2145  C CG2 . ILE A 294 ? 1.4278 2.0351 1.9723 0.0101  -0.0490 -0.1709 294 ILE A CG2 
2146  C CD1 . ILE A 294 ? 1.3802 1.9531 1.9232 0.0193  -0.0525 -0.1634 294 ILE A CD1 
2147  N N   . HIS A 295 ? 1.0819 1.7050 1.6227 -0.0037 -0.0432 -0.1563 295 HIS A N   
2148  C CA  . HIS A 295 ? 1.0485 1.6879 1.5921 -0.0072 -0.0435 -0.1621 295 HIS A CA  
2149  C C   . HIS A 295 ? 1.0379 1.6876 1.5836 -0.0036 -0.0462 -0.1749 295 HIS A C   
2150  O O   . HIS A 295 ? 1.0608 1.7127 1.6041 0.0023  -0.0464 -0.1770 295 HIS A O   
2151  C CB  . HIS A 295 ? 1.0159 1.6717 1.5546 -0.0079 -0.0408 -0.1545 295 HIS A CB  
2152  C CG  . HIS A 295 ? 1.0114 1.6819 1.5532 -0.0124 -0.0413 -0.1581 295 HIS A CG  
2153  N ND1 . HIS A 295 ? 0.9998 1.6874 1.5414 -0.0108 -0.0433 -0.1670 295 HIS A ND1 
2154  C CD2 . HIS A 295 ? 1.0480 1.7188 1.5933 -0.0183 -0.0403 -0.1543 295 HIS A CD2 
2155  C CE1 . HIS A 295 ? 1.0660 1.7636 1.6105 -0.0155 -0.0440 -0.1683 295 HIS A CE1 
2156  N NE2 . HIS A 295 ? 1.0567 1.7448 1.6043 -0.0200 -0.0422 -0.1608 295 HIS A NE2 
2157  N N   . PRO A 296 ? 1.0177 1.6738 1.5681 -0.0071 -0.0482 -0.1838 296 PRO A N   
2158  C CA  . PRO A 296 ? 1.0029 1.6692 1.5543 -0.0037 -0.0505 -0.1966 296 PRO A CA  
2159  C C   . PRO A 296 ? 0.9629 1.6504 1.5078 0.0001  -0.0491 -0.1967 296 PRO A C   
2160  O O   . PRO A 296 ? 1.0016 1.6966 1.5458 0.0042  -0.0501 -0.2060 296 PRO A O   
2161  C CB  . PRO A 296 ? 1.1615 1.8301 1.7189 -0.0093 -0.0530 -0.2047 296 PRO A CB  
2162  C CG  . PRO A 296 ? 1.1319 1.7999 1.6904 -0.0153 -0.0512 -0.1951 296 PRO A CG  
2163  C CD  . PRO A 296 ? 1.0669 1.7195 1.6228 -0.0142 -0.0485 -0.1836 296 PRO A CD  
2164  N N   . SER A 297 ? 0.9373 1.6343 1.4774 -0.0012 -0.0467 -0.1867 297 SER A N   
2165  C CA  . SER A 297 ? 1.0309 1.7476 1.5644 0.0018  -0.0452 -0.1857 297 SER A CA  
2166  C C   . SER A 297 ? 0.9398 1.6554 1.4690 0.0072  -0.0428 -0.1800 297 SER A C   
2167  O O   . SER A 297 ? 0.9453 1.6761 1.4690 0.0094  -0.0410 -0.1771 297 SER A O   
2168  C CB  . SER A 297 ? 1.0852 1.8132 1.6162 -0.0022 -0.0441 -0.1780 297 SER A CB  
2169  O OG  . SER A 297 ? 1.1315 1.8784 1.6558 0.0005  -0.0430 -0.1772 297 SER A OG  
2170  N N   . VAL A 298 ? 0.9061 1.6044 1.4379 0.0093  -0.0431 -0.1780 298 VAL A N   
2171  C CA  . VAL A 298 ? 0.8225 1.5195 1.3510 0.0143  -0.0414 -0.1726 298 VAL A CA  
2172  C C   . VAL A 298 ? 0.8331 1.5367 1.3629 0.0198  -0.0420 -0.1826 298 VAL A C   
2173  O O   . VAL A 298 ? 0.8736 1.5773 1.4072 0.0200  -0.0440 -0.1939 298 VAL A O   
2174  C CB  . VAL A 298 ? 0.8434 1.5190 1.3734 0.0144  -0.0417 -0.1655 298 VAL A CB  
2175  C CG1 . VAL A 298 ? 0.9227 1.5907 1.4523 0.0085  -0.0409 -0.1575 298 VAL A CG1 
2176  C CG2 . VAL A 298 ? 0.8815 1.5426 1.4173 0.0165  -0.0447 -0.1739 298 VAL A CG2 
2177  N N   . LYS A 299 ? 0.8364 1.5458 1.3634 0.0241  -0.0400 -0.1787 299 LYS A N   
2178  C CA  . LYS A 299 ? 0.7885 1.5039 1.3175 0.0298  -0.0398 -0.1871 299 LYS A CA  
2179  C C   . LYS A 299 ? 0.7675 1.4687 1.2996 0.0338  -0.0406 -0.1833 299 LYS A C   
2180  O O   . LYS A 299 ? 0.7431 1.4415 1.2723 0.0339  -0.0393 -0.1727 299 LYS A O   
2181  C CB  . LYS A 299 ? 0.7828 1.5197 1.3063 0.0314  -0.0367 -0.1864 299 LYS A CB  
2182  C CG  . LYS A 299 ? 0.8682 1.6124 1.3939 0.0373  -0.0355 -0.1941 299 LYS A CG  
2183  C CD  . LYS A 299 ? 0.9900 1.7555 1.5097 0.0381  -0.0318 -0.1930 299 LYS A CD  
2184  C CE  . LYS A 299 ? 1.1056 1.8843 1.6209 0.0355  -0.0320 -0.1999 299 LYS A CE  
2185  N NZ  . LYS A 299 ? 1.1122 1.8911 1.6313 0.0378  -0.0335 -0.2144 299 LYS A NZ  
2186  N N   . LEU A 300 ? 0.8666 1.5585 1.4048 0.0373  -0.0429 -0.1921 300 LEU A N   
2187  C CA  . LEU A 300 ? 0.8655 1.5413 1.4075 0.0412  -0.0448 -0.1893 300 LEU A CA  
2188  C C   . LEU A 300 ? 0.8850 1.5668 1.4320 0.0479  -0.0449 -0.1979 300 LEU A C   
2189  O O   . LEU A 300 ? 0.8955 1.5907 1.4436 0.0493  -0.0438 -0.2080 300 LEU A O   
2190  C CB  . LEU A 300 ? 0.8564 1.5104 1.4020 0.0390  -0.0483 -0.1904 300 LEU A CB  
2191  C CG  . LEU A 300 ? 0.8411 1.4882 1.3829 0.0321  -0.0478 -0.1822 300 LEU A CG  
2192  C CD1 . LEU A 300 ? 0.9265 1.5524 1.4724 0.0297  -0.0507 -0.1839 300 LEU A CD1 
2193  C CD2 . LEU A 300 ? 0.8177 1.4638 1.3539 0.0313  -0.0459 -0.1687 300 LEU A CD2 
2194  N N   . HIS A 301 ? 0.8052 1.4768 1.3552 0.0520  -0.0464 -0.1940 301 HIS A N   
2195  C CA  . HIS A 301 ? 0.7716 1.4457 1.3284 0.0589  -0.0471 -0.2014 301 HIS A CA  
2196  C C   . HIS A 301 ? 0.7731 1.4249 1.3356 0.0618  -0.0518 -0.2021 301 HIS A C   
2197  O O   . HIS A 301 ? 0.7565 1.3933 1.3162 0.0601  -0.0536 -0.1923 301 HIS A O   
2198  C CB  . HIS A 301 ? 0.7282 1.4146 1.2840 0.0618  -0.0445 -0.1956 301 HIS A CB  
2199  C CG  . HIS A 301 ? 0.7058 1.4019 1.2689 0.0682  -0.0437 -0.2046 301 HIS A CG  
2200  N ND1 . HIS A 301 ? 0.7010 1.3853 1.2722 0.0738  -0.0471 -0.2078 301 HIS A ND1 
2201  C CD2 . HIS A 301 ? 0.6989 1.4154 1.2624 0.0700  -0.0397 -0.2113 301 HIS A CD2 
2202  C CE1 . HIS A 301 ? 0.7297 1.4274 1.3070 0.0789  -0.0452 -0.2163 301 HIS A CE1 
2203  N NE2 . HIS A 301 ? 0.7189 1.4362 1.2914 0.0765  -0.0404 -0.2185 301 HIS A NE2 
2204  N N   . PRO A 302 ? 0.8711 1.5198 1.4412 0.0664  -0.0538 -0.2136 302 PRO A N   
2205  C CA  . PRO A 302 ? 0.9055 1.5314 1.4811 0.0692  -0.0587 -0.2146 302 PRO A CA  
2206  C C   . PRO A 302 ? 0.9132 1.5301 1.4903 0.0734  -0.0611 -0.2067 302 PRO A C   
2207  O O   . PRO A 302 ? 0.9311 1.5272 1.5104 0.0749  -0.0655 -0.2045 302 PRO A O   
2208  C CB  . PRO A 302 ? 0.9135 1.5424 1.4974 0.0739  -0.0597 -0.2297 302 PRO A CB  
2209  C CG  . PRO A 302 ? 0.8966 1.5469 1.4772 0.0715  -0.0555 -0.2365 302 PRO A CG  
2210  C CD  . PRO A 302 ? 0.8671 1.5322 1.4407 0.0692  -0.0516 -0.2265 302 PRO A CD  
2211  N N   . THR A 303 ? 0.7938 1.4252 1.3699 0.0753  -0.0585 -0.2022 303 THR A N   
2212  C CA  . THR A 303 ? 0.6608 1.2848 1.2389 0.0794  -0.0611 -0.1952 303 THR A CA  
2213  C C   . THR A 303 ? 0.6786 1.2920 1.2480 0.0751  -0.0618 -0.1812 303 THR A C   
2214  O O   . THR A 303 ? 0.6927 1.2974 1.2626 0.0780  -0.0647 -0.1749 303 THR A O   
2215  C CB  . THR A 303 ? 0.6133 1.2576 1.1955 0.0834  -0.0582 -0.1972 303 THR A CB  
2216  O OG1 . THR A 303 ? 0.6037 1.2654 1.1787 0.0787  -0.0530 -0.1929 303 THR A OG1 
2217  C CG2 . THR A 303 ? 0.6466 1.3001 1.2383 0.0888  -0.0576 -0.2113 303 THR A CG2 
2218  N N   . ALA A 304 ? 0.6919 1.3058 1.2536 0.0683  -0.0593 -0.1765 304 ALA A N   
2219  C CA  . ALA A 304 ? 0.6384 1.2431 1.1917 0.0640  -0.0592 -0.1637 304 ALA A CA  
2220  C C   . ALA A 304 ? 0.6147 1.1944 1.1663 0.0625  -0.0630 -0.1604 304 ALA A C   
2221  O O   . ALA A 304 ? 0.6687 1.2406 1.2236 0.0615  -0.0643 -0.1673 304 ALA A O   
2222  C CB  . ALA A 304 ? 0.6153 1.2325 1.1618 0.0576  -0.0545 -0.1601 304 ALA A CB  
2223  N N   . LYS A 305 ? 0.6068 1.1737 1.1529 0.0622  -0.0648 -0.1498 305 LYS A N   
2224  C CA  . LYS A 305 ? 0.5847 1.1273 1.1271 0.0604  -0.0680 -0.1446 305 LYS A CA  
2225  C C   . LYS A 305 ? 0.6292 1.1689 1.1622 0.0532  -0.0646 -0.1352 305 LYS A C   
2226  O O   . LYS A 305 ? 0.5200 1.0623 1.0467 0.0523  -0.0632 -0.1263 305 LYS A O   
2227  C CB  . LYS A 305 ? 0.5714 1.1001 1.1138 0.0658  -0.0729 -0.1400 305 LYS A CB  
2228  C CG  . LYS A 305 ? 0.6278 1.1302 1.1656 0.0644  -0.0765 -0.1345 305 LYS A CG  
2229  C CD  . LYS A 305 ? 0.5919 1.0811 1.1295 0.0704  -0.0822 -0.1305 305 LYS A CD  
2230  C CE  . LYS A 305 ? 0.6062 1.0930 1.1551 0.0773  -0.0866 -0.1406 305 LYS A CE  
2231  N NZ  . LYS A 305 ? 0.6367 1.1089 1.1862 0.0834  -0.0932 -0.1368 305 LYS A NZ  
2232  N N   . ILE A 306 ? 0.6358 1.1703 1.1687 0.0481  -0.0633 -0.1374 306 ILE A N   
2233  C CA  . ILE A 306 ? 0.6280 1.1600 1.1537 0.0410  -0.0598 -0.1297 306 ILE A CA  
2234  C C   . ILE A 306 ? 0.6954 1.2021 1.2166 0.0393  -0.0621 -0.1229 306 ILE A C   
2235  O O   . ILE A 306 ? 0.7267 1.2206 1.2510 0.0375  -0.0636 -0.1268 306 ILE A O   
2236  C CB  . ILE A 306 ? 0.6621 1.2046 1.1910 0.0362  -0.0571 -0.1363 306 ILE A CB  
2237  C CG1 . ILE A 306 ? 0.6611 1.2255 1.1955 0.0393  -0.0561 -0.1459 306 ILE A CG1 
2238  C CG2 . ILE A 306 ? 0.6271 1.1748 1.1500 0.0297  -0.0528 -0.1285 306 ILE A CG2 
2239  C CD1 . ILE A 306 ? 0.5976 1.1799 1.1283 0.0403  -0.0532 -0.1411 306 ILE A CD1 
2240  N N   . GLY A 307 ? 0.7118 1.2106 1.2250 0.0397  -0.0623 -0.1127 307 GLY A N   
2241  C CA  . GLY A 307 ? 0.7452 1.2198 1.2524 0.0387  -0.0646 -0.1055 307 GLY A CA  
2242  C C   . GLY A 307 ? 0.7862 1.2520 1.2888 0.0311  -0.0609 -0.1006 307 GLY A C   
2243  O O   . GLY A 307 ? 0.8215 1.2974 1.3282 0.0266  -0.0578 -0.1052 307 GLY A O   
2244  N N   . PRO A 308 ? 0.7750 1.2220 1.2687 0.0293  -0.0613 -0.0911 308 PRO A N   
2245  C CA  . PRO A 308 ? 0.8550 1.2918 1.3446 0.0220  -0.0575 -0.0862 308 PRO A CA  
2246  C C   . PRO A 308 ? 0.8275 1.2773 1.3123 0.0173  -0.0517 -0.0803 308 PRO A C   
2247  O O   . PRO A 308 ? 0.7987 1.2586 1.2794 0.0197  -0.0510 -0.0765 308 PRO A O   
2248  C CB  . PRO A 308 ? 0.8419 1.2532 1.3228 0.0228  -0.0602 -0.0782 308 PRO A CB  
2249  C CG  . PRO A 308 ? 0.8220 1.2356 1.2989 0.0293  -0.0637 -0.0752 308 PRO A CG  
2250  C CD  . PRO A 308 ? 0.7874 1.2204 1.2747 0.0342  -0.0655 -0.0851 308 PRO A CD  
2251  N N   . ASN A 309 ? 0.7575 1.2067 1.2436 0.0104  -0.0477 -0.0799 309 ASN A N   
2252  C CA  . ASN A 309 ? 0.6342 1.0928 1.1163 0.0054  -0.0420 -0.0738 309 ASN A CA  
2253  C C   . ASN A 309 ? 0.6141 1.0976 1.0992 0.0073  -0.0407 -0.0768 309 ASN A C   
2254  O O   . ASN A 309 ? 0.6299 1.1195 1.1089 0.0086  -0.0391 -0.0708 309 ASN A O   
2255  C CB  . ASN A 309 ? 0.6653 1.1096 1.1353 0.0047  -0.0404 -0.0625 309 ASN A CB  
2256  C CG  . ASN A 309 ? 0.6994 1.1517 1.1656 -0.0006 -0.0342 -0.0564 309 ASN A CG  
2257  O OD1 . ASN A 309 ? 0.7049 1.1697 1.1779 -0.0049 -0.0311 -0.0600 309 ASN A OD1 
2258  N ND2 . ASN A 309 ? 0.7184 1.1638 1.1740 -0.0002 -0.0326 -0.0474 309 ASN A ND2 
2259  N N   . VAL A 310 ? 0.6618 1.1591 1.1559 0.0074  -0.0414 -0.0864 310 VAL A N   
2260  C CA  . VAL A 310 ? 0.6415 1.1626 1.1386 0.0088  -0.0401 -0.0899 310 VAL A CA  
2261  C C   . VAL A 310 ? 0.6825 1.2152 1.1863 0.0039  -0.0381 -0.0960 310 VAL A C   
2262  O O   . VAL A 310 ? 0.7837 1.3110 1.2937 0.0027  -0.0400 -0.1032 310 VAL A O   
2263  C CB  . VAL A 310 ? 0.5728 1.1014 1.0733 0.0157  -0.0438 -0.0964 310 VAL A CB  
2264  C CG1 . VAL A 310 ? 0.6814 1.1992 1.1881 0.0177  -0.0477 -0.1045 310 VAL A CG1 
2265  C CG2 . VAL A 310 ? 0.5670 1.1203 1.0712 0.0163  -0.0421 -0.1013 310 VAL A CG2 
2266  N N   . SER A 311 ? 0.6608 1.2091 1.1637 0.0012  -0.0345 -0.0931 311 SER A N   
2267  C CA  . SER A 311 ? 0.7007 1.2612 1.2096 -0.0036 -0.0328 -0.0978 311 SER A CA  
2268  C C   . SER A 311 ? 0.6880 1.2717 1.1983 -0.0011 -0.0327 -0.1018 311 SER A C   
2269  O O   . SER A 311 ? 0.6878 1.2814 1.1940 -0.0010 -0.0302 -0.0956 311 SER A O   
2270  C CB  . SER A 311 ? 0.6563 1.2133 1.1631 -0.0096 -0.0285 -0.0901 311 SER A CB  
2271  O OG  . SER A 311 ? 0.6719 1.2069 1.1750 -0.0114 -0.0280 -0.0847 311 SER A OG  
2272  N N   . ILE A 312 ? 0.8122 1.4041 1.3281 0.0008  -0.0353 -0.1120 312 ILE A N   
2273  C CA  . ILE A 312 ? 0.8679 1.4812 1.3845 0.0034  -0.0353 -0.1165 312 ILE A CA  
2274  C C   . ILE A 312 ? 0.9466 1.5736 1.4668 -0.0012 -0.0342 -0.1201 312 ILE A C   
2275  O O   . ILE A 312 ? 0.9731 1.5951 1.4987 -0.0049 -0.0353 -0.1254 312 ILE A O   
2276  C CB  . ILE A 312 ? 0.8725 1.4877 1.3924 0.0086  -0.0384 -0.1261 312 ILE A CB  
2277  C CG1 . ILE A 312 ? 0.7902 1.3949 1.3072 0.0138  -0.0398 -0.1222 312 ILE A CG1 
2278  C CG2 . ILE A 312 ? 0.8709 1.5088 1.3915 0.0104  -0.0379 -0.1317 312 ILE A CG2 
2279  C CD1 . ILE A 312 ? 0.7601 1.3631 1.2819 0.0190  -0.0431 -0.1316 312 ILE A CD1 
2280  N N   . SER A 313 ? 1.0656 1.7100 1.5831 -0.0011 -0.0324 -0.1171 313 SER A N   
2281  C CA  . SER A 313 ? 1.0272 1.6858 1.5475 -0.0051 -0.0317 -0.1193 313 SER A CA  
2282  C C   . SER A 313 ? 1.0388 1.7133 1.5611 -0.0029 -0.0339 -0.1295 313 SER A C   
2283  O O   . SER A 313 ? 1.0721 1.7459 1.5943 0.0015  -0.0354 -0.1351 313 SER A O   
2284  C CB  . SER A 313 ? 0.9973 1.6649 1.5135 -0.0061 -0.0287 -0.1098 313 SER A CB  
2285  O OG  . SER A 313 ? 1.0048 1.6578 1.5189 -0.0084 -0.0263 -0.1010 313 SER A OG  
2286  N N   . ALA A 314 ? 0.9782 1.6676 1.5021 -0.0058 -0.0340 -0.1319 314 ALA A N   
2287  C CA  . ALA A 314 ? 0.9715 1.6758 1.4963 -0.0044 -0.0362 -0.1420 314 ALA A CA  
2288  C C   . ALA A 314 ? 0.9341 1.6535 1.4527 0.0000  -0.0350 -0.1400 314 ALA A C   
2289  O O   . ALA A 314 ? 0.8966 1.6187 1.4110 0.0007  -0.0326 -0.1305 314 ALA A O   
2290  C CB  . ALA A 314 ? 1.0209 1.7352 1.5496 -0.0092 -0.0374 -0.1454 314 ALA A CB  
2291  N N   . ASN A 315 ? 0.9898 1.7188 1.5080 0.0029  -0.0365 -0.1494 315 ASN A N   
2292  C CA  . ASN A 315 ? 1.0312 1.7768 1.5437 0.0065  -0.0352 -0.1491 315 ASN A CA  
2293  C C   . ASN A 315 ? 1.0214 1.7628 1.5304 0.0100  -0.0327 -0.1408 315 ASN A C   
2294  O O   . ASN A 315 ? 1.0310 1.7818 1.5353 0.0106  -0.0306 -0.1334 315 ASN A O   
2295  C CB  . ASN A 315 ? 1.0393 1.8011 1.5487 0.0039  -0.0349 -0.1459 315 ASN A CB  
2296  C CG  . ASN A 315 ? 1.0135 1.7838 1.5253 0.0015  -0.0379 -0.1560 315 ASN A CG  
2297  O OD1 . ASN A 315 ? 1.0736 1.8393 1.5905 -0.0029 -0.0396 -0.1570 315 ASN A OD1 
2298  N ND2 . ASN A 315 ? 0.9683 1.7513 1.4765 0.0042  -0.0386 -0.1637 315 ASN A ND2 
2299  N N   . VAL A 316 ? 0.9336 1.6604 1.4453 0.0124  -0.0333 -0.1421 316 VAL A N   
2300  C CA  . VAL A 316 ? 0.8411 1.5630 1.3505 0.0161  -0.0319 -0.1357 316 VAL A CA  
2301  C C   . VAL A 316 ? 0.7754 1.4985 1.2872 0.0210  -0.0327 -0.1442 316 VAL A C   
2302  O O   . VAL A 316 ? 0.8031 1.5203 1.3195 0.0215  -0.0349 -0.1533 316 VAL A O   
2303  C CB  . VAL A 316 ? 0.8216 1.5237 1.3317 0.0147  -0.0320 -0.1282 316 VAL A CB  
2304  C CG1 . VAL A 316 ? 0.8500 1.5366 1.3652 0.0140  -0.0346 -0.1348 316 VAL A CG1 
2305  C CG2 . VAL A 316 ? 0.7626 1.4599 1.2700 0.0186  -0.0312 -0.1219 316 VAL A CG2 
2306  N N   . ARG A 317 ? 0.7637 1.4948 1.2731 0.0246  -0.0309 -0.1413 317 ARG A N   
2307  C CA  . ARG A 317 ? 0.7898 1.5247 1.3021 0.0295  -0.0310 -0.1491 317 ARG A CA  
2308  C C   . ARG A 317 ? 0.7711 1.4918 1.2861 0.0327  -0.0320 -0.1451 317 ARG A C   
2309  O O   . ARG A 317 ? 0.7358 1.4572 1.2482 0.0335  -0.0305 -0.1365 317 ARG A O   
2310  C CB  . ARG A 317 ? 0.8680 1.6232 1.3766 0.0312  -0.0281 -0.1496 317 ARG A CB  
2311  C CG  . ARG A 317 ? 0.8575 1.6273 1.3627 0.0288  -0.0277 -0.1549 317 ARG A CG  
2312  C CD  . ARG A 317 ? 0.9338 1.7220 1.4358 0.0316  -0.0250 -0.1589 317 ARG A CD  
2313  N NE  . ARG A 317 ? 0.9923 1.7880 1.4903 0.0321  -0.0220 -0.1490 317 ARG A NE  
2314  C CZ  . ARG A 317 ? 1.0550 1.8629 1.5465 0.0298  -0.0202 -0.1433 317 ARG A CZ  
2315  N NH1 . ARG A 317 ? 1.0979 1.9129 1.5862 0.0271  -0.0215 -0.1466 317 ARG A NH1 
2316  N NH2 . ARG A 317 ? 1.0124 1.8256 1.5010 0.0304  -0.0175 -0.1344 317 ARG A NH2 
2317  N N   . VAL A 318 ? 0.7439 1.4514 1.2642 0.0347  -0.0348 -0.1515 318 VAL A N   
2318  C CA  . VAL A 318 ? 0.7225 1.4151 1.2456 0.0381  -0.0367 -0.1487 318 VAL A CA  
2319  C C   . VAL A 318 ? 0.7397 1.4402 1.2676 0.0438  -0.0367 -0.1560 318 VAL A C   
2320  O O   . VAL A 318 ? 0.7856 1.4912 1.3174 0.0456  -0.0371 -0.1669 318 VAL A O   
2321  C CB  . VAL A 318 ? 0.6866 1.3587 1.2126 0.0369  -0.0400 -0.1505 318 VAL A CB  
2322  C CG1 . VAL A 318 ? 0.6482 1.3057 1.1776 0.0415  -0.0428 -0.1497 318 VAL A CG1 
2323  C CG2 . VAL A 318 ? 0.7041 1.3678 1.2257 0.0312  -0.0394 -0.1418 318 VAL A CG2 
2324  N N   . GLY A 319 ? 0.7817 1.4835 1.3098 0.0468  -0.0360 -0.1504 319 GLY A N   
2325  C CA  . GLY A 319 ? 0.7195 1.4295 1.2533 0.0522  -0.0357 -0.1566 319 GLY A CA  
2326  C C   . GLY A 319 ? 0.6867 1.3815 1.2276 0.0565  -0.0397 -0.1621 319 GLY A C   
2327  O O   . GLY A 319 ? 0.6676 1.3447 1.2086 0.0551  -0.0429 -0.1612 319 GLY A O   
2328  N N   . PRO A 320 ? 0.7225 1.4243 1.2699 0.0618  -0.0395 -0.1678 320 PRO A N   
2329  C CA  . PRO A 320 ? 0.7010 1.3898 1.2564 0.0669  -0.0436 -0.1737 320 PRO A CA  
2330  C C   . PRO A 320 ? 0.6745 1.3499 1.2309 0.0691  -0.0469 -0.1654 320 PRO A C   
2331  O O   . PRO A 320 ? 0.6978 1.3792 1.2518 0.0686  -0.0455 -0.1575 320 PRO A O   
2332  C CB  . PRO A 320 ? 0.7077 1.4131 1.2700 0.0716  -0.0413 -0.1838 320 PRO A CB  
2333  C CG  . PRO A 320 ? 0.7609 1.4842 1.3193 0.0701  -0.0367 -0.1780 320 PRO A CG  
2334  C CD  . PRO A 320 ? 0.7648 1.4877 1.3131 0.0636  -0.0353 -0.1697 320 PRO A CD  
2335  N N   . GLY A 321 ? 0.6353 1.2918 1.1953 0.0715  -0.0517 -0.1673 321 GLY A N   
2336  C CA  . GLY A 321 ? 0.5818 1.2239 1.1427 0.0743  -0.0559 -0.1604 321 GLY A CA  
2337  C C   . GLY A 321 ? 0.5825 1.2175 1.1340 0.0698  -0.0556 -0.1476 321 GLY A C   
2338  O O   . GLY A 321 ? 0.5985 1.2298 1.1495 0.0718  -0.0575 -0.1412 321 GLY A O   
2339  N N   . VAL A 322 ? 0.5808 1.2140 1.1250 0.0639  -0.0533 -0.1441 322 VAL A N   
2340  C CA  . VAL A 322 ? 0.5835 1.2101 1.1187 0.0595  -0.0524 -0.1324 322 VAL A CA  
2341  C C   . VAL A 322 ? 0.5373 1.1404 1.0690 0.0579  -0.0558 -0.1287 322 VAL A C   
2342  O O   . VAL A 322 ? 0.5331 1.1273 1.0682 0.0581  -0.0577 -0.1350 322 VAL A O   
2343  C CB  . VAL A 322 ? 0.5797 1.2204 1.1096 0.0540  -0.0475 -0.1301 322 VAL A CB  
2344  C CG1 . VAL A 322 ? 0.6300 1.2934 1.1626 0.0556  -0.0440 -0.1339 322 VAL A CG1 
2345  C CG2 . VAL A 322 ? 0.5905 1.2278 1.1201 0.0505  -0.0471 -0.1353 322 VAL A CG2 
2346  N N   . ARG A 323 ? 0.4818 1.0744 1.0064 0.0562  -0.0566 -0.1183 323 ARG A N   
2347  C CA  . ARG A 323 ? 0.4928 1.0622 1.0126 0.0549  -0.0596 -0.1132 323 ARG A CA  
2348  C C   . ARG A 323 ? 0.5269 1.0930 1.0379 0.0483  -0.0561 -0.1052 323 ARG A C   
2349  O O   . ARG A 323 ? 0.5628 1.1366 1.0688 0.0467  -0.0536 -0.0985 323 ARG A O   
2350  C CB  . ARG A 323 ? 0.5001 1.0578 1.0185 0.0593  -0.0641 -0.1081 323 ARG A CB  
2351  C CG  . ARG A 323 ? 0.5108 1.0435 1.0239 0.0588  -0.0679 -0.1033 323 ARG A CG  
2352  C CD  . ARG A 323 ? 0.5234 1.0461 1.0439 0.0625  -0.0719 -0.1114 323 ARG A CD  
2353  N NE  . ARG A 323 ? 0.5864 1.0842 1.1015 0.0624  -0.0759 -0.1062 323 ARG A NE  
2354  C CZ  . ARG A 323 ? 0.6238 1.1085 1.1354 0.0578  -0.0748 -0.1052 323 ARG A CZ  
2355  N NH1 . ARG A 323 ? 0.6285 1.1235 1.1424 0.0532  -0.0704 -0.1096 323 ARG A NH1 
2356  N NH2 . ARG A 323 ? 0.7093 1.1709 1.2152 0.0578  -0.0782 -0.0997 323 ARG A NH2 
2357  N N   . LEU A 324 ? 0.5396 1.0944 1.0494 0.0446  -0.0559 -0.1061 324 LEU A N   
2358  C CA  . LEU A 324 ? 0.4956 1.0480 0.9987 0.0381  -0.0521 -0.0996 324 LEU A CA  
2359  C C   . LEU A 324 ? 0.5090 1.0378 1.0076 0.0358  -0.0538 -0.0949 324 LEU A C   
2360  O O   . LEU A 324 ? 0.5721 1.0919 1.0748 0.0350  -0.0553 -0.1003 324 LEU A O   
2361  C CB  . LEU A 324 ? 0.5581 1.1250 1.0651 0.0343  -0.0489 -0.1057 324 LEU A CB  
2362  C CG  . LEU A 324 ? 0.5330 1.1233 1.0437 0.0362  -0.0470 -0.1108 324 LEU A CG  
2363  C CD1 . LEU A 324 ? 0.5892 1.1915 1.1028 0.0326  -0.0447 -0.1172 324 LEU A CD1 
2364  C CD2 . LEU A 324 ? 0.5076 1.1071 1.0128 0.0358  -0.0444 -0.1025 324 LEU A CD2 
2365  N N   . ILE A 325 ? 0.5107 1.0293 1.0005 0.0347  -0.0534 -0.0850 325 ILE A N   
2366  C CA  . ILE A 325 ? 0.5984 1.0950 1.0817 0.0319  -0.0540 -0.0790 325 ILE A CA  
2367  C C   . ILE A 325 ? 0.6128 1.1097 1.0874 0.0271  -0.0494 -0.0698 325 ILE A C   
2368  O O   . ILE A 325 ? 0.6199 1.1280 1.0916 0.0280  -0.0479 -0.0662 325 ILE A O   
2369  C CB  . ILE A 325 ? 0.6208 1.0990 1.1007 0.0368  -0.0595 -0.0761 325 ILE A CB  
2370  C CG1 . ILE A 325 ? 0.6309 1.1112 1.1042 0.0393  -0.0604 -0.0692 325 ILE A CG1 
2371  C CG2 . ILE A 325 ? 0.6631 1.1426 1.1526 0.0425  -0.0642 -0.0854 325 ILE A CG2 
2372  C CD1 . ILE A 325 ? 0.6334 1.0970 1.1035 0.0445  -0.0666 -0.0665 325 ILE A CD1 
2373  N N   . SER A 326 ? 0.6204 1.1053 1.0915 0.0218  -0.0470 -0.0664 326 SER A N   
2374  C CA  . SER A 326 ? 0.6109 1.0920 1.0732 0.0174  -0.0426 -0.0572 326 SER A CA  
2375  C C   . SER A 326 ? 0.5903 1.0928 1.0542 0.0156  -0.0384 -0.0567 326 SER A C   
2376  O O   . SER A 326 ? 0.5636 1.0683 1.0208 0.0156  -0.0365 -0.0500 326 SER A O   
2377  C CB  . SER A 326 ? 0.6037 1.0701 1.0556 0.0202  -0.0448 -0.0493 326 SER A CB  
2378  O OG  . SER A 326 ? 0.6046 1.0515 1.0550 0.0225  -0.0494 -0.0496 326 SER A OG  
2379  N N   . CYS A 327 ? 0.6602 1.1780 1.1325 0.0142  -0.0372 -0.0639 327 CYS A N   
2380  C CA  . CYS A 327 ? 0.6581 1.1965 1.1320 0.0130  -0.0339 -0.0637 327 CYS A CA  
2381  C C   . CYS A 327 ? 0.6603 1.2088 1.1408 0.0085  -0.0315 -0.0689 327 CYS A C   
2382  O O   . CYS A 327 ? 0.6930 1.2353 1.1786 0.0072  -0.0331 -0.0747 327 CYS A O   
2383  C CB  . CYS A 327 ? 0.6036 1.1566 1.0808 0.0183  -0.0361 -0.0678 327 CYS A CB  
2384  S SG  . CYS A 327 ? 0.5743 1.1313 1.0612 0.0219  -0.0401 -0.0799 327 CYS A SG  
2385  N N   . ILE A 328 ? 0.6479 1.2118 1.1284 0.0062  -0.0281 -0.0667 328 ILE A N   
2386  C CA  . ILE A 328 ? 0.6356 1.2127 1.1226 0.0025  -0.0263 -0.0717 328 ILE A CA  
2387  C C   . ILE A 328 ? 0.6305 1.2292 1.1188 0.0046  -0.0258 -0.0733 328 ILE A C   
2388  O O   . ILE A 328 ? 0.5537 1.1567 1.0371 0.0059  -0.0242 -0.0669 328 ILE A O   
2389  C CB  . ILE A 328 ? 0.5891 1.1621 1.0753 -0.0035 -0.0223 -0.0665 328 ILE A CB  
2390  C CG1 . ILE A 328 ? 0.5783 1.1504 1.0569 -0.0035 -0.0192 -0.0569 328 ILE A CG1 
2391  C CG2 . ILE A 328 ? 0.6158 1.1687 1.1021 -0.0063 -0.0227 -0.0663 328 ILE A CG2 
2392  C CD1 . ILE A 328 ? 0.5926 1.1618 1.0709 -0.0090 -0.0146 -0.0519 328 ILE A CD1 
2393  N N   . ILE A 329 ? 0.8046 1.4162 1.2990 0.0048  -0.0271 -0.0818 329 ILE A N   
2394  C CA  . ILE A 329 ? 0.7791 1.4107 1.2743 0.0072  -0.0268 -0.0843 329 ILE A CA  
2395  C C   . ILE A 329 ? 0.7774 1.4231 1.2760 0.0033  -0.0253 -0.0869 329 ILE A C   
2396  O O   . ILE A 329 ? 0.8106 1.4544 1.3142 0.0005  -0.0264 -0.0929 329 ILE A O   
2397  C CB  . ILE A 329 ? 0.7946 1.4304 1.2931 0.0118  -0.0298 -0.0927 329 ILE A CB  
2398  C CG1 . ILE A 329 ? 0.7979 1.4197 1.2941 0.0159  -0.0319 -0.0901 329 ILE A CG1 
2399  C CG2 . ILE A 329 ? 0.7648 1.4215 1.2634 0.0139  -0.0289 -0.0948 329 ILE A CG2 
2400  C CD1 . ILE A 329 ? 0.8655 1.4889 1.3664 0.0206  -0.0349 -0.0987 329 ILE A CD1 
2401  N N   . LEU A 330 ? 0.6654 1.3249 1.1616 0.0031  -0.0233 -0.0823 330 LEU A N   
2402  C CA  . LEU A 330 ? 0.6608 1.3343 1.1599 -0.0002 -0.0223 -0.0839 330 LEU A CA  
2403  C C   . LEU A 330 ? 0.7187 1.4087 1.2199 0.0019  -0.0242 -0.0921 330 LEU A C   
2404  O O   . LEU A 330 ? 0.7956 1.4853 1.2970 0.0055  -0.0258 -0.0973 330 LEU A O   
2405  C CB  . LEU A 330 ? 0.5924 1.2716 1.0880 -0.0012 -0.0193 -0.0747 330 LEU A CB  
2406  C CG  . LEU A 330 ? 0.5748 1.2384 1.0682 -0.0037 -0.0169 -0.0672 330 LEU A CG  
2407  C CD1 . LEU A 330 ? 0.5577 1.2275 1.0481 -0.0044 -0.0139 -0.0589 330 LEU A CD1 
2408  C CD2 . LEU A 330 ? 0.5679 1.2235 1.0665 -0.0083 -0.0168 -0.0704 330 LEU A CD2 
2409  N N   . ASP A 331 ? 0.7409 1.4456 1.2437 -0.0004 -0.0239 -0.0935 331 ASP A N   
2410  C CA  . ASP A 331 ? 0.7941 1.5141 1.2981 0.0008  -0.0258 -0.1018 331 ASP A CA  
2411  C C   . ASP A 331 ? 0.8443 1.5763 1.3434 0.0049  -0.0250 -0.0999 331 ASP A C   
2412  O O   . ASP A 331 ? 0.7637 1.4960 1.2589 0.0058  -0.0229 -0.0912 331 ASP A O   
2413  C CB  . ASP A 331 ? 0.8628 1.5943 1.3697 -0.0030 -0.0264 -0.1037 331 ASP A CB  
2414  C CG  . ASP A 331 ? 0.8270 1.5485 1.3403 -0.0074 -0.0274 -0.1071 331 ASP A CG  
2415  O OD1 . ASP A 331 ? 0.7567 1.4764 1.2722 -0.0110 -0.0258 -0.1016 331 ASP A OD1 
2416  O OD2 . ASP A 331 ? 0.9020 1.6169 1.4186 -0.0074 -0.0295 -0.1153 331 ASP A OD2 
2417  N N   . ASP A 332 ? 1.2327 1.9741 1.7319 0.0072  -0.0263 -0.1083 332 ASP A N   
2418  C CA  . ASP A 332 ? 1.2205 1.9766 1.7155 0.0103  -0.0252 -0.1079 332 ASP A CA  
2419  C C   . ASP A 332 ? 1.2136 1.9636 1.7065 0.0138  -0.0237 -0.1028 332 ASP A C   
2420  O O   . ASP A 332 ? 1.1961 1.9563 1.6853 0.0156  -0.0220 -0.0985 332 ASP A O   
2421  C CB  . ASP A 332 ? 1.2054 1.9753 1.6969 0.0087  -0.0242 -0.1022 332 ASP A CB  
2422  C CG  . ASP A 332 ? 1.2525 2.0404 1.7409 0.0099  -0.0247 -0.1078 332 ASP A CG  
2423  O OD1 . ASP A 332 ? 1.3479 2.1394 1.8353 0.0130  -0.0244 -0.1132 332 ASP A OD1 
2424  O OD2 . ASP A 332 ? 1.3067 2.1054 1.7938 0.0078  -0.0255 -0.1069 332 ASP A OD2 
2425  N N   . VAL A 333 ? 0.8872 1.6210 1.3826 0.0148  -0.0247 -0.1032 333 VAL A N   
2426  C CA  . VAL A 333 ? 0.7546 1.4819 1.2488 0.0182  -0.0241 -0.0991 333 VAL A CA  
2427  C C   . VAL A 333 ? 0.7569 1.4903 1.2534 0.0222  -0.0248 -0.1073 333 VAL A C   
2428  O O   . VAL A 333 ? 0.7888 1.5227 1.2887 0.0225  -0.0264 -0.1167 333 VAL A O   
2429  C CB  . VAL A 333 ? 0.7542 1.4608 1.2491 0.0177  -0.0252 -0.0954 333 VAL A CB  
2430  C CG1 . VAL A 333 ? 0.7664 1.4666 1.2600 0.0214  -0.0253 -0.0913 333 VAL A CG1 
2431  C CG2 . VAL A 333 ? 0.7218 1.4232 1.2145 0.0137  -0.0237 -0.0877 333 VAL A CG2 
2432  N N   . GLU A 334 ? 0.7710 1.5093 1.2662 0.0252  -0.0235 -0.1041 334 GLU A N   
2433  C CA  . GLU A 334 ? 0.7776 1.5227 1.2758 0.0292  -0.0234 -0.1112 334 GLU A CA  
2434  C C   . GLU A 334 ? 0.8025 1.5351 1.3035 0.0324  -0.0248 -0.1089 334 GLU A C   
2435  O O   . GLU A 334 ? 0.7112 1.4422 1.2100 0.0327  -0.0238 -0.1007 334 GLU A O   
2436  C CB  . GLU A 334 ? 0.7549 1.5191 1.2500 0.0299  -0.0205 -0.1099 334 GLU A CB  
2437  C CG  . GLU A 334 ? 0.7943 1.5673 1.2926 0.0339  -0.0195 -0.1173 334 GLU A CG  
2438  C CD  . GLU A 334 ? 0.8387 1.6303 1.3331 0.0340  -0.0160 -0.1155 334 GLU A CD  
2439  O OE1 . GLU A 334 ? 0.9101 1.7079 1.3990 0.0311  -0.0149 -0.1093 334 GLU A OE1 
2440  O OE2 . GLU A 334 ? 0.8571 1.6572 1.3540 0.0370  -0.0142 -0.1201 334 GLU A OE2 
2441  N N   . ILE A 335 ? 1.0201 1.7436 1.5261 0.0348  -0.0273 -0.1162 335 ILE A N   
2442  C CA  . ILE A 335 ? 1.0300 1.7413 1.5393 0.0384  -0.0295 -0.1151 335 ILE A CA  
2443  C C   . ILE A 335 ? 1.0282 1.7502 1.5427 0.0429  -0.0290 -0.1223 335 ILE A C   
2444  O O   . ILE A 335 ? 1.0347 1.7620 1.5528 0.0443  -0.0292 -0.1322 335 ILE A O   
2445  C CB  . ILE A 335 ? 1.0555 1.7474 1.5670 0.0382  -0.0329 -0.1176 335 ILE A CB  
2446  C CG1 . ILE A 335 ? 1.0609 1.7436 1.5677 0.0332  -0.0325 -0.1110 335 ILE A CG1 
2447  C CG2 . ILE A 335 ? 1.0687 1.7475 1.5828 0.0421  -0.0358 -0.1157 335 ILE A CG2 
2448  C CD1 . ILE A 335 ? 1.0552 1.7316 1.5568 0.0322  -0.0317 -0.0998 335 ILE A CD1 
2449  N N   . LYS A 336 ? 0.8728 1.5984 1.3883 0.0452  -0.0282 -0.1177 336 LYS A N   
2450  C CA  . LYS A 336 ? 0.8447 1.5827 1.3658 0.0491  -0.0268 -0.1237 336 LYS A CA  
2451  C C   . LYS A 336 ? 0.8901 1.6168 1.4187 0.0538  -0.0305 -0.1281 336 LYS A C   
2452  O O   . LYS A 336 ? 0.8750 1.5840 1.4038 0.0540  -0.0342 -0.1275 336 LYS A O   
2453  C CB  . LYS A 336 ? 0.7589 1.5091 1.2780 0.0486  -0.0236 -0.1167 336 LYS A CB  
2454  C CG  . LYS A 336 ? 0.6678 1.4338 1.1809 0.0453  -0.0196 -0.1150 336 LYS A CG  
2455  C CD  . LYS A 336 ? 0.5885 1.3669 1.1009 0.0453  -0.0162 -0.1091 336 LYS A CD  
2456  C CE  . LYS A 336 ? 0.5029 1.2972 1.0089 0.0425  -0.0124 -0.1076 336 LYS A CE  
2457  N NZ  . LYS A 336 ? 0.4265 1.2324 0.9319 0.0422  -0.0089 -0.1016 336 LYS A NZ  
2458  N N   . GLU A 337 ? 0.9794 1.7165 1.5143 0.0577  -0.0294 -0.1325 337 GLU A N   
2459  C CA  . GLU A 337 ? 0.9901 1.7197 1.5338 0.0630  -0.0328 -0.1384 337 GLU A CA  
2460  C C   . GLU A 337 ? 0.9994 1.7111 1.5431 0.0640  -0.0373 -0.1312 337 GLU A C   
2461  O O   . GLU A 337 ? 0.9885 1.7010 1.5296 0.0628  -0.0369 -0.1228 337 GLU A O   
2462  C CB  . GLU A 337 ? 0.9768 1.7233 1.5277 0.0665  -0.0300 -0.1432 337 GLU A CB  
2463  C CG  . GLU A 337 ? 1.0358 1.8019 1.5843 0.0650  -0.0246 -0.1482 337 GLU A CG  
2464  C CD  . GLU A 337 ? 1.2335 2.0010 1.7854 0.0672  -0.0249 -0.1605 337 GLU A CD  
2465  O OE1 . GLU A 337 ? 1.2516 2.0049 1.8088 0.0701  -0.0292 -0.1650 337 GLU A OE1 
2466  O OE2 . GLU A 337 ? 1.2764 2.0586 1.8250 0.0659  -0.0210 -0.1655 337 GLU A OE2 
2467  N N   . ASN A 338 ? 0.8230 1.5182 1.3694 0.0662  -0.0418 -0.1347 338 ASN A N   
2468  C CA  . ASN A 338 ? 0.8330 1.5103 1.3799 0.0683  -0.0469 -0.1295 338 ASN A CA  
2469  C C   . ASN A 338 ? 0.8554 1.5244 1.3927 0.0640  -0.0468 -0.1178 338 ASN A C   
2470  O O   . ASN A 338 ? 0.8717 1.5389 1.4083 0.0649  -0.0480 -0.1114 338 ASN A O   
2471  C CB  . ASN A 338 ? 0.8023 1.4851 1.3582 0.0736  -0.0486 -0.1316 338 ASN A CB  
2472  C CG  . ASN A 338 ? 0.7991 1.4893 1.3652 0.0784  -0.0487 -0.1436 338 ASN A CG  
2473  O OD1 . ASN A 338 ? 0.8119 1.4934 1.3793 0.0793  -0.0505 -0.1499 338 ASN A OD1 
2474  N ND2 . ASN A 338 ? 0.8077 1.5141 1.3816 0.0813  -0.0464 -0.1470 338 ASN A ND2 
2475  N N   . ALA A 339 ? 0.7907 1.4548 1.3210 0.0594  -0.0453 -0.1154 339 ALA A N   
2476  C CA  . ALA A 339 ? 0.7858 1.4414 1.3070 0.0552  -0.0447 -0.1050 339 ALA A CA  
2477  C C   . ALA A 339 ? 0.7997 1.4324 1.3174 0.0549  -0.0487 -0.1022 339 ALA A C   
2478  O O   . ALA A 339 ? 0.8011 1.4251 1.3224 0.0564  -0.0511 -0.1084 339 ALA A O   
2479  C CB  . ALA A 339 ? 0.7840 1.4498 1.3001 0.0501  -0.0402 -0.1035 339 ALA A CB  
2480  N N   . VAL A 340 ? 0.7187 1.3412 1.2289 0.0529  -0.0492 -0.0927 340 VAL A N   
2481  C CA  . VAL A 340 ? 0.6818 1.2822 1.1867 0.0522  -0.0525 -0.0884 340 VAL A CA  
2482  C C   . VAL A 340 ? 0.7005 1.2968 1.1961 0.0467  -0.0492 -0.0803 340 VAL A C   
2483  O O   . VAL A 340 ? 0.6975 1.3018 1.1895 0.0452  -0.0468 -0.0746 340 VAL A O   
2484  C CB  . VAL A 340 ? 0.6557 1.2451 1.1605 0.0565  -0.0574 -0.0849 340 VAL A CB  
2485  C CG1 . VAL A 340 ? 0.6846 1.2504 1.1826 0.0558  -0.0608 -0.0804 340 VAL A CG1 
2486  C CG2 . VAL A 340 ? 0.6383 1.2340 1.1539 0.0623  -0.0605 -0.0931 340 VAL A CG2 
2487  N N   . VAL A 341 ? 0.6425 1.2266 1.1349 0.0436  -0.0490 -0.0800 341 VAL A N   
2488  C CA  . VAL A 341 ? 0.5923 1.1723 1.0772 0.0383  -0.0455 -0.0731 341 VAL A CA  
2489  C C   . VAL A 341 ? 0.6574 1.2145 1.1366 0.0372  -0.0477 -0.0690 341 VAL A C   
2490  O O   . VAL A 341 ? 0.6214 1.1693 1.1035 0.0369  -0.0493 -0.0736 341 VAL A O   
2491  C CB  . VAL A 341 ? 0.5337 1.1257 1.0212 0.0343  -0.0418 -0.0771 341 VAL A CB  
2492  C CG1 . VAL A 341 ? 0.5747 1.1618 1.0557 0.0290  -0.0384 -0.0701 341 VAL A CG1 
2493  C CG2 . VAL A 341 ? 0.5459 1.1603 1.0373 0.0353  -0.0395 -0.0803 341 VAL A CG2 
2494  N N   . ILE A 342 ? 0.6834 1.2306 1.1541 0.0364  -0.0477 -0.0604 342 ILE A N   
2495  C CA  . ILE A 342 ? 0.7158 1.2408 1.1789 0.0353  -0.0494 -0.0552 342 ILE A CA  
2496  C C   . ILE A 342 ? 0.7224 1.2446 1.1769 0.0305  -0.0448 -0.0472 342 ILE A C   
2497  O O   . ILE A 342 ? 0.7222 1.2525 1.1735 0.0305  -0.0431 -0.0429 342 ILE A O   
2498  C CB  . ILE A 342 ? 0.7338 1.2468 1.1939 0.0403  -0.0550 -0.0527 342 ILE A CB  
2499  C CG1 . ILE A 342 ? 0.7760 1.2979 1.2464 0.0458  -0.0589 -0.0605 342 ILE A CG1 
2500  C CG2 . ILE A 342 ? 0.7773 1.2665 1.2306 0.0397  -0.0576 -0.0492 342 ILE A CG2 
2501  C CD1 . ILE A 342 ? 0.7757 1.2930 1.2532 0.0470  -0.0609 -0.0683 342 ILE A CD1 
2502  N N   . ASN A 343 ? 0.6604 1.1713 1.1117 0.0263  -0.0427 -0.0454 343 ASN A N   
2503  C CA  . ASN A 343 ? 0.6004 1.1065 1.0435 0.0217  -0.0381 -0.0379 343 ASN A CA  
2504  C C   . ASN A 343 ? 0.5811 1.1066 1.0262 0.0199  -0.0338 -0.0368 343 ASN A C   
2505  O O   . ASN A 343 ? 0.5345 1.0607 0.9733 0.0197  -0.0320 -0.0307 343 ASN A O   
2506  C CB  . ASN A 343 ? 0.6216 1.1112 1.0535 0.0232  -0.0399 -0.0303 343 ASN A CB  
2507  C CG  . ASN A 343 ? 0.6211 1.0894 1.0493 0.0244  -0.0438 -0.0298 343 ASN A CG  
2508  O OD1 . ASN A 343 ? 0.5572 1.0181 0.9874 0.0213  -0.0425 -0.0316 343 ASN A OD1 
2509  N ND2 . ASN A 343 ? 0.6380 1.0963 1.0610 0.0288  -0.0489 -0.0273 343 ASN A ND2 
2510  N N   . SER A 344 ? 0.5101 1.0509 0.9637 0.0187  -0.0324 -0.0431 344 SER A N   
2511  C CA  . SER A 344 ? 0.5154 1.0757 0.9716 0.0177  -0.0292 -0.0428 344 SER A CA  
2512  C C   . SER A 344 ? 0.5193 1.0880 0.9802 0.0133  -0.0259 -0.0457 344 SER A C   
2513  O O   . SER A 344 ? 0.5401 1.1018 1.0043 0.0113  -0.0265 -0.0497 344 SER A O   
2514  C CB  . SER A 344 ? 0.4901 1.0651 0.9520 0.0219  -0.0316 -0.0479 344 SER A CB  
2515  O OG  . SER A 344 ? 0.5446 1.1114 1.0045 0.0263  -0.0356 -0.0469 344 SER A OG  
2516  N N   . ILE A 345 ? 0.4864 1.0701 0.9481 0.0116  -0.0227 -0.0437 345 ILE A N   
2517  C CA  . ILE A 345 ? 0.4671 1.0623 0.9340 0.0079  -0.0201 -0.0466 345 ILE A CA  
2518  C C   . ILE A 345 ? 0.4486 1.0644 0.9186 0.0096  -0.0198 -0.0487 345 ILE A C   
2519  O O   . ILE A 345 ? 0.4206 1.0426 0.8872 0.0098  -0.0178 -0.0430 345 ILE A O   
2520  C CB  . ILE A 345 ? 0.5155 1.1063 0.9793 0.0035  -0.0159 -0.0404 345 ILE A CB  
2521  C CG1 . ILE A 345 ? 0.5428 1.1123 1.0021 0.0016  -0.0156 -0.0375 345 ILE A CG1 
2522  C CG2 . ILE A 345 ? 0.5034 1.1074 0.9740 -0.0002 -0.0139 -0.0440 345 ILE A CG2 
2523  C CD1 . ILE A 345 ? 0.5628 1.1278 1.0195 -0.0030 -0.0107 -0.0318 345 ILE A CD1 
2524  N N   . ILE A 346 ? 0.4658 1.0919 0.9418 0.0107  -0.0216 -0.0566 346 ILE A N   
2525  C CA  . ILE A 346 ? 0.4876 1.1328 0.9656 0.0125  -0.0214 -0.0589 346 ILE A CA  
2526  C C   . ILE A 346 ? 0.4824 1.1406 0.9628 0.0090  -0.0191 -0.0593 346 ILE A C   
2527  O O   . ILE A 346 ? 0.5376 1.1952 1.0220 0.0063  -0.0194 -0.0641 346 ILE A O   
2528  C CB  . ILE A 346 ? 0.5327 1.1831 1.0154 0.0158  -0.0242 -0.0676 346 ILE A CB  
2529  C CG1 . ILE A 346 ? 0.4846 1.1207 0.9663 0.0194  -0.0270 -0.0676 346 ILE A CG1 
2530  C CG2 . ILE A 346 ? 0.5355 1.2049 1.0190 0.0178  -0.0233 -0.0689 346 ILE A CG2 
2531  C CD1 . ILE A 346 ? 0.5094 1.1438 0.9865 0.0217  -0.0269 -0.0606 346 ILE A CD1 
2532  N N   . GLY A 347 ? 0.5094 1.1790 0.9875 0.0092  -0.0171 -0.0545 347 GLY A N   
2533  C CA  . GLY A 347 ? 0.4909 1.1727 0.9710 0.0063  -0.0153 -0.0536 347 GLY A CA  
2534  C C   . GLY A 347 ? 0.6794 1.3770 1.1634 0.0064  -0.0167 -0.0611 347 GLY A C   
2535  O O   . GLY A 347 ? 0.4616 1.1595 0.9478 0.0082  -0.0189 -0.0684 347 GLY A O   
2536  N N   . TRP A 348 ? 0.4306 1.1414 0.9154 0.0046  -0.0157 -0.0596 348 TRP A N   
2537  C CA  . TRP A 348 ? 0.4632 1.1895 0.9506 0.0045  -0.0172 -0.0665 348 TRP A CA  
2538  C C   . TRP A 348 ? 0.4715 1.2099 0.9557 0.0079  -0.0172 -0.0666 348 TRP A C   
2539  O O   . TRP A 348 ? 0.4518 1.1918 0.9324 0.0092  -0.0155 -0.0595 348 TRP A O   
2540  C CB  . TRP A 348 ? 0.5540 1.2895 1.0434 0.0013  -0.0166 -0.0645 348 TRP A CB  
2541  C CG  . TRP A 348 ? 0.5442 1.2682 1.0365 -0.0021 -0.0152 -0.0613 348 TRP A CG  
2542  C CD1 . TRP A 348 ? 0.4709 1.1865 0.9608 -0.0027 -0.0124 -0.0530 348 TRP A CD1 
2543  C CD2 . TRP A 348 ? 0.5134 1.2329 1.0115 -0.0057 -0.0161 -0.0666 348 TRP A CD2 
2544  N NE1 . TRP A 348 ? 0.4209 1.1275 0.9145 -0.0064 -0.0112 -0.0526 348 TRP A NE1 
2545  C CE2 . TRP A 348 ? 0.4616 1.1703 0.9606 -0.0085 -0.0134 -0.0607 348 TRP A CE2 
2546  C CE3 . TRP A 348 ? 0.5300 1.2535 1.0327 -0.0070 -0.0188 -0.0760 348 TRP A CE3 
2547  C CZ2 . TRP A 348 ? 0.4787 1.1808 0.9834 -0.0127 -0.0131 -0.0634 348 TRP A CZ2 
2548  C CZ3 . TRP A 348 ? 0.5200 1.2364 1.0286 -0.0112 -0.0189 -0.0789 348 TRP A CZ3 
2549  C CH2 . TRP A 348 ? 0.4914 1.1974 1.0012 -0.0142 -0.0160 -0.0724 348 TRP A CH2 
2550  N N   . LYS A 349 ? 0.6285 1.3755 1.1141 0.0091  -0.0188 -0.0750 349 LYS A N   
2551  C CA  . LYS A 349 ? 0.6481 1.4083 1.1309 0.0120  -0.0183 -0.0763 349 LYS A CA  
2552  C C   . LYS A 349 ? 0.5471 1.3015 1.0281 0.0150  -0.0172 -0.0719 349 LYS A C   
2553  O O   . LYS A 349 ? 0.4804 1.2451 0.9588 0.0168  -0.0159 -0.0699 349 LYS A O   
2554  C CB  . LYS A 349 ? 0.6246 1.4002 1.1043 0.0111  -0.0174 -0.0721 349 LYS A CB  
2555  C CG  . LYS A 349 ? 0.7700 1.5568 1.2510 0.0092  -0.0192 -0.0784 349 LYS A CG  
2556  C CD  . LYS A 349 ? 0.7593 1.5399 1.2445 0.0056  -0.0202 -0.0780 349 LYS A CD  
2557  C CE  . LYS A 349 ? 0.9018 1.6947 1.3887 0.0037  -0.0226 -0.0843 349 LYS A CE  
2558  N NZ  . LYS A 349 ? 0.9445 1.7324 1.4369 -0.0001 -0.0235 -0.0838 349 LYS A NZ  
2559  N N   . SER A 350 ? 0.6023 1.3402 1.0844 0.0154  -0.0178 -0.0704 350 SER A N   
2560  C CA  . SER A 350 ? 0.4434 1.1754 0.9241 0.0181  -0.0174 -0.0665 350 SER A CA  
2561  C C   . SER A 350 ? 0.5002 1.2371 0.9836 0.0214  -0.0184 -0.0739 350 SER A C   
2562  O O   . SER A 350 ? 0.5858 1.3241 1.0724 0.0218  -0.0198 -0.0824 350 SER A O   
2563  C CB  . SER A 350 ? 0.4336 1.1462 0.9138 0.0177  -0.0183 -0.0629 350 SER A CB  
2564  O OG  . SER A 350 ? 0.4296 1.1379 0.9077 0.0146  -0.0168 -0.0569 350 SER A OG  
2565  N N   . SER A 351 ? 0.4628 1.2023 0.9456 0.0239  -0.0176 -0.0707 351 SER A N   
2566  C CA  . SER A 351 ? 0.5128 1.2588 0.9989 0.0272  -0.0178 -0.0771 351 SER A CA  
2567  C C   . SER A 351 ? 0.4635 1.1977 0.9517 0.0299  -0.0194 -0.0751 351 SER A C   
2568  O O   . SER A 351 ? 0.4060 1.1378 0.8919 0.0299  -0.0187 -0.0675 351 SER A O   
2569  C CB  . SER A 351 ? 0.5047 1.2688 0.9889 0.0276  -0.0151 -0.0759 351 SER A CB  
2570  O OG  . SER A 351 ? 0.4938 1.2654 0.9818 0.0306  -0.0147 -0.0827 351 SER A OG  
2571  N N   . ILE A 352 ? 0.5517 1.2784 1.0444 0.0322  -0.0218 -0.0820 352 ILE A N   
2572  C CA  . ILE A 352 ? 0.5755 1.2901 1.0707 0.0352  -0.0243 -0.0810 352 ILE A CA  
2573  C C   . ILE A 352 ? 0.6238 1.3491 1.1247 0.0389  -0.0240 -0.0869 352 ILE A C   
2574  O O   . ILE A 352 ? 0.6671 1.3975 1.1720 0.0406  -0.0243 -0.0959 352 ILE A O   
2575  C CB  . ILE A 352 ? 0.6426 1.3396 1.1390 0.0354  -0.0275 -0.0841 352 ILE A CB  
2576  C CG1 . ILE A 352 ? 0.6231 1.3098 1.1141 0.0314  -0.0270 -0.0779 352 ILE A CG1 
2577  C CG2 . ILE A 352 ? 0.6568 1.3419 1.1556 0.0391  -0.0307 -0.0834 352 ILE A CG2 
2578  C CD1 . ILE A 352 ? 0.5815 1.2639 1.0674 0.0304  -0.0260 -0.0679 352 ILE A CD1 
2579  N N   . GLY A 353 ? 0.6170 1.3460 1.1186 0.0402  -0.0233 -0.0822 353 GLY A N   
2580  C CA  . GLY A 353 ? 0.6341 1.3746 1.1419 0.0434  -0.0224 -0.0871 353 GLY A CA  
2581  C C   . GLY A 353 ? 0.6762 1.4082 1.1910 0.0476  -0.0259 -0.0940 353 GLY A C   
2582  O O   . GLY A 353 ? 0.6704 1.3858 1.1847 0.0481  -0.0295 -0.0939 353 GLY A O   
2583  N N   . ARG A 354 ? 0.6959 1.4396 1.2175 0.0507  -0.0248 -0.1000 354 ARG A N   
2584  C CA  . ARG A 354 ? 0.6767 1.4145 1.2065 0.0553  -0.0280 -0.1074 354 ARG A CA  
2585  C C   . ARG A 354 ? 0.6761 1.4026 1.2086 0.0575  -0.0318 -0.1024 354 ARG A C   
2586  O O   . ARG A 354 ? 0.6921 1.4231 1.2238 0.0565  -0.0307 -0.0959 354 ARG A O   
2587  C CB  . ARG A 354 ? 0.6633 1.4185 1.2000 0.0580  -0.0251 -0.1159 354 ARG A CB  
2588  C CG  . ARG A 354 ? 0.6315 1.4020 1.1694 0.0574  -0.0211 -0.1118 354 ARG A CG  
2589  C CD  . ARG A 354 ? 0.6468 1.4353 1.1904 0.0595  -0.0172 -0.1203 354 ARG A CD  
2590  N NE  . ARG A 354 ? 0.6573 1.4526 1.1955 0.0578  -0.0148 -0.1256 354 ARG A NE  
2591  C CZ  . ARG A 354 ? 0.6356 1.4429 1.1664 0.0543  -0.0107 -0.1222 354 ARG A CZ  
2592  N NH1 . ARG A 354 ? 0.5996 1.4129 1.1277 0.0520  -0.0083 -0.1134 354 ARG A NH1 
2593  N NH2 . ARG A 354 ? 0.6360 1.4491 1.1622 0.0531  -0.0094 -0.1278 354 ARG A NH2 
2594  N N   . TRP A 355 ? 0.7254 1.4369 1.2611 0.0605  -0.0367 -0.1056 355 TRP A N   
2595  C CA  . TRP A 355 ? 0.7473 1.4454 1.2846 0.0629  -0.0415 -0.1013 355 TRP A CA  
2596  C C   . TRP A 355 ? 0.7914 1.4796 1.3193 0.0593  -0.0419 -0.0906 355 TRP A C   
2597  O O   . TRP A 355 ? 0.7863 1.4680 1.3145 0.0605  -0.0448 -0.0857 355 TRP A O   
2598  C CB  . TRP A 355 ? 0.7481 1.4570 1.2951 0.0665  -0.0417 -0.1035 355 TRP A CB  
2599  C CG  . TRP A 355 ? 0.6930 1.4062 1.2505 0.0715  -0.0430 -0.1140 355 TRP A CG  
2600  C CD1 . TRP A 355 ? 0.6728 1.3719 1.2346 0.0756  -0.0484 -0.1184 355 TRP A CD1 
2601  C CD2 . TRP A 355 ? 0.6761 1.4088 1.2411 0.0731  -0.0386 -0.1216 355 TRP A CD2 
2602  N NE1 . TRP A 355 ? 0.6813 1.3899 1.2536 0.0799  -0.0478 -0.1285 355 TRP A NE1 
2603  C CE2 . TRP A 355 ? 0.6463 1.3759 1.2206 0.0784  -0.0416 -0.1308 355 TRP A CE2 
2604  C CE3 . TRP A 355 ? 0.6622 1.4144 1.2265 0.0706  -0.0323 -0.1214 355 TRP A CE3 
2605  C CZ2 . TRP A 355 ? 0.5712 1.3169 1.1543 0.0813  -0.0382 -0.1403 355 TRP A CZ2 
2606  C CZ3 . TRP A 355 ? 0.5761 1.3442 1.1484 0.0733  -0.0289 -0.1303 355 TRP A CZ3 
2607  C CH2 . TRP A 355 ? 0.5586 1.3236 1.1403 0.0786  -0.0317 -0.1399 355 TRP A CH2 
2608  N N   . SER A 356 ? 0.7502 1.4372 1.2701 0.0549  -0.0392 -0.0872 356 SER A N   
2609  C CA  . SER A 356 ? 0.7444 1.4217 1.2554 0.0515  -0.0391 -0.0776 356 SER A CA  
2610  C C   . SER A 356 ? 0.7439 1.4011 1.2498 0.0509  -0.0423 -0.0763 356 SER A C   
2611  O O   . SER A 356 ? 0.7232 1.3763 1.2313 0.0514  -0.0432 -0.0824 356 SER A O   
2612  C CB  . SER A 356 ? 0.7099 1.3987 1.2156 0.0471  -0.0340 -0.0742 356 SER A CB  
2613  O OG  . SER A 356 ? 0.7219 1.4158 1.2280 0.0459  -0.0323 -0.0802 356 SER A OG  
2614  N N   . ARG A 357 ? 0.6627 1.3070 1.1617 0.0496  -0.0438 -0.0684 357 ARG A N   
2615  C CA  . ARG A 357 ? 0.5975 1.2213 1.0909 0.0492  -0.0469 -0.0660 357 ARG A CA  
2616  C C   . ARG A 357 ? 0.5631 1.1807 1.0468 0.0447  -0.0441 -0.0580 357 ARG A C   
2617  O O   . ARG A 357 ? 0.6027 1.2247 1.0829 0.0434  -0.0425 -0.0522 357 ARG A O   
2618  C CB  . ARG A 357 ? 0.6011 1.2120 1.0952 0.0532  -0.0526 -0.0646 357 ARG A CB  
2619  C CG  . ARG A 357 ? 0.5654 1.1545 1.0540 0.0535  -0.0562 -0.0632 357 ARG A CG  
2620  C CD  . ARG A 357 ? 0.5782 1.1549 1.0660 0.0575  -0.0623 -0.0608 357 ARG A CD  
2621  N NE  . ARG A 357 ? 0.5388 1.0941 1.0211 0.0582  -0.0661 -0.0594 357 ARG A NE  
2622  C CZ  . ARG A 357 ? 0.5537 1.1018 1.0418 0.0620  -0.0704 -0.0650 357 ARG A CZ  
2623  N NH1 . ARG A 357 ? 0.5350 1.0960 1.0349 0.0656  -0.0711 -0.0729 357 ARG A NH1 
2624  N NH2 . ARG A 357 ? 0.5827 1.1102 1.0645 0.0622  -0.0736 -0.0626 357 ARG A NH2 
2625  N N   . VAL A 358 ? 0.6229 1.2302 1.1027 0.0422  -0.0435 -0.0580 358 VAL A N   
2626  C CA  . VAL A 358 ? 0.4461 1.0466 0.9175 0.0378  -0.0406 -0.0511 358 VAL A CA  
2627  C C   . VAL A 358 ? 0.5396 1.1187 1.0058 0.0375  -0.0432 -0.0492 358 VAL A C   
2628  O O   . VAL A 358 ? 0.5088 1.0831 0.9772 0.0364  -0.0433 -0.0535 358 VAL A O   
2629  C CB  . VAL A 358 ? 0.4518 1.0644 0.9244 0.0340  -0.0361 -0.0529 358 VAL A CB  
2630  C CG1 . VAL A 358 ? 0.5192 1.1256 0.9843 0.0299  -0.0330 -0.0457 358 VAL A CG1 
2631  C CG2 . VAL A 358 ? 0.5028 1.1363 0.9800 0.0347  -0.0338 -0.0550 358 VAL A CG2 
2632  N N   . GLN A 359 ? 0.4532 1.0191 0.9122 0.0383  -0.0453 -0.0430 359 GLN A N   
2633  C CA  . GLN A 359 ? 0.5410 1.0856 0.9936 0.0381  -0.0479 -0.0404 359 GLN A CA  
2634  C C   . GLN A 359 ? 0.4769 1.0116 0.9183 0.0351  -0.0455 -0.0318 359 GLN A C   
2635  O O   . GLN A 359 ? 0.4554 0.9989 0.8946 0.0337  -0.0426 -0.0281 359 GLN A O   
2636  C CB  . GLN A 359 ? 0.5517 1.0864 1.0057 0.0433  -0.0544 -0.0420 359 GLN A CB  
2637  C CG  . GLN A 359 ? 0.5033 1.0381 0.9540 0.0455  -0.0568 -0.0375 359 GLN A CG  
2638  C CD  . GLN A 359 ? 0.5656 1.0844 1.0138 0.0497  -0.0637 -0.0368 359 GLN A CD  
2639  O OE1 . GLN A 359 ? 0.5602 1.0734 1.0135 0.0526  -0.0672 -0.0416 359 GLN A OE1 
2640  N NE2 . GLN A 359 ? 0.6139 1.1252 1.0542 0.0504  -0.0659 -0.0308 359 GLN A NE2 
2641  N N   . ALA A 360 ? 0.5330 1.0485 0.9672 0.0341  -0.0466 -0.0289 360 ALA A N   
2642  C CA  . ALA A 360 ? 0.5753 1.0787 0.9978 0.0314  -0.0444 -0.0210 360 ALA A CA  
2643  C C   . ALA A 360 ? 0.5860 1.0669 1.0010 0.0324  -0.0480 -0.0187 360 ALA A C   
2644  O O   . ALA A 360 ? 0.5830 1.0584 1.0028 0.0346  -0.0518 -0.0232 360 ALA A O   
2645  C CB  . ALA A 360 ? 0.5594 1.0679 0.9808 0.0261  -0.0377 -0.0190 360 ALA A CB  
2646  N N   . SER A 361 ? 0.6685 1.1363 1.0713 0.0308  -0.0468 -0.0115 361 SER A N   
2647  C CA  . SER A 361 ? 0.7243 1.1697 1.1177 0.0316  -0.0503 -0.0081 361 SER A CA  
2648  C C   . SER A 361 ? 0.7242 1.1603 1.1178 0.0280  -0.0475 -0.0088 361 SER A C   
2649  O O   . SER A 361 ? 0.6802 1.1019 1.0725 0.0296  -0.0516 -0.0097 361 SER A O   
2650  C CB  . SER A 361 ? 0.7872 1.2215 1.1663 0.0308  -0.0494 -0.0004 361 SER A CB  
2651  O OG  . SER A 361 ? 0.7940 1.2421 1.1734 0.0290  -0.0448 0.0013  361 SER A OG  
2652  N N   . GLY A 362 ? 0.7375 1.1815 1.1331 0.0230  -0.0409 -0.0084 362 GLY A N   
2653  C CA  . GLY A 362 ? 0.7256 1.1611 1.1214 0.0187  -0.0376 -0.0086 362 GLY A CA  
2654  C C   . GLY A 362 ? 0.7712 1.1922 1.1546 0.0147  -0.0331 -0.0010 362 GLY A C   
2655  O O   . GLY A 362 ? 0.8151 1.2268 1.1980 0.0107  -0.0302 -0.0003 362 GLY A O   
2656  N N   . ASP A 363 ? 0.8114 1.2301 1.1850 0.0154  -0.0321 0.0046  363 ASP A N   
2657  C CA  . ASP A 363 ? 0.9025 1.3078 1.2631 0.0119  -0.0273 0.0117  363 ASP A CA  
2658  C C   . ASP A 363 ? 0.9467 1.3639 1.3122 0.0067  -0.0193 0.0120  363 ASP A C   
2659  O O   . ASP A 363 ? 0.9215 1.3539 1.2902 0.0069  -0.0169 0.0118  363 ASP A O   
2660  C CB  . ASP A 363 ? 0.8900 1.2903 1.2390 0.0148  -0.0293 0.0165  363 ASP A CB  
2661  C CG  . ASP A 363 ? 0.9160 1.2984 1.2491 0.0121  -0.0257 0.0238  363 ASP A CG  
2662  O OD1 . ASP A 363 ? 0.9342 1.3037 1.2639 0.0090  -0.0235 0.0256  363 ASP A OD1 
2663  O OD2 . ASP A 363 ? 0.9226 1.3033 1.2461 0.0131  -0.0249 0.0277  363 ASP A OD2 
2664  N N   . TYR A 364 ? 1.0083 1.4186 1.3749 0.0020  -0.0153 0.0125  364 TYR A N   
2665  C CA  . TYR A 364 ? 1.0044 1.4256 1.3765 -0.0031 -0.0078 0.0127  364 TYR A CA  
2666  C C   . TYR A 364 ? 1.0237 1.4407 1.3851 -0.0051 -0.0019 0.0194  364 TYR A C   
2667  O O   . TYR A 364 ? 1.0144 1.4408 1.3804 -0.0090 0.0045  0.0199  364 TYR A O   
2668  C CB  . TYR A 364 ? 1.0234 1.4383 1.4009 -0.0078 -0.0053 0.0109  364 TYR A CB  
2669  C CG  . TYR A 364 ? 1.0278 1.4464 1.4163 -0.0061 -0.0106 0.0036  364 TYR A CG  
2670  C CD1 . TYR A 364 ? 0.9912 1.4303 1.3931 -0.0060 -0.0108 -0.0030 364 TYR A CD1 
2671  C CD2 . TYR A 364 ? 1.0648 1.4662 1.4499 -0.0043 -0.0155 0.0033  364 TYR A CD2 
2672  C CE1 . TYR A 364 ? 0.9870 1.4295 1.3984 -0.0043 -0.0154 -0.0103 364 TYR A CE1 
2673  C CE2 . TYR A 364 ? 1.0708 1.4754 1.4663 -0.0024 -0.0203 -0.0039 364 TYR A CE2 
2674  C CZ  . TYR A 364 ? 1.0347 1.4601 1.4433 -0.0025 -0.0200 -0.0109 364 TYR A CZ  
2675  O OH  . TYR A 364 ? 1.0062 1.4348 1.4246 -0.0005 -0.0245 -0.0186 364 TYR A OH  
2676  N N   . ASN A 365 ? 1.0932 1.4968 1.4407 -0.0024 -0.0042 0.0241  365 ASN A N   
2677  C CA  . ASN A 365 ? 1.1034 1.5035 1.4399 -0.0035 0.0008  0.0298  365 ASN A CA  
2678  C C   . ASN A 365 ? 1.0748 1.4872 1.4117 0.0002  -0.0011 0.0294  365 ASN A C   
2679  O O   . ASN A 365 ? 1.1223 1.5393 1.4559 -0.0010 0.0041  0.0322  365 ASN A O   
2680  C CB  . ASN A 365 ? 1.1639 1.5405 1.4830 -0.0032 -0.0002 0.0356  365 ASN A CB  
2681  C CG  . ASN A 365 ? 1.1977 1.5597 1.5159 -0.0059 -0.0004 0.0361  365 ASN A CG  
2682  O OD1 . ASN A 365 ? 1.1899 1.5567 1.5173 -0.0104 0.0043  0.0343  365 ASN A OD1 
2683  N ND2 . ASN A 365 ? 1.2396 1.5836 1.5473 -0.0031 -0.0061 0.0385  365 ASN A ND2 
2684  N N   . ASP A 366 ? 0.9866 1.4045 1.3283 0.0048  -0.0082 0.0257  366 ASP A N   
2685  C CA  . ASP A 366 ? 0.9217 1.3520 1.2654 0.0080  -0.0102 0.0250  366 ASP A CA  
2686  C C   . ASP A 366 ? 0.9175 1.3696 1.2754 0.0068  -0.0073 0.0211  366 ASP A C   
2687  O O   . ASP A 366 ? 0.9196 1.3790 1.2880 0.0053  -0.0074 0.0167  366 ASP A O   
2688  C CB  . ASP A 366 ? 0.9137 1.3415 1.2575 0.0131  -0.0188 0.0227  366 ASP A CB  
2689  C CG  . ASP A 366 ? 0.9066 1.3460 1.2523 0.0161  -0.0209 0.0222  366 ASP A CG  
2690  O OD1 . ASP A 366 ? 0.9044 1.3493 1.2476 0.0147  -0.0162 0.0249  366 ASP A OD1 
2691  O OD2 . ASP A 366 ? 0.9252 1.3684 1.2756 0.0200  -0.0273 0.0191  366 ASP A OD2 
2692  N N   . ARG A 367 ? 0.9860 1.4483 1.3439 0.0073  -0.0050 0.0227  367 ARG A N   
2693  C CA  . ARG A 367 ? 0.9747 1.4576 1.3450 0.0064  -0.0024 0.0198  367 ARG A CA  
2694  C C   . ARG A 367 ? 0.9217 1.4164 1.3022 0.0092  -0.0078 0.0142  367 ARG A C   
2695  O O   . ARG A 367 ? 0.8794 1.3868 1.2705 0.0078  -0.0069 0.0101  367 ARG A O   
2696  C CB  . ARG A 367 ? 0.9274 1.4171 1.2950 0.0070  0.0005  0.0230  367 ARG A CB  
2697  C CG  . ARG A 367 ? 0.9083 1.4166 1.2866 0.0053  0.0045  0.0216  367 ARG A CG  
2698  C CD  . ARG A 367 ? 0.9235 1.4370 1.2990 0.0063  0.0071  0.0250  367 ARG A CD  
2699  N NE  . ARG A 367 ? 0.9212 1.4516 1.3066 0.0048  0.0108  0.0242  367 ARG A NE  
2700  C CZ  . ARG A 367 ? 0.8204 1.3584 1.2063 0.0057  0.0130  0.0266  367 ARG A CZ  
2701  N NH1 . ARG A 367 ? 0.7730 1.3032 1.1502 0.0079  0.0119  0.0296  367 ARG A NH1 
2702  N NH2 . ARG A 367 ? 0.7306 1.2837 1.1258 0.0045  0.0158  0.0260  367 ARG A NH2 
2703  N N   . LEU A 368 ? 0.8752 1.3661 1.2527 0.0132  -0.0135 0.0138  368 LEU A N   
2704  C CA  . LEU A 368 ? 0.8295 1.3311 1.2163 0.0161  -0.0185 0.0086  368 LEU A CA  
2705  C C   . LEU A 368 ? 0.8373 1.3291 1.2255 0.0174  -0.0229 0.0051  368 LEU A C   
2706  O O   . LEU A 368 ? 0.8175 1.3138 1.2113 0.0208  -0.0280 0.0011  368 LEU A O   
2707  C CB  . LEU A 368 ? 0.8144 1.3192 1.1994 0.0197  -0.0222 0.0096  368 LEU A CB  
2708  C CG  . LEU A 368 ? 0.7561 1.2709 1.1408 0.0189  -0.0184 0.0127  368 LEU A CG  
2709  C CD1 . LEU A 368 ? 0.7303 1.2486 1.1149 0.0221  -0.0226 0.0131  368 LEU A CD1 
2710  C CD2 . LEU A 368 ? 0.6514 1.1842 1.0464 0.0168  -0.0146 0.0103  368 LEU A CD2 
2711  N N   . GLY A 369 ? 0.8353 1.3136 1.2187 0.0146  -0.0209 0.0066  369 GLY A N   
2712  C CA  . GLY A 369 ? 0.8091 1.2770 1.1941 0.0157  -0.0250 0.0036  369 GLY A CA  
2713  C C   . GLY A 369 ? 0.7274 1.2079 1.1255 0.0152  -0.0255 -0.0034 369 GLY A C   
2714  O O   . GLY A 369 ? 0.7260 1.2013 1.1277 0.0174  -0.0300 -0.0074 369 GLY A O   
2715  N N   . ILE A 370 ? 0.7067 1.2034 1.1119 0.0126  -0.0211 -0.0051 370 ILE A N   
2716  C CA  . ILE A 370 ? 0.6111 1.1216 1.0282 0.0121  -0.0214 -0.0120 370 ILE A CA  
2717  C C   . ILE A 370 ? 0.5798 1.1107 1.0026 0.0132  -0.0204 -0.0133 370 ILE A C   
2718  O O   . ILE A 370 ? 0.6101 1.1488 1.0325 0.0108  -0.0160 -0.0103 370 ILE A O   
2719  C CB  . ILE A 370 ? 0.6161 1.1258 1.0365 0.0070  -0.0170 -0.0128 370 ILE A CB  
2720  C CG1 . ILE A 370 ? 0.6750 1.1634 1.0892 0.0053  -0.0174 -0.0106 370 ILE A CG1 
2721  C CG2 . ILE A 370 ? 0.6093 1.1337 1.0416 0.0065  -0.0179 -0.0205 370 ILE A CG2 
2722  C CD1 . ILE A 370 ? 0.6820 1.1618 1.0984 0.0086  -0.0234 -0.0150 370 ILE A CD1 
2723  N N   . THR A 371 ? 0.4560 0.9953 0.8841 0.0170  -0.0244 -0.0177 371 THR A N   
2724  C CA  . THR A 371 ? 0.4426 1.0010 0.8758 0.0180  -0.0234 -0.0189 371 THR A CA  
2725  C C   . THR A 371 ? 0.5432 1.1161 0.9840 0.0153  -0.0206 -0.0230 371 THR A C   
2726  O O   . THR A 371 ? 0.4972 1.0699 0.9433 0.0147  -0.0218 -0.0287 371 THR A O   
2727  C CB  . THR A 371 ? 0.5432 1.1071 0.9806 0.0226  -0.0280 -0.0226 371 THR A CB  
2728  O OG1 . THR A 371 ? 0.4351 1.0186 0.8782 0.0229  -0.0265 -0.0244 371 THR A OG1 
2729  C CG2 . THR A 371 ? 0.5380 1.0977 0.9807 0.0243  -0.0315 -0.0293 371 THR A CG2 
2730  N N   . ILE A 372 ? 0.4544 1.0394 0.8959 0.0137  -0.0171 -0.0202 372 ILE A N   
2731  C CA  . ILE A 372 ? 0.4655 1.0640 0.9132 0.0109  -0.0144 -0.0231 372 ILE A CA  
2732  C C   . ILE A 372 ? 0.4671 1.0844 0.9186 0.0125  -0.0144 -0.0242 372 ILE A C   
2733  O O   . ILE A 372 ? 0.5623 1.1824 1.0105 0.0137  -0.0135 -0.0193 372 ILE A O   
2734  C CB  . ILE A 372 ? 0.5055 1.1008 0.9507 0.0070  -0.0099 -0.0183 372 ILE A CB  
2735  C CG1 . ILE A 372 ? 0.5336 1.1096 0.9742 0.0050  -0.0094 -0.0167 372 ILE A CG1 
2736  C CG2 . ILE A 372 ? 0.5955 1.2055 1.0481 0.0043  -0.0079 -0.0216 372 ILE A CG2 
2737  C CD1 . ILE A 372 ? 0.5734 1.1439 1.0100 0.0016  -0.0045 -0.0110 372 ILE A CD1 
2738  N N   . LEU A 373 ? 0.5683 1.1980 1.0264 0.0126  -0.0153 -0.0307 373 LEU A N   
2739  C CA  . LEU A 373 ? 0.5255 1.1735 0.9869 0.0139  -0.0151 -0.0321 373 LEU A CA  
2740  C C   . LEU A 373 ? 0.5294 1.1897 0.9936 0.0110  -0.0126 -0.0324 373 LEU A C   
2741  O O   . LEU A 373 ? 0.4620 1.1214 0.9296 0.0085  -0.0125 -0.0363 373 LEU A O   
2742  C CB  . LEU A 373 ? 0.4452 1.0992 0.9111 0.0167  -0.0179 -0.0396 373 LEU A CB  
2743  C CG  . LEU A 373 ? 0.5040 1.1580 0.9694 0.0205  -0.0199 -0.0390 373 LEU A CG  
2744  C CD1 . LEU A 373 ? 0.5224 1.1578 0.9830 0.0216  -0.0218 -0.0351 373 LEU A CD1 
2745  C CD2 . LEU A 373 ? 0.5133 1.1750 0.9845 0.0230  -0.0221 -0.0472 373 LEU A CD2 
2746  N N   . GLY A 374 ? 0.5384 1.2100 1.0017 0.0113  -0.0109 -0.0283 374 GLY A N   
2747  C CA  . GLY A 374 ? 0.6034 1.2871 1.0693 0.0090  -0.0091 -0.0277 374 GLY A CA  
2748  C C   . GLY A 374 ? 0.5480 1.2462 1.0184 0.0091  -0.0106 -0.0347 374 GLY A C   
2749  O O   . GLY A 374 ? 0.5298 1.2279 1.0021 0.0106  -0.0127 -0.0409 374 GLY A O   
2750  N N   . GLU A 375 ? 0.5366 1.2477 1.0088 0.0076  -0.0096 -0.0338 375 GLU A N   
2751  C CA  . GLU A 375 ? 0.4507 1.1766 0.9259 0.0076  -0.0110 -0.0400 375 GLU A CA  
2752  C C   . GLU A 375 ? 0.4655 1.2025 0.9384 0.0104  -0.0113 -0.0399 375 GLU A C   
2753  O O   . GLU A 375 ? 0.3947 1.1350 0.8648 0.0112  -0.0099 -0.0332 375 GLU A O   
2754  C CB  . GLU A 375 ? 0.4682 1.2040 0.9458 0.0051  -0.0104 -0.0387 375 GLU A CB  
2755  C CG  . GLU A 375 ? 0.4154 1.1673 0.8948 0.0051  -0.0123 -0.0447 375 GLU A CG  
2756  C CD  . GLU A 375 ? 0.4060 1.1693 0.8870 0.0035  -0.0121 -0.0419 375 GLU A CD  
2757  O OE1 . GLU A 375 ? 0.4652 1.2244 0.9465 0.0026  -0.0102 -0.0352 375 GLU A OE1 
2758  O OE2 . GLU A 375 ? 0.3826 1.1593 0.8644 0.0033  -0.0141 -0.0464 375 GLU A OE2 
2759  N N   . ALA A 376 ? 0.4258 1.1685 0.9003 0.0117  -0.0129 -0.0473 376 ALA A N   
2760  C CA  . ALA A 376 ? 0.5093 1.2639 0.9822 0.0141  -0.0126 -0.0482 376 ALA A CA  
2761  C C   . ALA A 376 ? 0.3699 1.1186 0.8407 0.0162  -0.0116 -0.0425 376 ALA A C   
2762  O O   . ALA A 376 ? 0.3658 1.1227 0.8343 0.0169  -0.0102 -0.0378 376 ALA A O   
2763  C CB  . ALA A 376 ? 0.4969 1.2676 0.9679 0.0133  -0.0119 -0.0460 376 ALA A CB  
2764  N N   . VAL A 377 ? 0.3729 1.1067 0.8443 0.0169  -0.0126 -0.0429 377 VAL A N   
2765  C CA  . VAL A 377 ? 0.4514 1.1790 0.9213 0.0191  -0.0126 -0.0390 377 VAL A CA  
2766  C C   . VAL A 377 ? 0.4095 1.1412 0.8827 0.0218  -0.0139 -0.0456 377 VAL A C   
2767  O O   . VAL A 377 ? 0.4149 1.1428 0.8910 0.0224  -0.0156 -0.0527 377 VAL A O   
2768  C CB  . VAL A 377 ? 0.4660 1.1751 0.9341 0.0187  -0.0134 -0.0354 377 VAL A CB  
2769  C CG1 . VAL A 377 ? 0.5269 1.2265 0.9971 0.0179  -0.0150 -0.0411 377 VAL A CG1 
2770  C CG2 . VAL A 377 ? 0.4503 1.1528 0.9175 0.0212  -0.0145 -0.0332 377 VAL A CG2 
2771  N N   . THR A 378 ? 0.4160 1.1557 0.8892 0.0234  -0.0129 -0.0435 378 THR A N   
2772  C CA  . THR A 378 ? 0.3711 1.1178 0.8481 0.0259  -0.0133 -0.0498 378 THR A CA  
2773  C C   . THR A 378 ? 0.3714 1.1082 0.8504 0.0282  -0.0149 -0.0480 378 THR A C   
2774  O O   . THR A 378 ? 0.3676 1.1062 0.8456 0.0283  -0.0139 -0.0422 378 THR A O   
2775  C CB  . THR A 378 ? 0.3677 1.1324 0.8440 0.0259  -0.0107 -0.0492 378 THR A CB  
2776  O OG1 . THR A 378 ? 0.3631 1.1283 0.8373 0.0254  -0.0092 -0.0408 378 THR A OG1 
2777  C CG2 . THR A 378 ? 0.3907 1.1646 0.8641 0.0237  -0.0099 -0.0502 378 THR A CG2 
2778  N N   . VAL A 379 ? 0.4496 1.1755 0.9313 0.0299  -0.0176 -0.0530 379 VAL A N   
2779  C CA  . VAL A 379 ? 0.4485 1.1658 0.9328 0.0326  -0.0200 -0.0526 379 VAL A CA  
2780  C C   . VAL A 379 ? 0.4620 1.1918 0.9524 0.0353  -0.0195 -0.0586 379 VAL A C   
2781  O O   . VAL A 379 ? 0.5262 1.2605 1.0201 0.0365  -0.0198 -0.0666 379 VAL A O   
2782  C CB  . VAL A 379 ? 0.4944 1.1940 0.9788 0.0335  -0.0234 -0.0551 379 VAL A CB  
2783  C CG1 . VAL A 379 ? 0.5412 1.2327 1.0285 0.0368  -0.0266 -0.0552 379 VAL A CG1 
2784  C CG2 . VAL A 379 ? 0.5688 1.2565 1.0469 0.0306  -0.0230 -0.0489 379 VAL A CG2 
2785  N N   . GLU A 380 ? 0.4563 1.1919 0.9483 0.0360  -0.0186 -0.0549 380 GLU A N   
2786  C CA  . GLU A 380 ? 0.4788 1.2280 0.9772 0.0382  -0.0172 -0.0601 380 GLU A CA  
2787  C C   . GLU A 380 ? 0.5484 1.2903 1.0535 0.0420  -0.0207 -0.0664 380 GLU A C   
2788  O O   . GLU A 380 ? 0.5888 1.3146 1.0929 0.0429  -0.0245 -0.0659 380 GLU A O   
2789  C CB  . GLU A 380 ? 0.4589 1.2162 0.9577 0.0374  -0.0149 -0.0539 380 GLU A CB  
2790  C CG  . GLU A 380 ? 0.4905 1.2669 0.9920 0.0373  -0.0109 -0.0567 380 GLU A CG  
2791  C CD  . GLU A 380 ? 0.5059 1.2899 1.0050 0.0350  -0.0079 -0.0486 380 GLU A CD  
2792  O OE1 . GLU A 380 ? 0.3903 1.1649 0.8852 0.0333  -0.0089 -0.0412 380 GLU A OE1 
2793  O OE2 . GLU A 380 ? 0.6542 1.4531 1.1555 0.0347  -0.0043 -0.0497 380 GLU A OE2 
2794  N N   . ASP A 381 ? 0.5982 1.3523 1.1102 0.0443  -0.0194 -0.0723 381 ASP A N   
2795  C CA  . ASP A 381 ? 0.6393 1.3887 1.1593 0.0485  -0.0227 -0.0792 381 ASP A CA  
2796  C C   . ASP A 381 ? 0.7473 1.4849 1.2694 0.0500  -0.0266 -0.0745 381 ASP A C   
2797  O O   . ASP A 381 ? 0.7565 1.4972 1.2777 0.0486  -0.0255 -0.0681 381 ASP A O   
2798  C CB  . ASP A 381 ? 0.6753 1.4421 1.2026 0.0506  -0.0196 -0.0860 381 ASP A CB  
2799  C CG  . ASP A 381 ? 0.5943 1.3748 1.1175 0.0485  -0.0152 -0.0891 381 ASP A CG  
2800  O OD1 . ASP A 381 ? 0.5575 1.3323 1.0758 0.0472  -0.0161 -0.0910 381 ASP A OD1 
2801  O OD2 . ASP A 381 ? 0.5972 1.3940 1.1218 0.0481  -0.0109 -0.0897 381 ASP A OD2 
2802  N N   . GLU A 382 ? 1.0254 1.7490 1.5499 0.0529  -0.0314 -0.0778 382 GLU A N   
2803  C CA  . GLU A 382 ? 1.0394 1.7493 1.5652 0.0550  -0.0364 -0.0743 382 GLU A CA  
2804  C C   . GLU A 382 ? 1.0446 1.7419 1.5606 0.0520  -0.0374 -0.0651 382 GLU A C   
2805  O O   . GLU A 382 ? 1.0588 1.7434 1.5739 0.0534  -0.0418 -0.0619 382 GLU A O   
2806  C CB  . GLU A 382 ? 1.0335 1.7531 1.5681 0.0572  -0.0368 -0.0747 382 GLU A CB  
2807  C CG  . GLU A 382 ? 1.0567 1.7852 1.6027 0.0614  -0.0372 -0.0841 382 GLU A CG  
2808  C CD  . GLU A 382 ? 1.1068 1.8409 1.6625 0.0639  -0.0390 -0.0840 382 GLU A CD  
2809  O OE1 . GLU A 382 ? 1.0692 1.7950 1.6224 0.0630  -0.0420 -0.0773 382 GLU A OE1 
2810  O OE2 . GLU A 382 ? 1.0883 1.8354 1.6545 0.0666  -0.0374 -0.0909 382 GLU A OE2 
2811  N N   . VAL A 383 ? 0.8145 1.5148 1.3232 0.0480  -0.0336 -0.0608 383 VAL A N   
2812  C CA  . VAL A 383 ? 0.7776 1.4669 1.2775 0.0452  -0.0339 -0.0523 383 VAL A CA  
2813  C C   . VAL A 383 ? 0.7692 1.4394 1.2637 0.0454  -0.0372 -0.0518 383 VAL A C   
2814  O O   . VAL A 383 ? 0.7400 1.4079 1.2349 0.0454  -0.0371 -0.0566 383 VAL A O   
2815  C CB  . VAL A 383 ? 0.7169 1.4160 1.2118 0.0413  -0.0288 -0.0483 383 VAL A CB  
2816  C CG1 . VAL A 383 ? 0.7386 1.4267 1.2251 0.0388  -0.0288 -0.0400 383 VAL A CG1 
2817  C CG2 . VAL A 383 ? 0.6514 1.3686 1.1509 0.0410  -0.0255 -0.0481 383 VAL A CG2 
2818  N N   . ALA A 384 ? 0.7884 1.4446 1.2777 0.0454  -0.0400 -0.0460 384 ALA A N   
2819  C CA  . ALA A 384 ? 0.7031 1.3398 1.1862 0.0457  -0.0432 -0.0447 384 ALA A CA  
2820  C C   . ALA A 384 ? 0.7206 1.3495 1.1936 0.0419  -0.0407 -0.0374 384 ALA A C   
2821  O O   . ALA A 384 ? 0.7241 1.3564 1.1942 0.0405  -0.0391 -0.0320 384 ALA A O   
2822  C CB  . ALA A 384 ? 0.7500 1.3750 1.2341 0.0493  -0.0492 -0.0443 384 ALA A CB  
2823  N N   . VAL A 385 ? 0.5514 1.1699 1.0198 0.0403  -0.0403 -0.0374 385 VAL A N   
2824  C CA  . VAL A 385 ? 0.5293 1.1396 0.9887 0.0367  -0.0376 -0.0311 385 VAL A CA  
2825  C C   . VAL A 385 ? 0.5317 1.1215 0.9849 0.0370  -0.0405 -0.0298 385 VAL A C   
2826  O O   . VAL A 385 ? 0.5301 1.1150 0.9850 0.0368  -0.0409 -0.0337 385 VAL A O   
2827  C CB  . VAL A 385 ? 0.5069 1.1275 0.9671 0.0334  -0.0328 -0.0322 385 VAL A CB  
2828  C CG1 . VAL A 385 ? 0.5199 1.1320 0.9721 0.0299  -0.0300 -0.0259 385 VAL A CG1 
2829  C CG2 . VAL A 385 ? 0.4993 1.1398 0.9644 0.0332  -0.0301 -0.0330 385 VAL A CG2 
2830  N N   . ILE A 386 ? 0.5386 1.1160 0.9844 0.0375  -0.0425 -0.0242 386 ILE A N   
2831  C CA  . ILE A 386 ? 0.5221 1.0791 0.9603 0.0379  -0.0454 -0.0220 386 ILE A CA  
2832  C C   . ILE A 386 ? 0.5047 1.0535 0.9326 0.0343  -0.0416 -0.0153 386 ILE A C   
2833  O O   . ILE A 386 ? 0.5157 1.0641 0.9386 0.0340  -0.0410 -0.0106 386 ILE A O   
2834  C CB  . ILE A 386 ? 0.5083 1.0562 0.9452 0.0419  -0.0517 -0.0213 386 ILE A CB  
2835  C CG1 . ILE A 386 ? 0.5271 1.0830 0.9753 0.0459  -0.0554 -0.0285 386 ILE A CG1 
2836  C CG2 . ILE A 386 ? 0.5073 1.0330 0.9337 0.0421  -0.0545 -0.0178 386 ILE A CG2 
2837  C CD1 . ILE A 386 ? 0.5721 1.1464 1.0288 0.0471  -0.0547 -0.0304 386 ILE A CD1 
2838  N N   . GLY A 387 ? 0.4876 1.0296 0.9128 0.0315  -0.0389 -0.0152 387 GLY A N   
2839  C CA  . GLY A 387 ? 0.5343 1.0674 0.9503 0.0280  -0.0349 -0.0093 387 GLY A CA  
2840  C C   . GLY A 387 ? 0.5297 1.0738 0.9448 0.0261  -0.0305 -0.0057 387 GLY A C   
2841  O O   . GLY A 387 ? 0.5864 1.1235 0.9936 0.0260  -0.0300 -0.0005 387 GLY A O   
2842  N N   . SER A 388 ? 0.5344 1.0955 0.9573 0.0247  -0.0274 -0.0084 388 SER A N   
2843  C CA  . SER A 388 ? 0.5160 1.0885 0.9391 0.0232  -0.0236 -0.0050 388 SER A CA  
2844  C C   . SER A 388 ? 0.5020 1.0852 0.9299 0.0201  -0.0194 -0.0068 388 SER A C   
2845  O O   . SER A 388 ? 0.5434 1.1275 0.9758 0.0194  -0.0199 -0.0116 388 SER A O   
2846  C CB  . SER A 388 ? 0.5071 1.0923 0.9352 0.0255  -0.0253 -0.0060 388 SER A CB  
2847  O OG  . SER A 388 ? 0.5726 1.1482 0.9964 0.0280  -0.0292 -0.0039 388 SER A OG  
2848  N N   . ILE A 389 ? 0.6458 1.2371 1.0731 0.0185  -0.0156 -0.0031 389 ILE A N   
2849  C CA  . ILE A 389 ? 0.6404 1.2425 1.0723 0.0157  -0.0119 -0.0040 389 ILE A CA  
2850  C C   . ILE A 389 ? 0.6160 1.2360 1.0527 0.0164  -0.0112 -0.0040 389 ILE A C   
2851  O O   . ILE A 389 ? 0.6794 1.3011 1.1134 0.0170  -0.0102 0.0006  389 ILE A O   
2852  C CB  . ILE A 389 ? 0.5138 1.1085 0.9407 0.0129  -0.0077 0.0008  389 ILE A CB  
2853  C CG1 . ILE A 389 ? 0.5623 1.1376 0.9823 0.0122  -0.0082 0.0020  389 ILE A CG1 
2854  C CG2 . ILE A 389 ? 0.6781 1.2841 1.1112 0.0100  -0.0046 -0.0009 389 ILE A CG2 
2855  C CD1 . ILE A 389 ? 0.5807 1.1523 1.0046 0.0114  -0.0100 -0.0032 389 ILE A CD1 
2856  N N   . VAL A 390 ? 0.9085 1.5415 1.3519 0.0162  -0.0116 -0.0092 390 VAL A N   
2857  C CA  . VAL A 390 ? 0.8835 1.5340 1.3310 0.0168  -0.0108 -0.0095 390 VAL A CA  
2858  C C   . VAL A 390 ? 0.8743 1.5349 1.3247 0.0142  -0.0081 -0.0096 390 VAL A C   
2859  O O   . VAL A 390 ? 0.8836 1.5427 1.3365 0.0125  -0.0080 -0.0133 390 VAL A O   
2860  C CB  . VAL A 390 ? 0.8728 1.5319 1.3253 0.0190  -0.0135 -0.0155 390 VAL A CB  
2861  C CG1 . VAL A 390 ? 0.8498 1.5262 1.3051 0.0194  -0.0122 -0.0149 390 VAL A CG1 
2862  C CG2 . VAL A 390 ? 0.8830 1.5316 1.3340 0.0216  -0.0167 -0.0159 390 VAL A CG2 
2863  N N   . LEU A 391 ? 0.9048 1.5755 1.3552 0.0141  -0.0063 -0.0055 391 LEU A N   
2864  C CA  . LEU A 391 ? 0.8962 1.5776 1.3497 0.0121  -0.0042 -0.0052 391 LEU A CA  
2865  C C   . LEU A 391 ? 0.8872 1.5836 1.3454 0.0123  -0.0056 -0.0109 391 LEU A C   
2866  O O   . LEU A 391 ? 0.8865 1.5858 1.3457 0.0141  -0.0075 -0.0148 391 LEU A O   
2867  C CB  . LEU A 391 ? 0.8806 1.5665 1.3323 0.0123  -0.0021 0.0015  391 LEU A CB  
2868  C CG  . LEU A 391 ? 0.8881 1.5638 1.3369 0.0111  0.0006  0.0064  391 LEU A CG  
2869  C CD1 . LEU A 391 ? 0.9065 1.5646 1.3495 0.0117  0.0002  0.0076  391 LEU A CD1 
2870  C CD2 . LEU A 391 ? 0.8794 1.5612 1.3275 0.0118  0.0023  0.0123  391 LEU A CD2 
2871  N N   . GLN A 392 ? 0.6926 1.3989 1.1537 0.0106  -0.0046 -0.0115 392 GLN A N   
2872  C CA  . GLN A 392 ? 0.5547 1.2751 1.0192 0.0105  -0.0061 -0.0172 392 GLN A CA  
2873  C C   . GLN A 392 ? 0.9057 1.6387 1.3689 0.0123  -0.0060 -0.0150 392 GLN A C   
2874  O O   . GLN A 392 ? 0.4514 1.1845 0.9123 0.0130  -0.0047 -0.0084 392 GLN A O   
2875  C CB  . GLN A 392 ? 0.5934 1.3209 1.0616 0.0081  -0.0057 -0.0187 392 GLN A CB  
2876  C CG  . GLN A 392 ? 0.6302 1.3662 1.0984 0.0078  -0.0042 -0.0127 392 GLN A CG  
2877  C CD  . GLN A 392 ? 0.7096 1.4345 1.1765 0.0071  -0.0017 -0.0065 392 GLN A CD  
2878  O OE1 . GLN A 392 ? 0.7991 1.5097 1.2641 0.0066  -0.0009 -0.0065 392 GLN A OE1 
2879  N NE2 . GLN A 392 ? 0.6551 1.3865 1.1227 0.0071  -0.0003 -0.0014 392 GLN A NE2 
2880  N N   . ASN A 393 ? 0.5428 1.2865 1.0076 0.0131  -0.0073 -0.0208 393 ASN A N   
2881  C CA  . ASN A 393 ? 0.5558 1.3128 1.0191 0.0144  -0.0069 -0.0194 393 ASN A CA  
2882  C C   . ASN A 393 ? 0.5226 1.2744 0.9840 0.0161  -0.0062 -0.0149 393 ASN A C   
2883  O O   . ASN A 393 ? 0.5500 1.3048 1.0093 0.0163  -0.0049 -0.0084 393 ASN A O   
2884  C CB  . ASN A 393 ? 0.5822 1.3499 1.0446 0.0135  -0.0062 -0.0149 393 ASN A CB  
2885  C CG  . ASN A 393 ? 0.5863 1.3568 1.0516 0.0115  -0.0071 -0.0183 393 ASN A CG  
2886  O OD1 . ASN A 393 ? 0.5499 1.3213 1.0175 0.0108  -0.0086 -0.0257 393 ASN A OD1 
2887  N ND2 . ASN A 393 ? 0.5520 1.3238 1.0178 0.0105  -0.0064 -0.0130 393 ASN A ND2 
2888  N N   . LYS A 394 ? 0.4866 1.2301 0.9491 0.0174  -0.0074 -0.0187 394 LYS A N   
2889  C CA  . LYS A 394 ? 0.4212 1.1578 0.8826 0.0188  -0.0074 -0.0151 394 LYS A CA  
2890  C C   . LYS A 394 ? 0.4401 1.1803 0.9045 0.0208  -0.0086 -0.0207 394 LYS A C   
2891  O O   . LYS A 394 ? 0.4173 1.1564 0.8842 0.0214  -0.0100 -0.0278 394 LYS A O   
2892  C CB  . LYS A 394 ? 0.4560 1.1749 0.9155 0.0186  -0.0081 -0.0125 394 LYS A CB  
2893  C CG  . LYS A 394 ? 0.4599 1.1720 0.9170 0.0196  -0.0081 -0.0067 394 LYS A CG  
2894  C CD  . LYS A 394 ? 0.4904 1.2079 0.9455 0.0187  -0.0059 0.0001  394 LYS A CD  
2895  C CE  . LYS A 394 ? 0.5607 1.2717 1.0138 0.0195  -0.0059 0.0055  394 LYS A CE  
2896  N NZ  . LYS A 394 ? 0.6660 1.3800 1.1171 0.0186  -0.0038 0.0123  394 LYS A NZ  
2897  N N   . THR A 395 ? 0.3560 1.1005 0.8208 0.0219  -0.0079 -0.0178 395 THR A N   
2898  C CA  . THR A 395 ? 0.3792 1.1282 0.8479 0.0238  -0.0085 -0.0227 395 THR A CA  
2899  C C   . THR A 395 ? 0.4422 1.1793 0.9120 0.0252  -0.0103 -0.0206 395 THR A C   
2900  O O   . THR A 395 ? 0.4227 1.1543 0.8899 0.0246  -0.0100 -0.0139 395 THR A O   
2901  C CB  . THR A 395 ? 0.3603 1.1258 0.8295 0.0237  -0.0060 -0.0216 395 THR A CB  
2902  O OG1 . THR A 395 ? 0.3548 1.1236 0.8285 0.0256  -0.0061 -0.0251 395 THR A OG1 
2903  C CG2 . THR A 395 ? 0.4252 1.1914 0.8912 0.0224  -0.0044 -0.0125 395 THR A CG2 
2904  N N   . LEU A 396 ? 0.4762 1.2092 0.9499 0.0273  -0.0126 -0.0266 396 LEU A N   
2905  C CA  . LEU A 396 ? 0.4973 1.2186 0.9723 0.0291  -0.0153 -0.0256 396 LEU A CA  
2906  C C   . LEU A 396 ? 0.5471 1.2765 1.0290 0.0314  -0.0159 -0.0303 396 LEU A C   
2907  O O   . LEU A 396 ? 0.5706 1.3025 1.0565 0.0332  -0.0169 -0.0377 396 LEU A O   
2908  C CB  . LEU A 396 ? 0.4812 1.1864 0.9544 0.0297  -0.0182 -0.0278 396 LEU A CB  
2909  C CG  . LEU A 396 ? 0.5558 1.2509 1.0227 0.0274  -0.0174 -0.0228 396 LEU A CG  
2910  C CD1 . LEU A 396 ? 0.6280 1.3071 1.0930 0.0278  -0.0199 -0.0250 396 LEU A CD1 
2911  C CD2 . LEU A 396 ? 0.6122 1.3029 1.0752 0.0267  -0.0167 -0.0150 396 LEU A CD2 
2912  N N   . ASN A 397 ? 0.6003 1.3338 1.0841 0.0314  -0.0153 -0.0263 397 ASN A N   
2913  C CA  . ASN A 397 ? 0.5439 1.2843 1.0354 0.0335  -0.0159 -0.0302 397 ASN A CA  
2914  C C   . ASN A 397 ? 0.5872 1.3146 1.0811 0.0356  -0.0203 -0.0300 397 ASN A C   
2915  O O   . ASN A 397 ? 0.5861 1.3173 1.0876 0.0380  -0.0219 -0.0347 397 ASN A O   
2916  C CB  . ASN A 397 ? 0.5229 1.2771 1.0162 0.0319  -0.0123 -0.0263 397 ASN A CB  
2917  C CG  . ASN A 397 ? 0.5576 1.3053 1.0466 0.0299  -0.0122 -0.0176 397 ASN A CG  
2918  O OD1 . ASN A 397 ? 0.5667 1.3037 1.0493 0.0289  -0.0130 -0.0140 397 ASN A OD1 
2919  N ND2 . ASN A 397 ? 0.6008 1.3550 1.0937 0.0292  -0.0109 -0.0144 397 ASN A ND2 
2920  N N   . VAL A 398 ? 0.6920 1.4046 1.1797 0.0348  -0.0224 -0.0249 398 VAL A N   
2921  C CA  . VAL A 398 ? 0.7707 1.4701 1.2589 0.0366  -0.0271 -0.0239 398 VAL A CA  
2922  C C   . VAL A 398 ? 0.8375 1.5202 1.3198 0.0373  -0.0299 -0.0246 398 VAL A C   
2923  O O   . VAL A 398 ? 0.7484 1.4279 1.2249 0.0354  -0.0278 -0.0231 398 VAL A O   
2924  C CB  . VAL A 398 ? 0.7882 1.4843 1.2734 0.0349  -0.0269 -0.0166 398 VAL A CB  
2925  C CG1 . VAL A 398 ? 0.8057 1.4949 1.2817 0.0324  -0.0248 -0.0109 398 VAL A CG1 
2926  C CG2 . VAL A 398 ? 0.8751 1.5595 1.3616 0.0369  -0.0322 -0.0163 398 VAL A CG2 
2927  N N   . SER A 399 ? 1.2029 1.8750 1.6870 0.0401  -0.0348 -0.0269 399 SER A N   
2928  C CA  . SER A 399 ? 1.2261 1.8810 1.7042 0.0409  -0.0378 -0.0272 399 SER A CA  
2929  C C   . SER A 399 ? 1.2359 1.8778 1.7039 0.0388  -0.0377 -0.0200 399 SER A C   
2930  O O   . SER A 399 ? 1.2310 1.8719 1.6975 0.0383  -0.0383 -0.0157 399 SER A O   
2931  C CB  . SER A 399 ? 1.2398 1.8868 1.7224 0.0448  -0.0436 -0.0311 399 SER A CB  
2932  O OG  . SER A 399 ? 1.2320 1.8904 1.7244 0.0471  -0.0435 -0.0384 399 SER A OG  
2933  N N   . VAL A 400 ? 0.8737 1.5058 1.3350 0.0374  -0.0367 -0.0190 400 VAL A N   
2934  C CA  . VAL A 400 ? 0.7626 1.3818 1.2139 0.0354  -0.0359 -0.0128 400 VAL A CA  
2935  C C   . VAL A 400 ? 0.6540 1.2547 1.0995 0.0367  -0.0395 -0.0131 400 VAL A C   
2936  O O   . VAL A 400 ? 0.6480 1.2461 1.0970 0.0384  -0.0417 -0.0181 400 VAL A O   
2937  C CB  . VAL A 400 ? 0.7175 1.3421 1.1658 0.0321  -0.0306 -0.0103 400 VAL A CB  
2938  C CG1 . VAL A 400 ? 0.7455 1.3875 1.1984 0.0310  -0.0273 -0.0092 400 VAL A CG1 
2939  C CG2 . VAL A 400 ? 0.6397 1.2648 1.0897 0.0315  -0.0296 -0.0149 400 VAL A CG2 
2940  N N   . GLN A 401 ? 0.5892 1.1763 1.0252 0.0359  -0.0401 -0.0078 401 GLN A N   
2941  C CA  . GLN A 401 ? 0.5177 1.0857 0.9461 0.0369  -0.0436 -0.0070 401 GLN A CA  
2942  C C   . GLN A 401 ? 0.5053 1.0615 0.9221 0.0347  -0.0414 -0.0007 401 GLN A C   
2943  O O   . GLN A 401 ? 0.5008 1.0573 0.9147 0.0346  -0.0414 0.0028  401 GLN A O   
2944  C CB  . GLN A 401 ? 0.5910 1.1535 1.0217 0.0407  -0.0503 -0.0088 401 GLN A CB  
2945  C CG  . GLN A 401 ? 0.6438 1.1858 1.0655 0.0422  -0.0547 -0.0072 401 GLN A CG  
2946  C CD  . GLN A 401 ? 0.6442 1.1813 1.0683 0.0462  -0.0620 -0.0087 401 GLN A CD  
2947  O OE1 . GLN A 401 ? 0.6675 1.2175 1.1023 0.0481  -0.0637 -0.0121 401 GLN A OE1 
2948  N NE2 . GLN A 401 ? 0.7006 1.2190 1.1148 0.0476  -0.0664 -0.0061 401 GLN A NE2 
2949  N N   . ASP A 402 ? 0.5230 1.0685 0.9335 0.0330  -0.0393 0.0005  402 ASP A N   
2950  C CA  . ASP A 402 ? 0.5289 1.0614 0.9275 0.0310  -0.0369 0.0060  402 ASP A CA  
2951  C C   . ASP A 402 ? 0.5374 1.0791 0.9357 0.0290  -0.0322 0.0095  402 ASP A C   
2952  O O   . ASP A 402 ? 0.5418 1.0777 0.9335 0.0292  -0.0327 0.0133  402 ASP A O   
2953  C CB  . ASP A 402 ? 0.5341 1.0500 0.9236 0.0332  -0.0421 0.0084  402 ASP A CB  
2954  C CG  . ASP A 402 ? 0.5410 1.0465 0.9305 0.0356  -0.0471 0.0055  402 ASP A CG  
2955  O OD1 . ASP A 402 ? 0.4736 0.9788 0.8659 0.0344  -0.0452 0.0031  402 ASP A OD1 
2956  O OD2 . ASP A 402 ? 0.6262 1.1237 1.0131 0.0386  -0.0533 0.0055  402 ASP A OD2 
2957  N N   . ASP A 403 ? 0.5417 1.0976 0.9469 0.0271  -0.0280 0.0081  403 ASP A N   
2958  C CA  . ASP A 403 ? 0.5973 1.1631 1.0034 0.0254  -0.0237 0.0112  403 ASP A CA  
2959  C C   . ASP A 403 ? 0.5760 1.1498 0.9856 0.0228  -0.0189 0.0105  403 ASP A C   
2960  O O   . ASP A 403 ? 0.5515 1.1234 0.9632 0.0221  -0.0189 0.0072  403 ASP A O   
2961  C CB  . ASP A 403 ? 0.5780 1.1580 0.9917 0.0268  -0.0252 0.0101  403 ASP A CB  
2962  C CG  . ASP A 403 ? 0.6427 1.2274 1.0548 0.0257  -0.0223 0.0147  403 ASP A CG  
2963  O OD1 . ASP A 403 ? 0.6878 1.2701 1.0957 0.0238  -0.0181 0.0178  403 ASP A OD1 
2964  O OD2 . ASP A 403 ? 0.6866 1.2773 1.1021 0.0267  -0.0241 0.0152  403 ASP A OD2 
2965  N N   . ILE A 404 ? 0.6363 1.2186 1.0468 0.0213  -0.0149 0.0135  404 ILE A N   
2966  C CA  . ILE A 404 ? 0.5593 1.1514 0.9742 0.0190  -0.0107 0.0130  404 ILE A CA  
2967  C C   . ILE A 404 ? 0.5916 1.2009 1.0129 0.0193  -0.0099 0.0132  404 ILE A C   
2968  O O   . ILE A 404 ? 0.6121 1.2232 1.0316 0.0193  -0.0083 0.0175  404 ILE A O   
2969  C CB  . ILE A 404 ? 0.6321 1.2165 1.0412 0.0169  -0.0064 0.0171  404 ILE A CB  
2970  C CG1 . ILE A 404 ? 0.6731 1.2392 1.0741 0.0165  -0.0069 0.0175  404 ILE A CG1 
2971  C CG2 . ILE A 404 ? 0.5987 1.1942 1.0138 0.0146  -0.0026 0.0161  404 ILE A CG2 
2972  C CD1 . ILE A 404 ? 0.7247 1.2827 1.1195 0.0143  -0.0020 0.0214  404 ILE A CD1 
2973  N N   . ILE A 405 ? 0.6270 1.2486 1.0556 0.0196  -0.0109 0.0088  405 ILE A N   
2974  C CA  . ILE A 405 ? 0.5962 1.2341 1.0303 0.0200  -0.0104 0.0088  405 ILE A CA  
2975  C C   . ILE A 405 ? 0.6393 1.2880 1.0760 0.0181  -0.0069 0.0098  405 ILE A C   
2976  O O   . ILE A 405 ? 0.6882 1.3399 1.1276 0.0169  -0.0063 0.0063  405 ILE A O   
2977  C CB  . ILE A 405 ? 0.6278 1.2739 1.0678 0.0216  -0.0132 0.0032  405 ILE A CB  
2978  C CG1 . ILE A 405 ? 0.6048 1.2428 1.0438 0.0239  -0.0169 0.0027  405 ILE A CG1 
2979  C CG2 . ILE A 405 ? 0.6824 1.3465 1.1276 0.0214  -0.0116 0.0029  405 ILE A CG2 
2980  C CD1 . ILE A 405 ? 0.6328 1.2556 1.0686 0.0248  -0.0199 0.0003  405 ILE A CD1 
2981  N N   . LEU A 406 ? 0.6716 1.3259 1.1079 0.0180  -0.0050 0.0145  406 LEU A N   
2982  C CA  . LEU A 406 ? 0.7081 1.3731 1.1471 0.0166  -0.0022 0.0162  406 LEU A CA  
2983  C C   . LEU A 406 ? 0.6823 1.3643 1.1264 0.0169  -0.0027 0.0142  406 LEU A C   
2984  O O   . LEU A 406 ? 0.6522 1.3391 1.0969 0.0180  -0.0036 0.0154  406 LEU A O   
2985  C CB  . LEU A 406 ? 0.6983 1.3601 1.1342 0.0166  0.0001  0.0224  406 LEU A CB  
2986  C CG  . LEU A 406 ? 0.6026 1.2478 1.0322 0.0164  0.0012  0.0247  406 LEU A CG  
2987  C CD1 . LEU A 406 ? 0.5538 1.1967 0.9808 0.0168  0.0034  0.0303  406 LEU A CD1 
2988  C CD2 . LEU A 406 ? 0.6486 1.2896 1.0784 0.0146  0.0030  0.0225  406 LEU A CD2 
2989  O OXT . LEU A 406 ? 0.6781 1.3694 1.1254 0.0160  -0.0022 0.0113  406 LEU A OXT 
2990  N N   . GLU B 4   ? 0.9533 1.7907 1.2429 -0.0146 0.0396  0.3053  4   GLU B N   
2991  C CA  . GLU B 4   ? 0.9146 1.7648 1.2069 -0.0145 0.0413  0.2903  4   GLU B CA  
2992  C C   . GLU B 4   ? 0.8943 1.7461 1.1898 -0.0079 0.0333  0.2814  4   GLU B C   
2993  O O   . GLU B 4   ? 0.9112 1.7557 1.2061 -0.0033 0.0265  0.2868  4   GLU B O   
2994  C CB  . GLU B 4   ? 0.8823 1.7297 1.1899 -0.0189 0.0470  0.2830  4   GLU B CB  
2995  C CG  . GLU B 4   ? 0.9077 1.7566 1.2140 -0.0261 0.0559  0.2894  4   GLU B CG  
2996  C CD  . GLU B 4   ? 0.9260 1.7730 1.2484 -0.0301 0.0606  0.2812  4   GLU B CD  
2997  O OE1 . GLU B 4   ? 0.9688 1.8111 1.3028 -0.0271 0.0566  0.2718  4   GLU B OE1 
2998  O OE2 . GLU B 4   ? 0.8654 1.7160 1.1891 -0.0362 0.0683  0.2841  4   GLU B OE2 
2999  N N   . LYS B 5   ? 0.7072 1.5687 1.0066 -0.0076 0.0342  0.2676  5   LYS B N   
3000  C CA  . LYS B 5   ? 0.6881 1.5513 0.9920 -0.0021 0.0275  0.2580  5   LYS B CA  
3001  C C   . LYS B 5   ? 0.6543 1.5195 0.9705 -0.0034 0.0302  0.2442  5   LYS B C   
3002  O O   . LYS B 5   ? 0.6563 1.5293 0.9720 -0.0075 0.0365  0.2396  5   LYS B O   
3003  C CB  . LYS B 5   ? 0.7512 1.6278 1.0409 0.0010  0.0237  0.2560  5   LYS B CB  
3004  C CG  . LYS B 5   ? 0.7400 1.6147 1.0321 0.0073  0.0147  0.2536  5   LYS B CG  
3005  C CD  . LYS B 5   ? 0.9045 1.7930 1.1830 0.0099  0.0107  0.2507  5   LYS B CD  
3006  C CE  . LYS B 5   ? 1.0840 1.9701 1.3646 0.0160  0.0013  0.2514  5   LYS B CE  
3007  N NZ  . LYS B 5   ? 1.0504 1.9232 1.3334 0.0178  -0.0014 0.2644  5   LYS B NZ  
3008  N N   . VAL B 6   ? 0.6445 1.5026 0.9716 0.0002  0.0254  0.2380  6   VAL B N   
3009  C CA  . VAL B 6   ? 0.5296 1.3865 0.8690 -0.0006 0.0272  0.2260  6   VAL B CA  
3010  C C   . VAL B 6   ? 0.5241 1.3860 0.8652 0.0038  0.0219  0.2156  6   VAL B C   
3011  O O   . VAL B 6   ? 0.6208 1.4797 0.9611 0.0082  0.0158  0.2180  6   VAL B O   
3012  C CB  . VAL B 6   ? 0.5769 1.4178 0.9293 -0.0014 0.0273  0.2284  6   VAL B CB  
3013  C CG1 . VAL B 6   ? 0.6265 1.4660 0.9904 -0.0022 0.0288  0.2162  6   VAL B CG1 
3014  C CG2 . VAL B 6   ? 0.5982 1.4335 0.9497 -0.0062 0.0323  0.2390  6   VAL B CG2 
3015  N N   . VAL B 7   ? 0.5080 1.3775 0.8520 0.0027  0.0242  0.2039  7   VAL B N   
3016  C CA  . VAL B 7   ? 0.4964 1.3699 0.8438 0.0062  0.0200  0.1929  7   VAL B CA  
3017  C C   . VAL B 7   ? 0.4807 1.3474 0.8411 0.0053  0.0216  0.1840  7   VAL B C   
3018  O O   . VAL B 7   ? 0.4789 1.3425 0.8442 0.0016  0.0265  0.1841  7   VAL B O   
3019  C CB  . VAL B 7   ? 0.4999 1.3891 0.8372 0.0063  0.0204  0.1864  7   VAL B CB  
3020  C CG1 . VAL B 7   ? 0.5051 1.4004 0.8447 0.0026  0.0267  0.1788  7   VAL B CG1 
3021  C CG2 . VAL B 7   ? 0.5281 1.4208 0.8671 0.0103  0.0143  0.1780  7   VAL B CG2 
3022  N N   . ALA B 8   ? 0.4700 1.3343 0.8362 0.0086  0.0173  0.1764  8   ALA B N   
3023  C CA  . ALA B 8   ? 0.4559 1.3128 0.8335 0.0083  0.0181  0.1682  8   ALA B CA  
3024  C C   . ALA B 8   ? 0.4688 1.3332 0.8473 0.0099  0.0163  0.1562  8   ALA B C   
3025  O O   . ALA B 8   ? 0.5663 1.4356 0.9411 0.0128  0.0119  0.1546  8   ALA B O   
3026  C CB  . ALA B 8   ? 0.4518 1.2943 0.8373 0.0105  0.0150  0.1717  8   ALA B CB  
3027  N N   . VAL B 9   ? 0.4387 1.3037 0.8226 0.0080  0.0193  0.1478  9   VAL B N   
3028  C CA  . VAL B 9   ? 0.4883 1.3588 0.8739 0.0092  0.0180  0.1360  9   VAL B CA  
3029  C C   . VAL B 9   ? 0.4785 1.3383 0.8749 0.0092  0.0181  0.1300  9   VAL B C   
3030  O O   . VAL B 9   ? 0.6214 1.4769 1.0225 0.0067  0.0215  0.1302  9   VAL B O   
3031  C CB  . VAL B 9   ? 0.4802 1.3638 0.8603 0.0072  0.0216  0.1306  9   VAL B CB  
3032  C CG1 . VAL B 9   ? 0.4969 1.3846 0.8800 0.0086  0.0200  0.1181  9   VAL B CG1 
3033  C CG2 . VAL B 9   ? 0.6011 1.4952 0.9688 0.0073  0.0214  0.1365  9   VAL B CG2 
3034  N N   . ILE B 10  ? 0.5240 1.3798 0.9242 0.0118  0.0143  0.1247  10  ILE B N   
3035  C CA  . ILE B 10  ? 0.5616 1.4066 0.9707 0.0121  0.0139  0.1193  10  ILE B CA  
3036  C C   . ILE B 10  ? 0.5660 1.4159 0.9767 0.0125  0.0134  0.1079  10  ILE B C   
3037  O O   . ILE B 10  ? 0.5718 1.4293 0.9789 0.0140  0.0109  0.1042  10  ILE B O   
3038  C CB  . ILE B 10  ? 0.6527 1.4873 1.0655 0.0147  0.0106  0.1228  10  ILE B CB  
3039  C CG1 . ILE B 10  ? 0.6993 1.5286 1.1106 0.0146  0.0109  0.1341  10  ILE B CG1 
3040  C CG2 . ILE B 10  ? 0.7132 1.5363 1.1337 0.0149  0.0106  0.1172  10  ILE B CG2 
3041  C CD1 . ILE B 10  ? 0.7036 1.5227 1.1190 0.0175  0.0079  0.1376  10  ILE B CD1 
3042  N N   . MET B 11  ? 0.6158 1.4611 1.0320 0.0112  0.0153  0.1023  11  MET B N   
3043  C CA  . MET B 11  ? 0.6070 1.4542 1.0258 0.0119  0.0145  0.0916  11  MET B CA  
3044  C C   . MET B 11  ? 0.6466 1.4843 1.0696 0.0139  0.0113  0.0890  11  MET B C   
3045  O O   . MET B 11  ? 0.6706 1.4972 1.0968 0.0144  0.0107  0.0936  11  MET B O   
3046  C CB  . MET B 11  ? 0.6735 1.5188 1.0971 0.0102  0.0172  0.0867  11  MET B CB  
3047  C CG  . MET B 11  ? 0.6619 1.5190 1.0823 0.0082  0.0210  0.0867  11  MET B CG  
3048  S SD  . MET B 11  ? 0.4455 1.3175 0.8593 0.0092  0.0206  0.0791  11  MET B SD  
3049  C CE  . MET B 11  ? 0.7661 1.6501 1.1765 0.0066  0.0262  0.0805  11  MET B CE  
3050  N N   . VAL B 12  ? 0.6010 1.4429 1.0240 0.0149  0.0093  0.0813  12  VAL B N   
3051  C CA  . VAL B 12  ? 0.5553 1.3900 0.9819 0.0165  0.0066  0.0784  12  VAL B CA  
3052  C C   . VAL B 12  ? 0.5323 1.3623 0.9631 0.0163  0.0066  0.0691  12  VAL B C   
3053  O O   . VAL B 12  ? 0.5756 1.3940 1.0106 0.0168  0.0061  0.0681  12  VAL B O   
3054  C CB  . VAL B 12  ? 0.5452 1.3884 0.9689 0.0179  0.0037  0.0783  12  VAL B CB  
3055  C CG1 . VAL B 12  ? 0.5456 1.3830 0.9742 0.0190  0.0015  0.0732  12  VAL B CG1 
3056  C CG2 . VAL B 12  ? 0.5587 1.4031 0.9793 0.0189  0.0028  0.0883  12  VAL B CG2 
3057  N N   . GLY B 13  ? 0.5513 1.3897 0.9807 0.0157  0.0073  0.0623  13  GLY B N   
3058  C CA  . GLY B 13  ? 0.6408 1.4753 1.0740 0.0157  0.0068  0.0533  13  GLY B CA  
3059  C C   . GLY B 13  ? 0.6528 1.4884 1.0866 0.0166  0.0041  0.0483  13  GLY B C   
3060  O O   . GLY B 13  ? 0.6551 1.4932 1.0876 0.0173  0.0023  0.0519  13  GLY B O   
3061  N N   . GLY B 14  ? 0.7432 1.5768 1.1796 0.0165  0.0036  0.0397  14  GLY B N   
3062  C CA  . GLY B 14  ? 0.7122 1.5468 1.1499 0.0168  0.0012  0.0340  14  GLY B CA  
3063  C C   . GLY B 14  ? 0.7204 1.5415 1.1629 0.0168  0.0006  0.0315  14  GLY B C   
3064  O O   . GLY B 14  ? 0.8219 1.6322 1.2660 0.0169  0.0017  0.0349  14  GLY B O   
3065  N N   . PRO B 15  ? 0.6956 1.5168 1.1402 0.0166  -0.0012 0.0253  15  PRO B N   
3066  C CA  . PRO B 15  ? 0.7570 1.5653 1.2056 0.0163  -0.0014 0.0232  15  PRO B CA  
3067  C C   . PRO B 15  ? 0.7921 1.5911 1.2419 0.0163  -0.0007 0.0192  15  PRO B C   
3068  O O   . PRO B 15  ? 0.7408 1.5277 1.1926 0.0162  -0.0008 0.0181  15  PRO B O   
3069  C CB  . PRO B 15  ? 0.6743 1.4873 1.1249 0.0157  -0.0035 0.0171  15  PRO B CB  
3070  C CG  . PRO B 15  ? 0.6245 1.4511 1.0721 0.0157  -0.0043 0.0129  15  PRO B CG  
3071  C CD  . PRO B 15  ? 0.6518 1.4850 1.0950 0.0163  -0.0030 0.0200  15  PRO B CD  
3072  N N   . THR B 16  ? 0.8359 1.6404 1.2846 0.0166  0.0001  0.0171  16  THR B N   
3073  C CA  . THR B 16  ? 0.8656 1.6623 1.3163 0.0170  0.0005  0.0137  16  THR B CA  
3074  C C   . THR B 16  ? 1.0064 1.7966 1.4570 0.0172  0.0017  0.0200  16  THR B C   
3075  O O   . THR B 16  ? 0.9654 1.7475 1.4180 0.0176  0.0015  0.0179  16  THR B O   
3076  C CB  . THR B 16  ? 0.7598 1.5661 1.2107 0.0174  0.0007  0.0070  16  THR B CB  
3077  O OG1 . THR B 16  ? 0.8154 1.6339 1.2633 0.0172  0.0025  0.0107  16  THR B OG1 
3078  C CG2 . THR B 16  ? 0.6733 1.4842 1.1247 0.0171  -0.0009 -0.0004 16  THR B CG2 
3079  N N   . LYS B 17  ? 1.5119 2.3055 1.9604 0.0169  0.0028  0.0275  17  LYS B N   
3080  C CA  . LYS B 17  ? 1.5193 2.3060 1.9680 0.0168  0.0038  0.0337  17  LYS B CA  
3081  C C   . LYS B 17  ? 1.5289 2.3025 1.9776 0.0171  0.0033  0.0375  17  LYS B C   
3082  O O   . LYS B 17  ? 1.5364 2.2991 1.9859 0.0172  0.0032  0.0387  17  LYS B O   
3083  C CB  . LYS B 17  ? 1.5189 2.3153 1.9654 0.0163  0.0054  0.0402  17  LYS B CB  
3084  C CG  . LYS B 17  ? 1.5195 2.3303 1.9644 0.0160  0.0064  0.0369  17  LYS B CG  
3085  C CD  . LYS B 17  ? 1.5280 2.3388 1.9762 0.0159  0.0072  0.0316  17  LYS B CD  
3086  C CE  . LYS B 17  ? 1.5327 2.3582 1.9793 0.0157  0.0089  0.0277  17  LYS B CE  
3087  N NZ  . LYS B 17  ? 1.5858 2.4205 2.0285 0.0147  0.0111  0.0348  17  LYS B NZ  
3088  N N   . GLY B 18  ? 1.0705 1.8454 1.5187 0.0172  0.0029  0.0391  18  GLY B N   
3089  C CA  . GLY B 18  ? 0.9118 1.6751 1.3603 0.0176  0.0030  0.0418  18  GLY B CA  
3090  C C   . GLY B 18  ? 0.8231 1.5770 1.2726 0.0174  0.0024  0.0361  18  GLY B C   
3091  O O   . GLY B 18  ? 0.7683 1.5155 1.2181 0.0173  0.0027  0.0368  18  GLY B O   
3092  N N   . THR B 19  ? 0.8515 1.6047 1.3016 0.0173  0.0016  0.0305  19  THR B N   
3093  C CA  . THR B 19  ? 0.7710 1.5142 1.2216 0.0172  0.0007  0.0253  19  THR B CA  
3094  C C   . THR B 19  ? 0.7066 1.4344 1.1555 0.0176  0.0006  0.0276  19  THR B C   
3095  O O   . THR B 19  ? 0.6211 1.3392 1.0695 0.0176  -0.0003 0.0239  19  THR B O   
3096  C CB  . THR B 19  ? 0.7665 1.5145 1.2189 0.0174  -0.0005 0.0182  19  THR B CB  
3097  O OG1 . THR B 19  ? 0.6755 1.4137 1.1285 0.0173  -0.0017 0.0133  19  THR B OG1 
3098  C CG2 . THR B 19  ? 0.8434 1.5911 1.2963 0.0181  -0.0007 0.0189  19  THR B CG2 
3099  N N   . ARG B 20  ? 0.7491 1.4741 1.1967 0.0179  0.0014  0.0335  20  ARG B N   
3100  C CA  . ARG B 20  ? 0.7034 1.4136 1.1485 0.0183  0.0013  0.0359  20  ARG B CA  
3101  C C   . ARG B 20  ? 0.7375 1.4421 1.1808 0.0183  0.0030  0.0402  20  ARG B C   
3102  O O   . ARG B 20  ? 0.7578 1.4492 1.1982 0.0185  0.0033  0.0409  20  ARG B O   
3103  C CB  . ARG B 20  ? 0.7878 1.4973 1.2331 0.0185  0.0008  0.0389  20  ARG B CB  
3104  C CG  . ARG B 20  ? 0.8995 1.6229 1.3478 0.0182  0.0008  0.0380  20  ARG B CG  
3105  C CD  . ARG B 20  ? 0.9860 1.7069 1.4362 0.0184  -0.0006 0.0362  20  ARG B CD  
3106  N NE  . ARG B 20  ? 1.0195 1.7283 1.4681 0.0184  -0.0013 0.0399  20  ARG B NE  
3107  C CZ  . ARG B 20  ? 1.0341 1.7395 1.4847 0.0185  -0.0029 0.0393  20  ARG B CZ  
3108  N NH1 . ARG B 20  ? 1.0251 1.7386 1.4800 0.0186  -0.0036 0.0352  20  ARG B NH1 
3109  N NH2 . ARG B 20  ? 1.0173 1.7115 1.4660 0.0185  -0.0039 0.0424  20  ARG B NH2 
3110  N N   . PHE B 21  ? 0.6953 1.4097 1.1404 0.0183  0.0041  0.0431  21  PHE B N   
3111  C CA  . PHE B 21  ? 0.6496 1.3607 1.0946 0.0186  0.0058  0.0469  21  PHE B CA  
3112  C C   . PHE B 21  ? 0.6566 1.3685 1.1033 0.0179  0.0064  0.0433  21  PHE B C   
3113  O O   . PHE B 21  ? 0.6801 1.3948 1.1289 0.0182  0.0077  0.0458  21  PHE B O   
3114  C CB  . PHE B 21  ? 0.6419 1.3631 1.0884 0.0193  0.0062  0.0522  21  PHE B CB  
3115  C CG  . PHE B 21  ? 0.6344 1.3537 1.0797 0.0196  0.0061  0.0568  21  PHE B CG  
3116  C CD1 . PHE B 21  ? 0.6541 1.3677 1.0989 0.0205  0.0071  0.0624  21  PHE B CD1 
3117  C CD2 . PHE B 21  ? 0.7145 1.4380 1.1599 0.0190  0.0051  0.0554  21  PHE B CD2 
3118  C CE1 . PHE B 21  ? 0.6873 1.3987 1.1314 0.0205  0.0070  0.0667  21  PHE B CE1 
3119  C CE2 . PHE B 21  ? 0.7771 1.4992 1.2223 0.0188  0.0052  0.0597  21  PHE B CE2 
3120  C CZ  . PHE B 21  ? 0.7638 1.4795 1.2082 0.0195  0.0060  0.0654  21  PHE B CZ  
3121  N N   . ARG B 22  ? 0.6388 1.3485 1.0856 0.0171  0.0054  0.0376  22  ARG B N   
3122  C CA  . ARG B 22  ? 0.6617 1.3736 1.1110 0.0158  0.0057  0.0333  22  ARG B CA  
3123  C C   . ARG B 22  ? 0.7212 1.4295 1.1719 0.0155  0.0081  0.0357  22  ARG B C   
3124  O O   . ARG B 22  ? 0.6835 1.4016 1.1386 0.0150  0.0082  0.0350  22  ARG B O   
3125  C CB  . ARG B 22  ? 0.5914 1.2945 1.0392 0.0151  0.0046  0.0280  22  ARG B CB  
3126  C CG  . ARG B 22  ? 0.5954 1.3035 1.0435 0.0157  0.0023  0.0244  22  ARG B CG  
3127  C CD  . ARG B 22  ? 0.5822 1.3065 1.0337 0.0153  0.0015  0.0217  22  ARG B CD  
3128  N NE  . ARG B 22  ? 0.5413 1.2677 0.9954 0.0141  0.0009  0.0160  22  ARG B NE  
3129  C CZ  . ARG B 22  ? 0.5074 1.2359 0.9627 0.0140  -0.0008 0.0097  22  ARG B CZ  
3130  N NH1 . ARG B 22  ? 0.5538 1.2834 1.0082 0.0152  -0.0018 0.0084  22  ARG B NH1 
3131  N NH2 . ARG B 22  ? 0.5464 1.2761 1.0043 0.0126  -0.0014 0.0045  22  ARG B NH2 
3132  N N   . PRO B 23  ? 0.7280 1.4229 1.1752 0.0158  0.0100  0.0381  23  PRO B N   
3133  C CA  . PRO B 23  ? 0.7305 1.4228 1.1797 0.0155  0.0130  0.0400  23  PRO B CA  
3134  C C   . PRO B 23  ? 0.7221 1.4258 1.1758 0.0166  0.0133  0.0437  23  PRO B C   
3135  O O   . PRO B 23  ? 0.7296 1.4391 1.1885 0.0161  0.0145  0.0432  23  PRO B O   
3136  C CB  . PRO B 23  ? 0.6222 1.2987 1.0654 0.0161  0.0149  0.0425  23  PRO B CB  
3137  C CG  . PRO B 23  ? 0.5911 1.2645 1.0305 0.0171  0.0124  0.0434  23  PRO B CG  
3138  C CD  . PRO B 23  ? 0.5967 1.2788 1.0383 0.0165  0.0096  0.0393  23  PRO B CD  
3139  N N   . LEU B 24  ? 0.6337 1.3406 1.0861 0.0182  0.0122  0.0477  24  LEU B N   
3140  C CA  . LEU B 24  ? 0.5985 1.3159 1.0545 0.0195  0.0119  0.0518  24  LEU B CA  
3141  C C   . LEU B 24  ? 0.6089 1.3414 1.0672 0.0192  0.0092  0.0502  24  LEU B C   
3142  O O   . LEU B 24  ? 0.6672 1.4101 1.1295 0.0198  0.0085  0.0520  24  LEU B O   
3143  C CB  . LEU B 24  ? 0.6006 1.3130 1.0539 0.0212  0.0122  0.0574  24  LEU B CB  
3144  C CG  . LEU B 24  ? 0.5898 1.2859 1.0384 0.0214  0.0141  0.0579  24  LEU B CG  
3145  C CD1 . LEU B 24  ? 0.6269 1.3183 1.0724 0.0225  0.0134  0.0620  24  LEU B CD1 
3146  C CD2 . LEU B 24  ? 0.5876 1.2784 1.0379 0.0221  0.0174  0.0590  24  LEU B CD2 
3147  N N   . SER B 25  ? 0.6025 1.3364 1.0583 0.0183  0.0076  0.0468  25  SER B N   
3148  C CA  . SER B 25  ? 0.5743 1.3224 1.0312 0.0180  0.0053  0.0446  25  SER B CA  
3149  C C   . SER B 25  ? 0.6203 1.3760 1.0816 0.0169  0.0045  0.0402  25  SER B C   
3150  O O   . SER B 25  ? 0.6912 1.4599 1.1538 0.0170  0.0026  0.0396  25  SER B O   
3151  C CB  . SER B 25  ? 0.6091 1.3564 1.0632 0.0174  0.0043  0.0409  25  SER B CB  
3152  O OG  . SER B 25  ? 0.6781 1.4269 1.1297 0.0182  0.0042  0.0451  25  SER B OG  
3153  N N   . PHE B 26  ? 0.6452 1.3927 1.1083 0.0156  0.0059  0.0371  26  PHE B N   
3154  C CA  . PHE B 26  ? 0.6820 1.4360 1.1502 0.0141  0.0052  0.0327  26  PHE B CA  
3155  C C   . PHE B 26  ? 0.7175 1.4811 1.1908 0.0150  0.0050  0.0359  26  PHE B C   
3156  O O   . PHE B 26  ? 0.6507 1.4254 1.1282 0.0142  0.0029  0.0328  26  PHE B O   
3157  C CB  . PHE B 26  ? 0.7030 1.4451 1.1720 0.0123  0.0074  0.0295  26  PHE B CB  
3158  C CG  . PHE B 26  ? 0.6439 1.3789 1.1095 0.0114  0.0065  0.0248  26  PHE B CG  
3159  C CD1 . PHE B 26  ? 0.6497 1.3696 1.1122 0.0107  0.0083  0.0243  26  PHE B CD1 
3160  C CD2 . PHE B 26  ? 0.6217 1.3652 1.0868 0.0114  0.0038  0.0208  26  PHE B CD2 
3161  C CE1 . PHE B 26  ? 0.6334 1.3465 1.0930 0.0102  0.0070  0.0202  26  PHE B CE1 
3162  C CE2 . PHE B 26  ? 0.5949 1.3321 1.0577 0.0110  0.0029  0.0162  26  PHE B CE2 
3163  C CZ  . PHE B 26  ? 0.5938 1.3156 1.0541 0.0105  0.0042  0.0160  26  PHE B CZ  
3164  N N   . ASN B 27  ? 0.8762 1.6356 1.3496 0.0167  0.0068  0.0419  27  ASN B N   
3165  C CA  . ASN B 27  ? 0.8612 1.6295 1.3400 0.0181  0.0062  0.0453  27  ASN B CA  
3166  C C   . ASN B 27  ? 0.8558 1.6336 1.3323 0.0201  0.0037  0.0498  27  ASN B C   
3167  O O   . ASN B 27  ? 0.8675 1.6580 1.3470 0.0206  0.0009  0.0499  27  ASN B O   
3168  C CB  . ASN B 27  ? 0.8672 1.6261 1.3480 0.0193  0.0097  0.0491  27  ASN B CB  
3169  C CG  . ASN B 27  ? 0.8764 1.6446 1.3643 0.0211  0.0092  0.0524  27  ASN B CG  
3170  O OD1 . ASN B 27  ? 0.8749 1.6497 1.3698 0.0201  0.0089  0.0494  27  ASN B OD1 
3171  N ND2 . ASN B 27  ? 0.8739 1.6425 1.3605 0.0239  0.0088  0.0584  27  ASN B ND2 
3172  N N   . THR B 28  ? 0.6769 1.4485 1.1478 0.0211  0.0043  0.0537  28  THR B N   
3173  C CA  . THR B 28  ? 0.6048 1.3837 1.0731 0.0227  0.0026  0.0590  28  THR B CA  
3174  C C   . THR B 28  ? 0.5904 1.3671 1.0526 0.0219  0.0025  0.0583  28  THR B C   
3175  O O   . THR B 28  ? 0.6140 1.3790 1.0738 0.0214  0.0043  0.0576  28  THR B O   
3176  C CB  . THR B 28  ? 0.6013 1.3747 1.0707 0.0251  0.0039  0.0659  28  THR B CB  
3177  O OG1 . THR B 28  ? 0.6743 1.4530 1.1503 0.0263  0.0035  0.0668  28  THR B OG1 
3178  C CG2 . THR B 28  ? 0.5155 1.2932 0.9810 0.0264  0.0024  0.0719  28  THR B CG2 
3179  N N   . PRO B 29  ? 0.5238 1.3116 0.9834 0.0217  0.0004  0.0582  29  PRO B N   
3180  C CA  . PRO B 29  ? 0.5094 1.2965 0.9642 0.0209  0.0008  0.0572  29  PRO B CA  
3181  C C   . PRO B 29  ? 0.6163 1.3945 1.0690 0.0216  0.0024  0.0632  29  PRO B C   
3182  O O   . PRO B 29  ? 0.4269 1.2013 0.8808 0.0230  0.0029  0.0689  29  PRO B O   
3183  C CB  . PRO B 29  ? 0.5329 1.3349 0.9852 0.0209  -0.0013 0.0575  29  PRO B CB  
3184  C CG  . PRO B 29  ? 0.5594 1.3693 1.0153 0.0212  -0.0034 0.0552  29  PRO B CG  
3185  C CD  . PRO B 29  ? 0.5843 1.3864 1.0450 0.0223  -0.0024 0.0583  29  PRO B CD  
3186  N N   . LYS B 30  ? 0.4389 1.2138 0.8889 0.0206  0.0031  0.0614  30  LYS B N   
3187  C CA  . LYS B 30  ? 0.4060 1.1721 0.8544 0.0207  0.0044  0.0660  30  LYS B CA  
3188  C C   . LYS B 30  ? 0.4256 1.1952 0.8731 0.0216  0.0044  0.0740  30  LYS B C   
3189  O O   . LYS B 30  ? 0.3901 1.1504 0.8384 0.0225  0.0053  0.0785  30  LYS B O   
3190  C CB  . LYS B 30  ? 0.4767 1.2430 0.9236 0.0194  0.0046  0.0625  30  LYS B CB  
3191  C CG  . LYS B 30  ? 0.5152 1.2740 0.9613 0.0191  0.0055  0.0667  30  LYS B CG  
3192  C CD  . LYS B 30  ? 0.5571 1.3246 1.0023 0.0179  0.0059  0.0667  30  LYS B CD  
3193  C CE  . LYS B 30  ? 0.6628 1.4225 1.1091 0.0171  0.0063  0.0647  30  LYS B CE  
3194  N NZ  . LYS B 30  ? 0.8199 1.5742 1.2670 0.0173  0.0053  0.0573  30  LYS B NZ  
3195  N N   . PRO B 31  ? 0.3525 1.1346 0.7982 0.0216  0.0035  0.0762  31  PRO B N   
3196  C CA  . PRO B 31  ? 0.3666 1.1504 0.8108 0.0224  0.0035  0.0846  31  PRO B CA  
3197  C C   . PRO B 31  ? 0.6399 1.4213 1.0868 0.0246  0.0027  0.0890  31  PRO B C   
3198  O O   . PRO B 31  ? 0.5003 1.2788 0.9468 0.0256  0.0028  0.0961  31  PRO B O   
3199  C CB  . PRO B 31  ? 0.3595 1.1579 0.8000 0.0218  0.0027  0.0851  31  PRO B CB  
3200  C CG  . PRO B 31  ? 0.3685 1.1710 0.8086 0.0204  0.0028  0.0766  31  PRO B CG  
3201  C CD  . PRO B 31  ? 0.3752 1.1698 0.8191 0.0208  0.0024  0.0714  31  PRO B CD  
3202  N N   . LEU B 32  ? 0.3556 1.1383 0.8057 0.0254  0.0018  0.0850  32  LEU B N   
3203  C CA  . LEU B 32  ? 0.3569 1.1394 0.8108 0.0277  0.0010  0.0885  32  LEU B CA  
3204  C C   . LEU B 32  ? 0.4018 1.1711 0.8591 0.0284  0.0031  0.0877  32  LEU B C   
3205  O O   . LEU B 32  ? 0.5012 1.2699 0.9627 0.0304  0.0030  0.0897  32  LEU B O   
3206  C CB  . LEU B 32  ? 0.4543 1.2485 0.9105 0.0280  -0.0013 0.0848  32  LEU B CB  
3207  C CG  . LEU B 32  ? 0.3647 1.1719 0.8164 0.0269  -0.0033 0.0831  32  LEU B CG  
3208  C CD1 . LEU B 32  ? 0.4353 1.2530 0.8898 0.0270  -0.0059 0.0784  32  LEU B CD1 
3209  C CD2 . LEU B 32  ? 0.3637 1.1758 0.8111 0.0278  -0.0041 0.0910  32  LEU B CD2 
3210  N N   . ILE B 33  ? 0.3804 1.1394 0.8358 0.0270  0.0049  0.0847  33  ILE B N   
3211  C CA  . ILE B 33  ? 0.4701 1.2159 0.9271 0.0276  0.0070  0.0837  33  ILE B CA  
3212  C C   . ILE B 33  ? 0.4662 1.2042 0.9231 0.0293  0.0078  0.0903  33  ILE B C   
3213  O O   . ILE B 33  ? 0.5036 1.2400 0.9577 0.0286  0.0075  0.0936  33  ILE B O   
3214  C CB  . ILE B 33  ? 0.4616 1.1988 0.9157 0.0257  0.0080  0.0784  33  ILE B CB  
3215  C CG1 . ILE B 33  ? 0.4367 1.1804 0.8916 0.0242  0.0073  0.0717  33  ILE B CG1 
3216  C CG2 . ILE B 33  ? 0.4737 1.1964 0.9276 0.0263  0.0102  0.0781  33  ILE B CG2 
3217  C CD1 . ILE B 33  ? 0.4565 1.1920 0.9088 0.0226  0.0078  0.0664  33  ILE B CD1 
3218  N N   . PRO B 34  ? 0.4460 1.1789 0.9062 0.0315  0.0089  0.0920  34  PRO B N   
3219  C CA  . PRO B 34  ? 0.5084 1.2349 0.9693 0.0336  0.0093  0.0983  34  PRO B CA  
3220  C C   . PRO B 34  ? 0.5915 1.3045 1.0487 0.0326  0.0106  0.0988  34  PRO B C   
3221  O O   . PRO B 34  ? 0.6096 1.3125 1.0654 0.0322  0.0124  0.0949  34  PRO B O   
3222  C CB  . PRO B 34  ? 0.5525 1.2770 1.0187 0.0361  0.0107  0.0982  34  PRO B CB  
3223  C CG  . PRO B 34  ? 0.5640 1.2983 1.0331 0.0352  0.0102  0.0932  34  PRO B CG  
3224  C CD  . PRO B 34  ? 0.5193 1.2533 0.9838 0.0321  0.0100  0.0882  34  PRO B CD  
3225  N N   . LEU B 35  ? 0.7296 1.4425 1.1851 0.0321  0.0096  0.1036  35  LEU B N   
3226  C CA  . LEU B 35  ? 0.7574 1.4580 1.2105 0.0312  0.0103  0.1049  35  LEU B CA  
3227  C C   . LEU B 35  ? 0.7662 1.4603 1.2214 0.0336  0.0106  0.1108  35  LEU B C   
3228  O O   . LEU B 35  ? 0.7558 1.4565 1.2125 0.0346  0.0094  0.1165  35  LEU B O   
3229  C CB  . LEU B 35  ? 0.7672 1.4720 1.2181 0.0285  0.0093  0.1059  35  LEU B CB  
3230  C CG  . LEU B 35  ? 0.7685 1.4775 1.2174 0.0262  0.0091  0.0996  35  LEU B CG  
3231  C CD1 . LEU B 35  ? 0.7937 1.5063 1.2416 0.0238  0.0086  0.1010  35  LEU B CD1 
3232  C CD2 . LEU B 35  ? 0.8139 1.5114 1.2613 0.0261  0.0099  0.0941  35  LEU B CD2 
3233  N N   . ALA B 36  ? 0.6855 1.3664 1.1403 0.0347  0.0122  0.1094  36  ALA B N   
3234  C CA  . ALA B 36  ? 0.6163 1.2894 1.0734 0.0374  0.0127  0.1141  36  ALA B CA  
3235  C C   . ALA B 36  ? 0.6344 1.3157 1.0965 0.0406  0.0124  0.1171  36  ALA B C   
3236  O O   . ALA B 36  ? 0.6729 1.3533 1.1375 0.0427  0.0115  0.1230  36  ALA B O   
3237  C CB  . ALA B 36  ? 0.5859 1.2552 1.0421 0.0362  0.0115  0.1195  36  ALA B CB  
3238  N N   . GLY B 37  ? 0.6145 1.3038 1.0785 0.0409  0.0128  0.1131  37  GLY B N   
3239  C CA  . GLY B 37  ? 0.5567 1.2548 1.0264 0.0438  0.0122  0.1148  37  GLY B CA  
3240  C C   . GLY B 37  ? 0.5984 1.3120 1.0687 0.0432  0.0093  0.1169  37  GLY B C   
3241  O O   . GLY B 37  ? 0.5323 1.2555 1.0070 0.0447  0.0084  0.1159  37  GLY B O   
3242  N N   . GLN B 38  ? 0.5496 1.2658 1.0156 0.0410  0.0078  0.1197  38  GLN B N   
3243  C CA  . GLN B 38  ? 0.5047 1.2350 0.9693 0.0401  0.0053  0.1219  38  GLN B CA  
3244  C C   . GLN B 38  ? 1.0054 1.7405 1.4660 0.0366  0.0055  0.1163  38  GLN B C   
3245  O O   . GLN B 38  ? 0.6623 1.3889 1.1204 0.0345  0.0071  0.1131  38  GLN B O   
3246  C CB  . GLN B 38  ? 0.5702 1.3005 1.0327 0.0402  0.0039  0.1299  38  GLN B CB  
3247  C CG  . GLN B 38  ? 0.5730 1.2969 1.0392 0.0438  0.0034  0.1360  38  GLN B CG  
3248  C CD  . GLN B 38  ? 0.4910 1.2237 0.9625 0.0474  0.0014  0.1370  38  GLN B CD  
3249  O OE1 . GLN B 38  ? 0.4714 1.2168 0.9425 0.0470  -0.0005 0.1351  38  GLN B OE1 
3250  N NE2 . GLN B 38  ? 0.5529 1.2789 1.0296 0.0512  0.0017  0.1397  38  GLN B NE2 
3251  N N   . PRO B 39  ? 0.3976 1.1462 0.8576 0.0359  0.0036  0.1147  39  PRO B N   
3252  C CA  . PRO B 39  ? 0.6390 1.3924 1.0956 0.0329  0.0038  0.1091  39  PRO B CA  
3253  C C   . PRO B 39  ? 0.3907 1.1407 0.8431 0.0305  0.0046  0.1109  39  PRO B C   
3254  O O   . PRO B 39  ? 0.7098 1.4556 1.1615 0.0308  0.0047  0.1173  39  PRO B O   
3255  C CB  . PRO B 39  ? 0.4078 1.1767 0.8641 0.0331  0.0012  0.1088  39  PRO B CB  
3256  C CG  . PRO B 39  ? 0.5333 1.3044 0.9949 0.0363  -0.0001 0.1111  39  PRO B CG  
3257  C CD  . PRO B 39  ? 0.5398 1.2994 1.0029 0.0383  0.0011  0.1170  39  PRO B CD  
3258  N N   . MET B 40  ? 0.4303 1.1821 0.8806 0.0280  0.0052  0.1051  40  MET B N   
3259  C CA  . MET B 40  ? 0.4895 1.2381 0.9373 0.0257  0.0061  0.1055  40  MET B CA  
3260  C C   . MET B 40  ? 0.4892 1.2457 0.9347 0.0250  0.0058  0.1120  40  MET B C   
3261  O O   . MET B 40  ? 0.5788 1.3292 1.0239 0.0241  0.0066  0.1170  40  MET B O   
3262  C CB  . MET B 40  ? 0.4616 1.2133 0.9083 0.0237  0.0064  0.0979  40  MET B CB  
3263  C CG  . MET B 40  ? 0.5185 1.2680 0.9639 0.0214  0.0073  0.0974  40  MET B CG  
3264  S SD  . MET B 40  ? 0.6131 1.3649 1.0583 0.0199  0.0072  0.0879  40  MET B SD  
3265  C CE  . MET B 40  ? 0.6093 1.3478 1.0557 0.0211  0.0072  0.0837  40  MET B CE  
3266  N N   . ILE B 41  ? 0.5566 1.3263 1.0000 0.0252  0.0045  0.1121  41  ILE B N   
3267  C CA  . ILE B 41  ? 0.4422 1.2199 0.8819 0.0244  0.0043  0.1185  41  ILE B CA  
3268  C C   . ILE B 41  ? 0.6339 1.4097 1.0741 0.0268  0.0030  0.1270  41  ILE B C   
3269  O O   . ILE B 41  ? 0.4908 1.2719 0.9273 0.0263  0.0027  0.1335  41  ILE B O   
3270  C CB  . ILE B 41  ? 0.3800 1.1727 0.8160 0.0239  0.0032  0.1152  41  ILE B CB  
3271  C CG1 . ILE B 41  ? 0.3983 1.1958 0.8363 0.0262  0.0006  0.1125  41  ILE B CG1 
3272  C CG2 . ILE B 41  ? 0.4939 1.2888 0.9293 0.0215  0.0047  0.1075  41  ILE B CG2 
3273  C CD1 . ILE B 41  ? 0.4346 1.2463 0.8691 0.0257  -0.0010 0.1085  41  ILE B CD1 
3274  N N   . HIS B 42  ? 0.5748 1.3430 1.0192 0.0294  0.0023  0.1272  42  HIS B N   
3275  C CA  . HIS B 42  ? 0.6061 1.3721 1.0520 0.0322  0.0008  0.1350  42  HIS B CA  
3276  C C   . HIS B 42  ? 0.6574 1.4136 1.1028 0.0313  0.0021  0.1417  42  HIS B C   
3277  O O   . HIS B 42  ? 0.7015 1.4561 1.1471 0.0332  0.0009  0.1493  42  HIS B O   
3278  C CB  . HIS B 42  ? 0.6178 1.3785 1.0694 0.0353  0.0003  0.1327  42  HIS B CB  
3279  C CG  . HIS B 42  ? 0.6619 1.4242 1.1161 0.0389  -0.0020 0.1392  42  HIS B CG  
3280  N ND1 . HIS B 42  ? 0.6741 1.4485 1.1289 0.0408  -0.0050 0.1395  42  HIS B ND1 
3281  C CD2 . HIS B 42  ? 0.6904 1.4436 1.1470 0.0412  -0.0021 0.1456  42  HIS B CD2 
3282  C CE1 . HIS B 42  ? 0.7473 1.5202 1.2050 0.0443  -0.0070 0.1460  42  HIS B CE1 
3283  N NE2 . HIS B 42  ? 0.7885 1.5484 1.2474 0.0447  -0.0051 0.1498  42  HIS B NE2 
3284  N N   . HIS B 43  ? 0.5411 1.2903 0.9862 0.0285  0.0043  0.1390  43  HIS B N   
3285  C CA  . HIS B 43  ? 0.6186 1.3584 1.0640 0.0271  0.0055  0.1448  43  HIS B CA  
3286  C C   . HIS B 43  ? 0.7028 1.4504 1.1442 0.0242  0.0063  0.1495  43  HIS B C   
3287  O O   . HIS B 43  ? 0.7578 1.5020 1.1986 0.0239  0.0064  0.1577  43  HIS B O   
3288  C CB  . HIS B 43  ? 0.5763 1.3045 1.0239 0.0255  0.0070  0.1397  43  HIS B CB  
3289  C CG  . HIS B 43  ? 0.5606 1.2808 1.0110 0.0281  0.0069  0.1348  43  HIS B CG  
3290  N ND1 . HIS B 43  ? 0.5787 1.3045 1.0293 0.0290  0.0065  0.1284  43  HIS B ND1 
3291  C CD2 . HIS B 43  ? 0.6193 1.3261 1.0721 0.0297  0.0073  0.1354  43  HIS B CD2 
3292  C CE1 . HIS B 43  ? 0.5599 1.2764 1.0129 0.0310  0.0071  0.1256  43  HIS B CE1 
3293  N NE2 . HIS B 43  ? 0.6148 1.3199 1.0689 0.0316  0.0076  0.1296  43  HIS B NE2 
3294  N N   . PRO B 44  ? 0.6005 1.3583 1.0391 0.0219  0.0072  0.1448  44  PRO B N   
3295  C CA  . PRO B 44  ? 0.6767 1.4437 1.1108 0.0193  0.0085  0.1496  44  PRO B CA  
3296  C C   . PRO B 44  ? 0.7370 1.5112 1.1668 0.0212  0.0066  0.1569  44  PRO B C   
3297  O O   . PRO B 44  ? 0.7784 1.5524 1.2054 0.0199  0.0074  0.1651  44  PRO B O   
3298  C CB  . PRO B 44  ? 0.6374 1.4144 1.0698 0.0175  0.0095  0.1414  44  PRO B CB  
3299  C CG  . PRO B 44  ? 0.5591 1.3276 0.9961 0.0178  0.0095  0.1337  44  PRO B CG  
3300  C CD  . PRO B 44  ? 0.5757 1.3354 1.0154 0.0210  0.0077  0.1351  44  PRO B CD  
3301  N N   . ILE B 45  ? 0.7576 1.5382 1.1868 0.0242  0.0039  0.1543  45  ILE B N   
3302  C CA  . ILE B 45  ? 0.7309 1.5188 1.1561 0.0265  0.0013  0.1610  45  ILE B CA  
3303  C C   . ILE B 45  ? 0.8797 1.6573 1.3074 0.0286  0.0002  0.1698  45  ILE B C   
3304  O O   . ILE B 45  ? 0.9250 1.7055 1.3483 0.0293  -0.0011 0.1783  45  ILE B O   
3305  C CB  . ILE B 45  ? 0.6044 1.4009 1.0302 0.0292  -0.0018 0.1555  45  ILE B CB  
3306  C CG1 . ILE B 45  ? 0.5198 1.3255 0.9432 0.0270  -0.0007 0.1465  45  ILE B CG1 
3307  C CG2 . ILE B 45  ? 0.8272 1.6320 1.2486 0.0317  -0.0053 0.1622  45  ILE B CG2 
3308  C CD1 . ILE B 45  ? 0.4942 1.3077 0.9191 0.0291  -0.0036 0.1403  45  ILE B CD1 
3309  N N   . SER B 46  ? 1.1902 1.9551 1.6243 0.0298  0.0007  0.1679  46  SER B N   
3310  C CA  . SER B 46  ? 1.2096 1.9636 1.6467 0.0321  -0.0002 0.1755  46  SER B CA  
3311  C C   . SER B 46  ? 1.2281 1.9773 1.6626 0.0290  0.0016  0.1833  46  SER B C   
3312  O O   . SER B 46  ? 1.2502 1.9940 1.6847 0.0306  0.0004  0.1920  46  SER B O   
3313  C CB  . SER B 46  ? 1.2017 1.9429 1.6455 0.0336  0.0005  0.1707  46  SER B CB  
3314  O OG  . SER B 46  ? 1.1954 1.9398 1.6426 0.0371  -0.0012 0.1660  46  SER B OG  
3315  N N   . ALA B 47  ? 0.9220 1.6731 1.3548 0.0246  0.0046  0.1805  47  ALA B N   
3316  C CA  . ALA B 47  ? 0.9019 1.6493 1.3330 0.0209  0.0069  0.1875  47  ALA B CA  
3317  C C   . ALA B 47  ? 0.8515 1.6105 1.2749 0.0196  0.0072  0.1941  47  ALA B C   
3318  O O   . ALA B 47  ? 0.8271 1.5830 1.2486 0.0169  0.0090  0.2020  47  ALA B O   
3319  C CB  . ALA B 47  ? 0.8325 1.5775 1.2663 0.0167  0.0101  0.1816  47  ALA B CB  
3320  N N   . CYS B 48  ? 0.8100 1.5819 1.2285 0.0212  0.0055  0.1912  48  CYS B N   
3321  C CA  . CYS B 48  ? 0.7798 1.5631 1.1895 0.0201  0.0057  0.1970  48  CYS B CA  
3322  C C   . CYS B 48  ? 0.7372 1.5179 1.1436 0.0229  0.0026  0.2078  48  CYS B C   
3323  O O   . CYS B 48  ? 0.7208 1.5067 1.1195 0.0212  0.0034  0.2155  48  CYS B O   
3324  C CB  . CYS B 48  ? 0.7887 1.5864 1.1940 0.0210  0.0044  0.1896  48  CYS B CB  
3325  S SG  . CYS B 48  ? 0.7712 1.5739 1.1788 0.0175  0.0080  0.1776  48  CYS B SG  
3326  N N   . LYS B 49  ? 0.7910 1.5639 1.2030 0.0273  -0.0008 0.2088  49  LYS B N   
3327  C CA  . LYS B 49  ? 0.8211 1.5913 1.2308 0.0307  -0.0042 0.2190  49  LYS B CA  
3328  C C   . LYS B 49  ? 0.7878 1.5466 1.1975 0.0284  -0.0022 0.2288  49  LYS B C   
3329  O O   . LYS B 49  ? 0.8069 1.5651 1.2117 0.0298  -0.0042 0.2390  49  LYS B O   
3330  C CB  . LYS B 49  ? 0.9129 1.6783 1.3300 0.0362  -0.0081 0.2167  49  LYS B CB  
3331  C CG  . LYS B 49  ? 0.9547 1.7202 1.3699 0.0407  -0.0127 0.2261  49  LYS B CG  
3332  C CD  . LYS B 49  ? 1.0379 1.8172 1.4422 0.0401  -0.0146 0.2302  49  LYS B CD  
3333  C CE  . LYS B 49  ? 1.1063 1.8840 1.5072 0.0439  -0.0191 0.2416  49  LYS B CE  
3334  N NZ  . LYS B 49  ? 1.2317 2.0240 1.6259 0.0466  -0.0239 0.2417  49  LYS B NZ  
3335  N N   . LYS B 50  ? 0.7421 1.4916 1.1570 0.0249  0.0015  0.2261  50  LYS B N   
3336  C CA  . LYS B 50  ? 0.7327 1.4711 1.1485 0.0222  0.0034  0.2349  50  LYS B CA  
3337  C C   . LYS B 50  ? 0.7734 1.5193 1.1808 0.0177  0.0064  0.2418  50  LYS B C   
3338  O O   . LYS B 50  ? 0.8301 1.5678 1.2370 0.0154  0.0078  0.2511  50  LYS B O   
3339  C CB  . LYS B 50  ? 0.7902 1.5175 1.2141 0.0195  0.0062  0.2293  50  LYS B CB  
3340  C CG  . LYS B 50  ? 0.9057 1.6390 1.3286 0.0137  0.0106  0.2250  50  LYS B CG  
3341  C CD  . LYS B 50  ? 0.9595 1.6802 1.3903 0.0106  0.0127  0.2223  50  LYS B CD  
3342  C CE  . LYS B 50  ? 0.8886 1.6158 1.3213 0.0069  0.0156  0.2130  50  LYS B CE  
3343  N NZ  . LYS B 50  ? 0.8300 1.5643 1.2623 0.0100  0.0139  0.2030  50  LYS B NZ  
3344  N N   . ILE B 51  ? 0.7533 1.5142 1.1540 0.0163  0.0075  0.2376  51  ILE B N   
3345  C CA  . ILE B 51  ? 0.7390 1.5086 1.1304 0.0123  0.0105  0.2440  51  ILE B CA  
3346  C C   . ILE B 51  ? 0.6968 1.4727 1.0789 0.0160  0.0064  0.2514  51  ILE B C   
3347  O O   . ILE B 51  ? 0.6519 1.4385 1.0302 0.0190  0.0035  0.2461  51  ILE B O   
3348  C CB  . ILE B 51  ? 0.7773 1.5598 1.1663 0.0089  0.0142  0.2350  51  ILE B CB  
3349  C CG1 . ILE B 51  ? 0.7697 1.5458 1.1685 0.0058  0.0175  0.2275  51  ILE B CG1 
3350  C CG2 . ILE B 51  ? 0.7600 1.5519 1.1389 0.0049  0.0180  0.2415  51  ILE B CG2 
3351  C CD1 . ILE B 51  ? 0.7284 1.5040 1.1333 0.0088  0.0152  0.2159  51  ILE B CD1 
3352  N N   . SER B 52  ? 0.6369 1.4056 1.0153 0.0158  0.0059  0.2638  52  SER B N   
3353  C CA  . SER B 52  ? 0.6824 1.4552 1.0523 0.0198  0.0012  0.2719  52  SER B CA  
3354  C C   . SER B 52  ? 0.6673 1.4560 1.0239 0.0179  0.0024  0.2728  52  SER B C   
3355  O O   . SER B 52  ? 0.6978 1.4942 1.0471 0.0219  -0.0025 0.2747  52  SER B O   
3356  C CB  . SER B 52  ? 0.7283 1.4880 1.0977 0.0200  0.0004  0.2854  52  SER B CB  
3357  O OG  . SER B 52  ? 0.7861 1.5437 1.1517 0.0136  0.0062  0.2915  52  SER B OG  
3358  N N   . ASN B 53  ? 0.6754 1.4696 1.0287 0.0121  0.0087  0.2710  53  ASN B N   
3359  C CA  . ASN B 53  ? 0.6838 1.4932 1.0242 0.0101  0.0106  0.2711  53  ASN B CA  
3360  C C   . ASN B 53  ? 0.6879 1.5097 1.0293 0.0105  0.0110  0.2571  53  ASN B C   
3361  O O   . ASN B 53  ? 0.7199 1.5542 1.0527 0.0078  0.0143  0.2544  53  ASN B O   
3362  C CB  . ASN B 53  ? 0.7096 1.5193 1.0454 0.0036  0.0178  0.2775  53  ASN B CB  
3363  C CG  . ASN B 53  ? 0.6819 1.4834 1.0302 -0.0006 0.0226  0.2731  53  ASN B CG  
3364  O OD1 . ASN B 53  ? 0.6761 1.4646 1.0351 0.0010  0.0204  0.2724  53  ASN B OD1 
3365  N ND2 . ASN B 53  ? 0.6765 1.4858 1.0237 -0.0060 0.0291  0.2697  53  ASN B ND2 
3366  N N   . LEU B 54  ? 0.8379 1.6563 1.1895 0.0137  0.0079  0.2481  54  LEU B N   
3367  C CA  . LEU B 54  ? 0.8157 1.6443 1.1690 0.0144  0.0076  0.2350  54  LEU B CA  
3368  C C   . LEU B 54  ? 0.8417 1.6786 1.1899 0.0194  0.0012  0.2333  54  LEU B C   
3369  O O   . LEU B 54  ? 0.9313 1.7626 1.2806 0.0235  -0.0039 0.2394  54  LEU B O   
3370  C CB  . LEU B 54  ? 0.7935 1.6136 1.1605 0.0147  0.0081  0.2260  54  LEU B CB  
3371  C CG  . LEU B 54  ? 0.7637 1.5918 1.1337 0.0135  0.0100  0.2127  54  LEU B CG  
3372  C CD1 . LEU B 54  ? 0.7365 1.5553 1.1170 0.0107  0.0136  0.2078  54  LEU B CD1 
3373  C CD2 . LEU B 54  ? 0.7757 1.6078 1.1480 0.0180  0.0048  0.2051  54  LEU B CD2 
3374  N N   . ALA B 55  ? 0.7108 1.5610 1.0539 0.0190  0.0012  0.2246  55  ALA B N   
3375  C CA  . ALA B 55  ? 0.6959 1.5554 1.0339 0.0232  -0.0049 0.2221  55  ALA B CA  
3376  C C   . ALA B 55  ? 0.7122 1.5774 1.0569 0.0243  -0.0062 0.2082  55  ALA B C   
3377  O O   . ALA B 55  ? 0.8821 1.7400 1.2380 0.0266  -0.0083 0.2039  55  ALA B O   
3378  C CB  . ALA B 55  ? 0.6992 1.5708 1.0212 0.0220  -0.0047 0.2265  55  ALA B CB  
3379  N N   . GLN B 56  ? 0.6412 1.5191 0.9788 0.0227  -0.0049 0.2011  56  GLN B N   
3380  C CA  . GLN B 56  ? 0.6012 1.4850 0.9440 0.0237  -0.0065 0.1881  56  GLN B CA  
3381  C C   . GLN B 56  ? 0.5671 1.4432 0.9213 0.0216  -0.0023 0.1806  56  GLN B C   
3382  O O   . GLN B 56  ? 0.5853 1.4565 0.9408 0.0182  0.0030  0.1830  56  GLN B O   
3383  C CB  . GLN B 56  ? 0.5318 1.4305 0.8637 0.0224  -0.0059 0.1823  56  GLN B CB  
3384  N N   . ILE B 57  ? 0.5960 1.4712 0.9586 0.0235  -0.0049 0.1715  57  ILE B N   
3385  C CA  . ILE B 57  ? 0.5642 1.4327 0.9366 0.0220  -0.0018 0.1633  57  ILE B CA  
3386  C C   . ILE B 57  ? 0.6672 1.5450 1.0399 0.0220  -0.0026 0.1511  57  ILE B C   
3387  O O   . ILE B 57  ? 0.6785 1.5632 1.0492 0.0244  -0.0072 0.1483  57  ILE B O   
3388  C CB  . ILE B 57  ? 0.5904 1.4460 0.9736 0.0243  -0.0036 0.1644  57  ILE B CB  
3389  C CG1 . ILE B 57  ? 0.7299 1.5764 1.1125 0.0249  -0.0037 0.1767  57  ILE B CG1 
3390  C CG2 . ILE B 57  ? 0.5585 1.4063 0.9502 0.0225  -0.0003 0.1568  57  ILE B CG2 
3391  C CD1 . ILE B 57  ? 0.9526 1.7848 1.3458 0.0264  -0.0038 0.1775  57  ILE B CD1 
3392  N N   . PHE B 58  ? 0.7568 1.6343 1.1324 0.0193  0.0017  0.1439  58  PHE B N   
3393  C CA  . PHE B 58  ? 0.7405 1.6266 1.1156 0.0188  0.0016  0.1325  58  PHE B CA  
3394  C C   . PHE B 58  ? 0.7146 1.5924 1.1001 0.0183  0.0030  0.1244  58  PHE B C   
3395  O O   . PHE B 58  ? 0.7383 1.6092 1.1277 0.0163  0.0069  0.1251  58  PHE B O   
3396  C CB  . PHE B 58  ? 0.7544 1.6507 1.1209 0.0162  0.0057  0.1311  58  PHE B CB  
3397  C CG  . PHE B 58  ? 0.8131 1.7193 1.1671 0.0167  0.0041  0.1372  58  PHE B CG  
3398  C CD1 . PHE B 58  ? 0.9262 1.8434 1.2740 0.0182  0.0004  0.1314  58  PHE B CD1 
3399  C CD2 . PHE B 58  ? 0.8327 1.7368 1.1808 0.0157  0.0059  0.1489  58  PHE B CD2 
3400  C CE1 . PHE B 58  ? 1.0109 1.9371 1.3461 0.0188  -0.0016 0.1370  58  PHE B CE1 
3401  C CE2 . PHE B 58  ? 0.8929 1.8056 1.2284 0.0162  0.0043  0.1550  58  PHE B CE2 
3402  C CZ  . PHE B 58  ? 0.9859 1.9098 1.3146 0.0179  0.0004  0.1491  58  PHE B CZ  
3403  N N   . LEU B 59  ? 0.6380 1.5161 1.0279 0.0201  -0.0003 0.1170  59  LEU B N   
3404  C CA  . LEU B 59  ? 0.6214 1.4927 1.0197 0.0196  0.0008  0.1085  59  LEU B CA  
3405  C C   . LEU B 59  ? 0.6391 1.5197 1.0352 0.0188  0.0010  0.0981  59  LEU B C   
3406  O O   . LEU B 59  ? 0.7102 1.5990 1.1035 0.0200  -0.0024 0.0944  59  LEU B O   
3407  C CB  . LEU B 59  ? 0.5724 1.4362 0.9780 0.0219  -0.0025 0.1077  59  LEU B CB  
3408  C CG  . LEU B 59  ? 0.5419 1.3979 0.9496 0.0237  -0.0037 0.1175  59  LEU B CG  
3409  C CD1 . LEU B 59  ? 0.5258 1.3769 0.9409 0.0262  -0.0067 0.1152  59  LEU B CD1 
3410  C CD2 . LEU B 59  ? 0.5012 1.3462 0.9114 0.0222  0.0000  0.1220  59  LEU B CD2 
3411  N N   . ILE B 60  ? 0.6030 1.4826 1.0009 0.0168  0.0048  0.0932  60  ILE B N   
3412  C CA  . ILE B 60  ? 0.5996 1.4875 0.9957 0.0161  0.0055  0.0832  60  ILE B CA  
3413  C C   . ILE B 60  ? 0.5941 1.4735 0.9988 0.0159  0.0060  0.0752  60  ILE B C   
3414  O O   . ILE B 60  ? 0.5025 1.3715 0.9125 0.0153  0.0078  0.0775  60  ILE B O   
3415  C CB  . ILE B 60  ? 0.6751 1.5718 1.0648 0.0142  0.0097  0.0839  60  ILE B CB  
3416  C CG1 . ILE B 60  ? 0.6772 1.5664 1.0717 0.0123  0.0140  0.0874  60  ILE B CG1 
3417  C CG2 . ILE B 60  ? 0.7760 1.6813 1.1554 0.0144  0.0090  0.0918  60  ILE B CG2 
3418  C CD1 . ILE B 60  ? 0.7603 1.6586 1.1501 0.0102  0.0188  0.0879  60  ILE B CD1 
3419  N N   . GLY B 61  ? 0.6223 1.5058 1.0279 0.0164  0.0041  0.0658  61  GLY B N   
3420  C CA  . GLY B 61  ? 0.6298 1.5055 1.0427 0.0163  0.0041  0.0579  61  GLY B CA  
3421  C C   . GLY B 61  ? 0.7213 1.6019 1.1345 0.0170  0.0010  0.0494  61  GLY B C   
3422  O O   . GLY B 61  ? 0.7360 1.6229 1.1461 0.0178  -0.0021 0.0510  61  GLY B O   
3423  N N   . PHE B 62  ? 0.7221 1.5998 1.1395 0.0167  0.0014  0.0405  62  PHE B N   
3424  C CA  . PHE B 62  ? 0.7721 1.6547 1.1898 0.0169  -0.0013 0.0317  62  PHE B CA  
3425  C C   . PHE B 62  ? 0.6889 1.5634 1.1128 0.0173  -0.0041 0.0307  62  PHE B C   
3426  O O   . PHE B 62  ? 0.6426 1.5158 1.0699 0.0169  -0.0057 0.0226  62  PHE B O   
3427  C CB  . PHE B 62  ? 0.8734 1.7570 1.2927 0.0165  0.0003  0.0221  62  PHE B CB  
3428  C CG  . PHE B 62  ? 0.8437 1.7150 1.2695 0.0163  0.0021  0.0209  62  PHE B CG  
3429  C CD1 . PHE B 62  ? 0.8321 1.7009 1.2581 0.0160  0.0053  0.0258  62  PHE B CD1 
3430  C CD2 . PHE B 62  ? 0.8108 1.6730 1.2422 0.0165  0.0005  0.0149  62  PHE B CD2 
3431  C CE1 . PHE B 62  ? 0.8587 1.7166 1.2906 0.0159  0.0063  0.0245  62  PHE B CE1 
3432  C CE2 . PHE B 62  ? 0.7863 1.6370 1.2227 0.0165  0.0017  0.0140  62  PHE B CE2 
3433  C CZ  . PHE B 62  ? 0.8466 1.6953 1.2831 0.0164  0.0044  0.0187  62  PHE B CZ  
3434  N N   . TYR B 63  ? 0.7128 1.5817 1.1383 0.0178  -0.0046 0.0389  63  TYR B N   
3435  C CA  . TYR B 63  ? 0.6902 1.5546 1.1209 0.0183  -0.0071 0.0387  63  TYR B CA  
3436  C C   . TYR B 63  ? 0.7123 1.5887 1.1407 0.0187  -0.0109 0.0371  63  TYR B C   
3437  O O   . TYR B 63  ? 0.7285 1.6159 1.1499 0.0188  -0.0116 0.0370  63  TYR B O   
3438  C CB  . TYR B 63  ? 0.6755 1.5312 1.1086 0.0192  -0.0064 0.0477  63  TYR B CB  
3439  C CG  . TYR B 63  ? 0.6577 1.4988 1.0958 0.0189  -0.0043 0.0472  63  TYR B CG  
3440  C CD1 . TYR B 63  ? 0.6892 1.5244 1.1315 0.0181  -0.0044 0.0397  63  TYR B CD1 
3441  C CD2 . TYR B 63  ? 0.6834 1.5161 1.1217 0.0193  -0.0023 0.0544  63  TYR B CD2 
3442  C CE1 . TYR B 63  ? 0.7516 1.5731 1.1971 0.0179  -0.0027 0.0397  63  TYR B CE1 
3443  C CE2 . TYR B 63  ? 0.7144 1.5337 1.1562 0.0190  -0.0007 0.0538  63  TYR B CE2 
3444  C CZ  . TYR B 63  ? 0.7229 1.5367 1.1679 0.0184  -0.0010 0.0466  63  TYR B CZ  
3445  O OH  . TYR B 63  ? 0.6426 1.4427 1.0899 0.0183  0.0004  0.0464  63  TYR B OH  
3446  N N   . GLU B 64  ? 0.6859 1.5604 1.1201 0.0189  -0.0134 0.0358  64  GLU B N   
3447  C CA  . GLU B 64  ? 0.6609 1.5465 1.0943 0.0194  -0.0176 0.0344  64  GLU B CA  
3448  C C   . GLU B 64  ? 0.7056 1.5937 1.1378 0.0213  -0.0192 0.0442  64  GLU B C   
3449  O O   . GLU B 64  ? 0.6807 1.5598 1.1176 0.0221  -0.0179 0.0498  64  GLU B O   
3450  C CB  . GLU B 64  ? 0.7104 1.5939 1.1519 0.0184  -0.0196 0.0275  64  GLU B CB  
3451  C CG  . GLU B 64  ? 0.6710 1.5535 1.1131 0.0167  -0.0191 0.0172  64  GLU B CG  
3452  C CD  . GLU B 64  ? 0.6632 1.5583 1.0980 0.0167  -0.0208 0.0122  64  GLU B CD  
3453  O OE1 . GLU B 64  ? 0.7217 1.6274 1.1516 0.0176  -0.0237 0.0153  64  GLU B OE1 
3454  O OE2 . GLU B 64  ? 0.5601 1.4540 0.9935 0.0159  -0.0193 0.0052  64  GLU B OE2 
3455  N N   . GLU B 65  ? 0.8215 1.7218 1.2471 0.0221  -0.0222 0.0462  65  GLU B N   
3456  C CA  . GLU B 65  ? 0.8674 1.7705 1.2908 0.0241  -0.0242 0.0559  65  GLU B CA  
3457  C C   . GLU B 65  ? 0.8224 1.7237 1.2549 0.0255  -0.0271 0.0575  65  GLU B C   
3458  O O   . GLU B 65  ? 0.8245 1.7239 1.2580 0.0275  -0.0278 0.0660  65  GLU B O   
3459  C CB  . GLU B 65  ? 0.9106 1.8273 1.3240 0.0247  -0.0273 0.0569  65  GLU B CB  
3460  C CG  . GLU B 65  ? 0.9256 1.8450 1.3348 0.0269  -0.0293 0.0680  65  GLU B CG  
3461  C CD  . GLU B 65  ? 0.9878 1.9198 1.3851 0.0273  -0.0320 0.0695  65  GLU B CD  
3462  O OE1 . GLU B 65  ? 1.0055 1.9443 1.3976 0.0259  -0.0318 0.0615  65  GLU B OE1 
3463  O OE2 . GLU B 65  ? 1.0029 1.9376 1.3956 0.0292  -0.0342 0.0786  65  GLU B OE2 
3464  N N   . ARG B 66  ? 0.7492 1.6511 1.1888 0.0243  -0.0286 0.0495  66  ARG B N   
3465  C CA  . ARG B 66  ? 0.7585 1.6599 1.2079 0.0253  -0.0309 0.0505  66  ARG B CA  
3466  C C   . ARG B 66  ? 0.7511 1.6397 1.2059 0.0263  -0.0273 0.0565  66  ARG B C   
3467  O O   . ARG B 66  ? 0.7743 1.6630 1.2347 0.0284  -0.0289 0.0615  66  ARG B O   
3468  C CB  . ARG B 66  ? 0.8188 1.7215 1.2754 0.0232  -0.0321 0.0405  66  ARG B CB  
3469  C CG  . ARG B 66  ? 0.8626 1.7764 1.3140 0.0219  -0.0354 0.0329  66  ARG B CG  
3470  C CD  . ARG B 66  ? 0.9238 1.8353 1.3819 0.0192  -0.0353 0.0226  66  ARG B CD  
3471  N NE  . ARG B 66  ? 0.9458 1.8443 1.4050 0.0179  -0.0301 0.0206  66  ARG B NE  
3472  C CZ  . ARG B 66  ? 1.0034 1.8964 1.4678 0.0156  -0.0290 0.0127  66  ARG B CZ  
3473  N NH1 . ARG B 66  ? 1.0319 1.9313 1.5017 0.0140  -0.0325 0.0059  66  ARG B NH1 
3474  N NH2 . ARG B 66  ? 1.0037 1.8846 1.4681 0.0147  -0.0247 0.0117  66  ARG B NH2 
3475  N N   . GLU B 67  ? 0.6925 1.5702 1.1457 0.0251  -0.0226 0.0560  67  GLU B N   
3476  C CA  . GLU B 67  ? 0.6508 1.5159 1.1080 0.0260  -0.0193 0.0613  67  GLU B CA  
3477  C C   . GLU B 67  ? 0.5628 1.4272 1.0154 0.0281  -0.0192 0.0712  67  GLU B C   
3478  O O   . GLU B 67  ? 0.5713 1.4297 1.0284 0.0300  -0.0186 0.0768  67  GLU B O   
3479  C CB  . GLU B 67  ? 0.6794 1.5332 1.1357 0.0240  -0.0150 0.0575  67  GLU B CB  
3480  C CG  . GLU B 67  ? 0.7789 1.6295 1.2409 0.0221  -0.0146 0.0489  67  GLU B CG  
3481  C CD  . GLU B 67  ? 0.7739 1.6138 1.2339 0.0205  -0.0112 0.0453  67  GLU B CD  
3482  O OE1 . GLU B 67  ? 0.6646 1.5073 1.1188 0.0199  -0.0108 0.0437  67  GLU B OE1 
3483  O OE2 . GLU B 67  ? 0.7939 1.6230 1.2583 0.0199  -0.0089 0.0441  67  GLU B OE2 
3484  N N   . PHE B 68  ? 0.6227 1.4932 1.0664 0.0278  -0.0195 0.0733  68  PHE B N   
3485  C CA  . PHE B 68  ? 0.6073 1.4761 1.0460 0.0293  -0.0190 0.0830  68  PHE B CA  
3486  C C   . PHE B 68  ? 0.6405 1.5184 1.0780 0.0318  -0.0235 0.0888  68  PHE B C   
3487  O O   . PHE B 68  ? 0.6078 1.4818 1.0445 0.0337  -0.0236 0.0976  68  PHE B O   
3488  C CB  . PHE B 68  ? 0.6104 1.4815 1.0402 0.0275  -0.0167 0.0832  68  PHE B CB  
3489  C CG  . PHE B 68  ? 0.5930 1.4538 1.0242 0.0256  -0.0123 0.0800  68  PHE B CG  
3490  C CD1 . PHE B 68  ? 0.5780 1.4306 1.0076 0.0254  -0.0092 0.0862  68  PHE B CD1 
3491  C CD2 . PHE B 68  ? 0.6087 1.4677 1.0432 0.0241  -0.0115 0.0707  68  PHE B CD2 
3492  C CE1 . PHE B 68  ? 0.5482 1.3917 0.9794 0.0238  -0.0058 0.0831  68  PHE B CE1 
3493  C CE2 . PHE B 68  ? 0.5762 1.4255 1.0119 0.0227  -0.0081 0.0679  68  PHE B CE2 
3494  C CZ  . PHE B 68  ? 0.5414 1.3834 0.9756 0.0226  -0.0054 0.0740  68  PHE B CZ  
3495  N N   . ALA B 69  ? 0.8136 1.7029 1.2512 0.0319  -0.0277 0.0840  69  ALA B N   
3496  C CA  . ALA B 69  ? 0.8380 1.7366 1.2742 0.0346  -0.0329 0.0892  69  ALA B CA  
3497  C C   . ALA B 69  ? 0.8314 1.7248 1.2771 0.0374  -0.0340 0.0943  69  ALA B C   
3498  O O   . ALA B 69  ? 0.8473 1.7421 1.2914 0.0401  -0.0364 0.1027  69  ALA B O   
3499  C CB  . ALA B 69  ? 0.8717 1.7832 1.3075 0.0340  -0.0376 0.0818  69  ALA B CB  
3500  N N   . LEU B 70  ? 0.6151 1.5022 1.0709 0.0368  -0.0320 0.0893  70  LEU B N   
3501  C CA  . LEU B 70  ? 0.6073 1.4896 1.0728 0.0395  -0.0322 0.0933  70  LEU B CA  
3502  C C   . LEU B 70  ? 0.6175 1.4873 1.0816 0.0408  -0.0286 0.1010  70  LEU B C   
3503  O O   . LEU B 70  ? 0.5646 1.4324 1.0330 0.0440  -0.0299 0.1074  70  LEU B O   
3504  C CB  . LEU B 70  ? 0.6530 1.5320 1.1289 0.0381  -0.0304 0.0857  70  LEU B CB  
3505  C CG  . LEU B 70  ? 0.6538 1.5447 1.1359 0.0375  -0.0346 0.0790  70  LEU B CG  
3506  C CD1 . LEU B 70  ? 0.5856 1.4838 1.0606 0.0346  -0.0361 0.0720  70  LEU B CD1 
3507  C CD2 . LEU B 70  ? 0.5699 1.4556 1.0639 0.0365  -0.0319 0.0741  70  LEU B CD2 
3508  N N   . TYR B 71  ? 0.6038 1.4652 1.0625 0.0384  -0.0242 0.1003  71  TYR B N   
3509  C CA  . TYR B 71  ? 0.6142 1.4632 1.0720 0.0392  -0.0208 0.1069  71  TYR B CA  
3510  C C   . TYR B 71  ? 0.6865 1.5380 1.1368 0.0405  -0.0224 0.1159  71  TYR B C   
3511  O O   . TYR B 71  ? 0.7371 1.5820 1.1894 0.0429  -0.0223 0.1233  71  TYR B O   
3512  C CB  . TYR B 71  ? 0.5635 1.4030 1.0190 0.0362  -0.0160 0.1027  71  TYR B CB  
3513  C CG  . TYR B 71  ? 0.6524 1.4798 1.1061 0.0364  -0.0129 0.1089  71  TYR B CG  
3514  C CD1 . TYR B 71  ? 0.7143 1.5326 1.1738 0.0389  -0.0120 0.1131  71  TYR B CD1 
3515  C CD2 . TYR B 71  ? 0.6451 1.4702 1.0918 0.0342  -0.0108 0.1103  71  TYR B CD2 
3516  C CE1 . TYR B 71  ? 0.7224 1.5291 1.1802 0.0390  -0.0095 0.1183  71  TYR B CE1 
3517  C CE2 . TYR B 71  ? 0.6342 1.4484 1.0800 0.0340  -0.0081 0.1157  71  TYR B CE2 
3518  C CZ  . TYR B 71  ? 0.6705 1.4753 1.1217 0.0364  -0.0077 0.1196  71  TYR B CZ  
3519  O OH  . TYR B 71  ? 0.6217 1.4151 1.0720 0.0362  -0.0054 0.1246  71  TYR B OH  
3520  N N   . VAL B 72  ? 0.6922 1.5529 1.1337 0.0389  -0.0237 0.1155  72  VAL B N   
3521  C CA  . VAL B 72  ? 0.6746 1.5381 1.1076 0.0397  -0.0249 0.1242  72  VAL B CA  
3522  C C   . VAL B 72  ? 0.7195 1.5871 1.1547 0.0436  -0.0298 0.1311  72  VAL B C   
3523  O O   . VAL B 72  ? 0.7929 1.6573 1.2243 0.0451  -0.0303 0.1404  72  VAL B O   
3524  C CB  . VAL B 72  ? 0.5997 1.4737 1.0227 0.0372  -0.0252 0.1212  72  VAL B CB  
3525  C CG1 . VAL B 72  ? 0.6883 1.5665 1.1015 0.0379  -0.0266 0.1306  72  VAL B CG1 
3526  C CG2 . VAL B 72  ? 0.6116 1.4804 1.0330 0.0338  -0.0201 0.1157  72  VAL B CG2 
3527  N N   . SER B 73  ? 0.6929 1.5675 1.1350 0.0453  -0.0336 0.1267  73  SER B N   
3528  C CA  . SER B 73  ? 0.6959 1.5755 1.1415 0.0495  -0.0389 0.1325  73  SER B CA  
3529  C C   . SER B 73  ? 0.7207 1.5888 1.1731 0.0524  -0.0374 0.1393  73  SER B C   
3530  O O   . SER B 73  ? 0.7560 1.6259 1.2091 0.0561  -0.0414 0.1469  73  SER B O   
3531  C CB  . SER B 73  ? 0.6305 1.5199 1.0843 0.0504  -0.0429 0.1254  73  SER B CB  
3532  O OG  . SER B 73  ? 0.5892 1.4892 1.0367 0.0478  -0.0447 0.1188  73  SER B OG  
3533  N N   . SER B 74  ? 0.7176 1.5736 1.1747 0.0511  -0.0322 0.1368  74  SER B N   
3534  C CA  . SER B 74  ? 0.7602 1.6049 1.2243 0.0540  -0.0306 0.1419  74  SER B CA  
3535  C C   . SER B 74  ? 0.8925 1.7266 1.3503 0.0535  -0.0280 0.1498  74  SER B C   
3536  O O   . SER B 74  ? 0.9389 1.7655 1.4005 0.0567  -0.0284 0.1564  74  SER B O   
3537  C CB  . SER B 74  ? 0.7657 1.6025 1.2384 0.0531  -0.0264 0.1348  74  SER B CB  
3538  O OG  . SER B 74  ? 0.7514 1.5975 1.2304 0.0529  -0.0283 0.1273  74  SER B OG  
3539  N N   . ILE B 75  ? 0.9866 1.8201 1.4357 0.0497  -0.0253 0.1490  75  ILE B N   
3540  C CA  . ILE B 75  ? 1.0455 1.8690 1.4897 0.0485  -0.0224 0.1560  75  ILE B CA  
3541  C C   . ILE B 75  ? 1.1083 1.9349 1.5469 0.0507  -0.0259 0.1664  75  ILE B C   
3542  O O   . ILE B 75  ? 1.1384 1.9555 1.5786 0.0525  -0.0256 0.1740  75  ILE B O   
3543  C CB  . ILE B 75  ? 1.0026 1.8257 1.4402 0.0438  -0.0185 0.1520  75  ILE B CB  
3544  C CG1 . ILE B 75  ? 0.9378 1.7614 1.3797 0.0419  -0.0166 0.1411  75  ILE B CG1 
3545  C CG2 . ILE B 75  ? 0.9273 1.7376 1.3639 0.0422  -0.0147 0.1570  75  ILE B CG2 
3546  C CD1 . ILE B 75  ? 0.9016 1.7274 1.3375 0.0378  -0.0137 0.1363  75  ILE B CD1 
3547  N N   . SER B 76  ? 1.3296 2.1693 1.7611 0.0504  -0.0293 0.1669  76  SER B N   
3548  C CA  . SER B 76  ? 1.3623 2.2055 1.7866 0.0523  -0.0329 0.1770  76  SER B CA  
3549  C C   . SER B 76  ? 1.3696 2.2104 1.8011 0.0577  -0.0373 0.1827  76  SER B C   
3550  O O   . SER B 76  ? 1.4051 2.2449 1.8318 0.0597  -0.0400 0.1926  76  SER B O   
3551  C CB  . SER B 76  ? 1.3729 2.2312 1.7877 0.0512  -0.0361 0.1751  76  SER B CB  
3552  O OG  . SER B 76  ? 1.3659 2.2265 1.7739 0.0466  -0.0317 0.1701  76  SER B OG  
3553  N N   . ASN B 77  ? 1.1374 1.9771 1.5804 0.0600  -0.0379 0.1770  77  ASN B N   
3554  C CA  . ASN B 77  ? 1.0954 1.9316 1.5474 0.0653  -0.0412 0.1817  77  ASN B CA  
3555  C C   . ASN B 77  ? 1.1404 1.9603 1.5959 0.0662  -0.0376 0.1870  77  ASN B C   
3556  O O   . ASN B 77  ? 1.1815 1.9970 1.6425 0.0708  -0.0403 0.1932  77  ASN B O   
3557  C CB  . ASN B 77  ? 1.0213 1.8626 1.4852 0.0671  -0.0423 0.1732  77  ASN B CB  
3558  C CG  . ASN B 77  ? 0.8797 1.7372 1.3416 0.0665  -0.0467 0.1678  77  ASN B CG  
3559  O OD1 . ASN B 77  ? 0.8239 1.6898 1.2770 0.0669  -0.0510 0.1723  77  ASN B OD1 
3560  N ND2 . ASN B 77  ? 0.8811 1.7426 1.3509 0.0653  -0.0455 0.1581  77  ASN B ND2 
3561  N N   . GLU B 78  ? 1.1143 1.9252 1.5673 0.0621  -0.0319 0.1844  78  GLU B N   
3562  C CA  . GLU B 78  ? 1.1109 1.9059 1.5671 0.0625  -0.0284 0.1883  78  GLU B CA  
3563  C C   . GLU B 78  ? 1.1748 1.9645 1.6221 0.0604  -0.0276 0.1976  78  GLU B C   
3564  O O   . GLU B 78  ? 1.1876 1.9693 1.6363 0.0633  -0.0291 0.2060  78  GLU B O   
3565  C CB  . GLU B 78  ? 1.0556 1.8431 1.5151 0.0593  -0.0230 0.1797  78  GLU B CB  
3566  C CG  . GLU B 78  ? 1.0773 1.8671 1.5461 0.0612  -0.0228 0.1713  78  GLU B CG  
3567  C CD  . GLU B 78  ? 1.0562 1.8365 1.5273 0.0584  -0.0175 0.1640  78  GLU B CD  
3568  O OE1 . GLU B 78  ? 1.0468 1.8196 1.5125 0.0550  -0.0146 0.1650  78  GLU B OE1 
3569  O OE2 . GLU B 78  ? 1.0320 1.8124 1.5103 0.0595  -0.0164 0.1575  78  GLU B OE2 
3570  N N   . LEU B 79  ? 1.1835 1.9772 1.6221 0.0556  -0.0251 0.1961  79  LEU B N   
3571  C CA  . LEU B 79  ? 1.2583 2.0471 1.6891 0.0527  -0.0232 0.2042  79  LEU B CA  
3572  C C   . LEU B 79  ? 1.3413 2.1408 1.7617 0.0526  -0.0264 0.2110  79  LEU B C   
3573  O O   . LEU B 79  ? 1.3400 2.1358 1.7534 0.0504  -0.0249 0.2190  79  LEU B O   
3574  C CB  . LEU B 79  ? 1.3062 2.0919 1.7344 0.0472  -0.0177 0.1988  79  LEU B CB  
3575  C CG  . LEU B 79  ? 1.2126 1.9844 1.6482 0.0463  -0.0141 0.1948  79  LEU B CG  
3576  C CD1 . LEU B 79  ? 1.2504 2.0090 1.6904 0.0492  -0.0148 0.2027  79  LEU B CD1 
3577  C CD2 . LEU B 79  ? 1.1208 1.8938 1.5632 0.0475  -0.0137 0.1845  79  LEU B CD2 
3578  N N   . LYS B 80  ? 1.3697 2.1822 1.7887 0.0549  -0.0308 0.2080  80  LYS B N   
3579  C CA  . LYS B 80  ? 1.4239 2.2472 1.8323 0.0554  -0.0347 0.2140  80  LYS B CA  
3580  C C   . LYS B 80  ? 1.5976 2.4255 1.9946 0.0499  -0.0307 0.2141  80  LYS B C   
3581  O O   . LYS B 80  ? 1.5730 2.3994 1.9611 0.0486  -0.0301 0.2234  80  LYS B O   
3582  C CB  . LYS B 80  ? 1.3021 2.1193 1.7092 0.0591  -0.0384 0.2264  80  LYS B CB  
3583  C CG  . LYS B 80  ? 1.2410 2.0540 1.6600 0.0651  -0.0425 0.2270  80  LYS B CG  
3584  C CD  . LYS B 80  ? 1.2824 2.0790 1.7106 0.0656  -0.0387 0.2277  80  LYS B CD  
3585  C CE  . LYS B 80  ? 1.2948 2.0804 1.7167 0.0628  -0.0357 0.2371  80  LYS B CE  
3586  N NZ  . LYS B 80  ? 1.2515 2.0213 1.6816 0.0622  -0.0316 0.2361  80  LYS B NZ  
3587  N N   . ILE B 81  ? 2.2103 3.0436 2.6078 0.0468  -0.0278 0.2036  81  ILE B N   
3588  C CA  . ILE B 81  ? 2.2147 3.0537 2.6027 0.0419  -0.0237 0.2019  81  ILE B CA  
3589  C C   . ILE B 81  ? 2.1990 3.0521 2.5837 0.0413  -0.0253 0.1923  81  ILE B C   
3590  O O   . ILE B 81  ? 2.1740 3.0283 2.5669 0.0423  -0.0261 0.1832  81  ILE B O   
3591  C CB  . ILE B 81  ? 2.2047 3.0337 2.5972 0.0381  -0.0174 0.1989  81  ILE B CB  
3592  C CG1 . ILE B 81  ? 2.1800 3.0010 2.5846 0.0397  -0.0171 0.1916  81  ILE B CG1 
3593  C CG2 . ILE B 81  ? 2.2303 3.0490 2.6205 0.0366  -0.0150 0.2096  81  ILE B CG2 
3594  C CD1 . ILE B 81  ? 2.1725 2.9822 2.5815 0.0364  -0.0119 0.1892  81  ILE B CD1 
3595  N N   . PRO B 82  ? 1.3475 2.2114 1.7201 0.0396  -0.0255 0.1938  82  PRO B N   
3596  C CA  . PRO B 82  ? 1.0739 1.9511 1.4428 0.0390  -0.0272 0.1842  82  PRO B CA  
3597  C C   . PRO B 82  ? 0.9447 1.8218 1.3170 0.0353  -0.0220 0.1737  82  PRO B C   
3598  O O   . PRO B 82  ? 0.8608 1.7405 1.2263 0.0317  -0.0175 0.1732  82  PRO B O   
3599  C CB  . PRO B 82  ? 0.9810 1.8680 1.3347 0.0380  -0.0282 0.1900  82  PRO B CB  
3600  C CG  . PRO B 82  ? 1.0115 1.8905 1.3620 0.0395  -0.0290 0.2037  82  PRO B CG  
3601  C CD  . PRO B 82  ? 1.2000 2.0642 1.5612 0.0385  -0.0249 0.2050  82  PRO B CD  
3602  N N   . VAL B 83  ? 0.8958 1.7699 1.2787 0.0362  -0.0226 0.1653  83  VAL B N   
3603  C CA  . VAL B 83  ? 0.7833 1.6565 1.1702 0.0333  -0.0185 0.1550  83  VAL B CA  
3604  C C   . VAL B 83  ? 0.6879 1.5736 1.0724 0.0332  -0.0210 0.1455  83  VAL B C   
3605  O O   . VAL B 83  ? 0.6962 1.5878 1.0822 0.0359  -0.0264 0.1444  83  VAL B O   
3606  C CB  . VAL B 83  ? 0.7477 1.6088 1.1469 0.0341  -0.0172 0.1517  83  VAL B CB  
3607  C CG1 . VAL B 83  ? 0.6266 1.4852 1.0287 0.0310  -0.0130 0.1424  83  VAL B CG1 
3608  C CG2 . VAL B 83  ? 0.9475 1.7962 1.3492 0.0348  -0.0157 0.1612  83  VAL B CG2 
3609  N N   . ARG B 84  ? 0.6304 1.5199 1.0117 0.0301  -0.0174 0.1383  84  ARG B N   
3610  C CA  . ARG B 84  ? 0.5947 1.4953 0.9733 0.0296  -0.0192 0.1285  84  ARG B CA  
3611  C C   . ARG B 84  ? 0.5590 1.4565 0.9425 0.0271  -0.0151 0.1188  84  ARG B C   
3612  O O   . ARG B 84  ? 0.6574 1.5493 1.0407 0.0249  -0.0101 0.1201  84  ARG B O   
3613  C CB  . ARG B 84  ? 0.6428 1.5554 1.0077 0.0288  -0.0198 0.1306  84  ARG B CB  
3614  C CG  . ARG B 84  ? 0.6539 1.5782 1.0153 0.0283  -0.0219 0.1199  84  ARG B CG  
3615  C CD  . ARG B 84  ? 0.7224 1.6583 1.0690 0.0276  -0.0220 0.1218  84  ARG B CD  
3616  N NE  . ARG B 84  ? 0.7918 1.7315 1.1315 0.0301  -0.0271 0.1311  84  ARG B NE  
3617  C CZ  . ARG B 84  ? 0.8270 1.7750 1.1647 0.0324  -0.0339 0.1287  84  ARG B CZ  
3618  N NH1 . ARG B 84  ? 0.8253 1.7787 1.1678 0.0323  -0.0361 0.1172  84  ARG B NH1 
3619  N NH2 . ARG B 84  ? 0.8389 1.7898 1.1702 0.0350  -0.0387 0.1380  84  ARG B NH2 
3620  N N   . TYR B 85  ? 0.5754 1.4764 0.9636 0.0273  -0.0172 0.1091  85  TYR B N   
3621  C CA  . TYR B 85  ? 0.6535 1.5519 1.0459 0.0253  -0.0141 0.0993  85  TYR B CA  
3622  C C   . TYR B 85  ? 0.7215 1.6319 1.1064 0.0240  -0.0141 0.0919  85  TYR B C   
3623  O O   . TYR B 85  ? 0.7488 1.6690 1.1294 0.0251  -0.0185 0.0899  85  TYR B O   
3624  C CB  . TYR B 85  ? 0.6742 1.5668 1.0772 0.0261  -0.0158 0.0931  85  TYR B CB  
3625  C CG  . TYR B 85  ? 0.6519 1.5417 1.0586 0.0241  -0.0132 0.0830  85  TYR B CG  
3626  C CD1 . TYR B 85  ? 0.6182 1.4974 1.0285 0.0228  -0.0090 0.0830  85  TYR B CD1 
3627  C CD2 . TYR B 85  ? 0.6802 1.5776 1.0868 0.0236  -0.0153 0.0735  85  TYR B CD2 
3628  C CE1 . TYR B 85  ? 0.6018 1.4781 1.0153 0.0213  -0.0070 0.0741  85  TYR B CE1 
3629  C CE2 . TYR B 85  ? 0.6367 1.5308 1.0467 0.0220  -0.0131 0.0645  85  TYR B CE2 
3630  C CZ  . TYR B 85  ? 0.6248 1.5083 1.0382 0.0210  -0.0090 0.0651  85  TYR B CZ  
3631  O OH  . TYR B 85  ? 0.6109 1.4908 1.0277 0.0198  -0.0073 0.0564  85  TYR B OH  
3632  N N   . LEU B 86  ? 0.9514 1.8611 1.3351 0.0218  -0.0095 0.0876  86  LEU B N   
3633  C CA  . LEU B 86  ? 0.9612 1.8813 1.3387 0.0207  -0.0087 0.0795  86  LEU B CA  
3634  C C   . LEU B 86  ? 0.9543 1.8697 1.3391 0.0195  -0.0065 0.0693  86  LEU B C   
3635  O O   . LEU B 86  ? 0.9471 1.8537 1.3370 0.0185  -0.0028 0.0702  86  LEU B O   
3636  C CB  . LEU B 86  ? 0.9801 1.9061 1.3477 0.0192  -0.0047 0.0843  86  LEU B CB  
3637  C CG  . LEU B 86  ? 1.0444 1.9743 1.4033 0.0201  -0.0063 0.0955  86  LEU B CG  
3638  C CD1 . LEU B 86  ? 1.0709 2.0063 1.4202 0.0181  -0.0013 0.0997  86  LEU B CD1 
3639  C CD2 . LEU B 86  ? 1.0902 2.0294 1.4437 0.0221  -0.0125 0.0938  86  LEU B CD2 
3640  N N   . LYS B 87  ? 0.8694 1.7903 1.2550 0.0197  -0.0092 0.0597  87  LYS B N   
3641  C CA  . LYS B 87  ? 0.8922 1.8087 1.2843 0.0188  -0.0076 0.0496  87  LYS B CA  
3642  C C   . LYS B 87  ? 1.0589 1.9835 1.4450 0.0178  -0.0045 0.0437  87  LYS B C   
3643  O O   . LYS B 87  ? 1.1840 2.1195 1.5633 0.0179  -0.0063 0.0389  87  LYS B O   
3644  C CB  . LYS B 87  ? 0.8452 1.7622 1.2426 0.0193  -0.0120 0.0421  87  LYS B CB  
3645  C CG  . LYS B 87  ? 0.8884 1.8026 1.2904 0.0183  -0.0107 0.0310  87  LYS B CG  
3646  C CD  . LYS B 87  ? 0.8674 1.7819 1.2749 0.0183  -0.0148 0.0235  87  LYS B CD  
3647  C CE  . LYS B 87  ? 0.9259 1.8392 1.3360 0.0173  -0.0137 0.0122  87  LYS B CE  
3648  N NZ  . LYS B 87  ? 0.9030 1.8063 1.3169 0.0170  -0.0094 0.0124  87  LYS B NZ  
3649  N N   . GLU B 88  ? 1.0585 1.9782 1.4472 0.0168  0.0002  0.0438  88  GLU B N   
3650  C CA  . GLU B 88  ? 1.2439 2.1708 1.6290 0.0159  0.0038  0.0374  88  GLU B CA  
3651  C C   . GLU B 88  ? 1.4014 2.3286 1.7907 0.0163  0.0021  0.0249  88  GLU B C   
3652  O O   . GLU B 88  ? 1.3189 2.2362 1.7170 0.0163  0.0023  0.0210  88  GLU B O   
3653  C CB  . GLU B 88  ? 1.2114 2.1326 1.6003 0.0148  0.0089  0.0407  88  GLU B CB  
3654  C CG  . GLU B 88  ? 1.1232 2.0300 1.5225 0.0149  0.0086  0.0413  88  GLU B CG  
3655  C CD  . GLU B 88  ? 1.2224 2.1247 1.6260 0.0138  0.0130  0.0424  88  GLU B CD  
3656  O OE1 . GLU B 88  ? 1.3532 2.2643 1.7535 0.0130  0.0166  0.0404  88  GLU B OE1 
3657  O OE2 . GLU B 88  ? 1.1159 2.0064 1.5264 0.0138  0.0128  0.0450  88  GLU B OE2 
3658  N N   . ASP B 89  ? 1.8905 2.8286 2.2733 0.0166  0.0001  0.0189  89  ASP B N   
3659  C CA  . ASP B 89  ? 1.8873 2.8258 2.2738 0.0169  -0.0018 0.0067  89  ASP B CA  
3660  C C   . ASP B 89  ? 1.8789 2.8146 2.2699 0.0167  0.0023  0.0000  89  ASP B C   
3661  O O   . ASP B 89  ? 1.8697 2.7984 2.2683 0.0169  0.0012  -0.0075 89  ASP B O   
3662  C CB  . ASP B 89  ? 1.9306 2.8820 2.3081 0.0172  -0.0046 0.0014  89  ASP B CB  
3663  C CG  . ASP B 89  ? 1.9471 2.9037 2.3180 0.0176  -0.0083 0.0097  89  ASP B CG  
3664  O OD1 . ASP B 89  ? 1.9737 2.9373 2.3349 0.0176  -0.0064 0.0163  89  ASP B OD1 
3665  O OD2 . ASP B 89  ? 1.9117 2.8653 2.2874 0.0180  -0.0131 0.0098  89  ASP B OD2 
3666  N N   . LYS B 90  ? 1.7143 2.6555 2.1009 0.0163  0.0071  0.0028  90  LYS B N   
3667  C CA  . LYS B 90  ? 1.7365 2.6759 2.1285 0.0163  0.0113  -0.0026 90  LYS B CA  
3668  C C   . LYS B 90  ? 1.7277 2.6588 2.1249 0.0155  0.0142  0.0061  90  LYS B C   
3669  O O   . LYS B 90  ? 1.7324 2.6687 2.1249 0.0146  0.0178  0.0131  90  LYS B O   
3670  C CB  . LYS B 90  ? 1.7984 2.7512 2.1828 0.0163  0.0152  -0.0072 90  LYS B CB  
3671  N N   . PRO B 91  ? 1.6789 2.5970 2.0852 0.0158  0.0128  0.0061  91  PRO B N   
3672  C CA  . PRO B 91  ? 1.6445 2.5542 2.0554 0.0150  0.0150  0.0141  91  PRO B CA  
3673  C C   . PRO B 91  ? 1.8010 2.7138 2.2153 0.0146  0.0196  0.0114  91  PRO B C   
3674  O O   . PRO B 91  ? 1.8233 2.7359 2.2425 0.0156  0.0199  0.0022  91  PRO B O   
3675  C CB  . PRO B 91  ? 1.4206 2.3160 1.8394 0.0156  0.0118  0.0128  91  PRO B CB  
3676  C CG  . PRO B 91  ? 1.3748 2.2717 1.7923 0.0163  0.0078  0.0067  91  PRO B CG  
3677  C CD  . PRO B 91  ? 1.5502 2.4601 1.9623 0.0165  0.0088  -0.0005 91  PRO B CD  
3678  N N   . HIS B 92  ? 2.1833 3.0992 2.5955 0.0132  0.0232  0.0196  92  HIS B N   
3679  C CA  . HIS B 92  ? 2.1833 3.1031 2.5996 0.0125  0.0280  0.0181  92  HIS B CA  
3680  C C   . HIS B 92  ? 2.1772 3.0875 2.5998 0.0112  0.0290  0.0259  92  HIS B C   
3681  O O   . HIS B 92  ? 2.1829 3.0980 2.6052 0.0094  0.0332  0.0313  92  HIS B O   
3682  C CB  . HIS B 92  ? 2.1985 3.1331 2.6062 0.0114  0.0324  0.0196  92  HIS B CB  
3683  C CG  . HIS B 92  ? 2.2117 3.1559 2.6112 0.0125  0.0311  0.0129  92  HIS B CG  
3684  N ND1 . HIS B 92  ? 2.2289 3.1820 2.6166 0.0119  0.0313  0.0179  92  HIS B ND1 
3685  C CD2 . HIS B 92  ? 2.2124 3.1585 2.6134 0.0142  0.0292  0.0015  92  HIS B CD2 
3686  C CE1 . HIS B 92  ? 2.2349 3.1952 2.6171 0.0131  0.0294  0.0095  92  HIS B CE1 
3687  N NE2 . HIS B 92  ? 2.2281 3.1842 2.6184 0.0144  0.0282  -0.0006 92  HIS B NE2 
3688  N N   . GLY B 93  ? 1.6841 2.5809 2.1123 0.0120  0.0253  0.0263  93  GLY B N   
3689  C CA  . GLY B 93  ? 1.4546 2.3413 1.8885 0.0109  0.0256  0.0330  93  GLY B CA  
3690  C C   . GLY B 93  ? 1.2393 2.1262 1.6684 0.0093  0.0268  0.0444  93  GLY B C   
3691  O O   . GLY B 93  ? 1.2102 2.0927 1.6354 0.0098  0.0239  0.0491  93  GLY B O   
3692  N N   . SER B 94  ? 1.1711 2.0630 1.6009 0.0072  0.0310  0.0490  94  SER B N   
3693  C CA  . SER B 94  ? 1.0217 1.9130 1.4474 0.0054  0.0324  0.0604  94  SER B CA  
3694  C C   . SER B 94  ? 1.0502 1.9554 1.4685 0.0037  0.0370  0.0634  94  SER B C   
3695  O O   . SER B 94  ? 1.0007 1.9097 1.4101 0.0037  0.0363  0.0693  94  SER B O   
3696  C CB  . SER B 94  ? 0.9470 1.8283 1.3806 0.0038  0.0332  0.0651  94  SER B CB  
3697  O OG  . SER B 94  ? 0.9707 1.8387 1.4097 0.0054  0.0290  0.0627  94  SER B OG  
3698  N N   . ALA B 95  ? 1.0929 2.0062 1.5148 0.0024  0.0416  0.0595  95  ALA B N   
3699  C CA  . ALA B 95  ? 1.0587 1.9850 1.4736 0.0004  0.0469  0.0630  95  ALA B CA  
3700  C C   . ALA B 95  ? 1.0891 2.0256 1.4929 0.0019  0.0463  0.0591  95  ALA B C   
3701  O O   . ALA B 95  ? 1.0416 1.9837 1.4350 0.0010  0.0473  0.0661  95  ALA B O   
3702  C CB  . ALA B 95  ? 1.0762 2.0095 1.4988 -0.0011 0.0522  0.0583  95  ALA B CB  
3703  N N   . GLY B 96  ? 1.2500 2.1888 1.6556 0.0042  0.0443  0.0480  96  GLY B N   
3704  C CA  . GLY B 96  ? 1.3483 2.2961 1.7439 0.0057  0.0430  0.0432  96  GLY B CA  
3705  C C   . GLY B 96  ? 1.2815 2.2245 1.6708 0.0068  0.0374  0.0478  96  GLY B C   
3706  O O   . GLY B 96  ? 1.2011 2.1524 1.5801 0.0075  0.0363  0.0469  96  GLY B O   
3707  N N   . ALA B 97  ? 1.3355 2.2655 1.7308 0.0072  0.0338  0.0522  97  ALA B N   
3708  C CA  . ALA B 97  ? 1.3194 2.2448 1.7104 0.0085  0.0287  0.0566  97  ALA B CA  
3709  C C   . ALA B 97  ? 1.2728 2.2035 1.6536 0.0075  0.0295  0.0671  97  ALA B C   
3710  O O   . ALA B 97  ? 1.3480 2.2835 1.7209 0.0087  0.0261  0.0679  97  ALA B O   
3711  C CB  . ALA B 97  ? 1.3321 2.2425 1.7318 0.0090  0.0257  0.0594  97  ALA B CB  
3712  N N   . LEU B 98  ? 0.9779 1.9078 1.3591 0.0052  0.0337  0.0753  98  LEU B N   
3713  C CA  . LEU B 98  ? 0.9198 1.8530 1.2913 0.0042  0.0345  0.0863  98  LEU B CA  
3714  C C   . LEU B 98  ? 0.9046 1.8523 1.2655 0.0029  0.0388  0.0858  98  LEU B C   
3715  O O   . LEU B 98  ? 0.8906 1.8429 1.2404 0.0028  0.0382  0.0932  98  LEU B O   
3716  C CB  . LEU B 98  ? 0.8093 1.7336 1.1860 0.0021  0.0367  0.0964  98  LEU B CB  
3717  C CG  . LEU B 98  ? 0.8112 1.7394 1.1911 -0.0011 0.0434  0.0976  98  LEU B CG  
3718  C CD1 . LEU B 98  ? 0.7370 1.6618 1.1141 -0.0036 0.0458  0.1107  98  LEU B CD1 
3719  C CD2 . LEU B 98  ? 0.8585 1.7796 1.2519 -0.0013 0.0439  0.0911  98  LEU B CD2 
3720  N N   . TYR B 99  ? 0.9042 1.8591 1.2678 0.0022  0.0432  0.0773  99  TYR B N   
3721  C CA  . TYR B 99  ? 0.8271 1.7964 1.1798 0.0014  0.0473  0.0751  99  TYR B CA  
3722  C C   . TYR B 99  ? 0.9067 1.8820 1.2499 0.0039  0.0425  0.0697  99  TYR B C   
3723  O O   . TYR B 99  ? 0.9089 1.8935 1.2387 0.0037  0.0433  0.0730  99  TYR B O   
3724  C CB  . TYR B 99  ? 0.8495 1.8253 1.2088 0.0006  0.0529  0.0659  99  TYR B CB  
3725  C CG  . TYR B 99  ? 0.8489 1.8398 1.1970 0.0002  0.0574  0.0618  99  TYR B CG  
3726  C CD1 . TYR B 99  ? 0.8636 1.8615 1.2005 -0.0021 0.0618  0.0710  99  TYR B CD1 
3727  C CD2 . TYR B 99  ? 0.8943 1.8921 1.2425 0.0022  0.0572  0.0487  99  TYR B CD2 
3728  C CE1 . TYR B 99  ? 0.8976 1.9094 1.2229 -0.0025 0.0662  0.0673  99  TYR B CE1 
3729  C CE2 . TYR B 99  ? 0.8836 1.8953 1.2210 0.0020  0.0615  0.0444  99  TYR B CE2 
3730  C CZ  . TYR B 99  ? 0.8906 1.9094 1.2162 -0.0004 0.0661  0.0537  99  TYR B CZ  
3731  O OH  . TYR B 99  ? 0.8772 1.9098 1.1908 -0.0006 0.0707  0.0494  99  TYR B OH  
3732  N N   . TYR B 100 ? 0.9590 1.9293 1.3088 0.0062  0.0375  0.0612  100 TYR B N   
3733  C CA  . TYR B 100 ? 0.9701 1.9433 1.3132 0.0084  0.0315  0.0576  100 TYR B CA  
3734  C C   . TYR B 100 ? 0.9589 1.9293 1.2952 0.0086  0.0278  0.0694  100 TYR B C   
3735  O O   . TYR B 100 ? 0.9430 1.9034 1.2850 0.0081  0.0274  0.0779  100 TYR B O   
3736  C CB  . TYR B 100 ? 1.0840 2.0490 1.4377 0.0102  0.0268  0.0489  100 TYR B CB  
3737  C CG  . TYR B 100 ? 1.1237 2.0940 1.4729 0.0120  0.0218  0.0406  100 TYR B CG  
3738  C CD1 . TYR B 100 ? 1.2017 2.1659 1.5599 0.0133  0.0183  0.0315  100 TYR B CD1 
3739  C CD2 . TYR B 100 ? 1.1193 2.1001 1.4550 0.0124  0.0202  0.0420  100 TYR B CD2 
3740  C CE1 . TYR B 100 ? 1.2329 2.2015 1.5878 0.0146  0.0136  0.0237  100 TYR B CE1 
3741  C CE2 . TYR B 100 ? 1.1247 2.1104 1.4568 0.0139  0.0151  0.0341  100 TYR B CE2 
3742  C CZ  . TYR B 100 ? 1.1591 2.1388 1.5014 0.0149  0.0119  0.0248  100 TYR B CZ  
3743  O OH  . TYR B 100 ? 1.1679 2.1522 1.5074 0.0160  0.0067  0.0167  100 TYR B OH  
3744  N N   . PHE B 101 ? 1.0234 2.0026 1.3474 0.0096  0.0249  0.0696  101 PHE B N   
3745  C CA  . PHE B 101 ? 1.0560 2.0349 1.3715 0.0103  0.0211  0.0806  101 PHE B CA  
3746  C C   . PHE B 101 ? 1.0306 2.0039 1.3460 0.0083  0.0250  0.0936  101 PHE B C   
3747  O O   . PHE B 101 ? 1.0264 1.9907 1.3451 0.0090  0.0219  0.1022  101 PHE B O   
3748  C CB  . PHE B 101 ? 1.0760 2.0481 1.3974 0.0127  0.0134  0.0801  101 PHE B CB  
3749  C CG  . PHE B 101 ? 1.0787 2.0386 1.4155 0.0129  0.0130  0.0769  101 PHE B CG  
3750  C CD1 . PHE B 101 ? 1.0705 2.0295 1.4146 0.0136  0.0115  0.0648  101 PHE B CD1 
3751  C CD2 . PHE B 101 ? 1.0817 2.0305 1.4252 0.0124  0.0138  0.0859  101 PHE B CD2 
3752  C CE1 . PHE B 101 ? 1.0239 1.9713 1.3809 0.0138  0.0111  0.0623  101 PHE B CE1 
3753  C CE2 . PHE B 101 ? 1.0243 1.9618 1.3807 0.0127  0.0133  0.0829  101 PHE B CE2 
3754  C CZ  . PHE B 101 ? 0.9877 1.9245 1.3504 0.0134  0.0120  0.0713  101 PHE B CZ  
3755  N N   . ARG B 102 ? 0.8855 1.8644 1.1974 0.0058  0.0323  0.0947  102 ARG B N   
3756  C CA  . ARG B 102 ? 0.8385 1.8141 1.1480 0.0033  0.0364  0.1073  102 ARG B CA  
3757  C C   . ARG B 102 ? 0.8432 1.8229 1.1377 0.0038  0.0341  0.1175  102 ARG B C   
3758  O O   . ARG B 102 ? 0.8063 1.7804 1.0991 0.0024  0.0354  0.1297  102 ARG B O   
3759  C CB  . ARG B 102 ? 0.8354 1.8176 1.1453 0.0002  0.0451  0.1053  102 ARG B CB  
3760  C CG  . ARG B 102 ? 0.8238 1.8207 1.1208 0.0001  0.0482  0.0995  102 ARG B CG  
3761  C CD  . ARG B 102 ? 0.7994 1.8030 1.0954 -0.0033 0.0576  0.1009  102 ARG B CD  
3762  N NE  . ARG B 102 ? 0.7978 1.7989 1.0875 -0.0059 0.0604  0.1155  102 ARG B NE  
3763  C CZ  . ARG B 102 ? 0.7925 1.7991 1.0795 -0.0095 0.0687  0.1202  102 ARG B CZ  
3764  N NH1 . ARG B 102 ? 0.8515 1.8669 1.1422 -0.0107 0.0751  0.1110  102 ARG B NH1 
3765  N NH2 . ARG B 102 ? 0.7592 1.7621 1.0404 -0.0120 0.0708  0.1341  102 ARG B NH2 
3766  N N   . ASP B 103 ? 0.9582 1.9473 1.2417 0.0057  0.0304  0.1126  103 ASP B N   
3767  C CA  . ASP B 103 ? 0.9874 1.9808 1.2557 0.0066  0.0271  0.1217  103 ASP B CA  
3768  C C   . ASP B 103 ? 0.9908 1.9743 1.2636 0.0089  0.0199  0.1296  103 ASP B C   
3769  O O   . ASP B 103 ? 0.9774 1.9579 1.2432 0.0088  0.0190  0.1422  103 ASP B O   
3770  C CB  . ASP B 103 ? 0.9946 2.0004 1.2511 0.0082  0.0241  0.1129  103 ASP B CB  
3771  C CG  . ASP B 103 ? 1.0810 2.0860 1.3475 0.0104  0.0191  0.0998  103 ASP B CG  
3772  O OD1 . ASP B 103 ? 1.0096 2.0041 1.2911 0.0109  0.0175  0.0986  103 ASP B OD1 
3773  O OD2 . ASP B 103 ? 1.1892 2.2036 1.4483 0.0115  0.0169  0.0906  103 ASP B OD2 
3774  N N   . ARG B 104 ? 0.9071 1.8853 1.1916 0.0111  0.0148  0.1224  104 ARG B N   
3775  C CA  . ARG B 104 ? 0.8923 1.8616 1.1825 0.0136  0.0083  0.1288  104 ARG B CA  
3776  C C   . ARG B 104 ? 0.8875 1.8445 1.1853 0.0123  0.0112  0.1390  104 ARG B C   
3777  O O   . ARG B 104 ? 0.9260 1.8767 1.2235 0.0139  0.0073  0.1487  104 ARG B O   
3778  C CB  . ARG B 104 ? 0.9155 1.8817 1.2173 0.0156  0.0035  0.1183  104 ARG B CB  
3779  C CG  . ARG B 104 ? 0.9311 1.9085 1.2275 0.0165  0.0009  0.1066  104 ARG B CG  
3780  C CD  . ARG B 104 ? 0.9645 1.9376 1.2737 0.0179  -0.0030 0.0964  104 ARG B CD  
3781  N NE  . ARG B 104 ? 1.0014 1.9704 1.3149 0.0205  -0.0101 0.1005  104 ARG B NE  
3782  C CZ  . ARG B 104 ? 0.9945 1.9705 1.3051 0.0224  -0.0166 0.0960  104 ARG B CZ  
3783  N NH1 . ARG B 104 ? 1.0514 2.0382 1.3539 0.0220  -0.0171 0.0871  104 ARG B NH1 
3784  N NH2 . ARG B 104 ? 0.8871 1.8596 1.2032 0.0247  -0.0227 0.1001  104 ARG B NH2 
3785  N N   . ILE B 105 ? 0.8357 1.7892 1.1408 0.0095  0.0177  0.1368  105 ILE B N   
3786  C CA  . ILE B 105 ? 0.8219 1.7635 1.1349 0.0079  0.0204  0.1456  105 ILE B CA  
3787  C C   . ILE B 105 ? 0.8234 1.7665 1.1258 0.0058  0.0238  0.1582  105 ILE B C   
3788  O O   . ILE B 105 ? 0.8044 1.7386 1.1077 0.0062  0.0221  0.1690  105 ILE B O   
3789  C CB  . ILE B 105 ? 0.7699 1.7077 1.0946 0.0056  0.0256  0.1385  105 ILE B CB  
3790  C CG1 . ILE B 105 ? 0.7923 1.7293 1.1256 0.0076  0.0223  0.1258  105 ILE B CG1 
3791  C CG2 . ILE B 105 ? 0.6998 1.6244 1.0339 0.0042  0.0273  0.1464  105 ILE B CG2 
3792  C CD1 . ILE B 105 ? 0.8099 1.7438 1.1540 0.0059  0.0266  0.1181  105 ILE B CD1 
3793  N N   . MET B 106 ? 0.8208 1.7749 1.1127 0.0035  0.0290  0.1570  106 MET B N   
3794  C CA  . MET B 106 ? 0.8114 1.7682 1.0911 0.0011  0.0328  0.1687  106 MET B CA  
3795  C C   . MET B 106 ? 0.8805 1.8437 1.1443 0.0036  0.0276  0.1739  106 MET B C   
3796  O O   . MET B 106 ? 0.8781 1.8485 1.1275 0.0017  0.0311  0.1798  106 MET B O   
3797  C CB  . MET B 106 ? 0.8039 1.7698 1.0804 -0.0027 0.0417  0.1651  106 MET B CB  
3798  C CG  . MET B 106 ? 0.7588 1.7178 1.0500 -0.0059 0.0474  0.1642  106 MET B CG  
3799  S SD  . MET B 106 ? 0.8957 1.8426 1.1891 -0.0088 0.0497  0.1808  106 MET B SD  
3800  C CE  . MET B 106 ? 0.7233 1.6583 1.0381 -0.0099 0.0508  0.1757  106 MET B CE  
3801  N N   . GLU B 107 ? 0.9152 1.8761 1.1811 0.0076  0.0192  0.1720  107 GLU B N   
3802  C CA  . GLU B 107 ? 0.9821 1.9497 1.2337 0.0103  0.0132  0.1761  107 GLU B CA  
3803  C C   . GLU B 107 ? 1.0859 2.0470 1.3303 0.0105  0.0119  0.1922  107 GLU B C   
3804  O O   . GLU B 107 ? 1.1479 2.1157 1.3761 0.0110  0.0101  0.1984  107 GLU B O   
3805  C CB  . GLU B 107 ? 0.9960 1.9636 1.2538 0.0144  0.0046  0.1687  107 GLU B CB  
3806  C CG  . GLU B 107 ? 1.1415 2.1180 1.3853 0.0173  -0.0024 0.1704  107 GLU B CG  
3807  C CD  . GLU B 107 ? 1.1790 2.1575 1.4303 0.0208  -0.0103 0.1610  107 GLU B CD  
3808  O OE1 . GLU B 107 ? 1.1400 2.1224 1.3974 0.0202  -0.0091 0.1481  107 GLU B OE1 
3809  O OE2 . GLU B 107 ? 1.2138 2.1899 1.4655 0.0241  -0.0177 0.1667  107 GLU B OE2 
3810  N N   . GLU B 108 ? 1.2674 2.2153 1.5233 0.0101  0.0125  0.1991  108 GLU B N   
3811  C CA  . GLU B 108 ? 1.2984 2.2384 1.5492 0.0101  0.0115  0.2145  108 GLU B CA  
3812  C C   . GLU B 108 ? 1.3099 2.2462 1.5595 0.0051  0.0203  0.2220  108 GLU B C   
3813  O O   . GLU B 108 ? 1.3289 2.2550 1.5792 0.0044  0.0204  0.2343  108 GLU B O   
3814  C CB  . GLU B 108 ? 1.2825 2.2097 1.5466 0.0135  0.0056  0.2179  108 GLU B CB  
3815  C CG  . GLU B 108 ? 1.2749 2.2058 1.5410 0.0184  -0.0032 0.2120  108 GLU B CG  
3816  C CD  . GLU B 108 ? 1.4322 2.3509 1.7112 0.0218  -0.0083 0.2158  108 GLU B CD  
3817  O OE1 . GLU B 108 ? 1.4240 2.3316 1.7146 0.0202  -0.0047 0.2170  108 GLU B OE1 
3818  O OE2 . GLU B 108 ? 1.5088 2.4294 1.7865 0.0261  -0.0161 0.2173  108 GLU B OE2 
3819  N N   . LYS B 109 ? 0.9854 1.9300 1.2336 0.0015  0.0276  0.2149  109 LYS B N   
3820  C CA  . LYS B 109 ? 0.8640 1.8069 1.1129 -0.0038 0.0367  0.2205  109 LYS B CA  
3821  C C   . LYS B 109 ? 0.8136 1.7413 1.0779 -0.0052 0.0376  0.2258  109 LYS B C   
3822  O O   . LYS B 109 ? 0.7845 1.7048 1.0462 -0.0073 0.0397  0.2384  109 LYS B O   
3823  C CB  . LYS B 109 ? 0.8629 1.8099 1.0933 -0.0057 0.0392  0.2327  109 LYS B CB  
3824  C CG  . LYS B 109 ? 0.8783 1.8413 1.0927 -0.0060 0.0415  0.2269  109 LYS B CG  
3825  C CD  . LYS B 109 ? 0.8359 1.8021 1.0305 -0.0075 0.0433  0.2400  109 LYS B CD  
3826  C CE  . LYS B 109 ? 0.8979 1.8577 1.0943 -0.0129 0.0517  0.2510  109 LYS B CE  
3827  N NZ  . LYS B 109 ? 0.9474 1.9152 1.1481 -0.0177 0.0620  0.2437  109 LYS B NZ  
3828  N N   . PRO B 110 ? 0.7750 1.6973 1.0551 -0.0040 0.0362  0.2164  110 PRO B N   
3829  C CA  . PRO B 110 ? 0.7112 1.6191 1.0055 -0.0053 0.0370  0.2206  110 PRO B CA  
3830  C C   . PRO B 110 ? 0.6837 1.5917 0.9824 -0.0111 0.0458  0.2221  110 PRO B C   
3831  O O   . PRO B 110 ? 0.6795 1.5979 0.9780 -0.0133 0.0510  0.2139  110 PRO B O   
3832  C CB  . PRO B 110 ? 0.6302 1.5343 0.9380 -0.0024 0.0329  0.2089  110 PRO B CB  
3833  C CG  . PRO B 110 ? 0.7366 1.6518 1.0370 0.0010  0.0286  0.2005  110 PRO B CG  
3834  C CD  . PRO B 110 ? 0.7916 1.7197 1.0772 -0.0013 0.0330  0.2019  110 PRO B CD  
3835  N N   . SER B 111 ? 0.6342 1.5306 0.9376 -0.0134 0.0475  0.2326  111 SER B N   
3836  C CA  . SER B 111 ? 0.5690 1.4647 0.8783 -0.0193 0.0556  0.2348  111 SER B CA  
3837  C C   . SER B 111 ? 0.5500 1.4441 0.8753 -0.0200 0.0571  0.2228  111 SER B C   
3838  O O   . SER B 111 ? 0.5472 1.4501 0.8755 -0.0233 0.0632  0.2167  111 SER B O   
3839  C CB  . SER B 111 ? 0.6314 1.5138 0.9429 -0.0216 0.0562  0.2486  111 SER B CB  
3840  O OG  . SER B 111 ? 0.7034 1.5837 1.0238 -0.0273 0.0634  0.2497  111 SER B OG  
3841  N N   . HIS B 112 ? 0.5892 1.4724 0.9250 -0.0169 0.0515  0.2195  112 HIS B N   
3842  C CA  . HIS B 112 ? 0.5200 1.3998 0.8704 -0.0171 0.0518  0.2088  112 HIS B CA  
3843  C C   . HIS B 112 ? 0.5079 1.3871 0.8604 -0.0118 0.0452  0.1994  112 HIS B C   
3844  O O   . HIS B 112 ? 0.5108 1.3869 0.8585 -0.0080 0.0396  0.2030  112 HIS B O   
3845  C CB  . HIS B 112 ? 0.5172 1.3820 0.8793 -0.0192 0.0521  0.2141  112 HIS B CB  
3846  C CG  . HIS B 112 ? 0.5308 1.3944 0.8909 -0.0245 0.0579  0.2249  112 HIS B CG  
3847  N ND1 . HIS B 112 ? 0.5557 1.4285 0.9175 -0.0294 0.0653  0.2229  112 HIS B ND1 
3848  C CD2 . HIS B 112 ? 0.6145 1.4689 0.9711 -0.0257 0.0575  0.2380  112 HIS B CD2 
3849  C CE1 . HIS B 112 ? 0.6540 1.5234 1.0136 -0.0338 0.0696  0.2344  112 HIS B CE1 
3850  N NE2 . HIS B 112 ? 0.6780 1.5358 1.0342 -0.0317 0.0648  0.2438  112 HIS B NE2 
3851  N N   . VAL B 113 ? 0.4946 1.3772 0.8551 -0.0117 0.0461  0.1873  113 VAL B N   
3852  C CA  . VAL B 113 ? 0.4826 1.3648 0.8463 -0.0074 0.0407  0.1775  113 VAL B CA  
3853  C C   . VAL B 113 ? 0.4688 1.3398 0.8466 -0.0074 0.0398  0.1720  113 VAL B C   
3854  O O   . VAL B 113 ? 0.4643 1.3361 0.8494 -0.0104 0.0439  0.1681  113 VAL B O   
3855  C CB  . VAL B 113 ? 0.4808 1.3773 0.8392 -0.0067 0.0419  0.1673  113 VAL B CB  
3856  C CG1 . VAL B 113 ? 0.4820 1.3864 0.8426 -0.0108 0.0492  0.1640  113 VAL B CG1 
3857  C CG2 . VAL B 113 ? 0.4665 1.3608 0.8319 -0.0034 0.0375  0.1559  113 VAL B CG2 
3858  N N   . PHE B 114 ? 0.4626 1.3238 0.8443 -0.0039 0.0343  0.1717  114 PHE B N   
3859  C CA  . PHE B 114 ? 0.4503 1.3005 0.8437 -0.0034 0.0328  0.1660  114 PHE B CA  
3860  C C   . PHE B 114 ? 0.4392 1.2945 0.8354 -0.0015 0.0315  0.1533  114 PHE B C   
3861  O O   . PHE B 114 ? 0.4574 1.3196 0.8481 0.0012  0.0286  0.1496  114 PHE B O   
3862  C CB  . PHE B 114 ? 0.4493 1.2866 0.8456 -0.0004 0.0281  0.1710  114 PHE B CB  
3863  C CG  . PHE B 114 ? 0.4575 1.2847 0.8555 -0.0024 0.0293  0.1819  114 PHE B CG  
3864  C CD1 . PHE B 114 ? 0.4919 1.3199 0.8917 -0.0071 0.0344  0.1857  114 PHE B CD1 
3865  C CD2 . PHE B 114 ? 0.5861 1.4028 0.9849 0.0005  0.0254  0.1880  114 PHE B CD2 
3866  C CE1 . PHE B 114 ? 0.5770 1.3950 0.9789 -0.0092 0.0354  0.1956  114 PHE B CE1 
3867  C CE2 . PHE B 114 ? 0.6329 1.4393 1.0336 -0.0011 0.0262  0.1978  114 PHE B CE2 
3868  C CZ  . PHE B 114 ? 0.6019 1.4087 1.0041 -0.0061 0.0312  0.2017  114 PHE B CZ  
3869  N N   . LEU B 115 ? 0.5041 1.3559 0.9093 -0.0030 0.0332  0.1467  115 LEU B N   
3870  C CA  . LEU B 115 ? 0.5382 1.3923 0.9471 -0.0012 0.0316  0.1348  115 LEU B CA  
3871  C C   . LEU B 115 ? 0.6513 1.4921 1.0703 -0.0009 0.0300  0.1317  115 LEU B C   
3872  O O   . LEU B 115 ? 0.6980 1.5355 1.1234 -0.0036 0.0325  0.1317  115 LEU B O   
3873  C CB  . LEU B 115 ? 0.5398 1.4064 0.9481 -0.0031 0.0358  0.1282  115 LEU B CB  
3874  C CG  . LEU B 115 ? 0.5406 1.4103 0.9519 -0.0010 0.0340  0.1159  115 LEU B CG  
3875  C CD1 . LEU B 115 ? 0.6231 1.5081 1.0281 -0.0013 0.0367  0.1108  115 LEU B CD1 
3876  C CD2 . LEU B 115 ? 0.6067 1.4695 1.0289 -0.0019 0.0347  0.1101  115 LEU B CD2 
3877  N N   . LEU B 116 ? 0.8645 1.6978 1.2847 0.0023  0.0257  0.1290  116 LEU B N   
3878  C CA  . LEU B 116 ? 0.8572 1.6776 1.2853 0.0029  0.0239  0.1255  116 LEU B CA  
3879  C C   . LEU B 116 ? 0.9033 1.7237 1.3322 0.0057  0.0211  0.1162  116 LEU B C   
3880  O O   . LEU B 116 ? 0.8504 1.6784 1.2743 0.0074  0.0196  0.1142  116 LEU B O   
3881  C CB  . LEU B 116 ? 0.8703 1.6782 1.2997 0.0038  0.0221  0.1334  116 LEU B CB  
3882  C CG  . LEU B 116 ? 0.8808 1.6895 1.3047 0.0065  0.0195  0.1391  116 LEU B CG  
3883  C CD1 . LEU B 116 ? 0.9405 1.7435 1.3666 0.0100  0.0160  0.1338  116 LEU B CD1 
3884  C CD2 . LEU B 116 ? 0.9046 1.7057 1.3282 0.0059  0.0197  0.1499  116 LEU B CD2 
3885  N N   . ASN B 117 ? 1.2522 2.0636 1.6873 0.0059  0.0202  0.1107  117 ASN B N   
3886  C CA  . ASN B 117 ? 1.2414 2.0514 1.6779 0.0079  0.0180  0.1018  117 ASN B CA  
3887  C C   . ASN B 117 ? 1.2396 2.0393 1.6765 0.0104  0.0150  0.1029  117 ASN B C   
3888  O O   . ASN B 117 ? 1.2477 2.0395 1.6851 0.0108  0.0145  0.1097  117 ASN B O   
3889  C CB  . ASN B 117 ? 1.2340 2.0402 1.6763 0.0069  0.0185  0.0950  117 ASN B CB  
3890  C CG  . ASN B 117 ? 1.2286 2.0360 1.6715 0.0087  0.0168  0.0854  117 ASN B CG  
3891  O OD1 . ASN B 117 ? 1.2320 2.0461 1.6711 0.0100  0.0158  0.0831  117 ASN B OD1 
3892  N ND2 . ASN B 117 ? 1.2140 2.0146 1.6619 0.0086  0.0161  0.0799  117 ASN B ND2 
3893  N N   . CYS B 118 ? 0.9454 1.7453 1.3825 0.0121  0.0131  0.0958  118 CYS B N   
3894  C CA  . CYS B 118 ? 0.7881 1.5798 1.2261 0.0144  0.0108  0.0958  118 CYS B CA  
3895  C C   . CYS B 118 ? 0.8386 1.6153 1.2805 0.0145  0.0106  0.0957  118 CYS B C   
3896  O O   . CYS B 118 ? 0.8147 1.5830 1.2571 0.0155  0.0100  0.1007  118 CYS B O   
3897  C CB  . CYS B 118 ? 0.6778 1.4743 1.1154 0.0156  0.0093  0.0880  118 CYS B CB  
3898  S SG  . CYS B 118 ? 0.5667 1.3525 1.0068 0.0177  0.0073  0.0858  118 CYS B SG  
3899  N N   . ASP B 119 ? 0.9191 1.6921 1.3636 0.0135  0.0108  0.0897  119 ASP B N   
3900  C CA  . ASP B 119 ? 0.9041 1.6626 1.3511 0.0138  0.0100  0.0884  119 ASP B CA  
3901  C C   . ASP B 119 ? 0.8637 1.6174 1.3131 0.0118  0.0109  0.0929  119 ASP B C   
3902  O O   . ASP B 119 ? 0.8537 1.6058 1.3062 0.0104  0.0110  0.0895  119 ASP B O   
3903  C CB  . ASP B 119 ? 0.9063 1.6625 1.3547 0.0140  0.0090  0.0798  119 ASP B CB  
3904  C CG  . ASP B 119 ? 0.8902 1.6575 1.3397 0.0128  0.0099  0.0755  119 ASP B CG  
3905  O OD1 . ASP B 119 ? 0.9086 1.6857 1.3574 0.0115  0.0117  0.0792  119 ASP B OD1 
3906  O OD2 . ASP B 119 ? 0.8699 1.6360 1.3208 0.0132  0.0090  0.0684  119 ASP B OD2 
3907  N N   . VAL B 120 ? 0.8636 1.6149 1.3123 0.0118  0.0114  0.1006  120 VAL B N   
3908  C CA  . VAL B 120 ? 0.8098 1.5555 1.2610 0.0098  0.0122  0.1057  120 VAL B CA  
3909  C C   . VAL B 120 ? 0.8020 1.5364 1.2528 0.0112  0.0114  0.1111  120 VAL B C   
3910  O O   . VAL B 120 ? 0.8432 1.5795 1.2917 0.0133  0.0111  0.1144  120 VAL B O   
3911  C CB  . VAL B 120 ? 0.7812 1.5384 1.2318 0.0075  0.0146  0.1107  120 VAL B CB  
3912  C CG1 . VAL B 120 ? 0.7359 1.4865 1.1892 0.0053  0.0155  0.1176  120 VAL B CG1 
3913  C CG2 . VAL B 120 ? 0.8398 1.6070 1.2920 0.0058  0.0159  0.1048  120 VAL B CG2 
3914  N N   . CYS B 121 ? 0.7845 1.5069 1.2379 0.0103  0.0109  0.1117  121 CYS B N   
3915  C CA  . CYS B 121 ? 0.7801 1.4902 1.2335 0.0118  0.0101  0.1159  121 CYS B CA  
3916  C C   . CYS B 121 ? 0.7917 1.4958 1.2481 0.0093  0.0106  0.1210  121 CYS B C   
3917  O O   . CYS B 121 ? 0.8672 1.5609 1.3257 0.0084  0.0095  0.1186  121 CYS B O   
3918  C CB  . CYS B 121 ? 0.7794 1.4782 1.2319 0.0138  0.0088  0.1103  121 CYS B CB  
3919  S SG  . CYS B 121 ? 0.8754 1.5793 1.3251 0.0166  0.0086  0.1057  121 CYS B SG  
3920  N N   . CYS B 122 ? 0.7459 1.4563 1.2023 0.0080  0.0120  0.1282  122 CYS B N   
3921  C CA  . CYS B 122 ? 0.8127 1.5179 1.2721 0.0053  0.0127  0.1342  122 CYS B CA  
3922  C C   . CYS B 122 ? 0.8097 1.5100 1.2676 0.0071  0.0126  0.1422  122 CYS B C   
3923  O O   . CYS B 122 ? 0.8153 1.5161 1.2705 0.0106  0.0118  0.1425  122 CYS B O   
3924  C CB  . CYS B 122 ? 0.7764 1.4933 1.2375 0.0016  0.0150  0.1361  122 CYS B CB  
3925  S SG  . CYS B 122 ? 0.6295 1.3633 1.0851 0.0022  0.0169  0.1393  122 CYS B SG  
3926  N N   . SER B 123 ? 0.8010 1.4965 1.2615 0.0046  0.0134  0.1487  123 SER B N   
3927  C CA  . SER B 123 ? 0.7387 1.4285 1.1983 0.0062  0.0131  0.1568  123 SER B CA  
3928  C C   . SER B 123 ? 0.7162 1.4181 1.1720 0.0064  0.0142  0.1633  123 SER B C   
3929  O O   . SER B 123 ? 0.7643 1.4631 1.2185 0.0088  0.0133  0.1697  123 SER B O   
3930  C CB  . SER B 123 ? 0.7960 1.4747 1.2600 0.0033  0.0132  0.1613  123 SER B CB  
3931  O OG  . SER B 123 ? 0.7600 1.4457 1.2262 -0.0015 0.0154  0.1637  123 SER B OG  
3932  N N   . PHE B 124 ? 0.6716 1.3870 1.1255 0.0040  0.0160  0.1618  124 PHE B N   
3933  C CA  . PHE B 124 ? 0.6536 1.3817 1.1025 0.0040  0.0171  0.1672  124 PHE B CA  
3934  C C   . PHE B 124 ? 0.6762 1.4009 1.1242 0.0024  0.0181  0.1782  124 PHE B C   
3935  O O   . PHE B 124 ? 0.6813 1.4041 1.1265 0.0055  0.0164  0.1839  124 PHE B O   
3936  C CB  . PHE B 124 ? 0.6130 1.3458 1.0578 0.0085  0.0150  0.1654  124 PHE B CB  
3937  C CG  . PHE B 124 ? 0.5864 1.3246 1.0312 0.0096  0.0144  0.1553  124 PHE B CG  
3938  C CD1 . PHE B 124 ? 0.5440 1.2957 0.9861 0.0081  0.0158  0.1515  124 PHE B CD1 
3939  C CD2 . PHE B 124 ? 0.6481 1.3772 1.0953 0.0122  0.0127  0.1496  124 PHE B CD2 
3940  C CE1 . PHE B 124 ? 0.5777 1.3334 1.0201 0.0091  0.0151  0.1423  124 PHE B CE1 
3941  C CE2 . PHE B 124 ? 0.6503 1.3834 1.0972 0.0130  0.0122  0.1408  124 PHE B CE2 
3942  C CZ  . PHE B 124 ? 0.6263 1.3724 1.0711 0.0115  0.0133  0.1372  124 PHE B CZ  
3943  N N   . PRO B 125 ? 0.6814 1.4053 1.1324 -0.0023 0.0206  0.1815  125 PRO B N   
3944  C CA  . PRO B 125 ? 0.6943 1.4155 1.1441 -0.0044 0.0220  0.1926  125 PRO B CA  
3945  C C   . PRO B 125 ? 0.7346 1.4706 1.1779 -0.0063 0.0246  0.1973  125 PRO B C   
3946  O O   . PRO B 125 ? 0.7887 1.5291 1.2327 -0.0110 0.0282  0.2009  125 PRO B O   
3947  C CB  . PRO B 125 ? 0.6823 1.3948 1.1395 -0.0090 0.0234  0.1926  125 PRO B CB  
3948  C CG  . PRO B 125 ? 0.7124 1.4264 1.1738 -0.0094 0.0230  0.1814  125 PRO B CG  
3949  C CD  . PRO B 125 ? 0.7052 1.4298 1.1615 -0.0060 0.0222  0.1753  125 PRO B CD  
3950  N N   . LEU B 126 ? 0.7815 1.5255 1.2181 -0.0025 0.0229  0.1971  126 LEU B N   
3951  C CA  . LEU B 126 ? 0.7482 1.5074 1.1772 -0.0037 0.0250  0.1998  126 LEU B CA  
3952  C C   . LEU B 126 ? 0.9029 1.6613 1.3282 -0.0066 0.0272  0.2118  126 LEU B C   
3953  O O   . LEU B 126 ? 0.8174 1.5864 1.2385 -0.0101 0.0310  0.2142  126 LEU B O   
3954  C CB  . LEU B 126 ? 0.7335 1.5000 1.1565 0.0011  0.0218  0.1975  126 LEU B CB  
3955  C CG  . LEU B 126 ? 0.6750 1.4431 1.1009 0.0037  0.0199  0.1860  126 LEU B CG  
3956  C CD1 . LEU B 126 ? 0.7049 1.4819 1.1250 0.0077  0.0170  0.1843  126 LEU B CD1 
3957  C CD2 . LEU B 126 ? 0.6721 1.4471 1.1004 0.0005  0.0229  0.1780  126 LEU B CD2 
3958  N N   . GLN B 127 ? 1.3278 2.0736 1.7544 -0.0051 0.0251  0.2195  127 GLN B N   
3959  C CA  . GLN B 127 ? 1.3575 2.1011 1.7804 -0.0078 0.0270  0.2316  127 GLN B CA  
3960  C C   . GLN B 127 ? 1.3636 2.1034 1.7926 -0.0141 0.0313  0.2336  127 GLN B C   
3961  O O   . GLN B 127 ? 1.3817 2.1246 1.8070 -0.0180 0.0347  0.2421  127 GLN B O   
3962  C CB  . GLN B 127 ? 1.3853 2.1159 1.8086 -0.0039 0.0231  0.2390  127 GLN B CB  
3963  C CG  . GLN B 127 ? 1.4314 2.1605 1.8486 -0.0053 0.0239  0.2525  127 GLN B CG  
3964  C CD  . GLN B 127 ? 1.5422 2.2597 1.9597 -0.0003 0.0193  0.2591  127 GLN B CD  
3965  O OE1 . GLN B 127 ? 1.4502 2.1633 1.8717 0.0046  0.0156  0.2533  127 GLN B OE1 
3966  N NE2 . GLN B 127 ? 1.6771 2.3897 2.0906 -0.0014 0.0195  0.2713  127 GLN B NE2 
3967  N N   . GLY B 128 ? 1.0016 1.7349 1.4398 -0.0154 0.0312  0.2258  128 GLY B N   
3968  C CA  . GLY B 128 ? 0.9960 1.7262 1.4414 -0.0214 0.0348  0.2267  128 GLY B CA  
3969  C C   . GLY B 128 ? 0.9368 1.6822 1.3822 -0.0252 0.0392  0.2218  128 GLY B C   
3970  O O   . GLY B 128 ? 0.9401 1.6887 1.3879 -0.0308 0.0436  0.2264  128 GLY B O   
3971  N N   . ILE B 129 ? 0.8802 1.6350 1.3235 -0.0224 0.0381  0.2123  129 ILE B N   
3972  C CA  . ILE B 129 ? 0.8380 1.6077 1.2814 -0.0252 0.0422  0.2067  129 ILE B CA  
3973  C C   . ILE B 129 ? 0.7926 1.5752 1.2257 -0.0263 0.0456  0.2131  129 ILE B C   
3974  O O   . ILE B 129 ? 0.8200 1.6132 1.2532 -0.0305 0.0507  0.2131  129 ILE B O   
3975  C CB  . ILE B 129 ? 0.7570 1.5312 1.2019 -0.0217 0.0397  0.1943  129 ILE B CB  
3976  C CG1 . ILE B 129 ? 0.7310 1.5203 1.1768 -0.0242 0.0437  0.1878  129 ILE B CG1 
3977  C CG2 . ILE B 129 ? 0.8132 1.5891 1.2502 -0.0161 0.0360  0.1934  129 ILE B CG2 
3978  C CD1 . ILE B 129 ? 0.8564 1.6466 1.3109 -0.0300 0.0478  0.1885  129 ILE B CD1 
3979  N N   . LEU B 130 ? 0.8872 1.6693 1.3111 -0.0225 0.0427  0.2187  130 LEU B N   
3980  C CA  . LEU B 130 ? 0.7850 1.5780 1.1976 -0.0234 0.0454  0.2257  130 LEU B CA  
3981  C C   . LEU B 130 ? 0.8902 1.6806 1.3030 -0.0290 0.0501  0.2364  130 LEU B C   
3982  O O   . LEU B 130 ? 0.8859 1.6880 1.2941 -0.0328 0.0555  0.2386  130 LEU B O   
3983  C CB  . LEU B 130 ? 0.8121 1.6032 1.2160 -0.0179 0.0404  0.2303  130 LEU B CB  
3984  C CG  . LEU B 130 ? 0.6967 1.5016 1.0873 -0.0165 0.0408  0.2328  130 LEU B CG  
3985  C CD1 . LEU B 130 ? 0.7498 1.5513 1.1352 -0.0105 0.0345  0.2353  130 LEU B CD1 
3986  C CD2 . LEU B 130 ? 0.7874 1.5965 1.1705 -0.0210 0.0457  0.2437  130 LEU B CD2 
3987  N N   . ASP B 131 ? 1.0608 1.8358 1.4790 -0.0298 0.0484  0.2430  131 ASP B N   
3988  C CA  . ASP B 131 ? 1.0862 1.8571 1.5055 -0.0354 0.0527  0.2536  131 ASP B CA  
3989  C C   . ASP B 131 ? 1.0745 1.8494 1.5038 -0.0416 0.0579  0.2492  131 ASP B C   
3990  O O   . ASP B 131 ? 1.0894 1.8689 1.5179 -0.0471 0.0636  0.2560  131 ASP B O   
3991  C CB  . ASP B 131 ? 1.1088 1.8611 1.5319 -0.0343 0.0491  0.2612  131 ASP B CB  
3992  C CG  . ASP B 131 ? 1.1274 1.8757 1.5423 -0.0278 0.0436  0.2652  131 ASP B CG  
3993  O OD1 . ASP B 131 ? 1.1327 1.8927 1.5368 -0.0255 0.0434  0.2663  131 ASP B OD1 
3994  O OD2 . ASP B 131 ? 1.1430 1.8768 1.5626 -0.0248 0.0394  0.2671  131 ASP B OD2 
3995  N N   . ALA B 132 ? 0.9303 1.7035 1.3694 -0.0407 0.0561  0.2380  132 ALA B N   
3996  C CA  . ALA B 132 ? 0.8723 1.6511 1.3215 -0.0459 0.0604  0.2326  132 ALA B CA  
3997  C C   . ALA B 132 ? 0.8851 1.6831 1.3294 -0.0475 0.0656  0.2290  132 ALA B C   
3998  O O   . ALA B 132 ? 0.9441 1.7494 1.3941 -0.0530 0.0714  0.2294  132 ALA B O   
3999  C CB  . ALA B 132 ? 0.8518 1.6244 1.3115 -0.0440 0.0564  0.2213  132 ALA B CB  
4000  N N   . HIS B 133 ? 0.7510 1.5574 1.1851 -0.0427 0.0638  0.2254  133 HIS B N   
4001  C CA  . HIS B 133 ? 0.7369 1.5613 1.1651 -0.0437 0.0685  0.2216  133 HIS B CA  
4002  C C   . HIS B 133 ? 0.8327 1.6633 1.2509 -0.0474 0.0739  0.2329  133 HIS B C   
4003  O O   . HIS B 133 ? 0.8716 1.7151 1.2892 -0.0513 0.0805  0.2320  133 HIS B O   
4004  C CB  . HIS B 133 ? 0.6707 1.5013 1.0911 -0.0376 0.0644  0.2139  133 HIS B CB  
4005  C CG  . HIS B 133 ? 0.5997 1.4481 1.0124 -0.0380 0.0688  0.2099  133 HIS B CG  
4006  N ND1 . HIS B 133 ? 0.6011 1.4602 1.0197 -0.0421 0.0749  0.2051  133 HIS B ND1 
4007  C CD2 . HIS B 133 ? 0.5502 1.4076 0.9498 -0.0348 0.0678  0.2096  133 HIS B CD2 
4008  C CE1 . HIS B 133 ? 0.5881 1.4619 0.9972 -0.0413 0.0779  0.2020  133 HIS B CE1 
4009  N NE2 . HIS B 133 ? 0.5585 1.4314 0.9556 -0.0369 0.0735  0.2046  133 HIS B NE2 
4010  N N   . ARG B 134 ? 0.9055 1.7272 1.3156 -0.0459 0.0713  0.2437  134 ARG B N   
4011  C CA  . ARG B 134 ? 0.9416 1.7674 1.3414 -0.0494 0.0760  0.2558  134 ARG B CA  
4012  C C   . ARG B 134 ? 1.0621 1.8866 1.4705 -0.0570 0.0827  0.2611  134 ARG B C   
4013  O O   . ARG B 134 ? 0.9648 1.7992 1.3669 -0.0614 0.0895  0.2666  134 ARG B O   
4014  C CB  . ARG B 134 ? 0.9257 1.7398 1.3169 -0.0461 0.0710  0.2665  134 ARG B CB  
4015  C CG  . ARG B 134 ? 0.8399 1.6590 1.2198 -0.0394 0.0656  0.2637  134 ARG B CG  
4016  C CD  . ARG B 134 ? 0.8073 1.6141 1.1817 -0.0357 0.0600  0.2737  134 ARG B CD  
4017  N NE  . ARG B 134 ? 0.8444 1.6577 1.2072 -0.0298 0.0552  0.2724  134 ARG B NE  
4018  C CZ  . ARG B 134 ? 0.8571 1.6620 1.2156 -0.0250 0.0490  0.2785  134 ARG B CZ  
4019  N NH1 . ARG B 134 ? 0.9026 1.6916 1.2668 -0.0251 0.0470  0.2863  134 ARG B NH1 
4020  N NH2 . ARG B 134 ? 0.7950 1.6075 1.1437 -0.0199 0.0446  0.2764  134 ARG B NH2 
4021  N N   . ARG B 135 ? 1.9478 2.7604 2.3705 -0.0589 0.0809  0.2594  135 ARG B N   
4022  C CA  . ARG B 135 ? 1.9500 2.7612 2.3830 -0.0664 0.0867  0.2634  135 ARG B CA  
4023  C C   . ARG B 135 ? 1.9240 2.7502 2.3652 -0.0696 0.0921  0.2536  135 ARG B C   
4024  O O   . ARG B 135 ? 1.9301 2.7649 2.3728 -0.0756 0.0997  0.2579  135 ARG B O   
4025  C CB  . ARG B 135 ? 1.9507 2.7438 2.3962 -0.0671 0.0823  0.2642  135 ARG B CB  
4026  C CG  . ARG B 135 ? 1.9491 2.7409 2.4089 -0.0746 0.0871  0.2650  135 ARG B CG  
4027  C CD  . ARG B 135 ? 1.9575 2.7302 2.4278 -0.0751 0.0822  0.2664  135 ARG B CD  
4028  N NE  . ARG B 135 ? 1.9529 2.7251 2.4390 -0.0817 0.0853  0.2637  135 ARG B NE  
4029  C CZ  . ARG B 135 ? 1.9288 2.7013 2.4268 -0.0810 0.0825  0.2520  135 ARG B CZ  
4030  N NH1 . ARG B 135 ? 1.9186 2.6911 2.4137 -0.0742 0.0770  0.2425  135 ARG B NH1 
4031  N NH2 . ARG B 135 ? 1.9120 2.6846 2.4247 -0.0870 0.0850  0.2499  135 ARG B NH2 
4032  N N   . TYR B 136 ? 1.2084 2.0380 1.6553 -0.0655 0.0884  0.2406  136 TYR B N   
4033  C CA  . TYR B 136 ? 0.9516 1.7953 1.4066 -0.0677 0.0929  0.2306  136 TYR B CA  
4034  C C   . TYR B 136 ? 0.8546 1.7160 1.2981 -0.0680 0.0989  0.2306  136 TYR B C   
4035  O O   . TYR B 136 ? 0.8042 1.6778 1.2526 -0.0727 0.1062  0.2291  136 TYR B O   
4036  C CB  . TYR B 136 ? 0.8017 1.6439 1.2635 -0.0626 0.0869  0.2172  136 TYR B CB  
4037  C CG  . TYR B 136 ? 0.7824 1.6087 1.2563 -0.0626 0.0815  0.2152  136 TYR B CG  
4038  C CD1 . TYR B 136 ? 0.9153 1.7338 1.3990 -0.0684 0.0836  0.2215  136 TYR B CD1 
4039  C CD2 . TYR B 136 ? 0.7235 1.5423 1.1987 -0.0569 0.0744  0.2070  136 TYR B CD2 
4040  C CE1 . TYR B 136 ? 0.9243 1.7281 1.4185 -0.0683 0.0784  0.2191  136 TYR B CE1 
4041  C CE2 . TYR B 136 ? 0.7433 1.5475 1.2283 -0.0567 0.0696  0.2049  136 TYR B CE2 
4042  C CZ  . TYR B 136 ? 0.7898 1.5865 1.2841 -0.0624 0.0715  0.2108  136 TYR B CZ  
4043  O OH  . TYR B 136 ? 0.8109 1.5927 1.3143 -0.0622 0.0664  0.2082  136 TYR B OH  
4044  N N   . GLY B 137 ? 0.8677 1.7311 1.2959 -0.0630 0.0959  0.2321  137 GLY B N   
4045  C CA  . GLY B 137 ? 0.7520 1.6321 1.1684 -0.0624 0.1005  0.2301  137 GLY B CA  
4046  C C   . GLY B 137 ? 0.6281 1.5186 1.0496 -0.0592 0.0997  0.2150  137 GLY B C   
4047  O O   . GLY B 137 ? 0.6254 1.5088 1.0546 -0.0554 0.0935  0.2070  137 GLY B O   
4048  N N   . GLY B 138 ? 0.5938 1.5009 1.0108 -0.0606 0.1062  0.2113  138 GLY B N   
4049  C CA  . GLY B 138 ? 0.6202 1.5376 1.0415 -0.0574 0.1057  0.1971  138 GLY B CA  
4050  C C   . GLY B 138 ? 0.5489 1.4649 0.9604 -0.0505 0.0987  0.1914  138 GLY B C   
4051  O O   . GLY B 138 ? 0.5190 1.4292 0.9186 -0.0481 0.0948  0.1985  138 GLY B O   
4052  N N   . ILE B 139 ? 0.5185 1.4401 0.9361 -0.0473 0.0969  0.1783  139 ILE B N   
4053  C CA  . ILE B 139 ? 0.5119 1.4339 0.9217 -0.0412 0.0908  0.1713  139 ILE B CA  
4054  C C   . ILE B 139 ? 0.5045 1.4100 0.9188 -0.0379 0.0825  0.1714  139 ILE B C   
4055  O O   . ILE B 139 ? 0.5775 1.4765 0.9824 -0.0353 0.0781  0.1774  139 ILE B O   
4056  C CB  . ILE B 139 ? 0.5297 1.4632 0.9443 -0.0392 0.0922  0.1572  139 ILE B CB  
4057  C CG1 . ILE B 139 ? 0.5993 1.5497 1.0094 -0.0424 0.1012  0.1568  139 ILE B CG1 
4058  C CG2 . ILE B 139 ? 0.5233 1.4566 0.9301 -0.0333 0.0859  0.1502  139 ILE B CG2 
4059  C CD1 . ILE B 139 ? 0.5787 1.5365 0.9696 -0.0415 0.1027  0.1620  139 ILE B CD1 
4060  N N   . GLY B 140 ? 0.4712 1.3703 0.8998 -0.0378 0.0802  0.1648  140 GLY B N   
4061  C CA  . GLY B 140 ? 0.4619 1.3461 0.8945 -0.0343 0.0727  0.1632  140 GLY B CA  
4062  C C   . GLY B 140 ? 0.4738 1.3447 0.9171 -0.0372 0.0716  0.1683  140 GLY B C   
4063  O O   . GLY B 140 ? 0.5501 1.4228 0.9978 -0.0424 0.0767  0.1743  140 GLY B O   
4064  N N   . THR B 141 ? 0.4666 1.3240 0.9141 -0.0342 0.0652  0.1659  141 THR B N   
4065  C CA  . THR B 141 ? 0.5290 1.3726 0.9862 -0.0365 0.0635  0.1699  141 THR B CA  
4066  C C   . THR B 141 ? 0.6506 1.4839 1.1156 -0.0334 0.0577  0.1615  141 THR B C   
4067  O O   . THR B 141 ? 0.7390 1.5617 1.2131 -0.0354 0.0562  0.1625  141 THR B O   
4068  C CB  . THR B 141 ? 0.5385 1.3718 0.9890 -0.0366 0.0620  0.1818  141 THR B CB  
4069  O OG1 . THR B 141 ? 0.5538 1.3945 0.9905 -0.0342 0.0623  0.1854  141 THR B OG1 
4070  C CG2 . THR B 141 ? 0.6018 1.4332 1.0568 -0.0427 0.0667  0.1908  141 THR B CG2 
4071  N N   . MET B 142 ? 0.6138 1.4497 1.0750 -0.0288 0.0545  0.1533  142 MET B N   
4072  C CA  . MET B 142 ? 0.7260 1.5530 1.1934 -0.0258 0.0494  0.1449  142 MET B CA  
4073  C C   . MET B 142 ? 0.8021 1.6118 1.2714 -0.0249 0.0450  0.1492  142 MET B C   
4074  O O   . MET B 142 ? 0.8232 1.6274 1.2870 -0.0250 0.0447  0.1582  142 MET B O   
4075  C CB  . MET B 142 ? 0.7111 1.5421 1.1902 -0.0279 0.0508  0.1375  142 MET B CB  
4076  C CG  . MET B 142 ? 0.7375 1.5774 1.2172 -0.0250 0.0502  0.1265  142 MET B CG  
4077  S SD  . MET B 142 ? 0.8009 1.6399 1.2957 -0.0261 0.0492  0.1176  142 MET B SD  
4078  C CE  . MET B 142 ? 1.0034 1.8216 1.5015 -0.0253 0.0429  0.1197  142 MET B CE  
4079  N N   . LEU B 143 ? 0.8238 1.6245 1.3005 -0.0238 0.0413  0.1428  143 LEU B N   
4080  C CA  . LEU B 143 ? 0.9096 1.6936 1.3894 -0.0234 0.0375  0.1454  143 LEU B CA  
4081  C C   . LEU B 143 ? 0.9647 1.7432 1.4534 -0.0233 0.0348  0.1370  143 LEU B C   
4082  O O   . LEU B 143 ? 0.9562 1.7400 1.4455 -0.0211 0.0337  0.1285  143 LEU B O   
4083  C CB  . LEU B 143 ? 0.9130 1.6888 1.3850 -0.0188 0.0338  0.1468  143 LEU B CB  
4084  C CG  . LEU B 143 ? 0.9497 1.7088 1.4237 -0.0185 0.0309  0.1517  143 LEU B CG  
4085  C CD1 . LEU B 143 ? 0.9911 1.7489 1.4602 -0.0195 0.0326  0.1628  143 LEU B CD1 
4086  C CD2 . LEU B 143 ? 0.8437 1.5926 1.3153 -0.0138 0.0264  0.1469  143 LEU B CD2 
4087  N N   . VAL B 144 ? 1.1069 1.8742 1.6023 -0.0257 0.0333  0.1393  144 VAL B N   
4088  C CA  . VAL B 144 ? 1.0795 1.8413 1.5837 -0.0261 0.0303  0.1321  144 VAL B CA  
4089  C C   . VAL B 144 ? 1.0667 1.8104 1.5709 -0.0249 0.0258  0.1334  144 VAL B C   
4090  O O   . VAL B 144 ? 1.0800 1.8161 1.5795 -0.0245 0.0257  0.1404  144 VAL B O   
4091  C CB  . VAL B 144 ? 1.1576 1.9266 1.6726 -0.0313 0.0333  0.1322  144 VAL B CB  
4092  C CG1 . VAL B 144 ? 1.1619 1.9487 1.6779 -0.0318 0.0374  0.1282  144 VAL B CG1 
4093  C CG2 . VAL B 144 ? 1.1544 1.9204 1.6708 -0.0358 0.0363  0.1424  144 VAL B CG2 
4094  N N   . ILE B 145 ? 1.0072 1.7440 1.5165 -0.0242 0.0219  0.1263  145 ILE B N   
4095  C CA  . ILE B 145 ? 1.0490 1.7686 1.5584 -0.0231 0.0176  0.1261  145 ILE B CA  
4096  C C   . ILE B 145 ? 1.1362 1.8521 1.6543 -0.0247 0.0144  0.1196  145 ILE B C   
4097  O O   . ILE B 145 ? 1.1817 1.9045 1.7023 -0.0235 0.0134  0.1125  145 ILE B O   
4098  C CB  . ILE B 145 ? 1.0304 1.7424 1.5306 -0.0178 0.0148  0.1235  145 ILE B CB  
4099  C CG1 . ILE B 145 ? 1.0472 1.7413 1.5470 -0.0167 0.0107  0.1227  145 ILE B CG1 
4100  C CG2 . ILE B 145 ? 0.9743 1.6932 1.4729 -0.0150 0.0137  0.1151  145 ILE B CG2 
4101  C CD1 . ILE B 145 ? 1.0452 1.7314 1.5364 -0.0118 0.0090  0.1214  145 ILE B CD1 
4102  N N   . LYS B 146 ? 1.1602 1.8653 1.6834 -0.0274 0.0125  0.1220  146 LYS B N   
4103  C CA  . LYS B 146 ? 1.2473 1.9487 1.7793 -0.0293 0.0089  0.1162  146 LYS B CA  
4104  C C   . LYS B 146 ? 1.3823 2.0736 1.9094 -0.0248 0.0035  0.1088  146 LYS B C   
4105  O O   . LYS B 146 ? 1.3118 1.9896 1.8320 -0.0224 0.0012  0.1098  146 LYS B O   
4106  C CB  . LYS B 146 ? 1.1924 1.8842 1.7308 -0.0335 0.0081  0.1208  146 LYS B CB  
4107  C CG  . LYS B 146 ? 1.1665 1.8673 1.7104 -0.0386 0.0135  0.1286  146 LYS B CG  
4108  C CD  . LYS B 146 ? 1.0762 1.7664 1.6273 -0.0431 0.0124  0.1327  146 LYS B CD  
4109  C CE  . LYS B 146 ? 0.9830 1.6820 1.5398 -0.0487 0.0182  0.1409  146 LYS B CE  
4110  N NZ  . LYS B 146 ? 0.8778 1.5661 1.4425 -0.0535 0.0171  0.1450  146 LYS B NZ  
4111  N N   . VAL B 147 ? 1.7990 2.4966 2.3295 -0.0236 0.0016  0.1014  147 VAL B N   
4112  C CA  . VAL B 147 ? 1.8216 2.5101 2.3475 -0.0197 -0.0036 0.0944  147 VAL B CA  
4113  C C   . VAL B 147 ? 1.9271 2.6148 2.4625 -0.0213 -0.0079 0.0887  147 VAL B C   
4114  O O   . VAL B 147 ? 1.9157 2.6128 2.4620 -0.0252 -0.0063 0.0892  147 VAL B O   
4115  C CB  . VAL B 147 ? 1.7924 2.4881 2.3118 -0.0157 -0.0026 0.0906  147 VAL B CB  
4116  C CG1 . VAL B 147 ? 1.7704 2.4686 2.2815 -0.0143 0.0014  0.0962  147 VAL B CG1 
4117  C CG2 . VAL B 147 ? 1.7785 2.4900 2.3056 -0.0167 -0.0009 0.0867  147 VAL B CG2 
4118  N N   . SER B 148 ? 2.0668 2.7431 2.5978 -0.0183 -0.0134 0.0831  148 SER B N   
4119  C CA  . SER B 148 ? 2.0723 2.7467 2.6111 -0.0191 -0.0187 0.0772  148 SER B CA  
4120  C C   . SER B 148 ? 2.0560 2.7452 2.6017 -0.0183 -0.0181 0.0723  148 SER B C   
4121  O O   . SER B 148 ? 2.0424 2.7387 2.5830 -0.0156 -0.0154 0.0713  148 SER B O   
4122  C CB  . SER B 148 ? 2.0860 2.7441 2.6164 -0.0156 -0.0248 0.0728  148 SER B CB  
4123  O OG  . SER B 148 ? 2.0809 2.7389 2.6022 -0.0112 -0.0248 0.0698  148 SER B OG  
4124  N N   . ALA B 149 ? 1.7498 2.4436 2.3077 -0.0207 -0.0209 0.0689  149 ALA B N   
4125  C CA  . ALA B 149 ? 1.6189 2.3267 2.1851 -0.0198 -0.0207 0.0636  149 ALA B CA  
4126  C C   . ALA B 149 ? 1.5083 2.2106 2.0676 -0.0145 -0.0254 0.0571  149 ALA B C   
4127  O O   . ALA B 149 ? 1.4586 2.1716 2.0205 -0.0124 -0.0241 0.0533  149 ALA B O   
4128  C CB  . ALA B 149 ? 1.5387 2.2524 2.1208 -0.0235 -0.0230 0.0614  149 ALA B CB  
4129  N N   . GLU B 150 ? 1.5091 2.1947 2.0597 -0.0123 -0.0308 0.0558  150 GLU B N   
4130  C CA  . GLU B 150 ? 1.3988 2.0776 1.9411 -0.0074 -0.0349 0.0506  150 GLU B CA  
4131  C C   . GLU B 150 ? 1.3752 2.0574 1.9080 -0.0048 -0.0302 0.0519  150 GLU B C   
4132  O O   . GLU B 150 ? 1.2904 1.9746 1.8207 -0.0014 -0.0316 0.0473  150 GLU B O   
4133  C CB  . GLU B 150 ? 1.2976 1.9573 1.8309 -0.0060 -0.0408 0.0496  150 GLU B CB  
4134  C CG  . GLU B 150 ? 1.1742 1.8278 1.7071 -0.0030 -0.0483 0.0430  150 GLU B CG  
4135  C CD  . GLU B 150 ? 1.1275 1.7815 1.6528 0.0014  -0.0481 0.0399  150 GLU B CD  
4136  O OE1 . GLU B 150 ? 1.1546 1.8057 1.6696 0.0027  -0.0439 0.0427  150 GLU B OE1 
4137  O OE2 . GLU B 150 ? 1.0735 1.7306 1.6036 0.0036  -0.0523 0.0347  150 GLU B OE2 
4138  N N   . ALA B 151 ? 1.4399 2.1228 1.9678 -0.0063 -0.0250 0.0580  151 ALA B N   
4139  C CA  . ALA B 151 ? 1.5253 2.2130 2.0453 -0.0042 -0.0205 0.0596  151 ALA B CA  
4140  C C   . ALA B 151 ? 1.5328 2.2392 2.0605 -0.0056 -0.0156 0.0596  151 ALA B C   
4141  O O   . ALA B 151 ? 1.5451 2.2593 2.0732 -0.0079 -0.0103 0.0649  151 ALA B O   
4142  C CB  . ALA B 151 ? 1.6146 2.2953 2.1265 -0.0048 -0.0176 0.0660  151 ALA B CB  
4143  N N   . ALA B 152 ? 1.6327 2.3460 2.1663 -0.0040 -0.0175 0.0534  152 ALA B N   
4144  C CA  . ALA B 152 ? 1.6349 2.3660 2.1764 -0.0049 -0.0131 0.0519  152 ALA B CA  
4145  C C   . ALA B 152 ? 1.6953 2.4315 2.2338 -0.0010 -0.0132 0.0463  152 ALA B C   
4146  O O   . ALA B 152 ? 1.6342 2.3848 2.1762 -0.0013 -0.0086 0.0453  152 ALA B O   
4147  C CB  . ALA B 152 ? 1.5552 2.2938 2.1115 -0.0074 -0.0146 0.0494  152 ALA B CB  
4148  N N   . SER B 153 ? 1.8781 2.6025 2.4100 0.0025  -0.0181 0.0425  153 SER B N   
4149  C CA  . SER B 153 ? 1.9055 2.6331 2.4341 0.0061  -0.0182 0.0373  153 SER B CA  
4150  C C   . SER B 153 ? 1.8534 2.5840 2.3729 0.0065  -0.0134 0.0403  153 SER B C   
4151  O O   . SER B 153 ? 1.8308 2.5698 2.3499 0.0083  -0.0115 0.0366  153 SER B O   
4152  C CB  . SER B 153 ? 1.9186 2.6313 2.4420 0.0094  -0.0247 0.0333  153 SER B CB  
4153  O OG  . SER B 153 ? 1.8833 2.5815 2.3959 0.0095  -0.0258 0.0372  153 SER B OG  
4154  N N   . GLN B 154 ? 1.6831 2.4070 2.1955 0.0051  -0.0118 0.0465  154 GLN B N   
4155  C CA  . GLN B 154 ? 1.6890 2.4157 2.1932 0.0057  -0.0079 0.0494  154 GLN B CA  
4156  C C   . GLN B 154 ? 1.7078 2.4520 2.2159 0.0041  -0.0026 0.0505  154 GLN B C   
4157  O O   . GLN B 154 ? 1.7086 2.4592 2.2124 0.0056  -0.0004 0.0487  154 GLN B O   
4158  C CB  . GLN B 154 ? 1.7253 2.4420 2.2229 0.0046  -0.0074 0.0560  154 GLN B CB  
4159  C CG  . GLN B 154 ? 1.6936 2.4069 2.1966 0.0015  -0.0080 0.0600  154 GLN B CG  
4160  C CD  . GLN B 154 ? 1.7061 2.4043 2.2084 0.0024  -0.0136 0.0577  154 GLN B CD  
4161  O OE1 . GLN B 154 ? 1.6983 2.3964 2.2063 0.0029  -0.0173 0.0527  154 GLN B OE1 
4162  N NE2 . GLN B 154 ? 1.7117 2.3970 2.2068 0.0026  -0.0145 0.0612  154 GLN B NE2 
4163  N N   . PHE B 155 ? 1.5821 2.3341 2.0980 0.0009  -0.0003 0.0532  155 PHE B N   
4164  C CA  . PHE B 155 ? 1.5032 2.2718 2.0221 -0.0008 0.0053  0.0545  155 PHE B CA  
4165  C C   . PHE B 155 ? 1.5450 2.3243 2.0757 -0.0016 0.0057  0.0495  155 PHE B C   
4166  O O   . PHE B 155 ? 1.5643 2.3506 2.0970 0.0008  0.0058  0.0430  155 PHE B O   
4167  C CB  . PHE B 155 ? 1.4338 2.2040 1.9511 -0.0043 0.0090  0.0632  155 PHE B CB  
4168  C CG  . PHE B 155 ? 1.4265 2.2132 1.9487 -0.0071 0.0147  0.0652  155 PHE B CG  
4169  C CD1 . PHE B 155 ? 1.5183 2.3172 2.0368 -0.0059 0.0182  0.0630  155 PHE B CD1 
4170  C CD2 . PHE B 155 ? 1.4204 2.2103 1.9508 -0.0111 0.0166  0.0691  155 PHE B CD2 
4171  C CE1 . PHE B 155 ? 1.5789 2.3929 2.1008 -0.0085 0.0237  0.0647  155 PHE B CE1 
4172  C CE2 . PHE B 155 ? 1.3938 2.1988 1.9283 -0.0140 0.0224  0.0711  155 PHE B CE2 
4173  C CZ  . PHE B 155 ? 1.4950 2.3121 2.0249 -0.0126 0.0261  0.0689  155 PHE B CZ  
4174  N N   . GLY B 156 ? 1.5741 2.3547 2.1135 -0.0048 0.0060  0.0521  156 GLY B N   
4175  C CA  . GLY B 156 ? 1.6060 2.3989 2.1580 -0.0062 0.0075  0.0482  156 GLY B CA  
4176  C C   . GLY B 156 ? 1.5527 2.3501 2.1118 -0.0113 0.0108  0.0543  156 GLY B C   
4177  O O   . GLY B 156 ? 1.5011 2.2872 2.0590 -0.0131 0.0085  0.0590  156 GLY B O   
4178  N N   . GLU B 157 ? 1.5428 2.3566 2.1089 -0.0135 0.0165  0.0541  157 GLU B N   
4179  C CA  . GLU B 157 ? 1.5535 2.3734 2.1283 -0.0188 0.0203  0.0593  157 GLU B CA  
4180  C C   . GLU B 157 ? 1.5024 2.3299 2.0702 -0.0216 0.0272  0.0669  157 GLU B C   
4181  O O   . GLU B 157 ? 1.4451 2.2804 2.0053 -0.0197 0.0306  0.0658  157 GLU B O   
4182  C CB  . GLU B 157 ? 1.5832 2.4166 2.1733 -0.0198 0.0218  0.0536  157 GLU B CB  
4183  N N   . LEU B 158 ? 1.4172 2.2416 1.9873 -0.0261 0.0291  0.0745  158 LEU B N   
4184  C CA  . LEU B 158 ? 1.3002 2.1309 1.8642 -0.0293 0.0356  0.0829  158 LEU B CA  
4185  C C   . LEU B 158 ? 1.3012 2.1326 1.8748 -0.0352 0.0381  0.0888  158 LEU B C   
4186  O O   . LEU B 158 ? 1.3723 2.1906 1.9488 -0.0365 0.0338  0.0910  158 LEU B O   
4187  C CB  . LEU B 158 ? 1.2691 2.0885 1.8186 -0.0272 0.0339  0.0883  158 LEU B CB  
4188  C CG  . LEU B 158 ? 1.2540 2.0802 1.7938 -0.0286 0.0395  0.0957  158 LEU B CG  
4189  C CD1 . LEU B 158 ? 1.1873 2.0051 1.7139 -0.0245 0.0366  0.0969  158 LEU B CD1 
4190  C CD2 . LEU B 158 ? 1.1965 2.0204 1.7386 -0.0338 0.0426  0.1054  158 LEU B CD2 
4191  N N   . ILE B 159 ? 1.2938 2.1402 1.8720 -0.0389 0.0454  0.0915  159 ILE B N   
4192  C CA  . ILE B 159 ? 1.2353 2.0846 1.8241 -0.0451 0.0488  0.0969  159 ILE B CA  
4193  C C   . ILE B 159 ? 1.1032 1.9547 1.6830 -0.0485 0.0550  0.1074  159 ILE B C   
4194  O O   . ILE B 159 ? 1.1047 1.9666 1.6758 -0.0474 0.0598  0.1084  159 ILE B O   
4195  C CB  . ILE B 159 ? 1.2731 2.1387 1.8768 -0.0473 0.0527  0.0911  159 ILE B CB  
4196  C CG1 . ILE B 159 ? 1.4418 2.3061 2.0535 -0.0429 0.0462  0.0803  159 ILE B CG1 
4197  C CG2 . ILE B 159 ? 1.1600 2.0277 1.7765 -0.0541 0.0557  0.0964  159 ILE B CG2 
4198  C CD1 . ILE B 159 ? 1.5366 2.3862 2.1551 -0.0434 0.0386  0.0793  159 ILE B CD1 
4199  N N   . ALA B 160 ? 0.9571 1.7985 1.5386 -0.0525 0.0545  0.1152  160 ALA B N   
4200  C CA  . ALA B 160 ? 0.8632 1.7049 1.4368 -0.0559 0.0598  0.1262  160 ALA B CA  
4201  C C   . ALA B 160 ? 0.8367 1.6745 1.4211 -0.0625 0.0615  0.1325  160 ALA B C   
4202  O O   . ALA B 160 ? 0.8331 1.6577 1.4235 -0.0631 0.0558  0.1315  160 ALA B O   
4203  C CB  . ALA B 160 ? 0.8292 1.6575 1.3878 -0.0522 0.0560  0.1307  160 ALA B CB  
4204  N N   . ASP B 161 ? 0.8540 1.7031 1.4405 -0.0678 0.0695  0.1388  161 ASP B N   
4205  C CA  . ASP B 161 ? 0.8001 1.6470 1.3975 -0.0749 0.0724  0.1453  161 ASP B CA  
4206  C C   . ASP B 161 ? 0.7308 1.5617 1.3199 -0.0763 0.0708  0.1557  161 ASP B C   
4207  O O   . ASP B 161 ? 0.7199 1.5522 1.2967 -0.0764 0.0748  0.1637  161 ASP B O   
4208  C CB  . ASP B 161 ? 0.6098 1.4747 1.2117 -0.0800 0.0822  0.1486  161 ASP B CB  
4209  N N   . PRO B 162 ? 0.6733 1.4889 1.2689 -0.0775 0.0650  0.1559  162 PRO B N   
4210  C CA  . PRO B 162 ? 0.6415 1.4402 1.2287 -0.0775 0.0624  0.1645  162 PRO B CA  
4211  C C   . PRO B 162 ? 0.5698 1.3688 1.1566 -0.0838 0.0688  0.1765  162 PRO B C   
4212  O O   . PRO B 162 ? 0.6033 1.3895 1.1815 -0.0832 0.0673  0.1845  162 PRO B O   
4213  C CB  . PRO B 162 ? 0.6697 1.4536 1.2659 -0.0775 0.0549  0.1599  162 PRO B CB  
4214  C CG  . PRO B 162 ? 0.6941 1.4887 1.3072 -0.0812 0.0559  0.1532  162 PRO B CG  
4215  C CD  . PRO B 162 ? 0.7083 1.5214 1.3195 -0.0787 0.0602  0.1480  162 PRO B CD  
4216  N N   . ASP B 163 ? 0.5456 1.3587 1.1416 -0.0896 0.0759  0.1782  163 ASP B N   
4217  C CA  . ASP B 163 ? 0.5011 1.3140 1.0960 -0.0959 0.0823  0.1903  163 ASP B CA  
4218  C C   . ASP B 163 ? 0.4920 1.3103 1.0692 -0.0936 0.0868  0.1974  163 ASP B C   
4219  O O   . ASP B 163 ? 0.5007 1.3087 1.0688 -0.0943 0.0870  0.2076  163 ASP B O   
4220  C CB  . ASP B 163 ? 0.5568 1.3834 1.1675 -0.1033 0.0890  0.1901  163 ASP B CB  
4221  C CG  . ASP B 163 ? 0.4922 1.3082 1.1183 -0.1091 0.0865  0.1916  163 ASP B CG  
4222  O OD1 . ASP B 163 ? 0.4947 1.2921 1.1176 -0.1078 0.0803  0.1944  163 ASP B OD1 
4223  O OD2 . ASP B 163 ? 0.5384 1.3649 1.1803 -0.1150 0.0905  0.1896  163 ASP B OD2 
4224  N N   . THR B 164 ? 0.5303 1.3645 1.1025 -0.0907 0.0901  0.1920  164 THR B N   
4225  C CA  . THR B 164 ? 0.5327 1.3729 1.0874 -0.0877 0.0934  0.1969  164 THR B CA  
4226  C C   . THR B 164 ? 0.5541 1.3894 1.0977 -0.0794 0.0867  0.1908  164 THR B C   
4227  O O   . THR B 164 ? 0.5512 1.3907 1.0801 -0.0763 0.0881  0.1940  164 THR B O   
4228  C CB  . THR B 164 ? 0.5794 1.4408 1.1343 -0.0900 0.1019  0.1948  164 THR B CB  
4229  O OG1 . THR B 164 ? 0.6116 1.4823 1.1751 -0.0869 0.1000  0.1816  164 THR B OG1 
4230  C CG2 . THR B 164 ? 0.5924 1.4594 1.1574 -0.0987 0.1096  0.2017  164 THR B CG2 
4231  N N   . LYS B 165 ? 0.6038 1.4304 1.1541 -0.0760 0.0795  0.1824  165 LYS B N   
4232  C CA  . LYS B 165 ? 0.5949 1.4167 1.1364 -0.0685 0.0733  0.1759  165 LYS B CA  
4233  C C   . LYS B 165 ? 0.5786 1.4166 1.1133 -0.0652 0.0762  0.1698  165 LYS B C   
4234  O O   . LYS B 165 ? 0.6038 1.4414 1.1257 -0.0603 0.0742  0.1696  165 LYS B O   
4235  C CB  . LYS B 165 ? 0.5748 1.3825 1.1040 -0.0656 0.0697  0.1835  165 LYS B CB  
4236  C CG  . LYS B 165 ? 0.5843 1.3752 1.1195 -0.0686 0.0669  0.1897  165 LYS B CG  
4237  C CD  . LYS B 165 ? 0.6768 1.4557 1.2189 -0.0656 0.0595  0.1813  165 LYS B CD  
4238  C CE  . LYS B 165 ? 0.8139 1.5843 1.3446 -0.0584 0.0540  0.1788  165 LYS B CE  
4239  N NZ  . LYS B 165 ? 0.8762 1.6316 1.4006 -0.0575 0.0518  0.1875  165 LYS B NZ  
4240  N N   . GLU B 166 ? 0.6517 1.5042 1.1960 -0.0678 0.0809  0.1643  166 GLU B N   
4241  C CA  . GLU B 166 ? 0.6087 1.4775 1.1479 -0.0652 0.0846  0.1582  166 GLU B CA  
4242  C C   . GLU B 166 ? 0.7174 1.5890 1.2650 -0.0612 0.0802  0.1452  166 GLU B C   
4243  O O   . GLU B 166 ? 0.7819 1.6514 1.3441 -0.0632 0.0782  0.1408  166 GLU B O   
4244  C CB  . GLU B 166 ? 0.6672 1.5520 1.2102 -0.0709 0.0941  0.1617  166 GLU B CB  
4245  C CG  . GLU B 166 ? 0.7485 1.6485 1.2797 -0.0687 0.0992  0.1600  166 GLU B CG  
4246  C CD  . GLU B 166 ? 0.8194 1.7334 1.3586 -0.0666 0.1008  0.1477  166 GLU B CD  
4247  O OE1 . GLU B 166 ? 0.8809 1.8026 1.4353 -0.0705 0.1045  0.1447  166 GLU B OE1 
4248  O OE2 . GLU B 166 ? 0.8284 1.7459 1.3593 -0.0610 0.0983  0.1409  166 GLU B OE2 
4249  N N   . LEU B 167 ? 0.6728 1.5488 1.2111 -0.0557 0.0785  0.1391  167 LEU B N   
4250  C CA  . LEU B 167 ? 0.8284 1.7060 1.3727 -0.0513 0.0740  0.1270  167 LEU B CA  
4251  C C   . LEU B 167 ? 0.9914 1.8854 1.5476 -0.0534 0.0792  0.1205  167 LEU B C   
4252  O O   . LEU B 167 ? 0.9942 1.9027 1.5454 -0.0533 0.0852  0.1192  167 LEU B O   
4253  C CB  . LEU B 167 ? 0.8305 1.7083 1.3614 -0.0453 0.0713  0.1230  167 LEU B CB  
4254  C CG  . LEU B 167 ? 1.0088 1.8873 1.5439 -0.0403 0.0667  0.1108  167 LEU B CG  
4255  C CD1 . LEU B 167 ? 0.9294 1.7942 1.4555 -0.0355 0.0597  0.1097  167 LEU B CD1 
4256  C CD2 . LEU B 167 ? 1.2412 2.1367 1.7739 -0.0387 0.0713  0.1044  167 LEU B CD2 
4257  N N   . LEU B 168 ? 0.9975 1.8896 1.5696 -0.0551 0.0769  0.1159  168 LEU B N   
4258  C CA  . LEU B 168 ? 1.0285 1.9362 1.6145 -0.0571 0.0815  0.1097  168 LEU B CA  
4259  C C   . LEU B 168 ? 1.2008 2.1148 1.7892 -0.0514 0.0787  0.0975  168 LEU B C   
4260  O O   . LEU B 168 ? 1.2247 2.1546 1.8206 -0.0519 0.0839  0.0920  168 LEU B O   
4261  C CB  . LEU B 168 ? 0.9183 1.8221 1.5216 -0.0617 0.0799  0.1102  168 LEU B CB  
4262  C CG  . LEU B 168 ? 0.8020 1.7145 1.4127 -0.0693 0.0881  0.1178  168 LEU B CG  
4263  C CD1 . LEU B 168 ? 0.7792 1.7129 1.3958 -0.0703 0.0963  0.1130  168 LEU B CD1 
4264  C CD2 . LEU B 168 ? 0.7551 1.6612 1.3512 -0.0718 0.0913  0.1300  168 LEU B CD2 
4265  N N   . HIS B 169 ? 1.5933 2.4954 2.1760 -0.0461 0.0709  0.0931  169 HIS B N   
4266  C CA  . HIS B 169 ? 1.5829 2.4888 2.1682 -0.0407 0.0675  0.0818  169 HIS B CA  
4267  C C   . HIS B 169 ? 1.5847 2.4762 2.1582 -0.0355 0.0603  0.0803  169 HIS B C   
4268  O O   . HIS B 169 ? 1.5904 2.4672 2.1594 -0.0360 0.0562  0.0860  169 HIS B O   
4269  C CB  . HIS B 169 ? 1.5782 2.4854 2.1818 -0.0410 0.0643  0.0748  169 HIS B CB  
4270  C CG  . HIS B 169 ? 1.6664 2.5713 2.2719 -0.0349 0.0583  0.0642  169 HIS B CG  
4271  N ND1 . HIS B 169 ? 1.7169 2.6057 2.3218 -0.0319 0.0495  0.0619  169 HIS B ND1 
4272  C CD2 . HIS B 169 ? 1.6821 2.5983 2.2897 -0.0312 0.0598  0.0555  169 HIS B CD2 
4273  C CE1 . HIS B 169 ? 1.7224 2.6122 2.3288 -0.0268 0.0458  0.0527  169 HIS B CE1 
4274  N NE2 . HIS B 169 ? 1.7141 2.6203 2.3226 -0.0261 0.0518  0.0485  169 HIS B NE2 
4275  N N   . TYR B 170 ? 1.4075 2.3034 1.9765 -0.0306 0.0590  0.0724  170 TYR B N   
4276  C CA  . TYR B 170 ? 1.3556 2.2393 1.9136 -0.0258 0.0529  0.0706  170 TYR B CA  
4277  C C   . TYR B 170 ? 1.3921 2.2792 1.9525 -0.0209 0.0501  0.0595  170 TYR B C   
4278  O O   . TYR B 170 ? 1.3661 2.2668 1.9257 -0.0197 0.0545  0.0550  170 TYR B O   
4279  C CB  . TYR B 170 ? 1.2915 2.1759 1.8337 -0.0256 0.0557  0.0769  170 TYR B CB  
4280  C CG  . TYR B 170 ? 1.3570 2.2326 1.8887 -0.0207 0.0505  0.0737  170 TYR B CG  
4281  C CD1 . TYR B 170 ? 1.4113 2.2703 1.9420 -0.0189 0.0438  0.0743  170 TYR B CD1 
4282  C CD2 . TYR B 170 ? 1.3484 2.2325 1.8715 -0.0179 0.0523  0.0698  170 TYR B CD2 
4283  C CE1 . TYR B 170 ? 1.4663 2.3176 1.9881 -0.0148 0.0396  0.0715  170 TYR B CE1 
4284  C CE2 . TYR B 170 ? 1.4638 2.3400 1.9784 -0.0138 0.0475  0.0668  170 TYR B CE2 
4285  C CZ  . TYR B 170 ? 1.5264 2.3864 2.0407 -0.0123 0.0414  0.0678  170 TYR B CZ  
4286  O OH  . TYR B 170 ? 1.5459 2.3981 2.0524 -0.0086 0.0372  0.0650  170 TYR B OH  
4287  N N   . THR B 171 ? 1.4582 2.3326 2.0213 -0.0179 0.0427  0.0553  171 THR B N   
4288  C CA  . THR B 171 ? 1.6986 2.5722 2.2620 -0.0127 0.0388  0.0457  171 THR B CA  
4289  C C   . THR B 171 ? 1.9689 2.8263 2.5216 -0.0097 0.0328  0.0465  171 THR B C   
4290  O O   . THR B 171 ? 1.8511 2.6950 2.4034 -0.0106 0.0287  0.0505  171 THR B O   
4291  C CB  . THR B 171 ? 1.6501 2.5245 2.2287 -0.0118 0.0355  0.0387  171 THR B CB  
4292  O OG1 . THR B 171 ? 1.6617 2.5268 2.2466 -0.0148 0.0324  0.0433  171 THR B OG1 
4293  C CG2 . THR B 171 ? 1.5070 2.4002 2.0960 -0.0130 0.0417  0.0345  171 THR B CG2 
4294  N N   . GLU B 172 ? 3.0332 3.8920 3.5773 -0.0062 0.0325  0.0423  172 GLU B N   
4295  C CA  . GLU B 172 ? 3.0386 3.8837 3.5721 -0.0037 0.0279  0.0435  172 GLU B CA  
4296  C C   . GLU B 172 ? 3.0344 3.8652 3.5717 -0.0013 0.0209  0.0398  172 GLU B C   
4297  O O   . GLU B 172 ? 3.0396 3.8573 3.5742 -0.0021 0.0177  0.0445  172 GLU B O   
4298  C CB  . GLU B 172 ? 3.0387 3.8896 3.5639 -0.0007 0.0290  0.0391  172 GLU B CB  
4299  C CG  . GLU B 172 ? 3.0349 3.9025 3.5651 -0.0003 0.0336  0.0328  172 GLU B CG  
4300  C CD  . GLU B 172 ? 3.0336 3.9011 3.5742 0.0026  0.0304  0.0235  172 GLU B CD  
4301  O OE1 . GLU B 172 ? 3.0314 3.8869 3.5704 0.0057  0.0246  0.0199  172 GLU B OE1 
4302  O OE2 . GLU B 172 ? 3.0316 3.9111 3.5822 0.0019  0.0338  0.0200  172 GLU B OE2 
4303  N N   . LYS B 173 ? 2.2998 3.1325 2.8430 0.0017  0.0184  0.0312  173 LYS B N   
4304  C CA  . LYS B 173 ? 1.9839 2.8022 2.5285 0.0044  0.0115  0.0276  173 LYS B CA  
4305  C C   . LYS B 173 ? 1.9313 2.7514 2.4897 0.0043  0.0089  0.0237  173 LYS B C   
4306  O O   . LYS B 173 ? 1.7790 2.5874 2.3395 0.0038  0.0041  0.0255  173 LYS B O   
4307  C CB  . LYS B 173 ? 1.8156 2.6306 2.3547 0.0087  0.0090  0.0212  173 LYS B CB  
4308  C CG  . LYS B 173 ? 1.6016 2.3996 2.1310 0.0102  0.0045  0.0233  173 LYS B CG  
4309  C CD  . LYS B 173 ? 1.5358 2.3319 2.0558 0.0080  0.0072  0.0312  173 LYS B CD  
4310  C CE  . LYS B 173 ? 1.3127 2.0916 1.8250 0.0091  0.0031  0.0339  173 LYS B CE  
4311  N NZ  . LYS B 173 ? 1.4156 2.1835 1.9321 0.0084  -0.0009 0.0351  173 LYS B NZ  
4312  N N   . PRO B 174 ? 1.9081 2.7426 2.4764 0.0047  0.0118  0.0182  174 PRO B N   
4313  C CA  . PRO B 174 ? 1.7987 2.6359 2.3817 0.0043  0.0094  0.0149  174 PRO B CA  
4314  C C   . PRO B 174 ? 1.7064 2.5451 2.2947 -0.0008 0.0116  0.0219  174 PRO B C   
4315  O O   . PRO B 174 ? 1.6539 2.5064 2.2467 -0.0041 0.0182  0.0244  174 PRO B O   
4316  C CB  . PRO B 174 ? 1.7724 2.6266 2.3642 0.0059  0.0135  0.0079  174 PRO B CB  
4317  C CG  . PRO B 174 ? 1.8959 2.7517 2.4765 0.0084  0.0155  0.0055  174 PRO B CG  
4318  C CD  . PRO B 174 ? 1.9955 2.8442 2.5628 0.0061  0.0169  0.0138  174 PRO B CD  
4319  N N   . GLU B 175 ? 1.7303 2.5546 2.3179 -0.0015 0.0061  0.0250  175 GLU B N   
4320  C CA  . GLU B 175 ? 1.7125 2.5356 2.3037 -0.0065 0.0076  0.0320  175 GLU B CA  
4321  C C   . GLU B 175 ? 1.7547 2.5895 2.3632 -0.0091 0.0090  0.0296  175 GLU B C   
4322  O O   . GLU B 175 ? 1.7705 2.6173 2.3839 -0.0132 0.0157  0.0334  175 GLU B O   
4323  C CB  . GLU B 175 ? 1.7025 2.5063 2.2877 -0.0063 0.0011  0.0350  175 GLU B CB  
4324  C CG  . GLU B 175 ? 1.8119 2.6058 2.3998 -0.0024 -0.0069 0.0285  175 GLU B CG  
4325  C CD  . GLU B 175 ? 1.8588 2.6338 2.4391 -0.0023 -0.0126 0.0316  175 GLU B CD  
4326  O OE1 . GLU B 175 ? 1.7804 2.5510 2.3560 -0.0055 -0.0104 0.0385  175 GLU B OE1 
4327  O OE2 . GLU B 175 ? 1.9390 2.7033 2.5176 0.0010  -0.0194 0.0273  175 GLU B OE2 
4328  N N   . THR B 176 ? 1.6910 2.5229 2.3091 -0.0066 0.0028  0.0233  176 THR B N   
4329  C CA  . THR B 176 ? 1.6600 2.5020 2.2962 -0.0088 0.0028  0.0205  176 THR B CA  
4330  C C   . THR B 176 ? 1.6645 2.5065 2.3051 -0.0151 0.0055  0.0280  176 THR B C   
4331  O O   . THR B 176 ? 1.6450 2.5005 2.2914 -0.0192 0.0129  0.0312  176 THR B O   
4332  C CB  . THR B 176 ? 1.6174 2.4790 2.2627 -0.0080 0.0089  0.0153  176 THR B CB  
4333  O OG1 . THR B 176 ? 1.6251 2.4860 2.2614 -0.0029 0.0085  0.0104  176 THR B OG1 
4334  C CG2 . THR B 176 ? 1.5475 2.4171 2.2122 -0.0075 0.0059  0.0090  176 THR B CG2 
4335  N N   . PHE B 177 ? 1.6215 2.4470 2.2580 -0.0158 -0.0008 0.0309  177 PHE B N   
4336  C CA  . PHE B 177 ? 1.6100 2.4308 2.2487 -0.0213 0.0002  0.0380  177 PHE B CA  
4337  C C   . PHE B 177 ? 1.6600 2.4791 2.2856 -0.0236 0.0063  0.0463  177 PHE B C   
4338  O O   . PHE B 177 ? 1.6558 2.4871 2.2785 -0.0238 0.0132  0.0474  177 PHE B O   
4339  C CB  . PHE B 177 ? 1.5744 2.4093 2.2320 -0.0259 0.0033  0.0374  177 PHE B CB  
4340  C CG  . PHE B 177 ? 1.5935 2.4257 2.2536 -0.0323 0.0060  0.0454  177 PHE B CG  
4341  C CD1 . PHE B 177 ? 1.5863 2.4039 2.2478 -0.0339 -0.0007 0.0469  177 PHE B CD1 
4342  C CD2 . PHE B 177 ? 1.6199 2.4635 2.2806 -0.0368 0.0152  0.0514  177 PHE B CD2 
4343  C CE1 . PHE B 177 ? 1.6221 2.4364 2.2863 -0.0398 0.0017  0.0540  177 PHE B CE1 
4344  C CE2 . PHE B 177 ? 1.6291 2.4693 2.2921 -0.0428 0.0178  0.0592  177 PHE B CE2 
4345  C CZ  . PHE B 177 ? 1.6374 2.4628 2.3026 -0.0443 0.0110  0.0603  177 PHE B CZ  
4346  N N   . VAL B 178 ? 1.7180 2.5220 2.3357 -0.0250 0.0036  0.0519  178 VAL B N   
4347  C CA  . VAL B 178 ? 1.7603 2.5602 2.3648 -0.0262 0.0080  0.0596  178 VAL B CA  
4348  C C   . VAL B 178 ? 1.8585 2.6564 2.4673 -0.0322 0.0107  0.0673  178 VAL B C   
4349  O O   . VAL B 178 ? 1.7979 2.6003 2.4208 -0.0358 0.0102  0.0665  178 VAL B O   
4350  C CB  . VAL B 178 ? 1.7146 2.4977 2.3043 -0.0221 0.0031  0.0597  178 VAL B CB  
4351  C CG1 . VAL B 178 ? 1.6445 2.4289 2.2303 -0.0167 0.0006  0.0524  178 VAL B CG1 
4352  C CG2 . VAL B 178 ? 1.7015 2.4685 2.2924 -0.0227 -0.0038 0.0598  178 VAL B CG2 
4353  N N   . SER B 179 ? 2.3081 3.0994 2.9055 -0.0332 0.0134  0.0749  179 SER B N   
4354  C CA  . SER B 179 ? 2.3227 3.1104 2.9230 -0.0386 0.0159  0.0829  179 SER B CA  
4355  C C   . SER B 179 ? 2.3338 3.1041 2.9220 -0.0376 0.0132  0.0883  179 SER B C   
4356  O O   . SER B 179 ? 2.3448 3.1121 2.9322 -0.0414 0.0163  0.0961  179 SER B O   
4357  C CB  . SER B 179 ? 2.3184 3.1210 2.9199 -0.0423 0.0248  0.0887  179 SER B CB  
4358  O OG  . SER B 179 ? 2.3288 3.1365 2.9436 -0.0484 0.0275  0.0918  179 SER B OG  
4359  N N   . ASP B 180 ? 1.7461 2.5052 2.3250 -0.0326 0.0079  0.0844  180 ASP B N   
4360  C CA  . ASP B 180 ? 1.5618 2.3042 2.1295 -0.0308 0.0050  0.0879  180 ASP B CA  
4361  C C   . ASP B 180 ? 1.4266 2.1707 1.9829 -0.0298 0.0098  0.0943  180 ASP B C   
4362  O O   . ASP B 180 ? 1.3784 2.1100 1.9251 -0.0277 0.0079  0.0971  180 ASP B O   
4363  C CB  . ASP B 180 ? 1.5339 2.2645 2.1067 -0.0345 0.0023  0.0913  180 ASP B CB  
4364  C CG  . ASP B 180 ? 1.4522 2.1787 2.0204 -0.0372 0.0064  0.1008  180 ASP B CG  
4365  O OD1 . ASP B 180 ? 1.4419 2.1552 2.0000 -0.0348 0.0044  0.1033  180 ASP B OD1 
4366  O OD2 . ASP B 180 ? 1.4273 2.1635 2.0018 -0.0418 0.0116  0.1059  180 ASP B OD2 
4367  N N   . LEU B 181 ? 1.3825 2.1420 1.9393 -0.0309 0.0158  0.0962  181 LEU B N   
4368  C CA  . LEU B 181 ? 1.1684 1.9309 1.7144 -0.0299 0.0199  0.1020  181 LEU B CA  
4369  C C   . LEU B 181 ? 1.0915 1.8612 1.6308 -0.0254 0.0201  0.0965  181 LEU B C   
4370  O O   . LEU B 181 ? 1.1390 1.9171 1.6841 -0.0243 0.0197  0.0894  181 LEU B O   
4371  C CB  . LEU B 181 ? 1.1430 1.9170 1.6922 -0.0346 0.0266  0.1090  181 LEU B CB  
4372  C CG  . LEU B 181 ? 1.0716 1.8372 1.6244 -0.0391 0.0273  0.1170  181 LEU B CG  
4373  C CD1 . LEU B 181 ? 0.8833 1.6604 1.4371 -0.0436 0.0345  0.1246  181 LEU B CD1 
4374  C CD2 . LEU B 181 ? 1.0715 1.8209 1.6146 -0.0365 0.0240  0.1210  181 LEU B CD2 
4375  N N   . ILE B 182 ? 1.1073 1.8735 1.6351 -0.0227 0.0206  0.0996  182 ILE B N   
4376  C CA  . ILE B 182 ? 1.0775 1.8485 1.5982 -0.0184 0.0203  0.0946  182 ILE B CA  
4377  C C   . ILE B 182 ? 1.0234 1.7995 1.5345 -0.0180 0.0240  0.1006  182 ILE B C   
4378  O O   . ILE B 182 ? 1.0024 1.7741 1.5108 -0.0198 0.0253  0.1086  182 ILE B O   
4379  C CB  . ILE B 182 ? 1.0522 1.8095 1.5681 -0.0143 0.0146  0.0897  182 ILE B CB  
4380  C CG1 . ILE B 182 ? 1.0306 1.7731 1.5414 -0.0142 0.0127  0.0954  182 ILE B CG1 
4381  C CG2 . ILE B 182 ? 1.1331 1.8873 1.6570 -0.0139 0.0105  0.0825  182 ILE B CG2 
4382  C CD1 . ILE B 182 ? 1.0610 1.7938 1.5628 -0.0099 0.0097  0.0930  182 ILE B CD1 
4383  N N   . ASN B 183 ? 1.0358 1.8215 1.5422 -0.0154 0.0253  0.0965  183 ASN B N   
4384  C CA  . ASN B 183 ? 0.9612 1.7517 1.4578 -0.0143 0.0277  0.1012  183 ASN B CA  
4385  C C   . ASN B 183 ? 0.9515 1.7287 1.4411 -0.0116 0.0242  0.1038  183 ASN B C   
4386  O O   . ASN B 183 ? 0.9310 1.6965 1.4214 -0.0096 0.0201  0.1000  183 ASN B O   
4387  C CB  . ASN B 183 ? 0.9479 1.7507 1.4412 -0.0120 0.0291  0.0950  183 ASN B CB  
4388  C CG  . ASN B 183 ? 1.1112 1.9279 1.6116 -0.0142 0.0329  0.0912  183 ASN B CG  
4389  O OD1 . ASN B 183 ? 1.2153 2.0315 1.7244 -0.0141 0.0312  0.0851  183 ASN B OD1 
4390  N ND2 . ASN B 183 ? 1.0604 1.8898 1.5571 -0.0159 0.0380  0.0948  183 ASN B ND2 
4391  N N   . CYS B 184 ? 0.9264 1.7055 1.4088 -0.0114 0.0259  0.1106  184 CYS B N   
4392  C CA  . CYS B 184 ? 0.8534 1.6226 1.3292 -0.0083 0.0232  0.1130  184 CYS B CA  
4393  C C   . CYS B 184 ? 0.7965 1.5738 1.2647 -0.0056 0.0236  0.1118  184 CYS B C   
4394  O O   . CYS B 184 ? 0.8492 1.6195 1.3132 -0.0026 0.0210  0.1115  184 CYS B O   
4395  C CB  . CYS B 184 ? 0.9079 1.6695 1.3828 -0.0099 0.0238  0.1226  184 CYS B CB  
4396  S SG  . CYS B 184 ? 0.8822 1.6285 1.3648 -0.0120 0.0214  0.1234  184 CYS B SG  
4397  N N   . GLY B 185 ? 0.7811 1.5731 1.2476 -0.0065 0.0267  0.1107  185 GLY B N   
4398  C CA  . GLY B 185 ? 0.7815 1.5820 1.2408 -0.0041 0.0268  0.1088  185 GLY B CA  
4399  C C   . GLY B 185 ? 0.7677 1.5724 1.2199 -0.0043 0.0281  0.1174  185 GLY B C   
4400  O O   . GLY B 185 ? 0.7513 1.5662 1.1973 -0.0030 0.0287  0.1161  185 GLY B O   
4401  N N   . VAL B 186 ? 0.7841 1.5812 1.2367 -0.0057 0.0284  0.1259  186 VAL B N   
4402  C CA  . VAL B 186 ? 0.7857 1.5855 1.2317 -0.0057 0.0293  0.1349  186 VAL B CA  
4403  C C   . VAL B 186 ? 0.7547 1.5643 1.2001 -0.0097 0.0340  0.1399  186 VAL B C   
4404  O O   . VAL B 186 ? 0.7610 1.5665 1.2124 -0.0131 0.0359  0.1431  186 VAL B O   
4405  C CB  . VAL B 186 ? 0.8515 1.6371 1.2982 -0.0048 0.0269  0.1416  186 VAL B CB  
4406  C CG1 . VAL B 186 ? 0.8358 1.6105 1.2906 -0.0071 0.0267  0.1410  186 VAL B CG1 
4407  C CG2 . VAL B 186 ? 0.7833 1.5711 1.2247 -0.0057 0.0283  0.1523  186 VAL B CG2 
4408  N N   . TYR B 187 ? 0.6642 1.4869 1.1024 -0.0095 0.0360  0.1402  187 TYR B N   
4409  C CA  . TYR B 187 ? 0.5657 1.3995 1.0020 -0.0132 0.0413  0.1439  187 TYR B CA  
4410  C C   . TYR B 187 ? 0.4755 1.3134 0.9015 -0.0131 0.0420  0.1534  187 TYR B C   
4411  O O   . TYR B 187 ? 0.5333 1.3701 0.9531 -0.0096 0.0384  0.1543  187 TYR B O   
4412  C CB  . TYR B 187 ? 0.5925 1.4396 1.0288 -0.0131 0.0436  0.1346  187 TYR B CB  
4413  C CG  . TYR B 187 ? 0.6355 1.4790 1.0815 -0.0125 0.0422  0.1248  187 TYR B CG  
4414  C CD1 . TYR B 187 ? 0.6452 1.4963 1.0912 -0.0104 0.0417  0.1148  187 TYR B CD1 
4415  C CD2 . TYR B 187 ? 0.6929 1.5248 1.1478 -0.0139 0.0408  0.1256  187 TYR B CD2 
4416  C CE1 . TYR B 187 ? 0.7131 1.5602 1.1676 -0.0096 0.0400  0.1063  187 TYR B CE1 
4417  C CE2 . TYR B 187 ? 0.7413 1.5695 1.2042 -0.0131 0.0389  0.1170  187 TYR B CE2 
4418  C CZ  . TYR B 187 ? 0.7648 1.6006 1.2275 -0.0109 0.0385  0.1076  187 TYR B CZ  
4419  O OH  . TYR B 187 ? 0.8339 1.6654 1.3043 -0.0099 0.0362  0.0995  187 TYR B OH  
4420  N N   . VAL B 188 ? 0.4408 1.2838 0.8651 -0.0170 0.0468  0.1604  188 VAL B N   
4421  C CA  . VAL B 188 ? 0.4534 1.3012 0.8668 -0.0174 0.0481  0.1699  188 VAL B CA  
4422  C C   . VAL B 188 ? 0.4608 1.3222 0.8711 -0.0213 0.0546  0.1709  188 VAL B C   
4423  O O   . VAL B 188 ? 0.4764 1.3377 0.8945 -0.0254 0.0588  0.1718  188 VAL B O   
4424  C CB  . VAL B 188 ? 0.4610 1.2963 0.8749 -0.0183 0.0469  0.1814  188 VAL B CB  
4425  C CG1 . VAL B 188 ? 0.4901 1.3166 0.9154 -0.0220 0.0487  0.1821  188 VAL B CG1 
4426  C CG2 . VAL B 188 ? 0.4762 1.3174 0.8796 -0.0202 0.0497  0.1920  188 VAL B CG2 
4427  N N   . PHE B 189 ? 0.4666 1.3399 0.8658 -0.0201 0.0557  0.1702  189 PHE B N   
4428  C CA  . PHE B 189 ? 0.4745 1.3618 0.8693 -0.0234 0.0623  0.1705  189 PHE B CA  
4429  C C   . PHE B 189 ? 0.4909 1.3816 0.8725 -0.0247 0.0642  0.1821  189 PHE B C   
4430  O O   . PHE B 189 ? 0.4958 1.3778 0.8728 -0.0228 0.0600  0.1901  189 PHE B O   
4431  C CB  . PHE B 189 ? 0.4687 1.3682 0.8613 -0.0212 0.0627  0.1585  189 PHE B CB  
4432  C CG  . PHE B 189 ? 0.5152 1.4108 0.9200 -0.0198 0.0606  0.1474  189 PHE B CG  
4433  C CD1 . PHE B 189 ? 0.5444 1.4443 0.9592 -0.0226 0.0651  0.1424  189 PHE B CD1 
4434  C CD2 . PHE B 189 ? 0.4873 1.3749 0.8940 -0.0156 0.0542  0.1423  189 PHE B CD2 
4435  C CE1 . PHE B 189 ? 0.5156 1.4115 0.9412 -0.0210 0.0626  0.1326  189 PHE B CE1 
4436  C CE2 . PHE B 189 ? 0.4827 1.3661 0.8995 -0.0144 0.0522  0.1327  189 PHE B CE2 
4437  C CZ  . PHE B 189 ? 0.5310 1.4183 0.9571 -0.0169 0.0561  0.1279  189 PHE B CZ  
4438  N N   . THR B 190 ? 0.5000 1.4036 0.8755 -0.0277 0.0706  0.1829  190 THR B N   
4439  C CA  . THR B 190 ? 0.5168 1.4263 0.8771 -0.0286 0.0727  0.1924  190 THR B CA  
4440  C C   . THR B 190 ? 0.6271 1.5494 0.9761 -0.0253 0.0716  0.1851  190 THR B C   
4441  O O   . THR B 190 ? 0.5065 1.4323 0.8604 -0.0227 0.0694  0.1731  190 THR B O   
4442  C CB  . THR B 190 ? 0.5484 1.4631 0.9085 -0.0346 0.0812  0.1993  190 THR B CB  
4443  O OG1 . THR B 190 ? 0.5681 1.4874 0.9120 -0.0355 0.0831  0.2095  190 THR B OG1 
4444  C CG2 . THR B 190 ? 0.5251 1.4535 0.8902 -0.0365 0.0873  0.1889  190 THR B CG2 
4445  N N   . SER B 191 ? 0.7109 1.6398 1.0442 -0.0256 0.0728  0.1923  191 SER B N   
4446  C CA  . SER B 191 ? 0.7158 1.6571 1.0373 -0.0227 0.0715  0.1854  191 SER B CA  
4447  C C   . SER B 191 ? 0.7026 1.6573 1.0259 -0.0245 0.0781  0.1750  191 SER B C   
4448  O O   . SER B 191 ? 0.7021 1.6666 1.0184 -0.0218 0.0768  0.1664  191 SER B O   
4449  C CB  . SER B 191 ? 0.7697 1.7150 1.0730 -0.0226 0.0713  0.1960  191 SER B CB  
4450  O OG  . SER B 191 ? 0.8819 1.8392 1.1733 -0.0198 0.0696  0.1889  191 SER B OG  
4451  N N   . ASP B 192 ? 0.6481 1.6038 0.9815 -0.0288 0.0848  0.1753  192 ASP B N   
4452  C CA  . ASP B 192 ? 0.6405 1.6094 0.9769 -0.0307 0.0918  0.1662  192 ASP B CA  
4453  C C   . ASP B 192 ? 0.6479 1.6167 0.9976 -0.0279 0.0891  0.1519  192 ASP B C   
4454  O O   . ASP B 192 ? 0.6533 1.6328 1.0068 -0.0286 0.0941  0.1429  192 ASP B O   
4455  C CB  . ASP B 192 ? 0.6310 1.6013 0.9742 -0.0366 0.1001  0.1727  192 ASP B CB  
4456  C CG  . ASP B 192 ? 0.7449 1.7315 1.0871 -0.0390 0.1089  0.1661  192 ASP B CG  
4457  O OD1 . ASP B 192 ? 0.7531 1.7503 1.0857 -0.0362 0.1089  0.1583  192 ASP B OD1 
4458  O OD2 . ASP B 192 ? 0.7785 1.7676 1.1304 -0.0437 0.1159  0.1683  192 ASP B OD2 
4459  N N   . ILE B 193 ? 0.6675 1.6243 1.0241 -0.0247 0.0814  0.1496  193 ILE B N   
4460  C CA  . ILE B 193 ? 0.6603 1.6152 1.0296 -0.0224 0.0789  0.1371  193 ILE B CA  
4461  C C   . ILE B 193 ? 0.6902 1.6557 1.0532 -0.0191 0.0777  0.1257  193 ILE B C   
4462  O O   . ILE B 193 ? 0.6928 1.6626 1.0644 -0.0183 0.0792  0.1146  193 ILE B O   
4463  C CB  . ILE B 193 ? 0.6671 1.6060 1.0442 -0.0200 0.0714  0.1382  193 ILE B CB  
4464  C CG1 . ILE B 193 ? 0.7040 1.6401 1.0933 -0.0177 0.0687  0.1259  193 ILE B CG1 
4465  C CG2 . ILE B 193 ? 0.7425 1.6778 1.1086 -0.0166 0.0651  0.1421  193 ILE B CG2 
4466  C CD1 . ILE B 193 ? 0.7570 1.6969 1.1585 -0.0206 0.0740  0.1212  193 ILE B CD1 
4467  N N   . PHE B 194 ? 0.6835 1.6531 1.0316 -0.0171 0.0750  0.1280  194 PHE B N   
4468  C CA  . PHE B 194 ? 0.7053 1.6848 1.0471 -0.0140 0.0736  0.1169  194 PHE B CA  
4469  C C   . PHE B 194 ? 0.7403 1.7343 1.0795 -0.0160 0.0817  0.1112  194 PHE B C   
4470  O O   . PHE B 194 ? 0.7783 1.7796 1.1184 -0.0138 0.0817  0.0990  194 PHE B O   
4471  C CB  . PHE B 194 ? 0.7271 1.7085 1.0533 -0.0117 0.0687  0.1212  194 PHE B CB  
4472  C CG  . PHE B 194 ? 0.7120 1.6806 1.0411 -0.0091 0.0605  0.1250  194 PHE B CG  
4473  C CD1 . PHE B 194 ? 0.7055 1.6694 1.0424 -0.0059 0.0549  0.1155  194 PHE B CD1 
4474  C CD2 . PHE B 194 ? 0.7132 1.6746 1.0375 -0.0097 0.0586  0.1382  194 PHE B CD2 
4475  C CE1 . PHE B 194 ? 0.7295 1.6824 1.0694 -0.0035 0.0480  0.1189  194 PHE B CE1 
4476  C CE2 . PHE B 194 ? 0.6605 1.6108 0.9882 -0.0070 0.0514  0.1413  194 PHE B CE2 
4477  C CZ  . PHE B 194 ? 0.6968 1.6432 1.0323 -0.0039 0.0463  0.1316  194 PHE B CZ  
4478  N N   . ASN B 195 ? 0.7145 1.7130 1.0510 -0.0202 0.0889  0.1196  195 ASN B N   
4479  C CA  . ASN B 195 ? 0.7756 1.7885 1.1106 -0.0224 0.0976  0.1144  195 ASN B CA  
4480  C C   . ASN B 195 ? 0.8012 1.8147 1.1546 -0.0228 0.1004  0.1050  195 ASN B C   
4481  O O   . ASN B 195 ? 0.8665 1.8917 1.2213 -0.0224 0.1052  0.0952  195 ASN B O   
4482  C CB  . ASN B 195 ? 0.7283 1.7452 1.0554 -0.0271 0.1048  0.1268  195 ASN B CB  
4483  C CG  . ASN B 195 ? 0.7096 1.7246 1.0185 -0.0266 0.1016  0.1374  195 ASN B CG  
4484  O OD1 . ASN B 195 ? 0.7795 1.7970 1.0780 -0.0229 0.0962  0.1332  195 ASN B OD1 
4485  N ND2 . ASN B 195 ? 0.7193 1.7298 1.0247 -0.0303 0.1046  0.1513  195 ASN B ND2 
4486  N N   . ALA B 196 ? 0.7462 1.7473 1.1137 -0.0234 0.0973  0.1076  196 ALA B N   
4487  C CA  . ALA B 196 ? 0.7747 1.7756 1.1599 -0.0235 0.0988  0.0989  196 ALA B CA  
4488  C C   . ALA B 196 ? 0.8704 1.8711 1.2594 -0.0188 0.0937  0.0853  196 ALA B C   
4489  O O   . ALA B 196 ? 0.8999 1.9057 1.2998 -0.0181 0.0961  0.0755  196 ALA B O   
4490  C CB  . ALA B 196 ? 0.8084 1.7954 1.2064 -0.0255 0.0962  0.1054  196 ALA B CB  
4491  N N   . ILE B 197 ? 0.8598 1.8548 1.2406 -0.0154 0.0866  0.0846  197 ILE B N   
4492  C CA  . ILE B 197 ? 0.8927 1.8870 1.2765 -0.0112 0.0817  0.0721  197 ILE B CA  
4493  C C   . ILE B 197 ? 1.0025 2.0117 1.3781 -0.0100 0.0857  0.0632  197 ILE B C   
4494  O O   . ILE B 197 ? 1.1272 2.1396 1.5096 -0.0076 0.0853  0.0511  197 ILE B O   
4495  C CB  . ILE B 197 ? 0.8564 1.8403 1.2350 -0.0085 0.0732  0.0743  197 ILE B CB  
4496  C CG1 . ILE B 197 ? 0.8080 1.7774 1.1935 -0.0097 0.0700  0.0837  197 ILE B CG1 
4497  C CG2 . ILE B 197 ? 0.9707 1.9523 1.3541 -0.0046 0.0681  0.0617  197 ILE B CG2 
4498  C CD1 . ILE B 197 ? 0.8179 1.7768 1.2000 -0.0069 0.0620  0.0859  197 ILE B CD1 
4499  N N   . GLU B 198 ? 0.9933 2.0117 1.3540 -0.0117 0.0895  0.0690  198 GLU B N   
4500  C CA  . GLU B 198 ? 1.0345 2.0676 1.3860 -0.0108 0.0940  0.0608  198 GLU B CA  
4501  C C   . GLU B 198 ? 1.0451 2.0876 1.4071 -0.0123 0.1022  0.0545  198 GLU B C   
4502  O O   . GLU B 198 ? 1.0728 2.1250 1.4341 -0.0103 0.1047  0.0431  198 GLU B O   
4503  C CB  . GLU B 198 ? 1.0425 2.0824 1.3746 -0.0124 0.0964  0.0697  198 GLU B CB  
4504  C CG  . GLU B 198 ? 1.0545 2.0869 1.3766 -0.0102 0.0877  0.0745  198 GLU B CG  
4505  C CD  . GLU B 198 ? 1.0980 2.1374 1.4000 -0.0112 0.0891  0.0825  198 GLU B CD  
4506  O OE1 . GLU B 198 ? 1.0787 2.1276 1.3740 -0.0141 0.0973  0.0861  198 GLU B OE1 
4507  O OE2 . GLU B 198 ? 1.1425 2.1781 1.4354 -0.0090 0.0819  0.0852  198 GLU B OE2 
4508  N N   . GLU B 199 ? 0.9992 2.0391 1.3714 -0.0159 0.1064  0.0616  199 GLU B N   
4509  C CA  . GLU B 199 ? 0.9736 2.0222 1.3583 -0.0174 0.1138  0.0558  199 GLU B CA  
4510  C C   . GLU B 199 ? 1.0143 2.0575 1.4166 -0.0144 0.1098  0.0451  199 GLU B C   
4511  O O   . GLU B 199 ? 1.0184 2.0688 1.4328 -0.0149 0.1149  0.0388  199 GLU B O   
4512  C CB  . GLU B 199 ? 0.9171 1.9653 1.3071 -0.0227 0.1196  0.0674  199 GLU B CB  
4513  C CG  . GLU B 199 ? 0.9395 1.9948 1.3122 -0.0260 0.1252  0.0778  199 GLU B CG  
4514  C CD  . GLU B 199 ? 1.0575 2.1288 1.4182 -0.0250 0.1312  0.0704  199 GLU B CD  
4515  O OE1 . GLU B 199 ? 1.1015 2.1830 1.4717 -0.0248 0.1370  0.0608  199 GLU B OE1 
4516  O OE2 . GLU B 199 ? 1.0710 2.1448 1.4129 -0.0242 0.1297  0.0738  199 GLU B OE2 
4517  N N   . VAL B 200 ? 1.0665 2.0970 1.4705 -0.0114 0.1008  0.0431  200 VAL B N   
4518  C CA  . VAL B 200 ? 1.1605 2.1853 1.5782 -0.0081 0.0964  0.0323  200 VAL B CA  
4519  C C   . VAL B 200 ? 1.3247 2.3483 1.7360 -0.0037 0.0907  0.0229  200 VAL B C   
4520  O O   . VAL B 200 ? 1.3318 2.3548 1.7524 -0.0007 0.0889  0.0117  200 VAL B O   
4521  C CB  . VAL B 200 ? 1.1322 2.1414 1.5615 -0.0087 0.0909  0.0377  200 VAL B CB  
4522  C CG1 . VAL B 200 ? 1.1910 2.1877 1.6122 -0.0071 0.0831  0.0424  200 VAL B CG1 
4523  C CG2 . VAL B 200 ? 1.1387 2.1445 1.5846 -0.0063 0.0888  0.0277  200 VAL B CG2 
4524  N N   . TYR B 201 ? 1.8375 2.8607 2.2334 -0.0033 0.0877  0.0268  201 TYR B N   
4525  C CA  . TYR B 201 ? 1.8390 2.8620 2.2284 0.0004  0.0824  0.0178  201 TYR B CA  
4526  C C   . TYR B 201 ? 1.8561 2.8943 2.2351 0.0012  0.0874  0.0103  201 TYR B C   
4527  O O   . TYR B 201 ? 1.8533 2.8939 2.2333 0.0043  0.0853  -0.0017 201 TYR B O   
4528  C CB  . TYR B 201 ? 1.8463 2.8607 2.2257 0.0007  0.0757  0.0254  201 TYR B CB  
4529  C CG  . TYR B 201 ? 1.8303 2.8319 2.2168 0.0034  0.0676  0.0210  201 TYR B CG  
4530  C CD1 . TYR B 201 ? 1.8226 2.8236 2.2165 0.0063  0.0656  0.0082  201 TYR B CD1 
4531  C CD2 . TYR B 201 ? 1.8265 2.8161 2.2123 0.0031  0.0621  0.0296  201 TYR B CD2 
4532  C CE1 . TYR B 201 ? 1.8324 2.8212 2.2322 0.0084  0.0586  0.0046  201 TYR B CE1 
4533  C CE2 . TYR B 201 ? 1.8349 2.8130 2.2268 0.0053  0.0554  0.0257  201 TYR B CE2 
4534  C CZ  . TYR B 201 ? 1.8544 2.8321 2.2531 0.0078  0.0537  0.0134  201 TYR B CZ  
4535  O OH  . TYR B 201 ? 1.8424 2.8082 2.2467 0.0097  0.0474  0.0100  201 TYR B OH  
4536  N N   . SER B 202 ? 1.4010 2.4493 1.7695 -0.0017 0.0939  0.0172  202 SER B N   
4537  C CA  . SER B 202 ? 1.2827 2.3461 1.6399 -0.0013 0.0996  0.0108  202 SER B CA  
4538  C C   . SER B 202 ? 1.1731 2.2473 1.5396 -0.0024 0.1088  0.0057  202 SER B C   
4539  O O   . SER B 202 ? 1.1730 2.2573 1.5383 -0.0003 0.1121  -0.0058 202 SER B O   
4540  C CB  . SER B 202 ? 1.2174 2.2860 1.5554 -0.0036 0.1014  0.0212  202 SER B CB  
4541  O OG  . SER B 202 ? 1.1999 2.2588 1.5306 -0.0025 0.0928  0.0268  202 SER B OG  
4542  N N   . GLN B 203 ? 1.1245 2.1970 1.5009 -0.0058 0.1129  0.0139  203 GLN B N   
4543  C CA  . GLN B 203 ? 1.0932 2.1769 1.4794 -0.0073 0.1221  0.0099  203 GLN B CA  
4544  C C   . GLN B 203 ? 1.1023 2.1827 1.5084 -0.0044 0.1200  -0.0009 203 GLN B C   
4545  O O   . GLN B 203 ? 1.0873 2.1783 1.4989 -0.0026 0.1248  -0.0118 203 GLN B O   
4546  C CB  . GLN B 203 ? 1.0562 2.1401 1.4452 -0.0126 0.1276  0.0233  203 GLN B CB  
4547  C CG  . GLN B 203 ? 1.0005 2.0965 1.4014 -0.0148 0.1374  0.0199  203 GLN B CG  
4548  C CD  . GLN B 203 ? 0.9665 2.0553 1.3859 -0.0176 0.1374  0.0257  203 GLN B CD  
4549  O OE1 . GLN B 203 ? 0.9359 2.0150 1.3536 -0.0205 0.1348  0.0377  203 GLN B OE1 
4550  N NE2 . GLN B 203 ? 0.9662 2.0599 1.4036 -0.0164 0.1399  0.0167  203 GLN B NE2 
4551  N N   . ILE B 204 ? 1.1326 2.1983 1.5494 -0.0038 0.1127  0.0018  204 ILE B N   
4552  C CA  . ILE B 204 ? 1.1406 2.2016 1.5759 -0.0012 0.1101  -0.0071 204 ILE B CA  
4553  C C   . ILE B 204 ? 1.1477 2.2005 1.5818 0.0035  0.1019  -0.0164 204 ILE B C   
4554  O O   . ILE B 204 ? 1.1290 2.1817 1.5744 0.0068  0.1005  -0.0274 204 ILE B O   
4555  C CB  . ILE B 204 ? 1.1292 2.1792 1.5776 -0.0036 0.1076  0.0012  204 ILE B CB  
4556  C CG1 . ILE B 204 ? 1.0386 2.0962 1.4874 -0.0088 0.1156  0.0112  204 ILE B CG1 
4557  C CG2 . ILE B 204 ? 1.1575 2.2039 1.6249 -0.0009 0.1051  -0.0079 204 ILE B CG2 
4558  C CD1 . ILE B 204 ? 0.9869 2.0342 1.4483 -0.0116 0.1135  0.0195  204 ILE B CD1 
4559  N N   . ARG B 205 ? 1.1807 2.2266 1.6017 0.0037  0.0963  -0.0118 205 ARG B N   
4560  C CA  . ARG B 205 ? 1.2410 2.2792 1.6598 0.0075  0.0886  -0.0196 205 ARG B CA  
4561  C C   . ARG B 205 ? 1.2824 2.3073 1.7167 0.0095  0.0827  -0.0232 205 ARG B C   
4562  O O   . ARG B 205 ? 1.3923 2.4043 1.8284 0.0087  0.0775  -0.0157 205 ARG B O   
4563  C CB  . ARG B 205 ? 1.1678 2.2172 1.5817 0.0103  0.0912  -0.0325 205 ARG B CB  
4564  C CG  . ARG B 205 ? 1.1482 2.2106 1.5446 0.0087  0.0964  -0.0300 205 ARG B CG  
4565  C CD  . ARG B 205 ? 1.0640 2.1413 1.4608 0.0100  0.1039  -0.0409 205 ARG B CD  
4566  N NE  . ARG B 205 ? 1.0721 2.1560 1.4814 0.0082  0.1114  -0.0393 205 ARG B NE  
4567  C CZ  . ARG B 205 ? 1.1155 2.1984 1.5428 0.0103  0.1117  -0.0471 205 ARG B CZ  
4568  N NH1 . ARG B 205 ? 1.0845 2.1591 1.5186 0.0144  0.1050  -0.0568 205 ARG B NH1 
4569  N NH2 . ARG B 205 ? 1.1317 2.2217 1.5704 0.0083  0.1186  -0.0452 205 ARG B NH2 
4570  N N   . PHE B 222 ? 1.7066 2.6459 2.1355 0.0132  0.0392  -0.0005 222 PHE B N   
4571  C CA  . PHE B 222 ? 1.6438 2.5762 2.0850 0.0140  0.0391  -0.0046 222 PHE B CA  
4572  C C   . PHE B 222 ? 1.5345 2.4694 1.9809 0.0118  0.0435  0.0019  222 PHE B C   
4573  O O   . PHE B 222 ? 1.4144 2.3452 1.8716 0.0123  0.0437  -0.0007 222 PHE B O   
4574  C CB  . PHE B 222 ? 1.5876 2.5257 2.0331 0.0165  0.0398  -0.0173 222 PHE B CB  
4575  C CG  . PHE B 222 ? 1.5854 2.5400 2.0260 0.0161  0.0457  -0.0208 222 PHE B CG  
4576  C CD1 . PHE B 222 ? 1.5268 2.4889 1.9737 0.0152  0.0513  -0.0209 222 PHE B CD1 
4577  C CD2 . PHE B 222 ? 1.6126 2.5754 2.0421 0.0165  0.0456  -0.0241 222 PHE B CD2 
4578  C CE1 . PHE B 222 ? 1.5016 2.4793 1.9437 0.0148  0.0573  -0.0241 222 PHE B CE1 
4579  C CE2 . PHE B 222 ? 1.5935 2.5713 2.0172 0.0162  0.0512  -0.0275 222 PHE B CE2 
4580  C CZ  . PHE B 222 ? 1.5101 2.4954 1.9399 0.0153  0.0574  -0.0274 222 PHE B CZ  
4581  N N   . VAL B 223 ? 1.6533 2.5948 2.0922 0.0093  0.0469  0.0106  223 VAL B N   
4582  C CA  . VAL B 223 ? 1.5318 2.4759 1.9749 0.0065  0.0515  0.0178  223 VAL B CA  
4583  C C   . VAL B 223 ? 1.4952 2.4252 1.9414 0.0054  0.0480  0.0267  223 VAL B C   
4584  O O   . VAL B 223 ? 1.5053 2.4302 1.9440 0.0052  0.0453  0.0330  223 VAL B O   
4585  C CB  . VAL B 223 ? 1.5342 2.4912 1.9673 0.0042  0.0571  0.0234  223 VAL B CB  
4586  C CG1 . VAL B 223 ? 1.4137 2.3709 1.8508 0.0007  0.0613  0.0329  223 VAL B CG1 
4587  C CG2 . VAL B 223 ? 1.5362 2.5076 1.9672 0.0052  0.0615  0.0140  223 VAL B CG2 
4588  N N   . ARG B 224 ? 1.2645 2.1885 1.7218 0.0048  0.0480  0.0268  224 ARG B N   
4589  C CA  . ARG B 224 ? 1.2296 2.1398 1.6903 0.0038  0.0448  0.0342  224 ARG B CA  
4590  C C   . ARG B 224 ? 1.1624 2.0758 1.6225 0.0001  0.0490  0.0443  224 ARG B C   
4591  O O   . ARG B 224 ? 1.0957 2.0183 1.5608 -0.0018 0.0540  0.0437  224 ARG B O   
4592  C CB  . ARG B 224 ? 1.2482 2.1492 1.7207 0.0051  0.0418  0.0291  224 ARG B CB  
4593  C CG  . ARG B 224 ? 1.2425 2.1385 1.7165 0.0086  0.0375  0.0193  224 ARG B CG  
4594  C CD  . ARG B 224 ? 1.2179 2.1261 1.6954 0.0101  0.0405  0.0096  224 ARG B CD  
4595  N NE  . ARG B 224 ? 1.2110 2.1271 1.6969 0.0084  0.0451  0.0101  224 ARG B NE  
4596  C CZ  . ARG B 224 ? 1.2047 2.1357 1.6916 0.0082  0.0505  0.0057  224 ARG B CZ  
4597  N NH1 . ARG B 224 ? 1.2864 2.2257 1.7654 0.0096  0.0519  0.0003  224 ARG B NH1 
4598  N NH2 . ARG B 224 ? 1.1045 2.0425 1.6005 0.0063  0.0548  0.0064  224 ARG B NH2 
4599  N N   . LEU B 225 ? 1.1819 2.0874 1.6363 -0.0010 0.0470  0.0536  225 LEU B N   
4600  C CA  . LEU B 225 ? 1.1522 2.0595 1.6050 -0.0045 0.0507  0.0640  225 LEU B CA  
4601  C C   . LEU B 225 ? 1.2124 2.1160 1.6775 -0.0067 0.0521  0.0651  225 LEU B C   
4602  O O   . LEU B 225 ? 1.1128 2.0245 1.5805 -0.0100 0.0575  0.0687  225 LEU B O   
4603  C CB  . LEU B 225 ? 1.1028 2.0004 1.5488 -0.0045 0.0473  0.0729  225 LEU B CB  
4604  C CG  . LEU B 225 ? 0.9939 1.8949 1.4323 -0.0072 0.0504  0.0841  225 LEU B CG  
4605  C CD1 . LEU B 225 ? 0.9347 1.8294 1.3645 -0.0054 0.0462  0.0895  225 LEU B CD1 
4606  C CD2 . LEU B 225 ? 1.0203 1.9156 1.4663 -0.0106 0.0525  0.0911  225 LEU B CD2 
4607  N N   . ASP B 226 ? 1.5845 2.4759 2.0569 -0.0052 0.0474  0.0619  226 ASP B N   
4608  C CA  . ASP B 226 ? 1.5793 2.4650 2.0631 -0.0071 0.0472  0.0630  226 ASP B CA  
4609  C C   . ASP B 226 ? 1.5759 2.4674 2.0703 -0.0061 0.0479  0.0534  226 ASP B C   
4610  O O   . ASP B 226 ? 1.6967 2.5796 2.1999 -0.0053 0.0443  0.0504  226 ASP B O   
4611  C CB  . ASP B 226 ? 1.5794 2.4477 2.0640 -0.0060 0.0413  0.0656  226 ASP B CB  
4612  C CG  . ASP B 226 ? 1.6602 2.5222 2.1400 -0.0021 0.0366  0.0599  226 ASP B CG  
4613  O OD1 . ASP B 226 ? 1.6709 2.5357 2.1544 0.0001  0.0356  0.0508  226 ASP B OD1 
4614  O OD2 . ASP B 226 ? 1.7382 2.5925 2.2110 -0.0013 0.0341  0.0645  226 ASP B OD2 
4615  N N   . GLN B 227 ? 1.2988 2.2050 1.7925 -0.0057 0.0524  0.0482  227 GLN B N   
4616  C CA  . GLN B 227 ? 1.2206 2.1334 1.7252 -0.0043 0.0533  0.0387  227 GLN B CA  
4617  C C   . GLN B 227 ? 1.0440 1.9746 1.5499 -0.0063 0.0610  0.0374  227 GLN B C   
4618  O O   . GLN B 227 ? 1.0158 1.9528 1.5335 -0.0076 0.0639  0.0346  227 GLN B O   
4619  C CB  . GLN B 227 ? 1.2856 2.1950 1.7887 0.0002  0.0490  0.0291  227 GLN B CB  
4620  C CG  . GLN B 227 ? 1.4633 2.3577 1.9730 0.0024  0.0423  0.0263  227 GLN B CG  
4621  C CD  . GLN B 227 ? 1.3473 2.2313 1.8487 0.0052  0.0372  0.0244  227 GLN B CD  
4622  O OE1 . GLN B 227 ? 1.4220 2.2964 1.9172 0.0045  0.0349  0.0311  227 GLN B OE1 
4623  N NE2 . GLN B 227 ? 1.1850 2.0709 1.6871 0.0085  0.0356  0.0151  227 GLN B NE2 
4624  N N   . ASP B 228 ? 0.9876 1.9264 1.4813 -0.0065 0.0643  0.0393  228 ASP B N   
4625  C CA  . ASP B 228 ? 0.9650 1.9209 1.4572 -0.0082 0.0720  0.0378  228 ASP B CA  
4626  C C   . ASP B 228 ? 0.9727 1.9330 1.4545 -0.0120 0.0766  0.0488  228 ASP B C   
4627  O O   . ASP B 228 ? 0.9532 1.9274 1.4299 -0.0135 0.0832  0.0487  228 ASP B O   
4628  C CB  . ASP B 228 ? 0.9551 1.9191 1.4418 -0.0045 0.0723  0.0277  228 ASP B CB  
4629  C CG  . ASP B 228 ? 1.0632 2.0208 1.5365 -0.0024 0.0676  0.0288  228 ASP B CG  
4630  O OD1 . ASP B 228 ? 1.1029 2.0555 1.5677 -0.0043 0.0668  0.0386  228 ASP B OD1 
4631  O OD2 . ASP B 228 ? 1.1219 2.0793 1.5938 0.0011  0.0646  0.0198  228 ASP B OD2 
4632  N N   . ILE B 229 ? 1.0164 1.9649 1.4945 -0.0136 0.0734  0.0584  229 ILE B N   
4633  C CA  . ILE B 229 ? 1.0547 2.0054 1.5236 -0.0171 0.0771  0.0698  229 ILE B CA  
4634  C C   . ILE B 229 ? 1.1507 2.0919 1.6279 -0.0207 0.0766  0.0781  229 ILE B C   
4635  O O   . ILE B 229 ? 1.2356 2.1821 1.7137 -0.0250 0.0823  0.0853  229 ILE B O   
4636  C CB  . ILE B 229 ? 1.0453 1.9912 1.4993 -0.0152 0.0733  0.0738  229 ILE B CB  
4637  C CG1 . ILE B 229 ? 1.0556 2.0120 1.5011 -0.0122 0.0740  0.0656  229 ILE B CG1 
4638  C CG2 . ILE B 229 ? 0.9944 1.9404 1.4396 -0.0186 0.0762  0.0866  229 ILE B CG2 
4639  C CD1 . ILE B 229 ? 1.0259 1.9789 1.4577 -0.0102 0.0698  0.0686  229 ILE B CD1 
4640  N N   . LEU B 230 ? 1.2194 2.1460 1.7021 -0.0189 0.0700  0.0771  230 LEU B N   
4641  C CA  . LEU B 230 ? 1.2515 2.1679 1.7422 -0.0219 0.0687  0.0840  230 LEU B CA  
4642  C C   . LEU B 230 ? 1.2416 2.1630 1.7479 -0.0241 0.0713  0.0797  230 LEU B C   
4643  O O   . LEU B 230 ? 1.3158 2.2381 1.8281 -0.0286 0.0747  0.0862  230 LEU B O   
4644  C CB  . LEU B 230 ? 1.2520 2.1512 1.7423 -0.0192 0.0609  0.0841  230 LEU B CB  
4645  C CG  . LEU B 230 ? 1.2092 2.1021 1.6861 -0.0176 0.0582  0.0900  230 LEU B CG  
4646  C CD1 . LEU B 230 ? 1.2261 2.1020 1.7042 -0.0154 0.0514  0.0906  230 LEU B CD1 
4647  C CD2 . LEU B 230 ? 1.1516 2.0474 1.6219 -0.0212 0.0623  0.1014  230 LEU B CD2 
4648  N N   . SER B 231 ? 1.2068 2.1315 1.7204 -0.0209 0.0694  0.0688  231 SER B N   
4649  C CA  . SER B 231 ? 1.2113 2.1418 1.7408 -0.0225 0.0714  0.0640  231 SER B CA  
4650  C C   . SER B 231 ? 1.2992 2.2468 1.8315 -0.0262 0.0805  0.0655  231 SER B C   
4651  O O   . SER B 231 ? 1.3419 2.2921 1.8857 -0.0302 0.0834  0.0685  231 SER B O   
4652  C CB  . SER B 231 ? 1.1642 2.0945 1.7002 -0.0176 0.0672  0.0520  231 SER B CB  
4653  O OG  . SER B 231 ? 1.1671 2.0813 1.6999 -0.0145 0.0593  0.0510  231 SER B OG  
4654  N N   . PRO B 232 ? 1.2642 2.2240 1.7867 -0.0253 0.0854  0.0635  232 PRO B N   
4655  C CA  . PRO B 232 ? 1.3741 2.3502 1.8987 -0.0291 0.0948  0.0653  232 PRO B CA  
4656  C C   . PRO B 232 ? 1.6966 2.6713 2.2179 -0.0349 0.0990  0.0782  232 PRO B C   
4657  O O   . PRO B 232 ? 1.7124 2.6966 2.2425 -0.0393 0.1057  0.0804  232 PRO B O   
4658  C CB  . PRO B 232 ? 1.2377 2.2244 1.7490 -0.0264 0.0979  0.0608  232 PRO B CB  
4659  C CG  . PRO B 232 ? 1.1126 2.0912 1.6225 -0.0207 0.0903  0.0522  232 PRO B CG  
4660  C CD  . PRO B 232 ? 1.1727 2.1333 1.6837 -0.0206 0.0829  0.0577  232 PRO B CD  
4661  N N   . LEU B 233 ? 2.5991 3.5623 3.1086 -0.0350 0.0954  0.0869  233 LEU B N   
4662  C CA  . LEU B 233 ? 2.6165 3.5767 3.1224 -0.0402 0.0989  0.0997  233 LEU B CA  
4663  C C   . LEU B 233 ? 2.6108 3.5592 3.1303 -0.0429 0.0954  0.1029  233 LEU B C   
4664  O O   . LEU B 233 ? 2.6207 3.5541 3.1370 -0.0427 0.0900  0.1088  233 LEU B O   
4665  C CB  . LEU B 233 ? 2.6345 3.5875 3.1228 -0.0389 0.0962  0.1073  233 LEU B CB  
4666  C CG  . LEU B 233 ? 2.6585 3.6206 3.1346 -0.0423 0.1034  0.1163  233 LEU B CG  
4667  C CD1 . LEU B 233 ? 2.6573 3.6366 3.1276 -0.0410 0.1090  0.1090  233 LEU B CD1 
4668  C CD2 . LEU B 233 ? 2.6754 3.6276 3.1364 -0.0411 0.0993  0.1253  233 LEU B CD2 
4669  N N   . ALA B 234 ? 1.6944 2.6504 2.2299 -0.0454 0.0987  0.0985  234 ALA B N   
4670  C CA  . ALA B 234 ? 1.4826 2.4294 2.0327 -0.0481 0.0955  0.1002  234 ALA B CA  
4671  C C   . ALA B 234 ? 1.3077 2.2604 1.8645 -0.0553 0.1027  0.1085  234 ALA B C   
4672  O O   . ALA B 234 ? 1.2124 2.1549 1.7659 -0.0586 0.1020  0.1186  234 ALA B O   
4673  C CB  . ALA B 234 ? 1.4776 2.4269 2.0427 -0.0452 0.0919  0.0883  234 ALA B CB  
4674  N N   . GLY B 235 ? 1.3366 2.3058 1.9031 -0.0578 0.1100  0.1045  235 GLY B N   
4675  C CA  . GLY B 235 ? 1.2308 2.2062 1.8047 -0.0650 0.1175  0.1123  235 GLY B CA  
4676  C C   . GLY B 235 ? 1.2513 2.2279 1.8088 -0.0682 0.1232  0.1239  235 GLY B C   
4677  O O   . GLY B 235 ? 1.2322 2.2043 1.7916 -0.0739 0.1262  0.1341  235 GLY B O   
4678  N N   . LYS B 236 ? 1.2075 2.1895 1.7485 -0.0644 0.1246  0.1225  236 LYS B N   
4679  C CA  . LYS B 236 ? 1.1277 2.1111 1.6514 -0.0668 0.1294  0.1332  236 LYS B CA  
4680  C C   . LYS B 236 ? 1.0752 2.0400 1.5911 -0.0670 0.1232  0.1433  236 LYS B C   
4681  O O   . LYS B 236 ? 1.1125 2.0656 1.6245 -0.0620 0.1147  0.1403  236 LYS B O   
4682  C CB  . LYS B 236 ? 1.2146 2.2073 1.7225 -0.0621 0.1308  0.1281  236 LYS B CB  
4683  C CG  . LYS B 236 ? 1.4565 2.4487 1.9676 -0.0554 0.1243  0.1149  236 LYS B CG  
4684  C CD  . LYS B 236 ? 1.4270 2.4374 1.9423 -0.0540 0.1304  0.1043  236 LYS B CD  
4685  C CE  . LYS B 236 ? 1.3154 2.3324 1.8527 -0.0565 0.1332  0.0988  236 LYS B CE  
4686  N NZ  . LYS B 236 ? 1.4084 2.4143 1.9581 -0.0528 0.1239  0.0915  236 LYS B NZ  
4687  N N   . LYS B 237 ? 1.0319 1.9940 1.5458 -0.0728 0.1277  0.1554  237 LYS B N   
4688  C CA  . LYS B 237 ? 1.0049 1.9492 1.5137 -0.0737 0.1225  0.1657  237 LYS B CA  
4689  C C   . LYS B 237 ? 1.0047 1.9445 1.4928 -0.0695 0.1195  0.1705  237 LYS B C   
4690  O O   . LYS B 237 ? 1.0114 1.9516 1.4873 -0.0720 0.1233  0.1811  237 LYS B O   
4691  C CB  . LYS B 237 ? 1.0335 1.9765 1.5475 -0.0814 0.1286  0.1771  237 LYS B CB  
4692  C CG  . LYS B 237 ? 1.0318 1.9764 1.5679 -0.0860 0.1301  0.1733  237 LYS B CG  
4693  C CD  . LYS B 237 ? 1.0298 1.9556 1.5747 -0.0855 0.1213  0.1739  237 LYS B CD  
4694  C CE  . LYS B 237 ? 1.0102 1.9205 1.5439 -0.0865 0.1188  0.1864  237 LYS B CE  
4695  N NZ  . LYS B 237 ? 1.0406 1.9515 1.5770 -0.0944 0.1259  0.1980  237 LYS B NZ  
4696  N N   . GLN B 238 ? 0.9025 1.8379 1.3871 -0.0630 0.1121  0.1624  238 GLN B N   
4697  C CA  . GLN B 238 ? 0.8000 1.7296 1.2676 -0.0584 0.1074  0.1655  238 GLN B CA  
4698  C C   . GLN B 238 ? 0.7088 1.6231 1.1783 -0.0535 0.0977  0.1619  238 GLN B C   
4699  O O   . GLN B 238 ? 0.6209 1.5259 1.0799 -0.0513 0.0935  0.1682  238 GLN B O   
4700  C CB  . GLN B 238 ? 0.8097 1.7537 1.2661 -0.0550 0.1099  0.1588  238 GLN B CB  
4701  C CG  . GLN B 238 ? 0.8065 1.7640 1.2533 -0.0588 0.1190  0.1647  238 GLN B CG  
4702  C CD  . GLN B 238 ? 0.9730 1.9471 1.4282 -0.0603 0.1260  0.1557  238 GLN B CD  
4703  O OE1 . GLN B 238 ? 1.0160 1.9973 1.4707 -0.0559 0.1246  0.1444  238 GLN B OE1 
4704  N NE2 . GLN B 238 ? 1.0199 2.0001 1.4833 -0.0665 0.1338  0.1605  238 GLN B NE2 
4705  N N   . LEU B 239 ? 0.7558 1.6674 1.2383 -0.0518 0.0940  0.1521  239 LEU B N   
4706  C CA  . LEU B 239 ? 0.6661 1.5632 1.1504 -0.0474 0.0853  0.1484  239 LEU B CA  
4707  C C   . LEU B 239 ? 0.6309 1.5135 1.1245 -0.0505 0.0827  0.1542  239 LEU B C   
4708  O O   . LEU B 239 ? 0.6639 1.5486 1.1708 -0.0546 0.0853  0.1530  239 LEU B O   
4709  C CB  . LEU B 239 ? 0.8438 1.7446 1.3360 -0.0438 0.0823  0.1349  239 LEU B CB  
4710  C CG  . LEU B 239 ? 0.8235 1.7201 1.3071 -0.0376 0.0763  0.1290  239 LEU B CG  
4711  C CD1 . LEU B 239 ? 0.7620 1.6407 1.2451 -0.0358 0.0695  0.1327  239 LEU B CD1 
4712  C CD2 . LEU B 239 ? 0.8631 1.7683 1.3310 -0.0363 0.0790  0.1324  239 LEU B CD2 
4713  N N   . TYR B 240 ? 0.5653 1.4338 1.0524 -0.0486 0.0777  0.1602  240 TYR B N   
4714  C CA  . TYR B 240 ? 0.5848 1.4388 1.0794 -0.0514 0.0753  0.1662  240 TYR B CA  
4715  C C   . TYR B 240 ? 0.6229 1.4623 1.1194 -0.0469 0.0671  0.1611  240 TYR B C   
4716  O O   . TYR B 240 ? 0.6328 1.4739 1.1267 -0.0421 0.0637  0.1527  240 TYR B O   
4717  C CB  . TYR B 240 ? 0.5821 1.4314 1.0680 -0.0541 0.0777  0.1795  240 TYR B CB  
4718  C CG  . TYR B 240 ? 0.6163 1.4779 1.1025 -0.0599 0.0862  0.1855  240 TYR B CG  
4719  C CD1 . TYR B 240 ? 0.6445 1.5048 1.1432 -0.0661 0.0898  0.1890  240 TYR B CD1 
4720  C CD2 . TYR B 240 ? 0.6223 1.4972 1.0963 -0.0593 0.0909  0.1873  240 TYR B CD2 
4721  C CE1 . TYR B 240 ? 0.6532 1.5249 1.1525 -0.0717 0.0983  0.1945  240 TYR B CE1 
4722  C CE2 . TYR B 240 ? 0.6909 1.5771 1.1642 -0.0648 0.0993  0.1927  240 TYR B CE2 
4723  C CZ  . TYR B 240 ? 0.7039 1.5886 1.1901 -0.0710 0.1032  0.1965  240 TYR B CZ  
4724  O OH  . TYR B 240 ? 0.6675 1.5636 1.1534 -0.0768 0.1122  0.2021  240 TYR B OH  
4725  N N   . THR B 241 ? 0.5954 1.4200 1.0964 -0.0485 0.0641  0.1663  241 THR B N   
4726  C CA  . THR B 241 ? 0.6893 1.4993 1.1926 -0.0448 0.0570  0.1618  241 THR B CA  
4727  C C   . THR B 241 ? 0.8051 1.5997 1.3053 -0.0452 0.0546  0.1710  241 THR B C   
4728  O O   . THR B 241 ? 0.7641 1.5578 1.2646 -0.0495 0.0581  0.1804  241 THR B O   
4729  C CB  . THR B 241 ? 0.6703 1.4777 1.1875 -0.0462 0.0548  0.1540  241 THR B CB  
4730  O OG1 . THR B 241 ? 0.6687 1.4802 1.1957 -0.0526 0.0593  0.1582  241 THR B OG1 
4731  C CG2 . THR B 241 ? 0.6888 1.5071 1.2082 -0.0433 0.0545  0.1429  241 THR B CG2 
4732  N N   . TYR B 242 ? 1.0814 1.8637 1.5788 -0.0406 0.0486  0.1683  242 TYR B N   
4733  C CA  . TYR B 242 ? 1.1076 1.8743 1.6026 -0.0400 0.0458  0.1756  242 TYR B CA  
4734  C C   . TYR B 242 ? 1.0909 1.8447 1.5882 -0.0361 0.0396  0.1688  242 TYR B C   
4735  O O   . TYR B 242 ? 1.0201 1.7758 1.5126 -0.0315 0.0371  0.1624  242 TYR B O   
4736  C CB  . TYR B 242 ? 1.1009 1.8692 1.5836 -0.0374 0.0463  0.1831  242 TYR B CB  
4737  C CG  . TYR B 242 ? 1.1025 1.8550 1.5821 -0.0350 0.0426  0.1894  242 TYR B CG  
4738  C CD1 . TYR B 242 ? 1.1366 1.8803 1.6190 -0.0387 0.0438  0.1988  242 TYR B CD1 
4739  C CD2 . TYR B 242 ? 1.0969 1.8436 1.5712 -0.0292 0.0381  0.1860  242 TYR B CD2 
4740  C CE1 . TYR B 242 ? 1.1357 1.8648 1.6157 -0.0362 0.0404  0.2042  242 TYR B CE1 
4741  C CE2 . TYR B 242 ? 1.1108 1.8438 1.5830 -0.0267 0.0350  0.1914  242 TYR B CE2 
4742  C CZ  . TYR B 242 ? 1.1026 1.8267 1.5776 -0.0300 0.0360  0.2004  242 TYR B CZ  
4743  O OH  . TYR B 242 ? 1.1190 1.8291 1.5924 -0.0272 0.0329  0.2054  242 TYR B OH  
4744  N N   . GLU B 243 ? 1.1892 1.9298 1.6936 -0.0382 0.0374  0.1701  243 GLU B N   
4745  C CA  . GLU B 243 ? 1.1638 1.8919 1.6705 -0.0351 0.0319  0.1631  243 GLU B CA  
4746  C C   . GLU B 243 ? 1.1667 1.8856 1.6644 -0.0297 0.0287  0.1646  243 GLU B C   
4747  O O   . GLU B 243 ? 1.1880 1.9050 1.6802 -0.0290 0.0299  0.1729  243 GLU B O   
4748  C CB  . GLU B 243 ? 1.1757 1.8919 1.6918 -0.0389 0.0302  0.1644  243 GLU B CB  
4749  N N   . ASN B 244 ? 0.9513 1.6647 1.4479 -0.0257 0.0248  0.1566  244 ASN B N   
4750  C CA  . ASN B 244 ? 0.8969 1.6016 1.3863 -0.0206 0.0220  0.1568  244 ASN B CA  
4751  C C   . ASN B 244 ? 0.8673 1.5550 1.3584 -0.0205 0.0198  0.1609  244 ASN B C   
4752  O O   . ASN B 244 ? 0.9203 1.6034 1.4073 -0.0189 0.0200  0.1679  244 ASN B O   
4753  C CB  . ASN B 244 ? 0.8689 1.5733 1.3565 -0.0168 0.0192  0.1470  244 ASN B CB  
4754  C CG  . ASN B 244 ? 0.8732 1.5731 1.3532 -0.0116 0.0174  0.1468  244 ASN B CG  
4755  O OD1 . ASN B 244 ? 0.8734 1.5662 1.3508 -0.0103 0.0171  0.1532  244 ASN B OD1 
4756  N ND2 . ASN B 244 ? 0.8766 1.5804 1.3537 -0.0087 0.0161  0.1395  244 ASN B ND2 
4757  N N   . LYS B 245 ? 0.7906 1.4687 1.2878 -0.0221 0.0173  0.1563  245 LYS B N   
4758  C CA  . LYS B 245 ? 0.7984 1.4594 1.2974 -0.0220 0.0147  0.1584  245 LYS B CA  
4759  C C   . LYS B 245 ? 0.8594 1.5111 1.3516 -0.0162 0.0123  0.1568  245 LYS B C   
4760  O O   . LYS B 245 ? 0.9010 1.5406 1.3926 -0.0150 0.0113  0.1610  245 LYS B O   
4761  C CB  . LYS B 245 ? 0.7997 1.4576 1.3015 -0.0256 0.0170  0.1685  245 LYS B CB  
4762  N N   . ASP B 246 ? 0.8853 1.5424 1.3728 -0.0126 0.0116  0.1505  246 ASP B N   
4763  C CA  . ASP B 246 ? 0.9217 1.5710 1.4035 -0.0073 0.0097  0.1481  246 ASP B CA  
4764  C C   . ASP B 246 ? 0.9672 1.6178 1.4466 -0.0052 0.0080  0.1387  246 ASP B C   
4765  O O   . ASP B 246 ? 0.9887 1.6343 1.4712 -0.0067 0.0059  0.1332  246 ASP B O   
4766  C CB  . ASP B 246 ? 0.9293 1.5853 1.4060 -0.0045 0.0114  0.1538  246 ASP B CB  
4767  C CG  . ASP B 246 ? 0.9212 1.5688 1.3985 -0.0042 0.0116  0.1625  246 ASP B CG  
4768  O OD1 . ASP B 246 ? 0.9534 1.5866 1.4313 -0.0024 0.0097  0.1618  246 ASP B OD1 
4769  O OD2 . ASP B 246 ? 0.8624 1.5173 1.3390 -0.0058 0.0137  0.1701  246 ASP B OD2 
4770  N N   . PHE B 247 ? 1.2999 1.9572 1.7741 -0.0017 0.0085  0.1368  247 PHE B N   
4771  C CA  . PHE B 247 ? 1.2899 1.9477 1.7613 0.0006  0.0070  0.1285  247 PHE B CA  
4772  C C   . PHE B 247 ? 1.2677 1.9415 1.7380 0.0004  0.0086  0.1264  247 PHE B C   
4773  O O   . PHE B 247 ? 1.2656 1.9498 1.7352 -0.0002 0.0109  0.1315  247 PHE B O   
4774  C CB  . PHE B 247 ? 1.2944 1.9431 1.7608 0.0050  0.0061  0.1268  247 PHE B CB  
4775  C CG  . PHE B 247 ? 1.2951 1.9478 1.7591 0.0075  0.0076  0.1327  247 PHE B CG  
4776  C CD1 . PHE B 247 ? 1.3174 1.9628 1.7827 0.0079  0.0078  0.1395  247 PHE B CD1 
4777  C CD2 . PHE B 247 ? 1.2780 1.9412 1.7388 0.0097  0.0084  0.1312  247 PHE B CD2 
4778  C CE1 . PHE B 247 ? 1.3208 1.9698 1.7842 0.0106  0.0087  0.1450  247 PHE B CE1 
4779  C CE2 . PHE B 247 ? 1.2832 1.9505 1.7422 0.0122  0.0091  0.1364  247 PHE B CE2 
4780  C CZ  . PHE B 247 ? 1.3050 1.9653 1.7654 0.0128  0.0092  0.1434  247 PHE B CZ  
4781  N N   . TRP B 248 ? 1.0413 1.7165 1.5110 0.0012  0.0073  0.1187  248 TRP B N   
4782  C CA  . TRP B 248 ? 0.9373 1.6263 1.4059 0.0016  0.0084  0.1152  248 TRP B CA  
4783  C C   . TRP B 248 ? 0.9170 1.6021 1.3837 0.0036  0.0062  0.1069  248 TRP B C   
4784  O O   . TRP B 248 ? 0.9262 1.6025 1.3948 0.0030  0.0039  0.1032  248 TRP B O   
4785  C CB  . TRP B 248 ? 0.9430 1.6434 1.4167 -0.0021 0.0102  0.1159  248 TRP B CB  
4786  C CG  . TRP B 248 ? 0.9300 1.6450 1.4021 -0.0015 0.0118  0.1125  248 TRP B CG  
4787  C CD1 . TRP B 248 ? 0.9473 1.6727 1.4155 -0.0008 0.0139  0.1159  248 TRP B CD1 
4788  C CD2 . TRP B 248 ? 0.8958 1.6161 1.3701 -0.0014 0.0110  0.1048  248 TRP B CD2 
4789  N NE1 . TRP B 248 ? 0.9007 1.6376 1.3683 -0.0004 0.0147  0.1104  248 TRP B NE1 
4790  C CE2 . TRP B 248 ? 0.8769 1.6108 1.3486 -0.0007 0.0130  0.1035  248 TRP B CE2 
4791  C CE3 . TRP B 248 ? 0.8932 1.6078 1.3714 -0.0017 0.0084  0.0986  248 TRP B CE3 
4792  C CZ2 . TRP B 248 ? 0.8942 1.6358 1.3675 -0.0002 0.0129  0.0963  248 TRP B CZ2 
4793  C CZ3 . TRP B 248 ? 0.8899 1.6124 1.3699 -0.0011 0.0080  0.0919  248 TRP B CZ3 
4794  C CH2 . TRP B 248 ? 0.9255 1.6612 1.4032 -0.0003 0.0104  0.0906  248 TRP B CH2 
4795  N N   . GLU B 249 ? 0.8937 1.5850 1.3566 0.0060  0.0067  0.1042  249 GLU B N   
4796  C CA  . GLU B 249 ? 0.8543 1.5419 1.3149 0.0078  0.0049  0.0968  249 GLU B CA  
4797  C C   . GLU B 249 ? 0.8443 1.5442 1.3032 0.0089  0.0060  0.0939  249 GLU B C   
4798  O O   . GLU B 249 ? 0.8714 1.5758 1.3275 0.0103  0.0072  0.0966  249 GLU B O   
4799  C CB  . GLU B 249 ? 0.8617 1.5356 1.3180 0.0103  0.0038  0.0962  249 GLU B CB  
4800  N N   . GLN B 250 ? 0.8566 1.5621 1.3176 0.0083  0.0054  0.0882  250 GLN B N   
4801  C CA  . GLN B 250 ? 0.9155 1.6318 1.3751 0.0093  0.0061  0.0842  250 GLN B CA  
4802  C C   . GLN B 250 ? 0.9722 1.6814 1.4274 0.0119  0.0049  0.0806  250 GLN B C   
4803  O O   . GLN B 250 ? 0.9513 1.6489 1.4053 0.0126  0.0030  0.0775  250 GLN B O   
4804  C CB  . GLN B 250 ? 0.9424 1.6654 1.4062 0.0082  0.0057  0.0787  250 GLN B CB  
4805  C CG  . GLN B 250 ? 0.9458 1.6850 1.4102 0.0077  0.0080  0.0776  250 GLN B CG  
4806  C CD  . GLN B 250 ? 0.9486 1.6912 1.4103 0.0098  0.0073  0.0714  250 GLN B CD  
4807  O OE1 . GLN B 250 ? 0.9792 1.7175 1.4367 0.0114  0.0068  0.0717  250 GLN B OE1 
4808  N NE2 . GLN B 250 ? 0.9332 1.6834 1.3979 0.0097  0.0074  0.0656  250 GLN B NE2 
4809  N N   . ILE B 251 ? 1.2070 1.9235 1.6597 0.0130  0.0061  0.0810  251 ILE B N   
4810  C CA  . ILE B 251 ? 1.2048 1.9155 1.6544 0.0151  0.0055  0.0783  251 ILE B CA  
4811  C C   . ILE B 251 ? 1.1934 1.9130 1.6424 0.0156  0.0055  0.0728  251 ILE B C   
4812  O O   . ILE B 251 ? 1.1856 1.9118 1.6334 0.0164  0.0062  0.0736  251 ILE B O   
4813  C CB  . ILE B 251 ? 1.2032 1.9120 1.6511 0.0164  0.0065  0.0839  251 ILE B CB  
4814  C CG1 . ILE B 251 ? 1.2019 1.9231 1.6505 0.0157  0.0078  0.0891  251 ILE B CG1 
4815  C CG2 . ILE B 251 ? 1.2158 1.9110 1.6633 0.0166  0.0062  0.0871  251 ILE B CG2 
4816  C CD1 . ILE B 251 ? 1.2066 1.9313 1.6538 0.0176  0.0081  0.0920  251 ILE B CD1 
4817  N N   . LYS B 252 ? 0.9967 1.7163 1.4472 0.0153  0.0043  0.0671  252 LYS B N   
4818  C CA  . LYS B 252 ? 0.9426 1.6676 1.3927 0.0160  0.0039  0.0610  252 LYS B CA  
4819  C C   . LYS B 252 ? 0.8835 1.5968 1.3310 0.0171  0.0028  0.0576  252 LYS B C   
4820  O O   . LYS B 252 ? 0.8437 1.5599 1.2907 0.0176  0.0026  0.0533  252 LYS B O   
4821  C CB  . LYS B 252 ? 0.9778 1.7092 1.4311 0.0153  0.0034  0.0562  252 LYS B CB  
4822  C CG  . LYS B 252 ? 0.9702 1.6910 1.4252 0.0154  0.0011  0.0534  252 LYS B CG  
4823  C CD  . LYS B 252 ? 0.9474 1.6706 1.4064 0.0139  0.0014  0.0564  252 LYS B CD  
4824  C CE  . LYS B 252 ? 0.9612 1.6702 1.4203 0.0139  -0.0011 0.0568  252 LYS B CE  
4825  N NZ  . LYS B 252 ? 0.9902 1.6888 1.4447 0.0144  -0.0008 0.0612  252 LYS B NZ  
4826  N N   . THR B 253 ? 0.9278 1.6276 1.3733 0.0175  0.0020  0.0594  253 THR B N   
4827  C CA  . THR B 253 ? 0.9106 1.5975 1.3525 0.0184  0.0014  0.0572  253 THR B CA  
4828  C C   . THR B 253 ? 0.8730 1.5569 1.3128 0.0192  0.0033  0.0609  253 THR B C   
4829  O O   . THR B 253 ? 0.8914 1.5760 1.3318 0.0193  0.0043  0.0661  253 THR B O   
4830  C CB  . THR B 253 ? 0.9663 1.6403 1.4065 0.0185  -0.0006 0.0571  253 THR B CB  
4831  O OG1 . THR B 253 ? 0.9665 1.6460 1.4109 0.0174  -0.0017 0.0576  253 THR B OG1 
4832  C CG2 . THR B 253 ? 0.9783 1.6433 1.4155 0.0192  -0.0025 0.0518  253 THR B CG2 
4833  N N   . PRO B 254 ? 0.8745 1.5550 1.3124 0.0197  0.0040  0.0583  254 PRO B N   
4834  C CA  . PRO B 254 ? 0.8510 1.5279 1.2878 0.0206  0.0061  0.0614  254 PRO B CA  
4835  C C   . PRO B 254 ? 0.9349 1.5977 1.3681 0.0213  0.0065  0.0637  254 PRO B C   
4836  O O   . PRO B 254 ? 0.8819 1.5425 1.3151 0.0223  0.0083  0.0673  254 PRO B O   
4837  C CB  . PRO B 254 ? 0.7562 1.4326 1.1923 0.0205  0.0069  0.0571  254 PRO B CB  
4838  C CG  . PRO B 254 ? 0.8478 1.5201 1.2825 0.0199  0.0048  0.0522  254 PRO B CG  
4839  C CD  . PRO B 254 ? 0.8669 1.5471 1.3043 0.0195  0.0032  0.0524  254 PRO B CD  
4840  N N   . GLY B 255 ? 1.3101 1.9632 1.7403 0.0210  0.0046  0.0617  255 GLY B N   
4841  C CA  . GLY B 255 ? 1.3286 1.9680 1.7546 0.0216  0.0045  0.0635  255 GLY B CA  
4842  C C   . GLY B 255 ? 1.3269 1.9679 1.7555 0.0215  0.0043  0.0681  255 GLY B C   
4843  O O   . GLY B 255 ? 1.3365 1.9695 1.7632 0.0224  0.0054  0.0709  255 GLY B O   
4844  N N   . LYS B 256 ? 0.9952 1.6462 1.4283 0.0203  0.0031  0.0690  256 LYS B N   
4845  C CA  . LYS B 256 ? 0.9245 1.5777 1.3605 0.0197  0.0031  0.0739  256 LYS B CA  
4846  C C   . LYS B 256 ? 0.8536 1.5112 1.2910 0.0207  0.0054  0.0789  256 LYS B C   
4847  O O   . LYS B 256 ? 0.7661 1.4226 1.2052 0.0204  0.0056  0.0836  256 LYS B O   
4848  C CB  . LYS B 256 ? 0.9720 1.6367 1.4126 0.0180  0.0021  0.0737  256 LYS B CB  
4849  C CG  . LYS B 256 ? 0.9304 1.5905 1.3719 0.0170  -0.0006 0.0703  256 LYS B CG  
4850  C CD  . LYS B 256 ? 0.8994 1.5491 1.3407 0.0164  -0.0018 0.0730  256 LYS B CD  
4851  C CE  . LYS B 256 ? 0.8701 1.5204 1.3153 0.0148  -0.0045 0.0707  256 LYS B CE  
4852  N NZ  . LYS B 256 ? 0.8414 1.5069 1.2928 0.0131  -0.0033 0.0719  256 LYS B NZ  
4853  N N   . SER B 257 ? 0.8794 1.5416 1.3166 0.0218  0.0070  0.0779  257 SER B N   
4854  C CA  . SER B 257 ? 0.7988 1.4661 1.2380 0.0231  0.0086  0.0824  257 SER B CA  
4855  C C   . SER B 257 ? 0.6825 1.3382 1.1204 0.0246  0.0097  0.0854  257 SER B C   
4856  O O   . SER B 257 ? 0.6740 1.3330 1.1144 0.0261  0.0108  0.0896  257 SER B O   
4857  C CB  . SER B 257 ? 0.7619 1.4358 1.2018 0.0238  0.0097  0.0798  257 SER B CB  
4858  O OG  . SER B 257 ? 0.7690 1.4529 1.2099 0.0225  0.0086  0.0763  257 SER B OG  
4859  N N   . LEU B 258 ? 0.6871 1.3294 1.1211 0.0246  0.0092  0.0831  258 LEU B N   
4860  C CA  . LEU B 258 ? 0.6667 1.2970 1.0987 0.0260  0.0102  0.0852  258 LEU B CA  
4861  C C   . LEU B 258 ? 0.7296 1.3554 1.1627 0.0249  0.0084  0.0881  258 LEU B C   
4862  O O   . LEU B 258 ? 0.6252 1.2480 1.0601 0.0260  0.0091  0.0924  258 LEU B O   
4863  C CB  . LEU B 258 ? 0.7917 1.4092 1.2175 0.0266  0.0108  0.0808  258 LEU B CB  
4864  C CG  . LEU B 258 ? 0.7029 1.3213 1.1276 0.0278  0.0137  0.0787  258 LEU B CG  
4865  C CD1 . LEU B 258 ? 0.6555 1.2604 1.0728 0.0279  0.0144  0.0747  258 LEU B CD1 
4866  C CD2 . LEU B 258 ? 0.7401 1.3608 1.1684 0.0300  0.0163  0.0823  258 LEU B CD2 
4867  N N   . LYS B 259 ? 0.6809 1.3056 1.1134 0.0229  0.0060  0.0857  259 LYS B N   
4868  C CA  . LYS B 259 ? 0.6995 1.3206 1.1342 0.0213  0.0042  0.0880  259 LYS B CA  
4869  C C   . LYS B 259 ? 0.5987 1.2294 1.0387 0.0206  0.0050  0.0941  259 LYS B C   
4870  O O   . LYS B 259 ? 0.6313 1.2565 1.0730 0.0203  0.0048  0.0980  259 LYS B O   
4871  C CB  . LYS B 259 ? 0.7867 1.4088 1.2217 0.0193  0.0015  0.0842  259 LYS B CB  
4872  C CG  . LYS B 259 ? 0.8097 1.4275 1.2476 0.0172  -0.0007 0.0857  259 LYS B CG  
4873  C CD  . LYS B 259 ? 0.8256 1.4458 1.2651 0.0156  -0.0035 0.0814  259 LYS B CD  
4874  C CE  . LYS B 259 ? 0.8370 1.4522 1.2801 0.0134  -0.0061 0.0822  259 LYS B CE  
4875  N NZ  . LYS B 259 ? 0.9605 1.5595 1.3986 0.0143  -0.0076 0.0813  259 LYS B NZ  
4876  N N   . CYS B 260 ? 0.5974 1.2419 1.0395 0.0204  0.0059  0.0949  260 CYS B N   
4877  C CA  . CYS B 260 ? 0.6306 1.2845 1.0764 0.0199  0.0067  0.1010  260 CYS B CA  
4878  C C   . CYS B 260 ? 0.5920 1.2442 1.0380 0.0226  0.0081  0.1051  260 CYS B C   
4879  O O   . CYS B 260 ? 0.6536 1.3071 1.1019 0.0226  0.0083  0.1111  260 CYS B O   
4880  C CB  . CYS B 260 ? 0.6461 1.3154 1.0931 0.0189  0.0070  0.1001  260 CYS B CB  
4881  S SG  . CYS B 260 ? 0.8010 1.4770 1.2463 0.0211  0.0079  0.0968  260 CYS B SG  
4882  N N   . SER B 261 ? 0.5861 1.2356 1.0300 0.0249  0.0091  0.1020  261 SER B N   
4883  C CA  . SER B 261 ? 0.5873 1.2355 1.0326 0.0278  0.0105  0.1052  261 SER B CA  
4884  C C   . SER B 261 ? 0.6100 1.2455 1.0555 0.0288  0.0106  0.1082  261 SER B C   
4885  O O   . SER B 261 ? 0.5921 1.2279 1.0403 0.0308  0.0112  0.1131  261 SER B O   
4886  C CB  . SER B 261 ? 0.5680 1.2150 1.0117 0.0295  0.0120  0.1007  261 SER B CB  
4887  O OG  . SER B 261 ? 0.6124 1.2589 1.0586 0.0325  0.0136  0.1034  261 SER B OG  
4888  N N   . ALA B 262 ? 0.5885 1.2124 1.0310 0.0276  0.0098  0.1051  262 ALA B N   
4889  C CA  . ALA B 262 ? 0.6158 1.2269 1.0583 0.0283  0.0096  0.1073  262 ALA B CA  
4890  C C   . ALA B 262 ? 0.6234 1.2372 1.0700 0.0266  0.0085  0.1134  262 ALA B C   
4891  O O   . ALA B 262 ? 0.6589 1.2662 1.1075 0.0279  0.0088  0.1175  262 ALA B O   
4892  C CB  . ALA B 262 ? 0.6463 1.2449 1.0842 0.0272  0.0084  0.1021  262 ALA B CB  
4893  N N   . LEU B 263 ? 0.6653 1.2888 1.1136 0.0235  0.0075  0.1141  263 LEU B N   
4894  C CA  . LEU B 263 ? 0.6692 1.2958 1.1212 0.0213  0.0071  0.1203  263 LEU B CA  
4895  C C   . LEU B 263 ? 0.7304 1.3644 1.1844 0.0232  0.0081  0.1268  263 LEU B C   
4896  O O   . LEU B 263 ? 0.7475 1.3778 1.2039 0.0231  0.0079  0.1329  263 LEU B O   
4897  C CB  . LEU B 263 ? 0.7837 1.4198 1.2371 0.0177  0.0064  0.1190  263 LEU B CB  
4898  C CG  . LEU B 263 ? 0.7131 1.3428 1.1653 0.0160  0.0047  0.1127  263 LEU B CG  
4899  C CD1 . LEU B 263 ? 0.7766 1.4175 1.2314 0.0129  0.0043  0.1111  263 LEU B CD1 
4900  C CD2 . LEU B 263 ? 0.6898 1.3054 1.1430 0.0150  0.0033  0.1133  263 LEU B CD2 
4901  N N   . TYR B 264 ? 0.6361 1.2803 1.0892 0.0251  0.0088  0.1257  264 TYR B N   
4902  C CA  . TYR B 264 ? 0.6519 1.3034 1.1067 0.0273  0.0090  0.1315  264 TYR B CA  
4903  C C   . TYR B 264 ? 0.6376 1.2788 1.0940 0.0309  0.0094  0.1338  264 TYR B C   
4904  O O   . TYR B 264 ? 0.7053 1.3467 1.1642 0.0322  0.0090  0.1405  264 TYR B O   
4905  C CB  . TYR B 264 ? 0.6234 1.2876 1.0773 0.0285  0.0093  0.1286  264 TYR B CB  
4906  C CG  . TYR B 264 ? 0.6197 1.2972 1.0725 0.0257  0.0090  0.1284  264 TYR B CG  
4907  C CD1 . TYR B 264 ? 0.7336 1.4149 1.1869 0.0232  0.0089  0.1338  264 TYR B CD1 
4908  C CD2 . TYR B 264 ? 0.5975 1.2835 1.0490 0.0255  0.0090  0.1227  264 TYR B CD2 
4909  C CE1 . TYR B 264 ? 0.7304 1.4242 1.1824 0.0207  0.0092  0.1333  264 TYR B CE1 
4910  C CE2 . TYR B 264 ? 0.6472 1.3452 1.0976 0.0232  0.0089  0.1219  264 TYR B CE2 
4911  C CZ  . TYR B 264 ? 0.6663 1.3685 1.1169 0.0209  0.0091  0.1271  264 TYR B CZ  
4912  O OH  . TYR B 264 ? 0.6035 1.3180 1.0528 0.0187  0.0095  0.1260  264 TYR B OH  
4913  N N   . LEU B 265 ? 0.7566 1.3886 1.2116 0.0327  0.0102  0.1284  265 LEU B N   
4914  C CA  . LEU B 265 ? 0.7057 1.3275 1.1624 0.0363  0.0110  0.1296  265 LEU B CA  
4915  C C   . LEU B 265 ? 0.7345 1.3443 1.1923 0.0354  0.0102  0.1332  265 LEU B C   
4916  O O   . LEU B 265 ? 0.7800 1.3853 1.2408 0.0380  0.0102  0.1379  265 LEU B O   
4917  C CB  . LEU B 265 ? 0.7691 1.3837 1.2230 0.0379  0.0127  0.1226  265 LEU B CB  
4918  C CG  . LEU B 265 ? 0.7322 1.3570 1.1860 0.0391  0.0139  0.1191  265 LEU B CG  
4919  C CD1 . LEU B 265 ? 0.7560 1.3722 1.2065 0.0402  0.0161  0.1127  265 LEU B CD1 
4920  C CD2 . LEU B 265 ? 0.7495 1.3833 1.2084 0.0422  0.0140  0.1236  265 LEU B CD2 
4921  N N   . SER B 266 ? 0.8012 1.4058 1.2571 0.0318  0.0093  0.1308  266 SER B N   
4922  C CA  . SER B 266 ? 0.8199 1.4145 1.2778 0.0301  0.0082  0.1344  266 SER B CA  
4923  C C   . SER B 266 ? 0.8217 1.4231 1.2831 0.0290  0.0078  0.1429  266 SER B C   
4924  O O   . SER B 266 ? 0.8197 1.4127 1.2837 0.0294  0.0073  0.1478  266 SER B O   
4925  C CB  . SER B 266 ? 0.8217 1.4119 1.2779 0.0260  0.0069  0.1302  266 SER B CB  
4926  O OG  . SER B 266 ? 0.9410 1.5228 1.4001 0.0237  0.0057  0.1337  266 SER B OG  
4927  N N   . GLN B 267 ? 0.7809 1.3972 1.2419 0.0277  0.0079  0.1447  267 GLN B N   
4928  C CA  . GLN B 267 ? 0.7479 1.3717 1.2107 0.0269  0.0077  0.1531  267 GLN B CA  
4929  C C   . GLN B 267 ? 0.7444 1.3674 1.2090 0.0316  0.0075  0.1578  267 GLN B C   
4930  O O   . GLN B 267 ? 0.7605 1.3818 1.2271 0.0319  0.0068  0.1656  267 GLN B O   
4931  C CB  . GLN B 267 ? 0.7355 1.3758 1.1965 0.0248  0.0080  0.1529  267 GLN B CB  
4932  C CG  . GLN B 267 ? 0.7996 1.4483 1.2608 0.0232  0.0081  0.1612  267 GLN B CG  
4933  C CD  . GLN B 267 ? 0.8158 1.4810 1.2743 0.0218  0.0085  0.1600  267 GLN B CD  
4934  O OE1 . GLN B 267 ? 0.7763 1.4475 1.2332 0.0236  0.0084  0.1544  267 GLN B OE1 
4935  N NE2 . GLN B 267 ? 0.8256 1.4979 1.2833 0.0184  0.0093  0.1652  267 GLN B NE2 
4936  N N   . PHE B 268 ? 0.7318 1.3560 1.1962 0.0354  0.0080  0.1534  268 PHE B N   
4937  C CA  . PHE B 268 ? 0.7808 1.4037 1.2483 0.0404  0.0077  0.1567  268 PHE B CA  
4938  C C   . PHE B 268 ? 0.7968 1.4032 1.2662 0.0429  0.0083  0.1556  268 PHE B C   
4939  O O   . PHE B 268 ? 0.9067 1.5105 1.3796 0.0474  0.0082  0.1580  268 PHE B O   
4940  C CB  . PHE B 268 ? 0.7981 1.4308 1.2656 0.0432  0.0083  0.1524  268 PHE B CB  
4941  C CG  . PHE B 268 ? 0.7939 1.4425 1.2592 0.0411  0.0076  0.1525  268 PHE B CG  
4942  C CD1 . PHE B 268 ? 0.8300 1.4856 1.2941 0.0386  0.0065  0.1588  268 PHE B CD1 
4943  C CD2 . PHE B 268 ? 0.7473 1.4039 1.2117 0.0415  0.0083  0.1462  268 PHE B CD2 
4944  C CE1 . PHE B 268 ? 0.8163 1.4866 1.2778 0.0368  0.0061  0.1584  268 PHE B CE1 
4945  C CE2 . PHE B 268 ? 0.7348 1.4057 1.1973 0.0396  0.0075  0.1457  268 PHE B CE2 
4946  C CZ  . PHE B 268 ? 0.7849 1.4627 1.2456 0.0374  0.0064  0.1516  268 PHE B CZ  
4947  N N   . ARG B 269 ? 0.8056 1.4013 1.2731 0.0401  0.0086  0.1517  269 ARG B N   
4948  C CA  . ARG B 269 ? 0.8350 1.4142 1.3037 0.0419  0.0088  0.1506  269 ARG B CA  
4949  C C   . ARG B 269 ? 0.8522 1.4238 1.3233 0.0393  0.0074  0.1568  269 ARG B C   
4950  O O   . ARG B 269 ? 0.8844 1.4440 1.3581 0.0417  0.0071  0.1587  269 ARG B O   
4951  C CB  . ARG B 269 ? 0.8387 1.4095 1.3032 0.0407  0.0096  0.1419  269 ARG B CB  
4952  C CG  . ARG B 269 ? 0.8939 1.4508 1.3582 0.0445  0.0108  0.1383  269 ARG B CG  
4953  C CD  . ARG B 269 ? 0.9184 1.4799 1.3861 0.0499  0.0124  0.1396  269 ARG B CD  
4954  N NE  . ARG B 269 ? 1.0024 1.5622 1.4674 0.0522  0.0150  0.1323  269 ARG B NE  
4955  C CZ  . ARG B 269 ? 1.0966 1.6580 1.5650 0.0570  0.0170  0.1317  269 ARG B CZ  
4956  N NH1 . ARG B 269 ? 1.1646 1.7292 1.6394 0.0603  0.0161  0.1378  269 ARG B NH1 
4957  N NH2 . ARG B 269 ? 1.1194 1.6790 1.5850 0.0585  0.0199  0.1251  269 ARG B NH2 
4958  N N   . GLU B 270 ? 0.8271 1.4055 1.2976 0.0345  0.0067  0.1597  270 GLU B N   
4959  C CA  . GLU B 270 ? 0.7898 1.3637 1.2631 0.0318  0.0057  0.1672  270 GLU B CA  
4960  C C   . GLU B 270 ? 0.7955 1.3755 1.2707 0.0344  0.0053  0.1760  270 GLU B C   
4961  O O   . GLU B 270 ? 0.8440 1.4144 1.3224 0.0365  0.0045  0.1813  270 GLU B O   
4962  C CB  . GLU B 270 ? 0.7415 1.3220 1.2141 0.0256  0.0057  0.1673  270 GLU B CB  
4963  N N   . THR B 271 ? 0.7942 1.3900 1.2674 0.0345  0.0054  0.1776  271 THR B N   
4964  C CA  . THR B 271 ? 0.8044 1.4075 1.2783 0.0373  0.0044  0.1856  271 THR B CA  
4965  C C   . THR B 271 ? 0.9577 1.5642 1.4329 0.0432  0.0041  0.1826  271 THR B C   
4966  O O   . THR B 271 ? 0.9730 1.5860 1.4465 0.0436  0.0050  0.1754  271 THR B O   
4967  C CB  . THR B 271 ? 0.7018 1.3205 1.1722 0.0339  0.0045  0.1890  271 THR B CB  
4968  O OG1 . THR B 271 ? 0.6223 1.2532 1.0904 0.0354  0.0047  0.1833  271 THR B OG1 
4969  C CG2 . THR B 271 ? 0.8072 1.4252 1.2767 0.0276  0.0057  0.1878  271 THR B CG2 
4970  N N   . SER B 272 ? 1.0795 1.6820 1.5582 0.0477  0.0028  0.1883  272 SER B N   
4971  C CA  . SER B 272 ? 1.0827 1.6882 1.5646 0.0538  0.0024  0.1865  272 SER B CA  
4972  C C   . SER B 272 ? 1.1047 1.7066 1.5868 0.0551  0.0046  0.1763  272 SER B C   
4973  O O   . SER B 272 ? 1.0433 1.6560 1.5239 0.0551  0.0053  0.1713  272 SER B O   
4974  C CB  . SER B 272 ? 0.9886 1.6116 1.4691 0.0548  0.0009  0.1892  272 SER B CB  
4975  O OG  . SER B 272 ? 0.8565 1.4898 1.3328 0.0511  0.0021  0.1834  272 SER B OG  
4976  N N   . PRO B 273 ? 1.2926 1.8792 1.7761 0.0562  0.0057  0.1730  273 PRO B N   
4977  C CA  . PRO B 273 ? 1.3009 1.8834 1.7833 0.0574  0.0081  0.1635  273 PRO B CA  
4978  C C   . PRO B 273 ? 1.2792 1.8650 1.7660 0.0633  0.0091  0.1615  273 PRO B C   
4979  O O   . PRO B 273 ? 1.2671 1.8538 1.7527 0.0641  0.0115  0.1541  273 PRO B O   
4980  C CB  . PRO B 273 ? 1.3318 1.8965 1.8136 0.0564  0.0086  0.1614  273 PRO B CB  
4981  C CG  . PRO B 273 ? 1.3798 1.9382 1.8659 0.0581  0.0068  0.1697  273 PRO B CG  
4982  C CD  . PRO B 273 ? 1.3237 1.8954 1.8095 0.0561  0.0049  0.1774  273 PRO B CD  
4983  N N   . HIS B 274 ? 1.2775 1.8652 1.7698 0.0675  0.0074  0.1680  274 HIS B N   
4984  C CA  . HIS B 274 ? 1.2737 1.8657 1.7719 0.0735  0.0080  0.1664  274 HIS B CA  
4985  C C   . HIS B 274 ? 1.2486 1.8575 1.7466 0.0731  0.0082  0.1635  274 HIS B C   
4986  O O   . HIS B 274 ? 1.2344 1.8473 1.7370 0.0769  0.0098  0.1595  274 HIS B O   
4987  C CB  . HIS B 274 ? 1.2921 1.8830 1.7963 0.0780  0.0053  0.1747  274 HIS B CB  
4988  C CG  . HIS B 274 ? 1.3243 1.9208 1.8258 0.0751  0.0020  0.1836  274 HIS B CG  
4989  N ND1 . HIS B 274 ? 1.3925 1.9784 1.8918 0.0720  0.0011  0.1887  274 HIS B ND1 
4990  C CD2 . HIS B 274 ? 1.3090 1.9206 1.8093 0.0746  -0.0004 0.1880  274 HIS B CD2 
4991  C CE1 . HIS B 274 ? 1.3797 1.9739 1.8762 0.0697  -0.0012 0.1963  274 HIS B CE1 
4992  N NE2 . HIS B 274 ? 1.3243 1.9341 1.8210 0.0713  -0.0023 0.1960  274 HIS B NE2 
4993  N N   . ILE B 275 ? 1.1505 1.7693 1.6436 0.0686  0.0068  0.1652  275 ILE B N   
4994  C CA  . ILE B 275 ? 1.1108 1.7447 1.6032 0.0677  0.0069  0.1614  275 ILE B CA  
4995  C C   . ILE B 275 ? 1.0860 1.7171 1.5758 0.0660  0.0104  0.1521  275 ILE B C   
4996  O O   . ILE B 275 ? 1.0244 1.6657 1.5152 0.0662  0.0112  0.1478  275 ILE B O   
4997  C CB  . ILE B 275 ? 1.1029 1.7475 1.5903 0.0633  0.0047  0.1653  275 ILE B CB  
4998  C CG1 . ILE B 275 ? 1.0299 1.6700 1.5110 0.0577  0.0062  0.1614  275 ILE B CG1 
4999  C CG2 . ILE B 275 ? 1.1678 1.8116 1.6557 0.0642  0.0017  0.1753  275 ILE B CG2 
5000  C CD1 . ILE B 275 ? 0.9509 1.6039 1.4275 0.0536  0.0051  0.1622  275 ILE B CD1 
5001  N N   . LEU B 276 ? 1.1445 1.7617 1.6306 0.0641  0.0122  0.1489  276 LEU B N   
5002  C CA  . LEU B 276 ? 1.1322 1.7446 1.6147 0.0628  0.0153  0.1405  276 LEU B CA  
5003  C C   . LEU B 276 ? 1.1726 1.7767 1.6590 0.0675  0.0182  0.1371  276 LEU B C   
5004  O O   . LEU B 276 ? 1.2168 1.8118 1.7066 0.0706  0.0179  0.1402  276 LEU B O   
5005  C CB  . LEU B 276 ? 1.1290 1.7309 1.6050 0.0584  0.0153  0.1385  276 LEU B CB  
5006  C CG  . LEU B 276 ? 1.1181 1.7278 1.5900 0.0532  0.0135  0.1395  276 LEU B CG  
5007  C CD1 . LEU B 276 ? 1.0812 1.6814 1.5474 0.0495  0.0141  0.1344  276 LEU B CD1 
5008  C CD2 . LEU B 276 ? 1.1408 1.7661 1.6128 0.0527  0.0134  0.1377  276 LEU B CD2 
5009  N N   . ALA B 277 ? 1.1153 1.7226 1.6013 0.0679  0.0212  0.1307  277 ALA B N   
5010  C CA  . ALA B 277 ? 1.2048 1.8048 1.6938 0.0720  0.0249  0.1266  277 ALA B CA  
5011  C C   . ALA B 277 ? 1.2692 1.8513 1.7527 0.0715  0.0264  0.1239  277 ALA B C   
5012  O O   . ALA B 277 ? 1.1882 1.7647 1.6638 0.0674  0.0265  0.1205  277 ALA B O   
5013  C CB  . ALA B 277 ? 1.0540 1.6608 1.5427 0.0715  0.0283  0.1204  277 ALA B CB  
5014  N N   . SER B 278 ? 1.5398 2.1128 2.0277 0.0760  0.0273  0.1250  278 SER B N   
5015  C CA  . SER B 278 ? 1.5771 2.1325 2.0603 0.0762  0.0286  0.1220  278 SER B CA  
5016  C C   . SER B 278 ? 1.6258 2.1754 2.1136 0.0818  0.0326  0.1186  278 SER B C   
5017  O O   . SER B 278 ? 1.6716 2.2140 2.1646 0.0858  0.0321  0.1212  278 SER B O   
5018  C CB  . SER B 278 ? 1.5824 2.1301 2.0661 0.0752  0.0248  0.1279  278 SER B CB  
5019  O OG  . SER B 278 ? 1.5757 2.1318 2.0670 0.0776  0.0221  0.1354  278 SER B OG  
5020  N N   . GLY B 279 ? 1.4919 2.0445 1.9779 0.0823  0.0370  0.1125  279 GLY B N   
5021  C CA  . GLY B 279 ? 1.5741 2.1222 2.0643 0.0873  0.0418  0.1086  279 GLY B CA  
5022  C C   . GLY B 279 ? 1.7806 2.3101 2.2642 0.0882  0.0437  0.1044  279 GLY B C   
5023  O O   . GLY B 279 ? 1.8620 2.3836 2.3506 0.0926  0.0439  0.1054  279 GLY B O   
5024  N N   . ASP B 280 ? 2.1924 2.7145 2.6645 0.0841  0.0447  0.0996  280 ASP B N   
5025  C CA  . ASP B 280 ? 2.2240 2.7282 2.6878 0.0841  0.0457  0.0952  280 ASP B CA  
5026  C C   . ASP B 280 ? 2.2430 2.7401 2.7098 0.0898  0.0509  0.0910  280 ASP B C   
5027  O O   . ASP B 280 ? 2.2677 2.7529 2.7359 0.0927  0.0503  0.0909  280 ASP B O   
5028  C CB  . ASP B 280 ? 2.2428 2.7387 2.7065 0.0824  0.0404  0.0994  280 ASP B CB  
5029  C CG  . ASP B 280 ? 2.2235 2.7250 2.6830 0.0764  0.0360  0.1023  280 ASP B CG  
5030  O OD1 . ASP B 280 ? 2.1980 2.7139 2.6628 0.0754  0.0342  0.1071  280 ASP B OD1 
5031  O OD2 . ASP B 280 ? 2.2379 2.7297 2.6890 0.0729  0.0343  0.0995  280 ASP B OD2 
5032  N N   . GLY B 281 ? 1.5496 2.0541 2.0179 0.0913  0.0561  0.0875  281 GLY B N   
5033  C CA  . GLY B 281 ? 1.4087 1.9090 1.8811 0.0968  0.0619  0.0834  281 GLY B CA  
5034  C C   . GLY B 281 ? 1.2715 1.7845 1.7479 0.0975  0.0673  0.0809  281 GLY B C   
5035  O O   . GLY B 281 ? 1.2013 1.7226 1.6739 0.0932  0.0669  0.0810  281 GLY B O   
5036  N N   . THR B 282 ? 1.2446 1.7589 1.7295 0.1031  0.0723  0.0786  282 THR B N   
5037  C CA  . THR B 282 ? 1.1876 1.7142 1.6786 0.1041  0.0780  0.0761  282 THR B CA  
5038  C C   . THR B 282 ? 1.2317 1.7652 1.7390 0.1109  0.0796  0.0775  282 THR B C   
5039  O O   . THR B 282 ? 1.2021 1.7324 1.7129 0.1152  0.0859  0.0728  282 THR B O   
5040  C CB  . THR B 282 ? 1.1143 1.6326 1.5941 0.1030  0.0854  0.0687  282 THR B CB  
5041  O OG1 . THR B 282 ? 1.1514 1.6520 1.6234 0.1053  0.0867  0.0651  282 THR B OG1 
5042  C CG2 . THR B 282 ? 1.0786 1.5972 1.5460 0.0963  0.0843  0.0679  282 THR B CG2 
5043  N N   . ASN B 283 ? 1.4585 2.0023 1.9763 0.1120  0.0736  0.0842  283 ASN B N   
5044  C CA  . ASN B 283 ? 1.4520 2.0053 1.9864 0.1182  0.0738  0.0864  283 ASN B CA  
5045  C C   . ASN B 283 ? 1.4230 1.9962 1.9660 0.1166  0.0731  0.0885  283 ASN B C   
5046  O O   . ASN B 283 ? 1.4231 2.0067 1.9754 0.1181  0.0674  0.0945  283 ASN B O   
5047  C CB  . ASN B 283 ? 1.4763 2.0255 2.0163 0.1213  0.0671  0.0929  283 ASN B CB  
5048  C CG  . ASN B 283 ? 1.5176 2.0477 2.0461 0.1198  0.0653  0.0923  283 ASN B CG  
5049  O OD1 . ASN B 283 ? 1.5181 2.0360 2.0377 0.1195  0.0701  0.0859  283 ASN B OD1 
5050  N ND2 . ASN B 283 ? 1.5247 2.0522 2.0533 0.1186  0.0584  0.0990  283 ASN B ND2 
5051  N N   . ARG B 284 ? 1.1729 1.7510 1.7123 0.1135  0.0786  0.0836  284 ARG B N   
5052  C CA  . ARG B 284 ? 1.1249 1.7195 1.6684 0.1098  0.0779  0.0844  284 ARG B CA  
5053  C C   . ARG B 284 ? 1.0956 1.6911 1.6294 0.1038  0.0718  0.0881  284 ARG B C   
5054  O O   . ARG B 284 ? 1.0457 1.6534 1.5809 0.1001  0.0708  0.0884  284 ARG B O   
5055  C CB  . ARG B 284 ? 1.1582 1.7696 1.7198 0.1140  0.0757  0.0877  284 ARG B CB  
5056  C CG  . ARG B 284 ? 1.1670 1.7887 1.7393 0.1160  0.0828  0.0828  284 ARG B CG  
5057  C CD  . ARG B 284 ? 1.1871 1.8277 1.7769 0.1188  0.0790  0.0863  284 ARG B CD  
5058  N NE  . ARG B 284 ? 1.1809 1.8335 1.7815 0.1192  0.0854  0.0817  284 ARG B NE  
5059  C CZ  . ARG B 284 ? 1.1659 1.8331 1.7709 0.1152  0.0845  0.0814  284 ARG B CZ  
5060  N NH1 . ARG B 284 ? 1.1655 1.8370 1.7646 0.1108  0.0776  0.0854  284 ARG B NH1 
5061  N NH2 . ARG B 284 ? 1.1358 1.8135 1.7516 0.1154  0.0908  0.0771  284 ARG B NH2 
5062  N N   . LYS B 285 ? 1.1123 1.6952 1.6368 0.1026  0.0677  0.0905  285 LYS B N   
5063  C CA  . LYS B 285 ? 1.0787 1.6608 1.5937 0.0970  0.0623  0.0934  285 LYS B CA  
5064  C C   . LYS B 285 ? 1.0668 1.6360 1.5665 0.0928  0.0651  0.0886  285 LYS B C   
5065  O O   . LYS B 285 ? 1.1114 1.6663 1.6055 0.0947  0.0681  0.0852  285 LYS B O   
5066  C CB  . LYS B 285 ? 1.0439 1.6208 1.5598 0.0983  0.0559  0.0996  285 LYS B CB  
5067  N N   . PRO B 286 ? 1.0052 1.5786 1.4977 0.0873  0.0640  0.0878  286 PRO B N   
5068  C CA  . PRO B 286 ? 0.9570 1.5182 1.4349 0.0835  0.0663  0.0833  286 PRO B CA  
5069  C C   . PRO B 286 ? 0.9901 1.5373 1.4591 0.0824  0.0621  0.0845  286 PRO B C   
5070  O O   . PRO B 286 ? 1.0529 1.5999 1.5269 0.0839  0.0575  0.0892  286 PRO B O   
5071  C CB  . PRO B 286 ? 0.9130 1.4841 1.3879 0.0784  0.0648  0.0833  286 PRO B CB  
5072  C CG  . PRO B 286 ? 0.9913 1.5800 1.4800 0.0800  0.0644  0.0858  286 PRO B CG  
5073  C CD  . PRO B 286 ? 1.0155 1.6054 1.5135 0.0847  0.0612  0.0904  286 PRO B CD  
5074  N N   . THR B 287 ? 0.9630 1.4983 1.4188 0.0796  0.0637  0.0802  287 THR B N   
5075  C CA  . THR B 287 ? 0.9837 1.5052 1.4305 0.0780  0.0598  0.0803  287 THR B CA  
5076  C C   . THR B 287 ? 0.9723 1.4997 1.4174 0.0734  0.0536  0.0840  287 THR B C   
5077  O O   . THR B 287 ? 0.9094 1.4379 1.3469 0.0694  0.0532  0.0820  287 THR B O   
5078  C CB  . THR B 287 ? 0.8473 1.3544 1.2803 0.0769  0.0632  0.0741  287 THR B CB  
5079  O OG1 . THR B 287 ? 0.8517 1.3636 1.2830 0.0766  0.0693  0.0706  287 THR B OG1 
5080  C CG2 . THR B 287 ? 0.8638 1.3570 1.2953 0.0810  0.0652  0.0715  287 THR B CG2 
5081  N N   . ILE B 288 ? 1.0684 1.5995 1.5205 0.0740  0.0489  0.0896  288 ILE B N   
5082  C CA  . ILE B 288 ? 1.0928 1.6301 1.5442 0.0699  0.0434  0.0936  288 ILE B CA  
5083  C C   . ILE B 288 ? 1.1984 1.7222 1.6426 0.0676  0.0400  0.0933  288 ILE B C   
5084  O O   . ILE B 288 ? 1.3202 1.8341 1.7660 0.0701  0.0396  0.0941  288 ILE B O   
5085  C CB  . ILE B 288 ? 1.1888 1.7386 1.6514 0.0715  0.0404  0.1002  288 ILE B CB  
5086  C CG1 . ILE B 288 ? 1.0520 1.6172 1.5211 0.0724  0.0426  0.1000  288 ILE B CG1 
5087  C CG2 . ILE B 288 ? 1.2078 1.7610 1.6690 0.0675  0.0350  0.1047  288 ILE B CG2 
5088  C CD1 . ILE B 288 ? 1.1394 1.7152 1.6205 0.0761  0.0409  0.1053  288 ILE B CD1 
5089  N N   . ILE B 289 ? 1.1379 1.6615 1.5749 0.0630  0.0375  0.0921  289 ILE B N   
5090  C CA  . ILE B 289 ? 1.1244 1.6357 1.5545 0.0605  0.0341  0.0909  289 ILE B CA  
5091  C C   . ILE B 289 ? 1.0980 1.6163 1.5317 0.0570  0.0290  0.0960  289 ILE B C   
5092  O O   . ILE B 289 ? 1.0647 1.5810 1.4928 0.0531  0.0262  0.0945  289 ILE B O   
5093  C CB  . ILE B 289 ? 1.0806 1.5840 1.4988 0.0581  0.0351  0.0848  289 ILE B CB  
5094  C CG1 . ILE B 289 ? 1.0511 1.5536 1.4662 0.0607  0.0411  0.0806  289 ILE B CG1 
5095  C CG2 . ILE B 289 ? 1.0427 1.5299 1.4536 0.0573  0.0327  0.0821  289 ILE B CG2 
5096  C CD1 . ILE B 289 ? 1.0136 1.5054 1.4288 0.0651  0.0446  0.0784  289 ILE B CD1 
5097  N N   . GLY B 290 ? 1.1883 1.7147 1.6311 0.0585  0.0279  0.1020  290 GLY B N   
5098  C CA  . GLY B 290 ? 1.1030 1.6351 1.5490 0.0554  0.0236  0.1074  290 GLY B CA  
5099  C C   . GLY B 290 ? 1.1288 1.6748 1.5744 0.0520  0.0222  0.1082  290 GLY B C   
5100  O O   . GLY B 290 ? 1.1370 1.6845 1.5772 0.0505  0.0234  0.1034  290 GLY B O   
5101  N N   . ASP B 291 ? 0.9680 1.5239 1.4190 0.0508  0.0198  0.1142  291 ASP B N   
5102  C CA  . ASP B 291 ? 0.8967 1.4663 1.3477 0.0476  0.0183  0.1153  291 ASP B CA  
5103  C C   . ASP B 291 ? 0.8876 1.4670 1.3389 0.0489  0.0207  0.1122  291 ASP B C   
5104  O O   . ASP B 291 ? 0.8554 1.4374 1.3021 0.0466  0.0209  0.1080  291 ASP B O   
5105  C CB  . ASP B 291 ? 0.8855 1.4514 1.3312 0.0432  0.0163  0.1124  291 ASP B CB  
5106  C CG  . ASP B 291 ? 0.9155 1.4841 1.3642 0.0401  0.0133  0.1176  291 ASP B CG  
5107  O OD1 . ASP B 291 ? 0.9308 1.4994 1.3843 0.0416  0.0129  0.1235  291 ASP B OD1 
5108  O OD2 . ASP B 291 ? 0.8905 1.4611 1.3369 0.0364  0.0116  0.1159  291 ASP B OD2 
5109  N N   . VAL B 292 ? 0.9323 1.5169 1.3894 0.0527  0.0222  0.1145  292 VAL B N   
5110  C CA  . VAL B 292 ? 0.8859 1.4804 1.3452 0.0541  0.0245  0.1119  292 VAL B CA  
5111  C C   . VAL B 292 ? 0.9129 1.5211 1.3797 0.0558  0.0229  0.1173  292 VAL B C   
5112  O O   . VAL B 292 ? 0.9872 1.5938 1.4589 0.0588  0.0220  0.1221  292 VAL B O   
5113  C CB  . VAL B 292 ? 0.9032 1.4897 1.3625 0.0575  0.0287  0.1078  292 VAL B CB  
5114  C CG1 . VAL B 292 ? 0.9131 1.5103 1.3755 0.0582  0.0313  0.1051  292 VAL B CG1 
5115  C CG2 . VAL B 292 ? 0.9742 1.5458 1.4247 0.0560  0.0300  0.1028  292 VAL B CG2 
5116  N N   . TYR B 293 ? 0.8373 1.4589 1.3049 0.0541  0.0222  0.1165  293 TYR B N   
5117  C CA  . TYR B 293 ? 0.7851 1.4208 1.2592 0.0559  0.0206  0.1204  293 TYR B CA  
5118  C C   . TYR B 293 ? 0.8526 1.4947 1.3309 0.0579  0.0232  0.1163  293 TYR B C   
5119  O O   . TYR B 293 ? 0.9387 1.5834 1.4140 0.0554  0.0247  0.1113  293 TYR B O   
5120  C CB  . TYR B 293 ? 0.7836 1.4309 1.2558 0.0525  0.0176  0.1224  293 TYR B CB  
5121  C CG  . TYR B 293 ? 0.7737 1.4364 1.2514 0.0542  0.0159  0.1249  293 TYR B CG  
5122  C CD1 . TYR B 293 ? 0.7983 1.4712 1.2768 0.0530  0.0164  0.1205  293 TYR B CD1 
5123  C CD2 . TYR B 293 ? 0.8092 1.4757 1.2914 0.0571  0.0136  0.1317  293 TYR B CD2 
5124  C CE1 . TYR B 293 ? 0.7293 1.4164 1.2131 0.0545  0.0144  0.1223  293 TYR B CE1 
5125  C CE2 . TYR B 293 ? 0.7682 1.4488 1.2551 0.0589  0.0114  0.1339  293 TYR B CE2 
5126  C CZ  . TYR B 293 ? 0.7001 1.3912 1.1879 0.0575  0.0117  0.1289  293 TYR B CZ  
5127  O OH  . TYR B 293 ? 0.6378 1.3431 1.1304 0.0591  0.0091  0.1307  293 TYR B OH  
5128  N N   . ILE B 294 ? 0.8309 1.4752 1.3167 0.0623  0.0239  0.1185  294 ILE B N   
5129  C CA  . ILE B 294 ? 0.8459 1.4970 1.3378 0.0644  0.0266  0.1150  294 ILE B CA  
5130  C C   . ILE B 294 ? 0.7216 1.3882 1.2213 0.0663  0.0233  0.1190  294 ILE B C   
5131  O O   . ILE B 294 ? 0.6932 1.3607 1.1968 0.0692  0.0206  0.1249  294 ILE B O   
5132  C CB  . ILE B 294 ? 0.8593 1.5002 1.3545 0.0684  0.0305  0.1133  294 ILE B CB  
5133  C CG1 . ILE B 294 ? 0.9079 1.5349 1.3944 0.0663  0.0342  0.1079  294 ILE B CG1 
5134  C CG2 . ILE B 294 ? 0.8581 1.5090 1.3631 0.0715  0.0327  0.1115  294 ILE B CG2 
5135  C CD1 . ILE B 294 ? 0.9316 1.5481 1.4197 0.0701  0.0387  0.1053  294 ILE B CD1 
5136  N N   . HIS B 295 ? 0.7538 1.4325 1.2556 0.0645  0.0231  0.1159  295 HIS B N   
5137  C CA  . HIS B 295 ? 0.7106 1.4046 1.2199 0.0663  0.0197  0.1188  295 HIS B CA  
5138  C C   . HIS B 295 ? 0.7947 1.4905 1.3145 0.0714  0.0213  0.1191  295 HIS B C   
5139  O O   . HIS B 295 ? 0.7860 1.4754 1.3077 0.0723  0.0262  0.1146  295 HIS B O   
5140  C CB  . HIS B 295 ? 0.6911 1.3968 1.2000 0.0629  0.0191  0.1146  295 HIS B CB  
5141  C CG  . HIS B 295 ? 0.6679 1.3895 1.1819 0.0638  0.0144  0.1176  295 HIS B CG  
5142  N ND1 . HIS B 295 ? 0.7162 1.4476 1.2407 0.0671  0.0137  0.1175  295 HIS B ND1 
5143  C CD2 . HIS B 295 ? 0.7395 1.4692 1.2491 0.0619  0.0102  0.1205  295 HIS B CD2 
5144  C CE1 . HIS B 295 ? 0.7797 1.5241 1.3057 0.0673  0.0086  0.1204  295 HIS B CE1 
5145  N NE2 . HIS B 295 ? 0.7837 1.5273 1.3003 0.0641  0.0066  0.1222  295 HIS B NE2 
5146  N N   . PRO B 296 ? 0.7358 1.4403 1.2625 0.0750  0.0173  0.1243  296 PRO B N   
5147  C CA  . PRO B 296 ? 0.7493 1.4566 1.2876 0.0803  0.0185  0.1244  296 PRO B CA  
5148  C C   . PRO B 296 ? 0.7172 1.4349 1.2633 0.0800  0.0210  0.1186  296 PRO B C   
5149  O O   . PRO B 296 ? 0.6719 1.3900 1.2275 0.0838  0.0239  0.1169  296 PRO B O   
5150  C CB  . PRO B 296 ? 0.8365 1.5518 1.3792 0.0837  0.0124  0.1318  296 PRO B CB  
5151  C CG  . PRO B 296 ? 0.7920 1.5137 1.3262 0.0794  0.0085  0.1340  296 PRO B CG  
5152  C CD  . PRO B 296 ? 0.7047 1.4152 1.2286 0.0747  0.0117  0.1308  296 PRO B CD  
5153  N N   . SER B 297 ? 0.7169 1.4428 1.2599 0.0755  0.0203  0.1152  297 SER B N   
5154  C CA  . SER B 297 ? 0.7557 1.4919 1.3065 0.0744  0.0223  0.1099  297 SER B CA  
5155  C C   . SER B 297 ? 0.7867 1.5137 1.3344 0.0718  0.0292  0.1036  297 SER B C   
5156  O O   . SER B 297 ? 0.8027 1.5369 1.3556 0.0699  0.0316  0.0989  297 SER B O   
5157  C CB  . SER B 297 ? 0.7789 1.5282 1.3279 0.0708  0.0179  0.1090  297 SER B CB  
5158  O OG  . SER B 297 ? 0.8455 1.6055 1.4035 0.0698  0.0193  0.1040  297 SER B OG  
5159  N N   . VAL B 298 ? 0.8481 1.5593 1.3872 0.0715  0.0324  0.1035  298 VAL B N   
5160  C CA  . VAL B 298 ? 0.9780 1.6792 1.5120 0.0691  0.0386  0.0980  298 VAL B CA  
5161  C C   . VAL B 298 ? 1.0641 1.7625 1.6064 0.0730  0.0440  0.0960  298 VAL B C   
5162  O O   . VAL B 298 ? 1.0098 1.7104 1.5603 0.0780  0.0429  0.0991  298 VAL B O   
5163  C CB  . VAL B 298 ? 1.0407 1.7263 1.5612 0.0669  0.0391  0.0983  298 VAL B CB  
5164  C CG1 . VAL B 298 ? 0.9153 1.6045 1.4294 0.0639  0.0336  0.1011  298 VAL B CG1 
5165  C CG2 . VAL B 298 ? 1.1162 1.7903 1.6364 0.0711  0.0402  0.1010  298 VAL B CG2 
5166  N N   . LYS B 299 ? 1.5305 2.2238 2.0704 0.0707  0.0502  0.0907  299 LYS B N   
5167  C CA  . LYS B 299 ? 1.5475 2.2363 2.0929 0.0737  0.0568  0.0878  299 LYS B CA  
5168  C C   . LYS B 299 ? 1.5683 2.2388 2.1006 0.0725  0.0613  0.0855  299 LYS B C   
5169  O O   . LYS B 299 ? 1.5679 2.2329 2.0899 0.0679  0.0623  0.0830  299 LYS B O   
5170  C CB  . LYS B 299 ? 1.5462 2.2455 2.1005 0.0719  0.0610  0.0835  299 LYS B CB  
5171  C CG  . LYS B 299 ? 1.6245 2.3194 2.1839 0.0743  0.0691  0.0800  299 LYS B CG  
5172  C CD  . LYS B 299 ? 1.6244 2.3307 2.1938 0.0719  0.0733  0.0760  299 LYS B CD  
5173  C CE  . LYS B 299 ? 1.6865 2.4113 2.2729 0.0745  0.0690  0.0776  299 LYS B CE  
5174  N NZ  . LYS B 299 ? 1.7238 2.4500 2.3209 0.0812  0.0699  0.0794  299 LYS B NZ  
5175  N N   . LEU B 300 ? 1.2712 1.9321 1.8038 0.0768  0.0636  0.0862  300 LEU B N   
5176  C CA  . LEU B 300 ? 1.1929 1.8359 1.7125 0.0762  0.0667  0.0842  300 LEU B CA  
5177  C C   . LEU B 300 ? 1.2045 1.8410 1.7263 0.0791  0.0745  0.0803  300 LEU B C   
5178  O O   . LEU B 300 ? 1.2416 1.8868 1.7765 0.0828  0.0771  0.0798  300 LEU B O   
5179  C CB  . LEU B 300 ? 1.2001 1.8344 1.7149 0.0781  0.0617  0.0885  300 LEU B CB  
5180  C CG  . LEU B 300 ? 1.2503 1.8899 1.7619 0.0752  0.0545  0.0927  300 LEU B CG  
5181  C CD1 . LEU B 300 ? 1.2896 1.9202 1.7978 0.0771  0.0505  0.0972  300 LEU B CD1 
5182  C CD2 . LEU B 300 ? 1.2296 1.8660 1.7300 0.0694  0.0546  0.0899  300 LEU B CD2 
5183  N N   . HIS B 301 ? 1.0122 1.6333 1.5207 0.0775  0.0781  0.0773  301 HIS B N   
5184  C CA  . HIS B 301 ? 0.9061 1.5180 1.4130 0.0802  0.0858  0.0733  301 HIS B CA  
5185  C C   . HIS B 301 ? 0.8988 1.4936 1.3950 0.0819  0.0845  0.0734  301 HIS B C   
5186  O O   . HIS B 301 ? 0.9280 1.5149 1.4124 0.0785  0.0805  0.0743  301 HIS B O   
5187  C CB  . HIS B 301 ? 0.8289 1.4382 1.3286 0.0761  0.0922  0.0687  301 HIS B CB  
5188  C CG  . HIS B 301 ? 0.8310 1.4359 1.3324 0.0788  0.1012  0.0645  301 HIS B CG  
5189  N ND1 . HIS B 301 ? 0.8144 1.4030 1.3049 0.0807  0.1048  0.0620  301 HIS B ND1 
5190  C CD2 . HIS B 301 ? 0.8208 1.4355 1.3333 0.0796  0.1076  0.0622  301 HIS B CD2 
5191  C CE1 . HIS B 301 ? 0.8032 1.3919 1.2976 0.0829  0.1133  0.0583  301 HIS B CE1 
5192  N NE2 . HIS B 301 ? 0.7950 1.3996 1.3032 0.0821  0.1153  0.0584  301 HIS B NE2 
5193  N N   . PRO B 302 ? 0.8891 1.4781 1.3896 0.0871  0.0875  0.0725  302 PRO B N   
5194  C CA  . PRO B 302 ? 0.8674 1.4403 1.3589 0.0889  0.0855  0.0727  302 PRO B CA  
5195  C C   . PRO B 302 ? 0.8657 1.4231 1.3395 0.0856  0.0881  0.0686  302 PRO B C   
5196  O O   . PRO B 302 ? 0.8995 1.4439 1.3647 0.0858  0.0851  0.0688  302 PRO B O   
5197  C CB  . PRO B 302 ? 0.9463 1.5173 1.4475 0.0955  0.0894  0.0715  302 PRO B CB  
5198  C CG  . PRO B 302 ? 1.0001 1.5893 1.5181 0.0975  0.0907  0.0726  302 PRO B CG  
5199  C CD  . PRO B 302 ? 0.9182 1.5155 1.4331 0.0919  0.0925  0.0710  302 PRO B CD  
5200  N N   . THR B 303 ? 0.8265 1.3848 1.2947 0.0825  0.0935  0.0650  303 THR B N   
5201  C CA  . THR B 303 ? 0.8128 1.3563 1.2635 0.0796  0.0962  0.0612  303 THR B CA  
5202  C C   . THR B 303 ? 0.7899 1.3308 1.2303 0.0743  0.0903  0.0628  303 THR B C   
5203  O O   . THR B 303 ? 0.7733 1.3011 1.1985 0.0720  0.0909  0.0601  303 THR B O   
5204  C CB  . THR B 303 ? 0.7759 1.3205 1.2245 0.0786  0.1052  0.0570  303 THR B CB  
5205  O OG1 . THR B 303 ? 0.7630 1.3225 1.2196 0.0755  0.1051  0.0585  303 THR B OG1 
5206  C CG2 . THR B 303 ? 0.7752 1.3206 1.2328 0.0841  0.1119  0.0545  303 THR B CG2 
5207  N N   . ALA B 304 ? 0.7778 1.3306 1.2257 0.0726  0.0844  0.0669  304 ALA B N   
5208  C CA  . ALA B 304 ? 0.7227 1.2745 1.1624 0.0679  0.0788  0.0682  304 ALA B CA  
5209  C C   . ALA B 304 ? 0.7197 1.2625 1.1547 0.0683  0.0727  0.0704  304 ALA B C   
5210  O O   . ALA B 304 ? 0.7754 1.3198 1.2185 0.0716  0.0705  0.0732  304 ALA B O   
5211  C CB  . ALA B 304 ? 0.7102 1.2790 1.1599 0.0658  0.0755  0.0712  304 ALA B CB  
5212  N N   . LYS B 305 ? 0.6830 1.2167 1.1055 0.0648  0.0697  0.0692  305 LYS B N   
5213  C CA  . LYS B 305 ? 0.6875 1.2134 1.1058 0.0642  0.0636  0.0711  305 LYS B CA  
5214  C C   . LYS B 305 ? 0.8511 1.3867 1.2718 0.0606  0.0577  0.0744  305 LYS B C   
5215  O O   . LYS B 305 ? 0.7800 1.3152 1.1935 0.0570  0.0567  0.0727  305 LYS B O   
5216  C CB  . LYS B 305 ? 0.6731 1.1817 1.0762 0.0631  0.0639  0.0671  305 LYS B CB  
5217  C CG  . LYS B 305 ? 0.7366 1.2372 1.1365 0.0623  0.0575  0.0686  305 LYS B CG  
5218  C CD  . LYS B 305 ? 0.7426 1.2262 1.1277 0.0613  0.0571  0.0643  305 LYS B CD  
5219  C CE  . LYS B 305 ? 0.8121 1.2842 1.1943 0.0653  0.0613  0.0611  305 LYS B CE  
5220  N NZ  . LYS B 305 ? 0.6926 1.1479 1.0597 0.0642  0.0597  0.0569  305 LYS B NZ  
5221  N N   . ILE B 306 ? 0.7684 1.3125 1.1990 0.0617  0.0539  0.0790  306 ILE B N   
5222  C CA  . ILE B 306 ? 0.8400 1.3943 1.2734 0.0587  0.0487  0.0824  306 ILE B CA  
5223  C C   . ILE B 306 ? 1.0120 1.5574 1.4403 0.0572  0.0438  0.0838  306 ILE B C   
5224  O O   . ILE B 306 ? 1.0230 1.5668 1.4562 0.0590  0.0416  0.0873  306 ILE B O   
5225  C CB  . ILE B 306 ? 0.7975 1.3668 1.2439 0.0606  0.0475  0.0868  306 ILE B CB  
5226  C CG1 . ILE B 306 ? 0.7438 1.3192 1.1971 0.0635  0.0529  0.0850  306 ILE B CG1 
5227  C CG2 . ILE B 306 ? 0.8326 1.4143 1.2808 0.0572  0.0437  0.0887  306 ILE B CG2 
5228  C CD1 . ILE B 306 ? 0.7116 1.2914 1.1619 0.0607  0.0561  0.0813  306 ILE B CD1 
5229  N N   . GLY B 307 ? 1.5033 2.0426 1.9220 0.0538  0.0419  0.0812  307 GLY B N   
5230  C CA  . GLY B 307 ? 1.5138 2.0439 1.9274 0.0521  0.0375  0.0815  307 GLY B CA  
5231  C C   . GLY B 307 ? 1.4987 2.0379 1.9184 0.0501  0.0325  0.0861  307 GLY B C   
5232  O O   . GLY B 307 ? 1.4818 2.0331 1.9104 0.0510  0.0323  0.0901  307 GLY B O   
5233  N N   . PRO B 308 ? 1.1302 1.6639 1.5451 0.0472  0.0285  0.0857  308 PRO B N   
5234  C CA  . PRO B 308 ? 1.1016 1.6432 1.5222 0.0450  0.0243  0.0900  308 PRO B CA  
5235  C C   . PRO B 308 ? 1.0309 1.5862 1.4533 0.0425  0.0231  0.0904  308 PRO B C   
5236  O O   . PRO B 308 ? 1.0047 1.5603 1.4222 0.0415  0.0242  0.0866  308 PRO B O   
5237  C CB  . PRO B 308 ? 1.1279 1.6579 1.5430 0.0428  0.0208  0.0884  308 PRO B CB  
5238  C CG  . PRO B 308 ? 1.1040 1.6243 1.5088 0.0426  0.0221  0.0825  308 PRO B CG  
5239  C CD  . PRO B 308 ? 1.0928 1.6124 1.4971 0.0459  0.0275  0.0811  308 PRO B CD  
5240  N N   . ASN B 309 ? 0.9175 1.4835 1.3467 0.0416  0.0210  0.0952  309 ASN B N   
5241  C CA  . ASN B 309 ? 0.8666 1.4458 1.2977 0.0391  0.0193  0.0957  309 ASN B CA  
5242  C C   . ASN B 309 ? 0.8283 1.4159 1.2602 0.0400  0.0219  0.0935  309 ASN B C   
5243  O O   . ASN B 309 ? 0.8092 1.3979 1.2371 0.0382  0.0219  0.0896  309 ASN B O   
5244  C CB  . ASN B 309 ? 0.8607 1.4359 1.2867 0.0358  0.0164  0.0927  309 ASN B CB  
5245  C CG  . ASN B 309 ? 0.7912 1.3797 1.2196 0.0333  0.0146  0.0930  309 ASN B CG  
5246  O OD1 . ASN B 309 ? 0.7607 1.3615 1.1946 0.0336  0.0149  0.0964  309 ASN B OD1 
5247  N ND2 . ASN B 309 ? 0.7298 1.3158 1.1540 0.0311  0.0127  0.0893  309 ASN B ND2 
5248  N N   . VAL B 310 ? 0.8226 1.4160 1.2604 0.0428  0.0240  0.0959  310 VAL B N   
5249  C CA  . VAL B 310 ? 0.8275 1.4303 1.2683 0.0436  0.0264  0.0942  310 VAL B CA  
5250  C C   . VAL B 310 ? 0.9106 1.5269 1.3597 0.0450  0.0253  0.0990  310 VAL B C   
5251  O O   . VAL B 310 ? 0.9425 1.5573 1.3957 0.0475  0.0250  0.1031  310 VAL B O   
5252  C CB  . VAL B 310 ? 0.8200 1.4148 1.2590 0.0460  0.0309  0.0910  310 VAL B CB  
5253  C CG1 . VAL B 310 ? 0.9117 1.4978 1.3525 0.0491  0.0318  0.0932  310 VAL B CG1 
5254  C CG2 . VAL B 310 ? 0.8646 1.4708 1.3096 0.0469  0.0334  0.0902  310 VAL B CG2 
5255  N N   . SER B 311 ? 0.9838 1.6130 1.4353 0.0436  0.0244  0.0983  311 SER B N   
5256  C CA  . SER B 311 ? 0.9617 1.6050 1.4200 0.0446  0.0227  0.1025  311 SER B CA  
5257  C C   . SER B 311 ? 1.1284 1.7805 1.5911 0.0455  0.0246  0.0997  311 SER B C   
5258  O O   . SER B 311 ? 1.0138 1.6714 1.4749 0.0431  0.0245  0.0960  311 SER B O   
5259  C CB  . SER B 311 ? 0.7447 1.3963 1.2016 0.0418  0.0194  0.1043  311 SER B CB  
5260  O OG  . SER B 311 ? 0.7054 1.3484 1.1585 0.0402  0.0180  0.1059  311 SER B OG  
5261  N N   . ILE B 312 ? 1.7255 2.3791 2.1944 0.0490  0.0263  0.1012  312 ILE B N   
5262  C CA  . ILE B 312 ? 1.7148 2.3763 2.1894 0.0500  0.0286  0.0984  312 ILE B CA  
5263  C C   . ILE B 312 ? 1.6991 2.3768 2.1807 0.0508  0.0254  0.1015  312 ILE B C   
5264  O O   . ILE B 312 ? 1.7025 2.3832 2.1868 0.0528  0.0227  0.1069  312 ILE B O   
5265  C CB  . ILE B 312 ? 1.7278 2.3821 2.2059 0.0535  0.0327  0.0977  312 ILE B CB  
5266  C CG1 . ILE B 312 ? 1.7493 2.3865 2.2197 0.0535  0.0345  0.0965  312 ILE B CG1 
5267  C CG2 . ILE B 312 ? 1.7204 2.3788 2.2019 0.0530  0.0365  0.0930  312 ILE B CG2 
5268  C CD1 . ILE B 312 ? 1.7648 2.3939 2.2373 0.0569  0.0390  0.0950  312 ILE B CD1 
5269  N N   . SER B 313 ? 1.1633 1.8510 1.6475 0.0490  0.0254  0.0980  313 SER B N   
5270  C CA  . SER B 313 ? 0.9551 1.6586 1.4450 0.0494  0.0220  0.0998  313 SER B CA  
5271  C C   . SER B 313 ? 0.8898 1.6003 1.3900 0.0527  0.0230  0.1001  313 SER B C   
5272  O O   . SER B 313 ? 0.9200 1.6230 1.4230 0.0550  0.0268  0.0993  313 SER B O   
5273  C CB  . SER B 313 ? 0.7549 1.4656 1.2422 0.0455  0.0209  0.0954  313 SER B CB  
5274  O OG  . SER B 313 ? 0.7568 1.4625 1.2359 0.0428  0.0196  0.0953  313 SER B OG  
5275  N N   . ALA B 314 ? 0.7986 1.5239 1.3046 0.0531  0.0197  0.1009  314 ALA B N   
5276  C CA  . ALA B 314 ? 0.7372 1.4711 1.2543 0.0565  0.0196  0.1016  314 ALA B CA  
5277  C C   . ALA B 314 ? 0.7585 1.4952 1.2809 0.0549  0.0234  0.0954  314 ALA B C   
5278  O O   . ALA B 314 ? 0.7332 1.4693 1.2513 0.0509  0.0246  0.0910  314 ALA B O   
5279  C CB  . ALA B 314 ? 0.6808 1.4297 1.2016 0.0575  0.0138  0.1049  314 ALA B CB  
5280  N N   . ASN B 315 ? 0.7403 1.4801 1.2730 0.0582  0.0256  0.0953  315 ASN B N   
5281  C CA  . ASN B 315 ? 0.7201 1.4655 1.2608 0.0570  0.0291  0.0902  315 ASN B CA  
5282  C C   . ASN B 315 ? 0.7922 1.5261 1.3257 0.0533  0.0346  0.0854  315 ASN B C   
5283  O O   . ASN B 315 ? 0.7816 1.5195 1.3156 0.0495  0.0356  0.0810  315 ASN B O   
5284  C CB  . ASN B 315 ? 0.6724 1.4341 1.2187 0.0551  0.0247  0.0885  315 ASN B CB  
5285  C CG  . ASN B 315 ? 0.6418 1.4160 1.1972 0.0592  0.0196  0.0926  315 ASN B CG  
5286  O OD1 . ASN B 315 ? 0.6445 1.4221 1.1953 0.0601  0.0144  0.0970  315 ASN B OD1 
5287  N ND2 . ASN B 315 ? 0.6872 1.4685 1.2555 0.0617  0.0211  0.0914  315 ASN B ND2 
5288  N N   . VAL B 316 ? 0.9350 1.6541 1.4616 0.0544  0.0380  0.0862  316 VAL B N   
5289  C CA  . VAL B 316 ? 0.9110 1.6174 1.4293 0.0515  0.0431  0.0823  316 VAL B CA  
5290  C C   . VAL B 316 ? 0.9035 1.6022 1.4250 0.0543  0.0492  0.0813  316 VAL B C   
5291  O O   . VAL B 316 ? 0.9133 1.6099 1.4382 0.0587  0.0489  0.0845  316 VAL B O   
5292  C CB  . VAL B 316 ? 0.9079 1.6028 1.4131 0.0497  0.0411  0.0834  316 VAL B CB  
5293  C CG1 . VAL B 316 ? 0.9654 1.6538 1.4689 0.0534  0.0396  0.0881  316 VAL B CG1 
5294  C CG2 . VAL B 316 ? 0.9323 1.6140 1.4284 0.0470  0.0456  0.0795  316 VAL B CG2 
5295  N N   . ARG B 317 ? 0.8243 1.5184 1.3443 0.0519  0.0549  0.0770  317 ARG B N   
5296  C CA  . ARG B 317 ? 0.8976 1.5855 1.4206 0.0541  0.0617  0.0753  317 ARG B CA  
5297  C C   . ARG B 317 ? 0.8516 1.5212 1.3604 0.0531  0.0653  0.0740  317 ARG B C   
5298  O O   . ARG B 317 ? 0.7939 1.4571 1.2940 0.0491  0.0670  0.0713  317 ARG B O   
5299  C CB  . ARG B 317 ? 0.9361 1.6324 1.4681 0.0519  0.0663  0.0715  317 ARG B CB  
5300  C CG  . ARG B 317 ? 0.9010 1.6158 1.4488 0.0535  0.0630  0.0723  317 ARG B CG  
5301  C CD  . ARG B 317 ? 0.9413 1.6633 1.5008 0.0527  0.0690  0.0687  317 ARG B CD  
5302  N NE  . ARG B 317 ? 0.9683 1.6885 1.5238 0.0469  0.0721  0.0649  317 ARG B NE  
5303  C CZ  . ARG B 317 ? 0.9557 1.6880 1.5185 0.0435  0.0695  0.0630  317 ARG B CZ  
5304  N NH1 . ARG B 317 ? 0.9066 1.6543 1.4806 0.0454  0.0637  0.0643  317 ARG B NH1 
5305  N NH2 . ARG B 317 ? 1.0022 1.7310 1.5609 0.0383  0.0726  0.0596  317 ARG B NH2 
5306  N N   . VAL B 318 ? 0.9294 1.5900 1.4357 0.0570  0.0660  0.0759  318 VAL B N   
5307  C CA  . VAL B 318 ? 0.8756 1.5186 1.3686 0.0567  0.0688  0.0746  318 VAL B CA  
5308  C C   . VAL B 318 ? 0.8609 1.4981 1.3551 0.0584  0.0769  0.0716  318 VAL B C   
5309  O O   . VAL B 318 ? 0.9311 1.5732 1.4358 0.0626  0.0790  0.0722  318 VAL B O   
5310  C CB  . VAL B 318 ? 0.9095 1.5452 1.3984 0.0595  0.0646  0.0782  318 VAL B CB  
5311  C CG1 . VAL B 318 ? 0.8286 1.4463 1.3057 0.0600  0.0679  0.0762  318 VAL B CG1 
5312  C CG2 . VAL B 318 ? 0.9463 1.5856 1.4313 0.0569  0.0576  0.0808  318 VAL B CG2 
5313  N N   . GLY B 319 ? 0.8004 1.4273 1.2839 0.0553  0.0814  0.0683  319 GLY B N   
5314  C CA  . GLY B 319 ? 0.7883 1.4087 1.2706 0.0565  0.0897  0.0653  319 GLY B CA  
5315  C C   . GLY B 319 ? 0.7516 1.3579 1.2262 0.0601  0.0913  0.0651  319 GLY B C   
5316  O O   . GLY B 319 ? 0.7820 1.3834 1.2530 0.0617  0.0857  0.0676  319 GLY B O   
5317  N N   . PRO B 320 ? 0.7444 1.3436 1.2161 0.0613  0.0992  0.0620  320 PRO B N   
5318  C CA  . PRO B 320 ? 0.7280 1.3134 1.1921 0.0649  0.1013  0.0610  320 PRO B CA  
5319  C C   . PRO B 320 ? 0.7723 1.3407 1.2170 0.0622  0.1007  0.0594  320 PRO B C   
5320  O O   . PRO B 320 ? 0.7929 1.3580 1.2290 0.0580  0.1024  0.0580  320 PRO B O   
5321  C CB  . PRO B 320 ? 0.7738 1.3610 1.2443 0.0673  0.1106  0.0578  320 PRO B CB  
5322  C CG  . PRO B 320 ? 0.8473 1.4404 1.3181 0.0625  0.1146  0.0563  320 PRO B CG  
5323  C CD  . PRO B 320 ? 0.8507 1.4550 1.3270 0.0595  0.1069  0.0591  320 PRO B CD  
5324  N N   . GLY B 321 ? 0.7379 1.2951 1.1760 0.0648  0.0980  0.0597  321 GLY B N   
5325  C CA  . GLY B 321 ? 0.7163 1.2567 1.1363 0.0629  0.0970  0.0579  321 GLY B CA  
5326  C C   . GLY B 321 ? 0.6201 1.1600 1.0327 0.0583  0.0910  0.0593  321 GLY B C   
5327  O O   . GLY B 321 ? 0.7117 1.2405 1.1100 0.0557  0.0918  0.0573  321 GLY B O   
5328  N N   . VAL B 322 ? 0.6376 1.1892 1.0595 0.0574  0.0849  0.0626  322 VAL B N   
5329  C CA  . VAL B 322 ? 0.7213 1.2737 1.1376 0.0534  0.0791  0.0637  322 VAL B CA  
5330  C C   . VAL B 322 ? 0.7220 1.2676 1.1337 0.0539  0.0724  0.0655  322 VAL B C   
5331  O O   . VAL B 322 ? 0.6750 1.2204 1.0922 0.0571  0.0710  0.0673  322 VAL B O   
5332  C CB  . VAL B 322 ? 0.6830 1.2527 1.1114 0.0516  0.0768  0.0656  322 VAL B CB  
5333  C CG1 . VAL B 322 ? 0.7572 1.3344 1.1924 0.0510  0.0835  0.0637  322 VAL B CG1 
5334  C CG2 . VAL B 322 ? 0.6570 1.2369 1.0971 0.0543  0.0722  0.0693  322 VAL B CG2 
5335  N N   . ARG B 323 ? 0.6503 1.1901 1.0521 0.0506  0.0683  0.0650  323 ARG B N   
5336  C CA  . ARG B 323 ? 0.6120 1.1446 1.0086 0.0504  0.0621  0.0661  323 ARG B CA  
5337  C C   . ARG B 323 ? 0.6066 1.1493 1.0075 0.0476  0.0561  0.0685  323 ARG B C   
5338  O O   . ARG B 323 ? 0.5841 1.1295 0.9820 0.0447  0.0558  0.0673  323 ARG B O   
5339  C CB  . ARG B 323 ? 0.6413 1.1570 1.0218 0.0493  0.0621  0.0629  323 ARG B CB  
5340  C CG  . ARG B 323 ? 0.6896 1.1969 1.0653 0.0492  0.0559  0.0635  323 ARG B CG  
5341  C CD  . ARG B 323 ? 0.7038 1.2042 1.0811 0.0527  0.0571  0.0635  323 ARG B CD  
5342  N NE  . ARG B 323 ? 0.8019 1.2933 1.1743 0.0520  0.0512  0.0636  323 ARG B NE  
5343  C CZ  . ARG B 323 ? 0.8350 1.3317 1.2159 0.0521  0.0465  0.0672  323 ARG B CZ  
5344  N NH1 . ARG B 323 ? 0.8451 1.3557 1.2386 0.0530  0.0469  0.0709  323 ARG B NH1 
5345  N NH2 . ARG B 323 ? 0.8759 1.3643 1.2528 0.0510  0.0415  0.0671  323 ARG B NH2 
5346  N N   . LEU B 324 ? 0.6590 1.2071 1.0669 0.0486  0.0517  0.0719  324 LEU B N   
5347  C CA  . LEU B 324 ? 0.6611 1.2203 1.0740 0.0463  0.0466  0.0744  324 LEU B CA  
5348  C C   . LEU B 324 ? 0.7643 1.3183 1.1748 0.0458  0.0412  0.0762  324 LEU B C   
5349  O O   . LEU B 324 ? 0.8639 1.4178 1.2795 0.0480  0.0403  0.0791  324 LEU B O   
5350  C CB  . LEU B 324 ? 0.6755 1.2504 1.1015 0.0478  0.0469  0.0774  324 LEU B CB  
5351  C CG  . LEU B 324 ? 0.6108 1.1924 1.0421 0.0486  0.0522  0.0757  324 LEU B CG  
5352  C CD1 . LEU B 324 ? 0.5882 1.1853 1.0328 0.0504  0.0513  0.0788  324 LEU B CD1 
5353  C CD2 . LEU B 324 ? 0.6400 1.2226 1.0664 0.0450  0.0533  0.0727  324 LEU B CD2 
5354  N N   . ILE B 325 ? 0.7716 1.3216 1.1752 0.0429  0.0377  0.0747  325 ILE B N   
5355  C CA  . ILE B 325 ? 0.7949 1.3418 1.1976 0.0418  0.0325  0.0764  325 ILE B CA  
5356  C C   . ILE B 325 ? 0.7192 1.2744 1.1228 0.0388  0.0287  0.0764  325 ILE B C   
5357  O O   . ILE B 325 ? 0.6874 1.2436 1.0873 0.0373  0.0293  0.0737  325 ILE B O   
5358  C CB  . ILE B 325 ? 0.8162 1.3461 1.2086 0.0419  0.0316  0.0736  325 ILE B CB  
5359  C CG1 . ILE B 325 ? 0.7046 1.2279 1.0867 0.0399  0.0311  0.0697  325 ILE B CG1 
5360  C CG2 . ILE B 325 ? 0.8552 1.3763 1.2458 0.0451  0.0359  0.0726  325 ILE B CG2 
5361  C CD1 . ILE B 325 ? 0.7466 1.2532 1.1174 0.0401  0.0297  0.0668  325 ILE B CD1 
5362  N N   . SER B 326 ? 0.7658 1.3268 1.1746 0.0378  0.0249  0.0796  326 SER B N   
5363  C CA  . SER B 326 ? 0.7422 1.3100 1.1517 0.0350  0.0210  0.0794  326 SER B CA  
5364  C C   . SER B 326 ? 0.7698 1.3495 1.1823 0.0341  0.0220  0.0783  326 SER B C   
5365  O O   . SER B 326 ? 0.7249 1.3052 1.1341 0.0322  0.0203  0.0756  326 SER B O   
5366  C CB  . SER B 326 ? 0.6721 1.2286 1.0732 0.0334  0.0182  0.0759  326 SER B CB  
5367  O OG  . SER B 326 ? 0.6566 1.2014 1.0546 0.0342  0.0170  0.0762  326 SER B OG  
5368  N N   . CYS B 327 ? 0.9142 1.5035 1.3334 0.0356  0.0245  0.0804  327 CYS B N   
5369  C CA  . CYS B 327 ? 0.8948 1.4951 1.3172 0.0347  0.0255  0.0790  327 CYS B CA  
5370  C C   . CYS B 327 ? 0.8800 1.4943 1.3116 0.0358  0.0255  0.0827  327 CYS B C   
5371  O O   . CYS B 327 ? 0.9130 1.5270 1.3481 0.0379  0.0256  0.0864  327 CYS B O   
5372  C CB  . CYS B 327 ? 0.9035 1.4980 1.3223 0.0352  0.0298  0.0757  327 CYS B CB  
5373  S SG  . CYS B 327 ? 0.9137 1.5032 1.3348 0.0386  0.0345  0.0771  327 CYS B SG  
5374  N N   . ILE B 328 ? 0.6638 1.2901 1.0989 0.0346  0.0250  0.0816  328 ILE B N   
5375  C CA  . ILE B 328 ? 0.6150 1.2554 1.0581 0.0356  0.0245  0.0846  328 ILE B CA  
5376  C C   . ILE B 328 ? 0.5961 1.2433 1.0426 0.0354  0.0268  0.0816  328 ILE B C   
5377  O O   . ILE B 328 ? 0.5702 1.2163 1.0135 0.0332  0.0270  0.0776  328 ILE B O   
5378  C CB  . ILE B 328 ? 0.5355 1.1861 0.9802 0.0341  0.0208  0.0866  328 ILE B CB  
5379  C CG1 . ILE B 328 ? 0.4870 1.1384 0.9279 0.0313  0.0194  0.0822  328 ILE B CG1 
5380  C CG2 . ILE B 328 ? 0.6346 1.2807 1.0785 0.0344  0.0190  0.0908  328 ILE B CG2 
5381  C CD1 . ILE B 328 ? 0.5255 1.1874 0.9680 0.0298  0.0164  0.0835  328 ILE B CD1 
5382  N N   . ILE B 329 ? 0.5978 1.2519 1.0513 0.0376  0.0283  0.0835  329 ILE B N   
5383  C CA  . ILE B 329 ? 0.5313 1.1919 0.9897 0.0375  0.0308  0.0809  329 ILE B CA  
5384  C C   . ILE B 329 ? 0.6164 1.2935 1.0827 0.0379  0.0281  0.0827  329 ILE B C   
5385  O O   . ILE B 329 ? 0.7399 1.4217 1.2098 0.0402  0.0262  0.0873  329 ILE B O   
5386  C CB  . ILE B 329 ? 0.5119 1.1659 0.9725 0.0400  0.0353  0.0808  329 ILE B CB  
5387  C CG1 . ILE B 329 ? 0.4994 1.1366 0.9505 0.0395  0.0379  0.0786  329 ILE B CG1 
5388  C CG2 . ILE B 329 ? 0.5249 1.1871 0.9923 0.0396  0.0382  0.0781  329 ILE B CG2 
5389  C CD1 . ILE B 329 ? 0.6196 1.2491 1.0714 0.0422  0.0426  0.0785  329 ILE B CD1 
5390  N N   . LEU B 330 ? 0.5825 1.2679 1.0511 0.0358  0.0277  0.0792  330 LEU B N   
5391  C CA  . LEU B 330 ? 0.5663 1.2676 1.0414 0.0358  0.0248  0.0800  330 LEU B CA  
5392  C C   . LEU B 330 ? 0.5511 1.2590 1.0355 0.0378  0.0267  0.0801  330 LEU B C   
5393  O O   . LEU B 330 ? 0.6247 1.3251 1.1105 0.0395  0.0306  0.0801  330 LEU B O   
5394  C CB  . LEU B 330 ? 0.5822 1.2887 1.0553 0.0325  0.0231  0.0756  330 LEU B CB  
5395  C CG  . LEU B 330 ? 0.5426 1.2445 1.0082 0.0309  0.0209  0.0754  330 LEU B CG  
5396  C CD1 . LEU B 330 ? 0.5548 1.2624 1.0194 0.0281  0.0193  0.0706  330 LEU B CD1 
5397  C CD2 . LEU B 330 ? 0.5142 1.2208 0.9794 0.0323  0.0181  0.0805  330 LEU B CD2 
5398  N N   . ASP B 331 ? 0.5216 1.2441 1.0125 0.0377  0.0240  0.0799  331 ASP B N   
5399  C CA  . ASP B 331 ? 0.5655 1.2964 1.0668 0.0400  0.0249  0.0804  331 ASP B CA  
5400  C C   . ASP B 331 ? 0.5881 1.3177 1.0935 0.0380  0.0291  0.0754  331 ASP B C   
5401  O O   . ASP B 331 ? 0.6046 1.3308 1.1057 0.0345  0.0300  0.0713  331 ASP B O   
5402  C CB  . ASP B 331 ? 0.5828 1.3301 1.0895 0.0405  0.0198  0.0817  331 ASP B CB  
5403  C CG  . ASP B 331 ? 0.5728 1.3223 1.0763 0.0427  0.0160  0.0876  331 ASP B CG  
5404  O OD1 . ASP B 331 ? 0.5226 1.2778 1.0213 0.0410  0.0126  0.0878  331 ASP B OD1 
5405  O OD2 . ASP B 331 ? 0.6485 1.3937 1.1540 0.0460  0.0166  0.0921  331 ASP B OD2 
5406  N N   . ASP B 332 ? 0.6492 1.3814 1.1633 0.0404  0.0319  0.0759  332 ASP B N   
5407  C CA  . ASP B 332 ? 0.6989 1.4336 1.2201 0.0387  0.0360  0.0717  332 ASP B CA  
5408  C C   . ASP B 332 ? 0.7040 1.4240 1.2176 0.0363  0.0415  0.0688  332 ASP B C   
5409  O O   . ASP B 332 ? 0.7130 1.4337 1.2293 0.0333  0.0446  0.0649  332 ASP B O   
5410  C CB  . ASP B 332 ? 0.7241 1.4722 1.2509 0.0359  0.0328  0.0684  332 ASP B CB  
5411  C CG  . ASP B 332 ? 0.7845 1.5443 1.3254 0.0366  0.0338  0.0670  332 ASP B CG  
5412  O OD1 . ASP B 332 ? 0.8464 1.6019 1.3921 0.0378  0.0393  0.0666  332 ASP B OD1 
5413  O OD2 . ASP B 332 ? 0.8301 1.6039 1.3774 0.0361  0.0292  0.0660  332 ASP B OD2 
5414  N N   . VAL B 333 ? 0.6950 1.4014 1.1990 0.0374  0.0428  0.0706  333 VAL B N   
5415  C CA  . VAL B 333 ? 0.6938 1.3854 1.1891 0.0355  0.0475  0.0682  333 VAL B CA  
5416  C C   . VAL B 333 ? 0.7103 1.3975 1.2097 0.0375  0.0538  0.0679  333 VAL B C   
5417  O O   . VAL B 333 ? 0.7213 1.4117 1.2269 0.0414  0.0540  0.0705  333 VAL B O   
5418  C CB  . VAL B 333 ? 0.6773 1.3565 1.1604 0.0357  0.0456  0.0698  333 VAL B CB  
5419  C CG1 . VAL B 333 ? 0.7102 1.3740 1.1833 0.0337  0.0497  0.0672  333 VAL B CG1 
5420  C CG2 . VAL B 333 ? 0.5905 1.2757 1.0709 0.0339  0.0398  0.0700  333 VAL B CG2 
5421  N N   . GLU B 334 ? 0.7137 1.3933 1.2097 0.0349  0.0591  0.0647  334 GLU B N   
5422  C CA  . GLU B 334 ? 0.7683 1.4434 1.2673 0.0363  0.0662  0.0639  334 GLU B CA  
5423  C C   . GLU B 334 ? 0.7483 1.4050 1.2330 0.0358  0.0698  0.0633  334 GLU B C   
5424  O O   . GLU B 334 ? 0.7434 1.3925 1.2196 0.0322  0.0708  0.0612  334 GLU B O   
5425  C CB  . GLU B 334 ? 0.8729 1.5563 1.3813 0.0335  0.0701  0.0608  334 GLU B CB  
5426  C CG  . GLU B 334 ? 0.9081 1.5885 1.4209 0.0347  0.0781  0.0598  334 GLU B CG  
5427  C CD  . GLU B 334 ? 0.9700 1.6597 1.4936 0.0315  0.0821  0.0568  334 GLU B CD  
5428  O OE1 . GLU B 334 ? 1.0202 1.7201 1.5494 0.0287  0.0778  0.0557  334 GLU B OE1 
5429  O OE2 . GLU B 334 ? 0.9738 1.6608 1.5005 0.0315  0.0897  0.0555  334 GLU B OE2 
5430  N N   . ILE B 335 ? 0.7601 1.4093 1.2420 0.0396  0.0715  0.0650  335 ILE B N   
5431  C CA  . ILE B 335 ? 0.8186 1.4503 1.2868 0.0397  0.0746  0.0643  335 ILE B CA  
5432  C C   . ILE B 335 ? 0.8439 1.4716 1.3140 0.0409  0.0829  0.0625  335 ILE B C   
5433  O O   . ILE B 335 ? 0.8356 1.4695 1.3157 0.0446  0.0850  0.0632  335 ILE B O   
5434  C CB  . ILE B 335 ? 0.8733 1.4983 1.3363 0.0429  0.0705  0.0670  335 ILE B CB  
5435  C CG1 . ILE B 335 ? 0.8848 1.5154 1.3472 0.0416  0.0629  0.0689  335 ILE B CG1 
5436  C CG2 . ILE B 335 ? 0.8658 1.4726 1.3143 0.0429  0.0730  0.0657  335 ILE B CG2 
5437  C CD1 . ILE B 335 ? 0.8792 1.5030 1.3311 0.0377  0.0609  0.0670  335 ILE B CD1 
5438  N N   . LYS B 336 ? 0.8734 1.4909 1.3339 0.0379  0.0877  0.0601  336 LYS B N   
5439  C CA  . LYS B 336 ? 0.9055 1.5195 1.3669 0.0382  0.0966  0.0582  336 LYS B CA  
5440  C C   . LYS B 336 ? 1.0004 1.5988 1.4499 0.0410  0.0997  0.0578  336 LYS B C   
5441  O O   . LYS B 336 ? 0.9990 1.5908 1.4422 0.0431  0.0948  0.0593  336 LYS B O   
5442  C CB  . LYS B 336 ? 0.8877 1.4994 1.3454 0.0331  0.1007  0.0561  336 LYS B CB  
5443  C CG  . LYS B 336 ? 0.7974 1.4251 1.2698 0.0305  0.1003  0.0554  336 LYS B CG  
5444  C CD  . LYS B 336 ? 0.7184 1.3418 1.1871 0.0255  0.1059  0.0534  336 LYS B CD  
5445  C CE  . LYS B 336 ? 0.6390 1.2783 1.1235 0.0225  0.1060  0.0521  336 LYS B CE  
5446  N NZ  . LYS B 336 ? 0.6742 1.3083 1.1553 0.0173  0.1119  0.0504  336 LYS B NZ  
5447  N N   . GLU B 337 ? 1.2314 1.8239 1.6778 0.0408  0.1083  0.0557  337 GLU B N   
5448  C CA  . GLU B 337 ? 1.2545 1.8332 1.6905 0.0439  0.1123  0.0547  337 GLU B CA  
5449  C C   . GLU B 337 ? 1.2742 1.8367 1.6915 0.0427  0.1082  0.0548  337 GLU B C   
5450  O O   . GLU B 337 ? 1.2846 1.8409 1.6921 0.0387  0.1078  0.0543  337 GLU B O   
5451  C CB  . GLU B 337 ? 1.2750 1.8505 1.7095 0.0430  0.1228  0.0522  337 GLU B CB  
5452  C CG  . GLU B 337 ? 1.2555 1.8478 1.7091 0.0428  0.1275  0.0516  337 GLU B CG  
5453  C CD  . GLU B 337 ? 1.3645 1.9642 1.8311 0.0485  0.1291  0.0515  337 GLU B CD  
5454  O OE1 . GLU B 337 ? 1.4027 1.9933 1.8628 0.0524  0.1273  0.0518  337 GLU B OE1 
5455  O OE2 . GLU B 337 ? 1.3911 2.0057 1.8750 0.0491  0.1318  0.0511  337 GLU B OE2 
5456  N N   . ASN B 338 ? 1.0380 1.5934 1.4510 0.0462  0.1048  0.0554  338 ASN B N   
5457  C CA  . ASN B 338 ? 1.0401 1.5794 1.4359 0.0458  0.1013  0.0550  338 ASN B CA  
5458  C C   . ASN B 338 ? 1.0836 1.6226 1.4742 0.0421  0.0944  0.0561  338 ASN B C   
5459  O O   . ASN B 338 ? 1.2086 1.7371 1.5860 0.0393  0.0947  0.0551  338 ASN B O   
5460  C CB  . ASN B 338 ? 1.0376 1.5625 1.4189 0.0454  0.1085  0.0522  338 ASN B CB  
5461  C CG  . ASN B 338 ? 0.9646 1.4887 1.3501 0.0494  0.1156  0.0505  338 ASN B CG  
5462  O OD1 . ASN B 338 ? 0.9300 1.4568 1.3230 0.0534  0.1132  0.0511  338 ASN B OD1 
5463  N ND2 . ASN B 338 ? 1.0111 1.5312 1.3917 0.0485  0.1246  0.0483  338 ASN B ND2 
5464  N N   . ALA B 339 ? 1.0981 1.6489 1.4993 0.0422  0.0882  0.0584  339 ALA B N   
5465  C CA  . ALA B 339 ? 1.0879 1.6398 1.4859 0.0392  0.0814  0.0592  339 ALA B CA  
5466  C C   . ALA B 339 ? 1.0944 1.6398 1.4868 0.0406  0.0747  0.0604  339 ALA B C   
5467  O O   . ALA B 339 ? 1.0983 1.6432 1.4943 0.0439  0.0741  0.0615  339 ALA B O   
5468  C CB  . ALA B 339 ? 1.0651 1.6346 1.4775 0.0379  0.0788  0.0605  339 ALA B CB  
5469  N N   . VAL B 340 ? 0.8067 1.3472 1.1911 0.0381  0.0696  0.0602  340 VAL B N   
5470  C CA  . VAL B 340 ? 0.6789 1.2130 1.0579 0.0387  0.0632  0.0610  340 VAL B CA  
5471  C C   . VAL B 340 ? 0.6339 1.1767 1.0171 0.0365  0.0569  0.0621  340 VAL B C   
5472  O O   . VAL B 340 ? 0.6278 1.1718 1.0088 0.0338  0.0568  0.0610  340 VAL B O   
5473  C CB  . VAL B 340 ? 0.6787 1.1948 1.0410 0.0384  0.0633  0.0589  340 VAL B CB  
5474  C CG1 . VAL B 340 ? 0.6907 1.2010 1.0491 0.0390  0.0564  0.0595  340 VAL B CG1 
5475  C CG2 . VAL B 340 ? 0.7626 1.2703 1.1198 0.0406  0.0702  0.0573  340 VAL B CG2 
5476  N N   . VAL B 341 ? 0.5939 1.1424 0.9831 0.0375  0.0521  0.0644  341 VAL B N   
5477  C CA  . VAL B 341 ? 0.5124 1.0701 0.9060 0.0356  0.0465  0.0654  341 VAL B CA  
5478  C C   . VAL B 341 ? 0.5511 1.1031 0.9410 0.0359  0.0411  0.0664  341 VAL B C   
5479  O O   . VAL B 341 ? 0.5860 1.1383 0.9799 0.0380  0.0404  0.0686  341 VAL B O   
5480  C CB  . VAL B 341 ? 0.5269 1.1017 0.9342 0.0362  0.0462  0.0677  341 VAL B CB  
5481  C CG1 . VAL B 341 ? 0.5339 1.1177 0.9445 0.0343  0.0407  0.0684  341 VAL B CG1 
5482  C CG2 . VAL B 341 ? 0.5339 1.1150 0.9461 0.0355  0.0512  0.0663  341 VAL B CG2 
5483  N N   . ILE B 342 ? 0.4854 1.0321 0.8684 0.0339  0.0372  0.0649  342 ILE B N   
5484  C CA  . ILE B 342 ? 0.5044 1.0456 0.8841 0.0338  0.0319  0.0653  342 ILE B CA  
5485  C C   . ILE B 342 ? 0.5271 1.0769 0.9105 0.0317  0.0272  0.0652  342 ILE B C   
5486  O O   . ILE B 342 ? 0.6162 1.1660 0.9966 0.0301  0.0270  0.0631  342 ILE B O   
5487  C CB  . ILE B 342 ? 0.5415 1.0655 0.9079 0.0338  0.0313  0.0627  342 ILE B CB  
5488  C CG1 . ILE B 342 ? 0.5948 1.1101 0.9554 0.0355  0.0374  0.0616  342 ILE B CG1 
5489  C CG2 . ILE B 342 ? 0.5868 1.1053 0.9520 0.0341  0.0264  0.0633  342 ILE B CG2 
5490  C CD1 . ILE B 342 ? 0.6091 1.1244 0.9747 0.0382  0.0395  0.0632  342 ILE B CD1 
5491  N N   . ASN B 343 ? 0.5367 1.0933 0.9264 0.0316  0.0237  0.0675  343 ASN B N   
5492  C CA  . ASN B 343 ? 0.5130 1.0776 0.9061 0.0297  0.0193  0.0673  343 ASN B CA  
5493  C C   . ASN B 343 ? 0.4411 1.0162 0.8381 0.0286  0.0205  0.0660  343 ASN B C   
5494  O O   . ASN B 343 ? 0.4727 1.0470 0.8669 0.0272  0.0184  0.0634  343 ASN B O   
5495  C CB  . ASN B 343 ? 0.5502 1.1044 0.9357 0.0287  0.0152  0.0648  343 ASN B CB  
5496  C CG  . ASN B 343 ? 0.5346 1.0799 0.9176 0.0294  0.0130  0.0657  343 ASN B CG  
5497  O OD1 . ASN B 343 ? 0.5839 1.1348 0.9736 0.0296  0.0124  0.0686  343 ASN B OD1 
5498  N ND2 . ASN B 343 ? 0.4942 1.0253 0.8673 0.0295  0.0116  0.0632  343 ASN B ND2 
5499  N N   . SER B 344 ? 0.6030 1.1877 1.0068 0.0294  0.0235  0.0677  344 SER B N   
5500  C CA  . SER B 344 ? 0.4416 1.0355 0.8493 0.0283  0.0251  0.0662  344 SER B CA  
5501  C C   . SER B 344 ? 0.4215 1.0313 0.8391 0.0286  0.0246  0.0686  344 SER B C   
5502  O O   . SER B 344 ? 0.6190 1.2318 1.0402 0.0300  0.0240  0.0721  344 SER B O   
5503  C CB  . SER B 344 ? 0.4035 0.9919 0.8086 0.0287  0.0302  0.0649  344 SER B CB  
5504  O OG  . SER B 344 ? 0.4758 1.0484 0.8704 0.0288  0.0311  0.0634  344 SER B OG  
5505  N N   . ILE B 345 ? 0.3850 1.0047 0.8066 0.0273  0.0246  0.0668  345 ILE B N   
5506  C CA  . ILE B 345 ? 0.4548 1.0900 0.8850 0.0276  0.0241  0.0686  345 ILE B CA  
5507  C C   . ILE B 345 ? 0.4036 1.0439 0.8375 0.0269  0.0268  0.0662  345 ILE B C   
5508  O O   . ILE B 345 ? 0.4984 1.1401 0.9314 0.0249  0.0262  0.0628  345 ILE B O   
5509  C CB  . ILE B 345 ? 0.3921 1.0368 0.8243 0.0264  0.0201  0.0683  345 ILE B CB  
5510  C CG1 . ILE B 345 ? 0.4506 1.0903 0.8801 0.0266  0.0177  0.0706  345 ILE B CG1 
5511  C CG2 . ILE B 345 ? 0.3684 1.0287 0.8080 0.0267  0.0196  0.0701  345 ILE B CG2 
5512  C CD1 . ILE B 345 ? 0.5390 1.1887 0.9710 0.0253  0.0145  0.0706  345 ILE B CD1 
5513  N N   . ILE B 346 ? 0.4916 1.1348 0.9303 0.0285  0.0298  0.0680  346 ILE B N   
5514  C CA  . ILE B 346 ? 0.4215 1.0696 0.8649 0.0277  0.0329  0.0658  346 ILE B CA  
5515  C C   . ILE B 346 ? 0.4597 1.1247 0.9118 0.0274  0.0306  0.0660  346 ILE B C   
5516  O O   . ILE B 346 ? 0.4595 1.1324 0.9158 0.0293  0.0288  0.0695  346 ILE B O   
5517  C CB  . ILE B 346 ? 0.4537 1.0972 0.8989 0.0298  0.0376  0.0671  346 ILE B CB  
5518  C CG1 . ILE B 346 ? 0.4319 1.0583 0.8672 0.0303  0.0396  0.0669  346 ILE B CG1 
5519  C CG2 . ILE B 346 ? 0.5117 1.1598 0.9622 0.0284  0.0413  0.0646  346 ILE B CG2 
5520  C CD1 . ILE B 346 ? 0.4588 1.0756 0.8859 0.0278  0.0403  0.0635  346 ILE B CD1 
5521  N N   . GLY B 347 ? 0.4842 1.1542 0.9383 0.0251  0.0305  0.0623  347 GLY B N   
5522  C CA  . GLY B 347 ? 0.5410 1.2267 1.0023 0.0245  0.0278  0.0615  347 GLY B CA  
5523  C C   . GLY B 347 ? 0.5707 1.2664 1.0413 0.0258  0.0292  0.0629  347 GLY B C   
5524  O O   . GLY B 347 ? 0.5508 1.2421 1.0230 0.0279  0.0321  0.0652  347 GLY B O   
5525  N N   . TRP B 348 ? 0.6055 1.3148 1.0826 0.0249  0.0268  0.0611  348 TRP B N   
5526  C CA  . TRP B 348 ? 0.6002 1.3208 1.0871 0.0263  0.0271  0.0622  348 TRP B CA  
5527  C C   . TRP B 348 ? 0.5987 1.3174 1.0907 0.0246  0.0315  0.0591  348 TRP B C   
5528  O O   . TRP B 348 ? 0.6013 1.3153 1.0908 0.0215  0.0327  0.0552  348 TRP B O   
5529  C CB  . TRP B 348 ? 0.6262 1.3623 1.1174 0.0258  0.0223  0.0613  348 TRP B CB  
5530  C CG  . TRP B 348 ? 0.6340 1.3715 1.1188 0.0260  0.0187  0.0631  348 TRP B CG  
5531  C CD1 . TRP B 348 ? 0.6115 1.3455 1.0901 0.0239  0.0174  0.0600  348 TRP B CD1 
5532  C CD2 . TRP B 348 ? 0.5923 1.3352 1.0766 0.0286  0.0160  0.0682  348 TRP B CD2 
5533  N NE1 . TRP B 348 ? 0.5884 1.3259 1.0630 0.0248  0.0145  0.0628  348 TRP B NE1 
5534  C CE2 . TRP B 348 ? 0.6162 1.3589 1.0938 0.0275  0.0137  0.0681  348 TRP B CE2 
5535  C CE3 . TRP B 348 ? 0.5733 1.3210 1.0624 0.0317  0.0154  0.0732  348 TRP B CE3 
5536  C CZ2 . TRP B 348 ? 0.6483 1.3955 1.1235 0.0290  0.0113  0.0729  348 TRP B CZ2 
5537  C CZ3 . TRP B 348 ? 0.5890 1.3403 1.0752 0.0334  0.0125  0.0781  348 TRP B CZ3 
5538  C CH2 . TRP B 348 ? 0.6050 1.3560 1.0842 0.0318  0.0107  0.0781  348 TRP B CH2 
5539  N N   . LYS B 349 ? 0.6063 1.3288 1.1060 0.0268  0.0339  0.0609  349 LYS B N   
5540  C CA  . LYS B 349 ? 0.6339 1.3571 1.1407 0.0253  0.0385  0.0582  349 LYS B CA  
5541  C C   . LYS B 349 ? 0.6291 1.3367 1.1282 0.0231  0.0436  0.0563  349 LYS B C   
5542  O O   . LYS B 349 ? 0.6606 1.3676 1.1635 0.0205  0.0474  0.0534  349 LYS B O   
5543  C CB  . LYS B 349 ? 0.6092 1.3457 1.1245 0.0226  0.0361  0.0545  349 LYS B CB  
5544  C CG  . LYS B 349 ? 0.6264 1.3794 1.1518 0.0249  0.0321  0.0561  349 LYS B CG  
5545  C CD  . LYS B 349 ? 0.7005 1.4589 1.2207 0.0264  0.0261  0.0585  349 LYS B CD  
5546  C CE  . LYS B 349 ? 0.7926 1.5671 1.3216 0.0287  0.0216  0.0603  349 LYS B CE  
5547  N NZ  . LYS B 349 ? 0.7168 1.4966 1.2398 0.0299  0.0161  0.0629  349 LYS B NZ  
5548  N N   . SER B 350 ? 0.5726 1.2675 1.0606 0.0240  0.0436  0.0579  350 SER B N   
5549  C CA  . SER B 350 ? 0.7193 1.3988 1.1983 0.0221  0.0476  0.0564  350 SER B CA  
5550  C C   . SER B 350 ? 0.7006 1.3740 1.1811 0.0235  0.0540  0.0572  350 SER B C   
5551  O O   . SER B 350 ? 0.7160 1.3939 1.2022 0.0268  0.0548  0.0596  350 SER B O   
5552  C CB  . SER B 350 ? 0.5659 1.2343 1.0332 0.0229  0.0450  0.0577  350 SER B CB  
5553  O OG  . SER B 350 ? 0.6300 1.3050 1.0967 0.0220  0.0395  0.0570  350 SER B OG  
5554  N N   . SER B 351 ? 0.9081 1.5711 1.3832 0.0209  0.0587  0.0551  351 SER B N   
5555  C CA  . SER B 351 ? 0.9256 1.5825 1.4012 0.0216  0.0658  0.0553  351 SER B CA  
5556  C C   . SER B 351 ? 0.9491 1.5875 1.4096 0.0213  0.0684  0.0554  351 SER B C   
5557  O O   . SER B 351 ? 0.9614 1.5917 1.4142 0.0182  0.0682  0.0538  351 SER B O   
5558  C CB  . SER B 351 ? 0.9756 1.6388 1.4601 0.0184  0.0703  0.0527  351 SER B CB  
5559  O OG  . SER B 351 ? 0.9676 1.6264 1.4536 0.0192  0.0777  0.0529  351 SER B OG  
5560  N N   . ILE B 352 ? 0.8009 1.4321 1.2571 0.0246  0.0704  0.0573  352 ILE B N   
5561  C CA  . ILE B 352 ? 0.7893 1.4028 1.2308 0.0249  0.0725  0.0574  352 ILE B CA  
5562  C C   . ILE B 352 ? 0.7694 1.3775 1.2103 0.0250  0.0809  0.0566  352 ILE B C   
5563  O O   . ILE B 352 ? 0.7647 1.3773 1.2127 0.0281  0.0839  0.0574  352 ILE B O   
5564  C CB  . ILE B 352 ? 0.7963 1.4048 1.2326 0.0283  0.0685  0.0596  352 ILE B CB  
5565  C CG1 . ILE B 352 ? 0.6894 1.3037 1.1262 0.0277  0.0609  0.0604  352 ILE B CG1 
5566  C CG2 . ILE B 352 ? 0.8282 1.4186 1.2495 0.0286  0.0706  0.0592  352 ILE B CG2 
5567  C CD1 . ILE B 352 ? 0.6240 1.2325 1.0532 0.0244  0.0586  0.0584  352 ILE B CD1 
5568  N N   . GLY B 353 ? 0.7338 1.3321 1.1664 0.0218  0.0848  0.0551  353 GLY B N   
5569  C CA  . GLY B 353 ? 0.7896 1.3829 1.2210 0.0213  0.0935  0.0543  353 GLY B CA  
5570  C C   . GLY B 353 ? 0.8324 1.4146 1.2549 0.0248  0.0966  0.0549  353 GLY B C   
5571  O O   . GLY B 353 ? 0.8579 1.4341 1.2736 0.0273  0.0918  0.0559  353 GLY B O   
5572  N N   . ARG B 354 ? 0.8665 1.4459 1.2892 0.0250  0.1051  0.0539  354 ARG B N   
5573  C CA  . ARG B 354 ? 0.9374 1.5067 1.3523 0.0285  0.1090  0.0538  354 ARG B CA  
5574  C C   . ARG B 354 ? 1.0268 1.5770 1.4211 0.0274  0.1087  0.0535  354 ARG B C   
5575  O O   . ARG B 354 ? 1.0543 1.5979 1.4405 0.0236  0.1103  0.0532  354 ARG B O   
5576  C CB  . ARG B 354 ? 0.9467 1.5199 1.3689 0.0291  0.1187  0.0525  354 ARG B CB  
5577  C CG  . ARG B 354 ? 0.8976 1.4690 1.3178 0.0243  0.1253  0.0515  354 ARG B CG  
5578  C CD  . ARG B 354 ? 0.9149 1.4932 1.3457 0.0248  0.1351  0.0501  354 ARG B CD  
5579  N NE  . ARG B 354 ? 0.8296 1.4267 1.2814 0.0270  0.1333  0.0501  354 ARG B NE  
5580  C CZ  . ARG B 354 ? 0.7551 1.3663 1.2215 0.0240  0.1327  0.0497  354 ARG B CZ  
5581  N NH1 . ARG B 354 ? 0.7112 1.3195 1.1737 0.0185  0.1341  0.0493  354 ARG B NH1 
5582  N NH2 . ARG B 354 ? 0.7165 1.3444 1.2012 0.0265  0.1304  0.0498  354 ARG B NH2 
5583  N N   . TRP B 355 ? 1.4248 1.9659 1.8107 0.0308  0.1063  0.0537  355 TRP B N   
5584  C CA  . TRP B 355 ? 1.4602 1.9835 1.8267 0.0304  0.1043  0.0533  355 TRP B CA  
5585  C C   . TRP B 355 ? 1.4564 1.9775 1.8178 0.0275  0.0969  0.0541  355 TRP B C   
5586  O O   . TRP B 355 ? 1.4862 1.9934 1.8321 0.0261  0.0959  0.0538  355 TRP B O   
5587  C CB  . TRP B 355 ? 1.4908 2.0022 1.8450 0.0291  0.1129  0.0520  355 TRP B CB  
5588  C CG  . TRP B 355 ? 1.5028 2.0117 1.8570 0.0327  0.1196  0.0506  355 TRP B CG  
5589  C CD1 . TRP B 355 ? 1.5156 2.0157 1.8625 0.0365  0.1177  0.0498  355 TRP B CD1 
5590  C CD2 . TRP B 355 ? 1.5056 2.0207 1.8680 0.0329  0.1294  0.0495  355 TRP B CD2 
5591  N NE1 . TRP B 355 ? 1.5230 2.0232 1.8727 0.0393  0.1257  0.0480  355 TRP B NE1 
5592  C CE2 . TRP B 355 ? 1.5152 2.0249 1.8745 0.0372  0.1330  0.0478  355 TRP B CE2 
5593  C CE3 . TRP B 355 ? 1.5047 2.0297 1.8773 0.0298  0.1354  0.0494  355 TRP B CE3 
5594  C CZ2 . TRP B 355 ? 1.5172 2.0314 1.8836 0.0389  0.1427  0.0461  355 TRP B CZ2 
5595  C CZ3 . TRP B 355 ? 1.5020 2.0319 1.8821 0.0310  0.1449  0.0479  355 TRP B CZ3 
5596  C CH2 . TRP B 355 ? 1.5091 2.0337 1.8861 0.0357  0.1486  0.0462  355 TRP B CH2 
5597  N N   . SER B 356 ? 1.0238 1.5583 1.3977 0.0270  0.0915  0.0550  356 SER B N   
5598  C CA  . SER B 356 ? 0.8934 1.4274 1.2643 0.0248  0.0843  0.0553  356 SER B CA  
5599  C C   . SER B 356 ? 0.8349 1.3681 1.2045 0.0273  0.0768  0.0562  356 SER B C   
5600  O O   . SER B 356 ? 0.8569 1.3956 1.2335 0.0303  0.0765  0.0571  356 SER B O   
5601  C CB  . SER B 356 ? 0.8544 1.4035 1.2390 0.0224  0.0831  0.0553  356 SER B CB  
5602  O OG  . SER B 356 ? 0.8934 1.4573 1.2925 0.0247  0.0812  0.0561  356 SER B OG  
5603  N N   . ARG B 357 ? 0.7976 1.3241 1.1589 0.0260  0.0709  0.0560  357 ARG B N   
5604  C CA  . ARG B 357 ? 0.6612 1.1847 1.0196 0.0279  0.0641  0.0567  357 ARG B CA  
5605  C C   . ARG B 357 ? 0.6079 1.1389 0.9711 0.0264  0.0572  0.0569  357 ARG B C   
5606  O O   . ARG B 357 ? 0.6560 1.1852 1.0161 0.0239  0.0562  0.0559  357 ARG B O   
5607  C CB  . ARG B 357 ? 0.6235 1.1288 0.9649 0.0284  0.0635  0.0557  357 ARG B CB  
5608  C CG  . ARG B 357 ? 0.5792 1.0800 0.9176 0.0305  0.0576  0.0560  357 ARG B CG  
5609  C CD  . ARG B 357 ? 0.5748 1.0577 0.8960 0.0307  0.0563  0.0546  357 ARG B CD  
5610  N NE  . ARG B 357 ? 0.5416 1.0194 0.8601 0.0326  0.0511  0.0544  357 ARG B NE  
5611  C CZ  . ARG B 357 ? 0.5181 0.9891 0.8328 0.0349  0.0535  0.0538  357 ARG B CZ  
5612  N NH1 . ARG B 357 ? 0.5090 0.9782 0.8224 0.0359  0.0613  0.0532  357 ARG B NH1 
5613  N NH2 . ARG B 357 ? 0.5288 0.9951 0.8418 0.0362  0.0483  0.0535  357 ARG B NH2 
5614  N N   . VAL B 358 ? 0.5599 1.0990 0.9305 0.0279  0.0527  0.0581  358 VAL B N   
5615  C CA  . VAL B 358 ? 0.5566 1.1038 0.9321 0.0268  0.0464  0.0583  358 VAL B CA  
5616  C C   . VAL B 358 ? 0.4376 0.9804 0.8100 0.0283  0.0413  0.0592  358 VAL B C   
5617  O O   . VAL B 358 ? 0.5880 1.1365 0.9669 0.0301  0.0407  0.0611  358 VAL B O   
5618  C CB  . VAL B 358 ? 0.5041 1.0691 0.8940 0.0266  0.0464  0.0592  358 VAL B CB  
5619  C CG1 . VAL B 358 ? 0.5266 1.0995 0.9202 0.0254  0.0403  0.0589  358 VAL B CG1 
5620  C CG2 . VAL B 358 ? 0.5494 1.1189 0.9436 0.0250  0.0516  0.0581  358 VAL B CG2 
5621  N N   . GLN B 359 ? 0.5231 1.0556 0.8859 0.0276  0.0373  0.0579  359 GLN B N   
5622  C CA  . GLN B 359 ? 0.4443 0.9717 0.8040 0.0287  0.0323  0.0583  359 GLN B CA  
5623  C C   . GLN B 359 ? 0.4400 0.9694 0.8000 0.0273  0.0261  0.0573  359 GLN B C   
5624  O O   . GLN B 359 ? 0.5939 1.1256 0.9539 0.0258  0.0257  0.0559  359 GLN B O   
5625  C CB  . GLN B 359 ? 0.5170 1.0275 0.8638 0.0297  0.0335  0.0573  359 GLN B CB  
5626  C CG  . GLN B 359 ? 0.5422 1.0409 0.8767 0.0285  0.0332  0.0554  359 GLN B CG  
5627  C CD  . GLN B 359 ? 0.5050 0.9873 0.8257 0.0295  0.0314  0.0542  359 GLN B CD  
5628  O OE1 . GLN B 359 ? 0.4855 0.9634 0.8045 0.0312  0.0332  0.0544  359 GLN B OE1 
5629  N NE2 . GLN B 359 ? 0.6167 1.0895 0.9275 0.0286  0.0276  0.0529  359 GLN B NE2 
5630  N N   . ALA B 360 ? 0.4391 0.9673 0.7995 0.0279  0.0214  0.0578  360 ALA B N   
5631  C CA  . ALA B 360 ? 0.5113 1.0414 0.8725 0.0269  0.0154  0.0566  360 ALA B CA  
5632  C C   . ALA B 360 ? 0.5450 1.0682 0.9033 0.0275  0.0110  0.0567  360 ALA B C   
5633  O O   . ALA B 360 ? 0.5819 1.1001 0.9386 0.0286  0.0125  0.0578  360 ALA B O   
5634  C CB  . ALA B 360 ? 0.5122 1.0592 0.8854 0.0260  0.0143  0.0573  360 ALA B CB  
5635  N N   . SER B 361 ? 0.5713 1.0944 0.9297 0.0268  0.0055  0.0552  361 SER B N   
5636  C CA  . SER B 361 ? 0.6080 1.1244 0.9640 0.0270  0.0006  0.0547  361 SER B CA  
5637  C C   . SER B 361 ? 0.5444 1.0701 0.9104 0.0268  0.0001  0.0572  361 SER B C   
5638  O O   . SER B 361 ? 0.5777 1.0967 0.9420 0.0272  -0.0012 0.0578  361 SER B O   
5639  C CB  . SER B 361 ? 0.6378 1.1523 0.9923 0.0264  -0.0053 0.0523  361 SER B CB  
5640  O OG  . SER B 361 ? 0.6472 1.1741 1.0097 0.0256  -0.0054 0.0518  361 SER B OG  
5641  N N   . GLY B 362 ? 0.7004 1.2411 1.0766 0.0261  0.0010  0.0587  362 GLY B N   
5642  C CA  . GLY B 362 ? 0.6000 1.1499 0.9853 0.0256  0.0002  0.0615  362 GLY B CA  
5643  C C   . GLY B 362 ? 0.7850 1.3412 1.1758 0.0242  -0.0045 0.0607  362 GLY B C   
5644  O O   . GLY B 362 ? 0.8732 1.4364 1.2713 0.0234  -0.0051 0.0632  362 GLY B O   
5645  N N   . ASP B 363 ? 0.9412 1.4951 1.3293 0.0239  -0.0077 0.0574  363 ASP B N   
5646  C CA  . ASP B 363 ? 0.9262 1.4866 1.3205 0.0228  -0.0120 0.0561  363 ASP B CA  
5647  C C   . ASP B 363 ? 0.9064 1.4835 1.3097 0.0221  -0.0102 0.0569  363 ASP B C   
5648  O O   . ASP B 363 ? 0.8907 1.4719 1.2937 0.0223  -0.0091 0.0550  363 ASP B O   
5649  C CB  . ASP B 363 ? 0.9323 1.4847 1.3210 0.0233  -0.0163 0.0521  363 ASP B CB  
5650  C CG  . ASP B 363 ? 1.0003 1.5363 1.3793 0.0240  -0.0190 0.0511  363 ASP B CG  
5651  O OD1 . ASP B 363 ? 1.0541 1.5862 1.4330 0.0238  -0.0187 0.0529  363 ASP B OD1 
5652  O OD2 . ASP B 363 ? 1.0319 1.5586 1.4031 0.0249  -0.0217 0.0486  363 ASP B OD2 
5653  N N   . TYR B 364 ? 1.0505 1.6369 1.4615 0.0210  -0.0097 0.0598  364 TYR B N   
5654  C CA  . TYR B 364 ? 1.0243 1.6269 1.4430 0.0202  -0.0081 0.0608  364 TYR B CA  
5655  C C   . TYR B 364 ? 1.0579 1.6669 1.4807 0.0196  -0.0111 0.0572  364 TYR B C   
5656  O O   . TYR B 364 ? 1.0422 1.6647 1.4709 0.0190  -0.0099 0.0571  364 TYR B O   
5657  C CB  . TYR B 364 ? 1.0227 1.6323 1.4472 0.0192  -0.0066 0.0655  364 TYR B CB  
5658  C CG  . TYR B 364 ? 1.0663 1.6691 1.4875 0.0203  -0.0038 0.0689  364 TYR B CG  
5659  C CD1 . TYR B 364 ? 1.0415 1.6491 1.4624 0.0214  -0.0002 0.0704  364 TYR B CD1 
5660  C CD2 . TYR B 364 ? 1.0831 1.6749 1.5021 0.0203  -0.0050 0.0702  364 TYR B CD2 
5661  C CE1 . TYR B 364 ? 1.0292 1.6311 1.4482 0.0228  0.0023  0.0732  364 TYR B CE1 
5662  C CE2 . TYR B 364 ? 1.1178 1.7032 1.5341 0.0216  -0.0024 0.0728  364 TYR B CE2 
5663  C CZ  . TYR B 364 ? 1.0574 1.6480 1.4739 0.0230  0.0014  0.0743  364 TYR B CZ  
5664  O OH  . TYR B 364 ? 1.0517 1.6365 1.4666 0.0247  0.0040  0.0767  364 TYR B OH  
5665  N N   . ASN B 365 ? 0.9727 1.5725 1.3927 0.0199  -0.0152 0.0541  365 ASN B N   
5666  C CA  . ASN B 365 ? 0.9276 1.5318 1.3513 0.0200  -0.0186 0.0501  365 ASN B CA  
5667  C C   . ASN B 365 ? 0.9105 1.5085 1.3282 0.0215  -0.0193 0.0466  365 ASN B C   
5668  O O   . ASN B 365 ? 0.9189 1.5236 1.3405 0.0218  -0.0205 0.0434  365 ASN B O   
5669  C CB  . ASN B 365 ? 0.9364 1.5346 1.3617 0.0197  -0.0235 0.0488  365 ASN B CB  
5670  C CG  . ASN B 365 ? 0.9252 1.5248 1.3547 0.0180  -0.0229 0.0525  365 ASN B CG  
5671  O OD1 . ASN B 365 ? 1.0411 1.6291 1.4664 0.0179  -0.0251 0.0529  365 ASN B OD1 
5672  N ND2 . ASN B 365 ? 0.8663 1.4795 1.3035 0.0165  -0.0200 0.0551  365 ASN B ND2 
5673  N N   . ASP B 366 ? 0.8301 1.4154 1.2385 0.0223  -0.0183 0.0472  366 ASP B N   
5674  C CA  . ASP B 366 ? 0.7443 1.3231 1.1465 0.0232  -0.0182 0.0447  366 ASP B CA  
5675  C C   . ASP B 366 ? 0.6370 1.2244 1.0412 0.0228  -0.0134 0.0454  366 ASP B C   
5676  O O   . ASP B 366 ? 0.7259 1.3185 1.1321 0.0224  -0.0098 0.0486  366 ASP B O   
5677  C CB  . ASP B 366 ? 0.7769 1.3384 1.1675 0.0240  -0.0187 0.0451  366 ASP B CB  
5678  C CG  . ASP B 366 ? 0.7688 1.3222 1.1522 0.0247  -0.0185 0.0430  366 ASP B CG  
5679  O OD1 . ASP B 366 ? 0.7592 1.3187 1.1469 0.0248  -0.0196 0.0405  366 ASP B OD1 
5680  O OD2 . ASP B 366 ? 0.7193 1.2600 1.0926 0.0251  -0.0171 0.0438  366 ASP B OD2 
5681  N N   . ARG B 367 ? 0.6332 1.2221 1.0374 0.0231  -0.0138 0.0423  367 ARG B N   
5682  C CA  . ARG B 367 ? 0.6353 1.2327 1.0421 0.0225  -0.0098 0.0423  367 ARG B CA  
5683  C C   . ARG B 367 ? 0.6810 1.2711 1.0818 0.0224  -0.0058 0.0446  367 ARG B C   
5684  O O   . ARG B 367 ? 0.6637 1.2619 1.0679 0.0219  -0.0021 0.0466  367 ARG B O   
5685  C CB  . ARG B 367 ? 0.6457 1.2442 1.0536 0.0227  -0.0114 0.0380  367 ARG B CB  
5686  C CG  . ARG B 367 ? 0.6354 1.2466 1.0488 0.0219  -0.0085 0.0369  367 ARG B CG  
5687  C CD  . ARG B 367 ? 0.6605 1.2714 1.0751 0.0222  -0.0104 0.0322  367 ARG B CD  
5688  N NE  . ARG B 367 ? 0.7397 1.3635 1.1600 0.0214  -0.0082 0.0303  367 ARG B NE  
5689  C CZ  . ARG B 367 ? 0.7266 1.3516 1.1487 0.0213  -0.0091 0.0259  367 ARG B CZ  
5690  N NH1 . ARG B 367 ? 0.7134 1.3272 1.1322 0.0223  -0.0122 0.0235  367 ARG B NH1 
5691  N NH2 . ARG B 367 ? 0.7026 1.3397 1.1299 0.0205  -0.0073 0.0240  367 ARG B NH2 
5692  N N   . LEU B 368 ? 0.7648 1.3396 1.1564 0.0229  -0.0064 0.0444  368 LEU B N   
5693  C CA  . LEU B 368 ? 0.7264 1.2933 1.1116 0.0228  -0.0021 0.0463  368 LEU B CA  
5694  C C   . LEU B 368 ? 0.7163 1.2775 1.0983 0.0234  -0.0012 0.0492  368 LEU B C   
5695  O O   . LEU B 368 ? 0.7054 1.2564 1.0800 0.0238  0.0016  0.0502  368 LEU B O   
5696  C CB  . LEU B 368 ? 0.7701 1.3230 1.1459 0.0229  -0.0026 0.0445  368 LEU B CB  
5697  C CG  . LEU B 368 ? 0.7469 1.3035 1.1255 0.0222  -0.0031 0.0417  368 LEU B CG  
5698  C CD1 . LEU B 368 ? 0.7387 1.2800 1.1072 0.0220  -0.0031 0.0409  368 LEU B CD1 
5699  C CD2 . LEU B 368 ? 0.6822 1.2518 1.0685 0.0210  0.0011  0.0419  368 LEU B CD2 
5700  N N   . GLY B 369 ? 0.6845 1.2518 1.0720 0.0235  -0.0034 0.0505  369 GLY B N   
5701  C CA  . GLY B 369 ? 0.6485 1.2104 1.0339 0.0240  -0.0026 0.0531  369 GLY B CA  
5702  C C   . GLY B 369 ? 0.6432 1.2104 1.0314 0.0242  0.0024  0.0561  369 GLY B C   
5703  O O   . GLY B 369 ? 0.6620 1.2219 1.0467 0.0250  0.0040  0.0579  369 GLY B O   
5704  N N   . ILE B 370 ? 0.5486 1.1282 0.9433 0.0237  0.0046  0.0563  370 ILE B N   
5705  C CA  . ILE B 370 ? 0.5409 1.1271 0.9395 0.0242  0.0089  0.0589  370 ILE B CA  
5706  C C   . ILE B 370 ? 0.4709 1.0604 0.8699 0.0236  0.0116  0.0570  370 ILE B C   
5707  O O   . ILE B 370 ? 0.4880 1.0876 0.8920 0.0227  0.0105  0.0554  370 ILE B O   
5708  C CB  . ILE B 370 ? 0.5967 1.1969 1.0041 0.0240  0.0085  0.0617  370 ILE B CB  
5709  C CG1 . ILE B 370 ? 0.6802 1.2768 1.0879 0.0241  0.0060  0.0638  370 ILE B CG1 
5710  C CG2 . ILE B 370 ? 0.5646 1.1714 0.9760 0.0248  0.0123  0.0644  370 ILE B CG2 
5711  C CD1 . ILE B 370 ? 0.6926 1.2774 1.0956 0.0253  0.0075  0.0655  370 ILE B CD1 
5712  N N   . THR B 371 ? 0.5057 1.0867 0.8996 0.0239  0.0153  0.0570  371 THR B N   
5713  C CA  . THR B 371 ? 0.6330 1.2168 1.0279 0.0229  0.0182  0.0553  371 THR B CA  
5714  C C   . THR B 371 ? 0.3928 0.9917 0.7974 0.0229  0.0203  0.0568  371 THR B C   
5715  O O   . THR B 371 ? 0.5325 1.1346 0.9403 0.0242  0.0219  0.0597  371 THR B O   
5716  C CB  . THR B 371 ? 0.4790 1.0500 0.8660 0.0231  0.0223  0.0552  371 THR B CB  
5717  O OG1 . THR B 371 ? 0.4163 0.9917 0.8064 0.0218  0.0259  0.0541  371 THR B OG1 
5718  C CG2 . THR B 371 ? 0.4616 1.0292 0.8478 0.0248  0.0250  0.0578  371 THR B CG2 
5719  N N   . ILE B 372 ? 0.6520 1.2601 1.0614 0.0216  0.0198  0.0546  372 ILE B N   
5720  C CA  . ILE B 372 ? 0.3807 1.0042 0.7991 0.0215  0.0206  0.0554  372 ILE B CA  
5721  C C   . ILE B 372 ? 0.5560 1.1814 0.9768 0.0202  0.0237  0.0533  372 ILE B C   
5722  O O   . ILE B 372 ? 0.4261 1.0473 0.8444 0.0186  0.0232  0.0501  372 ILE B O   
5723  C CB  . ILE B 372 ? 0.4906 1.1255 0.9135 0.0210  0.0168  0.0544  372 ILE B CB  
5724  C CG1 . ILE B 372 ? 0.4933 1.1262 0.9145 0.0219  0.0142  0.0567  372 ILE B CG1 
5725  C CG2 . ILE B 372 ? 0.4900 1.1406 0.9209 0.0210  0.0174  0.0553  372 ILE B CG2 
5726  C CD1 . ILE B 372 ? 0.5938 1.2360 1.0183 0.0213  0.0108  0.0552  372 ILE B CD1 
5727  N N   . LEU B 373 ? 0.4690 1.1009 0.8953 0.0208  0.0268  0.0550  373 LEU B N   
5728  C CA  . LEU B 373 ? 0.4801 1.1155 0.9106 0.0193  0.0300  0.0532  373 LEU B CA  
5729  C C   . LEU B 373 ? 0.4816 1.1341 0.9217 0.0190  0.0283  0.0526  373 LEU B C   
5730  O O   . LEU B 373 ? 0.4889 1.1502 0.9331 0.0207  0.0269  0.0554  373 LEU B O   
5731  C CB  . LEU B 373 ? 0.4697 1.1000 0.9002 0.0204  0.0350  0.0552  373 LEU B CB  
5732  C CG  . LEU B 373 ? 0.4450 1.0600 0.8670 0.0193  0.0387  0.0539  373 LEU B CG  
5733  C CD1 . LEU B 373 ? 0.4552 1.0570 0.8665 0.0198  0.0359  0.0540  373 LEU B CD1 
5734  C CD2 . LEU B 373 ? 0.5143 1.1262 0.9372 0.0205  0.0442  0.0556  373 LEU B CD2 
5735  N N   . GLY B 374 ? 0.5039 1.1605 0.9470 0.0167  0.0282  0.0490  374 GLY B N   
5736  C CA  . GLY B 374 ? 0.6029 1.2752 1.0542 0.0161  0.0260  0.0475  374 GLY B CA  
5737  C C   . GLY B 374 ? 0.6410 1.3227 1.1004 0.0169  0.0282  0.0493  374 GLY B C   
5738  O O   . GLY B 374 ? 0.6020 1.2792 1.0616 0.0183  0.0314  0.0521  374 GLY B O   
5739  N N   . GLU B 375 ? 0.7161 1.4116 1.1828 0.0160  0.0261  0.0473  375 GLU B N   
5740  C CA  . GLU B 375 ? 0.6976 1.4041 1.1735 0.0167  0.0271  0.0484  375 GLU B CA  
5741  C C   . GLU B 375 ? 0.6842 1.3873 1.1642 0.0145  0.0314  0.0460  375 GLU B C   
5742  O O   . GLU B 375 ? 0.7151 1.4157 1.1947 0.0115  0.0316  0.0421  375 GLU B O   
5743  C CB  . GLU B 375 ? 0.6959 1.4184 1.1772 0.0164  0.0228  0.0469  375 GLU B CB  
5744  C CG  . GLU B 375 ? 0.6688 1.4038 1.1602 0.0171  0.0228  0.0475  375 GLU B CG  
5745  C CD  . GLU B 375 ? 0.7184 1.4683 1.2144 0.0162  0.0183  0.0446  375 GLU B CD  
5746  O OE1 . GLU B 375 ? 0.7700 1.5199 1.2613 0.0148  0.0158  0.0416  375 GLU B OE1 
5747  O OE2 . GLU B 375 ? 0.7795 1.5410 1.2837 0.0169  0.0171  0.0451  375 GLU B OE2 
5748  N N   . ALA B 376 ? 0.6370 1.3403 1.1215 0.0159  0.0351  0.0485  376 ALA B N   
5749  C CA  . ALA B 376 ? 0.6262 1.3277 1.1160 0.0139  0.0400  0.0467  376 ALA B CA  
5750  C C   . ALA B 376 ? 0.6100 1.2956 1.0910 0.0114  0.0433  0.0450  376 ALA B C   
5751  O O   . ALA B 376 ? 0.5844 1.2688 1.0679 0.0080  0.0452  0.0418  376 ALA B O   
5752  C CB  . ALA B 376 ? 0.7117 1.4274 1.2124 0.0116  0.0383  0.0433  376 ALA B CB  
5753  N N   . VAL B 377 ? 0.6206 1.2937 1.0912 0.0130  0.0438  0.0472  377 VAL B N   
5754  C CA  . VAL B 377 ? 0.6734 1.3302 1.1344 0.0113  0.0469  0.0464  377 VAL B CA  
5755  C C   . VAL B 377 ? 0.7039 1.3539 1.1641 0.0121  0.0533  0.0482  377 VAL B C   
5756  O O   . VAL B 377 ? 0.7130 1.3636 1.1736 0.0153  0.0541  0.0510  377 VAL B O   
5757  C CB  . VAL B 377 ? 0.6674 1.3141 1.1173 0.0126  0.0434  0.0472  377 VAL B CB  
5758  C CG1 . VAL B 377 ? 0.7116 1.3606 1.1609 0.0162  0.0417  0.0508  377 VAL B CG1 
5759  C CG2 . VAL B 377 ? 0.6497 1.2788 1.0887 0.0116  0.0465  0.0472  377 VAL B CG2 
5760  N N   . THR B 378 ? 0.7597 1.4030 1.2187 0.0092  0.0581  0.0466  378 THR B N   
5761  C CA  . THR B 378 ? 0.7883 1.4265 1.2474 0.0095  0.0652  0.0479  378 THR B CA  
5762  C C   . THR B 378 ? 0.7925 1.4116 1.2366 0.0090  0.0679  0.0485  378 THR B C   
5763  O O   . THR B 378 ? 0.7933 1.4042 1.2323 0.0057  0.0696  0.0471  378 THR B O   
5764  C CB  . THR B 378 ? 0.8035 1.4495 1.2737 0.0063  0.0695  0.0459  378 THR B CB  
5765  O OG1 . THR B 378 ? 0.8778 1.5169 1.3439 0.0021  0.0699  0.0436  378 THR B OG1 
5766  C CG2 . THR B 378 ? 0.7613 1.4264 1.2459 0.0069  0.0657  0.0449  378 THR B CG2 
5767  N N   . VAL B 379 ? 0.7821 1.3938 1.2186 0.0123  0.0680  0.0507  379 VAL B N   
5768  C CA  . VAL B 379 ? 0.7477 1.3415 1.1695 0.0123  0.0707  0.0514  379 VAL B CA  
5769  C C   . VAL B 379 ? 0.7414 1.3321 1.1640 0.0120  0.0792  0.0517  379 VAL B C   
5770  O O   . VAL B 379 ? 0.7096 1.3064 1.1387 0.0148  0.0817  0.0527  379 VAL B O   
5771  C CB  . VAL B 379 ? 0.7069 1.2944 1.1209 0.0158  0.0668  0.0531  379 VAL B CB  
5772  C CG1 . VAL B 379 ? 0.6997 1.2687 1.0982 0.0160  0.0695  0.0535  379 VAL B CG1 
5773  C CG2 . VAL B 379 ? 0.7332 1.3245 1.1471 0.0159  0.0591  0.0527  379 VAL B CG2 
5774  N N   . GLU B 380 ? 0.7552 1.3365 1.1715 0.0087  0.0837  0.0510  380 GLU B N   
5775  C CA  . GLU B 380 ? 0.7486 1.3277 1.1661 0.0077  0.0926  0.0510  380 GLU B CA  
5776  C C   . GLU B 380 ? 0.7247 1.2917 1.1305 0.0109  0.0959  0.0523  380 GLU B C   
5777  O O   . GLU B 380 ? 0.7600 1.3199 1.1569 0.0135  0.0910  0.0531  380 GLU B O   
5778  C CB  . GLU B 380 ? 0.7676 1.3395 1.1812 0.0029  0.0967  0.0503  380 GLU B CB  
5779  C CG  . GLU B 380 ? 0.8251 1.4050 1.2500 0.0003  0.1047  0.0495  380 GLU B CG  
5780  C CD  . GLU B 380 ? 0.9855 1.5634 1.4120 -0.0052 0.1065  0.0485  380 GLU B CD  
5781  O OE1 . GLU B 380 ? 0.9413 1.5135 1.3618 -0.0066 0.1007  0.0481  380 GLU B OE1 
5782  O OE2 . GLU B 380 ? 1.1339 1.7161 1.5683 -0.0082 0.1137  0.0480  380 GLU B OE2 
5783  N N   . ASP B 381 ? 0.7693 1.3345 1.1758 0.0106  0.1045  0.0522  381 ASP B N   
5784  C CA  . ASP B 381 ? 0.7904 1.3446 1.1862 0.0136  0.1085  0.0527  381 ASP B CA  
5785  C C   . ASP B 381 ? 0.8344 1.3695 1.2098 0.0129  0.1069  0.0533  381 ASP B C   
5786  O O   . ASP B 381 ? 0.8544 1.3824 1.2231 0.0092  0.1075  0.0534  381 ASP B O   
5787  C CB  . ASP B 381 ? 0.7747 1.3310 1.1754 0.0130  0.1189  0.0521  381 ASP B CB  
5788  C CG  . ASP B 381 ? 0.7463 1.3222 1.1685 0.0127  0.1203  0.0513  381 ASP B CG  
5789  O OD1 . ASP B 381 ? 0.7523 1.3394 1.1846 0.0155  0.1143  0.0517  381 ASP B OD1 
5790  O OD2 . ASP B 381 ? 0.7124 1.2924 1.1413 0.0096  0.1274  0.0505  381 ASP B OD2 
5791  N N   . GLU B 382 ? 0.9091 1.4357 1.2749 0.0165  0.1045  0.0536  382 GLU B N   
5792  C CA  . GLU B 382 ? 0.9194 1.4282 1.2658 0.0167  0.1017  0.0539  382 GLU B CA  
5793  C C   . GLU B 382 ? 0.8999 1.4065 1.2430 0.0153  0.0929  0.0542  382 GLU B C   
5794  O O   . GLU B 382 ? 0.8887 1.3814 1.2168 0.0157  0.0893  0.0544  382 GLU B O   
5795  C CB  . GLU B 382 ? 0.9165 1.4121 1.2496 0.0142  0.1094  0.0540  382 GLU B CB  
5796  C CG  . GLU B 382 ? 0.9238 1.4160 1.2538 0.0162  0.1180  0.0533  382 GLU B CG  
5797  C CD  . GLU B 382 ? 0.9838 1.4595 1.2955 0.0141  0.1243  0.0536  382 GLU B CD  
5798  O OE1 . GLU B 382 ? 0.9415 1.4056 1.2400 0.0123  0.1199  0.0546  382 GLU B OE1 
5799  O OE2 . GLU B 382 ? 1.0441 1.5184 1.3543 0.0144  0.1336  0.0529  382 GLU B OE2 
5800  N N   . VAL B 383 ? 0.8381 1.3582 1.1947 0.0138  0.0893  0.0540  383 VAL B N   
5801  C CA  . VAL B 383 ? 0.8369 1.3557 1.1912 0.0126  0.0815  0.0538  383 VAL B CA  
5802  C C   . VAL B 383 ? 0.8739 1.3924 1.2262 0.0159  0.0741  0.0540  383 VAL B C   
5803  O O   . VAL B 383 ? 0.8104 1.3383 1.1716 0.0184  0.0733  0.0545  383 VAL B O   
5804  C CB  . VAL B 383 ? 0.8228 1.3564 1.1921 0.0101  0.0801  0.0529  383 VAL B CB  
5805  C CG1 . VAL B 383 ? 0.8578 1.3903 1.2252 0.0092  0.0723  0.0521  383 VAL B CG1 
5806  C CG2 . VAL B 383 ? 0.8439 1.3771 1.2157 0.0064  0.0875  0.0525  383 VAL B CG2 
5807  N N   . ALA B 384 ? 1.0403 1.5480 1.3815 0.0157  0.0686  0.0539  384 ALA B N   
5808  C CA  . ALA B 384 ? 0.9683 1.4742 1.3067 0.0183  0.0617  0.0540  384 ALA B CA  
5809  C C   . ALA B 384 ? 0.9316 1.4440 1.2754 0.0175  0.0544  0.0534  384 ALA B C   
5810  O O   . ALA B 384 ? 0.9222 1.4315 1.2637 0.0152  0.0533  0.0526  384 ALA B O   
5811  C CB  . ALA B 384 ? 0.9664 1.4541 1.2872 0.0194  0.0607  0.0541  384 ALA B CB  
5812  N N   . VAL B 385 ? 0.8182 1.3397 1.1695 0.0194  0.0497  0.0536  385 VAL B N   
5813  C CA  . VAL B 385 ? 0.7357 1.2646 1.0926 0.0190  0.0430  0.0528  385 VAL B CA  
5814  C C   . VAL B 385 ? 0.7583 1.2831 1.1112 0.0211  0.0376  0.0533  385 VAL B C   
5815  O O   . VAL B 385 ? 0.7182 1.2493 1.0767 0.0228  0.0374  0.0545  385 VAL B O   
5816  C CB  . VAL B 385 ? 0.6396 1.1867 1.0117 0.0185  0.0431  0.0527  385 VAL B CB  
5817  C CG1 . VAL B 385 ? 0.7187 1.2731 1.0954 0.0182  0.0366  0.0516  385 VAL B CG1 
5818  C CG2 . VAL B 385 ? 0.6161 1.1674 0.9931 0.0161  0.0483  0.0519  385 VAL B CG2 
5819  N N   . ILE B 386 ? 0.9497 1.4642 1.2936 0.0210  0.0329  0.0523  386 ILE B N   
5820  C CA  . ILE B 386 ? 0.9510 1.4604 1.2906 0.0227  0.0274  0.0523  386 ILE B CA  
5821  C C   . ILE B 386 ? 0.9341 1.4505 1.2797 0.0223  0.0211  0.0511  386 ILE B C   
5822  O O   . ILE B 386 ? 0.9441 1.4555 1.2857 0.0214  0.0186  0.0496  386 ILE B O   
5823  C CB  . ILE B 386 ? 0.9961 1.4871 1.3199 0.0233  0.0267  0.0520  386 ILE B CB  
5824  C CG1 . ILE B 386 ? 1.0131 1.4974 1.3308 0.0239  0.0334  0.0528  386 ILE B CG1 
5825  C CG2 . ILE B 386 ? 1.0081 1.4947 1.3289 0.0247  0.0198  0.0514  386 ILE B CG2 
5826  C CD1 . ILE B 386 ? 1.0349 1.5148 1.3479 0.0221  0.0397  0.0529  386 ILE B CD1 
5827  N N   . GLY B 387 ? 0.7030 1.2306 1.0578 0.0231  0.0186  0.0518  387 GLY B N   
5828  C CA  . GLY B 387 ? 0.7084 1.2436 1.0692 0.0229  0.0130  0.0506  387 GLY B CA  
5829  C C   . GLY B 387 ? 0.7010 1.2419 1.0659 0.0215  0.0126  0.0485  387 GLY B C   
5830  O O   . GLY B 387 ? 0.7202 1.2559 1.0818 0.0214  0.0086  0.0466  387 GLY B O   
5831  N N   . SER B 388 ? 0.6541 1.2055 1.0265 0.0205  0.0166  0.0488  388 SER B N   
5832  C CA  . SER B 388 ? 0.6149 1.1722 0.9919 0.0189  0.0165  0.0465  388 SER B CA  
5833  C C   . SER B 388 ? 0.5451 1.1200 0.9339 0.0185  0.0178  0.0467  388 SER B C   
5834  O O   . SER B 388 ? 0.5745 1.1556 0.9671 0.0195  0.0194  0.0491  388 SER B O   
5835  C CB  . SER B 388 ? 0.6296 1.1774 1.0005 0.0174  0.0207  0.0462  388 SER B CB  
5836  O OG  . SER B 388 ? 0.6835 1.2148 1.0424 0.0178  0.0189  0.0461  388 SER B OG  
5837  N N   . ILE B 389 ? 0.6336 1.2160 1.0279 0.0173  0.0167  0.0440  389 ILE B N   
5838  C CA  . ILE B 389 ? 0.6334 1.2326 1.0381 0.0168  0.0171  0.0435  389 ILE B CA  
5839  C C   . ILE B 389 ? 0.6118 1.2133 1.0197 0.0147  0.0203  0.0418  389 ILE B C   
5840  O O   . ILE B 389 ? 0.6110 1.2072 1.0169 0.0134  0.0194  0.0390  389 ILE B O   
5841  C CB  . ILE B 389 ? 0.6044 1.2126 1.0136 0.0171  0.0125  0.0413  389 ILE B CB  
5842  C CG1 . ILE B 389 ? 0.5617 1.1662 0.9679 0.0187  0.0093  0.0428  389 ILE B CG1 
5843  C CG2 . ILE B 389 ? 0.5753 1.2008 0.9937 0.0168  0.0130  0.0412  389 ILE B CG2 
5844  C CD1 . ILE B 389 ? 0.5505 1.1579 0.9578 0.0197  0.0110  0.0468  389 ILE B CD1 
5845  N N   . VAL B 390 ? 0.5267 1.1361 0.9401 0.0145  0.0240  0.0433  390 VAL B N   
5846  C CA  . VAL B 390 ? 0.5491 1.1625 0.9675 0.0123  0.0272  0.0417  390 VAL B CA  
5847  C C   . VAL B 390 ? 0.5716 1.2026 1.0003 0.0120  0.0255  0.0403  390 VAL B C   
5848  O O   . VAL B 390 ? 0.5994 1.2398 1.0319 0.0137  0.0244  0.0424  390 VAL B O   
5849  C CB  . VAL B 390 ? 0.5053 1.1145 0.9229 0.0122  0.0329  0.0442  390 VAL B CB  
5850  C CG1 . VAL B 390 ? 0.5030 1.1155 0.9262 0.0095  0.0364  0.0423  390 VAL B CG1 
5851  C CG2 . VAL B 390 ? 0.4912 1.0831 0.8971 0.0129  0.0344  0.0457  390 VAL B CG2 
5852  N N   . LEU B 391 ? 0.5580 1.1929 0.9909 0.0098  0.0251  0.0366  391 LEU B N   
5853  C CA  . LEU B 391 ? 0.6164 1.2677 1.0583 0.0093  0.0232  0.0345  391 LEU B CA  
5854  C C   . LEU B 391 ? 0.6625 1.3225 1.1118 0.0088  0.0265  0.0360  391 LEU B C   
5855  O O   . LEU B 391 ? 0.6165 1.2697 1.0644 0.0087  0.0308  0.0382  391 LEU B O   
5856  C CB  . LEU B 391 ? 0.6339 1.2858 1.0778 0.0071  0.0212  0.0295  391 LEU B CB  
5857  C CG  . LEU B 391 ? 0.5287 1.1825 0.9709 0.0082  0.0165  0.0268  391 LEU B CG  
5858  C CD1 . LEU B 391 ? 0.5300 1.1708 0.9636 0.0099  0.0153  0.0286  391 LEU B CD1 
5859  C CD2 . LEU B 391 ? 0.5715 1.2255 1.0164 0.0062  0.0149  0.0213  391 LEU B CD2 
5860  N N   . GLN B 392 ? 0.7535 1.4289 1.2106 0.0087  0.0244  0.0346  392 GLN B N   
5861  C CA  . GLN B 392 ? 0.7290 1.4144 1.1942 0.0087  0.0265  0.0359  392 GLN B CA  
5862  C C   . GLN B 392 ? 0.7032 1.3872 1.1733 0.0055  0.0296  0.0330  392 GLN B C   
5863  O O   . GLN B 392 ? 0.6965 1.3753 1.1653 0.0031  0.0289  0.0293  392 GLN B O   
5864  C CB  . GLN B 392 ? 0.7274 1.4299 1.1989 0.0096  0.0227  0.0354  392 GLN B CB  
5865  C CG  . GLN B 392 ? 0.7597 1.4701 1.2351 0.0074  0.0198  0.0299  392 GLN B CG  
5866  C CD  . GLN B 392 ? 0.7833 1.4901 1.2528 0.0076  0.0167  0.0273  392 GLN B CD  
5867  O OE1 . GLN B 392 ? 0.7746 1.4731 1.2375 0.0092  0.0165  0.0297  392 GLN B OE1 
5868  N NE2 . GLN B 392 ? 0.7774 1.4907 1.2500 0.0059  0.0141  0.0221  392 GLN B NE2 
5869  N N   . ASN B 393 ? 0.6772 1.3659 1.1538 0.0055  0.0330  0.0348  393 ASN B N   
5870  C CA  . ASN B 393 ? 0.6150 1.3042 1.0983 0.0022  0.0366  0.0325  393 ASN B CA  
5871  C C   . ASN B 393 ? 0.6152 1.2873 1.0908 0.0000  0.0401  0.0319  393 ASN B C   
5872  O O   . ASN B 393 ? 0.6278 1.2968 1.1044 -0.0032 0.0400  0.0284  393 ASN B O   
5873  C CB  . ASN B 393 ? 0.6448 1.3465 1.1365 0.0000  0.0331  0.0278  393 ASN B CB  
5874  C CG  . ASN B 393 ? 0.6736 1.3906 1.1692 0.0024  0.0282  0.0282  393 ASN B CG  
5875  O OD1 . ASN B 393 ? 0.6610 1.3834 1.1586 0.0052  0.0285  0.0321  393 ASN B OD1 
5876  N ND2 . ASN B 393 ? 0.6591 1.3827 1.1553 0.0015  0.0238  0.0242  393 ASN B ND2 
5877  N N   . LYS B 394 ? 0.6225 1.2830 1.0899 0.0017  0.0432  0.0355  394 LYS B N   
5878  C CA  . LYS B 394 ? 0.6092 1.2524 1.0666 0.0002  0.0459  0.0356  394 LYS B CA  
5879  C C   . LYS B 394 ? 0.5714 1.2066 1.0258 0.0005  0.0524  0.0386  394 LYS B C   
5880  O O   . LYS B 394 ? 0.5703 1.2087 1.0254 0.0035  0.0535  0.0413  394 LYS B O   
5881  C CB  . LYS B 394 ? 0.6582 1.2924 1.1050 0.0023  0.0417  0.0363  394 LYS B CB  
5882  C CG  . LYS B 394 ? 0.6373 1.2556 1.0748 0.0005  0.0419  0.0351  394 LYS B CG  
5883  C CD  . LYS B 394 ? 0.6660 1.2881 1.1088 -0.0024 0.0396  0.0308  394 LYS B CD  
5884  C CE  . LYS B 394 ? 0.6712 1.2769 1.1054 -0.0042 0.0397  0.0299  394 LYS B CE  
5885  N NZ  . LYS B 394 ? 0.7099 1.3188 1.1494 -0.0065 0.0366  0.0254  394 LYS B NZ  
5886  N N   . THR B 395 ? 0.5718 1.1963 1.0224 -0.0026 0.0569  0.0381  395 THR B N   
5887  C CA  . THR B 395 ? 0.6272 1.2431 1.0737 -0.0027 0.0638  0.0405  395 THR B CA  
5888  C C   . THR B 395 ? 0.6050 1.2015 1.0354 -0.0026 0.0645  0.0420  395 THR B C   
5889  O O   . THR B 395 ? 0.6379 1.2265 1.0631 -0.0045 0.0621  0.0406  395 THR B O   
5890  C CB  . THR B 395 ? 0.6452 1.2648 1.1004 -0.0066 0.0696  0.0393  395 THR B CB  
5891  O OG1 . THR B 395 ? 0.6173 1.2254 1.0656 -0.0072 0.0770  0.0415  395 THR B OG1 
5892  C CG2 . THR B 395 ? 0.7649 1.3818 1.2213 -0.0107 0.0678  0.0363  395 THR B CG2 
5893  N N   . LEU B 396 ? 0.6395 1.2283 1.0621 -0.0001 0.0675  0.0446  396 LEU B N   
5894  C CA  . LEU B 396 ? 0.6732 1.2437 1.0796 0.0005  0.0677  0.0461  396 LEU B CA  
5895  C C   . LEU B 396 ? 0.6880 1.2494 1.0885 -0.0003 0.0759  0.0478  396 LEU B C   
5896  O O   . LEU B 396 ? 0.7230 1.2872 1.1250 0.0022  0.0791  0.0490  396 LEU B O   
5897  C CB  . LEU B 396 ? 0.7348 1.3030 1.1351 0.0045  0.0625  0.0473  396 LEU B CB  
5898  C CG  . LEU B 396 ? 0.6625 1.2374 1.0659 0.0053  0.0547  0.0457  396 LEU B CG  
5899  C CD1 . LEU B 396 ? 0.6223 1.1946 1.0202 0.0089  0.0505  0.0472  396 LEU B CD1 
5900  C CD2 . LEU B 396 ? 0.6097 1.1759 1.0078 0.0030  0.0521  0.0439  396 LEU B CD2 
5901  N N   . ASN B 397 ? 0.7953 1.3456 1.1891 -0.0037 0.0794  0.0479  397 ASN B N   
5902  C CA  . ASN B 397 ? 0.7792 1.3183 1.1642 -0.0048 0.0874  0.0496  397 ASN B CA  
5903  C C   . ASN B 397 ? 0.9004 1.4206 1.2661 -0.0033 0.0861  0.0513  397 ASN B C   
5904  O O   . ASN B 397 ? 0.8730 1.3836 1.2291 -0.0031 0.0922  0.0528  397 ASN B O   
5905  C CB  . ASN B 397 ? 0.7721 1.3099 1.1610 -0.0099 0.0930  0.0492  397 ASN B CB  
5906  C CG  . ASN B 397 ? 0.8187 1.3491 1.2034 -0.0125 0.0882  0.0483  397 ASN B CG  
5907  O OD1 . ASN B 397 ? 0.8131 1.3471 1.1996 -0.0109 0.0804  0.0469  397 ASN B OD1 
5908  N ND2 . ASN B 397 ? 0.8045 1.3241 1.1836 -0.0166 0.0931  0.0493  397 ASN B ND2 
5909  N N   . VAL B 398 ? 1.1597 1.6747 1.5195 -0.0022 0.0783  0.0509  398 VAL B N   
5910  C CA  . VAL B 398 ? 1.1882 1.6855 1.5301 -0.0008 0.0757  0.0523  398 VAL B CA  
5911  C C   . VAL B 398 ? 1.1765 1.6766 1.5176 0.0033  0.0685  0.0519  398 VAL B C   
5912  O O   . VAL B 398 ? 1.1422 1.6560 1.4952 0.0043  0.0640  0.0505  398 VAL B O   
5913  C CB  . VAL B 398 ? 1.2153 1.7020 1.5505 -0.0034 0.0727  0.0522  398 VAL B CB  
5914  C CG1 . VAL B 398 ? 1.2059 1.7022 1.5511 -0.0030 0.0650  0.0498  398 VAL B CG1 
5915  C CG2 . VAL B 398 ? 1.2586 1.7260 1.5743 -0.0019 0.0705  0.0540  398 VAL B CG2 
5916  N N   . SER B 399 ? 0.9842 1.4714 1.3112 0.0056  0.0677  0.0531  399 SER B N   
5917  C CA  . SER B 399 ? 0.9348 1.4233 1.2606 0.0091  0.0611  0.0528  399 SER B CA  
5918  C C   . SER B 399 ? 0.8949 1.3823 1.2203 0.0093  0.0527  0.0517  399 SER B C   
5919  O O   . SER B 399 ? 0.8706 1.3475 1.1882 0.0077  0.0513  0.0517  399 SER B O   
5920  C CB  . SER B 399 ? 0.9278 1.4020 1.2383 0.0112  0.0622  0.0539  399 SER B CB  
5921  O OG  . SER B 399 ? 0.9804 1.4560 1.2917 0.0115  0.0701  0.0544  399 SER B OG  
5922  N N   . VAL B 400 ? 0.8218 1.3202 1.1560 0.0112  0.0474  0.0507  400 VAL B N   
5923  C CA  . VAL B 400 ? 0.7229 1.2220 1.0581 0.0118  0.0396  0.0493  400 VAL B CA  
5924  C C   . VAL B 400 ? 0.7630 1.2583 1.0931 0.0148  0.0346  0.0497  400 VAL B C   
5925  O O   . VAL B 400 ? 0.7666 1.2634 1.0966 0.0164  0.0366  0.0507  400 VAL B O   
5926  C CB  . VAL B 400 ? 0.7205 1.2369 1.0712 0.0111  0.0375  0.0475  400 VAL B CB  
5927  C CG1 . VAL B 400 ? 0.8000 1.3198 1.1563 0.0079  0.0420  0.0466  400 VAL B CG1 
5928  C CG2 . VAL B 400 ? 0.7392 1.2692 1.0994 0.0128  0.0381  0.0481  400 VAL B CG2 
5929  N N   . GLN B 401 ? 0.7554 1.2460 1.0820 0.0156  0.0278  0.0486  401 GLN B N   
5930  C CA  . GLN B 401 ? 0.7901 1.2763 1.1119 0.0181  0.0224  0.0486  401 GLN B CA  
5931  C C   . GLN B 401 ? 0.7585 1.2472 1.0839 0.0187  0.0150  0.0467  401 GLN B C   
5932  O O   . GLN B 401 ? 0.7682 1.2491 1.0888 0.0180  0.0129  0.0459  401 GLN B O   
5933  C CB  . GLN B 401 ? 0.8445 1.3127 1.1497 0.0188  0.0230  0.0497  401 GLN B CB  
5934  C CG  . GLN B 401 ? 0.9469 1.4093 1.2467 0.0211  0.0166  0.0493  401 GLN B CG  
5935  C CD  . GLN B 401 ? 0.9754 1.4193 1.2574 0.0219  0.0164  0.0500  401 GLN B CD  
5936  O OE1 . GLN B 401 ? 0.9493 1.3850 1.2227 0.0207  0.0223  0.0512  401 GLN B OE1 
5937  N NE2 . GLN B 401 ? 0.9378 1.3752 1.2143 0.0237  0.0096  0.0492  401 GLN B NE2 
5938  N N   . ASP B 402 ? 0.7186 1.2179 1.0525 0.0200  0.0113  0.0461  402 ASP B N   
5939  C CA  . ASP B 402 ? 0.7344 1.2372 1.0726 0.0209  0.0044  0.0440  402 ASP B CA  
5940  C C   . ASP B 402 ? 0.7211 1.2286 1.0650 0.0196  0.0039  0.0419  402 ASP B C   
5941  O O   . ASP B 402 ? 0.7254 1.2251 1.0653 0.0201  -0.0003 0.0405  402 ASP B O   
5942  C CB  . ASP B 402 ? 0.7545 1.2425 1.0815 0.0224  -0.0009 0.0439  402 ASP B CB  
5943  C CG  . ASP B 402 ? 0.7410 1.2235 1.0620 0.0235  -0.0007 0.0454  402 ASP B CG  
5944  O OD1 . ASP B 402 ? 0.7401 1.2329 1.0690 0.0237  0.0013  0.0462  402 ASP B OD1 
5945  O OD2 . ASP B 402 ? 0.7406 1.2081 1.0487 0.0244  -0.0026 0.0457  402 ASP B OD2 
5946  N N   . ASP B 403 ? 0.6913 1.2115 1.0448 0.0182  0.0078  0.0416  403 ASP B N   
5947  C CA  . ASP B 403 ? 0.7033 1.2291 1.0632 0.0167  0.0078  0.0392  403 ASP B CA  
5948  C C   . ASP B 403 ? 0.6930 1.2376 1.0658 0.0162  0.0092  0.0383  403 ASP B C   
5949  O O   . ASP B 403 ? 0.6860 1.2382 1.0623 0.0170  0.0104  0.0401  403 ASP B O   
5950  C CB  . ASP B 403 ? 0.7048 1.2213 1.0590 0.0145  0.0125  0.0399  403 ASP B CB  
5951  C CG  . ASP B 403 ? 0.7554 1.2709 1.1125 0.0132  0.0106  0.0372  403 ASP B CG  
5952  O OD1 . ASP B 403 ? 0.7478 1.2743 1.1142 0.0138  0.0072  0.0343  403 ASP B OD1 
5953  O OD2 . ASP B 403 ? 0.8154 1.3186 1.1652 0.0117  0.0127  0.0380  403 ASP B OD2 
5954  N N   . ILE B 404 ? 0.6839 1.2355 1.0635 0.0150  0.0086  0.0354  404 ILE B N   
5955  C CA  . ILE B 404 ? 0.6005 1.1698 0.9916 0.0144  0.0096  0.0341  404 ILE B CA  
5956  C C   . ILE B 404 ? 0.6014 1.1720 0.9957 0.0118  0.0132  0.0327  404 ILE B C   
5957  O O   . ILE B 404 ? 0.5920 1.1597 0.9871 0.0108  0.0115  0.0297  404 ILE B O   
5958  C CB  . ILE B 404 ? 0.5909 1.1695 0.9882 0.0155  0.0047  0.0309  404 ILE B CB  
5959  C CG1 . ILE B 404 ? 0.7052 1.2816 1.0998 0.0177  0.0012  0.0323  404 ILE B CG1 
5960  C CG2 . ILE B 404 ? 0.5729 1.1695 0.9804 0.0149  0.0060  0.0298  404 ILE B CG2 
5961  C CD1 . ILE B 404 ? 0.7941 1.3798 1.1952 0.0189  -0.0031 0.0293  404 ILE B CD1 
5962  N N   . ILE B 405 ? 0.6527 1.2281 1.0497 0.0107  0.0182  0.0347  405 ILE B N   
5963  C CA  . ILE B 405 ? 0.5047 1.0807 0.9049 0.0078  0.0223  0.0338  405 ILE B CA  
5964  C C   . ILE B 405 ? 0.5763 1.1694 0.9884 0.0069  0.0214  0.0309  405 ILE B C   
5965  O O   . ILE B 405 ? 0.5583 1.1640 0.9761 0.0079  0.0217  0.0320  405 ILE B O   
5966  C CB  . ILE B 405 ? 0.5008 1.0733 0.8985 0.0072  0.0282  0.0371  405 ILE B CB  
5967  C CG1 . ILE B 405 ? 0.5649 1.1188 0.9493 0.0076  0.0295  0.0393  405 ILE B CG1 
5968  C CG2 . ILE B 405 ? 0.5781 1.1559 0.9828 0.0041  0.0326  0.0359  405 ILE B CG2 
5969  C CD1 . ILE B 405 ? 0.6160 1.1658 0.9942 0.0105  0.0272  0.0414  405 ILE B CD1 
5970  N N   . LEU B 406 ? 0.5213 1.1144 0.9365 0.0050  0.0203  0.0273  406 LEU B N   
5971  C CA  . LEU B 406 ? 0.5550 1.1634 0.9806 0.0039  0.0192  0.0237  406 LEU B CA  
5972  C C   . LEU B 406 ? 0.6276 1.2413 1.0595 0.0011  0.0237  0.0238  406 LEU B C   
5973  O O   . LEU B 406 ? 0.6170 1.2208 1.0465 -0.0013 0.0270  0.0241  406 LEU B O   
5974  C CB  . LEU B 406 ? 0.5364 1.1421 0.9630 0.0033  0.0155  0.0190  406 LEU B CB  
5975  C CG  . LEU B 406 ? 0.4919 1.0931 0.9142 0.0061  0.0107  0.0180  406 LEU B CG  
5976  C CD1 . LEU B 406 ? 0.5147 1.1131 0.9391 0.0056  0.0074  0.0129  406 LEU B CD1 
5977  C CD2 . LEU B 406 ? 0.5407 1.1556 0.9667 0.0083  0.0086  0.0184  406 LEU B CD2 
5978  O OXT . LEU B 406 ? 0.6879 1.3161 1.1276 0.0011  0.0242  0.0237  406 LEU B OXT 
5979  N N   . GLU C 4   ? 3.1308 2.3777 3.0423 0.2214  -0.4472 0.2956  4   GLU C N   
5980  C CA  . GLU C 4   ? 3.1670 2.4528 3.1132 0.2189  -0.4373 0.2770  4   GLU C CA  
5981  C C   . GLU C 4   ? 3.2841 2.6007 3.2474 0.2298  -0.4487 0.2650  4   GLU C C   
5982  O O   . GLU C 4   ? 3.2649 2.5725 3.2149 0.2397  -0.4651 0.2706  4   GLU C O   
5983  C CB  . GLU C 4   ? 3.0252 2.3260 2.9615 0.2031  -0.4156 0.2771  4   GLU C CB  
5984  C CG  . GLU C 4   ? 2.9182 2.1949 2.8440 0.1908  -0.4016 0.2862  4   GLU C CG  
5985  C CD  . GLU C 4   ? 2.8031 2.0977 2.7218 0.1758  -0.3804 0.2852  4   GLU C CD  
5986  O OE1 . GLU C 4   ? 2.7601 2.0826 2.6775 0.1750  -0.3773 0.2792  4   GLU C OE1 
5987  O OE2 . GLU C 4   ? 2.8118 2.0925 2.7269 0.1647  -0.3671 0.2902  4   GLU C OE2 
5988  N N   . LYS C 5   ? 3.4759 2.8289 3.4687 0.2276  -0.4398 0.2485  5   LYS C N   
5989  C CA  . LYS C 5   ? 3.4394 2.8255 3.4503 0.2359  -0.4475 0.2362  5   LYS C CA  
5990  C C   . LYS C 5   ? 3.4178 2.8396 3.4417 0.2261  -0.4302 0.2250  5   LYS C C   
5991  O O   . LYS C 5   ? 3.4178 2.8446 3.4548 0.2174  -0.4158 0.2201  5   LYS C O   
5992  C CB  . LYS C 5   ? 3.4183 2.8114 3.4637 0.2496  -0.4614 0.2245  5   LYS C CB  
5993  C CG  . LYS C 5   ? 3.4268 2.8369 3.4791 0.2620  -0.4778 0.2193  5   LYS C CG  
5994  C CD  . LYS C 5   ? 3.4602 2.8795 3.5492 0.2751  -0.4899 0.2067  5   LYS C CD  
5995  C CE  . LYS C 5   ? 3.4524 2.8812 3.5452 0.2884  -0.5088 0.2044  5   LYS C CE  
5996  N NZ  . LYS C 5   ? 3.4256 2.8243 3.4814 0.2912  -0.5209 0.2216  5   LYS C NZ  
5997  N N   . VAL C 6   ? 3.1489 2.5948 3.1690 0.2274  -0.4318 0.2210  6   VAL C N   
5998  C CA  . VAL C 6   ? 3.0225 2.5015 3.0511 0.2184  -0.4162 0.2119  6   VAL C CA  
5999  C C   . VAL C 6   ? 2.9135 2.4270 2.9706 0.2271  -0.4235 0.1966  6   VAL C C   
6000  O O   . VAL C 6   ? 2.8901 2.4035 2.9450 0.2375  -0.4396 0.1973  6   VAL C O   
6001  C CB  . VAL C 6   ? 2.9464 2.4216 2.9395 0.2092  -0.4082 0.2227  6   VAL C CB  
6002  C CG1 . VAL C 6   ? 2.8038 2.3133 2.8071 0.2002  -0.3922 0.2129  6   VAL C CG1 
6003  C CG2 . VAL C 6   ? 2.9254 2.3662 2.8902 0.2004  -0.4005 0.2380  6   VAL C CG2 
6004  N N   . VAL C 7   ? 2.8274 2.3706 2.9115 0.2227  -0.4117 0.1829  7   VAL C N   
6005  C CA  . VAL C 7   ? 2.7107 2.2896 2.8224 0.2289  -0.4153 0.1680  7   VAL C CA  
6006  C C   . VAL C 7   ? 2.6192 2.2253 2.7282 0.2184  -0.3997 0.1636  7   VAL C C   
6007  O O   . VAL C 7   ? 2.6133 2.2145 2.7092 0.2066  -0.3846 0.1684  7   VAL C O   
6008  C CB  . VAL C 7   ? 2.6753 2.2663 2.8250 0.2349  -0.4166 0.1541  7   VAL C CB  
6009  C CG1 . VAL C 7   ? 2.5735 2.1769 2.7358 0.2238  -0.3979 0.1474  7   VAL C CG1 
6010  C CG2 . VAL C 7   ? 2.6378 2.2591 2.8140 0.2449  -0.4258 0.1409  7   VAL C CG2 
6011  N N   . ALA C 8   ? 2.5829 2.2180 2.7048 0.2229  -0.4038 0.1545  8   ALA C N   
6012  C CA  . ALA C 8   ? 2.4805 2.1422 2.6002 0.2142  -0.3909 0.1502  8   ALA C CA  
6013  C C   . ALA C 8   ? 2.5553 2.2536 2.7108 0.2176  -0.3889 0.1333  8   ALA C C   
6014  O O   . ALA C 8   ? 2.6094 2.3171 2.7836 0.2286  -0.4020 0.1264  8   ALA C O   
6015  C CB  . ALA C 8   ? 2.4241 2.0838 2.5171 0.2148  -0.3971 0.1580  8   ALA C CB  
6016  N N   . VAL C 9   ? 2.6477 2.3666 2.8124 0.2080  -0.3724 0.1268  9   VAL C N   
6017  C CA  . VAL C 9   ? 2.6825 2.4370 2.8788 0.2094  -0.3679 0.1113  9   VAL C CA  
6018  C C   . VAL C 9   ? 2.6672 2.4438 2.8554 0.2003  -0.3557 0.1101  9   VAL C C   
6019  O O   . VAL C 9   ? 2.5976 2.3685 2.7705 0.1895  -0.3423 0.1155  9   VAL C O   
6020  C CB  . VAL C 9   ? 2.7012 2.4601 2.9215 0.2073  -0.3598 0.1026  9   VAL C CB  
6021  C CG1 . VAL C 9   ? 2.6939 2.4903 2.9444 0.2082  -0.3543 0.0870  9   VAL C CG1 
6022  C CG2 . VAL C 9   ? 2.7260 2.4623 2.9550 0.2168  -0.3721 0.1035  9   VAL C CG2 
6023  N N   . ILE C 10  ? 2.7014 2.5032 2.9006 0.2046  -0.3604 0.1029  10  ILE C N   
6024  C CA  . ILE C 10  ? 2.6575 2.4812 2.8505 0.1972  -0.3505 0.1012  10  ILE C CA  
6025  C C   . ILE C 10  ? 2.8918 2.7499 3.1165 0.1967  -0.3432 0.0865  10  ILE C C   
6026  O O   . ILE C 10  ? 2.8234 2.6949 3.0728 0.2056  -0.3519 0.0772  10  ILE C O   
6027  C CB  . ILE C 10  ? 2.5363 2.3607 2.7140 0.2017  -0.3615 0.1055  10  ILE C CB  
6028  C CG1 . ILE C 10  ? 2.3807 2.1699 2.5256 0.2027  -0.3695 0.1204  10  ILE C CG1 
6029  C CG2 . ILE C 10  ? 2.4637 2.3101 2.6353 0.1939  -0.3510 0.1035  10  ILE C CG2 
6030  C CD1 . ILE C 10  ? 2.2688 2.0564 2.3963 0.2072  -0.3811 0.1250  10  ILE C CD1 
6031  N N   . MET C 11  ? 3.6732 3.5457 3.8972 0.1864  -0.3273 0.0843  11  MET C N   
6032  C CA  . MET C 11  ? 3.6295 3.5356 3.8801 0.1850  -0.3196 0.0713  11  MET C CA  
6033  C C   . MET C 11  ? 3.5930 3.5213 3.8462 0.1874  -0.3236 0.0678  11  MET C C   
6034  O O   . MET C 11  ? 3.6037 3.5248 3.8337 0.1850  -0.3253 0.0757  11  MET C O   
6035  C CB  . MET C 11  ? 3.6470 3.5606 3.8953 0.1733  -0.3018 0.0707  11  MET C CB  
6036  C CG  . MET C 11  ? 3.6736 3.5735 3.9284 0.1706  -0.2964 0.0701  11  MET C CG  
6037  S SD  . MET C 11  ? 3.7552 3.6729 4.0479 0.1786  -0.3003 0.0547  11  MET C SD  
6038  C CE  . MET C 11  ? 3.6780 3.5740 3.9715 0.1738  -0.2936 0.0563  11  MET C CE  
6039  N N   . VAL C 12  ? 3.1355 3.0907 3.4172 0.1920  -0.3249 0.0555  12  VAL C N   
6040  C CA  . VAL C 12  ? 3.0556 3.0334 3.3447 0.1951  -0.3295 0.0508  12  VAL C CA  
6041  C C   . VAL C 12  ? 2.9748 2.9841 3.2803 0.1890  -0.3165 0.0416  12  VAL C C   
6042  O O   . VAL C 12  ? 2.9738 2.9963 3.2717 0.1846  -0.3124 0.0425  12  VAL C O   
6043  C CB  . VAL C 12  ? 3.0132 2.9953 3.3219 0.2074  -0.3451 0.0449  12  VAL C CB  
6044  C CG1 . VAL C 12  ? 2.9849 2.9959 3.3081 0.2096  -0.3475 0.0375  12  VAL C CG1 
6045  C CG2 . VAL C 12  ? 3.0398 2.9923 3.3290 0.2136  -0.3596 0.0551  12  VAL C CG2 
6046  N N   . GLY C 13  ? 2.6898 2.7108 3.0172 0.1886  -0.3099 0.0328  13  GLY C N   
6047  C CA  . GLY C 13  ? 2.3950 2.4464 2.7398 0.1839  -0.2986 0.0235  13  GLY C CA  
6048  C C   . GLY C 13  ? 2.3828 2.4589 2.7514 0.1913  -0.3055 0.0138  13  GLY C C   
6049  O O   . GLY C 13  ? 2.3949 2.4660 2.7654 0.1995  -0.3190 0.0147  13  GLY C O   
6050  N N   . GLY C 14  ? 2.2114 2.3149 2.5990 0.1882  -0.2959 0.0043  14  GLY C N   
6051  C CA  . GLY C 14  ? 2.1988 2.3281 2.6109 0.1942  -0.3003 -0.0056 14  GLY C CA  
6052  C C   . GLY C 14  ? 2.0234 2.1753 2.4348 0.1890  -0.2943 -0.0068 14  GLY C C   
6053  O O   . GLY C 14  ? 1.9270 2.0729 2.3171 0.1817  -0.2887 0.0008  14  GLY C O   
6054  N N   . PRO C 15  ? 2.0188 2.1972 2.4541 0.1927  -0.2952 -0.0164 15  PRO C N   
6055  C CA  . PRO C 15  ? 1.9481 2.1486 2.3847 0.1882  -0.2904 -0.0178 15  PRO C CA  
6056  C C   . PRO C 15  ? 1.8517 2.0639 2.2840 0.1781  -0.2745 -0.0184 15  PRO C C   
6057  O O   . PRO C 15  ? 1.7900 2.0189 2.2216 0.1737  -0.2696 -0.0187 15  PRO C O   
6058  C CB  . PRO C 15  ? 1.9388 2.1637 2.4047 0.1951  -0.2950 -0.0286 15  PRO C CB  
6059  C CG  . PRO C 15  ? 1.9851 2.2070 2.4671 0.2001  -0.2955 -0.0351 15  PRO C CG  
6060  C CD  . PRO C 15  ? 2.0883 2.2775 2.5509 0.2012  -0.3007 -0.0265 15  PRO C CD  
6061  N N   . THR C 16  ? 1.8079 2.0121 2.2381 0.1744  -0.2665 -0.0185 16  THR C N   
6062  C CA  . THR C 16  ? 1.6920 1.9063 2.1177 0.1649  -0.2519 -0.0187 16  THR C CA  
6063  C C   . THR C 16  ? 1.6000 1.7947 1.9976 0.1577  -0.2474 -0.0076 16  THR C C   
6064  O O   . THR C 16  ? 1.4887 1.6920 1.8807 0.1496  -0.2359 -0.0067 16  THR C O   
6065  C CB  . THR C 16  ? 1.7203 1.9388 2.1602 0.1642  -0.2449 -0.0258 16  THR C CB  
6066  O OG1 . THR C 16  ? 1.7657 1.9577 2.1978 0.1667  -0.2499 -0.0218 16  THR C OG1 
6067  C CG2 . THR C 16  ? 1.6691 1.9104 2.1371 0.1705  -0.2471 -0.0376 16  THR C CG2 
6068  N N   . LYS C 17  ? 1.6225 1.7913 2.0023 0.1604  -0.2562 0.0008  17  LYS C N   
6069  C CA  . LYS C 17  ? 1.5549 1.7046 1.9067 0.1540  -0.2525 0.0116  17  LYS C CA  
6070  C C   . LYS C 17  ? 1.5089 1.6618 1.8479 0.1533  -0.2562 0.0161  17  LYS C C   
6071  O O   . LYS C 17  ? 1.4254 1.5786 1.7489 0.1460  -0.2479 0.0209  17  LYS C O   
6072  C CB  . LYS C 17  ? 1.5719 1.6903 1.9089 0.1567  -0.2593 0.0191  17  LYS C CB  
6073  C CG  . LYS C 17  ? 1.6054 1.7184 1.9564 0.1587  -0.2580 0.0143  17  LYS C CG  
6074  C CD  . LYS C 17  ? 1.4358 1.5582 1.7901 0.1501  -0.2432 0.0115  17  LYS C CD  
6075  C CE  . LYS C 17  ? 1.4584 1.5760 1.8273 0.1520  -0.2422 0.0058  17  LYS C CE  
6076  N NZ  . LYS C 17  ? 1.4693 1.5553 1.8249 0.1545  -0.2491 0.0133  17  LYS C NZ  
6077  N N   . GLY C 18  ? 1.5579 1.7133 1.9036 0.1610  -0.2687 0.0142  18  GLY C N   
6078  C CA  . GLY C 18  ? 1.5248 1.6850 1.8611 0.1609  -0.2732 0.0171  18  GLY C CA  
6079  C C   . GLY C 18  ? 1.4277 1.6175 1.7791 0.1575  -0.2661 0.0102  18  GLY C C   
6080  O O   . GLY C 18  ? 1.3682 1.5680 1.7222 0.1596  -0.2720 0.0090  18  GLY C O   
6081  N N   . THR C 19  ? 1.5164 1.7201 1.8777 0.1522  -0.2535 0.0058  19  THR C N   
6082  C CA  . THR C 19  ? 1.4413 1.6724 1.8157 0.1482  -0.2453 0.0000  19  THR C CA  
6083  C C   . THR C 19  ? 1.3879 1.6186 1.7432 0.1407  -0.2382 0.0060  19  THR C C   
6084  O O   . THR C 19  ? 1.3164 1.5681 1.6801 0.1366  -0.2306 0.0023  19  THR C O   
6085  C CB  . THR C 19  ? 1.4269 1.6726 1.8182 0.1456  -0.2350 -0.0070 19  THR C CB  
6086  O OG1 . THR C 19  ? 1.2678 1.5408 1.6730 0.1426  -0.2281 -0.0128 19  THR C OG1 
6087  C CG2 . THR C 19  ? 1.4714 1.7036 1.8469 0.1385  -0.2251 -0.0017 19  THR C CG2 
6088  N N   . ARG C 20  ? 1.3317 1.5389 1.6615 0.1388  -0.2403 0.0153  20  ARG C N   
6089  C CA  . ARG C 20  ? 1.3113 1.5165 1.6219 0.1327  -0.2350 0.0210  20  ARG C CA  
6090  C C   . ARG C 20  ? 1.3680 1.5678 1.6685 0.1364  -0.2460 0.0240  20  ARG C C   
6091  O O   . ARG C 20  ? 1.3962 1.6019 1.6877 0.1323  -0.2425 0.0257  20  ARG C O   
6092  C CB  . ARG C 20  ? 1.3632 1.5467 1.6508 0.1273  -0.2283 0.0293  20  ARG C CB  
6093  C CG  . ARG C 20  ? 1.3668 1.5396 1.6596 0.1282  -0.2267 0.0288  20  ARG C CG  
6094  C CD  . ARG C 20  ? 1.3921 1.5644 1.6787 0.1198  -0.2126 0.0309  20  ARG C CD  
6095  N NE  . ARG C 20  ? 1.4220 1.5870 1.6860 0.1140  -0.2072 0.0382  20  ARG C NE  
6096  C CZ  . ARG C 20  ? 1.3982 1.5630 1.6541 0.1063  -0.1949 0.0410  20  ARG C CZ  
6097  N NH1 . ARG C 20  ? 1.3601 1.5313 1.6284 0.1033  -0.1871 0.0373  20  ARG C NH1 
6098  N NH2 . ARG C 20  ? 1.4342 1.5925 1.6700 0.1017  -0.1904 0.0472  20  ARG C NH2 
6099  N N   . PHE C 21  ? 1.4106 1.5991 1.7124 0.1440  -0.2594 0.0243  21  PHE C N   
6100  C CA  . PHE C 21  ? 1.4364 1.6200 1.7306 0.1484  -0.2717 0.0264  21  PHE C CA  
6101  C C   . PHE C 21  ? 1.4609 1.6688 1.7804 0.1526  -0.2773 0.0178  21  PHE C C   
6102  O O   . PHE C 21  ? 1.6174 1.8220 1.9379 0.1585  -0.2903 0.0176  21  PHE C O   
6103  C CB  . PHE C 21  ? 1.5198 1.6778 1.8017 0.1547  -0.2840 0.0318  21  PHE C CB  
6104  C CG  . PHE C 21  ? 1.5534 1.6852 1.8068 0.1505  -0.2798 0.0416  21  PHE C CG  
6105  C CD1 . PHE C 21  ? 1.6370 1.7491 1.8642 0.1511  -0.2869 0.0495  21  PHE C CD1 
6106  C CD2 . PHE C 21  ? 1.5504 1.6774 1.8033 0.1459  -0.2688 0.0428  21  PHE C CD2 
6107  C CE1 . PHE C 21  ? 1.6915 1.7796 1.8922 0.1471  -0.2824 0.0587  21  PHE C CE1 
6108  C CE2 . PHE C 21  ? 1.6090 1.7123 1.8366 0.1417  -0.2645 0.0519  21  PHE C CE2 
6109  C CZ  . PHE C 21  ? 1.6884 1.7723 1.8898 0.1423  -0.2710 0.0600  21  PHE C CZ  
6110  N N   . ARG C 22  ? 1.3457 1.5776 1.6857 0.1496  -0.2677 0.0108  22  ARG C N   
6111  C CA  . ARG C 22  ? 1.3246 1.5815 1.6921 0.1532  -0.2707 0.0018  22  ARG C CA  
6112  C C   . ARG C 22  ? 1.4862 1.7471 1.8550 0.1568  -0.2821 0.0013  22  ARG C C   
6113  O O   . ARG C 22  ? 1.5590 1.8254 1.9448 0.1640  -0.2925 -0.0034 22  ARG C O   
6114  C CB  . ARG C 22  ? 1.1244 1.4048 1.5045 0.1468  -0.2569 -0.0029 22  ARG C CB  
6115  C CG  . ARG C 22  ? 1.0919 1.3726 1.4758 0.1439  -0.2464 -0.0044 22  ARG C CG  
6116  C CD  . ARG C 22  ? 1.1287 1.4092 1.5303 0.1510  -0.2525 -0.0098 22  ARG C CD  
6117  N NE  . ARG C 22  ? 1.0336 1.3400 1.4626 0.1541  -0.2530 -0.0191 22  ARG C NE  
6118  C CZ  . ARG C 22  ? 0.9021 1.2258 1.3486 0.1527  -0.2442 -0.0259 22  ARG C CZ  
6119  N NH1 . ARG C 22  ? 0.9316 1.2495 1.3716 0.1483  -0.2347 -0.0247 22  ARG C NH1 
6120  N NH2 . ARG C 22  ? 0.8296 1.1765 1.3001 0.1556  -0.2448 -0.0340 22  ARG C NH2 
6121  N N   . PRO C 23  ? 1.4920 1.7514 1.8449 0.1522  -0.2808 0.0053  23  PRO C N   
6122  C CA  . PRO C 23  ? 1.6377 1.9015 1.9933 0.1556  -0.2923 0.0040  23  PRO C CA  
6123  C C   . PRO C 23  ? 1.8354 2.0814 2.1854 0.1637  -0.3082 0.0064  23  PRO C C   
6124  O O   . PRO C 23  ? 1.7741 2.0295 2.1402 0.1694  -0.3191 0.0018  23  PRO C O   
6125  C CB  . PRO C 23  ? 1.5155 1.7735 1.8484 0.1491  -0.2876 0.0094  23  PRO C CB  
6126  C CG  . PRO C 23  ? 1.4446 1.6878 1.7582 0.1440  -0.2770 0.0154  23  PRO C CG  
6127  C CD  . PRO C 23  ? 1.3379 1.5903 1.6695 0.1441  -0.2696 0.0111  23  PRO C CD  
6128  N N   . LEU C 24  ? 2.5353 2.7556 2.8630 0.1642  -0.3097 0.0137  24  LEU C N   
6129  C CA  . LEU C 24  ? 2.5571 2.7581 2.8777 0.1719  -0.3246 0.0169  24  LEU C CA  
6130  C C   . LEU C 24  ? 2.5495 2.7498 2.8881 0.1779  -0.3274 0.0133  24  LEU C C   
6131  O O   . LEU C 24  ? 2.5499 2.7447 2.8957 0.1861  -0.3412 0.0121  24  LEU C O   
6132  C CB  . LEU C 24  ? 2.6091 2.7812 2.8950 0.1695  -0.3252 0.0274  24  LEU C CB  
6133  C CG  . LEU C 24  ? 2.6203 2.7914 2.8856 0.1617  -0.3168 0.0314  24  LEU C CG  
6134  C CD1 . LEU C 24  ? 2.6694 2.8142 2.9036 0.1579  -0.3121 0.0411  24  LEU C CD1 
6135  C CD2 . LEU C 24  ? 2.6112 2.7859 2.8725 0.1635  -0.3272 0.0306  24  LEU C CD2 
6136  N N   . SER C 25  ? 1.8726 2.0782 2.2187 0.1743  -0.3150 0.0112  25  SER C N   
6137  C CA  . SER C 25  ? 1.7557 1.9596 2.1181 0.1796  -0.3168 0.0074  25  SER C CA  
6138  C C   . SER C 25  ? 1.7056 1.9315 2.0995 0.1863  -0.3235 -0.0024 25  SER C C   
6139  O O   . SER C 25  ? 1.7016 1.9230 2.1083 0.1936  -0.3308 -0.0053 25  SER C O   
6140  C CB  . SER C 25  ? 1.6272 1.8346 1.9917 0.1735  -0.3015 0.0063  25  SER C CB  
6141  O OG  . SER C 25  ? 1.6764 1.8577 2.0172 0.1711  -0.2993 0.0147  25  SER C OG  
6142  N N   . PHE C 26  ? 1.6159 1.8656 2.0233 0.1839  -0.3208 -0.0076 26  PHE C N   
6143  C CA  . PHE C 26  ? 1.5414 1.8135 1.9796 0.1896  -0.3260 -0.0170 26  PHE C CA  
6144  C C   . PHE C 26  ? 1.6431 1.9064 2.0845 0.1987  -0.3439 -0.0167 26  PHE C C   
6145  O O   . PHE C 26  ? 1.5285 1.8015 1.9939 0.2059  -0.3502 -0.0234 26  PHE C O   
6146  C CB  . PHE C 26  ? 1.3953 1.6930 1.8449 0.1844  -0.3193 -0.0214 26  PHE C CB  
6147  C CG  . PHE C 26  ? 1.3141 1.6261 1.7688 0.1771  -0.3025 -0.0240 26  PHE C CG  
6148  C CD1 . PHE C 26  ? 1.3354 1.6596 1.7855 0.1696  -0.2938 -0.0232 26  PHE C CD1 
6149  C CD2 . PHE C 26  ? 1.2352 1.5484 1.6994 0.1780  -0.2959 -0.0274 26  PHE C CD2 
6150  C CE1 . PHE C 26  ? 1.1895 1.5267 1.6439 0.1632  -0.2789 -0.0254 26  PHE C CE1 
6151  C CE2 . PHE C 26  ? 1.1659 1.4924 1.6343 0.1714  -0.2810 -0.0300 26  PHE C CE2 
6152  C CZ  . PHE C 26  ? 1.1196 1.4583 1.5830 0.1641  -0.2727 -0.0287 26  PHE C CZ  
6153  N N   . ASN C 27  ? 1.8259 2.0710 2.2436 0.1987  -0.3524 -0.0091 27  ASN C N   
6154  C CA  . ASN C 27  ? 1.8702 2.1048 2.2879 0.2072  -0.3704 -0.0080 27  ASN C CA  
6155  C C   . ASN C 27  ? 1.9403 2.1465 2.3426 0.2122  -0.3771 -0.0017 27  ASN C C   
6156  O O   . ASN C 27  ? 1.9915 2.1944 2.4075 0.2210  -0.3884 -0.0044 27  ASN C O   
6157  C CB  . ASN C 27  ? 2.0146 2.2447 2.4147 0.2050  -0.3773 -0.0037 27  ASN C CB  
6158  C CG  . ASN C 27  ? 2.1053 2.3260 2.5059 0.2139  -0.3967 -0.0028 27  ASN C CG  
6159  O OD1 . ASN C 27  ? 2.2011 2.4398 2.6273 0.2191  -0.4045 -0.0101 27  ASN C OD1 
6160  N ND2 . ASN C 27  ? 2.1230 2.3155 2.4951 0.2156  -0.4046 0.0061  27  ASN C ND2 
6161  N N   . THR C 28  ? 1.8856 2.0711 2.2599 0.2066  -0.3702 0.0068  28  THR C N   
6162  C CA  . THR C 28  ? 1.9266 2.0830 2.2827 0.2101  -0.3758 0.0142  28  THR C CA  
6163  C C   . THR C 28  ? 1.9241 2.0730 2.2718 0.2035  -0.3608 0.0169  28  THR C C   
6164  O O   . THR C 28  ? 1.9365 2.0886 2.2713 0.1947  -0.3485 0.0194  28  THR C O   
6165  C CB  . THR C 28  ? 1.9959 2.1292 2.3204 0.2100  -0.3850 0.0239  28  THR C CB  
6166  O OG1 . THR C 28  ? 2.0267 2.1638 2.3598 0.2176  -0.4016 0.0214  28  THR C OG1 
6167  C CG2 . THR C 28  ? 2.0674 2.1693 2.3687 0.2113  -0.3873 0.0331  28  THR C CG2 
6168  N N   . PRO C 29  ? 2.0069 2.1459 2.3619 0.2075  -0.3614 0.0162  29  PRO C N   
6169  C CA  . PRO C 29  ? 2.0678 2.1990 2.4153 0.2012  -0.3477 0.0185  29  PRO C CA  
6170  C C   . PRO C 29  ? 2.3096 2.4165 2.6221 0.1950  -0.3439 0.0300  29  PRO C C   
6171  O O   . PRO C 29  ? 2.4022 2.4932 2.6944 0.1970  -0.3536 0.0368  29  PRO C O   
6172  C CB  . PRO C 29  ? 2.2023 2.3228 2.5624 0.2085  -0.3534 0.0164  29  PRO C CB  
6173  C CG  . PRO C 29  ? 2.1495 2.2851 2.5346 0.2178  -0.3657 0.0087  29  PRO C CG  
6174  C CD  . PRO C 29  ? 2.0457 2.1827 2.4195 0.2181  -0.3743 0.0119  29  PRO C CD  
6175  N N   . LYS C 30  ? 2.3118 2.4166 2.6178 0.1873  -0.3293 0.0317  30  LYS C N   
6176  C CA  . LYS C 30  ? 2.4753 2.5594 2.7498 0.1802  -0.3229 0.0420  30  LYS C CA  
6177  C C   . LYS C 30  ? 2.8574 2.9097 3.1090 0.1844  -0.3338 0.0517  30  LYS C C   
6178  O O   . LYS C 30  ? 2.8473 2.8860 3.0729 0.1822  -0.3364 0.0594  30  LYS C O   
6179  C CB  . LYS C 30  ? 2.1880 2.2745 2.4643 0.1726  -0.3068 0.0414  30  LYS C CB  
6180  C CG  . LYS C 30  ? 2.0593 2.1292 2.3064 0.1642  -0.2976 0.0509  30  LYS C CG  
6181  C CD  . LYS C 30  ? 1.9356 1.9936 2.1806 0.1600  -0.2882 0.0532  30  LYS C CD  
6182  C CE  . LYS C 30  ? 1.6960 1.7592 1.9307 0.1495  -0.2721 0.0555  30  LYS C CE  
6183  N NZ  . LYS C 30  ? 1.6229 1.7167 1.8802 0.1466  -0.2633 0.0459  30  LYS C NZ  
6184  N N   . PRO C 31  ? 3.9627 4.0012 4.2212 0.1904  -0.3403 0.0520  31  PRO C N   
6185  C CA  . PRO C 31  ? 4.0026 4.0086 4.2363 0.1935  -0.3495 0.0625  31  PRO C CA  
6186  C C   . PRO C 31  ? 3.9982 3.9970 4.2216 0.2002  -0.3657 0.0658  31  PRO C C   
6187  O O   . PRO C 31  ? 4.0342 4.0064 4.2305 0.2011  -0.3721 0.0759  31  PRO C O   
6188  C CB  . PRO C 31  ? 4.0124 4.0096 4.2620 0.1992  -0.3532 0.0600  31  PRO C CB  
6189  C CG  . PRO C 31  ? 3.9823 4.0047 4.2590 0.1962  -0.3416 0.0495  31  PRO C CG  
6190  C CD  . PRO C 31  ? 3.9403 3.9906 4.2281 0.1947  -0.3395 0.0430  31  PRO C CD  
6191  N N   . LEU C 32  ? 2.9647 2.9858 3.2084 0.2049  -0.3727 0.0577  32  LEU C N   
6192  C CA  . LEU C 32  ? 2.7100 2.7261 2.9472 0.2117  -0.3893 0.0596  32  LEU C CA  
6193  C C   . LEU C 32  ? 2.6584 2.6829 2.8811 0.2065  -0.3873 0.0610  32  LEU C C   
6194  O O   . LEU C 32  ? 2.5883 2.6121 2.8069 0.2115  -0.4006 0.0614  32  LEU C O   
6195  C CB  . LEU C 32  ? 2.5135 2.5477 2.7836 0.2210  -0.4001 0.0498  32  LEU C CB  
6196  C CG  . LEU C 32  ? 2.6084 2.6415 2.8999 0.2259  -0.3997 0.0452  32  LEU C CG  
6197  C CD1 . LEU C 32  ? 2.4838 2.5381 2.8088 0.2348  -0.4093 0.0347  32  LEU C CD1 
6198  C CD2 . LEU C 32  ? 2.5871 2.5866 2.8590 0.2297  -0.4071 0.0548  32  LEU C CD2 
6199  N N   . ILE C 33  ? 2.5989 2.6310 2.8140 0.1969  -0.3714 0.0615  33  ILE C N   
6200  C CA  . ILE C 33  ? 2.5768 2.6171 2.7787 0.1917  -0.3685 0.0623  33  ILE C CA  
6201  C C   . ILE C 33  ? 2.6457 2.6580 2.8105 0.1908  -0.3739 0.0734  33  ILE C C   
6202  O O   . ILE C 33  ? 2.6649 2.6560 2.8095 0.1873  -0.3677 0.0814  33  ILE C O   
6203  C CB  . ILE C 33  ? 2.5195 2.5759 2.7251 0.1820  -0.3497 0.0596  33  ILE C CB  
6204  C CG1 . ILE C 33  ? 2.3282 2.4136 2.5697 0.1829  -0.3449 0.0483  33  ILE C CG1 
6205  C CG2 . ILE C 33  ? 2.6303 2.6910 2.8187 0.1763  -0.3461 0.0616  33  ILE C CG2 
6206  C CD1 . ILE C 33  ? 2.1493 2.2512 2.3959 0.1739  -0.3271 0.0454  33  ILE C CD1 
6207  N N   . PRO C 34  ? 2.7887 2.8000 2.9432 0.1937  -0.3853 0.0743  34  PRO C N   
6208  C CA  . PRO C 34  ? 2.8350 2.8183 2.9533 0.1940  -0.3922 0.0848  34  PRO C CA  
6209  C C   . PRO C 34  ? 2.7796 2.7544 2.8710 0.1842  -0.3776 0.0911  34  PRO C C   
6210  O O   . PRO C 34  ? 2.6690 2.6590 2.7598 0.1789  -0.3706 0.0877  34  PRO C O   
6211  C CB  . PRO C 34  ? 2.8134 2.8035 2.9323 0.1992  -0.4073 0.0819  34  PRO C CB  
6212  C CG  . PRO C 34  ? 2.7051 2.7222 2.8631 0.2040  -0.4115 0.0707  34  PRO C CG  
6213  C CD  . PRO C 34  ? 2.7203 2.7548 2.8966 0.1977  -0.3939 0.0657  34  PRO C CD  
6214  N N   . LEU C 35  ? 2.7070 2.6573 2.7766 0.1818  -0.3728 0.1002  35  LEU C N   
6215  C CA  . LEU C 35  ? 2.5994 2.5377 2.6402 0.1731  -0.3600 0.1074  35  LEU C CA  
6216  C C   . LEU C 35  ? 2.5855 2.4969 2.5912 0.1755  -0.3704 0.1170  35  LEU C C   
6217  O O   . LEU C 35  ? 2.6644 2.5543 2.6608 0.1809  -0.3803 0.1231  35  LEU C O   
6218  C CB  . LEU C 35  ? 2.5372 2.4675 2.5780 0.1677  -0.3461 0.1109  35  LEU C CB  
6219  C CG  . LEU C 35  ? 2.5277 2.4842 2.5989 0.1637  -0.3334 0.1018  35  LEU C CG  
6220  C CD1 . LEU C 35  ? 2.5498 2.4967 2.6173 0.1575  -0.3196 0.1059  35  LEU C CD1 
6221  C CD2 . LEU C 35  ? 2.3069 2.2858 2.3821 0.1584  -0.3254 0.0965  35  LEU C CD2 
6222  N N   . ALA C 36  ? 2.4511 2.3633 2.4370 0.1715  -0.3682 0.1183  36  ALA C N   
6223  C CA  . ALA C 36  ? 2.4037 2.2926 2.3552 0.1737  -0.3783 0.1264  36  ALA C CA  
6224  C C   . ALA C 36  ? 2.4930 2.3772 2.4501 0.1842  -0.3998 0.1253  36  ALA C C   
6225  O O   . ALA C 36  ? 2.5088 2.3679 2.4410 0.1882  -0.4105 0.1337  36  ALA C O   
6226  C CB  . ALA C 36  ? 2.2596 2.1196 2.1808 0.1700  -0.3716 0.1382  36  ALA C CB  
6227  N N   . GLY C 37  ? 2.6541 2.5629 2.6444 0.1886  -0.4063 0.1151  37  GLY C N   
6228  C CA  . GLY C 37  ? 2.7033 2.6125 2.7044 0.1985  -0.4263 0.1123  37  GLY C CA  
6229  C C   . GLY C 37  ? 2.9954 2.9030 3.0196 0.2055  -0.4327 0.1108  37  GLY C C   
6230  O O   . GLY C 37  ? 2.9188 2.8387 2.9666 0.2131  -0.4459 0.1043  37  GLY C O   
6231  N N   . GLN C 38  ? 3.6478 3.5408 3.6664 0.2029  -0.4237 0.1164  38  GLN C N   
6232  C CA  . GLN C 38  ? 3.6434 3.5323 3.6820 0.2092  -0.4290 0.1154  38  GLN C CA  
6233  C C   . GLN C 38  ? 3.6228 3.5313 3.6893 0.2046  -0.4135 0.1083  38  GLN C C   
6234  O O   . GLN C 38  ? 3.6256 3.5410 3.6865 0.1955  -0.3971 0.1083  38  GLN C O   
6235  C CB  . GLN C 38  ? 3.6883 3.5428 3.6993 0.2104  -0.4319 0.1276  38  GLN C CB  
6236  C CG  . GLN C 38  ? 3.7157 3.5474 3.6934 0.2140  -0.4457 0.1363  38  GLN C CG  
6237  C CD  . GLN C 38  ? 3.6962 3.5334 3.6873 0.2247  -0.4668 0.1318  38  GLN C CD  
6238  O OE1 . GLN C 38  ? 3.6716 3.5222 3.6949 0.2310  -0.4728 0.1246  38  GLN C OE1 
6239  N NE2 . GLN C 38  ? 3.7079 3.5348 3.6744 0.2268  -0.4781 0.1360  38  GLN C NE2 
6240  N N   . PRO C 39  ? 2.9091 2.8273 3.0059 0.2108  -0.4185 0.1018  39  PRO C N   
6241  C CA  . PRO C 39  ? 2.7979 2.7350 2.9211 0.2068  -0.4043 0.0945  39  PRO C CA  
6242  C C   . PRO C 39  ? 2.8151 2.7373 2.9221 0.1987  -0.3889 0.1012  39  PRO C C   
6243  O O   . PRO C 39  ? 2.7672 2.6618 2.8449 0.1973  -0.3901 0.1119  39  PRO C O   
6244  C CB  . PRO C 39  ? 2.5944 2.5350 2.7454 0.2164  -0.4150 0.0890  39  PRO C CB  
6245  C CG  . PRO C 39  ? 2.3761 2.3146 2.5259 0.2250  -0.4342 0.0888  39  PRO C CG  
6246  C CD  . PRO C 39  ? 2.6717 2.5868 2.7818 0.2222  -0.4377 0.0998  39  PRO C CD  
6247  N N   . MET C 40  ? 2.8153 2.7565 2.9423 0.1932  -0.3743 0.0946  40  MET C N   
6248  C CA  . MET C 40  ? 2.8259 2.7573 2.9406 0.1844  -0.3583 0.0996  40  MET C CA  
6249  C C   . MET C 40  ? 2.8187 2.7224 2.9239 0.1870  -0.3618 0.1070  40  MET C C   
6250  O O   . MET C 40  ? 2.8037 2.6846 2.8812 0.1819  -0.3564 0.1171  40  MET C O   
6251  C CB  . MET C 40  ? 2.8353 2.7934 2.9768 0.1794  -0.3442 0.0902  40  MET C CB  
6252  C CG  . MET C 40  ? 2.7896 2.7408 2.9215 0.1700  -0.3273 0.0942  40  MET C CG  
6253  S SD  . MET C 40  ? 2.7229 2.7071 2.8843 0.1640  -0.3115 0.0830  40  MET C SD  
6254  C CE  . MET C 40  ? 2.5700 2.5765 2.7305 0.1617  -0.3107 0.0790  40  MET C CE  
6255  N N   . ILE C 41  ? 2.6918 2.5970 2.8201 0.1949  -0.3705 0.1022  41  ILE C N   
6256  C CA  . ILE C 41  ? 2.5824 2.4612 2.7039 0.1979  -0.3745 0.1087  41  ILE C CA  
6257  C C   . ILE C 41  ? 2.4622 2.3138 2.5591 0.2042  -0.3902 0.1185  41  ILE C C   
6258  O O   . ILE C 41  ? 2.4527 2.2793 2.5405 0.2069  -0.3945 0.1255  41  ILE C O   
6259  C CB  . ILE C 41  ? 2.6868 2.5754 2.8418 0.2046  -0.3785 0.0997  41  ILE C CB  
6260  C CG1 . ILE C 41  ? 2.5841 2.4892 2.7597 0.2145  -0.3934 0.0920  41  ILE C CG1 
6261  C CG2 . ILE C 41  ? 2.8153 2.7257 2.9915 0.1979  -0.3622 0.0913  41  ILE C CG2 
6262  C CD1 . ILE C 41  ? 2.6153 2.5321 2.8250 0.2217  -0.3975 0.0823  41  ILE C CD1 
6263  N N   . HIS C 42  ? 2.5052 2.3606 2.5909 0.2068  -0.3993 0.1193  42  HIS C N   
6264  C CA  . HIS C 42  ? 2.4447 2.2751 2.5067 0.2133  -0.4154 0.1282  42  HIS C CA  
6265  C C   . HIS C 42  ? 2.5348 2.3355 2.5580 0.2071  -0.4099 0.1418  42  HIS C C   
6266  O O   . HIS C 42  ? 2.6624 2.4376 2.6640 0.2123  -0.4223 0.1508  42  HIS C O   
6267  C CB  . HIS C 42  ? 2.4878 2.3318 2.5492 0.2173  -0.4265 0.1245  42  HIS C CB  
6268  C CG  . HIS C 42  ? 2.4006 2.2255 2.4494 0.2270  -0.4470 0.1300  42  HIS C CG  
6269  N ND1 . HIS C 42  ? 2.1427 1.9737 2.2168 0.2377  -0.4618 0.1242  42  HIS C ND1 
6270  C CD2 . HIS C 42  ? 2.4067 2.2069 2.4205 0.2279  -0.4552 0.1407  42  HIS C CD2 
6271  C CE1 . HIS C 42  ? 2.1491 1.9598 2.2046 0.2448  -0.4788 0.1312  42  HIS C CE1 
6272  N NE2 . HIS C 42  ? 2.3137 2.1053 2.3319 0.2390  -0.4753 0.1414  42  HIS C NE2 
6273  N N   . HIS C 43  ? 2.4417 2.2451 2.4555 0.1964  -0.3916 0.1437  43  HIS C N   
6274  C CA  . HIS C 43  ? 2.4954 2.2718 2.4734 0.1898  -0.3845 0.1563  43  HIS C CA  
6275  C C   . HIS C 43  ? 2.6297 2.3866 2.6085 0.1883  -0.3796 0.1616  43  HIS C C   
6276  O O   . HIS C 43  ? 2.7859 2.5127 2.7380 0.1887  -0.3837 0.1733  43  HIS C O   
6277  C CB  . HIS C 43  ? 2.3053 2.0934 2.2718 0.1789  -0.3673 0.1561  43  HIS C CB  
6278  C CG  . HIS C 43  ? 2.2475 2.0532 2.2113 0.1794  -0.3709 0.1513  43  HIS C CG  
6279  N ND1 . HIS C 43  ? 2.3635 2.1980 2.3574 0.1833  -0.3752 0.1395  43  HIS C ND1 
6280  C CD2 . HIS C 43  ? 2.1834 1.9819 2.1180 0.1762  -0.3705 0.1567  43  HIS C CD2 
6281  C CE1 . HIS C 43  ? 2.4334 2.2771 2.4171 0.1824  -0.3776 0.1379  43  HIS C CE1 
6282  N NE2 . HIS C 43  ? 2.2526 2.0749 2.2004 0.1783  -0.3750 0.1479  43  HIS C NE2 
6283  N N   . PRO C 44  ? 2.5409 2.3129 2.5487 0.1864  -0.3709 0.1536  44  PRO C N   
6284  C CA  . PRO C 44  ? 2.6039 2.3561 2.6146 0.1865  -0.3690 0.1579  44  PRO C CA  
6285  C C   . PRO C 44  ? 2.7860 2.5181 2.7967 0.1975  -0.3876 0.1617  44  PRO C C   
6286  O O   . PRO C 44  ? 2.8647 2.5670 2.8562 0.1973  -0.3896 0.1723  44  PRO C O   
6287  C CB  . PRO C 44  ? 2.4638 2.2415 2.5098 0.1841  -0.3590 0.1459  44  PRO C CB  
6288  C CG  . PRO C 44  ? 2.4295 2.2335 2.4788 0.1777  -0.3482 0.1399  44  PRO C CG  
6289  C CD  . PRO C 44  ? 2.4612 2.2665 2.4960 0.1823  -0.3598 0.1416  44  PRO C CD  
6290  N N   . ILE C 45  ? 2.7515 2.4993 2.7837 0.2071  -0.4012 0.1534  45  ILE C N   
6291  C CA  . ILE C 45  ? 2.8706 2.6010 2.9050 0.2185  -0.4198 0.1563  45  ILE C CA  
6292  C C   . ILE C 45  ? 3.1868 2.8883 3.1830 0.2201  -0.4297 0.1698  45  ILE C C   
6293  O O   . ILE C 45  ? 3.1616 2.8360 3.1470 0.2257  -0.4400 0.1779  45  ILE C O   
6294  C CB  . ILE C 45  ? 2.7189 2.4748 2.7840 0.2279  -0.4319 0.1442  45  ILE C CB  
6295  C CG1 . ILE C 45  ? 2.6597 2.4442 2.7612 0.2259  -0.4212 0.1309  45  ILE C CG1 
6296  C CG2 . ILE C 45  ? 2.7628 2.5017 2.8324 0.2403  -0.4514 0.1466  45  ILE C CG2 
6297  C CD1 . ILE C 45  ? 2.4990 2.3112 2.6316 0.2341  -0.4307 0.1185  45  ILE C CD1 
6298  N N   . SER C 46  ? 4.0927 3.7989 4.0672 0.2154  -0.4266 0.1725  46  SER C N   
6299  C CA  . SER C 46  ? 4.1283 3.8076 4.0643 0.2165  -0.4352 0.1851  46  SER C CA  
6300  C C   . SER C 46  ? 4.1712 3.8200 4.0798 0.2099  -0.4263 0.1981  46  SER C C   
6301  O O   . SER C 46  ? 4.1973 3.8171 4.0782 0.2133  -0.4362 0.2096  46  SER C O   
6302  C CB  . SER C 46  ? 4.1142 3.8067 4.0340 0.2121  -0.4322 0.1840  46  SER C CB  
6303  O OG  . SER C 46  ? 4.0744 3.7872 4.0123 0.2199  -0.4456 0.1750  46  SER C OG  
6304  N N   . ALA C 47  ? 3.2638 2.9183 3.1796 0.2004  -0.4078 0.1966  47  ALA C N   
6305  C CA  . ALA C 47  ? 3.0871 2.7142 2.9793 0.1932  -0.3979 0.2084  47  ALA C CA  
6306  C C   . ALA C 47  ? 2.9593 2.5673 2.8628 0.1978  -0.4034 0.2113  47  ALA C C   
6307  O O   . ALA C 47  ? 2.8859 2.4658 2.7674 0.1936  -0.3991 0.2228  47  ALA C O   
6308  C CB  . ALA C 47  ? 2.9582 2.5994 2.8533 0.1807  -0.3757 0.2057  47  ALA C CB  
6309  N N   . CYS C 48  ? 2.9276 2.5496 2.8647 0.2064  -0.4127 0.2011  48  CYS C N   
6310  C CA  . CYS C 48  ? 2.7500 2.3540 2.6994 0.2115  -0.4185 0.2029  48  CYS C CA  
6311  C C   . CYS C 48  ? 2.6900 2.2634 2.6180 0.2204  -0.4367 0.2140  48  CYS C C   
6312  O O   . CYS C 48  ? 2.6039 2.1526 2.5297 0.2225  -0.4399 0.2204  48  CYS C O   
6313  C CB  . CYS C 48  ? 2.6735 2.3032 2.6659 0.2183  -0.4224 0.1879  48  CYS C CB  
6314  N N   . LYS C 49  ? 2.6712 2.2454 2.5836 0.2257  -0.4491 0.2161  49  LYS C N   
6315  C CA  . LYS C 49  ? 2.6043 2.1504 2.4960 0.2347  -0.4678 0.2263  49  LYS C CA  
6316  C C   . LYS C 49  ? 2.5823 2.0933 2.4329 0.2284  -0.4630 0.2432  49  LYS C C   
6317  O O   . LYS C 49  ? 2.5645 2.0465 2.3998 0.2348  -0.4759 0.2531  49  LYS C O   
6318  C CB  . LYS C 49  ? 2.7082 2.2667 2.5948 0.2416  -0.4821 0.2232  49  LYS C CB  
6319  C CG  . LYS C 49  ? 2.6518 2.1874 2.5257 0.2534  -0.5047 0.2306  49  LYS C CG  
6320  C CD  . LYS C 49  ? 2.6552 2.1828 2.5553 0.2621  -0.5136 0.2280  49  LYS C CD  
6321  C CE  . LYS C 49  ? 2.5949 2.0932 2.4775 0.2728  -0.5346 0.2382  49  LYS C CE  
6322  N NZ  . LYS C 49  ? 2.6567 2.1640 2.5743 0.2858  -0.5503 0.2293  49  LYS C NZ  
6323  N N   . LYS C 50  ? 2.5420 2.0548 2.3746 0.2161  -0.4448 0.2467  50  LYS C N   
6324  C CA  . LYS C 50  ? 2.4796 1.9603 2.2729 0.2093  -0.4387 0.2626  50  LYS C CA  
6325  C C   . LYS C 50  ? 2.4771 1.9341 2.2734 0.2071  -0.4341 0.2692  50  LYS C C   
6326  O O   . LYS C 50  ? 2.5031 1.9292 2.2675 0.2031  -0.4319 0.2836  50  LYS C O   
6327  C CB  . LYS C 50  ? 2.4491 1.9402 2.2251 0.1967  -0.4196 0.2636  50  LYS C CB  
6328  C CG  . LYS C 50  ? 2.3517 1.8512 2.1432 0.1861  -0.3990 0.2603  50  LYS C CG  
6329  C CD  . LYS C 50  ? 2.3828 1.8832 2.1489 0.1738  -0.3812 0.2655  50  LYS C CD  
6330  C CE  . LYS C 50  ? 2.5937 2.1194 2.3844 0.1645  -0.3621 0.2559  50  LYS C CE  
6331  N NZ  . LYS C 50  ? 2.6818 2.2431 2.5071 0.1690  -0.3650 0.2399  50  LYS C NZ  
6332  N N   . ILE C 51  ? 2.5561 2.0263 2.3893 0.2094  -0.4324 0.2591  51  ILE C N   
6333  C CA  . ILE C 51  ? 2.5829 2.0309 2.4225 0.2086  -0.4301 0.2640  51  ILE C CA  
6334  C C   . ILE C 51  ? 2.6661 2.0977 2.5127 0.2224  -0.4518 0.2658  51  ILE C C   
6335  O O   . ILE C 51  ? 2.6803 2.1319 2.5591 0.2314  -0.4613 0.2537  51  ILE C O   
6336  C CB  . ILE C 51  ? 2.5170 1.9873 2.3921 0.2033  -0.4163 0.2517  51  ILE C CB  
6337  C CG1 . ILE C 51  ? 2.3795 1.8671 2.2485 0.1900  -0.3954 0.2497  51  ILE C CG1 
6338  C CG2 . ILE C 51  ? 2.6364 2.0827 2.5185 0.2028  -0.4149 0.2563  51  ILE C CG2 
6339  C CD1 . ILE C 51  ? 2.4757 2.0014 2.3641 0.1907  -0.3931 0.2361  51  ILE C CD1 
6340  N N   . SER C 52  ? 2.6049 2.0001 2.4214 0.2244  -0.4597 0.2811  52  SER C N   
6341  C CA  . SER C 52  ? 2.6628 2.0399 2.4821 0.2379  -0.4814 0.2845  52  SER C CA  
6342  C C   . SER C 52  ? 2.7478 2.1233 2.6012 0.2429  -0.4838 0.2778  52  SER C C   
6343  O O   . SER C 52  ? 2.7768 2.1510 2.6473 0.2557  -0.5014 0.2739  52  SER C O   
6344  C CB  . SER C 52  ? 2.7225 2.0593 2.4990 0.2379  -0.4881 0.3035  52  SER C CB  
6345  O OG  . SER C 52  ? 2.8052 2.1195 2.5693 0.2279  -0.4737 0.3129  52  SER C OG  
6346  N N   . ASN C 53  ? 2.7836 2.1596 2.6478 0.2333  -0.4667 0.2759  53  ASN C N   
6347  C CA  . ASN C 53  ? 2.8282 2.2027 2.7242 0.2368  -0.4671 0.2689  53  ASN C CA  
6348  C C   . ASN C 53  ? 2.9272 2.3412 2.8645 0.2378  -0.4615 0.2496  53  ASN C C   
6349  O O   . ASN C 53  ? 3.0192 2.4365 2.9830 0.2372  -0.4562 0.2423  53  ASN C O   
6350  C CB  . ASN C 53  ? 2.8356 2.1864 2.7204 0.2258  -0.4525 0.2778  53  ASN C CB  
6351  C CG  . ASN C 53  ? 2.7339 2.0927 2.5994 0.2110  -0.4323 0.2812  53  ASN C CG  
6352  O OD1 . ASN C 53  ? 2.7327 2.0927 2.5713 0.2087  -0.4323 0.2871  53  ASN C OD1 
6353  N ND2 . ASN C 53  ? 2.7028 2.0675 2.5824 0.2010  -0.4154 0.2772  53  ASN C ND2 
6354  N N   . LEU C 54  ? 3.0624 2.5061 3.0053 0.2391  -0.4624 0.2413  54  LEU C N   
6355  C CA  . LEU C 54  ? 3.0334 2.5151 3.0142 0.2408  -0.4583 0.2235  54  LEU C CA  
6356  C C   . LEU C 54  ? 3.0466 2.5383 3.0506 0.2558  -0.4778 0.2153  54  LEU C C   
6357  O O   . LEU C 54  ? 3.0567 2.5358 3.0441 0.2638  -0.4939 0.2221  54  LEU C O   
6358  C CB  . LEU C 54  ? 2.9943 2.5041 2.9699 0.2326  -0.4465 0.2186  54  LEU C CB  
6359  C CG  . LEU C 54  ? 2.9593 2.5063 2.9696 0.2291  -0.4348 0.2021  54  LEU C CG  
6360  C CD1 . LEU C 54  ? 2.9632 2.5233 2.9609 0.2154  -0.4153 0.2026  54  LEU C CD1 
6361  C CD2 . LEU C 54  ? 2.9204 2.4956 2.9543 0.2389  -0.4463 0.1900  54  LEU C CD2 
6362  N N   . ALA C 55  ? 2.8618 2.3768 2.9045 0.2596  -0.4763 0.2005  55  ALA C N   
6363  C CA  . ALA C 55  ? 2.7646 2.2913 2.8337 0.2738  -0.4934 0.1914  55  ALA C CA  
6364  C C   . ALA C 55  ? 2.7005 2.2698 2.8012 0.2744  -0.4885 0.1744  55  ALA C C   
6365  O O   . ALA C 55  ? 2.7382 2.3262 2.8323 0.2731  -0.4889 0.1724  55  ALA C O   
6366  C CB  . ALA C 55  ? 2.8105 2.3189 2.8980 0.2810  -0.4999 0.1901  55  ALA C CB  
6367  N N   . GLN C 56  ? 2.6264 2.2107 2.7610 0.2763  -0.4837 0.1620  56  GLN C N   
6368  C CA  . GLN C 56  ? 2.5526 2.1767 2.7193 0.2780  -0.4799 0.1456  56  GLN C CA  
6369  C C   . GLN C 56  ? 2.5395 2.1854 2.7002 0.2649  -0.4614 0.1428  56  GLN C C   
6370  O O   . GLN C 56  ? 2.5617 2.1951 2.7041 0.2540  -0.4478 0.1498  56  GLN C O   
6371  C CB  . GLN C 56  ? 2.5506 2.1832 2.7530 0.2829  -0.4786 0.1335  56  GLN C CB  
6372  N N   . ILE C 57  ? 2.5775 2.2566 2.7544 0.2662  -0.4610 0.1324  57  ILE C N   
6373  C CA  . ILE C 57  ? 2.5764 2.2801 2.7524 0.2552  -0.4444 0.1278  57  ILE C CA  
6374  C C   . ILE C 57  ? 2.6327 2.3717 2.8471 0.2574  -0.4396 0.1108  57  ILE C C   
6375  O O   . ILE C 57  ? 2.5928 2.3445 2.8300 0.2681  -0.4517 0.1028  57  ILE C O   
6376  C CB  . ILE C 57  ? 2.5315 2.2405 2.6843 0.2530  -0.4475 0.1333  57  ILE C CB  
6377  C CG1 . ILE C 57  ? 2.5862 2.2591 2.7005 0.2526  -0.4545 0.1501  57  ILE C CG1 
6378  C CG2 . ILE C 57  ? 2.4928 2.2241 2.6427 0.2411  -0.4296 0.1297  57  ILE C CG2 
6379  C CD1 . ILE C 57  ? 2.6450 2.3200 2.7309 0.2472  -0.4529 0.1566  57  ILE C CD1 
6380  N N   . PHE C 58  ? 2.9489 2.7040 3.1706 0.2473  -0.4219 0.1054  58  PHE C N   
6381  C CA  . PHE C 58  ? 2.9127 2.6989 3.1693 0.2483  -0.4153 0.0897  58  PHE C CA  
6382  C C   . PHE C 58  ? 2.8906 2.7048 3.1471 0.2389  -0.4016 0.0851  58  PHE C C   
6383  O O   . PHE C 58  ? 2.9115 2.7204 3.1499 0.2279  -0.3884 0.0908  58  PHE C O   
6384  C CB  . PHE C 58  ? 2.9284 2.7063 3.1984 0.2460  -0.4073 0.0859  58  PHE C CB  
6385  C CG  . PHE C 58  ? 2.9557 2.7118 3.2347 0.2566  -0.4208 0.0868  58  PHE C CG  
6386  C CD1 . PHE C 58  ? 2.9104 2.6828 3.2218 0.2670  -0.4286 0.0743  58  PHE C CD1 
6387  C CD2 . PHE C 58  ? 2.9816 2.7008 3.2368 0.2562  -0.4255 0.1002  58  PHE C CD2 
6388  C CE1 . PHE C 58  ? 2.9181 2.6704 3.2386 0.2773  -0.4411 0.0748  58  PHE C CE1 
6389  C CE2 . PHE C 58  ? 2.9906 2.6889 3.2542 0.2663  -0.4382 0.1012  58  PHE C CE2 
6390  C CZ  . PHE C 58  ? 2.9593 2.6741 3.2558 0.2770  -0.4462 0.0884  58  PHE C CZ  
6391  N N   . LEU C 59  ? 2.6872 2.5308 2.9642 0.2433  -0.4049 0.0749  59  LEU C N   
6392  C CA  . LEU C 59  ? 2.6871 2.5604 2.9699 0.2356  -0.3924 0.0685  59  LEU C CA  
6393  C C   . LEU C 59  ? 2.5865 2.4851 2.9030 0.2364  -0.3850 0.0541  59  LEU C C   
6394  O O   . LEU C 59  ? 2.5328 2.4439 2.8743 0.2460  -0.3940 0.0452  59  LEU C O   
6395  C CB  . LEU C 59  ? 2.6950 2.5835 2.9757 0.2392  -0.4009 0.0677  59  LEU C CB  
6396  C CG  . LEU C 59  ? 2.7627 2.6267 3.0131 0.2417  -0.4128 0.0804  59  LEU C CG  
6397  C CD1 . LEU C 59  ? 2.7346 2.6167 2.9886 0.2462  -0.4223 0.0771  59  LEU C CD1 
6398  C CD2 . LEU C 59  ? 2.8165 2.6626 3.0336 0.2307  -0.4020 0.0919  59  LEU C CD2 
6399  N N   . ILE C 60  ? 2.4937 2.4003 2.8111 0.2266  -0.3687 0.0517  60  ILE C N   
6400  C CA  . ILE C 60  ? 2.3612 2.2899 2.7079 0.2264  -0.3606 0.0385  60  ILE C CA  
6401  C C   . ILE C 60  ? 2.3608 2.3196 2.7128 0.2184  -0.3476 0.0326  60  ILE C C   
6402  O O   . ILE C 60  ? 2.5353 2.4915 2.8658 0.2095  -0.3396 0.0398  60  ILE C O   
6403  C CB  . ILE C 60  ? 2.3424 2.2533 2.6893 0.2226  -0.3534 0.0394  60  ILE C CB  
6404  C CG1 . ILE C 60  ? 2.5222 2.4210 2.8435 0.2100  -0.3408 0.0489  60  ILE C CG1 
6405  C CG2 . ILE C 60  ? 2.4011 2.2827 2.7457 0.2313  -0.3668 0.0443  60  ILE C CG2 
6406  C CD1 . ILE C 60  ? 2.5451 2.4275 2.8672 0.2053  -0.3331 0.0496  60  ILE C CD1 
6407  N N   . GLY C 61  ? 2.3414 2.3284 2.7221 0.2217  -0.3454 0.0196  61  GLY C N   
6408  C CA  . GLY C 61  ? 2.3954 2.4126 2.7844 0.2151  -0.3339 0.0129  61  GLY C CA  
6409  C C   . GLY C 61  ? 2.3963 2.4421 2.8167 0.2219  -0.3365 -0.0005 61  GLY C C   
6410  O O   . GLY C 61  ? 2.3318 2.3757 2.7641 0.2322  -0.3495 -0.0031 61  GLY C O   
6411  N N   . PHE C 62  ? 2.7595 2.8321 3.1938 0.2165  -0.3242 -0.0090 62  PHE C N   
6412  C CA  . PHE C 62  ? 2.7191 2.8198 3.1838 0.2222  -0.3246 -0.0223 62  PHE C CA  
6413  C C   . PHE C 62  ? 2.6805 2.8021 3.1510 0.2244  -0.3292 -0.0242 62  PHE C C   
6414  O O   . PHE C 62  ? 2.6385 2.7888 3.1301 0.2247  -0.3242 -0.0342 62  PHE C O   
6415  C CB  . PHE C 62  ? 2.7052 2.8242 3.1822 0.2156  -0.3096 -0.0307 62  PHE C CB  
6416  C CG  . PHE C 62  ? 2.7029 2.8306 3.1647 0.2041  -0.2969 -0.0265 62  PHE C CG  
6417  C CD1 . PHE C 62  ? 2.7392 2.8456 3.1773 0.1964  -0.2912 -0.0169 62  PHE C CD1 
6418  C CD2 . PHE C 62  ? 2.6620 2.8191 3.1339 0.2011  -0.2904 -0.0323 62  PHE C CD2 
6419  C CE1 . PHE C 62  ? 2.7354 2.8500 3.1604 0.1862  -0.2796 -0.0133 62  PHE C CE1 
6420  C CE2 . PHE C 62  ? 2.6578 2.8224 3.1162 0.1909  -0.2790 -0.0285 62  PHE C CE2 
6421  C CZ  . PHE C 62  ? 2.6933 2.8368 3.1285 0.1837  -0.2737 -0.0191 62  PHE C CZ  
6422  N N   . TYR C 63  ? 2.2880 2.3960 2.7401 0.2259  -0.3386 -0.0150 63  TYR C N   
6423  C CA  . TYR C 63  ? 2.1648 2.2890 2.6243 0.2303  -0.3468 -0.0171 63  TYR C CA  
6424  C C   . TYR C 63  ? 2.0634 2.1923 2.5474 0.2424  -0.3594 -0.0245 63  TYR C C   
6425  O O   . TYR C 63  ? 2.0582 2.1757 2.5515 0.2478  -0.3624 -0.0274 63  TYR C O   
6426  C CB  . TYR C 63  ? 2.2644 2.3702 2.6958 0.2286  -0.3540 -0.0051 63  TYR C CB  
6427  C CG  . TYR C 63  ? 2.2705 2.3869 2.6868 0.2187  -0.3440 -0.0015 63  TYR C CG  
6428  C CD1 . TYR C 63  ? 2.1632 2.3105 2.5965 0.2156  -0.3365 -0.0097 63  TYR C CD1 
6429  C CD2 . TYR C 63  ? 2.3849 2.4800 2.7698 0.2126  -0.3421 0.0102  63  TYR C CD2 
6430  C CE1 . TYR C 63  ? 2.1395 2.2957 2.5595 0.2069  -0.3277 -0.0064 63  TYR C CE1 
6431  C CE2 . TYR C 63  ? 2.3364 2.4410 2.7081 0.2039  -0.3330 0.0130  63  TYR C CE2 
6432  C CZ  . TYR C 63  ? 2.1768 2.3118 2.5664 0.2013  -0.3261 0.0047  63  TYR C CZ  
6433  O OH  . TYR C 63  ? 2.1419 2.2859 2.5189 0.1930  -0.3173 0.0076  63  TYR C OH  
6434  N N   . GLU C 64  ? 1.9383 2.0844 2.4337 0.2468  -0.3670 -0.0279 64  GLU C N   
6435  C CA  . GLU C 64  ? 1.7601 1.9114 2.2786 0.2586  -0.3800 -0.0344 64  GLU C CA  
6436  C C   . GLU C 64  ? 1.9215 2.0459 2.4232 0.2651  -0.3964 -0.0249 64  GLU C C   
6437  O O   . GLU C 64  ? 2.1389 2.2552 2.6187 0.2617  -0.4001 -0.0164 64  GLU C O   
6438  C CB  . GLU C 64  ? 1.5743 1.7583 2.1154 0.2603  -0.3802 -0.0433 64  GLU C CB  
6439  C CG  . GLU C 64  ? 1.4368 1.6483 1.9992 0.2563  -0.3658 -0.0542 64  GLU C CG  
6440  C CD  . GLU C 64  ? 1.4203 1.6311 2.0027 0.2625  -0.3650 -0.0625 64  GLU C CD  
6441  O OE1 . GLU C 64  ? 1.4393 1.6359 2.0282 0.2722  -0.3777 -0.0626 64  GLU C OE1 
6442  O OE2 . GLU C 64  ? 1.3456 1.5695 1.9367 0.2577  -0.3518 -0.0691 64  GLU C OE2 
6443  N N   . GLU C 65  ? 1.8271 1.9374 2.3389 0.2745  -0.4063 -0.0265 65  GLU C N   
6444  C CA  . GLU C 65  ? 1.9804 2.0626 2.4760 0.2813  -0.4223 -0.0171 65  GLU C CA  
6445  C C   . GLU C 65  ? 2.1479 2.2398 2.6473 0.2868  -0.4356 -0.0169 65  GLU C C   
6446  O O   . GLU C 65  ? 2.3103 2.3802 2.7891 0.2898  -0.4478 -0.0072 65  GLU C O   
6447  C CB  . GLU C 65  ? 1.9252 1.9927 2.4347 0.2907  -0.4296 -0.0202 65  GLU C CB  
6448  C CG  . GLU C 65  ? 1.9504 1.9845 2.4411 0.2973  -0.4451 -0.0094 65  GLU C CG  
6449  C CD  . GLU C 65  ? 1.9227 1.9409 2.4264 0.3056  -0.4505 -0.0122 65  GLU C CD  
6450  O OE1 . GLU C 65  ? 1.8993 1.9321 2.4257 0.3058  -0.4416 -0.0228 65  GLU C OE1 
6451  O OE2 . GLU C 65  ? 1.9327 1.9232 2.4235 0.3119  -0.4637 -0.0039 65  GLU C OE2 
6452  N N   . ARG C 66  ? 2.0596 2.1836 2.5845 0.2880  -0.4335 -0.0272 66  ARG C N   
6453  C CA  . ARG C 66  ? 2.1157 2.2510 2.6472 0.2930  -0.4461 -0.0281 66  ARG C CA  
6454  C C   . ARG C 66  ? 2.3338 2.4596 2.8348 0.2859  -0.4471 -0.0177 66  ARG C C   
6455  O O   . ARG C 66  ? 2.3713 2.4898 2.8649 0.2909  -0.4617 -0.0134 66  ARG C O   
6456  C CB  . ARG C 66  ? 1.8095 1.9824 2.3731 0.2932  -0.4404 -0.0409 66  ARG C CB  
6457  C CG  . ARG C 66  ? 1.6452 1.8308 2.2388 0.2989  -0.4362 -0.0522 66  ARG C CG  
6458  C CD  . ARG C 66  ? 1.3721 1.5942 1.9904 0.2952  -0.4249 -0.0634 66  ARG C CD  
6459  N NE  . ARG C 66  ? 1.3774 1.6052 1.9792 0.2826  -0.4089 -0.0604 66  ARG C NE  
6460  C CZ  . ARG C 66  ? 1.2878 1.5445 1.9041 0.2768  -0.3968 -0.0677 66  ARG C CZ  
6461  N NH1 . ARG C 66  ? 1.2480 1.5310 1.8955 0.2822  -0.3982 -0.0786 66  ARG C NH1 
6462  N NH2 . ARG C 66  ? 1.2465 1.5058 1.8462 0.2657  -0.3832 -0.0641 66  ARG C NH2 
6463  N N   . GLU C 67  ? 2.7042 2.8300 3.1874 0.2745  -0.4321 -0.0140 67  GLU C N   
6464  C CA  . GLU C 67  ? 2.7345 2.8518 3.1888 0.2675  -0.4317 -0.0048 67  GLU C CA  
6465  C C   . GLU C 67  ? 2.8203 2.9013 3.2428 0.2687  -0.4399 0.0080  67  GLU C C   
6466  O O   . GLU C 67  ? 2.7997 2.8701 3.2019 0.2688  -0.4489 0.0152  67  GLU C O   
6467  C CB  . GLU C 67  ? 2.7247 2.8538 3.1712 0.2553  -0.4127 -0.0051 67  GLU C CB  
6468  C CG  . GLU C 67  ? 2.7396 2.9045 3.2119 0.2528  -0.4049 -0.0158 67  GLU C CG  
6469  C CD  . GLU C 67  ? 2.7553 2.9308 3.2208 0.2413  -0.3863 -0.0162 67  GLU C CD  
6470  O OE1 . GLU C 67  ? 2.6799 2.8484 3.1437 0.2383  -0.3766 -0.0163 67  GLU C OE1 
6471  O OE2 . GLU C 67  ? 2.7648 2.9554 3.2271 0.2354  -0.3815 -0.0164 67  GLU C OE2 
6472  N N   . PHE C 68  ? 3.2043 3.2655 3.6216 0.2694  -0.4369 0.0110  68  PHE C N   
6473  C CA  . PHE C 68  ? 3.2490 3.2747 3.6349 0.2694  -0.4426 0.0239  68  PHE C CA  
6474  C C   . PHE C 68  ? 3.2558 3.2641 3.6435 0.2814  -0.4623 0.0268  68  PHE C C   
6475  O O   . PHE C 68  ? 3.2870 3.2678 3.6464 0.2822  -0.4705 0.0382  68  PHE C O   
6476  C CB  . PHE C 68  ? 3.2748 3.2857 3.6532 0.2639  -0.4302 0.0266  68  PHE C CB  
6477  C CG  . PHE C 68  ? 3.2769 3.2961 3.6431 0.2512  -0.4122 0.0280  68  PHE C CG  
6478  C CD1 . PHE C 68  ? 3.3158 3.3122 3.6487 0.2437  -0.4071 0.0396  68  PHE C CD1 
6479  C CD2 . PHE C 68  ? 3.2392 3.2893 3.6270 0.2469  -0.4005 0.0177  68  PHE C CD2 
6480  C CE1 . PHE C 68  ? 3.3198 3.3244 3.6424 0.2324  -0.3907 0.0407  68  PHE C CE1 
6481  C CE2 . PHE C 68  ? 3.2406 3.2984 3.6175 0.2356  -0.3845 0.0191  68  PHE C CE2 
6482  C CZ  . PHE C 68  ? 3.2824 3.3176 3.6272 0.2285  -0.3798 0.0304  68  PHE C CZ  
6483  N N   . ALA C 69  ? 2.7861 2.8095 3.2060 0.2908  -0.4698 0.0168  69  ALA C N   
6484  C CA  . ALA C 69  ? 2.7105 2.7181 3.1345 0.3030  -0.4890 0.0190  69  ALA C CA  
6485  C C   . ALA C 69  ? 2.6094 2.6110 3.0161 0.3055  -0.5031 0.0255  69  ALA C C   
6486  O O   . ALA C 69  ? 2.6307 2.6061 3.0204 0.3117  -0.5172 0.0341  69  ALA C O   
6487  C CB  . ALA C 69  ? 2.6365 2.6664 3.1009 0.3124  -0.4935 0.0057  69  ALA C CB  
6488  N N   . LEU C 70  ? 2.4757 2.5009 2.8863 0.3008  -0.4997 0.0215  70  LEU C N   
6489  C CA  . LEU C 70  ? 2.3392 2.3603 2.7341 0.3027  -0.5129 0.0267  70  LEU C CA  
6490  C C   . LEU C 70  ? 2.3103 2.3033 2.6622 0.2959  -0.5113 0.0404  70  LEU C C   
6491  O O   . LEU C 70  ? 2.2750 2.2505 2.6071 0.3002  -0.5259 0.0479  70  LEU C O   
6492  C CB  . LEU C 70  ? 2.2055 2.2596 2.6170 0.2989  -0.5090 0.0182  70  LEU C CB  
6493  C CG  . LEU C 70  ? 2.0895 2.1719 2.5416 0.3070  -0.5158 0.0055  70  LEU C CG  
6494  C CD1 . LEU C 70  ? 2.1718 2.2700 2.6522 0.3075  -0.5039 -0.0041 70  LEU C CD1 
6495  C CD2 . LEU C 70  ? 1.9358 2.0445 2.3962 0.3029  -0.5150 0.0004  70  LEU C CD2 
6496  N N   . TYR C 71  ? 2.3584 2.3471 2.6953 0.2854  -0.4938 0.0438  71  TYR C N   
6497  C CA  . TYR C 71  ? 2.2822 2.2462 2.5790 0.2782  -0.4903 0.0564  71  TYR C CA  
6498  C C   . TYR C 71  ? 2.3295 2.2579 2.6060 0.2822  -0.4970 0.0668  71  TYR C C   
6499  O O   . TYR C 71  ? 2.2958 2.2006 2.5419 0.2827  -0.5057 0.0775  71  TYR C O   
6500  C CB  . TYR C 71  ? 2.1910 2.1642 2.4806 0.2656  -0.4690 0.0559  71  TYR C CB  
6501  C CG  . TYR C 71  ? 2.0486 1.9959 2.2986 0.2577  -0.4627 0.0686  71  TYR C CG  
6502  C CD1 . TYR C 71  ? 1.9894 1.9249 2.2117 0.2569  -0.4707 0.0763  71  TYR C CD1 
6503  C CD2 . TYR C 71  ? 2.0363 1.9718 2.2770 0.2508  -0.4485 0.0725  71  TYR C CD2 
6504  C CE1 . TYR C 71  ? 1.9444 1.8568 2.1304 0.2497  -0.4642 0.0876  71  TYR C CE1 
6505  C CE2 . TYR C 71  ? 1.9894 1.9023 2.1950 0.2433  -0.4420 0.0839  71  TYR C CE2 
6506  C CZ  . TYR C 71  ? 2.0077 1.9090 2.1858 0.2428  -0.4497 0.0914  71  TYR C CZ  
6507  O OH  . TYR C 71  ? 2.0448 1.9239 2.1878 0.2354  -0.4426 0.1026  71  TYR C OH  
6508  N N   . VAL C 72  ? 2.4634 2.3873 2.7558 0.2847  -0.4929 0.0639  72  VAL C N   
6509  C CA  . VAL C 72  ? 2.5097 2.3993 2.7842 0.2880  -0.4983 0.0737  72  VAL C CA  
6510  C C   . VAL C 72  ? 2.4971 2.3702 2.7666 0.2996  -0.5204 0.0784  72  VAL C C   
6511  O O   . VAL C 72  ? 2.5258 2.3670 2.7674 0.3009  -0.5272 0.0905  72  VAL C O   
6512  C CB  . VAL C 72  ? 2.5033 2.3946 2.8010 0.2892  -0.4903 0.0675  72  VAL C CB  
6513  C CG1 . VAL C 72  ? 2.5046 2.3606 2.7876 0.2937  -0.4975 0.0769  72  VAL C CG1 
6514  C CG2 . VAL C 72  ? 2.4741 2.3777 2.7716 0.2770  -0.4687 0.0646  72  VAL C CG2 
6515  N N   . SER C 73  ? 2.4138 2.3081 2.7094 0.3079  -0.5320 0.0694  73  SER C N   
6516  C CA  . SER C 73  ? 2.3107 2.1915 2.6044 0.3196  -0.5539 0.0730  73  SER C CA  
6517  C C   . SER C 73  ? 2.3578 2.2203 2.6144 0.3175  -0.5624 0.0844  73  SER C C   
6518  O O   . SER C 73  ? 2.3449 2.1853 2.5883 0.3257  -0.5795 0.0917  73  SER C O   
6519  C CB  . SER C 73  ? 2.1858 2.0968 2.5169 0.3279  -0.5632 0.0601  73  SER C CB  
6520  O OG  . SER C 73  ? 2.1489 2.0764 2.5141 0.3306  -0.5559 0.0493  73  SER C OG  
6521  N N   . SER C 74  ? 2.4724 2.3432 2.7115 0.3069  -0.5509 0.0860  74  SER C N   
6522  C CA  . SER C 74  ? 2.5301 2.3858 2.7343 0.3045  -0.5580 0.0956  74  SER C CA  
6523  C C   . SER C 74  ? 2.5941 2.4176 2.7587 0.2976  -0.5507 0.1094  74  SER C C   
6524  O O   . SER C 74  ? 2.6588 2.4608 2.7917 0.2986  -0.5604 0.1195  74  SER C O   
6525  C CB  . SER C 74  ? 2.5533 2.4355 2.7597 0.2973  -0.5507 0.0896  74  SER C CB  
6526  O OG  . SER C 74  ? 2.4894 2.4025 2.7332 0.3027  -0.5561 0.0767  74  SER C OG  
6527  N N   . ILE C 75  ? 2.4416 2.2615 2.6073 0.2906  -0.5338 0.1100  75  ILE C N   
6528  C CA  . ILE C 75  ? 2.4464 2.2371 2.5760 0.2832  -0.5253 0.1229  75  ILE C CA  
6529  C C   . ILE C 75  ? 2.5952 2.3520 2.7092 0.2911  -0.5393 0.1332  75  ILE C C   
6530  O O   . ILE C 75  ? 2.7125 2.4430 2.7903 0.2896  -0.5440 0.1456  75  ILE C O   
6531  C CB  . ILE C 75  ? 2.2886 2.0859 2.4266 0.2737  -0.5040 0.1200  75  ILE C CB  
6532  C CG1 . ILE C 75  ? 2.1892 2.0241 2.3542 0.2690  -0.4927 0.1071  75  ILE C CG1 
6533  C CG2 . ILE C 75  ? 2.1892 1.9644 2.2899 0.2633  -0.4920 0.1320  75  ILE C CG2 
6534  C CD1 . ILE C 75  ? 2.1743 2.0184 2.3537 0.2617  -0.4740 0.1023  75  ILE C CD1 
6535  N N   . SER C 76  ? 2.4973 2.2539 2.6382 0.2996  -0.5459 0.1283  76  SER C N   
6536  C CA  . SER C 76  ? 2.6044 2.3287 2.7335 0.3076  -0.5591 0.1376  76  SER C CA  
6537  C C   . SER C 76  ? 2.5676 2.2792 2.6803 0.3164  -0.5805 0.1437  76  SER C C   
6538  O O   . SER C 76  ? 2.5864 2.2670 2.6794 0.3217  -0.5917 0.1545  76  SER C O   
6539  C CB  . SER C 76  ? 2.6196 2.3500 2.7849 0.3157  -0.5622 0.1291  76  SER C CB  
6540  O OG  . SER C 76  ? 2.6594 2.3988 2.8379 0.3077  -0.5431 0.1239  76  SER C OG  
6541  N N   . ASN C 77  ? 2.5756 2.3103 2.6959 0.3180  -0.5868 0.1371  77  ASN C N   
6542  C CA  . ASN C 77  ? 2.6119 2.3350 2.7134 0.3250  -0.6066 0.1430  77  ASN C CA  
6543  C C   . ASN C 77  ? 2.7723 2.4727 2.8268 0.3173  -0.6034 0.1560  77  ASN C C   
6544  O O   . ASN C 77  ? 2.7440 2.4253 2.7749 0.3230  -0.6198 0.1642  77  ASN C O   
6545  C CB  . ASN C 77  ? 2.4645 2.2204 2.5911 0.3289  -0.6144 0.1311  77  ASN C CB  
6546  C CG  . ASN C 77  ? 2.3109 2.0888 2.4836 0.3378  -0.6197 0.1184  77  ASN C CG  
6547  O OD1 . ASN C 77  ? 2.2737 2.0373 2.4568 0.3454  -0.6261 0.1199  77  ASN C OD1 
6548  N ND2 . ASN C 77  ? 2.1910 2.0038 2.3917 0.3370  -0.6169 0.1058  77  ASN C ND2 
6549  N N   . GLU C 78  ? 3.1286 2.8310 3.1691 0.3047  -0.5829 0.1579  78  GLU C N   
6550  C CA  . GLU C 78  ? 3.1612 2.8443 3.1581 0.2966  -0.5775 0.1694  78  GLU C CA  
6551  C C   . GLU C 78  ? 3.1961 2.8446 3.1659 0.2930  -0.5714 0.1828  78  GLU C C   
6552  O O   . GLU C 78  ? 3.2265 2.8461 3.1626 0.2953  -0.5813 0.1951  78  GLU C O   
6553  C CB  . GLU C 78  ? 3.1448 2.8514 3.1419 0.2848  -0.5589 0.1635  78  GLU C CB  
6554  C CG  . GLU C 78  ? 3.1091 2.8473 3.1267 0.2870  -0.5646 0.1520  78  GLU C CG  
6555  C CD  . GLU C 78  ? 3.0960 2.8539 3.1095 0.2753  -0.5467 0.1478  78  GLU C CD  
6556  O OE1 . GLU C 78  ? 3.1074 2.8559 3.1044 0.2659  -0.5297 0.1531  78  GLU C OE1 
6557  O OE2 . GLU C 78  ? 3.0915 2.8741 3.1190 0.2756  -0.5498 0.1391  78  GLU C OE2 
6558  N N   . LEU C 79  ? 2.9322 2.5831 2.9158 0.2871  -0.5552 0.1805  79  LEU C N   
6559  C CA  . LEU C 79  ? 2.9392 2.5594 2.8989 0.2820  -0.5468 0.1926  79  LEU C CA  
6560  C C   . LEU C 79  ? 2.9149 2.5171 2.8888 0.2906  -0.5560 0.1948  79  LEU C C   
6561  O O   . LEU C 79  ? 2.8842 2.4574 2.8375 0.2874  -0.5517 0.2059  79  LEU C O   
6562  C CB  . LEU C 79  ? 3.0253 2.6566 2.9880 0.2690  -0.5223 0.1899  79  LEU C CB  
6563  C CG  . LEU C 79  ? 3.0704 2.7087 3.0087 0.2580  -0.5093 0.1923  79  LEU C CG  
6564  C CD1 . LEU C 79  ? 3.0682 2.6782 2.9623 0.2580  -0.5175 0.2061  79  LEU C CD1 
6565  C CD2 . LEU C 79  ? 3.0703 2.7448 3.0305 0.2579  -0.5086 0.1793  79  LEU C CD2 
6566  N N   . LYS C 80  ? 2.8882 2.5066 2.8968 0.3012  -0.5683 0.1845  80  LYS C N   
6567  C CA  . LYS C 80  ? 2.8595 2.4621 2.8842 0.3109  -0.5788 0.1854  80  LYS C CA  
6568  C C   . LYS C 80  ? 3.0250 2.6205 3.0584 0.3043  -0.5623 0.1855  80  LYS C C   
6569  O O   . LYS C 80  ? 2.9396 2.5038 2.9563 0.3044  -0.5632 0.1961  80  LYS C O   
6570  C CB  . LYS C 80  ? 2.6294 2.1964 2.6238 0.3181  -0.5966 0.1997  80  LYS C CB  
6571  C CG  . LYS C 80  ? 2.5454 2.1172 2.5301 0.3254  -0.6150 0.2000  80  LYS C CG  
6572  C CD  . LYS C 80  ? 2.5371 2.1016 2.4818 0.3165  -0.6095 0.2085  80  LYS C CD  
6573  C CE  . LYS C 80  ? 2.5210 2.0495 2.4271 0.3097  -0.6017 0.2244  80  LYS C CE  
6574  N NZ  . LYS C 80  ? 2.4336 1.9580 2.3029 0.2996  -0.5924 0.2312  80  LYS C NZ  
6575  N N   . ILE C 81  ? 3.6572 3.2823 3.7172 0.2984  -0.5471 0.1733  81  ILE C N   
6576  C CA  . ILE C 81  ? 3.6639 3.2871 3.7360 0.2919  -0.5311 0.1710  81  ILE C CA  
6577  C C   . ILE C 81  ? 3.6238 3.2769 3.7413 0.2967  -0.5294 0.1545  81  ILE C C   
6578  O O   . ILE C 81  ? 3.5876 3.2723 3.7236 0.2969  -0.5283 0.1439  81  ILE C O   
6579  C CB  . ILE C 81  ? 3.6760 3.3026 3.7286 0.2769  -0.5101 0.1744  81  ILE C CB  
6580  C CG1 . ILE C 81  ? 3.6529 3.3057 3.7025 0.2730  -0.5071 0.1691  81  ILE C CG1 
6581  C CG2 . ILE C 81  ? 3.7241 3.3137 3.7359 0.2714  -0.5077 0.1914  81  ILE C CG2 
6582  C CD1 . ILE C 81  ? 3.6659 3.3211 3.6942 0.2590  -0.4878 0.1731  81  ILE C CD1 
6583  N N   . PRO C 82  ? 2.9872 2.6314 3.1237 0.3006  -0.5292 0.1518  82  PRO C N   
6584  C CA  . PRO C 82  ? 2.7833 2.4557 2.9629 0.3056  -0.5275 0.1357  82  PRO C CA  
6585  C C   . PRO C 82  ? 2.6591 2.3590 2.8522 0.2947  -0.5069 0.1263  82  PRO C C   
6586  O O   . PRO C 82  ? 2.5613 2.2546 2.7556 0.2876  -0.4934 0.1266  82  PRO C O   
6587  C CB  . PRO C 82  ? 2.6618 2.3111 2.8515 0.3116  -0.5319 0.1373  82  PRO C CB  
6588  C CG  . PRO C 82  ? 2.6821 2.2920 2.8360 0.3132  -0.5419 0.1544  82  PRO C CG  
6589  C CD  . PRO C 82  ? 2.8590 2.4657 2.9786 0.3018  -0.5324 0.1634  82  PRO C CD  
6590  N N   . VAL C 83  ? 2.5811 2.3117 2.7845 0.2932  -0.5047 0.1182  83  VAL C N   
6591  C CA  . VAL C 83  ? 2.5200 2.2792 2.7375 0.2836  -0.4864 0.1088  83  VAL C CA  
6592  C C   . VAL C 83  ? 2.4154 2.2023 2.6752 0.2902  -0.4870 0.0930  83  VAL C C   
6593  O O   . VAL C 83  ? 2.3930 2.1886 2.6709 0.3011  -0.5018 0.0877  83  VAL C O   
6594  C CB  . VAL C 83  ? 2.5897 2.3654 2.7924 0.2774  -0.4826 0.1097  83  VAL C CB  
6595  C CG1 . VAL C 83  ? 2.5195 2.3213 2.7331 0.2666  -0.4628 0.1019  83  VAL C CG1 
6596  C CG2 . VAL C 83  ? 2.6917 2.4389 2.8520 0.2729  -0.4848 0.1252  83  VAL C CG2 
6597  N N   . ARG C 84  ? 2.4105 2.2116 2.6864 0.2835  -0.4710 0.0854  84  ARG C N   
6598  C CA  . ARG C 84  ? 2.3486 2.1757 2.6634 0.2887  -0.4694 0.0702  84  ARG C CA  
6599  C C   . ARG C 84  ? 2.3614 2.2152 2.6866 0.2782  -0.4503 0.0620  84  ARG C C   
6600  O O   . ARG C 84  ? 2.4413 2.2859 2.7486 0.2677  -0.4369 0.0676  84  ARG C O   
6601  C CB  . ARG C 84  ? 2.3525 2.1619 2.6810 0.2951  -0.4732 0.0686  84  ARG C CB  
6602  C CG  . ARG C 84  ? 2.3213 2.1564 2.6897 0.3010  -0.4714 0.0524  84  ARG C CG  
6603  C CD  . ARG C 84  ? 2.3255 2.1406 2.7053 0.3070  -0.4750 0.0511  84  ARG C CD  
6604  N NE  . ARG C 84  ? 2.2942 2.0846 2.6673 0.3182  -0.4942 0.0585  84  ARG C NE  
6605  C CZ  . ARG C 84  ? 2.2259 2.0260 2.6230 0.3310  -0.5084 0.0512  84  ARG C CZ  
6606  N NH1 . ARG C 84  ? 2.2401 2.0745 2.6692 0.3339  -0.5050 0.0363  84  ARG C NH1 
6607  N NH2 . ARG C 84  ? 2.1905 1.9664 2.5795 0.3409  -0.5260 0.0589  84  ARG C NH2 
6608  N N   . TYR C 85  ? 2.3182 2.2050 2.6722 0.2812  -0.4490 0.0490  85  TYR C N   
6609  C CA  . TYR C 85  ? 2.3082 2.2225 2.6756 0.2726  -0.4318 0.0400  85  TYR C CA  
6610  C C   . TYR C 85  ? 2.2394 2.1639 2.6369 0.2762  -0.4273 0.0284  85  TYR C C   
6611  O O   . TYR C 85  ? 2.1784 2.1077 2.5988 0.2872  -0.4383 0.0214  85  TYR C O   
6612  C CB  . TYR C 85  ? 2.2950 2.2404 2.6729 0.2721  -0.4318 0.0335  85  TYR C CB  
6613  C CG  . TYR C 85  ? 2.2738 2.2485 2.6676 0.2641  -0.4148 0.0238  85  TYR C CG  
6614  C CD1 . TYR C 85  ? 2.3702 2.3455 2.7448 0.2520  -0.4003 0.0286  85  TYR C CD1 
6615  C CD2 . TYR C 85  ? 2.1593 2.1610 2.5872 0.2689  -0.4133 0.0099  85  TYR C CD2 
6616  C CE1 . TYR C 85  ? 2.3750 2.3766 2.7637 0.2449  -0.3854 0.0201  85  TYR C CE1 
6617  C CE2 . TYR C 85  ? 2.1378 2.1657 2.5790 0.2617  -0.3980 0.0015  85  TYR C CE2 
6618  C CZ  . TYR C 85  ? 2.1929 2.2204 2.6142 0.2498  -0.3845 0.0067  85  TYR C CZ  
6619  O OH  . TYR C 85  ? 2.1945 2.2478 2.6288 0.2429  -0.3698 -0.0014 85  TYR C OH  
6620  N N   . LEU C 86  ? 2.2336 2.1617 2.6312 0.2670  -0.4114 0.0260  86  LEU C N   
6621  C CA  . LEU C 86  ? 2.1665 2.1058 2.5911 0.2688  -0.4049 0.0143  86  LEU C CA  
6622  C C   . LEU C 86  ? 2.1456 2.1151 2.5804 0.2600  -0.3887 0.0059  86  LEU C C   
6623  O O   . LEU C 86  ? 2.1932 2.1608 2.6086 0.2491  -0.3774 0.0118  86  LEU C O   
6624  C CB  . LEU C 86  ? 2.2465 2.1566 2.6617 0.2667  -0.4021 0.0196  86  LEU C CB  
6625  C CG  . LEU C 86  ? 2.3194 2.1955 2.7217 0.2747  -0.4173 0.0294  86  LEU C CG  
6626  C CD1 . LEU C 86  ? 2.3748 2.2238 2.7693 0.2711  -0.4125 0.0340  86  LEU C CD1 
6627  C CD2 . LEU C 86  ? 2.2482 2.1313 2.6756 0.2889  -0.4324 0.0216  86  LEU C CD2 
6628  N N   . LYS C 87  ? 2.0153 2.0127 2.4804 0.2647  -0.3875 -0.0077 87  LYS C N   
6629  C CA  . LYS C 87  ? 1.9816 2.0092 2.4584 0.2572  -0.3727 -0.0164 87  LYS C CA  
6630  C C   . LYS C 87  ? 1.9059 1.9331 2.3937 0.2540  -0.3622 -0.0231 87  LYS C C   
6631  O O   . LYS C 87  ? 1.8814 1.9131 2.3927 0.2617  -0.3657 -0.0327 87  LYS C O   
6632  C CB  . LYS C 87  ? 1.9175 1.9765 2.4203 0.2634  -0.3764 -0.0273 87  LYS C CB  
6633  C CG  . LYS C 87  ? 1.9195 2.0098 2.4390 0.2573  -0.3616 -0.0379 87  LYS C CG  
6634  C CD  . LYS C 87  ? 1.7959 1.9166 2.3415 0.2635  -0.3651 -0.0485 87  LYS C CD  
6635  C CE  . LYS C 87  ? 1.7336 1.8834 2.2977 0.2586  -0.3506 -0.0598 87  LYS C CE  
6636  N NZ  . LYS C 87  ? 1.8736 2.0251 2.4188 0.2459  -0.3366 -0.0549 87  LYS C NZ  
6637  N N   . GLU C 88  ? 1.9795 2.0012 2.4507 0.2427  -0.3494 -0.0184 88  GLU C N   
6638  C CA  . GLU C 88  ? 1.9607 1.9846 2.4422 0.2384  -0.3385 -0.0253 88  GLU C CA  
6639  C C   . GLU C 88  ? 1.9877 2.0476 2.4944 0.2383  -0.3305 -0.0394 88  GLU C C   
6640  O O   . GLU C 88  ? 1.9973 2.0771 2.5002 0.2309  -0.3212 -0.0399 88  GLU C O   
6641  C CB  . GLU C 88  ? 1.9313 1.9416 2.3892 0.2262  -0.3271 -0.0166 88  GLU C CB  
6642  C CG  . GLU C 88  ? 1.9722 1.9946 2.4134 0.2175  -0.3198 -0.0109 88  GLU C CG  
6643  C CD  . GLU C 88  ? 1.9115 1.9253 2.3349 0.2054  -0.3066 -0.0050 88  GLU C CD  
6644  O OE1 . GLU C 88  ? 1.8565 1.8610 2.2850 0.2031  -0.3015 -0.0077 88  GLU C OE1 
6645  O OE2 . GLU C 88  ? 1.9387 1.9552 2.3438 0.1983  -0.3013 0.0021  88  GLU C OE2 
6646  N N   . ASP C 89  ? 2.0382 2.1063 2.5706 0.2468  -0.3342 -0.0507 89  ASP C N   
6647  C CA  . ASP C 89  ? 2.0059 2.1079 2.5626 0.2473  -0.3267 -0.0645 89  ASP C CA  
6648  C C   . ASP C 89  ? 1.9783 2.0904 2.5318 0.2364  -0.3106 -0.0676 89  ASP C C   
6649  O O   . ASP C 89  ? 1.9349 2.0749 2.4963 0.2321  -0.3018 -0.0736 89  ASP C O   
6650  C CB  . ASP C 89  ? 2.0071 2.1129 2.5908 0.2585  -0.3333 -0.0760 89  ASP C CB  
6651  C CG  . ASP C 89  ? 1.9982 2.0857 2.5828 0.2695  -0.3502 -0.0714 89  ASP C CG  
6652  O OD1 . ASP C 89  ? 2.0596 2.1181 2.6364 0.2724  -0.3562 -0.0662 89  ASP C OD1 
6653  O OD2 . ASP C 89  ? 1.9308 2.0326 2.5236 0.2751  -0.3577 -0.0726 89  ASP C OD2 
6654  N N   . LYS C 90  ? 1.9633 2.0531 2.5057 0.2316  -0.3067 -0.0636 90  LYS C N   
6655  C CA  . LYS C 90  ? 1.9676 2.0644 2.5054 0.2208  -0.2921 -0.0656 90  LYS C CA  
6656  C C   . LYS C 90  ? 2.0428 2.1220 2.5515 0.2111  -0.2881 -0.0516 90  LYS C C   
6657  O O   . LYS C 90  ? 2.0595 2.1102 2.5544 0.2093  -0.2901 -0.0438 90  LYS C O   
6658  C CB  . LYS C 90  ? 1.9834 2.0700 2.5322 0.2219  -0.2896 -0.0729 90  LYS C CB  
6659  N N   . PRO C 91  ? 1.9729 2.0678 2.4717 0.2048  -0.2822 -0.0478 91  PRO C N   
6660  C CA  . PRO C 91  ? 1.9732 2.0518 2.4443 0.1959  -0.2781 -0.0346 91  PRO C CA  
6661  C C   . PRO C 91  ? 1.9777 2.0513 2.4431 0.1861  -0.2659 -0.0345 91  PRO C C   
6662  O O   . PRO C 91  ? 1.9255 2.0212 2.4032 0.1820  -0.2562 -0.0433 91  PRO C O   
6663  C CB  . PRO C 91  ? 2.0171 2.1181 2.4841 0.1927  -0.2749 -0.0334 91  PRO C CB  
6664  C CG  . PRO C 91  ? 2.0279 2.1519 2.5188 0.2015  -0.2807 -0.0438 91  PRO C CG  
6665  C CD  . PRO C 91  ? 1.9435 2.0704 2.4556 0.2060  -0.2798 -0.0548 91  PRO C CD  
6666  N N   . HIS C 92  ? 2.0052 2.0497 2.4520 0.1824  -0.2666 -0.0243 92  HIS C N   
6667  C CA  . HIS C 92  ? 2.0724 2.1096 2.5130 0.1727  -0.2556 -0.0231 92  HIS C CA  
6668  C C   . HIS C 92  ? 2.1309 2.1547 2.5446 0.1636  -0.2505 -0.0098 92  HIS C C   
6669  O O   . HIS C 92  ? 2.2402 2.2399 2.6407 0.1587  -0.2482 -0.0025 92  HIS C O   
6670  C CB  . HIS C 92  ? 2.1420 2.1558 2.5881 0.1758  -0.2596 -0.0245 92  HIS C CB  
6671  C CG  . HIS C 92  ? 2.1181 2.1409 2.5895 0.1861  -0.2664 -0.0369 92  HIS C CG  
6672  N ND1 . HIS C 92  ? 2.1188 2.1203 2.5943 0.1953  -0.2783 -0.0359 92  HIS C ND1 
6673  C CD2 . HIS C 92  ? 2.0564 2.1073 2.5503 0.1888  -0.2628 -0.0506 92  HIS C CD2 
6674  C CE1 . HIS C 92  ? 2.0980 2.1145 2.5982 0.2034  -0.2816 -0.0488 92  HIS C CE1 
6675  N NE2 . HIS C 92  ? 2.0519 2.0986 2.5634 0.1996  -0.2721 -0.0579 92  HIS C NE2 
6676  N N   . GLY C 93  ? 2.1301 2.1691 2.5356 0.1613  -0.2483 -0.0067 93  GLY C N   
6677  C CA  . GLY C 93  ? 2.2144 2.2424 2.5944 0.1532  -0.2433 0.0053  93  GLY C CA  
6678  C C   . GLY C 93  ? 2.3260 2.3220 2.6856 0.1559  -0.2523 0.0175  93  GLY C C   
6679  O O   . GLY C 93  ? 2.3428 2.3352 2.6979 0.1630  -0.2630 0.0207  93  GLY C O   
6680  N N   . SER C 94  ? 2.4265 2.3989 2.7733 0.1500  -0.2482 0.0245  94  SER C N   
6681  C CA  . SER C 94  ? 2.5155 2.4556 2.8406 0.1514  -0.2555 0.0372  94  SER C CA  
6682  C C   . SER C 94  ? 2.5579 2.4743 2.8884 0.1542  -0.2598 0.0373  94  SER C C   
6683  O O   . SER C 94  ? 2.5647 2.4644 2.8946 0.1630  -0.2724 0.0399  94  SER C O   
6684  C CB  . SER C 94  ? 2.7302 2.6605 3.0296 0.1410  -0.2463 0.0485  94  SER C CB  
6685  O OG  . SER C 94  ? 2.6479 2.5988 2.9419 0.1388  -0.2427 0.0485  94  SER C OG  
6686  N N   . ALA C 95  ? 2.7064 2.6209 3.0426 0.1469  -0.2500 0.0343  95  ALA C N   
6687  C CA  . ALA C 95  ? 2.7139 2.6033 3.0532 0.1483  -0.2533 0.0354  95  ALA C CA  
6688  C C   . ALA C 95  ? 2.5353 2.4292 2.8985 0.1596  -0.2633 0.0246  95  ALA C C   
6689  O O   . ALA C 95  ? 2.5565 2.4271 2.9181 0.1667  -0.2740 0.0283  95  ALA C O   
6690  C CB  . ALA C 95  ? 2.8502 2.7398 3.1926 0.1377  -0.2404 0.0332  95  ALA C CB  
6691  N N   . GLY C 96  ? 2.5097 2.4333 2.8953 0.1615  -0.2597 0.0110  96  GLY C N   
6692  C CA  . GLY C 96  ? 2.4403 2.3709 2.8493 0.1725  -0.2685 0.0000  96  GLY C CA  
6693  C C   . GLY C 96  ? 2.3909 2.3219 2.7998 0.1831  -0.2817 0.0020  96  GLY C C   
6694  O O   . GLY C 96  ? 2.3690 2.2968 2.7938 0.1933  -0.2914 -0.0041 96  GLY C O   
6695  N N   . ALA C 97  ? 2.3404 2.2754 2.7322 0.1810  -0.2822 0.0100  97  ALA C N   
6696  C CA  . ALA C 97  ? 2.3564 2.2918 2.7471 0.1906  -0.2952 0.0123  97  ALA C CA  
6697  C C   . ALA C 97  ? 2.4963 2.3988 2.8776 0.1976  -0.3079 0.0205  97  ALA C C   
6698  O O   . ALA C 97  ? 2.4345 2.3367 2.8285 0.2087  -0.3202 0.0166  97  ALA C O   
6699  C CB  . ALA C 97  ? 2.3663 2.3099 2.7380 0.1859  -0.2927 0.0200  97  ALA C CB  
6700  N N   . LEU C 98  ? 2.7973 2.6720 3.1567 0.1912  -0.3052 0.0322  98  LEU C N   
6701  C CA  . LEU C 98  ? 2.8268 2.6681 3.1738 0.1969  -0.3169 0.0418  98  LEU C CA  
6702  C C   . LEU C 98  ? 2.8444 2.6693 3.2056 0.2002  -0.3191 0.0373  98  LEU C C   
6703  O O   . LEU C 98  ? 2.8558 2.6583 3.2157 0.2087  -0.3316 0.0414  98  LEU C O   
6704  C CB  . LEU C 98  ? 2.8657 2.6833 3.1799 0.1886  -0.3132 0.0578  98  LEU C CB  
6705  C CG  . LEU C 98  ? 2.8985 2.6998 3.2046 0.1780  -0.3018 0.0621  98  LEU C CG  
6706  C CD1 . LEU C 98  ? 2.9460 2.7100 3.2255 0.1763  -0.3062 0.0778  98  LEU C CD1 
6707  C CD2 . LEU C 98  ? 2.8916 2.7133 3.1935 0.1663  -0.2860 0.0606  98  LEU C CD2 
6708  N N   . TYR C 99  ? 2.6472 2.4824 3.0219 0.1939  -0.3078 0.0289  99  TYR C N   
6709  C CA  . TYR C 99  ? 2.6123 2.4351 3.0040 0.1979  -0.3105 0.0222  99  TYR C CA  
6710  C C   . TYR C 99  ? 2.5315 2.3683 2.9486 0.2110  -0.3208 0.0104  99  TYR C C   
6711  O O   . TYR C 99  ? 2.4889 2.3074 2.9149 0.2192  -0.3302 0.0088  99  TYR C O   
6712  C CB  . TYR C 99  ? 2.6058 2.4392 3.0074 0.1884  -0.2963 0.0144  99  TYR C CB  
6713  C CG  . TYR C 99  ? 2.6368 2.4594 3.0575 0.1926  -0.2989 0.0059  99  TYR C CG  
6714  C CD1 . TYR C 99  ? 2.5967 2.3839 3.0088 0.1945  -0.3056 0.0141  99  TYR C CD1 
6715  C CD2 . TYR C 99  ? 2.6597 2.5067 3.1066 0.1948  -0.2948 -0.0104 99  TYR C CD2 
6716  C CE1 . TYR C 99  ? 2.5621 2.3384 2.9917 0.1985  -0.3082 0.0062  99  TYR C CE1 
6717  C CE2 . TYR C 99  ? 2.6388 2.4754 3.1028 0.1989  -0.2973 -0.0188 99  TYR C CE2 
6718  C CZ  . TYR C 99  ? 2.5852 2.3863 3.0409 0.2008  -0.3041 -0.0106 99  TYR C CZ  
6719  O OH  . TYR C 99  ? 2.5712 2.3610 3.0441 0.2049  -0.3067 -0.0190 99  TYR C OH  
6720  N N   . TYR C 100 ? 2.4317 2.3011 2.8613 0.2131  -0.3189 0.0017  100 TYR C N   
6721  C CA  . TYR C 100 ? 2.3579 2.2414 2.8080 0.2257  -0.3297 -0.0071 100 TYR C CA  
6722  C C   . TYR C 100 ? 2.3983 2.2580 2.8361 0.2344  -0.3452 0.0032  100 TYR C C   
6723  O O   . TYR C 100 ? 2.4313 2.2778 2.8437 0.2304  -0.3468 0.0163  100 TYR C O   
6724  C CB  . TYR C 100 ? 2.2827 2.2021 2.7409 0.2248  -0.3250 -0.0138 100 TYR C CB  
6725  C CG  . TYR C 100 ? 2.2155 2.1589 2.7021 0.2353  -0.3308 -0.0275 100 TYR C CG  
6726  C CD1 . TYR C 100 ? 2.1241 2.1015 2.6217 0.2340  -0.3251 -0.0353 100 TYR C CD1 
6727  C CD2 . TYR C 100 ? 2.2300 2.1619 2.7326 0.2465  -0.3417 -0.0326 100 TYR C CD2 
6728  C CE1 . TYR C 100 ? 2.0707 2.0706 2.5943 0.2433  -0.3296 -0.0477 100 TYR C CE1 
6729  C CE2 . TYR C 100 ? 2.1822 2.1369 2.7115 0.2562  -0.3464 -0.0454 100 TYR C CE2 
6730  C CZ  . TYR C 100 ? 2.1145 2.1034 2.6541 0.2543  -0.3401 -0.0529 100 TYR C CZ  
6731  O OH  . TYR C 100 ? 2.1178 2.1298 2.6841 0.2636  -0.3441 -0.0655 100 TYR C OH  
6732  N N   . PHE C 101 ? 2.4012 2.2558 2.8574 0.2464  -0.3567 -0.0030 101 PHE C N   
6733  C CA  . PHE C 101 ? 2.3470 2.1773 2.7952 0.2562  -0.3729 0.0056  101 PHE C CA  
6734  C C   . PHE C 101 ? 2.3296 2.1250 2.7460 0.2500  -0.3738 0.0228  101 PHE C C   
6735  O O   . PHE C 101 ? 2.3153 2.0991 2.7114 0.2516  -0.3817 0.0341  101 PHE C O   
6736  C CB  . PHE C 101 ? 2.3601 2.2086 2.8117 0.2635  -0.3823 0.0048  101 PHE C CB  
6737  C CG  . PHE C 101 ? 2.4164 2.2859 2.8555 0.2548  -0.3736 0.0075  101 PHE C CG  
6738  C CD1 . PHE C 101 ? 2.3984 2.3036 2.8562 0.2527  -0.3649 -0.0046 101 PHE C CD1 
6739  C CD2 . PHE C 101 ? 2.4115 2.2649 2.8200 0.2490  -0.3741 0.0220  101 PHE C CD2 
6740  C CE1 . PHE C 101 ? 2.3363 2.2601 2.7831 0.2449  -0.3571 -0.0021 101 PHE C CE1 
6741  C CE2 . PHE C 101 ? 2.3830 2.2554 2.7805 0.2413  -0.3662 0.0241  101 PHE C CE2 
6742  C CZ  . PHE C 101 ? 2.3353 2.2427 2.7523 0.2393  -0.3579 0.0120  101 PHE C CZ  
6743  N N   . ARG C 102 ? 2.2365 2.0149 2.6488 0.2427  -0.3656 0.0246  102 ARG C N   
6744  C CA  . ARG C 102 ? 2.1617 1.9041 2.5466 0.2377  -0.3669 0.0404  102 ARG C CA  
6745  C C   . ARG C 102 ? 2.1106 1.8242 2.4937 0.2491  -0.3834 0.0464  102 ARG C C   
6746  O O   . ARG C 102 ? 2.1263 1.8101 2.4838 0.2471  -0.3879 0.0613  102 ARG C O   
6747  C CB  . ARG C 102 ? 2.1189 1.8513 2.5028 0.2271  -0.3540 0.0399  102 ARG C CB  
6748  C CG  . ARG C 102 ? 2.0343 1.7644 2.4442 0.2323  -0.3553 0.0279  102 ARG C CG  
6749  C CD  . ARG C 102 ? 2.0452 1.7577 2.4501 0.2218  -0.3448 0.0302  102 ARG C CD  
6750  N NE  . ARG C 102 ? 2.0031 1.6766 2.3843 0.2197  -0.3496 0.0462  102 ARG C NE  
6751  C CZ  . ARG C 102 ? 2.0057 1.6571 2.3801 0.2112  -0.3426 0.0509  102 ARG C CZ  
6752  N NH1 . ARG C 102 ? 2.0702 1.7351 2.4597 0.2041  -0.3310 0.0405  102 ARG C NH1 
6753  N NH2 . ARG C 102 ? 1.9383 1.5544 2.2905 0.2096  -0.3473 0.0662  102 ARG C NH2 
6754  N N   . ASP C 103 ? 2.0546 1.7766 2.4644 0.2610  -0.3925 0.0350  103 ASP C N   
6755  C CA  . ASP C 103 ? 2.0651 1.7614 2.4758 0.2730  -0.4091 0.0398  103 ASP C CA  
6756  C C   . ASP C 103 ? 2.1560 1.8485 2.5499 0.2787  -0.4214 0.0496  103 ASP C C   
6757  O O   . ASP C 103 ? 2.2232 1.8844 2.5984 0.2824  -0.4320 0.0624  103 ASP C O   
6758  C CB  . ASP C 103 ? 2.0120 1.7219 2.4575 0.2845  -0.4150 0.0238  103 ASP C CB  
6759  C CG  . ASP C 103 ? 2.0209 1.7728 2.4876 0.2866  -0.4110 0.0100  103 ASP C CG  
6760  O OD1 . ASP C 103 ? 2.0414 1.8103 2.4956 0.2803  -0.4056 0.0135  103 ASP C OD1 
6761  O OD2 . ASP C 103 ? 1.9792 1.7468 2.4751 0.2946  -0.4130 -0.0044 103 ASP C OD2 
6762  N N   . ARG C 104 ? 2.1553 1.8789 2.5555 0.2795  -0.4204 0.0439  104 ARG C N   
6763  C CA  . ARG C 104 ? 2.1735 1.8958 2.5594 0.2850  -0.4324 0.0519  104 ARG C CA  
6764  C C   . ARG C 104 ? 2.2332 1.9332 2.5812 0.2760  -0.4299 0.0691  104 ARG C C   
6765  O O   . ARG C 104 ? 2.2863 1.9685 2.6163 0.2814  -0.4426 0.0798  104 ARG C O   
6766  C CB  . ARG C 104 ? 2.1295 1.8911 2.5311 0.2864  -0.4303 0.0415  104 ARG C CB  
6767  C CG  . ARG C 104 ? 2.0769 1.8640 2.5160 0.2940  -0.4304 0.0238  104 ARG C CG  
6768  C CD  . ARG C 104 ? 2.0634 1.8895 2.5166 0.2937  -0.4265 0.0143  104 ARG C CD  
6769  N NE  . ARG C 104 ? 2.0112 1.8412 2.4627 0.3023  -0.4410 0.0176  104 ARG C NE  
6770  C CZ  . ARG C 104 ? 1.9052 1.7504 2.3828 0.3143  -0.4514 0.0079  104 ARG C CZ  
6771  N NH1 . ARG C 104 ? 1.8802 1.7383 2.3873 0.3192  -0.4487 -0.0058 104 ARG C NH1 
6772  N NH2 . ARG C 104 ? 1.8220 1.6701 2.2966 0.3213  -0.4647 0.0115  104 ARG C NH2 
6773  N N   . ILE C 105 ? 2.2346 1.9354 2.5701 0.2625  -0.4138 0.0720  105 ILE C N   
6774  C CA  . ILE C 105 ? 2.2384 1.9196 2.5382 0.2534  -0.4097 0.0878  105 ILE C CA  
6775  C C   . ILE C 105 ? 2.2704 1.9103 2.5524 0.2536  -0.4148 0.1004  105 ILE C C   
6776  O O   . ILE C 105 ? 2.3671 1.9837 2.6224 0.2548  -0.4229 0.1143  105 ILE C O   
6777  C CB  . ILE C 105 ? 2.1433 1.8413 2.4374 0.2390  -0.3905 0.0861  105 ILE C CB  
6778  N N   . MET C 106 ? 2.2491 1.8788 2.5453 0.2523  -0.4102 0.0957  106 MET C N   
6779  C CA  . MET C 106 ? 2.3309 1.9213 2.6138 0.2527  -0.4149 0.1066  106 MET C CA  
6780  C C   . MET C 106 ? 2.4982 2.0735 2.7938 0.2678  -0.4332 0.1053  106 MET C C   
6781  O O   . MET C 106 ? 2.5550 2.1045 2.8542 0.2702  -0.4364 0.1076  106 MET C O   
6782  C CB  . MET C 106 ? 2.1709 1.7563 2.4628 0.2436  -0.4013 0.1023  106 MET C CB  
6783  C CG  . MET C 106 ? 2.0974 1.6847 2.3693 0.2278  -0.3845 0.1088  106 MET C CG  
6784  S SD  . MET C 106 ? 2.3249 1.8714 2.5544 0.2218  -0.3863 0.1317  106 MET C SD  
6785  C CE  . MET C 106 ? 2.2818 1.8478 2.4913 0.2073  -0.3694 0.1357  106 MET C CE  
6786  N N   . GLU C 107 ? 2.6418 2.2324 2.9451 0.2783  -0.4454 0.1016  107 GLU C N   
6787  C CA  . GLU C 107 ? 2.7327 2.3122 3.0509 0.2934  -0.4632 0.0993  107 GLU C CA  
6788  C C   . GLU C 107 ? 2.9376 2.4773 3.2280 0.2972  -0.4758 0.1167  107 GLU C C   
6789  O O   . GLU C 107 ? 2.9727 2.4911 3.2719 0.3069  -0.4876 0.1176  107 GLU C O   
6790  C CB  . GLU C 107 ? 2.6749 2.2858 3.0115 0.3028  -0.4717 0.0893  107 GLU C CB  
6791  C CG  . GLU C 107 ? 2.7206 2.3278 3.0800 0.3191  -0.4889 0.0833  107 GLU C CG  
6792  C CD  . GLU C 107 ? 2.6946 2.3379 3.0774 0.3269  -0.4942 0.0709  107 GLU C CD  
6793  O OE1 . GLU C 107 ? 2.5936 2.2685 2.9971 0.3228  -0.4825 0.0576  107 GLU C OE1 
6794  O OE2 . GLU C 107 ? 2.8039 2.4442 3.1846 0.3369  -0.5101 0.0746  107 GLU C OE2 
6795  N N   . GLU C 108 ? 3.3052 2.8339 3.5618 0.2898  -0.4736 0.1307  108 GLU C N   
6796  C CA  . GLU C 108 ? 3.3422 2.8328 3.5685 0.2920  -0.4842 0.1484  108 GLU C CA  
6797  C C   . GLU C 108 ? 3.3821 2.8445 3.5846 0.2795  -0.4723 0.1604  108 GLU C C   
6798  O O   . GLU C 108 ? 3.4101 2.8432 3.5806 0.2777  -0.4770 0.1769  108 GLU C O   
6799  C CB  . GLU C 108 ? 3.4094 2.9042 3.6119 0.2934  -0.4916 0.1566  108 GLU C CB  
6800  C CG  . GLU C 108 ? 3.4290 2.9484 3.6523 0.3059  -0.5052 0.1468  108 GLU C CG  
6801  C CD  . GLU C 108 ? 3.4746 2.9956 3.6726 0.3067  -0.5130 0.1555  108 GLU C CD  
6802  O OE1 . GLU C 108 ? 3.4462 2.9656 3.6176 0.2951  -0.5020 0.1635  108 GLU C OE1 
6803  O OE2 . GLU C 108 ? 3.4983 3.0221 3.7032 0.3188  -0.5301 0.1541  108 GLU C OE2 
6804  N N   . LYS C 109 ? 3.1481 2.6187 3.3656 0.2711  -0.4574 0.1525  109 LYS C N   
6805  C CA  . LYS C 109 ? 3.1452 2.5932 3.3439 0.2581  -0.4443 0.1622  109 LYS C CA  
6806  C C   . LYS C 109 ? 3.1764 2.6172 3.3384 0.2476  -0.4371 0.1764  109 LYS C C   
6807  O O   . LYS C 109 ? 3.2309 2.6376 3.3647 0.2448  -0.4397 0.1925  109 LYS C O   
6808  C CB  . LYS C 109 ? 3.2322 2.6412 3.4275 0.2627  -0.4530 0.1704  109 LYS C CB  
6809  C CG  . LYS C 109 ? 3.2021 2.6148 3.4324 0.2683  -0.4539 0.1563  109 LYS C CG  
6810  C CD  . LYS C 109 ? 3.2532 2.6251 3.4788 0.2737  -0.4638 0.1653  109 LYS C CD  
6811  C CE  . LYS C 109 ? 3.2746 2.6155 3.4700 0.2607  -0.4542 0.1815  109 LYS C CE  
6812  N NZ  . LYS C 109 ? 3.2224 2.5736 3.4281 0.2474  -0.4354 0.1746  109 LYS C NZ  
6813  N N   . PRO C 110 ? 3.1414 2.6125 3.3021 0.2416  -0.4278 0.1714  110 PRO C N   
6814  C CA  . PRO C 110 ? 3.1449 2.6099 3.2713 0.2313  -0.4198 0.1840  110 PRO C CA  
6815  C C   . PRO C 110 ? 3.0836 2.5374 3.1993 0.2166  -0.4021 0.1894  110 PRO C C   
6816  O O   . PRO C 110 ? 2.9855 2.4540 3.1236 0.2113  -0.3911 0.1787  110 PRO C O   
6817  C CB  . PRO C 110 ? 3.0163 2.5204 3.1509 0.2305  -0.4156 0.1742  110 PRO C CB  
6818  C CG  . PRO C 110 ? 2.9579 2.4849 3.1281 0.2424  -0.4250 0.1585  110 PRO C CG  
6819  C CD  . PRO C 110 ? 2.9566 2.4688 3.1461 0.2448  -0.4254 0.1542  110 PRO C CD  
6820  N N   . SER C 111 ? 3.1206 2.5479 3.2013 0.2098  -0.3994 0.2062  111 SER C N   
6821  C CA  . SER C 111 ? 3.0255 2.4411 3.0938 0.1952  -0.3824 0.2127  111 SER C CA  
6822  C C   . SER C 111 ? 2.8898 2.3377 2.9618 0.1847  -0.3657 0.2054  111 SER C C   
6823  O O   . SER C 111 ? 2.8168 2.2749 2.9044 0.1761  -0.3522 0.1985  111 SER C O   
6824  C CB  . SER C 111 ? 3.0093 2.3889 3.0383 0.1910  -0.3838 0.2328  111 SER C CB  
6825  O OG  . SER C 111 ? 2.9565 2.3283 2.9724 0.1760  -0.3660 0.2391  111 SER C OG  
6826  N N   . HIS C 112 ? 2.9693 2.4336 3.0276 0.1852  -0.3667 0.2066  112 HIS C N   
6827  C CA  . HIS C 112 ? 2.8897 2.3847 2.9502 0.1761  -0.3521 0.2002  112 HIS C CA  
6828  C C   . HIS C 112 ? 2.8594 2.3872 2.9378 0.1846  -0.3593 0.1880  112 HIS C C   
6829  O O   . HIS C 112 ? 2.8706 2.3941 2.9457 0.1956  -0.3751 0.1896  112 HIS C O   
6830  C CB  . HIS C 112 ? 2.8891 2.3731 2.9132 0.1666  -0.3437 0.2140  112 HIS C CB  
6831  C CG  . HIS C 112 ? 2.9232 2.3729 2.9259 0.1585  -0.3374 0.2281  112 HIS C CG  
6832  N ND1 . HIS C 112 ? 2.9245 2.3726 2.9374 0.1481  -0.3231 0.2261  112 HIS C ND1 
6833  C CD2 . HIS C 112 ? 2.9362 2.3519 2.9073 0.1589  -0.3434 0.2445  112 HIS C CD2 
6834  C CE1 . HIS C 112 ? 2.9551 2.3697 2.9445 0.1423  -0.3202 0.2407  112 HIS C CE1 
6835  N NE2 . HIS C 112 ? 2.9596 2.3538 2.9229 0.1487  -0.3322 0.2523  112 HIS C NE2 
6836  N N   . VAL C 113 ? 2.5627 2.1233 2.6600 0.1792  -0.3476 0.1760  113 VAL C N   
6837  C CA  . VAL C 113 ? 2.3496 1.9440 2.4657 0.1855  -0.3518 0.1636  113 VAL C CA  
6838  C C   . VAL C 113 ? 2.2545 1.8695 2.3579 0.1764  -0.3397 0.1640  113 VAL C C   
6839  O O   . VAL C 113 ? 2.2933 1.9144 2.3958 0.1651  -0.3238 0.1636  113 VAL C O   
6840  C CB  . VAL C 113 ? 2.2117 1.8285 2.3660 0.1892  -0.3503 0.1470  113 VAL C CB  
6841  C CG1 . VAL C 113 ? 2.3386 1.9565 2.5007 0.1779  -0.3341 0.1441  113 VAL C CG1 
6842  C CG2 . VAL C 113 ? 2.1867 1.8412 2.3589 0.1927  -0.3505 0.1347  113 VAL C CG2 
6843  N N   . PHE C 114 ? 2.2288 1.8545 2.3229 0.1814  -0.3474 0.1647  114 PHE C N   
6844  C CA  . PHE C 114 ? 2.1048 1.7510 2.1879 0.1741  -0.3374 0.1643  114 PHE C CA  
6845  C C   . PHE C 114 ? 2.0680 1.7527 2.1815 0.1744  -0.3320 0.1484  114 PHE C C   
6846  O O   . PHE C 114 ? 2.1916 1.8902 2.3286 0.1841  -0.3420 0.1386  114 PHE C O   
6847  C CB  . PHE C 114 ? 2.0659 1.7057 2.1249 0.1791  -0.3483 0.1720  114 PHE C CB  
6848  C CG  . PHE C 114 ? 2.0419 1.6475 2.0639 0.1753  -0.3489 0.1889  114 PHE C CG  
6849  C CD1 . PHE C 114 ? 2.0514 1.6384 2.0622 0.1655  -0.3366 0.1964  114 PHE C CD1 
6850  C CD2 . PHE C 114 ? 2.0866 1.6788 2.0850 0.1814  -0.3618 0.1972  114 PHE C CD2 
6851  C CE1 . PHE C 114 ? 2.1560 1.7115 2.1323 0.1617  -0.3366 0.2123  114 PHE C CE1 
6852  C CE2 . PHE C 114 ? 2.1897 1.7502 2.1528 0.1779  -0.3622 0.2130  114 PHE C CE2 
6853  C CZ  . PHE C 114 ? 2.2200 1.7622 2.1718 0.1680  -0.3493 0.2206  114 PHE C CZ  
6854  N N   . LEU C 115 ? 1.8515 1.5534 1.9643 0.1638  -0.3160 0.1458  115 LEU C N   
6855  C CA  . LEU C 115 ? 1.7753 1.5138 1.9137 0.1629  -0.3094 0.1318  115 LEU C CA  
6856  C C   . LEU C 115 ? 1.7259 1.4794 1.8488 0.1550  -0.2994 0.1341  115 LEU C C   
6857  O O   . LEU C 115 ? 1.6715 1.4199 1.7811 0.1445  -0.2859 0.1394  115 LEU C O   
6858  C CB  . LEU C 115 ? 1.7764 1.5232 1.9379 0.1580  -0.2990 0.1233  115 LEU C CB  
6859  C CG  . LEU C 115 ? 1.7011 1.4850 1.8908 0.1577  -0.2928 0.1082  115 LEU C CG  
6860  C CD1 . LEU C 115 ? 1.9388 1.7266 2.1565 0.1609  -0.2932 0.0980  115 LEU C CD1 
6861  C CD2 . LEU C 115 ? 1.7099 1.5096 1.8934 0.1458  -0.2761 0.1081  115 LEU C CD2 
6862  N N   . LEU C 116 ? 1.8241 1.5960 1.9492 0.1601  -0.3059 0.1300  116 LEU C N   
6863  C CA  . LEU C 116 ? 1.8198 1.6083 1.9331 0.1538  -0.2975 0.1305  116 LEU C CA  
6864  C C   . LEU C 116 ? 1.9570 1.7804 2.0959 0.1573  -0.2982 0.1173  116 LEU C C   
6865  O O   . LEU C 116 ? 2.1804 2.0126 2.3408 0.1664  -0.3086 0.1095  116 LEU C O   
6866  C CB  . LEU C 116 ? 1.7820 1.5525 1.8635 0.1554  -0.3050 0.1419  116 LEU C CB  
6867  N N   . ASN C 117 ? 1.8864 1.7298 2.0230 0.1500  -0.2867 0.1148  117 ASN C N   
6868  C CA  . ASN C 117 ? 2.0204 1.8974 2.1803 0.1517  -0.2852 0.1028  117 ASN C CA  
6869  C C   . ASN C 117 ? 2.0229 1.9074 2.1741 0.1565  -0.2944 0.1036  117 ASN C C   
6870  O O   . ASN C 117 ? 1.9889 1.8546 2.1131 0.1566  -0.2992 0.1135  117 ASN C O   
6871  C CB  . ASN C 117 ? 1.8946 1.7904 2.0592 0.1413  -0.2679 0.0991  117 ASN C CB  
6872  C CG  . ASN C 117 ? 1.8764 1.8062 2.0693 0.1429  -0.2652 0.0858  117 ASN C CG  
6873  O OD1 . ASN C 117 ? 1.9996 1.9389 2.2126 0.1514  -0.2748 0.0783  117 ASN C OD1 
6874  N ND2 . ASN C 117 ? 1.7838 1.7322 1.9786 0.1349  -0.2519 0.0830  117 ASN C ND2 
6875  N N   . CYS C 118 ? 2.0828 1.9954 2.2573 0.1605  -0.2968 0.0927  118 CYS C N   
6876  C CA  . CYS C 118 ? 2.0506 1.9730 2.2210 0.1651  -0.3058 0.0919  118 CYS C CA  
6877  C C   . CYS C 118 ? 1.9480 1.8759 2.0986 0.1570  -0.2964 0.0961  118 CYS C C   
6878  O O   . CYS C 118 ? 1.9378 1.8531 2.0649 0.1580  -0.3026 0.1034  118 CYS C O   
6879  C CB  . CYS C 118 ? 2.3030 2.2545 2.5055 0.1709  -0.3099 0.0790  118 CYS C CB  
6880  S SG  . CYS C 118 ? 2.4997 2.4707 2.7021 0.1740  -0.3172 0.0759  118 CYS C SG  
6881  N N   . ASP C 119 ? 1.9065 1.8532 2.0662 0.1492  -0.2817 0.0914  119 ASP C N   
6882  C CA  . ASP C 119 ? 1.8805 1.8359 2.0253 0.1419  -0.2723 0.0938  119 ASP C CA  
6883  C C   . ASP C 119 ? 1.8792 1.8125 1.9972 0.1339  -0.2628 0.1044  119 ASP C C   
6884  O O   . ASP C 119 ? 1.8749 1.8150 1.9942 0.1256  -0.2485 0.1039  119 ASP C O   
6885  C CB  . ASP C 119 ? 1.8321 1.8188 1.9997 0.1378  -0.2618 0.0838  119 ASP C CB  
6886  C CG  . ASP C 119 ? 1.7981 1.7903 1.9852 0.1353  -0.2539 0.0785  119 ASP C CG  
6887  O OD1 . ASP C 119 ? 1.8336 1.8049 2.0168 0.1366  -0.2564 0.0826  119 ASP C OD1 
6888  O OD2 . ASP C 119 ? 1.7756 1.7926 1.9815 0.1322  -0.2454 0.0702  119 ASP C OD2 
6889  N N   . VAL C 120 ? 1.9255 1.8320 2.0189 0.1366  -0.2712 0.1143  120 VAL C N   
6890  C CA  . VAL C 120 ? 2.0257 1.9083 2.0906 0.1298  -0.2637 0.1256  120 VAL C CA  
6891  C C   . VAL C 120 ? 2.1644 2.0308 2.2004 0.1326  -0.2726 0.1338  120 VAL C C   
6892  O O   . VAL C 120 ? 2.1382 1.9979 2.1739 0.1413  -0.2880 0.1340  120 VAL C O   
6893  C CB  . VAL C 120 ? 2.0231 1.8832 2.0877 0.1299  -0.2641 0.1304  120 VAL C CB  
6894  C CG1 . VAL C 120 ? 2.2193 2.0508 2.2509 0.1243  -0.2596 0.1437  120 VAL C CG1 
6895  C CG2 . VAL C 120 ? 1.9768 1.8516 2.0658 0.1250  -0.2528 0.1230  120 VAL C CG2 
6896  N N   . CYS C 121 ? 2.4018 2.2622 2.4135 0.1252  -0.2629 0.1403  121 CYS C N   
6897  C CA  . CYS C 121 ? 2.4245 2.2703 2.4064 0.1268  -0.2696 0.1478  121 CYS C CA  
6898  C C   . CYS C 121 ? 2.5378 2.3580 2.4891 0.1200  -0.2609 0.1597  121 CYS C C   
6899  O O   . CYS C 121 ? 2.6260 2.4497 2.5632 0.1126  -0.2488 0.1621  121 CYS C O   
6900  C CB  . CYS C 121 ? 2.3856 2.2536 2.3685 0.1254  -0.2670 0.1422  121 CYS C CB  
6901  S SG  . CYS C 121 ? 2.4377 2.3322 2.4514 0.1342  -0.2798 0.1299  121 CYS C SG  
6902  N N   . CYS C 122 ? 2.6603 2.4546 2.6014 0.1226  -0.2671 0.1674  122 CYS C N   
6903  C CA  . CYS C 122 ? 2.8379 2.6049 2.7490 0.1167  -0.2605 0.1798  122 CYS C CA  
6904  C C   . CYS C 122 ? 2.8702 2.6112 2.7546 0.1233  -0.2754 0.1890  122 CYS C C   
6905  O O   . CYS C 122 ? 2.7639 2.5095 2.6534 0.1321  -0.2904 0.1853  122 CYS C O   
6906  C CB  . CYS C 122 ? 2.7764 2.5335 2.6979 0.1124  -0.2527 0.1819  122 CYS C CB  
6907  S SG  . CYS C 122 ? 2.7181 2.4690 2.6638 0.1221  -0.2675 0.1780  122 CYS C SG  
6908  N N   . SER C 123 ? 2.9554 2.6688 2.8109 0.1190  -0.2711 0.2011  123 SER C N   
6909  C CA  . SER C 123 ? 2.9282 2.6145 2.7552 0.1247  -0.2846 0.2111  123 SER C CA  
6910  C C   . SER C 123 ? 2.8915 2.5617 2.7284 0.1325  -0.2982 0.2132  123 SER C C   
6911  O O   . SER C 123 ? 2.8842 2.5357 2.7037 0.1398  -0.3132 0.2193  123 SER C O   
6912  C CB  . SER C 123 ? 2.9812 2.6436 2.7720 0.1170  -0.2744 0.2239  123 SER C CB  
6913  O OG  . SER C 123 ? 2.9281 2.5798 2.7231 0.1102  -0.2628 0.2282  123 SER C OG  
6914  N N   . PHE C 124 ? 2.9119 2.5885 2.7761 0.1314  -0.2935 0.2081  124 PHE C N   
6915  C CA  . PHE C 124 ? 2.8976 2.5606 2.7752 0.1386  -0.3050 0.2087  124 PHE C CA  
6916  C C   . PHE C 124 ? 3.0000 2.6254 2.8468 0.1390  -0.3101 0.2235  124 PHE C C   
6917  O O   . PHE C 124 ? 2.9610 2.5713 2.7955 0.1477  -0.3265 0.2280  124 PHE C O   
6918  C CB  . PHE C 124 ? 2.7657 2.4419 2.6620 0.1503  -0.3226 0.2004  124 PHE C CB  
6919  C CG  . PHE C 124 ? 2.6435 2.3557 2.5732 0.1505  -0.3186 0.1858  124 PHE C CG  
6920  C CD1 . PHE C 124 ? 2.5079 2.2324 2.4693 0.1509  -0.3148 0.1775  124 PHE C CD1 
6921  C CD2 . PHE C 124 ? 2.5987 2.3320 2.5279 0.1505  -0.3185 0.1803  124 PHE C CD2 
6922  C CE1 . PHE C 124 ? 2.3865 2.1437 2.3775 0.1511  -0.3109 0.1643  124 PHE C CE1 
6923  C CE2 . PHE C 124 ? 2.4570 2.2227 2.4164 0.1505  -0.3146 0.1674  124 PHE C CE2 
6924  C CZ  . PHE C 124 ? 2.3811 2.1589 2.3710 0.1508  -0.3107 0.1596  124 PHE C CZ  
6925  N N   . PRO C 125 ? 3.3196 2.9290 3.1534 0.1298  -0.2965 0.2315  125 PRO C N   
6926  C CA  . PRO C 125 ? 3.3472 2.9198 3.1531 0.1298  -0.3006 0.2460  125 PRO C CA  
6927  C C   . PRO C 125 ? 3.3505 2.9099 3.1755 0.1339  -0.3068 0.2460  125 PRO C C   
6928  O O   . PRO C 125 ? 3.3700 2.9138 3.1927 0.1272  -0.2972 0.2517  125 PRO C O   
6929  C CB  . PRO C 125 ? 3.3739 2.9394 3.1592 0.1170  -0.2811 0.2534  125 PRO C CB  
6930  C CG  . PRO C 125 ? 3.3475 2.9472 3.1566 0.1107  -0.2669 0.2415  125 PRO C CG  
6931  C CD  . PRO C 125 ? 3.3124 2.9365 3.1564 0.1187  -0.2765 0.2279  125 PRO C CD  
6932  N N   . LEU C 126 ? 2.9283 2.4943 2.7731 0.1452  -0.3231 0.2391  126 LEU C N   
6933  C CA  . LEU C 126 ? 2.7893 2.3485 2.6583 0.1501  -0.3292 0.2359  126 LEU C CA  
6934  C C   . LEU C 126 ? 2.7541 2.2746 2.6009 0.1499  -0.3329 0.2501  126 LEU C C   
6935  O O   . LEU C 126 ? 2.7708 2.2814 2.6313 0.1477  -0.3288 0.2504  126 LEU C O   
6936  C CB  . LEU C 126 ? 2.6074 2.1803 2.4991 0.1630  -0.3468 0.2264  126 LEU C CB  
6937  C CG  . LEU C 126 ? 2.5844 2.1957 2.5010 0.1643  -0.3448 0.2119  126 LEU C CG  
6938  C CD1 . LEU C 126 ? 2.5032 2.1253 2.4437 0.1771  -0.3624 0.2033  126 LEU C CD1 
6939  C CD2 . LEU C 126 ? 2.5852 2.2176 2.5257 0.1558  -0.3278 0.2031  126 LEU C CD2 
6940  N N   . GLN C 127 ? 2.6543 2.1520 2.4663 0.1521  -0.3405 0.2622  127 GLN C N   
6941  C CA  . GLN C 127 ? 2.5358 1.9955 2.3241 0.1519  -0.3445 0.2768  127 GLN C CA  
6942  C C   . GLN C 127 ? 2.6611 2.1073 2.4325 0.1385  -0.3253 0.2856  127 GLN C C   
6943  O O   . GLN C 127 ? 2.6101 2.0286 2.3732 0.1365  -0.3248 0.2951  127 GLN C O   
6944  C CB  . GLN C 127 ? 2.3621 1.8022 2.1173 0.1587  -0.3592 0.2870  127 GLN C CB  
6945  C CG  . GLN C 127 ? 2.2464 1.6470 1.9804 0.1622  -0.3687 0.3013  127 GLN C CG  
6946  C CD  . GLN C 127 ? 2.2339 1.6177 1.9390 0.1708  -0.3860 0.3096  127 GLN C CD  
6947  O OE1 . GLN C 127 ? 2.2760 1.6789 1.9812 0.1755  -0.3930 0.3032  127 GLN C OE1 
6948  N NE2 . GLN C 127 ? 2.1729 1.5206 1.8531 0.1729  -0.3934 0.3240  127 GLN C NE2 
6949  N N   . GLY C 128 ? 2.8194 2.2847 2.5867 0.1292  -0.3096 0.2825  128 GLY C N   
6950  C CA  . GLY C 128 ? 2.8994 2.3553 2.6532 0.1162  -0.2906 0.2897  128 GLY C CA  
6951  C C   . GLY C 128 ? 3.1194 2.5874 2.9052 0.1103  -0.2792 0.2817  128 GLY C C   
6952  O O   . GLY C 128 ? 2.9937 2.4435 2.7738 0.1023  -0.2693 0.2892  128 GLY C O   
6953  N N   . ILE C 129 ? 3.9938 3.4928 3.8135 0.1140  -0.2806 0.2665  129 ILE C N   
6954  C CA  . ILE C 129 ? 3.9881 3.5004 3.8394 0.1091  -0.2710 0.2576  129 ILE C CA  
6955  C C   . ILE C 129 ? 3.9939 3.4871 3.8596 0.1153  -0.2814 0.2583  129 ILE C C   
6956  O O   . ILE C 129 ? 4.0017 3.4899 3.8813 0.1092  -0.2727 0.2574  129 ILE C O   
6957  C CB  . ILE C 129 ? 3.9536 3.5055 3.8346 0.1109  -0.2686 0.2412  129 ILE C CB  
6958  C CG1 . ILE C 129 ? 3.9472 3.5138 3.8603 0.1059  -0.2587 0.2315  129 ILE C CG1 
6959  C CG2 . ILE C 129 ? 3.9294 3.4908 3.8230 0.1242  -0.2870 0.2342  129 ILE C CG2 
6960  C CD1 . ILE C 129 ? 3.9719 3.5293 3.8769 0.0929  -0.2412 0.2377  129 ILE C CD1 
6961  N N   . LEU C 130 ? 3.1263 2.6082 2.9890 0.1273  -0.3001 0.2600  130 LEU C N   
6962  C CA  . LEU C 130 ? 2.8521 2.3129 2.7262 0.1338  -0.3109 0.2617  130 LEU C CA  
6963  C C   . LEU C 130 ? 2.7851 2.2104 2.6360 0.1266  -0.3050 0.2768  130 LEU C C   
6964  O O   . LEU C 130 ? 2.7468 2.1617 2.6131 0.1239  -0.3015 0.2761  130 LEU C O   
6965  C CB  . LEU C 130 ? 2.7572 2.2113 2.6285 0.1480  -0.3325 0.2622  130 LEU C CB  
6966  C CG  . LEU C 130 ? 2.6627 2.1099 2.5589 0.1589  -0.3470 0.2569  130 LEU C CG  
6967  C CD1 . LEU C 130 ? 2.6017 2.0492 2.4949 0.1723  -0.3670 0.2562  130 LEU C CD1 
6968  C CD2 . LEU C 130 ? 2.5974 2.0087 2.4845 0.1571  -0.3477 0.2679  130 LEU C CD2 
6969  N N   . ASP C 131 ? 2.7551 2.1611 2.5684 0.1234  -0.3038 0.2904  131 ASP C N   
6970  C CA  . ASP C 131 ? 2.6061 1.9776 2.3947 0.1162  -0.2977 0.3058  131 ASP C CA  
6971  C C   . ASP C 131 ? 2.6580 2.0364 2.4519 0.1017  -0.2761 0.3052  131 ASP C C   
6972  O O   . ASP C 131 ? 2.5964 1.9521 2.3873 0.0955  -0.2700 0.3129  131 ASP C O   
6973  C CB  . ASP C 131 ? 2.4423 1.7926 2.1884 0.1168  -0.3022 0.3202  131 ASP C CB  
6974  C CG  . ASP C 131 ? 2.3842 1.7293 2.1248 0.1312  -0.3242 0.3204  131 ASP C CG  
6975  O OD1 . ASP C 131 ? 2.3642 1.7103 2.1299 0.1406  -0.3370 0.3137  131 ASP C OD1 
6976  O OD2 . ASP C 131 ? 2.3851 1.7256 2.0968 0.1331  -0.3288 0.3269  131 ASP C OD2 
6977  N N   . ALA C 132 ? 2.7105 2.1200 2.5128 0.0961  -0.2643 0.2964  132 ALA C N   
6978  C CA  . ALA C 132 ? 2.6923 2.1121 2.5043 0.0830  -0.2444 0.2941  132 ALA C CA  
6979  C C   . ALA C 132 ? 2.6761 2.1041 2.5247 0.0828  -0.2432 0.2836  132 ALA C C   
6980  O O   . ALA C 132 ? 2.6639 2.0851 2.5178 0.0728  -0.2304 0.2858  132 ALA C O   
6981  C CB  . ALA C 132 ? 2.7612 2.2131 2.5751 0.0782  -0.2335 0.2863  132 ALA C CB  
6982  N N   . HIS C 133 ? 2.7134 2.1557 2.5875 0.0937  -0.2563 0.2721  133 HIS C N   
6983  C CA  . HIS C 133 ? 2.6355 2.0850 2.5439 0.0945  -0.2561 0.2617  133 HIS C CA  
6984  C C   . HIS C 133 ? 2.6142 2.0282 2.5185 0.0963  -0.2628 0.2706  133 HIS C C   
6985  O O   . HIS C 133 ? 2.6054 2.0152 2.5276 0.0908  -0.2560 0.2675  133 HIS C O   
6986  C CB  . HIS C 133 ? 2.6272 2.1032 2.5637 0.1057  -0.2675 0.2466  133 HIS C CB  
6987  C CG  . HIS C 133 ? 2.5977 2.0809 2.5688 0.1077  -0.2684 0.2352  133 HIS C CG  
6988  N ND1 . HIS C 133 ? 2.5410 2.0303 2.5270 0.0973  -0.2539 0.2310  133 HIS C ND1 
6989  C CD2 . HIS C 133 ? 2.6192 2.1047 2.6132 0.1189  -0.2821 0.2268  133 HIS C CD2 
6990  C CE1 . HIS C 133 ? 2.5316 2.0261 2.5471 0.1020  -0.2586 0.2204  133 HIS C CE1 
6991  N NE2 . HIS C 133 ? 2.5523 2.0448 2.5734 0.1152  -0.2754 0.2176  133 HIS C NE2 
6992  N N   . ARG C 134 ? 2.6489 2.0371 2.5301 0.1040  -0.2767 0.2816  134 ARG C N   
6993  C CA  . ARG C 134 ? 2.6054 1.9572 2.4794 0.1058  -0.2834 0.2918  134 ARG C CA  
6994  C C   . ARG C 134 ? 2.6890 2.0206 2.5468 0.0917  -0.2675 0.3030  134 ARG C C   
6995  O O   . ARG C 134 ? 2.6618 1.9731 2.5282 0.0890  -0.2664 0.3059  134 ARG C O   
6996  C CB  . ARG C 134 ? 2.4846 1.8128 2.3326 0.1161  -0.3006 0.3027  134 ARG C CB  
6997  C CG  . ARG C 134 ? 2.4720 1.8126 2.3397 0.1313  -0.3192 0.2927  134 ARG C CG  
6998  C CD  . ARG C 134 ? 2.4175 1.7368 2.2571 0.1407  -0.3356 0.3038  134 ARG C CD  
6999  N NE  . ARG C 134 ? 2.4376 1.7642 2.2975 0.1556  -0.3545 0.2952  134 ARG C NE  
7000  C CZ  . ARG C 134 ? 2.4081 1.7247 2.2515 0.1661  -0.3713 0.3007  134 ARG C CZ  
7001  N NH1 . ARG C 134 ? 2.2112 1.5096 2.0160 0.1634  -0.3717 0.3147  134 ARG C NH1 
7002  N NH2 . ARG C 134 ? 2.4988 1.8240 2.3646 0.1794  -0.3877 0.2918  134 ARG C NH2 
7003  N N   . ARG C 135 ? 2.8444 2.1812 2.6794 0.0826  -0.2547 0.3092  135 ARG C N   
7004  C CA  . ARG C 135 ? 2.8696 2.1904 2.6907 0.0685  -0.2380 0.3192  135 ARG C CA  
7005  C C   . ARG C 135 ? 2.8623 2.2058 2.7136 0.0592  -0.2233 0.3076  135 ARG C C   
7006  O O   . ARG C 135 ? 2.8986 2.2262 2.7557 0.0513  -0.2155 0.3113  135 ARG C O   
7007  C CB  . ARG C 135 ? 2.9215 2.2403 2.7077 0.0622  -0.2291 0.3295  135 ARG C CB  
7008  C CG  . ARG C 135 ? 3.0091 2.3186 2.7841 0.0467  -0.2093 0.3377  135 ARG C CG  
7009  C CD  . ARG C 135 ? 3.1208 2.4254 2.8592 0.0412  -0.2011 0.3487  135 ARG C CD  
7010  N NE  . ARG C 135 ? 3.1391 2.4432 2.8723 0.0261  -0.1802 0.3535  135 ARG C NE  
7011  C CZ  . ARG C 135 ? 3.0858 2.4195 2.8295 0.0187  -0.1658 0.3452  135 ARG C CZ  
7012  N NH1 . ARG C 135 ? 2.9525 2.3181 2.7116 0.0248  -0.1698 0.3321  135 ARG C NH1 
7013  N NH2 . ARG C 135 ? 3.1494 2.4810 2.8887 0.0051  -0.1473 0.3502  135 ARG C NH2 
7014  N N   . TYR C 136 ? 2.6994 2.0801 2.5704 0.0600  -0.2195 0.2935  136 TYR C N   
7015  C CA  . TYR C 136 ? 2.6533 2.0574 2.5534 0.0519  -0.2064 0.2818  136 TYR C CA  
7016  C C   . TYR C 136 ? 2.6898 2.0896 2.6197 0.0561  -0.2132 0.2734  136 TYR C C   
7017  O O   . TYR C 136 ? 2.6559 2.0538 2.6006 0.0472  -0.2030 0.2711  136 TYR C O   
7018  C CB  . TYR C 136 ? 2.5880 2.0319 2.5018 0.0531  -0.2025 0.2688  136 TYR C CB  
7019  C CG  . TYR C 136 ? 2.5642 2.0154 2.4522 0.0469  -0.1925 0.2753  136 TYR C CG  
7020  C CD1 . TYR C 136 ? 2.6135 2.0439 2.4759 0.0364  -0.1807 0.2889  136 TYR C CD1 
7021  C CD2 . TYR C 136 ? 2.5073 1.9859 2.3965 0.0516  -0.1946 0.2677  136 TYR C CD2 
7022  C CE1 . TYR C 136 ? 2.6107 2.0478 2.4495 0.0309  -0.1711 0.2944  136 TYR C CE1 
7023  C CE2 . TYR C 136 ? 2.4836 1.9683 2.3493 0.0462  -0.1856 0.2732  136 TYR C CE2 
7024  C CZ  . TYR C 136 ? 2.5087 1.9727 2.3492 0.0361  -0.1738 0.2863  136 TYR C CZ  
7025  O OH  . TYR C 136 ? 2.4614 1.9317 2.2786 0.0310  -0.1644 0.2913  136 TYR C OH  
7026  N N   . GLY C 137 ? 3.0186 2.4173 2.9584 0.0696  -0.2305 0.2683  137 GLY C N   
7027  C CA  . GLY C 137 ? 3.0093 2.4075 2.9795 0.0746  -0.2371 0.2584  137 GLY C CA  
7028  C C   . GLY C 137 ? 2.9816 2.4179 2.9846 0.0736  -0.2311 0.2402  137 GLY C C   
7029  O O   . GLY C 137 ? 2.9634 2.4282 2.9680 0.0742  -0.2280 0.2338  137 GLY C O   
7030  N N   . GLY C 138 ? 2.5868 2.0230 2.6159 0.0719  -0.2294 0.2319  138 GLY C N   
7031  C CA  . GLY C 138 ? 2.4138 1.8846 2.4742 0.0714  -0.2243 0.2145  138 GLY C CA  
7032  C C   . GLY C 138 ? 2.3574 1.8485 2.4331 0.0851  -0.2378 0.2034  138 GLY C C   
7033  O O   . GLY C 138 ? 2.3687 1.8451 2.4356 0.0958  -0.2524 0.2079  138 GLY C O   
7034  N N   . ILE C 139 ? 2.2276 1.7536 2.3270 0.0845  -0.2325 0.1886  139 ILE C N   
7035  C CA  . ILE C 139 ? 2.2498 1.7987 2.3672 0.0965  -0.2434 0.1765  139 ILE C CA  
7036  C C   . ILE C 139 ? 2.3596 1.9192 2.4578 0.1003  -0.2469 0.1810  139 ILE C C   
7037  O O   . ILE C 139 ? 2.4155 1.9629 2.5033 0.1103  -0.2608 0.1857  139 ILE C O   
7038  C CB  . ILE C 139 ? 2.2301 1.8122 2.3786 0.0944  -0.2362 0.1593  139 ILE C CB  
7039  C CG1 . ILE C 139 ? 2.2304 1.8013 2.3975 0.0904  -0.2329 0.1545  139 ILE C CG1 
7040  C CG2 . ILE C 139 ? 2.4754 2.0807 2.6423 0.1069  -0.2473 0.1473  139 ILE C CG2 
7041  C CD1 . ILE C 139 ? 2.3304 1.8819 2.5085 0.1013  -0.2473 0.1522  139 ILE C CD1 
7042  N N   . GLY C 140 ? 2.5074 2.0890 2.6004 0.0922  -0.2345 0.1797  140 GLY C N   
7043  C CA  . GLY C 140 ? 2.6308 2.2273 2.7091 0.0951  -0.2365 0.1815  140 GLY C CA  
7044  C C   . GLY C 140 ? 2.6414 2.2274 2.6884 0.0861  -0.2269 0.1946  140 GLY C C   
7045  O O   . GLY C 140 ? 2.5746 2.1380 2.6084 0.0777  -0.2194 0.2044  140 GLY C O   
7046  N N   . THR C 141 ? 2.6911 2.2928 2.7257 0.0876  -0.2271 0.1951  141 THR C N   
7047  C CA  . THR C 141 ? 2.7133 2.3064 2.7177 0.0797  -0.2180 0.2068  141 THR C CA  
7048  C C   . THR C 141 ? 2.6662 2.2899 2.6706 0.0775  -0.2113 0.2009  141 THR C C   
7049  O O   . THR C 141 ? 2.6511 2.2730 2.6343 0.0698  -0.2010 0.2083  141 THR C O   
7050  C CB  . THR C 141 ? 2.7693 2.3328 2.7439 0.0854  -0.2294 0.2203  141 THR C CB  
7051  O OG1 . THR C 141 ? 2.7627 2.3178 2.7498 0.0974  -0.2462 0.2169  141 THR C OG1 
7052  C CG2 . THR C 141 ? 2.7155 2.2470 2.6672 0.0769  -0.2221 0.2348  141 THR C CG2 
7053  N N   . VAL C 144 ? 2.6805 2.3883 2.6281 0.0596  -0.1744 0.2000  144 VAL C N   
7054  C CA  . VAL C 144 ? 2.6767 2.4060 2.6265 0.0514  -0.1593 0.1966  144 VAL C CA  
7055  C C   . VAL C 144 ? 2.6997 2.4257 2.6206 0.0511  -0.1582 0.2031  144 VAL C C   
7056  O O   . VAL C 144 ? 2.7017 2.4060 2.5984 0.0557  -0.1674 0.2116  144 VAL C O   
7057  C CB  . VAL C 144 ? 2.6731 2.3968 2.6251 0.0400  -0.1437 0.2000  144 VAL C CB  
7058  C CG1 . VAL C 144 ? 2.6301 2.3644 2.6145 0.0395  -0.1432 0.1906  144 VAL C CG1 
7059  C CG2 . VAL C 144 ? 2.6885 2.3776 2.6133 0.0364  -0.1426 0.2145  144 VAL C CG2 
7060  N N   . ILE C 145 ? 2.5870 2.3352 2.5108 0.0458  -0.1468 0.1986  145 ILE C N   
7061  C CA  . ILE C 145 ? 2.5595 2.3073 2.4577 0.0446  -0.1437 0.2034  145 ILE C CA  
7062  C C   . ILE C 145 ? 2.4986 2.2636 2.4002 0.0349  -0.1259 0.2012  145 ILE C C   
7063  O O   . ILE C 145 ? 2.4674 2.2574 2.3957 0.0330  -0.1206 0.1913  145 ILE C O   
7064  C CB  . ILE C 145 ? 2.5334 2.2952 2.4334 0.0539  -0.1563 0.1972  145 ILE C CB  
7065  C CG1 . ILE C 145 ? 2.5472 2.3085 2.4206 0.0523  -0.1526 0.2017  145 ILE C CG1 
7066  C CG2 . ILE C 145 ? 2.4875 2.2814 2.4212 0.0559  -0.1561 0.1834  145 ILE C CG2 
7067  C CD1 . ILE C 145 ? 2.6935 2.4634 2.5644 0.0613  -0.1662 0.1972  145 ILE C CD1 
7068  N N   . LYS C 146 ? 2.5092 2.2608 2.3836 0.0289  -0.1165 0.2105  146 LYS C N   
7069  C CA  . LYS C 146 ? 2.4849 2.2507 2.3611 0.0195  -0.0990 0.2094  146 LYS C CA  
7070  C C   . LYS C 146 ? 2.4826 2.2756 2.3661 0.0217  -0.0980 0.2007  146 LYS C C   
7071  O O   . LYS C 146 ? 2.4450 2.2353 2.3097 0.0263  -0.1039 0.2026  146 LYS C O   
7072  C CB  . LYS C 146 ? 2.4139 2.1572 2.2580 0.0129  -0.0895 0.2218  146 LYS C CB  
7073  C CG  . LYS C 146 ? 2.3390 2.0547 2.1751 0.0093  -0.0887 0.2314  146 LYS C CG  
7074  C CD  . LYS C 146 ? 2.2044 1.8995 2.0086 0.0021  -0.0778 0.2437  146 LYS C CD  
7075  C CE  . LYS C 146 ? 2.1776 1.8450 1.9745 -0.0022 -0.0763 0.2535  146 LYS C CE  
7076  N NZ  . LYS C 146 ? 2.1767 1.8239 1.9422 -0.0097 -0.0647 0.2659  146 LYS C NZ  
7077  N N   . VAL C 147 ? 2.5282 2.3472 2.4390 0.0185  -0.0905 0.1913  147 VAL C N   
7078  C CA  . VAL C 147 ? 2.4910 2.3369 2.4114 0.0198  -0.0881 0.1829  147 VAL C CA  
7079  C C   . VAL C 147 ? 2.5955 2.4551 2.5219 0.0103  -0.0704 0.1817  147 VAL C C   
7080  O O   . VAL C 147 ? 2.6823 2.5344 2.6119 0.0032  -0.0612 0.1854  147 VAL C O   
7081  C CB  . VAL C 147 ? 2.4101 2.2776 2.3599 0.0264  -0.0976 0.1715  147 VAL C CB  
7082  C CG1 . VAL C 147 ? 2.3820 2.2358 2.3281 0.0358  -0.1151 0.1725  147 VAL C CG1 
7083  C CG2 . VAL C 147 ? 2.4392 2.3182 2.4167 0.0220  -0.0914 0.1657  147 VAL C CG2 
7084  N N   . SER C 148 ? 2.5437 2.4237 2.4725 0.0103  -0.0660 0.1765  148 SER C N   
7085  C CA  . SER C 148 ? 2.6353 2.5306 2.5712 0.0021  -0.0499 0.1746  148 SER C CA  
7086  C C   . SER C 148 ? 2.7180 2.6322 2.6865 -0.0006 -0.0463 0.1666  148 SER C C   
7087  O O   . SER C 148 ? 2.7012 2.6257 2.6893 0.0050  -0.0561 0.1594  148 SER C O   
7088  C CB  . SER C 148 ? 2.6365 2.5489 2.5677 0.0037  -0.0472 0.1706  148 SER C CB  
7089  O OG  . SER C 148 ? 2.6697 2.6029 2.6217 0.0099  -0.0562 0.1609  148 SER C OG  
7090  N N   . ALA C 149 ? 2.9051 2.8243 2.8794 -0.0094 -0.0319 0.1676  149 ALA C N   
7091  C CA  . ALA C 149 ? 2.9018 2.8393 2.9062 -0.0126 -0.0278 0.1599  149 ALA C CA  
7092  C C   . ALA C 149 ? 2.8809 2.8481 2.9050 -0.0093 -0.0291 0.1494  149 ALA C C   
7093  O O   . ALA C 149 ? 2.8498 2.8325 2.8992 -0.0084 -0.0315 0.1415  149 ALA C O   
7094  C CB  . ALA C 149 ? 2.9069 2.8435 2.9127 -0.0230 -0.0121 0.1634  149 ALA C CB  
7095  N N   . GLU C 150 ? 2.7803 2.7552 2.7928 -0.0076 -0.0275 0.1493  150 GLU C N   
7096  C CA  . GLU C 150 ? 2.7293 2.7307 2.7589 -0.0039 -0.0297 0.1400  150 GLU C CA  
7097  C C   . GLU C 150 ? 2.6962 2.7011 2.7362 0.0047  -0.0448 0.1347  150 GLU C C   
7098  O O   . GLU C 150 ? 2.6516 2.6787 2.7141 0.0070  -0.0471 0.1259  150 GLU C O   
7099  C CB  . GLU C 150 ? 2.7281 2.7341 2.7413 -0.0036 -0.0254 0.1415  150 GLU C CB  
7100  C CG  . GLU C 150 ? 2.6955 2.7281 2.7252 -0.0064 -0.0165 0.1349  150 GLU C CG  
7101  C CD  . GLU C 150 ? 2.6639 2.7185 2.7166 -0.0011 -0.0244 0.1253  150 GLU C CD  
7102  O OE1 . GLU C 150 ? 2.6678 2.7191 2.7175 0.0059  -0.0366 0.1239  150 GLU C OE1 
7103  O OE2 . GLU C 150 ? 2.6312 2.7066 2.7050 -0.0040 -0.0182 0.1194  150 GLU C OE2 
7104  N N   . ALA C 151 ? 2.7342 2.7176 2.7584 0.0095  -0.0551 0.1399  151 ALA C N   
7105  C CA  . ALA C 151 ? 2.7261 2.7108 2.7602 0.0178  -0.0699 0.1353  151 ALA C CA  
7106  C C   . ALA C 151 ? 2.6985 2.6795 2.7504 0.0172  -0.0722 0.1330  151 ALA C C   
7107  O O   . ALA C 151 ? 2.6925 2.6522 2.7366 0.0196  -0.0792 0.1378  151 ALA C O   
7108  C CB  . ALA C 151 ? 2.6789 2.6424 2.6886 0.0236  -0.0805 0.1417  151 ALA C CB  
7109  N N   . ALA C 152 ? 2.7669 2.7692 2.8433 0.0142  -0.0663 0.1253  152 ALA C N   
7110  C CA  . ALA C 152 ? 2.7255 2.7275 2.8209 0.0130  -0.0673 0.1217  152 ALA C CA  
7111  C C   . ALA C 152 ? 2.7928 2.8182 2.9150 0.0174  -0.0726 0.1105  152 ALA C C   
7112  O O   . ALA C 152 ? 2.8032 2.8267 2.9403 0.0187  -0.0766 0.1066  152 ALA C O   
7113  C CB  . ALA C 152 ? 2.7276 2.7300 2.8272 0.0033  -0.0535 0.1236  152 ALA C CB  
7114  N N   . SER C 153 ? 2.6522 2.6992 2.7807 0.0197  -0.0725 0.1051  153 SER C N   
7115  C CA  . SER C 153 ? 2.6598 2.7290 2.8127 0.0241  -0.0775 0.0948  153 SER C CA  
7116  C C   . SER C 153 ? 2.6923 2.7546 2.8475 0.0329  -0.0919 0.0928  153 SER C C   
7117  O O   . SER C 153 ? 2.6376 2.7118 2.8134 0.0364  -0.0966 0.0849  153 SER C O   
7118  C CB  . SER C 153 ? 2.6653 2.7581 2.8230 0.0241  -0.0736 0.0905  153 SER C CB  
7119  O OG  . SER C 153 ? 2.6862 2.7727 2.8258 0.0279  -0.0784 0.0945  153 SER C OG  
7120  N N   . GLN C 154 ? 2.9224 2.9659 3.0568 0.0367  -0.0989 0.0996  154 GLN C N   
7121  C CA  . GLN C 154 ? 2.9187 2.9554 3.0551 0.0454  -0.1132 0.0979  154 GLN C CA  
7122  C C   . GLN C 154 ? 2.9217 2.9466 3.0686 0.0468  -0.1175 0.0968  154 GLN C C   
7123  O O   . GLN C 154 ? 2.9413 2.9733 3.1047 0.0532  -0.1263 0.0901  154 GLN C O   
7124  C CB  . GLN C 154 ? 2.9152 2.9322 3.0254 0.0487  -0.1197 0.1062  154 GLN C CB  
7125  C CG  . GLN C 154 ? 2.9150 2.9118 3.0010 0.0422  -0.1114 0.1164  154 GLN C CG  
7126  C CD  . GLN C 154 ? 2.9243 2.9311 2.9995 0.0377  -0.1020 0.1179  154 GLN C CD  
7127  O OE1 . GLN C 154 ? 2.9178 2.9409 3.0041 0.0320  -0.0910 0.1145  154 GLN C OE1 
7128  N NE2 . GLN C 154 ? 2.9170 2.9143 2.9707 0.0406  -0.1066 0.1227  154 GLN C NE2 
7129  N N   . PHE C 155 ? 2.7258 2.7323 2.8634 0.0410  -0.1114 0.1032  155 PHE C N   
7130  C CA  . PHE C 155 ? 2.6141 2.6075 2.7610 0.0419  -0.1153 0.1026  155 PHE C CA  
7131  C C   . PHE C 155 ? 2.5966 2.5977 2.7580 0.0341  -0.1043 0.0992  155 PHE C C   
7132  O O   . PHE C 155 ? 2.5087 2.5285 2.6932 0.0351  -0.1043 0.0895  155 PHE C O   
7133  C CB  . PHE C 155 ? 2.5194 2.4805 2.6433 0.0426  -0.1199 0.1134  155 PHE C CB  
7134  C CG  . PHE C 155 ? 2.4646 2.4089 2.5946 0.0407  -0.1202 0.1149  155 PHE C CG  
7135  C CD1 . PHE C 155 ? 2.4483 2.3959 2.5986 0.0464  -0.1285 0.1073  155 PHE C CD1 
7136  C CD2 . PHE C 155 ? 2.5162 2.4413 2.6321 0.0329  -0.1118 0.1236  155 PHE C CD2 
7137  C CE1 . PHE C 155 ? 2.5037 2.4352 2.6599 0.0446  -0.1287 0.1083  155 PHE C CE1 
7138  C CE2 . PHE C 155 ? 2.5549 2.4640 2.6768 0.0307  -0.1119 0.1249  155 PHE C CE2 
7139  C CZ  . PHE C 155 ? 2.5754 2.4874 2.7175 0.0366  -0.1206 0.1172  155 PHE C CZ  
7140  N N   . GLY C 156 ? 2.7404 2.7276 2.8886 0.0263  -0.0950 0.1068  156 GLY C N   
7141  C CA  . GLY C 156 ? 2.8364 2.8270 2.9975 0.0186  -0.0854 0.1045  156 GLY C CA  
7142  C C   . GLY C 156 ? 2.8960 2.8599 3.0395 0.0123  -0.0801 0.1151  156 GLY C C   
7143  O O   . GLY C 156 ? 2.8974 2.8491 3.0178 0.0104  -0.0771 0.1240  156 GLY C O   
7144  N N   . GLU C 157 ? 3.0924 3.0470 3.2468 0.0092  -0.0790 0.1139  157 GLU C N   
7145  C CA  . GLU C 157 ? 3.1288 3.0599 3.2706 0.0019  -0.0726 0.1232  157 GLU C CA  
7146  C C   . GLU C 157 ? 3.1044 3.0077 3.2386 0.0066  -0.0829 0.1282  157 GLU C C   
7147  O O   . GLU C 157 ? 3.0472 2.9526 3.1960 0.0136  -0.0930 0.1215  157 GLU C O   
7148  C CB  . GLU C 157 ? 3.1452 3.0855 3.3051 -0.0067 -0.0625 0.1186  157 GLU C CB  
7149  N N   . LEU C 158 ? 3.0557 2.9331 3.1669 0.0029  -0.0802 0.1401  158 LEU C N   
7150  C CA  . LEU C 158 ? 3.0920 2.9401 3.1937 0.0062  -0.0889 0.1468  158 LEU C CA  
7151  C C   . LEU C 158 ? 3.2801 3.1052 3.3633 -0.0029 -0.0793 0.1585  158 LEU C C   
7152  O O   . LEU C 158 ? 3.2016 3.0232 3.2638 -0.0063 -0.0728 0.1660  158 LEU C O   
7153  C CB  . LEU C 158 ? 2.8301 2.6688 2.9160 0.0163  -0.1019 0.1503  158 LEU C CB  
7154  N N   . ILE C 159 ? 3.5736 3.3832 3.6646 -0.0069 -0.0783 0.1599  159 ILE C N   
7155  C CA  . ILE C 159 ? 3.5914 3.3798 3.6683 -0.0166 -0.0682 0.1705  159 ILE C CA  
7156  C C   . ILE C 159 ? 3.6140 3.3685 3.6757 -0.0131 -0.0773 0.1798  159 ILE C C   
7157  O O   . ILE C 159 ? 3.6152 3.3634 3.6906 -0.0073 -0.0875 0.1751  159 ILE C O   
7158  C CB  . ILE C 159 ? 3.5846 3.3826 3.6836 -0.0258 -0.0580 0.1649  159 ILE C CB  
7159  C CG1 . ILE C 159 ? 3.5573 3.3903 3.6739 -0.0279 -0.0511 0.1545  159 ILE C CG1 
7160  C CG2 . ILE C 159 ? 3.5993 3.3776 3.6840 -0.0367 -0.0463 0.1760  159 ILE C CG2 
7161  C CD1 . ILE C 159 ? 3.5540 3.3954 3.6545 -0.0328 -0.0404 0.1598  159 ILE C CD1 
7162  N N   . ALA C 160 ? 3.1858 2.9184 3.2190 -0.0164 -0.0735 0.1930  160 ALA C N   
7163  C CA  . ALA C 160 ? 3.0010 2.6995 3.0162 -0.0137 -0.0814 0.2036  160 ALA C CA  
7164  C C   . ALA C 160 ? 2.8028 2.4802 2.7952 -0.0238 -0.0695 0.2169  160 ALA C C   
7165  O O   . ALA C 160 ? 2.7374 2.4203 2.7125 -0.0275 -0.0611 0.2215  160 ALA C O   
7166  C CB  . ALA C 160 ? 2.9219 2.6134 2.9204 -0.0024 -0.0955 0.2064  160 ALA C CB  
7167  N N   . ASP C 161 ? 2.8316 2.4851 2.8243 -0.0284 -0.0686 0.2228  161 ASP C N   
7168  C CA  . ASP C 161 ? 2.7547 2.3859 2.7269 -0.0384 -0.0573 0.2360  161 ASP C CA  
7169  C C   . ASP C 161 ? 2.7293 2.3340 2.6669 -0.0336 -0.0641 0.2491  161 ASP C C   
7170  O O   . ASP C 161 ? 2.7527 2.3361 2.6850 -0.0264 -0.0773 0.2528  161 ASP C O   
7171  C CB  . ASP C 161 ? 2.7339 2.3481 2.7195 -0.0450 -0.0546 0.2376  161 ASP C CB  
7172  N N   . PRO C 162 ? 2.5221 2.1273 2.4357 -0.0373 -0.0556 0.2562  162 PRO C N   
7173  C CA  . PRO C 162 ? 2.4588 2.0421 2.3386 -0.0317 -0.0631 0.2674  162 PRO C CA  
7174  C C   . PRO C 162 ? 2.5195 2.0648 2.3789 -0.0345 -0.0646 0.2816  162 PRO C C   
7175  O O   . PRO C 162 ? 2.5024 2.0269 2.3341 -0.0287 -0.0732 0.2910  162 PRO C O   
7176  C CB  . PRO C 162 ? 2.2763 1.8717 2.1382 -0.0368 -0.0506 0.2703  162 PRO C CB  
7177  C CG  . PRO C 162 ? 2.2464 1.8561 2.1262 -0.0487 -0.0337 0.2669  162 PRO C CG  
7178  C CD  . PRO C 162 ? 2.3794 2.0047 2.2954 -0.0469 -0.0386 0.2545  162 PRO C CD  
7179  N N   . ASP C 163 ? 2.5182 2.0535 2.3900 -0.0431 -0.0569 0.2836  163 ASP C N   
7180  C CA  . ASP C 163 ? 2.5970 2.0953 2.4499 -0.0463 -0.0578 0.2976  163 ASP C CA  
7181  C C   . ASP C 163 ? 2.6716 2.1518 2.5283 -0.0355 -0.0765 0.2975  163 ASP C C   
7182  O O   . ASP C 163 ? 2.6726 2.1262 2.5028 -0.0304 -0.0854 0.3086  163 ASP C O   
7183  C CB  . ASP C 163 ? 2.6146 2.1085 2.4814 -0.0593 -0.0436 0.2993  163 ASP C CB  
7184  C CG  . ASP C 163 ? 2.6293 2.1165 2.4737 -0.0707 -0.0264 0.3101  163 ASP C CG  
7185  O OD1 . ASP C 163 ? 2.6403 2.1211 2.4550 -0.0682 -0.0263 0.3178  163 ASP C OD1 
7186  O OD2 . ASP C 163 ? 2.6406 2.1294 2.4976 -0.0822 -0.0129 0.3106  163 ASP C OD2 
7187  N N   . THR C 164 ? 2.8540 2.3485 2.7433 -0.0316 -0.0829 0.2848  164 THR C N   
7188  C CA  . THR C 164 ? 2.8583 2.3398 2.7553 -0.0205 -0.1007 0.2824  164 THR C CA  
7189  C C   . THR C 164 ? 2.8404 2.3444 2.7460 -0.0082 -0.1132 0.2718  164 THR C C   
7190  O O   . THR C 164 ? 2.8310 2.3276 2.7444 0.0022  -0.1286 0.2687  164 THR C O   
7191  C CB  . THR C 164 ? 2.8582 2.3386 2.7856 -0.0234 -0.1007 0.2751  164 THR C CB  
7192  O OG1 . THR C 164 ? 2.8544 2.3699 2.8110 -0.0261 -0.0940 0.2601  164 THR C OG1 
7193  C CG2 . THR C 164 ? 2.8614 2.3167 2.7806 -0.0354 -0.0895 0.2862  164 THR C CG2 
7194  N N   . LYS C 165 ? 2.6418 2.1729 2.5465 -0.0092 -0.1068 0.2664  165 LYS C N   
7195  C CA  . LYS C 165 ? 2.5578 2.1130 2.4719 0.0012  -0.1169 0.2559  165 LYS C CA  
7196  C C   . LYS C 165 ? 2.5933 2.1647 2.5427 0.0068  -0.1245 0.2417  165 LYS C C   
7197  O O   . LYS C 165 ? 2.5464 2.1223 2.5030 0.0181  -0.1389 0.2360  165 LYS C O   
7198  C CB  . LYS C 165 ? 2.4702 2.0075 2.3585 0.0113  -0.1312 0.2636  165 LYS C CB  
7199  C CG  . LYS C 165 ? 2.4357 1.9531 2.2863 0.0063  -0.1248 0.2785  165 LYS C CG  
7200  C CD  . LYS C 165 ? 2.3157 1.8564 2.1571 0.0039  -0.1162 0.2756  165 LYS C CD  
7201  C CE  . LYS C 165 ? 2.2088 1.7611 2.0466 0.0158  -0.1304 0.2704  165 LYS C CE  
7202  N NZ  . LYS C 165 ? 2.1559 1.6815 1.9586 0.0208  -0.1395 0.2829  165 LYS C NZ  
7203  N N   . GLU C 166 ? 2.7037 2.2845 2.6755 -0.0014 -0.1144 0.2356  166 GLU C N   
7204  C CA  . GLU C 166 ? 2.7448 2.3395 2.7499 0.0024  -0.1199 0.2223  166 GLU C CA  
7205  C C   . GLU C 166 ? 2.9104 2.5430 2.9375 -0.0003 -0.1120 0.2090  166 GLU C C   
7206  O O   . GLU C 166 ? 2.8607 2.5041 2.8852 -0.0100 -0.0977 0.2103  166 GLU C O   
7207  C CB  . GLU C 166 ? 2.6978 2.2727 2.7129 -0.0045 -0.1159 0.2248  166 GLU C CB  
7208  C CG  . GLU C 166 ? 2.6694 2.2441 2.7107 0.0028  -0.1271 0.2147  166 GLU C CG  
7209  C CD  . GLU C 166 ? 2.7484 2.3515 2.8217 -0.0012 -0.1206 0.1997  166 GLU C CD  
7210  O OE1 . GLU C 166 ? 2.7453 2.3503 2.8242 -0.0128 -0.1074 0.2004  166 GLU C OE1 
7211  O OE2 . GLU C 166 ? 2.8107 2.4342 2.9038 0.0073  -0.1287 0.1872  166 GLU C OE2 
7212  N N   . LEU C 167 ? 3.6764 3.3290 3.7252 0.0085  -0.1213 0.1963  167 LEU C N   
7213  C CA  . LEU C 167 ? 3.6551 3.3440 3.7249 0.0074  -0.1156 0.1834  167 LEU C CA  
7214  C C   . LEU C 167 ? 3.6537 3.3515 3.7461 -0.0018 -0.1053 0.1768  167 LEU C C   
7215  O O   . LEU C 167 ? 3.6512 3.3451 3.7630 0.0005  -0.1107 0.1703  167 LEU C O   
7216  C CB  . LEU C 167 ? 3.6349 3.3405 3.7209 0.0195  -0.1289 0.1724  167 LEU C CB  
7217  C CG  . LEU C 167 ? 3.6069 3.3501 3.7151 0.0200  -0.1249 0.1586  167 LEU C CG  
7218  C CD1 . LEU C 167 ? 3.5900 3.3475 3.6926 0.0292  -0.1334 0.1559  167 LEU C CD1 
7219  C CD2 . LEU C 167 ? 3.5927 3.3464 3.7312 0.0221  -0.1281 0.1461  167 LEU C CD2 
7220  N N   . LEU C 168 ? 3.1532 2.8633 3.2436 -0.0120 -0.0906 0.1781  168 LEU C N   
7221  C CA  . LEU C 168 ? 2.9350 2.6540 3.0459 -0.0216 -0.0802 0.1725  168 LEU C CA  
7222  C C   . LEU C 168 ? 2.8641 2.6170 3.0030 -0.0196 -0.0799 0.1567  168 LEU C C   
7223  O O   . LEU C 168 ? 2.6345 2.3933 2.7948 -0.0243 -0.0764 0.1493  168 LEU C O   
7224  C CB  . LEU C 168 ? 2.6986 2.4163 2.7964 -0.0336 -0.0644 0.1807  168 LEU C CB  
7225  C CG  . LEU C 168 ? 2.3083 1.9973 2.3974 -0.0427 -0.0581 0.1912  168 LEU C CG  
7226  C CD1 . LEU C 168 ? 1.9447 1.6363 2.0612 -0.0474 -0.0564 0.1827  168 LEU C CD1 
7227  C CD2 . LEU C 168 ? 2.3722 2.0276 2.4390 -0.0368 -0.0683 0.2025  168 LEU C CD2 
7228  N N   . HIS C 169 ? 2.8465 2.6214 2.9856 -0.0130 -0.0836 0.1513  169 HIS C N   
7229  C CA  . HIS C 169 ? 2.8139 2.6217 2.9777 -0.0113 -0.0827 0.1371  169 HIS C CA  
7230  C C   . HIS C 169 ? 2.8456 2.6689 3.0057 -0.0014 -0.0909 0.1335  169 HIS C C   
7231  O O   . HIS C 169 ? 2.9442 2.7595 3.0816 0.0007  -0.0922 0.1420  169 HIS C O   
7232  C CB  . HIS C 169 ? 2.7281 2.5549 2.8981 -0.0220 -0.0677 0.1352  169 HIS C CB  
7233  C CG  . HIS C 169 ? 2.6500 2.5117 2.8385 -0.0199 -0.0662 0.1229  169 HIS C CG  
7234  N ND1 . HIS C 169 ? 2.6922 2.5718 2.8723 -0.0186 -0.0630 0.1233  169 HIS C ND1 
7235  C CD2 . HIS C 169 ? 2.5799 2.4614 2.7943 -0.0190 -0.0675 0.1101  169 HIS C CD2 
7236  C CE1 . HIS C 169 ? 2.6075 2.5161 2.8075 -0.0169 -0.0624 0.1117  169 HIS C CE1 
7237  N NE2 . HIS C 169 ? 2.5371 2.4476 2.7578 -0.0171 -0.0651 0.1036  169 HIS C NE2 
7238  N N   . TYR C 170 ? 2.6981 2.5438 2.8805 0.0044  -0.0962 0.1207  170 TYR C N   
7239  C CA  . TYR C 170 ? 2.5829 2.4445 2.7652 0.0139  -0.1044 0.1162  170 TYR C CA  
7240  C C   . TYR C 170 ? 2.4845 2.3783 2.6923 0.0155  -0.1033 0.1020  170 TYR C C   
7241  O O   . TYR C 170 ? 2.4224 2.3195 2.6502 0.0172  -0.1066 0.0933  170 TYR C O   
7242  C CB  . TYR C 170 ? 2.5867 2.4302 2.7644 0.0245  -0.1193 0.1180  170 TYR C CB  
7243  C CG  . TYR C 170 ? 2.5309 2.3939 2.7153 0.0344  -0.1284 0.1107  170 TYR C CG  
7244  C CD1 . TYR C 170 ? 2.5418 2.4160 2.7128 0.0355  -0.1271 0.1136  170 TYR C CD1 
7245  C CD2 . TYR C 170 ? 2.4491 2.3198 2.6541 0.0425  -0.1378 0.1005  170 TYR C CD2 
7246  C CE1 . TYR C 170 ? 2.4845 2.3766 2.6624 0.0441  -0.1351 0.1070  170 TYR C CE1 
7247  C CE2 . TYR C 170 ? 2.4929 2.3822 2.7050 0.0512  -0.1455 0.0938  170 TYR C CE2 
7248  C CZ  . TYR C 170 ? 2.4980 2.3979 2.6966 0.0517  -0.1441 0.0972  170 TYR C CZ  
7249  O OH  . TYR C 170 ? 2.5216 2.4399 2.7277 0.0599  -0.1516 0.0908  170 TYR C OH  
7250  N N   . THR C 171 ? 2.6310 2.5478 2.8375 0.0149  -0.0986 0.0996  171 THR C N   
7251  C CA  . THR C 171 ? 2.6328 2.5807 2.8604 0.0176  -0.0986 0.0871  171 THR C CA  
7252  C C   . THR C 171 ? 2.8001 2.7592 3.0206 0.0254  -0.1050 0.0867  171 THR C C   
7253  O O   . THR C 171 ? 2.7930 2.7487 2.9942 0.0237  -0.1020 0.0946  171 THR C O   
7254  C CB  . THR C 171 ? 2.5409 2.5086 2.7768 0.0083  -0.0855 0.0839  171 THR C CB  
7255  O OG1 . THR C 171 ? 2.6894 2.6490 2.9049 0.0019  -0.0770 0.0943  171 THR C OG1 
7256  C CG2 . THR C 171 ? 2.3512 2.3157 2.6031 0.0023  -0.0813 0.0793  171 THR C CG2 
7257  N N   . GLU C 172 ? 3.2367 3.2091 3.4729 0.0337  -0.1139 0.0774  172 GLU C N   
7258  C CA  . GLU C 172 ? 3.2066 3.1881 3.4377 0.0417  -0.1215 0.0768  172 GLU C CA  
7259  C C   . GLU C 172 ? 3.1841 3.1882 3.4125 0.0381  -0.1136 0.0759  172 GLU C C   
7260  O O   . GLU C 172 ? 3.1947 3.1933 3.4037 0.0379  -0.1130 0.0835  172 GLU C O   
7261  C CB  . GLU C 172 ? 3.1686 3.1619 3.4201 0.0506  -0.1313 0.0661  172 GLU C CB  
7262  C CG  . GLU C 172 ? 3.1654 3.1646 3.4386 0.0487  -0.1290 0.0570  172 GLU C CG  
7263  C CD  . GLU C 172 ? 3.1357 3.1625 3.4228 0.0429  -0.1192 0.0493  172 GLU C CD  
7264  O OE1 . GLU C 172 ? 3.0924 3.1412 3.3825 0.0453  -0.1187 0.0456  172 GLU C OE1 
7265  O OE2 . GLU C 172 ? 3.1509 3.1772 3.4457 0.0360  -0.1121 0.0471  172 GLU C OE2 
7266  N N   . LYS C 173 ? 2.7380 2.7673 2.9852 0.0354  -0.1077 0.0666  173 LYS C N   
7267  C CA  . LYS C 173 ? 2.5530 2.6050 2.7997 0.0331  -0.1013 0.0650  173 LYS C CA  
7268  C C   . LYS C 173 ? 2.5358 2.5949 2.7836 0.0229  -0.0880 0.0661  173 LYS C C   
7269  O O   . LYS C 173 ? 2.5430 2.6045 2.7775 0.0190  -0.0814 0.0718  173 LYS C O   
7270  C CB  . LYS C 173 ? 2.3548 2.4330 2.6208 0.0389  -0.1055 0.0539  173 LYS C CB  
7271  C CG  . LYS C 173 ? 2.1675 2.2557 2.4260 0.0438  -0.1096 0.0550  173 LYS C CG  
7272  C CD  . LYS C 173 ? 2.1296 2.1952 2.3711 0.0496  -0.1194 0.0624  173 LYS C CD  
7273  C CE  . LYS C 173 ? 2.1003 2.1727 2.3297 0.0524  -0.1216 0.0654  173 LYS C CE  
7274  N NZ  . LYS C 173 ? 2.2554 2.3289 2.4703 0.0449  -0.1109 0.0715  173 LYS C NZ  
7275  N N   . PRO C 174 ? 2.5246 2.5877 2.7883 0.0185  -0.0838 0.0606  174 PRO C N   
7276  C CA  . PRO C 174 ? 2.5648 2.6336 2.8293 0.0086  -0.0715 0.0622  174 PRO C CA  
7277  C C   . PRO C 174 ? 2.8769 2.9208 3.1213 0.0028  -0.0665 0.0740  174 PRO C C   
7278  O O   . PRO C 174 ? 2.7707 2.7949 3.0145 0.0003  -0.0671 0.0769  174 PRO C O   
7279  C CB  . PRO C 174 ? 2.3530 2.4283 2.6388 0.0061  -0.0705 0.0534  174 PRO C CB  
7280  C CG  . PRO C 174 ? 2.3307 2.4129 2.6291 0.0152  -0.0809 0.0450  174 PRO C CG  
7281  C CD  . PRO C 174 ? 2.4917 2.5563 2.7743 0.0221  -0.0897 0.0518  174 PRO C CD  
7282  N N   . GLU C 175 ? 3.8978 3.9422 4.1255 0.0006  -0.0613 0.0809  175 GLU C N   
7283  C CA  . GLU C 175 ? 3.9424 3.9625 4.1483 -0.0041 -0.0569 0.0926  175 GLU C CA  
7284  C C   . GLU C 175 ? 3.9573 3.9743 4.1681 -0.0144 -0.0457 0.0944  175 GLU C C   
7285  O O   . GLU C 175 ? 3.9753 3.9707 4.1827 -0.0175 -0.0458 0.0990  175 GLU C O   
7286  C CB  . GLU C 175 ? 3.9404 3.9628 4.1271 -0.0035 -0.0541 0.0986  175 GLU C CB  
7287  C CG  . GLU C 175 ? 3.9172 3.9674 4.1127 -0.0061 -0.0465 0.0934  175 GLU C CG  
7288  C CD  . GLU C 175 ? 3.9227 3.9734 4.0989 -0.0053 -0.0440 0.0992  175 GLU C CD  
7289  O OE1 . GLU C 175 ? 3.9410 3.9696 4.0955 -0.0040 -0.0467 0.1079  175 GLU C OE1 
7290  O OE2 . GLU C 175 ? 3.9499 4.0224 4.1322 -0.0059 -0.0394 0.0951  175 GLU C OE2 
7291  N N   . THR C 176 ? 3.2444 3.2831 3.4646 -0.0198 -0.0363 0.0906  176 THR C N   
7292  C CA  . THR C 176 ? 3.0183 3.0572 3.2436 -0.0299 -0.0248 0.0922  176 THR C CA  
7293  C C   . THR C 176 ? 3.1060 3.1179 3.3099 -0.0350 -0.0199 0.1044  176 THR C C   
7294  O O   . THR C 176 ? 3.0484 3.0409 3.2523 -0.0384 -0.0202 0.1077  176 THR C O   
7295  C CB  . THR C 176 ? 2.7353 2.7782 2.9829 -0.0320 -0.0263 0.0840  176 THR C CB  
7296  O OG1 . THR C 176 ? 2.6535 2.7127 2.9157 -0.0243 -0.0350 0.0740  176 THR C OG1 
7297  C CG2 . THR C 176 ? 2.4989 2.5577 2.7597 -0.0412 -0.0150 0.0809  176 THR C CG2 
7298  N N   . PHE C 177 ? 3.1773 3.1880 3.3624 -0.0353 -0.0156 0.1111  177 PHE C N   
7299  C CA  . PHE C 177 ? 3.1629 3.1497 3.3238 -0.0393 -0.0107 0.1232  177 PHE C CA  
7300  C C   . PHE C 177 ? 3.1868 3.1483 3.3314 -0.0326 -0.0219 0.1290  177 PHE C C   
7301  O O   . PHE C 177 ? 3.2030 3.1560 3.3574 -0.0293 -0.0302 0.1259  177 PHE C O   
7302  C CB  . PHE C 177 ? 3.1466 3.1245 3.3116 -0.0497 -0.0001 0.1268  177 PHE C CB  
7303  C CG  . PHE C 177 ? 3.1925 3.1424 3.3331 -0.0538 0.0041  0.1395  177 PHE C CG  
7304  C CD1 . PHE C 177 ? 3.2220 3.1707 3.3435 -0.0569 0.0127  0.1465  177 PHE C CD1 
7305  C CD2 . PHE C 177 ? 3.2147 3.1389 3.3509 -0.0546 -0.0003 0.1445  177 PHE C CD2 
7306  C CE1 . PHE C 177 ? 3.2675 3.1904 3.3654 -0.0607 0.0170  0.1583  177 PHE C CE1 
7307  C CE2 . PHE C 177 ? 3.2724 3.1702 3.3851 -0.0585 0.0037  0.1567  177 PHE C CE2 
7308  C CZ  . PHE C 177 ? 3.2899 3.1872 3.3831 -0.0617 0.0125  0.1637  177 PHE C CZ  
7309  N N   . VAL C 178 ? 3.1141 3.0633 3.2338 -0.0304 -0.0226 0.1373  178 VAL C N   
7310  C CA  . VAL C 178 ? 3.0788 3.0057 3.1815 -0.0232 -0.0342 0.1429  178 VAL C CA  
7311  C C   . VAL C 178 ? 3.0819 2.9802 3.1595 -0.0281 -0.0294 0.1558  178 VAL C C   
7312  O O   . VAL C 178 ? 3.1113 3.0070 3.1876 -0.0374 -0.0170 0.1597  178 VAL C O   
7313  C CB  . VAL C 178 ? 3.0301 2.9669 3.1243 -0.0149 -0.0417 0.1409  178 VAL C CB  
7314  C CG1 . VAL C 178 ? 3.1373 3.1027 3.2563 -0.0106 -0.0455 0.1286  178 VAL C CG1 
7315  C CG2 . VAL C 178 ? 2.9775 2.9166 3.0526 -0.0185 -0.0325 0.1466  178 VAL C CG2 
7316  N N   . SER C 179 ? 3.0202 2.8970 3.0776 -0.0219 -0.0392 0.1626  179 SER C N   
7317  C CA  . SER C 179 ? 3.0116 2.8598 3.0423 -0.0258 -0.0357 0.1755  179 SER C CA  
7318  C C   . SER C 179 ? 3.0328 2.8695 3.0365 -0.0193 -0.0428 0.1819  179 SER C C   
7319  O O   . SER C 179 ? 3.0479 2.8576 3.0280 -0.0198 -0.0444 0.1926  179 SER C O   
7320  C CB  . SER C 179 ? 3.0373 2.8613 3.0701 -0.0264 -0.0408 0.1796  179 SER C CB  
7321  O OG  . SER C 179 ? 3.0167 2.8139 3.0253 -0.0322 -0.0349 0.1924  179 SER C OG  
7322  N N   . ASP C 180 ? 3.1112 2.9674 3.1180 -0.0131 -0.0476 0.1755  180 ASP C N   
7323  C CA  . ASP C 180 ? 3.0758 2.9262 3.0600 -0.0067 -0.0547 0.1793  180 ASP C CA  
7324  C C   . ASP C 180 ? 3.0479 2.8812 3.0262 0.0025  -0.0714 0.1812  180 ASP C C   
7325  O O   . ASP C 180 ? 3.0239 2.8531 2.9857 0.0089  -0.0796 0.1833  180 ASP C O   
7326  C CB  . ASP C 180 ? 3.0938 2.9287 3.0482 -0.0124 -0.0450 0.1901  180 ASP C CB  
7327  C CG  . ASP C 180 ? 3.0760 2.8783 3.0029 -0.0097 -0.0524 0.2014  180 ASP C CG  
7328  O OD1 . ASP C 180 ? 3.0669 2.8635 2.9769 -0.0025 -0.0622 0.2034  180 ASP C OD1 
7329  O OD2 . ASP C 180 ? 3.0886 2.8707 3.0103 -0.0149 -0.0485 0.2086  180 ASP C OD2 
7330  N N   . LEU C 181 ? 2.8452 2.6699 2.8379 0.0039  -0.0772 0.1795  181 LEU C N   
7331  C CA  . LEU C 181 ? 2.6885 2.4978 2.6783 0.0131  -0.0931 0.1806  181 LEU C CA  
7332  C C   . LEU C 181 ? 2.5211 2.3522 2.5392 0.0202  -0.1020 0.1680  181 LEU C C   
7333  O O   . LEU C 181 ? 2.5519 2.4032 2.5941 0.0167  -0.0959 0.1594  181 LEU C O   
7334  C CB  . LEU C 181 ? 2.7506 2.5316 2.7350 0.0107  -0.0945 0.1883  181 LEU C CB  
7335  C CG  . LEU C 181 ? 2.7917 2.5440 2.7432 0.0065  -0.0905 0.2027  181 LEU C CG  
7336  C CD1 . LEU C 181 ? 2.8202 2.5445 2.7688 0.0053  -0.0940 0.2097  181 LEU C CD1 
7337  C CD2 . LEU C 181 ? 2.6923 2.4368 2.6193 0.0139  -0.1001 0.2073  181 LEU C CD2 
7338  N N   . ILE C 182 ? 2.4438 2.2708 2.4586 0.0301  -0.1166 0.1670  182 ILE C N   
7339  C CA  . ILE C 182 ? 2.3141 2.1618 2.3535 0.0377  -0.1257 0.1554  182 ILE C CA  
7340  C C   . ILE C 182 ? 2.3008 2.1308 2.3382 0.0470  -0.1417 0.1571  182 ILE C C   
7341  O O   . ILE C 182 ? 2.3710 2.1755 2.3845 0.0489  -0.1471 0.1672  182 ILE C O   
7342  C CB  . ILE C 182 ? 2.2570 2.1284 2.2971 0.0406  -0.1262 0.1499  182 ILE C CB  
7343  C CG1 . ILE C 182 ? 2.2752 2.1313 2.2853 0.0435  -0.1311 0.1586  182 ILE C CG1 
7344  C CG2 . ILE C 182 ? 2.2621 2.1549 2.3104 0.0325  -0.1114 0.1460  182 ILE C CG2 
7345  C CD1 . ILE C 182 ? 2.2229 2.0953 2.2355 0.0510  -0.1401 0.1529  182 ILE C CD1 
7346  N N   . ASN C 183 ? 2.2332 2.0769 2.2962 0.0530  -0.1492 0.1469  183 ASN C N   
7347  C CA  . ASN C 183 ? 2.2554 2.0863 2.3202 0.0630  -0.1650 0.1469  183 ASN C CA  
7348  C C   . ASN C 183 ? 2.3492 2.1809 2.3993 0.0701  -0.1749 0.1489  183 ASN C C   
7349  O O   . ASN C 183 ? 2.3154 2.1648 2.3621 0.0687  -0.1706 0.1465  183 ASN C O   
7350  C CB  . ASN C 183 ? 2.2335 2.0820 2.3303 0.0679  -0.1699 0.1344  183 ASN C CB  
7351  C CG  . ASN C 183 ? 2.2413 2.0909 2.3542 0.0610  -0.1606 0.1309  183 ASN C CG  
7352  O OD1 . ASN C 183 ? 2.2196 2.0865 2.3400 0.0535  -0.1484 0.1273  183 ASN C OD1 
7353  N ND2 . ASN C 183 ? 2.2375 2.0684 2.3561 0.0635  -0.1666 0.1319  183 ASN C ND2 
7354  N N   . CYS C 184 ? 2.7556 2.5675 2.7972 0.0781  -0.1888 0.1533  184 CYS C N   
7355  C CA  . CYS C 184 ? 2.7422 2.5544 2.7726 0.0860  -0.2008 0.1543  184 CYS C CA  
7356  C C   . CYS C 184 ? 2.7243 2.5449 2.7758 0.0967  -0.2153 0.1461  184 CYS C C   
7357  O O   . CYS C 184 ? 2.6980 2.5264 2.7468 0.1032  -0.2246 0.1441  184 CYS C O   
7358  C CB  . CYS C 184 ? 2.7758 2.5564 2.7729 0.0867  -0.2059 0.1680  184 CYS C CB  
7359  S SG  . CYS C 184 ? 2.8314 2.6052 2.7978 0.0763  -0.1911 0.1777  184 CYS C SG  
7360  N N   . GLY C 185 ? 2.2817 2.1009 2.3542 0.0988  -0.2174 0.1410  185 GLY C N   
7361  C CA  . GLY C 185 ? 2.0879 1.9154 2.1821 0.1089  -0.2303 0.1326  185 GLY C CA  
7362  C C   . GLY C 185 ? 1.9440 1.7447 2.0286 0.1171  -0.2450 0.1391  185 GLY C C   
7363  O O   . GLY C 185 ? 1.8384 1.6424 1.9433 0.1252  -0.2549 0.1323  185 GLY C O   
7364  N N   . VAL C 188 ? 2.3628 2.0059 2.4121 0.1252  -0.2720 0.1780  188 VAL C N   
7365  C CA  . VAL C 188 ? 2.4534 2.0684 2.4998 0.1331  -0.2856 0.1837  188 VAL C CA  
7366  C C   . VAL C 188 ? 2.6607 2.2621 2.7191 0.1279  -0.2790 0.1833  188 VAL C C   
7367  O O   . VAL C 188 ? 2.6500 2.2423 2.6967 0.1167  -0.2657 0.1897  188 VAL C O   
7368  C CB  . VAL C 188 ? 2.3869 1.9721 2.3971 0.1343  -0.2922 0.1997  188 VAL C CB  
7369  C CG1 . VAL C 188 ? 2.6455 2.2231 2.6308 0.1217  -0.2769 0.2093  188 VAL C CG1 
7370  C CG2 . VAL C 188 ? 2.4542 2.0064 2.4605 0.1398  -0.3030 0.2071  188 VAL C CG2 
7371  N N   . PHE C 189 ? 3.0733 2.6738 3.1557 0.1359  -0.2879 0.1753  189 PHE C N   
7372  C CA  . PHE C 189 ? 3.0798 2.6679 3.1766 0.1322  -0.2833 0.1733  189 PHE C CA  
7373  C C   . PHE C 189 ? 3.0878 2.6415 3.1775 0.1395  -0.2966 0.1815  189 PHE C C   
7374  O O   . PHE C 189 ? 3.0968 2.6357 3.1685 0.1470  -0.3089 0.1897  189 PHE C O   
7375  C CB  . PHE C 189 ? 3.0889 2.7060 3.2218 0.1345  -0.2811 0.1558  189 PHE C CB  
7376  C CG  . PHE C 189 ? 3.1005 2.7511 3.2412 0.1273  -0.2682 0.1478  189 PHE C CG  
7377  C CD1 . PHE C 189 ? 3.1027 2.7590 3.2478 0.1155  -0.2527 0.1461  189 PHE C CD1 
7378  C CD2 . PHE C 189 ? 3.1553 2.8314 3.2996 0.1324  -0.2719 0.1419  189 PHE C CD2 
7379  C CE1 . PHE C 189 ? 3.1342 2.8209 3.2866 0.1093  -0.2413 0.1389  189 PHE C CE1 
7380  C CE2 . PHE C 189 ? 3.1795 2.8855 3.3309 0.1259  -0.2603 0.1348  189 PHE C CE2 
7381  C CZ  . PHE C 189 ? 3.2415 2.9526 3.3967 0.1145  -0.2451 0.1335  189 PHE C CZ  
7382  N N   . THR C 190 ? 2.6516 2.1922 2.7556 0.1375  -0.2944 0.1793  190 THR C N   
7383  C CA  . THR C 190 ? 2.5847 2.0956 2.6892 0.1456  -0.3073 0.1840  190 THR C CA  
7384  C C   . THR C 190 ? 2.5654 2.0926 2.7044 0.1559  -0.3159 0.1683  190 THR C C   
7385  O O   . THR C 190 ? 2.5973 2.1578 2.7577 0.1563  -0.3114 0.1547  190 THR C O   
7386  C CB  . THR C 190 ? 2.4419 1.9236 2.5376 0.1363  -0.2995 0.1931  190 THR C CB  
7387  O OG1 . THR C 190 ? 2.4163 1.8672 2.5110 0.1446  -0.3129 0.1987  190 THR C OG1 
7388  C CG2 . THR C 190 ? 2.3832 1.8818 2.5047 0.1286  -0.2870 0.1812  190 THR C CG2 
7389  N N   . SER C 191 ? 2.4571 1.9602 2.6013 0.1645  -0.3284 0.1704  191 SER C N   
7390  C CA  . SER C 191 ? 2.4045 1.9206 2.5811 0.1751  -0.3370 0.1558  191 SER C CA  
7391  C C   . SER C 191 ? 2.4420 1.9732 2.6447 0.1689  -0.3256 0.1429  191 SER C C   
7392  O O   . SER C 191 ? 2.4190 1.9678 2.6501 0.1766  -0.3302 0.1285  191 SER C O   
7393  C CB  . SER C 191 ? 2.3460 1.8304 2.5214 0.1857  -0.3529 0.1617  191 SER C CB  
7394  O OG  . SER C 191 ? 2.2477 1.7447 2.4550 0.1963  -0.3612 0.1471  191 SER C OG  
7395  N N   . ASP C 192 ? 2.5410 2.0664 2.7351 0.1554  -0.3110 0.1474  192 ASP C N   
7396  C CA  . ASP C 192 ? 2.6061 2.1431 2.8232 0.1487  -0.3003 0.1361  192 ASP C CA  
7397  C C   . ASP C 192 ? 2.6754 2.2535 2.9087 0.1452  -0.2908 0.1228  192 ASP C C   
7398  O O   . ASP C 192 ? 2.6530 2.2444 2.9062 0.1399  -0.2820 0.1122  192 ASP C O   
7399  C CB  . ASP C 192 ? 2.6081 2.1221 2.8095 0.1352  -0.2887 0.1468  192 ASP C CB  
7400  C CG  . ASP C 192 ? 2.6362 2.1512 2.8608 0.1297  -0.2814 0.1369  192 ASP C CG  
7401  O OD1 . ASP C 192 ? 2.5927 2.1195 2.8438 0.1378  -0.2873 0.1230  192 ASP C OD1 
7402  O OD2 . ASP C 192 ? 2.6595 2.1642 2.8761 0.1172  -0.2695 0.1426  192 ASP C OD2 
7403  N N   . ILE C 193 ? 3.3415 2.9396 3.5670 0.1481  -0.2925 0.1230  193 ILE C N   
7404  C CA  . ILE C 193 ? 3.3174 2.9532 3.5554 0.1438  -0.2826 0.1121  193 ILE C CA  
7405  C C   . ILE C 193 ? 3.2829 2.9427 3.5539 0.1515  -0.2863 0.0944  193 ILE C C   
7406  O O   . ILE C 193 ? 3.2671 2.9527 3.5540 0.1461  -0.2760 0.0835  193 ILE C O   
7407  C CB  . ILE C 193 ? 3.3082 2.9571 3.5285 0.1450  -0.2841 0.1174  193 ILE C CB  
7408  C CG1 . ILE C 193 ? 3.3119 2.9990 3.5446 0.1403  -0.2737 0.1068  193 ILE C CG1 
7409  C CG2 . ILE C 193 ? 3.2917 2.9374 3.5131 0.1591  -0.3012 0.1174  193 ILE C CG2 
7410  C CD1 . ILE C 193 ? 3.3378 3.0307 3.5709 0.1267  -0.2571 0.1060  193 ILE C CD1 
7411  N N   . PHE C 194 ? 2.6551 2.3069 2.9370 0.1643  -0.3007 0.0910  194 PHE C N   
7412  C CA  . PHE C 194 ? 2.4417 2.1163 2.7550 0.1720  -0.3039 0.0739  194 PHE C CA  
7413  C C   . PHE C 194 ? 2.3940 2.0662 2.7252 0.1669  -0.2964 0.0653  194 PHE C C   
7414  O O   . PHE C 194 ? 2.3683 2.0664 2.7236 0.1684  -0.2928 0.0502  194 PHE C O   
7415  C CB  . PHE C 194 ? 2.2581 1.9228 2.5793 0.1870  -0.3211 0.0726  194 PHE C CB  
7416  C CG  . PHE C 194 ? 2.2269 1.8992 2.5358 0.1933  -0.3297 0.0779  194 PHE C CG  
7417  C CD1 . PHE C 194 ? 2.2726 1.9800 2.5947 0.1961  -0.3285 0.0678  194 PHE C CD1 
7418  C CD2 . PHE C 194 ? 2.1927 1.8370 2.4767 0.1962  -0.3390 0.0929  194 PHE C CD2 
7419  C CE1 . PHE C 194 ? 2.2622 1.9767 2.5738 0.2017  -0.3366 0.0722  194 PHE C CE1 
7420  C CE2 . PHE C 194 ? 2.1492 1.8007 2.4219 0.2020  -0.3474 0.0972  194 PHE C CE2 
7421  C CZ  . PHE C 194 ? 2.1828 1.8695 2.4699 0.2046  -0.3462 0.0867  194 PHE C CZ  
7422  N N   . ASN C 195 ? 2.3985 2.0400 2.7180 0.1607  -0.2940 0.0746  195 ASN C N   
7423  C CA  . ASN C 195 ? 2.3432 1.9814 2.6787 0.1547  -0.2865 0.0669  195 ASN C CA  
7424  C C   . ASN C 195 ? 2.4022 2.0632 2.7389 0.1418  -0.2703 0.0628  195 ASN C C   
7425  O O   . ASN C 195 ? 2.4167 2.0900 2.7733 0.1384  -0.2640 0.0508  195 ASN C O   
7426  C CB  . ASN C 195 ? 2.2420 1.8397 2.5648 0.1516  -0.2889 0.0786  195 ASN C CB  
7427  C CG  . ASN C 195 ? 2.1803 1.7536 2.5003 0.1644  -0.3054 0.0839  195 ASN C CG  
7428  O OD1 . ASN C 195 ? 2.1306 1.7167 2.4686 0.1764  -0.3151 0.0739  195 ASN C OD1 
7429  N ND2 . ASN C 195 ? 2.2121 1.7501 2.5094 0.1620  -0.3087 0.0998  195 ASN C ND2 
7430  N N   . ALA C 196 ? 2.4377 2.1044 2.7533 0.1348  -0.2637 0.0724  196 ALA C N   
7431  C CA  . ALA C 196 ? 2.4703 2.1595 2.7869 0.1230  -0.2487 0.0688  196 ALA C CA  
7432  C C   . ALA C 196 ? 2.5716 2.2995 2.9092 0.1267  -0.2466 0.0534  196 ALA C C   
7433  O O   . ALA C 196 ? 2.5341 2.2817 2.8827 0.1190  -0.2357 0.0453  196 ALA C O   
7434  C CB  . ALA C 196 ? 2.4056 2.0904 2.6941 0.1154  -0.2426 0.0831  196 ALA C CB  
7435  N N   . ILE C 197 ? 2.8130 2.5523 3.1566 0.1382  -0.2569 0.0493  197 ILE C N   
7436  C CA  . ILE C 197 ? 2.7936 2.5692 3.1576 0.1420  -0.2551 0.0347  197 ILE C CA  
7437  C C   . ILE C 197 ? 2.7859 2.5675 3.1770 0.1463  -0.2565 0.0199  197 ILE C C   
7438  O O   . ILE C 197 ? 2.7998 2.6094 3.2076 0.1442  -0.2495 0.0074  197 ILE C O   
7439  C CB  . ILE C 197 ? 2.7854 2.5719 3.1472 0.1524  -0.2653 0.0353  197 ILE C CB  
7440  C CG1 . ILE C 197 ? 2.8346 2.6123 3.1680 0.1483  -0.2646 0.0502  197 ILE C CG1 
7441  C CG2 . ILE C 197 ? 2.7975 2.6224 3.1791 0.1552  -0.2621 0.0213  197 ILE C CG2 
7442  C CD1 . ILE C 197 ? 2.8320 2.6213 3.1625 0.1576  -0.2744 0.0509  197 ILE C CD1 
7443  N N   . GLU C 198 ? 2.5428 2.2982 2.9383 0.1524  -0.2654 0.0209  198 GLU C N   
7444  C CA  . GLU C 198 ? 2.5151 2.2737 2.9357 0.1565  -0.2666 0.0067  198 GLU C CA  
7445  C C   . GLU C 198 ? 2.6172 2.3788 3.0431 0.1445  -0.2541 0.0021  198 GLU C C   
7446  O O   . GLU C 198 ? 2.6512 2.4295 3.0986 0.1455  -0.2511 -0.0127 198 GLU C O   
7447  C CB  . GLU C 198 ? 2.4374 2.1642 2.8600 0.1652  -0.2789 0.0100  198 GLU C CB  
7448  C CG  . GLU C 198 ? 2.3584 2.0837 2.7801 0.1785  -0.2928 0.0124  198 GLU C CG  
7449  C CD  . GLU C 198 ? 2.2372 1.9325 2.6636 0.1880  -0.3053 0.0144  198 GLU C CD  
7450  O OE1 . GLU C 198 ? 2.2240 1.8960 2.6507 0.1834  -0.3031 0.0161  198 GLU C OE1 
7451  O OE2 . GLU C 198 ? 2.1946 1.8894 2.6248 0.2001  -0.3176 0.0142  198 GLU C OE2 
7452  N N   . GLU C 199 ? 2.6428 2.3888 3.0494 0.1332  -0.2465 0.0142  199 GLU C N   
7453  C CA  . GLU C 199 ? 2.6359 2.3854 3.0470 0.1211  -0.2344 0.0106  199 GLU C CA  
7454  C C   . GLU C 199 ? 2.5896 2.3745 3.0048 0.1147  -0.2237 0.0039  199 GLU C C   
7455  O O   . GLU C 199 ? 2.5462 2.3383 2.9671 0.1050  -0.2137 -0.0006 199 GLU C O   
7456  C CB  . GLU C 199 ? 2.6158 2.3356 3.0056 0.1111  -0.2299 0.0262  199 GLU C CB  
7457  C CG  . GLU C 199 ? 2.6378 2.3203 3.0245 0.1157  -0.2392 0.0326  199 GLU C CG  
7458  C CD  . GLU C 199 ? 2.7032 2.3839 3.1150 0.1206  -0.2430 0.0184  199 GLU C CD  
7459  O OE1 . GLU C 199 ? 2.7432 2.4366 3.1684 0.1132  -0.2342 0.0087  199 GLU C OE1 
7460  O OE2 . GLU C 199 ? 2.6867 2.3538 3.1052 0.1321  -0.2550 0.0166  199 GLU C OE2 
7461  N N   . VAL C 200 ? 2.5944 2.4012 3.0072 0.1198  -0.2257 0.0031  200 VAL C N   
7462  C CA  . VAL C 200 ? 2.4879 2.3295 2.9070 0.1154  -0.2167 -0.0045 200 VAL C CA  
7463  C C   . VAL C 200 ? 2.5692 2.4377 3.0078 0.1254  -0.2215 -0.0183 200 VAL C C   
7464  O O   . VAL C 200 ? 2.4622 2.3593 2.9120 0.1222  -0.2141 -0.0283 200 VAL C O   
7465  C CB  . VAL C 200 ? 2.3340 2.1810 2.7313 0.1096  -0.2115 0.0074  200 VAL C CB  
7466  C CG1 . VAL C 200 ? 2.4590 2.3110 2.8500 0.1195  -0.2209 0.0108  200 VAL C CG1 
7467  C CG2 . VAL C 200 ? 2.1395 2.0161 2.5413 0.1009  -0.1992 0.0016  200 VAL C CG2 
7468  N N   . TYR C 201 ? 2.9816 2.8423 3.4251 0.1375  -0.2336 -0.0193 201 TYR C N   
7469  C CA  . TYR C 201 ? 2.9437 2.8290 3.4070 0.1475  -0.2383 -0.0326 201 TYR C CA  
7470  C C   . TYR C 201 ? 2.9403 2.8234 3.4259 0.1524  -0.2410 -0.0461 201 TYR C C   
7471  O O   . TYR C 201 ? 2.9084 2.8178 3.4126 0.1557  -0.2387 -0.0601 201 TYR C O   
7472  C CB  . TYR C 201 ? 2.9390 2.8196 3.3971 0.1582  -0.2502 -0.0271 201 TYR C CB  
7473  C CG  . TYR C 201 ? 2.9364 2.8464 3.3940 0.1598  -0.2486 -0.0288 201 TYR C CG  
7474  C CD1 . TYR C 201 ? 2.8780 2.8208 3.3524 0.1591  -0.2420 -0.0418 201 TYR C CD1 
7475  C CD2 . TYR C 201 ? 2.9221 2.8265 3.3618 0.1617  -0.2536 -0.0173 201 TYR C CD2 
7476  C CE1 . TYR C 201 ? 2.8303 2.7993 3.3044 0.1603  -0.2404 -0.0430 201 TYR C CE1 
7477  C CE2 . TYR C 201 ? 2.9070 2.8375 3.3466 0.1628  -0.2523 -0.0189 201 TYR C CE2 
7478  C CZ  . TYR C 201 ? 2.8555 2.8181 3.3126 0.1620  -0.2456 -0.0316 201 TYR C CZ  
7479  O OH  . TYR C 201 ? 2.7925 2.7804 3.2497 0.1629  -0.2442 -0.0329 201 TYR C OH  
7480  N N   . SER C 202 ? 2.6542 2.5061 3.1381 0.1533  -0.2459 -0.0421 202 SER C N   
7481  C CA  . SER C 202 ? 2.6442 2.4903 3.1481 0.1575  -0.2484 -0.0544 202 SER C CA  
7482  C C   . SER C 202 ? 2.5982 2.4403 3.1045 0.1460  -0.2384 -0.0578 202 SER C C   
7483  O O   . SER C 202 ? 2.5615 2.4167 3.0866 0.1467  -0.2356 -0.0723 202 SER C O   
7484  C CB  . SER C 202 ? 2.6690 2.4826 3.1719 0.1662  -0.2607 -0.0490 202 SER C CB  
7485  O OG  . SER C 202 ? 2.6757 2.4914 3.1751 0.1765  -0.2706 -0.0447 202 SER C OG  
7486  N N   . GLN C 203 ? 2.7217 2.5462 3.2094 0.1354  -0.2330 -0.0448 203 GLN C N   
7487  C CA  . GLN C 203 ? 2.7173 2.5363 3.2077 0.1242  -0.2239 -0.0473 203 GLN C CA  
7488  C C   . GLN C 203 ? 2.6750 2.5256 3.1676 0.1155  -0.2122 -0.0529 203 GLN C C   
7489  O O   . GLN C 203 ? 2.6608 2.5238 3.1680 0.1116  -0.2068 -0.0650 203 GLN C O   
7490  C CB  . GLN C 203 ? 2.7372 2.5233 3.2078 0.1162  -0.2226 -0.0310 203 GLN C CB  
7491  C CG  . GLN C 203 ? 2.7506 2.5299 3.2236 0.1037  -0.2131 -0.0324 203 GLN C CG  
7492  C CD  . GLN C 203 ? 2.7576 2.5334 3.2104 0.0914  -0.2038 -0.0188 203 GLN C CD  
7493  O OE1 . GLN C 203 ? 2.7665 2.5240 3.1994 0.0914  -0.2064 -0.0040 203 GLN C OE1 
7494  N NE2 . GLN C 203 ? 2.7477 2.5413 3.2055 0.0810  -0.1928 -0.0240 203 GLN C NE2 
7495  N N   . ILE C 204 ? 2.4727 2.3366 2.9509 0.1126  -0.2086 -0.0446 204 ILE C N   
7496  C CA  . ILE C 204 ? 2.3124 2.2049 2.7910 0.1043  -0.1976 -0.0483 204 ILE C CA  
7497  C C   . ILE C 204 ? 2.2538 2.1784 2.7437 0.1121  -0.1992 -0.0586 204 ILE C C   
7498  O O   . ILE C 204 ? 2.1690 2.1205 2.6680 0.1082  -0.1919 -0.0679 204 ILE C O   
7499  C CB  . ILE C 204 ? 2.1843 2.0717 2.6403 0.0954  -0.1914 -0.0330 204 ILE C CB  
7500  C CG1 . ILE C 204 ? 2.2181 2.0719 2.6622 0.0882  -0.1902 -0.0219 204 ILE C CG1 
7501  C CG2 . ILE C 204 ? 1.9618 1.8773 2.4191 0.0865  -0.1800 -0.0369 204 ILE C CG2 
7502  C CD1 . ILE C 204 ? 2.0346 1.8818 2.4561 0.0793  -0.1835 -0.0068 204 ILE C CD1 
7503  N N   . ARG C 205 ? 2.2842 2.2060 2.7738 0.1230  -0.2089 -0.0568 205 ARG C N   
7504  C CA  . ARG C 205 ? 2.2094 2.1599 2.7104 0.1312  -0.2114 -0.0660 205 ARG C CA  
7505  C C   . ARG C 205 ? 2.1116 2.0885 2.6052 0.1250  -0.2030 -0.0637 205 ARG C C   
7506  O O   . ARG C 205 ? 2.1731 2.1575 2.6585 0.1288  -0.2061 -0.0580 205 ARG C O   
7507  C CB  . ARG C 205 ? 2.1487 2.1137 2.6734 0.1358  -0.2114 -0.0836 205 ARG C CB  
7508  C CG  . ARG C 205 ? 2.2188 2.1599 2.7535 0.1435  -0.2204 -0.0876 205 ARG C CG  
7509  C CD  . ARG C 205 ? 2.1492 2.0933 2.7004 0.1409  -0.2163 -0.1013 205 ARG C CD  
7510  N NE  . ARG C 205 ? 2.2087 2.1405 2.7514 0.1283  -0.2085 -0.0962 205 ARG C NE  
7511  C CZ  . ARG C 205 ? 2.1508 2.1026 2.6930 0.1186  -0.1981 -0.0994 205 ARG C CZ  
7512  N NH1 . ARG C 205 ? 2.0730 2.0574 2.6217 0.1200  -0.1942 -0.1073 205 ARG C NH1 
7513  N NH2 . ARG C 205 ? 2.1447 2.0837 2.6801 0.1074  -0.1918 -0.0944 205 ARG C NH2 
7514  N N   . PHE C 222 ? 2.3630 2.4094 2.8212 0.1536  -0.2281 -0.0385 222 PHE C N   
7515  C CA  . PHE C 222 ? 2.3283 2.3896 2.7798 0.1429  -0.2156 -0.0374 222 PHE C CA  
7516  C C   . PHE C 222 ? 2.6140 2.6520 3.0466 0.1336  -0.2104 -0.0266 222 PHE C C   
7517  O O   . PHE C 222 ? 2.6633 2.7104 3.0897 0.1242  -0.1999 -0.0249 222 PHE C O   
7518  C CB  . PHE C 222 ? 2.1403 2.2254 2.6116 0.1410  -0.2082 -0.0512 222 PHE C CB  
7519  C CG  . PHE C 222 ? 2.1299 2.2018 2.6127 0.1424  -0.2093 -0.0581 222 PHE C CG  
7520  C CD1 . PHE C 222 ? 2.1123 2.1714 2.5890 0.1334  -0.2023 -0.0555 222 PHE C CD1 
7521  C CD2 . PHE C 222 ? 2.0805 2.1534 2.5811 0.1526  -0.2171 -0.0675 222 PHE C CD2 
7522  C CE1 . PHE C 222 ? 2.0222 2.0688 2.5098 0.1344  -0.2035 -0.0621 222 PHE C CE1 
7523  C CE2 . PHE C 222 ? 2.0316 2.0920 2.5429 0.1540  -0.2182 -0.0743 222 PHE C CE2 
7524  C CZ  . PHE C 222 ? 2.0150 2.0618 2.5196 0.1448  -0.2114 -0.0716 222 PHE C CZ  
7525  N N   . VAL C 223 ? 3.0378 3.0456 3.4614 0.1363  -0.2176 -0.0192 223 VAL C N   
7526  C CA  . VAL C 223 ? 3.0972 3.0802 3.5024 0.1279  -0.2131 -0.0081 223 VAL C CA  
7527  C C   . VAL C 223 ? 3.1243 3.1000 3.5059 0.1255  -0.2137 0.0050  223 VAL C C   
7528  O O   . VAL C 223 ? 3.1072 3.0744 3.4823 0.1331  -0.2238 0.0097  223 VAL C O   
7529  C CB  . VAL C 223 ? 3.1302 3.0831 3.5361 0.1316  -0.2203 -0.0058 223 VAL C CB  
7530  C CG1 . VAL C 223 ? 3.1858 3.1111 3.5694 0.1234  -0.2167 0.0080  223 VAL C CG1 
7531  C CG2 . VAL C 223 ? 3.1165 3.0755 3.5440 0.1319  -0.2178 -0.0187 223 VAL C CG2 
7532  N N   . ARG C 224 ? 3.0711 3.0504 3.4402 0.1151  -0.2030 0.0105  224 ARG C N   
7533  C CA  . ARG C 224 ? 3.0987 3.0718 3.4447 0.1119  -0.2019 0.0225  224 ARG C CA  
7534  C C   . ARG C 224 ? 3.1429 3.0824 3.4690 0.1079  -0.2025 0.0351  224 ARG C C   
7535  O O   . ARG C 224 ? 3.0201 2.9492 3.3469 0.1009  -0.1958 0.0358  224 ARG C O   
7536  C CB  . ARG C 224 ? 2.9959 2.9910 3.3388 0.1030  -0.1896 0.0219  224 ARG C CB  
7537  C CG  . ARG C 224 ? 3.0071 3.0361 3.3682 0.1056  -0.1876 0.0103  224 ARG C CG  
7538  C CD  . ARG C 224 ? 2.9807 3.0227 3.3628 0.1038  -0.1825 -0.0015 224 ARG C CD  
7539  N NE  . ARG C 224 ? 2.9604 2.9906 3.3371 0.0941  -0.1739 0.0018  224 ARG C NE  
7540  C CZ  . ARG C 224 ? 2.9258 2.9516 3.3154 0.0925  -0.1722 -0.0049 224 ARG C CZ  
7541  N NH1 . ARG C 224 ? 2.9343 2.9659 3.3424 0.1003  -0.1784 -0.0155 224 ARG C NH1 
7542  N NH2 . ARG C 224 ? 2.8718 2.8871 3.2561 0.0831  -0.1643 -0.0012 224 ARG C NH2 
7543  N N   . LEU C 225 ? 3.7358 3.6582 4.0439 0.1123  -0.2107 0.0450  225 LEU C N   
7544  C CA  . LEU C 225 ? 3.7830 3.6720 4.0706 0.1094  -0.2122 0.0578  225 LEU C CA  
7545  C C   . LEU C 225 ? 3.8102 3.6957 4.0827 0.0970  -0.1989 0.0651  225 LEU C C   
7546  O O   . LEU C 225 ? 3.8434 3.7083 4.1102 0.0911  -0.1948 0.0704  225 LEU C O   
7547  C CB  . LEU C 225 ? 3.7866 3.6606 4.0565 0.1165  -0.2235 0.0668  225 LEU C CB  
7548  C CG  . LEU C 225 ? 3.8261 3.6638 4.0810 0.1192  -0.2315 0.0774  225 LEU C CG  
7549  C CD1 . LEU C 225 ? 3.8145 3.6445 4.0629 0.1302  -0.2464 0.0807  225 LEU C CD1 
7550  C CD2 . LEU C 225 ? 3.8662 3.6839 4.0955 0.1091  -0.2231 0.0907  225 LEU C CD2 
7551  N N   . ASP C 226 ? 3.0412 2.9463 3.3075 0.0928  -0.1920 0.0656  226 ASP C N   
7552  C CA  . ASP C 226 ? 2.7806 2.6836 3.0314 0.0817  -0.1796 0.0731  226 ASP C CA  
7553  C C   . ASP C 226 ? 2.6253 2.5493 2.8924 0.0739  -0.1678 0.0646  226 ASP C C   
7554  O O   . ASP C 226 ? 2.5592 2.4980 2.8210 0.0672  -0.1582 0.0658  226 ASP C O   
7555  C CB  . ASP C 226 ? 2.6569 2.5673 2.8901 0.0817  -0.1791 0.0790  226 ASP C CB  
7556  C CG  . ASP C 226 ? 2.6078 2.5448 2.8546 0.0888  -0.1844 0.0699  226 ASP C CG  
7557  O OD1 . ASP C 226 ? 2.5248 2.4868 2.7914 0.0874  -0.1790 0.0593  226 ASP C OD1 
7558  O OD2 . ASP C 226 ? 2.4918 2.4249 2.7295 0.0958  -0.1939 0.0732  226 ASP C OD2 
7559  N N   . GLN C 227 ? 2.6493 2.5749 2.9363 0.0748  -0.1685 0.0558  227 GLN C N   
7560  C CA  . GLN C 227 ? 2.5608 2.5057 2.8636 0.0676  -0.1581 0.0473  227 GLN C CA  
7561  C C   . GLN C 227 ? 2.4771 2.4070 2.7908 0.0650  -0.1576 0.0440  227 GLN C C   
7562  O O   . GLN C 227 ? 2.3487 2.2787 2.6640 0.0555  -0.1478 0.0443  227 GLN C O   
7563  C CB  . GLN C 227 ? 2.5474 2.5243 2.8695 0.0725  -0.1591 0.0346  227 GLN C CB  
7564  C CG  . GLN C 227 ? 2.4814 2.4818 2.7989 0.0680  -0.1511 0.0349  227 GLN C CG  
7565  C CD  . GLN C 227 ? 2.4464 2.4646 2.7672 0.0761  -0.1576 0.0311  227 GLN C CD  
7566  O OE1 . GLN C 227 ? 2.4352 2.4434 2.7409 0.0800  -0.1637 0.0386  227 GLN C OE1 
7567  N NE2 . GLN C 227 ? 2.3320 2.3767 2.6724 0.0784  -0.1565 0.0194  227 GLN C NE2 
7568  N N   . ASP C 228 ? 2.5895 2.5064 2.9111 0.0734  -0.1681 0.0409  228 ASP C N   
7569  C CA  . ASP C 228 ? 2.5962 2.4984 2.9296 0.0721  -0.1688 0.0367  228 ASP C CA  
7570  C C   . ASP C 228 ? 2.6275 2.4944 2.9487 0.0756  -0.1770 0.0464  228 ASP C C   
7571  O O   . ASP C 228 ? 2.6757 2.5279 3.0073 0.0766  -0.1801 0.0428  228 ASP C O   
7572  C CB  . ASP C 228 ? 2.6014 2.5224 2.9604 0.0789  -0.1730 0.0211  228 ASP C CB  
7573  N N   . ILE C 229 ? 2.5087 2.3614 2.8079 0.0774  -0.1809 0.0584  229 ILE C N   
7574  C CA  . ILE C 229 ? 2.4299 2.2481 2.7146 0.0804  -0.1887 0.0691  229 ILE C CA  
7575  C C   . ILE C 229 ? 2.3667 2.1683 2.6245 0.0720  -0.1820 0.0840  229 ILE C C   
7576  O O   . ILE C 229 ? 2.2903 2.0649 2.5379 0.0671  -0.1803 0.0927  229 ILE C O   
7577  C CB  . ILE C 229 ? 2.5392 2.3536 2.8233 0.0935  -0.2032 0.0689  229 ILE C CB  
7578  N N   . LEU C 230 ? 2.3702 2.1877 2.6164 0.0703  -0.1778 0.0871  230 LEU C N   
7579  C CA  . LEU C 230 ? 2.3223 2.1263 2.5427 0.0625  -0.1706 0.1005  230 LEU C CA  
7580  C C   . LEU C 230 ? 2.2864 2.0960 2.5097 0.0498  -0.1558 0.1004  230 LEU C C   
7581  O O   . LEU C 230 ? 2.3369 2.1245 2.5453 0.0423  -0.1502 0.1108  230 LEU C O   
7582  C CB  . LEU C 230 ? 2.4624 2.2814 2.6699 0.0652  -0.1715 0.1031  230 LEU C CB  
7583  C CG  . LEU C 230 ? 2.5731 2.3835 2.7721 0.0767  -0.1860 0.1060  230 LEU C CG  
7584  C CD1 . LEU C 230 ? 2.5920 2.4154 2.7760 0.0773  -0.1852 0.1096  230 LEU C CD1 
7585  C CD2 . LEU C 230 ? 2.5685 2.3422 2.7500 0.0784  -0.1928 0.1178  230 LEU C CD2 
7586  N N   . SER C 231 ? 2.2589 2.0979 2.5013 0.0471  -0.1494 0.0890  231 SER C N   
7587  C CA  . SER C 231 ? 2.2196 2.0661 2.4668 0.0354  -0.1359 0.0880  231 SER C CA  
7588  C C   . SER C 231 ? 2.2143 2.0413 2.4697 0.0306  -0.1343 0.0879  231 SER C C   
7589  O O   . SER C 231 ? 2.2392 2.0544 2.4855 0.0205  -0.1250 0.0954  231 SER C O   
7590  C CB  . SER C 231 ? 2.1896 2.0719 2.4561 0.0347  -0.1308 0.0753  231 SER C CB  
7591  O OG  . SER C 231 ? 2.2475 2.1472 2.5067 0.0388  -0.1321 0.0757  231 SER C OG  
7592  N N   . PRO C 232 ? 2.2202 2.0431 2.4929 0.0369  -0.1426 0.0795  232 PRO C N   
7593  C CA  . PRO C 232 ? 2.1828 1.9851 2.4625 0.0319  -0.1410 0.0798  232 PRO C CA  
7594  C C   . PRO C 232 ? 2.2701 2.0365 2.5281 0.0295  -0.1426 0.0949  232 PRO C C   
7595  O O   . PRO C 232 ? 2.2973 2.0482 2.5543 0.0203  -0.1357 0.0993  232 PRO C O   
7596  C CB  . PRO C 232 ? 2.1015 1.9068 2.4023 0.0415  -0.1513 0.0677  232 PRO C CB  
7597  C CG  . PRO C 232 ? 2.1537 1.9914 2.4648 0.0476  -0.1531 0.0578  232 PRO C CG  
7598  C CD  . PRO C 232 ? 2.2119 2.0516 2.5014 0.0480  -0.1521 0.0679  232 PRO C CD  
7599  N N   . LEU C 233 ? 2.2690 2.0217 2.5096 0.0372  -0.1516 0.1031  233 LEU C N   
7600  C CA  . LEU C 233 ? 2.3681 2.0860 2.5855 0.0354  -0.1537 0.1184  233 LEU C CA  
7601  C C   . LEU C 233 ? 2.6278 2.3454 2.8232 0.0261  -0.1424 0.1293  233 LEU C C   
7602  O O   . LEU C 233 ? 2.7022 2.4146 2.8761 0.0292  -0.1452 0.1380  233 LEU C O   
7603  C CB  . LEU C 233 ? 2.2756 1.9789 2.4835 0.0478  -0.1686 0.1224  233 LEU C CB  
7604  C CG  . LEU C 233 ? 2.1739 1.8431 2.3793 0.0511  -0.1770 0.1281  233 LEU C CG  
7605  C CD1 . LEU C 233 ? 2.0510 1.7248 2.2849 0.0539  -0.1803 0.1148  233 LEU C CD1 
7606  C CD2 . LEU C 233 ? 2.1481 1.8012 2.3385 0.0624  -0.1911 0.1351  233 LEU C CD2 
7607  N N   . ALA C 234 ? 3.2963 3.0197 3.4977 0.0145  -0.1296 0.1284  234 ALA C N   
7608  C CA  . ALA C 234 ? 3.3074 3.0323 3.4913 0.0046  -0.1171 0.1375  234 ALA C CA  
7609  C C   . ALA C 234 ? 3.3310 3.0256 3.5024 -0.0044 -0.1112 0.1493  234 ALA C C   
7610  O O   . ALA C 234 ? 3.3510 3.0231 3.4968 -0.0046 -0.1121 0.1628  234 ALA C O   
7611  C CB  . ALA C 234 ? 3.2885 3.0462 3.4888 -0.0019 -0.1062 0.1277  234 ALA C CB  
7612  N N   . GLY C 235 ? 2.9799 2.6731 3.1683 -0.0121 -0.1050 0.1446  235 GLY C N   
7613  C CA  . GLY C 235 ? 2.9605 2.6251 3.1386 -0.0213 -0.0989 0.1556  235 GLY C CA  
7614  C C   . GLY C 235 ? 2.9760 2.6061 3.1431 -0.0151 -0.1101 0.1638  235 GLY C C   
7615  O O   . GLY C 235 ? 2.9981 2.6010 3.1442 -0.0202 -0.1070 0.1779  235 GLY C O   
7616  N N   . LYS C 236 ? 2.7072 2.3378 2.8880 -0.0041 -0.1232 0.1553  236 LYS C N   
7617  C CA  . LYS C 236 ? 2.5196 2.1182 2.6920 0.0031  -0.1351 0.1622  236 LYS C CA  
7618  C C   . LYS C 236 ? 2.5130 2.0972 2.6557 0.0084  -0.1406 0.1753  236 LYS C C   
7619  O O   . LYS C 236 ? 2.5012 2.1043 2.6399 0.0154  -0.1448 0.1721  236 LYS C O   
7620  C CB  . LYS C 236 ? 2.3655 1.9718 2.5609 0.0144  -0.1476 0.1489  236 LYS C CB  
7621  C CG  . LYS C 236 ? 2.3733 2.0182 2.5864 0.0191  -0.1477 0.1343  236 LYS C CG  
7622  C CD  . LYS C 236 ? 2.2246 1.8854 2.4677 0.0170  -0.1453 0.1191  236 LYS C CD  
7623  C CE  . LYS C 236 ? 2.2250 1.8964 2.4732 0.0030  -0.1302 0.1181  236 LYS C CE  
7624  N NZ  . LYS C 236 ? 2.3664 2.0679 2.6114 0.0000  -0.1221 0.1161  236 LYS C NZ  
7625  N N   . LYS C 237 ? 2.4532 2.0036 2.5748 0.0049  -0.1405 0.1900  237 LYS C N   
7626  C CA  . LYS C 237 ? 2.4797 2.0124 2.5697 0.0083  -0.1446 0.2042  237 LYS C CA  
7627  C C   . LYS C 237 ? 2.4521 1.9765 2.5411 0.0233  -0.1627 0.2028  237 LYS C C   
7628  O O   . LYS C 237 ? 2.4179 1.9115 2.4975 0.0276  -0.1716 0.2110  237 LYS C O   
7629  C CB  . LYS C 237 ? 2.4826 1.9813 2.5512 -0.0006 -0.1385 0.2202  237 LYS C CB  
7630  C CG  . LYS C 237 ? 2.4941 2.0004 2.5605 -0.0156 -0.1201 0.2234  237 LYS C CG  
7631  C CD  . LYS C 237 ? 2.5477 2.0609 2.5882 -0.0186 -0.1128 0.2319  237 LYS C CD  
7632  C CE  . LYS C 237 ? 2.5447 2.0289 2.5534 -0.0127 -0.1216 0.2466  237 LYS C CE  
7633  N NZ  . LYS C 237 ? 2.5750 2.0237 2.5671 -0.0205 -0.1170 0.2611  237 LYS C NZ  
7634  N N   . GLN C 238 ? 2.4018 1.9543 2.5013 0.0316  -0.1682 0.1922  238 GLN C N   
7635  C CA  . GLN C 238 ? 2.3211 1.8694 2.4204 0.0459  -0.1850 0.1904  238 GLN C CA  
7636  C C   . GLN C 238 ? 2.3621 1.9311 2.4503 0.0511  -0.1875 0.1897  238 GLN C C   
7637  O O   . GLN C 238 ? 2.3572 1.9160 2.4320 0.0607  -0.1998 0.1946  238 GLN C O   
7638  C CB  . GLN C 238 ? 2.2414 1.8023 2.3729 0.0531  -0.1924 0.1750  238 GLN C CB  
7639  C CG  . GLN C 238 ? 2.2384 1.7731 2.3795 0.0519  -0.1951 0.1760  238 GLN C CG  
7640  C CD  . GLN C 238 ? 2.2092 1.7576 2.3738 0.0427  -0.1842 0.1657  238 GLN C CD  
7641  O OE1 . GLN C 238 ? 2.1693 1.7454 2.3581 0.0458  -0.1843 0.1506  238 GLN C OE1 
7642  N NE2 . GLN C 238 ? 2.2223 1.7513 2.3799 0.0313  -0.1746 0.1740  238 GLN C NE2 
7643  N N   . LEU C 239 ? 2.4713 2.0693 2.5656 0.0448  -0.1762 0.1835  239 LEU C N   
7644  C CA  . LEU C 239 ? 2.4987 2.1180 2.5839 0.0486  -0.1771 0.1820  239 LEU C CA  
7645  C C   . LEU C 239 ? 2.5596 2.1672 2.6137 0.0411  -0.1686 0.1959  239 LEU C C   
7646  O O   . LEU C 239 ? 2.5918 2.1988 2.6427 0.0295  -0.1544 0.1994  239 LEU C O   
7647  C CB  . LEU C 239 ? 2.5193 2.1766 2.6285 0.0465  -0.1699 0.1675  239 LEU C CB  
7648  C CG  . LEU C 239 ? 2.5196 2.2018 2.6395 0.0570  -0.1791 0.1577  239 LEU C CG  
7649  C CD1 . LEU C 239 ? 2.5723 2.2556 2.6673 0.0592  -0.1809 0.1655  239 LEU C CD1 
7650  C CD2 . LEU C 239 ? 2.4773 2.1499 2.6100 0.0687  -0.1945 0.1530  239 LEU C CD2 
7651  N N   . TYR C 240 ? 2.5444 2.1429 2.5757 0.0477  -0.1770 0.2034  240 TYR C N   
7652  C CA  . TYR C 240 ? 2.5401 2.1248 2.5391 0.0417  -0.1702 0.2170  240 TYR C CA  
7653  C C   . TYR C 240 ? 2.5339 2.1411 2.5239 0.0448  -0.1704 0.2143  240 TYR C C   
7654  O O   . TYR C 240 ? 2.5164 2.1513 2.5266 0.0502  -0.1740 0.2020  240 TYR C O   
7655  C CB  . TYR C 240 ? 2.4951 2.0420 2.4696 0.0453  -0.1795 0.2311  240 TYR C CB  
7656  C CG  . TYR C 240 ? 2.4727 1.9947 2.4510 0.0391  -0.1757 0.2364  240 TYR C CG  
7657  C CD1 . TYR C 240 ? 2.4719 1.9806 2.4351 0.0266  -0.1612 0.2463  240 TYR C CD1 
7658  C CD2 . TYR C 240 ? 2.4614 1.9736 2.4592 0.0457  -0.1861 0.2313  240 TYR C CD2 
7659  C CE1 . TYR C 240 ? 2.4636 1.9495 2.4309 0.0204  -0.1575 0.2512  240 TYR C CE1 
7660  C CE2 . TYR C 240 ? 2.4603 1.9492 2.4621 0.0398  -0.1826 0.2359  240 TYR C CE2 
7661  C CZ  . TYR C 240 ? 2.4325 1.9082 2.4190 0.0270  -0.1684 0.2460  240 TYR C CZ  
7662  O OH  . TYR C 240 ? 2.3685 1.8208 2.3594 0.0206  -0.1648 0.2508  240 TYR C OH  
7663  N N   . THR C 241 ? 2.4417 2.0366 2.4008 0.0413  -0.1662 0.2260  241 THR C N   
7664  C CA  . THR C 241 ? 2.4128 2.0265 2.3604 0.0429  -0.1650 0.2245  241 THR C CA  
7665  C C   . THR C 241 ? 2.3931 1.9821 2.3042 0.0454  -0.1704 0.2383  241 THR C C   
7666  O O   . THR C 241 ? 2.3673 1.9264 2.2593 0.0420  -0.1694 0.2504  241 THR C O   
7667  C CB  . THR C 241 ? 2.3866 2.0217 2.3378 0.0321  -0.1471 0.2215  241 THR C CB  
7668  O OG1 . THR C 241 ? 2.3468 1.9640 2.2893 0.0213  -0.1349 0.2301  241 THR C OG1 
7669  C CG2 . THR C 241 ? 2.3972 2.0646 2.3829 0.0324  -0.1443 0.2058  241 THR C CG2 
7670  N N   . ASN C 244 ? 2.5859 2.2342 2.4124 0.0617  -0.1826 0.2363  244 ASN C N   
7671  C CA  . ASN C 244 ? 2.6362 2.2886 2.4551 0.0714  -0.1973 0.2339  244 ASN C CA  
7672  C C   . ASN C 244 ? 2.6988 2.3337 2.4786 0.0703  -0.1971 0.2445  244 ASN C C   
7673  O O   . ASN C 244 ? 2.7229 2.3377 2.4831 0.0772  -0.2109 0.2511  244 ASN C O   
7674  C CB  . ASN C 244 ? 2.6446 2.3325 2.4880 0.0733  -0.1961 0.2202  244 ASN C CB  
7675  C CG  . ASN C 244 ? 2.7533 2.4481 2.5980 0.0841  -0.2131 0.2156  244 ASN C CG  
7676  O OD1 . ASN C 244 ? 2.7885 2.4629 2.6091 0.0893  -0.2242 0.2233  244 ASN C OD1 
7677  N ND2 . ASN C 244 ? 2.7795 2.5033 2.6522 0.0873  -0.2151 0.2031  244 ASN C ND2 
7678  N N   . LYS C 245 ? 2.6794 2.3224 2.4476 0.0619  -0.1817 0.2457  245 LYS C N   
7679  C CA  . LYS C 245 ? 2.7513 2.3807 2.4826 0.0598  -0.1789 0.2545  245 LYS C CA  
7680  C C   . LYS C 245 ? 2.7890 2.4272 2.5125 0.0683  -0.1920 0.2501  245 LYS C C   
7681  O O   . LYS C 245 ? 2.8037 2.4239 2.4952 0.0705  -0.1975 0.2581  245 LYS C O   
7682  C CB  . LYS C 245 ? 2.7675 2.3605 2.4689 0.0586  -0.1810 0.2693  245 LYS C CB  
7683  N N   . ASP C 246 ? 2.8359 2.5017 2.5884 0.0728  -0.1969 0.2375  246 ASP C N   
7684  C CA  . ASP C 246 ? 2.9739 2.6514 2.7228 0.0800  -0.2082 0.2321  246 ASP C CA  
7685  C C   . ASP C 246 ? 3.1053 2.8176 2.8831 0.0791  -0.2029 0.2188  246 ASP C C   
7686  O O   . ASP C 246 ? 3.0981 2.8234 2.8777 0.0713  -0.1872 0.2168  246 ASP C O   
7687  C CB  . ASP C 246 ? 2.9758 2.6426 2.7275 0.0910  -0.2290 0.2323  246 ASP C CB  
7688  C CG  . ASP C 246 ? 2.8913 2.5263 2.6057 0.0939  -0.2378 0.2450  246 ASP C CG  
7689  O OD1 . ASP C 246 ? 2.9058 2.5373 2.5937 0.0930  -0.2369 0.2482  246 ASP C OD1 
7690  O OD2 . ASP C 246 ? 2.8122 2.4254 2.5234 0.0972  -0.2458 0.2516  246 ASP C OD2 
7691  N N   . PHE C 247 ? 3.5709 3.2987 3.3716 0.0872  -0.2158 0.2099  247 PHE C N   
7692  C CA  . PHE C 247 ? 3.5362 3.2966 3.3637 0.0873  -0.2126 0.1975  247 PHE C CA  
7693  C C   . PHE C 247 ? 3.5132 3.2881 3.3769 0.0903  -0.2158 0.1891  247 PHE C C   
7694  O O   . PHE C 247 ? 3.5180 3.2784 3.3866 0.0949  -0.2250 0.1916  247 PHE C O   
7695  C CB  . PHE C 247 ? 3.5151 3.2845 3.3369 0.0940  -0.2245 0.1932  247 PHE C CB  
7696  C CG  . PHE C 247 ? 3.5132 3.2679 3.3298 0.1039  -0.2443 0.1956  247 PHE C CG  
7697  C CD1 . PHE C 247 ? 3.5411 3.2677 3.3236 0.1059  -0.2513 0.2065  247 PHE C CD1 
7698  C CD2 . PHE C 247 ? 3.4823 3.2516 3.3282 0.1114  -0.2559 0.1870  247 PHE C CD2 
7699  C CE1 . PHE C 247 ? 3.5379 3.2511 3.3159 0.1153  -0.2701 0.2088  247 PHE C CE1 
7700  C CE2 . PHE C 247 ? 3.4788 3.2352 3.3212 0.1208  -0.2743 0.1889  247 PHE C CE2 
7701  C CZ  . PHE C 247 ? 3.5073 3.2356 3.3159 0.1229  -0.2817 0.1999  247 PHE C CZ  
7702  N N   . TRP C 248 ? 2.9738 2.7774 2.8626 0.0876  -0.2080 0.1789  248 TRP C N   
7703  C CA  . TRP C 248 ? 2.7328 2.5543 2.6567 0.0906  -0.2107 0.1693  248 TRP C CA  
7704  C C   . TRP C 248 ? 2.5417 2.3955 2.4863 0.0890  -0.2046 0.1587  248 TRP C C   
7705  O O   . TRP C 248 ? 2.5371 2.3993 2.4755 0.0818  -0.1914 0.1589  248 TRP C O   
7706  C CB  . TRP C 248 ? 2.6633 2.4778 2.5976 0.0851  -0.2015 0.1711  248 TRP C CB  
7707  C CG  . TRP C 248 ? 2.5593 2.3896 2.5278 0.0890  -0.2057 0.1613  248 TRP C CG  
7708  C CD1 . TRP C 248 ? 2.5432 2.3660 2.5227 0.0974  -0.2197 0.1596  248 TRP C CD1 
7709  C CD2 . TRP C 248 ? 2.4422 2.2990 2.4382 0.0851  -0.1960 0.1515  248 TRP C CD2 
7710  N NE1 . TRP C 248 ? 2.3996 2.2426 2.4115 0.0988  -0.2187 0.1491  248 TRP C NE1 
7711  C CE2 . TRP C 248 ? 2.3684 2.2324 2.3904 0.0913  -0.2044 0.1441  248 TRP C CE2 
7712  C CE3 . TRP C 248 ? 2.3650 2.2402 2.3660 0.0772  -0.1812 0.1482  248 TRP C CE3 
7713  C CZ2 . TRP C 248 ? 2.2939 2.1824 2.3453 0.0896  -0.1984 0.1336  248 TRP C CZ2 
7714  C CZ3 . TRP C 248 ? 2.2910 2.1903 2.3215 0.0756  -0.1757 0.1382  248 TRP C CZ3 
7715  C CH2 . TRP C 248 ? 2.2869 2.1925 2.3416 0.0817  -0.1842 0.1310  248 TRP C CH2 
7716  N N   . GLU C 249 ? 2.4295 2.3009 2.3985 0.0957  -0.2142 0.1495  249 GLU C N   
7717  C CA  . GLU C 249 ? 2.2792 2.1815 2.2695 0.0948  -0.2096 0.1392  249 GLU C CA  
7718  C C   . GLU C 249 ? 2.1877 2.1059 2.2100 0.1006  -0.2170 0.1298  249 GLU C C   
7719  O O   . GLU C 249 ? 2.1695 2.0835 2.1956 0.1090  -0.2316 0.1285  249 GLU C O   
7720  C CB  . GLU C 249 ? 2.1947 2.1029 2.1719 0.0973  -0.2149 0.1385  249 GLU C CB  
7721  N N   . GLN C 250 ? 2.0352 1.9719 2.0805 0.0964  -0.2070 0.1231  250 GLN C N   
7722  C CA  . GLN C 250 ? 1.9303 1.8847 2.0066 0.1014  -0.2122 0.1132  250 GLN C CA  
7723  C C   . GLN C 250 ? 1.8744 1.8515 1.9628 0.1059  -0.2182 0.1056  250 GLN C C   
7724  O O   . GLN C 250 ? 1.8286 1.8197 1.9137 0.1017  -0.2109 0.1040  250 GLN C O   
7725  C CB  . GLN C 250 ? 1.9424 1.9105 2.0376 0.0951  -0.1993 0.1082  250 GLN C CB  
7726  C CG  . GLN C 250 ? 1.9432 1.9091 2.0588 0.0986  -0.2034 0.1039  250 GLN C CG  
7727  C CD  . GLN C 250 ? 1.8648 1.8542 2.0083 0.1050  -0.2100 0.0927  250 GLN C CD  
7728  O OE1 . GLN C 250 ? 1.8477 1.8384 1.9927 0.1124  -0.2222 0.0910  250 GLN C OE1 
7729  N NE2 . GLN C 250 ? 1.9127 1.9211 2.0785 0.1019  -0.2019 0.0847  250 GLN C NE2 
7730  N N   . ILE C 251 ? 1.8736 1.8543 1.9765 0.1144  -0.2315 0.1008  251 ILE C N   
7731  C CA  . ILE C 251 ? 1.8343 1.8343 1.9480 0.1192  -0.2388 0.0943  251 ILE C CA  
7732  C C   . ILE C 251 ? 1.8036 1.8267 1.9508 0.1231  -0.2410 0.0834  251 ILE C C   
7733  O O   . ILE C 251 ? 1.7739 1.7983 1.9325 0.1312  -0.2537 0.0798  251 ILE C O   
7734  C CB  . ILE C 251 ? 1.8187 1.8027 1.9163 0.1263  -0.2543 0.0989  251 ILE C CB  
7735  C CG1 . ILE C 251 ? 1.8860 1.8478 1.9815 0.1318  -0.2639 0.1031  251 ILE C CG1 
7736  C CG2 . ILE C 251 ? 1.8699 1.8399 1.9358 0.1221  -0.2514 0.1072  251 ILE C CG2 
7737  C CD1 . ILE C 251 ? 1.9574 1.9151 2.0555 0.1417  -0.2818 0.1020  251 ILE C CD1 
7738  N N   . LYS C 252 ? 1.8353 1.8769 1.9983 0.1177  -0.2288 0.0778  252 LYS C N   
7739  C CA  . LYS C 252 ? 1.7798 1.8464 1.9732 0.1207  -0.2294 0.0670  252 LYS C CA  
7740  C C   . LYS C 252 ? 1.7326 1.8230 1.9340 0.1204  -0.2285 0.0617  252 LYS C C   
7741  O O   . LYS C 252 ? 1.7008 1.8117 1.9262 0.1241  -0.2314 0.0531  252 LYS C O   
7742  C CB  . LYS C 252 ? 1.7833 1.8586 1.9909 0.1153  -0.2174 0.0631  252 LYS C CB  
7743  C CG  . LYS C 252 ? 1.8031 1.8885 2.0045 0.1063  -0.2029 0.0642  252 LYS C CG  
7744  C CD  . LYS C 252 ? 1.8471 1.9109 2.0279 0.1000  -0.1953 0.0730  252 LYS C CD  
7745  C CE  . LYS C 252 ? 1.8545 1.9205 2.0181 0.0932  -0.1856 0.0775  252 LYS C CE  
7746  N NZ  . LYS C 252 ? 1.8459 1.9025 1.9898 0.0962  -0.1934 0.0824  252 LYS C NZ  
7747  N N   . THR C 253 ? 1.7236 1.8114 1.9057 0.1160  -0.2244 0.0665  253 THR C N   
7748  C CA  . THR C 253 ? 1.7209 1.8270 1.9053 0.1148  -0.2230 0.0632  253 THR C CA  
7749  C C   . THR C 253 ? 1.7711 1.8705 1.9467 0.1210  -0.2371 0.0647  253 THR C C   
7750  O O   . THR C 253 ? 1.7602 1.8359 1.9139 0.1229  -0.2437 0.0721  253 THR C O   
7751  C CB  . THR C 253 ? 1.7530 1.8575 1.9197 0.1066  -0.2106 0.0679  253 THR C CB  
7752  O OG1 . THR C 253 ? 1.7615 1.8499 1.9173 0.1020  -0.2027 0.0735  253 THR C OG1 
7753  C CG2 . THR C 253 ? 1.7124 1.8440 1.8965 0.1025  -0.2009 0.0612  253 THR C CG2 
7754  N N   . PRO C 254 ? 1.9811 2.1008 2.1732 0.1240  -0.2420 0.0579  254 PRO C N   
7755  C CA  . PRO C 254 ? 1.9786 2.0934 2.1621 0.1291  -0.2550 0.0590  254 PRO C CA  
7756  C C   . PRO C 254 ? 2.0103 2.1144 2.1665 0.1249  -0.2523 0.0653  254 PRO C C   
7757  O O   . PRO C 254 ? 2.0190 2.1106 2.1601 0.1288  -0.2635 0.0686  254 PRO C O   
7758  C CB  . PRO C 254 ? 1.9256 2.0679 2.1360 0.1316  -0.2576 0.0496  254 PRO C CB  
7759  C CG  . PRO C 254 ? 1.9068 2.0678 2.1308 0.1254  -0.2429 0.0455  254 PRO C CG  
7760  C CD  . PRO C 254 ? 1.9361 2.0841 2.1553 0.1228  -0.2359 0.0489  254 PRO C CD  
7761  N N   . GLY C 255 ? 1.8589 1.9676 2.0082 0.1173  -0.2382 0.0668  255 GLY C N   
7762  C CA  . GLY C 255 ? 1.8578 1.9559 1.9807 0.1133  -0.2348 0.0725  255 GLY C CA  
7763  C C   . GLY C 255 ? 1.8560 1.9249 1.9506 0.1129  -0.2363 0.0820  255 GLY C C   
7764  O O   . GLY C 255 ? 1.8543 1.9093 1.9252 0.1134  -0.2409 0.0869  255 GLY C O   
7765  N N   . LYS C 256 ? 1.7832 1.8422 1.8797 0.1120  -0.2324 0.0847  256 LYS C N   
7766  C CA  . LYS C 256 ? 1.7754 1.8059 1.8461 0.1114  -0.2334 0.0942  256 LYS C CA  
7767  C C   . LYS C 256 ? 1.7954 1.8087 1.8544 0.1191  -0.2502 0.0976  256 LYS C C   
7768  O O   . LYS C 256 ? 1.8314 1.8197 1.8647 0.1189  -0.2524 0.1063  256 LYS C O   
7769  C CB  . LYS C 256 ? 1.7403 1.7651 1.8194 0.1091  -0.2267 0.0955  256 LYS C CB  
7770  C CG  . LYS C 256 ? 1.7023 1.7342 1.7817 0.1004  -0.2094 0.0960  256 LYS C CG  
7771  C CD  . LYS C 256 ? 1.7127 1.7269 1.7613 0.0951  -0.2026 0.1047  256 LYS C CD  
7772  C CE  . LYS C 256 ? 1.6247 1.6399 1.6732 0.0868  -0.1865 0.1068  256 LYS C CE  
7773  N NZ  . LYS C 256 ? 1.6187 1.6248 1.6764 0.0868  -0.1859 0.1079  256 LYS C NZ  
7774  N N   . SER C 257 ? 1.8013 1.8273 1.8784 0.1257  -0.2620 0.0912  257 SER C N   
7775  C CA  . SER C 257 ? 1.8230 1.8345 1.8917 0.1335  -0.2790 0.0937  257 SER C CA  
7776  C C   . SER C 257 ? 1.8681 1.8647 1.9063 0.1332  -0.2838 0.0997  257 SER C C   
7777  O O   . SER C 257 ? 1.8995 1.8798 1.9250 0.1392  -0.2977 0.1035  257 SER C O   
7778  C CB  . SER C 257 ? 1.7576 1.7896 1.8546 0.1400  -0.2894 0.0845  257 SER C CB  
7779  N N   . LEU C 258 ? 1.8322 1.8340 1.8584 0.1266  -0.2730 0.1004  258 LEU C N   
7780  C CA  . LEU C 258 ? 1.8302 1.8174 1.8258 0.1256  -0.2758 0.1058  258 LEU C CA  
7781  C C   . LEU C 258 ? 1.9504 1.9145 1.9169 0.1204  -0.2666 0.1155  258 LEU C C   
7782  O O   . LEU C 258 ? 2.0124 1.9537 1.9518 0.1227  -0.2740 0.1228  258 LEU C O   
7783  C CB  . LEU C 258 ? 1.7878 1.7942 1.7873 0.1219  -0.2701 0.1002  258 LEU C CB  
7784  C CG  . LEU C 258 ? 1.7078 1.7325 1.7272 0.1270  -0.2816 0.0921  258 LEU C CG  
7785  C CD1 . LEU C 258 ? 1.6221 1.6648 1.6453 0.1223  -0.2739 0.0873  258 LEU C CD1 
7786  C CD2 . LEU C 258 ? 1.6499 1.6583 1.6530 0.1337  -0.2990 0.0951  258 LEU C CD2 
7787  N N   . LYS C 259 ? 2.1452 2.1152 2.1168 0.1135  -0.2505 0.1158  259 LYS C N   
7788  C CA  . LYS C 259 ? 2.1907 2.1403 2.1368 0.1079  -0.2403 0.1248  259 LYS C CA  
7789  C C   . LYS C 259 ? 2.2306 2.1551 2.1648 0.1115  -0.2483 0.1323  259 LYS C C   
7790  O O   . LYS C 259 ? 2.2819 2.1829 2.1860 0.1099  -0.2477 0.1414  259 LYS C O   
7791  C CB  . LYS C 259 ? 2.1899 2.1524 2.1496 0.1004  -0.2229 0.1228  259 LYS C CB  
7792  C CG  . LYS C 259 ? 2.2610 2.2061 2.1964 0.0935  -0.2103 0.1313  259 LYS C CG  
7793  C CD  . LYS C 259 ? 2.3212 2.2815 2.2731 0.0863  -0.1940 0.1284  259 LYS C CD  
7794  C CE  . LYS C 259 ? 2.4117 2.3571 2.3403 0.0790  -0.1806 0.1363  259 LYS C CE  
7795  N NZ  . LYS C 259 ? 2.4017 2.3440 2.3069 0.0773  -0.1779 0.1383  259 LYS C NZ  
7796  N N   . CYS C 260 ? 2.0651 1.9939 2.0224 0.1165  -0.2556 0.1288  260 CYS C N   
7797  C CA  . CYS C 260 ? 2.0747 1.9798 2.0229 0.1208  -0.2646 0.1354  260 CYS C CA  
7798  C C   . CYS C 260 ? 2.1004 1.9921 2.0333 0.1286  -0.2824 0.1382  260 CYS C C   
7799  O O   . CYS C 260 ? 2.1086 1.9744 2.0197 0.1308  -0.2887 0.1470  260 CYS C O   
7800  C CB  . CYS C 260 ? 1.9825 1.8971 1.9615 0.1239  -0.2665 0.1299  260 CYS C CB  
7801  N N   . SER C 261 ? 2.1025 2.0114 2.0468 0.1327  -0.2909 0.1310  261 SER C N   
7802  C CA  . SER C 261 ? 2.1563 2.0541 2.0874 0.1400  -0.3085 0.1329  261 SER C CA  
7803  C C   . SER C 261 ? 2.2897 2.1651 2.1811 0.1375  -0.3082 0.1419  261 SER C C   
7804  O O   . SER C 261 ? 2.2629 2.1178 2.1349 0.1429  -0.3214 0.1479  261 SER C O   
7805  C CB  . SER C 261 ? 2.0742 1.9965 2.0259 0.1435  -0.3159 0.1230  261 SER C CB  
7806  O OG  . SER C 261 ? 2.1237 2.0362 2.0632 0.1505  -0.3333 0.1244  261 SER C OG  
7807  N N   . ALA C 262 ? 2.7841 2.6631 2.6629 0.1296  -0.2933 0.1430  262 ALA C N   
7808  C CA  . ALA C 262 ? 2.8052 2.6633 2.6457 0.1269  -0.2915 0.1512  262 ALA C CA  
7809  C C   . ALA C 262 ? 2.8369 2.6669 2.6553 0.1257  -0.2894 0.1624  262 ALA C C   
7810  O O   . ALA C 262 ? 2.8508 2.6578 2.6377 0.1275  -0.2961 0.1703  262 ALA C O   
7811  C CB  . ALA C 262 ? 2.8067 2.6764 2.6414 0.1188  -0.2750 0.1492  262 ALA C CB  
7812  N N   . LEU C 263 ? 2.3722 2.2032 2.2063 0.1225  -0.2802 0.1632  263 LEU C N   
7813  C CA  . LEU C 263 ? 2.3038 2.1081 2.1188 0.1208  -0.2777 0.1738  263 LEU C CA  
7814  C C   . LEU C 263 ? 2.2381 2.0242 2.0482 0.1297  -0.2963 0.1779  263 LEU C C   
7815  O O   . LEU C 263 ? 2.2408 1.9996 2.0216 0.1303  -0.2999 0.1884  263 LEU C O   
7816  C CB  . LEU C 263 ? 2.4584 2.2696 2.2943 0.1154  -0.2642 0.1725  263 LEU C CB  
7817  C CG  . LEU C 263 ? 2.3570 2.1865 2.2000 0.1066  -0.2456 0.1685  263 LEU C CG  
7818  C CD1 . LEU C 263 ? 2.4335 2.2705 2.2999 0.1023  -0.2349 0.1665  263 LEU C CD1 
7819  C CD2 . LEU C 263 ? 2.3520 2.1662 2.1608 0.1003  -0.2356 0.1766  263 LEU C CD2 
7820  N N   . TYR C 264 ? 2.1588 1.9597 1.9974 0.1368  -0.3081 0.1700  264 TYR C N   
7821  C CA  . TYR C 264 ? 2.1109 1.8967 1.9469 0.1462  -0.3270 0.1730  264 TYR C CA  
7822  C C   . TYR C 264 ? 2.1893 1.9630 1.9969 0.1500  -0.3391 0.1768  264 TYR C C   
7823  O O   . TYR C 264 ? 2.1879 1.9366 1.9735 0.1546  -0.3503 0.1853  264 TYR C O   
7824  C CB  . TYR C 264 ? 2.0406 1.8478 1.9151 0.1528  -0.3361 0.1625  264 TYR C CB  
7825  C CG  . TYR C 264 ? 2.0311 1.8408 1.9289 0.1517  -0.3294 0.1609  264 TYR C CG  
7826  C CD1 . TYR C 264 ? 2.0981 1.8832 1.9804 0.1489  -0.3246 0.1704  264 TYR C CD1 
7827  C CD2 . TYR C 264 ? 2.0304 1.8667 1.9653 0.1531  -0.3276 0.1497  264 TYR C CD2 
7828  C CE1 . TYR C 264 ? 2.1597 1.9465 2.0633 0.1477  -0.3187 0.1685  264 TYR C CE1 
7829  C CE2 . TYR C 264 ? 2.0229 1.8614 1.9785 0.1521  -0.3215 0.1477  264 TYR C CE2 
7830  C CZ  . TYR C 264 ? 2.1123 1.9258 2.0524 0.1494  -0.3173 0.1569  264 TYR C CZ  
7831  O OH  . TYR C 264 ? 2.1564 1.9715 2.1172 0.1482  -0.3116 0.1545  264 TYR C OH  
7832  N N   . LEU C 265 ? 2.2881 2.0791 2.0956 0.1483  -0.3375 0.1706  265 LEU C N   
7833  C CA  . LEU C 265 ? 2.2905 2.0700 2.0691 0.1510  -0.3476 0.1739  265 LEU C CA  
7834  C C   . LEU C 265 ? 2.3189 2.0722 2.0571 0.1456  -0.3394 0.1854  265 LEU C C   
7835  O O   . LEU C 265 ? 2.3088 2.0400 2.0179 0.1494  -0.3505 0.1927  265 LEU C O   
7836  C CB  . LEU C 265 ? 2.2771 2.0808 2.0652 0.1494  -0.3459 0.1644  265 LEU C CB  
7837  C CG  . LEU C 265 ? 2.2473 2.0767 2.0725 0.1550  -0.3558 0.1531  265 LEU C CG  
7838  C CD1 . LEU C 265 ? 2.1768 2.0281 2.0086 0.1522  -0.3523 0.1448  265 LEU C CD1 
7839  C CD2 . LEU C 265 ? 2.2148 2.0340 2.0398 0.1651  -0.3776 0.1542  265 LEU C CD2 
7840  N N   . SER C 266 ? 2.2766 2.0326 2.0126 0.1366  -0.3198 0.1871  266 SER C N   
7841  C CA  . SER C 266 ? 2.2346 1.9658 1.9350 0.1310  -0.3103 0.1985  266 SER C CA  
7842  C C   . SER C 266 ? 2.2597 1.9642 1.9490 0.1343  -0.3175 0.2084  266 SER C C   
7843  O O   . SER C 266 ? 2.3065 1.9848 1.9604 0.1339  -0.3194 0.2189  266 SER C O   
7844  C CB  . SER C 266 ? 2.1434 1.8848 1.8496 0.1210  -0.2880 0.1976  266 SER C CB  
7845  O OG  . SER C 266 ? 2.1094 1.8272 1.7838 0.1153  -0.2778 0.2087  266 SER C OG  
7846  N N   . GLN C 267 ? 2.2116 1.9220 1.9304 0.1377  -0.3214 0.2053  267 GLN C N   
7847  C CA  . GLN C 267 ? 2.1734 1.8590 1.8846 0.1421  -0.3303 0.2139  267 GLN C CA  
7848  C C   . GLN C 267 ? 2.2366 1.9087 1.9335 0.1519  -0.3521 0.2166  267 GLN C C   
7849  O O   . GLN C 267 ? 2.2923 1.9361 1.9646 0.1545  -0.3593 0.2274  267 GLN C O   
7850  C CB  . GLN C 267 ? 2.1336 1.8304 1.8819 0.1438  -0.3295 0.2085  267 GLN C CB  
7851  C CG  . GLN C 267 ? 2.1144 1.7851 1.8566 0.1468  -0.3354 0.2175  267 GLN C CG  
7852  C CD  . GLN C 267 ? 2.0983 1.7811 1.8784 0.1496  -0.3362 0.2106  267 GLN C CD  
7853  O OE1 . GLN C 267 ? 1.9757 1.6843 1.7863 0.1533  -0.3402 0.1992  267 GLN C OE1 
7854  N NE2 . GLN C 267 ? 2.1560 1.8199 1.9342 0.1476  -0.3323 0.2176  267 GLN C NE2 
7855  N N   . PHE C 268 ? 2.2097 1.9013 1.9214 0.1572  -0.3628 0.2072  268 PHE C N   
7856  C CA  . PHE C 268 ? 2.2299 1.9115 1.9283 0.1661  -0.3837 0.2088  268 PHE C CA  
7857  C C   . PHE C 268 ? 2.3888 2.0595 2.0494 0.1638  -0.3840 0.2132  268 PHE C C   
7858  O O   . PHE C 268 ? 2.4143 2.0741 2.0582 0.1706  -0.4010 0.2155  268 PHE C O   
7859  C CB  . PHE C 268 ? 2.1547 1.8629 1.8880 0.1728  -0.3955 0.1962  268 PHE C CB  
7860  C CG  . PHE C 268 ? 2.0972 1.8187 1.8690 0.1754  -0.3950 0.1904  268 PHE C CG  
7861  C CD1 . PHE C 268 ? 2.0627 1.7655 1.8341 0.1761  -0.3939 0.1975  268 PHE C CD1 
7862  C CD2 . PHE C 268 ? 2.0718 1.8244 1.8801 0.1770  -0.3953 0.1777  268 PHE C CD2 
7863  C CE1 . PHE C 268 ? 2.0010 1.7159 1.8075 0.1786  -0.3933 0.1915  268 PHE C CE1 
7864  C CE2 . PHE C 268 ? 2.0415 1.8065 1.8844 0.1794  -0.3944 0.1719  268 PHE C CE2 
7865  C CZ  . PHE C 268 ? 1.9748 1.7211 1.8168 0.1804  -0.3935 0.1785  268 PHE C CZ  
7866  N N   . ARG C 269 ? 2.6826 2.3560 2.3295 0.1544  -0.3656 0.2144  269 ARG C N   
7867  C CA  . ARG C 269 ? 2.7041 2.3644 2.3121 0.1513  -0.3632 0.2196  269 ARG C CA  
7868  C C   . ARG C 269 ? 2.7454 2.3755 2.3186 0.1469  -0.3553 0.2334  269 ARG C C   
7869  O O   . ARG C 269 ? 2.8134 2.4249 2.3492 0.1468  -0.3585 0.2403  269 ARG C O   
7870  C CB  . ARG C 269 ? 2.6881 2.3706 2.3017 0.1442  -0.3481 0.2118  269 ARG C CB  
7871  C CG  . ARG C 269 ? 2.6970 2.3735 2.2786 0.1438  -0.3513 0.2124  269 ARG C CG  
7872  C CD  . ARG C 269 ? 2.6910 2.3621 2.2670 0.1535  -0.3750 0.2110  269 ARG C CD  
7873  N NE  . ARG C 269 ? 2.6779 2.3723 2.2687 0.1552  -0.3804 0.1995  269 ARG C NE  
7874  C CZ  . ARG C 269 ? 2.6825 2.3770 2.2708 0.1627  -0.4000 0.1962  269 ARG C CZ  
7875  N NH1 . ARG C 269 ? 2.7315 2.4040 2.3025 0.1696  -0.4163 0.2036  269 ARG C NH1 
7876  N NH2 . ARG C 269 ? 2.6297 2.3460 2.2328 0.1632  -0.4034 0.1855  269 ARG C NH2 
7877  N N   . GLU C 270 ? 2.5628 2.1880 2.1469 0.1427  -0.3442 0.2375  270 GLU C N   
7878  C CA  . GLU C 270 ? 2.5802 2.1743 2.1341 0.1399  -0.3400 0.2515  270 GLU C CA  
7879  C C   . GLU C 270 ? 2.5765 2.1488 2.1219 0.1493  -0.3605 0.2582  270 GLU C C   
7880  O O   . GLU C 270 ? 2.6532 2.2004 2.1618 0.1513  -0.3679 0.2679  270 GLU C O   
7881  C CB  . GLU C 270 ? 2.5244 2.1206 2.0949 0.1323  -0.3222 0.2533  270 GLU C CB  
7882  N N   . THR C 271 ? 2.4788 2.0603 2.0580 0.1552  -0.3697 0.2530  271 THR C N   
7883  C CA  . THR C 271 ? 2.4423 2.0058 2.0194 0.1650  -0.3898 0.2579  271 THR C CA  
7884  C C   . THR C 271 ? 2.4656 2.0439 2.0561 0.1744  -0.4092 0.2491  271 THR C C   
7885  O O   . THR C 271 ? 2.4123 2.0201 2.0351 0.1749  -0.4079 0.2366  271 THR C O   
7886  C CB  . THR C 271 ? 2.3329 1.8958 1.9392 0.1664  -0.3885 0.2577  271 THR C CB  
7887  O OG1 . THR C 271 ? 2.2153 1.8072 1.8638 0.1711  -0.3941 0.2442  271 THR C OG1 
7888  C CG2 . THR C 271 ? 2.3221 1.8835 1.9290 0.1554  -0.3660 0.2611  271 THR C CG2 
7889  N N   . SER C 272 ? 2.5791 2.1367 2.1449 0.1819  -0.4274 0.2559  272 SER C N   
7890  C CA  . SER C 272 ? 2.5889 2.1555 2.1632 0.1917  -0.4486 0.2494  272 SER C CA  
7891  C C   . SER C 272 ? 2.6302 2.2266 2.2193 0.1897  -0.4458 0.2367  272 SER C C   
7892  O O   . SER C 272 ? 2.5301 2.1532 2.1584 0.1919  -0.4471 0.2253  272 SER C O   
7893  C CB  . SER C 272 ? 2.4587 2.0311 2.0681 0.2003  -0.4616 0.2452  272 SER C CB  
7894  O OG  . SER C 272 ? 2.3287 1.9277 1.9782 0.1970  -0.4498 0.2349  272 SER C OG  
7895  N N   . PRO C 273 ? 2.9443 2.5369 2.5030 0.1856  -0.4418 0.2383  273 PRO C N   
7896  C CA  . PRO C 273 ? 2.9182 2.5379 2.4900 0.1835  -0.4391 0.2264  273 PRO C CA  
7897  C C   . PRO C 273 ? 2.8968 2.5258 2.4779 0.1926  -0.4608 0.2196  273 PRO C C   
7898  O O   . PRO C 273 ? 2.8672 2.5224 2.4699 0.1919  -0.4603 0.2082  273 PRO C O   
7899  C CB  . PRO C 273 ? 2.9452 2.5527 2.4769 0.1764  -0.4282 0.2319  273 PRO C CB  
7900  C CG  . PRO C 273 ? 2.9805 2.5542 2.4752 0.1808  -0.4398 0.2449  273 PRO C CG  
7901  C CD  . PRO C 273 ? 2.9840 2.5465 2.4940 0.1838  -0.4423 0.2508  273 PRO C CD  
7902  N N   . HIS C 274 ? 2.6945 2.3027 2.2597 0.2009  -0.4801 0.2262  274 HIS C N   
7903  C CA  . HIS C 274 ? 2.6668 2.2834 2.2402 0.2097  -0.5017 0.2198  274 HIS C CA  
7904  C C   . HIS C 274 ? 2.5900 2.2352 2.2135 0.2141  -0.5066 0.2079  274 HIS C C   
7905  O O   . HIS C 274 ? 2.5665 2.2284 2.2055 0.2190  -0.5197 0.1991  274 HIS C O   
7906  C CB  . HIS C 274 ? 2.7245 2.3122 2.2720 0.2181  -0.5213 0.2301  274 HIS C CB  
7907  C CG  . HIS C 274 ? 2.7787 2.3468 2.3268 0.2195  -0.5193 0.2397  274 HIS C CG  
7908  N ND1 . HIS C 274 ? 2.8457 2.3876 2.3605 0.2137  -0.5076 0.2524  274 HIS C ND1 
7909  C CD2 . HIS C 274 ? 2.7767 2.3475 2.3552 0.2260  -0.5274 0.2383  274 HIS C CD2 
7910  C CE1 . HIS C 274 ? 2.8655 2.3943 2.3902 0.2164  -0.5088 0.2585  274 HIS C CE1 
7911  N NE2 . HIS C 274 ? 2.8521 2.3979 2.4151 0.2241  -0.5208 0.2500  274 HIS C NE2 
7912  N N   . ILE C 275 ? 2.4802 2.1314 2.1295 0.2122  -0.4961 0.2074  275 ILE C N   
7913  C CA  . ILE C 275 ? 2.3481 2.0288 2.0451 0.2147  -0.4966 0.1953  275 ILE C CA  
7914  C C   . ILE C 275 ? 2.2930 2.0015 2.0050 0.2075  -0.4831 0.1851  275 ILE C C   
7915  O O   . ILE C 275 ? 2.2025 1.9379 1.9502 0.2099  -0.4864 0.1738  275 ILE C O   
7916  C CB  . ILE C 275 ? 2.2623 1.9404 1.9802 0.2141  -0.4882 0.1976  275 ILE C CB  
7917  C CG1 . ILE C 275 ? 2.2321 1.9163 1.9497 0.2029  -0.4633 0.1979  275 ILE C CG1 
7918  C CG2 . ILE C 275 ? 2.2832 1.9280 1.9773 0.2189  -0.4974 0.2104  275 ILE C CG2 
7919  C CD1 . ILE C 275 ? 2.0929 1.7856 1.8420 0.2017  -0.4539 0.1952  275 ILE C CD1 
7920  N N   . LEU C 276 ? 2.2796 1.9823 1.9654 0.1987  -0.4677 0.1887  276 LEU C N   
7921  C CA  . LEU C 276 ? 2.2421 1.9686 1.9379 0.1919  -0.4549 0.1799  276 LEU C CA  
7922  C C   . LEU C 276 ? 2.2960 2.0224 1.9716 0.1936  -0.4658 0.1773  276 LEU C C   
7923  O O   . LEU C 276 ? 2.3803 2.0822 2.0186 0.1954  -0.4734 0.1857  276 LEU C O   
7924  C CB  . LEU C 276 ? 2.2654 1.9866 1.9454 0.1815  -0.4318 0.1848  276 LEU C CB  
7925  C CG  . LEU C 276 ? 2.2366 1.9630 1.9396 0.1777  -0.4176 0.1853  276 LEU C CG  
7926  C CD1 . LEU C 276 ? 2.2834 2.0173 1.9813 0.1669  -0.3945 0.1850  276 LEU C CD1 
7927  C CD2 . LEU C 276 ? 2.1561 1.9078 1.9048 0.1823  -0.4230 0.1749  276 LEU C CD2 
7928  N N   . ALA C 277 ? 2.2432 1.9964 1.9432 0.1931  -0.4665 0.1658  277 ALA C N   
7929  C CA  . ALA C 277 ? 2.2672 2.0225 1.9508 0.1940  -0.4758 0.1619  277 ALA C CA  
7930  C C   . ALA C 277 ? 2.3450 2.0877 1.9915 0.1862  -0.4621 0.1669  277 ALA C C   
7931  O O   . ALA C 277 ? 2.3056 2.0575 1.9571 0.1783  -0.4422 0.1655  277 ALA C O   
7932  C CB  . ALA C 277 ? 2.2295 2.0173 1.9496 0.1940  -0.4772 0.1485  277 ALA C CB  
7933  N N   . SER C 278 ? 2.4058 2.1272 2.0147 0.1887  -0.4728 0.1725  278 SER C N   
7934  C CA  . SER C 278 ? 2.4292 2.1375 2.0000 0.1823  -0.4617 0.1768  278 SER C CA  
7935  C C   . SER C 278 ? 2.4885 2.1941 2.0403 0.1860  -0.4776 0.1730  278 SER C C   
7936  O O   . SER C 278 ? 2.5517 2.2331 2.0666 0.1890  -0.4875 0.1805  278 SER C O   
7937  C CB  . SER C 278 ? 2.4620 2.1399 1.9977 0.1804  -0.4555 0.1907  278 SER C CB  
7938  O OG  . SER C 278 ? 2.4723 2.1332 2.0044 0.1885  -0.4725 0.1974  278 SER C OG  
7939  N N   . GLY C 279 ? 2.5939 2.3249 2.1712 0.1857  -0.4801 0.1611  279 GLY C N   
7940  C CA  . GLY C 279 ? 2.5793 2.3111 2.1436 0.1887  -0.4949 0.1558  279 GLY C CA  
7941  C C   . GLY C 279 ? 2.6494 2.3688 2.1746 0.1830  -0.4855 0.1579  279 GLY C C   
7942  O O   . GLY C 279 ? 2.7473 2.4447 2.2355 0.1858  -0.4961 0.1635  279 GLY C O   
7943  N N   . ASP C 280 ? 2.4102 2.1435 1.9431 0.1750  -0.4657 0.1536  280 ASP C N   
7944  C CA  . ASP C 280 ? 2.4634 2.1865 1.9618 0.1689  -0.4535 0.1552  280 ASP C CA  
7945  C C   . ASP C 280 ? 2.5799 2.2974 2.0557 0.1720  -0.4689 0.1509  280 ASP C C   
7946  O O   . ASP C 280 ? 2.6072 2.3015 2.0407 0.1723  -0.4716 0.1573  280 ASP C O   
7947  C CB  . ASP C 280 ? 2.5052 2.2015 1.9684 0.1662  -0.4433 0.1683  280 ASP C CB  
7948  C CG  . ASP C 280 ? 2.4214 2.1236 1.9051 0.1616  -0.4255 0.1719  280 ASP C CG  
7949  O OD1 . ASP C 280 ? 2.3919 2.0989 1.9020 0.1655  -0.4316 0.1728  280 ASP C OD1 
7950  O OD2 . ASP C 280 ? 2.4120 2.1138 1.8853 0.1540  -0.4055 0.1737  280 ASP C OD2 
7951  N N   . GLY C 281 ? 2.3828 2.1219 1.8874 0.1745  -0.4794 0.1399  281 GLY C N   
7952  C CA  . GLY C 281 ? 2.3249 2.0606 1.8126 0.1777  -0.4956 0.1346  281 GLY C CA  
7953  C C   . GLY C 281 ? 2.1824 1.9437 1.7103 0.1809  -0.5083 0.1231  281 GLY C C   
7954  O O   . GLY C 281 ? 2.0817 1.8654 1.6489 0.1791  -0.5006 0.1181  281 GLY C O   
7955  N N   . THR C 282 ? 2.2254 1.9830 1.7424 0.1857  -0.5281 0.1189  282 THR C N   
7956  C CA  . THR C 282 ? 2.1921 1.9722 1.7443 0.1892  -0.5427 0.1080  282 THR C CA  
7957  C C   . THR C 282 ? 2.2997 2.0666 1.8365 0.1975  -0.5688 0.1092  282 THR C C   
7958  O O   . THR C 282 ? 2.3433 2.1094 1.8674 0.1986  -0.5807 0.1034  282 THR C O   
7959  C CB  . THR C 282 ? 2.0803 1.8773 1.6408 0.1834  -0.5355 0.0974  282 THR C CB  
7960  O OG1 . THR C 282 ? 2.1303 1.9091 1.6477 0.1797  -0.5287 0.1000  282 THR C OG1 
7961  C CG2 . THR C 282 ? 1.9795 1.7993 1.5745 0.1773  -0.5154 0.0933  282 THR C CG2 
7962  N N   . ASN C 283 ? 2.4099 2.1659 1.9479 0.2038  -0.5783 0.1169  283 ASN C N   
7963  C CA  . ASN C 283 ? 2.4586 2.2055 1.9906 0.2127  -0.6042 0.1177  283 ASN C CA  
7964  C C   . ASN C 283 ? 2.3822 2.1508 1.9629 0.2179  -0.6140 0.1123  283 ASN C C   
7965  O O   . ASN C 283 ? 2.3821 2.1417 1.9669 0.2247  -0.6248 0.1184  283 ASN C O   
7966  C CB  . ASN C 283 ? 2.5310 2.2461 2.0235 0.2167  -0.6096 0.1313  283 ASN C CB  
7967  C CG  . ASN C 283 ? 2.6821 2.3776 2.1326 0.2100  -0.5915 0.1386  283 ASN C CG  
7968  O OD1 . ASN C 283 ? 2.7304 2.4303 2.1688 0.2042  -0.5825 0.1331  283 ASN C OD1 
7969  N ND2 . ASN C 283 ? 2.7799 2.4535 2.2084 0.2106  -0.5861 0.1511  283 ASN C ND2 
7970  N N   . ARG C 284 ? 2.1957 1.9926 1.8132 0.2147  -0.6100 0.1009  284 ARG C N   
7971  C CA  . ARG C 284 ? 2.0917 1.9143 1.7598 0.2170  -0.6118 0.0945  284 ARG C CA  
7972  C C   . ARG C 284 ? 2.0273 1.8542 1.7119 0.2138  -0.5925 0.0991  284 ARG C C   
7973  O O   . ARG C 284 ? 1.9481 1.7966 1.6743 0.2150  -0.5910 0.0940  284 ARG C O   
7974  C CB  . ARG C 284 ? 2.1120 1.9345 1.7949 0.2271  -0.6363 0.0941  284 ARG C CB  
7975  C CG  . ARG C 284 ? 2.0963 1.9402 1.8060 0.2293  -0.6517 0.0821  284 ARG C CG  
7976  C CD  . ARG C 284 ? 2.1612 2.0106 1.8960 0.2390  -0.6728 0.0809  284 ARG C CD  
7977  N NE  . ARG C 284 ? 2.2780 2.1527 2.0470 0.2402  -0.6846 0.0687  284 ARG C NE  
7978  C CZ  . ARG C 284 ? 2.3113 2.2121 2.1279 0.2415  -0.6840 0.0618  284 ARG C CZ  
7979  N NH1 . ARG C 284 ? 2.2635 2.1680 2.0985 0.2421  -0.6725 0.0657  284 ARG C NH1 
7980  N NH2 . ARG C 284 ? 2.3789 2.3018 2.2245 0.2422  -0.6947 0.0510  284 ARG C NH2 
7981  N N   . LYS C 285 ? 2.0474 1.8544 1.7006 0.2097  -0.5777 0.1086  285 LYS C N   
7982  C CA  . LYS C 285 ? 2.0105 1.8199 1.6754 0.2055  -0.5580 0.1132  285 LYS C CA  
7983  C C   . LYS C 285 ? 2.0029 1.8236 1.6682 0.1959  -0.5361 0.1092  285 LYS C C   
7984  O O   . LYS C 285 ? 2.0500 1.8596 1.6832 0.1921  -0.5319 0.1101  285 LYS C O   
7985  C CB  . LYS C 285 ? 2.0434 1.8232 1.6743 0.2070  -0.5557 0.1266  285 LYS C CB  
7986  N N   . PRO C 286 ? 1.9433 1.7857 1.6436 0.1921  -0.5220 0.1048  286 PRO C N   
7987  C CA  . PRO C 286 ? 1.8983 1.7531 1.6016 0.1833  -0.5020 0.1005  286 PRO C CA  
7988  C C   . PRO C 286 ? 1.9399 1.7746 1.6085 0.1779  -0.4851 0.1096  286 PRO C C   
7989  O O   . PRO C 286 ? 2.0155 1.8273 1.6592 0.1803  -0.4873 0.1196  286 PRO C O   
7990  C CB  . PRO C 286 ? 1.8265 1.7073 1.5756 0.1818  -0.4929 0.0951  286 PRO C CB  
7991  C CG  . PRO C 286 ? 1.9048 1.7920 1.6787 0.1901  -0.5116 0.0928  286 PRO C CG  
7992  C CD  . PRO C 286 ? 1.9258 1.7847 1.6668 0.1961  -0.5253 0.1021  286 PRO C CD  
7993  N N   . THR C 287 ? 1.9356 1.7798 1.6036 0.1703  -0.4677 0.1060  287 THR C N   
7994  C CA  . THR C 287 ? 1.9416 1.7707 1.5804 0.1642  -0.4494 0.1132  287 THR C CA  
7995  C C   . THR C 287 ? 1.9131 1.7458 1.5696 0.1620  -0.4354 0.1180  287 THR C C   
7996  O O   . THR C 287 ? 1.8494 1.7032 1.5351 0.1577  -0.4226 0.1128  287 THR C O   
7997  C CB  . THR C 287 ? 1.8403 1.6793 1.4747 0.1574  -0.4365 0.1069  287 THR C CB  
7998  O OG1 . THR C 287 ? 1.7826 1.6489 1.4550 0.1571  -0.4390 0.0961  287 THR C OG1 
7999  C CG2 . THR C 287 ? 1.8475 1.6686 1.4423 0.1581  -0.4442 0.1076  287 THR C CG2 
8000  N N   . ILE C 288 ? 2.0761 1.8875 1.7142 0.1647  -0.4379 0.1280  288 ILE C N   
8001  C CA  . ILE C 288 ? 2.1133 1.9249 1.7657 0.1629  -0.4261 0.1332  288 ILE C CA  
8002  C C   . ILE C 288 ? 2.1548 1.9534 1.7806 0.1555  -0.4060 0.1401  288 ILE C C   
8003  O O   . ILE C 288 ? 2.1671 1.9428 1.7534 0.1550  -0.4068 0.1470  288 ILE C O   
8004  C CB  . ILE C 288 ? 2.1844 1.9806 1.8352 0.1703  -0.4405 0.1400  288 ILE C CB  
8005  C CG1 . ILE C 288 ? 2.1585 1.9735 1.8460 0.1770  -0.4568 0.1320  288 ILE C CG1 
8006  C CG2 . ILE C 288 ? 2.1962 1.9846 1.8497 0.1675  -0.4272 0.1476  288 ILE C CG2 
8007  C CD1 . ILE C 288 ? 2.3388 2.1379 2.0193 0.1859  -0.4773 0.1369  288 ILE C CD1 
8008  N N   . ILE C 289 ? 2.1185 1.9320 1.7660 0.1498  -0.3880 0.1382  289 ILE C N   
8009  C CA  . ILE C 289 ? 2.1649 1.9708 1.7929 0.1421  -0.3675 0.1431  289 ILE C CA  
8010  C C   . ILE C 289 ? 2.2633 2.0611 1.8956 0.1403  -0.3577 0.1510  289 ILE C C   
8011  O O   . ILE C 289 ? 2.1270 1.9351 1.7722 0.1341  -0.3399 0.1503  289 ILE C O   
8012  C CB  . ILE C 289 ? 2.0173 1.8468 1.6643 0.1361  -0.3533 0.1344  289 ILE C CB  
8013  C CG1 . ILE C 289 ? 1.9227 1.7672 1.5821 0.1390  -0.3659 0.1245  289 ILE C CG1 
8014  C CG2 . ILE C 289 ? 2.1282 1.9475 1.7457 0.1294  -0.3368 0.1381  289 ILE C CG2 
8015  C CD1 . ILE C 289 ? 1.9351 1.7632 1.5583 0.1405  -0.3748 0.1253  289 ILE C CD1 
8016  N N   . GLY C 290 ? 2.7961 2.5751 2.4177 0.1456  -0.3695 0.1584  290 GLY C N   
8017  C CA  . GLY C 290 ? 2.8134 2.5800 2.4338 0.1439  -0.3613 0.1670  290 GLY C CA  
8018  C C   . GLY C 290 ? 2.7847 2.5700 2.4466 0.1442  -0.3574 0.1627  290 GLY C C   
8019  O O   . GLY C 290 ? 2.7549 2.5658 2.4460 0.1420  -0.3517 0.1534  290 GLY C O   
8020  N N   . ASP C 291 ? 2.3918 2.1637 2.0556 0.1468  -0.3604 0.1695  291 ASP C N   
8021  C CA  . ASP C 291 ? 2.2508 2.0371 1.9513 0.1473  -0.3568 0.1662  291 ASP C CA  
8022  C C   . ASP C 291 ? 2.1667 1.9777 1.9028 0.1527  -0.3684 0.1552  291 ASP C C   
8023  O O   . ASP C 291 ? 2.0799 1.9156 1.8462 0.1497  -0.3596 0.1471  291 ASP C O   
8024  C CB  . ASP C 291 ? 2.1371 1.9343 1.8476 0.1384  -0.3343 0.1654  291 ASP C CB  
8025  C CG  . ASP C 291 ? 2.1899 1.9681 1.8895 0.1353  -0.3253 0.1751  291 ASP C CG  
8026  O OD1 . ASP C 291 ? 2.2480 2.0007 1.9227 0.1388  -0.3343 0.1842  291 ASP C OD1 
8027  O OD2 . ASP C 291 ? 2.1934 1.9821 1.9095 0.1294  -0.3096 0.1738  291 ASP C OD2 
8028  N N   . VAL C 292 ? 2.1510 1.9551 1.8831 0.1607  -0.3886 0.1550  292 VAL C N   
8029  C CA  . VAL C 292 ? 2.0968 1.9226 1.8608 0.1664  -0.4016 0.1450  292 VAL C CA  
8030  C C   . VAL C 292 ? 2.1376 1.9534 1.9097 0.1753  -0.4189 0.1478  292 VAL C C   
8031  O O   . VAL C 292 ? 2.1682 1.9594 1.9118 0.1794  -0.4300 0.1558  292 VAL C O   
8032  C CB  . VAL C 292 ? 2.0854 1.9169 1.8389 0.1674  -0.4104 0.1398  292 VAL C CB  
8033  C CG1 . VAL C 292 ? 2.0346 1.8905 1.8241 0.1725  -0.4226 0.1291  292 VAL C CG1 
8034  C CG2 . VAL C 292 ? 2.0690 1.9074 1.8111 0.1589  -0.3935 0.1377  292 VAL C CG2 
8035  N N   . TYR C 293 ? 2.1266 1.9613 1.9370 0.1785  -0.4212 0.1411  293 TYR C N   
8036  C CA  . TYR C 293 ? 2.1554 1.9859 1.9803 0.1879  -0.4388 0.1412  293 TYR C CA  
8037  C C   . TYR C 293 ? 2.1735 2.0272 2.0252 0.1929  -0.4516 0.1304  293 TYR C C   
8038  O O   . TYR C 293 ? 2.1541 2.0343 2.0366 0.1902  -0.4439 0.1214  293 TYR C O   
8039  C CB  . TYR C 293 ? 2.1708 2.0039 2.0198 0.1885  -0.4324 0.1416  293 TYR C CB  
8040  C CG  . TYR C 293 ? 2.1671 2.0012 2.0377 0.1986  -0.4501 0.1393  293 TYR C CG  
8041  C CD1 . TYR C 293 ? 2.1843 2.0458 2.0958 0.2017  -0.4529 0.1284  293 TYR C CD1 
8042  C CD2 . TYR C 293 ? 2.1652 1.9729 2.0153 0.2052  -0.4644 0.1479  293 TYR C CD2 
8043  C CE1 . TYR C 293 ? 2.1520 2.0152 2.0843 0.2112  -0.4689 0.1258  293 TYR C CE1 
8044  C CE2 . TYR C 293 ? 2.1655 1.9742 2.0362 0.2149  -0.4810 0.1456  293 TYR C CE2 
8045  C CZ  . TYR C 293 ? 2.1065 1.9433 2.0187 0.2179  -0.4831 0.1343  293 TYR C CZ  
8046  O OH  . TYR C 293 ? 2.0102 1.8487 1.9439 0.2278  -0.4993 0.1316  293 TYR C OH  
8047  N N   . ILE C 294 ? 2.3935 2.2373 2.2332 0.1999  -0.4710 0.1316  294 ILE C N   
8048  C CA  . ILE C 294 ? 2.3602 2.2239 2.2233 0.2050  -0.4853 0.1220  294 ILE C CA  
8049  C C   . ILE C 294 ? 2.3476 2.2075 2.2274 0.2151  -0.5031 0.1221  294 ILE C C   
8050  O O   . ILE C 294 ? 2.3756 2.2102 2.2313 0.2202  -0.5143 0.1307  294 ILE C O   
8051  C CB  . ILE C 294 ? 2.3776 2.2348 2.2139 0.2046  -0.4940 0.1219  294 ILE C CB  
8052  C CG1 . ILE C 294 ? 2.4027 2.2710 2.2324 0.1951  -0.4768 0.1184  294 ILE C CG1 
8053  C CG2 . ILE C 294 ? 2.3429 2.2145 2.2003 0.2117  -0.5135 0.1138  294 ILE C CG2 
8054  C CD1 . ILE C 294 ? 2.5163 2.3788 2.3202 0.1943  -0.4844 0.1174  294 ILE C CD1 
8055  N N   . HIS C 295 ? 1.9490 1.8340 1.8701 0.2183  -0.5055 0.1127  295 HIS C N   
8056  C CA  . HIS C 295 ? 1.7321 1.6165 1.6725 0.2284  -0.5229 0.1114  295 HIS C CA  
8057  C C   . HIS C 295 ? 1.6677 1.5495 1.6001 0.2348  -0.5441 0.1097  295 HIS C C   
8058  O O   . HIS C 295 ? 1.7404 1.6339 1.6703 0.2314  -0.5446 0.1045  295 HIS C O   
8059  C CB  . HIS C 295 ? 1.6477 1.5608 1.6348 0.2298  -0.5189 0.1012  295 HIS C CB  
8060  C CG  . HIS C 295 ? 1.5254 1.4366 1.5335 0.2399  -0.5330 0.1005  295 HIS C CG  
8061  N ND1 . HIS C 295 ? 1.4597 1.3778 1.4822 0.2484  -0.5530 0.0958  295 HIS C ND1 
8062  C CD2 . HIS C 295 ? 1.4869 1.3897 1.5045 0.2429  -0.5302 0.1036  295 HIS C CD2 
8063  C CE1 . HIS C 295 ? 1.3567 1.2710 1.3967 0.2565  -0.5618 0.0961  295 HIS C CE1 
8064  N NE2 . HIS C 295 ? 1.3624 1.2671 1.3997 0.2534  -0.5483 0.1007  295 HIS C NE2 
8065  N N   . PRO C 296 ? 1.5495 1.4154 1.4772 0.2441  -0.5621 0.1142  296 PRO C N   
8066  C CA  . PRO C 296 ? 1.4768 1.3403 1.3974 0.2506  -0.5837 0.1124  296 PRO C CA  
8067  C C   . PRO C 296 ? 1.4733 1.3681 1.4331 0.2534  -0.5914 0.0996  296 PRO C C   
8068  O O   . PRO C 296 ? 1.4726 1.3698 1.4269 0.2562  -0.6061 0.0965  296 PRO C O   
8069  C CB  . PRO C 296 ? 1.4342 1.2744 1.3456 0.2603  -0.5997 0.1203  296 PRO C CB  
8070  C CG  . PRO C 296 ? 1.4280 1.2687 1.3584 0.2601  -0.5880 0.1218  296 PRO C CG  
8071  C CD  . PRO C 296 ? 1.5579 1.4036 1.4812 0.2487  -0.5638 0.1222  296 PRO C CD  
8072  N N   . SER C 297 ? 1.4654 1.3842 1.4639 0.2525  -0.5821 0.0920  297 SER C N   
8073  C CA  . SER C 297 ? 1.4538 1.4030 1.4914 0.2550  -0.5886 0.0800  297 SER C CA  
8074  C C   . SER C 297 ? 1.5389 1.5088 1.5824 0.2460  -0.5766 0.0730  297 SER C C   
8075  O O   . SER C 297 ? 1.5155 1.5126 1.5929 0.2464  -0.5784 0.0629  297 SER C O   
8076  C CB  . SER C 297 ? 1.4538 1.4194 1.5310 0.2588  -0.5848 0.0747  297 SER C CB  
8077  O OG  . SER C 297 ? 1.4974 1.4918 1.6124 0.2620  -0.5921 0.0635  297 SER C OG  
8078  N N   . VAL C 298 ? 1.6413 1.5991 1.6531 0.2380  -0.5641 0.0782  298 VAL C N   
8079  C CA  . VAL C 298 ? 1.7456 1.7213 1.7616 0.2294  -0.5520 0.0721  298 VAL C CA  
8080  C C   . VAL C 298 ? 1.8081 1.7844 1.8127 0.2305  -0.5664 0.0688  298 VAL C C   
8081  O O   . VAL C 298 ? 1.7734 1.7315 1.7573 0.2366  -0.5837 0.0732  298 VAL C O   
8082  C CB  . VAL C 298 ? 1.7933 1.7570 1.7821 0.2204  -0.5317 0.0784  298 VAL C CB  
8083  C CG1 . VAL C 298 ? 1.7323 1.6894 1.7265 0.2201  -0.5203 0.0833  298 VAL C CG1 
8084  C CG2 . VAL C 298 ? 1.8734 1.8096 1.8163 0.2196  -0.5370 0.0867  298 VAL C CG2 
8085  N N   . LYS C 299 ? 1.9546 1.9521 1.9731 0.2245  -0.5594 0.0609  299 LYS C N   
8086  C CA  . LYS C 299 ? 2.0095 2.0089 2.0171 0.2236  -0.5701 0.0569  299 LYS C CA  
8087  C C   . LYS C 299 ? 2.1104 2.1052 2.0931 0.2140  -0.5539 0.0585  299 LYS C C   
8088  O O   . LYS C 299 ? 2.1629 2.1737 2.1615 0.2073  -0.5362 0.0552  299 LYS C O   
8089  C CB  . LYS C 299 ? 2.0904 2.1195 2.1388 0.2251  -0.5774 0.0454  299 LYS C CB  
8090  C CG  . LYS C 299 ? 2.1754 2.2092 2.2168 0.2233  -0.5874 0.0401  299 LYS C CG  
8091  C CD  . LYS C 299 ? 2.3587 2.4223 2.4434 0.2249  -0.5946 0.0291  299 LYS C CD  
8092  C CE  . LYS C 299 ? 2.3631 2.4277 2.4661 0.2354  -0.6142 0.0281  299 LYS C CE  
8093  N NZ  . LYS C 299 ? 2.3137 2.3578 2.3886 0.2410  -0.6348 0.0316  299 LYS C NZ  
8094  N N   . LEU C 300 ? 2.0692 2.0422 2.0129 0.2136  -0.5600 0.0635  300 LEU C N   
8095  C CA  . LEU C 300 ? 2.1038 2.0682 2.0188 0.2053  -0.5450 0.0663  300 LEU C CA  
8096  C C   . LEU C 300 ? 2.0699 2.0345 1.9706 0.2038  -0.5543 0.0614  300 LEU C C   
8097  O O   . LEU C 300 ? 2.1375 2.1022 2.0415 0.2097  -0.5743 0.0583  300 LEU C O   
8098  C CB  . LEU C 300 ? 2.0924 2.0267 1.9675 0.2050  -0.5397 0.0781  300 LEU C CB  
8099  C CG  . LEU C 300 ? 2.0706 1.9993 1.9530 0.2058  -0.5300 0.0843  300 LEU C CG  
8100  C CD1 . LEU C 300 ? 2.1383 2.0355 1.9782 0.2054  -0.5268 0.0962  300 LEU C CD1 
8101  C CD2 . LEU C 300 ? 2.0753 2.0241 1.9817 0.1986  -0.5088 0.0803  300 LEU C CD2 
8102  N N   . HIS C 301 ? 2.0758 2.0404 1.9609 0.1958  -0.5397 0.0607  301 HIS C N   
8103  C CA  . HIS C 301 ? 1.9758 1.9374 1.8419 0.1934  -0.5458 0.0567  301 HIS C CA  
8104  C C   . HIS C 301 ? 1.9696 1.9074 1.7910 0.1889  -0.5350 0.0641  301 HIS C C   
8105  O O   . HIS C 301 ? 1.9530 1.8896 1.7705 0.1835  -0.5155 0.0681  301 HIS C O   
8106  C CB  . HIS C 301 ? 2.0014 1.9898 1.8966 0.1877  -0.5384 0.0464  301 HIS C CB  
8107  C CG  . HIS C 301 ? 1.9923 1.9813 1.8775 0.1868  -0.5497 0.0402  301 HIS C CG  
8108  N ND1 . HIS C 301 ? 1.9450 1.9195 1.7954 0.1822  -0.5440 0.0417  301 HIS C ND1 
8109  C CD2 . HIS C 301 ? 2.0182 2.0204 1.9238 0.1900  -0.5665 0.0323  301 HIS C CD2 
8110  C CE1 . HIS C 301 ? 1.9077 1.8861 1.7572 0.1825  -0.5569 0.0347  301 HIS C CE1 
8111  N NE2 . HIS C 301 ? 1.9556 1.9508 1.8385 0.1870  -0.5708 0.0290  301 HIS C NE2 
8112  N N   . PRO C 302 ? 1.9256 1.8445 1.7127 0.1909  -0.5470 0.0662  302 PRO C N   
8113  C CA  . PRO C 302 ? 1.9072 1.8019 1.6496 0.1872  -0.5372 0.0739  302 PRO C CA  
8114  C C   . PRO C 302 ? 1.8421 1.7445 1.5805 0.1784  -0.5173 0.0705  302 PRO C C   
8115  O O   . PRO C 302 ? 1.7994 1.6845 1.5055 0.1746  -0.5050 0.0770  302 PRO C O   
8116  C CB  . PRO C 302 ? 1.8921 1.7691 1.6035 0.1918  -0.5568 0.0745  302 PRO C CB  
8117  C CG  . PRO C 302 ? 1.8759 1.7633 1.6146 0.1996  -0.5780 0.0702  302 PRO C CG  
8118  C CD  . PRO C 302 ? 1.9249 1.8429 1.7119 0.1971  -0.5708 0.0619  302 PRO C CD  
8119  N N   . THR C 303 ? 1.8253 1.7526 1.5954 0.1749  -0.5136 0.0609  303 THR C N   
8120  C CA  . THR C 303 ? 1.7726 1.7074 1.5401 0.1669  -0.4955 0.0575  303 THR C CA  
8121  C C   . THR C 303 ? 1.7179 1.6623 1.5020 0.1622  -0.4744 0.0603  303 THR C C   
8122  O O   . THR C 303 ? 1.6596 1.6088 1.4402 0.1555  -0.4579 0.0586  303 THR C O   
8123  C CB  . THR C 303 ? 1.7547 1.7112 1.5478 0.1649  -0.5007 0.0461  303 THR C CB  
8124  O OG1 . THR C 303 ? 1.8023 1.7817 1.6392 0.1672  -0.5049 0.0415  303 THR C OG1 
8125  C CG2 . THR C 303 ? 1.7323 1.6786 1.5057 0.1684  -0.5203 0.0427  303 THR C CG2 
8126  N N   . ALA C 304 ? 1.6882 1.6351 1.4899 0.1655  -0.4747 0.0642  304 ALA C N   
8127  C CA  . ALA C 304 ? 1.6494 1.6053 1.4677 0.1614  -0.4558 0.0666  304 ALA C CA  
8128  C C   . ALA C 304 ? 1.6433 1.5761 1.4276 0.1592  -0.4443 0.0768  304 ALA C C   
8129  O O   . ALA C 304 ? 1.6928 1.6030 1.4491 0.1634  -0.4538 0.0837  304 ALA C O   
8130  C CB  . ALA C 304 ? 1.6895 1.6586 1.5426 0.1660  -0.4612 0.0656  304 ALA C CB  
8131  N N   . LYS C 305 ? 1.5836 1.5222 1.3705 0.1526  -0.4237 0.0777  305 LYS C N   
8132  C CA  . LYS C 305 ? 1.6014 1.5213 1.3608 0.1494  -0.4101 0.0869  305 LYS C CA  
8133  C C   . LYS C 305 ? 1.5812 1.5081 1.3639 0.1492  -0.4014 0.0901  305 LYS C C   
8134  O O   . LYS C 305 ? 1.5695 1.5166 1.3792 0.1451  -0.3889 0.0857  305 LYS C O   
8135  C CB  . LYS C 305 ? 1.6097 1.5301 1.3537 0.1421  -0.3930 0.0858  305 LYS C CB  
8136  C CG  . LYS C 305 ? 1.6414 1.5426 1.3565 0.1385  -0.3786 0.0952  305 LYS C CG  
8137  C CD  . LYS C 305 ? 1.6592 1.5612 1.3594 0.1317  -0.3621 0.0936  305 LYS C CD  
8138  C CE  . LYS C 305 ? 1.8184 1.7048 1.4839 0.1325  -0.3696 0.0930  305 LYS C CE  
8139  N NZ  . LYS C 305 ? 1.8644 1.7497 1.5134 0.1261  -0.3528 0.0918  305 LYS C NZ  
8140  N N   . ILE C 306 ? 1.6318 1.5416 1.4035 0.1537  -0.4082 0.0977  306 ILE C N   
8141  C CA  . ILE C 306 ? 1.6228 1.5360 1.4140 0.1542  -0.4016 0.1010  306 ILE C CA  
8142  C C   . ILE C 306 ? 1.6981 1.5952 1.4644 0.1487  -0.3846 0.1095  306 ILE C C   
8143  O O   . ILE C 306 ? 1.7961 1.6685 1.5318 0.1504  -0.3880 0.1182  306 ILE C O   
8144  C CB  . ILE C 306 ? 1.6653 1.5695 1.4614 0.1625  -0.4193 0.1041  306 ILE C CB  
8145  C CG1 . ILE C 306 ? 1.6774 1.5910 1.4857 0.1681  -0.4387 0.0969  306 ILE C CG1 
8146  C CG2 . ILE C 306 ? 1.7198 1.6361 1.5482 0.1635  -0.4143 0.1034  306 ILE C CG2 
8147  C CD1 . ILE C 306 ? 1.6335 1.5780 1.4829 0.1669  -0.4369 0.0862  306 ILE C CD1 
8148  N N   . GLY C 307 ? 1.6380 1.5492 1.4173 0.1420  -0.3662 0.1070  307 GLY C N   
8149  C CA  . GLY C 307 ? 1.6364 1.5356 1.3945 0.1360  -0.3487 0.1138  307 GLY C CA  
8150  C C   . GLY C 307 ? 1.6942 1.5823 1.4528 0.1364  -0.3441 0.1214  307 GLY C C   
8151  O O   . GLY C 307 ? 1.7779 1.6587 1.5416 0.1425  -0.3572 0.1240  307 GLY C O   
8152  N N   . PRO C 308 ? 1.6458 1.5324 1.3998 0.1299  -0.3255 0.1251  308 PRO C N   
8153  C CA  . PRO C 308 ? 1.7129 1.5868 1.4646 0.1294  -0.3202 0.1330  308 PRO C CA  
8154  C C   . PRO C 308 ? 1.6596 1.5517 1.4501 0.1305  -0.3187 0.1286  308 PRO C C   
8155  O O   . PRO C 308 ? 1.6229 1.5396 1.4417 0.1288  -0.3141 0.1203  308 PRO C O   
8156  C CB  . PRO C 308 ? 1.6109 1.4783 1.3436 0.1214  -0.3003 0.1375  308 PRO C CB  
8157  C CG  . PRO C 308 ? 1.5254 1.4140 1.2705 0.1175  -0.2922 0.1291  308 PRO C CG  
8158  C CD  . PRO C 308 ? 1.5734 1.4674 1.3207 0.1227  -0.3090 0.1229  308 PRO C CD  
8159  N N   . ASN C 309 ? 1.7317 1.6106 1.5224 0.1335  -0.3227 0.1346  309 ASN C N   
8160  C CA  . ASN C 309 ? 1.7290 1.6207 1.5525 0.1344  -0.3199 0.1319  309 ASN C CA  
8161  C C   . ASN C 309 ? 1.7171 1.6323 1.5745 0.1393  -0.3307 0.1219  309 ASN C C   
8162  O O   . ASN C 309 ? 1.6773 1.6161 1.5628 0.1365  -0.3224 0.1147  309 ASN C O   
8163  C CB  . ASN C 309 ? 1.6968 1.5985 1.5294 0.1263  -0.2991 0.1315  309 ASN C CB  
8164  C CG  . ASN C 309 ? 1.7971 1.7095 1.6601 0.1268  -0.2956 0.1293  309 ASN C CG  
8165  O OD1 . ASN C 309 ? 1.8843 1.7906 1.7562 0.1329  -0.3073 0.1303  309 ASN C OD1 
8166  N ND2 . ASN C 309 ? 1.8317 1.7600 1.7109 0.1206  -0.2796 0.1260  309 ASN C ND2 
8167  N N   . VAL C 310 ? 1.7588 1.6672 1.6130 0.1468  -0.3494 0.1216  310 VAL C N   
8168  C CA  . VAL C 310 ? 1.7890 1.7181 1.6746 0.1521  -0.3613 0.1126  310 VAL C CA  
8169  C C   . VAL C 310 ? 1.9714 1.8891 1.8612 0.1607  -0.3781 0.1152  310 VAL C C   
8170  O O   . VAL C 310 ? 2.0342 1.9281 1.8959 0.1641  -0.3881 0.1224  310 VAL C O   
8171  C CB  . VAL C 310 ? 1.7223 1.6603 1.6035 0.1524  -0.3683 0.1069  310 VAL C CB  
8172  C CG1 . VAL C 310 ? 1.7712 1.6841 1.6123 0.1537  -0.3759 0.1137  310 VAL C CG1 
8173  C CG2 . VAL C 310 ? 1.8197 1.7756 1.7309 0.1588  -0.3833 0.0987  310 VAL C CG2 
8174  N N   . SER C 311 ? 2.2844 2.2188 2.2090 0.1642  -0.3810 0.1094  311 SER C N   
8175  C CA  . SER C 311 ? 2.2880 2.2141 2.2221 0.1726  -0.3958 0.1109  311 SER C CA  
8176  C C   . SER C 311 ? 2.2650 2.2135 2.2304 0.1784  -0.4083 0.1010  311 SER C C   
8177  O O   . SER C 311 ? 2.2198 2.1919 2.2178 0.1773  -0.4020 0.0935  311 SER C O   
8178  C CB  . SER C 311 ? 2.3501 2.2733 2.2968 0.1717  -0.3868 0.1134  311 SER C CB  
8179  O OG  . SER C 311 ? 2.4005 2.3071 2.3220 0.1649  -0.3726 0.1215  311 SER C OG  
8180  N N   . ILE C 312 ? 2.3502 2.2916 2.3059 0.1844  -0.4260 0.1011  312 ILE C N   
8181  C CA  . ILE C 312 ? 2.3123 2.2740 2.2958 0.1898  -0.4391 0.0920  312 ILE C CA  
8182  C C   . ILE C 312 ? 2.3053 2.2633 2.3057 0.1989  -0.4531 0.0921  312 ILE C C   
8183  O O   . ILE C 312 ? 2.3362 2.2692 2.3152 0.2033  -0.4616 0.1003  312 ILE C O   
8184  C CB  . ILE C 312 ? 2.3184 2.2762 2.2831 0.1909  -0.4508 0.0911  312 ILE C CB  
8185  C CG1 . ILE C 312 ? 2.3447 2.2933 2.2787 0.1827  -0.4379 0.0951  312 ILE C CG1 
8186  C CG2 . ILE C 312 ? 2.2747 2.2603 2.2708 0.1922  -0.4570 0.0801  312 ILE C CG2 
8187  C CD1 . ILE C 312 ? 2.3534 2.2979 2.2677 0.1832  -0.4482 0.0937  312 ILE C CD1 
8188  N N   . SER C 313 ? 2.0010 1.9836 2.0400 0.2019  -0.4554 0.0830  313 SER C N   
8189  C CA  . SER C 313 ? 1.8377 1.8212 1.8987 0.2107  -0.4672 0.0812  313 SER C CA  
8190  C C   . SER C 313 ? 1.7783 1.7663 1.8472 0.2184  -0.4880 0.0771  313 SER C C   
8191  O O   . SER C 313 ? 1.8296 1.8176 1.8842 0.2169  -0.4937 0.0764  313 SER C O   
8192  C CB  . SER C 313 ? 1.7478 1.7557 1.8463 0.2094  -0.4565 0.0734  313 SER C CB  
8193  O OG  . SER C 313 ? 1.8453 1.8475 1.9363 0.2028  -0.4387 0.0774  313 SER C OG  
8194  N N   . ALA C 314 ? 1.6587 1.6514 1.7520 0.2268  -0.4995 0.0740  314 ALA C N   
8195  C CA  . ALA C 314 ? 1.5431 1.5378 1.6445 0.2354  -0.5208 0.0709  314 ALA C CA  
8196  C C   . ALA C 314 ? 1.5446 1.5707 1.6772 0.2346  -0.5226 0.0595  314 ALA C C   
8197  O O   . ALA C 314 ? 1.5970 1.6457 1.7539 0.2297  -0.5088 0.0530  314 ALA C O   
8198  C CB  . ALA C 314 ? 1.5043 1.4919 1.6210 0.2451  -0.5323 0.0718  314 ALA C CB  
8199  N N   . ASN C 315 ? 1.5378 1.5646 1.6689 0.2395  -0.5403 0.0572  315 ASN C N   
8200  C CA  . ASN C 315 ? 1.5275 1.5826 1.6899 0.2404  -0.5462 0.0465  315 ASN C CA  
8201  C C   . ASN C 315 ? 1.6123 1.6860 1.7796 0.2303  -0.5297 0.0417  315 ASN C C   
8202  O O   . ASN C 315 ? 1.6225 1.7231 1.8232 0.2283  -0.5230 0.0333  315 ASN C O   
8203  C CB  . ASN C 315 ? 1.4633 1.5372 1.6670 0.2470  -0.5501 0.0395  315 ASN C CB  
8204  C CG  . ASN C 315 ? 1.4945 1.5543 1.6988 0.2583  -0.5704 0.0421  315 ASN C CG  
8205  O OD1 . ASN C 315 ? 1.5042 1.5458 1.6999 0.2622  -0.5706 0.0483  315 ASN C OD1 
8206  N ND2 . ASN C 315 ? 1.4909 1.5591 1.7060 0.2636  -0.5880 0.0374  315 ASN C ND2 
8207  N N   . VAL C 316 ? 1.7940 1.8530 1.9274 0.2239  -0.5233 0.0472  316 VAL C N   
8208  C CA  . VAL C 316 ? 1.9130 1.9861 2.0464 0.2144  -0.5086 0.0436  316 VAL C CA  
8209  C C   . VAL C 316 ? 2.0990 2.1668 2.2121 0.2131  -0.5183 0.0431  316 VAL C C   
8210  O O   . VAL C 316 ? 2.0362 2.0805 2.1191 0.2165  -0.5297 0.0495  316 VAL C O   
8211  C CB  . VAL C 316 ? 1.8902 1.9522 2.0034 0.2071  -0.4886 0.0499  316 VAL C CB  
8212  C CG1 . VAL C 316 ? 1.9188 1.9486 1.9900 0.2078  -0.4922 0.0605  316 VAL C CG1 
8213  C CG2 . VAL C 316 ? 1.9808 2.0578 2.0952 0.1978  -0.4736 0.0461  316 VAL C CG2 
8214  N N   . ARG C 317 ? 2.5833 2.6729 2.7132 0.2081  -0.5140 0.0355  317 ARG C N   
8215  C CA  . ARG C 317 ? 2.5904 2.6787 2.7060 0.2062  -0.5226 0.0332  317 ARG C CA  
8216  C C   . ARG C 317 ? 2.6134 2.6975 2.7068 0.1968  -0.5057 0.0354  317 ARG C C   
8217  O O   . ARG C 317 ? 2.5895 2.6928 2.7017 0.1906  -0.4911 0.0308  317 ARG C O   
8218  C CB  . ARG C 317 ? 2.5518 2.6674 2.7036 0.2074  -0.5306 0.0227  317 ARG C CB  
8219  C CG  . ARG C 317 ? 2.5567 2.6766 2.7303 0.2172  -0.5489 0.0200  317 ARG C CG  
8220  C CD  . ARG C 317 ? 2.6406 2.7824 2.8410 0.2183  -0.5605 0.0106  317 ARG C CD  
8221  N NE  . ARG C 317 ? 2.6263 2.7963 2.8589 0.2123  -0.5466 0.0032  317 ARG C NE  
8222  C CZ  . ARG C 317 ? 2.5893 2.7814 2.8604 0.2153  -0.5460 -0.0028 317 ARG C CZ  
8223  N NH1 . ARG C 317 ? 2.7164 2.9061 3.0000 0.2244  -0.5587 -0.0027 317 ARG C NH1 
8224  N NH2 . ARG C 317 ? 2.4363 2.6531 2.7335 0.2093  -0.5326 -0.0089 317 ARG C NH2 
8225  N N   . VAL C 318 ? 2.3981 2.4571 2.4513 0.1958  -0.5076 0.0424  318 VAL C N   
8226  C CA  . VAL C 318 ? 2.3589 2.4110 2.3873 0.1875  -0.4922 0.0451  318 VAL C CA  
8227  C C   . VAL C 318 ? 2.4617 2.5176 2.4820 0.1850  -0.4990 0.0400  318 VAL C C   
8228  O O   . VAL C 318 ? 2.3862 2.4308 2.3918 0.1897  -0.5165 0.0403  318 VAL C O   
8229  C CB  . VAL C 318 ? 2.2392 2.2615 2.2277 0.1874  -0.4884 0.0559  318 VAL C CB  
8230  C CG1 . VAL C 318 ? 2.1840 2.1980 2.1442 0.1796  -0.4755 0.0581  318 VAL C CG1 
8231  C CG2 . VAL C 318 ? 2.1438 2.1637 2.1413 0.1879  -0.4780 0.0605  318 VAL C CG2 
8232  N N   . GLY C 319 ? 2.9644 3.0358 2.9944 0.1776  -0.4855 0.0353  319 GLY C N   
8233  C CA  . GLY C 319 ? 2.9610 3.0373 2.9859 0.1744  -0.4901 0.0298  319 GLY C CA  
8234  C C   . GLY C 319 ? 3.0009 3.0537 2.9823 0.1715  -0.4878 0.0349  319 GLY C C   
8235  O O   . GLY C 319 ? 3.0329 3.0645 2.9860 0.1720  -0.4832 0.0434  319 GLY C O   
8236  N N   . PRO C 320 ? 2.2961 2.3527 2.2719 0.1682  -0.4910 0.0296  320 PRO C N   
8237  C CA  . PRO C 320 ? 2.1012 2.1368 2.0362 0.1657  -0.4901 0.0329  320 PRO C CA  
8238  C C   . PRO C 320 ? 1.9268 1.9626 1.8513 0.1578  -0.4684 0.0343  320 PRO C C   
8239  O O   . PRO C 320 ? 1.8771 1.9334 1.8279 0.1531  -0.4564 0.0298  320 PRO C O   
8240  C CB  . PRO C 320 ? 2.1139 2.1566 2.0537 0.1661  -0.5044 0.0249  320 PRO C CB  
8241  C CG  . PRO C 320 ? 2.1735 2.2456 2.1568 0.1633  -0.4993 0.0171  320 PRO C CG  
8242  C CD  . PRO C 320 ? 2.2186 2.2996 2.2264 0.1665  -0.4953 0.0197  320 PRO C CD  
8243  N N   . GLY C 321 ? 1.8670 1.8797 1.7521 0.1563  -0.4636 0.0408  321 GLY C N   
8244  C CA  . GLY C 321 ? 1.7498 1.7611 1.6216 0.1491  -0.4441 0.0419  321 GLY C CA  
8245  C C   . GLY C 321 ? 1.6347 1.6592 1.5284 0.1455  -0.4262 0.0435  321 GLY C C   
8246  O O   . GLY C 321 ? 1.6053 1.6401 1.5053 0.1393  -0.4112 0.0409  321 GLY C O   
8247  N N   . VAL C 322 ? 1.6673 1.6917 1.5731 0.1492  -0.4277 0.0476  322 VAL C N   
8248  C CA  . VAL C 322 ? 1.6016 1.6384 1.5288 0.1463  -0.4120 0.0489  322 VAL C CA  
8249  C C   . VAL C 322 ? 1.5240 1.5407 1.4230 0.1444  -0.4004 0.0581  322 VAL C C   
8250  O O   . VAL C 322 ? 1.5433 1.5368 1.4115 0.1474  -0.4076 0.0643  322 VAL C O   
8251  C CB  . VAL C 322 ? 1.6616 1.7124 1.6224 0.1513  -0.4199 0.0466  322 VAL C CB  
8252  C CG1 . VAL C 322 ? 1.7597 1.8299 1.7477 0.1532  -0.4322 0.0376  322 VAL C CG1 
8253  C CG2 . VAL C 322 ? 1.7494 1.7804 1.6947 0.1580  -0.4316 0.0533  322 VAL C CG2 
8254  N N   . ARG C 323 ? 1.4831 1.5088 1.3926 0.1392  -0.3821 0.0590  323 ARG C N   
8255  C CA  . ARG C 323 ? 1.4785 1.4881 1.3644 0.1361  -0.3684 0.0670  323 ARG C CA  
8256  C C   . ARG C 323 ? 1.4848 1.5004 1.3915 0.1370  -0.3625 0.0697  323 ARG C C   
8257  O O   . ARG C 323 ? 1.4708 1.5085 1.4093 0.1352  -0.3561 0.0646  323 ARG C O   
8258  C CB  . ARG C 323 ? 1.4773 1.4916 1.3558 0.1287  -0.3511 0.0657  323 ARG C CB  
8259  C CG  . ARG C 323 ? 1.5291 1.5261 1.3802 0.1251  -0.3370 0.0737  323 ARG C CG  
8260  C CD  . ARG C 323 ? 1.5991 1.5714 1.4093 0.1262  -0.3429 0.0782  323 ARG C CD  
8261  N NE  . ARG C 323 ? 1.6534 1.6100 1.4374 0.1220  -0.3280 0.0856  323 ARG C NE  
8262  C CZ  . ARG C 323 ? 1.6451 1.5827 1.4107 0.1237  -0.3286 0.0942  323 ARG C CZ  
8263  N NH1 . ARG C 323 ? 1.5914 1.5228 1.3613 0.1299  -0.3437 0.0964  323 ARG C NH1 
8264  N NH2 . ARG C 323 ? 1.6720 1.5965 1.4150 0.1193  -0.3141 0.1007  323 ARG C NH2 
8265  N N   . LEU C 324 ? 1.5726 1.5683 1.4611 0.1397  -0.3648 0.0776  324 LEU C N   
8266  C CA  . LEU C 324 ? 1.5590 1.5573 1.4650 0.1412  -0.3608 0.0804  324 LEU C CA  
8267  C C   . LEU C 324 ? 1.5936 1.5723 1.4735 0.1376  -0.3485 0.0894  324 LEU C C   
8268  O O   . LEU C 324 ? 1.6484 1.6034 1.4991 0.1402  -0.3550 0.0965  324 LEU C O   
8269  C CB  . LEU C 324 ? 1.5930 1.5870 1.5083 0.1494  -0.3791 0.0807  324 LEU C CB  
8270  C CG  . LEU C 324 ? 1.5662 1.5773 1.5056 0.1537  -0.3939 0.0723  324 LEU C CG  
8271  C CD1 . LEU C 324 ? 1.6373 1.6410 1.5823 0.1622  -0.4120 0.0737  324 LEU C CD1 
8272  C CD2 . LEU C 324 ? 1.5016 1.5418 1.4788 0.1507  -0.3852 0.0643  324 LEU C CD2 
8273  N N   . ILE C 325 ? 1.4842 1.4729 1.3747 0.1318  -0.3308 0.0893  325 ILE C N   
8274  C CA  . ILE C 325 ? 1.5004 1.4734 1.3711 0.1278  -0.3177 0.0973  325 ILE C CA  
8275  C C   . ILE C 325 ? 1.4828 1.4694 1.3810 0.1258  -0.3072 0.0963  325 ILE C C   
8276  O O   . ILE C 325 ? 1.4454 1.4558 1.3730 0.1244  -0.3031 0.0890  325 ILE C O   
8277  C CB  . ILE C 325 ? 1.4699 1.4381 1.3174 0.1213  -0.3043 0.0988  325 ILE C CB  
8278  C CG1 . ILE C 325 ? 1.3637 1.3565 1.2355 0.1162  -0.2914 0.0919  325 ILE C CG1 
8279  C CG2 . ILE C 325 ? 1.5438 1.5012 1.3664 0.1233  -0.3146 0.0981  325 ILE C CG2 
8280  C CD1 . ILE C 325 ? 1.3893 1.3789 1.2410 0.1104  -0.2788 0.0925  325 ILE C CD1 
8281  N N   . SER C 326 ? 1.5118 1.4828 1.4002 0.1256  -0.3032 0.1035  326 SER C N   
8282  C CA  . SER C 326 ? 1.5098 1.4902 1.4189 0.1226  -0.2913 0.1035  326 SER C CA  
8283  C C   . SER C 326 ? 1.5449 1.5474 1.4919 0.1263  -0.2971 0.0957  326 SER C C   
8284  O O   . SER C 326 ? 1.5179 1.5399 1.4885 0.1228  -0.2865 0.0911  326 SER C O   
8285  C CB  . SER C 326 ? 1.4444 1.4335 1.3520 0.1146  -0.2723 0.1029  326 SER C CB  
8286  O OG  . SER C 326 ? 1.3704 1.3401 1.2434 0.1113  -0.2666 0.1094  326 SER C OG  
8287  N N   . CYS C 327 ? 1.6220 1.6217 1.5749 0.1336  -0.3143 0.0943  327 CYS C N   
8288  C CA  . CYS C 327 ? 1.5985 1.6194 1.5870 0.1376  -0.3208 0.0866  327 CYS C CA  
8289  C C   . CYS C 327 ? 1.6736 1.6827 1.6642 0.1457  -0.3368 0.0888  327 CYS C C   
8290  O O   . CYS C 327 ? 1.7750 1.7608 1.7388 0.1486  -0.3454 0.0955  327 CYS C O   
8291  C CB  . CYS C 327 ? 1.4941 1.5344 1.4963 0.1377  -0.3255 0.0786  327 CYS C CB  
8292  S SG  . CYS C 327 ? 1.5872 1.6127 1.5636 0.1418  -0.3422 0.0799  327 CYS C SG  
8293  N N   . ILE C 328 ? 1.6593 1.6847 1.6821 0.1495  -0.3408 0.0829  328 ILE C N   
8294  C CA  . ILE C 328 ? 1.7617 1.7798 1.7924 0.1579  -0.3565 0.0833  328 ILE C CA  
8295  C C   . ILE C 328 ? 1.7467 1.7887 1.8092 0.1623  -0.3658 0.0737  328 ILE C C   
8296  O O   . ILE C 328 ? 1.5692 1.6349 1.6572 0.1591  -0.3569 0.0669  328 ILE C O   
8297  C CB  . ILE C 328 ? 1.7122 1.7226 1.7503 0.1589  -0.3518 0.0866  328 ILE C CB  
8298  C CG1 . ILE C 328 ? 1.5531 1.5857 1.6179 0.1542  -0.3369 0.0808  328 ILE C CG1 
8299  C CG2 . ILE C 328 ? 1.8002 1.7826 1.8045 0.1559  -0.3465 0.0973  328 ILE C CG2 
8300  C CD1 . ILE C 328 ? 1.6122 1.6384 1.6861 0.1550  -0.3324 0.0829  328 ILE C CD1 
8301  N N   . ILE C 329 ? 2.0347 2.0708 2.0959 0.1695  -0.3838 0.0732  329 ILE C N   
8302  C CA  . ILE C 329 ? 1.9919 2.0493 2.0809 0.1738  -0.3944 0.0644  329 ILE C CA  
8303  C C   . ILE C 329 ? 1.9856 2.0414 2.0925 0.1825  -0.4071 0.0633  329 ILE C C   
8304  O O   . ILE C 329 ? 2.0151 2.0479 2.1032 0.1874  -0.4171 0.0699  329 ILE C O   
8305  C CB  . ILE C 329 ? 1.9941 2.0484 2.0679 0.1747  -0.4056 0.0636  329 ILE C CB  
8306  C CG1 . ILE C 329 ? 2.0032 2.0588 2.0596 0.1663  -0.3926 0.0643  329 ILE C CG1 
8307  C CG2 . ILE C 329 ? 1.9512 2.0280 2.0557 0.1790  -0.4168 0.0544  329 ILE C CG2 
8308  C CD1 . ILE C 329 ? 2.0134 2.0618 2.0494 0.1667  -0.4027 0.0643  329 ILE C CD1 
8309  N N   . LEU C 330 ? 1.7903 1.8703 1.9333 0.1844  -0.4064 0.0549  330 LEU C N   
8310  C CA  . LEU C 330 ? 1.7688 1.8506 1.9331 0.1927  -0.4170 0.0524  330 LEU C CA  
8311  C C   . LEU C 330 ? 1.7191 1.8058 1.8926 0.1998  -0.4361 0.0484  330 LEU C C   
8312  O O   . LEU C 330 ? 1.7309 1.8156 1.8900 0.1984  -0.4420 0.0487  330 LEU C O   
8313  C CB  . LEU C 330 ? 1.8011 1.9064 1.9991 0.1913  -0.4061 0.0452  330 LEU C CB  
8314  C CG  . LEU C 330 ? 1.8200 1.9202 2.0109 0.1849  -0.3884 0.0488  330 LEU C CG  
8315  C CD1 . LEU C 330 ? 1.8834 2.0073 2.1078 0.1842  -0.3791 0.0410  330 LEU C CD1 
8316  C CD2 . LEU C 330 ? 1.9733 2.0447 2.1422 0.1876  -0.3915 0.0577  330 LEU C CD2 
8317  N N   . ASP C 331 ? 1.6745 1.7675 1.8725 0.2076  -0.4462 0.0445  331 ASP C N   
8318  C CA  . ASP C 331 ? 1.5857 1.6815 1.7930 0.2154  -0.4657 0.0412  331 ASP C CA  
8319  C C   . ASP C 331 ? 1.5554 1.6802 1.7888 0.2135  -0.4661 0.0316  331 ASP C C   
8320  O O   . ASP C 331 ? 1.5894 1.7354 1.8430 0.2083  -0.4524 0.0261  331 ASP C O   
8321  C CB  . ASP C 331 ? 1.5924 1.6860 1.8191 0.2248  -0.4759 0.0399  331 ASP C CB  
8322  C CG  . ASP C 331 ? 1.6254 1.6882 1.8262 0.2276  -0.4783 0.0498  331 ASP C CG  
8323  O OD1 . ASP C 331 ? 1.6578 1.7186 1.8680 0.2279  -0.4702 0.0503  331 ASP C OD1 
8324  O OD2 . ASP C 331 ? 1.6749 1.7152 1.8452 0.2291  -0.4879 0.0572  331 ASP C OD2 
8325  N N   . ASP C 332 ? 1.5580 1.6829 1.7900 0.2176  -0.4823 0.0298  332 ASP C N   
8326  C CA  . ASP C 332 ? 1.5690 1.7204 1.8288 0.2176  -0.4870 0.0205  332 ASP C CA  
8327  C C   . ASP C 332 ? 1.6077 1.7727 1.8655 0.2078  -0.4731 0.0179  332 ASP C C   
8328  O O   . ASP C 332 ? 1.5817 1.7725 1.8676 0.2058  -0.4704 0.0098  332 ASP C O   
8329  C CB  . ASP C 332 ? 1.4935 1.6673 1.7940 0.2224  -0.4874 0.0126  332 ASP C CB  
8330  C CG  . ASP C 332 ? 1.5085 1.6948 1.8316 0.2295  -0.5054 0.0063  332 ASP C CG  
8331  O OD1 . ASP C 332 ? 1.5601 1.7489 1.8764 0.2278  -0.5132 0.0048  332 ASP C OD1 
8332  O OD2 . ASP C 332 ? 1.4533 1.6470 1.8012 0.2369  -0.5120 0.0024  332 ASP C OD2 
8333  N N   . VAL C 333 ? 1.7042 1.8522 1.9294 0.2018  -0.4645 0.0246  333 VAL C N   
8334  C CA  . VAL C 333 ? 1.7094 1.8678 1.9301 0.1927  -0.4514 0.0227  333 VAL C CA  
8335  C C   . VAL C 333 ? 1.8497 2.0072 2.0602 0.1925  -0.4631 0.0209  333 VAL C C   
8336  O O   . VAL C 333 ? 1.9666 2.1058 2.1572 0.1974  -0.4780 0.0246  333 VAL C O   
8337  C CB  . VAL C 333 ? 1.6807 1.8220 1.8722 0.1864  -0.4361 0.0304  333 VAL C CB  
8338  C CG1 . VAL C 333 ? 1.6791 1.8315 1.8671 0.1775  -0.4226 0.0283  333 VAL C CG1 
8339  C CG2 . VAL C 333 ? 1.6621 1.8036 1.8641 0.1868  -0.4258 0.0319  333 VAL C CG2 
8340  N N   . GLU C 334 ? 1.8272 2.0046 2.0518 0.1867  -0.4567 0.0149  334 GLU C N   
8341  C CA  . GLU C 334 ? 1.8589 2.0375 2.0761 0.1854  -0.4664 0.0121  334 GLU C CA  
8342  C C   . GLU C 334 ? 1.7965 1.9711 1.9924 0.1766  -0.4525 0.0142  334 GLU C C   
8343  O O   . GLU C 334 ? 1.7033 1.8953 1.9149 0.1706  -0.4379 0.0110  334 GLU C O   
8344  C CB  . GLU C 334 ? 1.8960 2.1020 2.1505 0.1866  -0.4727 0.0026  334 GLU C CB  
8345  C CG  . GLU C 334 ? 1.9461 2.1542 2.1958 0.1852  -0.4836 -0.0010 334 GLU C CG  
8346  C CD  . GLU C 334 ? 1.9778 2.2132 2.2660 0.1862  -0.4900 -0.0103 334 GLU C CD  
8347  O OE1 . GLU C 334 ? 2.0330 2.2843 2.3507 0.1893  -0.4879 -0.0138 334 GLU C OE1 
8348  O OE2 . GLU C 334 ? 1.9352 2.1760 2.2242 0.1839  -0.4970 -0.0143 334 GLU C OE2 
8349  N N   . ILE C 335 ? 1.8119 1.9638 1.9721 0.1761  -0.4571 0.0197  335 ILE C N   
8350  C CA  . ILE C 335 ? 1.7472 1.8925 1.8839 0.1685  -0.4451 0.0219  335 ILE C CA  
8351  C C   . ILE C 335 ? 1.7428 1.8921 1.8767 0.1673  -0.4552 0.0170  335 ILE C C   
8352  O O   . ILE C 335 ? 1.8367 1.9734 1.9566 0.1722  -0.4719 0.0177  335 ILE C O   
8353  C CB  . ILE C 335 ? 1.8202 1.9370 1.9176 0.1681  -0.4414 0.0314  335 ILE C CB  
8354  C CG1 . ILE C 335 ? 1.7166 1.8288 1.8184 0.1697  -0.4333 0.0361  335 ILE C CG1 
8355  C CG2 . ILE C 335 ? 1.7393 1.8510 1.8146 0.1603  -0.4277 0.0331  335 ILE C CG2 
8356  C CD1 . ILE C 335 ? 1.6208 1.7493 1.7397 0.1635  -0.4137 0.0342  335 ILE C CD1 
8357  N N   . LYS C 336 ? 1.5970 1.7632 1.7438 0.1608  -0.4455 0.0119  336 LYS C N   
8358  C CA  . LYS C 336 ? 1.5764 1.7492 1.7259 0.1591  -0.4544 0.0061  336 LYS C CA  
8359  C C   . LYS C 336 ? 1.6356 1.7907 1.7492 0.1546  -0.4502 0.0093  336 LYS C C   
8360  O O   . LYS C 336 ? 1.7130 1.8488 1.7978 0.1538  -0.4429 0.0164  336 LYS C O   
8361  C CB  . LYS C 336 ? 1.5456 1.7472 1.7313 0.1549  -0.4474 -0.0014 336 LYS C CB  
8362  C CG  . LYS C 336 ? 1.5445 1.7649 1.7664 0.1600  -0.4564 -0.0066 336 LYS C CG  
8363  C CD  . LYS C 336 ? 1.4880 1.7361 1.7435 0.1553  -0.4508 -0.0141 336 LYS C CD  
8364  C CE  . LYS C 336 ? 1.4768 1.7440 1.7683 0.1606  -0.4605 -0.0197 336 LYS C CE  
8365  N NZ  . LYS C 336 ? 1.4282 1.7224 1.7524 0.1558  -0.4549 -0.0269 336 LYS C NZ  
8366  N N   . GLU C 337 ? 1.6171 1.7788 1.7329 0.1517  -0.4550 0.0036  337 GLU C N   
8367  C CA  . GLU C 337 ? 1.6466 1.7916 1.7292 0.1483  -0.4544 0.0051  337 GLU C CA  
8368  C C   . GLU C 337 ? 1.6676 1.8072 1.7340 0.1421  -0.4339 0.0093  337 GLU C C   
8369  O O   . GLU C 337 ? 1.6423 1.7993 1.7295 0.1371  -0.4203 0.0067  337 GLU C O   
8370  C CB  . GLU C 337 ? 1.6759 1.8331 1.7708 0.1456  -0.4615 -0.0029 337 GLU C CB  
8371  C CG  . GLU C 337 ? 1.7287 1.8986 1.8500 0.1507  -0.4796 -0.0087 337 GLU C CG  
8372  C CD  . GLU C 337 ? 2.0066 2.1576 2.1047 0.1569  -0.4992 -0.0071 337 GLU C CD  
8373  O OE1 . GLU C 337 ? 2.0765 2.2043 2.1368 0.1568  -0.4985 -0.0018 337 GLU C OE1 
8374  O OE2 . GLU C 337 ? 2.0929 2.2524 2.2107 0.1619  -0.5154 -0.0112 337 GLU C OE2 
8375  N N   . ASN C 338 ? 1.7442 1.8596 1.7732 0.1423  -0.4318 0.0159  338 ASN C N   
8376  C CA  . ASN C 338 ? 1.7418 1.8492 1.7502 0.1364  -0.4139 0.0197  338 ASN C CA  
8377  C C   . ASN C 338 ? 1.6850 1.8056 1.7134 0.1333  -0.3968 0.0215  338 ASN C C   
8378  O O   . ASN C 338 ? 1.6346 1.7680 1.6741 0.1276  -0.3834 0.0189  338 ASN C O   
8379  C CB  . ASN C 338 ? 1.7614 1.8728 1.7650 0.1313  -0.4110 0.0144  338 ASN C CB  
8380  C CG  . ASN C 338 ? 1.7345 1.8314 1.7152 0.1340  -0.4272 0.0125  338 ASN C CG  
8381  O OD1 . ASN C 338 ? 1.7373 1.8132 1.6895 0.1379  -0.4347 0.0178  338 ASN C OD1 
8382  N ND2 . ASN C 338 ? 1.7373 1.8452 1.7303 0.1318  -0.4329 0.0049  338 ASN C ND2 
8383  N N   . ALA C 339 ? 1.5666 1.6834 1.5992 0.1373  -0.3979 0.0259  339 ALA C N   
8384  C CA  . ALA C 339 ? 1.4505 1.5772 1.4994 0.1350  -0.3829 0.0280  339 ALA C CA  
8385  C C   . ALA C 339 ? 1.3892 1.4961 1.4085 0.1330  -0.3715 0.0361  339 ALA C C   
8386  O O   . ALA C 339 ? 1.4824 1.5669 1.4708 0.1353  -0.3778 0.0412  339 ALA C O   
8387  C CB  . ALA C 339 ? 1.4739 1.6103 1.5491 0.1405  -0.3904 0.0269  339 ALA C CB  
8388  N N   . VAL C 340 ? 1.2992 1.4150 1.3284 0.1286  -0.3545 0.0374  340 VAL C N   
8389  C CA  . VAL C 340 ? 1.2703 1.3706 1.2758 0.1257  -0.3415 0.0446  340 VAL C CA  
8390  C C   . VAL C 340 ? 1.2679 1.3759 1.2924 0.1258  -0.3332 0.0465  340 VAL C C   
8391  O O   . VAL C 340 ? 1.2890 1.4190 1.3433 0.1241  -0.3273 0.0417  340 VAL C O   
8392  C CB  . VAL C 340 ? 1.2526 1.3548 1.2472 0.1189  -0.3271 0.0439  340 VAL C CB  
8393  C CG1 . VAL C 340 ? 1.2763 1.3623 1.2462 0.1160  -0.3140 0.0514  340 VAL C CG1 
8394  C CG2 . VAL C 340 ? 1.3306 1.4265 1.3088 0.1187  -0.3354 0.0407  340 VAL C CG2 
8395  N N   . VAL C 341 ? 1.2487 1.3385 1.2557 0.1278  -0.3328 0.0536  341 VAL C N   
8396  C CA  . VAL C 341 ? 1.2356 1.3295 1.2580 0.1284  -0.3261 0.0558  341 VAL C CA  
8397  C C   . VAL C 341 ? 1.2852 1.3616 1.2824 0.1247  -0.3136 0.0636  341 VAL C C   
8398  O O   . VAL C 341 ? 1.3248 1.3781 1.2934 0.1267  -0.3188 0.0698  341 VAL C O   
8399  C CB  . VAL C 341 ? 1.2850 1.3748 1.3171 0.1358  -0.3411 0.0562  341 VAL C CB  
8400  C CG1 . VAL C 341 ? 1.3113 1.4034 1.3573 0.1362  -0.3336 0.0584  341 VAL C CG1 
8401  C CG2 . VAL C 341 ? 1.2007 1.3096 1.2602 0.1393  -0.3530 0.0482  341 VAL C CG2 
8402  N N   . ILE C 342 ? 1.3172 1.4044 1.3249 0.1194  -0.2972 0.0632  342 ILE C N   
8403  C CA  . ILE C 342 ? 1.2856 1.3595 1.2735 0.1151  -0.2836 0.0699  342 ILE C CA  
8404  C C   . ILE C 342 ? 1.2838 1.3677 1.2934 0.1139  -0.2747 0.0700  342 ILE C C   
8405  O O   . ILE C 342 ? 1.2817 1.3879 1.3187 0.1122  -0.2695 0.0642  342 ILE C O   
8406  C CB  . ILE C 342 ? 1.2449 1.3216 1.2211 0.1088  -0.2708 0.0693  342 ILE C CB  
8407  C CG1 . ILE C 342 ? 1.2423 1.3175 1.2075 0.1098  -0.2797 0.0658  342 ILE C CG1 
8408  C CG2 . ILE C 342 ? 1.2464 1.3040 1.1947 0.1052  -0.2598 0.0770  342 ILE C CG2 
8409  C CD1 . ILE C 342 ? 1.3361 1.3867 1.2690 0.1131  -0.2905 0.0707  342 ILE C CD1 
8410  N N   . ASN C 343 ? 1.3185 1.3857 1.3157 0.1146  -0.2730 0.0765  343 ASN C N   
8411  C CA  . ASN C 343 ? 1.3102 1.3838 1.3245 0.1130  -0.2638 0.0771  343 ASN C CA  
8412  C C   . ASN C 343 ? 1.3000 1.3952 1.3495 0.1164  -0.2690 0.0699  343 ASN C C   
8413  O O   . ASN C 343 ? 1.3182 1.4324 1.3895 0.1132  -0.2591 0.0657  343 ASN C O   
8414  C CB  . ASN C 343 ? 1.3055 1.3858 1.3183 0.1055  -0.2454 0.0778  343 ASN C CB  
8415  C CG  . ASN C 343 ? 1.3430 1.4019 1.3225 0.1020  -0.2385 0.0853  343 ASN C CG  
8416  O OD1 . ASN C 343 ? 1.3789 1.4168 1.3397 0.1040  -0.2428 0.0918  343 ASN C OD1 
8417  N ND2 . ASN C 343 ? 1.3755 1.4394 1.3475 0.0968  -0.2274 0.0846  343 ASN C ND2 
8418  N N   . SER C 344 ? 1.2918 1.3838 1.3465 0.1231  -0.2849 0.0684  344 SER C N   
8419  C CA  . SER C 344 ? 1.2434 1.3561 1.3308 0.1269  -0.2914 0.0610  344 SER C CA  
8420  C C   . SER C 344 ? 1.2609 1.3639 1.3537 0.1338  -0.3031 0.0625  344 SER C C   
8421  O O   . SER C 344 ? 1.4122 1.4918 1.4817 0.1363  -0.3089 0.0693  344 SER C O   
8422  C CB  . SER C 344 ? 1.2199 1.3446 1.3148 0.1284  -0.3003 0.0554  344 SER C CB  
8423  O OG  . SER C 344 ? 1.2366 1.3646 1.3203 0.1225  -0.2912 0.0550  344 SER C OG  
8424  N N   . ILE C 345 ? 1.1893 1.3108 1.3132 0.1371  -0.3063 0.0561  345 ILE C N   
8425  C CA  . ILE C 345 ? 1.2526 1.3691 1.3875 0.1445  -0.3184 0.0557  345 ILE C CA  
8426  C C   . ILE C 345 ? 1.2516 1.3898 1.4147 0.1487  -0.3278 0.0472  345 ILE C C   
8427  O O   . ILE C 345 ? 1.2699 1.4306 1.4597 0.1471  -0.3209 0.0409  345 ILE C O   
8428  C CB  . ILE C 345 ? 1.2392 1.3555 1.3856 0.1442  -0.3104 0.0564  345 ILE C CB  
8429  C CG1 . ILE C 345 ? 1.2693 1.3654 1.3893 0.1392  -0.3000 0.0647  345 ILE C CG1 
8430  C CG2 . ILE C 345 ? 1.3219 1.4328 1.4804 0.1526  -0.3238 0.0554  345 ILE C CG2 
8431  C CD1 . ILE C 345 ? 1.2841 1.3778 1.4137 0.1385  -0.2926 0.0657  345 ILE C CD1 
8432  N N   . ILE C 346 ? 1.3179 1.4494 1.4752 0.1540  -0.3435 0.0470  346 ILE C N   
8433  C CA  . ILE C 346 ? 1.3328 1.4840 1.5156 0.1578  -0.3535 0.0392  346 ILE C CA  
8434  C C   . ILE C 346 ? 1.4038 1.5576 1.6077 0.1654  -0.3628 0.0366  346 ILE C C   
8435  O O   . ILE C 346 ? 1.5046 1.6380 1.6947 0.1705  -0.3719 0.0417  346 ILE C O   
8436  C CB  . ILE C 346 ? 1.4191 1.5624 1.5859 0.1597  -0.3664 0.0398  346 ILE C CB  
8437  C CG1 . ILE C 346 ? 1.3332 1.4703 1.4756 0.1525  -0.3569 0.0429  346 ILE C CG1 
8438  C CG2 . ILE C 346 ? 1.4108 1.5762 1.6055 0.1625  -0.3755 0.0314  346 ILE C CG2 
8439  C CD1 . ILE C 346 ? 1.2823 1.4420 1.4420 0.1460  -0.3431 0.0378  346 ILE C CD1 
8440  N N   . GLY C 347 ? 1.4042 1.5828 1.6411 0.1663  -0.3604 0.0287  347 GLY C N   
8441  C CA  . GLY C 347 ? 1.5978 1.7815 1.8574 0.1732  -0.3672 0.0252  347 GLY C CA  
8442  C C   . GLY C 347 ? 1.6966 1.8778 1.9621 0.1813  -0.3866 0.0232  347 GLY C C   
8443  O O   . GLY C 347 ? 1.6562 1.8267 1.9034 0.1821  -0.3962 0.0260  347 GLY C O   
8444  N N   . TRP C 348 ? 1.9777 2.1696 2.2701 0.1876  -0.3924 0.0180  348 TRP C N   
8445  C CA  . TRP C 348 ? 1.9560 2.1471 2.2584 0.1962  -0.4110 0.0156  348 TRP C CA  
8446  C C   . TRP C 348 ? 1.9141 2.1290 2.2377 0.1956  -0.4154 0.0079  348 TRP C C   
8447  O O   . TRP C 348 ? 1.9019 2.1398 2.2460 0.1909  -0.4043 0.0022  348 TRP C O   
8448  C CB  . TRP C 348 ? 1.9848 2.1783 2.3090 0.2035  -0.4151 0.0125  348 TRP C CB  
8449  C CG  . TRP C 348 ? 2.0444 2.2209 2.3559 0.2025  -0.4064 0.0180  348 TRP C CG  
8450  C CD1 . TRP C 348 ? 2.0724 2.2574 2.3906 0.1968  -0.3896 0.0166  348 TRP C CD1 
8451  C CD2 . TRP C 348 ? 2.0796 2.2280 2.3706 0.2072  -0.4143 0.0256  348 TRP C CD2 
8452  N NE1 . TRP C 348 ? 2.1093 2.2734 2.4129 0.1974  -0.3864 0.0226  348 TRP C NE1 
8453  C CE2 . TRP C 348 ? 2.1408 2.2820 2.4276 0.2037  -0.4012 0.0284  348 TRP C CE2 
8454  C CE3 . TRP C 348 ? 2.0624 2.1908 2.3380 0.2141  -0.4313 0.0305  348 TRP C CE3 
8455  C CZ2 . TRP C 348 ? 2.2009 2.3153 2.4690 0.2065  -0.4042 0.0360  348 TRP C CZ2 
8456  C CZ3 . TRP C 348 ? 2.1067 2.2082 2.3628 0.2171  -0.4343 0.0385  348 TRP C CZ3 
8457  C CH2 . TRP C 348 ? 2.1620 2.2567 2.4148 0.2131  -0.4206 0.0412  348 TRP C CH2 
8458  N N   . LYS C 349 ? 1.6145 1.8238 1.9333 0.2003  -0.4319 0.0080  349 LYS C N   
8459  C CA  . LYS C 349 ? 1.5570 1.7873 1.8966 0.2006  -0.4391 0.0008  349 LYS C CA  
8460  C C   . LYS C 349 ? 1.5535 1.7965 1.8907 0.1913  -0.4267 -0.0010 349 LYS C C   
8461  O O   . LYS C 349 ? 1.4702 1.7358 1.8307 0.1897  -0.4274 -0.0079 349 LYS C O   
8462  C CB  . LYS C 349 ? 1.4808 1.7345 1.8601 0.2057  -0.4418 -0.0078 349 LYS C CB  
8463  C CG  . LYS C 349 ? 1.4422 1.6873 1.8291 0.2164  -0.4588 -0.0080 349 LYS C CG  
8464  C CD  . LYS C 349 ? 1.4670 1.6932 1.8431 0.2196  -0.4556 -0.0027 349 LYS C CD  
8465  C CE  . LYS C 349 ? 1.3964 1.6142 1.7818 0.2306  -0.4724 -0.0031 349 LYS C CE  
8466  N NZ  . LYS C 349 ? 1.3046 1.5036 1.6804 0.2336  -0.4690 0.0020  349 LYS C NZ  
8467  N N   . SER C 350 ? 1.6035 1.8324 1.9134 0.1850  -0.4154 0.0053  350 SER C N   
8468  C CA  . SER C 350 ? 1.5858 1.8251 1.8921 0.1763  -0.4033 0.0041  350 SER C CA  
8469  C C   . SER C 350 ? 1.5675 1.8034 1.8618 0.1754  -0.4135 0.0036  350 SER C C   
8470  O O   . SER C 350 ? 1.6108 1.8289 1.8873 0.1802  -0.4278 0.0069  350 SER C O   
8471  C CB  . SER C 350 ? 1.5695 1.7944 1.8506 0.1703  -0.3884 0.0108  350 SER C CB  
8472  O OG  . SER C 350 ? 1.6057 1.8317 1.8963 0.1712  -0.3799 0.0114  350 SER C OG  
8473  N N   . SER C 351 ? 1.5671 1.8199 1.8708 0.1691  -0.4063 -0.0005 351 SER C N   
8474  C CA  . SER C 351 ? 1.5915 1.8436 1.8868 0.1674  -0.4148 -0.0021 351 SER C CA  
8475  C C   . SER C 351 ? 1.5779 1.8267 1.8542 0.1589  -0.4012 0.0004  351 SER C C   
8476  O O   . SER C 351 ? 1.6257 1.8915 1.9170 0.1534  -0.3873 -0.0022 351 SER C O   
8477  C CB  . SER C 351 ? 1.5859 1.8633 1.9151 0.1684  -0.4214 -0.0107 351 SER C CB  
8478  O OG  . SER C 351 ? 1.5385 1.8140 1.8596 0.1670  -0.4311 -0.0125 351 SER C OG  
8479  N N   . ILE C 352 ? 1.5271 1.7543 1.7704 0.1580  -0.4052 0.0055  352 ILE C N   
8480  C CA  . ILE C 352 ? 1.5283 1.7498 1.7507 0.1506  -0.3932 0.0081  352 ILE C CA  
8481  C C   . ILE C 352 ? 1.5089 1.7344 1.7298 0.1488  -0.4016 0.0039  352 ILE C C   
8482  O O   . ILE C 352 ? 1.5170 1.7284 1.7216 0.1526  -0.4162 0.0050  352 ILE C O   
8483  C CB  . ILE C 352 ? 1.5259 1.7200 1.7113 0.1504  -0.3900 0.0166  352 ILE C CB  
8484  C CG1 . ILE C 352 ? 1.4684 1.6591 1.6569 0.1515  -0.3810 0.0205  352 ILE C CG1 
8485  C CG2 . ILE C 352 ? 1.5122 1.7007 1.6762 0.1432  -0.3786 0.0187  352 ILE C CG2 
8486  C CD1 . ILE C 352 ? 1.4417 1.6520 1.6509 0.1461  -0.3641 0.0177  352 ILE C CD1 
8487  N N   . GLY C 353 ? 1.4928 1.7370 1.7305 0.1430  -0.3927 -0.0007 353 GLY C N   
8488  C CA  . GLY C 353 ? 1.4553 1.7055 1.6957 0.1407  -0.3999 -0.0054 353 GLY C CA  
8489  C C   . GLY C 353 ? 1.4656 1.6948 1.6702 0.1384  -0.4011 -0.0018 353 GLY C C   
8490  O O   . GLY C 353 ? 1.4562 1.6671 1.6336 0.1375  -0.3942 0.0046  353 GLY C O   
8491  N N   . ARG C 354 ? 1.4744 1.7063 1.6794 0.1371  -0.4101 -0.0063 354 ARG C N   
8492  C CA  . ARG C 354 ? 1.5059 1.7185 1.6777 0.1353  -0.4129 -0.0041 354 ARG C CA  
8493  C C   . ARG C 354 ? 1.4923 1.7054 1.6541 0.1278  -0.3954 -0.0028 354 ARG C C   
8494  O O   . ARG C 354 ? 1.4811 1.7135 1.6661 0.1233  -0.3856 -0.0064 354 ARG C O   
8495  C CB  . ARG C 354 ? 1.5063 1.7217 1.6825 0.1364  -0.4290 -0.0100 354 ARG C CB  
8496  C CG  . ARG C 354 ? 1.4943 1.7353 1.7046 0.1326  -0.4273 -0.0174 354 ARG C CG  
8497  C CD  . ARG C 354 ? 1.5588 1.8019 1.7744 0.1342  -0.4449 -0.0233 354 ARG C CD  
8498  N NE  . ARG C 354 ? 1.5012 1.7396 1.7196 0.1421  -0.4623 -0.0233 354 ARG C NE  
8499  C CZ  . ARG C 354 ? 1.4611 1.7175 1.7125 0.1457  -0.4691 -0.0273 354 ARG C CZ  
8500  N NH1 . ARG C 354 ? 1.5116 1.7921 1.7954 0.1418  -0.4596 -0.0316 354 ARG C NH1 
8501  N NH2 . ARG C 354 ? 1.3872 1.6377 1.6392 0.1533  -0.4854 -0.0271 354 ARG C NH2 
8502  N N   . TRP C 355 ? 1.5414 1.7327 1.6681 0.1267  -0.3914 0.0024  355 TRP C N   
8503  C CA  . TRP C 355 ? 1.5367 1.7253 1.6499 0.1204  -0.3747 0.0044  355 TRP C CA  
8504  C C   . TRP C 355 ? 1.5311 1.7321 1.6608 0.1176  -0.3582 0.0064  355 TRP C C   
8505  O O   . TRP C 355 ? 1.5229 1.7306 1.6544 0.1120  -0.3442 0.0061  355 TRP C O   
8506  C CB  . TRP C 355 ? 1.5471 1.7445 1.6662 0.1158  -0.3745 -0.0015 355 TRP C CB  
8507  C CG  . TRP C 355 ? 1.6261 1.8070 1.7202 0.1173  -0.3872 -0.0028 355 TRP C CG  
8508  C CD1 . TRP C 355 ? 1.6540 1.8123 1.7112 0.1171  -0.3854 0.0015  355 TRP C CD1 
8509  C CD2 . TRP C 355 ? 1.6361 1.8216 1.7399 0.1193  -0.4038 -0.0088 355 TRP C CD2 
8510  N NE1 . TRP C 355 ? 1.6793 1.8275 1.7214 0.1189  -0.4000 -0.0017 355 TRP C NE1 
8511  C CE2 . TRP C 355 ? 1.6616 1.8261 1.7321 0.1203  -0.4118 -0.0081 355 TRP C CE2 
8512  C CE3 . TRP C 355 ? 1.5752 1.7808 1.7128 0.1202  -0.4127 -0.0150 355 TRP C CE3 
8513  C CZ2 . TRP C 355 ? 1.6143 1.7772 1.6842 0.1221  -0.4288 -0.0134 355 TRP C CZ2 
8514  C CZ3 . TRP C 355 ? 1.5852 1.7897 1.7233 0.1219  -0.4293 -0.0202 355 TRP C CZ3 
8515  C CH2 . TRP C 355 ? 1.5989 1.7820 1.7033 0.1229  -0.4375 -0.0195 355 TRP C CH2 
8516  N N   . SER C 356 ? 1.4503 1.6541 1.5919 0.1216  -0.3598 0.0084  356 SER C N   
8517  C CA  . SER C 356 ? 1.4036 1.6170 1.5584 0.1195  -0.3451 0.0105  356 SER C CA  
8518  C C   . SER C 356 ? 1.3425 1.5354 1.4698 0.1198  -0.3383 0.0181  356 SER C C   
8519  O O   . SER C 356 ? 1.3688 1.5420 1.4732 0.1238  -0.3478 0.0220  356 SER C O   
8520  C CB  . SER C 356 ? 1.4151 1.6449 1.6013 0.1234  -0.3500 0.0075  356 SER C CB  
8521  O OG  . SER C 356 ? 1.3974 1.6155 1.5775 0.1303  -0.3652 0.0088  356 SER C OG  
8522  N N   . ARG C 357 ? 1.2948 1.4927 1.4246 0.1156  -0.3219 0.0205  357 ARG C N   
8523  C CA  . ARG C 357 ? 1.2133 1.3934 1.3182 0.1145  -0.3129 0.0275  357 ARG C CA  
8524  C C   . ARG C 357 ? 1.2291 1.4180 1.3511 0.1144  -0.3037 0.0290  357 ARG C C   
8525  O O   . ARG C 357 ? 1.2998 1.5094 1.4471 0.1118  -0.2960 0.0252  357 ARG C O   
8526  C CB  . ARG C 357 ? 1.2345 1.4095 1.3208 0.1086  -0.3003 0.0291  357 ARG C CB  
8527  C CG  . ARG C 357 ? 1.2324 1.3866 1.2889 0.1075  -0.2924 0.0364  357 ARG C CG  
8528  C CD  . ARG C 357 ? 1.2287 1.3817 1.2722 0.1016  -0.2785 0.0371  357 ARG C CD  
8529  N NE  . ARG C 357 ? 1.2152 1.3483 1.2290 0.1002  -0.2707 0.0438  357 ARG C NE  
8530  C CZ  . ARG C 357 ? 1.2681 1.3823 1.2514 0.1004  -0.2740 0.0462  357 ARG C CZ  
8531  N NH1 . ARG C 357 ? 1.2786 1.3908 1.2567 0.1022  -0.2857 0.0421  357 ARG C NH1 
8532  N NH2 . ARG C 357 ? 1.3489 1.4462 1.3066 0.0988  -0.2656 0.0524  357 ARG C NH2 
8533  N N   . VAL C 358 ? 1.2160 1.3887 1.3236 0.1172  -0.3047 0.0346  358 VAL C N   
8534  C CA  . VAL C 358 ? 1.2071 1.3847 1.3277 0.1173  -0.2967 0.0364  358 VAL C CA  
8535  C C   . VAL C 358 ? 1.2050 1.3629 1.2979 0.1149  -0.2873 0.0438  358 VAL C C   
8536  O O   . VAL C 358 ? 1.2338 1.3712 1.3061 0.1182  -0.2944 0.0489  358 VAL C O   
8537  C CB  . VAL C 358 ? 1.1620 1.3404 1.2974 0.1241  -0.3089 0.0353  358 VAL C CB  
8538  C CG1 . VAL C 358 ? 1.2541 1.4382 1.4040 0.1239  -0.3000 0.0363  358 VAL C CG1 
8539  C CG2 . VAL C 358 ? 1.1522 1.3492 1.3136 0.1267  -0.3193 0.0279  358 VAL C CG2 
8540  N N   . GLN C 359 ? 1.1725 1.3362 1.2650 0.1090  -0.2715 0.0447  359 GLN C N   
8541  C CA  . GLN C 359 ? 1.2007 1.3475 1.2684 0.1059  -0.2612 0.0514  359 GLN C CA  
8542  C C   . GLN C 359 ? 1.2054 1.3625 1.2878 0.1024  -0.2472 0.0520  359 GLN C C   
8543  O O   . GLN C 359 ? 1.2080 1.3857 1.3180 0.1020  -0.2445 0.0470  359 GLN C O   
8544  C CB  . GLN C 359 ? 1.2209 1.3608 1.2668 0.1017  -0.2552 0.0524  359 GLN C CB  
8545  C CG  . GLN C 359 ? 1.1741 1.3336 1.2361 0.0967  -0.2441 0.0480  359 GLN C CG  
8546  C CD  . GLN C 359 ? 1.2424 1.3929 1.2816 0.0921  -0.2337 0.0505  359 GLN C CD  
8547  O OE1 . GLN C 359 ? 1.2857 1.4176 1.2976 0.0930  -0.2379 0.0535  359 GLN C OE1 
8548  N NE2 . GLN C 359 ? 1.2721 1.4359 1.3223 0.0874  -0.2200 0.0492  359 GLN C NE2 
8549  N N   . ALA C 360 ? 1.2208 1.3630 1.2837 0.0998  -0.2383 0.0581  360 ALA C N   
8550  C CA  . ALA C 360 ? 1.2385 1.3879 1.3114 0.0959  -0.2245 0.0592  360 ALA C CA  
8551  C C   . ALA C 360 ? 1.3274 1.4599 1.3734 0.0917  -0.2141 0.0657  360 ALA C C   
8552  O O   . ALA C 360 ? 1.3381 1.4528 1.3579 0.0923  -0.2182 0.0694  360 ALA C O   
8553  C CB  . ALA C 360 ? 1.2367 1.3866 1.3245 0.0993  -0.2284 0.0594  360 ALA C CB  
8554  N N   . SER C 361 ? 1.3336 1.4725 1.3866 0.0873  -0.2004 0.0668  361 SER C N   
8555  C CA  . SER C 361 ? 1.3450 1.4704 1.3754 0.0827  -0.1890 0.0725  361 SER C CA  
8556  C C   . SER C 361 ? 1.3964 1.4982 1.4059 0.0843  -0.1924 0.0795  361 SER C C   
8557  O O   . SER C 361 ? 1.4184 1.5025 1.4005 0.0826  -0.1895 0.0847  361 SER C O   
8558  C CB  . SER C 361 ? 1.3137 1.4535 1.3591 0.0776  -0.1740 0.0714  361 SER C CB  
8559  O OG  . SER C 361 ? 1.2852 1.4466 1.3606 0.0787  -0.1753 0.0654  361 SER C OG  
8560  N N   . GLY C 362 ? 1.4779 1.5786 1.4997 0.0877  -0.1985 0.0797  362 GLY C N   
8561  C CA  . GLY C 362 ? 1.5377 1.6164 1.5424 0.0890  -0.2010 0.0866  362 GLY C CA  
8562  C C   . GLY C 362 ? 1.6030 1.6807 1.6124 0.0847  -0.1888 0.0895  362 GLY C C   
8563  O O   . GLY C 362 ? 1.6575 1.7159 1.6518 0.0848  -0.1892 0.0959  362 GLY C O   
8564  N N   . ASP C 363 ? 1.5755 1.6732 1.6053 0.0808  -0.1782 0.0852  363 ASP C N   
8565  C CA  . ASP C 363 ? 1.6054 1.7045 1.6418 0.0764  -0.1664 0.0872  363 ASP C CA  
8566  C C   . ASP C 363 ? 1.6744 1.7742 1.7282 0.0799  -0.1726 0.0858  363 ASP C C   
8567  O O   . ASP C 363 ? 1.6565 1.7749 1.7354 0.0822  -0.1759 0.0792  363 ASP C O   
8568  C CB  . ASP C 363 ? 1.5416 1.6625 1.5945 0.0716  -0.1544 0.0826  363 ASP C CB  
8569  C CG  . ASP C 363 ? 1.5877 1.7083 1.6425 0.0661  -0.1410 0.0852  363 ASP C CG  
8570  O OD1 . ASP C 363 ? 1.6253 1.7264 1.6625 0.0646  -0.1389 0.0917  363 ASP C OD1 
8571  O OD2 . ASP C 363 ? 1.5868 1.7267 1.6609 0.0631  -0.1328 0.0809  363 ASP C OD2 
8572  N N   . TYR C 364 ? 1.8654 1.9447 1.9055 0.0803  -0.1740 0.0920  364 TYR C N   
8573  C CA  . TYR C 364 ? 1.8720 1.9494 1.9271 0.0836  -0.1796 0.0910  364 TYR C CA  
8574  C C   . TYR C 364 ? 1.8533 1.9450 1.9295 0.0794  -0.1687 0.0877  364 TYR C C   
8575  O O   . TYR C 364 ? 1.8588 1.9505 1.9493 0.0819  -0.1723 0.0859  364 TYR C O   
8576  C CB  . TYR C 364 ? 1.9365 1.9859 1.9694 0.0850  -0.1843 0.0993  364 TYR C CB  
8577  C CG  . TYR C 364 ? 2.0213 2.0553 2.0321 0.0895  -0.1961 0.1028  364 TYR C CG  
8578  C CD1 . TYR C 364 ? 2.0403 2.0754 2.0597 0.0969  -0.2116 0.0997  364 TYR C CD1 
8579  C CD2 . TYR C 364 ? 2.0437 2.0626 2.0253 0.0864  -0.1919 0.1090  364 TYR C CD2 
8580  C CE1 . TYR C 364 ? 2.0013 2.0227 2.0007 0.1011  -0.2232 0.1027  364 TYR C CE1 
8581  C CE2 . TYR C 364 ? 2.0488 2.0535 2.0091 0.0905  -0.2031 0.1119  364 TYR C CE2 
8582  C CZ  . TYR C 364 ? 2.0201 2.0261 1.9895 0.0978  -0.2190 0.1088  364 TYR C CZ  
8583  O OH  . TYR C 364 ? 2.0380 2.0302 1.9866 0.1020  -0.2309 0.1115  364 TYR C OH  
8584  N N   . ASN C 365 ? 1.7081 1.8118 1.7865 0.0735  -0.1559 0.0865  365 ASN C N   
8585  C CA  . ASN C 365 ? 1.6583 1.7784 1.7579 0.0697  -0.1461 0.0825  365 ASN C CA  
8586  C C   . ASN C 365 ? 1.6129 1.7597 1.7366 0.0708  -0.1462 0.0742  365 ASN C C   
8587  O O   . ASN C 365 ? 1.5937 1.7547 1.7388 0.0702  -0.1431 0.0694  365 ASN C O   
8588  C CB  . ASN C 365 ? 1.6507 1.7681 1.7396 0.0623  -0.1315 0.0864  365 ASN C CB  
8589  C CG  . ASN C 365 ? 1.7227 1.8138 1.7839 0.0605  -0.1302 0.0953  365 ASN C CG  
8590  O OD1 . ASN C 365 ? 1.7816 1.8558 1.8364 0.0634  -0.1374 0.0989  365 ASN C OD1 
8591  N ND2 . ASN C 365 ? 1.7151 1.8024 1.7595 0.0559  -0.1210 0.0989  365 ASN C ND2 
8592  N N   . ASP C 366 ? 1.6652 1.8187 1.7853 0.0721  -0.1496 0.0724  366 ASP C N   
8593  C CA  . ASP C 366 ? 1.6525 1.8303 1.7944 0.0731  -0.1502 0.0651  366 ASP C CA  
8594  C C   . ASP C 366 ? 1.6871 1.8697 1.8438 0.0798  -0.1632 0.0607  366 ASP C C   
8595  O O   . ASP C 366 ? 1.7204 1.8874 1.8658 0.0843  -0.1739 0.0634  366 ASP C O   
8596  C CB  . ASP C 366 ? 1.6406 1.8231 1.7731 0.0716  -0.1483 0.0650  366 ASP C CB  
8597  C CG  . ASP C 366 ? 1.6275 1.8347 1.7820 0.0718  -0.1478 0.0581  366 ASP C CG  
8598  O OD1 . ASP C 366 ? 1.6330 1.8554 1.8092 0.0719  -0.1457 0.0537  366 ASP C OD1 
8599  O OD2 . ASP C 366 ? 1.6030 1.8142 1.7527 0.0719  -0.1495 0.0571  366 ASP C OD2 
8600  N N   . ARG C 367 ? 1.5294 1.7338 1.7115 0.0805  -0.1621 0.0539  367 ARG C N   
8601  C CA  . ARG C 367 ? 1.4434 1.6548 1.6423 0.0867  -0.1734 0.0490  367 ARG C CA  
8602  C C   . ARG C 367 ? 1.3627 1.5743 1.5569 0.0902  -0.1834 0.0481  367 ARG C C   
8603  O O   . ARG C 367 ? 1.3156 1.5194 1.5097 0.0959  -0.1955 0.0479  367 ARG C O   
8604  C CB  . ARG C 367 ? 1.4484 1.6843 1.6745 0.0861  -0.1688 0.0417  367 ARG C CB  
8605  C CG  . ARG C 367 ? 1.4034 1.6455 1.6485 0.0923  -0.1784 0.0365  367 ARG C CG  
8606  C CD  . ARG C 367 ? 1.3297 1.5962 1.6004 0.0914  -0.1729 0.0293  367 ARG C CD  
8607  N NE  . ARG C 367 ? 1.3046 1.5767 1.5934 0.0973  -0.1810 0.0240  367 ARG C NE  
8608  C CZ  . ARG C 367 ? 1.2615 1.5545 1.5734 0.0980  -0.1784 0.0170  367 ARG C CZ  
8609  N NH1 . ARG C 367 ? 1.2618 1.5719 1.5810 0.0931  -0.1682 0.0149  367 ARG C NH1 
8610  N NH2 . ARG C 367 ? 1.1428 1.4396 1.4703 0.1038  -0.1860 0.0122  367 ARG C NH2 
8611  N N   . LEU C 368 ? 1.3839 1.6042 1.5745 0.0869  -0.1787 0.0476  368 LEU C N   
8612  C CA  . LEU C 368 ? 1.3630 1.5837 1.5489 0.0895  -0.1875 0.0465  368 LEU C CA  
8613  C C   . LEU C 368 ? 1.4125 1.6113 1.5687 0.0889  -0.1897 0.0527  368 LEU C C   
8614  O O   . LEU C 368 ? 1.3832 1.5825 1.5321 0.0892  -0.1938 0.0520  368 LEU C O   
8615  C CB  . LEU C 368 ? 1.3214 1.5637 1.5210 0.0865  -0.1819 0.0419  368 LEU C CB  
8616  C CG  . LEU C 368 ? 1.2078 1.4731 1.4363 0.0872  -0.1801 0.0354  368 LEU C CG  
8617  C CD1 . LEU C 368 ? 1.1814 1.4661 1.4213 0.0844  -0.1755 0.0318  368 LEU C CD1 
8618  C CD2 . LEU C 368 ? 1.1830 1.4497 1.4247 0.0936  -0.1924 0.0319  368 LEU C CD2 
8619  N N   . GLY C 369 ? 1.4699 1.6495 1.6086 0.0878  -0.1869 0.0587  369 GLY C N   
8620  C CA  . GLY C 369 ? 1.4657 1.6236 1.5748 0.0874  -0.1889 0.0650  369 GLY C CA  
8621  C C   . GLY C 369 ? 1.4170 1.5619 1.5166 0.0935  -0.2045 0.0661  369 GLY C C   
8622  O O   . GLY C 369 ? 1.3966 1.5271 1.4728 0.0937  -0.2080 0.0697  369 GLY C O   
8623  N N   . ILE C 370 ? 1.4018 1.5516 1.5190 0.0988  -0.2142 0.0627  370 ILE C N   
8624  C CA  . ILE C 370 ? 1.4235 1.5629 1.5355 0.1053  -0.2302 0.0631  370 ILE C CA  
8625  C C   . ILE C 370 ? 1.3771 1.5381 1.5173 0.1091  -0.2375 0.0551  370 ILE C C   
8626  O O   . ILE C 370 ? 1.3535 1.5257 1.5159 0.1109  -0.2371 0.0513  370 ILE C O   
8627  C CB  . ILE C 370 ? 1.4687 1.5888 1.5727 0.1089  -0.2358 0.0680  370 ILE C CB  
8628  C CG1 . ILE C 370 ? 1.5141 1.6127 1.5902 0.1046  -0.2277 0.0763  370 ILE C CG1 
8629  C CG2 . ILE C 370 ? 1.4044 1.5147 1.5042 0.1162  -0.2532 0.0681  370 ILE C CG2 
8630  C CD1 . ILE C 370 ? 1.5346 1.6191 1.5825 0.1038  -0.2303 0.0805  370 ILE C CD1 
8631  N N   . THR C 371 ? 1.3281 1.4949 1.4675 0.1101  -0.2439 0.0524  371 THR C N   
8632  C CA  . THR C 371 ? 1.3105 1.4980 1.4765 0.1132  -0.2508 0.0449  371 THR C CA  
8633  C C   . THR C 371 ? 1.2495 1.4317 1.4237 0.1207  -0.2653 0.0438  371 THR C C   
8634  O O   . THR C 371 ? 1.2559 1.4183 1.4108 0.1243  -0.2753 0.0482  371 THR C O   
8635  C CB  . THR C 371 ? 1.2601 1.4539 1.4226 0.1120  -0.2542 0.0425  371 THR C CB  
8636  O OG1 . THR C 371 ? 1.2224 1.4336 1.4095 0.1156  -0.2632 0.0358  371 THR C OG1 
8637  C CG2 . THR C 371 ? 1.2429 1.4142 1.3757 0.1135  -0.2623 0.0475  371 THR C CG2 
8638  N N   . ILE C 372 ? 1.2070 1.4068 1.4095 0.1232  -0.2662 0.0380  372 ILE C N   
8639  C CA  . ILE C 372 ? 1.1534 1.3505 1.3678 0.1305  -0.2785 0.0362  372 ILE C CA  
8640  C C   . ILE C 372 ? 1.1530 1.3721 1.3939 0.1336  -0.2855 0.0283  372 ILE C C   
8641  O O   . ILE C 372 ? 1.1723 1.4132 1.4331 0.1304  -0.2772 0.0232  372 ILE C O   
8642  C CB  . ILE C 372 ? 1.1976 1.3935 1.4218 0.1312  -0.2729 0.0363  372 ILE C CB  
8643  C CG1 . ILE C 372 ? 1.2966 1.4706 1.4949 0.1275  -0.2654 0.0443  372 ILE C CG1 
8644  C CG2 . ILE C 372 ? 1.2998 1.4925 1.5368 0.1394  -0.2860 0.0341  372 ILE C CG2 
8645  C CD1 . ILE C 372 ? 1.4117 1.5859 1.6193 0.1263  -0.2570 0.0443  372 ILE C CD1 
8646  N N   . LEU C 373 ? 1.1983 1.4119 1.4395 0.1397  -0.3009 0.0275  373 LEU C N   
8647  C CA  . LEU C 373 ? 1.2371 1.4703 1.5032 0.1431  -0.3093 0.0202  373 LEU C CA  
8648  C C   . LEU C 373 ? 1.2959 1.5322 1.5819 0.1504  -0.3180 0.0169  373 LEU C C   
8649  O O   . LEU C 373 ? 1.3578 1.5746 1.6316 0.1551  -0.3259 0.0211  373 LEU C O   
8650  C CB  . LEU C 373 ? 1.2810 1.5077 1.5346 0.1445  -0.3211 0.0208  373 LEU C CB  
8651  C CG  . LEU C 373 ? 1.2767 1.5163 1.5313 0.1387  -0.3153 0.0183  373 LEU C CG  
8652  C CD1 . LEU C 373 ? 1.2439 1.4776 1.4802 0.1315  -0.3000 0.0228  373 LEU C CD1 
8653  C CD2 . LEU C 373 ? 1.3530 1.5848 1.5954 0.1407  -0.3286 0.0184  373 LEU C CD2 
8654  N N   . GLY C 374 ? 1.3848 1.6454 1.7012 0.1514  -0.3163 0.0093  374 GLY C N   
8655  C CA  . GLY C 374 ? 1.5968 1.8632 1.9350 0.1582  -0.3231 0.0049  374 GLY C CA  
8656  C C   . GLY C 374 ? 1.7716 2.0332 2.1133 0.1657  -0.3412 0.0037  374 GLY C C   
8657  O O   . GLY C 374 ? 1.7211 1.9708 2.0444 0.1659  -0.3496 0.0072  374 GLY C O   
8658  N N   . GLU C 375 ? 2.3982 2.6697 2.7646 0.1721  -0.3474 -0.0017 375 GLU C N   
8659  C CA  . GLU C 375 ? 2.3998 2.6693 2.7744 0.1800  -0.3649 -0.0038 375 GLU C CA  
8660  C C   . GLU C 375 ? 2.3705 2.6621 2.7642 0.1791  -0.3690 -0.0101 375 GLU C C   
8661  O O   . GLU C 375 ? 2.3314 2.6467 2.7483 0.1760  -0.3600 -0.0162 375 GLU C O   
8662  C CB  . GLU C 375 ? 2.3925 2.6645 2.7874 0.1875  -0.3698 -0.0075 375 GLU C CB  
8663  C CG  . GLU C 375 ? 2.3910 2.6637 2.7988 0.1963  -0.3880 -0.0106 375 GLU C CG  
8664  C CD  . GLU C 375 ? 2.4056 2.6872 2.8403 0.2035  -0.3910 -0.0164 375 GLU C CD  
8665  O OE1 . GLU C 375 ? 2.3940 2.6826 2.8379 0.2013  -0.3787 -0.0187 375 GLU C OE1 
8666  O OE2 . GLU C 375 ? 2.4174 2.6992 2.8641 0.2115  -0.4060 -0.0190 375 GLU C OE2 
8667  N N   . ALA C 376 ? 1.8855 2.1689 2.2692 0.1817  -0.3827 -0.0087 376 ALA C N   
8668  C CA  . ALA C 376 ? 1.7459 2.0480 2.1470 0.1812  -0.3888 -0.0145 376 ALA C CA  
8669  C C   . ALA C 376 ? 1.6657 1.9827 2.0685 0.1720  -0.3747 -0.0160 376 ALA C C   
8670  O O   . ALA C 376 ? 1.6132 1.9546 2.0421 0.1702  -0.3712 -0.0225 376 ALA C O   
8671  C CB  . ALA C 376 ? 1.7331 2.0555 2.1699 0.1874  -0.3952 -0.0226 376 ALA C CB  
8672  N N   . VAL C 377 ? 1.6385 1.9404 2.0132 0.1663  -0.3666 -0.0097 377 VAL C N   
8673  C CA  . VAL C 377 ? 1.6117 1.9239 1.9836 0.1579  -0.3545 -0.0101 377 VAL C CA  
8674  C C   . VAL C 377 ? 1.6544 1.9609 2.0130 0.1565  -0.3635 -0.0094 377 VAL C C   
8675  O O   . VAL C 377 ? 1.6179 1.9023 1.9513 0.1589  -0.3726 -0.0044 377 VAL C O   
8676  C CB  . VAL C 377 ? 1.5215 1.8219 1.8722 0.1525  -0.3399 -0.0042 377 VAL C CB  
8677  C CG1 . VAL C 377 ? 1.5269 1.7981 1.8464 0.1549  -0.3455 0.0034  377 VAL C CG1 
8678  C CG2 . VAL C 377 ? 1.4846 1.7921 1.8284 0.1444  -0.3292 -0.0039 377 VAL C CG2 
8679  N N   . THR C 378 ? 2.0521 2.3782 2.4276 0.1526  -0.3612 -0.0144 378 THR C N   
8680  C CA  . THR C 378 ? 2.0552 2.3791 2.4230 0.1511  -0.3702 -0.0153 378 THR C CA  
8681  C C   . THR C 378 ? 2.0607 2.3843 2.4140 0.1428  -0.3577 -0.0131 378 THR C C   
8682  O O   . THR C 378 ? 2.0323 2.3756 2.4038 0.1378  -0.3480 -0.0167 378 THR C O   
8683  C CB  . THR C 378 ? 2.0245 2.3705 2.4238 0.1532  -0.3786 -0.0230 378 THR C CB  
8684  O OG1 . THR C 378 ? 1.9997 2.3695 2.4223 0.1480  -0.3654 -0.0271 378 THR C OG1 
8685  C CG2 . THR C 378 ? 2.0181 2.3656 2.4337 0.1619  -0.3903 -0.0255 378 THR C CG2 
8686  N N   . VAL C 379 ? 1.7547 2.0557 2.0753 0.1413  -0.3577 -0.0071 379 VAL C N   
8687  C CA  . VAL C 379 ? 1.6795 1.9780 1.9843 0.1341  -0.3478 -0.0052 379 VAL C CA  
8688  C C   . VAL C 379 ? 1.6285 1.9293 1.9333 0.1334  -0.3584 -0.0087 379 VAL C C   
8689  O O   . VAL C 379 ? 1.6391 1.9246 1.9282 0.1374  -0.3721 -0.0074 379 VAL C O   
8690  C CB  . VAL C 379 ? 1.6443 1.9182 1.9143 0.1328  -0.3426 0.0023  379 VAL C CB  
8691  C CG1 . VAL C 379 ? 1.6086 1.8800 1.8626 0.1258  -0.3331 0.0037  379 VAL C CG1 
8692  C CG2 . VAL C 379 ? 1.6546 1.9267 1.9260 0.1331  -0.3322 0.0054  379 VAL C CG2 
8693  N N   . GLU C 380 ? 1.5419 1.8613 1.8643 0.1283  -0.3523 -0.0130 380 GLU C N   
8694  C CA  . GLU C 380 ? 1.4438 1.7676 1.7704 0.1271  -0.3621 -0.0171 380 GLU C CA  
8695  C C   . GLU C 380 ? 1.4002 1.7040 1.6940 0.1243  -0.3627 -0.0136 380 GLU C C   
8696  O O   . GLU C 380 ? 1.4252 1.7132 1.6941 0.1228  -0.3545 -0.0079 380 GLU C O   
8697  C CB  . GLU C 380 ? 1.4256 1.7746 1.7806 0.1220  -0.3546 -0.0224 380 GLU C CB  
8698  C CG  . GLU C 380 ? 1.3438 1.7056 1.7201 0.1234  -0.3677 -0.0287 380 GLU C CG  
8699  C CD  . GLU C 380 ? 1.3475 1.7367 1.7580 0.1200  -0.3604 -0.0338 380 GLU C CD  
8700  O OE1 . GLU C 380 ? 1.4124 1.8109 1.8307 0.1175  -0.3463 -0.0325 380 GLU C OE1 
8701  O OE2 . GLU C 380 ? 1.2453 1.6468 1.6747 0.1196  -0.3689 -0.0390 380 GLU C OE2 
8702  N N   . ASP C 381 ? 1.3866 1.6915 1.6808 0.1234  -0.3726 -0.0173 381 ASP C N   
8703  C CA  . ASP C 381 ? 1.4152 1.7017 1.6791 0.1211  -0.3746 -0.0151 381 ASP C CA  
8704  C C   . ASP C 381 ? 1.4052 1.6923 1.6601 0.1141  -0.3573 -0.0130 381 ASP C C   
8705  O O   . ASP C 381 ? 1.4133 1.7194 1.6903 0.1099  -0.3474 -0.0156 381 ASP C O   
8706  C CB  . ASP C 381 ? 1.4255 1.7164 1.6965 0.1210  -0.3881 -0.0208 381 ASP C CB  
8707  C CG  . ASP C 381 ? 1.4130 1.7109 1.7033 0.1273  -0.4043 -0.0244 381 ASP C CG  
8708  O OD1 . ASP C 381 ? 1.4069 1.6938 1.6887 0.1333  -0.4105 -0.0210 381 ASP C OD1 
8709  O OD2 . ASP C 381 ? 1.4429 1.7574 1.7576 0.1263  -0.4108 -0.0305 381 ASP C OD2 
8710  N N   . GLU C 382 ? 1.4543 1.7204 1.6762 0.1131  -0.3536 -0.0081 382 GLU C N   
8711  C CA  . GLU C 382 ? 1.4761 1.7388 1.6843 0.1072  -0.3380 -0.0055 382 GLU C CA  
8712  C C   . GLU C 382 ? 1.4740 1.7457 1.6922 0.1052  -0.3224 -0.0026 382 GLU C C   
8713  O O   . GLU C 382 ? 1.4854 1.7545 1.6929 0.1006  -0.3090 -0.0001 382 GLU C O   
8714  C CB  . GLU C 382 ? 1.5173 1.7911 1.7357 0.1020  -0.3358 -0.0103 382 GLU C CB  
8715  C CG  . GLU C 382 ? 1.5474 1.8091 1.7492 0.1026  -0.3484 -0.0129 382 GLU C CG  
8716  C CD  . GLU C 382 ? 1.5876 1.8562 1.7940 0.0968  -0.3435 -0.0167 382 GLU C CD  
8717  O OE1 . GLU C 382 ? 1.6189 1.8962 1.8324 0.0921  -0.3286 -0.0156 382 GLU C OE1 
8718  O OE2 . GLU C 382 ? 1.5689 1.8339 1.7720 0.0968  -0.3550 -0.0208 382 GLU C OE2 
8719  N N   . VAL C 383 ? 1.4394 1.7214 1.6778 0.1085  -0.3236 -0.0031 383 VAL C N   
8720  C CA  . VAL C 383 ? 1.4147 1.7060 1.6635 0.1065  -0.3092 -0.0011 383 VAL C CA  
8721  C C   . VAL C 383 ? 1.4504 1.7219 1.6723 0.1070  -0.3030 0.0056  383 VAL C C   
8722  O O   . VAL C 383 ? 1.4242 1.6784 1.6288 0.1115  -0.3122 0.0086  383 VAL C O   
8723  C CB  . VAL C 383 ? 1.4318 1.7397 1.7100 0.1102  -0.3129 -0.0044 383 VAL C CB  
8724  C CG1 . VAL C 383 ? 1.4432 1.7603 1.7313 0.1082  -0.2983 -0.0027 383 VAL C CG1 
8725  C CG2 . VAL C 383 ? 1.4524 1.7804 1.7577 0.1092  -0.3184 -0.0109 383 VAL C CG2 
8726  N N   . ALA C 384 ? 1.6348 1.9088 1.8533 0.1024  -0.2874 0.0081  384 ALA C N   
8727  C CA  . ALA C 384 ? 1.6614 1.9182 1.8555 0.1018  -0.2795 0.0143  384 ALA C CA  
8728  C C   . ALA C 384 ? 1.6454 1.9107 1.8534 0.1018  -0.2703 0.0157  384 ALA C C   
8729  O O   . ALA C 384 ? 1.6118 1.8970 1.8432 0.0993  -0.2629 0.0125  384 ALA C O   
8730  C CB  . ALA C 384 ? 1.6768 1.9279 1.8532 0.0964  -0.2687 0.0162  384 ALA C CB  
8731  N N   . VAL C 385 ? 1.3698 1.6194 1.5629 0.1044  -0.2708 0.0204  385 VAL C N   
8732  C CA  . VAL C 385 ? 1.2512 1.5053 1.4544 0.1046  -0.2628 0.0220  385 VAL C CA  
8733  C C   . VAL C 385 ? 1.2052 1.4410 1.3822 0.1023  -0.2540 0.0285  385 VAL C C   
8734  O O   . VAL C 385 ? 1.2132 1.4287 1.3687 0.1051  -0.2604 0.0328  385 VAL C O   
8735  C CB  . VAL C 385 ? 1.2411 1.4952 1.4567 0.1110  -0.2737 0.0207  385 VAL C CB  
8736  C CG1 . VAL C 385 ? 1.2579 1.5153 1.4825 0.1110  -0.2651 0.0221  385 VAL C CG1 
8737  C CG2 . VAL C 385 ? 1.2979 1.5713 1.5407 0.1132  -0.2822 0.0139  385 VAL C CG2 
8738  N N   . ILE C 386 ? 1.2268 1.4698 1.4056 0.0971  -0.2393 0.0294  386 ILE C N   
8739  C CA  . ILE C 386 ? 1.1914 1.4194 1.3476 0.0940  -0.2292 0.0352  386 ILE C CA  
8740  C C   . ILE C 386 ? 1.2271 1.4613 1.3953 0.0931  -0.2204 0.0363  386 ILE C C   
8741  O O   . ILE C 386 ? 1.2612 1.5138 1.4485 0.0902  -0.2116 0.0333  386 ILE C O   
8742  C CB  . ILE C 386 ? 1.1547 1.3849 1.3017 0.0887  -0.2193 0.0354  386 ILE C CB  
8743  C CG1 . ILE C 386 ? 1.1733 1.3955 1.3063 0.0896  -0.2282 0.0342  386 ILE C CG1 
8744  C CG2 . ILE C 386 ? 1.1756 1.3932 1.3029 0.0854  -0.2074 0.0410  386 ILE C CG2 
8745  C CD1 . ILE C 386 ? 1.1853 1.4256 1.3400 0.0895  -0.2333 0.0279  386 ILE C CD1 
8746  N N   . GLY C 387 ? 1.2624 1.4806 1.4189 0.0956  -0.2228 0.0405  387 GLY C N   
8747  C CA  . GLY C 387 ? 1.3258 1.5461 1.4901 0.0945  -0.2147 0.0420  387 GLY C CA  
8748  C C   . GLY C 387 ? 1.3733 1.6158 1.5686 0.0955  -0.2135 0.0363  387 GLY C C   
8749  O O   . GLY C 387 ? 1.4045 1.6599 1.6108 0.0915  -0.2020 0.0350  387 GLY C O   
8750  N N   . SER C 388 ? 1.6193 1.8665 1.8288 0.1008  -0.2252 0.0327  388 SER C N   
8751  C CA  . SER C 388 ? 1.5789 1.8475 1.8180 0.1021  -0.2247 0.0268  388 SER C CA  
8752  C C   . SER C 388 ? 1.5795 1.8430 1.8266 0.1087  -0.2358 0.0255  388 SER C C   
8753  O O   . SER C 388 ? 1.6121 1.8570 1.8431 0.1124  -0.2455 0.0290  388 SER C O   
8754  C CB  . SER C 388 ? 1.5436 1.8313 1.7991 0.1012  -0.2265 0.0215  388 SER C CB  
8755  O OG  . SER C 388 ? 1.5404 1.8343 1.7914 0.0953  -0.2154 0.0223  388 SER C OG  
8756  N N   . ILE C 389 ? 1.2382 1.5187 1.5106 0.1103  -0.2343 0.0205  389 ILE C N   
8757  C CA  . ILE C 389 ? 1.1518 1.4300 1.4356 0.1166  -0.2436 0.0184  389 ILE C CA  
8758  C C   . ILE C 389 ? 1.1397 1.4391 1.4501 0.1197  -0.2497 0.0111  389 ILE C C   
8759  O O   . ILE C 389 ? 1.1452 1.4654 1.4745 0.1169  -0.2417 0.0067  389 ILE C O   
8760  C CB  . ILE C 389 ? 1.1210 1.3988 1.4107 0.1161  -0.2357 0.0185  389 ILE C CB  
8761  C CG1 . ILE C 389 ? 1.1524 1.4122 1.4178 0.1117  -0.2273 0.0255  389 ILE C CG1 
8762  C CG2 . ILE C 389 ? 1.0987 1.3702 1.3971 0.1232  -0.2461 0.0170  389 ILE C CG2 
8763  C CD1 . ILE C 389 ? 1.2250 1.4588 1.4643 0.1140  -0.2354 0.0320  389 ILE C CD1 
8764  N N   . VAL C 390 ? 1.1638 1.4580 1.4757 0.1253  -0.2639 0.0101  390 VAL C N   
8765  C CA  . VAL C 390 ? 1.1396 1.4529 1.4769 0.1286  -0.2712 0.0032  390 VAL C CA  
8766  C C   . VAL C 390 ? 1.1855 1.4989 1.5378 0.1356  -0.2789 0.0003  390 VAL C C   
8767  O O   . VAL C 390 ? 1.2188 1.5121 1.5572 0.1398  -0.2864 0.0043  390 VAL C O   
8768  C CB  . VAL C 390 ? 1.1123 1.4221 1.4426 0.1298  -0.2822 0.0033  390 VAL C CB  
8769  C CG1 . VAL C 390 ? 1.1708 1.5026 1.5295 0.1321  -0.2882 -0.0040 390 VAL C CG1 
8770  C CG2 . VAL C 390 ? 1.1236 1.4296 1.4358 0.1232  -0.2746 0.0066  390 VAL C CG2 
8771  N N   . LEU C 391 ? 1.1769 1.5126 1.5575 0.1370  -0.2770 -0.0066 391 LEU C N   
8772  C CA  . LEU C 391 ? 1.2668 1.6055 1.6650 0.1438  -0.2837 -0.0107 391 LEU C CA  
8773  C C   . LEU C 391 ? 1.3824 1.7202 1.7878 0.1502  -0.2999 -0.0129 391 LEU C C   
8774  O O   . LEU C 391 ? 1.3780 1.7145 1.7761 0.1490  -0.3057 -0.0118 391 LEU C O   
8775  C CB  . LEU C 391 ? 1.2360 1.5995 1.6613 0.1428  -0.2747 -0.0175 391 LEU C CB  
8776  C CG  . LEU C 391 ? 1.1501 1.5123 1.5747 0.1407  -0.2634 -0.0172 391 LEU C CG  
8777  C CD1 . LEU C 391 ? 1.1536 1.5066 1.5561 0.1334  -0.2524 -0.0111 391 LEU C CD1 
8778  C CD2 . LEU C 391 ? 1.0988 1.4865 1.5509 0.1405  -0.2562 -0.0248 391 LEU C CD2 
8779  N N   . GLN C 392 ? 1.5950 1.9334 2.0154 0.1573  -0.3075 -0.0163 392 GLN C N   
8780  C CA  . GLN C 392 ? 1.6580 1.9950 2.0865 0.1643  -0.3238 -0.0184 392 GLN C CA  
8781  C C   . GLN C 392 ? 1.5976 1.9609 2.0527 0.1640  -0.3253 -0.0257 392 GLN C C   
8782  O O   . GLN C 392 ? 1.5159 1.8999 1.9887 0.1603  -0.3142 -0.0302 392 GLN C O   
8783  C CB  . GLN C 392 ? 1.7272 2.0570 2.1648 0.1723  -0.3311 -0.0200 392 GLN C CB  
8784  C CG  . GLN C 392 ? 1.6770 2.0290 2.1451 0.1743  -0.3251 -0.0280 392 GLN C CG  
8785  C CD  . GLN C 392 ? 1.6367 1.9905 2.1020 0.1692  -0.3095 -0.0275 392 GLN C CD  
8786  O OE1 . GLN C 392 ? 1.6960 2.0350 2.1375 0.1641  -0.3028 -0.0210 392 GLN C OE1 
8787  N NE2 . GLN C 392 ? 1.5739 1.9463 2.0637 0.1707  -0.3037 -0.0346 392 GLN C NE2 
8788  N N   . ASN C 393 ? 1.5355 1.8976 1.9930 0.1678  -0.3393 -0.0267 393 ASN C N   
8789  C CA  . ASN C 393 ? 1.4273 1.8128 1.9105 0.1680  -0.3431 -0.0335 393 ASN C CA  
8790  C C   . ASN C 393 ? 1.3547 1.7553 1.8399 0.1592  -0.3306 -0.0343 393 ASN C C   
8791  O O   . ASN C 393 ? 1.3093 1.7327 1.8175 0.1569  -0.3221 -0.0396 393 ASN C O   
8792  C CB  . ASN C 393 ? 1.4100 1.8133 1.9247 0.1737  -0.3443 -0.0410 393 ASN C CB  
8793  C CG  . ASN C 393 ? 1.4492 1.8363 1.9612 0.1821  -0.3541 -0.0398 393 ASN C CG  
8794  O OD1 . ASN C 393 ? 1.5416 1.9087 2.0362 0.1859  -0.3665 -0.0353 393 ASN C OD1 
8795  N ND2 . ASN C 393 ? 1.4774 1.8725 2.0062 0.1852  -0.3487 -0.0440 393 ASN C ND2 
8796  N N   . LYS C 394 ? 1.3824 1.7693 1.8424 0.1545  -0.3296 -0.0288 394 LYS C N   
8797  C CA  . LYS C 394 ? 1.3757 1.7726 1.8331 0.1461  -0.3177 -0.0283 394 LYS C CA  
8798  C C   . LYS C 394 ? 1.4586 1.8491 1.9032 0.1439  -0.3253 -0.0266 394 LYS C C   
8799  O O   . LYS C 394 ? 1.5488 1.9183 1.9717 0.1467  -0.3352 -0.0224 394 LYS C O   
8800  C CB  . LYS C 394 ? 1.3422 1.7285 1.7795 0.1412  -0.3041 -0.0229 394 LYS C CB  
8801  C CG  . LYS C 394 ? 1.3221 1.7242 1.7647 0.1335  -0.2897 -0.0238 394 LYS C CG  
8802  C CD  . LYS C 394 ? 1.2293 1.6565 1.7016 0.1335  -0.2829 -0.0301 394 LYS C CD  
8803  C CE  . LYS C 394 ? 1.1961 1.6386 1.6731 0.1259  -0.2693 -0.0305 394 LYS C CE  
8804  N NZ  . LYS C 394 ? 1.1761 1.6418 1.6792 0.1257  -0.2614 -0.0361 394 LYS C NZ  
8805  N N   . THR C 395 ? 1.4358 1.8439 1.8934 0.1388  -0.3207 -0.0298 395 THR C N   
8806  C CA  . THR C 395 ? 1.5528 1.9571 2.0010 0.1359  -0.3269 -0.0292 395 THR C CA  
8807  C C   . THR C 395 ? 1.5819 1.9844 2.0148 0.1279  -0.3138 -0.0257 395 THR C C   
8808  O O   . THR C 395 ? 1.5361 1.9529 1.9800 0.1237  -0.3005 -0.0268 395 THR C O   
8809  C CB  . THR C 395 ? 1.5619 1.9876 2.0385 0.1363  -0.3334 -0.0360 395 THR C CB  
8810  O OG1 . THR C 395 ? 1.5572 1.9812 2.0255 0.1316  -0.3361 -0.0356 395 THR C OG1 
8811  C CG2 . THR C 395 ? 1.5681 2.0191 2.0718 0.1335  -0.3214 -0.0404 395 THR C CG2 
8812  N N   . LEU C 396 ? 1.7184 2.1029 2.1255 0.1261  -0.3176 -0.0217 396 LEU C N   
8813  C CA  . LEU C 396 ? 1.7029 2.0826 2.0926 0.1192  -0.3060 -0.0181 396 LEU C CA  
8814  C C   . LEU C 396 ? 1.6967 2.0763 2.0823 0.1162  -0.3117 -0.0195 396 LEU C C   
8815  O O   . LEU C 396 ? 1.7218 2.0848 2.0893 0.1186  -0.3229 -0.0179 396 LEU C O   
8816  C CB  . LEU C 396 ? 1.7513 2.1071 2.1103 0.1195  -0.3027 -0.0113 396 LEU C CB  
8817  C CG  . LEU C 396 ? 1.8234 2.1778 2.1840 0.1212  -0.2950 -0.0094 396 LEU C CG  
8818  C CD1 . LEU C 396 ? 1.8624 2.1923 2.1919 0.1208  -0.2920 -0.0024 396 LEU C CD1 
8819  C CD2 . LEU C 396 ? 1.7198 2.0940 2.0978 0.1164  -0.2802 -0.0115 396 LEU C CD2 
8820  N N   . ASN C 397 ? 1.4364 1.8341 1.8384 0.1109  -0.3043 -0.0224 397 ASN C N   
8821  C CA  . ASN C 397 ? 1.3628 1.7607 1.7610 0.1068  -0.3073 -0.0237 397 ASN C CA  
8822  C C   . ASN C 397 ? 1.3453 1.7347 1.7231 0.1009  -0.2957 -0.0197 397 ASN C C   
8823  O O   . ASN C 397 ? 1.3389 1.7218 1.7059 0.0982  -0.2990 -0.0199 397 ASN C O   
8824  C CB  . ASN C 397 ? 1.3606 1.7832 1.7903 0.1044  -0.3070 -0.0295 397 ASN C CB  
8825  C CG  . ASN C 397 ? 1.3999 1.8405 1.8464 0.1007  -0.2919 -0.0299 397 ASN C CG  
8826  O OD1 . ASN C 397 ? 1.4401 1.8791 1.8838 0.1024  -0.2849 -0.0277 397 ASN C OD1 
8827  N ND2 . ASN C 397 ? 1.3971 1.8547 1.8609 0.0956  -0.2868 -0.0325 397 ASN C ND2 
8828  N N   . VAL C 398 ? 1.3596 1.7489 1.7324 0.0990  -0.2825 -0.0163 398 VAL C N   
8829  C CA  . VAL C 398 ? 1.2158 1.5992 1.5721 0.0936  -0.2704 -0.0126 398 VAL C CA  
8830  C C   . VAL C 398 ? 1.1614 1.5253 1.4922 0.0951  -0.2665 -0.0071 398 VAL C C   
8831  O O   . VAL C 398 ? 1.2203 1.5809 1.5525 0.0991  -0.2682 -0.0061 398 VAL C O   
8832  C CB  . VAL C 398 ? 1.1714 1.5753 1.5472 0.0889  -0.2568 -0.0138 398 VAL C CB  
8833  C CG1 . VAL C 398 ? 1.1256 1.5371 1.5120 0.0911  -0.2507 -0.0135 398 VAL C CG1 
8834  C CG2 . VAL C 398 ? 1.1212 1.5202 1.4820 0.0833  -0.2456 -0.0105 398 VAL C CG2 
8835  N N   . SER C 399 ? 1.1458 1.4964 1.4535 0.0917  -0.2610 -0.0036 399 SER C N   
8836  C CA  . SER C 399 ? 1.1646 1.4967 1.4473 0.0923  -0.2561 0.0020  399 SER C CA  
8837  C C   . SER C 399 ? 1.1396 1.4801 1.4297 0.0901  -0.2424 0.0038  399 SER C C   
8838  O O   . SER C 399 ? 1.0897 1.4462 1.3941 0.0861  -0.2329 0.0023  399 SER C O   
8839  C CB  . SER C 399 ? 1.1754 1.4925 1.4326 0.0892  -0.2534 0.0046  399 SER C CB  
8840  O OG  . SER C 399 ? 1.2240 1.5319 1.4723 0.0913  -0.2667 0.0028  399 SER C OG  
8841  N N   . VAL C 400 ? 1.1485 1.4779 1.4286 0.0928  -0.2415 0.0071  400 VAL C N   
8842  C CA  . VAL C 400 ? 1.1209 1.4559 1.4060 0.0911  -0.2295 0.0088  400 VAL C CA  
8843  C C   . VAL C 400 ? 1.1868 1.5028 1.4450 0.0894  -0.2228 0.0147  400 VAL C C   
8844  O O   . VAL C 400 ? 1.2027 1.4997 1.4385 0.0909  -0.2290 0.0176  400 VAL C O   
8845  C CB  . VAL C 400 ? 1.1202 1.4612 1.4216 0.0956  -0.2336 0.0068  400 VAL C CB  
8846  C CG1 . VAL C 400 ? 1.0868 1.4483 1.4162 0.0971  -0.2390 0.0008  400 VAL C CG1 
8847  C CG2 . VAL C 400 ? 1.1881 1.5089 1.4734 0.1008  -0.2443 0.0096  400 VAL C CG2 
8848  N N   . GLN C 401 ? 1.3293 1.6507 1.5899 0.0861  -0.2100 0.0164  401 GLN C N   
8849  C CA  . GLN C 401 ? 1.3766 1.6825 1.6143 0.0837  -0.2018 0.0217  401 GLN C CA  
8850  C C   . GLN C 401 ? 1.3534 1.6670 1.5998 0.0816  -0.1906 0.0226  401 GLN C C   
8851  O O   . GLN C 401 ? 1.3300 1.6619 1.5939 0.0789  -0.1833 0.0200  401 GLN C O   
8852  C CB  . GLN C 401 ? 1.4359 1.7391 1.6609 0.0795  -0.1961 0.0228  401 GLN C CB  
8853  C CG  . GLN C 401 ? 1.4954 1.7850 1.6988 0.0766  -0.1861 0.0280  401 GLN C CG  
8854  C CD  . GLN C 401 ? 1.5363 1.8249 1.7296 0.0728  -0.1798 0.0284  401 GLN C CD  
8855  O OE1 . GLN C 401 ? 1.5670 1.8613 1.7657 0.0725  -0.1846 0.0252  401 GLN C OE1 
8856  N NE2 . GLN C 401 ? 1.5314 1.8128 1.7107 0.0697  -0.1690 0.0321  401 GLN C NE2 
8857  N N   . ASP C 402 ? 1.3572 1.6565 1.5911 0.0828  -0.1895 0.0264  402 ASP C N   
8858  C CA  . ASP C 402 ? 1.3678 1.6709 1.6063 0.0806  -0.1790 0.0277  402 ASP C CA  
8859  C C   . ASP C 402 ? 1.3438 1.6679 1.6099 0.0815  -0.1778 0.0227  402 ASP C C   
8860  O O   . ASP C 402 ? 1.3674 1.7060 1.6446 0.0780  -0.1680 0.0214  402 ASP C O   
8861  C CB  . ASP C 402 ? 1.4476 1.7514 1.6768 0.0751  -0.1662 0.0303  402 ASP C CB  
8862  C CG  . ASP C 402 ? 1.5198 1.8033 1.7214 0.0741  -0.1661 0.0350  402 ASP C CG  
8863  O OD1 . ASP C 402 ? 1.5290 1.7947 1.7154 0.0770  -0.1730 0.0379  402 ASP C OD1 
8864  O OD2 . ASP C 402 ? 1.5370 1.8219 1.7317 0.0705  -0.1589 0.0358  402 ASP C OD2 
8865  N N   . ASP C 403 ? 1.2553 1.5808 1.5322 0.0865  -0.1881 0.0198  403 ASP C N   
8866  C CA  . ASP C 403 ? 1.1856 1.5306 1.4885 0.0880  -0.1878 0.0145  403 ASP C CA  
8867  C C   . ASP C 403 ? 1.1240 1.4623 1.4318 0.0937  -0.1970 0.0133  403 ASP C C   
8868  O O   . ASP C 403 ? 1.1706 1.4892 1.4615 0.0965  -0.2039 0.0169  403 ASP C O   
8869  C CB  . ASP C 403 ? 1.2103 1.5729 1.5296 0.0875  -0.1906 0.0102  403 ASP C CB  
8870  C CG  . ASP C 403 ? 1.2412 1.6269 1.5855 0.0866  -0.1847 0.0055  403 ASP C CG  
8871  O OD1 . ASP C 403 ? 1.2002 1.5884 1.5522 0.0883  -0.1826 0.0041  403 ASP C OD1 
8872  O OD2 . ASP C 403 ? 1.3021 1.7030 1.6578 0.0841  -0.1822 0.0032  403 ASP C OD2 
8873  N N   . ILE C 404 ? 1.0749 1.4297 1.4058 0.0957  -0.1968 0.0082  404 ILE C N   
8874  C CA  . ILE C 404 ? 1.0570 1.4086 1.3970 0.1016  -0.2053 0.0058  404 ILE C CA  
8875  C C   . ILE C 404 ? 1.0371 1.4082 1.4013 0.1044  -0.2111 -0.0006 404 ILE C C   
8876  O O   . ILE C 404 ? 1.0174 1.4083 1.4006 0.1028  -0.2044 -0.0048 404 ILE C O   
8877  C CB  . ILE C 404 ? 1.0522 1.4042 1.3973 0.1015  -0.1985 0.0053  404 ILE C CB  
8878  C CG1 . ILE C 404 ? 1.1225 1.4564 1.4447 0.0978  -0.1917 0.0117  404 ILE C CG1 
8879  C CG2 . ILE C 404 ? 1.0007 1.3486 1.3556 0.1081  -0.2079 0.0025  404 ILE C CG2 
8880  C CD1 . ILE C 404 ? 1.1312 1.4646 1.4577 0.0970  -0.1848 0.0113  404 ILE C CD1 
8881  N N   . ILE C 405 ? 1.0509 1.4168 1.4146 0.1085  -0.2234 -0.0013 405 ILE C N   
8882  C CA  . ILE C 405 ? 1.0522 1.4361 1.4382 0.1106  -0.2294 -0.0071 405 ILE C CA  
8883  C C   . ILE C 405 ? 1.0884 1.4770 1.4920 0.1170  -0.2360 -0.0115 405 ILE C C   
8884  O O   . ILE C 405 ? 1.0887 1.4610 1.4840 0.1220  -0.2454 -0.0097 405 ILE C O   
8885  C CB  . ILE C 405 ? 1.0286 1.4059 1.4064 0.1115  -0.2396 -0.0061 405 ILE C CB  
8886  C CG1 . ILE C 405 ? 0.9894 1.3671 1.3553 0.1051  -0.2323 -0.0035 405 ILE C CG1 
8887  C CG2 . ILE C 405 ? 1.0879 1.4818 1.4900 0.1149  -0.2481 -0.0123 405 ILE C CG2 
8888  C CD1 . ILE C 405 ? 1.0787 1.4343 1.4152 0.1030  -0.2293 0.0031  405 ILE C CD1 
8889  N N   . LEU C 406 ? 1.2128 1.6233 1.6405 0.1168  -0.2311 -0.0173 406 LEU C N   
8890  C CA  . LEU C 406 ? 1.2140 1.6317 1.6612 0.1229  -0.2366 -0.0226 406 LEU C CA  
8891  C C   . LEU C 406 ? 1.2037 1.6316 1.6674 0.1268  -0.2476 -0.0269 406 LEU C C   
8892  O O   . LEU C 406 ? 1.1585 1.6021 1.6328 0.1235  -0.2453 -0.0291 406 LEU C O   
8893  C CB  . LEU C 406 ? 1.2041 1.6406 1.6689 0.1211  -0.2256 -0.0271 406 LEU C CB  
8894  C CG  . LEU C 406 ? 1.2041 1.6331 1.6557 0.1172  -0.2146 -0.0237 406 LEU C CG  
8895  C CD1 . LEU C 406 ? 1.1506 1.5997 1.6203 0.1156  -0.2046 -0.0289 406 LEU C CD1 
8896  C CD2 . LEU C 406 ? 1.2249 1.6314 1.6625 0.1210  -0.2198 -0.0205 406 LEU C CD2 
8897  O OXT . LEU C 406 ? 1.2583 1.6791 1.7259 0.1332  -0.2590 -0.0283 406 LEU C OXT 
8898  N N   . MET D 1   ? 0.8827 1.9187 2.1118 0.1472  -0.1892 -0.1964 1   MET D N   
8899  C CA  . MET D 1   ? 0.9669 1.9924 2.1767 0.1395  -0.1907 -0.1885 1   MET D CA  
8900  C C   . MET D 1   ? 0.9595 1.9609 2.1478 0.1456  -0.2035 -0.1866 1   MET D C   
8901  O O   . MET D 1   ? 0.9114 1.9052 2.0938 0.1536  -0.2042 -0.1901 1   MET D O   
8902  C CB  . MET D 1   ? 0.9210 1.9560 2.1227 0.1312  -0.1725 -0.1848 1   MET D CB  
8903  C CG  . MET D 1   ? 1.0014 2.0289 2.1867 0.1221  -0.1723 -0.1766 1   MET D CG  
8904  S SD  . MET D 1   ? 1.1860 2.2274 2.3657 0.1118  -0.1506 -0.1722 1   MET D SD  
8905  C CE  . MET D 1   ? 1.2350 2.3021 2.4438 0.1070  -0.1413 -0.1750 1   MET D CE  
8906  N N   . LYS D 2   ? 1.0027 1.9919 2.1794 0.1416  -0.2136 -0.1811 2   LYS D N   
8907  C CA  . LYS D 2   ? 1.0324 1.9984 2.1889 0.1468  -0.2271 -0.1786 2   LYS D CA  
8908  C C   . LYS D 2   ? 1.1661 2.1236 2.3001 0.1402  -0.2214 -0.1720 2   LYS D C   
8909  O O   . LYS D 2   ? 1.2182 2.1874 2.3525 0.1313  -0.2080 -0.1690 2   LYS D O   
8910  C CB  . LYS D 2   ? 1.0059 1.9626 2.1656 0.1486  -0.2452 -0.1780 2   LYS D CB  
8911  C CG  . LYS D 2   ? 1.0199 1.9832 2.2011 0.1560  -0.2529 -0.1845 2   LYS D CG  
8912  C CD  . LYS D 2   ? 0.9665 1.9182 2.1437 0.1678  -0.2592 -0.1886 2   LYS D CD  
8913  C CE  . LYS D 2   ? 0.9482 1.9046 2.1462 0.1756  -0.2688 -0.1948 2   LYS D CE  
8914  N NZ  . LYS D 2   ? 0.8437 1.7859 2.0366 0.1874  -0.2774 -0.1982 2   LYS D NZ  
8915  N N   . ALA D 3   ? 1.2504 2.1873 2.3650 0.1446  -0.2319 -0.1696 3   ALA D N   
8916  C CA  . ALA D 3   ? 1.4031 2.3299 2.4955 0.1395  -0.2283 -0.1635 3   ALA D CA  
8917  C C   . ALA D 3   ? 1.3994 2.3029 2.4741 0.1451  -0.2446 -0.1612 3   ALA D C   
8918  O O   . ALA D 3   ? 1.2762 2.1707 2.3534 0.1544  -0.2557 -0.1647 3   ALA D O   
8919  C CB  . ALA D 3   ? 1.2412 2.1728 2.3264 0.1393  -0.2132 -0.1642 3   ALA D CB  
8920  N N   . LEU D 4   ? 1.7005 2.5941 2.7575 0.1395  -0.2459 -0.1552 4   LEU D N   
8921  C CA  . LEU D 4   ? 1.6944 2.5657 2.7323 0.1437  -0.2603 -0.1522 4   LEU D CA  
8922  C C   . LEU D 4   ? 1.7213 2.5854 2.7386 0.1394  -0.2531 -0.1473 4   LEU D C   
8923  O O   . LEU D 4   ? 1.8070 2.6810 2.8237 0.1305  -0.2417 -0.1443 4   LEU D O   
8924  C CB  . LEU D 4   ? 1.6998 2.5648 2.7382 0.1413  -0.2741 -0.1501 4   LEU D CB  
8925  C CG  . LEU D 4   ? 1.6984 2.5403 2.7155 0.1442  -0.2889 -0.1461 4   LEU D CG  
8926  C CD1 . LEU D 4   ? 1.7054 2.5330 2.7179 0.1557  -0.3008 -0.1485 4   LEU D CD1 
8927  C CD2 . LEU D 4   ? 1.7505 2.5893 2.7688 0.1399  -0.2998 -0.1442 4   LEU D CD2 
8928  N N   . ILE D 5   ? 1.5023 2.3493 2.5033 0.1457  -0.2598 -0.1464 5   ILE D N   
8929  C CA  . ILE D 5   ? 1.4896 2.3289 2.4710 0.1428  -0.2540 -0.1422 5   ILE D CA  
8930  C C   . ILE D 5   ? 1.4398 2.2577 2.4029 0.1451  -0.2691 -0.1380 5   ILE D C   
8931  O O   . ILE D 5   ? 1.3625 2.1667 2.3222 0.1535  -0.2824 -0.1393 5   ILE D O   
8932  C CB  . ILE D 5   ? 1.4301 2.2696 2.4083 0.1479  -0.2459 -0.1451 5   ILE D CB  
8933  C CG1 . ILE D 5   ? 1.3670 2.2278 2.3617 0.1453  -0.2301 -0.1492 5   ILE D CG1 
8934  C CG2 . ILE D 5   ? 1.4693 2.2997 2.4268 0.1453  -0.2414 -0.1408 5   ILE D CG2 
8935  C CD1 . ILE D 5   ? 1.2220 2.0841 2.2141 0.1500  -0.2216 -0.1529 5   ILE D CD1 
8936  N N   . LEU D 6   ? 1.4648 2.2796 2.4160 0.1378  -0.2672 -0.1330 6   LEU D N   
8937  C CA  . LEU D 6   ? 1.4561 2.2509 2.3882 0.1392  -0.2802 -0.1288 6   LEU D CA  
8938  C C   . LEU D 6   ? 1.4931 2.2690 2.3971 0.1407  -0.2741 -0.1243 6   LEU D C   
8939  O O   . LEU D 6   ? 1.4807 2.2596 2.3746 0.1347  -0.2597 -0.1213 6   LEU D O   
8940  C CB  . LEU D 6   ? 1.5028 2.2969 2.4273 0.1295  -0.2782 -0.1239 6   LEU D CB  
8941  C CG  . LEU D 6   ? 1.5328 2.3381 2.4762 0.1259  -0.2835 -0.1261 6   LEU D CG  
8942  C CD1 . LEU D 6   ? 1.5860 2.3933 2.5248 0.1163  -0.2803 -0.1221 6   LEU D CD1 
8943  C CD2 . LEU D 6   ? 1.4846 2.2768 2.4273 0.1329  -0.3022 -0.1276 6   LEU D CD2 
8944  N N   . VAL D 7   ? 1.5448 2.3009 2.4357 0.1485  -0.2851 -0.1235 7   VAL D N   
8945  C CA  . VAL D 7   ? 1.5157 2.2519 2.3796 0.1501  -0.2806 -0.1191 7   VAL D CA  
8946  C C   . VAL D 7   ? 1.5261 2.2372 2.3586 0.1467  -0.2861 -0.1108 7   VAL D C   
8947  O O   . VAL D 7   ? 1.5174 2.2201 2.3286 0.1408  -0.2760 -0.1053 7   VAL D O   
8948  C CB  . VAL D 7   ? 1.4368 2.1658 2.3051 0.1606  -0.2881 -0.1230 7   VAL D CB  
8949  C CG1 . VAL D 7   ? 1.4134 2.1217 2.2541 0.1615  -0.2830 -0.1182 7   VAL D CG1 
8950  C CG2 . VAL D 7   ? 1.3874 2.1421 2.2878 0.1643  -0.2824 -0.1318 7   VAL D CG2 
8951  N N   . GLY D 8   ? 1.4017 2.1007 2.2308 0.1504  -0.3020 -0.1101 8   GLY D N   
8952  C CA  . GLY D 8   ? 1.3649 2.0391 2.1636 0.1481  -0.3084 -0.1028 8   GLY D CA  
8953  C C   . GLY D 8   ? 1.3623 2.0122 2.1413 0.1556  -0.3176 -0.1001 8   GLY D C   
8954  O O   . GLY D 8   ? 1.3291 1.9782 2.1202 0.1638  -0.3293 -0.1039 8   GLY D O   
8955  N N   . GLY D 9   ? 1.4096 2.0395 2.1585 0.1529  -0.3124 -0.0934 9   GLY D N   
8956  C CA  . GLY D 9   ? 1.4157 2.0210 2.1431 0.1588  -0.3194 -0.0897 9   GLY D CA  
8957  C C   . GLY D 9   ? 1.3582 1.9638 2.0866 0.1620  -0.3104 -0.0912 9   GLY D C   
8958  O O   . GLY D 9   ? 1.2962 1.9228 2.0486 0.1630  -0.3033 -0.0973 9   GLY D O   
8959  N N   . PHE D 10  ? 1.2002 1.7823 1.9021 0.1633  -0.3106 -0.0856 10  PHE D N   
8960  C CA  . PHE D 10  ? 1.0643 1.6425 1.7642 0.1665  -0.3037 -0.0865 10  PHE D CA  
8961  C C   . PHE D 10  ? 1.0507 1.6356 1.7436 0.1592  -0.2862 -0.0849 10  PHE D C   
8962  O O   . PHE D 10  ? 1.0386 1.6264 1.7353 0.1610  -0.2786 -0.0873 10  PHE D O   
8963  C CB  . PHE D 10  ? 1.0758 1.6249 1.7508 0.1713  -0.3122 -0.0811 10  PHE D CB  
8964  C CG  . PHE D 10  ? 1.0344 1.5797 1.7179 0.1793  -0.3147 -0.0846 10  PHE D CG  
8965  C CD1 . PHE D 10  ? 1.0588 1.6079 1.7616 0.1878  -0.3275 -0.0896 10  PHE D CD1 
8966  C CD2 . PHE D 10  ? 1.0014 1.5393 1.6742 0.1783  -0.3047 -0.0832 10  PHE D CD2 
8967  C CE1 . PHE D 10  ? 1.0593 1.6044 1.7703 0.1955  -0.3300 -0.0930 10  PHE D CE1 
8968  C CE2 . PHE D 10  ? 1.0688 1.6025 1.7496 0.1856  -0.3071 -0.0867 10  PHE D CE2 
8969  C CZ  . PHE D 10  ? 1.0394 1.5764 1.7392 0.1943  -0.3197 -0.0916 10  PHE D CZ  
8970  N N   . GLY D 11  ? 1.1208 1.7080 1.8039 0.1511  -0.2800 -0.0810 11  GLY D N   
8971  C CA  . GLY D 11  ? 1.1168 1.7081 1.7906 0.1441  -0.2644 -0.0785 11  GLY D CA  
8972  C C   . GLY D 11  ? 1.1198 1.6866 1.7615 0.1415  -0.2626 -0.0707 11  GLY D C   
8973  O O   . GLY D 11  ? 1.0395 1.6008 1.6718 0.1409  -0.2542 -0.0694 11  GLY D O   
8974  N N   . THR D 12  ? 1.1868 1.7388 1.8116 0.1399  -0.2703 -0.0658 12  THR D N   
8975  C CA  . THR D 12  ? 1.1451 1.6729 1.7389 0.1378  -0.2693 -0.0584 12  THR D CA  
8976  C C   . THR D 12  ? 1.1299 1.6612 1.7135 0.1302  -0.2540 -0.0552 12  THR D C   
8977  O O   . THR D 12  ? 1.1078 1.6244 1.6721 0.1292  -0.2489 -0.0510 12  THR D O   
8978  C CB  . THR D 12  ? 1.1942 1.7076 1.7729 0.1374  -0.2803 -0.0545 12  THR D CB  
8979  O OG1 . THR D 12  ? 1.2996 1.8272 1.8867 0.1315  -0.2774 -0.0555 12  THR D OG1 
8980  C CG2 . THR D 12  ? 1.1674 1.6756 1.7544 0.1454  -0.2965 -0.0572 12  THR D CG2 
8981  N N   . ARG D 13  ? 1.3450 1.8956 1.9415 0.1248  -0.2466 -0.0571 13  ARG D N   
8982  C CA  . ARG D 13  ? 1.3590 1.9142 1.9470 0.1177  -0.2326 -0.0540 13  ARG D CA  
8983  C C   . ARG D 13  ? 1.3206 1.8885 1.9190 0.1177  -0.2216 -0.0572 13  ARG D C   
8984  O O   . ARG D 13  ? 1.3095 1.8843 1.9040 0.1119  -0.2098 -0.0554 13  ARG D O   
8985  C CB  . ARG D 13  ? 1.4187 1.9882 2.0156 0.1118  -0.2297 -0.0542 13  ARG D CB  
8986  C CG  . ARG D 13  ? 1.4026 1.9906 2.0268 0.1141  -0.2357 -0.0604 13  ARG D CG  
8987  C CD  . ARG D 13  ? 1.5086 2.1027 2.1363 0.1089  -0.2374 -0.0594 13  ARG D CD  
8988  N NE  . ARG D 13  ? 1.6354 2.2083 2.2410 0.1085  -0.2460 -0.0548 13  ARG D NE  
8989  C CZ  . ARG D 13  ? 1.7049 2.2691 2.2924 0.1027  -0.2409 -0.0497 13  ARG D CZ  
8990  N NH1 . ARG D 13  ? 1.7028 2.2777 2.2919 0.0968  -0.2277 -0.0483 13  ARG D NH1 
8991  N NH2 . ARG D 13  ? 1.7552 2.3001 2.3227 0.1030  -0.2491 -0.0462 13  ARG D NH2 
8992  N N   . LEU D 14  ? 1.0863 1.6571 1.6974 0.1241  -0.2254 -0.0621 14  LEU D N   
8993  C CA  . LEU D 14  ? 0.9952 1.5771 1.6158 0.1247  -0.2158 -0.0660 14  LEU D CA  
8994  C C   . LEU D 14  ? 0.9053 1.4692 1.5131 0.1289  -0.2174 -0.0648 14  LEU D C   
8995  O O   . LEU D 14  ? 0.8347 1.4061 1.4518 0.1310  -0.2119 -0.0692 14  LEU D O   
8996  C CB  . LEU D 14  ? 0.9865 1.5909 1.6367 0.1283  -0.2166 -0.0740 14  LEU D CB  
8997  C CG  . LEU D 14  ? 1.0014 1.6286 1.6686 0.1234  -0.2113 -0.0762 14  LEU D CG  
8998  C CD1 . LEU D 14  ? 1.0671 1.6920 1.7365 0.1229  -0.2215 -0.0747 14  LEU D CD1 
8999  C CD2 . LEU D 14  ? 1.0199 1.6700 1.7140 0.1264  -0.2073 -0.0842 14  LEU D CD2 
9000  N N   . ARG D 15  ? 0.8905 1.4307 1.4770 0.1300  -0.2247 -0.0592 15  ARG D N   
9001  C CA  . ARG D 15  ? 0.8418 1.3631 1.4145 0.1333  -0.2260 -0.0571 15  ARG D CA  
9002  C C   . ARG D 15  ? 0.7945 1.3164 1.3577 0.1282  -0.2127 -0.0553 15  ARG D C   
9003  O O   . ARG D 15  ? 0.8099 1.3403 1.3695 0.1217  -0.2039 -0.0531 15  ARG D O   
9004  C CB  . ARG D 15  ? 0.8758 1.3719 1.4255 0.1344  -0.2355 -0.0505 15  ARG D CB  
9005  C CG  . ARG D 15  ? 0.9525 1.4451 1.5097 0.1405  -0.2504 -0.0522 15  ARG D CG  
9006  C CD  . ARG D 15  ? 0.9778 1.4432 1.5100 0.1423  -0.2598 -0.0456 15  ARG D CD  
9007  N NE  . ARG D 15  ? 1.0447 1.5059 1.5838 0.1489  -0.2751 -0.0473 15  ARG D NE  
9008  C CZ  . ARG D 15  ? 1.0485 1.5095 1.5856 0.1482  -0.2830 -0.0463 15  ARG D CZ  
9009  N NH1 . ARG D 15  ? 1.0715 1.5360 1.6000 0.1412  -0.2769 -0.0435 15  ARG D NH1 
9010  N NH2 . ARG D 15  ? 1.0670 1.5243 1.6111 0.1547  -0.2974 -0.0481 15  ARG D NH2 
9011  N N   . PRO D 16  ? 0.7897 1.3023 1.3491 0.1309  -0.2111 -0.0561 16  PRO D N   
9012  C CA  . PRO D 16  ? 0.7960 1.2960 1.3578 0.1385  -0.2206 -0.0581 16  PRO D CA  
9013  C C   . PRO D 16  ? 0.7849 1.3024 1.3734 0.1441  -0.2221 -0.0669 16  PRO D C   
9014  O O   . PRO D 16  ? 0.7977 1.3063 1.3905 0.1506  -0.2287 -0.0695 16  PRO D O   
9015  C CB  . PRO D 16  ? 0.7800 1.2641 1.3253 0.1369  -0.2149 -0.0548 16  PRO D CB  
9016  C CG  . PRO D 16  ? 0.7402 1.2400 1.2882 0.1306  -0.2011 -0.0561 16  PRO D CG  
9017  C CD  . PRO D 16  ? 0.7780 1.2909 1.3285 0.1260  -0.1989 -0.0546 16  PRO D CD  
9018  N N   . LEU D 17  ? 0.7787 1.3207 1.3851 0.1416  -0.2157 -0.0716 17  LEU D N   
9019  C CA  . LEU D 17  ? 0.8108 1.3712 1.4431 0.1465  -0.2158 -0.0804 17  LEU D CA  
9020  C C   . LEU D 17  ? 0.8730 1.4338 1.5189 0.1532  -0.2292 -0.0831 17  LEU D C   
9021  O O   . LEU D 17  ? 0.8787 1.4461 1.5427 0.1598  -0.2330 -0.0898 17  LEU D O   
9022  C CB  . LEU D 17  ? 0.7722 1.3586 1.4186 0.1415  -0.2046 -0.0840 17  LEU D CB  
9023  C CG  . LEU D 17  ? 0.7461 1.3351 1.3815 0.1351  -0.1914 -0.0820 17  LEU D CG  
9024  C CD1 . LEU D 17  ? 0.7931 1.4077 1.4426 0.1305  -0.1814 -0.0852 17  LEU D CD1 
9025  C CD2 . LEU D 17  ? 0.8250 1.4075 1.4593 0.1384  -0.1886 -0.0854 17  LEU D CD2 
9026  N N   . THR D 18  ? 0.8814 1.4354 1.5192 0.1518  -0.2366 -0.0784 18  THR D N   
9027  C CA  . THR D 18  ? 0.8738 1.4276 1.5233 0.1578  -0.2503 -0.0806 18  THR D CA  
9028  C C   . THR D 18  ? 1.0249 1.5515 1.6563 0.1626  -0.2625 -0.0756 18  THR D C   
9029  O O   . THR D 18  ? 1.1239 1.6466 1.7595 0.1669  -0.2751 -0.0756 18  THR D O   
9030  C CB  . THR D 18  ? 0.8726 1.4381 1.5273 0.1534  -0.2518 -0.0796 18  THR D CB  
9031  O OG1 . THR D 18  ? 0.9188 1.4715 1.5490 0.1467  -0.2483 -0.0719 18  THR D OG1 
9032  C CG2 . THR D 18  ? 0.8452 1.4392 1.5225 0.1501  -0.2416 -0.0854 18  THR D CG2 
9033  N N   . LEU D 19  ? 1.0384 1.5462 1.6498 0.1617  -0.2590 -0.0711 19  LEU D N   
9034  C CA  . LEU D 19  ? 1.1452 1.6265 1.7392 0.1664  -0.2699 -0.0661 19  LEU D CA  
9035  C C   . LEU D 19  ? 1.4066 1.8864 2.0169 0.1758  -0.2792 -0.0715 19  LEU D C   
9036  O O   . LEU D 19  ? 1.4238 1.8861 2.0264 0.1813  -0.2920 -0.0685 19  LEU D O   
9037  C CB  . LEU D 19  ? 1.0184 1.4808 1.5878 0.1623  -0.2627 -0.0600 19  LEU D CB  
9038  C CG  . LEU D 19  ? 0.9625 1.4124 1.5066 0.1556  -0.2604 -0.0517 19  LEU D CG  
9039  C CD1 . LEU D 19  ? 0.9556 1.3886 1.4785 0.1520  -0.2526 -0.0464 19  LEU D CD1 
9040  C CD2 . LEU D 19  ? 1.0592 1.4937 1.5923 0.1591  -0.2745 -0.0476 19  LEU D CD2 
9041  N N   . SER D 20  ? 2.0172 2.5149 2.6495 0.1781  -0.2731 -0.0794 20  SER D N   
9042  C CA  . SER D 20  ? 2.0171 2.5153 2.6673 0.1873  -0.2808 -0.0855 20  SER D CA  
9043  C C   . SER D 20  ? 1.9832 2.5073 2.6637 0.1907  -0.2832 -0.0938 20  SER D C   
9044  O O   . SER D 20  ? 1.9847 2.5075 2.6753 0.1971  -0.2961 -0.0953 20  SER D O   
9045  C CB  . SER D 20  ? 2.0272 2.5233 2.6785 0.1881  -0.2721 -0.0887 20  SER D CB  
9046  O OG  . SER D 20  ? 2.0623 2.5342 2.6868 0.1850  -0.2702 -0.0811 20  SER D OG  
9047  N N   . PHE D 21  ? 1.3820 1.9300 2.0774 0.1865  -0.2710 -0.0991 21  PHE D N   
9048  C CA  . PHE D 21  ? 1.2174 1.7917 1.9418 0.1887  -0.2714 -0.1068 21  PHE D CA  
9049  C C   . PHE D 21  ? 1.0774 1.6610 1.8011 0.1828  -0.2720 -0.1036 21  PHE D C   
9050  O O   . PHE D 21  ? 1.0473 1.6262 1.7525 0.1749  -0.2650 -0.0976 21  PHE D O   
9051  C CB  . PHE D 21  ? 1.1586 1.7544 1.8989 0.1869  -0.2575 -0.1140 21  PHE D CB  
9052  C CG  . PHE D 21  ? 1.2347 1.8250 1.9806 0.1933  -0.2570 -0.1192 21  PHE D CG  
9053  C CD1 . PHE D 21  ? 1.2991 1.8747 2.0485 0.2023  -0.2700 -0.1202 21  PHE D CD1 
9054  C CD2 . PHE D 21  ? 1.1901 1.7892 1.9374 0.1904  -0.2438 -0.1230 21  PHE D CD2 
9055  C CE1 . PHE D 21  ? 1.2432 1.8127 1.9979 0.2082  -0.2697 -0.1251 21  PHE D CE1 
9056  C CE2 . PHE D 21  ? 1.1886 1.7820 1.9411 0.1962  -0.2435 -0.1283 21  PHE D CE2 
9057  C CZ  . PHE D 21  ? 1.2072 1.7856 1.9636 0.2051  -0.2563 -0.1293 21  PHE D CZ  
9058  N N   . PRO D 22  ? 0.9951 1.5918 1.7393 0.1862  -0.2804 -0.1077 22  PRO D N   
9059  C CA  . PRO D 22  ? 0.9211 1.5259 1.6652 0.1804  -0.2816 -0.1049 22  PRO D CA  
9060  C C   . PRO D 22  ? 0.8606 1.4871 1.6121 0.1723  -0.2663 -0.1066 22  PRO D C   
9061  O O   . PRO D 22  ? 0.8254 1.4631 1.5845 0.1717  -0.2552 -0.1107 22  PRO D O   
9062  C CB  . PRO D 22  ? 0.9278 1.5433 1.6961 0.1869  -0.2941 -0.1102 22  PRO D CB  
9063  C CG  . PRO D 22  ? 0.9504 1.5706 1.7370 0.1955  -0.2959 -0.1174 22  PRO D CG  
9064  C CD  . PRO D 22  ? 0.9980 1.6063 1.7694 0.1950  -0.2870 -0.1161 22  PRO D CD  
9065  N N   . LYS D 23  ? 0.8177 1.4494 1.5663 0.1661  -0.2660 -0.1032 23  LYS D N   
9066  C CA  . LYS D 23  ? 0.8064 1.4559 1.5584 0.1576  -0.2520 -0.1031 23  LYS D CA  
9067  C C   . LYS D 23  ? 0.7683 1.4451 1.5481 0.1584  -0.2434 -0.1113 23  LYS D C   
9068  O O   . LYS D 23  ? 0.7915 1.4766 1.5687 0.1541  -0.2299 -0.1118 23  LYS D O   
9069  C CB  . LYS D 23  ? 0.8497 1.5007 1.5982 0.1520  -0.2556 -0.0991 23  LYS D CB  
9070  C CG  . LYS D 23  ? 0.8803 1.5495 1.6337 0.1433  -0.2422 -0.0986 23  LYS D CG  
9071  C CD  . LYS D 23  ? 0.9316 1.5973 1.6770 0.1374  -0.2459 -0.0937 23  LYS D CD  
9072  C CE  . LYS D 23  ? 1.0644 1.7344 1.8263 0.1414  -0.2597 -0.0970 23  LYS D CE  
9073  N NZ  . LYS D 23  ? 1.1696 1.8370 1.9247 0.1354  -0.2632 -0.0930 23  LYS D NZ  
9074  N N   . PRO D 24  ? 0.8021 1.4940 1.6084 0.1637  -0.2499 -0.1181 24  PRO D N   
9075  C CA  . PRO D 24  ? 0.7682 1.4874 1.6007 0.1637  -0.2402 -0.1259 24  PRO D CA  
9076  C C   . PRO D 24  ? 0.7008 1.4217 1.5385 0.1692  -0.2350 -0.1315 24  PRO D C   
9077  O O   . PRO D 24  ? 0.6441 1.3871 1.5008 0.1688  -0.2254 -0.1380 24  PRO D O   
9078  C CB  . PRO D 24  ? 0.7855 1.5182 1.6442 0.1679  -0.2505 -0.1310 24  PRO D CB  
9079  C CG  . PRO D 24  ? 0.7868 1.4969 1.6352 0.1745  -0.2668 -0.1284 24  PRO D CG  
9080  C CD  . PRO D 24  ? 0.8234 1.5093 1.6378 0.1696  -0.2664 -0.1189 24  PRO D CD  
9081  N N   . LEU D 25  ? 0.6943 1.3926 1.5159 0.1741  -0.2408 -0.1294 25  LEU D N   
9082  C CA  . LEU D 25  ? 0.6865 1.3844 1.5132 0.1797  -0.2370 -0.1351 25  LEU D CA  
9083  C C   . LEU D 25  ? 0.7006 1.3917 1.5074 0.1745  -0.2248 -0.1321 25  LEU D C   
9084  O O   . LEU D 25  ? 0.7285 1.4163 1.5360 0.1786  -0.2217 -0.1362 25  LEU D O   
9085  C CB  . LEU D 25  ? 0.7661 1.4434 1.5896 0.1889  -0.2512 -0.1352 25  LEU D CB  
9086  C CG  . LEU D 25  ? 0.7827 1.4680 1.6305 0.1968  -0.2638 -0.1406 25  LEU D CG  
9087  C CD1 . LEU D 25  ? 0.8338 1.4986 1.6781 0.2064  -0.2759 -0.1412 25  LEU D CD1 
9088  C CD2 . LEU D 25  ? 0.7890 1.5046 1.6681 0.1983  -0.2563 -0.1504 25  LEU D CD2 
9089  N N   . VAL D 26  ? 0.6782 1.3674 1.4681 0.1657  -0.2180 -0.1253 26  VAL D N   
9090  C CA  . VAL D 26  ? 0.6675 1.3517 1.4394 0.1605  -0.2064 -0.1223 26  VAL D CA  
9091  C C   . VAL D 26  ? 0.6484 1.3578 1.4361 0.1581  -0.1931 -0.1288 26  VAL D C   
9092  O O   . VAL D 26  ? 0.6454 1.3748 1.4469 0.1543  -0.1885 -0.1302 26  VAL D O   
9093  C CB  . VAL D 26  ? 0.7169 1.3900 1.4656 0.1524  -0.2042 -0.1128 26  VAL D CB  
9094  C CG1 . VAL D 26  ? 0.8252 1.4962 1.5580 0.1469  -0.1917 -0.1103 26  VAL D CG1 
9095  C CG2 . VAL D 26  ? 0.7238 1.3709 1.4547 0.1550  -0.2167 -0.1066 26  VAL D CG2 
9096  N N   . ASP D 27  ? 0.6467 1.3549 1.4321 0.1601  -0.1868 -0.1327 27  ASP D N   
9097  C CA  . ASP D 27  ? 0.5566 1.2874 1.3544 0.1580  -0.1739 -0.1391 27  ASP D CA  
9098  C C   . ASP D 27  ? 0.5498 1.2876 1.3352 0.1483  -0.1630 -0.1334 27  ASP D C   
9099  O O   . ASP D 27  ? 0.6125 1.3357 1.3756 0.1442  -0.1600 -0.1274 27  ASP D O   
9100  C CB  . ASP D 27  ? 0.5815 1.3067 1.3768 0.1622  -0.1704 -0.1444 27  ASP D CB  
9101  C CG  . ASP D 27  ? 0.6018 1.3255 1.4145 0.1722  -0.1791 -0.1519 27  ASP D CG  
9102  O OD1 . ASP D 27  ? 0.6243 1.3466 1.4473 0.1763  -0.1898 -0.1517 27  ASP D OD1 
9103  O OD2 . ASP D 27  ? 0.6032 1.3272 1.4197 0.1762  -0.1755 -0.1584 27  ASP D OD2 
9104  N N   . PHE D 28  ? 0.5568 1.3170 1.3572 0.1446  -0.1571 -0.1351 28  PHE D N   
9105  C CA  . PHE D 28  ? 0.5780 1.3479 1.3698 0.1357  -0.1459 -0.1305 28  PHE D CA  
9106  C C   . PHE D 28  ? 0.5735 1.3663 1.3787 0.1351  -0.1339 -0.1376 28  PHE D C   
9107  O O   . PHE D 28  ? 0.6169 1.4289 1.4450 0.1375  -0.1328 -0.1439 28  PHE D O   
9108  C CB  . PHE D 28  ? 0.6616 1.4377 1.4579 0.1309  -0.1483 -0.1258 28  PHE D CB  
9109  C CG  . PHE D 28  ? 0.7065 1.4952 1.4979 0.1222  -0.1365 -0.1217 28  PHE D CG  
9110  C CD1 . PHE D 28  ? 0.7254 1.5387 1.5361 0.1196  -0.1294 -0.1253 28  PHE D CD1 
9111  C CD2 . PHE D 28  ? 0.7479 1.5238 1.5155 0.1167  -0.1323 -0.1143 28  PHE D CD2 
9112  C CE1 . PHE D 28  ? 0.7648 1.5888 1.5703 0.1116  -0.1186 -0.1211 28  PHE D CE1 
9113  C CE2 . PHE D 28  ? 0.8178 1.6046 1.5808 0.1090  -0.1218 -0.1104 28  PHE D CE2 
9114  C CZ  . PHE D 28  ? 0.8008 1.6114 1.5824 0.1065  -0.1151 -0.1136 28  PHE D CZ  
9115  N N   . ALA D 29  ? 0.6020 1.3932 1.3928 0.1317  -0.1247 -0.1365 29  ALA D N   
9116  C CA  . ALA D 29  ? 0.6142 1.4248 1.4141 0.1314  -0.1133 -0.1434 29  ALA D CA  
9117  C C   . ALA D 29  ? 0.5371 1.3540 1.3564 0.1402  -0.1167 -0.1539 29  ALA D C   
9118  O O   . ALA D 29  ? 0.5221 1.3600 1.3629 0.1420  -0.1132 -0.1603 29  ALA D O   
9119  C CB  . ALA D 29  ? 0.6564 1.4896 1.4658 0.1252  -0.1043 -0.1423 29  ALA D CB  
9120  N N   . ASN D 30  ? 0.5392 1.3365 1.3507 0.1457  -0.1239 -0.1552 30  ASN D N   
9121  C CA  . ASN D 30  ? 0.5553 1.3531 1.3818 0.1547  -0.1283 -0.1645 30  ASN D CA  
9122  C C   . ASN D 30  ? 0.5319 1.3299 1.3761 0.1607  -0.1398 -0.1665 30  ASN D C   
9123  O O   . ASN D 30  ? 0.5208 1.3040 1.3669 0.1680  -0.1498 -0.1687 30  ASN D O   
9124  C CB  . ASN D 30  ? 0.5997 1.4204 1.4403 0.1556  -0.1171 -0.1740 30  ASN D CB  
9125  C CG  . ASN D 30  ? 0.6747 1.4921 1.4985 0.1523  -0.1081 -0.1743 30  ASN D CG  
9126  O OD1 . ASN D 30  ? 0.7238 1.5342 1.5470 0.1572  -0.1087 -0.1804 30  ASN D OD1 
9127  N ND2 . ASN D 30  ? 0.6518 1.4736 1.4620 0.1439  -0.1001 -0.1678 30  ASN D ND2 
9128  N N   . LYS D 31  ? 0.5584 1.3728 1.4158 0.1577  -0.1388 -0.1655 31  LYS D N   
9129  C CA  . LYS D 31  ? 0.4887 1.3072 1.3663 0.1633  -0.1492 -0.1684 31  LYS D CA  
9130  C C   . LYS D 31  ? 0.5364 1.3372 1.4021 0.1614  -0.1602 -0.1594 31  LYS D C   
9131  O O   . LYS D 31  ? 0.5438 1.3385 1.3917 0.1538  -0.1570 -0.1512 31  LYS D O   
9132  C CB  . LYS D 31  ? 0.4534 1.3008 1.3545 0.1612  -0.1421 -0.1732 31  LYS D CB  
9133  C CG  . LYS D 31  ? 0.4344 1.3008 1.3516 0.1649  -0.1328 -0.1837 31  LYS D CG  
9134  C CD  . LYS D 31  ? 0.4243 1.3166 1.3531 0.1587  -0.1204 -0.1850 31  LYS D CD  
9135  C CE  . LYS D 31  ? 0.4254 1.3302 1.3577 0.1598  -0.1079 -0.1927 31  LYS D CE  
9136  N NZ  . LYS D 31  ? 0.4180 1.3390 1.3460 0.1510  -0.0932 -0.1899 31  LYS D NZ  
9137  N N   . PRO D 32  ? 0.4846 1.2763 1.3591 0.1684  -0.1736 -0.1608 32  PRO D N   
9138  C CA  . PRO D 32  ? 0.5198 1.2966 1.3845 0.1668  -0.1846 -0.1529 32  PRO D CA  
9139  C C   . PRO D 32  ? 0.6369 1.4303 1.5095 0.1597  -0.1809 -0.1502 32  PRO D C   
9140  O O   . PRO D 32  ? 0.6226 1.4405 1.5158 0.1585  -0.1734 -0.1557 32  PRO D O   
9141  C CB  . PRO D 32  ? 0.5553 1.3261 1.4346 0.1765  -0.1988 -0.1574 32  PRO D CB  
9142  C CG  . PRO D 32  ? 0.5648 1.3360 1.4510 0.1833  -0.1960 -0.1651 32  PRO D CG  
9143  C CD  . PRO D 32  ? 0.5146 1.3073 1.4068 0.1785  -0.1799 -0.1696 32  PRO D CD  
9144  N N   . MET D 33  ? 0.6244 1.4038 1.4803 0.1550  -0.1862 -0.1415 33  MET D N   
9145  C CA  . MET D 33  ? 0.7111 1.5036 1.5720 0.1475  -0.1826 -0.1381 33  MET D CA  
9146  C C   . MET D 33  ? 0.7561 1.5663 1.6457 0.1506  -0.1885 -0.1436 33  MET D C   
9147  O O   . MET D 33  ? 0.7538 1.5827 1.6559 0.1449  -0.1824 -0.1438 33  MET D O   
9148  C CB  . MET D 33  ? 0.7119 1.4844 1.5494 0.1427  -0.1882 -0.1284 33  MET D CB  
9149  C CG  . MET D 33  ? 0.7766 1.5478 1.5950 0.1340  -0.1764 -0.1222 33  MET D CG  
9150  S SD  . MET D 33  ? 0.9588 1.7609 1.7959 0.1272  -0.1626 -0.1248 33  MET D SD  
9151  C CE  . MET D 33  ? 0.9831 1.7925 1.8366 0.1254  -0.1717 -0.1239 33  MET D CE  
9152  N N   . ILE D 34  ? 0.7586 1.5633 1.6595 0.1595  -0.2004 -0.1482 34  ILE D N   
9153  C CA  . ILE D 34  ? 0.7770 1.5982 1.7060 0.1627  -0.2072 -0.1536 34  ILE D CA  
9154  C C   . ILE D 34  ? 0.7700 1.6149 1.7196 0.1627  -0.1951 -0.1608 34  ILE D C   
9155  O O   . ILE D 34  ? 0.8286 1.6858 1.7920 0.1598  -0.1927 -0.1616 34  ILE D O   
9156  C CB  . ILE D 34  ? 0.7724 1.5786 1.7052 0.1724  -0.2239 -0.1555 34  ILE D CB  
9157  C CG1 . ILE D 34  ? 0.8498 1.6658 1.8027 0.1736  -0.2318 -0.1576 34  ILE D CG1 
9158  C CG2 . ILE D 34  ? 0.7667 1.5713 1.7060 0.1809  -0.2234 -0.1623 34  ILE D CG2 
9159  C CD1 . ILE D 34  ? 0.9461 1.7609 1.8935 0.1664  -0.2359 -0.1514 34  ILE D CD1 
9160  N N   . LEU D 35  ? 0.7511 1.5991 1.6985 0.1650  -0.1863 -0.1651 35  LEU D N   
9161  C CA  . LEU D 35  ? 0.7631 1.6287 1.7239 0.1648  -0.1739 -0.1712 35  LEU D CA  
9162  C C   . LEU D 35  ? 0.8349 1.7170 1.7941 0.1548  -0.1587 -0.1683 35  LEU D C   
9163  O O   . LEU D 35  ? 0.8348 1.7329 1.8058 0.1536  -0.1482 -0.1726 35  LEU D O   
9164  C CB  . LEU D 35  ? 0.6826 1.5450 1.6414 0.1712  -0.1706 -0.1775 35  LEU D CB  
9165  C CG  . LEU D 35  ? 0.7281 1.5750 1.6912 0.1818  -0.1850 -0.1811 35  LEU D CG  
9166  C CD1 . LEU D 35  ? 0.7776 1.6238 1.7425 0.1882  -0.1806 -0.1886 35  LEU D CD1 
9167  C CD2 . LEU D 35  ? 0.7837 1.6342 1.7643 0.1855  -0.1927 -0.1832 35  LEU D CD2 
9168  N N   . HIS D 36  ? 0.9359 1.8144 1.8808 0.1477  -0.1573 -0.1612 36  HIS D N   
9169  C CA  . HIS D 36  ? 0.9132 1.8061 1.8554 0.1383  -0.1430 -0.1579 36  HIS D CA  
9170  C C   . HIS D 36  ? 0.9268 1.8321 1.8836 0.1335  -0.1411 -0.1563 36  HIS D C   
9171  O O   . HIS D 36  ? 0.9110 1.8319 1.8723 0.1275  -0.1280 -0.1559 36  HIS D O   
9172  C CB  . HIS D 36  ? 0.9015 1.7863 1.8246 0.1327  -0.1426 -0.1508 36  HIS D CB  
9173  C CG  . HIS D 36  ? 0.9012 1.7697 1.8020 0.1345  -0.1401 -0.1495 36  HIS D CG  
9174  N ND1 . HIS D 36  ? 0.9148 1.7598 1.8027 0.1402  -0.1510 -0.1482 36  HIS D ND1 
9175  C CD2 . HIS D 36  ? 0.8907 1.7623 1.7793 0.1310  -0.1279 -0.1491 36  HIS D CD2 
9176  C CE1 . HIS D 36  ? 0.9230 1.7576 1.7927 0.1400  -0.1455 -0.1472 36  HIS D CE1 
9177  N NE2 . HIS D 36  ? 0.9039 1.7545 1.7737 0.1346  -0.1318 -0.1479 36  HIS D NE2 
9178  N N   . GLN D 37  ? 1.0755 1.9740 2.0395 0.1358  -0.1539 -0.1553 37  GLN D N   
9179  C CA  . GLN D 37  ? 1.0825 1.9924 2.0615 0.1314  -0.1533 -0.1543 37  GLN D CA  
9180  C C   . GLN D 37  ? 1.0901 2.0039 2.0883 0.1382  -0.1596 -0.1605 37  GLN D C   
9181  O O   . GLN D 37  ? 1.0945 2.0206 2.1079 0.1349  -0.1575 -0.1608 37  GLN D O   
9182  C CB  . GLN D 37  ? 1.1013 2.0026 2.0740 0.1266  -0.1624 -0.1476 37  GLN D CB  
9183  C CG  . GLN D 37  ? 1.1351 2.0199 2.1067 0.1333  -0.1805 -0.1479 37  GLN D CG  
9184  C CD  . GLN D 37  ? 1.0975 1.9652 2.0529 0.1392  -0.1868 -0.1478 37  GLN D CD  
9185  O OE1 . GLN D 37  ? 1.0889 1.9518 2.0284 0.1354  -0.1825 -0.1439 37  GLN D OE1 
9186  N NE2 . GLN D 37  ? 1.0999 1.9581 2.0594 0.1485  -0.1973 -0.1520 37  GLN D NE2 
9187  N N   . ILE D 38  ? 0.9576 1.8615 1.9560 0.1477  -0.1672 -0.1654 38  ILE D N   
9188  C CA  . ILE D 38  ? 0.9288 1.8374 1.9460 0.1547  -0.1720 -0.1719 38  ILE D CA  
9189  C C   . ILE D 38  ? 0.9209 1.8482 1.9502 0.1540  -0.1570 -0.1774 38  ILE D C   
9190  O O   . ILE D 38  ? 0.9533 1.8934 2.0010 0.1541  -0.1551 -0.1806 38  ILE D O   
9191  C CB  . ILE D 38  ? 0.8905 1.7819 1.9041 0.1652  -0.1848 -0.1753 38  ILE D CB  
9192  C CG1 . ILE D 38  ? 0.8594 1.7338 1.8655 0.1667  -0.2015 -0.1703 38  ILE D CG1 
9193  C CG2 . ILE D 38  ? 0.9233 1.8213 1.9560 0.1730  -0.1863 -0.1833 38  ILE D CG2 
9194  C CD1 . ILE D 38  ? 0.8414 1.6984 1.8446 0.1772  -0.2152 -0.1729 38  ILE D CD1 
9195  N N   . GLU D 39  ? 0.8803 1.8096 1.8995 0.1533  -0.1463 -0.1789 39  GLU D N   
9196  C CA  . GLU D 39  ? 0.8758 1.8231 1.9042 0.1518  -0.1313 -0.1838 39  GLU D CA  
9197  C C   . GLU D 39  ? 0.9062 1.8692 1.9395 0.1418  -0.1209 -0.1793 39  GLU D C   
9198  O O   . GLU D 39  ? 0.9311 1.9107 1.9789 0.1406  -0.1115 -0.1830 39  GLU D O   
9199  C CB  . GLU D 39  ? 0.9287 1.8739 1.9433 0.1527  -0.1227 -0.1861 39  GLU D CB  
9200  C CG  . GLU D 39  ? 0.9685 1.9300 1.9922 0.1535  -0.1088 -0.1931 39  GLU D CG  
9201  C CD  . GLU D 39  ? 1.0212 1.9987 2.0427 0.1437  -0.0937 -0.1893 39  GLU D CD  
9202  O OE1 . GLU D 39  ? 1.0483 2.0227 2.0584 0.1363  -0.0931 -0.1812 39  GLU D OE1 
9203  O OE2 . GLU D 39  ? 1.0166 2.0094 2.0478 0.1435  -0.0825 -0.1943 39  GLU D OE2 
9204  N N   . ALA D 40  ? 0.9181 1.8761 1.9401 0.1345  -0.1224 -0.1712 40  ALA D N   
9205  C CA  . ALA D 40  ? 0.9375 1.9090 1.9650 0.1250  -0.1140 -0.1664 40  ALA D CA  
9206  C C   . ALA D 40  ? 0.9594 1.9376 2.0068 0.1253  -0.1204 -0.1676 40  ALA D C   
9207  O O   . ALA D 40  ? 0.9579 1.9522 2.0175 0.1195  -0.1114 -0.1669 40  ALA D O   
9208  C CB  . ALA D 40  ? 0.9314 1.8946 1.9420 0.1178  -0.1151 -0.1579 40  ALA D CB  
9209  N N   . LEU D 41  ? 0.9504 1.9166 2.0016 0.1319  -0.1359 -0.1693 41  LEU D N   
9210  C CA  . LEU D 41  ? 0.8933 1.8658 1.9642 0.1334  -0.1429 -0.1715 41  LEU D CA  
9211  C C   . LEU D 41  ? 0.8446 1.8305 1.9339 0.1388  -0.1372 -0.1796 41  LEU D C   
9212  O O   . LEU D 41  ? 0.8392 1.8366 1.9473 0.1380  -0.1378 -0.1815 41  LEU D O   
9213  C CB  . LEU D 41  ? 0.9038 1.8587 1.9718 0.1393  -0.1617 -0.1709 41  LEU D CB  
9214  C CG  . LEU D 41  ? 0.9534 1.8965 2.0074 0.1337  -0.1693 -0.1633 41  LEU D CG  
9215  C CD1 . LEU D 41  ? 0.9876 1.9117 2.0361 0.1408  -0.1878 -0.1633 41  LEU D CD1 
9216  C CD2 . LEU D 41  ? 1.1064 2.0615 2.1709 0.1248  -0.1661 -0.1598 41  LEU D CD2 
9217  N N   . LYS D 42  ? 0.8892 1.8740 1.9738 0.1443  -0.1317 -0.1847 42  LYS D N   
9218  C CA  . LYS D 42  ? 0.9034 1.9021 2.0047 0.1489  -0.1242 -0.1927 42  LYS D CA  
9219  C C   . LYS D 42  ? 0.9462 1.9647 2.0525 0.1412  -0.1065 -0.1921 42  LYS D C   
9220  O O   . LYS D 42  ? 0.8958 1.9291 2.0194 0.1432  -0.0999 -0.1978 42  LYS D O   
9221  C CB  . LYS D 42  ? 0.9103 1.9003 2.0049 0.1577  -0.1250 -0.1990 42  LYS D CB  
9222  C CG  . LYS D 42  ? 0.9698 1.9582 2.0806 0.1681  -0.1337 -0.2068 42  LYS D CG  
9223  C CD  . LYS D 42  ? 1.0429 2.0520 2.1759 0.1679  -0.1249 -0.2122 42  LYS D CD  
9224  C CE  . LYS D 42  ? 1.0320 2.0395 2.1817 0.1786  -0.1340 -0.2202 42  LYS D CE  
9225  N NZ  . LYS D 42  ? 0.9975 1.9932 2.1511 0.1817  -0.1515 -0.2174 42  LYS D NZ  
9226  N N   . ALA D 43  ? 0.9101 1.9289 2.0016 0.1327  -0.0987 -0.1853 43  ALA D N   
9227  C CA  . ALA D 43  ? 0.9075 1.9444 2.0031 0.1248  -0.0824 -0.1837 43  ALA D CA  
9228  C C   . ALA D 43  ? 0.9352 1.9848 2.0495 0.1197  -0.0821 -0.1815 43  ALA D C   
9229  O O   . ALA D 43  ? 0.9447 2.0119 2.0698 0.1155  -0.0695 -0.1825 43  ALA D O   
9230  C CB  . ALA D 43  ? 0.9077 1.9407 1.9827 0.1171  -0.0752 -0.1764 43  ALA D CB  
9231  N N   . VAL D 44  ? 0.9098 1.9509 2.0279 0.1197  -0.0959 -0.1786 44  VAL D N   
9232  C CA  . VAL D 44  ? 0.8823 1.9344 2.0191 0.1155  -0.0977 -0.1773 44  VAL D CA  
9233  C C   . VAL D 44  ? 0.7899 1.8432 1.9453 0.1240  -0.1078 -0.1843 44  VAL D C   
9234  O O   . VAL D 44  ? 0.8004 1.8608 1.9719 0.1218  -0.1126 -0.1839 44  VAL D O   
9235  C CB  . VAL D 44  ? 0.9184 1.9620 2.0479 0.1085  -0.1054 -0.1693 44  VAL D CB  
9236  C CG1 . VAL D 44  ? 1.1330 2.1799 2.2489 0.0990  -0.0934 -0.1624 44  VAL D CG1 
9237  C CG2 . VAL D 44  ? 0.9113 1.9332 2.0271 0.1143  -0.1215 -0.1686 44  VAL D CG2 
9238  N N   . GLY D 45  ? 0.7373 1.7839 1.8912 0.1337  -0.1114 -0.1909 45  GLY D N   
9239  C CA  . GLY D 45  ? 0.7470 1.7953 1.9190 0.1424  -0.1201 -0.1980 45  GLY D CA  
9240  C C   . GLY D 45  ? 0.7959 1.8308 1.9696 0.1456  -0.1386 -0.1963 45  GLY D C   
9241  O O   . GLY D 45  ? 0.8233 1.8655 2.0159 0.1469  -0.1444 -0.1987 45  GLY D O   
9242  N N   . VAL D 46  ? 0.7908 1.8061 1.9449 0.1468  -0.1481 -0.1922 46  VAL D N   
9243  C CA  . VAL D 46  ? 0.8015 1.8019 1.9542 0.1506  -0.1664 -0.1905 46  VAL D CA  
9244  C C   . VAL D 46  ? 0.8197 1.8083 1.9729 0.1626  -0.1764 -0.1965 46  VAL D C   
9245  O O   . VAL D 46  ? 0.8709 1.8506 2.0109 0.1666  -0.1739 -0.1979 46  VAL D O   
9246  C CB  . VAL D 46  ? 0.8291 1.8144 1.9601 0.1453  -0.1716 -0.1825 46  VAL D CB  
9247  C CG1 . VAL D 46  ? 0.8828 1.8507 2.0100 0.1504  -0.1911 -0.1814 46  VAL D CG1 
9248  C CG2 . VAL D 46  ? 0.8507 1.8470 1.9830 0.1336  -0.1633 -0.1767 46  VAL D CG2 
9249  N N   . ASP D 47  ? 0.8455 1.8340 2.0145 0.1684  -0.1878 -0.2002 47  ASP D N   
9250  C CA  . ASP D 47  ? 0.8812 1.8597 2.0539 0.1801  -0.1977 -0.2061 47  ASP D CA  
9251  C C   . ASP D 47  ? 0.9469 1.9015 2.1035 0.1848  -0.2148 -0.2024 47  ASP D C   
9252  O O   . ASP D 47  ? 0.9875 1.9286 2.1346 0.1922  -0.2192 -0.2045 47  ASP D O   
9253  C CB  . ASP D 47  ? 0.8293 1.8199 2.0278 0.1847  -0.2016 -0.2122 47  ASP D CB  
9254  C CG  . ASP D 47  ? 0.7789 1.7843 1.9905 0.1762  -0.1992 -0.2094 47  ASP D CG  
9255  O OD1 . ASP D 47  ? 0.8074 1.8243 2.0165 0.1668  -0.1857 -0.2059 47  ASP D OD1 
9256  O OD2 . ASP D 47  ? 0.6656 1.6711 1.8904 0.1788  -0.2110 -0.2107 47  ASP D OD2 
9257  N N   . GLU D 48  ? 0.9334 1.8822 2.0866 0.1805  -0.2247 -0.1971 48  GLU D N   
9258  C CA  . GLU D 48  ? 0.9667 1.8932 2.1054 0.1850  -0.2419 -0.1936 48  GLU D CA  
9259  C C   . GLU D 48  ? 1.0314 1.9489 2.1490 0.1769  -0.2413 -0.1856 48  GLU D C   
9260  O O   . GLU D 48  ? 1.0281 1.9566 2.1476 0.1674  -0.2335 -0.1822 48  GLU D O   
9261  C CB  . GLU D 48  ? 0.9091 1.8343 2.0609 0.1881  -0.2568 -0.1947 48  GLU D CB  
9262  N N   . VAL D 49  ? 1.1350 2.0322 2.2328 0.1810  -0.2496 -0.1827 49  VAL D N   
9263  C CA  . VAL D 49  ? 1.1139 2.0003 2.1904 0.1746  -0.2503 -0.1755 49  VAL D CA  
9264  C C   . VAL D 49  ? 1.1689 2.0325 2.2318 0.1805  -0.2688 -0.1726 49  VAL D C   
9265  O O   . VAL D 49  ? 1.2728 2.1246 2.3331 0.1898  -0.2765 -0.1752 49  VAL D O   
9266  C CB  . VAL D 49  ? 1.0479 1.9341 2.1107 0.1724  -0.2372 -0.1744 49  VAL D CB  
9267  C CG1 . VAL D 49  ? 1.1414 2.0161 2.1828 0.1663  -0.2387 -0.1671 49  VAL D CG1 
9268  C CG2 . VAL D 49  ? 0.9570 1.8653 2.0316 0.1667  -0.2188 -0.1770 49  VAL D CG2 
9269  N N   . VAL D 50  ? 1.0995 1.9565 2.1533 0.1750  -0.2761 -0.1671 50  VAL D N   
9270  C CA  . VAL D 50  ? 1.1339 1.9691 2.1730 0.1796  -0.2938 -0.1637 50  VAL D CA  
9271  C C   . VAL D 50  ? 1.2267 2.0500 2.2423 0.1748  -0.2922 -0.1574 50  VAL D C   
9272  O O   . VAL D 50  ? 1.2949 2.1278 2.3077 0.1659  -0.2805 -0.1547 50  VAL D O   
9273  C CB  . VAL D 50  ? 1.1404 1.9763 2.1879 0.1781  -0.3058 -0.1631 50  VAL D CB  
9274  C CG1 . VAL D 50  ? 1.0594 1.8721 2.0914 0.1841  -0.3250 -0.1601 50  VAL D CG1 
9275  C CG2 . VAL D 50  ? 1.0914 1.9426 2.1645 0.1815  -0.3051 -0.1695 50  VAL D CG2 
9276  N N   . LEU D 51  ? 1.1666 1.9689 2.1654 0.1811  -0.3040 -0.1550 51  LEU D N   
9277  C CA  . LEU D 51  ? 1.1852 1.9742 2.1610 0.1780  -0.3041 -0.1493 51  LEU D CA  
9278  C C   . LEU D 51  ? 1.1813 1.9537 2.1442 0.1782  -0.3206 -0.1447 51  LEU D C   
9279  O O   . LEU D 51  ? 1.1692 1.9281 2.1300 0.1861  -0.3355 -0.1452 51  LEU D O   
9280  C CB  . LEU D 51  ? 1.1744 1.9520 2.1397 0.1847  -0.3034 -0.1499 51  LEU D CB  
9281  C CG  . LEU D 51  ? 1.1890 1.9811 2.1648 0.1852  -0.2877 -0.1549 51  LEU D CG  
9282  C CD1 . LEU D 51  ? 1.2150 1.9935 2.1797 0.1921  -0.2891 -0.1556 51  LEU D CD1 
9283  C CD2 . LEU D 51  ? 1.1961 2.0039 2.1715 0.1748  -0.2709 -0.1532 51  LEU D CD2 
9284  N N   . ALA D 52  ? 1.2308 2.0039 2.1847 0.1697  -0.3181 -0.1403 52  ALA D N   
9285  C CA  . ALA D 52  ? 1.2759 2.0334 2.2158 0.1691  -0.3330 -0.1361 52  ALA D CA  
9286  C C   . ALA D 52  ? 1.2298 1.9676 2.1449 0.1713  -0.3375 -0.1312 52  ALA D C   
9287  O O   . ALA D 52  ? 1.2614 1.9903 2.1548 0.1633  -0.3305 -0.1251 52  ALA D O   
9288  C CB  . ALA D 52  ? 1.3559 2.1240 2.3001 0.1589  -0.3287 -0.1343 52  ALA D CB  
9289  N N   . ILE D 53  ? 1.1993 1.9217 2.1061 0.1802  -0.3448 -0.1313 53  ILE D N   
9290  C CA  . ILE D 53  ? 1.2251 1.9191 2.0963 0.1806  -0.3448 -0.1239 53  ILE D CA  
9291  C C   . ILE D 53  ? 1.2378 1.9101 2.0893 0.1818  -0.3608 -0.1188 53  ILE D C   
9292  O O   . ILE D 53  ? 1.2123 1.8913 2.0793 0.1840  -0.3733 -0.1219 53  ILE D O   
9293  C CB  . ILE D 53  ? 1.2125 1.8987 2.0833 0.1892  -0.3450 -0.1260 53  ILE D CB  
9294  C CG1 . ILE D 53  ? 1.1533 1.8354 2.0375 0.1997  -0.3631 -0.1296 53  ILE D CG1 
9295  C CG2 . ILE D 53  ? 1.2394 1.9486 2.1317 0.1886  -0.3300 -0.1322 53  ILE D CG2 
9296  C CD1 . ILE D 53  ? 1.1381 1.8111 2.0226 0.2088  -0.3649 -0.1317 53  ILE D CD1 
9297  N N   . ASN D 54  ? 1.2447 1.8911 2.0619 0.1805  -0.3606 -0.1112 54  ASN D N   
9298  C CA  . ASN D 54  ? 1.3047 1.9279 2.0992 0.1823  -0.3753 -0.1060 54  ASN D CA  
9299  C C   . ASN D 54  ? 1.2961 1.8946 2.0712 0.1902  -0.3835 -0.1025 54  ASN D C   
9300  O O   . ASN D 54  ? 1.2839 1.8653 2.0461 0.1944  -0.3988 -0.0997 54  ASN D O   
9301  C CB  . ASN D 54  ? 1.3684 1.9804 2.1364 0.1729  -0.3692 -0.0993 54  ASN D CB  
9302  C CG  . ASN D 54  ? 1.4522 2.0438 2.1996 0.1740  -0.3845 -0.0951 54  ASN D CG  
9303  O OD1 . ASN D 54  ? 1.4359 2.0358 2.1965 0.1735  -0.3944 -0.0981 54  ASN D OD1 
9304  N ND2 . ASN D 54  ? 1.5014 2.0663 2.2164 0.1753  -0.3865 -0.0883 54  ASN D ND2 
9305  N N   . TYR D 55  ? 1.2715 1.8676 2.0442 0.1924  -0.3740 -0.1026 55  TYR D N   
9306  C CA  . TYR D 55  ? 1.2873 1.8606 2.0437 0.1999  -0.3808 -0.0995 55  TYR D CA  
9307  C C   . TYR D 55  ? 1.2761 1.8589 2.0599 0.2101  -0.3900 -0.1066 55  TYR D C   
9308  O O   . TYR D 55  ? 1.2299 1.8370 2.0447 0.2113  -0.3912 -0.1138 55  TYR D O   
9309  C CB  . TYR D 55  ? 1.2414 1.8058 1.9800 0.1965  -0.3659 -0.0959 55  TYR D CB  
9310  C CG  . TYR D 55  ? 1.2130 1.8011 1.9746 0.1949  -0.3513 -0.1022 55  TYR D CG  
9311  C CD1 . TYR D 55  ? 1.1956 1.8018 1.9633 0.1860  -0.3379 -0.1031 55  TYR D CD1 
9312  C CD2 . TYR D 55  ? 1.2147 1.8067 1.9915 0.2023  -0.3509 -0.1074 55  TYR D CD2 
9313  C CE1 . TYR D 55  ? 1.1509 1.7787 1.9383 0.1845  -0.3245 -0.1087 55  TYR D CE1 
9314  C CE2 . TYR D 55  ? 1.1574 1.7712 1.9543 0.2009  -0.3375 -0.1136 55  TYR D CE2 
9315  C CZ  . TYR D 55  ? 1.1029 1.7346 1.9046 0.1919  -0.3242 -0.1141 55  TYR D CZ  
9316  O OH  . TYR D 55  ? 1.0338 1.6869 1.8541 0.1904  -0.3108 -0.1200 55  TYR D OH  
9317  N N   . GLN D 56  ? 1.3903 1.9537 2.1629 0.2175  -0.3965 -0.1044 56  GLN D N   
9318  C CA  . GLN D 56  ? 1.3963 1.9659 2.1932 0.2281  -0.4060 -0.1107 56  GLN D CA  
9319  C C   . GLN D 56  ? 1.4025 1.9908 2.2210 0.2289  -0.3922 -0.1175 56  GLN D C   
9320  O O   . GLN D 56  ? 1.4041 1.9848 2.2075 0.2256  -0.3799 -0.1149 56  GLN D O   
9321  C CB  . GLN D 56  ? 1.4421 1.9824 2.2184 0.2360  -0.4188 -0.1055 56  GLN D CB  
9322  C CG  . GLN D 56  ? 1.5629 2.0828 2.3137 0.2345  -0.4092 -0.0999 56  GLN D CG  
9323  C CD  . GLN D 56  ? 1.5920 2.0998 2.3119 0.2244  -0.4001 -0.0920 56  GLN D CD  
9324  O OE1 . GLN D 56  ? 1.5971 2.1031 2.3073 0.2200  -0.4049 -0.0889 56  GLN D OE1 
9325  N NE2 . GLN D 56  ? 1.5214 2.0210 2.2264 0.2207  -0.3870 -0.0890 56  GLN D NE2 
9326  N N   . PRO D 57  ? 1.3223 1.9356 2.1761 0.2331  -0.3935 -0.1265 57  PRO D N   
9327  C CA  . PRO D 57  ? 1.3166 1.9489 2.1912 0.2340  -0.3799 -0.1336 57  PRO D CA  
9328  C C   . PRO D 57  ? 1.3597 1.9796 2.2348 0.2432  -0.3827 -0.1356 57  PRO D C   
9329  O O   . PRO D 57  ? 1.3314 1.9662 2.2240 0.2449  -0.3723 -0.1423 57  PRO D O   
9330  C CB  . PRO D 57  ? 1.2876 1.9499 2.1997 0.2357  -0.3822 -0.1424 57  PRO D CB  
9331  C CG  . PRO D 57  ? 1.3018 1.9533 2.2133 0.2409  -0.4011 -0.1406 57  PRO D CG  
9332  C CD  . PRO D 57  ? 1.3047 1.9306 2.1814 0.2372  -0.4075 -0.1309 57  PRO D CD  
9333  N N   . GLU D 58  ? 1.4208 2.0137 2.2767 0.2490  -0.3962 -0.1300 58  GLU D N   
9334  C CA  . GLU D 58  ? 1.4475 2.0271 2.3047 0.2584  -0.4007 -0.1317 58  GLU D CA  
9335  C C   . GLU D 58  ? 1.4996 2.0738 2.3450 0.2551  -0.3851 -0.1312 58  GLU D C   
9336  O O   . GLU D 58  ? 1.4620 2.0331 2.3165 0.2621  -0.3849 -0.1354 58  GLU D O   
9337  C CB  . GLU D 58  ? 1.4914 2.0407 2.3255 0.2639  -0.4176 -0.1240 58  GLU D CB  
9338  C CG  . GLU D 58  ? 1.4868 2.0390 2.3283 0.2665  -0.4340 -0.1238 58  GLU D CG  
9339  C CD  . GLU D 58  ? 1.4992 2.0230 2.3060 0.2648  -0.4444 -0.1133 58  GLU D CD  
9340  O OE1 . GLU D 58  ? 1.5102 2.0122 2.2875 0.2614  -0.4383 -0.1061 58  GLU D OE1 
9341  O OE2 . GLU D 58  ? 1.4793 2.0028 2.2881 0.2667  -0.4585 -0.1125 58  GLU D OE2 
9342  N N   . VAL D 59  ? 1.7542 2.3273 2.5801 0.2446  -0.3722 -0.1262 59  VAL D N   
9343  C CA  . VAL D 59  ? 1.7666 2.3336 2.5793 0.2409  -0.3579 -0.1251 59  VAL D CA  
9344  C C   . VAL D 59  ? 1.7312 2.3262 2.5672 0.2382  -0.3427 -0.1338 59  VAL D C   
9345  O O   . VAL D 59  ? 1.7323 2.3248 2.5642 0.2378  -0.3325 -0.1355 59  VAL D O   
9346  C CB  . VAL D 59  ? 1.8143 2.3653 2.5936 0.2312  -0.3514 -0.1154 59  VAL D CB  
9347  C CG1 . VAL D 59  ? 1.8142 2.3352 2.5675 0.2339  -0.3652 -0.1067 59  VAL D CG1 
9348  C CG2 . VAL D 59  ? 1.7565 2.3261 2.5397 0.2225  -0.3451 -0.1152 59  VAL D CG2 
9349  N N   . MET D 60  ? 1.4529 2.0744 2.3129 0.2363  -0.3407 -0.1392 60  MET D N   
9350  C CA  . MET D 60  ? 1.2752 1.9241 2.1561 0.2330  -0.3256 -0.1468 60  MET D CA  
9351  C C   . MET D 60  ? 1.2067 1.8780 2.1242 0.2409  -0.3296 -0.1573 60  MET D C   
9352  O O   . MET D 60  ? 1.1782 1.8754 2.1162 0.2382  -0.3179 -0.1641 60  MET D O   
9353  C CB  . MET D 60  ? 1.2202 1.8835 2.0975 0.2220  -0.3159 -0.1440 60  MET D CB  
9354  C CG  . MET D 60  ? 1.2194 1.8926 2.1093 0.2214  -0.3259 -0.1439 60  MET D CG  
9355  S SD  . MET D 60  ? 1.0986 1.7833 1.9798 0.2081  -0.3153 -0.1392 60  MET D SD  
9356  C CE  . MET D 60  ? 1.1473 1.8461 2.0517 0.2098  -0.3289 -0.1421 60  MET D CE  
9357  N N   . LEU D 61  ? 1.1862 1.8483 2.1124 0.2506  -0.3458 -0.1587 61  LEU D N   
9358  C CA  . LEU D 61  ? 1.1202 1.8022 2.0803 0.2582  -0.3496 -0.1684 61  LEU D CA  
9359  C C   . LEU D 61  ? 1.0758 1.7673 2.0487 0.2615  -0.3378 -0.1763 61  LEU D C   
9360  O O   . LEU D 61  ? 1.0888 1.7999 2.0804 0.2605  -0.3284 -0.1830 61  LEU D O   
9361  C CB  . LEU D 61  ? 1.1463 1.8108 2.1065 0.2674  -0.3685 -0.1668 61  LEU D CB  
9362  C CG  . LEU D 61  ? 1.2071 1.8665 2.1601 0.2647  -0.3804 -0.1610 61  LEU D CG  
9363  C CD1 . LEU D 61  ? 1.2660 1.9079 2.2190 0.2746  -0.3990 -0.1598 61  LEU D CD1 
9364  C CD2 . LEU D 61  ? 1.1805 1.8641 2.1490 0.2572  -0.3715 -0.1642 61  LEU D CD2 
9365  N N   . ASN D 62  ? 1.0626 1.7363 2.0195 0.2637  -0.3359 -0.1745 62  ASN D N   
9366  C CA  . ASN D 62  ? 1.0067 1.6892 1.9760 0.2673  -0.3255 -0.1828 62  ASN D CA  
9367  C C   . ASN D 62  ? 1.0282 1.7338 2.0020 0.2583  -0.3065 -0.1862 62  ASN D C   
9368  O O   . ASN D 62  ? 1.0433 1.7665 2.0357 0.2604  -0.2970 -0.1951 62  ASN D O   
9369  C CB  . ASN D 62  ? 0.9864 1.6400 1.9319 0.2699  -0.3267 -0.1786 62  ASN D CB  
9370  C CG  . ASN D 62  ? 0.9461 1.5803 1.8945 0.2812  -0.3441 -0.1783 62  ASN D CG  
9371  O OD1 . ASN D 62  ? 0.8746 1.5215 1.8504 0.2897  -0.3523 -0.1854 62  ASN D OD1 
9372  N ND2 . ASN D 62  ? 0.9162 1.5195 1.8364 0.2815  -0.3498 -0.1698 62  ASN D ND2 
9373  N N   . PHE D 63  ? 1.0397 1.7433 1.9931 0.2477  -0.2998 -0.1786 63  PHE D N   
9374  C CA  . PHE D 63  ? 1.0786 1.8029 2.0345 0.2390  -0.2821 -0.1809 63  PHE D CA  
9375  C C   . PHE D 63  ? 1.1373 1.8893 2.1180 0.2366  -0.2778 -0.1859 63  PHE D C   
9376  O O   . PHE D 63  ? 1.0991 1.8693 2.0907 0.2340  -0.2637 -0.1918 63  PHE D O   
9377  C CB  . PHE D 63  ? 1.0591 1.7708 1.9843 0.2283  -0.2763 -0.1705 63  PHE D CB  
9378  C CG  . PHE D 63  ? 0.9746 1.6601 1.8720 0.2278  -0.2749 -0.1651 63  PHE D CG  
9379  C CD1 . PHE D 63  ? 0.8770 1.5661 1.7672 0.2237  -0.2605 -0.1671 63  PHE D CD1 
9380  C CD2 . PHE D 63  ? 1.0218 1.6791 1.9001 0.2311  -0.2879 -0.1580 63  PHE D CD2 
9381  C CE1 . PHE D 63  ? 0.9237 1.5891 1.7894 0.2228  -0.2592 -0.1623 63  PHE D CE1 
9382  C CE2 . PHE D 63  ? 1.0340 1.6674 1.8873 0.2302  -0.2861 -0.1528 63  PHE D CE2 
9383  C CZ  . PHE D 63  ? 1.0028 1.6405 1.8505 0.2259  -0.2718 -0.1551 63  PHE D CZ  
9384  N N   . LEU D 64  ? 1.5401 2.2899 2.5219 0.2355  -0.2877 -0.1817 64  LEU D N   
9385  C CA  . LEU D 64  ? 1.5398 2.3092 2.5373 0.2309  -0.2819 -0.1840 64  LEU D CA  
9386  C C   . LEU D 64  ? 1.5483 2.3261 2.5670 0.2382  -0.2817 -0.1923 64  LEU D C   
9387  O O   . LEU D 64  ? 1.5420 2.3399 2.5761 0.2346  -0.2720 -0.1963 64  LEU D O   
9388  C CB  . LEU D 64  ? 1.5625 2.3262 2.5555 0.2281  -0.2936 -0.1778 64  LEU D CB  
9389  C CG  . LEU D 64  ? 1.5402 2.2937 2.5115 0.2217  -0.2953 -0.1697 64  LEU D CG  
9390  C CD1 . LEU D 64  ? 1.5475 2.2949 2.5145 0.2193  -0.3074 -0.1643 64  LEU D CD1 
9391  C CD2 . LEU D 64  ? 1.5316 2.3006 2.4996 0.2120  -0.2777 -0.1692 64  LEU D CD2 
9392  N N   . LYS D 65  ? 1.2370 1.9994 2.2569 0.2484  -0.2924 -0.1947 65  LYS D N   
9393  C CA  . LYS D 65  ? 1.1921 1.9612 2.2322 0.2562  -0.2927 -0.2030 65  LYS D CA  
9394  C C   . LYS D 65  ? 1.1853 1.9677 2.2327 0.2558  -0.2766 -0.2104 65  LYS D C   
9395  O O   . LYS D 65  ? 1.2210 2.0175 2.2872 0.2588  -0.2710 -0.2179 65  LYS D O   
9396  C CB  . LYS D 65  ? 1.1168 1.8635 2.1547 0.2674  -0.3096 -0.2028 65  LYS D CB  
9397  C CG  . LYS D 65  ? 1.0648 1.8152 2.1233 0.2757  -0.3157 -0.2093 65  LYS D CG  
9398  C CD  . LYS D 65  ? 1.0126 1.7382 2.0655 0.2862  -0.3338 -0.2071 65  LYS D CD  
9399  C CE  . LYS D 65  ? 0.9182 1.6266 1.9523 0.2840  -0.3474 -0.1972 65  LYS D CE  
9400  N NZ  . LYS D 65  ? 0.8268 1.5093 1.8526 0.2940  -0.3649 -0.1941 65  LYS D NZ  
9401  N N   . ASP D 66  ? 1.1220 1.9006 2.1548 0.2523  -0.2691 -0.2088 66  ASP D N   
9402  C CA  . ASP D 66  ? 1.1129 1.9036 2.1501 0.2515  -0.2538 -0.2157 66  ASP D CA  
9403  C C   . ASP D 66  ? 1.1035 1.9173 2.1442 0.2414  -0.2373 -0.2161 66  ASP D C   
9404  O O   . ASP D 66  ? 1.0580 1.8853 2.1055 0.2407  -0.2241 -0.2227 66  ASP D O   
9405  C CB  . ASP D 66  ? 1.0833 1.8601 2.1035 0.2519  -0.2529 -0.2140 66  ASP D CB  
9406  C CG  . ASP D 66  ? 1.1087 1.8622 2.1259 0.2623  -0.2681 -0.2139 66  ASP D CG  
9407  O OD1 . ASP D 66  ? 1.1456 1.8966 2.1769 0.2705  -0.2755 -0.2186 66  ASP D OD1 
9408  O OD2 . ASP D 66  ? 1.1122 1.8494 2.1125 0.2621  -0.2725 -0.2090 66  ASP D OD2 
9409  N N   . PHE D 67  ? 1.1947 2.0128 2.2306 0.2336  -0.2380 -0.2092 67  PHE D N   
9410  C CA  . PHE D 67  ? 1.1730 2.0120 2.2122 0.2238  -0.2231 -0.2086 67  PHE D CA  
9411  C C   . PHE D 67  ? 1.2261 2.0813 2.2860 0.2236  -0.2216 -0.2120 67  PHE D C   
9412  O O   . PHE D 67  ? 1.1753 2.0495 2.2416 0.2167  -0.2080 -0.2131 67  PHE D O   
9413  C CB  . PHE D 67  ? 1.1339 1.9694 2.1569 0.2147  -0.2236 -0.1993 67  PHE D CB  
9414  C CG  . PHE D 67  ? 1.0470 1.8692 2.0498 0.2135  -0.2233 -0.1955 67  PHE D CG  
9415  C CD1 . PHE D 67  ? 1.0172 1.8386 2.0173 0.2167  -0.2163 -0.2007 67  PHE D CD1 
9416  C CD2 . PHE D 67  ? 0.9968 1.8075 1.9837 0.2091  -0.2303 -0.1872 67  PHE D CD2 
9417  C CE1 . PHE D 67  ? 0.9983 1.8079 1.9806 0.2154  -0.2162 -0.1974 67  PHE D CE1 
9418  C CE2 . PHE D 67  ? 0.9776 1.7766 1.9466 0.2080  -0.2300 -0.1837 67  PHE D CE2 
9419  C CZ  . PHE D 67  ? 0.9530 1.7502 1.9182 0.2106  -0.2225 -0.1883 67  PHE D CZ  
9420  N N   . GLU D 68  ? 1.5907 2.4386 2.6611 0.2310  -0.2352 -0.2136 68  GLU D N   
9421  C CA  . GLU D 68  ? 1.5974 2.4606 2.6885 0.2311  -0.2347 -0.2170 68  GLU D CA  
9422  C C   . GLU D 68  ? 1.5994 2.4776 2.7074 0.2350  -0.2238 -0.2265 68  GLU D C   
9423  O O   . GLU D 68  ? 1.5962 2.4938 2.7194 0.2313  -0.2153 -0.2292 68  GLU D O   
9424  C CB  . GLU D 68  ? 1.6142 2.4644 2.7106 0.2382  -0.2533 -0.2158 68  GLU D CB  
9425  C CG  . GLU D 68  ? 1.6330 2.4730 2.7165 0.2332  -0.2636 -0.2068 68  GLU D CG  
9426  C CD  . GLU D 68  ? 1.6636 2.4927 2.7532 0.2399  -0.2816 -0.2060 68  GLU D CD  
9427  O OE1 . GLU D 68  ? 1.6588 2.4731 2.7480 0.2497  -0.2918 -0.2083 68  GLU D OE1 
9428  O OE2 . GLU D 68  ? 1.6913 2.5265 2.7861 0.2354  -0.2857 -0.2031 68  GLU D OE2 
9429  N N   . THR D 69  ? 1.2637 2.1335 2.3698 0.2425  -0.2239 -0.2319 69  THR D N   
9430  C CA  . THR D 69  ? 1.1852 2.0683 2.3065 0.2467  -0.2137 -0.2418 69  THR D CA  
9431  C C   . THR D 69  ? 1.1366 2.0323 2.2508 0.2399  -0.1956 -0.2435 69  THR D C   
9432  O O   . THR D 69  ? 1.0762 1.9908 2.2032 0.2384  -0.1833 -0.2493 69  THR D O   
9433  C CB  . THR D 69  ? 1.1154 1.9830 2.2393 0.2585  -0.2228 -0.2476 69  THR D CB  
9434  O OG1 . THR D 69  ? 1.0983 1.9431 2.2035 0.2603  -0.2340 -0.2413 69  THR D OG1 
9435  C CG2 . THR D 69  ? 1.0624 1.9302 2.2057 0.2666  -0.2335 -0.2516 69  THR D CG2 
9436  N N   . LYS D 70  ? 1.1666 2.0524 2.2604 0.2358  -0.1940 -0.2385 70  LYS D N   
9437  C CA  . LYS D 70  ? 1.2029 2.0997 2.2881 0.2291  -0.1775 -0.2395 70  LYS D CA  
9438  C C   . LYS D 70  ? 1.1688 2.0846 2.2570 0.2188  -0.1664 -0.2357 70  LYS D C   
9439  O O   . LYS D 70  ? 1.1726 2.1048 2.2643 0.2150  -0.1514 -0.2395 70  LYS D O   
9440  C CB  . LYS D 70  ? 1.1867 2.0681 2.2496 0.2269  -0.1796 -0.2343 70  LYS D CB  
9441  C CG  . LYS D 70  ? 1.1806 2.0722 2.2326 0.2197  -0.1636 -0.2346 70  LYS D CG  
9442  C CD  . LYS D 70  ? 1.2074 2.0840 2.2378 0.2167  -0.1668 -0.2283 70  LYS D CD  
9443  C CE  . LYS D 70  ? 1.1802 2.0495 2.2023 0.2115  -0.1754 -0.2181 70  LYS D CE  
9444  N NZ  . LYS D 70  ? 1.1841 2.0387 2.1857 0.2089  -0.1789 -0.2120 70  LYS D NZ  
9445  N N   . LEU D 71  ? 1.1278 2.0411 2.2143 0.2142  -0.1736 -0.2280 71  LEU D N   
9446  C CA  . LEU D 71  ? 1.0571 1.9863 2.1457 0.2039  -0.1643 -0.2233 71  LEU D CA  
9447  C C   . LEU D 71  ? 1.0420 1.9844 2.1523 0.2044  -0.1659 -0.2256 71  LEU D C   
9448  O O   . LEU D 71  ? 1.0238 1.9812 2.1388 0.1962  -0.1573 -0.2226 71  LEU D O   
9449  C CB  . LEU D 71  ? 1.0360 1.9548 2.1077 0.1971  -0.1699 -0.2132 71  LEU D CB  
9450  C CG  . LEU D 71  ? 1.0875 1.9946 2.1374 0.1953  -0.1677 -0.2100 71  LEU D CG  
9451  C CD1 . LEU D 71  ? 1.0419 1.9385 2.0766 0.1893  -0.1744 -0.2004 71  LEU D CD1 
9452  C CD2 . LEU D 71  ? 1.0676 1.9888 2.1133 0.1900  -0.1499 -0.2124 71  LEU D CD2 
9453  N N   . GLU D 72  ? 1.0530 1.9901 2.1766 0.2138  -0.1767 -0.2307 72  GLU D N   
9454  C CA  . GLU D 72  ? 1.0637 2.0123 2.2088 0.2152  -0.1800 -0.2332 72  GLU D CA  
9455  C C   . GLU D 72  ? 1.0679 2.0172 2.2112 0.2076  -0.1855 -0.2250 72  GLU D C   
9456  O O   . GLU D 72  ? 1.0332 1.9995 2.1862 0.2005  -0.1771 -0.2237 72  GLU D O   
9457  C CB  . GLU D 72  ? 1.0361 2.0075 2.1970 0.2135  -0.1643 -0.2398 72  GLU D CB  
9458  C CG  . GLU D 72  ? 1.0260 1.9981 2.1947 0.2227  -0.1612 -0.2498 72  GLU D CG  
9459  C CD  . GLU D 72  ? 0.9838 1.9790 2.1693 0.2213  -0.1463 -0.2566 72  GLU D CD  
9460  O OE1 . GLU D 72  ? 0.9761 1.9861 2.1621 0.2119  -0.1353 -0.2527 72  GLU D OE1 
9461  O OE2 . GLU D 72  ? 0.9521 1.9503 2.1505 0.2296  -0.1457 -0.2657 72  GLU D OE2 
9462  N N   . ILE D 73  ? 1.1021 2.0320 2.2327 0.2094  -0.2000 -0.2195 73  ILE D N   
9463  C CA  . ILE D 73  ? 1.0972 2.0243 2.2233 0.2029  -0.2071 -0.2118 73  ILE D CA  
9464  C C   . ILE D 73  ? 1.2210 2.1291 2.3446 0.2102  -0.2269 -0.2103 73  ILE D C   
9465  O O   . ILE D 73  ? 1.3329 2.2242 2.4467 0.2174  -0.2344 -0.2111 73  ILE D O   
9466  C CB  . ILE D 73  ? 1.1216 2.0446 2.2266 0.1939  -0.2007 -0.2043 73  ILE D CB  
9467  C CG1 . ILE D 73  ? 1.0830 2.0266 2.1926 0.1845  -0.1830 -0.2037 73  ILE D CG1 
9468  C CG2 . ILE D 73  ? 1.1214 2.0315 2.2159 0.1906  -0.2135 -0.1966 73  ILE D CG2 
9469  C CD1 . ILE D 73  ? 0.9935 1.9345 2.0842 0.1752  -0.1767 -0.1961 73  ILE D CD1 
9470  N N   . LYS D 74  ? 1.1749 2.0854 2.3072 0.2083  -0.2355 -0.2079 74  LYS D N   
9471  C CA  . LYS D 74  ? 1.3039 2.1969 2.4330 0.2144  -0.2548 -0.2057 74  LYS D CA  
9472  C C   . LYS D 74  ? 1.4157 2.2931 2.5218 0.2093  -0.2611 -0.1972 74  LYS D C   
9473  O O   . LYS D 74  ? 1.2982 2.1829 2.4005 0.1998  -0.2557 -0.1925 74  LYS D O   
9474  C CB  . LYS D 74  ? 1.2308 2.1336 2.3795 0.2146  -0.2616 -0.2075 74  LYS D CB  
9475  C CG  . LYS D 74  ? 1.2527 2.1382 2.3998 0.2219  -0.2820 -0.2062 74  LYS D CG  
9476  C CD  . LYS D 74  ? 1.2973 2.1710 2.4458 0.2338  -0.2888 -0.2111 74  LYS D CD  
9477  C CE  . LYS D 74  ? 1.2558 2.1128 2.4036 0.2415  -0.3093 -0.2098 74  LYS D CE  
9478  N NZ  . LYS D 74  ? 1.2665 2.1362 2.4349 0.2412  -0.3144 -0.2123 74  LYS D NZ  
9479  N N   . ILE D 75  ? 1.9895 2.8455 3.0806 0.2158  -0.2724 -0.1953 75  ILE D N   
9480  C CA  . ILE D 75  ? 1.9828 2.8225 3.0510 0.2120  -0.2785 -0.1875 75  ILE D CA  
9481  C C   . ILE D 75  ? 2.0021 2.8227 3.0648 0.2187  -0.2987 -0.1850 75  ILE D C   
9482  O O   . ILE D 75  ? 2.0176 2.8255 3.0800 0.2283  -0.3075 -0.1875 75  ILE D O   
9483  C CB  . ILE D 75  ? 1.9750 2.8061 3.0267 0.2127  -0.2717 -0.1867 75  ILE D CB  
9484  C CG1 . ILE D 75  ? 1.9626 2.8129 3.0189 0.2060  -0.2517 -0.1892 75  ILE D CG1 
9485  C CG2 . ILE D 75  ? 1.9721 2.7865 3.0008 0.2091  -0.2785 -0.1787 75  ILE D CG2 
9486  C CD1 . ILE D 75  ? 1.9572 2.8011 2.9989 0.2066  -0.2442 -0.1893 75  ILE D CD1 
9487  N N   . THR D 76  ? 1.4961 2.3140 2.5540 0.2135  -0.3062 -0.1799 76  THR D N   
9488  C CA  . THR D 76  ? 1.2922 2.0914 2.3420 0.2187  -0.3256 -0.1767 76  THR D CA  
9489  C C   . THR D 76  ? 1.1840 1.9711 2.2118 0.2125  -0.3299 -0.1690 76  THR D C   
9490  O O   . THR D 76  ? 1.1928 1.9901 2.2176 0.2029  -0.3192 -0.1665 76  THR D O   
9491  C CB  . THR D 76  ? 1.1550 1.9629 2.2234 0.2199  -0.3336 -0.1795 76  THR D CB  
9492  O OG1 . THR D 76  ? 1.1475 1.9729 2.2237 0.2095  -0.3245 -0.1785 76  THR D OG1 
9493  C CG2 . THR D 76  ? 1.1676 1.9853 2.2575 0.2275  -0.3315 -0.1873 76  THR D CG2 
9494  N N   . CYS D 77  ? 1.0741 1.8390 2.0862 0.2180  -0.3458 -0.1651 77  CYS D N   
9495  C CA  . CYS D 77  ? 1.0245 1.7750 2.0138 0.2136  -0.3514 -0.1579 77  CYS D CA  
9496  C C   . CYS D 77  ? 1.0082 1.7525 1.9954 0.2125  -0.3659 -0.1552 77  CYS D C   
9497  O O   . CYS D 77  ? 1.0025 1.7469 2.0018 0.2180  -0.3760 -0.1581 77  CYS D O   
9498  C CB  . CYS D 77  ? 1.0229 1.7512 1.9926 0.2201  -0.3584 -0.1547 77  CYS D CB  
9499  S SG  . CYS D 77  ? 1.1078 1.8414 2.0765 0.2203  -0.3417 -0.1574 77  CYS D SG  
9500  N N   . SER D 78  ? 1.0237 1.7626 1.9952 0.2054  -0.3670 -0.1497 78  SER D N   
9501  C CA  . SER D 78  ? 1.0365 1.7664 2.0012 0.2041  -0.3815 -0.1466 78  SER D CA  
9502  C C   . SER D 78  ? 1.0989 1.8084 2.0359 0.2030  -0.3883 -0.1399 78  SER D C   
9503  O O   . SER D 78  ? 1.1540 1.8666 2.0821 0.1962  -0.3777 -0.1372 78  SER D O   
9504  C CB  . SER D 78  ? 1.0654 1.8139 2.0436 0.1946  -0.3749 -0.1478 78  SER D CB  
9505  O OG  . SER D 78  ? 1.0944 1.8489 2.0647 0.1855  -0.3622 -0.1447 78  SER D OG  
9506  N N   . GLN D 79  ? 1.1075 1.7964 2.0308 0.2096  -0.4059 -0.1370 79  GLN D N   
9507  C CA  . GLN D 79  ? 1.1582 1.8257 2.0539 0.2097  -0.4141 -0.1304 79  GLN D CA  
9508  C C   . GLN D 79  ? 1.1507 1.8107 2.0376 0.2069  -0.4272 -0.1278 79  GLN D C   
9509  O O   . GLN D 79  ? 1.1514 1.8077 2.0443 0.2117  -0.4397 -0.1294 79  GLN D O   
9510  C CB  . GLN D 79  ? 1.1959 1.8425 2.0790 0.2200  -0.4242 -0.1283 79  GLN D CB  
9511  C CG  . GLN D 79  ? 1.2417 1.8596 2.0861 0.2180  -0.4277 -0.1192 79  GLN D CG  
9512  C CD  . GLN D 79  ? 1.2709 1.8644 2.0984 0.2270  -0.4363 -0.1158 79  GLN D CD  
9513  O OE1 . GLN D 79  ? 1.2793 1.8782 2.1269 0.2360  -0.4421 -0.1208 79  GLN D OE1 
9514  N NE2 . GLN D 79  ? 1.2722 1.8384 2.0628 0.2246  -0.4370 -0.1070 79  GLN D NE2 
9515  N N   . GLU D 80  ? 1.1541 1.8118 2.0271 0.1993  -0.4243 -0.1239 80  GLU D N   
9516  C CA  . GLU D 80  ? 1.1847 1.8341 2.0470 0.1960  -0.4363 -0.1215 80  GLU D CA  
9517  C C   . GLU D 80  ? 1.2098 1.8270 2.0331 0.1979  -0.4443 -0.1135 80  GLU D C   
9518  O O   . GLU D 80  ? 1.2499 1.8525 2.0501 0.1967  -0.4342 -0.1083 80  GLU D O   
9519  C CB  . GLU D 80  ? 1.2618 1.9255 2.1283 0.1847  -0.4255 -0.1215 80  GLU D CB  
9520  C CG  . GLU D 80  ? 1.2685 1.9574 2.1634 0.1796  -0.4147 -0.1268 80  GLU D CG  
9521  C CD  . GLU D 80  ? 1.2406 1.9451 2.1498 0.1794  -0.3975 -0.1296 80  GLU D CD  
9522  O OE1 . GLU D 80  ? 1.1893 1.8858 2.0866 0.1823  -0.3931 -0.1275 80  GLU D OE1 
9523  O OE2 . GLU D 80  ? 1.2470 1.9717 2.1792 0.1763  -0.3885 -0.1340 80  GLU D OE2 
9524  N N   . THR D 81  ? 1.2338 1.8393 2.0487 0.2006  -0.4619 -0.1124 81  THR D N   
9525  C CA  . THR D 81  ? 1.2520 1.8259 2.0273 0.2017  -0.4693 -0.1044 81  THR D CA  
9526  C C   . THR D 81  ? 1.3501 1.9149 2.0988 0.1915  -0.4558 -0.0986 81  THR D C   
9527  O O   . THR D 81  ? 1.3595 1.9035 2.0786 0.1909  -0.4499 -0.0920 81  THR D O   
9528  C CB  . THR D 81  ? 1.1101 1.6757 1.8827 0.2058  -0.4906 -0.1050 81  THR D CB  
9529  O OG1 . THR D 81  ? 1.0654 1.6488 1.8551 0.1991  -0.4916 -0.1092 81  THR D OG1 
9530  C CG2 . THR D 81  ? 0.9201 1.4903 1.7147 0.2172  -0.5051 -0.1096 81  THR D CG2 
9531  N N   . GLU D 82  ? 1.3585 1.9419 2.1219 0.1832  -0.4486 -0.1015 82  GLU D N   
9532  C CA  . GLU D 82  ? 1.5018 2.0798 2.2442 0.1732  -0.4342 -0.0967 82  GLU D CA  
9533  C C   . GLU D 82  ? 1.6145 2.2213 2.3857 0.1665  -0.4200 -0.1015 82  GLU D C   
9534  O O   . GLU D 82  ? 1.5845 2.2121 2.3872 0.1678  -0.4259 -0.1081 82  GLU D O   
9535  C CB  . GLU D 82  ? 1.4636 2.0268 2.1845 0.1694  -0.4438 -0.0937 82  GLU D CB  
9536  C CG  . GLU D 82  ? 1.4152 1.9888 2.1570 0.1716  -0.4603 -0.0993 82  GLU D CG  
9537  C CD  . GLU D 82  ? 1.4606 2.0342 2.1957 0.1632  -0.4615 -0.0992 82  GLU D CD  
9538  O OE1 . GLU D 82  ? 1.4192 1.9698 2.1214 0.1616  -0.4656 -0.0940 82  GLU D OE1 
9539  O OE2 . GLU D 82  ? 1.5214 2.1180 2.2843 0.1582  -0.4580 -0.1044 82  GLU D OE2 
9540  N N   . PRO D 83  ? 1.8297 2.4394 2.5926 0.1596  -0.4017 -0.0985 83  PRO D N   
9541  C CA  . PRO D 83  ? 1.8004 2.4369 2.5899 0.1535  -0.3884 -0.1027 83  PRO D CA  
9542  C C   . PRO D 83  ? 1.8564 2.4976 2.6476 0.1456  -0.3905 -0.1028 83  PRO D C   
9543  O O   . PRO D 83  ? 1.8837 2.5120 2.6506 0.1395  -0.3847 -0.0975 83  PRO D O   
9544  C CB  . PRO D 83  ? 1.8091 2.4423 2.5836 0.1496  -0.3702 -0.0984 83  PRO D CB  
9545  C CG  . PRO D 83  ? 1.8987 2.5014 2.6342 0.1505  -0.3733 -0.0910 83  PRO D CG  
9546  C CD  . PRO D 83  ? 1.8414 2.4292 2.5692 0.1566  -0.3934 -0.0910 83  PRO D CD  
9547  N N   . LEU D 84  ? 1.9834 2.6432 2.8040 0.1459  -0.3986 -0.1090 84  LEU D N   
9548  C CA  . LEU D 84  ? 1.9454 2.6089 2.7690 0.1387  -0.4029 -0.1097 84  LEU D CA  
9549  C C   . LEU D 84  ? 1.9252 2.6023 2.7546 0.1283  -0.3854 -0.1086 84  LEU D C   
9550  O O   . LEU D 84  ? 1.8934 2.5948 2.7536 0.1249  -0.3815 -0.1135 84  LEU D O   
9551  C CB  . LEU D 84  ? 1.8730 2.5534 2.7289 0.1424  -0.4168 -0.1171 84  LEU D CB  
9552  C CG  . LEU D 84  ? 1.8567 2.5292 2.7146 0.1539  -0.4324 -0.1191 84  LEU D CG  
9553  C CD1 . LEU D 84  ? 1.8023 2.4919 2.6850 0.1577  -0.4245 -0.1234 84  LEU D CD1 
9554  C CD2 . LEU D 84  ? 1.8823 2.5479 2.7396 0.1554  -0.4504 -0.1209 84  LEU D CD2 
9555  N N   . GLY D 85  ? 1.7816 2.4429 2.5819 0.1233  -0.3758 -0.1022 85  GLY D N   
9556  C CA  . GLY D 85  ? 1.6644 2.3370 2.4687 0.1136  -0.3604 -0.1006 85  GLY D CA  
9557  C C   . GLY D 85  ? 1.6207 2.3145 2.4458 0.1130  -0.3455 -0.1026 85  GLY D C   
9558  O O   . GLY D 85  ? 1.6653 2.3556 2.4848 0.1182  -0.3409 -0.1019 85  GLY D O   
9559  N N   . THR D 86  ? 1.5109 2.2267 2.3602 0.1063  -0.3376 -0.1053 86  THR D N   
9560  C CA  . THR D 86  ? 1.4907 2.2288 2.3614 0.1050  -0.3231 -0.1077 86  THR D CA  
9561  C C   . THR D 86  ? 1.4776 2.2408 2.3866 0.1075  -0.3275 -0.1154 86  THR D C   
9562  O O   . THR D 86  ? 1.4505 2.2292 2.3765 0.1106  -0.3198 -0.1188 86  THR D O   
9563  C CB  . THR D 86  ? 1.4746 2.2197 2.3423 0.0949  -0.3071 -0.1040 86  THR D CB  
9564  O OG1 . THR D 86  ? 1.5149 2.2369 2.3502 0.0914  -0.3072 -0.0976 86  THR D OG1 
9565  C CG2 . THR D 86  ? 1.4557 2.2116 2.3265 0.0948  -0.2908 -0.1033 86  THR D CG2 
9566  N N   . ALA D 87  ? 1.6258 2.3937 2.5492 0.1061  -0.3396 -0.1187 87  ALA D N   
9567  C CA  . ALA D 87  ? 1.6463 2.4299 2.5945 0.1063  -0.3395 -0.1233 87  ALA D CA  
9568  C C   . ALA D 87  ? 1.6102 2.3847 2.5591 0.1155  -0.3555 -0.1263 87  ALA D C   
9569  O O   . ALA D 87  ? 1.5954 2.3820 2.5641 0.1172  -0.3553 -0.1303 87  ALA D O   
9570  C CB  . ALA D 87  ? 1.6639 2.4569 2.6245 0.0970  -0.3387 -0.1238 87  ALA D CB  
9571  N N   . GLY D 88  ? 1.6278 2.3812 2.5554 0.1214  -0.3692 -0.1243 88  GLY D N   
9572  C CA  . GLY D 88  ? 1.6325 2.3749 2.5578 0.1304  -0.3851 -0.1263 88  GLY D CA  
9573  C C   . GLY D 88  ? 1.5895 2.3379 2.5259 0.1381  -0.3818 -0.1291 88  GLY D C   
9574  O O   . GLY D 88  ? 1.5270 2.2809 2.4787 0.1420  -0.3880 -0.1330 88  GLY D O   
9575  N N   . PRO D 89  ? 1.5703 2.3171 2.4992 0.1407  -0.3722 -0.1275 89  PRO D N   
9576  C CA  . PRO D 89  ? 1.5464 2.2986 2.4859 0.1481  -0.3685 -0.1306 89  PRO D CA  
9577  C C   . PRO D 89  ? 1.5424 2.3174 2.5097 0.1457  -0.3593 -0.1354 89  PRO D C   
9578  O O   . PRO D 89  ? 1.5237 2.3028 2.5029 0.1525  -0.3605 -0.1391 89  PRO D O   
9579  C CB  . PRO D 89  ? 1.5133 2.2640 2.4417 0.1480  -0.3562 -0.1281 89  PRO D CB  
9580  C CG  . PRO D 89  ? 1.5630 2.2973 2.4679 0.1454  -0.3620 -0.1230 89  PRO D CG  
9581  C CD  . PRO D 89  ? 1.5801 2.3174 2.4887 0.1383  -0.3669 -0.1229 89  PRO D CD  
9582  N N   . LEU D 90  ? 1.4753 2.2647 2.4530 0.1360  -0.3501 -0.1352 90  LEU D N   
9583  C CA  . LEU D 90  ? 1.4037 2.2149 2.4077 0.1330  -0.3415 -0.1394 90  LEU D CA  
9584  C C   . LEU D 90  ? 1.3449 2.1568 2.3617 0.1358  -0.3554 -0.1429 90  LEU D C   
9585  O O   . LEU D 90  ? 1.2999 2.1264 2.3382 0.1378  -0.3522 -0.1473 90  LEU D O   
9586  C CB  . LEU D 90  ? 1.4192 2.2448 2.4297 0.1216  -0.3276 -0.1375 90  LEU D CB  
9587  C CG  . LEU D 90  ? 1.4524 2.2842 2.4570 0.1177  -0.3101 -0.1349 90  LEU D CG  
9588  C CD1 . LEU D 90  ? 1.5040 2.3186 2.4832 0.1173  -0.3127 -0.1300 90  LEU D CD1 
9589  C CD2 . LEU D 90  ? 1.4708 2.3221 2.4902 0.1075  -0.2957 -0.1344 90  LEU D CD2 
9590  N N   . ALA D 91  ? 1.3481 2.1447 2.3522 0.1361  -0.3708 -0.1412 91  ALA D N   
9591  C CA  . ALA D 91  ? 1.3316 2.1280 2.3466 0.1389  -0.3851 -0.1446 91  ALA D CA  
9592  C C   . ALA D 91  ? 1.3491 2.1386 2.3661 0.1504  -0.3946 -0.1472 91  ALA D C   
9593  O O   . ALA D 91  ? 1.2928 2.0895 2.3272 0.1535  -0.4013 -0.1514 91  ALA D O   
9594  C CB  . ALA D 91  ? 1.2975 2.0781 2.2959 0.1364  -0.3993 -0.1421 91  ALA D CB  
9595  N N   . LEU D 92  ? 1.3387 2.1143 2.3386 0.1569  -0.3954 -0.1449 92  LEU D N   
9596  C CA  . LEU D 92  ? 1.3164 2.0838 2.3172 0.1681  -0.4047 -0.1470 92  LEU D CA  
9597  C C   . LEU D 92  ? 1.3122 2.0972 2.3348 0.1708  -0.3924 -0.1516 92  LEU D C   
9598  O O   . LEU D 92  ? 1.3461 2.1332 2.3818 0.1780  -0.3993 -0.1556 92  LEU D O   
9599  C CB  . LEU D 92  ? 1.3292 2.0742 2.3034 0.1738  -0.4105 -0.1426 92  LEU D CB  
9600  C CG  . LEU D 92  ? 1.3161 2.0478 2.2863 0.1857  -0.4213 -0.1435 92  LEU D CG  
9601  C CD1 . LEU D 92  ? 1.3252 2.0306 2.2670 0.1899  -0.4366 -0.1383 92  LEU D CD1 
9602  C CD2 . LEU D 92  ? 1.2640 2.0011 2.2390 0.1894  -0.4087 -0.1449 92  LEU D CD2 
9603  N N   . ALA D 93  ? 1.3427 2.1404 2.3691 0.1653  -0.3744 -0.1512 93  ALA D N   
9604  C CA  . ALA D 93  ? 1.3662 2.1801 2.4107 0.1676  -0.3615 -0.1555 93  ALA D CA  
9605  C C   . ALA D 93  ? 1.3869 2.2244 2.4574 0.1616  -0.3530 -0.1592 93  ALA D C   
9606  O O   . ALA D 93  ? 1.3653 2.2187 2.4503 0.1613  -0.3392 -0.1623 93  ALA D O   
9607  C CB  . ALA D 93  ? 1.3823 2.1973 2.4163 0.1651  -0.3463 -0.1532 93  ALA D CB  
9608  N N   . ARG D 94  ? 1.3936 2.2335 2.4701 0.1569  -0.3608 -0.1592 94  ARG D N   
9609  C CA  . ARG D 94  ? 1.4227 2.2848 2.5246 0.1511  -0.3535 -0.1627 94  ARG D CA  
9610  C C   . ARG D 94  ? 1.4831 2.3550 2.6065 0.1586  -0.3560 -0.1687 94  ARG D C   
9611  O O   . ARG D 94  ? 1.4115 2.3042 2.5571 0.1550  -0.3454 -0.1721 94  ARG D O   
9612  C CB  . ARG D 94  ? 1.4141 2.2748 2.5172 0.1447  -0.3630 -0.1616 94  ARG D CB  
9613  C CG  . ARG D 94  ? 1.3562 2.2041 2.4575 0.1519  -0.3837 -0.1633 94  ARG D CG  
9614  C CD  . ARG D 94  ? 1.2571 2.1158 2.3764 0.1468  -0.3896 -0.1661 94  ARG D CD  
9615  N NE  . ARG D 94  ? 1.3502 2.2072 2.4614 0.1367  -0.3886 -0.1627 94  ARG D NE  
9616  C CZ  . ARG D 94  ? 1.3254 2.1913 2.4503 0.1303  -0.3921 -0.1645 94  ARG D CZ  
9617  N NH1 . ARG D 94  ? 1.1721 2.0500 2.3199 0.1328  -0.3968 -0.1695 94  ARG D NH1 
9618  N NH2 . ARG D 94  ? 1.4470 2.3101 2.5636 0.1213  -0.3911 -0.1614 94  ARG D NH2 
9619  N N   . ASP D 95  ? 1.9230 2.7803 3.0405 0.1691  -0.3697 -0.1701 95  ASP D N   
9620  C CA  . ASP D 95  ? 1.9346 2.7999 3.0724 0.1770  -0.3733 -0.1760 95  ASP D CA  
9621  C C   . ASP D 95  ? 1.9253 2.8012 3.0717 0.1802  -0.3584 -0.1790 95  ASP D C   
9622  O O   . ASP D 95  ? 1.9289 2.8209 3.0984 0.1826  -0.3539 -0.1844 95  ASP D O   
9623  C CB  . ASP D 95  ? 1.9542 2.7992 3.0816 0.1873  -0.3930 -0.1759 95  ASP D CB  
9624  C CG  . ASP D 95  ? 1.9530 2.7754 3.0517 0.1908  -0.3971 -0.1709 95  ASP D CG  
9625  O OD1 . ASP D 95  ? 1.9363 2.7597 3.0243 0.1855  -0.3844 -0.1679 95  ASP D OD1 
9626  O OD2 . ASP D 95  ? 2.0306 2.8344 3.1175 0.1989  -0.4129 -0.1698 95  ASP D OD2 
9627  N N   . LYS D 96  ? 1.4735 2.3408 2.6018 0.1802  -0.3508 -0.1758 96  LYS D N   
9628  C CA  . LYS D 96  ? 1.3376 2.2139 2.4717 0.1828  -0.3364 -0.1787 96  LYS D CA  
9629  C C   . LYS D 96  ? 1.2283 2.1249 2.3713 0.1730  -0.3170 -0.1785 96  LYS D C   
9630  O O   . LYS D 96  ? 1.1409 2.0474 2.2900 0.1742  -0.3038 -0.1812 96  LYS D O   
9631  C CB  . LYS D 96  ? 1.2844 2.1420 2.3952 0.1876  -0.3375 -0.1757 96  LYS D CB  
9632  C CG  . LYS D 96  ? 1.2670 2.1037 2.3683 0.1983  -0.3556 -0.1756 96  LYS D CG  
9633  C CD  . LYS D 96  ? 1.2322 2.0756 2.3537 0.2073  -0.3583 -0.1823 96  LYS D CD  
9634  C CE  . LYS D 96  ? 1.0714 1.9234 2.1986 0.2097  -0.3433 -0.1860 96  LYS D CE  
9635  N NZ  . LYS D 96  ? 0.9842 1.8421 2.1311 0.2190  -0.3459 -0.1929 96  LYS D NZ  
9636  N N   . LEU D 97  ? 1.2603 2.1628 2.4040 0.1633  -0.3153 -0.1753 97  LEU D N   
9637  C CA  . LEU D 97  ? 1.2002 2.1209 2.3513 0.1534  -0.2974 -0.1742 97  LEU D CA  
9638  C C   . LEU D 97  ? 1.1697 2.1117 2.3478 0.1495  -0.2933 -0.1780 97  LEU D C   
9639  O O   . LEU D 97  ? 1.1397 2.0994 2.3283 0.1436  -0.2771 -0.1785 97  LEU D O   
9640  C CB  . LEU D 97  ? 1.1674 2.0808 2.3010 0.1443  -0.2962 -0.1677 97  LEU D CB  
9641  C CG  . LEU D 97  ? 1.0697 1.9668 2.1777 0.1457  -0.2946 -0.1634 97  LEU D CG  
9642  C CD1 . LEU D 97  ? 1.1642 2.0540 2.2566 0.1371  -0.2954 -0.1575 97  LEU D CD1 
9643  C CD2 . LEU D 97  ? 1.0985 2.0053 2.2072 0.1455  -0.2773 -0.1646 97  LEU D CD2 
9644  N N   . LEU D 98  ? 1.1716 2.1123 2.3608 0.1527  -0.3074 -0.1806 98  LEU D N   
9645  C CA  . LEU D 98  ? 1.2100 2.1707 2.4257 0.1491  -0.3048 -0.1844 98  LEU D CA  
9646  C C   . LEU D 98  ? 1.2713 2.2419 2.5059 0.1578  -0.3033 -0.1911 98  LEU D C   
9647  O O   . LEU D 98  ? 1.2298 2.1910 2.4667 0.1670  -0.3175 -0.1941 98  LEU D O   
9648  C CB  . LEU D 98  ? 1.2189 2.1739 2.4375 0.1475  -0.3210 -0.1839 98  LEU D CB  
9649  C CG  . LEU D 98  ? 1.2435 2.1885 2.4445 0.1389  -0.3237 -0.1780 98  LEU D CG  
9650  C CD1 . LEU D 98  ? 1.3296 2.2721 2.5373 0.1370  -0.3388 -0.1788 98  LEU D CD1 
9651  C CD2 . LEU D 98  ? 1.1372 2.0965 2.3407 0.1280  -0.3053 -0.1749 98  LEU D CD2 
9652  N N   . ASP D 99  ? 1.3802 2.3696 2.6282 0.1550  -0.2862 -0.1934 99  ASP D N   
9653  C CA  . ASP D 99  ? 1.3752 2.3770 2.6437 0.1622  -0.2827 -0.2003 99  ASP D CA  
9654  C C   . ASP D 99  ? 1.4096 2.4307 2.7058 0.1593  -0.2830 -0.2041 99  ASP D C   
9655  O O   . ASP D 99  ? 1.4183 2.4488 2.7335 0.1661  -0.2837 -0.2104 99  ASP D O   
9656  C CB  . ASP D 99  ? 1.3294 2.3412 2.5972 0.1614  -0.2639 -0.2014 99  ASP D CB  
9657  C CG  . ASP D 99  ? 1.3581 2.3845 2.6272 0.1493  -0.2477 -0.1975 99  ASP D CG  
9658  O OD1 . ASP D 99  ? 1.3965 2.4182 2.6569 0.1415  -0.2511 -0.1922 99  ASP D OD1 
9659  O OD2 . ASP D 99  ? 1.3600 2.4023 2.6385 0.1476  -0.2318 -0.1998 99  ASP D OD2 
9660  N N   . GLY D 100 ? 1.5061 2.5332 2.8055 0.1493  -0.2826 -0.2007 100 GLY D N   
9661  C CA  . GLY D 100 ? 1.4651 2.5104 2.7904 0.1453  -0.2828 -0.2039 100 GLY D CA  
9662  C C   . GLY D 100 ? 1.5954 2.6615 2.9319 0.1346  -0.2642 -0.2023 100 GLY D C   
9663  O O   . GLY D 100 ? 1.4889 2.5670 2.8412 0.1275  -0.2645 -0.2022 100 GLY D O   
9664  N N   . SER D 101 ? 1.9482 3.0182 3.2764 0.1331  -0.2483 -0.2008 101 SER D N   
9665  C CA  . SER D 101 ? 1.9400 3.0295 3.2777 0.1234  -0.2299 -0.1990 101 SER D CA  
9666  C C   . SER D 101 ? 1.9332 3.0191 3.2587 0.1119  -0.2272 -0.1918 101 SER D C   
9667  O O   . SER D 101 ? 1.9403 3.0424 3.2761 0.1027  -0.2144 -0.1897 101 SER D O   
9668  C CB  . SER D 101 ? 1.9282 3.0222 3.2597 0.1259  -0.2143 -0.1999 101 SER D CB  
9669  O OG  . SER D 101 ? 1.9109 3.0226 3.2491 0.1164  -0.1963 -0.1974 101 SER D OG  
9670  N N   . GLY D 102 ? 1.7100 2.7750 3.0140 0.1123  -0.2389 -0.1879 102 GLY D N   
9671  C CA  . GLY D 102 ? 1.6073 2.6676 2.8993 0.1020  -0.2372 -0.1814 102 GLY D CA  
9672  C C   . GLY D 102 ? 1.6206 2.6851 2.9008 0.0955  -0.2194 -0.1766 102 GLY D C   
9673  O O   . GLY D 102 ? 1.5318 2.6061 2.8161 0.0851  -0.2102 -0.1727 102 GLY D O   
9674  N N   . GLU D 103 ? 1.7325 2.7894 2.9980 0.1017  -0.2147 -0.1768 103 GLU D N   
9675  C CA  . GLU D 103 ? 1.7416 2.8007 2.9938 0.0970  -0.1987 -0.1726 103 GLU D CA  
9676  C C   . GLU D 103 ? 1.7019 2.7404 2.9267 0.0958  -0.2040 -0.1671 103 GLU D C   
9677  O O   . GLU D 103 ? 1.7044 2.7252 2.9176 0.1027  -0.2186 -0.1679 103 GLU D O   
9678  C CB  . GLU D 103 ? 1.8126 2.8772 3.0664 0.1043  -0.1893 -0.1770 103 GLU D CB  
9679  C CG  . GLU D 103 ? 1.8492 2.9370 3.1281 0.1036  -0.1783 -0.1816 103 GLU D CG  
9680  C CD  . GLU D 103 ? 1.8790 2.9822 3.1600 0.0934  -0.1597 -0.1775 103 GLU D CD  
9681  O OE1 . GLU D 103 ? 1.8471 2.9423 3.1088 0.0879  -0.1547 -0.1714 103 GLU D OE1 
9682  O OE2 . GLU D 103 ? 1.9348 3.0579 3.2365 0.0910  -0.1501 -0.1802 103 GLU D OE2 
9683  N N   . PRO D 104 ? 1.5713 2.6116 2.7852 0.0872  -0.1924 -0.1614 104 PRO D N   
9684  C CA  . PRO D 104 ? 1.5353 2.5568 2.7237 0.0860  -0.1967 -0.1562 104 PRO D CA  
9685  C C   . PRO D 104 ? 1.5326 2.5419 2.7045 0.0948  -0.1975 -0.1575 104 PRO D C   
9686  O O   . PRO D 104 ? 1.4829 2.5007 2.6588 0.0984  -0.1871 -0.1605 104 PRO D O   
9687  C CB  . PRO D 104 ? 1.5139 2.5441 2.6983 0.0749  -0.1816 -0.1503 104 PRO D CB  
9688  C CG  . PRO D 104 ? 1.5844 2.6364 2.7875 0.0729  -0.1668 -0.1528 104 PRO D CG  
9689  C CD  . PRO D 104 ? 1.5798 2.6394 2.8047 0.0780  -0.1754 -0.1591 104 PRO D CD  
9690  N N   . PHE D 105 ? 1.4803 2.4691 2.6335 0.0983  -0.2100 -0.1555 105 PHE D N   
9691  C CA  . PHE D 105 ? 1.5669 2.5416 2.7027 0.1062  -0.2122 -0.1561 105 PHE D CA  
9692  C C   . PHE D 105 ? 1.8337 2.7980 2.9467 0.1013  -0.2076 -0.1499 105 PHE D C   
9693  O O   . PHE D 105 ? 1.7407 2.7037 2.8493 0.0931  -0.2076 -0.1453 105 PHE D O   
9694  C CB  . PHE D 105 ? 1.3995 2.3579 2.5317 0.1155  -0.2311 -0.1588 105 PHE D CB  
9695  C CG  . PHE D 105 ? 1.2752 2.2223 2.4015 0.1124  -0.2451 -0.1558 105 PHE D CG  
9696  C CD1 . PHE D 105 ? 1.2163 2.1709 2.3603 0.1104  -0.2524 -0.1580 105 PHE D CD1 
9697  C CD2 . PHE D 105 ? 1.3399 2.2689 2.4431 0.1116  -0.2511 -0.1511 105 PHE D CD2 
9698  C CE1 . PHE D 105 ? 1.1798 2.1237 2.3179 0.1075  -0.2655 -0.1557 105 PHE D CE1 
9699  C CE2 . PHE D 105 ? 1.2495 2.1677 2.3466 0.1089  -0.2640 -0.1488 105 PHE D CE2 
9700  C CZ  . PHE D 105 ? 1.1414 2.0669 2.2558 0.1068  -0.2713 -0.1512 105 PHE D CZ  
9701  N N   . PHE D 106 ? 2.7020 3.6587 3.8009 0.1064  -0.2039 -0.1502 106 PHE D N   
9702  C CA  . PHE D 106 ? 2.6908 3.6381 3.7681 0.1027  -0.1989 -0.1449 106 PHE D CA  
9703  C C   . PHE D 106 ? 2.6944 3.6191 3.7534 0.1080  -0.2140 -0.1433 106 PHE D C   
9704  O O   . PHE D 106 ? 2.7044 3.6200 3.7641 0.1169  -0.2254 -0.1469 106 PHE D O   
9705  C CB  . PHE D 106 ? 2.6832 3.6363 3.7554 0.1044  -0.1847 -0.1461 106 PHE D CB  
9706  C CG  . PHE D 106 ? 2.6778 3.6515 3.7621 0.0974  -0.1678 -0.1458 106 PHE D CG  
9707  C CD1 . PHE D 106 ? 2.6673 3.6449 3.7431 0.0882  -0.1573 -0.1399 106 PHE D CD1 
9708  C CD2 . PHE D 106 ? 2.6839 3.6728 3.7878 0.1001  -0.1624 -0.1512 106 PHE D CD2 
9709  C CE1 . PHE D 106 ? 2.6635 3.6594 3.7496 0.0818  -0.1418 -0.1391 106 PHE D CE1 
9710  C CE2 . PHE D 106 ? 2.6799 3.6877 3.7944 0.0937  -0.1467 -0.1507 106 PHE D CE2 
9711  C CZ  . PHE D 106 ? 2.6699 3.6809 3.7751 0.0845  -0.1365 -0.1444 106 PHE D CZ  
9712  N N   . VAL D 107 ? 2.2682 3.1840 3.3107 0.1024  -0.2140 -0.1378 107 VAL D N   
9713  C CA  . VAL D 107 ? 2.2660 3.1606 3.2889 0.1064  -0.2266 -0.1355 107 VAL D CA  
9714  C C   . VAL D 107 ? 2.2512 3.1411 3.2558 0.1039  -0.2171 -0.1316 107 VAL D C   
9715  O O   . VAL D 107 ? 2.2422 3.1379 3.2434 0.0954  -0.2080 -0.1275 107 VAL D O   
9716  C CB  . VAL D 107 ? 2.2690 3.1556 3.2895 0.1022  -0.2384 -0.1327 107 VAL D CB  
9717  C CG1 . VAL D 107 ? 2.2675 3.1318 3.2669 0.1069  -0.2516 -0.1304 107 VAL D CG1 
9718  C CG2 . VAL D 107 ? 2.2788 3.1718 3.3186 0.1039  -0.2472 -0.1366 107 VAL D CG2 
9719  N N   . LEU D 108 ? 1.8706 2.7501 2.8637 0.1113  -0.2194 -0.1330 108 LEU D N   
9720  C CA  . LEU D 108 ? 1.6465 2.5221 2.6231 0.1099  -0.2105 -0.1303 108 LEU D CA  
9721  C C   . LEU D 108 ? 1.5571 2.4116 2.5140 0.1142  -0.2225 -0.1279 108 LEU D C   
9722  O O   . LEU D 108 ? 1.5510 2.3934 2.5069 0.1212  -0.2369 -0.1296 108 LEU D O   
9723  C CB  . LEU D 108 ? 1.5239 2.4075 2.5043 0.1144  -0.2002 -0.1345 108 LEU D CB  
9724  C CG  . LEU D 108 ? 1.5014 2.4060 2.5008 0.1112  -0.1877 -0.1375 108 LEU D CG  
9725  C CD1 . LEU D 108 ? 1.2418 2.1519 2.2432 0.1167  -0.1792 -0.1423 108 LEU D CD1 
9726  C CD2 . LEU D 108 ? 1.4669 2.3828 2.4660 0.1005  -0.1754 -0.1327 108 LEU D CD2 
9727  N N   . ASN D 109 ? 1.4911 2.3412 2.4322 0.1101  -0.2165 -0.1237 109 ASN D N   
9728  C CA  . ASN D 109 ? 1.4772 2.2998 2.3877 0.1120  -0.2228 -0.1181 109 ASN D CA  
9729  C C   . ASN D 109 ? 1.5466 2.3630 2.4438 0.1160  -0.2153 -0.1183 109 ASN D C   
9730  O O   . ASN D 109 ? 1.4389 2.2690 2.3400 0.1129  -0.2013 -0.1192 109 ASN D O   
9731  C CB  . ASN D 109 ? 1.3499 2.1620 2.2399 0.1032  -0.2190 -0.1102 109 ASN D CB  
9732  C CG  . ASN D 109 ? 1.3243 2.1072 2.1841 0.1051  -0.2279 -0.1045 109 ASN D CG  
9733  O OD1 . ASN D 109 ? 1.3965 2.1658 2.2443 0.1117  -0.2321 -0.1048 109 ASN D OD1 
9734  N ND2 . ASN D 109 ? 1.2038 1.9770 2.0511 0.0992  -0.2306 -0.0994 109 ASN D ND2 
9735  N N   . SER D 110 ? 2.0824 2.8778 2.9637 0.1227  -0.2248 -0.1173 110 SER D N   
9736  C CA  . SER D 110 ? 2.0875 2.8754 2.9568 0.1268  -0.2190 -0.1178 110 SER D CA  
9737  C C   . SER D 110 ? 2.0956 2.8725 2.9384 0.1205  -0.2085 -0.1109 110 SER D C   
9738  O O   . SER D 110 ? 2.0965 2.8716 2.9312 0.1221  -0.2007 -0.1115 110 SER D O   
9739  C CB  . SER D 110 ? 2.1075 2.8753 2.9680 0.1357  -0.2327 -0.1185 110 SER D CB  
9740  O OG  . SER D 110 ? 2.1141 2.8747 2.9647 0.1396  -0.2274 -0.1194 110 SER D OG  
9741  N N   . ASP D 111 ? 1.4914 2.2610 2.3208 0.1136  -0.2083 -0.1045 111 ASP D N   
9742  C CA  . ASP D 111 ? 1.3041 2.0622 2.1081 0.1079  -0.1995 -0.0976 111 ASP D CA  
9743  C C   . ASP D 111 ? 1.1550 1.9316 1.9655 0.1004  -0.1846 -0.0966 111 ASP D C   
9744  O O   . ASP D 111 ? 1.1006 1.8696 1.8925 0.0944  -0.1779 -0.0904 111 ASP D O   
9745  C CB  . ASP D 111 ? 1.1769 1.9147 1.9605 0.1050  -0.2075 -0.0911 111 ASP D CB  
9746  C CG  . ASP D 111 ? 1.2382 1.9570 2.0136 0.1122  -0.2225 -0.0914 111 ASP D CG  
9747  O OD1 . ASP D 111 ? 1.3207 2.0431 2.1093 0.1195  -0.2279 -0.0969 111 ASP D OD1 
9748  O OD2 . ASP D 111 ? 1.1497 1.8494 1.9049 0.1106  -0.2290 -0.0862 111 ASP D OD2 
9749  N N   . VAL D 112 ? 1.1273 1.9278 1.9634 0.1005  -0.1792 -0.1025 112 VAL D N   
9750  C CA  . VAL D 112 ? 0.9927 1.8119 1.8365 0.0933  -0.1654 -0.1016 112 VAL D CA  
9751  C C   . VAL D 112 ? 0.9335 1.7702 1.7909 0.0962  -0.1560 -0.1077 112 VAL D C   
9752  O O   . VAL D 112 ? 1.0146 1.8577 1.8884 0.1033  -0.1612 -0.1147 112 VAL D O   
9753  C CB  . VAL D 112 ? 0.9741 1.8077 1.8378 0.0884  -0.1672 -0.1021 112 VAL D CB  
9754  C CG1 . VAL D 112 ? 0.9277 1.7776 1.7954 0.0801  -0.1528 -0.0994 112 VAL D CG1 
9755  C CG2 . VAL D 112 ? 1.0467 1.8627 1.8988 0.0867  -0.1787 -0.0976 112 VAL D CG2 
9756  N N   . ILE D 113 ? 0.8282 1.6727 1.6785 0.0911  -0.1423 -0.1053 113 ILE D N   
9757  C CA  . ILE D 113 ? 0.8328 1.6961 1.6954 0.0925  -0.1316 -0.1109 113 ILE D CA  
9758  C C   . ILE D 113 ? 0.8785 1.7610 1.7497 0.0843  -0.1196 -0.1088 113 ILE D C   
9759  O O   . ILE D 113 ? 0.9257 1.8024 1.7852 0.0775  -0.1174 -0.1015 113 ILE D O   
9760  C CB  . ILE D 113 ? 0.8582 1.7113 1.7016 0.0949  -0.1263 -0.1105 113 ILE D CB  
9761  C CG1 . ILE D 113 ? 0.9272 1.7659 1.7444 0.0887  -0.1220 -0.1016 113 ILE D CG1 
9762  C CG2 . ILE D 113 ? 0.8635 1.7010 1.7032 0.1036  -0.1371 -0.1141 113 ILE D CG2 
9763  C CD1 . ILE D 113 ? 0.9830 1.8139 1.7823 0.0899  -0.1156 -0.1010 113 ILE D CD1 
9764  N N   . SER D 114 ? 0.9110 1.8161 1.8025 0.0851  -0.1118 -0.1150 114 SER D N   
9765  C CA  . SER D 114 ? 0.9574 1.8825 1.8590 0.0776  -0.0998 -0.1133 114 SER D CA  
9766  C C   . SER D 114 ? 0.9727 1.9133 1.8858 0.0799  -0.0899 -0.1192 114 SER D C   
9767  O O   . SER D 114 ? 0.9841 1.9215 1.8976 0.0873  -0.0922 -0.1251 114 SER D O   
9768  C CB  . SER D 114 ? 0.9687 1.8992 1.8854 0.0731  -0.1047 -0.1114 114 SER D CB  
9769  O OG  . SER D 114 ? 0.9543 1.8882 1.8885 0.0778  -0.1105 -0.1166 114 SER D OG  
9770  N N   . GLU D 115 ? 1.0232 1.9786 1.9436 0.0734  -0.0785 -0.1171 115 GLU D N   
9771  C CA  . GLU D 115 ? 1.0531 2.0223 1.9832 0.0748  -0.0682 -0.1219 115 GLU D CA  
9772  C C   . GLU D 115 ? 1.0964 2.0721 2.0481 0.0781  -0.0727 -0.1268 115 GLU D C   
9773  O O   . GLU D 115 ? 1.0628 2.0477 2.0235 0.0818  -0.0669 -0.1327 115 GLU D O   
9774  C CB  . GLU D 115 ? 1.0291 2.0114 1.9568 0.0663  -0.0535 -0.1172 115 GLU D CB  
9775  C CG  . GLU D 115 ? 1.0350 2.0116 1.9416 0.0621  -0.0493 -0.1113 115 GLU D CG  
9776  C CD  . GLU D 115 ? 1.0831 2.0724 1.9857 0.0550  -0.0343 -0.1073 115 GLU D CD  
9777  O OE1 . GLU D 115 ? 1.1088 2.1109 2.0259 0.0514  -0.0278 -0.1073 115 GLU D OE1 
9778  O OE2 . GLU D 115 ? 1.0664 2.0530 1.9513 0.0530  -0.0291 -0.1040 115 GLU D OE2 
9779  N N   . TYR D 116 ? 1.0319 2.0028 1.9917 0.0771  -0.0832 -0.1248 116 TYR D N   
9780  C CA  . TYR D 116 ? 1.0143 1.9898 1.9942 0.0803  -0.0897 -0.1289 116 TYR D CA  
9781  C C   . TYR D 116 ? 1.0577 2.0525 2.0536 0.0771  -0.0776 -0.1309 116 TYR D C   
9782  O O   . TYR D 116 ? 1.0428 2.0442 2.0472 0.0827  -0.0745 -0.1375 116 TYR D O   
9783  C CB  . TYR D 116 ? 1.0099 1.9761 1.9913 0.0908  -0.0998 -0.1356 116 TYR D CB  
9784  C CG  . TYR D 116 ? 0.9436 1.8903 1.9106 0.0946  -0.1128 -0.1339 116 TYR D CG  
9785  C CD1 . TYR D 116 ? 0.9331 1.8706 1.9032 0.0948  -0.1262 -0.1319 116 TYR D CD1 
9786  C CD2 . TYR D 116 ? 0.9094 1.8470 1.8597 0.0978  -0.1118 -0.1344 116 TYR D CD2 
9787  C CE1 . TYR D 116 ? 0.8822 1.8017 1.8386 0.0984  -0.1381 -0.1302 116 TYR D CE1 
9788  C CE2 . TYR D 116 ? 0.8806 1.8007 1.8181 0.1012  -0.1235 -0.1326 116 TYR D CE2 
9789  C CZ  . TYR D 116 ? 0.8470 1.7580 1.7874 0.1016  -0.1365 -0.1305 116 TYR D CZ  
9790  O OH  . TYR D 116 ? 0.8159 1.7093 1.7429 0.1051  -0.1481 -0.1287 116 TYR D OH  
9791  N N   . PRO D 117 ? 1.0754 2.0799 2.0762 0.0681  -0.0703 -0.1255 117 PRO D N   
9792  C CA  . PRO D 117 ? 1.0861 2.1092 2.1043 0.0648  -0.0596 -0.1271 117 PRO D CA  
9793  C C   . PRO D 117 ? 1.2002 2.2277 2.2392 0.0655  -0.0679 -0.1293 117 PRO D C   
9794  O O   . PRO D 117 ? 1.1900 2.2251 2.2391 0.0583  -0.0660 -0.1253 117 PRO D O   
9795  C CB  . PRO D 117 ? 1.0045 2.0340 2.0160 0.0547  -0.0485 -0.1196 117 PRO D CB  
9796  C CG  . PRO D 117 ? 1.0268 2.0421 2.0275 0.0519  -0.0583 -0.1141 117 PRO D CG  
9797  C CD  . PRO D 117 ? 1.0515 2.0507 2.0412 0.0604  -0.0702 -0.1176 117 PRO D CD  
9798  N N   . LEU D 118 ? 1.3895 2.4120 2.4353 0.0744  -0.0777 -0.1358 118 LEU D N   
9799  C CA  . LEU D 118 ? 1.4320 2.4564 2.4959 0.0762  -0.0879 -0.1382 118 LEU D CA  
9800  C C   . LEU D 118 ? 1.4452 2.4896 2.5304 0.0734  -0.0786 -0.1406 118 LEU D C   
9801  O O   . LEU D 118 ? 1.4304 2.4801 2.5310 0.0705  -0.0835 -0.1400 118 LEU D O   
9802  C CB  . LEU D 118 ? 1.4736 2.4866 2.5381 0.0869  -0.1009 -0.1444 118 LEU D CB  
9803  C CG  . LEU D 118 ? 1.5155 2.5080 2.5604 0.0907  -0.1118 -0.1425 118 LEU D CG  
9804  C CD1 . LEU D 118 ? 1.4287 2.4113 2.4763 0.1016  -0.1237 -0.1488 118 LEU D CD1 
9805  C CD2 . LEU D 118 ? 1.5944 2.5782 2.6344 0.0852  -0.1206 -0.1364 118 LEU D CD2 
9806  N N   . LYS D 119 ? 1.6032 2.6590 2.6898 0.0742  -0.0652 -0.1436 119 LYS D N   
9807  C CA  . LYS D 119 ? 1.6065 2.6816 2.7137 0.0723  -0.0560 -0.1465 119 LYS D CA  
9808  C C   . LYS D 119 ? 1.6047 2.6900 2.7186 0.0613  -0.0491 -0.1396 119 LYS D C   
9809  O O   . LYS D 119 ? 1.6081 2.7030 2.7412 0.0589  -0.0511 -0.1403 119 LYS D O   
9810  C CB  . LYS D 119 ? 1.6714 2.7558 2.7761 0.0753  -0.0427 -0.1511 119 LYS D CB  
9811  C CG  . LYS D 119 ? 1.6432 2.7190 2.7444 0.0863  -0.0491 -0.1589 119 LYS D CG  
9812  C CD  . LYS D 119 ? 1.6201 2.7106 2.7339 0.0906  -0.0392 -0.1666 119 LYS D CD  
9813  C CE  . LYS D 119 ? 1.6031 2.7077 2.7421 0.0899  -0.0396 -0.1691 119 LYS D CE  
9814  N NZ  . LYS D 119 ? 1.6025 2.6975 2.7504 0.0954  -0.0568 -0.1712 119 LYS D NZ  
9815  N N   . GLU D 120 ? 1.4261 2.5096 2.5247 0.0545  -0.0409 -0.1331 120 GLU D N   
9816  C CA  . GLU D 120 ? 1.3660 2.4585 2.4696 0.0438  -0.0333 -0.1260 120 GLU D CA  
9817  C C   . GLU D 120 ? 1.3151 2.3983 2.4197 0.0395  -0.0452 -0.1214 120 GLU D C   
9818  O O   . GLU D 120 ? 1.2362 2.3240 2.3426 0.0303  -0.0402 -0.1150 120 GLU D O   
9819  C CB  . GLU D 120 ? 1.3473 2.4406 2.4336 0.0386  -0.0203 -0.1208 120 GLU D CB  
9820  C CG  . GLU D 120 ? 1.3698 2.4737 2.4549 0.0418  -0.0073 -0.1254 120 GLU D CG  
9821  C CD  . GLU D 120 ? 1.3980 2.5028 2.4653 0.0365  0.0051  -0.1203 120 GLU D CD  
9822  O OE1 . GLU D 120 ? 1.3968 2.4937 2.4527 0.0306  0.0035  -0.1131 120 GLU D OE1 
9823  O OE2 . GLU D 120 ? 1.4384 2.5519 2.5028 0.0384  0.0164  -0.1238 120 GLU D OE2 
9824  N N   . MET D 121 ? 1.3603 2.4303 2.4636 0.0459  -0.0610 -0.1246 121 MET D N   
9825  C CA  . MET D 121 ? 1.3183 2.3803 2.4246 0.0425  -0.0733 -0.1216 121 MET D CA  
9826  C C   . MET D 121 ? 1.4336 2.5051 2.5635 0.0429  -0.0790 -0.1254 121 MET D C   
9827  O O   . MET D 121 ? 1.3862 2.4590 2.5241 0.0365  -0.0834 -0.1222 121 MET D O   
9828  C CB  . MET D 121 ? 1.2643 2.3056 2.3545 0.0489  -0.0877 -0.1225 121 MET D CB  
9829  C CG  . MET D 121 ? 1.2593 2.2900 2.3471 0.0448  -0.0995 -0.1186 121 MET D CG  
9830  S SD  . MET D 121 ? 1.3165 2.3233 2.3861 0.0530  -0.1167 -0.1201 121 MET D SD  
9831  C CE  . MET D 121 ? 1.1987 2.2011 2.2478 0.0564  -0.1068 -0.1196 121 MET D CE  
9832  N N   . LEU D 122 ? 1.6449 2.7233 2.7866 0.0503  -0.0791 -0.1324 122 LEU D N   
9833  C CA  . LEU D 122 ? 1.6537 2.7436 2.8194 0.0507  -0.0830 -0.1364 122 LEU D CA  
9834  C C   . LEU D 122 ? 1.6506 2.7591 2.8306 0.0411  -0.0699 -0.1329 122 LEU D C   
9835  O O   . LEU D 122 ? 1.6556 2.7705 2.8515 0.0364  -0.0741 -0.1322 122 LEU D O   
9836  C CB  . LEU D 122 ? 1.6910 2.7855 2.8661 0.0608  -0.0840 -0.1447 122 LEU D CB  
9837  C CG  . LEU D 122 ? 1.7737 2.8527 2.9449 0.0711  -0.1004 -0.1497 122 LEU D CG  
9838  C CD1 . LEU D 122 ? 1.7796 2.8411 2.9259 0.0748  -0.1032 -0.1480 122 LEU D CD1 
9839  C CD2 . LEU D 122 ? 1.7617 2.8497 2.9489 0.0795  -0.1003 -0.1581 122 LEU D CD2 
9840  N N   . GLU D 123 ? 1.3561 2.4735 2.5307 0.0379  -0.0538 -0.1307 123 GLU D N   
9841  C CA  . GLU D 123 ? 1.2593 2.3931 2.4448 0.0280  -0.0406 -0.1261 123 GLU D CA  
9842  C C   . GLU D 123 ? 1.2720 2.3995 2.4516 0.0187  -0.0432 -0.1183 123 GLU D C   
9843  O O   . GLU D 123 ? 1.2821 2.4204 2.4764 0.0107  -0.0397 -0.1152 123 GLU D O   
9844  C CB  . GLU D 123 ? 1.1559 2.2982 2.3335 0.0269  -0.0234 -0.1250 123 GLU D CB  
9845  C CG  . GLU D 123 ? 1.0718 2.2327 2.2625 0.0178  -0.0086 -0.1211 123 GLU D CG  
9846  C CD  . GLU D 123 ? 1.0441 2.2130 2.2261 0.0174  0.0081  -0.1207 123 GLU D CD  
9847  O OE1 . GLU D 123 ? 1.0331 2.1914 2.1953 0.0219  0.0084  -0.1214 123 GLU D OE1 
9848  O OE2 . GLU D 123 ? 1.0702 2.2563 2.2651 0.0124  0.0209  -0.1197 123 GLU D OE2 
9849  N N   . PHE D 124 ? 1.2860 2.3960 2.4445 0.0195  -0.0495 -0.1151 124 PHE D N   
9850  C CA  . PHE D 124 ? 1.2487 2.3507 2.4017 0.0118  -0.0545 -0.1088 124 PHE D CA  
9851  C C   . PHE D 124 ? 1.3456 2.4430 2.5108 0.0124  -0.0700 -0.1113 124 PHE D C   
9852  O O   . PHE D 124 ? 1.4039 2.4982 2.5704 0.0050  -0.0737 -0.1070 124 PHE D O   
9853  C CB  . PHE D 124 ? 1.2084 2.2931 2.3360 0.0133  -0.0574 -0.1054 124 PHE D CB  
9854  C CG  . PHE D 124 ? 1.1968 2.2737 2.3175 0.0052  -0.0605 -0.0987 124 PHE D CG  
9855  C CD1 . PHE D 124 ? 1.0874 2.1744 2.2126 -0.0050 -0.0487 -0.0924 124 PHE D CD1 
9856  C CD2 . PHE D 124 ? 1.2542 2.3134 2.3638 0.0077  -0.0750 -0.0986 124 PHE D CD2 
9857  C CE1 . PHE D 124 ? 1.0784 2.1579 2.1978 -0.0125 -0.0516 -0.0865 124 PHE D CE1 
9858  C CE2 . PHE D 124 ? 1.2281 2.2800 2.3317 0.0004  -0.0777 -0.0931 124 PHE D CE2 
9859  C CZ  . PHE D 124 ? 1.1719 2.2339 2.2808 -0.0097 -0.0661 -0.0871 124 PHE D CZ  
9860  N N   . HIS D 125 ? 1.3529 2.4497 2.5269 0.0210  -0.0792 -0.1185 125 HIS D N   
9861  C CA  . HIS D 125 ? 1.4181 2.5121 2.6053 0.0222  -0.0938 -0.1217 125 HIS D CA  
9862  C C   . HIS D 125 ? 1.4188 2.5321 2.6323 0.0192  -0.0894 -0.1245 125 HIS D C   
9863  O O   . HIS D 125 ? 1.4819 2.5976 2.7080 0.0141  -0.0960 -0.1241 125 HIS D O   
9864  C CB  . HIS D 125 ? 1.4355 2.5161 2.6168 0.0337  -0.1080 -0.1276 125 HIS D CB  
9865  C CG  . HIS D 125 ? 1.4582 2.5325 2.6488 0.0353  -0.1248 -0.1304 125 HIS D CG  
9866  N ND1 . HIS D 125 ? 1.4748 2.5344 2.6550 0.0321  -0.1357 -0.1272 125 HIS D ND1 
9867  C CD2 . HIS D 125 ? 1.4232 2.5037 2.6324 0.0398  -0.1327 -0.1364 125 HIS D CD2 
9868  C CE1 . HIS D 125 ? 1.3886 2.4454 2.5799 0.0346  -0.1497 -0.1310 125 HIS D CE1 
9869  N NE2 . HIS D 125 ? 1.3700 2.4394 2.5792 0.0392  -0.1483 -0.1365 125 HIS D NE2 
9870  N N   . LYS D 126 ? 1.3710 2.4985 2.5934 0.0223  -0.0782 -0.1278 126 LYS D N   
9871  C CA  . LYS D 126 ? 1.3758 2.5229 2.6236 0.0201  -0.0728 -0.1309 126 LYS D CA  
9872  C C   . LYS D 126 ? 1.4028 2.5646 2.6578 0.0087  -0.0576 -0.1248 126 LYS D C   
9873  O O   . LYS D 126 ? 1.3703 2.5505 2.6441 0.0068  -0.0482 -0.1267 126 LYS D O   
9874  C CB  . LYS D 126 ? 1.3095 2.4650 2.5643 0.0291  -0.0679 -0.1378 126 LYS D CB  
9875  C CG  . LYS D 126 ? 1.2803 2.4242 2.5341 0.0406  -0.0831 -0.1446 126 LYS D CG  
9876  C CD  . LYS D 126 ? 1.2020 2.3564 2.4661 0.0487  -0.0771 -0.1518 126 LYS D CD  
9877  C CE  . LYS D 126 ? 1.1848 2.3284 2.4502 0.0601  -0.0925 -0.1586 126 LYS D CE  
9878  N NZ  . LYS D 126 ? 1.0816 2.2361 2.3591 0.0680  -0.0869 -0.1661 126 LYS D NZ  
9879  N N   . SER D 127 ? 1.4750 2.6292 2.7158 0.0012  -0.0547 -0.1174 127 SER D N   
9880  C CA  . SER D 127 ? 1.5359 2.7023 2.7822 -0.0100 -0.0409 -0.1108 127 SER D CA  
9881  C C   . SER D 127 ? 1.6838 2.8486 2.9388 -0.0188 -0.0480 -0.1075 127 SER D C   
9882  O O   . SER D 127 ? 1.6605 2.8405 2.9350 -0.0257 -0.0423 -0.1066 127 SER D O   
9883  C CB  . SER D 127 ? 1.4926 2.6528 2.7169 -0.0128 -0.0304 -0.1046 127 SER D CB  
9884  O OG  . SER D 127 ? 1.5420 2.7137 2.7713 -0.0235 -0.0167 -0.0978 127 SER D OG  
9885  N N   . HIS D 128 ? 1.9901 3.1367 3.2313 -0.0186 -0.0604 -0.1059 128 HIS D N   
9886  C CA  . HIS D 128 ? 1.9948 3.1376 3.2429 -0.0263 -0.0686 -0.1037 128 HIS D CA  
9887  C C   . HIS D 128 ? 2.0085 3.1468 3.2681 -0.0213 -0.0858 -0.1103 128 HIS D C   
9888  O O   . HIS D 128 ? 2.0542 3.1924 3.3243 -0.0277 -0.0926 -0.1098 128 HIS D O   
9889  C CB  . HIS D 128 ? 1.9862 3.1118 3.2127 -0.0297 -0.0719 -0.0980 128 HIS D CB  
9890  C CG  . HIS D 128 ? 1.9797 3.0875 3.1856 -0.0201 -0.0812 -0.1003 128 HIS D CG  
9891  N ND1 . HIS D 128 ? 1.9835 3.0879 3.1912 -0.0095 -0.0904 -0.1073 128 HIS D ND1 
9892  C CD2 . HIS D 128 ? 1.9702 3.0628 3.1536 -0.0195 -0.0825 -0.0965 128 HIS D CD2 
9893  C CE1 . HIS D 128 ? 1.9781 3.0658 3.1651 -0.0030 -0.0970 -0.1075 128 HIS D CE1 
9894  N NE2 . HIS D 128 ? 1.9698 3.0503 3.1418 -0.0089 -0.0923 -0.1011 128 HIS D NE2 
9895  N N   . GLY D 129 ? 1.7709 2.9049 3.0288 -0.0102 -0.0932 -0.1165 129 GLY D N   
9896  C CA  . GLY D 129 ? 1.6075 2.7373 2.8762 -0.0049 -0.1096 -0.1227 129 GLY D CA  
9897  C C   . GLY D 129 ? 1.4814 2.5902 2.7359 -0.0034 -0.1261 -0.1224 129 GLY D C   
9898  O O   . GLY D 129 ? 1.3589 2.4652 2.6242 -0.0039 -0.1388 -0.1255 129 GLY D O   
9899  N N   . GLY D 130 ? 1.4853 2.5789 2.7160 -0.0017 -0.1263 -0.1188 130 GLY D N   
9900  C CA  . GLY D 130 ? 1.4022 2.4755 2.6181 0.0001  -0.1415 -0.1185 130 GLY D CA  
9901  C C   . GLY D 130 ? 1.2671 2.3309 2.4826 0.0110  -0.1573 -0.1249 130 GLY D C   
9902  O O   . GLY D 130 ? 1.2604 2.3326 2.4864 0.0177  -0.1565 -0.1298 130 GLY D O   
9903  N N   . GLU D 131 ? 1.2302 2.2755 2.4330 0.0128  -0.1720 -0.1249 131 GLU D N   
9904  C CA  . GLU D 131 ? 1.1249 2.1587 2.3248 0.0228  -0.1884 -0.1302 131 GLU D CA  
9905  C C   . GLU D 131 ? 1.2262 2.2435 2.4022 0.0309  -0.1918 -0.1294 131 GLU D C   
9906  O O   . GLU D 131 ? 1.1766 2.1909 2.3520 0.0406  -0.1971 -0.1337 131 GLU D O   
9907  C CB  . GLU D 131 ? 0.9740 1.9978 2.1761 0.0204  -0.2045 -0.1313 131 GLU D CB  
9908  C CG  . GLU D 131 ? 0.9537 1.9660 2.1535 0.0306  -0.2221 -0.1366 131 GLU D CG  
9909  C CD  . GLU D 131 ? 0.9259 1.9223 2.1183 0.0291  -0.2386 -0.1367 131 GLU D CD  
9910  O OE1 . GLU D 131 ? 0.9444 1.9380 2.1329 0.0202  -0.2364 -0.1329 131 GLU D OE1 
9911  O OE2 . GLU D 131 ? 0.9128 1.8992 2.1030 0.0368  -0.2541 -0.1407 131 GLU D OE2 
9912  N N   . ALA D 132 ? 1.4148 2.4214 2.5719 0.0271  -0.1888 -0.1242 132 ALA D N   
9913  C CA  . ALA D 132 ? 1.5412 2.5315 2.6752 0.0340  -0.1923 -0.1231 132 ALA D CA  
9914  C C   . ALA D 132 ? 1.8719 2.8648 2.9938 0.0296  -0.1768 -0.1178 132 ALA D C   
9915  O O   . ALA D 132 ? 1.8713 2.8713 2.9965 0.0201  -0.1677 -0.1135 132 ALA D O   
9916  C CB  . ALA D 132 ? 1.3922 2.3624 2.5118 0.0351  -0.2086 -0.1224 132 ALA D CB  
9917  N N   . SER D 133 ? 2.6269 3.6138 3.7346 0.0366  -0.1740 -0.1183 133 SER D N   
9918  C CA  . SER D 133 ? 2.6153 3.6045 3.7106 0.0336  -0.1596 -0.1139 133 SER D CA  
9919  C C   . SER D 133 ? 2.6108 3.5820 3.6827 0.0397  -0.1652 -0.1129 133 SER D C   
9920  O O   . SER D 133 ? 2.6165 3.5790 3.6842 0.0488  -0.1746 -0.1170 133 SER D O   
9921  C CB  . SER D 133 ? 2.6138 3.6195 3.7187 0.0353  -0.1456 -0.1158 133 SER D CB  
9922  O OG  . SER D 133 ? 2.6036 3.6118 3.6962 0.0320  -0.1317 -0.1115 133 SER D OG  
9923  N N   . ILE D 134 ? 1.9155 2.8812 2.9727 0.0345  -0.1595 -0.1076 134 ILE D N   
9924  C CA  . ILE D 134 ? 1.6851 2.6361 2.7201 0.0392  -0.1616 -0.1061 134 ILE D CA  
9925  C C   . ILE D 134 ? 1.5138 2.4724 2.5410 0.0353  -0.1449 -0.1023 134 ILE D C   
9926  O O   . ILE D 134 ? 1.5223 2.4953 2.5595 0.0282  -0.1329 -0.0998 134 ILE D O   
9927  C CB  . ILE D 134 ? 1.6072 2.5410 2.6290 0.0376  -0.1733 -0.1035 134 ILE D CB  
9928  C CG1 . ILE D 134 ? 1.5577 2.4955 2.5796 0.0270  -0.1655 -0.0980 134 ILE D CG1 
9929  C CG2 . ILE D 134 ? 1.7257 2.6524 2.7552 0.0407  -0.1900 -0.1072 134 ILE D CG2 
9930  C CD1 . ILE D 134 ? 1.5086 2.4296 2.5169 0.0252  -0.1754 -0.0955 134 ILE D CD1 
9931  N N   . MET D 135 ? 1.4117 2.3605 2.4207 0.0402  -0.1443 -0.1018 135 MET D N   
9932  C CA  . MET D 135 ? 1.3777 2.3314 2.3760 0.0371  -0.1299 -0.0982 135 MET D CA  
9933  C C   . MET D 135 ? 1.4071 2.3485 2.3877 0.0339  -0.1320 -0.0934 135 MET D C   
9934  O O   . MET D 135 ? 1.3970 2.3230 2.3682 0.0376  -0.1448 -0.0941 135 MET D O   
9935  C CB  . MET D 135 ? 1.2793 2.2333 2.2709 0.0450  -0.1259 -0.1019 135 MET D CB  
9936  C CG  . MET D 135 ? 1.2466 2.2150 2.2556 0.0477  -0.1204 -0.1066 135 MET D CG  
9937  S SD  . MET D 135 ? 1.4187 2.4081 2.4419 0.0376  -0.1037 -0.1031 135 MET D SD  
9938  C CE  . MET D 135 ? 1.5200 2.5101 2.5238 0.0350  -0.0894 -0.0988 135 MET D CE  
9939  N N   . VAL D 136 ? 1.4301 2.3785 2.4060 0.0269  -0.1192 -0.0885 136 VAL D N   
9940  C CA  . VAL D 136 ? 1.4208 2.3539 2.3753 0.0221  -0.1184 -0.0812 136 VAL D CA  
9941  C C   . VAL D 136 ? 1.4700 2.4026 2.4061 0.0211  -0.1052 -0.0769 136 VAL D C   
9942  O O   . VAL D 136 ? 1.6109 2.5626 2.5581 0.0193  -0.0933 -0.0782 136 VAL D O   
9943  C CB  . VAL D 136 ? 1.4826 2.4202 2.4475 0.0126  -0.1168 -0.0773 136 VAL D CB  
9944  C CG1 . VAL D 136 ? 1.5235 2.4433 2.4628 0.0073  -0.1135 -0.0685 136 VAL D CG1 
9945  C CG2 . VAL D 136 ? 1.4577 2.3932 2.4383 0.0135  -0.1315 -0.0816 136 VAL D CG2 
9946  N N   . THR D 137 ? 1.4550 2.3662 2.3630 0.0225  -0.1072 -0.0719 137 THR D N   
9947  C CA  . THR D 137 ? 1.3863 2.2948 2.2750 0.0216  -0.0960 -0.0675 137 THR D CA  
9948  C C   . THR D 137 ? 1.3816 2.2741 2.2494 0.0158  -0.0942 -0.0588 137 THR D C   
9949  O O   . THR D 137 ? 1.4379 2.3137 2.2974 0.0156  -0.1042 -0.0570 137 THR D O   
9950  C CB  . THR D 137 ? 1.3004 2.1989 2.1750 0.0301  -0.0992 -0.0707 137 THR D CB  
9951  O OG1 . THR D 137 ? 1.2606 2.1551 2.1152 0.0288  -0.0891 -0.0660 137 THR D OG1 
9952  C CG2 . THR D 137 ? 1.2938 2.1694 2.1547 0.0345  -0.1134 -0.0704 137 THR D CG2 
9953  N N   . LYS D 138 ? 1.2641 2.1620 2.1236 0.0111  -0.0816 -0.0536 138 LYS D N   
9954  C CA  . LYS D 138 ? 1.3047 2.1884 2.1446 0.0059  -0.0788 -0.0452 138 LYS D CA  
9955  C C   . LYS D 138 ? 1.3136 2.1770 2.1271 0.0107  -0.0822 -0.0432 138 LYS D C   
9956  O O   . LYS D 138 ? 1.2985 2.1634 2.1064 0.0161  -0.0801 -0.0462 138 LYS D O   
9957  C CB  . LYS D 138 ? 1.3202 2.2168 2.1604 -0.0005 -0.0644 -0.0400 138 LYS D CB  
9958  C CG  . LYS D 138 ? 1.2954 2.2040 2.1335 0.0029  -0.0552 -0.0426 138 LYS D CG  
9959  C CD  . LYS D 138 ? 1.2852 2.2009 2.1154 -0.0030 -0.0419 -0.0359 138 LYS D CD  
9960  C CE  . LYS D 138 ? 1.2913 2.2169 2.1165 0.0008  -0.0337 -0.0387 138 LYS D CE  
9961  N NZ  . LYS D 138 ? 1.3628 2.2727 2.1702 0.0078  -0.0397 -0.0409 138 LYS D NZ  
9962  N N   . VAL D 139 ? 1.3637 2.2082 2.1613 0.0087  -0.0873 -0.0382 139 VAL D N   
9963  C CA  . VAL D 139 ? 1.3651 2.1899 2.1373 0.0124  -0.0899 -0.0355 139 VAL D CA  
9964  C C   . VAL D 139 ? 1.3910 2.2063 2.1472 0.0068  -0.0843 -0.0273 139 VAL D C   
9965  O O   . VAL D 139 ? 1.3965 2.2134 2.1594 0.0007  -0.0834 -0.0240 139 VAL D O   
9966  C CB  . VAL D 139 ? 1.4471 2.2547 2.2133 0.0175  -0.1039 -0.0386 139 VAL D CB  
9967  C CG1 . VAL D 139 ? 1.4438 2.2595 2.2241 0.0241  -0.1096 -0.0464 139 VAL D CG1 
9968  C CG2 . VAL D 139 ? 1.4826 2.2843 2.2544 0.0132  -0.1109 -0.0372 139 VAL D CG2 
9969  N N   . ASP D 140 ? 1.3889 2.1942 2.1244 0.0089  -0.0806 -0.0242 140 ASP D N   
9970  C CA  . ASP D 140 ? 1.3727 2.1679 2.0921 0.0044  -0.0758 -0.0165 140 ASP D CA  
9971  C C   . ASP D 140 ? 1.4265 2.2012 2.1347 0.0043  -0.0851 -0.0147 140 ASP D C   
9972  O O   . ASP D 140 ? 1.4404 2.2081 2.1419 -0.0005 -0.0828 -0.0091 140 ASP D O   
9973  C CB  . ASP D 140 ? 1.3640 2.1558 2.0660 0.0068  -0.0693 -0.0142 140 ASP D CB  
9974  C CG  . ASP D 140 ? 1.3565 2.1680 2.0676 0.0071  -0.0601 -0.0164 140 ASP D CG  
9975  O OD1 . ASP D 140 ? 1.2942 2.1222 2.0224 0.0033  -0.0554 -0.0168 140 ASP D OD1 
9976  O OD2 . ASP D 140 ? 1.3873 2.1977 2.0885 0.0112  -0.0576 -0.0179 140 ASP D OD2 
9977  N N   . GLU D 141 ? 1.5346 2.2993 2.2404 0.0096  -0.0955 -0.0193 141 GLU D N   
9978  C CA  . GLU D 141 ? 1.6051 2.3500 2.2994 0.0102  -0.1051 -0.0184 141 GLU D CA  
9979  C C   . GLU D 141 ? 1.6369 2.3851 2.3483 0.0103  -0.1148 -0.0233 141 GLU D C   
9980  O O   . GLU D 141 ? 1.6762 2.4224 2.3909 0.0159  -0.1231 -0.0285 141 GLU D O   
9981  C CB  . GLU D 141 ? 1.6078 2.3364 2.2824 0.0163  -0.1096 -0.0191 141 GLU D CB  
9982  C CG  . GLU D 141 ? 1.6139 2.3372 2.2706 0.0162  -0.1011 -0.0143 141 GLU D CG  
9983  C CD  . GLU D 141 ? 1.6298 2.3388 2.2714 0.0125  -0.1000 -0.0084 141 GLU D CD  
9984  O OE1 . GLU D 141 ? 1.6204 2.3204 2.2625 0.0110  -0.1071 -0.0086 141 GLU D OE1 
9985  O OE2 . GLU D 141 ? 1.6805 2.3872 2.3100 0.0114  -0.0923 -0.0039 141 GLU D OE2 
9986  N N   . PRO D 142 ? 1.7028 2.4558 2.4260 0.0043  -0.1147 -0.0218 142 PRO D N   
9987  C CA  . PRO D 142 ? 1.7352 2.4912 2.4752 0.0042  -0.1248 -0.0267 142 PRO D CA  
9988  C C   . PRO D 142 ? 1.8743 2.6094 2.6011 0.0058  -0.1365 -0.0272 142 PRO D C   
9989  O O   . PRO D 142 ? 1.8114 2.5468 2.5494 0.0075  -0.1469 -0.0321 142 PRO D O   
9990  C CB  . PRO D 142 ? 1.6656 2.4349 2.4227 -0.0037 -0.1187 -0.0244 142 PRO D CB  
9991  C CG  . PRO D 142 ? 1.6531 2.4154 2.3942 -0.0077 -0.1096 -0.0169 142 PRO D CG  
9992  C CD  . PRO D 142 ? 1.6270 2.3850 2.3508 -0.0026 -0.1050 -0.0157 142 PRO D CD  
9993  N N   . SER D 143 ? 2.2651 2.9824 2.9686 0.0057  -0.1353 -0.0226 143 SER D N   
9994  C CA  . SER D 143 ? 2.2872 2.9844 2.9769 0.0071  -0.1458 -0.0231 143 SER D CA  
9995  C C   . SER D 143 ? 2.2939 2.9819 2.9752 0.0146  -0.1551 -0.0272 143 SER D C   
9996  O O   . SER D 143 ? 2.3031 2.9819 2.9838 0.0165  -0.1668 -0.0305 143 SER D O   
9997  C CB  . SER D 143 ? 2.3065 2.9880 2.9742 0.0048  -0.1409 -0.0171 143 SER D CB  
9998  O OG  . SER D 143 ? 2.3061 2.9836 2.9582 0.0084  -0.1349 -0.0148 143 SER D OG  
9999  N N   . LYS D 144 ? 1.9689 2.6588 2.6436 0.0190  -0.1505 -0.0271 144 LYS D N   
10000 C CA  . LYS D 144 ? 1.9223 2.6027 2.5884 0.0261  -0.1586 -0.0304 144 LYS D CA  
10001 C C   . LYS D 144 ? 1.8798 2.5719 2.5669 0.0295  -0.1666 -0.0368 144 LYS D C   
10002 O O   . LYS D 144 ? 1.8551 2.5385 2.5366 0.0355  -0.1754 -0.0398 144 LYS D O   
10003 C CB  . LYS D 144 ? 1.8330 2.5126 2.4873 0.0293  -0.1508 -0.0286 144 LYS D CB  
10004 C CG  . LYS D 144 ? 1.7475 2.4160 2.3814 0.0266  -0.1431 -0.0224 144 LYS D CG  
10005 C CD  . LYS D 144 ? 1.6201 2.2896 2.2446 0.0293  -0.1354 -0.0210 144 LYS D CD  
10006 C CE  . LYS D 144 ? 1.5788 2.2373 2.1938 0.0360  -0.1426 -0.0238 144 LYS D CE  
10007 N NZ  . LYS D 144 ? 1.5363 2.1954 2.1425 0.0383  -0.1352 -0.0227 144 LYS D NZ  
10008 N N   . TYR D 145 ? 1.8398 2.5510 2.5509 0.0257  -0.1638 -0.0389 145 TYR D N   
10009 C CA  . TYR D 145 ? 1.7739 2.4989 2.5080 0.0285  -0.1704 -0.0453 145 TYR D CA  
10010 C C   . TYR D 145 ? 1.7821 2.5115 2.5319 0.0240  -0.1769 -0.0471 145 TYR D C   
10011 O O   . TYR D 145 ? 1.7664 2.4880 2.5092 0.0185  -0.1758 -0.0435 145 TYR D O   
10012 C CB  . TYR D 145 ? 1.7454 2.4925 2.4969 0.0284  -0.1602 -0.0470 145 TYR D CB  
10013 C CG  . TYR D 145 ? 1.8148 2.5592 2.5519 0.0319  -0.1525 -0.0453 145 TYR D CG  
10014 C CD1 . TYR D 145 ? 1.8950 2.6232 2.6149 0.0383  -0.1587 -0.0459 145 TYR D CD1 
10015 C CD2 . TYR D 145 ? 1.8328 2.5906 2.5733 0.0287  -0.1392 -0.0429 145 TYR D CD2 
10016 C CE1 . TYR D 145 ? 1.9771 2.7029 2.6848 0.0410  -0.1518 -0.0445 145 TYR D CE1 
10017 C CE2 . TYR D 145 ? 1.9149 2.6705 2.6425 0.0317  -0.1326 -0.0417 145 TYR D CE2 
10018 C CZ  . TYR D 145 ? 1.9582 2.6979 2.6700 0.0377  -0.1389 -0.0426 145 TYR D CZ  
10019 O OH  . TYR D 145 ? 1.9330 2.6705 2.6329 0.0404  -0.1324 -0.0417 145 TYR D OH  
10020 N N   . GLY D 146 ? 1.6708 2.4128 2.4429 0.0263  -0.1839 -0.0531 146 GLY D N   
10021 C CA  . GLY D 146 ? 1.5643 2.3140 2.3558 0.0218  -0.1897 -0.0556 146 GLY D CA  
10022 C C   . GLY D 146 ? 1.5837 2.3567 2.3986 0.0158  -0.1787 -0.0555 146 GLY D C   
10023 O O   . GLY D 146 ? 1.6339 2.4244 2.4658 0.0183  -0.1748 -0.0590 146 GLY D O   
10024 N N   . VAL D 147 ? 1.5746 2.3477 2.3903 0.0080  -0.1735 -0.0514 147 VAL D N   
10025 C CA  . VAL D 147 ? 1.6510 2.4443 2.4855 0.0016  -0.1615 -0.0497 147 VAL D CA  
10026 C C   . VAL D 147 ? 1.7502 2.5601 2.6149 -0.0009 -0.1668 -0.0551 147 VAL D C   
10027 O O   . VAL D 147 ? 1.7299 2.5327 2.5988 -0.0017 -0.1785 -0.0577 147 VAL D O   
10028 C CB  . VAL D 147 ? 1.6048 2.3904 2.4275 -0.0058 -0.1536 -0.0425 147 VAL D CB  
10029 C CG1 . VAL D 147 ? 1.6989 2.5047 2.5390 -0.0124 -0.1406 -0.0400 147 VAL D CG1 
10030 C CG2 . VAL D 147 ? 1.5946 2.3633 2.3879 -0.0029 -0.1494 -0.0376 147 VAL D CG2 
10031 N N   . VAL D 148 ? 2.1460 2.9787 3.0320 -0.0023 -0.1582 -0.0570 148 VAL D N   
10032 C CA  . VAL D 148 ? 2.1327 2.9847 3.0501 -0.0055 -0.1606 -0.0618 148 VAL D CA  
10033 C C   . VAL D 148 ? 2.1297 2.9924 3.0572 -0.0153 -0.1491 -0.0570 148 VAL D C   
10034 O O   . VAL D 148 ? 2.1219 2.9937 3.0471 -0.0175 -0.1354 -0.0532 148 VAL D O   
10035 C CB  . VAL D 148 ? 2.1366 3.0077 3.0728 0.0002  -0.1590 -0.0679 148 VAL D CB  
10036 C CG1 . VAL D 148 ? 2.1053 2.9982 3.0755 -0.0037 -0.1601 -0.0728 148 VAL D CG1 
10037 C CG2 . VAL D 148 ? 2.1200 2.9792 3.0462 0.0100  -0.1711 -0.0723 148 VAL D CG2 
10038 N N   . VAL D 149 ? 1.8208 2.6820 2.7591 -0.0214 -0.1546 -0.0571 149 VAL D N   
10039 C CA  . VAL D 149 ? 1.7120 2.5804 2.6591 -0.0313 -0.1448 -0.0520 149 VAL D CA  
10040 C C   . VAL D 149 ? 1.6931 2.5878 2.6743 -0.0349 -0.1412 -0.0562 149 VAL D C   
10041 O O   . VAL D 149 ? 1.7735 2.6732 2.7747 -0.0371 -0.1502 -0.0608 149 VAL D O   
10042 C CB  . VAL D 149 ? 1.6104 2.4612 2.5491 -0.0364 -0.1520 -0.0495 149 VAL D CB  
10043 C CG1 . VAL D 149 ? 1.6773 2.5061 2.5834 -0.0352 -0.1492 -0.0431 149 VAL D CG1 
10044 C CG2 . VAL D 149 ? 1.6304 2.4739 2.5748 -0.0326 -0.1693 -0.0563 149 VAL D CG2 
10045 N N   . MET D 150 ? 1.5291 2.4409 2.5172 -0.0355 -0.1278 -0.0549 150 MET D N   
10046 C CA  . MET D 150 ? 1.5148 2.4530 2.5342 -0.0391 -0.1215 -0.0583 150 MET D CA  
10047 C C   . MET D 150 ? 1.4277 2.3744 2.4512 -0.0490 -0.1070 -0.0512 150 MET D C   
10048 O O   . MET D 150 ? 1.4154 2.3495 2.4165 -0.0515 -0.1004 -0.0438 150 MET D O   
10049 C CB  . MET D 150 ? 1.5628 2.5156 2.5882 -0.0317 -0.1171 -0.0632 150 MET D CB  
10050 C CG  . MET D 150 ? 1.5064 2.4538 2.5074 -0.0289 -0.1065 -0.0584 150 MET D CG  
10051 S SD  . MET D 150 ? 1.5634 2.5239 2.5687 -0.0192 -0.1036 -0.0651 150 MET D SD  
10052 C CE  . MET D 150 ? 1.5264 2.5155 2.5604 -0.0246 -0.0911 -0.0665 150 MET D CE  
10053 N N   . GLU D 151 ? 1.3738 2.3423 2.4266 -0.0546 -0.1020 -0.0535 151 GLU D N   
10054 C CA  . GLU D 151 ? 1.3096 2.2890 2.3688 -0.0640 -0.0872 -0.0469 151 GLU D CA  
10055 C C   . GLU D 151 ? 1.3093 2.3057 2.3690 -0.0618 -0.0732 -0.0464 151 GLU D C   
10056 O O   . GLU D 151 ? 1.3104 2.3176 2.3785 -0.0550 -0.0744 -0.0528 151 GLU D O   
10057 C CB  . GLU D 151 ? 1.2367 2.2309 2.3272 -0.0722 -0.0879 -0.0489 151 GLU D CB  
10058 C CG  . GLU D 151 ? 1.2459 2.2593 2.3535 -0.0708 -0.0834 -0.0532 151 GLU D CG  
10059 C CD  . GLU D 151 ? 1.3163 2.3259 2.4275 -0.0625 -0.0975 -0.0612 151 GLU D CD  
10060 O OE1 . GLU D 151 ? 1.3728 2.3685 2.4825 -0.0614 -0.1119 -0.0638 151 GLU D OE1 
10061 O OE2 . GLU D 151 ? 1.3275 2.3476 2.4430 -0.0568 -0.0943 -0.0647 151 GLU D OE2 
10062 N N   . GLU D 152 ? 1.3024 2.2984 2.3494 -0.0671 -0.0600 -0.0380 152 GLU D N   
10063 C CA  . GLU D 152 ? 1.2519 2.2620 2.2952 -0.0656 -0.0460 -0.0367 152 GLU D CA  
10064 C C   . GLU D 152 ? 1.1796 2.2165 2.2510 -0.0717 -0.0350 -0.0379 152 GLU D C   
10065 O O   . GLU D 152 ? 1.1730 2.2198 2.2400 -0.0752 -0.0206 -0.0329 152 GLU D O   
10066 C CB  . GLU D 152 ? 1.2279 2.2246 2.2429 -0.0679 -0.0375 -0.0270 152 GLU D CB  
10067 N N   . SER D 153 ? 1.1607 2.2028 2.2507 -0.0728 -0.0411 -0.0418 153 SER D N   
10068 C CA  . SER D 153 ? 1.1716 2.2321 2.2797 -0.0784 -0.0308 -0.0407 153 SER D CA  
10069 C C   . SER D 153 ? 1.1732 2.2420 2.2927 -0.0716 -0.0350 -0.0479 153 SER D C   
10070 O O   . SER D 153 ? 1.1534 2.2375 2.2804 -0.0717 -0.0239 -0.0478 153 SER D O   
10071 C CB  . SER D 153 ? 1.1699 2.2316 2.2935 -0.0892 -0.0315 -0.0374 153 SER D CB  
10072 O OG  . SER D 153 ? 1.1737 2.2255 2.3045 -0.0875 -0.0477 -0.0427 153 SER D OG  
10073 N N   . THR D 154 ? 1.2131 2.2720 2.3342 -0.0657 -0.0507 -0.0541 154 THR D N   
10074 C CA  . THR D 154 ? 1.1902 2.2558 2.3227 -0.0589 -0.0561 -0.0612 154 THR D CA  
10075 C C   . THR D 154 ? 1.2244 2.2773 2.3433 -0.0474 -0.0674 -0.0667 154 THR D C   
10076 O O   . THR D 154 ? 1.2034 2.2623 2.3240 -0.0402 -0.0657 -0.0710 154 THR D O   
10077 C CB  . THR D 154 ? 1.1044 2.1731 2.2571 -0.0634 -0.0648 -0.0642 154 THR D CB  
10078 O OG1 . THR D 154 ? 1.1182 2.1698 2.2648 -0.0648 -0.0780 -0.0644 154 THR D OG1 
10079 C CG2 . THR D 154 ? 1.0591 2.1433 2.2280 -0.0744 -0.0525 -0.0596 154 THR D CG2 
10080 N N   . GLY D 155 ? 1.2820 2.3171 2.3878 -0.0455 -0.0787 -0.0667 155 GLY D N   
10081 C CA  . GLY D 155 ? 1.3253 2.3473 2.4166 -0.0350 -0.0891 -0.0711 155 GLY D CA  
10082 C C   . GLY D 155 ? 1.4382 2.4481 2.5326 -0.0315 -0.1072 -0.0759 155 GLY D C   
10083 O O   . GLY D 155 ? 1.5308 2.5334 2.6193 -0.0223 -0.1165 -0.0808 155 GLY D O   
10084 N N   . ARG D 156 ? 1.4139 2.4210 2.5171 -0.0389 -0.1124 -0.0745 156 ARG D N   
10085 C CA  . ARG D 156 ? 1.6154 2.6108 2.7216 -0.0363 -0.1299 -0.0791 156 ARG D CA  
10086 C C   . ARG D 156 ? 1.7752 2.7506 2.8630 -0.0353 -0.1388 -0.0773 156 ARG D C   
10087 O O   . ARG D 156 ? 1.6371 2.6091 2.7181 -0.0414 -0.1323 -0.0717 156 ARG D O   
10088 C CB  . ARG D 156 ? 1.5543 2.5575 2.6813 -0.0448 -0.1316 -0.0795 156 ARG D CB  
10089 C CG  . ARG D 156 ? 1.5791 2.5735 2.7123 -0.0419 -0.1495 -0.0852 156 ARG D CG  
10090 C CD  . ARG D 156 ? 1.4622 2.4652 2.6166 -0.0509 -0.1503 -0.0857 156 ARG D CD  
10091 N NE  . ARG D 156 ? 1.4482 2.4725 2.6202 -0.0544 -0.1372 -0.0853 156 ARG D NE  
10092 C CZ  . ARG D 156 ? 1.4597 2.4954 2.6517 -0.0630 -0.1339 -0.0850 156 ARG D CZ  
10093 N NH1 . ARG D 156 ? 1.3994 2.4269 2.5967 -0.0691 -0.1430 -0.0853 156 ARG D NH1 
10094 N NH2 . ARG D 156 ? 1.5056 2.5609 2.7126 -0.0656 -0.1215 -0.0845 156 ARG D NH2 
10095 N N   . VAL D 157 ? 2.4554 3.4176 3.5353 -0.0274 -0.1539 -0.0819 157 VAL D N   
10096 C CA  . VAL D 157 ? 2.4532 3.3958 3.5151 -0.0252 -0.1635 -0.0808 157 VAL D CA  
10097 C C   . VAL D 157 ? 2.4623 3.3964 3.5312 -0.0296 -0.1763 -0.0824 157 VAL D C   
10098 O O   . VAL D 157 ? 2.4711 3.4129 3.5574 -0.0320 -0.1805 -0.0857 157 VAL D O   
10099 C CB  . VAL D 157 ? 2.4530 3.3848 3.4994 -0.0137 -0.1722 -0.0844 157 VAL D CB  
10100 C CG1 . VAL D 157 ? 2.4477 3.3910 3.4934 -0.0090 -0.1608 -0.0849 157 VAL D CG1 
10101 C CG2 . VAL D 157 ? 2.4648 3.3901 3.5167 -0.0086 -0.1889 -0.0903 157 VAL D CG2 
10102 N N   . GLU D 158 ? 2.0353 2.9490 3.0838 -0.0308 -0.1817 -0.0789 158 GLU D N   
10103 C CA  . GLU D 158 ? 1.9758 2.8793 3.0276 -0.0360 -0.1923 -0.0796 158 GLU D CA  
10104 C C   . GLU D 158 ? 1.9203 2.7980 2.9464 -0.0300 -0.2069 -0.0806 158 GLU D C   
10105 O O   . GLU D 158 ? 1.8928 2.7671 2.9277 -0.0285 -0.2217 -0.0860 158 GLU D O   
10106 C CB  . GLU D 158 ? 2.0254 2.9258 3.0735 -0.0465 -0.1816 -0.0723 158 GLU D CB  
10107 C CG  . GLU D 158 ? 2.0358 2.9610 3.1089 -0.0536 -0.1672 -0.0707 158 GLU D CG  
10108 C CD  . GLU D 158 ? 2.1647 3.0851 3.2326 -0.0638 -0.1569 -0.0628 158 GLU D CD  
10109 O OE1 . GLU D 158 ? 2.1959 3.0937 3.2392 -0.0646 -0.1600 -0.0584 158 GLU D OE1 
10110 O OE2 . GLU D 158 ? 2.1756 3.1149 3.2642 -0.0709 -0.1456 -0.0608 158 GLU D OE2 
10111 N N   . LYS D 159 ? 1.8413 2.7010 2.8359 -0.0266 -0.2028 -0.0754 159 LYS D N   
10112 C CA  . LYS D 159 ? 1.8030 2.6368 2.7704 -0.0220 -0.2146 -0.0752 159 LYS D CA  
10113 C C   . LYS D 159 ? 1.8648 2.6881 2.8066 -0.0142 -0.2109 -0.0726 159 LYS D C   
10114 O O   . LYS D 159 ? 1.8276 2.6620 2.7707 -0.0134 -0.1985 -0.0703 159 LYS D O   
10115 C CB  . LYS D 159 ? 1.7222 2.5396 2.6753 -0.0293 -0.2138 -0.0703 159 LYS D CB  
10116 C CG  . LYS D 159 ? 1.6675 2.4622 2.6029 -0.0266 -0.2293 -0.0725 159 LYS D CG  
10117 C CD  . LYS D 159 ? 1.5826 2.3850 2.5410 -0.0260 -0.2441 -0.0803 159 LYS D CD  
10118 C CE  . LYS D 159 ? 1.4530 2.2327 2.3932 -0.0240 -0.2596 -0.0826 159 LYS D CE  
10119 N NZ  . LYS D 159 ? 1.6260 2.3870 2.5358 -0.0151 -0.2641 -0.0815 159 LYS D NZ  
10120 N N   . PHE D 160 ? 2.1439 2.9454 3.0621 -0.0086 -0.2219 -0.0731 160 PHE D N   
10121 C CA  . PHE D 160 ? 2.1554 2.9436 3.0472 -0.0014 -0.2198 -0.0705 160 PHE D CA  
10122 C C   . PHE D 160 ? 2.1671 2.9320 3.0289 -0.0036 -0.2183 -0.0647 160 PHE D C   
10123 O O   . PHE D 160 ? 2.1827 2.9322 3.0349 -0.0042 -0.2290 -0.0658 160 PHE D O   
10124 C CB  . PHE D 160 ? 2.2004 2.9833 3.0902 0.0080  -0.2336 -0.0760 160 PHE D CB  
10125 C CG  . PHE D 160 ? 2.2387 3.0066 3.1226 0.0089  -0.2501 -0.0791 160 PHE D CG  
10126 C CD1 . PHE D 160 ? 2.2564 2.9996 3.1097 0.0134  -0.2573 -0.0772 160 PHE D CD1 
10127 C CD2 . PHE D 160 ? 2.1736 2.9522 3.0826 0.0052  -0.2585 -0.0840 160 PHE D CD2 
10128 C CE1 . PHE D 160 ? 2.2287 2.9578 3.0752 0.0144  -0.2725 -0.0801 160 PHE D CE1 
10129 C CE2 . PHE D 160 ? 2.1669 2.9317 3.0700 0.0061  -0.2742 -0.0872 160 PHE D CE2 
10130 C CZ  . PHE D 160 ? 2.1949 2.9347 3.0661 0.0108  -0.2812 -0.0853 160 PHE D CZ  
10131 N N   . VAL D 161 ? 1.8426 2.6055 2.6899 -0.0048 -0.2049 -0.0587 161 VAL D N   
10132 C CA  . VAL D 161 ? 1.7470 2.4898 2.5672 -0.0070 -0.2014 -0.0528 161 VAL D CA  
10133 C C   . VAL D 161 ? 1.7205 2.4522 2.5166 -0.0001 -0.1985 -0.0505 161 VAL D C   
10134 O O   . VAL D 161 ? 1.6417 2.3820 2.4365 0.0002  -0.1867 -0.0475 161 VAL D O   
10135 C CB  . VAL D 161 ? 1.6189 2.3685 2.4438 -0.0154 -0.1881 -0.0472 161 VAL D CB  
10136 C CG1 . VAL D 161 ? 1.6464 2.3747 2.4441 -0.0172 -0.1855 -0.0416 161 VAL D CG1 
10137 C CG2 . VAL D 161 ? 1.6260 2.3883 2.4774 -0.0226 -0.1902 -0.0496 161 VAL D CG2 
10138 N N   . GLU D 162 ? 1.7869 2.4995 2.5635 0.0053  -0.2093 -0.0519 162 GLU D N   
10139 C CA  . GLU D 162 ? 1.8225 2.5223 2.5748 0.0115  -0.2073 -0.0495 162 GLU D CA  
10140 C C   . GLU D 162 ? 1.8579 2.5401 2.5850 0.0087  -0.2016 -0.0435 162 GLU D C   
10141 O O   . GLU D 162 ? 1.8543 2.5251 2.5750 0.0051  -0.2063 -0.0430 162 GLU D O   
10142 C CB  . GLU D 162 ? 1.8314 2.5195 2.5754 0.0190  -0.2217 -0.0538 162 GLU D CB  
10143 C CG  . GLU D 162 ? 1.8773 2.5458 2.6065 0.0186  -0.2333 -0.0545 162 GLU D CG  
10144 C CD  . GLU D 162 ? 1.9091 2.5858 2.6599 0.0140  -0.2413 -0.0588 162 GLU D CD  
10145 O OE1 . GLU D 162 ? 1.8706 2.5687 2.6490 0.0114  -0.2382 -0.0612 162 GLU D OE1 
10146 O OE2 . GLU D 162 ? 1.9762 2.6380 2.7163 0.0129  -0.2506 -0.0598 162 GLU D OE2 
10147 N N   . LYS D 163 ? 1.7862 2.4666 2.4994 0.0104  -0.1914 -0.0393 163 LYS D N   
10148 C CA  . LYS D 163 ? 1.7547 2.4207 2.4452 0.0082  -0.1842 -0.0334 163 LYS D CA  
10149 C C   . LYS D 163 ? 1.7211 2.3887 2.4181 0.0003  -0.1800 -0.0307 163 LYS D C   
10150 O O   . LYS D 163 ? 1.6661 2.3185 2.3525 -0.0015 -0.1859 -0.0305 163 LYS D O   
10151 C CB  . LYS D 163 ? 1.7103 2.3528 2.3752 0.0127  -0.1929 -0.0335 163 LYS D CB  
10152 C CG  . LYS D 163 ? 1.6811 2.3081 2.3214 0.0115  -0.1856 -0.0279 163 LYS D CG  
10153 C CD  . LYS D 163 ? 1.7583 2.3934 2.3958 0.0118  -0.1726 -0.0238 163 LYS D CD  
10154 C CE  . LYS D 163 ? 1.6678 2.2894 2.2840 0.0101  -0.1653 -0.0182 163 LYS D CE  
10155 N NZ  . LYS D 163 ? 1.6230 2.2430 2.2429 0.0036  -0.1630 -0.0160 163 LYS D NZ  
10156 N N   . PRO D 164 ? 1.7201 2.4055 2.4345 -0.0047 -0.1699 -0.0286 164 PRO D N   
10157 C CA  . PRO D 164 ? 1.7288 2.4150 2.4491 -0.0125 -0.1652 -0.0252 164 PRO D CA  
10158 C C   . PRO D 164 ? 1.8099 2.4843 2.5090 -0.0138 -0.1562 -0.0186 164 PRO D C   
10159 O O   . PRO D 164 ? 1.8509 2.5312 2.5450 -0.0126 -0.1464 -0.0151 164 PRO D O   
10160 C CB  . PRO D 164 ? 1.7104 2.4210 2.4568 -0.0166 -0.1573 -0.0252 164 PRO D CB  
10161 C CG  . PRO D 164 ? 1.6469 2.3692 2.4025 -0.0106 -0.1597 -0.0299 164 PRO D CG  
10162 C CD  . PRO D 164 ? 1.7162 2.4224 2.4475 -0.0035 -0.1632 -0.0298 164 PRO D CD  
10163 N N   . LYS D 165 ? 1.8941 2.5518 2.5810 -0.0162 -0.1598 -0.0171 165 LYS D N   
10164 C CA  . LYS D 165 ? 1.9540 2.6006 2.6224 -0.0176 -0.1515 -0.0110 165 LYS D CA  
10165 C C   . LYS D 165 ? 1.9754 2.6349 2.6562 -0.0240 -0.1400 -0.0059 165 LYS D C   
10166 O O   . LYS D 165 ? 1.9805 2.6401 2.6512 -0.0239 -0.1302 -0.0006 165 LYS D O   
10167 C CB  . LYS D 165 ? 1.9364 2.5620 2.5894 -0.0183 -0.1583 -0.0114 165 LYS D CB  
10168 C CG  . LYS D 165 ? 1.8859 2.4955 2.5190 -0.0116 -0.1671 -0.0146 165 LYS D CG  
10169 C CD  . LYS D 165 ? 1.8444 2.4326 2.4587 -0.0122 -0.1715 -0.0143 165 LYS D CD  
10170 C CE  . LYS D 165 ? 1.8241 2.4040 2.4218 -0.0127 -0.1611 -0.0083 165 LYS D CE  
10171 N NZ  . LYS D 165 ? 1.7412 2.3083 2.3329 -0.0168 -0.1615 -0.0070 165 LYS D NZ  
10172 N N   . LEU D 166 ? 1.9786 2.6492 2.6812 -0.0296 -0.1411 -0.0072 166 LEU D N   
10173 C CA  . LEU D 166 ? 1.9810 2.6662 2.6979 -0.0358 -0.1303 -0.0025 166 LEU D CA  
10174 C C   . LEU D 166 ? 1.9548 2.6627 2.6918 -0.0353 -0.1269 -0.0050 166 LEU D C   
10175 O O   . LEU D 166 ? 1.8939 2.6062 2.6372 -0.0308 -0.1343 -0.0109 166 LEU D O   
10176 C CB  . LEU D 166 ? 2.0116 2.6943 2.7401 -0.0431 -0.1324 -0.0018 166 LEU D CB  
10177 C CG  . LEU D 166 ? 1.9939 2.6713 2.7162 -0.0483 -0.1231 0.0057  166 LEU D CG  
10178 C CD1 . LEU D 166 ? 2.0149 2.6702 2.7113 -0.0450 -0.1248 0.0077  166 LEU D CD1 
10179 C CD2 . LEU D 166 ? 1.9464 2.6270 2.6868 -0.0564 -0.1237 0.0064  166 LEU D CD2 
10180 N N   . TYR D 167 ? 1.9013 2.6234 2.6482 -0.0399 -0.1156 -0.0004 167 TYR D N   
10181 C CA  . TYR D 167 ? 1.8389 2.5830 2.6032 -0.0395 -0.1102 -0.0023 167 TYR D CA  
10182 C C   . TYR D 167 ? 1.9150 2.6723 2.7060 -0.0439 -0.1145 -0.0065 167 TYR D C   
10183 O O   . TYR D 167 ? 1.8683 2.6292 2.6706 -0.0513 -0.1110 -0.0034 167 TYR D O   
10184 C CB  . TYR D 167 ? 1.6872 2.4412 2.4498 -0.0426 -0.0961 0.0045  167 TYR D CB  
10185 C CG  . TYR D 167 ? 1.6158 2.3932 2.3961 -0.0427 -0.0895 0.0025  167 TYR D CG  
10186 C CD1 . TYR D 167 ? 1.6265 2.4096 2.4021 -0.0360 -0.0887 -0.0008 167 TYR D CD1 
10187 C CD2 . TYR D 167 ? 1.5536 2.3471 2.3552 -0.0496 -0.0837 0.0039  167 TYR D CD2 
10188 C CE1 . TYR D 167 ? 1.6072 2.4114 2.3988 -0.0358 -0.0824 -0.0032 167 TYR D CE1 
10189 C CE2 . TYR D 167 ? 1.5260 2.3413 2.3436 -0.0496 -0.0770 0.0019  167 TYR D CE2 
10190 C CZ  . TYR D 167 ? 1.5376 2.3582 2.3500 -0.0426 -0.0764 -0.0019 167 TYR D CZ  
10191 O OH  . TYR D 167 ? 1.5369 2.3790 2.3649 -0.0423 -0.0696 -0.0045 167 TYR D OH  
10192 N N   . VAL D 168 ? 2.3268 3.0914 3.1287 -0.0394 -0.1222 -0.0136 168 VAL D N   
10193 C CA  . VAL D 168 ? 2.3162 3.0976 3.1463 -0.0428 -0.1253 -0.0183 168 VAL D CA  
10194 C C   . VAL D 168 ? 2.2918 3.0948 3.1369 -0.0401 -0.1195 -0.0211 168 VAL D C   
10195 O O   . VAL D 168 ? 2.2804 3.1007 3.1510 -0.0431 -0.1198 -0.0248 168 VAL D O   
10196 C CB  . VAL D 168 ? 2.3272 3.1000 3.1617 -0.0402 -0.1410 -0.0250 168 VAL D CB  
10197 C CG1 . VAL D 168 ? 2.3488 3.1030 3.1732 -0.0444 -0.1462 -0.0229 168 VAL D CG1 
10198 C CG2 . VAL D 168 ? 2.3269 3.0909 3.1463 -0.0309 -0.1484 -0.0289 168 VAL D CG2 
10199 N N   . GLY D 169 ? 1.8859 2.6888 2.7167 -0.0346 -0.1142 -0.0200 169 GLY D N   
10200 C CA  . GLY D 169 ? 1.8014 2.6238 2.6445 -0.0317 -0.1081 -0.0230 169 GLY D CA  
10201 C C   . GLY D 169 ? 1.8335 2.6491 2.6567 -0.0243 -0.1066 -0.0231 169 GLY D C   
10202 O O   . GLY D 169 ? 1.8318 2.6279 2.6326 -0.0212 -0.1109 -0.0211 169 GLY D O   
10203 N N   . ASN D 170 ? 1.7316 2.5641 2.5639 -0.0216 -0.1001 -0.0256 170 ASN D N   
10204 C CA  . ASN D 170 ? 1.6877 2.5164 2.5044 -0.0146 -0.0982 -0.0265 170 ASN D CA  
10205 C C   . ASN D 170 ? 1.6757 2.5168 2.5068 -0.0085 -0.1019 -0.0343 170 ASN D C   
10206 O O   . ASN D 170 ? 1.6267 2.4655 2.4469 -0.0024 -0.1007 -0.0359 170 ASN D O   
10207 C CB  . ASN D 170 ? 1.6382 2.4731 2.4456 -0.0171 -0.0843 -0.0207 170 ASN D CB  
10208 C CG  . ASN D 170 ? 1.6036 2.4592 2.4306 -0.0238 -0.0743 -0.0190 170 ASN D CG  
10209 O OD1 . ASN D 170 ? 1.5656 2.4197 2.3901 -0.0305 -0.0682 -0.0125 170 ASN D OD1 
10210 N ND2 . ASN D 170 ? 1.5656 2.4403 2.4125 -0.0221 -0.0724 -0.0248 170 ASN D ND2 
10211 N N   . LYS D 171 ? 1.7045 2.5586 2.5603 -0.0098 -0.1064 -0.0393 171 LYS D N   
10212 C CA  . LYS D 171 ? 1.6750 2.5438 2.5485 -0.0043 -0.1091 -0.0469 171 LYS D CA  
10213 C C   . LYS D 171 ? 1.7715 2.6277 2.6432 0.0022  -0.1246 -0.0521 171 LYS D C   
10214 O O   . LYS D 171 ? 1.7787 2.6274 2.6544 -0.0002 -0.1339 -0.0526 171 LYS D O   
10215 C CB  . LYS D 171 ? 1.6116 2.5035 2.5148 -0.0095 -0.1045 -0.0494 171 LYS D CB  
10216 C CG  . LYS D 171 ? 1.5854 2.4896 2.4905 -0.0166 -0.0891 -0.0437 171 LYS D CG  
10217 C CD  . LYS D 171 ? 1.5899 2.5015 2.5125 -0.0254 -0.0876 -0.0413 171 LYS D CD  
10218 C CE  . LYS D 171 ? 1.6240 2.5143 2.5338 -0.0283 -0.0963 -0.0376 171 LYS D CE  
10219 N NZ  . LYS D 171 ? 1.5858 2.4825 2.5143 -0.0368 -0.0964 -0.0363 171 LYS D NZ  
10220 N N   . ILE D 172 ? 1.8875 2.7410 2.7530 0.0102  -0.1277 -0.0560 172 ILE D N   
10221 C CA  . ILE D 172 ? 1.8385 2.6791 2.7001 0.0171  -0.1422 -0.0603 172 ILE D CA  
10222 C C   . ILE D 172 ? 1.7455 2.6016 2.6276 0.0232  -0.1452 -0.0681 172 ILE D C   
10223 O O   . ILE D 172 ? 1.6838 2.5583 2.5786 0.0230  -0.1352 -0.0700 172 ILE D O   
10224 C CB  . ILE D 172 ? 1.8292 2.6471 2.6605 0.0217  -0.1450 -0.0572 172 ILE D CB  
10225 C CG1 . ILE D 172 ? 1.7804 2.6038 2.6068 0.0267  -0.1377 -0.0586 172 ILE D CG1 
10226 C CG2 . ILE D 172 ? 1.8212 2.6257 2.6327 0.0159  -0.1401 -0.0496 172 ILE D CG2 
10227 C CD1 . ILE D 172 ? 1.7117 2.5148 2.5146 0.0332  -0.1435 -0.0580 172 ILE D CD1 
10228 N N   . ASN D 173 ? 1.5662 2.4140 2.4507 0.0290  -0.1593 -0.0726 173 ASN D N   
10229 C CA  . ASN D 173 ? 1.4746 2.3347 2.3780 0.0359  -0.1641 -0.0802 173 ASN D CA  
10230 C C   . ASN D 173 ? 1.4088 2.2657 2.2996 0.0424  -0.1594 -0.0810 173 ASN D C   
10231 O O   . ASN D 173 ? 1.3856 2.2248 2.2502 0.0435  -0.1580 -0.0765 173 ASN D O   
10232 C CB  . ASN D 173 ? 1.4731 2.3230 2.3802 0.0406  -0.1814 -0.0841 173 ASN D CB  
10233 C CG  . ASN D 173 ? 1.4740 2.3402 2.4074 0.0466  -0.1871 -0.0923 173 ASN D CG  
10234 O OD1 . ASN D 173 ? 1.3955 2.2698 2.3330 0.0518  -0.1821 -0.0954 173 ASN D OD1 
10235 N ND2 . ASN D 173 ? 1.6100 2.4813 2.5622 0.0460  -0.1977 -0.0961 173 ASN D ND2 
10236 N N   . ALA D 174 ? 1.3703 2.2450 2.2808 0.0467  -0.1567 -0.0873 174 ALA D N   
10237 C CA  . ALA D 174 ? 1.2618 2.1360 2.1641 0.0528  -0.1520 -0.0893 174 ALA D CA  
10238 C C   . ALA D 174 ? 1.2263 2.0946 2.1330 0.0624  -0.1642 -0.0954 174 ALA D C   
10239 O O   . ALA D 174 ? 1.1703 2.0377 2.0720 0.0682  -0.1615 -0.0979 174 ALA D O   
10240 C CB  . ALA D 174 ? 1.2238 2.1223 2.1427 0.0507  -0.1378 -0.0919 174 ALA D CB  
10241 N N   . GLY D 175 ? 1.2790 2.1428 2.1947 0.0643  -0.1779 -0.0977 175 GLY D N   
10242 C CA  . GLY D 175 ? 1.2850 2.1415 2.2038 0.0736  -0.1908 -0.1028 175 GLY D CA  
10243 C C   . GLY D 175 ? 1.3104 2.1884 2.2591 0.0786  -0.1913 -0.1111 175 GLY D C   
10244 O O   . GLY D 175 ? 1.3690 2.2400 2.3193 0.0868  -0.2013 -0.1150 175 GLY D O   
10245 N N   . ILE D 176 ? 1.3035 2.1995 2.2662 0.0731  -0.1789 -0.1112 176 ILE D N   
10246 C CA  . ILE D 176 ? 1.3316 2.2404 2.3125 0.0761  -0.1756 -0.1159 176 ILE D CA  
10247 C C   . ILE D 176 ? 1.3989 2.3182 2.3976 0.0700  -0.1764 -0.1157 176 ILE D C   
10248 O O   . ILE D 176 ? 1.3876 2.3132 2.3874 0.0612  -0.1691 -0.1115 176 ILE D O   
10249 C CB  . ILE D 176 ? 1.2320 2.1535 2.2136 0.0755  -0.1593 -0.1167 176 ILE D CB  
10250 C CG1 . ILE D 176 ? 1.2537 2.1937 2.2566 0.0736  -0.1516 -0.1197 176 ILE D CG1 
10251 C CG2 . ILE D 176 ? 1.2116 2.1347 2.1803 0.0682  -0.1483 -0.1111 176 ILE D CG2 
10252 C CD1 . ILE D 176 ? 1.1655 2.1180 2.1693 0.0735  -0.1360 -0.1210 176 ILE D CD1 
10253 N N   . TYR D 177 ? 1.5102 2.4312 2.5229 0.0746  -0.1853 -0.1202 177 TYR D N   
10254 C CA  . TYR D 177 ? 1.5822 2.5113 2.6121 0.0697  -0.1891 -0.1206 177 TYR D CA  
10255 C C   . TYR D 177 ? 1.6662 2.6119 2.7171 0.0717  -0.1836 -0.1254 177 TYR D C   
10256 O O   . TYR D 177 ? 1.7686 2.7174 2.8204 0.0780  -0.1793 -0.1289 177 TYR D O   
10257 C CB  . TYR D 177 ? 1.6002 2.5143 2.6271 0.0732  -0.2080 -0.1217 177 TYR D CB  
10258 C CG  . TYR D 177 ? 1.5897 2.4856 2.5950 0.0729  -0.2150 -0.1178 177 TYR D CG  
10259 C CD1 . TYR D 177 ? 1.5811 2.4775 2.5770 0.0653  -0.2061 -0.1128 177 TYR D CD1 
10260 C CD2 . TYR D 177 ? 1.6133 2.4915 2.6073 0.0805  -0.2305 -0.1191 177 TYR D CD2 
10261 C CE1 . TYR D 177 ? 1.5960 2.4763 2.5727 0.0653  -0.2123 -0.1096 177 TYR D CE1 
10262 C CE2 . TYR D 177 ? 1.6346 2.4965 2.6088 0.0804  -0.2369 -0.1157 177 TYR D CE2 
10263 C CZ  . TYR D 177 ? 1.6353 2.4985 2.6012 0.0728  -0.2276 -0.1111 177 TYR D CZ  
10264 O OH  . TYR D 177 ? 1.7211 2.5623 2.6594 0.0720  -0.2315 -0.1057 177 TYR D OH  
10265 N N   . LEU D 178 ? 1.6775 2.6342 2.7458 0.0662  -0.1837 -0.1256 178 LEU D N   
10266 C CA  . LEU D 178 ? 1.6389 2.6119 2.7295 0.0677  -0.1801 -0.1303 178 LEU D CA  
10267 C C   . LEU D 178 ? 1.4876 2.4624 2.5925 0.0645  -0.1905 -0.1313 178 LEU D C   
10268 O O   . LEU D 178 ? 1.5671 2.5486 2.6778 0.0553  -0.1861 -0.1280 178 LEU D O   
10269 C CB  . LEU D 178 ? 1.7022 2.6936 2.8008 0.0617  -0.1612 -0.1288 178 LEU D CB  
10270 C CG  . LEU D 178 ? 1.6060 2.6163 2.7270 0.0629  -0.1540 -0.1334 178 LEU D CG  
10271 C CD1 . LEU D 178 ? 1.5899 2.6125 2.7095 0.0606  -0.1357 -0.1323 178 LEU D CD1 
10272 C CD2 . LEU D 178 ? 1.5385 2.5603 2.6791 0.0560  -0.1551 -0.1331 178 LEU D CD2 
10273 N N   . LEU D 179 ? 1.2793 2.2480 2.3898 0.0721  -0.2046 -0.1360 179 LEU D N   
10274 C CA  . LEU D 179 ? 1.1850 2.1516 2.3056 0.0704  -0.2176 -0.1373 179 LEU D CA  
10275 C C   . LEU D 179 ? 1.1496 2.1300 2.2940 0.0738  -0.2194 -0.1430 179 LEU D C   
10276 O O   . LEU D 179 ? 1.1972 2.1786 2.3451 0.0823  -0.2201 -0.1472 179 LEU D O   
10277 C CB  . LEU D 179 ? 1.1152 2.0597 2.2194 0.0764  -0.2354 -0.1373 179 LEU D CB  
10278 C CG  . LEU D 179 ? 1.0771 2.0068 2.1592 0.0724  -0.2369 -0.1319 179 LEU D CG  
10279 C CD1 . LEU D 179 ? 1.0314 1.9396 2.0968 0.0799  -0.2540 -0.1324 179 LEU D CD1 
10280 C CD2 . LEU D 179 ? 1.0755 2.0097 2.1632 0.0619  -0.2356 -0.1289 179 LEU D CD2 
10281 N N   . ASN D 180 ? 1.0995 2.0903 2.2609 0.0671  -0.2204 -0.1433 180 ASN D N   
10282 C CA  . ASN D 180 ? 1.0906 2.0936 2.2753 0.0700  -0.2245 -0.1489 180 ASN D CA  
10283 C C   . ASN D 180 ? 1.1099 2.0986 2.2922 0.0782  -0.2444 -0.1524 180 ASN D C   
10284 O O   . ASN D 180 ? 1.1031 2.0736 2.2676 0.0791  -0.2555 -0.1500 180 ASN D O   
10285 C CB  . ASN D 180 ? 1.0536 2.0714 2.2568 0.0599  -0.2201 -0.1480 180 ASN D CB  
10286 C CG  . ASN D 180 ? 1.1122 2.1504 2.3276 0.0541  -0.2006 -0.1468 180 ASN D CG  
10287 O OD1 . ASN D 180 ? 1.1972 2.2425 2.4150 0.0593  -0.1921 -0.1491 180 ASN D OD1 
10288 N ND2 . ASN D 180 ? 1.0576 2.1053 2.2812 0.0433  -0.1936 -0.1433 180 ASN D ND2 
10289 N N   . PRO D 181 ? 1.1524 2.1488 2.3523 0.0847  -0.2493 -0.1582 181 PRO D N   
10290 C CA  . PRO D 181 ? 1.1626 2.1460 2.3615 0.0922  -0.2689 -0.1614 181 PRO D CA  
10291 C C   . PRO D 181 ? 1.2473 2.2258 2.4479 0.0865  -0.2805 -0.1604 181 PRO D C   
10292 O O   . PRO D 181 ? 1.3045 2.2686 2.4985 0.0920  -0.2976 -0.1619 181 PRO D O   
10293 C CB  . PRO D 181 ? 1.1406 2.1380 2.3624 0.0985  -0.2687 -0.1677 181 PRO D CB  
10294 C CG  . PRO D 181 ? 1.2354 2.2465 2.4616 0.0977  -0.2501 -0.1679 181 PRO D CG  
10295 C CD  . PRO D 181 ? 1.2120 2.2279 2.4315 0.0864  -0.2375 -0.1620 181 PRO D CD  
10296 N N   . SER D 182 ? 1.2801 2.2697 2.4892 0.0756  -0.2720 -0.1579 182 SER D N   
10297 C CA  . SER D 182 ? 1.2695 2.2553 2.4816 0.0692  -0.2821 -0.1573 182 SER D CA  
10298 C C   . SER D 182 ? 1.3305 2.2958 2.5171 0.0671  -0.2892 -0.1528 182 SER D C   
10299 O O   . SER D 182 ? 1.3417 2.3027 2.5286 0.0610  -0.2967 -0.1520 182 SER D O   
10300 C CB  . SER D 182 ? 1.2316 2.2368 2.4627 0.0580  -0.2698 -0.1562 182 SER D CB  
10301 O OG  . SER D 182 ? 1.2551 2.2798 2.5105 0.0597  -0.2635 -0.1605 182 SER D OG  
10302 N N   . VAL D 183 ? 1.3673 2.3201 2.5327 0.0720  -0.2872 -0.1501 183 VAL D N   
10303 C CA  . VAL D 183 ? 1.3746 2.3080 2.5155 0.0705  -0.2936 -0.1460 183 VAL D CA  
10304 C C   . VAL D 183 ? 1.5355 2.4487 2.6606 0.0805  -0.3112 -0.1474 183 VAL D C   
10305 O O   . VAL D 183 ? 1.4495 2.3459 2.5566 0.0795  -0.3209 -0.1449 183 VAL D O   
10306 C CB  . VAL D 183 ? 1.1855 2.1182 2.3120 0.0677  -0.2786 -0.1411 183 VAL D CB  
10307 C CG1 . VAL D 183 ? 1.2375 2.1639 2.3533 0.0776  -0.2774 -0.1421 183 VAL D CG1 
10308 C CG2 . VAL D 183 ? 1.1192 2.0372 2.2261 0.0625  -0.2820 -0.1365 183 VAL D CG2 
10309 N N   . LEU D 184 ? 2.1248 3.0388 3.2559 0.0899  -0.3158 -0.1512 184 LEU D N   
10310 C CA  . LEU D 184 ? 2.1383 3.0330 3.2541 0.0999  -0.3319 -0.1521 184 LEU D CA  
10311 C C   . LEU D 184 ? 2.1525 3.0378 3.2683 0.1004  -0.3503 -0.1538 184 LEU D C   
10312 O O   . LEU D 184 ? 2.1645 3.0325 3.2661 0.1083  -0.3649 -0.1541 184 LEU D O   
10313 C CB  . LEU D 184 ? 2.1476 3.0468 3.2724 0.1097  -0.3315 -0.1561 184 LEU D CB  
10314 C CG  . LEU D 184 ? 2.1351 3.0388 3.2552 0.1117  -0.3162 -0.1549 184 LEU D CG  
10315 C CD1 . LEU D 184 ? 2.1378 3.0473 3.2703 0.1211  -0.3164 -0.1598 184 LEU D CD1 
10316 C CD2 . LEU D 184 ? 2.1272 3.0116 3.2195 0.1136  -0.3181 -0.1504 184 LEU D CD2 
10317 N N   . ASP D 185 ? 1.5390 2.4345 2.6698 0.0923  -0.3504 -0.1550 185 ASP D N   
10318 C CA  . ASP D 185 ? 1.4394 2.3260 2.5697 0.0922  -0.3680 -0.1569 185 ASP D CA  
10319 C C   . ASP D 185 ? 1.3515 2.2256 2.4648 0.0851  -0.3719 -0.1533 185 ASP D C   
10320 O O   . ASP D 185 ? 1.2717 2.1323 2.3762 0.0866  -0.3882 -0.1543 185 ASP D O   
10321 C CB  . ASP D 185 ? 1.3347 2.2398 2.4937 0.0883  -0.3681 -0.1614 185 ASP D CB  
10322 C CG  . ASP D 185 ? 1.3015 2.2227 2.4736 0.0763  -0.3533 -0.1597 185 ASP D CG  
10323 O OD1 . ASP D 185 ? 1.3642 2.2886 2.5293 0.0727  -0.3384 -0.1558 185 ASP D OD1 
10324 O OD2 . ASP D 185 ? 1.1966 2.1269 2.3858 0.0705  -0.3568 -0.1622 185 ASP D OD2 
10325 N N   . LYS D 186 ? 1.2890 2.1669 2.3971 0.0777  -0.3576 -0.1492 186 LYS D N   
10326 C CA  . LYS D 186 ? 1.2354 2.1027 2.3293 0.0705  -0.3601 -0.1460 186 LYS D CA  
10327 C C   . LYS D 186 ? 1.2318 2.0758 2.2962 0.0760  -0.3695 -0.1431 186 LYS D C   
10328 O O   . LYS D 186 ? 1.2240 2.0566 2.2745 0.0712  -0.3740 -0.1408 186 LYS D O   
10329 C CB  . LYS D 186 ? 1.2041 2.0834 2.3027 0.0608  -0.3414 -0.1424 186 LYS D CB  
10330 C CG  . LYS D 186 ? 1.2085 2.0852 2.3064 0.0507  -0.3430 -0.1408 186 LYS D CG  
10331 C CD  . LYS D 186 ? 1.2321 2.1184 2.3319 0.0419  -0.3247 -0.1364 186 LYS D CD  
10332 C CE  . LYS D 186 ? 1.2399 2.1265 2.3449 0.0313  -0.3258 -0.1356 186 LYS D CE  
10333 N NZ  . LYS D 186 ? 1.1797 2.0456 2.2672 0.0328  -0.3430 -0.1363 186 LYS D NZ  
10334 N N   . ILE D 187 ? 1.2925 2.1289 2.3473 0.0858  -0.3726 -0.1431 187 ILE D N   
10335 C CA  . ILE D 187 ? 1.2621 2.0765 2.2888 0.0913  -0.3810 -0.1401 187 ILE D CA  
10336 C C   . ILE D 187 ? 1.2606 2.0596 2.2787 0.0967  -0.4021 -0.1422 187 ILE D C   
10337 O O   . ILE D 187 ? 1.2102 2.0154 2.2441 0.0994  -0.4099 -0.1464 187 ILE D O   
10338 C CB  . ILE D 187 ? 1.2598 2.0723 2.2794 0.0990  -0.3743 -0.1388 187 ILE D CB  
10339 C CG1 . ILE D 187 ? 1.3164 2.1434 2.3576 0.1042  -0.3714 -0.1431 187 ILE D CG1 
10340 C CG2 . ILE D 187 ? 1.2053 2.0231 2.2192 0.0937  -0.3569 -0.1349 187 ILE D CG2 
10341 C CD1 . ILE D 187 ? 1.2777 2.0953 2.3192 0.1133  -0.3891 -0.1464 187 ILE D CD1 
10342 N N   . GLU D 188 ? 1.2787 2.0572 2.2711 0.0982  -0.4115 -0.1393 188 GLU D N   
10343 C CA  . GLU D 188 ? 1.3209 2.0819 2.2998 0.1039  -0.4318 -0.1405 188 GLU D CA  
10344 C C   . GLU D 188 ? 1.3929 2.1395 2.3553 0.1150  -0.4385 -0.1389 188 GLU D C   
10345 O O   . GLU D 188 ? 1.3981 2.1471 2.3579 0.1178  -0.4276 -0.1369 188 GLU D O   
10346 C CB  . GLU D 188 ? 1.3173 2.0638 2.2771 0.0986  -0.4388 -0.1384 188 GLU D CB  
10347 C CG  . GLU D 188 ? 1.3871 2.1300 2.3328 0.0945  -0.4267 -0.1338 188 GLU D CG  
10348 C CD  . GLU D 188 ? 1.4740 2.1969 2.3941 0.0930  -0.4368 -0.1314 188 GLU D CD  
10349 O OE1 . GLU D 188 ? 1.4309 2.1448 2.3464 0.0930  -0.4518 -0.1338 188 GLU D OE1 
10350 O OE2 . GLU D 188 ? 1.5637 2.2799 2.4682 0.0918  -0.4297 -0.1275 188 GLU D OE2 
10351 N N   . LEU D 189 ? 1.4985 2.2295 2.4491 0.1213  -0.4570 -0.1399 189 LEU D N   
10352 C CA  . LEU D 189 ? 1.5445 2.2589 2.4767 0.1318  -0.4652 -0.1377 189 LEU D CA  
10353 C C   . LEU D 189 ? 1.5658 2.2617 2.4685 0.1320  -0.4659 -0.1325 189 LEU D C   
10354 O O   . LEU D 189 ? 1.6252 2.3093 2.5131 0.1394  -0.4677 -0.1297 189 LEU D O   
10355 C CB  . LEU D 189 ? 1.5502 2.2539 2.4792 0.1386  -0.4849 -0.1400 189 LEU D CB  
10356 C CG  . LEU D 189 ? 1.5350 2.2346 2.4620 0.1334  -0.4968 -0.1421 189 LEU D CG  
10357 C CD1 . LEU D 189 ? 1.6071 2.2809 2.5008 0.1363  -0.5109 -0.1387 189 LEU D CD1 
10358 C CD2 . LEU D 189 ? 1.4516 2.1594 2.3986 0.1364  -0.5067 -0.1472 189 LEU D CD2 
10359 N N   . ARG D 190 ? 1.5509 2.2439 2.4451 0.1240  -0.4645 -0.1311 190 ARG D N   
10360 C CA  . ARG D 190 ? 1.5960 2.2724 2.4631 0.1238  -0.4647 -0.1264 190 ARG D CA  
10361 C C   . ARG D 190 ? 1.6084 2.2947 2.4792 0.1210  -0.4457 -0.1238 190 ARG D C   
10362 O O   . ARG D 190 ? 1.5862 2.2926 2.4790 0.1149  -0.4316 -0.1255 190 ARG D O   
10363 C CB  . ARG D 190 ? 1.6103 2.2798 2.4674 0.1165  -0.4704 -0.1264 190 ARG D CB  
10364 C CG  . ARG D 190 ? 1.6274 2.2889 2.4825 0.1179  -0.4884 -0.1297 190 ARG D CG  
10365 C CD  . ARG D 190 ? 1.6600 2.3002 2.4919 0.1282  -0.5047 -0.1279 190 ARG D CD  
10366 N NE  . ARG D 190 ? 1.7532 2.3728 2.5518 0.1300  -0.5015 -0.1217 190 ARG D NE  
10367 C CZ  . ARG D 190 ? 1.7460 2.3557 2.5311 0.1372  -0.4988 -0.1178 190 ARG D CZ  
10368 N NH1 . ARG D 190 ? 1.7475 2.3699 2.5560 0.1447  -0.5033 -0.1211 190 ARG D NH1 
10369 N NH2 . ARG D 190 ? 1.7015 2.2886 2.4502 0.1368  -0.4914 -0.1107 190 ARG D NH2 
10370 N N   . PRO D 191 ? 1.6757 2.3434 2.5173 0.1241  -0.4407 -0.1180 191 PRO D N   
10371 C CA  . PRO D 191 ? 1.7272 2.3993 2.5640 0.1201  -0.4200 -0.1142 191 PRO D CA  
10372 C C   . PRO D 191 ? 1.7213 2.4030 2.5630 0.1090  -0.4069 -0.1131 191 PRO D C   
10373 O O   . PRO D 191 ? 1.6958 2.3621 2.5148 0.1038  -0.4073 -0.1097 191 PRO D O   
10374 C CB  . PRO D 191 ? 1.7568 2.4004 2.5533 0.1234  -0.4192 -0.1073 191 PRO D CB  
10375 C CG  . PRO D 191 ? 1.7490 2.3797 2.5390 0.1328  -0.4383 -0.1085 191 PRO D CG  
10376 C CD  . PRO D 191 ? 1.6932 2.3345 2.5044 0.1318  -0.4529 -0.1145 191 PRO D CD  
10377 N N   . THR D 192 ? 1.8298 2.5367 2.7007 0.1054  -0.3950 -0.1161 192 THR D N   
10378 C CA  . THR D 192 ? 1.8087 2.5270 2.6874 0.0949  -0.3816 -0.1149 192 THR D CA  
10379 C C   . THR D 192 ? 1.7945 2.5198 2.6711 0.0928  -0.3619 -0.1115 192 THR D C   
10380 O O   . THR D 192 ? 1.7847 2.5216 2.6754 0.0981  -0.3579 -0.1138 192 THR D O   
10381 C CB  . THR D 192 ? 1.7972 2.5410 2.7145 0.0910  -0.3847 -0.1214 192 THR D CB  
10382 O OG1 . THR D 192 ? 1.7791 2.5371 2.7071 0.0814  -0.3682 -0.1198 192 THR D OG1 
10383 C CG2 . THR D 192 ? 1.7990 2.5542 2.7340 0.0969  -0.3837 -0.1248 192 THR D CG2 
10384 N N   . SER D 193 ? 1.5400 2.2583 2.3990 0.0853  -0.3500 -0.1062 193 SER D N   
10385 C CA  . SER D 193 ? 1.4763 2.2015 2.3327 0.0824  -0.3312 -0.1027 193 SER D CA  
10386 C C   . SER D 193 ? 1.4842 2.2369 2.3728 0.0759  -0.3211 -0.1057 193 SER D C   
10387 O O   . SER D 193 ? 1.4384 2.1957 2.3344 0.0683  -0.3205 -0.1057 193 SER D O   
10388 C CB  . SER D 193 ? 1.3449 2.0507 2.1687 0.0775  -0.3231 -0.0956 193 SER D CB  
10389 O OG  . SER D 193 ? 1.2616 1.9418 2.0569 0.0818  -0.3348 -0.0933 193 SER D OG  
10390 N N   . ILE D 194 ? 1.5126 2.2834 2.4204 0.0789  -0.3131 -0.1085 194 ILE D N   
10391 C CA  . ILE D 194 ? 1.6062 2.4043 2.5455 0.0733  -0.3032 -0.1116 194 ILE D CA  
10392 C C   . ILE D 194 ? 1.7836 2.5826 2.7144 0.0634  -0.2883 -0.1061 194 ILE D C   
10393 O O   . ILE D 194 ? 1.9260 2.7427 2.8787 0.0562  -0.2826 -0.1075 194 ILE D O   
10394 C CB  . ILE D 194 ? 1.6542 2.4687 2.6103 0.0787  -0.2956 -0.1150 194 ILE D CB  
10395 C CG1 . ILE D 194 ? 1.7731 2.6086 2.7541 0.0733  -0.2863 -0.1173 194 ILE D CG1 
10396 C CG2 . ILE D 194 ? 1.7260 2.5370 2.6648 0.0781  -0.2805 -0.1106 194 ILE D CG2 
10397 C CD1 . ILE D 194 ? 1.7128 2.5608 2.7049 0.0780  -0.2771 -0.1198 194 ILE D CD1 
10398 N N   . GLU D 195 ? 1.7247 2.5046 2.6239 0.0627  -0.2821 -0.0998 195 GLU D N   
10399 C CA  . GLU D 195 ? 1.7352 2.5147 2.6247 0.0540  -0.2683 -0.0942 195 GLU D CA  
10400 C C   . GLU D 195 ? 1.6732 2.4406 2.5534 0.0478  -0.2743 -0.0921 195 GLU D C   
10401 O O   . GLU D 195 ? 1.7351 2.5071 2.6169 0.0395  -0.2644 -0.0888 195 GLU D O   
10402 C CB  . GLU D 195 ? 1.7529 2.5177 2.6136 0.0559  -0.2590 -0.0886 195 GLU D CB  
10403 C CG  . GLU D 195 ? 1.7654 2.5407 2.6325 0.0613  -0.2514 -0.0904 195 GLU D CG  
10404 C CD  . GLU D 195 ? 1.7741 2.5724 2.6601 0.0559  -0.2357 -0.0905 195 GLU D CD  
10405 O OE1 . GLU D 195 ? 1.8062 2.6099 2.6963 0.0476  -0.2293 -0.0877 195 GLU D OE1 
10406 O OE2 . GLU D 195 ? 1.7622 2.5730 2.6586 0.0601  -0.2296 -0.0934 195 GLU D OE2 
10407 N N   . LYS D 196 ? 1.4513 2.2031 2.3214 0.0516  -0.2904 -0.0939 196 LYS D N   
10408 C CA  . LYS D 196 ? 1.3824 2.1200 2.2399 0.0465  -0.2969 -0.0922 196 LYS D CA  
10409 C C   . LYS D 196 ? 1.3570 2.1031 2.2375 0.0449  -0.3102 -0.0981 196 LYS D C   
10410 O O   . LYS D 196 ? 1.4072 2.1486 2.2862 0.0382  -0.3123 -0.0975 196 LYS D O   
10411 C CB  . LYS D 196 ? 1.2480 1.9573 2.0700 0.0513  -0.3046 -0.0890 196 LYS D CB  
10412 C CG  . LYS D 196 ? 1.1853 1.8857 1.9854 0.0540  -0.2933 -0.0839 196 LYS D CG  
10413 C CD  . LYS D 196 ? 1.0221 1.6952 1.7883 0.0586  -0.3009 -0.0808 196 LYS D CD  
10414 C CE  . LYS D 196 ? 0.9527 1.6183 1.6998 0.0617  -0.2903 -0.0762 196 LYS D CE  
10415 N NZ  . LYS D 196 ? 0.8753 1.5475 1.6208 0.0549  -0.2733 -0.0719 196 LYS D NZ  
10416 N N   . GLU D 197 ? 1.4015 2.1596 2.3032 0.0509  -0.3194 -0.1039 197 GLU D N   
10417 C CA  . GLU D 197 ? 1.4149 2.1811 2.3388 0.0502  -0.3335 -0.1100 197 GLU D CA  
10418 C C   . GLU D 197 ? 1.5245 2.3203 2.4884 0.0492  -0.3304 -0.1154 197 GLU D C   
10419 O O   . GLU D 197 ? 1.5211 2.3275 2.5042 0.0426  -0.3314 -0.1177 197 GLU D O   
10420 C CB  . GLU D 197 ? 1.3457 2.0959 2.2570 0.0590  -0.3523 -0.1126 197 GLU D CB  
10421 C CG  . GLU D 197 ? 1.2992 2.0205 2.1735 0.0590  -0.3585 -0.1084 197 GLU D CG  
10422 C CD  . GLU D 197 ? 1.2806 1.9853 2.1242 0.0626  -0.3497 -0.1023 197 GLU D CD  
10423 O OE1 . GLU D 197 ? 1.3211 2.0360 2.1719 0.0660  -0.3405 -0.1017 197 GLU D OE1 
10424 O OE2 . GLU D 197 ? 1.1962 1.8781 2.0088 0.0621  -0.3517 -0.0982 197 GLU D OE2 
10425 N N   . THR D 198 ? 1.5594 2.3650 2.5307 0.0551  -0.3244 -0.1165 198 THR D N   
10426 C CA  . THR D 198 ? 1.6427 2.4673 2.6379 0.0542  -0.3178 -0.1194 198 THR D CA  
10427 C C   . THR D 198 ? 1.8958 2.7381 2.9048 0.0452  -0.2992 -0.1170 198 THR D C   
10428 O O   . THR D 198 ? 1.8049 2.6606 2.8336 0.0392  -0.2960 -0.1186 198 THR D O   
10429 C CB  . THR D 198 ? 1.5738 2.3998 2.5690 0.0639  -0.3176 -0.1212 198 THR D CB  
10430 O OG1 . THR D 198 ? 1.5323 2.3416 2.5153 0.0722  -0.3355 -0.1231 198 THR D OG1 
10431 C CG2 . THR D 198 ? 1.5289 2.3747 2.5493 0.0633  -0.3110 -0.1247 198 THR D CG2 
10432 N N   . PHE D 199 ? 2.9369 3.7796 3.9355 0.0442  -0.2869 -0.1130 199 PHE D N   
10433 C CA  . PHE D 199 ? 2.9242 3.7828 3.9337 0.0358  -0.2692 -0.1101 199 PHE D CA  
10434 C C   . PHE D 199 ? 2.9246 3.7846 3.9412 0.0256  -0.2691 -0.1086 199 PHE D C   
10435 O O   . PHE D 199 ? 2.9218 3.7981 3.9569 0.0188  -0.2593 -0.1083 199 PHE D O   
10436 C CB  . PHE D 199 ? 2.9122 3.7688 3.9069 0.0366  -0.2575 -0.1061 199 PHE D CB  
10437 C CG  . PHE D 199 ? 2.9137 3.7772 3.9092 0.0435  -0.2504 -0.1074 199 PHE D CG  
10438 C CD1 . PHE D 199 ? 2.9164 3.7924 3.9296 0.0462  -0.2496 -0.1114 199 PHE D CD1 
10439 C CD2 . PHE D 199 ? 2.9038 3.7601 3.8809 0.0472  -0.2441 -0.1047 199 PHE D CD2 
10440 C CE1 . PHE D 199 ? 2.9144 3.7963 3.9288 0.0526  -0.2432 -0.1131 199 PHE D CE1 
10441 C CE2 . PHE D 199 ? 2.9003 3.7638 3.8803 0.0535  -0.2383 -0.1069 199 PHE D CE2 
10442 C CZ  . PHE D 199 ? 2.9060 3.7815 3.9037 0.0562  -0.2376 -0.1109 199 PHE D CZ  
10443 N N   . PRO D 200 ? 2.0571 2.9006 3.0593 0.0240  -0.2789 -0.1073 200 PRO D N   
10444 C CA  . PRO D 200 ? 1.9260 2.7701 2.9359 0.0143  -0.2794 -0.1064 200 PRO D CA  
10445 C C   . PRO D 200 ? 1.7608 2.6137 2.7922 0.0123  -0.2877 -0.1113 200 PRO D C   
10446 O O   . PRO D 200 ? 1.6757 2.5359 2.7209 0.0033  -0.2842 -0.1109 200 PRO D O   
10447 C CB  . PRO D 200 ? 1.8721 2.6869 2.8478 0.0146  -0.2870 -0.1027 200 PRO D CB  
10448 C CG  . PRO D 200 ? 1.8057 2.6068 2.7623 0.0252  -0.2956 -0.1036 200 PRO D CG  
10449 C CD  . PRO D 200 ? 1.8740 2.6902 2.8400 0.0294  -0.2849 -0.1038 200 PRO D CD  
10450 N N   . LYS D 201 ? 1.7408 2.5921 2.7742 0.0203  -0.2982 -0.1156 201 LYS D N   
10451 C CA  . LYS D 201 ? 1.5628 2.4220 2.6155 0.0188  -0.3057 -0.1202 201 LYS D CA  
10452 C C   . LYS D 201 ? 1.5354 2.4175 2.6117 0.0137  -0.2910 -0.1203 201 LYS D C   
10453 O O   . LYS D 201 ? 1.4367 2.3282 2.5314 0.0072  -0.2916 -0.1221 201 LYS D O   
10454 C CB  . LYS D 201 ? 1.3785 2.2299 2.4267 0.0292  -0.3204 -0.1245 201 LYS D CB  
10455 C CG  . LYS D 201 ? 1.2779 2.1078 2.3072 0.0329  -0.3387 -0.1256 201 LYS D CG  
10456 C CD  . LYS D 201 ? 1.1358 1.9588 2.1617 0.0432  -0.3529 -0.1294 201 LYS D CD  
10457 C CE  . LYS D 201 ? 0.8889 1.6903 1.8949 0.0466  -0.3715 -0.1303 201 LYS D CE  
10458 N NZ  . LYS D 201 ? 0.8338 1.6281 1.8364 0.0566  -0.3858 -0.1336 201 LYS D NZ  
10459 N N   . ILE D 202 ? 1.5883 2.4796 2.6644 0.0166  -0.2776 -0.1183 202 ILE D N   
10460 C CA  . ILE D 202 ? 1.5137 2.4267 2.6104 0.0119  -0.2627 -0.1181 202 ILE D CA  
10461 C C   . ILE D 202 ? 1.5296 2.4496 2.6281 0.0018  -0.2477 -0.1128 202 ILE D C   
10462 O O   . ILE D 202 ? 1.4742 2.4112 2.5916 -0.0049 -0.2373 -0.1123 202 ILE D O   
10463 C CB  . ILE D 202 ? 1.4738 2.3942 2.5706 0.0199  -0.2555 -0.1191 202 ILE D CB  
10464 C CG1 . ILE D 202 ? 1.4512 2.3592 2.5393 0.0310  -0.2708 -0.1231 202 ILE D CG1 
10465 C CG2 . ILE D 202 ? 1.3427 2.2853 2.4638 0.0169  -0.2449 -0.1209 202 ILE D CG2 
10466 C CD1 . ILE D 202 ? 1.2504 2.1635 2.3377 0.0392  -0.2648 -0.1243 202 ILE D CD1 
10467 N N   . ALA D 203 ? 1.5800 2.4875 2.6597 0.0005  -0.2462 -0.1087 203 ALA D N   
10468 C CA  . ALA D 203 ? 1.5980 2.5111 2.6790 -0.0090 -0.2325 -0.1033 203 ALA D CA  
10469 C C   . ALA D 203 ? 1.5206 2.4353 2.6149 -0.0186 -0.2359 -0.1034 203 ALA D C   
10470 O O   . ALA D 203 ? 1.5238 2.4515 2.6315 -0.0271 -0.2236 -0.1005 203 ALA D O   
10471 C CB  . ALA D 203 ? 1.7600 2.6585 2.8179 -0.0075 -0.2314 -0.0992 203 ALA D CB  
10472 N N   . ALA D 204 ? 1.5160 2.4171 2.6065 -0.0173 -0.2527 -0.1067 204 ALA D N   
10473 C CA  . ALA D 204 ? 1.4927 2.3945 2.5964 -0.0260 -0.2575 -0.1078 204 ALA D CA  
10474 C C   . ALA D 204 ? 1.3484 2.2682 2.4774 -0.0291 -0.2551 -0.1111 204 ALA D C   
10475 O O   . ALA D 204 ? 1.2688 2.1944 2.4127 -0.0383 -0.2533 -0.1109 204 ALA D O   
10476 C CB  . ALA D 204 ? 1.5058 2.3885 2.5982 -0.0230 -0.2771 -0.1113 204 ALA D CB  
10477 N N   . ALA D 205 ? 1.3493 2.2779 2.4841 -0.0217 -0.2549 -0.1142 205 ALA D N   
10478 C CA  . ALA D 205 ? 1.3025 2.2496 2.4621 -0.0241 -0.2514 -0.1172 205 ALA D CA  
10479 C C   . ALA D 205 ? 1.2995 2.2653 2.4703 -0.0297 -0.2312 -0.1133 205 ALA D C   
10480 O O   . ALA D 205 ? 1.2612 2.2436 2.4538 -0.0339 -0.2262 -0.1150 205 ALA D O   
10481 C CB  . ALA D 205 ? 1.2395 2.1877 2.4015 -0.0134 -0.2605 -0.1225 205 ALA D CB  
10482 N N   . GLN D 206 ? 1.3746 2.3383 2.5310 -0.0300 -0.2197 -0.1080 206 GLN D N   
10483 C CA  . GLN D 206 ? 1.3738 2.3540 2.5377 -0.0352 -0.2003 -0.1037 206 GLN D CA  
10484 C C   . GLN D 206 ? 1.3893 2.3867 2.5678 -0.0307 -0.1945 -0.1070 206 GLN D C   
10485 O O   . GLN D 206 ? 1.3540 2.3691 2.5492 -0.0367 -0.1822 -0.1056 206 GLN D O   
10486 C CB  . GLN D 206 ? 1.3478 2.3348 2.5248 -0.0478 -0.1934 -0.1003 206 GLN D CB  
10487 C CG  . GLN D 206 ? 1.2948 2.2648 2.4600 -0.0528 -0.1997 -0.0975 206 GLN D CG  
10488 C CD  . GLN D 206 ? 1.2886 2.2514 2.4347 -0.0531 -0.1902 -0.0914 206 GLN D CD  
10489 O OE1 . GLN D 206 ? 1.4084 2.3680 2.5401 -0.0451 -0.1883 -0.0911 206 GLN D OE1 
10490 N NE2 . GLN D 206 ? 1.2166 2.1768 2.3632 -0.0624 -0.1844 -0.0864 206 GLN D NE2 
10491 N N   . GLY D 207 ? 1.3971 2.3889 2.5694 -0.0199 -0.2035 -0.1113 207 GLY D N   
10492 C CA  . GLY D 207 ? 1.3977 2.4038 2.5832 -0.0143 -0.1995 -0.1150 207 GLY D CA  
10493 C C   . GLY D 207 ? 1.4743 2.4790 2.6455 -0.0065 -0.1923 -0.1140 207 GLY D C   
10494 O O   . GLY D 207 ? 1.3619 2.3731 2.5393 0.0009  -0.1924 -0.1180 207 GLY D O   
10495 N N   . LEU D 208 ? 1.7996 2.7955 2.9521 -0.0082 -0.1863 -0.1090 208 LEU D N   
10496 C CA  . LEU D 208 ? 1.7957 2.7890 2.9328 -0.0017 -0.1792 -0.1076 208 LEU D CA  
10497 C C   . LEU D 208 ? 1.8573 2.8598 2.9913 -0.0087 -0.1610 -0.1017 208 LEU D C   
10498 O O   . LEU D 208 ? 1.8281 2.8372 2.9704 -0.0185 -0.1545 -0.0981 208 LEU D O   
10499 C CB  . LEU D 208 ? 1.8028 2.7743 2.9168 0.0046  -0.1909 -0.1075 208 LEU D CB  
10500 C CG  . LEU D 208 ? 1.7876 2.7441 2.8935 0.0003  -0.2019 -0.1059 208 LEU D CG  
10501 C CD1 . LEU D 208 ? 1.8260 2.7856 2.9314 -0.0104 -0.1910 -0.1000 208 LEU D CD1 
10502 C CD2 . LEU D 208 ? 1.7987 2.7350 2.8817 0.0080  -0.2127 -0.1061 208 LEU D CD2 
10503 N N   . TYR D 209 ? 1.8716 2.8741 2.9934 -0.0034 -0.1530 -0.1007 209 TYR D N   
10504 C CA  . TYR D 209 ? 1.8303 2.8402 2.9461 -0.0086 -0.1362 -0.0952 209 TYR D CA  
10505 C C   . TYR D 209 ? 1.8138 2.8135 2.9082 -0.0013 -0.1348 -0.0947 209 TYR D C   
10506 O O   . TYR D 209 ? 1.8794 2.8698 2.9673 0.0078  -0.1449 -0.0989 209 TYR D O   
10507 C CB  . TYR D 209 ? 1.7999 2.8312 2.9332 -0.0116 -0.1223 -0.0954 209 TYR D CB  
10508 C CG  . TYR D 209 ? 1.8591 2.8958 2.9965 -0.0021 -0.1224 -0.1009 209 TYR D CG  
10509 C CD1 . TYR D 209 ? 1.8385 2.8769 2.9647 0.0024  -0.1128 -0.1005 209 TYR D CD1 
10510 C CD2 . TYR D 209 ? 1.7917 2.8314 2.9443 0.0024  -0.1327 -0.1070 209 TYR D CD2 
10511 C CE1 . TYR D 209 ? 1.8094 2.8520 2.9396 0.0112  -0.1130 -0.1059 209 TYR D CE1 
10512 C CE2 . TYR D 209 ? 1.7306 2.7747 2.8875 0.0114  -0.1331 -0.1123 209 TYR D CE2 
10513 C CZ  . TYR D 209 ? 1.7608 2.8063 2.9067 0.0156  -0.1231 -0.1118 209 TYR D CZ  
10514 O OH  . TYR D 209 ? 1.6904 2.7397 2.8408 0.0245  -0.1234 -0.1174 209 TYR D OH  
10515 N N   . ALA D 210 ? 1.6314 2.6332 2.7153 -0.0054 -0.1222 -0.0894 210 ALA D N   
10516 C CA  . ALA D 210 ? 1.5368 2.5292 2.5999 0.0004  -0.1201 -0.0885 210 ALA D CA  
10517 C C   . ALA D 210 ? 1.4707 2.4760 2.5322 -0.0009 -0.1029 -0.0862 210 ALA D C   
10518 O O   . ALA D 210 ? 1.4321 2.4511 2.5041 -0.0085 -0.0914 -0.0829 210 ALA D O   
10519 C CB  . ALA D 210 ? 1.5132 2.4905 2.5594 -0.0027 -0.1242 -0.0841 210 ALA D CB  
10520 N N   . MET D 211 ? 1.4798 2.4803 2.5278 0.0067  -0.1015 -0.0882 211 MET D N   
10521 C CA  . MET D 211 ? 1.5740 2.5840 2.6165 0.0067  -0.0864 -0.0866 211 MET D CA  
10522 C C   . MET D 211 ? 1.7763 2.7740 2.7953 0.0092  -0.0857 -0.0842 211 MET D C   
10523 O O   . MET D 211 ? 1.6587 2.6411 2.6667 0.0145  -0.0976 -0.0859 211 MET D O   
10524 C CB  . MET D 211 ? 1.4425 2.4609 2.4935 0.0140  -0.0840 -0.0927 211 MET D CB  
10525 C CG  . MET D 211 ? 1.3951 2.4240 2.4415 0.0138  -0.0681 -0.0918 211 MET D CG  
10526 S SD  . MET D 211 ? 1.2715 2.3074 2.3256 0.0237  -0.0667 -0.1000 211 MET D SD  
10527 C CE  . MET D 211 ? 1.0766 2.1204 2.1184 0.0224  -0.0487 -0.0980 211 MET D CE  
10528 N N   . VAL D 212 ? 2.6329 3.6374 3.6439 0.0053  -0.0717 -0.0801 212 VAL D N   
10529 C CA  . VAL D 212 ? 2.6252 3.6202 3.6138 0.0069  -0.0692 -0.0774 212 VAL D CA  
10530 C C   . VAL D 212 ? 2.6248 3.6203 3.6057 0.0150  -0.0660 -0.0818 212 VAL D C   
10531 O O   . VAL D 212 ? 2.6284 3.6364 3.6194 0.0161  -0.0579 -0.0846 212 VAL D O   
10532 C CB  . VAL D 212 ? 2.6230 3.6246 3.6058 -0.0019 -0.0564 -0.0702 212 VAL D CB  
10533 C CG1 . VAL D 212 ? 2.6146 3.6058 3.5729 -0.0004 -0.0546 -0.0670 212 VAL D CG1 
10534 C CG2 . VAL D 212 ? 2.6579 3.6600 3.6513 -0.0103 -0.0593 -0.0663 212 VAL D CG2 
10535 N N   . LEU D 213 ? 1.8872 2.8692 2.8507 0.0206  -0.0722 -0.0828 213 LEU D N   
10536 C CA  . LEU D 213 ? 1.7289 2.7095 2.6842 0.0284  -0.0703 -0.0873 213 LEU D CA  
10537 C C   . LEU D 213 ? 1.6779 2.6644 2.6200 0.0255  -0.0561 -0.0839 213 LEU D C   
10538 O O   . LEU D 213 ? 1.6783 2.6586 2.6047 0.0223  -0.0547 -0.0789 213 LEU D O   
10539 C CB  . LEU D 213 ? 1.6636 2.6271 2.6063 0.0355  -0.0832 -0.0897 213 LEU D CB  
10540 C CG  . LEU D 213 ? 1.5999 2.5600 2.5326 0.0434  -0.0818 -0.0941 213 LEU D CG  
10541 C CD1 . LEU D 213 ? 1.5578 2.5263 2.5063 0.0485  -0.0812 -0.1005 213 LEU D CD1 
10542 C CD2 . LEU D 213 ? 1.4751 2.4141 2.3911 0.0490  -0.0939 -0.0940 213 LEU D CD2 
10543 N N   . PRO D 214 ? 1.4553 2.4538 2.4025 0.0266  -0.0457 -0.0866 214 PRO D N   
10544 C CA  . PRO D 214 ? 1.3407 2.3446 2.2743 0.0240  -0.0325 -0.0835 214 PRO D CA  
10545 C C   . PRO D 214 ? 1.2912 2.2872 2.2083 0.0311  -0.0337 -0.0870 214 PRO D C   
10546 O O   . PRO D 214 ? 1.2171 2.2200 2.1291 0.0323  -0.0238 -0.0889 214 PRO D O   
10547 C CB  . PRO D 214 ? 1.2122 2.2330 2.1607 0.0219  -0.0212 -0.0855 214 PRO D CB  
10548 C CG  . PRO D 214 ? 1.1957 2.2173 2.1606 0.0284  -0.0296 -0.0928 214 PRO D CG  
10549 C CD  . PRO D 214 ? 1.3720 2.3808 2.3387 0.0296  -0.0449 -0.0922 214 PRO D CD  
10550 N N   . GLY D 215 ? 1.2497 2.2309 2.1583 0.0357  -0.0457 -0.0880 215 GLY D N   
10551 C CA  . GLY D 215 ? 1.1782 2.1512 2.0725 0.0425  -0.0478 -0.0914 215 GLY D CA  
10552 C C   . GLY D 215 ? 1.1486 2.0974 2.0204 0.0432  -0.0563 -0.0861 215 GLY D C   
10553 O O   . GLY D 215 ? 1.1492 2.0891 2.0133 0.0375  -0.0580 -0.0790 215 GLY D O   
10554 N N   . PHE D 216 ? 1.1379 2.0740 1.9976 0.0500  -0.0614 -0.0891 216 PHE D N   
10555 C CA  . PHE D 216 ? 1.1484 2.0598 1.9846 0.0511  -0.0686 -0.0840 216 PHE D CA  
10556 C C   . PHE D 216 ? 1.0843 1.9827 1.9250 0.0549  -0.0831 -0.0855 216 PHE D C   
10557 O O   . PHE D 216 ? 1.0927 1.9995 1.9531 0.0593  -0.0888 -0.0922 216 PHE D O   
10558 C CB  . PHE D 216 ? 1.1880 2.0915 2.0083 0.0560  -0.0665 -0.0861 216 PHE D CB  
10559 C CG  . PHE D 216 ? 1.1540 2.0605 1.9861 0.0643  -0.0716 -0.0952 216 PHE D CG  
10560 C CD1 . PHE D 216 ? 1.1340 2.0613 1.9829 0.0664  -0.0641 -0.1023 216 PHE D CD1 
10561 C CD2 . PHE D 216 ? 1.1024 1.9907 1.9286 0.0703  -0.0837 -0.0967 216 PHE D CD2 
10562 C CE1 . PHE D 216 ? 1.0794 2.0092 1.9397 0.0744  -0.0688 -0.1110 216 PHE D CE1 
10563 C CE2 . PHE D 216 ? 1.0801 1.9704 1.9173 0.0782  -0.0887 -0.1048 216 PHE D CE2 
10564 C CZ  . PHE D 216 ? 1.0715 1.9825 1.9262 0.0804  -0.0813 -0.1121 216 PHE D CZ  
10565 N N   . TRP D 217 ? 1.0253 1.9030 1.8472 0.0533  -0.0893 -0.0793 217 TRP D N   
10566 C CA  . TRP D 217 ? 0.9753 1.8379 1.7968 0.0567  -0.1034 -0.0799 217 TRP D CA  
10567 C C   . TRP D 217 ? 0.9371 1.7752 1.7322 0.0591  -0.1083 -0.0759 217 TRP D C   
10568 O O   . TRP D 217 ? 0.9808 1.8115 1.7577 0.0549  -0.1022 -0.0697 217 TRP D O   
10569 C CB  . TRP D 217 ? 1.0008 1.8641 1.8297 0.0508  -0.1070 -0.0763 217 TRP D CB  
10570 C CG  . TRP D 217 ? 1.0077 1.8562 1.8361 0.0542  -0.1218 -0.0773 217 TRP D CG  
10571 C CD1 . TRP D 217 ? 0.9954 1.8505 1.8441 0.0584  -0.1310 -0.0834 217 TRP D CD1 
10572 C CD2 . TRP D 217 ? 1.0000 1.8245 1.8060 0.0542  -0.1294 -0.0722 217 TRP D CD2 
10573 N NE1 . TRP D 217 ? 1.0227 1.8590 1.8622 0.0608  -0.1442 -0.0822 217 TRP D NE1 
10574 C CE2 . TRP D 217 ? 0.9876 1.8049 1.8006 0.0583  -0.1432 -0.0754 217 TRP D CE2 
10575 C CE3 . TRP D 217 ? 0.9890 1.7979 1.7700 0.0512  -0.1257 -0.0653 217 TRP D CE3 
10576 C CZ2 . TRP D 217 ? 0.9484 1.7430 1.7429 0.0593  -0.1531 -0.0719 217 TRP D CZ2 
10577 C CZ3 . TRP D 217 ? 1.0044 1.7913 1.7682 0.0523  -0.1352 -0.0621 217 TRP D CZ3 
10578 C CH2 . TRP D 217 ? 0.9773 1.7571 1.7473 0.0562  -0.1486 -0.0654 217 TRP D CH2 
10579 N N   . MET D 218 ? 0.8893 1.7151 1.6826 0.0659  -0.1194 -0.0792 218 MET D N   
10580 C CA  . MET D 218 ? 0.9052 1.7074 1.6741 0.0686  -0.1244 -0.0758 218 MET D CA  
10581 C C   . MET D 218 ? 0.8958 1.6844 1.6657 0.0741  -0.1390 -0.0780 218 MET D C   
10582 O O   . MET D 218 ? 0.9217 1.7177 1.7083 0.0797  -0.1443 -0.0845 218 MET D O   
10583 C CB  . MET D 218 ? 1.0014 1.8032 1.7623 0.0722  -0.1183 -0.0781 218 MET D CB  
10584 C CG  . MET D 218 ? 1.0303 1.8084 1.7681 0.0754  -0.1236 -0.0752 218 MET D CG  
10585 S SD  . MET D 218 ? 1.0638 1.8264 1.7760 0.0687  -0.1198 -0.0655 218 MET D SD  
10586 C CE  . MET D 218 ? 1.1424 1.9220 1.8546 0.0639  -0.1040 -0.0643 218 MET D CE  
10587 N N   . ASP D 219 ? 0.9182 1.6870 1.6699 0.0727  -0.1456 -0.0726 219 ASP D N   
10588 C CA  . ASP D 219 ? 0.9174 1.6701 1.6650 0.0779  -0.1597 -0.0737 219 ASP D CA  
10589 C C   . ASP D 219 ? 0.9941 1.7281 1.7212 0.0825  -0.1617 -0.0723 219 ASP D C   
10590 O O   . ASP D 219 ? 1.0234 1.7426 1.7284 0.0797  -0.1590 -0.0664 219 ASP D O   
10591 C CB  . ASP D 219 ? 0.8971 1.6390 1.6368 0.0737  -0.1659 -0.0690 219 ASP D CB  
10592 C CG  . ASP D 219 ? 0.8965 1.6254 1.6357 0.0788  -0.1813 -0.0709 219 ASP D CG  
10593 O OD1 . ASP D 219 ? 0.9176 1.6325 1.6458 0.0848  -0.1871 -0.0716 219 ASP D OD1 
10594 O OD2 . ASP D 219 ? 0.9124 1.6448 1.6622 0.0768  -0.1879 -0.0717 219 ASP D OD2 
10595 N N   . ILE D 220 ? 1.1155 1.8501 1.8505 0.0895  -0.1662 -0.0777 220 ILE D N   
10596 C CA  . ILE D 220 ? 1.1150 1.8323 1.8328 0.0942  -0.1682 -0.0770 220 ILE D CA  
10597 C C   . ILE D 220 ? 1.0893 1.7854 1.7953 0.0977  -0.1819 -0.0747 220 ILE D C   
10598 O O   . ILE D 220 ? 1.0726 1.7690 1.7908 0.1032  -0.1922 -0.0789 220 ILE D O   
10599 C CB  . ILE D 220 ? 1.1603 1.8874 1.8916 0.1001  -0.1664 -0.0839 220 ILE D CB  
10600 C CG1 . ILE D 220 ? 1.1249 1.8730 1.8662 0.0964  -0.1525 -0.0861 220 ILE D CG1 
10601 C CG2 . ILE D 220 ? 1.2099 1.9174 1.9235 0.1047  -0.1693 -0.0829 220 ILE D CG2 
10602 C CD1 . ILE D 220 ? 1.0868 1.8590 1.8552 0.0956  -0.1503 -0.0912 220 ILE D CD1 
10603 N N   . GLY D 221 ? 1.0302 1.7080 1.7122 0.0947  -0.1821 -0.0682 221 GLY D N   
10604 C CA  . GLY D 221 ? 1.1026 1.7587 1.7696 0.0976  -0.1940 -0.0654 221 GLY D CA  
10605 C C   . GLY D 221 ? 1.1427 1.7779 1.7841 0.0984  -0.1925 -0.0608 221 GLY D C   
10606 O O   . GLY D 221 ? 1.2331 1.8483 1.8573 0.0999  -0.2007 -0.0572 221 GLY D O   
10607 N N   . GLN D 222 ? 1.0663 1.7061 1.7050 0.0974  -0.1821 -0.0609 222 GLN D N   
10608 C CA  . GLN D 222 ? 1.0185 1.6406 1.6350 0.0976  -0.1793 -0.0569 222 GLN D CA  
10609 C C   . GLN D 222 ? 1.0132 1.6440 1.6364 0.0996  -0.1718 -0.0608 222 GLN D C   
10610 O O   . GLN D 222 ? 1.0166 1.6680 1.6563 0.0980  -0.1645 -0.0646 222 GLN D O   
10611 C CB  . GLN D 222 ? 0.9999 1.6158 1.5987 0.0908  -0.1721 -0.0504 222 GLN D CB  
10612 C CG  . GLN D 222 ? 1.0162 1.6516 1.6247 0.0852  -0.1607 -0.0505 222 GLN D CG  
10613 C CD  . GLN D 222 ? 1.0634 1.6930 1.6572 0.0789  -0.1558 -0.0442 222 GLN D CD  
10614 O OE1 . GLN D 222 ? 1.1079 1.7214 1.6877 0.0785  -0.1620 -0.0406 222 GLN D OE1 
10615 N NE2 . GLN D 222 ? 1.0705 1.7130 1.6671 0.0741  -0.1447 -0.0430 222 GLN D NE2 
10616 N N   . PRO D 223 ? 1.0054 1.6207 1.6161 0.1030  -0.1733 -0.0600 223 PRO D N   
10617 C CA  . PRO D 223 ? 1.0398 1.6625 1.6574 0.1054  -0.1672 -0.0646 223 PRO D CA  
10618 C C   . PRO D 223 ? 1.0153 1.6500 1.6312 0.0998  -0.1539 -0.0638 223 PRO D C   
10619 O O   . PRO D 223 ? 1.0475 1.6948 1.6742 0.1012  -0.1481 -0.0689 223 PRO D O   
10620 C CB  . PRO D 223 ? 1.0551 1.6549 1.6561 0.1091  -0.1723 -0.0624 223 PRO D CB  
10621 C CG  . PRO D 223 ? 1.0167 1.5983 1.5973 0.1063  -0.1765 -0.0552 223 PRO D CG  
10622 C CD  . PRO D 223 ? 0.9825 1.5727 1.5727 0.1050  -0.1813 -0.0554 223 PRO D CD  
10623 N N   . ARG D 224 ? 1.0058 1.6371 1.6084 0.0937  -0.1489 -0.0577 224 ARG D N   
10624 C CA  . ARG D 224 ? 1.0243 1.6668 1.6250 0.0887  -0.1368 -0.0566 224 ARG D CA  
10625 C C   . ARG D 224 ? 1.0277 1.6943 1.6473 0.0863  -0.1312 -0.0599 224 ARG D C   
10626 O O   . ARG D 224 ? 1.0467 1.7254 1.6678 0.0832  -0.1212 -0.0604 224 ARG D O   
10627 C CB  . ARG D 224 ? 1.0749 1.7062 1.6560 0.0833  -0.1333 -0.0491 224 ARG D CB  
10628 C CG  . ARG D 224 ? 1.0786 1.7099 1.6596 0.0802  -0.1367 -0.0457 224 ARG D CG  
10629 C CD  . ARG D 224 ? 1.0696 1.6887 1.6308 0.0754  -0.1331 -0.0387 224 ARG D CD  
10630 N NE  . ARG D 224 ? 1.0874 1.6854 1.6299 0.0773  -0.1361 -0.0358 224 ARG D NE  
10631 C CZ  . ARG D 224 ? 1.1430 1.7237 1.6757 0.0798  -0.1454 -0.0339 224 ARG D CZ  
10632 N NH1 . ARG D 224 ? 1.1227 1.7050 1.6629 0.0809  -0.1532 -0.0350 224 ARG D NH1 
10633 N NH2 . ARG D 224 ? 1.1897 1.7516 1.7050 0.0811  -0.1470 -0.0309 224 ARG D NH2 
10634 N N   . ASP D 225 ? 1.0107 1.6845 1.6446 0.0876  -0.1372 -0.0620 225 ASP D N   
10635 C CA  . ASP D 225 ? 1.0485 1.7454 1.7016 0.0851  -0.1318 -0.0651 225 ASP D CA  
10636 C C   . ASP D 225 ? 1.0827 1.7953 1.7528 0.0890  -0.1283 -0.0727 225 ASP D C   
10637 O O   . ASP D 225 ? 1.1165 1.8496 1.8022 0.0869  -0.1222 -0.0756 225 ASP D O   
10638 C CB  . ASP D 225 ? 1.0212 1.7208 1.6853 0.0851  -0.1397 -0.0653 225 ASP D CB  
10639 C CG  . ASP D 225 ? 1.0145 1.7037 1.6647 0.0799  -0.1408 -0.0584 225 ASP D CG  
10640 O OD1 . ASP D 225 ? 1.0814 1.7636 1.7151 0.0762  -0.1343 -0.0534 225 ASP D OD1 
10641 O OD2 . ASP D 225 ? 0.9918 1.6799 1.6480 0.0797  -0.1482 -0.0582 225 ASP D OD2 
10642 N N   . TYR D 226 ? 1.1145 1.8180 1.7818 0.0946  -0.1318 -0.0762 226 TYR D N   
10643 C CA  . TYR D 226 ? 1.1137 1.8311 1.7973 0.0989  -0.1290 -0.0841 226 TYR D CA  
10644 C C   . TYR D 226 ? 1.0959 1.8257 1.7775 0.0954  -0.1166 -0.0852 226 TYR D C   
10645 O O   . TYR D 226 ? 1.0357 1.7841 1.7333 0.0967  -0.1113 -0.0914 226 TYR D O   
10646 C CB  . TYR D 226 ? 1.1667 1.8690 1.8474 0.1059  -0.1369 -0.0873 226 TYR D CB  
10647 C CG  . TYR D 226 ? 1.1776 1.8767 1.8704 0.1115  -0.1489 -0.0900 226 TYR D CG  
10648 C CD1 . TYR D 226 ? 1.1415 1.8593 1.8562 0.1120  -0.1498 -0.0942 226 TYR D CD1 
10649 C CD2 . TYR D 226 ? 1.2286 1.9060 1.9109 0.1161  -0.1593 -0.0882 226 TYR D CD2 
10650 C CE1 . TYR D 226 ? 1.2136 1.9292 1.9402 0.1172  -0.1613 -0.0969 226 TYR D CE1 
10651 C CE2 . TYR D 226 ? 1.2484 1.9227 1.9412 0.1214  -0.1709 -0.0905 226 TYR D CE2 
10652 C CZ  . TYR D 226 ? 1.3033 1.9970 2.0187 0.1221  -0.1721 -0.0950 226 TYR D CZ  
10653 O OH  . TYR D 226 ? 1.3298 2.0210 2.0567 0.1276  -0.1842 -0.0976 226 TYR D OH  
10654 N N   . ILE D 227 ? 1.1716 1.8919 1.8343 0.0911  -0.1117 -0.0795 227 ILE D N   
10655 C CA  . ILE D 227 ? 1.1995 1.9310 1.8594 0.0880  -0.1006 -0.0805 227 ILE D CA  
10656 C C   . ILE D 227 ? 1.2024 1.9519 1.8687 0.0823  -0.0928 -0.0782 227 ILE D C   
10657 O O   . ILE D 227 ? 1.1834 1.9497 1.8566 0.0810  -0.0843 -0.0816 227 ILE D O   
10658 C CB  . ILE D 227 ? 1.2616 1.9769 1.9000 0.0858  -0.0985 -0.0755 227 ILE D CB  
10659 C CG1 . ILE D 227 ? 1.1841 1.8861 1.8083 0.0817  -0.1012 -0.0671 227 ILE D CG1 
10660 C CG2 . ILE D 227 ? 1.2020 1.9020 1.8358 0.0913  -0.1043 -0.0787 227 ILE D CG2 
10661 C CD1 . ILE D 227 ? 1.1702 1.8559 1.7739 0.0796  -0.0994 -0.0621 227 ILE D CD1 
10662 N N   . THR D 228 ? 1.1754 1.9215 1.8393 0.0787  -0.0955 -0.0725 228 THR D N   
10663 C CA  . THR D 228 ? 1.1583 1.9205 1.8292 0.0731  -0.0886 -0.0700 228 THR D CA  
10664 C C   . THR D 228 ? 1.1626 1.9416 1.8563 0.0745  -0.0901 -0.0750 228 THR D C   
10665 O O   . THR D 228 ? 1.2132 2.0105 1.9167 0.0709  -0.0821 -0.0755 228 THR D O   
10666 C CB  . THR D 228 ? 1.2208 1.9718 1.8791 0.0682  -0.0903 -0.0618 228 THR D CB  
10667 O OG1 . THR D 228 ? 1.2683 2.0344 1.9337 0.0627  -0.0836 -0.0592 228 THR D OG1 
10668 C CG2 . THR D 228 ? 1.1519 1.8895 1.8108 0.0708  -0.1018 -0.0611 228 THR D CG2 
10669 N N   . GLY D 229 ? 1.1515 1.9248 1.8542 0.0797  -0.1001 -0.0787 229 GLY D N   
10670 C CA  . GLY D 229 ? 1.1217 1.9119 1.8480 0.0817  -0.1017 -0.0843 229 GLY D CA  
10671 C C   . GLY D 229 ? 1.1279 1.9337 1.8671 0.0853  -0.0959 -0.0923 229 GLY D C   
10672 O O   . GLY D 229 ? 1.1247 1.9503 1.8832 0.0850  -0.0921 -0.0966 229 GLY D O   
10673 N N   . LEU D 230 ? 1.0757 1.8730 1.8046 0.0886  -0.0949 -0.0945 230 LEU D N   
10674 C CA  . LEU D 230 ? 1.0304 1.8417 1.7693 0.0918  -0.0887 -0.1023 230 LEU D CA  
10675 C C   . LEU D 230 ? 1.0447 1.8731 1.7829 0.0862  -0.0759 -0.1012 230 LEU D C   
10676 O O   . LEU D 230 ? 1.0274 1.8739 1.7789 0.0876  -0.0695 -0.1077 230 LEU D O   
10677 C CB  . LEU D 230 ? 0.9822 1.7781 1.7092 0.0964  -0.0914 -0.1046 230 LEU D CB  
10678 C CG  . LEU D 230 ? 0.9016 1.7079 1.6381 0.1010  -0.0870 -0.1137 230 LEU D CG  
10679 C CD1 . LEU D 230 ? 0.8086 1.6016 1.5490 0.1088  -0.0970 -0.1185 230 LEU D CD1 
10680 C CD2 . LEU D 230 ? 0.9329 1.7386 1.6543 0.0980  -0.0785 -0.1127 230 LEU D CD2 
10681 N N   . ARG D 231 ? 1.0828 1.9058 1.8054 0.0799  -0.0721 -0.0931 231 ARG D N   
10682 C CA  . ARG D 231 ? 1.1396 1.9782 1.8610 0.0742  -0.0606 -0.0909 231 ARG D CA  
10683 C C   . ARG D 231 ? 1.1737 2.0317 1.9142 0.0717  -0.0573 -0.0920 231 ARG D C   
10684 O O   . ARG D 231 ? 1.1450 2.0220 1.8951 0.0709  -0.0486 -0.0960 231 ARG D O   
10685 C CB  . ARG D 231 ? 1.1640 1.9913 1.8655 0.0685  -0.0586 -0.0815 231 ARG D CB  
10686 C CG  . ARG D 231 ? 1.1952 2.0369 1.8944 0.0623  -0.0477 -0.0777 231 ARG D CG  
10687 C CD  . ARG D 231 ? 1.2161 2.0733 1.9193 0.0637  -0.0394 -0.0839 231 ARG D CD  
10688 N NE  . ARG D 231 ? 1.3306 2.1905 2.0193 0.0593  -0.0312 -0.0796 231 ARG D NE  
10689 C CZ  . ARG D 231 ? 1.3330 2.2051 2.0212 0.0598  -0.0236 -0.0842 231 ARG D CZ  
10690 N NH1 . ARG D 231 ? 1.2059 2.0883 1.9074 0.0645  -0.0228 -0.0934 231 ARG D NH1 
10691 N NH2 . ARG D 231 ? 1.3416 2.2155 2.0159 0.0558  -0.0170 -0.0798 231 ARG D NH2 
10692 N N   . LEU D 232 ? 1.3840 2.2375 2.1304 0.0704  -0.0641 -0.0887 232 LEU D N   
10693 C CA  . LEU D 232 ? 1.3718 2.2432 2.1377 0.0676  -0.0615 -0.0898 232 LEU D CA  
10694 C C   . LEU D 232 ? 1.3621 2.2493 2.1496 0.0730  -0.0611 -0.0995 232 LEU D C   
10695 O O   . LEU D 232 ? 1.3498 2.2575 2.1526 0.0705  -0.0538 -0.1019 232 LEU D O   
10696 C CB  . LEU D 232 ? 1.3934 2.2552 2.1618 0.0659  -0.0705 -0.0854 232 LEU D CB  
10697 C CG  . LEU D 232 ? 1.4415 2.2882 2.1902 0.0605  -0.0709 -0.0760 232 LEU D CG  
10698 C CD1 . LEU D 232 ? 1.4029 2.2417 2.1562 0.0592  -0.0801 -0.0731 232 LEU D CD1 
10699 C CD2 . LEU D 232 ? 1.5199 2.3781 2.2644 0.0537  -0.0592 -0.0712 232 LEU D CD2 
10700 N N   . TYR D 233 ? 1.1166 1.9946 1.9059 0.0803  -0.0687 -0.1051 233 TYR D N   
10701 C CA  . TYR D 233 ? 1.0450 1.9372 1.8552 0.0861  -0.0689 -0.1149 233 TYR D CA  
10702 C C   . TYR D 233 ? 0.9790 1.8853 1.7891 0.0864  -0.0575 -0.1198 233 TYR D C   
10703 O O   . TYR D 233 ? 0.9323 1.8599 1.7598 0.0863  -0.0506 -0.1250 233 TYR D O   
10704 C CB  . TYR D 233 ? 0.9765 1.8531 1.7875 0.0941  -0.0808 -0.1190 233 TYR D CB  
10705 C CG  . TYR D 233 ? 0.9485 1.8377 1.7803 0.1012  -0.0815 -0.1295 233 TYR D CG  
10706 C CD1 . TYR D 233 ? 0.9397 1.8437 1.7958 0.1028  -0.0842 -0.1337 233 TYR D CD1 
10707 C CD2 . TYR D 233 ? 0.9399 1.8261 1.7676 0.1063  -0.0796 -0.1354 233 TYR D CD2 
10708 C CE1 . TYR D 233 ? 0.8769 1.7930 1.7530 0.1096  -0.0847 -0.1436 233 TYR D CE1 
10709 C CE2 . TYR D 233 ? 0.9156 1.8130 1.7626 0.1132  -0.0802 -0.1454 233 TYR D CE2 
10710 C CZ  . TYR D 233 ? 0.8482 1.7607 1.7195 0.1149  -0.0827 -0.1494 233 TYR D CZ  
10711 O OH  . TYR D 233 ? 0.8418 1.7658 1.7331 0.1221  -0.0832 -0.1597 233 TYR D OH  
10712 N N   . LEU D 234 ? 0.9706 1.8657 1.7615 0.0867  -0.0553 -0.1185 234 LEU D N   
10713 C CA  . LEU D 234 ? 0.9220 1.8294 1.7111 0.0871  -0.0451 -0.1235 234 LEU D CA  
10714 C C   . LEU D 234 ? 0.8967 1.8211 1.6850 0.0798  -0.0334 -0.1196 234 LEU D C   
10715 O O   . LEU D 234 ? 0.8216 1.7633 1.6164 0.0801  -0.0243 -0.1250 234 LEU D O   
10716 C CB  . LEU D 234 ? 0.9696 1.8601 1.7378 0.0884  -0.0460 -0.1225 234 LEU D CB  
10717 C CG  . LEU D 234 ? 0.9279 1.8041 1.6970 0.0961  -0.0550 -0.1282 234 LEU D CG  
10718 C CD1 . LEU D 234 ? 0.9117 1.7751 1.6618 0.0965  -0.0535 -0.1279 234 LEU D CD1 
10719 C CD2 . LEU D 234 ? 0.8878 1.7788 1.6787 0.1024  -0.0544 -0.1390 234 LEU D CD2 
10720 N N   . ASP D 235 ? 0.9702 1.8895 1.7502 0.0735  -0.0334 -0.1102 235 ASP D N   
10721 C CA  . ASP D 235 ? 0.9326 1.8674 1.7129 0.0665  -0.0229 -0.1058 235 ASP D CA  
10722 C C   . ASP D 235 ? 0.8571 1.8131 1.6615 0.0662  -0.0191 -0.1104 235 ASP D C   
10723 O O   . ASP D 235 ? 0.7904 1.7650 1.6000 0.0638  -0.0084 -0.1125 235 ASP D O   
10724 C CB  . ASP D 235 ? 0.9909 1.9142 1.7585 0.0602  -0.0248 -0.0949 235 ASP D CB  
10725 C CG  . ASP D 235 ? 0.9731 1.9096 1.7378 0.0529  -0.0140 -0.0893 235 ASP D CG  
10726 O OD1 . ASP D 235 ? 0.9173 1.8697 1.6846 0.0526  -0.0046 -0.0930 235 ASP D OD1 
10727 O OD2 . ASP D 235 ? 1.0678 1.9985 1.8274 0.0476  -0.0150 -0.0810 235 ASP D OD2 
10728 N N   . SER D 236 ? 0.8688 1.8227 1.6886 0.0685  -0.0278 -0.1120 236 SER D N   
10729 C CA  . SER D 236 ? 0.8203 1.7930 1.6642 0.0687  -0.0250 -0.1168 236 SER D CA  
10730 C C   . SER D 236 ? 0.7911 1.7712 1.6422 0.0743  -0.0204 -0.1260 236 SER D C   
10731 O O   . SER D 236 ? 0.8243 1.8175 1.6866 0.0727  -0.0126 -0.1283 236 SER D O   
10732 C CB  . SER D 236 ? 0.9035 1.8697 1.7609 0.0707  -0.0368 -0.1169 236 SER D CB  
10733 O OG  . SER D 236 ? 0.9618 1.9391 1.8380 0.0700  -0.0339 -0.1194 236 SER D OG  
10734 N N   . LEU D 237 ? 0.7823 1.7543 1.6274 0.0808  -0.0251 -0.1316 237 LEU D N   
10735 C CA  . LEU D 237 ? 0.7863 1.7650 1.6374 0.0864  -0.0207 -0.1409 237 LEU D CA  
10736 C C   . LEU D 237 ? 0.7678 1.7581 1.6092 0.0826  -0.0071 -0.1411 237 LEU D C   
10737 O O   . LEU D 237 ? 0.7803 1.7820 1.6298 0.0844  0.0002  -0.1474 237 LEU D O   
10738 C CB  . LEU D 237 ? 0.7978 1.7641 1.6454 0.0942  -0.0297 -0.1467 237 LEU D CB  
10739 C CG  . LEU D 237 ? 0.7973 1.7588 1.6617 0.1018  -0.0395 -0.1530 237 LEU D CG  
10740 C CD1 . LEU D 237 ? 0.8313 1.7876 1.7036 0.0999  -0.0484 -0.1476 237 LEU D CD1 
10741 C CD2 . LEU D 237 ? 0.7677 1.7150 1.6265 0.1092  -0.0478 -0.1580 237 LEU D CD2 
10742 N N   . ARG D 238 ? 0.7305 1.7183 1.5542 0.0775  -0.0037 -0.1344 238 ARG D N   
10743 C CA  . ARG D 238 ? 0.7010 1.7000 1.5146 0.0732  0.0090  -0.1335 238 ARG D CA  
10744 C C   . ARG D 238 ? 0.7067 1.7198 1.5298 0.0678  0.0181  -0.1308 238 ARG D C   
10745 O O   . ARG D 238 ? 0.6994 1.7243 1.5187 0.0658  0.0291  -0.1326 238 ARG D O   
10746 C CB  . ARG D 238 ? 0.7164 1.7088 1.5096 0.0685  0.0099  -0.1256 238 ARG D CB  
10747 C CG  . ARG D 238 ? 0.6918 1.6825 1.4690 0.0702  0.0146  -0.1290 238 ARG D CG  
10748 C CD  . ARG D 238 ? 0.6987 1.6822 1.4809 0.0785  0.0083  -0.1388 238 ARG D CD  
10749 N NE  . ARG D 238 ? 0.6604 1.6583 1.4458 0.0815  0.0163  -0.1483 238 ARG D NE  
10750 C CZ  . ARG D 238 ? 0.6456 1.6365 1.4193 0.0848  0.0162  -0.1532 238 ARG D CZ  
10751 N NH1 . ARG D 238 ? 0.6986 1.6682 1.4571 0.0853  0.0087  -0.1493 238 ARG D NH1 
10752 N NH2 . ARG D 238 ? 0.6198 1.6249 1.3973 0.0874  0.0237  -0.1624 238 ARG D NH2 
10753 N N   . LYS D 239 ? 0.7227 1.7348 1.5579 0.0654  0.0137  -0.1267 239 LYS D N   
10754 C CA  . LYS D 239 ? 0.7488 1.7738 1.5956 0.0601  0.0215  -0.1239 239 LYS D CA  
10755 C C   . LYS D 239 ? 0.8022 1.8348 1.6696 0.0648  0.0213  -0.1320 239 LYS D C   
10756 O O   . LYS D 239 ? 0.7716 1.8183 1.6454 0.0633  0.0316  -0.1347 239 LYS D O   
10757 C CB  . LYS D 239 ? 0.7128 1.7330 1.5618 0.0542  0.0169  -0.1148 239 LYS D CB  
10758 C CG  . LYS D 239 ? 0.7251 1.7337 1.5556 0.0517  0.0128  -0.1077 239 LYS D CG  
10759 C CD  . LYS D 239 ? 0.7730 1.7747 1.6079 0.0478  0.0054  -0.1009 239 LYS D CD  
10760 C CE  . LYS D 239 ? 0.7940 1.7838 1.6103 0.0456  0.0014  -0.0940 239 LYS D CE  
10761 N NZ  . LYS D 239 ? 0.8085 1.7804 1.6248 0.0469  -0.0113 -0.0913 239 LYS D NZ  
10762 N N   . LYS D 240 ? 0.8405 1.8640 1.7181 0.0707  0.0095  -0.1358 240 LYS D N   
10763 C CA  . LYS D 240 ? 0.8299 1.8599 1.7279 0.0756  0.0080  -0.1430 240 LYS D CA  
10764 C C   . LYS D 240 ? 0.8788 1.9159 1.7772 0.0811  0.0144  -0.1526 240 LYS D C   
10765 O O   . LYS D 240 ? 0.8961 1.9477 1.8033 0.0800  0.0243  -0.1559 240 LYS D O   
10766 C CB  . LYS D 240 ? 0.8050 1.8222 1.7115 0.0813  -0.0071 -0.1449 240 LYS D CB  
10767 C CG  . LYS D 240 ? 0.7656 1.7759 1.6741 0.0766  -0.0148 -0.1369 240 LYS D CG  
10768 C CD  . LYS D 240 ? 0.8046 1.8278 1.7265 0.0701  -0.0083 -0.1331 240 LYS D CD  
10769 C CE  . LYS D 240 ? 0.9031 1.9190 1.8306 0.0670  -0.0181 -0.1272 240 LYS D CE  
10770 N NZ  . LYS D 240 ? 0.8859 1.8874 1.8146 0.0742  -0.0330 -0.1306 240 LYS D NZ  
10771 N N   . SER D 241 ? 1.1344 2.1615 2.0237 0.0871  0.0090  -0.1574 241 SER D N   
10772 C CA  . SER D 241 ? 1.1402 2.1725 2.0296 0.0929  0.0138  -0.1673 241 SER D CA  
10773 C C   . SER D 241 ? 1.1345 2.1587 2.0037 0.0936  0.0136  -0.1674 241 SER D C   
10774 O O   . SER D 241 ? 1.1309 2.1413 1.9963 0.0983  0.0034  -0.1688 241 SER D O   
10775 C CB  . SER D 241 ? 1.1491 2.1774 2.0547 0.1018  0.0053  -0.1759 241 SER D CB  
10776 O OG  . SER D 241 ? 1.2061 2.2187 2.1120 0.1045  -0.0087 -0.1730 241 SER D OG  
10777 N N   . PRO D 242 ? 0.8336 1.8664 1.6897 0.0890  0.0246  -0.1659 242 PRO D N   
10778 C CA  . PRO D 242 ? 0.7764 1.8024 1.6132 0.0891  0.0245  -0.1655 242 PRO D CA  
10779 C C   . PRO D 242 ? 0.7459 1.7702 1.5826 0.0968  0.0232  -0.1766 242 PRO D C   
10780 O O   . PRO D 242 ? 0.7386 1.7556 1.5614 0.0977  0.0210  -0.1771 242 PRO D O   
10781 C CB  . PRO D 242 ? 0.7386 1.7761 1.5631 0.0817  0.0369  -0.1604 242 PRO D CB  
10782 C CG  . PRO D 242 ? 0.7771 1.8298 1.6156 0.0807  0.0457  -0.1636 242 PRO D CG  
10783 C CD  . PRO D 242 ? 0.8177 1.8669 1.6760 0.0834  0.0376  -0.1641 242 PRO D CD  
10784 N N   . ALA D 243 ? 0.7210 1.7520 1.5732 0.1022  0.0246  -0.1857 243 ALA D N   
10785 C CA  . ALA D 243 ? 0.6624 1.6917 1.5163 0.1100  0.0233  -0.1970 243 ALA D CA  
10786 C C   . ALA D 243 ? 0.6473 1.6611 1.5087 0.1172  0.0094  -0.2002 243 ALA D C   
10787 O O   . ALA D 243 ? 0.6045 1.6150 1.4683 0.1240  0.0069  -0.2096 243 ALA D O   
10788 C CB  . ALA D 243 ? 0.6582 1.7024 1.5253 0.1129  0.0317  -0.2059 243 ALA D CB  
10789 N N   . LYS D 244 ? 0.6652 1.6694 1.5302 0.1158  0.0003  -0.1928 244 LYS D N   
10790 C CA  . LYS D 244 ? 0.6356 1.6242 1.5057 0.1223  -0.0134 -0.1947 244 LYS D CA  
10791 C C   . LYS D 244 ? 0.7035 1.6788 1.5572 0.1216  -0.0191 -0.1907 244 LYS D C   
10792 O O   . LYS D 244 ? 0.7311 1.6908 1.5855 0.1269  -0.0301 -0.1920 244 LYS D O   
10793 C CB  . LYS D 244 ? 0.6710 1.6557 1.5531 0.1217  -0.0213 -0.1892 244 LYS D CB  
10794 C CG  . LYS D 244 ? 0.7564 1.7541 1.6570 0.1222  -0.0168 -0.1924 244 LYS D CG  
10795 C CD  . LYS D 244 ? 0.6514 1.6464 1.5678 0.1318  -0.0232 -0.2023 244 LYS D CD  
10796 C CE  . LYS D 244 ? 0.5212 1.5306 1.4447 0.1344  -0.0125 -0.2117 244 LYS D CE  
10797 N NZ  . LYS D 244 ? 0.4302 1.4358 1.3681 0.1444  -0.0190 -0.2218 244 LYS D NZ  
10798 N N   . LEU D 245 ? 0.7141 1.6930 1.5513 0.1150  -0.0119 -0.1853 245 LEU D N   
10799 C CA  . LEU D 245 ? 0.6640 1.6224 1.4778 0.1124  -0.0158 -0.1785 245 LEU D CA  
10800 C C   . LEU D 245 ? 0.6659 1.6250 1.4684 0.1137  -0.0099 -0.1848 245 LEU D C   
10801 O O   . LEU D 245 ? 0.6539 1.6309 1.4562 0.1113  0.0009  -0.1880 245 LEU D O   
10802 C CB  . LEU D 245 ? 0.6490 1.6064 1.4495 0.1036  -0.0127 -0.1665 245 LEU D CB  
10803 C CG  . LEU D 245 ? 0.6814 1.6396 1.4924 0.1011  -0.0175 -0.1600 245 LEU D CG  
10804 C CD1 . LEU D 245 ? 0.7497 1.7314 1.5757 0.0978  -0.0083 -0.1612 245 LEU D CD1 
10805 C CD2 . LEU D 245 ? 0.7036 1.6463 1.4965 0.0950  -0.0208 -0.1480 245 LEU D CD2 
10806 N N   . THR D 246 ? 0.6867 1.6263 1.4796 0.1175  -0.0170 -0.1864 246 THR D N   
10807 C CA  . THR D 246 ? 0.6941 1.6330 1.4777 0.1193  -0.0126 -0.1934 246 THR D CA  
10808 C C   . THR D 246 ? 0.6699 1.6125 1.4341 0.1118  -0.0047 -0.1875 246 THR D C   
10809 O O   . THR D 246 ? 0.6476 1.5853 1.4014 0.1058  -0.0051 -0.1766 246 THR D O   
10810 C CB  . THR D 246 ? 0.6788 1.5943 1.4560 0.1240  -0.0224 -0.1953 246 THR D CB  
10811 O OG1 . THR D 246 ? 0.6468 1.5626 1.4169 0.1259  -0.0182 -0.2032 246 THR D OG1 
10812 C CG2 . THR D 246 ? 0.7294 1.6249 1.4888 0.1193  -0.0282 -0.1836 246 THR D CG2 
10813 N N   . SER D 247 ? 0.6696 1.6208 1.4289 0.1126  0.0024  -0.1949 247 SER D N   
10814 C CA  . SER D 247 ? 0.6481 1.6042 1.3893 0.1063  0.0100  -0.1907 247 SER D CA  
10815 C C   . SER D 247 ? 0.6285 1.5789 1.3600 0.1090  0.0106  -0.1986 247 SER D C   
10816 O O   . SER D 247 ? 0.6156 1.5635 1.3569 0.1157  0.0078  -0.2088 247 SER D O   
10817 C CB  . SER D 247 ? 0.6199 1.6006 1.3660 0.1027  0.0213  -0.1910 247 SER D CB  
10818 O OG  . SER D 247 ? 0.6290 1.6140 1.3567 0.0972  0.0282  -0.1871 247 SER D OG  
10819 N N   . GLY D 248 ? 0.6041 1.5523 1.3167 0.1038  0.0141  -0.1939 248 GLY D N   
10820 C CA  . GLY D 248 ? 0.5875 1.5308 1.2897 0.1053  0.0148  -0.2009 248 GLY D CA  
10821 C C   . GLY D 248 ? 0.5851 1.5204 1.2664 0.0992  0.0153  -0.1928 248 GLY D C   
10822 O O   . GLY D 248 ? 0.5696 1.5036 1.2438 0.0938  0.0157  -0.1816 248 GLY D O   
10823 N N   . PRO D 249 ? 0.6289 1.5586 1.3003 0.1001  0.0152  -0.1987 249 PRO D N   
10824 C CA  . PRO D 249 ? 0.6035 1.5263 1.2559 0.0944  0.0153  -0.1916 249 PRO D CA  
10825 C C   . PRO D 249 ? 0.5987 1.4996 1.2452 0.0929  0.0068  -0.1827 249 PRO D C   
10826 O O   . PRO D 249 ? 0.6443 1.5406 1.2773 0.0875  0.0071  -0.1736 249 PRO D O   
10827 C CB  . PRO D 249 ? 0.6566 1.5799 1.3031 0.0966  0.0169  -0.2023 249 PRO D CB  
10828 C CG  . PRO D 249 ? 0.6621 1.5808 1.3237 0.1039  0.0130  -0.2129 249 PRO D CG  
10829 C CD  . PRO D 249 ? 0.6780 1.6074 1.3560 0.1062  0.0145  -0.2123 249 PRO D CD  
10830 N N   . HIS D 250 ? 0.6025 1.4898 1.2587 0.0976  -0.0007 -0.1849 250 HIS D N   
10831 C CA  . HIS D 250 ? 0.6292 1.4953 1.2800 0.0965  -0.0088 -0.1766 250 HIS D CA  
10832 C C   . HIS D 250 ? 0.5440 1.4089 1.2019 0.0958  -0.0117 -0.1685 250 HIS D C   
10833 O O   . HIS D 250 ? 0.5776 1.4249 1.2323 0.0956  -0.0188 -0.1621 250 HIS D O   
10834 C CB  . HIS D 250 ? 0.6572 1.5066 1.3122 0.1019  -0.0159 -0.1834 250 HIS D CB  
10835 C CG  . HIS D 250 ? 0.6115 1.4644 1.2846 0.1087  -0.0184 -0.1912 250 HIS D CG  
10836 N ND1 . HIS D 250 ? 0.6088 1.4787 1.2922 0.1123  -0.0128 -0.2021 250 HIS D ND1 
10837 C CD2 . HIS D 250 ? 0.6366 1.4784 1.3196 0.1128  -0.0260 -0.1898 250 HIS D CD2 
10838 C CE1 . HIS D 250 ? 0.6571 1.5266 1.3569 0.1185  -0.0167 -0.2071 250 HIS D CE1 
10839 N NE2 . HIS D 250 ? 0.6451 1.4976 1.3450 0.1189  -0.0251 -0.1998 250 HIS D NE2 
10840 N N   . ILE D 251 ? 0.5290 1.4121 1.1961 0.0952  -0.0062 -0.1687 251 ILE D N   
10841 C CA  . ILE D 251 ? 0.6016 1.4857 1.2775 0.0946  -0.0087 -0.1622 251 ILE D CA  
10842 C C   . ILE D 251 ? 0.6238 1.5163 1.2908 0.0875  -0.0031 -0.1523 251 ILE D C   
10843 O O   . ILE D 251 ? 0.5920 1.5002 1.2551 0.0848  0.0052  -0.1537 251 ILE D O   
10844 C CB  . ILE D 251 ? 0.6327 1.5311 1.3288 0.0994  -0.0071 -0.1701 251 ILE D CB  
10845 C CG1 . ILE D 251 ? 0.6189 1.5080 1.3242 0.1069  -0.0132 -0.1799 251 ILE D CG1 
10846 C CG2 . ILE D 251 ? 0.6639 1.5642 1.3695 0.0982  -0.0098 -0.1633 251 ILE D CG2 
10847 C CD1 . ILE D 251 ? 0.6472 1.5131 1.3506 0.1090  -0.0240 -0.1751 251 ILE D CD1 
10848 N N   . VAL D 252 ? 0.6993 1.5809 1.3626 0.0847  -0.0077 -0.1424 252 VAL D N   
10849 C CA  . VAL D 252 ? 0.7379 1.6250 1.3935 0.0782  -0.0035 -0.1324 252 VAL D CA  
10850 C C   . VAL D 252 ? 0.7710 1.6574 1.4368 0.0777  -0.0070 -0.1271 252 VAL D C   
10851 O O   . VAL D 252 ? 0.7866 1.6579 1.4554 0.0804  -0.0154 -0.1259 252 VAL D O   
10852 C CB  . VAL D 252 ? 0.7402 1.6130 1.3773 0.0742  -0.0053 -0.1247 252 VAL D CB  
10853 C CG1 . VAL D 252 ? 0.7192 1.5978 1.3461 0.0731  -0.0002 -0.1288 252 VAL D CG1 
10854 C CG2 . VAL D 252 ? 0.7542 1.6048 1.3887 0.0769  -0.0146 -0.1235 252 VAL D CG2 
10855 N N   . GLY D 253 ? 0.9595 1.8619 1.6306 0.0741  -0.0007 -0.1239 253 GLY D N   
10856 C CA  . GLY D 253 ? 0.9966 1.8999 1.6781 0.0729  -0.0036 -0.1190 253 GLY D CA  
10857 C C   . GLY D 253 ? 1.0036 1.9132 1.7052 0.0784  -0.0065 -0.1270 253 GLY D C   
10858 O O   . GLY D 253 ? 0.9633 1.8868 1.6740 0.0815  -0.0017 -0.1359 253 GLY D O   
10859 N N   . ASN D 254 ? 0.9281 1.8277 1.6369 0.0799  -0.0147 -0.1241 254 ASN D N   
10860 C CA  . ASN D 254 ? 0.8919 1.7965 1.6206 0.0852  -0.0189 -0.1309 254 ASN D CA  
10861 C C   . ASN D 254 ? 0.8948 1.7806 1.6224 0.0913  -0.0288 -0.1346 254 ASN D C   
10862 O O   . ASN D 254 ? 0.8878 1.7548 1.6054 0.0905  -0.0360 -0.1281 254 ASN D O   
10863 C CB  . ASN D 254 ? 0.8975 1.8052 1.6363 0.0825  -0.0216 -0.1252 254 ASN D CB  
10864 C CG  . ASN D 254 ? 0.8529 1.7774 1.5923 0.0759  -0.0120 -0.1204 254 ASN D CG  
10865 O OD1 . ASN D 254 ? 0.8346 1.7727 1.5712 0.0743  -0.0028 -0.1231 254 ASN D OD1 
10866 N ND2 . ASN D 254 ? 0.8458 1.7691 1.5884 0.0718  -0.0143 -0.1131 254 ASN D ND2 
10867 N N   . VAL D 255 ? 0.9687 1.8591 1.7063 0.0974  -0.0289 -0.1449 255 VAL D N   
10868 C CA  . VAL D 255 ? 0.9630 1.8361 1.7008 0.1036  -0.0379 -0.1491 255 VAL D CA  
10869 C C   . VAL D 255 ? 0.9813 1.8634 1.7412 0.1105  -0.0408 -0.1583 255 VAL D C   
10870 O O   . VAL D 255 ? 0.9464 1.8477 1.7175 0.1118  -0.0333 -0.1658 255 VAL D O   
10871 C CB  . VAL D 255 ? 0.9594 1.8251 1.6841 0.1046  -0.0357 -0.1529 255 VAL D CB  
10872 C CG1 . VAL D 255 ? 0.9738 1.8209 1.6996 0.1109  -0.0451 -0.1570 255 VAL D CG1 
10873 C CG2 . VAL D 255 ? 0.9657 1.8232 1.6695 0.0979  -0.0331 -0.1439 255 VAL D CG2 
10874 N N   . LEU D 256 ? 0.8478 1.7162 1.6137 0.1149  -0.0515 -0.1579 256 LEU D N   
10875 C CA  . LEU D 256 ? 0.8113 1.6861 1.5988 0.1221  -0.0561 -0.1661 256 LEU D CA  
10876 C C   . LEU D 256 ? 0.7786 1.6366 1.5639 0.1290  -0.0631 -0.1717 256 LEU D C   
10877 O O   . LEU D 256 ? 0.7338 1.5708 1.5117 0.1307  -0.0728 -0.1670 256 LEU D O   
10878 C CB  . LEU D 256 ? 0.8318 1.7047 1.6293 0.1221  -0.0637 -0.1613 256 LEU D CB  
10879 C CG  . LEU D 256 ? 0.8491 1.7278 1.6700 0.1298  -0.0700 -0.1691 256 LEU D CG  
10880 C CD1 . LEU D 256 ? 0.8223 1.7266 1.6614 0.1315  -0.0606 -0.1785 256 LEU D CD1 
10881 C CD2 . LEU D 256 ? 0.8235 1.6995 1.6525 0.1291  -0.0782 -0.1637 256 LEU D CD2 
10882 N N   . VAL D 257 ? 0.7805 1.6471 1.5718 0.1328  -0.0581 -0.1816 257 VAL D N   
10883 C CA  . VAL D 257 ? 0.7637 1.6154 1.5541 0.1394  -0.0638 -0.1879 257 VAL D CA  
10884 C C   . VAL D 257 ? 0.7952 1.6541 1.6091 0.1477  -0.0683 -0.1970 257 VAL D C   
10885 O O   . VAL D 257 ? 0.8184 1.6993 1.6491 0.1485  -0.0625 -0.2023 257 VAL D O   
10886 C CB  . VAL D 257 ? 0.7349 1.5894 1.5151 0.1382  -0.0559 -0.1932 257 VAL D CB  
10887 C CG1 . VAL D 257 ? 0.7608 1.6237 1.5562 0.1457  -0.0543 -0.2066 257 VAL D CG1 
10888 C CG2 . VAL D 257 ? 0.6509 1.4818 1.4107 0.1361  -0.0603 -0.1878 257 VAL D CG2 
10889 N N   . ASP D 258 ? 0.8199 1.6600 1.6352 0.1540  -0.0787 -0.1987 258 ASP D N   
10890 C CA  . ASP D 258 ? 0.7953 1.6392 1.6324 0.1629  -0.0845 -0.2073 258 ASP D CA  
10891 C C   . ASP D 258 ? 0.7643 1.6134 1.6077 0.1681  -0.0799 -0.2193 258 ASP D C   
10892 O O   . ASP D 258 ? 0.8300 1.6712 1.6584 0.1661  -0.0762 -0.2202 258 ASP D O   
10893 C CB  . ASP D 258 ? 0.7453 1.5655 1.5806 0.1675  -0.0986 -0.2030 258 ASP D CB  
10894 C CG  . ASP D 258 ? 0.7549 1.5802 1.6141 0.1764  -0.1059 -0.2102 258 ASP D CG  
10895 O OD1 . ASP D 258 ? 0.7480 1.5789 1.6195 0.1828  -0.1042 -0.2209 258 ASP D OD1 
10896 O OD2 . ASP D 258 ? 0.7878 1.6114 1.6539 0.1770  -0.1135 -0.2055 258 ASP D OD2 
10897 N N   . GLU D 259 ? 0.7442 1.6073 1.6108 0.1751  -0.0801 -0.2290 259 GLU D N   
10898 C CA  . GLU D 259 ? 0.7373 1.6052 1.6118 0.1811  -0.0763 -0.2414 259 GLU D CA  
10899 C C   . GLU D 259 ? 0.7448 1.5868 1.6119 0.1863  -0.0855 -0.2428 259 GLU D C   
10900 O O   . GLU D 259 ? 0.7536 1.5933 1.6179 0.1888  -0.0820 -0.2507 259 GLU D O   
10901 C CB  . GLU D 259 ? 0.7445 1.6325 1.6468 0.1879  -0.0752 -0.2513 259 GLU D CB  
10902 C CG  . GLU D 259 ? 0.8064 1.6865 1.7234 0.1938  -0.0879 -0.2493 259 GLU D CG  
10903 C CD  . GLU D 259 ? 0.8279 1.7301 1.7739 0.2000  -0.0865 -0.2588 259 GLU D CD  
10904 O OE1 . GLU D 259 ? 0.9116 1.8327 1.8636 0.1992  -0.0748 -0.2662 259 GLU D OE1 
10905 O OE2 . GLU D 259 ? 0.7816 1.6798 1.7420 0.2052  -0.0969 -0.2580 259 GLU D OE2 
10906 N N   . THR D 260 ? 0.6571 1.4791 1.5205 0.1880  -0.0974 -0.2353 260 THR D N   
10907 C CA  . THR D 260 ? 0.6322 1.4283 1.4882 0.1928  -0.1065 -0.2355 260 THR D CA  
10908 C C   . THR D 260 ? 0.6147 1.3935 1.4447 0.1859  -0.1047 -0.2282 260 THR D C   
10909 O O   . THR D 260 ? 0.6044 1.3671 1.4275 0.1885  -0.1072 -0.2314 260 THR D O   
10910 C CB  . THR D 260 ? 0.6486 1.4300 1.5105 0.1975  -0.1200 -0.2303 260 THR D CB  
10911 O OG1 . THR D 260 ? 0.6643 1.4650 1.5502 0.2021  -0.1210 -0.2353 260 THR D OG1 
10912 C CG2 . THR D 260 ? 0.6780 1.4364 1.5393 0.2050  -0.1293 -0.2336 260 THR D CG2 
10913 N N   . ALA D 261 ? 0.6391 1.4209 1.4552 0.1773  -0.1006 -0.2185 261 ALA D N   
10914 C CA  . ALA D 261 ? 0.5287 1.2950 1.3209 0.1706  -0.0989 -0.2111 261 ALA D CA  
10915 C C   . ALA D 261 ? 0.4808 1.2547 1.2677 0.1687  -0.0894 -0.2184 261 ALA D C   
10916 O O   . ALA D 261 ? 0.4755 1.2720 1.2712 0.1683  -0.0805 -0.2251 261 ALA D O   
10917 C CB  . ALA D 261 ? 0.5644 1.3340 1.3447 0.1623  -0.0964 -0.1997 261 ALA D CB  
10918 N N   . THR D 262 ? 0.4876 1.2424 1.2595 0.1673  -0.0913 -0.2169 262 THR D N   
10919 C CA  . THR D 262 ? 0.4889 1.2480 1.2540 0.1651  -0.0836 -0.2235 262 THR D CA  
10920 C C   . THR D 262 ? 0.5287 1.2801 1.2718 0.1563  -0.0803 -0.2143 262 THR D C   
10921 O O   . THR D 262 ? 0.5758 1.3072 1.3072 0.1541  -0.0866 -0.2051 262 THR D O   
10922 C CB  . THR D 262 ? 0.5281 1.2722 1.2972 0.1717  -0.0885 -0.2320 262 THR D CB  
10923 O OG1 . THR D 262 ? 0.5048 1.2487 1.2633 0.1682  -0.0822 -0.2365 262 THR D OG1 
10924 C CG2 . THR D 262 ? 0.5638 1.2802 1.3260 0.1735  -0.0997 -0.2244 262 THR D CG2 
10925 N N   . ILE D 263 ? 0.5079 1.2753 1.2453 0.1514  -0.0704 -0.2167 263 ILE D N   
10926 C CA  . ILE D 263 ? 0.4877 1.2512 1.2057 0.1430  -0.0664 -0.2087 263 ILE D CA  
10927 C C   . ILE D 263 ? 0.5355 1.2961 1.2464 0.1422  -0.0627 -0.2158 263 ILE D C   
10928 O O   . ILE D 263 ? 0.5784 1.3530 1.2979 0.1454  -0.0576 -0.2269 263 ILE D O   
10929 C CB  . ILE D 263 ? 0.4588 1.2432 1.1748 0.1373  -0.0583 -0.2040 263 ILE D CB  
10930 C CG1 . ILE D 263 ? 0.4533 1.2393 1.1762 0.1375  -0.0625 -0.1967 263 ILE D CG1 
10931 C CG2 . ILE D 263 ? 0.5164 1.2974 1.2129 0.1292  -0.0541 -0.1966 263 ILE D CG2 
10932 C CD1 . ILE D 263 ? 0.5315 1.3360 1.2524 0.1315  -0.0550 -0.1913 263 ILE D CD1 
10933 N N   . GLY D 264 ? 0.5991 1.3420 1.2946 0.1380  -0.0651 -0.2099 264 GLY D N   
10934 C CA  . GLY D 264 ? 0.8128 1.5528 1.5002 0.1359  -0.0617 -0.2155 264 GLY D CA  
10935 C C   . GLY D 264 ? 0.8369 1.5965 1.5168 0.1300  -0.0521 -0.2157 264 GLY D C   
10936 O O   . GLY D 264 ? 0.7533 1.5290 1.4346 0.1277  -0.0476 -0.2117 264 GLY D O   
10937 N N   . GLU D 265 ? 0.9496 1.7071 1.6211 0.1276  -0.0493 -0.2203 265 GLU D N   
10938 C CA  . GLU D 265 ? 0.9359 1.7106 1.5989 0.1222  -0.0409 -0.2211 265 GLU D CA  
10939 C C   . GLU D 265 ? 0.8598 1.6269 1.5064 0.1146  -0.0408 -0.2095 265 GLU D C   
10940 O O   . GLU D 265 ? 0.8545 1.6014 1.4952 0.1133  -0.0466 -0.2034 265 GLU D O   
10941 C CB  . GLU D 265 ? 0.9698 1.7486 1.6331 0.1239  -0.0379 -0.2337 265 GLU D CB  
10942 C CG  . GLU D 265 ? 1.0042 1.7922 1.6837 0.1317  -0.0370 -0.2463 265 GLU D CG  
10943 C CD  . GLU D 265 ? 0.9893 1.8028 1.6753 0.1320  -0.0293 -0.2485 265 GLU D CD  
10944 O OE1 . GLU D 265 ? 0.9310 1.7559 1.6074 0.1260  -0.0239 -0.2415 265 GLU D OE1 
10945 O OE2 . GLU D 265 ? 1.0424 1.8646 1.7437 0.1384  -0.0286 -0.2572 265 GLU D OE2 
10946 N N   . GLY D 266 ? 0.8052 1.5888 1.4447 0.1096  -0.0338 -0.2065 266 GLY D N   
10947 C CA  . GLY D 266 ? 0.7816 1.5604 1.4064 0.1026  -0.0330 -0.1961 266 GLY D CA  
10948 C C   . GLY D 266 ? 0.7550 1.5248 1.3773 0.1006  -0.0367 -0.1837 266 GLY D C   
10949 O O   . GLY D 266 ? 0.7561 1.5134 1.3674 0.0962  -0.0387 -0.1755 266 GLY D O   
10950 N N   . CYS D 267 ? 0.7193 1.4954 1.3518 0.1037  -0.0374 -0.1825 267 CYS D N   
10951 C CA  . CYS D 267 ? 0.6450 1.4139 1.2759 0.1020  -0.0410 -0.1715 267 CYS D CA  
10952 C C   . CYS D 267 ? 0.6593 1.4459 1.2880 0.0978  -0.0348 -0.1657 267 CYS D C   
10953 O O   . CYS D 267 ? 0.7210 1.5256 1.3501 0.0965  -0.0278 -0.1701 267 CYS D O   
10954 C CB  . CYS D 267 ? 0.6126 1.3752 1.2568 0.1083  -0.0473 -0.1737 267 CYS D CB  
10955 S SG  . CYS D 267 ? 0.5710 1.3135 1.2197 0.1144  -0.0546 -0.1814 267 CYS D SG  
10956 N N   . LEU D 268 ? 0.6079 1.3888 1.2339 0.0954  -0.0374 -0.1556 268 LEU D N   
10957 C CA  . LEU D 268 ? 0.6424 1.4381 1.2674 0.0915  -0.0322 -0.1493 268 LEU D CA  
10958 C C   . LEU D 268 ? 0.6526 1.4426 1.2837 0.0926  -0.0373 -0.1432 268 LEU D C   
10959 O O   . LEU D 268 ? 0.6463 1.4193 1.2697 0.0911  -0.0425 -0.1357 268 LEU D O   
10960 C CB  . LEU D 268 ? 0.6521 1.4471 1.2617 0.0849  -0.0288 -0.1416 268 LEU D CB  
10961 C CG  . LEU D 268 ? 0.6249 1.4374 1.2323 0.0806  -0.0220 -0.1365 268 LEU D CG  
10962 C CD1 . LEU D 268 ? 0.6594 1.4927 1.2752 0.0825  -0.0156 -0.1452 268 LEU D CD1 
10963 C CD2 . LEU D 268 ? 0.6263 1.4372 1.2185 0.0748  -0.0192 -0.1299 268 LEU D CD2 
10964 N N   . ILE D 269 ? 0.6315 1.4358 1.2763 0.0951  -0.0357 -0.1464 269 ILE D N   
10965 C CA  . ILE D 269 ? 0.6417 1.4420 1.2954 0.0972  -0.0412 -0.1427 269 ILE D CA  
10966 C C   . ILE D 269 ? 0.6457 1.4621 1.3022 0.0930  -0.0359 -0.1374 269 ILE D C   
10967 O O   . ILE D 269 ? 0.6784 1.5140 1.3401 0.0922  -0.0284 -0.1416 269 ILE D O   
10968 C CB  . ILE D 269 ? 0.6396 1.4417 1.3102 0.1046  -0.0452 -0.1520 269 ILE D CB  
10969 C CG1 . ILE D 269 ? 0.6132 1.3976 1.2811 0.1087  -0.0508 -0.1568 269 ILE D CG1 
10970 C CG2 . ILE D 269 ? 0.7091 1.5087 1.3896 0.1065  -0.0512 -0.1481 269 ILE D CG2 
10971 C CD1 . ILE D 269 ? 0.5748 1.3671 1.2445 0.1107  -0.0460 -0.1672 269 ILE D CD1 
10972 N N   . GLY D 270 ? 0.7191 1.5270 1.3716 0.0903  -0.0397 -0.1282 270 GLY D N   
10973 C CA  . GLY D 270 ? 0.7852 1.6058 1.4405 0.0862  -0.0356 -0.1224 270 GLY D CA  
10974 C C   . GLY D 270 ? 0.8782 1.6911 1.5178 0.0801  -0.0345 -0.1119 270 GLY D C   
10975 O O   . GLY D 270 ? 0.8658 1.6670 1.4921 0.0786  -0.0352 -0.1097 270 GLY D O   
10976 N N   . PRO D 271 ? 1.1109 1.9303 1.7525 0.0764  -0.0329 -0.1053 271 PRO D N   
10977 C CA  . PRO D 271 ? 1.1015 1.9344 1.7596 0.0776  -0.0323 -0.1076 271 PRO D CA  
10978 C C   . PRO D 271 ? 1.1265 1.9475 1.7919 0.0808  -0.0417 -0.1064 271 PRO D C   
10979 O O   . PRO D 271 ? 1.1441 1.9460 1.7990 0.0808  -0.0480 -0.1017 271 PRO D O   
10980 C CB  . PRO D 271 ? 1.0927 1.9361 1.7471 0.0712  -0.0260 -0.1000 271 PRO D CB  
10981 C CG  . PRO D 271 ? 1.2030 2.0393 1.8390 0.0673  -0.0232 -0.0946 271 PRO D CG  
10982 C CD  . PRO D 271 ? 1.1622 1.9790 1.7905 0.0703  -0.0299 -0.0958 271 PRO D CD  
10983 N N   . ASP D 272 ? 0.9639 1.7965 1.6470 0.0835  -0.0426 -0.1108 272 ASP D N   
10984 C CA  . ASP D 272 ? 0.8862 1.7106 1.5784 0.0865  -0.0517 -0.1100 272 ASP D CA  
10985 C C   . ASP D 272 ? 0.8105 1.6151 1.4984 0.0919  -0.0606 -0.1125 272 ASP D C   
10986 O O   . ASP D 272 ? 0.7540 1.5400 1.4310 0.0913  -0.0671 -0.1064 272 ASP D O   
10987 C CB  . ASP D 272 ? 0.9401 1.7587 1.6259 0.0813  -0.0536 -0.1002 272 ASP D CB  
10988 C CG  . ASP D 272 ? 1.0606 1.8977 1.7506 0.0758  -0.0450 -0.0972 272 ASP D CG  
10989 O OD1 . ASP D 272 ? 1.0961 1.9318 1.7725 0.0706  -0.0400 -0.0908 272 ASP D OD1 
10990 O OD2 . ASP D 272 ? 1.0827 1.9356 1.7900 0.0766  -0.0430 -0.1013 272 ASP D OD2 
10991 N N   . VAL D 273 ? 0.8088 1.6178 1.5056 0.0973  -0.0604 -0.1216 273 VAL D N   
10992 C CA  . VAL D 273 ? 0.7685 1.5604 1.4640 0.1031  -0.0684 -0.1252 273 VAL D CA  
10993 C C   . VAL D 273 ? 0.7656 1.5661 1.4818 0.1098  -0.0719 -0.1341 273 VAL D C   
10994 O O   . VAL D 273 ? 0.8092 1.6294 1.5377 0.1108  -0.0651 -0.1408 273 VAL D O   
10995 C CB  . VAL D 273 ? 0.7438 1.5290 1.4274 0.1030  -0.0650 -0.1280 273 VAL D CB  
10996 C CG1 . VAL D 273 ? 0.7315 1.4971 1.4133 0.1086  -0.0736 -0.1308 273 VAL D CG1 
10997 C CG2 . VAL D 273 ? 0.7590 1.5385 1.4239 0.0963  -0.0609 -0.1196 273 VAL D CG2 
10998 N N   . ALA D 274 ? 0.7022 1.4881 1.4220 0.1148  -0.0823 -0.1341 274 ALA D N   
10999 C CA  . ALA D 274 ? 0.6871 1.4795 1.4272 0.1219  -0.0873 -0.1420 274 ALA D CA  
11000 C C   . ALA D 274 ? 0.6738 1.4468 1.4109 0.1282  -0.0955 -0.1453 274 ALA D C   
11001 O O   . ALA D 274 ? 0.6878 1.4404 1.4143 0.1286  -0.1037 -0.1392 274 ALA D O   
11002 C CB  . ALA D 274 ? 0.6762 1.4720 1.4272 0.1219  -0.0932 -0.1387 274 ALA D CB  
11003 N N   . ILE D 275 ? 0.6805 1.4594 1.4266 0.1331  -0.0930 -0.1548 275 ILE D N   
11004 C CA  . ILE D 275 ? 0.6924 1.4537 1.4368 0.1392  -0.0999 -0.1588 275 ILE D CA  
11005 C C   . ILE D 275 ? 0.7544 1.5202 1.5201 0.1474  -0.1067 -0.1660 275 ILE D C   
11006 O O   . ILE D 275 ? 0.7490 1.5352 1.5320 0.1499  -0.1015 -0.1741 275 ILE D O   
11007 C CB  . ILE D 275 ? 0.6807 1.4438 1.4197 0.1390  -0.0928 -0.1650 275 ILE D CB  
11008 C CG1 . ILE D 275 ? 0.6726 1.4325 1.3914 0.1309  -0.0864 -0.1578 275 ILE D CG1 
11009 C CG2 . ILE D 275 ? 0.6806 1.4247 1.4186 0.1452  -0.1001 -0.1691 275 ILE D CG2 
11010 C CD1 . ILE D 275 ? 0.7225 1.4847 1.4354 0.1302  -0.0797 -0.1636 275 ILE D CD1 
11011 N N   . GLY D 276 ? 0.9977 1.7444 1.7620 0.1517  -0.1183 -0.1629 276 GLY D N   
11012 C CA  . GLY D 276 ? 0.9967 1.7454 1.7805 0.1599  -0.1263 -0.1690 276 GLY D CA  
11013 C C   . GLY D 276 ? 1.0030 1.7528 1.7968 0.1667  -0.1254 -0.1797 276 GLY D C   
11014 O O   . GLY D 276 ? 1.0094 1.7593 1.7949 0.1647  -0.1182 -0.1828 276 GLY D O   
11015 N N   . PRO D 277 ? 0.7078 1.4589 1.5201 0.1749  -0.1330 -0.1858 277 PRO D N   
11016 C CA  . PRO D 277 ? 0.6526 1.4035 1.4757 0.1824  -0.1331 -0.1964 277 PRO D CA  
11017 C C   . PRO D 277 ? 0.6108 1.3334 1.4203 0.1854  -0.1409 -0.1942 277 PRO D C   
11018 O O   . PRO D 277 ? 0.6488 1.3516 1.4437 0.1836  -0.1483 -0.1848 277 PRO D O   
11019 C CB  . PRO D 277 ? 0.7081 1.4708 1.5569 0.1900  -0.1391 -0.2027 277 PRO D CB  
11020 C CG  . PRO D 277 ? 0.7241 1.4788 1.5694 0.1883  -0.1481 -0.1934 277 PRO D CG  
11021 C CD  . PRO D 277 ? 0.7303 1.4853 1.5563 0.1780  -0.1414 -0.1840 277 PRO D CD  
11022 N N   . GLY D 278 ? 0.5703 1.2912 1.3846 0.1900  -0.1387 -0.2031 278 GLY D N   
11023 C CA  . GLY D 278 ? 0.6171 1.3119 1.4208 0.1932  -0.1455 -0.2021 278 GLY D CA  
11024 C C   . GLY D 278 ? 0.6071 1.2860 1.3856 0.1855  -0.1423 -0.1941 278 GLY D C   
11025 O O   . GLY D 278 ? 0.6338 1.2891 1.4018 0.1872  -0.1484 -0.1915 278 GLY D O   
11026 N N   . CYS D 279 ? 0.5759 1.2668 1.3447 0.1772  -0.1330 -0.1901 279 CYS D N   
11027 C CA  . CYS D 279 ? 0.5265 1.2042 1.2724 0.1697  -0.1297 -0.1825 279 CYS D CA  
11028 C C   . CYS D 279 ? 0.5679 1.2452 1.3102 0.1691  -0.1231 -0.1896 279 CYS D C   
11029 O O   . CYS D 279 ? 0.5945 1.2865 1.3508 0.1731  -0.1187 -0.2004 279 CYS D O   
11030 C CB  . CYS D 279 ? 0.5123 1.2031 1.2499 0.1613  -0.1226 -0.1755 279 CYS D CB  
11031 S SG  . CYS D 279 ? 0.4888 1.1835 1.2324 0.1614  -0.1291 -0.1684 279 CYS D SG  
11032 N N   . ILE D 280 ? 0.5546 1.2149 1.2778 0.1640  -0.1225 -0.1837 280 ILE D N   
11033 C CA  . ILE D 280 ? 0.5634 1.2207 1.2809 0.1625  -0.1171 -0.1893 280 ILE D CA  
11034 C C   . ILE D 280 ? 0.6537 1.3117 1.3529 0.1530  -0.1103 -0.1818 280 ILE D C   
11035 O O   . ILE D 280 ? 0.6954 1.3345 1.3792 0.1493  -0.1137 -0.1727 280 ILE D O   
11036 C CB  . ILE D 280 ? 0.6306 1.2626 1.3450 0.1668  -0.1248 -0.1904 280 ILE D CB  
11037 C CG1 . ILE D 280 ? 0.6937 1.3229 1.4257 0.1766  -0.1334 -0.1959 280 ILE D CG1 
11038 C CG2 . ILE D 280 ? 0.7571 1.3880 1.4684 0.1655  -0.1192 -0.1979 280 ILE D CG2 
11039 C CD1 . ILE D 280 ? 0.7104 1.3137 1.4399 0.1815  -0.1418 -0.1964 280 ILE D CD1 
11040 N N   . VAL D 281 ? 0.6949 1.3745 1.3956 0.1491  -0.1006 -0.1854 281 VAL D N   
11041 C CA  . VAL D 281 ? 0.6578 1.3406 1.3426 0.1405  -0.0938 -0.1790 281 VAL D CA  
11042 C C   . VAL D 281 ? 0.7077 1.3879 1.3865 0.1387  -0.0893 -0.1849 281 VAL D C   
11043 O O   . VAL D 281 ? 0.7523 1.4456 1.4408 0.1417  -0.0850 -0.1956 281 VAL D O   
11044 C CB  . VAL D 281 ? 0.6059 1.3135 1.2947 0.1370  -0.0862 -0.1782 281 VAL D CB  
11045 C CG1 . VAL D 281 ? 0.6164 1.3284 1.2898 0.1288  -0.0787 -0.1732 281 VAL D CG1 
11046 C CG2 . VAL D 281 ? 0.6208 1.3293 1.3138 0.1374  -0.0909 -0.1711 281 VAL D CG2 
11047 N N   . GLU D 282 ? 0.7231 1.3866 1.3861 0.1338  -0.0902 -0.1784 282 GLU D N   
11048 C CA  . GLU D 282 ? 0.7569 1.4166 1.4137 0.1314  -0.0865 -0.1834 282 GLU D CA  
11049 C C   . GLU D 282 ? 0.6884 1.3651 1.3371 0.1245  -0.0774 -0.1820 282 GLU D C   
11050 O O   . GLU D 282 ? 0.6150 1.3064 1.2638 0.1220  -0.0737 -0.1777 282 GLU D O   
11051 C CB  . GLU D 282 ? 0.7547 1.3876 1.4002 0.1299  -0.0922 -0.1776 282 GLU D CB  
11052 C CG  . GLU D 282 ? 0.8265 1.4422 1.4797 0.1372  -0.1015 -0.1791 282 GLU D CG  
11053 C CD  . GLU D 282 ? 0.8755 1.4648 1.5190 0.1362  -0.1063 -0.1756 282 GLU D CD  
11054 O OE1 . GLU D 282 ? 0.8483 1.4322 1.4788 0.1294  -0.1027 -0.1711 282 GLU D OE1 
11055 O OE2 . GLU D 282 ? 0.9289 1.5027 1.5780 0.1422  -0.1139 -0.1771 282 GLU D OE2 
11056 N N   . SER D 283 ? 0.7284 1.4027 1.3700 0.1213  -0.0740 -0.1856 283 SER D N   
11057 C CA  . SER D 283 ? 0.7757 1.4673 1.4111 0.1158  -0.0657 -0.1865 283 SER D CA  
11058 C C   . SER D 283 ? 0.6713 1.3572 1.2913 0.1083  -0.0642 -0.1750 283 SER D C   
11059 O O   . SER D 283 ? 0.6289 1.2951 1.2413 0.1067  -0.0689 -0.1681 283 SER D O   
11060 C CB  . SER D 283 ? 0.8795 1.5731 1.5154 0.1161  -0.0629 -0.1971 283 SER D CB  
11061 O OG  . SER D 283 ? 0.9860 1.6928 1.6356 0.1222  -0.0612 -0.2085 283 SER D OG  
11062 N N   . GLY D 284 ? 0.6439 1.3476 1.2595 0.1038  -0.0574 -0.1730 284 GLY D N   
11063 C CA  . GLY D 284 ? 0.5699 1.2710 1.1719 0.0969  -0.0551 -0.1631 284 GLY D CA  
11064 C C   . GLY D 284 ? 0.5985 1.2956 1.1972 0.0954  -0.0573 -0.1522 284 GLY D C   
11065 O O   . GLY D 284 ? 0.6330 1.3238 1.2203 0.0901  -0.0566 -0.1434 284 GLY D O   
11066 N N   . VAL D 285 ? 0.5910 1.2920 1.1999 0.0998  -0.0600 -0.1527 285 VAL D N   
11067 C CA  . VAL D 285 ? 0.6217 1.3172 1.2281 0.0988  -0.0633 -0.1430 285 VAL D CA  
11068 C C   . VAL D 285 ? 0.6213 1.3355 1.2266 0.0949  -0.0571 -0.1388 285 VAL D C   
11069 O O   . VAL D 285 ? 0.6030 1.3359 1.2124 0.0943  -0.0510 -0.1442 285 VAL D O   
11070 C CB  . VAL D 285 ? 0.6113 1.3011 1.2294 0.1054  -0.0700 -0.1454 285 VAL D CB  
11071 C CG1 . VAL D 285 ? 0.5771 1.2476 1.1961 0.1095  -0.0762 -0.1495 285 VAL D CG1 
11072 C CG2 . VAL D 285 ? 0.6271 1.3380 1.2604 0.1092  -0.0668 -0.1535 285 VAL D CG2 
11073 N N   . ARG D 286 ? 0.6574 1.3661 1.2566 0.0921  -0.0589 -0.1289 286 ARG D N   
11074 C CA  . ARG D 286 ? 0.6500 1.3735 1.2473 0.0879  -0.0537 -0.1234 286 ARG D CA  
11075 C C   . ARG D 286 ? 0.6881 1.4072 1.2889 0.0890  -0.0585 -0.1175 286 ARG D C   
11076 O O   . ARG D 286 ? 0.6742 1.3781 1.2657 0.0871  -0.0622 -0.1095 286 ARG D O   
11077 C CB  . ARG D 286 ? 0.6349 1.3557 1.2177 0.0816  -0.0500 -0.1167 286 ARG D CB  
11078 C CG  . ARG D 286 ? 0.6718 1.4041 1.2509 0.0772  -0.0456 -0.1093 286 ARG D CG  
11079 C CD  . ARG D 286 ? 0.6640 1.4186 1.2528 0.0778  -0.0402 -0.1140 286 ARG D CD  
11080 N NE  . ARG D 286 ? 0.7467 1.5114 1.3308 0.0730  -0.0355 -0.1066 286 ARG D NE  
11081 C CZ  . ARG D 286 ? 0.7284 1.5097 1.3206 0.0728  -0.0318 -0.1068 286 ARG D CZ  
11082 N NH1 . ARG D 286 ? 0.6866 1.4770 1.2923 0.0771  -0.0320 -0.1145 286 ARG D NH1 
11083 N NH2 . ARG D 286 ? 0.7894 1.5780 1.3765 0.0681  -0.0278 -0.0995 286 ARG D NH2 
11084 N N   . LEU D 287 ? 0.8086 1.5411 1.4231 0.0922  -0.0583 -0.1216 287 LEU D N   
11085 C CA  . LEU D 287 ? 0.8018 1.5322 1.4219 0.0936  -0.0630 -0.1172 287 LEU D CA  
11086 C C   . LEU D 287 ? 0.8182 1.5647 1.4392 0.0891  -0.0574 -0.1124 287 LEU D C   
11087 O O   . LEU D 287 ? 0.8645 1.6291 1.4893 0.0875  -0.0502 -0.1160 287 LEU D O   
11088 C CB  . LEU D 287 ? 0.8006 1.5346 1.4374 0.1004  -0.0675 -0.1249 287 LEU D CB  
11089 C CG  . LEU D 287 ? 0.8246 1.5425 1.4622 0.1056  -0.0735 -0.1302 287 LEU D CG  
11090 C CD1 . LEU D 287 ? 0.8475 1.5699 1.5028 0.1127  -0.0781 -0.1375 287 LEU D CD1 
11091 C CD2 . LEU D 287 ? 0.8445 1.5385 1.4690 0.1044  -0.0800 -0.1223 287 LEU D CD2 
11092 N N   . SER D 288 ? 0.7258 1.4651 1.3427 0.0869  -0.0608 -0.1043 288 SER D N   
11093 C CA  . SER D 288 ? 0.7256 1.4776 1.3426 0.0823  -0.0561 -0.0988 288 SER D CA  
11094 C C   . SER D 288 ? 0.7418 1.4855 1.3602 0.0824  -0.0624 -0.0930 288 SER D C   
11095 O O   . SER D 288 ? 0.7832 1.5080 1.3916 0.0824  -0.0680 -0.0882 288 SER D O   
11096 C CB  . SER D 288 ? 0.7821 1.5334 1.3842 0.0765  -0.0505 -0.0929 288 SER D CB  
11097 O OG  . SER D 288 ? 0.7160 1.4471 1.3051 0.0757  -0.0546 -0.0882 288 SER D OG  
11098 N N   . ARG D 289 ? 0.7348 1.4926 1.3656 0.0823  -0.0613 -0.0937 289 ARG D N   
11099 C CA  . ARG D 289 ? 0.8321 1.5850 1.4655 0.0816  -0.0667 -0.0884 289 ARG D CA  
11100 C C   . ARG D 289 ? 0.8179 1.5541 1.4530 0.0869  -0.0771 -0.0896 289 ARG D C   
11101 O O   . ARG D 289 ? 0.8362 1.5629 1.4687 0.0863  -0.0830 -0.0845 289 ARG D O   
11102 C CB  . ARG D 289 ? 0.9249 1.6707 1.5435 0.0757  -0.0648 -0.0788 289 ARG D CB  
11103 C CG  . ARG D 289 ? 1.0129 1.7612 1.6360 0.0734  -0.0671 -0.0738 289 ARG D CG  
11104 C CD  . ARG D 289 ? 1.0553 1.7939 1.6630 0.0682  -0.0658 -0.0648 289 ARG D CD  
11105 N NE  . ARG D 289 ? 1.1455 1.8795 1.7553 0.0670  -0.0709 -0.0604 289 ARG D NE  
11106 C CZ  . ARG D 289 ? 1.1802 1.9270 1.7980 0.0636  -0.0678 -0.0583 289 ARG D CZ  
11107 N NH1 . ARG D 289 ? 1.2211 1.9861 1.8449 0.0612  -0.0593 -0.0597 289 ARG D NH1 
11108 N NH2 . ARG D 289 ? 1.1864 1.9274 1.8059 0.0626  -0.0731 -0.0547 289 ARG D NH2 
11109 N N   . CYS D 290 ? 0.7413 1.4731 1.3805 0.0920  -0.0798 -0.0963 290 CYS D N   
11110 C CA  . CYS D 290 ? 0.6967 1.4118 1.3370 0.0973  -0.0898 -0.0973 290 CYS D CA  
11111 C C   . CYS D 290 ? 0.7308 1.4566 1.3913 0.1032  -0.0932 -0.1053 290 CYS D C   
11112 O O   . CYS D 290 ? 0.7532 1.4994 1.4266 0.1032  -0.0871 -0.1105 290 CYS D O   
11113 C CB  . CYS D 290 ? 0.6546 1.3529 1.2833 0.0988  -0.0914 -0.0981 290 CYS D CB  
11114 S SG  . CYS D 290 ? 0.6430 1.3537 1.2774 0.1003  -0.0840 -0.1074 290 CYS D SG  
11115 N N   . THR D 291 ? 0.7141 1.4260 1.3774 0.1085  -0.1031 -0.1061 291 THR D N   
11116 C CA  . THR D 291 ? 0.6145 1.3340 1.2971 0.1151  -0.1078 -0.1139 291 THR D CA  
11117 C C   . THR D 291 ? 0.6120 1.3130 1.2916 0.1211  -0.1154 -0.1167 291 THR D C   
11118 O O   . THR D 291 ? 0.7276 1.4077 1.3935 0.1210  -0.1219 -0.1106 291 THR D O   
11119 C CB  . THR D 291 ? 0.6849 1.4084 1.3780 0.1160  -0.1141 -0.1119 291 THR D CB  
11120 O OG1 . THR D 291 ? 0.7807 1.4824 1.4654 0.1188  -0.1250 -0.1077 291 THR D OG1 
11121 C CG2 . THR D 291 ? 0.7500 1.4833 1.4395 0.1088  -0.1085 -0.1058 291 THR D CG2 
11122 N N   . VAL D 292 ? 0.6140 1.3222 1.3062 0.1262  -0.1143 -0.1258 292 VAL D N   
11123 C CA  . VAL D 292 ? 0.6157 1.3075 1.3071 0.1323  -0.1208 -0.1294 292 VAL D CA  
11124 C C   . VAL D 292 ? 0.6629 1.3586 1.3737 0.1399  -0.1287 -0.1353 292 VAL D C   
11125 O O   . VAL D 292 ? 0.7101 1.4267 1.4391 0.1419  -0.1249 -0.1422 292 VAL D O   
11126 C CB  . VAL D 292 ? 0.6061 1.3015 1.2963 0.1324  -0.1137 -0.1358 292 VAL D CB  
11127 C CG1 . VAL D 292 ? 0.5871 1.2690 1.2819 0.1396  -0.1204 -0.1416 292 VAL D CG1 
11128 C CG2 . VAL D 292 ? 0.6380 1.3250 1.3077 0.1255  -0.1082 -0.1294 292 VAL D CG2 
11129 N N   . MET D 293 ? 0.6193 1.2950 1.3262 0.1443  -0.1397 -0.1326 293 MET D N   
11130 C CA  . MET D 293 ? 0.6740 1.3510 1.3984 0.1520  -0.1488 -0.1374 293 MET D CA  
11131 C C   . MET D 293 ? 0.7101 1.3807 1.4416 0.1591  -0.1512 -0.1453 293 MET D C   
11132 O O   . MET D 293 ? 0.7279 1.3966 1.4528 0.1576  -0.1448 -0.1480 293 MET D O   
11133 C CB  . MET D 293 ? 0.7414 1.4010 1.4576 0.1529  -0.1600 -0.1297 293 MET D CB  
11134 C CG  . MET D 293 ? 0.7210 1.3894 1.4347 0.1469  -0.1583 -0.1237 293 MET D CG  
11135 S SD  . MET D 293 ? 0.8406 1.4922 1.5486 0.1489  -0.1723 -0.1167 293 MET D SD  
11136 C CE  . MET D 293 ? 0.8237 1.4885 1.5285 0.1403  -0.1666 -0.1108 293 MET D CE  
11137 N N   . ARG D 294 ? 0.7065 1.3735 1.4517 0.1670  -0.1609 -0.1491 294 ARG D N   
11138 C CA  . ARG D 294 ? 0.6196 1.2855 1.3774 0.1746  -0.1629 -0.1584 294 ARG D CA  
11139 C C   . ARG D 294 ? 0.6568 1.2976 1.3985 0.1756  -0.1659 -0.1561 294 ARG D C   
11140 O O   . ARG D 294 ? 0.7435 1.3636 1.4672 0.1733  -0.1712 -0.1471 294 ARG D O   
11141 C CB  . ARG D 294 ? 0.6523 1.3200 1.4292 0.1831  -0.1736 -0.1623 294 ARG D CB  
11142 C CG  . ARG D 294 ? 0.6927 1.3854 1.4881 0.1824  -0.1713 -0.1650 294 ARG D CG  
11143 C CD  . ARG D 294 ? 0.6473 1.3413 1.4624 0.1910  -0.1827 -0.1691 294 ARG D CD  
11144 N NE  . ARG D 294 ? 0.6013 1.2912 1.4277 0.1996  -0.1856 -0.1778 294 ARG D NE  
11145 C CZ  . ARG D 294 ? 0.5800 1.2716 1.4258 0.2085  -0.1948 -0.1833 294 ARG D CZ  
11146 N NH1 . ARG D 294 ? 0.6064 1.3043 1.4627 0.2099  -0.2023 -0.1811 294 ARG D NH1 
11147 N NH2 . ARG D 294 ? 0.5981 1.2852 1.4535 0.2161  -0.1968 -0.1912 294 ARG D NH2 
11148 N N   . GLY D 295 ? 0.6336 1.2767 1.3822 0.1791  -0.1621 -0.1647 295 GLY D N   
11149 C CA  . GLY D 295 ? 0.6664 1.2866 1.4061 0.1822  -0.1664 -0.1651 295 GLY D CA  
11150 C C   . GLY D 295 ? 0.6437 1.2479 1.3597 0.1749  -0.1624 -0.1578 295 GLY D C   
11151 O O   . GLY D 295 ? 0.6582 1.2452 1.3677 0.1767  -0.1643 -0.1589 295 GLY D O   
11152 N N   . VAL D 296 ? 0.6418 1.2511 1.3453 0.1669  -0.1568 -0.1505 296 VAL D N   
11153 C CA  . VAL D 296 ? 0.6910 1.2854 1.3725 0.1601  -0.1531 -0.1433 296 VAL D CA  
11154 C C   . VAL D 296 ? 0.6256 1.2296 1.3068 0.1569  -0.1428 -0.1495 296 VAL D C   
11155 O O   . VAL D 296 ? 0.5847 1.2119 1.2764 0.1558  -0.1352 -0.1554 296 VAL D O   
11156 C CB  . VAL D 296 ? 0.7028 1.2988 1.3715 0.1530  -0.1512 -0.1334 296 VAL D CB  
11157 C CG1 . VAL D 296 ? 0.6455 1.2682 1.3265 0.1509  -0.1450 -0.1363 296 VAL D CG1 
11158 C CG2 . VAL D 296 ? 0.7132 1.2998 1.3620 0.1455  -0.1448 -0.1275 296 VAL D CG2 
11159 N N   . ARG D 297 ? 0.6216 1.2078 1.2907 0.1554  -0.1427 -0.1482 297 ARG D N   
11160 C CA  . ARG D 297 ? 0.6226 1.2151 1.2893 0.1519  -0.1339 -0.1536 297 ARG D CA  
11161 C C   . ARG D 297 ? 0.6822 1.2696 1.3296 0.1430  -0.1284 -0.1450 297 ARG D C   
11162 O O   . ARG D 297 ? 0.6750 1.2418 1.3081 0.1408  -0.1328 -0.1366 297 ARG D O   
11163 C CB  . ARG D 297 ? 0.6484 1.2254 1.3176 0.1566  -0.1375 -0.1596 297 ARG D CB  
11164 C CG  . ARG D 297 ? 0.6671 1.2450 1.3296 0.1519  -0.1296 -0.1634 297 ARG D CG  
11165 C CD  . ARG D 297 ? 0.6761 1.2341 1.3384 0.1555  -0.1340 -0.1675 297 ARG D CD  
11166 N NE  . ARG D 297 ? 0.7514 1.3124 1.4320 0.1646  -0.1386 -0.1773 297 ARG D NE  
11167 C CZ  . ARG D 297 ? 0.7654 1.3135 1.4504 0.1690  -0.1416 -0.1838 297 ARG D CZ  
11168 N NH1 . ARG D 297 ? 0.8496 1.3811 1.5219 0.1646  -0.1404 -0.1813 297 ARG D NH1 
11169 N NH2 . ARG D 297 ? 0.7288 1.2806 1.4313 0.1777  -0.1458 -0.1928 297 ARG D NH2 
11170 N N   . ILE D 298 ? 0.7873 1.3934 1.4342 0.1379  -0.1188 -0.1472 298 ILE D N   
11171 C CA  . ILE D 298 ? 0.7989 1.4029 1.4294 0.1297  -0.1128 -0.1403 298 ILE D CA  
11172 C C   . ILE D 298 ? 0.7952 1.3987 1.4232 0.1278  -0.1077 -0.1463 298 ILE D C   
11173 O O   . ILE D 298 ? 0.7952 1.4152 1.4336 0.1295  -0.1028 -0.1556 298 ILE D O   
11174 C CB  . ILE D 298 ? 0.7939 1.4186 1.4245 0.1250  -0.1063 -0.1373 298 ILE D CB  
11175 C CG1 . ILE D 298 ? 0.8249 1.4489 1.4577 0.1264  -0.1119 -0.1313 298 ILE D CG1 
11176 C CG2 . ILE D 298 ? 0.7802 1.4035 1.3948 0.1170  -0.1000 -0.1309 298 ILE D CG2 
11177 C CD1 . ILE D 298 ? 0.8432 1.4862 1.4768 0.1218  -0.1060 -0.1281 298 ILE D CD1 
11178 N N   . LYS D 299 ? 0.7269 1.3114 1.3412 0.1242  -0.1086 -0.1412 299 LYS D N   
11179 C CA  . LYS D 299 ? 0.6824 1.2634 1.2946 0.1225  -0.1050 -0.1469 299 LYS D CA  
11180 C C   . LYS D 299 ? 0.6469 1.2455 1.2545 0.1161  -0.0956 -0.1476 299 LYS D C   
11181 O O   . LYS D 299 ? 0.6503 1.2643 1.2573 0.1133  -0.0917 -0.1441 299 LYS D O   
11182 C CB  . LYS D 299 ? 0.7320 1.2867 1.3321 0.1206  -0.1092 -0.1409 299 LYS D CB  
11183 C CG  . LYS D 299 ? 0.7473 1.2831 1.3517 0.1273  -0.1186 -0.1411 299 LYS D CG  
11184 C CD  . LYS D 299 ? 0.7898 1.2993 1.3813 0.1248  -0.1219 -0.1350 299 LYS D CD  
11185 C CE  . LYS D 299 ? 0.8578 1.3476 1.4526 0.1317  -0.1317 -0.1345 299 LYS D CE  
11186 N NZ  . LYS D 299 ? 0.8800 1.3432 1.4616 0.1290  -0.1346 -0.1279 299 LYS D NZ  
11187 N N   . LYS D 300 ? 0.6616 1.2575 1.2661 0.1136  -0.0923 -0.1522 300 LYS D N   
11188 C CA  . LYS D 300 ? 0.5724 1.1861 1.1744 0.1087  -0.0841 -0.1552 300 LYS D CA  
11189 C C   . LYS D 300 ? 0.5421 1.1550 1.1301 0.1012  -0.0806 -0.1448 300 LYS D C   
11190 O O   . LYS D 300 ? 0.5601 1.1548 1.1383 0.0988  -0.0837 -0.1368 300 LYS D O   
11191 C CB  . LYS D 300 ? 0.5796 1.1902 1.1831 0.1086  -0.0825 -0.1640 300 LYS D CB  
11192 C CG  . LYS D 300 ? 0.6340 1.2522 1.2522 0.1155  -0.0835 -0.1763 300 LYS D CG  
11193 C CD  . LYS D 300 ? 0.5998 1.2133 1.2192 0.1155  -0.0824 -0.1855 300 LYS D CD  
11194 C CE  . LYS D 300 ? 0.7482 1.3355 1.3670 0.1179  -0.0895 -0.1847 300 LYS D CE  
11195 N NZ  . LYS D 300 ? 0.6671 1.2498 1.2899 0.1188  -0.0890 -0.1951 300 LYS D NZ  
11196 N N   . HIS D 301 ? 0.5641 1.1971 1.1512 0.0977  -0.0739 -0.1451 301 HIS D N   
11197 C CA  . HIS D 301 ? 0.5721 1.2078 1.1472 0.0907  -0.0695 -0.1369 301 HIS D CA  
11198 C C   . HIS D 301 ? 0.5189 1.1469 1.0875 0.0893  -0.0721 -0.1259 301 HIS D C   
11199 O O   . HIS D 301 ? 0.5229 1.1442 1.0801 0.0842  -0.0705 -0.1181 301 HIS D O   
11200 C CB  . HIS D 301 ? 0.5443 1.1678 1.1109 0.0865  -0.0687 -0.1364 301 HIS D CB  
11201 C CG  . HIS D 301 ? 0.5034 1.1315 1.0759 0.0878  -0.0671 -0.1475 301 HIS D CG  
11202 N ND1 . HIS D 301 ? 0.4944 1.1065 1.0648 0.0870  -0.0694 -0.1501 301 HIS D ND1 
11203 C CD2 . HIS D 301 ? 0.5189 1.1657 1.0990 0.0898  -0.0633 -0.1568 301 HIS D CD2 
11204 C CE1 . HIS D 301 ? 0.4975 1.1180 1.0743 0.0885  -0.0675 -0.1609 301 HIS D CE1 
11205 N NE2 . HIS D 301 ? 0.4933 1.1351 1.0757 0.0903  -0.0637 -0.1652 301 HIS D NE2 
11206 N N   . ALA D 302 ? 0.4881 1.1176 1.0642 0.0939  -0.0761 -0.1257 302 ALA D N   
11207 C CA  . ALA D 302 ? 0.5292 1.1524 1.0997 0.0929  -0.0790 -0.1162 302 ALA D CA  
11208 C C   . ALA D 302 ? 0.5306 1.1735 1.1023 0.0900  -0.0738 -0.1134 302 ALA D C   
11209 O O   . ALA D 302 ? 0.5756 1.2374 1.1562 0.0911  -0.0696 -0.1197 302 ALA D O   
11210 C CB  . ALA D 302 ? 0.5497 1.1636 1.1277 0.0992  -0.0869 -0.1170 302 ALA D CB  
11211 N N   . CYS D 303 ? 0.5444 1.1822 1.1065 0.0863  -0.0738 -0.1039 303 CYS D N   
11212 C CA  . CYS D 303 ? 0.5461 1.1998 1.1082 0.0832  -0.0693 -0.0998 303 CYS D CA  
11213 C C   . CYS D 303 ? 0.5729 1.2200 1.1346 0.0844  -0.0744 -0.0936 303 CYS D C   
11214 O O   . CYS D 303 ? 0.5977 1.2296 1.1481 0.0821  -0.0769 -0.0860 303 CYS D O   
11215 C CB  . CYS D 303 ? 0.5563 1.2120 1.1068 0.0768  -0.0636 -0.0945 303 CYS D CB  
11216 S SG  . CYS D 303 ? 0.5332 1.2061 1.0826 0.0728  -0.0583 -0.0885 303 CYS D SG  
11217 N N   . ILE D 304 ? 0.6370 1.2958 1.2110 0.0878  -0.0758 -0.0970 304 ILE D N   
11218 C CA  . ILE D 304 ? 0.5759 1.2304 1.1517 0.0892  -0.0811 -0.0922 304 ILE D CA  
11219 C C   . ILE D 304 ? 0.5789 1.2520 1.1590 0.0861  -0.0762 -0.0900 304 ILE D C   
11220 O O   . ILE D 304 ? 0.6128 1.3045 1.2033 0.0868  -0.0716 -0.0957 304 ILE D O   
11221 C CB  . ILE D 304 ? 0.5740 1.2250 1.1620 0.0961  -0.0883 -0.0977 304 ILE D CB  
11222 C CG1 . ILE D 304 ? 0.6488 1.2803 1.2322 0.0991  -0.0933 -0.0995 304 ILE D CG1 
11223 C CG2 . ILE D 304 ? 0.6430 1.2904 1.2329 0.0973  -0.0943 -0.0928 304 ILE D CG2 
11224 C CD1 . ILE D 304 ? 0.7288 1.3523 1.3216 0.1060  -0.1019 -0.1030 304 ILE D CD1 
11225 N N   . SER D 305 ? 0.5975 1.2652 1.1692 0.0827  -0.0770 -0.0817 305 SER D N   
11226 C CA  . SER D 305 ? 0.6145 1.2975 1.1894 0.0794  -0.0727 -0.0785 305 SER D CA  
11227 C C   . SER D 305 ? 0.6555 1.3308 1.2301 0.0798  -0.0787 -0.0733 305 SER D C   
11228 O O   . SER D 305 ? 0.7315 1.3889 1.2942 0.0791  -0.0828 -0.0677 305 SER D O   
11229 C CB  . SER D 305 ? 0.6799 1.3662 1.2436 0.0735  -0.0658 -0.0733 305 SER D CB  
11230 O OG  . SER D 305 ? 0.6862 1.3542 1.2359 0.0719  -0.0676 -0.0687 305 SER D OG  
11231 N N   . SER D 306 ? 0.6842 1.3733 1.2715 0.0807  -0.0790 -0.0751 306 SER D N   
11232 C CA  . SER D 306 ? 0.7605 1.4457 1.3494 0.0806  -0.0843 -0.0707 306 SER D CA  
11233 C C   . SER D 306 ? 0.7820 1.4461 1.3652 0.0843  -0.0939 -0.0692 306 SER D C   
11234 O O   . SER D 306 ? 0.7816 1.4313 1.3520 0.0822  -0.0968 -0.0625 306 SER D O   
11235 C CB  . SER D 306 ? 0.7771 1.4632 1.3563 0.0746  -0.0801 -0.0629 306 SER D CB  
11236 O OG  . SER D 306 ? 0.8650 1.5370 1.4276 0.0721  -0.0787 -0.0581 306 SER D OG  
11237 N N   . SER D 307 ? 0.8076 1.4700 1.4003 0.0900  -0.0988 -0.0755 307 SER D N   
11238 C CA  . SER D 307 ? 0.8000 1.4425 1.3879 0.0943  -0.1082 -0.0746 307 SER D CA  
11239 C C   . SER D 307 ? 0.8966 1.5451 1.5022 0.1006  -0.1145 -0.0812 307 SER D C   
11240 O O   . SER D 307 ? 0.8274 1.4955 1.4486 0.1015  -0.1107 -0.0868 307 SER D O   
11241 C CB  . SER D 307 ? 0.7721 1.3994 1.3487 0.0948  -0.1078 -0.0745 307 SER D CB  
11242 O OG  . SER D 307 ? 0.7868 1.4074 1.3473 0.0891  -0.1029 -0.0679 307 SER D OG  
11243 N N   . ILE D 308 ? 1.1974 1.8288 1.8002 0.1051  -0.1241 -0.0805 308 ILE D N   
11244 C CA  . ILE D 308 ? 1.1967 1.8310 1.8155 0.1118  -0.1317 -0.0861 308 ILE D CA  
11245 C C   . ILE D 308 ? 1.2213 1.8382 1.8364 0.1170  -0.1375 -0.0884 308 ILE D C   
11246 O O   . ILE D 308 ? 1.2460 1.8418 1.8449 0.1165  -0.1420 -0.0825 308 ILE D O   
11247 C CB  . ILE D 308 ? 1.1981 1.8292 1.8189 0.1125  -0.1398 -0.0825 308 ILE D CB  
11248 C CG1 . ILE D 308 ? 1.1781 1.8257 1.8030 0.1070  -0.1339 -0.0802 308 ILE D CG1 
11249 C CG2 . ILE D 308 ? 1.2004 1.8349 1.8388 0.1198  -0.1482 -0.0887 308 ILE D CG2 
11250 C CD1 . ILE D 308 ? 1.1525 1.8250 1.7983 0.1077  -0.1287 -0.0871 308 ILE D CD1 
11251 N N   . ILE D 309 ? 0.9291 1.5544 1.5589 0.1219  -0.1373 -0.0968 309 ILE D N   
11252 C CA  . ILE D 309 ? 0.8642 1.4743 1.4926 0.1271  -0.1422 -0.0999 309 ILE D CA  
11253 C C   . ILE D 309 ? 0.8577 1.4651 1.4996 0.1347  -0.1527 -0.1035 309 ILE D C   
11254 O O   . ILE D 309 ? 0.8271 1.4529 1.4879 0.1374  -0.1526 -0.1093 309 ILE D O   
11255 C CB  . ILE D 309 ? 0.8063 1.4265 1.4412 0.1275  -0.1345 -0.1074 309 ILE D CB  
11256 C CG1 . ILE D 309 ? 0.8225 1.4514 1.4478 0.1199  -0.1238 -0.1046 309 ILE D CG1 
11257 C CG2 . ILE D 309 ? 0.8248 1.4257 1.4542 0.1312  -0.1387 -0.1091 309 ILE D CG2 
11258 C CD1 . ILE D 309 ? 0.8509 1.4610 1.4547 0.1151  -0.1234 -0.0960 309 ILE D CD1 
11259 N N   . GLY D 310 ? 0.8656 1.4501 1.4979 0.1381  -0.1618 -0.0999 310 GLY D N   
11260 C CA  . GLY D 310 ? 0.8745 1.4538 1.5177 0.1457  -0.1731 -0.1024 310 GLY D CA  
11261 C C   . GLY D 310 ? 0.9213 1.5047 1.5806 0.1526  -0.1744 -0.1117 310 GLY D C   
11262 O O   . GLY D 310 ? 0.9003 1.4921 1.5633 0.1515  -0.1663 -0.1171 310 GLY D O   
11263 N N   . TRP D 311 ? 1.1340 1.7111 1.8031 0.1600  -0.1853 -0.1139 311 TRP D N   
11264 C CA  . TRP D 311 ? 1.1358 1.7161 1.8220 0.1677  -0.1880 -0.1230 311 TRP D CA  
11265 C C   . TRP D 311 ? 1.1652 1.7229 1.8395 0.1696  -0.1900 -0.1221 311 TRP D C   
11266 O O   . TRP D 311 ? 1.1936 1.7284 1.8500 0.1688  -0.1958 -0.1141 311 TRP D O   
11267 C CB  . TRP D 311 ? 1.1355 1.7171 1.8372 0.1753  -0.1996 -0.1255 311 TRP D CB  
11268 C CG  . TRP D 311 ? 1.1431 1.7472 1.8590 0.1736  -0.1983 -0.1269 311 TRP D CG  
11269 C CD1 . TRP D 311 ? 1.0775 1.7079 1.8139 0.1739  -0.1911 -0.1349 311 TRP D CD1 
11270 C CD2 . TRP D 311 ? 1.2347 1.8367 1.9455 0.1713  -0.2042 -0.1203 311 TRP D CD2 
11271 N NE1 . TRP D 311 ? 1.0820 1.7268 1.8268 0.1715  -0.1920 -0.1334 311 TRP D NE1 
11272 C CE2 . TRP D 311 ? 1.1923 1.8200 1.9219 0.1699  -0.2003 -0.1247 311 TRP D CE2 
11273 C CE3 . TRP D 311 ? 1.2099 1.7908 1.9017 0.1700  -0.2124 -0.1113 311 TRP D CE3 
11274 C CZ2 . TRP D 311 ? 1.1576 1.7901 1.8883 0.1673  -0.2045 -0.1205 311 TRP D CZ2 
11275 C CZ3 . TRP D 311 ? 1.2388 1.8245 1.9310 0.1677  -0.2167 -0.1075 311 TRP D CZ3 
11276 C CH2 . TRP D 311 ? 1.2108 1.8220 1.9227 0.1663  -0.2129 -0.1121 311 TRP D CH2 
11277 N N   . HIS D 312 ? 0.9199 1.4842 1.6044 0.1722  -0.1850 -0.1305 312 HIS D N   
11278 C CA  . HIS D 312 ? 0.8668 1.4112 1.5448 0.1752  -0.1874 -0.1317 312 HIS D CA  
11279 C C   . HIS D 312 ? 0.8402 1.3653 1.4933 0.1683  -0.1846 -0.1227 312 HIS D C   
11280 O O   . HIS D 312 ? 0.7943 1.2956 1.4364 0.1701  -0.1905 -0.1188 312 HIS D O   
11281 C CB  . HIS D 312 ? 0.9238 1.4534 1.6090 0.1843  -0.2005 -0.1327 312 HIS D CB  
11282 C CG  . HIS D 312 ? 0.9353 1.4837 1.6465 0.1916  -0.2037 -0.1419 312 HIS D CG  
11283 N ND1 . HIS D 312 ? 0.9704 1.5296 1.6914 0.1934  -0.2091 -0.1409 312 HIS D ND1 
11284 C CD2 . HIS D 312 ? 0.9115 1.4698 1.6415 0.1976  -0.2021 -0.1528 312 HIS D CD2 
11285 C CE1 . HIS D 312 ? 0.9603 1.5360 1.7056 0.2002  -0.2106 -0.1505 312 HIS D CE1 
11286 N NE2 . HIS D 312 ? 0.9225 1.4980 1.6735 0.2030  -0.2062 -0.1579 312 HIS D NE2 
11287 N N   . SER D 313 ? 0.8244 1.3597 1.4686 0.1602  -0.1754 -0.1192 313 SER D N   
11288 C CA  . SER D 313 ? 0.7501 1.2704 1.3723 0.1532  -0.1713 -0.1113 313 SER D CA  
11289 C C   . SER D 313 ? 0.7246 1.2476 1.3468 0.1508  -0.1629 -0.1166 313 SER D C   
11290 O O   . SER D 313 ? 0.7319 1.2657 1.3697 0.1550  -0.1612 -0.1263 313 SER D O   
11291 C CB  . SER D 313 ? 0.7489 1.2779 1.3617 0.1462  -0.1665 -0.1045 313 SER D CB  
11292 O OG  . SER D 313 ? 0.8222 1.3459 1.4333 0.1483  -0.1751 -0.0995 313 SER D OG  
11293 N N   . THR D 314 ? 0.7148 1.2280 1.3196 0.1439  -0.1576 -0.1107 314 THR D N   
11294 C CA  . THR D 314 ? 0.6970 1.2117 1.3007 0.1410  -0.1501 -0.1154 314 THR D CA  
11295 C C   . THR D 314 ? 0.6981 1.2126 1.2856 0.1321  -0.1423 -0.1086 314 THR D C   
11296 O O   . THR D 314 ? 0.6713 1.1676 1.2426 0.1290  -0.1446 -0.0998 314 THR D O   
11297 C CB  . THR D 314 ? 0.7340 1.2265 1.3352 0.1448  -0.1555 -0.1167 314 THR D CB  
11298 O OG1 . THR D 314 ? 0.7121 1.2070 1.3306 0.1535  -0.1620 -0.1244 314 THR D OG1 
11299 C CG2 . THR D 314 ? 0.7764 1.2690 1.3747 0.1406  -0.1478 -0.1208 314 THR D CG2 
11300 N N   . VAL D 315 ? 0.6988 1.2337 1.2907 0.1282  -0.1332 -0.1128 315 VAL D N   
11301 C CA  . VAL D 315 ? 0.7307 1.2679 1.3094 0.1200  -0.1254 -0.1075 315 VAL D CA  
11302 C C   . VAL D 315 ? 0.7578 1.2903 1.3343 0.1180  -0.1210 -0.1119 315 VAL D C   
11303 O O   . VAL D 315 ? 0.7820 1.3272 1.3703 0.1203  -0.1179 -0.1213 315 VAL D O   
11304 C CB  . VAL D 315 ? 0.7356 1.2975 1.3194 0.1167  -0.1184 -0.1085 315 VAL D CB  
11305 C CG1 . VAL D 315 ? 0.6871 1.2512 1.2580 0.1088  -0.1105 -0.1037 315 VAL D CG1 
11306 C CG2 . VAL D 315 ? 0.8017 1.3674 1.3877 0.1181  -0.1228 -0.1040 315 VAL D CG2 
11307 N N   . GLY D 316 ? 0.8540 1.3686 1.4156 0.1136  -0.1206 -0.1054 316 GLY D N   
11308 C CA  . GLY D 316 ? 0.8658 1.3742 1.4248 0.1110  -0.1169 -0.1089 316 GLY D CA  
11309 C C   . GLY D 316 ? 0.8377 1.3661 1.3985 0.1061  -0.1076 -0.1129 316 GLY D C   
11310 O O   . GLY D 316 ? 0.8069 1.3533 1.3695 0.1041  -0.1035 -0.1120 316 GLY D O   
11311 N N   . GLN D 317 ? 0.6855 1.2101 1.2458 0.1040  -0.1047 -0.1174 317 GLN D N   
11312 C CA  . GLN D 317 ? 0.6378 1.1799 1.1989 0.0994  -0.0965 -0.1216 317 GLN D CA  
11313 C C   . GLN D 317 ? 0.6363 1.1796 1.1844 0.0921  -0.0917 -0.1126 317 GLN D C   
11314 O O   . GLN D 317 ? 0.6527 1.1787 1.1895 0.0895  -0.0937 -0.1043 317 GLN D O   
11315 C CB  . GLN D 317 ? 0.6153 1.1521 1.1792 0.0990  -0.0953 -0.1291 317 GLN D CB  
11316 C CG  . GLN D 317 ? 0.6788 1.2166 1.2567 0.1063  -0.0991 -0.1396 317 GLN D CG  
11317 C CD  . GLN D 317 ? 0.7025 1.2335 1.2825 0.1056  -0.0981 -0.1470 317 GLN D CD  
11318 O OE1 . GLN D 317 ? 0.6447 1.1711 1.2163 0.0993  -0.0945 -0.1445 317 GLN D OE1 
11319 N NE2 . GLN D 317 ? 0.8302 1.3608 1.4223 0.1120  -0.1013 -0.1566 317 GLN D NE2 
11320 N N   . TRP D 318 ? 0.5813 1.1454 1.1310 0.0890  -0.0852 -0.1144 318 TRP D N   
11321 C CA  . TRP D 318 ? 0.5573 1.1259 1.0965 0.0823  -0.0799 -0.1071 318 TRP D CA  
11322 C C   . TRP D 318 ? 0.5401 1.1013 1.0712 0.0814  -0.0823 -0.0970 318 TRP D C   
11323 O O   . TRP D 318 ? 0.5867 1.1456 1.1074 0.0762  -0.0790 -0.0898 318 TRP D O   
11324 C CB  . TRP D 318 ? 0.5599 1.1176 1.0912 0.0773  -0.0775 -0.1058 318 TRP D CB  
11325 C CG  . TRP D 318 ? 0.5100 1.0783 1.0475 0.0764  -0.0740 -0.1151 318 TRP D CG  
11326 C CD1 . TRP D 318 ? 0.5095 1.0979 1.0484 0.0736  -0.0681 -0.1182 318 TRP D CD1 
11327 C CD2 . TRP D 318 ? 0.5100 1.0687 1.0524 0.0783  -0.0762 -0.1225 318 TRP D CD2 
11328 N NE1 . TRP D 318 ? 0.4922 1.0845 1.0362 0.0736  -0.0667 -0.1274 318 TRP D NE1 
11329 C CE2 . TRP D 318 ? 0.5025 1.0768 1.0491 0.0764  -0.0715 -0.1304 318 TRP D CE2 
11330 C CE3 . TRP D 318 ? 0.5250 1.0628 1.0683 0.0814  -0.0820 -0.1232 318 TRP D CE3 
11331 C CZ2 . TRP D 318 ? 0.5116 1.0815 1.0637 0.0775  -0.0724 -0.1394 318 TRP D CZ2 
11332 C CZ3 . TRP D 318 ? 0.5392 1.0723 1.0883 0.0825  -0.0827 -0.1318 318 TRP D CZ3 
11333 C CH2 . TRP D 318 ? 0.5259 1.0750 1.0795 0.0805  -0.0779 -0.1401 318 TRP D CH2 
11334 N N   . ALA D 319 ? 0.5557 1.1133 1.0915 0.0866  -0.0881 -0.0967 319 ALA D N   
11335 C CA  . ALA D 319 ? 0.5859 1.1367 1.1143 0.0861  -0.0910 -0.0879 319 ALA D CA  
11336 C C   . ALA D 319 ? 0.5722 1.1430 1.1037 0.0844  -0.0870 -0.0865 319 ALA D C   
11337 O O   . ALA D 319 ? 0.5511 1.1397 1.0942 0.0867  -0.0851 -0.0930 319 ALA D O   
11338 C CB  . ALA D 319 ? 0.5847 1.1231 1.1170 0.0924  -0.0997 -0.0881 319 ALA D CB  
11339 N N   . ARG D 320 ? 0.6618 1.2292 1.1827 0.0804  -0.0856 -0.0779 320 ARG D N   
11340 C CA  . ARG D 320 ? 0.6730 1.2569 1.1953 0.0783  -0.0819 -0.0753 320 ARG D CA  
11341 C C   . ARG D 320 ? 0.6781 1.2559 1.1989 0.0803  -0.0874 -0.0702 320 ARG D C   
11342 O O   . ARG D 320 ? 0.6798 1.2396 1.1894 0.0796  -0.0909 -0.0639 320 ARG D O   
11343 C CB  . ARG D 320 ? 0.6937 1.2807 1.2060 0.0719  -0.0754 -0.0700 320 ARG D CB  
11344 C CG  . ARG D 320 ? 0.7248 1.3280 1.2383 0.0695  -0.0715 -0.0669 320 ARG D CG  
11345 C CD  . ARG D 320 ? 0.6945 1.2998 1.1984 0.0637  -0.0655 -0.0615 320 ARG D CD  
11346 N NE  . ARG D 320 ? 0.7162 1.3360 1.2211 0.0615  -0.0620 -0.0582 320 ARG D NE  
11347 C CZ  . ARG D 320 ? 0.7329 1.3719 1.2437 0.0602  -0.0568 -0.0613 320 ARG D CZ  
11348 N NH1 . ARG D 320 ? 0.7161 1.3625 1.2320 0.0609  -0.0546 -0.0683 320 ARG D NH1 
11349 N NH2 . ARG D 320 ? 0.7758 1.4259 1.2869 0.0581  -0.0539 -0.0574 320 ARG D NH2 
11350 N N   . ILE D 321 ? 0.6354 1.2282 1.1672 0.0827  -0.0881 -0.0731 321 ILE D N   
11351 C CA  . ILE D 321 ? 0.6628 1.2527 1.1957 0.0848  -0.0936 -0.0695 321 ILE D CA  
11352 C C   . ILE D 321 ? 0.6718 1.2792 1.2076 0.0815  -0.0888 -0.0672 321 ILE D C   
11353 O O   . ILE D 321 ? 0.6795 1.3057 1.2252 0.0812  -0.0839 -0.0721 321 ILE D O   
11354 C CB  . ILE D 321 ? 0.6696 1.2604 1.2159 0.0915  -0.1003 -0.0757 321 ILE D CB  
11355 C CG1 . ILE D 321 ? 0.6595 1.2331 1.2038 0.0950  -0.1049 -0.0783 321 ILE D CG1 
11356 C CG2 . ILE D 321 ? 0.6805 1.2677 1.2279 0.0935  -0.1068 -0.0719 321 ILE D CG2 
11357 C CD1 . ILE D 321 ? 0.7021 1.2518 1.2307 0.0940  -0.1095 -0.0706 321 ILE D CD1 
11358 N N   . GLU D 322 ? 0.7345 1.3351 1.2610 0.0788  -0.0899 -0.0598 322 GLU D N   
11359 C CA  . GLU D 322 ? 0.7512 1.3665 1.2796 0.0753  -0.0854 -0.0569 322 GLU D CA  
11360 C C   . GLU D 322 ? 0.8368 1.4422 1.3585 0.0747  -0.0901 -0.0505 322 GLU D C   
11361 O O   . GLU D 322 ? 0.8372 1.4242 1.3506 0.0766  -0.0962 -0.0477 322 GLU D O   
11362 C CB  . GLU D 322 ? 0.7970 1.4182 1.3180 0.0701  -0.0772 -0.0543 322 GLU D CB  
11363 C CG  . GLU D 322 ? 0.7930 1.3969 1.2980 0.0670  -0.0770 -0.0477 322 GLU D CG  
11364 C CD  . GLU D 322 ? 0.8315 1.4425 1.3307 0.0620  -0.0692 -0.0453 322 GLU D CD  
11365 O OE1 . GLU D 322 ? 0.8670 1.4957 1.3737 0.0610  -0.0643 -0.0488 322 GLU D OE1 
11366 O OE2 . GLU D 322 ? 0.7945 1.3936 1.2817 0.0592  -0.0680 -0.0398 322 GLU D OE2 
11367 N N   . ASN D 323 ? 1.0505 1.6683 1.5757 0.0721  -0.0873 -0.0482 323 ASN D N   
11368 C CA  . ASN D 323 ? 1.0593 1.6698 1.5774 0.0703  -0.0902 -0.0420 323 ASN D CA  
11369 C C   . ASN D 323 ? 1.0691 1.6700 1.5904 0.0748  -0.0998 -0.0428 323 ASN D C   
11370 O O   . ASN D 323 ? 1.0917 1.6746 1.6011 0.0753  -0.1050 -0.0386 323 ASN D O   
11371 C CB  . ASN D 323 ? 1.0740 1.6697 1.5745 0.0668  -0.0879 -0.0355 323 ASN D CB  
11372 C CG  . ASN D 323 ? 1.0807 1.6702 1.5732 0.0645  -0.0895 -0.0294 323 ASN D CG  
11373 O OD1 . ASN D 323 ? 1.1311 1.7306 1.6315 0.0641  -0.0904 -0.0294 323 ASN D OD1 
11374 N ND2 . ASN D 323 ? 1.0985 1.6715 1.5754 0.0629  -0.0897 -0.0242 323 ASN D ND2 
11375 N N   . MET D 324 ? 0.8368 1.4508 1.3745 0.0779  -0.1022 -0.0483 324 MET D N   
11376 C CA  . MET D 324 ? 0.7815 1.3904 1.3255 0.0821  -0.1115 -0.0496 324 MET D CA  
11377 C C   . MET D 324 ? 0.7391 1.3270 1.2744 0.0862  -0.1189 -0.0491 324 MET D C   
11378 O O   . MET D 324 ? 0.7220 1.2960 1.2500 0.0876  -0.1263 -0.0457 324 MET D O   
11379 C CB  . MET D 324 ? 0.8137 1.4212 1.3541 0.0795  -0.1139 -0.0445 324 MET D CB  
11380 C CG  . MET D 324 ? 0.8494 1.4761 1.3984 0.0754  -0.1072 -0.0443 324 MET D CG  
11381 S SD  . MET D 324 ? 0.8782 1.4995 1.4201 0.0717  -0.1098 -0.0377 324 MET D SD  
11382 C CE  . MET D 324 ? 0.9175 1.5181 1.4353 0.0691  -0.1079 -0.0311 324 MET D CE  
11383 N N   . THR D 325 ? 0.7102 1.2957 1.2461 0.0879  -0.1169 -0.0527 325 THR D N   
11384 C CA  . THR D 325 ? 0.6465 1.2124 1.1754 0.0918  -0.1236 -0.0525 325 THR D CA  
11385 C C   . THR D 325 ? 0.7080 1.2761 1.2512 0.0983  -0.1318 -0.0579 325 THR D C   
11386 O O   . THR D 325 ? 0.7626 1.3465 1.3221 0.1007  -0.1298 -0.0648 325 THR D O   
11387 C CB  . THR D 325 ? 0.6120 1.1742 1.1370 0.0911  -0.1185 -0.0546 325 THR D CB  
11388 O OG1 . THR D 325 ? 0.6966 1.2595 1.2104 0.0850  -0.1106 -0.0501 325 THR D OG1 
11389 C CG2 . THR D 325 ? 0.5808 1.1206 1.0969 0.0944  -0.1251 -0.0533 325 THR D CG2 
11390 N N   . ILE D 326 ? 0.7586 1.3109 1.2958 0.1013  -0.1412 -0.0549 326 ILE D N   
11391 C CA  . ILE D 326 ? 0.7679 1.3216 1.3184 0.1076  -0.1504 -0.0592 326 ILE D CA  
11392 C C   . ILE D 326 ? 0.8113 1.3462 1.3568 0.1126  -0.1570 -0.0598 326 ILE D C   
11393 O O   . ILE D 326 ? 0.7813 1.2955 1.3091 0.1119  -0.1605 -0.0538 326 ILE D O   
11394 C CB  . ILE D 326 ? 0.6951 1.2462 1.2438 0.1076  -0.1573 -0.0555 326 ILE D CB  
11395 C CG1 . ILE D 326 ? 0.7111 1.2780 1.2622 0.1017  -0.1502 -0.0537 326 ILE D CG1 
11396 C CG2 . ILE D 326 ? 0.7643 1.3205 1.3299 0.1141  -0.1667 -0.0607 326 ILE D CG2 
11397 C CD1 . ILE D 326 ? 0.7755 1.3673 1.3468 0.1016  -0.1443 -0.0601 326 ILE D CD1 
11398 N N   . LEU D 327 ? 0.9496 1.4914 1.5104 0.1177  -0.1585 -0.0671 327 LEU D N   
11399 C CA  . LEU D 327 ? 0.9893 1.5141 1.5477 0.1228  -0.1647 -0.0685 327 LEU D CA  
11400 C C   . LEU D 327 ? 0.9897 1.5146 1.5617 0.1303  -0.1755 -0.0723 327 LEU D C   
11401 O O   . LEU D 327 ? 0.9517 1.4961 1.5424 0.1323  -0.1754 -0.0779 327 LEU D O   
11402 C CB  . LEU D 327 ? 0.9712 1.5017 1.5359 0.1231  -0.1579 -0.0744 327 LEU D CB  
11403 C CG  . LEU D 327 ? 0.9708 1.5014 1.5234 0.1162  -0.1476 -0.0715 327 LEU D CG  
11404 C CD1 . LEU D 327 ? 0.9713 1.5047 1.5301 0.1173  -0.1431 -0.0779 327 LEU D CD1 
11405 C CD2 . LEU D 327 ? 1.0012 1.5096 1.5317 0.1128  -0.1491 -0.0625 327 LEU D CD2 
11406 N N   . GLY D 328 ? 0.8505 1.3536 1.4133 0.1344  -0.1848 -0.0691 328 GLY D N   
11407 C CA  . GLY D 328 ? 0.8023 1.3029 1.3769 0.1421  -0.1961 -0.0724 328 GLY D CA  
11408 C C   . GLY D 328 ? 0.7811 1.2847 1.3709 0.1480  -0.1969 -0.0803 328 GLY D C   
11409 O O   . GLY D 328 ? 0.8047 1.3143 1.3970 0.1460  -0.1884 -0.0840 328 GLY D O   
11410 N N   . GLU D 329 ? 0.7944 1.2936 1.3946 0.1557  -0.2078 -0.0831 329 GLU D N   
11411 C CA  . GLU D 329 ? 0.8008 1.3013 1.4162 0.1624  -0.2100 -0.0908 329 GLU D CA  
11412 C C   . GLU D 329 ? 0.7247 1.2018 1.3255 0.1629  -0.2107 -0.0879 329 GLU D C   
11413 O O   . GLU D 329 ? 0.7420 1.1968 1.3240 0.1623  -0.2162 -0.0799 329 GLU D O   
11414 C CB  . GLU D 329 ? 0.8746 1.3761 1.5052 0.1707  -0.2224 -0.0941 329 GLU D CB  
11415 C CG  . GLU D 329 ? 0.8814 1.3811 1.5272 0.1788  -0.2264 -0.1017 329 GLU D CG  
11416 C CD  . GLU D 329 ? 0.8284 1.3270 1.4881 0.1874  -0.2396 -0.1041 329 GLU D CD  
11417 O OE1 . GLU D 329 ? 0.9230 1.4249 1.5820 0.1867  -0.2452 -0.1006 329 GLU D OE1 
11418 O OE2 . GLU D 329 ? 0.7942 1.2884 1.4656 0.1949  -0.2448 -0.1096 329 GLU D OE2 
11419 N N   . ASP D 330 ? 0.7335 1.2156 1.3430 0.1640  -0.2048 -0.0946 330 ASP D N   
11420 C CA  . ASP D 330 ? 0.7385 1.1998 1.3376 0.1647  -0.2052 -0.0932 330 ASP D CA  
11421 C C   . ASP D 330 ? 0.7274 1.1736 1.3018 0.1569  -0.2002 -0.0839 330 ASP D C   
11422 O O   . ASP D 330 ? 0.7373 1.1598 1.2954 0.1572  -0.2060 -0.0767 330 ASP D O   
11423 C CB  . ASP D 330 ? 0.7296 1.1721 1.3306 0.1731  -0.2182 -0.0927 330 ASP D CB  
11424 C CG  . ASP D 330 ? 0.7681 1.1880 1.3592 0.1739  -0.2188 -0.0911 330 ASP D CG  
11425 O OD1 . ASP D 330 ? 0.8698 1.2956 1.4715 0.1752  -0.2138 -0.0987 330 ASP D OD1 
11426 O OD2 . ASP D 330 ? 0.7389 1.1349 1.3111 0.1732  -0.2244 -0.0824 330 ASP D OD2 
11427 N N   . VAL D 331 ? 0.7227 1.1833 1.2948 0.1498  -0.1890 -0.0842 331 VAL D N   
11428 C CA  . VAL D 331 ? 0.7171 1.1671 1.2686 0.1421  -0.1826 -0.0766 331 VAL D CA  
11429 C C   . VAL D 331 ? 0.7267 1.1812 1.2803 0.1389  -0.1734 -0.0812 331 VAL D C   
11430 O O   . VAL D 331 ? 0.7287 1.2048 1.2960 0.1383  -0.1669 -0.0884 331 VAL D O   
11431 C CB  . VAL D 331 ? 0.7175 1.1793 1.2628 0.1361  -0.1779 -0.0720 331 VAL D CB  
11432 C CG1 . VAL D 331 ? 0.6895 1.1415 1.2149 0.1284  -0.1706 -0.0650 331 VAL D CG1 
11433 C CG2 . VAL D 331 ? 0.7727 1.2289 1.3151 0.1391  -0.1876 -0.0676 331 VAL D CG2 
11434 N N   . HIS D 332 ? 0.7247 1.1589 1.2644 0.1367  -0.1728 -0.0771 332 HIS D N   
11435 C CA  . HIS D 332 ? 0.7490 1.1842 1.2905 0.1340  -0.1655 -0.0815 332 HIS D CA  
11436 C C   . HIS D 332 ? 0.7312 1.1655 1.2572 0.1251  -0.1566 -0.0755 332 HIS D C   
11437 O O   . HIS D 332 ? 0.7050 1.1195 1.2139 0.1220  -0.1576 -0.0675 332 HIS D O   
11438 C CB  . HIS D 332 ? 0.7845 1.1977 1.3242 0.1381  -0.1713 -0.0822 332 HIS D CB  
11439 C CG  . HIS D 332 ? 0.7692 1.1838 1.3256 0.1473  -0.1798 -0.0889 332 HIS D CG  
11440 N ND1 . HIS D 332 ? 0.7960 1.2198 1.3691 0.1512  -0.1781 -0.0992 332 HIS D ND1 
11441 C CD2 . HIS D 332 ? 0.7791 1.1877 1.3386 0.1536  -0.1902 -0.0871 332 HIS D CD2 
11442 C CE1 . HIS D 332 ? 0.7964 1.2198 1.3827 0.1596  -0.1868 -0.1034 332 HIS D CE1 
11443 N NE2 . HIS D 332 ? 0.8129 1.2272 1.3915 0.1612  -0.1945 -0.0961 332 HIS D NE2 
11444 N N   . VAL D 333 ? 0.6915 1.1474 1.2238 0.1211  -0.1479 -0.0794 333 VAL D N   
11445 C CA  . VAL D 333 ? 0.6804 1.1386 1.2008 0.1131  -0.1391 -0.0749 333 VAL D CA  
11446 C C   . VAL D 333 ? 0.6957 1.1496 1.2164 0.1108  -0.1344 -0.0788 333 VAL D C   
11447 O O   . VAL D 333 ? 0.7176 1.1836 1.2522 0.1133  -0.1325 -0.0879 333 VAL D O   
11448 C CB  . VAL D 333 ? 0.6498 1.1331 1.1766 0.1099  -0.1325 -0.0767 333 VAL D CB  
11449 C CG1 . VAL D 333 ? 0.6627 1.1478 1.1773 0.1020  -0.1240 -0.0718 333 VAL D CG1 
11450 C CG2 . VAL D 333 ? 0.6876 1.1757 1.2163 0.1123  -0.1377 -0.0737 333 VAL D CG2 
11451 N N   . SER D 334 ? 0.6949 1.1317 1.2006 0.1061  -0.1324 -0.0724 334 SER D N   
11452 C CA  . SER D 334 ? 0.7528 1.1846 1.2584 0.1032  -0.1280 -0.0757 334 SER D CA  
11453 C C   . SER D 334 ? 0.7128 1.1667 1.2241 0.0987  -0.1188 -0.0805 334 SER D C   
11454 O O   . SER D 334 ? 0.6592 1.1307 1.1726 0.0972  -0.1155 -0.0800 334 SER D O   
11455 C CB  . SER D 334 ? 0.8105 1.2199 1.2988 0.0984  -0.1272 -0.0670 334 SER D CB  
11456 O OG  . SER D 334 ? 0.8142 1.2021 1.2961 0.1027  -0.1358 -0.0623 334 SER D OG  
11457 N N   . ASP D 335 ? 0.7213 1.1739 1.2349 0.0963  -0.1150 -0.0852 335 ASP D N   
11458 C CA  . ASP D 335 ? 0.6239 1.0959 1.1412 0.0918  -0.1067 -0.0895 335 ASP D CA  
11459 C C   . ASP D 335 ? 0.6142 1.0865 1.1184 0.0847  -0.1012 -0.0810 335 ASP D C   
11460 O O   . ASP D 335 ? 0.6500 1.1043 1.1416 0.0823  -0.1026 -0.0729 335 ASP D O   
11461 C CB  . ASP D 335 ? 0.6707 1.1401 1.1932 0.0909  -0.1046 -0.0967 335 ASP D CB  
11462 C CG  . ASP D 335 ? 0.7421 1.2093 1.2775 0.0982  -0.1100 -0.1054 335 ASP D CG  
11463 O OD1 . ASP D 335 ? 0.7788 1.2553 1.3228 0.1037  -0.1135 -0.1081 335 ASP D OD1 
11464 O OD2 . ASP D 335 ? 0.7936 1.2497 1.3310 0.0984  -0.1109 -0.1096 335 ASP D OD2 
11465 N N   . GLU D 336 ? 0.5979 1.0909 1.1050 0.0814  -0.0947 -0.0830 336 GLU D N   
11466 C CA  . GLU D 336 ? 0.5806 1.0769 1.0775 0.0746  -0.0886 -0.0764 336 GLU D CA  
11467 C C   . GLU D 336 ? 0.5897 1.0784 1.0759 0.0739  -0.0905 -0.0670 336 GLU D C   
11468 O O   . GLU D 336 ? 0.5932 1.0763 1.0684 0.0688  -0.0868 -0.0602 336 GLU D O   
11469 C CB  . GLU D 336 ? 0.5492 1.0331 1.0398 0.0698  -0.0857 -0.0751 336 GLU D CB  
11470 C CG  . GLU D 336 ? 0.5347 1.0206 1.0350 0.0710  -0.0855 -0.0846 336 GLU D CG  
11471 C CD  . GLU D 336 ? 0.5474 1.0150 1.0420 0.0673  -0.0850 -0.0829 336 GLU D CD  
11472 O OE1 . GLU D 336 ? 0.5677 1.0262 1.0511 0.0623  -0.0824 -0.0748 336 GLU D OE1 
11473 O OE2 . GLU D 336 ? 0.5561 1.0181 1.0577 0.0694  -0.0872 -0.0898 336 GLU D OE2 
11474 N N   . ILE D 337 ? 0.5774 1.0660 1.0671 0.0790  -0.0962 -0.0667 337 ILE D N   
11475 C CA  . ILE D 337 ? 0.5777 1.0585 1.0575 0.0788  -0.0991 -0.0585 337 ILE D CA  
11476 C C   . ILE D 337 ? 0.5708 1.0716 1.0546 0.0777  -0.0959 -0.0582 337 ILE D C   
11477 O O   . ILE D 337 ? 0.5854 1.1033 1.0822 0.0805  -0.0956 -0.0646 337 ILE D O   
11478 C CB  . ILE D 337 ? 0.5967 1.0631 1.0772 0.0849  -0.1084 -0.0580 337 ILE D CB  
11479 C CG1 . ILE D 337 ? 0.5621 1.0072 1.0378 0.0857  -0.1114 -0.0575 337 ILE D CG1 
11480 C CG2 . ILE D 337 ? 0.5866 1.0455 1.0566 0.0849  -0.1119 -0.0501 337 ILE D CG2 
11481 C CD1 . ILE D 337 ? 0.5883 1.0167 1.0472 0.0802  -0.1086 -0.0490 337 ILE D CD1 
11482 N N   . TYR D 338 ? 0.5979 1.0964 1.0706 0.0737  -0.0933 -0.0507 338 TYR D N   
11483 C CA  . TYR D 338 ? 0.6125 1.1278 1.0874 0.0720  -0.0901 -0.0491 338 TYR D CA  
11484 C C   . TYR D 338 ? 0.6116 1.1193 1.0813 0.0741  -0.0958 -0.0440 338 TYR D C   
11485 O O   . TYR D 338 ? 0.5832 1.0721 1.0404 0.0737  -0.0988 -0.0382 338 TYR D O   
11486 C CB  . TYR D 338 ? 0.5885 1.1084 1.0557 0.0657  -0.0823 -0.0450 338 TYR D CB  
11487 C CG  . TYR D 338 ? 0.5807 1.1141 1.0475 0.0636  -0.0792 -0.0417 338 TYR D CG  
11488 C CD1 . TYR D 338 ? 0.6003 1.1550 1.0783 0.0639  -0.0762 -0.0463 338 TYR D CD1 
11489 C CD2 . TYR D 338 ? 0.5705 1.0948 1.0253 0.0612  -0.0789 -0.0341 338 TYR D CD2 
11490 C CE1 . TYR D 338 ? 0.6024 1.1685 1.0800 0.0618  -0.0732 -0.0429 338 TYR D CE1 
11491 C CE2 . TYR D 338 ? 0.5647 1.1005 1.0195 0.0593  -0.0762 -0.0312 338 TYR D CE2 
11492 C CZ  . TYR D 338 ? 0.5924 1.1489 1.0588 0.0595  -0.0734 -0.0354 338 TYR D CZ  
11493 O OH  . TYR D 338 ? 0.6321 1.1992 1.0986 0.0574  -0.0707 -0.0322 338 TYR D OH  
11494 N N   . SER D 339 ? 0.5786 1.1010 1.0579 0.0763  -0.0972 -0.0463 339 SER D N   
11495 C CA  . SER D 339 ? 0.5758 1.0933 1.0522 0.0783  -0.1030 -0.0424 339 SER D CA  
11496 C C   . SER D 339 ? 0.5786 1.1124 1.0574 0.0753  -0.0986 -0.0406 339 SER D C   
11497 O O   . SER D 339 ? 0.6297 1.1827 1.1206 0.0752  -0.0950 -0.0453 339 SER D O   
11498 C CB  . SER D 339 ? 0.6494 1.1670 1.1372 0.0848  -0.1109 -0.0474 339 SER D CB  
11499 O OG  . SER D 339 ? 0.6826 1.1821 1.1666 0.0879  -0.1160 -0.0479 339 SER D OG  
11500 N N   . ASN D 340 ? 0.6939 1.2195 1.1607 0.0727  -0.0989 -0.0337 340 ASN D N   
11501 C CA  . ASN D 340 ? 0.7382 1.2764 1.2060 0.0697  -0.0952 -0.0312 340 ASN D CA  
11502 C C   . ASN D 340 ? 0.7895 1.3235 1.2570 0.0720  -0.1021 -0.0291 340 ASN D C   
11503 O O   . ASN D 340 ? 0.7604 1.2867 1.2168 0.0696  -0.1023 -0.0234 340 ASN D O   
11504 C CB  . ASN D 340 ? 0.7142 1.2479 1.1691 0.0644  -0.0888 -0.0254 340 ASN D CB  
11505 C CG  . ASN D 340 ? 0.7582 1.3066 1.2154 0.0611  -0.0840 -0.0233 340 ASN D CG  
11506 O OD1 . ASN D 340 ? 0.8294 1.3952 1.2991 0.0616  -0.0824 -0.0270 340 ASN D OD1 
11507 N ND2 . ASN D 340 ? 0.7398 1.2808 1.1849 0.0578  -0.0814 -0.0172 340 ASN D ND2 
11508 N N   . GLY D 341 ? 0.7365 1.2759 1.2165 0.0766  -0.1080 -0.0339 341 GLY D N   
11509 C CA  . GLY D 341 ? 0.7798 1.3166 1.2614 0.0789  -0.1153 -0.0327 341 GLY D CA  
11510 C C   . GLY D 341 ? 0.6991 1.2153 1.1724 0.0828  -0.1243 -0.0310 341 GLY D C   
11511 O O   . GLY D 341 ? 0.6776 1.1833 1.1416 0.0829  -0.1293 -0.0267 341 GLY D O   
11512 N N   . GLY D 342 ? 0.6170 1.1268 1.0932 0.0863  -0.1267 -0.0344 342 GLY D N   
11513 C CA  . GLY D 342 ? 0.6412 1.1306 1.1092 0.0902  -0.1354 -0.0324 342 GLY D CA  
11514 C C   . GLY D 342 ? 0.6703 1.1631 1.1515 0.0963  -0.1446 -0.0367 342 GLY D C   
11515 O O   . GLY D 342 ? 0.6688 1.1709 1.1650 0.0999  -0.1453 -0.0432 342 GLY D O   
11516 N N   . VAL D 343 ? 0.6612 1.1468 1.1371 0.0976  -0.1518 -0.0335 343 VAL D N   
11517 C CA  . VAL D 343 ? 0.6509 1.1385 1.1387 0.1035  -0.1618 -0.0371 343 VAL D CA  
11518 C C   . VAL D 343 ? 0.6492 1.1156 1.1288 0.1082  -0.1698 -0.0357 343 VAL D C   
11519 O O   . VAL D 343 ? 0.7101 1.1577 1.1726 0.1082  -0.1749 -0.0298 343 VAL D O   
11520 C CB  . VAL D 343 ? 0.6659 1.1556 1.1521 0.1026  -0.1665 -0.0345 343 VAL D CB  
11521 C CG1 . VAL D 343 ? 0.6621 1.1581 1.1645 0.1084  -0.1763 -0.0392 343 VAL D CG1 
11522 C CG2 . VAL D 343 ? 0.7068 1.2138 1.1970 0.0968  -0.1575 -0.0341 343 VAL D CG2 
11523 N N   . VAL D 344 ? 0.6733 1.1421 1.1647 0.1124  -0.1709 -0.0412 344 VAL D N   
11524 C CA  . VAL D 344 ? 0.6927 1.1412 1.1769 0.1165  -0.1771 -0.0401 344 VAL D CA  
11525 C C   . VAL D 344 ? 0.7865 1.2331 1.2818 0.1240  -0.1890 -0.0433 344 VAL D C   
11526 O O   . VAL D 344 ? 0.7894 1.2545 1.3043 0.1268  -0.1905 -0.0495 344 VAL D O   
11527 C CB  . VAL D 344 ? 0.6910 1.1414 1.1804 0.1161  -0.1705 -0.0441 344 VAL D CB  
11528 C CG1 . VAL D 344 ? 0.6782 1.1055 1.1584 0.1195  -0.1761 -0.0420 344 VAL D CG1 
11529 C CG2 . VAL D 344 ? 0.7164 1.1723 1.1975 0.1087  -0.1589 -0.0416 344 VAL D CG2 
11530 N N   . LEU D 345 ? 0.7715 1.1955 1.2540 0.1274  -0.1977 -0.0390 345 LEU D N   
11531 C CA  . LEU D 345 ? 0.7472 1.1660 1.2382 0.1351  -0.2101 -0.0414 345 LEU D CA  
11532 C C   . LEU D 345 ? 0.7661 1.1869 1.2722 0.1404  -0.2110 -0.0479 345 LEU D C   
11533 O O   . LEU D 345 ? 0.7891 1.2073 1.2927 0.1380  -0.2036 -0.0488 345 LEU D O   
11534 C CB  . LEU D 345 ? 0.7610 1.1536 1.2308 0.1368  -0.2189 -0.0338 345 LEU D CB  
11535 C CG  . LEU D 345 ? 0.7611 1.1518 1.2230 0.1363  -0.2255 -0.0300 345 LEU D CG  
11536 C CD1 . LEU D 345 ? 0.8109 1.2109 1.2654 0.1285  -0.2158 -0.0273 345 LEU D CD1 
11537 C CD2 . LEU D 345 ? 0.8466 1.2104 1.2870 0.1387  -0.2347 -0.0229 345 LEU D CD2 
11538 N N   . PRO D 346 ? 0.8092 1.2349 1.3317 0.1476  -0.2202 -0.0530 346 PRO D N   
11539 C CA  . PRO D 346 ? 0.7724 1.1997 1.3101 0.1533  -0.2216 -0.0598 346 PRO D CA  
11540 C C   . PRO D 346 ? 0.7707 1.1716 1.2940 0.1555  -0.2256 -0.0556 346 PRO D C   
11541 O O   . PRO D 346 ? 0.8175 1.1978 1.3204 0.1544  -0.2303 -0.0475 346 PRO D O   
11542 C CB  . PRO D 346 ? 0.8158 1.2529 1.3727 0.1607  -0.2319 -0.0650 346 PRO D CB  
11543 C CG  . PRO D 346 ? 0.8413 1.2710 1.3864 0.1598  -0.2394 -0.0587 346 PRO D CG  
11544 C CD  . PRO D 346 ? 0.8613 1.2935 1.3913 0.1509  -0.2294 -0.0535 346 PRO D CD  
11545 N N   . HIS D 347 ? 0.7526 1.1544 1.2868 0.1584  -0.2234 -0.0615 347 HIS D N   
11546 C CA  . HIS D 347 ? 0.7310 1.1090 1.2552 0.1607  -0.2267 -0.0588 347 HIS D CA  
11547 C C   . HIS D 347 ? 0.7357 1.0975 1.2355 0.1531  -0.2201 -0.0503 347 HIS D C   
11548 O O   . HIS D 347 ? 0.7846 1.1232 1.2658 0.1533  -0.2256 -0.0424 347 HIS D O   
11549 C CB  . HIS D 347 ? 0.7120 1.0731 1.2349 0.1686  -0.2412 -0.0564 347 HIS D CB  
11550 C CG  . HIS D 347 ? 0.7001 1.0774 1.2478 0.1763  -0.2482 -0.0646 347 HIS D CG  
11551 N ND1 . HIS D 347 ? 0.7340 1.1221 1.3023 0.1808  -0.2464 -0.0739 347 HIS D ND1 
11552 C CD2 . HIS D 347 ? 0.7081 1.0929 1.2637 0.1803  -0.2570 -0.0652 347 HIS D CD2 
11553 C CE1 . HIS D 347 ? 0.7608 1.1628 1.3490 0.1873  -0.2533 -0.0798 347 HIS D CE1 
11554 N NE2 . HIS D 347 ? 0.7394 1.1399 1.3208 0.1870  -0.2600 -0.0746 347 HIS D NE2 
11555 N N   . LYS D 348 ? 0.7052 1.0801 1.2055 0.1464  -0.2079 -0.0520 348 LYS D N   
11556 C CA  . LYS D 348 ? 0.6640 1.0278 1.1441 0.1387  -0.2002 -0.0449 348 LYS D CA  
11557 C C   . LYS D 348 ? 0.6614 1.0334 1.1475 0.1348  -0.1898 -0.0497 348 LYS D C   
11558 O O   . LYS D 348 ? 0.7013 1.0957 1.2039 0.1348  -0.1846 -0.0572 348 LYS D O   
11559 C CB  . LYS D 348 ? 0.6602 1.0328 1.1313 0.1332  -0.1962 -0.0404 348 LYS D CB  
11560 C CG  . LYS D 348 ? 0.7063 1.0652 1.1549 0.1260  -0.1898 -0.0321 348 LYS D CG  
11561 C CD  . LYS D 348 ? 0.7749 1.1057 1.2049 0.1281  -0.1976 -0.0245 348 LYS D CD  
11562 C CE  . LYS D 348 ? 0.8971 1.2140 1.3045 0.1209  -0.1908 -0.0162 348 LYS D CE  
11563 N NZ  . LYS D 348 ? 0.9971 1.2866 1.3848 0.1227  -0.1982 -0.0083 348 LYS D NZ  
11564 N N   . GLU D 349 ? 0.6556 1.0093 1.1279 0.1314  -0.1866 -0.0453 349 GLU D N   
11565 C CA  . GLU D 349 ? 0.6477 1.0073 1.1236 0.1269  -0.1769 -0.0491 349 GLU D CA  
11566 C C   . GLU D 349 ? 0.6378 1.0013 1.1004 0.1183  -0.1674 -0.0437 349 GLU D C   
11567 O O   . GLU D 349 ? 0.6489 0.9949 1.0926 0.1150  -0.1675 -0.0351 349 GLU D O   
11568 C CB  . GLU D 349 ? 0.6890 1.0271 1.1603 0.1281  -0.1790 -0.0483 349 GLU D CB  
11569 C CG  . GLU D 349 ? 0.7131 1.0476 1.1992 0.1367  -0.1875 -0.0547 349 GLU D CG  
11570 C CD  . GLU D 349 ? 0.7389 1.0527 1.2212 0.1372  -0.1885 -0.0543 349 GLU D CD  
11571 O OE1 . GLU D 349 ? 0.7521 1.0487 1.2166 0.1317  -0.1854 -0.0466 349 GLU D OE1 
11572 O OE2 . GLU D 349 ? 0.8258 1.1405 1.3231 0.1430  -0.1921 -0.0619 349 GLU D OE2 
11573 N N   . ILE D 350 ? 0.6179 1.0040 1.0901 0.1149  -0.1592 -0.0486 350 ILE D N   
11574 C CA  . ILE D 350 ? 0.6069 0.9993 1.0690 0.1072  -0.1501 -0.0442 350 ILE D CA  
11575 C C   . ILE D 350 ? 0.6220 1.0117 1.0825 0.1026  -0.1426 -0.0457 350 ILE D C   
11576 O O   . ILE D 350 ? 0.6808 1.0849 1.1550 0.1030  -0.1387 -0.0536 350 ILE D O   
11577 C CB  . ILE D 350 ? 0.5862 1.0044 1.0589 0.1060  -0.1458 -0.0479 350 ILE D CB  
11578 C CG1 . ILE D 350 ? 0.5870 1.0081 1.0632 0.1105  -0.1538 -0.0470 350 ILE D CG1 
11579 C CG2 . ILE D 350 ? 0.6127 1.0364 1.0748 0.0983  -0.1368 -0.0430 350 ILE D CG2 
11580 C CD1 . ILE D 350 ? 0.6104 1.0129 1.0678 0.1094  -0.1585 -0.0379 350 ILE D CD1 
11581 N N   . LYS D 351 ? 0.6178 0.9891 1.0616 0.0982  -0.1404 -0.0384 351 LYS D N   
11582 C CA  . LYS D 351 ? 0.6185 0.9861 1.0598 0.0931  -0.1332 -0.0389 351 LYS D CA  
11583 C C   . LYS D 351 ? 0.6099 0.9817 1.0401 0.0855  -0.1246 -0.0335 351 LYS D C   
11584 O O   . LYS D 351 ? 0.6109 0.9791 1.0378 0.0804  -0.1184 -0.0329 351 LYS D O   
11585 C CB  . LYS D 351 ? 0.6819 1.0234 1.1147 0.0941  -0.1375 -0.0354 351 LYS D CB  
11586 C CG  . LYS D 351 ? 0.6924 1.0280 1.1366 0.1020  -0.1463 -0.0408 351 LYS D CG  
11587 C CD  . LYS D 351 ? 0.6982 1.0081 1.1347 0.1023  -0.1495 -0.0376 351 LYS D CD  
11588 C CE  . LYS D 351 ? 0.7104 1.0151 1.1597 0.1105  -0.1581 -0.0437 351 LYS D CE  
11589 N NZ  . LYS D 351 ? 0.7051 0.9846 1.1481 0.1108  -0.1612 -0.0409 351 LYS D NZ  
11590 N N   . SER D 352 ? 0.6021 0.9811 1.0270 0.0846  -0.1242 -0.0296 352 SER D N   
11591 C CA  . SER D 352 ? 0.6002 0.9840 1.0155 0.0780  -0.1163 -0.0247 352 SER D CA  
11592 C C   . SER D 352 ? 0.5828 0.9901 1.0069 0.0778  -0.1136 -0.0276 352 SER D C   
11593 O O   . SER D 352 ? 0.5901 1.0062 1.0240 0.0826  -0.1189 -0.0314 352 SER D O   
11594 C CB  . SER D 352 ? 0.7020 1.0666 1.0978 0.0764  -0.1182 -0.0153 352 SER D CB  
11595 O OG  . SER D 352 ? 0.8171 1.1590 1.2037 0.0765  -0.1207 -0.0118 352 SER D OG  
11596 N N   . ASN D 353 ? 0.6139 1.0311 1.0349 0.0721  -0.1053 -0.0258 353 ASN D N   
11597 C CA  . ASN D 353 ? 0.6301 1.0692 1.0587 0.0711  -0.1018 -0.0280 353 ASN D CA  
11598 C C   . ASN D 353 ? 0.5743 1.0112 0.9952 0.0718  -0.1050 -0.0227 353 ASN D C   
11599 O O   . ASN D 353 ? 0.5696 0.9912 0.9751 0.0698  -0.1053 -0.0159 353 ASN D O   
11600 C CB  . ASN D 353 ? 0.6991 1.1488 1.1267 0.0650  -0.0923 -0.0275 353 ASN D CB  
11601 C CG  . ASN D 353 ? 0.6557 1.1090 1.0913 0.0639  -0.0891 -0.0333 353 ASN D CG  
11602 O OD1 . ASN D 353 ? 0.6506 1.1060 1.0967 0.0680  -0.0929 -0.0396 353 ASN D OD1 
11603 N ND2 . ASN D 353 ? 0.6277 1.0820 1.0590 0.0584  -0.0822 -0.0314 353 ASN D ND2 
11604 N N   . ILE D 354 ? 0.6442 1.0966 1.0759 0.0746  -0.1074 -0.0262 354 ILE D N   
11605 C CA  . ILE D 354 ? 0.6001 1.0543 1.0269 0.0746  -0.1096 -0.0222 354 ILE D CA  
11606 C C   . ILE D 354 ? 0.7040 1.1753 1.1329 0.0699  -0.1016 -0.0217 354 ILE D C   
11607 O O   . ILE D 354 ? 0.6500 1.1388 1.0903 0.0708  -0.1011 -0.0249 354 ILE D O   
11608 C CB  . ILE D 354 ? 0.6470 1.1067 1.0848 0.0803  -0.1177 -0.0259 354 ILE D CB  
11609 C CG1 . ILE D 354 ? 0.6083 1.0529 1.0467 0.0855  -0.1257 -0.0276 354 ILE D CG1 
11610 C CG2 . ILE D 354 ? 0.6887 1.1456 1.1191 0.0802  -0.1215 -0.0213 354 ILE D CG2 
11611 C CD1 . ILE D 354 ? 0.5488 0.9987 0.9991 0.0915  -0.1342 -0.0315 354 ILE D CD1 
11612 N N   . LEU D 355 ? 0.6406 1.1073 1.0593 0.0650  -0.0950 -0.0175 355 LEU D N   
11613 C CA  . LEU D 355 ? 0.7418 1.2245 1.1630 0.0607  -0.0871 -0.0171 355 LEU D CA  
11614 C C   . LEU D 355 ? 0.7789 1.2679 1.1981 0.0600  -0.0874 -0.0139 355 LEU D C   
11615 O O   . LEU D 355 ? 0.7721 1.2757 1.1952 0.0571  -0.0816 -0.0138 355 LEU D O   
11616 C CB  . LEU D 355 ? 0.6945 1.1699 1.1057 0.0558  -0.0805 -0.0133 355 LEU D CB  
11617 C CG  . LEU D 355 ? 0.6970 1.1493 1.0924 0.0550  -0.0822 -0.0076 355 LEU D CG  
11618 C CD1 . LEU D 355 ? 0.8218 1.2673 1.2053 0.0543  -0.0831 -0.0017 355 LEU D CD1 
11619 C CD2 . LEU D 355 ? 0.6444 1.0921 1.0353 0.0505  -0.0755 -0.0062 355 LEU D CD2 
11620 N N   . LYS D 356 ? 0.8959 1.3738 1.3090 0.0626  -0.0941 -0.0113 356 LYS D N   
11621 C CA  . LYS D 356 ? 0.8962 1.3787 1.3075 0.0620  -0.0952 -0.0088 356 LYS D CA  
11622 C C   . LYS D 356 ? 0.9067 1.3854 1.3222 0.0669  -0.1048 -0.0105 356 LYS D C   
11623 O O   . LYS D 356 ? 0.9278 1.3951 1.3424 0.0705  -0.1106 -0.0118 356 LYS D O   
11624 C CB  . LYS D 356 ? 0.9189 1.3885 1.3130 0.0587  -0.0924 -0.0021 356 LYS D CB  
11625 C CG  . LYS D 356 ? 0.9161 1.3928 1.3083 0.0538  -0.0829 -0.0003 356 LYS D CG  
11626 C CD  . LYS D 356 ? 1.0450 1.5082 1.4204 0.0510  -0.0799 0.0060  356 LYS D CD  
11627 C CE  . LYS D 356 ? 1.1839 1.6466 1.5550 0.0514  -0.0828 0.0084  356 LYS D CE  
11628 N NZ  . LYS D 356 ? 1.1430 1.6252 1.5255 0.0500  -0.0794 0.0067  356 LYS D NZ  
11629 N N   . PRO D 357 ? 0.7947 1.2827 1.2154 0.0672  -0.1068 -0.0107 357 PRO D N   
11630 C CA  . PRO D 357 ? 0.7565 1.2425 1.1829 0.0717  -0.1163 -0.0127 357 PRO D CA  
11631 C C   . PRO D 357 ? 0.8090 1.2721 1.2203 0.0741  -0.1234 -0.0090 357 PRO D C   
11632 O O   . PRO D 357 ? 0.8138 1.2647 1.2091 0.0716  -0.1222 -0.0036 357 PRO D O   
11633 C CB  . PRO D 357 ? 0.7396 1.2368 1.1700 0.0699  -0.1157 -0.0118 357 PRO D CB  
11634 C CG  . PRO D 357 ? 0.7650 1.2772 1.1999 0.0656  -0.1059 -0.0119 357 PRO D CG  
11635 C CD  . PRO D 357 ? 0.8224 1.3247 1.2461 0.0634  -0.1006 -0.0094 357 PRO D CD  
11636 N N   . GLU D 358 ? 0.8049 1.2622 1.2214 0.0790  -0.1310 -0.0119 358 GLU D N   
11637 C CA  . GLU D 358 ? 0.7874 1.2221 1.1896 0.0817  -0.1381 -0.0084 358 GLU D CA  
11638 C C   . GLU D 358 ? 0.7895 1.2234 1.2027 0.0880  -0.1481 -0.0126 358 GLU D C   
11639 O O   . GLU D 358 ? 0.7446 1.1915 1.1747 0.0903  -0.1475 -0.0185 358 GLU D O   
11640 C CB  . GLU D 358 ? 0.8164 1.2382 1.2080 0.0796  -0.1332 -0.0058 358 GLU D CB  
11641 C CG  . GLU D 358 ? 0.7960 1.1937 1.1726 0.0822  -0.1399 -0.0018 358 GLU D CG  
11642 C CD  . GLU D 358 ? 0.8435 1.2300 1.2124 0.0799  -0.1346 0.0002  358 GLU D CD  
11643 O OE1 . GLU D 358 ? 0.8460 1.2426 1.2187 0.0757  -0.1254 -0.0008 358 GLU D OE1 
11644 O OE2 . GLU D 358 ? 0.8992 1.2667 1.2585 0.0823  -0.1398 0.0029  358 GLU D OE2 
11645 N N   . ILE D 359 ? 0.8104 1.2291 1.2137 0.0910  -0.1573 -0.0097 359 ILE D N   
11646 C CA  . ILE D 359 ? 0.7607 1.1762 1.1727 0.0975  -0.1681 -0.0129 359 ILE D CA  
11647 C C   . ILE D 359 ? 0.7628 1.1582 1.1648 0.1001  -0.1714 -0.0107 359 ILE D C   
11648 O O   . ILE D 359 ? 0.8429 1.2187 1.2246 0.0988  -0.1726 -0.0045 359 ILE D O   
11649 C CB  . ILE D 359 ? 0.7724 1.1836 1.1801 0.0995  -0.1772 -0.0112 359 ILE D CB  
11650 C CG1 . ILE D 359 ? 0.8117 1.2436 1.2319 0.0969  -0.1740 -0.0138 359 ILE D CG1 
11651 C CG2 . ILE D 359 ? 0.7891 1.1945 1.2042 0.1066  -0.1893 -0.0139 359 ILE D CG2 
11652 C CD1 . ILE D 359 ? 0.9160 1.3445 1.3323 0.0979  -0.1823 -0.0125 359 ILE D CD1 
11653 N N   . VAL D 360 ? 0.7445 1.1443 1.1605 0.1038  -0.1727 -0.0159 360 VAL D N   
11654 C CA  . VAL D 360 ? 0.7518 1.1335 1.1611 0.1063  -0.1756 -0.0145 360 VAL D CA  
11655 C C   . VAL D 360 ? 0.7663 1.1404 1.1812 0.1138  -0.1883 -0.0163 360 VAL D C   
11656 O O   . VAL D 360 ? 0.7289 1.1185 1.1626 0.1176  -0.1924 -0.0223 360 VAL D O   
11657 C CB  . VAL D 360 ? 0.7240 1.1147 1.1445 0.1050  -0.1679 -0.0192 360 VAL D CB  
11658 C CG1 . VAL D 360 ? 0.7692 1.1399 1.1823 0.1070  -0.1704 -0.0175 360 VAL D CG1 
11659 C CG2 . VAL D 360 ? 0.7396 1.1405 1.1566 0.0979  -0.1559 -0.0179 360 VAL D CG2 
11660 N N   . MET D 361 ? 0.7848 1.1351 1.1837 0.1159  -0.1944 -0.0111 361 MET D N   
11661 C CA  . MET D 361 ? 0.8025 1.1429 1.2050 0.1234  -0.2073 -0.0120 361 MET D CA  
11662 C C   . MET D 361 ? 0.8911 1.2169 1.2929 0.1262  -0.2088 -0.0121 361 MET D C   
11663 O O   . MET D 361 ? 0.9110 1.2414 1.3294 0.1321  -0.2141 -0.0179 361 MET D O   
11664 C CB  . MET D 361 ? 0.8746 1.1980 1.2581 0.1244  -0.2158 -0.0055 361 MET D CB  
11665 C CG  . MET D 361 ? 0.8703 1.2012 1.2461 0.1195  -0.2119 -0.0031 361 MET D CG  
11666 S SD  . MET D 361 ? 0.8140 1.1245 1.1679 0.1218  -0.2234 0.0034  361 MET D SD  
11667 C CE  . MET D 361 ? 0.9632 1.2768 1.3350 0.1310  -0.2386 -0.0018 361 MET D CE  
11668 O OXT . MET D 361 ? 0.9699 1.2788 1.3547 0.1228  -0.2047 -0.0065 361 MET D OXT 
11669 N N   . MET E 1   ? 2.5765 2.4289 1.7428 -0.0091 0.3964  0.0805  1   MET E N   
11670 C CA  . MET E 1   ? 2.6275 2.4795 1.8107 -0.0118 0.3809  0.0900  1   MET E CA  
11671 C C   . MET E 1   ? 2.5936 2.4488 1.7928 -0.0054 0.3569  0.0839  1   MET E C   
11672 O O   . MET E 1   ? 2.5534 2.4220 1.7731 -0.0003 0.3554  0.0726  1   MET E O   
11673 C CB  . MET E 1   ? 2.6324 2.5051 1.8572 -0.0177 0.3926  0.0948  1   MET E CB  
11674 C CG  . MET E 1   ? 2.6198 2.4906 1.8590 -0.0216 0.3797  0.1057  1   MET E CG  
11675 S SD  . MET E 1   ? 2.6531 2.5452 1.9348 -0.0296 0.3957  0.1120  1   MET E SD  
11676 C CE  . MET E 1   ? 2.6550 2.5358 1.9035 -0.0364 0.4218  0.1183  1   MET E CE  
11677 N N   . LYS E 2   ? 2.5016 2.3442 1.6915 -0.0056 0.3382  0.0914  2   LYS E N   
11678 C CA  . LYS E 2   ? 2.4179 2.2610 1.6188 0.0001  0.3143  0.0867  2   LYS E CA  
11679 C C   . LYS E 2   ? 2.4520 2.3086 1.6924 -0.0022 0.3047  0.0923  2   LYS E C   
11680 O O   . LYS E 2   ? 2.5335 2.3971 1.7900 -0.0082 0.3154  0.1000  2   LYS E O   
11681 C CB  . LYS E 2   ? 2.3439 2.1613 1.5012 0.0027  0.2987  0.0897  2   LYS E CB  
11682 C CG  . LYS E 2   ? 2.3426 2.1456 1.4588 0.0055  0.3065  0.0834  2   LYS E CG  
11683 C CD  . LYS E 2   ? 2.2659 2.0786 1.3938 0.0120  0.3026  0.0686  2   LYS E CD  
11684 C CE  . LYS E 2   ? 2.2293 2.0260 1.3141 0.0152  0.3082  0.0619  2   LYS E CE  
11685 N NZ  . LYS E 2   ? 2.0667 1.8700 1.1608 0.0219  0.3014  0.0474  2   LYS E NZ  
11686 N N   . ALA E 3   ? 2.4325 2.2926 1.6883 0.0026  0.2842  0.0880  3   ALA E N   
11687 C CA  . ALA E 3   ? 2.3903 2.2630 1.6826 0.0013  0.2729  0.0920  3   ALA E CA  
11688 C C   . ALA E 3   ? 2.3764 2.2449 1.6699 0.0070  0.2486  0.0881  3   ALA E C   
11689 O O   . ALA E 3   ? 2.4257 2.2894 1.7052 0.0122  0.2423  0.0793  3   ALA E O   
11690 C CB  . ALA E 3   ? 2.3094 2.2089 1.6471 0.0003  0.2836  0.0872  3   ALA E CB  
11691 N N   . LEU E 4   ? 2.4037 2.2743 1.7150 0.0058  0.2351  0.0945  4   LEU E N   
11692 C CA  . LEU E 4   ? 2.4551 2.3233 1.7716 0.0106  0.2118  0.0918  4   LEU E CA  
11693 C C   . LEU E 4   ? 2.4328 2.3197 1.7933 0.0095  0.2050  0.0935  4   LEU E C   
11694 O O   . LEU E 4   ? 2.4656 2.3574 1.8400 0.0043  0.2123  0.1013  4   LEU E O   
11695 C CB  . LEU E 4   ? 2.4567 2.3006 1.7368 0.0110  0.1986  0.0994  4   LEU E CB  
11696 C CG  . LEU E 4   ? 2.3913 2.2313 1.6758 0.0154  0.1738  0.0984  4   LEU E CG  
11697 C CD1 . LEU E 4   ? 2.5031 2.3448 1.7847 0.0214  0.1646  0.0865  4   LEU E CD1 
11698 C CD2 . LEU E 4   ? 2.3344 2.1509 1.5843 0.0149  0.1634  0.1077  4   LEU E CD2 
11699 N N   . ILE E 5   ? 2.4048 2.3023 1.7873 0.0141  0.1913  0.0860  5   ILE E N   
11700 C CA  . ILE E 5   ? 2.3363 2.2524 1.7605 0.0136  0.1842  0.0865  5   ILE E CA  
11701 C C   . ILE E 5   ? 2.2502 2.1603 1.6743 0.0173  0.1610  0.0866  5   ILE E C   
11702 O O   . ILE E 5   ? 2.2426 2.1477 1.6559 0.0221  0.1502  0.0796  5   ILE E O   
11703 C CB  . ILE E 5   ? 2.3200 2.2583 1.7771 0.0154  0.1912  0.0774  5   ILE E CB  
11704 C CG1 . ILE E 5   ? 2.4029 2.3486 1.8631 0.0117  0.2144  0.0775  5   ILE E CG1 
11705 C CG2 . ILE E 5   ? 2.2239 2.1803 1.7218 0.0153  0.1821  0.0778  5   ILE E CG2 
11706 C CD1 . ILE E 5   ? 2.5725 2.5399 2.0652 0.0136  0.2221  0.0689  5   ILE E CD1 
11707 N N   . LEU E 6   ? 2.0756 1.9863 1.5124 0.0150  0.1532  0.0943  6   LEU E N   
11708 C CA  . LEU E 6   ? 1.9597 1.8672 1.4015 0.0183  0.1316  0.0947  6   LEU E CA  
11709 C C   . LEU E 6   ? 1.9066 1.8363 1.3894 0.0203  0.1253  0.0882  6   LEU E C   
11710 O O   . LEU E 6   ? 1.9151 1.8609 1.4284 0.0174  0.1316  0.0904  6   LEU E O   
11711 C CB  . LEU E 6   ? 1.8863 1.7846 1.3241 0.0153  0.1263  0.1055  6   LEU E CB  
11712 C CG  . LEU E 6   ? 1.9886 1.8627 1.3848 0.0133  0.1295  0.1136  6   LEU E CG  
11713 C CD1 . LEU E 6   ? 1.9542 1.8223 1.3543 0.0100  0.1253  0.1242  6   LEU E CD1 
11714 C CD2 . LEU E 6   ? 2.0931 1.9496 1.4565 0.0182  0.1156  0.1106  6   LEU E CD2 
11715 N N   . VAL E 7   ? 1.8814 1.8120 1.3648 0.0252  0.1129  0.0804  7   VAL E N   
11716 C CA  . VAL E 7   ? 1.8074 1.7576 1.3275 0.0274  0.1058  0.0744  7   VAL E CA  
11717 C C   . VAL E 7   ? 1.7732 1.7226 1.3031 0.0291  0.0864  0.0770  7   VAL E C   
11718 O O   . VAL E 7   ? 1.7591 1.7229 1.3197 0.0277  0.0838  0.0791  7   VAL E O   
11719 C CB  . VAL E 7   ? 1.8525 1.8057 1.3710 0.0314  0.1047  0.0638  7   VAL E CB  
11720 C CG1 . VAL E 7   ? 1.7969 1.7701 1.3535 0.0333  0.0976  0.0583  7   VAL E CG1 
11721 C CG2 . VAL E 7   ? 1.9990 1.9528 1.5075 0.0302  0.1242  0.0607  7   VAL E CG2 
11722 N N   . GLY E 8   ? 1.8497 1.7825 1.3536 0.0321  0.0726  0.0767  8   GLY E N   
11723 C CA  . GLY E 8   ? 1.9667 1.8982 1.4786 0.0344  0.0532  0.0784  8   GLY E CA  
11724 C C   . GLY E 8   ? 2.0887 2.0258 1.6100 0.0388  0.0401  0.0693  8   GLY E C   
11725 O O   . GLY E 8   ? 2.0606 1.9883 1.5600 0.0412  0.0386  0.0637  8   GLY E O   
11726 N N   . GLY E 9   ? 2.5345 2.4869 2.0883 0.0396  0.0307  0.0678  9   GLY E N   
11727 C CA  . GLY E 9   ? 2.5279 2.4875 2.0950 0.0432  0.0184  0.0597  9   GLY E CA  
11728 C C   . GLY E 9   ? 2.5079 2.4856 2.1010 0.0430  0.0278  0.0531  9   GLY E C   
11729 O O   . GLY E 9   ? 2.5087 2.4894 2.1000 0.0411  0.0443  0.0525  9   GLY E O   
11730 N N   . PHE E 10  ? 2.1441 2.1342 1.7623 0.0450  0.0172  0.0481  10  PHE E N   
11731 C CA  . PHE E 10  ? 2.0421 2.0489 1.6857 0.0453  0.0236  0.0417  10  PHE E CA  
11732 C C   . PHE E 10  ? 1.9512 1.9773 1.6279 0.0426  0.0317  0.0450  10  PHE E C   
11733 O O   . PHE E 10  ? 1.9333 1.9731 1.6297 0.0424  0.0403  0.0410  10  PHE E O   
11734 C CB  . PHE E 10  ? 2.0421 2.0529 1.6970 0.0484  0.0084  0.0349  10  PHE E CB  
11735 C CG  . PHE E 10  ? 2.0248 2.0410 1.6856 0.0499  0.0136  0.0265  10  PHE E CG  
11736 C CD1 . PHE E 10  ? 2.0630 2.0647 1.6955 0.0517  0.0153  0.0214  10  PHE E CD1 
11737 C CD2 . PHE E 10  ? 1.9765 2.0117 1.6708 0.0496  0.0166  0.0237  10  PHE E CD2 
11738 C CE1 . PHE E 10  ? 2.0510 2.0570 1.6895 0.0533  0.0200  0.0134  10  PHE E CE1 
11739 C CE2 . PHE E 10  ? 1.9604 1.9999 1.6606 0.0512  0.0211  0.0163  10  PHE E CE2 
11740 C CZ  . PHE E 10  ? 1.9889 2.0137 1.6617 0.0530  0.0228  0.0109  10  PHE E CZ  
11741 N N   . GLY E 11  ? 1.8586 1.8856 1.5415 0.0406  0.0289  0.0521  11  GLY E N   
11742 C CA  . GLY E 11  ? 1.7585 1.8038 1.4733 0.0382  0.0345  0.0549  11  GLY E CA  
11743 C C   . GLY E 11  ? 1.6804 1.7378 1.4211 0.0397  0.0207  0.0532  11  GLY E C   
11744 O O   . GLY E 11  ? 1.6408 1.7156 1.4093 0.0396  0.0229  0.0499  11  GLY E O   
11745 N N   . THR E 12  ? 1.6710 1.7191 1.4027 0.0412  0.0062  0.0554  12  THR E N   
11746 C CA  . THR E 12  ? 1.6206 1.6795 1.3758 0.0428  -0.0075 0.0536  12  THR E CA  
11747 C C   . THR E 12  ? 1.6129 1.6893 1.3986 0.0405  -0.0033 0.0567  12  THR E C   
11748 O O   . THR E 12  ? 1.6015 1.6934 1.4136 0.0412  -0.0084 0.0536  12  THR E O   
11749 C CB  . THR E 12  ? 1.6236 1.6688 1.3627 0.0449  -0.0232 0.0558  12  THR E CB  
11750 O OG1 . THR E 12  ? 1.6875 1.7236 1.4151 0.0431  -0.0202 0.0636  12  THR E OG1 
11751 C CG2 . THR E 12  ? 1.6086 1.6372 1.3181 0.0474  -0.0287 0.0520  12  THR E CG2 
11752 N N   . ARG E 13  ? 1.7632 1.8372 1.5453 0.0376  0.0060  0.0628  13  ARG E N   
11753 C CA  . ARG E 13  ? 1.7417 1.8308 1.5504 0.0351  0.0105  0.0659  13  ARG E CA  
11754 C C   . ARG E 13  ? 1.7299 1.8351 1.5581 0.0332  0.0241  0.0635  13  ARG E C   
11755 O O   . ARG E 13  ? 1.7071 1.8252 1.5565 0.0308  0.0295  0.0659  13  ARG E O   
11756 C CB  . ARG E 13  ? 1.7766 1.8553 1.5729 0.0325  0.0144  0.0735  13  ARG E CB  
11757 C CG  . ARG E 13  ? 1.8363 1.8972 1.6002 0.0314  0.0232  0.0760  13  ARG E CG  
11758 C CD  . ARG E 13  ? 1.8926 1.9376 1.6379 0.0299  0.0212  0.0837  13  ARG E CD  
11759 N NE  . ARG E 13  ? 1.9416 1.9787 1.6820 0.0331  0.0037  0.0844  13  ARG E NE  
11760 C CZ  . ARG E 13  ? 1.9947 2.0349 1.7492 0.0330  -0.0037 0.0879  13  ARG E CZ  
11761 N NH1 . ARG E 13  ? 1.9926 2.0433 1.7664 0.0296  0.0048  0.0909  13  ARG E NH1 
11762 N NH2 . ARG E 13  ? 2.0200 2.0529 1.7696 0.0363  -0.0197 0.0881  13  ARG E NH2 
11763 N N   . LEU E 14  ? 1.6356 1.7404 1.4573 0.0345  0.0295  0.0585  14  LEU E N   
11764 C CA  . LEU E 14  ? 1.5893 1.7089 1.4291 0.0334  0.0419  0.0558  14  LEU E CA  
11765 C C   . LEU E 14  ? 1.5317 1.6623 1.3888 0.0360  0.0363  0.0493  14  LEU E C   
11766 O O   . LEU E 14  ? 1.4964 1.6371 1.3655 0.0359  0.0455  0.0463  14  LEU E O   
11767 C CB  . LEU E 14  ? 1.6351 1.7456 1.4541 0.0324  0.0557  0.0555  14  LEU E CB  
11768 C CG  . LEU E 14  ? 1.6354 1.7380 1.4407 0.0289  0.0664  0.0618  14  LEU E CG  
11769 C CD1 . LEU E 14  ? 1.6410 1.7230 1.4172 0.0291  0.0587  0.0660  14  LEU E CD1 
11770 C CD2 . LEU E 14  ? 1.7067 1.8090 1.5038 0.0278  0.0828  0.0601  14  LEU E CD2 
11771 N N   . ARG E 15  ? 1.4595 1.5883 1.3184 0.0382  0.0214  0.0473  15  ARG E N   
11772 C CA  . ARG E 15  ? 1.3988 1.5379 1.2750 0.0402  0.0156  0.0417  15  ARG E CA  
11773 C C   . ARG E 15  ? 1.3628 1.5231 1.2718 0.0388  0.0195  0.0423  15  ARG E C   
11774 O O   . ARG E 15  ? 1.3761 1.5427 1.2953 0.0367  0.0219  0.0468  15  ARG E O   
11775 C CB  . ARG E 15  ? 1.4026 1.5360 1.2753 0.0423  -0.0014 0.0400  15  ARG E CB  
11776 C CG  . ARG E 15  ? 1.4348 1.5479 1.2757 0.0442  -0.0069 0.0382  15  ARG E CG  
11777 C CD  . ARG E 15  ? 1.4560 1.5662 1.2976 0.0465  -0.0239 0.0352  15  ARG E CD  
11778 N NE  . ARG E 15  ? 1.4453 1.5367 1.2570 0.0485  -0.0298 0.0326  15  ARG E NE  
11779 C CZ  . ARG E 15  ? 1.4866 1.5633 1.2767 0.0493  -0.0376 0.0358  15  ARG E CZ  
11780 N NH1 . ARG E 15  ? 1.5338 1.6118 1.3292 0.0484  -0.0404 0.0417  15  ARG E NH1 
11781 N NH2 . ARG E 15  ? 1.4546 1.5147 1.2172 0.0511  -0.0429 0.0330  15  ARG E NH2 
11782 N N   . PRO E 16  ? 1.3163 1.4875 1.2420 0.0400  0.0201  0.0378  16  PRO E N   
11783 C CA  . PRO E 16  ? 1.3193 1.4849 1.2375 0.0424  0.0169  0.0318  16  PRO E CA  
11784 C C   . PRO E 16  ? 1.3191 1.4790 1.2241 0.0428  0.0295  0.0293  16  PRO E C   
11785 O O   . PRO E 16  ? 1.3130 1.4694 1.2141 0.0449  0.0284  0.0239  16  PRO E O   
11786 C CB  . PRO E 16  ? 1.2590 1.4416 1.2061 0.0429  0.0131  0.0294  16  PRO E CB  
11787 C CG  . PRO E 16  ? 1.1524 1.3500 1.1194 0.0407  0.0220  0.0332  16  PRO E CG  
11788 C CD  . PRO E 16  ? 1.2304 1.4217 1.1866 0.0389  0.0232  0.0385  16  PRO E CD  
11789 N N   . LEU E 17  ? 1.3127 1.4717 1.2116 0.0409  0.0415  0.0330  17  LEU E N   
11790 C CA  . LEU E 17  ? 1.3105 1.4651 1.1980 0.0413  0.0545  0.0306  17  LEU E CA  
11791 C C   . LEU E 17  ? 1.3618 1.4961 1.2163 0.0428  0.0526  0.0282  17  LEU E C   
11792 O O   . LEU E 17  ? 1.3572 1.4866 1.2016 0.0443  0.0597  0.0237  17  LEU E O   
11793 C CB  . LEU E 17  ? 1.3052 1.4655 1.1968 0.0384  0.0681  0.0352  17  LEU E CB  
11794 C CG  . LEU E 17  ? 1.2064 1.3872 1.1300 0.0369  0.0709  0.0373  17  LEU E CG  
11795 C CD1 . LEU E 17  ? 1.2751 1.4602 1.2011 0.0337  0.0841  0.0416  17  LEU E CD1 
11796 C CD2 . LEU E 17  ? 1.1742 1.3671 1.1172 0.0390  0.0725  0.0325  17  LEU E CD2 
11797 N N   . THR E 18  ? 1.3808 1.5028 1.2179 0.0426  0.0429  0.0310  18  THR E N   
11798 C CA  . THR E 18  ? 1.4654 1.5675 1.2696 0.0440  0.0398  0.0292  18  THR E CA  
11799 C C   . THR E 18  ? 1.5055 1.6017 1.3055 0.0467  0.0243  0.0243  18  THR E C   
11800 O O   . THR E 18  ? 1.5651 1.6445 1.3379 0.0480  0.0182  0.0231  18  THR E O   
11801 C CB  . THR E 18  ? 1.5024 1.5923 1.2862 0.0422  0.0395  0.0358  18  THR E CB  
11802 O OG1 . THR E 18  ? 1.5051 1.6008 1.3036 0.0415  0.0289  0.0398  18  THR E OG1 
11803 C CG2 . THR E 18  ? 1.4679 1.5601 1.2498 0.0393  0.0563  0.0399  18  THR E CG2 
11804 N N   . LEU E 19  ? 1.4624 1.5721 1.2884 0.0474  0.0178  0.0214  19  LEU E N   
11805 C CA  . LEU E 19  ? 1.4822 1.5871 1.3060 0.0496  0.0040  0.0162  19  LEU E CA  
11806 C C   . LEU E 19  ? 1.5389 1.6350 1.3483 0.0516  0.0077  0.0093  19  LEU E C   
11807 O O   . LEU E 19  ? 1.4876 1.5728 1.2826 0.0533  -0.0028 0.0048  19  LEU E O   
11808 C CB  . LEU E 19  ? 1.4628 1.5847 1.3189 0.0494  -0.0029 0.0154  19  LEU E CB  
11809 C CG  . LEU E 19  ? 1.3517 1.4780 1.2181 0.0487  -0.0148 0.0193  19  LEU E CG  
11810 C CD1 . LEU E 19  ? 1.2130 1.3569 1.1111 0.0485  -0.0198 0.0179  19  LEU E CD1 
11811 C CD2 . LEU E 19  ? 1.3653 1.4760 1.2097 0.0503  -0.0282 0.0179  19  LEU E CD2 
11812 N N   . SER E 20  ? 1.7654 1.8664 1.5787 0.0515  0.0222  0.0079  20  SER E N   
11813 C CA  . SER E 20  ? 1.7876 1.8808 1.5882 0.0536  0.0273  0.0010  20  SER E CA  
11814 C C   . SER E 20  ? 1.7995 1.8813 1.5738 0.0534  0.0401  0.0019  20  SER E C   
11815 O O   . SER E 20  ? 1.8238 1.8890 1.5695 0.0547  0.0374  -0.0012 20  SER E O   
11816 C CB  . SER E 20  ? 1.8526 1.9607 1.6804 0.0543  0.0335  -0.0023 20  SER E CB  
11817 O OG  . SER E 20  ? 1.7660 1.8841 1.6170 0.0543  0.0221  -0.0030 20  SER E OG  
11818 N N   . PHE E 21  ? 1.6071 1.6978 1.3907 0.0516  0.0539  0.0060  21  PHE E N   
11819 C CA  . PHE E 21  ? 1.5655 1.6460 1.3247 0.0509  0.0667  0.0074  21  PHE E CA  
11820 C C   . PHE E 21  ? 1.5395 1.6122 1.2836 0.0484  0.0643  0.0150  21  PHE E C   
11821 O O   . PHE E 21  ? 1.5091 1.5914 1.2713 0.0465  0.0601  0.0203  21  PHE E O   
11822 C CB  . PHE E 21  ? 1.5280 1.6215 1.3039 0.0500  0.0834  0.0078  21  PHE E CB  
11823 C CG  . PHE E 21  ? 1.5782 1.6773 1.3658 0.0528  0.0877  0.0004  21  PHE E CG  
11824 C CD1 . PHE E 21  ? 1.6310 1.7181 1.4027 0.0557  0.0815  -0.0068 21  PHE E CD1 
11825 C CD2 . PHE E 21  ? 1.5949 1.7109 1.4095 0.0527  0.0974  0.0005  21  PHE E CD2 
11826 C CE1 . PHE E 21  ? 1.6626 1.7540 1.4453 0.0584  0.0853  -0.0137 21  PHE E CE1 
11827 C CE2 . PHE E 21  ? 1.6348 1.7554 1.4604 0.0556  0.1011  -0.0060 21  PHE E CE2 
11828 C CZ  . PHE E 21  ? 1.6493 1.7573 1.4590 0.0585  0.0951  -0.0131 21  PHE E CZ  
11829 N N   . PRO E 22  ? 1.5532 1.6085 1.2643 0.0484  0.0671  0.0158  22  PRO E N   
11830 C CA  . PRO E 22  ? 1.5658 1.6120 1.2610 0.0461  0.0644  0.0234  22  PRO E CA  
11831 C C   . PRO E 22  ? 1.4793 1.5352 1.1873 0.0426  0.0774  0.0300  22  PRO E C   
11832 O O   . PRO E 22  ? 1.4362 1.5056 1.1636 0.0419  0.0891  0.0285  22  PRO E O   
11833 C CB  . PRO E 22  ? 1.6617 1.6869 1.3173 0.0471  0.0660  0.0220  22  PRO E CB  
11834 C CG  . PRO E 22  ? 1.6764 1.7015 1.3284 0.0493  0.0745  0.0139  22  PRO E CG  
11835 C CD  . PRO E 22  ? 1.6153 1.6594 1.3028 0.0502  0.0755  0.0100  22  PRO E CD  
11836 N N   . LYS E 23  ? 1.5043 1.5529 1.2015 0.0403  0.0746  0.0373  23  LYS E N   
11837 C CA  . LYS E 23  ? 1.4976 1.5544 1.2071 0.0364  0.0850  0.0441  23  LYS E CA  
11838 C C   . LYS E 23  ? 1.3946 1.4540 1.1006 0.0347  0.1043  0.0436  23  LYS E C   
11839 O O   . LYS E 23  ? 1.3618 1.4376 1.0937 0.0328  0.1133  0.0446  23  LYS E O   
11840 C CB  . LYS E 23  ? 1.5762 1.6196 1.2673 0.0345  0.0794  0.0518  23  LYS E CB  
11841 C CG  . LYS E 23  ? 1.5017 1.5511 1.2028 0.0301  0.0902  0.0589  23  LYS E CG  
11842 C CD  . LYS E 23  ? 1.5255 1.5622 1.2120 0.0285  0.0826  0.0665  23  LYS E CD  
11843 C CE  . LYS E 23  ? 1.5973 1.6110 1.2436 0.0295  0.0806  0.0678  23  LYS E CE  
11844 N NZ  . LYS E 23  ? 1.5791 1.5794 1.2104 0.0281  0.0734  0.0759  23  LYS E NZ  
11845 N N   . PRO E 24  ? 1.4325 1.4773 1.1085 0.0353  0.1116  0.0419  24  PRO E N   
11846 C CA  . PRO E 24  ? 1.4832 1.5317 1.1576 0.0334  0.1309  0.0416  24  PRO E CA  
11847 C C   . PRO E 24  ? 1.5089 1.5707 1.2026 0.0359  0.1378  0.0339  24  PRO E C   
11848 O O   . PRO E 24  ? 1.5746 1.6430 1.2731 0.0346  0.1538  0.0333  24  PRO E O   
11849 C CB  . PRO E 24  ? 1.6291 1.6563 1.2627 0.0336  0.1348  0.0420  24  PRO E CB  
11850 C CG  . PRO E 24  ? 1.5071 1.5229 1.1256 0.0374  0.1183  0.0377  24  PRO E CG  
11851 C CD  . PRO E 24  ? 1.4757 1.4999 1.1171 0.0375  0.1031  0.0403  24  PRO E CD  
11852 N N   . LEU E 25  ? 1.3903 1.4565 1.0961 0.0394  0.1263  0.0281  25  LEU E N   
11853 C CA  . LEU E 25  ? 1.3798 1.4574 1.1038 0.0420  0.1317  0.0209  25  LEU E CA  
11854 C C   . LEU E 25  ? 1.3542 1.4532 1.1171 0.0414  0.1309  0.0220  25  LEU E C   
11855 O O   . LEU E 25  ? 1.3510 1.4605 1.1325 0.0438  0.1333  0.0166  25  LEU E O   
11856 C CB  . LEU E 25  ? 1.4388 1.5073 1.1516 0.0461  0.1207  0.0134  25  LEU E CB  
11857 C CG  . LEU E 25  ? 1.4843 1.5332 1.1596 0.0476  0.1241  0.0098  25  LEU E CG  
11858 C CD1 . LEU E 25  ? 1.6205 1.6632 1.2899 0.0518  0.1151  0.0008  25  LEU E CD1 
11859 C CD2 . LEU E 25  ? 1.5655 1.6150 1.2330 0.0466  0.1439  0.0094  25  LEU E CD2 
11860 N N   . VAL E 26  ? 1.3292 1.4345 1.1044 0.0383  0.1275  0.0289  26  VAL E N   
11861 C CA  . VAL E 26  ? 1.3002 1.4259 1.1112 0.0373  0.1272  0.0303  26  VAL E CA  
11862 C C   . VAL E 26  ? 1.3538 1.4909 1.1776 0.0354  0.1445  0.0312  26  VAL E C   
11863 O O   . VAL E 26  ? 1.3979 1.5300 1.2092 0.0323  0.1543  0.0355  26  VAL E O   
11864 C CB  . VAL E 26  ? 1.2817 1.4095 1.1004 0.0348  0.1174  0.0368  26  VAL E CB  
11865 C CG1 . VAL E 26  ? 1.3478 1.4968 1.2021 0.0335  0.1184  0.0383  26  VAL E CG1 
11866 C CG2 . VAL E 26  ? 1.2659 1.3839 1.0747 0.0370  0.0999  0.0355  26  VAL E CG2 
11867 N N   . ASP E 27  ? 1.3471 1.4997 1.1961 0.0373  0.1481  0.0271  27  ASP E N   
11868 C CA  . ASP E 27  ? 1.3656 1.5310 1.2301 0.0360  0.1637  0.0274  27  ASP E CA  
11869 C C   . ASP E 27  ? 1.3409 1.5171 1.2224 0.0316  0.1658  0.0342  27  ASP E C   
11870 O O   . ASP E 27  ? 1.3016 1.4892 1.2053 0.0314  0.1570  0.0358  27  ASP E O   
11871 C CB  . ASP E 27  ? 1.3680 1.5474 1.2568 0.0395  0.1650  0.0217  27  ASP E CB  
11872 C CG  . ASP E 27  ? 1.4274 1.5967 1.3004 0.0437  0.1668  0.0144  27  ASP E CG  
11873 O OD1 . ASP E 27  ? 1.4505 1.6019 1.2939 0.0441  0.1637  0.0133  27  ASP E OD1 
11874 O OD2 . ASP E 27  ? 1.4525 1.6315 1.3426 0.0466  0.1709  0.0096  27  ASP E OD2 
11875 N N   . PHE E 28  ? 1.4276 1.6002 1.2986 0.0280  0.1775  0.0381  28  PHE E N   
11876 C CA  . PHE E 28  ? 1.4585 1.6414 1.3461 0.0235  0.1816  0.0441  28  PHE E CA  
11877 C C   . PHE E 28  ? 1.4974 1.6932 1.3998 0.0221  0.1982  0.0431  28  PHE E C   
11878 O O   . PHE E 28  ? 1.5094 1.6976 1.3944 0.0212  0.2104  0.0426  28  PHE E O   
11879 C CB  . PHE E 28  ? 1.4969 1.6646 1.3614 0.0197  0.1808  0.0505  28  PHE E CB  
11880 C CG  . PHE E 28  ? 1.4836 1.6603 1.3632 0.0145  0.1867  0.0565  28  PHE E CG  
11881 C CD1 . PHE E 28  ? 1.5145 1.6884 1.3856 0.0106  0.2016  0.0595  28  PHE E CD1 
11882 C CD2 . PHE E 28  ? 1.5111 1.6993 1.4141 0.0135  0.1776  0.0588  28  PHE E CD2 
11883 C CE1 . PHE E 28  ? 1.5022 1.6844 1.3882 0.0056  0.2069  0.0648  28  PHE E CE1 
11884 C CE2 . PHE E 28  ? 1.5570 1.7532 1.4742 0.0088  0.1827  0.0637  28  PHE E CE2 
11885 C CZ  . PHE E 28  ? 1.5221 1.7152 1.4311 0.0047  0.1972  0.0667  28  PHE E CZ  
11886 N N   . ALA E 29  ? 1.6399 1.8554 1.5743 0.0219  0.1986  0.0428  29  ALA E N   
11887 C CA  . ALA E 29  ? 1.6114 1.8418 1.5645 0.0213  0.2129  0.0412  29  ALA E CA  
11888 C C   . ALA E 29  ? 1.6239 1.8508 1.5677 0.0255  0.2210  0.0347  29  ALA E C   
11889 O O   . ALA E 29  ? 1.6345 1.8573 1.5663 0.0243  0.2347  0.0342  29  ALA E O   
11890 C CB  . ALA E 29  ? 1.5997 1.8305 1.5503 0.0156  0.2243  0.0465  29  ALA E CB  
11891 N N   . ASN E 30  ? 1.3868 1.6143 1.3354 0.0304  0.2120  0.0298  30  ASN E N   
11892 C CA  . ASN E 30  ? 1.3466 1.5710 1.2893 0.0351  0.2170  0.0227  30  ASN E CA  
11893 C C   . ASN E 30  ? 1.3855 1.5881 1.2921 0.0361  0.2169  0.0207  30  ASN E C   
11894 O O   . ASN E 30  ? 1.3547 1.5494 1.2519 0.0403  0.2106  0.0153  30  ASN E O   
11895 C CB  . ASN E 30  ? 1.3727 1.6098 1.3301 0.0353  0.2335  0.0206  30  ASN E CB  
11896 C CG  . ASN E 30  ? 1.3746 1.6333 1.3681 0.0364  0.2326  0.0203  30  ASN E CG  
11897 O OD1 . ASN E 30  ? 1.3645 1.6297 1.3709 0.0410  0.2323  0.0152  30  ASN E OD1 
11898 N ND2 . ASN E 30  ? 1.3798 1.6493 1.3896 0.0321  0.2317  0.0258  30  ASN E ND2 
11899 N N   . LYS E 31  ? 1.4414 1.6341 1.3278 0.0322  0.2234  0.0250  31  LYS E N   
11900 C CA  . LYS E 31  ? 1.4815 1.6536 1.3319 0.0329  0.2251  0.0234  31  LYS E CA  
11901 C C   . LYS E 31  ? 1.4867 1.6440 1.3179 0.0319  0.2101  0.0271  31  LYS E C   
11902 O O   . LYS E 31  ? 1.4662 1.6276 1.3074 0.0289  0.2032  0.0330  31  LYS E O   
11903 C CB  . LYS E 31  ? 1.5111 1.6796 1.3479 0.0291  0.2418  0.0263  31  LYS E CB  
11904 C CG  . LYS E 31  ? 1.4596 1.6398 1.3097 0.0309  0.2576  0.0213  31  LYS E CG  
11905 C CD  . LYS E 31  ? 1.4342 1.6197 1.2864 0.0257  0.2736  0.0258  31  LYS E CD  
11906 C CE  . LYS E 31  ? 1.4218 1.6248 1.2980 0.0274  0.2873  0.0213  31  LYS E CE  
11907 N NZ  . LYS E 31  ? 1.4592 1.6752 1.3528 0.0220  0.2988  0.0263  31  LYS E NZ  
11908 N N   . PRO E 32  ? 1.5183 1.6586 1.3225 0.0347  0.2043  0.0234  32  PRO E N   
11909 C CA  . PRO E 32  ? 1.5515 1.6767 1.3352 0.0340  0.1902  0.0269  32  PRO E CA  
11910 C C   . PRO E 32  ? 1.7234 1.8408 1.4920 0.0290  0.1949  0.0350  32  PRO E C   
11911 O O   . PRO E 32  ? 1.8304 1.9485 1.5940 0.0262  0.2102  0.0369  32  PRO E O   
11912 C CB  . PRO E 32  ? 1.5907 1.6990 1.3457 0.0377  0.1873  0.0208  32  PRO E CB  
11913 C CG  . PRO E 32  ? 1.5490 1.6671 1.3193 0.0415  0.1941  0.0130  32  PRO E CG  
11914 C CD  . PRO E 32  ? 1.5772 1.7119 1.3700 0.0392  0.2091  0.0153  32  PRO E CD  
11915 N N   . MET E 33  ? 1.6905 1.8003 1.4524 0.0277  0.1814  0.0397  33  MET E N   
11916 C CA  . MET E 33  ? 1.7744 1.8765 1.5242 0.0230  0.1839  0.0480  33  MET E CA  
11917 C C   . MET E 33  ? 2.0648 2.1487 1.7786 0.0219  0.1932  0.0493  33  MET E C   
11918 O O   . MET E 33  ? 2.1999 2.2796 1.9052 0.0174  0.2020  0.0557  33  MET E O   
11919 C CB  . MET E 33  ? 1.6481 1.7442 1.3963 0.0229  0.1665  0.0520  33  MET E CB  
11920 C CG  . MET E 33  ? 1.6466 1.7578 1.4245 0.0201  0.1634  0.0566  33  MET E CG  
11921 S SD  . MET E 33  ? 1.6518 1.7670 1.4334 0.0138  0.1804  0.0633  33  MET E SD  
11922 C CE  . MET E 33  ? 1.7257 1.8145 1.4659 0.0117  0.1791  0.0696  33  MET E CE  
11923 N N   . ILE E 34  ? 2.4127 2.4852 2.1045 0.0258  0.1913  0.0433  34  ILE E N   
11924 C CA  . ILE E 34  ? 2.4739 2.5279 2.1287 0.0249  0.1993  0.0443  34  ILE E CA  
11925 C C   . ILE E 34  ? 2.5741 2.6344 2.2302 0.0231  0.2203  0.0429  34  ILE E C   
11926 O O   . ILE E 34  ? 2.8031 2.8518 2.4342 0.0203  0.2306  0.0467  34  ILE E O   
11927 C CB  . ILE E 34  ? 2.5065 2.5460 2.1367 0.0297  0.1895  0.0378  34  ILE E CB  
11928 C CG1 . ILE E 34  ? 2.7013 2.7189 2.2892 0.0287  0.1936  0.0403  34  ILE E CG1 
11929 C CG2 . ILE E 34  ? 2.4807 2.5290 2.1225 0.0338  0.1951  0.0282  34  ILE E CG2 
11930 C CD1 . ILE E 34  ? 2.7897 2.7952 2.3624 0.0256  0.1852  0.0496  34  ILE E CD1 
11931 N N   . LEU E 35  ? 2.3525 2.4313 2.0377 0.0248  0.2272  0.0378  35  LEU E N   
11932 C CA  . LEU E 35  ? 2.4253 2.5113 2.1138 0.0237  0.2469  0.0355  35  LEU E CA  
11933 C C   . LEU E 35  ? 2.5037 2.5985 2.2053 0.0177  0.2584  0.0429  35  LEU E C   
11934 O O   . LEU E 35  ? 2.5541 2.6536 2.2558 0.0159  0.2758  0.0421  35  LEU E O   
11935 C CB  . LEU E 35  ? 2.3530 2.4556 2.0690 0.0279  0.2497  0.0274  35  LEU E CB  
11936 C CG  . LEU E 35  ? 2.3722 2.4671 2.0772 0.0339  0.2417  0.0187  35  LEU E CG  
11937 C CD1 . LEU E 35  ? 2.3491 2.4602 2.0809 0.0376  0.2481  0.0114  35  LEU E CD1 
11938 C CD2 . LEU E 35  ? 2.5288 2.6034 2.1933 0.0347  0.2470  0.0165  35  LEU E CD2 
11939 N N   . HIS E 36  ? 2.5153 2.6128 2.2287 0.0144  0.2495  0.0497  36  HIS E N   
11940 C CA  . HIS E 36  ? 2.5430 2.6496 2.2713 0.0085  0.2598  0.0563  36  HIS E CA  
11941 C C   . HIS E 36  ? 2.8967 2.9872 2.5946 0.0040  0.2702  0.0624  36  HIS E C   
11942 O O   . HIS E 36  ? 2.8195 2.9170 2.5259 -0.0008 0.2847  0.0660  36  HIS E O   
11943 C CB  . HIS E 36  ? 2.2999 2.4138 2.0498 0.0067  0.2468  0.0612  36  HIS E CB  
11944 C CG  . HIS E 36  ? 1.9862 2.1191 1.7699 0.0100  0.2396  0.0562  36  HIS E CG  
11945 N ND1 . HIS E 36  ? 1.8578 1.9885 1.6415 0.0152  0.2253  0.0513  36  HIS E ND1 
11946 C CD2 . HIS E 36  ? 1.7728 1.9269 1.5910 0.0089  0.2446  0.0555  36  HIS E CD2 
11947 C CE1 . HIS E 36  ? 1.7006 1.8500 1.5168 0.0169  0.2221  0.0482  36  HIS E CE1 
11948 N NE2 . HIS E 36  ? 1.6871 1.8508 1.5242 0.0134  0.2335  0.0506  36  HIS E NE2 
11949 N N   . GLN E 37  ? 3.7532 3.8222 3.4157 0.0052  0.2631  0.0638  37  GLN E N   
11950 C CA  . GLN E 37  ? 3.7822 3.8343 3.4130 0.0011  0.2726  0.0700  37  GLN E CA  
11951 C C   . GLN E 37  ? 3.8056 3.8445 3.4042 0.0038  0.2808  0.0651  37  GLN E C   
11952 O O   . GLN E 37  ? 3.8242 3.8509 3.3969 0.0002  0.2920  0.0697  37  GLN E O   
11953 C CB  . GLN E 37  ? 3.8102 3.8457 3.4226 -0.0006 0.2586  0.0779  37  GLN E CB  
11954 C CG  . GLN E 37  ? 3.8381 3.8571 3.4248 0.0044  0.2426  0.0750  37  GLN E CG  
11955 C CD  . GLN E 37  ? 3.8207 3.8511 3.4311 0.0094  0.2277  0.0685  37  GLN E CD  
11956 O OE1 . GLN E 37  ? 3.7925 3.8353 3.4313 0.0085  0.2202  0.0706  37  GLN E OE1 
11957 N NE2 . GLN E 37  ? 3.8353 3.8608 3.4335 0.0146  0.2233  0.0607  37  GLN E NE2 
11958 N N   . ILE E 38  ? 3.1122 3.1530 2.7112 0.0098  0.2757  0.0559  38  ILE E N   
11959 C CA  . ILE E 38  ? 2.9400 2.9698 2.5104 0.0125  0.2848  0.0501  38  ILE E CA  
11960 C C   . ILE E 38  ? 2.7788 2.8211 2.3607 0.0107  0.3066  0.0475  38  ILE E C   
11961 O O   . ILE E 38  ? 2.6964 2.7286 2.2523 0.0090  0.3204  0.0482  38  ILE E O   
11962 C CB  . ILE E 38  ? 2.7785 2.8060 2.3467 0.0194  0.2725  0.0407  38  ILE E CB  
11963 C CG1 . ILE E 38  ? 2.7707 2.7808 2.3162 0.0210  0.2530  0.0432  38  ILE E CG1 
11964 C CG2 . ILE E 38  ? 2.5738 2.5959 2.1223 0.0225  0.2847  0.0327  38  ILE E CG2 
11965 C CD1 . ILE E 38  ? 2.6143 2.6202 2.1544 0.0272  0.2408  0.0340  38  ILE E CD1 
11966 N N   . GLU E 39  ? 2.7005 2.7652 2.3218 0.0112  0.3102  0.0446  39  GLU E N   
11967 C CA  . GLU E 39  ? 2.6151 2.6936 2.2513 0.0092  0.3305  0.0426  39  GLU E CA  
11968 C C   . GLU E 39  ? 2.5969 2.6736 2.2283 0.0016  0.3424  0.0519  39  GLU E C   
11969 O O   . GLU E 39  ? 2.4978 2.5772 2.1244 -0.0008 0.3612  0.0515  39  GLU E O   
11970 C CB  . GLU E 39  ? 2.6072 2.7100 2.2875 0.0114  0.3298  0.0381  39  GLU E CB  
11971 C CG  . GLU E 39  ? 2.6175 2.7359 2.3153 0.0113  0.3494  0.0337  39  GLU E CG  
11972 C CD  . GLU E 39  ? 2.6358 2.7654 2.3507 0.0043  0.3616  0.0407  39  GLU E CD  
11973 O OE1 . GLU E 39  ? 2.6377 2.7659 2.3576 0.0000  0.3534  0.0485  39  GLU E OE1 
11974 O OE2 . GLU E 39  ? 2.6379 2.7778 2.3620 0.0031  0.3794  0.0382  39  GLU E OE2 
11975 N N   . ALA E 40  ? 2.6751 2.7473 2.3079 -0.0022 0.3321  0.0603  40  ALA E N   
11976 C CA  . ALA E 40  ? 2.6435 2.7107 2.2684 -0.0096 0.3421  0.0697  40  ALA E CA  
11977 C C   . ALA E 40  ? 2.5743 2.6183 2.1539 -0.0110 0.3484  0.0729  40  ALA E C   
11978 O O   . ALA E 40  ? 2.4745 2.5154 2.0444 -0.0167 0.3641  0.0783  40  ALA E O   
11979 C CB  . ALA E 40  ? 2.6947 2.7614 2.3317 -0.0128 0.3282  0.0775  40  ALA E CB  
11980 N N   . LEU E 41  ? 2.7064 2.7339 2.2580 -0.0061 0.3364  0.0698  41  LEU E N   
11981 C CA  . LEU E 41  ? 2.6994 2.7050 2.2063 -0.0066 0.3423  0.0715  41  LEU E CA  
11982 C C   . LEU E 41  ? 2.6724 2.6818 2.1717 -0.0049 0.3607  0.0640  41  LEU E C   
11983 O O   . LEU E 41  ? 2.6819 2.6768 2.1478 -0.0070 0.3718  0.0663  41  LEU E O   
11984 C CB  . LEU E 41  ? 2.7379 2.7254 2.2182 -0.0016 0.3230  0.0697  41  LEU E CB  
11985 C CG  . LEU E 41  ? 2.7479 2.7256 2.2246 -0.0035 0.3056  0.0782  41  LEU E CG  
11986 C CD1 . LEU E 41  ? 2.7463 2.7099 2.2025 0.0023  0.2860  0.0746  41  LEU E CD1 
11987 C CD2 . LEU E 41  ? 2.7628 2.7256 2.2150 -0.0099 0.3134  0.0892  41  LEU E CD2 
11988 N N   . LYS E 42  ? 2.4236 2.4521 1.9528 -0.0010 0.3642  0.0552  42  LYS E N   
11989 C CA  . LYS E 42  ? 2.2879 2.3229 1.8157 0.0005  0.3830  0.0481  42  LYS E CA  
11990 C C   . LYS E 42  ? 2.2478 2.2954 1.7920 -0.0060 0.4029  0.0528  42  LYS E C   
11991 O O   . LYS E 42  ? 2.2059 2.2549 1.7406 -0.0064 0.4212  0.0493  42  LYS E O   
11992 C CB  . LYS E 42  ? 2.2480 2.2988 1.8033 0.0072  0.3791  0.0371  42  LYS E CB  
11993 C CG  . LYS E 42  ? 2.1374 2.1783 1.6685 0.0133  0.3814  0.0272  42  LYS E CG  
11994 C CD  . LYS E 42  ? 2.1199 2.1587 1.6331 0.0115  0.4041  0.0255  42  LYS E CD  
11995 C CE  . LYS E 42  ? 2.0989 2.1259 1.5846 0.0176  0.4059  0.0154  42  LYS E CE  
11996 N NZ  . LYS E 42  ? 2.1233 2.1258 1.5689 0.0187  0.3916  0.0174  42  LYS E NZ  
11997 N N   . ALA E 43  ? 2.2554 2.3126 1.8244 -0.0110 0.3999  0.0603  43  ALA E N   
11998 C CA  . ALA E 43  ? 2.1749 2.2429 1.7588 -0.0180 0.4180  0.0654  43  ALA E CA  
11999 C C   . ALA E 43  ? 2.2195 2.2683 1.7660 -0.0237 0.4289  0.0733  43  ALA E C   
12000 O O   . ALA E 43  ? 2.2074 2.2623 1.7569 -0.0287 0.4485  0.0754  43  ALA E O   
12001 C CB  . ALA E 43  ? 2.1102 2.1920 1.7291 -0.0220 0.4105  0.0712  43  ALA E CB  
12002 N N   . VAL E 44  ? 2.2594 2.2851 1.7708 -0.0231 0.4165  0.0778  44  VAL E N   
12003 C CA  . VAL E 44  ? 2.2905 2.2954 1.7619 -0.0278 0.4254  0.0854  44  VAL E CA  
12004 C C   . VAL E 44  ? 2.2908 2.2798 1.7230 -0.0230 0.4285  0.0794  44  VAL E C   
12005 O O   . VAL E 44  ? 2.3078 2.2764 1.7010 -0.0258 0.4329  0.0852  44  VAL E O   
12006 C CB  . VAL E 44  ? 2.2816 2.2705 1.7392 -0.0312 0.4106  0.0962  44  VAL E CB  
12007 C CG1 . VAL E 44  ? 2.2572 2.2599 1.7487 -0.0376 0.4126  0.1031  44  VAL E CG1 
12008 C CG2 . VAL E 44  ? 2.3109 2.2930 1.7650 -0.0247 0.3864  0.0928  44  VAL E CG2 
12009 N N   . GLY E 45  ? 2.3161 2.3133 1.7572 -0.0159 0.4261  0.0678  45  GLY E N   
12010 C CA  . GLY E 45  ? 2.3022 2.2861 1.7087 -0.0112 0.4304  0.0606  45  GLY E CA  
12011 C C   . GLY E 45  ? 2.2926 2.2519 1.6605 -0.0084 0.4130  0.0626  45  GLY E C   
12012 O O   . GLY E 45  ? 2.2667 2.2072 1.5934 -0.0091 0.4191  0.0642  45  GLY E O   
12013 N N   . VAL E 46  ? 2.3210 2.2805 1.7018 -0.0052 0.3913  0.0623  46  VAL E N   
12014 C CA  . VAL E 46  ? 2.3402 2.2785 1.6887 -0.0017 0.3726  0.0629  46  VAL E CA  
12015 C C   . VAL E 46  ? 2.3311 2.2703 1.6773 0.0062  0.3659  0.0500  46  VAL E C   
12016 O O   . VAL E 46  ? 2.3160 2.2727 1.6971 0.0097  0.3612  0.0432  46  VAL E O   
12017 C CB  . VAL E 46  ? 2.3767 2.3143 1.7401 -0.0028 0.3527  0.0700  46  VAL E CB  
12018 C CG1 . VAL E 46  ? 2.3479 2.2661 1.6823 0.0017  0.3323  0.0689  46  VAL E CG1 
12019 C CG2 . VAL E 46  ? 2.4134 2.3468 1.7747 -0.0106 0.3589  0.0828  46  VAL E CG2 
12020 N N   . ASP E 47  ? 2.3525 2.2723 1.6570 0.0089  0.3653  0.0467  47  ASP E N   
12021 C CA  . ASP E 47  ? 2.3957 2.3141 1.6937 0.0161  0.3606  0.0340  47  ASP E CA  
12022 C C   . ASP E 47  ? 2.4106 2.3209 1.7056 0.0207  0.3352  0.0316  47  ASP E C   
12023 O O   . ASP E 47  ? 2.4322 2.3523 1.7487 0.0257  0.3272  0.0224  47  ASP E O   
12024 C CB  . ASP E 47  ? 2.4593 2.3614 1.7138 0.0170  0.3732  0.0304  47  ASP E CB  
12025 C CG  . ASP E 47  ? 2.4647 2.3550 1.6922 0.0102  0.3858  0.0417  47  ASP E CG  
12026 O OD1 . ASP E 47  ? 2.4354 2.3372 1.6861 0.0044  0.3951  0.0495  47  ASP E OD1 
12027 O OD2 . ASP E 47  ? 2.4550 2.3241 1.6377 0.0105  0.3862  0.0429  47  ASP E OD2 
12028 N N   . GLU E 48  ? 2.4262 2.3187 1.6954 0.0189  0.3222  0.0397  48  GLU E N   
12029 C CA  . GLU E 48  ? 2.4354 2.3186 1.6979 0.0231  0.2982  0.0377  48  GLU E CA  
12030 C C   . GLU E 48  ? 2.3836 2.2709 1.6673 0.0202  0.2845  0.0471  48  GLU E C   
12031 O O   . GLU E 48  ? 2.3880 2.2724 1.6684 0.0146  0.2905  0.0578  48  GLU E O   
12032 C CB  . GLU E 48  ? 2.4010 2.2584 1.6125 0.0247  0.2922  0.0379  48  GLU E CB  
12033 N N   . VAL E 49  ? 2.4856 2.3796 1.7913 0.0240  0.2661  0.0430  49  VAL E N   
12034 C CA  . VAL E 49  ? 2.4948 2.3937 1.8227 0.0221  0.2516  0.0505  49  VAL E CA  
12035 C C   . VAL E 49  ? 2.6240 2.5129 1.9422 0.0267  0.2282  0.0473  49  VAL E C   
12036 O O   . VAL E 49  ? 2.5593 2.4512 1.8821 0.0316  0.2220  0.0371  49  VAL E O   
12037 C CB  . VAL E 49  ? 2.3804 2.3049 1.7580 0.0212  0.2552  0.0490  49  VAL E CB  
12038 C CG1 . VAL E 49  ? 2.4470 2.3757 1.8455 0.0196  0.2397  0.0561  49  VAL E CG1 
12039 C CG2 . VAL E 49  ? 2.3254 2.2607 1.7142 0.0165  0.2781  0.0520  49  VAL E CG2 
12040 N N   . VAL E 50  ? 3.0499 2.9269 2.3554 0.0252  0.2151  0.0560  50  VAL E N   
12041 C CA  . VAL E 50  ? 3.0626 2.9298 2.3589 0.0292  0.1921  0.0541  50  VAL E CA  
12042 C C   . VAL E 50  ? 3.0436 2.9233 2.3752 0.0284  0.1791  0.0584  50  VAL E C   
12043 O O   . VAL E 50  ? 3.0304 2.9172 2.3787 0.0239  0.1853  0.0665  50  VAL E O   
12044 C CB  . VAL E 50  ? 3.0937 2.9354 2.3438 0.0289  0.1857  0.0601  50  VAL E CB  
12045 C CG1 . VAL E 50  ? 3.1032 2.9351 2.3429 0.0336  0.1620  0.0565  50  VAL E CG1 
12046 C CG2 . VAL E 50  ? 3.1145 2.9445 2.3293 0.0287  0.2016  0.0571  50  VAL E CG2 
12047 N N   . LEU E 51  ? 2.8716 2.7543 2.2150 0.0327  0.1612  0.0525  51  LEU E N   
12048 C CA  . LEU E 51  ? 2.8534 2.7484 2.2303 0.0326  0.1478  0.0550  51  LEU E CA  
12049 C C   . LEU E 51  ? 2.8653 2.7453 2.2242 0.0345  0.1271  0.0587  51  LEU E C   
12050 O O   . LEU E 51  ? 2.8803 2.7500 2.2200 0.0385  0.1157  0.0526  51  LEU E O   
12051 C CB  . LEU E 51  ? 2.8312 2.7444 2.2414 0.0358  0.1442  0.0454  51  LEU E CB  
12052 C CG  . LEU E 51  ? 2.8168 2.7465 2.2489 0.0348  0.1630  0.0411  51  LEU E CG  
12053 C CD1 . LEU E 51  ? 2.7955 2.7408 2.2583 0.0384  0.1568  0.0321  51  LEU E CD1 
12054 C CD2 . LEU E 51  ? 2.7949 2.7360 2.2480 0.0296  0.1743  0.0495  51  LEU E CD2 
12055 N N   . ALA E 52  ? 2.4590 2.3378 1.8244 0.0317  0.1222  0.0684  52  ALA E N   
12056 C CA  . ALA E 52  ? 2.3335 2.1991 1.6851 0.0335  0.1024  0.0727  52  ALA E CA  
12057 C C   . ALA E 52  ? 2.1450 2.0252 1.5316 0.0359  0.0866  0.0693  52  ALA E C   
12058 O O   . ALA E 52  ? 2.0720 1.9588 1.4794 0.0343  0.0808  0.0752  52  ALA E O   
12059 C CB  . ALA E 52  ? 2.3639 2.2189 1.7025 0.0295  0.1052  0.0850  52  ALA E CB  
12060 N N   . ILE E 53  ? 2.1244 2.0096 1.5171 0.0398  0.0800  0.0592  53  ILE E N   
12061 C CA  . ILE E 53  ? 2.0588 1.9578 1.4833 0.0422  0.0655  0.0548  53  ILE E CA  
12062 C C   . ILE E 53  ? 2.0432 1.9292 1.4521 0.0451  0.0442  0.0557  53  ILE E C   
12063 O O   . ILE E 53  ? 2.1453 2.0115 1.5175 0.0459  0.0407  0.0584  53  ILE E O   
12064 C CB  . ILE E 53  ? 2.0706 1.9806 1.5099 0.0447  0.0683  0.0436  53  ILE E CB  
12065 C CG1 . ILE E 53  ? 2.1040 1.9975 1.5097 0.0481  0.0623  0.0368  53  ILE E CG1 
12066 C CG2 . ILE E 53  ? 2.1470 2.0690 1.5997 0.0423  0.0895  0.0425  53  ILE E CG2 
12067 C CD1 . ILE E 53  ? 2.1550 2.0566 1.5723 0.0509  0.0641  0.0255  53  ILE E CD1 
12068 N N   . ASN E 54  ? 2.0320 1.9291 1.4685 0.0469  0.0299  0.0535  54  ASN E N   
12069 C CA  . ASN E 54  ? 2.0272 1.9147 1.4535 0.0501  0.0089  0.0530  54  ASN E CA  
12070 C C   . ASN E 54  ? 2.0261 1.9202 1.4648 0.0535  -0.0023 0.0426  54  ASN E C   
12071 O O   . ASN E 54  ? 2.0472 1.9307 1.4705 0.0564  -0.0186 0.0401  54  ASN E O   
12072 C CB  . ASN E 54  ? 2.0193 1.9119 1.4653 0.0492  -0.0009 0.0604  54  ASN E CB  
12073 C CG  . ASN E 54  ? 2.0343 1.9146 1.4657 0.0525  -0.0218 0.0613  54  ASN E CG  
12074 O OD1 . ASN E 54  ? 2.1185 1.9797 1.5169 0.0529  -0.0252 0.0666  54  ASN E OD1 
12075 N ND2 . ASN E 54  ? 1.9697 1.8609 1.4257 0.0548  -0.0361 0.0564  54  ASN E ND2 
12076 N N   . TYR E 55  ? 2.0018 1.9129 1.4679 0.0531  0.0057  0.0366  55  TYR E N   
12077 C CA  . TYR E 55  ? 2.0260 1.9439 1.5057 0.0559  -0.0031 0.0268  55  TYR E CA  
12078 C C   . TYR E 55  ? 2.0767 1.9850 1.5322 0.0574  0.0042  0.0190  55  TYR E C   
12079 O O   . TYR E 55  ? 2.1093 2.0060 1.5370 0.0565  0.0159  0.0213  55  TYR E O   
12080 C CB  . TYR E 55  ? 2.0078 1.9487 1.5304 0.0548  0.0015  0.0249  55  TYR E CB  
12081 C CG  . TYR E 55  ? 2.0412 1.9909 1.5723 0.0524  0.0224  0.0255  55  TYR E CG  
12082 C CD1 . TYR E 55  ? 2.0365 1.9904 1.5736 0.0490  0.0329  0.0340  55  TYR E CD1 
12083 C CD2 . TYR E 55  ? 2.0714 2.0251 1.6050 0.0535  0.0314  0.0175  55  TYR E CD2 
12084 C CE1 . TYR E 55  ? 2.0410 2.0036 1.5869 0.0467  0.0518  0.0344  55  TYR E CE1 
12085 C CE2 . TYR E 55  ? 2.0521 2.0144 1.5944 0.0517  0.0503  0.0179  55  TYR E CE2 
12086 C CZ  . TYR E 55  ? 2.0219 1.9890 1.5705 0.0482  0.0604  0.0263  55  TYR E CZ  
12087 O OH  . TYR E 55  ? 1.9452 1.9216 1.5037 0.0463  0.0790  0.0265  55  TYR E OH  
12088 N N   . GLN E 56  ? 2.1167 2.0296 1.5827 0.0598  -0.0028 0.0096  56  GLN E N   
12089 C CA  . GLN E 56  ? 2.1905 2.0948 1.6358 0.0616  0.0032  0.0010  56  GLN E CA  
12090 C C   . GLN E 56  ? 2.2460 2.1626 1.7080 0.0604  0.0227  -0.0015 56  GLN E C   
12091 O O   . GLN E 56  ? 2.1858 2.1205 1.6836 0.0598  0.0246  -0.0023 56  GLN E O   
12092 C CB  . GLN E 56  ? 2.2116 2.1148 1.6611 0.0646  -0.0125 -0.0084 56  GLN E CB  
12093 C CG  . GLN E 56  ? 2.2075 2.1304 1.6990 0.0646  -0.0160 -0.0123 56  GLN E CG  
12094 C CD  . GLN E 56  ? 2.1095 2.0444 1.6280 0.0631  -0.0246 -0.0053 56  GLN E CD  
12095 O OE1 . GLN E 56  ? 2.1121 2.0391 1.6182 0.0629  -0.0336 0.0009  56  GLN E OE1 
12096 N NE2 . GLN E 56  ? 1.9976 1.9515 1.5532 0.0622  -0.0218 -0.0063 56  GLN E NE2 
12097 N N   . PRO E 57  ? 2.4983 2.4059 1.9355 0.0602  0.0375  -0.0027 57  PRO E N   
12098 C CA  . PRO E 57  ? 2.4881 2.4076 1.9412 0.0593  0.0564  -0.0054 57  PRO E CA  
12099 C C   . PRO E 57  ? 2.4875 2.4124 1.9528 0.0622  0.0565  -0.0166 57  PRO E C   
12100 O O   . PRO E 57  ? 2.4778 2.4116 1.9551 0.0622  0.0719  -0.0196 57  PRO E O   
12101 C CB  . PRO E 57  ? 2.5079 2.4138 1.9264 0.0582  0.0710  -0.0028 57  PRO E CB  
12102 C CG  . PRO E 57  ? 2.5645 2.4496 1.9456 0.0602  0.0585  -0.0046 57  PRO E CG  
12103 C CD  . PRO E 57  ? 2.5290 2.4151 1.9217 0.0607  0.0379  -0.0013 57  PRO E CD  
12104 N N   . GLU E 58  ? 2.4152 2.3349 1.8785 0.0646  0.0399  -0.0228 58  GLU E N   
12105 C CA  . GLU E 58  ? 2.4006 2.3229 1.8726 0.0673  0.0393  -0.0338 58  GLU E CA  
12106 C C   . GLU E 58  ? 2.3685 2.3118 1.8821 0.0668  0.0457  -0.0348 58  GLU E C   
12107 O O   . GLU E 58  ? 2.3694 2.3160 1.8915 0.0688  0.0510  -0.0429 58  GLU E O   
12108 C CB  . GLU E 58  ? 2.4554 2.3699 1.9219 0.0693  0.0187  -0.0393 58  GLU E CB  
12109 C CG  . GLU E 58  ? 2.5460 2.4404 1.9733 0.0700  0.0087  -0.0379 58  GLU E CG  
12110 C CD  . GLU E 58  ? 2.6283 2.5214 2.0620 0.0705  -0.0132 -0.0373 58  GLU E CD  
12111 O OE1 . GLU E 58  ? 2.5834 2.4914 2.0517 0.0701  -0.0198 -0.0380 58  GLU E OE1 
12112 O OE2 . GLU E 58  ? 2.7069 2.5843 2.1109 0.0714  -0.0239 -0.0360 58  GLU E OE2 
12113 N N   . VAL E 59  ? 2.1095 2.0664 1.6488 0.0644  0.0451  -0.0268 59  VAL E N   
12114 C CA  . VAL E 59  ? 2.0383 2.0154 1.6170 0.0639  0.0499  -0.0271 59  VAL E CA  
12115 C C   . VAL E 59  ? 2.0232 2.0089 1.6095 0.0627  0.0704  -0.0249 59  VAL E C   
12116 O O   . VAL E 59  ? 2.0112 2.0120 1.6264 0.0631  0.0767  -0.0272 59  VAL E O   
12117 C CB  . VAL E 59  ? 1.9812 1.9700 1.5855 0.0619  0.0393  -0.0202 59  VAL E CB  
12118 C CG1 . VAL E 59  ? 1.9482 1.9308 1.5496 0.0632  0.0191  -0.0232 59  VAL E CG1 
12119 C CG2 . VAL E 59  ? 1.9735 1.9605 1.5688 0.0591  0.0439  -0.0102 59  VAL E CG2 
12120 N N   . MET E 60  ? 1.9772 1.9540 1.5388 0.0612  0.0808  -0.0204 60  MET E N   
12121 C CA  . MET E 60  ? 1.9648 1.9503 1.5338 0.0595  0.1004  -0.0176 60  MET E CA  
12122 C C   . MET E 60  ? 1.9646 1.9385 1.5050 0.0609  0.1139  -0.0226 60  MET E C   
12123 O O   . MET E 60  ? 1.9510 1.9299 1.4923 0.0592  0.1309  -0.0198 60  MET E O   
12124 C CB  . MET E 60  ? 1.9615 1.9497 1.5318 0.0556  0.1034  -0.0065 60  MET E CB  
12125 C CG  . MET E 60  ? 2.0385 2.0073 1.5714 0.0546  0.0992  -0.0020 60  MET E CG  
12126 S SD  . MET E 60  ? 2.0707 2.0420 1.6081 0.0501  0.0995  0.0111  60  MET E SD  
12127 C CE  . MET E 60  ? 2.2184 2.1639 1.7061 0.0498  0.0971  0.0148  60  MET E CE  
12128 N N   . LEU E 61  ? 1.9815 1.9403 1.4967 0.0638  0.1070  -0.0301 61  LEU E N   
12129 C CA  . LEU E 61  ? 1.9942 1.9417 1.4811 0.0653  0.1199  -0.0356 61  LEU E CA  
12130 C C   . LEU E 61  ? 2.0427 2.0029 1.5508 0.0669  0.1350  -0.0414 61  LEU E C   
12131 O O   . LEU E 61  ? 2.1426 2.1011 1.6383 0.0668  0.1520  -0.0423 61  LEU E O   
12132 C CB  . LEU E 61  ? 1.9841 1.9136 1.4419 0.0683  0.1079  -0.0434 61  LEU E CB  
12133 C CG  . LEU E 61  ? 2.0684 1.9812 1.4946 0.0672  0.0960  -0.0382 61  LEU E CG  
12134 C CD1 . LEU E 61  ? 2.0876 1.9837 1.4865 0.0704  0.0844  -0.0471 61  LEU E CD1 
12135 C CD2 . LEU E 61  ? 2.0716 1.9768 1.4726 0.0646  0.1097  -0.0307 61  LEU E CD2 
12136 N N   . ASN E 62  ? 1.9518 1.9248 1.4923 0.0686  0.1292  -0.0455 62  ASN E N   
12137 C CA  . ASN E 62  ? 1.9524 1.9376 1.5150 0.0706  0.1423  -0.0509 62  ASN E CA  
12138 C C   . ASN E 62  ? 1.9814 1.9821 1.5641 0.0678  0.1572  -0.0437 62  ASN E C   
12139 O O   . ASN E 62  ? 1.9967 2.0036 1.5855 0.0690  0.1731  -0.0471 62  ASN E O   
12140 C CB  . ASN E 62  ? 1.9610 1.9554 1.5529 0.0728  0.1314  -0.0560 62  ASN E CB  
12141 C CG  . ASN E 62  ? 1.9451 1.9251 1.5193 0.0761  0.1212  -0.0659 62  ASN E CG  
12142 O OD1 . ASN E 62  ? 1.9638 1.9305 1.5097 0.0780  0.1277  -0.0720 62  ASN E OD1 
12143 N ND2 . ASN E 62  ? 1.9001 1.8826 1.4908 0.0766  0.1052  -0.0678 62  ASN E ND2 
12144 N N   . PHE E 63  ? 2.0067 2.0139 1.6005 0.0642  0.1524  -0.0340 63  PHE E N   
12145 C CA  . PHE E 63  ? 2.0658 2.0877 1.6790 0.0611  0.1657  -0.0272 63  PHE E CA  
12146 C C   . PHE E 63  ? 2.0964 2.1093 1.6822 0.0589  0.1804  -0.0238 63  PHE E C   
12147 O O   . PHE E 63  ? 2.1524 2.1746 1.7477 0.0581  0.1973  -0.0235 63  PHE E O   
12148 C CB  . PHE E 63  ? 2.0372 2.0683 1.6706 0.0579  0.1556  -0.0185 63  PHE E CB  
12149 C CG  . PHE E 63  ? 2.0434 2.0882 1.7103 0.0594  0.1451  -0.0205 63  PHE E CG  
12150 C CD1 . PHE E 63  ? 2.0008 2.0652 1.7017 0.0590  0.1526  -0.0192 63  PHE E CD1 
12151 C CD2 . PHE E 63  ? 2.0638 2.1021 1.7282 0.0611  0.1276  -0.0237 63  PHE E CD2 
12152 C CE1 . PHE E 63  ? 1.9775 2.0541 1.7080 0.0602  0.1432  -0.0206 63  PHE E CE1 
12153 C CE2 . PHE E 63  ? 2.0346 2.0855 1.7297 0.0621  0.1185  -0.0253 63  PHE E CE2 
12154 C CZ  . PHE E 63  ? 1.9606 2.0303 1.6880 0.0617  0.1265  -0.0235 63  PHE E CZ  
12155 N N   . LEU E 64  ? 2.1042 2.0993 1.6562 0.0577  0.1742  -0.0209 64  LEU E N   
12156 C CA  . LEU E 64  ? 2.2074 2.1925 1.7310 0.0553  0.1877  -0.0168 64  LEU E CA  
12157 C C   . LEU E 64  ? 2.3299 2.3084 1.8346 0.0581  0.2012  -0.0254 64  LEU E C   
12158 O O   . LEU E 64  ? 2.3737 2.3507 1.8655 0.0561  0.2179  -0.0232 64  LEU E O   
12159 C CB  . LEU E 64  ? 2.1695 2.1363 1.6611 0.0537  0.1761  -0.0113 64  LEU E CB  
12160 C CG  . LEU E 64  ? 2.0938 2.0656 1.6024 0.0514  0.1614  -0.0034 64  LEU E CG  
12161 C CD1 . LEU E 64  ? 2.0768 2.0295 1.5526 0.0506  0.1499  0.0015  64  LEU E CD1 
12162 C CD2 . LEU E 64  ? 2.1313 2.1186 1.6656 0.0473  0.1715  0.0045  64  LEU E CD2 
12163 N N   . LYS E 65  ? 2.5901 2.5647 2.0933 0.0626  0.1945  -0.0355 65  LYS E N   
12164 C CA  . LYS E 65  ? 2.6105 2.5785 2.0961 0.0658  0.2069  -0.0446 65  LYS E CA  
12165 C C   . LYS E 65  ? 2.5811 2.5669 2.0955 0.0667  0.2237  -0.0474 65  LYS E C   
12166 O O   . LYS E 65  ? 2.5875 2.5707 2.0885 0.0679  0.2397  -0.0521 65  LYS E O   
12167 C CB  . LYS E 65  ? 2.6334 2.5911 2.1090 0.0703  0.1939  -0.0548 65  LYS E CB  
12168 C CG  . LYS E 65  ? 2.6824 2.6257 2.1258 0.0733  0.2028  -0.0638 65  LYS E CG  
12169 C CD  . LYS E 65  ? 2.6793 2.6110 2.1117 0.0772  0.1874  -0.0734 65  LYS E CD  
12170 C CE  . LYS E 65  ? 2.6879 2.6102 2.1089 0.0755  0.1669  -0.0683 65  LYS E CE  
12171 N NZ  . LYS E 65  ? 2.7066 2.6191 2.1205 0.0789  0.1507  -0.0775 65  LYS E NZ  
12172 N N   . ASP E 66  ? 2.2888 2.2930 1.8424 0.0662  0.2205  -0.0448 66  ASP E N   
12173 C CA  . ASP E 66  ? 2.2217 2.2438 1.8049 0.0672  0.2351  -0.0470 66  ASP E CA  
12174 C C   . ASP E 66  ? 2.2854 2.3165 1.8740 0.0627  0.2503  -0.0388 66  ASP E C   
12175 O O   . ASP E 66  ? 2.2372 2.2816 1.8447 0.0634  0.2653  -0.0409 66  ASP E O   
12176 C CB  . ASP E 66  ? 2.0716 2.1095 1.6940 0.0687  0.2251  -0.0474 66  ASP E CB  
12177 C CG  . ASP E 66  ? 1.9335 1.9641 1.5547 0.0730  0.2117  -0.0561 66  ASP E CG  
12178 O OD1 . ASP E 66  ? 1.9602 1.9778 1.5576 0.0762  0.2150  -0.0644 66  ASP E OD1 
12179 O OD2 . ASP E 66  ? 1.8618 1.8995 1.5057 0.0732  0.1981  -0.0548 66  ASP E OD2 
12180 N N   . PHE E 67  ? 2.4581 2.4823 2.0314 0.0581  0.2467  -0.0296 67  PHE E N   
12181 C CA  . PHE E 67  ? 2.4463 2.4775 2.0233 0.0532  0.2605  -0.0213 67  PHE E CA  
12182 C C   . PHE E 67  ? 2.4697 2.4871 2.0107 0.0517  0.2747  -0.0213 67  PHE E C   
12183 O O   . PHE E 67  ? 2.4571 2.4808 2.0011 0.0479  0.2900  -0.0161 67  PHE E O   
12184 C CB  . PHE E 67  ? 2.4538 2.4853 2.0357 0.0487  0.2492  -0.0109 67  PHE E CB  
12185 C CG  . PHE E 67  ? 2.5174 2.5637 2.1353 0.0495  0.2364  -0.0100 67  PHE E CG  
12186 C CD1 . PHE E 67  ? 2.5201 2.5833 2.1701 0.0523  0.2405  -0.0153 67  PHE E CD1 
12187 C CD2 . PHE E 67  ? 2.5194 2.5623 2.1382 0.0476  0.2202  -0.0039 67  PHE E CD2 
12188 C CE1 . PHE E 67  ? 2.5126 2.5891 2.1943 0.0529  0.2289  -0.0141 67  PHE E CE1 
12189 C CE2 . PHE E 67  ? 2.4942 2.5507 2.1451 0.0482  0.2089  -0.0032 67  PHE E CE2 
12190 C CZ  . PHE E 67  ? 2.4988 2.5720 2.1807 0.0507  0.2133  -0.0081 67  PHE E CZ  
12191 N N   . GLU E 68  ? 2.3305 2.3293 1.8375 0.0546  0.2700  -0.0269 68  GLU E N   
12192 C CA  . GLU E 68  ? 2.3183 2.3029 1.7883 0.0534  0.2833  -0.0272 68  GLU E CA  
12193 C C   . GLU E 68  ? 2.2437 2.2370 1.7207 0.0556  0.3033  -0.0345 68  GLU E C   
12194 O O   . GLU E 68  ? 2.2241 2.2145 1.6842 0.0529  0.3201  -0.0321 68  GLU E O   
12195 C CB  . GLU E 68  ? 2.3358 2.2980 1.7671 0.0561  0.2714  -0.0316 68  GLU E CB  
12196 C CG  . GLU E 68  ? 2.3809 2.3313 1.7964 0.0534  0.2546  -0.0231 68  GLU E CG  
12197 C CD  . GLU E 68  ? 2.3828 2.3106 1.7574 0.0559  0.2441  -0.0273 68  GLU E CD  
12198 O OE1 . GLU E 68  ? 2.3625 2.2872 1.7363 0.0606  0.2365  -0.0374 68  GLU E OE1 
12199 O OE2 . GLU E 68  ? 2.4849 2.3978 1.8281 0.0531  0.2432  -0.0204 68  GLU E OE2 
12200 N N   . THR E 69  ? 2.1796 2.1832 1.6811 0.0605  0.3020  -0.0434 69  THR E N   
12201 C CA  . THR E 69  ? 2.1288 2.1417 1.6402 0.0633  0.3202  -0.0510 69  THR E CA  
12202 C C   . THR E 69  ? 2.1505 2.1865 1.7013 0.0611  0.3312  -0.0467 69  THR E C   
12203 O O   . THR E 69  ? 2.1317 2.1748 1.6848 0.0604  0.3504  -0.0480 69  THR E O   
12204 C CB  . THR E 69  ? 2.0354 2.0468 1.5531 0.0701  0.3137  -0.0631 69  THR E CB  
12205 O OG1 . THR E 69  ? 2.0354 2.0463 1.5659 0.0710  0.2924  -0.0622 69  THR E OG1 
12206 C CG2 . THR E 69  ? 1.9705 1.9620 1.4473 0.0730  0.3167  -0.0711 69  THR E CG2 
12207 N N   . LYS E 70  ? 2.1037 2.1521 1.6857 0.0599  0.3194  -0.0419 70  LYS E N   
12208 C CA  . LYS E 70  ? 2.0940 2.1646 1.7136 0.0578  0.3284  -0.0378 70  LYS E CA  
12209 C C   . LYS E 70  ? 2.1065 2.1785 1.7187 0.0511  0.3405  -0.0284 70  LYS E C   
12210 O O   . LYS E 70  ? 2.0336 2.1200 1.6640 0.0495  0.3567  -0.0277 70  LYS E O   
12211 C CB  . LYS E 70  ? 2.0798 2.1619 1.7313 0.0578  0.3121  -0.0344 70  LYS E CB  
12212 C CG  . LYS E 70  ? 2.1045 2.2096 1.7949 0.0555  0.3198  -0.0300 70  LYS E CG  
12213 C CD  . LYS E 70  ? 2.1363 2.2514 1.8543 0.0548  0.3034  -0.0255 70  LYS E CD  
12214 C CE  . LYS E 70  ? 2.1971 2.3005 1.8972 0.0506  0.2906  -0.0174 70  LYS E CE  
12215 N NZ  . LYS E 70  ? 2.2203 2.3335 1.9468 0.0501  0.2749  -0.0136 70  LYS E NZ  
12216 N N   . LEU E 71  ? 2.1201 2.1771 1.7058 0.0472  0.3328  -0.0210 71  LEU E N   
12217 C CA  . LEU E 71  ? 2.1296 2.1861 1.7075 0.0405  0.3426  -0.0111 71  LEU E CA  
12218 C C   . LEU E 71  ? 2.1328 2.1721 1.6694 0.0390  0.3550  -0.0111 71  LEU E C   
12219 O O   . LEU E 71  ? 2.1353 2.1738 1.6639 0.0332  0.3659  -0.0032 71  LEU E O   
12220 C CB  . LEU E 71  ? 2.1185 2.1705 1.6966 0.0367  0.3265  -0.0015 71  LEU E CB  
12221 C CG  . LEU E 71  ? 2.1486 2.2174 1.7663 0.0372  0.3143  0.0000  71  LEU E CG  
12222 C CD1 . LEU E 71  ? 2.2424 2.3043 1.8555 0.0338  0.2987  0.0088  71  LEU E CD1 
12223 C CD2 . LEU E 71  ? 2.1240 2.2151 1.7770 0.0349  0.3279  0.0016  71  LEU E CD2 
12224 N N   . GLU E 72  ? 2.1423 2.1681 1.6528 0.0438  0.3537  -0.0197 72  GLU E N   
12225 C CA  . GLU E 72  ? 2.1408 2.1489 1.6088 0.0429  0.3644  -0.0205 72  GLU E CA  
12226 C C   . GLU E 72  ? 2.1780 2.1702 1.6178 0.0376  0.3580  -0.0095 72  GLU E C   
12227 O O   . GLU E 72  ? 2.1678 2.1569 1.5937 0.0324  0.3716  -0.0026 72  GLU E O   
12228 C CB  . GLU E 72  ? 2.1334 2.1519 1.6073 0.0415  0.3892  -0.0225 72  GLU E CB  
12229 C CG  . GLU E 72  ? 2.1407 2.1698 1.6321 0.0478  0.3967  -0.0348 72  GLU E CG  
12230 C CD  . GLU E 72  ? 2.1559 2.1946 1.6510 0.0466  0.4216  -0.0372 72  GLU E CD  
12231 O OE1 . GLU E 72  ? 2.0919 2.1355 1.5892 0.0403  0.4325  -0.0283 72  GLU E OE1 
12232 O OE2 . GLU E 72  ? 2.1960 2.2377 1.6929 0.0520  0.4302  -0.0479 72  GLU E OE2 
12233 N N   . ILE E 73  ? 2.3051 2.2871 1.7368 0.0390  0.3369  -0.0080 73  ILE E N   
12234 C CA  . ILE E 73  ? 2.4059 2.3726 1.8135 0.0348  0.3271  0.0022  73  ILE E CA  
12235 C C   . ILE E 73  ? 2.5570 2.5057 1.9380 0.0389  0.3082  -0.0019 73  ILE E C   
12236 O O   . ILE E 73  ? 2.4631 2.4166 1.8603 0.0436  0.2961  -0.0092 73  ILE E O   
12237 C CB  . ILE E 73  ? 2.3243 2.3035 1.7635 0.0308  0.3192  0.0114  73  ILE E CB  
12238 C CG1 . ILE E 73  ? 2.2490 2.2390 1.7011 0.0248  0.3376  0.0186  73  ILE E CG1 
12239 C CG2 . ILE E 73  ? 2.3387 2.3025 1.7589 0.0293  0.3007  0.0189  73  ILE E CG2 
12240 C CD1 . ILE E 73  ? 2.1900 2.1902 1.6694 0.0204  0.3304  0.0279  73  ILE E CD1 
12241 N N   . LYS E 74  ? 3.1519 3.0799 2.4923 0.0371  0.3055  0.0030  74  LYS E N   
12242 C CA  . LYS E 74  ? 3.1809 3.0908 2.4939 0.0406  0.2868  0.0000  74  LYS E CA  
12243 C C   . LYS E 74  ? 3.1697 3.0797 2.4958 0.0391  0.2671  0.0077  74  LYS E C   
12244 O O   . LYS E 74  ? 3.1654 3.0735 2.4897 0.0342  0.2682  0.0187  74  LYS E O   
12245 C CB  . LYS E 74  ? 3.2146 3.1020 2.4772 0.0396  0.2920  0.0020  74  LYS E CB  
12246 C CG  . LYS E 74  ? 3.2462 3.1147 2.4783 0.0437  0.2736  -0.0027 74  LYS E CG  
12247 C CD  . LYS E 74  ? 3.2510 3.1236 2.4918 0.0498  0.2702  -0.0168 74  LYS E CD  
12248 C CE  . LYS E 74  ? 3.2851 3.1384 2.4939 0.0537  0.2528  -0.0223 74  LYS E CE  
12249 N NZ  . LYS E 74  ? 3.3911 3.2235 2.5502 0.0527  0.2595  -0.0205 74  LYS E NZ  
12250 N N   . ILE E 75  ? 2.5987 2.5110 1.9385 0.0432  0.2494  0.0019  75  ILE E N   
12251 C CA  . ILE E 75  ? 2.4532 2.3679 1.8096 0.0424  0.2304  0.0077  75  ILE E CA  
12252 C C   . ILE E 75  ? 2.4104 2.3079 1.7409 0.0460  0.2110  0.0040  75  ILE E C   
12253 O O   . ILE E 75  ? 2.4126 2.3097 1.7444 0.0505  0.2050  -0.0064 75  ILE E O   
12254 C CB  . ILE E 75  ? 2.3896 2.3268 1.7939 0.0435  0.2269  0.0048  75  ILE E CB  
12255 C CG1 . ILE E 75  ? 2.4264 2.3812 1.8568 0.0401  0.2457  0.0083  75  ILE E CG1 
12256 C CG2 . ILE E 75  ? 2.3396 2.2789 1.7596 0.0428  0.2073  0.0104  75  ILE E CG2 
12257 C CD1 . ILE E 75  ? 2.3921 2.3693 1.8685 0.0413  0.2435  0.0053  75  ILE E CD1 
12258 N N   . THR E 76  ? 2.3962 2.2794 1.7040 0.0439  0.2009  0.0124  76  THR E N   
12259 C CA  . THR E 76  ? 2.3209 2.1880 1.6049 0.0470  0.1810  0.0102  76  THR E CA  
12260 C C   . THR E 76  ? 2.2904 2.1586 1.5878 0.0454  0.1641  0.0186  76  THR E C   
12261 O O   . THR E 76  ? 2.3800 2.2540 1.6900 0.0412  0.1694  0.0282  76  THR E O   
12262 C CB  . THR E 76  ? 2.3629 2.2070 1.5964 0.0470  0.1843  0.0114  76  THR E CB  
12263 O OG1 . THR E 76  ? 2.4734 2.3122 1.6943 0.0419  0.1939  0.0232  76  THR E OG1 
12264 C CG2 . THR E 76  ? 2.4362 2.2782 1.6546 0.0493  0.1995  0.0014  76  THR E CG2 
12265 N N   . CYS E 77  ? 2.1497 2.0124 1.4450 0.0488  0.1439  0.0147  77  CYS E N   
12266 C CA  . CYS E 77  ? 2.2371 2.1019 1.5476 0.0482  0.1263  0.0210  77  CYS E CA  
12267 C C   . CYS E 77  ? 2.1779 2.0210 1.4509 0.0486  0.1136  0.0262  77  CYS E C   
12268 O O   . CYS E 77  ? 2.2229 2.0495 1.4597 0.0506  0.1129  0.0222  77  CYS E O   
12269 C CB  . CYS E 77  ? 2.2693 2.1457 1.6092 0.0514  0.1117  0.0134  77  CYS E CB  
12270 S SG  . CYS E 77  ? 2.3950 2.2978 1.7829 0.0512  0.1235  0.0086  77  CYS E SG  
12271 N N   . SER E 78  ? 2.3165 2.1596 1.5986 0.0468  0.1031  0.0352  78  SER E N   
12272 C CA  . SER E 78  ? 2.3368 2.1610 1.5892 0.0477  0.0878  0.0408  78  SER E CA  
12273 C C   . SER E 78  ? 2.3597 2.1918 1.6390 0.0489  0.0685  0.0425  78  SER E C   
12274 O O   . SER E 78  ? 2.3660 2.2119 1.6760 0.0463  0.0707  0.0480  78  SER E O   
12275 C CB  . SER E 78  ? 2.3949 2.2074 1.6240 0.0436  0.0977  0.0524  78  SER E CB  
12276 O OG  . SER E 78  ? 2.4386 2.2638 1.6979 0.0400  0.1016  0.0604  78  SER E OG  
12277 N N   . GLN E 79  ? 2.3001 2.1237 1.5682 0.0527  0.0497  0.0376  79  GLN E N   
12278 C CA  . GLN E 79  ? 2.2834 2.1143 1.5761 0.0543  0.0304  0.0381  79  GLN E CA  
12279 C C   . GLN E 79  ? 2.3348 2.1477 1.6004 0.0553  0.0152  0.0450  79  GLN E C   
12280 O O   . GLN E 79  ? 2.3799 2.1752 1.6095 0.0575  0.0091  0.0424  79  GLN E O   
12281 C CB  . GLN E 79  ? 2.2910 2.1290 1.5982 0.0578  0.0197  0.0264  79  GLN E CB  
12282 C CG  . GLN E 79  ? 2.2528 2.0997 1.5873 0.0592  0.0005  0.0266  79  GLN E CG  
12283 C CD  . GLN E 79  ? 2.2642 2.1165 1.6109 0.0623  -0.0106 0.0153  79  GLN E CD  
12284 O OE1 . GLN E 79  ? 2.3223 2.1705 1.6560 0.0637  -0.0048 0.0070  79  GLN E OE1 
12285 N NE2 . GLN E 79  ? 2.2486 2.1102 1.6211 0.0633  -0.0264 0.0148  79  GLN E NE2 
12286 N N   . GLU E 80  ? 2.5145 2.3317 1.7972 0.0538  0.0089  0.0535  80  GLU E N   
12287 C CA  . GLU E 80  ? 2.5313 2.3329 1.7933 0.0551  -0.0066 0.0605  80  GLU E CA  
12288 C C   . GLU E 80  ? 2.5036 2.3121 1.7870 0.0585  -0.0282 0.0564  80  GLU E C   
12289 O O   . GLU E 80  ? 2.4829 2.3107 1.8045 0.0583  -0.0293 0.0524  80  GLU E O   
12290 C CB  . GLU E 80  ? 2.5492 2.3492 1.8146 0.0515  -0.0001 0.0729  80  GLU E CB  
12291 C CG  . GLU E 80  ? 2.7049 2.4941 1.9431 0.0479  0.0193  0.0788  80  GLU E CG  
12292 C CD  . GLU E 80  ? 2.6842 2.4892 1.9422 0.0449  0.0404  0.0749  80  GLU E CD  
12293 O OE1 . GLU E 80  ? 2.5607 2.3852 1.8548 0.0455  0.0398  0.0687  80  GLU E OE1 
12294 O OE2 . GLU E 80  ? 2.7085 2.5065 1.9458 0.0420  0.0576  0.0782  80  GLU E OE2 
12295 N N   . THR E 81  ? 2.2905 2.0829 1.5486 0.0615  -0.0454 0.0575  81  THR E N   
12296 C CA  . THR E 81  ? 2.2434 2.0414 1.5204 0.0647  -0.0666 0.0540  81  THR E CA  
12297 C C   . THR E 81  ? 2.1962 2.0074 1.5073 0.0633  -0.0698 0.0607  81  THR E C   
12298 O O   . THR E 81  ? 2.1448 1.9735 1.4915 0.0640  -0.0763 0.0561  81  THR E O   
12299 C CB  . THR E 81  ? 2.2276 2.0050 1.4696 0.0682  -0.0842 0.0551  81  THR E CB  
12300 O OG1 . THR E 81  ? 2.2311 1.9930 1.4478 0.0669  -0.0814 0.0667  81  THR E OG1 
12301 C CG2 . THR E 81  ? 2.1841 1.9502 1.3955 0.0699  -0.0833 0.0465  81  THR E CG2 
12302 N N   . GLU E 82  ? 2.1917 1.9946 1.4923 0.0613  -0.0651 0.0716  82  GLU E N   
12303 C CA  . GLU E 82  ? 2.1749 1.9883 1.5049 0.0598  -0.0673 0.0783  82  GLU E CA  
12304 C C   . GLU E 82  ? 2.2101 2.0265 1.5440 0.0550  -0.0469 0.0855  82  GLU E C   
12305 O O   . GLU E 82  ? 2.2192 2.0232 1.5239 0.0530  -0.0341 0.0884  82  GLU E O   
12306 C CB  . GLU E 82  ? 2.1305 1.9299 1.4466 0.0624  -0.0847 0.0854  82  GLU E CB  
12307 C CG  . GLU E 82  ? 2.0994 1.8987 1.4185 0.0671  -0.1065 0.0789  82  GLU E CG  
12308 C CD  . GLU E 82  ? 2.1067 1.8916 1.3912 0.0693  -0.1105 0.0727  82  GLU E CD  
12309 O OE1 . GLU E 82  ? 2.1761 1.9424 1.4227 0.0687  -0.1044 0.0776  82  GLU E OE1 
12310 O OE2 . GLU E 82  ? 2.0617 1.8541 1.3568 0.0715  -0.1192 0.0628  82  GLU E OE2 
12311 N N   . PRO E 83  ? 2.2678 2.1010 1.6377 0.0529  -0.0433 0.0881  83  PRO E N   
12312 C CA  . PRO E 83  ? 2.2675 2.1018 1.6408 0.0481  -0.0266 0.0963  83  PRO E CA  
12313 C C   . PRO E 83  ? 2.3061 2.1192 1.6501 0.0478  -0.0310 0.1068  83  PRO E C   
12314 O O   . PRO E 83  ? 2.2862 2.0950 1.6342 0.0502  -0.0468 0.1105  83  PRO E O   
12315 C CB  . PRO E 83  ? 2.2043 2.0602 1.6225 0.0470  -0.0275 0.0961  83  PRO E CB  
12316 C CG  . PRO E 83  ? 2.1853 2.0546 1.6245 0.0503  -0.0379 0.0860  83  PRO E CG  
12317 C CD  . PRO E 83  ? 2.2235 2.0764 1.6333 0.0544  -0.0531 0.0831  83  PRO E CD  
12318 N N   . LEU E 84  ? 2.3739 2.1736 1.6884 0.0449  -0.0168 0.1117  84  LEU E N   
12319 C CA  . LEU E 84  ? 2.3710 2.1480 1.6521 0.0445  -0.0200 0.1219  84  LEU E CA  
12320 C C   . LEU E 84  ? 2.4050 2.1833 1.6975 0.0395  -0.0081 0.1318  84  LEU E C   
12321 O O   . LEU E 84  ? 2.4347 2.2012 1.7041 0.0357  0.0058  0.1385  84  LEU E O   
12322 C CB  . LEU E 84  ? 2.3630 2.1219 1.6003 0.0445  -0.0131 0.1215  84  LEU E CB  
12323 C CG  . LEU E 84  ? 2.2690 2.0263 1.4939 0.0490  -0.0230 0.1108  84  LEU E CG  
12324 C CD1 . LEU E 84  ? 2.1313 1.8717 1.3132 0.0486  -0.0133 0.1102  84  LEU E CD1 
12325 C CD2 . LEU E 84  ? 2.2402 1.9909 1.4626 0.0541  -0.0478 0.1101  84  LEU E CD2 
12326 N N   . GLY E 85  ? 2.3006 2.0937 1.6296 0.0394  -0.0139 0.1323  85  GLY E N   
12327 C CA  . GLY E 85  ? 2.3231 2.1197 1.6676 0.0347  -0.0035 0.1404  85  GLY E CA  
12328 C C   . GLY E 85  ? 2.2404 2.0510 1.5990 0.0298  0.0183  0.1380  85  GLY E C   
12329 O O   . GLY E 85  ? 2.1902 2.0185 1.5701 0.0306  0.0218  0.1289  85  GLY E O   
12330 N N   . THR E 86  ? 2.3815 2.1844 1.7288 0.0247  0.0333  0.1462  86  THR E N   
12331 C CA  . THR E 86  ? 2.3142 2.1296 1.6734 0.0197  0.0548  0.1446  86  THR E CA  
12332 C C   . THR E 86  ? 2.2984 2.0998 1.6212 0.0176  0.0691  0.1462  86  THR E C   
12333 O O   . THR E 86  ? 2.2399 2.0524 1.5694 0.0157  0.0844  0.1408  86  THR E O   
12334 C CB  . THR E 86  ? 2.2693 2.0915 1.6515 0.0145  0.0636  0.1518  86  THR E CB  
12335 O OG1 . THR E 86  ? 2.3085 2.1345 1.7123 0.0168  0.0474  0.1534  86  THR E OG1 
12336 C CG2 . THR E 86  ? 2.0632 1.9085 1.4768 0.0111  0.0795  0.1464  86  THR E CG2 
12337 N N   . ALA E 87  ? 2.3679 2.1451 1.6521 0.0180  0.0646  0.1535  87  ALA E N   
12338 C CA  . ALA E 87  ? 2.3834 2.1455 1.6297 0.0159  0.0780  0.1557  87  ALA E CA  
12339 C C   . ALA E 87  ? 2.3534 2.1045 1.5694 0.0212  0.0686  0.1492  87  ALA E C   
12340 O O   . ALA E 87  ? 2.2791 2.0198 1.4644 0.0200  0.0802  0.1489  87  ALA E O   
12341 C CB  . ALA E 87  ? 2.6211 2.3623 1.8412 0.0122  0.0815  0.1690  87  ALA E CB  
12342 N N   . GLY E 88  ? 2.4776 2.2306 1.7013 0.0267  0.0483  0.1439  88  GLY E N   
12343 C CA  . GLY E 88  ? 2.4865 2.2296 1.6839 0.0318  0.0374  0.1372  88  GLY E CA  
12344 C C   . GLY E 88  ? 2.5261 2.2781 1.7218 0.0321  0.0493  0.1268  88  GLY E C   
12345 O O   . GLY E 88  ? 2.5213 2.2590 1.6808 0.0330  0.0531  0.1250  88  GLY E O   
12346 N N   . PRO E 89  ? 2.8363 2.6119 2.0709 0.0316  0.0549  0.1194  89  PRO E N   
12347 C CA  . PRO E 89  ? 2.8391 2.6238 2.0748 0.0322  0.0665  0.1093  89  PRO E CA  
12348 C C   . PRO E 89  ? 2.8521 2.6282 2.0611 0.0284  0.0877  0.1120  89  PRO E C   
12349 O O   . PRO E 89  ? 2.8612 2.6372 2.0570 0.0298  0.0954  0.1041  89  PRO E O   
12350 C CB  . PRO E 89  ? 2.8116 2.6226 2.0959 0.0310  0.0711  0.1047  89  PRO E CB  
12351 C CG  . PRO E 89  ? 2.7958 2.6108 2.1016 0.0327  0.0533  0.1078  89  PRO E CG  
12352 C CD  . PRO E 89  ? 2.8085 2.6029 2.0871 0.0315  0.0480  0.1190  89  PRO E CD  
12353 N N   . LEU E 90  ? 2.5249 2.2938 1.7263 0.0236  0.0974  0.1230  90  LEU E N   
12354 C CA  . LEU E 90  ? 2.4591 2.2187 1.6334 0.0196  0.1176  0.1266  90  LEU E CA  
12355 C C   . LEU E 90  ? 2.5161 2.2505 1.6397 0.0218  0.1128  0.1286  90  LEU E C   
12356 O O   . LEU E 90  ? 2.5155 2.2433 1.6135 0.0204  0.1277  0.1268  90  LEU E O   
12357 C CB  . LEU E 90  ? 2.3558 2.1152 1.5384 0.0133  0.1295  0.1381  90  LEU E CB  
12358 C CG  . LEU E 90  ? 2.2837 2.0676 1.5119 0.0096  0.1409  0.1367  90  LEU E CG  
12359 C CD1 . LEU E 90  ? 2.2745 2.0711 1.5388 0.0118  0.1244  0.1358  90  LEU E CD1 
12360 C CD2 . LEU E 90  ? 2.3253 2.1058 1.5506 0.0025  0.1586  0.1469  90  LEU E CD2 
12361 N N   . ALA E 91  ? 2.5399 2.2602 1.6482 0.0252  0.0921  0.1322  91  ALA E N   
12362 C CA  . ALA E 91  ? 2.5579 2.2538 1.6173 0.0277  0.0856  0.1341  91  ALA E CA  
12363 C C   . ALA E 91  ? 2.7171 2.4136 1.7636 0.0322  0.0822  0.1213  91  ALA E C   
12364 O O   . ALA E 91  ? 2.7088 2.3883 1.7140 0.0331  0.0855  0.1208  91  ALA E O   
12365 C CB  . ALA E 91  ? 2.4695 2.1513 1.5189 0.0307  0.0632  0.1410  91  ALA E CB  
12366 N N   . LEU E 92  ? 3.1187 2.8341 2.1993 0.0351  0.0756  0.1110  92  LEU E N   
12367 C CA  . LEU E 92  ? 3.1293 2.8459 2.2008 0.0393  0.0721  0.0984  92  LEU E CA  
12368 C C   . LEU E 92  ? 3.1322 2.8561 2.2021 0.0371  0.0951  0.0925  92  LEU E C   
12369 O O   . LEU E 92  ? 3.1512 2.8663 2.1933 0.0394  0.0979  0.0854  92  LEU E O   
12370 C CB  . LEU E 92  ? 3.1084 2.8419 2.2172 0.0430  0.0565  0.0899  92  LEU E CB  
12371 C CG  . LEU E 92  ? 3.1322 2.8678 2.2370 0.0475  0.0497  0.0763  92  LEU E CG  
12372 C CD1 . LEU E 92  ? 3.1061 2.8435 2.2243 0.0517  0.0249  0.0727  92  LEU E CD1 
12373 C CD2 . LEU E 92  ? 3.0889 2.8452 2.2245 0.0465  0.0647  0.0677  92  LEU E CD2 
12374 N N   . ALA E 93  ? 2.7463 2.4865 1.8461 0.0328  0.1114  0.0951  93  ALA E N   
12375 C CA  . ALA E 93  ? 2.6454 2.3956 1.7498 0.0307  0.1334  0.0895  93  ALA E CA  
12376 C C   . ALA E 93  ? 2.5271 2.2642 1.5997 0.0262  0.1522  0.0974  93  ALA E C   
12377 O O   . ALA E 93  ? 2.4231 2.1699 1.5032 0.0235  0.1728  0.0948  93  ALA E O   
12378 C CB  . ALA E 93  ? 2.6015 2.3774 1.7561 0.0286  0.1414  0.0877  93  ALA E CB  
12379 N N   . ARG E 94  ? 2.6116 2.3270 1.6490 0.0254  0.1457  0.1069  94  ARG E N   
12380 C CA  . ARG E 94  ? 2.6141 2.3157 1.6189 0.0209  0.1635  0.1150  94  ARG E CA  
12381 C C   . ARG E 94  ? 2.5884 2.2831 1.5620 0.0226  0.1748  0.1066  94  ARG E C   
12382 O O   . ARG E 94  ? 2.5780 2.2691 1.5350 0.0185  0.1956  0.1099  94  ARG E O   
12383 C CB  . ARG E 94  ? 2.6557 2.3342 1.6284 0.0201  0.1523  0.1273  94  ARG E CB  
12384 C CG  . ARG E 94  ? 2.6655 2.3250 1.6011 0.0257  0.1340  0.1238  94  ARG E CG  
12385 C CD  . ARG E 94  ? 2.7446 2.3778 1.6311 0.0239  0.1356  0.1348  94  ARG E CD  
12386 N NE  . ARG E 94  ? 2.7669 2.3932 1.6589 0.0211  0.1286  0.1483  94  ARG E NE  
12387 C CZ  . ARG E 94  ? 2.7254 2.3295 1.5807 0.0187  0.1298  0.1604  94  ARG E CZ  
12388 N NH1 . ARG E 94  ? 2.7810 2.3679 1.5906 0.0186  0.1381  0.1608  94  ARG E NH1 
12389 N NH2 . ARG E 94  ? 2.6791 2.2777 1.5430 0.0165  0.1228  0.1721  94  ARG E NH2 
12390 N N   . ASP E 95  ? 2.5177 2.2103 1.4833 0.0284  0.1618  0.0956  95  ASP E N   
12391 C CA  . ASP E 95  ? 2.4690 2.1547 1.4050 0.0306  0.1716  0.0866  95  ASP E CA  
12392 C C   . ASP E 95  ? 2.4315 2.1376 1.3954 0.0295  0.1913  0.0781  95  ASP E C   
12393 O O   . ASP E 95  ? 2.4393 2.1413 1.3809 0.0287  0.2087  0.0744  95  ASP E O   
12394 C CB  . ASP E 95  ? 2.5177 2.1953 1.4387 0.0370  0.1508  0.0769  95  ASP E CB  
12395 C CG  . ASP E 95  ? 2.5287 2.2229 1.4923 0.0401  0.1339  0.0711  95  ASP E CG  
12396 O OD1 . ASP E 95  ? 2.4846 2.1968 1.4888 0.0374  0.1385  0.0743  95  ASP E OD1 
12397 O OD2 . ASP E 95  ? 2.6027 2.2921 1.5593 0.0450  0.1160  0.0634  95  ASP E OD2 
12398 N N   . LYS E 96  ? 2.3751 2.1032 1.3872 0.0296  0.1889  0.0748  96  LYS E N   
12399 C CA  . LYS E 96  ? 2.2512 2.0001 1.2939 0.0288  0.2063  0.0672  96  LYS E CA  
12400 C C   . LYS E 96  ? 2.2339 1.9926 1.2935 0.0224  0.2262  0.0759  96  LYS E C   
12401 O O   . LYS E 96  ? 2.1714 1.9473 1.2555 0.0213  0.2424  0.0705  96  LYS E O   
12402 C CB  . LYS E 96  ? 2.2143 1.9822 1.3004 0.0322  0.1938  0.0592  96  LYS E CB  
12403 C CG  . LYS E 96  ? 2.1419 1.9025 1.2158 0.0383  0.1751  0.0492  96  LYS E CG  
12404 C CD  . LYS E 96  ? 2.1020 1.8559 1.1495 0.0410  0.1855  0.0388  96  LYS E CD  
12405 C CE  . LYS E 96  ? 2.0284 1.8024 1.1066 0.0409  0.2029  0.0307  96  LYS E CE  
12406 N NZ  . LYS E 96  ? 1.9347 1.7017 0.9871 0.0441  0.2125  0.0198  96  LYS E NZ  
12407 N N   . LEU E 97  ? 2.3214 2.0694 1.3691 0.0181  0.2251  0.0891  97  LEU E N   
12408 C CA  . LEU E 97  ? 2.3654 2.1216 1.4291 0.0114  0.2430  0.0980  97  LEU E CA  
12409 C C   . LEU E 97  ? 2.4366 2.1777 1.4616 0.0072  0.2614  0.1042  97  LEU E C   
12410 O O   . LEU E 97  ? 2.4576 2.2079 1.4955 0.0018  0.2812  0.1083  97  LEU E O   
12411 C CB  . LEU E 97  ? 2.4717 2.2277 1.5529 0.0087  0.2308  0.1090  97  LEU E CB  
12412 C CG  . LEU E 97  ? 2.4481 2.2240 1.5766 0.0108  0.2179  0.1050  97  LEU E CG  
12413 C CD1 . LEU E 97  ? 2.5122 2.2839 1.6507 0.0086  0.2051  0.1159  97  LEU E CD1 
12414 C CD2 . LEU E 97  ? 2.4621 2.2627 1.6301 0.0085  0.2346  0.1002  97  LEU E CD2 
12415 N N   . LEU E 98  ? 2.4011 2.1195 1.3792 0.0095  0.2554  0.1049  98  LEU E N   
12416 C CA  . LEU E 98  ? 2.5102 2.2122 1.4473 0.0057  0.2720  0.1112  98  LEU E CA  
12417 C C   . LEU E 98  ? 2.6362 2.3419 1.5607 0.0079  0.2877  0.0995  98  LEU E C   
12418 O O   . LEU E 98  ? 2.6384 2.3352 1.5398 0.0135  0.2783  0.0906  98  LEU E O   
12419 C CB  . LEU E 98  ? 2.4861 2.1608 1.3775 0.0070  0.2571  0.1188  98  LEU E CB  
12420 C CG  . LEU E 98  ? 2.4319 2.1009 1.3335 0.0054  0.2406  0.1304  98  LEU E CG  
12421 C CD1 . LEU E 98  ? 2.5045 2.1452 1.3575 0.0065  0.2284  0.1387  98  LEU E CD1 
12422 C CD2 . LEU E 98  ? 2.4203 2.0994 1.3479 -0.0019 0.2555  0.1403  98  LEU E CD2 
12423 N N   . ASP E 99  ? 2.7632 2.4824 1.7034 0.0036  0.3114  0.0993  99  ASP E N   
12424 C CA  . ASP E 99  ? 2.7838 2.5072 1.7129 0.0052  0.3293  0.0889  99  ASP E CA  
12425 C C   . ASP E 99  ? 2.9561 2.6602 1.8363 0.0020  0.3446  0.0944  99  ASP E C   
12426 O O   . ASP E 99  ? 3.0049 2.7077 1.8660 0.0042  0.3572  0.0853  99  ASP E O   
12427 C CB  . ASP E 99  ? 2.7555 2.5055 1.7301 0.0028  0.3470  0.0847  99  ASP E CB  
12428 C CG  . ASP E 99  ? 2.8201 2.5757 1.8104 -0.0053 0.3600  0.0974  99  ASP E CG  
12429 O OD1 . ASP E 99  ? 2.7850 2.5292 1.7679 -0.0081 0.3490  0.1090  99  ASP E OD1 
12430 O OD2 . ASP E 99  ? 2.8910 2.6624 1.9020 -0.0086 0.3810  0.0956  99  ASP E OD2 
12431 N N   . GLY E 100 ? 2.9871 2.6759 1.8462 -0.0031 0.3442  0.1089  100 GLY E N   
12432 C CA  . GLY E 100 ? 3.0920 2.7612 1.9037 -0.0067 0.3582  0.1160  100 GLY E CA  
12433 C C   . GLY E 100 ? 3.2136 2.8887 2.0353 -0.0153 0.3808  0.1264  100 GLY E C   
12434 O O   . GLY E 100 ? 3.2872 2.9438 2.0734 -0.0199 0.3878  0.1377  100 GLY E O   
12435 N N   . SER E 101 ? 3.3674 3.0679 2.2368 -0.0176 0.3920  0.1229  101 SER E N   
12436 C CA  . SER E 101 ? 3.3777 3.0863 2.2611 -0.0259 0.4139  0.1317  101 SER E CA  
12437 C C   . SER E 101 ? 3.3573 3.0599 2.2503 -0.0313 0.4054  0.1466  101 SER E C   
12438 O O   . SER E 101 ? 3.4009 3.1040 2.2959 -0.0390 0.4222  0.1563  101 SER E O   
12439 C CB  . SER E 101 ? 3.3161 3.0542 2.2486 -0.0262 0.4273  0.1227  101 SER E CB  
12440 O OG  . SER E 101 ? 3.2968 3.0442 2.2465 -0.0344 0.4475  0.1310  101 SER E OG  
12441 N N   . GLY E 102 ? 3.1169 2.8141 2.0164 -0.0276 0.3802  0.1484  102 GLY E N   
12442 C CA  . GLY E 102 ? 2.9592 2.6507 1.8690 -0.0320 0.3709  0.1617  102 GLY E CA  
12443 C C   . GLY E 102 ? 2.8880 2.6034 1.8494 -0.0369 0.3804  0.1631  102 GLY E C   
12444 O O   . GLY E 102 ? 2.8186 2.5313 1.7847 -0.0442 0.3887  0.1748  102 GLY E O   
12445 N N   . GLU E 103 ? 2.8332 2.5719 1.8334 -0.0331 0.3788  0.1513  103 GLU E N   
12446 C CA  . GLU E 103 ? 2.8015 2.5644 1.8522 -0.0370 0.3865  0.1514  103 GLU E CA  
12447 C C   . GLU E 103 ? 2.7414 2.5109 1.8231 -0.0345 0.3640  0.1524  103 GLU E C   
12448 O O   . GLU E 103 ? 2.7425 2.5070 1.8184 -0.0278 0.3441  0.1470  103 GLU E O   
12449 C CB  . GLU E 103 ? 2.8233 2.6093 1.9004 -0.0345 0.4001  0.1382  103 GLU E CB  
12450 C CG  . GLU E 103 ? 2.8453 2.6316 1.9049 -0.0385 0.4268  0.1376  103 GLU E CG  
12451 C CD  . GLU E 103 ? 2.7761 2.5739 1.8601 -0.0474 0.4450  0.1458  103 GLU E CD  
12452 O OE1 . GLU E 103 ? 2.7219 2.5305 1.8409 -0.0499 0.4372  0.1501  103 GLU E OE1 
12453 O OE2 . GLU E 103 ? 2.8152 2.6114 1.8832 -0.0520 0.4673  0.1478  103 GLU E OE2 
12454 N N   . PRO E 104 ? 2.7705 2.5513 1.8854 -0.0400 0.3669  0.1592  104 PRO E N   
12455 C CA  . PRO E 104 ? 2.7895 2.5775 1.9350 -0.0377 0.3463  0.1599  104 PRO E CA  
12456 C C   . PRO E 104 ? 2.8641 2.6734 2.0430 -0.0315 0.3389  0.1465  104 PRO E C   
12457 O O   . PRO E 104 ? 2.8028 2.6300 2.0017 -0.0315 0.3536  0.1386  104 PRO E O   
12458 C CB  . PRO E 104 ? 2.7626 2.5598 1.9365 -0.0457 0.3559  0.1690  104 PRO E CB  
12459 C CG  . PRO E 104 ? 2.7371 2.5423 1.9106 -0.0510 0.3826  0.1683  104 PRO E CG  
12460 C CD  . PRO E 104 ? 2.7401 2.5268 1.8652 -0.0487 0.3887  0.1667  104 PRO E CD  
12461 N N   . PHE E 105 ? 3.1701 2.9771 2.3552 -0.0261 0.3158  0.1442  105 PHE E N   
12462 C CA  . PHE E 105 ? 3.1503 2.9758 2.3668 -0.0202 0.3058  0.1325  105 PHE E CA  
12463 C C   . PHE E 105 ? 3.1304 2.9700 2.3880 -0.0212 0.2944  0.1352  105 PHE E C   
12464 O O   . PHE E 105 ? 3.1401 2.9709 2.3961 -0.0249 0.2886  0.1455  105 PHE E O   
12465 C CB  . PHE E 105 ? 3.1686 2.9813 2.3596 -0.0127 0.2882  0.1260  105 PHE E CB  
12466 C CG  . PHE E 105 ? 3.1915 2.9830 2.3575 -0.0118 0.2695  0.1343  105 PHE E CG  
12467 C CD1 . PHE E 105 ? 3.2206 2.9876 2.3397 -0.0132 0.2721  0.1413  105 PHE E CD1 
12468 C CD2 . PHE E 105 ? 3.1821 2.9781 2.3711 -0.0093 0.2494  0.1350  105 PHE E CD2 
12469 C CE1 . PHE E 105 ? 3.2384 2.9857 2.3346 -0.0120 0.2544  0.1492  105 PHE E CE1 
12470 C CE2 . PHE E 105 ? 3.1989 2.9758 2.3661 -0.0080 0.2320  0.1425  105 PHE E CE2 
12471 C CZ  . PHE E 105 ? 3.2271 2.9796 2.3480 -0.0092 0.2342  0.1496  105 PHE E CZ  
12472 N N   . PHE E 106 ? 2.8770 2.7383 2.1711 -0.0179 0.2913  0.1258  106 PHE E N   
12473 C CA  . PHE E 106 ? 2.7528 2.6301 2.0879 -0.0185 0.2815  0.1269  106 PHE E CA  
12474 C C   . PHE E 106 ? 2.7559 2.6298 2.0935 -0.0122 0.2571  0.1233  106 PHE E C   
12475 O O   . PHE E 106 ? 2.6961 2.5654 2.0187 -0.0065 0.2498  0.1155  106 PHE E O   
12476 C CB  . PHE E 106 ? 2.4996 2.4037 1.8753 -0.0189 0.2931  0.1195  106 PHE E CB  
12477 N N   . VAL E 107 ? 2.8060 2.6825 2.1633 -0.0134 0.2448  0.1289  107 VAL E N   
12478 C CA  . VAL E 107 ? 2.8023 2.6784 2.1682 -0.0081 0.2219  0.1261  107 VAL E CA  
12479 C C   . VAL E 107 ? 2.7683 2.6672 2.1814 -0.0089 0.2183  0.1243  107 VAL E C   
12480 O O   . VAL E 107 ? 2.8503 2.7525 2.2788 -0.0138 0.2216  0.1317  107 VAL E O   
12481 C CB  . VAL E 107 ? 2.8355 2.6892 2.1743 -0.0080 0.2077  0.1351  107 VAL E CB  
12482 C CG1 . VAL E 107 ? 2.8250 2.6798 2.1742 -0.0022 0.1843  0.1313  107 VAL E CG1 
12483 C CG2 . VAL E 107 ? 2.8613 2.6919 2.1515 -0.0077 0.2121  0.1377  107 VAL E CG2 
12484 N N   . LEU E 108 ? 2.4628 2.3770 1.8986 -0.0041 0.2117  0.1146  108 LEU E N   
12485 C CA  . LEU E 108 ? 2.3113 2.2485 1.7917 -0.0044 0.2094  0.1117  108 LEU E CA  
12486 C C   . LEU E 108 ? 2.1655 2.1055 1.6587 0.0006  0.1877  0.1083  108 LEU E C   
12487 O O   . LEU E 108 ? 2.1274 2.0570 1.6007 0.0054  0.1764  0.1041  108 LEU E O   
12488 C CB  . LEU E 108 ? 2.2621 2.2184 1.7634 -0.0038 0.2233  0.1034  108 LEU E CB  
12489 C CG  . LEU E 108 ? 2.3008 2.2561 1.7908 -0.0085 0.2458  0.1056  108 LEU E CG  
12490 C CD1 . LEU E 108 ? 2.4876 2.4618 1.9989 -0.0069 0.2584  0.0966  108 LEU E CD1 
12491 C CD2 . LEU E 108 ? 2.4470 2.4040 1.9479 -0.0155 0.2537  0.1153  108 LEU E CD2 
12492 N N   . ASN E 109 ? 2.0465 2.0009 1.5734 -0.0006 0.1820  0.1099  109 ASN E N   
12493 C CA  . ASN E 109 ? 1.8918 1.8527 1.4369 0.0036  0.1631  0.1064  109 ASN E CA  
12494 C C   . ASN E 109 ? 1.8138 1.7984 1.3942 0.0055  0.1652  0.0981  109 ASN E C   
12495 O O   . ASN E 109 ? 1.7775 1.7772 1.3804 0.0023  0.1786  0.0979  109 ASN E O   
12496 C CB  . ASN E 109 ? 1.8505 1.8100 1.4076 0.0014  0.1537  0.1139  109 ASN E CB  
12497 C CG  . ASN E 109 ? 1.7361 1.6973 1.3037 0.0061  0.1327  0.1112  109 ASN E CG  
12498 O OD1 . ASN E 109 ? 1.7062 1.6776 1.2864 0.0102  0.1266  0.1031  109 ASN E OD1 
12499 N ND2 . ASN E 109 ? 1.7062 1.6573 1.2691 0.0056  0.1218  0.1179  109 ASN E ND2 
12500 N N   . SER E 110 ? 1.8852 1.8727 1.4705 0.0108  0.1517  0.0913  110 SER E N   
12501 C CA  . SER E 110 ? 1.8745 1.8828 1.4912 0.0131  0.1524  0.0835  110 SER E CA  
12502 C C   . SER E 110 ? 1.8239 1.8497 1.4774 0.0116  0.1473  0.0853  110 SER E C   
12503 O O   . SER E 110 ? 1.8006 1.8455 1.4827 0.0124  0.1510  0.0803  110 SER E O   
12504 C CB  . SER E 110 ? 1.8945 1.8992 1.5038 0.0188  0.1394  0.0759  110 SER E CB  
12505 O OG  . SER E 110 ? 1.9134 1.9371 1.5520 0.0210  0.1404  0.0686  110 SER E OG  
12506 N N   . ASP E 111 ? 1.6818 1.7016 1.3352 0.0098  0.1390  0.0921  111 ASP E N   
12507 C CA  . ASP E 111 ? 1.5941 1.6293 1.2806 0.0088  0.1327  0.0933  111 ASP E CA  
12508 C C   . ASP E 111 ? 1.5499 1.5942 1.2530 0.0031  0.1460  0.0983  111 ASP E C   
12509 O O   . ASP E 111 ? 1.5083 1.5614 1.2338 0.0015  0.1408  0.1009  111 ASP E O   
12510 C CB  . ASP E 111 ? 1.5731 1.5981 1.2535 0.0104  0.1151  0.0970  111 ASP E CB  
12511 C CG  . ASP E 111 ? 1.5607 1.5765 1.2249 0.0158  0.1011  0.0922  111 ASP E CG  
12512 O OD1 . ASP E 111 ? 1.6094 1.6238 1.2624 0.0179  0.1056  0.0866  111 ASP E OD1 
12513 O OD2 . ASP E 111 ? 1.4546 1.4648 1.1178 0.0179  0.0854  0.0939  111 ASP E OD2 
12514 N N   . VAL E 112 ? 1.5788 1.6213 1.2719 0.0000  0.1630  0.0993  112 VAL E N   
12515 C CA  . VAL E 112 ? 1.5944 1.6442 1.3010 -0.0060 0.1764  0.1042  112 VAL E CA  
12516 C C   . VAL E 112 ? 1.5789 1.6435 1.2988 -0.0069 0.1927  0.0993  112 VAL E C   
12517 O O   . VAL E 112 ? 1.6265 1.6869 1.3305 -0.0042 0.1978  0.0946  112 VAL E O   
12518 C CB  . VAL E 112 ? 1.7021 1.7316 1.3797 -0.0102 0.1820  0.1128  112 VAL E CB  
12519 C CG1 . VAL E 112 ? 1.7693 1.8066 1.4640 -0.0168 0.1943  0.1181  112 VAL E CG1 
12520 C CG2 . VAL E 112 ? 1.7706 1.7833 1.4316 -0.0083 0.1651  0.1173  112 VAL E CG2 
12521 N N   . ILE E 113 ? 1.5364 1.6184 1.2859 -0.0105 0.2005  0.1001  113 ILE E N   
12522 C CA  . ILE E 113 ? 1.6068 1.7038 1.3714 -0.0120 0.2167  0.0964  113 ILE E CA  
12523 C C   . ILE E 113 ? 1.6501 1.7489 1.4203 -0.0191 0.2300  0.1026  113 ILE E C   
12524 O O   . ILE E 113 ? 1.6362 1.7321 1.4120 -0.0225 0.2248  0.1084  113 ILE E O   
12525 C CB  . ILE E 113 ? 1.5336 1.6537 1.3336 -0.0091 0.2131  0.0899  113 ILE E CB  
12526 C CG1 . ILE E 113 ? 1.4950 1.6245 1.3195 -0.0107 0.2028  0.0926  113 ILE E CG1 
12527 C CG2 . ILE E 113 ? 1.5327 1.6511 1.3264 -0.0025 0.2035  0.0830  113 ILE E CG2 
12528 C CD1 . ILE E 113 ? 1.4555 1.6081 1.3150 -0.0085 0.2002  0.0872  113 ILE E CD1 
12529 N N   . SER E 114 ? 1.7252 1.8290 1.4947 -0.0213 0.2473  0.1012  114 SER E N   
12530 C CA  . SER E 114 ? 1.8146 1.9205 1.5890 -0.0285 0.2617  0.1069  114 SER E CA  
12531 C C   . SER E 114 ? 1.9228 2.0410 1.7054 -0.0291 0.2795  0.1023  114 SER E C   
12532 O O   . SER E 114 ? 1.9611 2.0876 1.7493 -0.0239 0.2795  0.0948  114 SER E O   
12533 C CB  . SER E 114 ? 2.0015 2.0835 1.7423 -0.0321 0.2634  0.1151  114 SER E CB  
12534 O OG  . SER E 114 ? 2.1059 2.1741 1.8149 -0.0301 0.2699  0.1136  114 SER E OG  
12535 N N   . GLU E 115 ? 1.8993 2.0191 1.6840 -0.0357 0.2948  0.1068  115 GLU E N   
12536 C CA  . GLU E 115 ? 1.9730 2.1042 1.7652 -0.0370 0.3132  0.1031  115 GLU E CA  
12537 C C   . GLU E 115 ? 2.2257 2.3403 1.9819 -0.0364 0.3235  0.1032  115 GLU E C   
12538 O O   . GLU E 115 ? 2.2681 2.3913 2.0277 -0.0355 0.3372  0.0982  115 GLU E O   
12539 C CB  . GLU E 115 ? 1.8710 2.0135 1.6850 -0.0446 0.3252  0.1075  115 GLU E CB  
12540 C CG  . GLU E 115 ? 1.7775 1.9347 1.6246 -0.0457 0.3147  0.1080  115 GLU E CG  
12541 C CD  . GLU E 115 ? 1.7930 1.9655 1.6666 -0.0527 0.3270  0.1102  115 GLU E CD  
12542 O OE1 . GLU E 115 ? 1.8815 2.0485 1.7439 -0.0581 0.3424  0.1139  115 GLU E OE1 
12543 O OE2 . GLU E 115 ? 1.6792 1.8690 1.5846 -0.0529 0.3211  0.1082  115 GLU E OE2 
12544 N N   . TYR E 116 ? 2.3914 2.4825 2.1135 -0.0368 0.3171  0.1086  116 TYR E N   
12545 C CA  . TYR E 116 ? 2.4737 2.5459 2.1568 -0.0359 0.3240  0.1091  116 TYR E CA  
12546 C C   . TYR E 116 ? 2.5793 2.6536 2.2572 -0.0411 0.3466  0.1108  116 TYR E C   
12547 O O   . TYR E 116 ? 2.5438 2.6256 2.2221 -0.0384 0.3574  0.1040  116 TYR E O   
12548 C CB  . TYR E 116 ? 2.4225 2.4948 2.0977 -0.0279 0.3177  0.1001  116 TYR E CB  
12549 C CG  . TYR E 116 ? 2.3959 2.4647 2.0732 -0.0228 0.2958  0.0983  116 TYR E CG  
12550 C CD1 . TYR E 116 ? 2.4325 2.4794 2.0789 -0.0215 0.2836  0.1025  116 TYR E CD1 
12551 C CD2 . TYR E 116 ? 2.3502 2.4378 2.0606 -0.0192 0.2874  0.0926  116 TYR E CD2 
12552 C CE1 . TYR E 116 ? 2.3875 2.4320 2.0372 -0.0169 0.2637  0.1007  116 TYR E CE1 
12553 C CE2 . TYR E 116 ? 2.3303 2.4155 2.0435 -0.0149 0.2680  0.0911  116 TYR E CE2 
12554 C CZ  . TYR E 116 ? 2.2853 2.3492 1.9686 -0.0137 0.2564  0.0950  116 TYR E CZ  
12555 O OH  . TYR E 116 ? 2.2561 2.3183 1.9434 -0.0095 0.2373  0.0932  116 TYR E OH  
12556 N N   . PRO E 117 ? 2.9960 3.0637 2.6693 -0.0487 0.3545  0.1196  117 PRO E N   
12557 C CA  . PRO E 117 ? 2.9967 3.0636 2.6602 -0.0542 0.3765  0.1221  117 PRO E CA  
12558 C C   . PRO E 117 ? 3.0348 3.0761 2.6512 -0.0545 0.3806  0.1263  117 PRO E C   
12559 O O   . PRO E 117 ? 3.0529 3.0795 2.6501 -0.0607 0.3864  0.1355  117 PRO E O   
12560 C CB  . PRO E 117 ? 2.9874 3.0600 2.6715 -0.0624 0.3810  0.1296  117 PRO E CB  
12561 C CG  . PRO E 117 ? 3.0081 3.0685 2.6871 -0.0616 0.3613  0.1347  117 PRO E CG  
12562 C CD  . PRO E 117 ? 3.0006 3.0641 2.6825 -0.0528 0.3444  0.1272  117 PRO E CD  
12563 N N   . LEU E 118 ? 2.5736 2.6089 2.1700 -0.0478 0.3775  0.1195  118 LEU E N   
12564 C CA  . LEU E 118 ? 2.4324 2.4428 1.9823 -0.0472 0.3790  0.1227  118 LEU E CA  
12565 C C   . LEU E 118 ? 2.4167 2.4242 1.9507 -0.0525 0.4022  0.1252  118 LEU E C   
12566 O O   . LEU E 118 ? 2.4356 2.4215 1.9323 -0.0552 0.4061  0.1320  118 LEU E O   
12567 C CB  . LEU E 118 ? 2.2926 2.2982 1.8269 -0.0385 0.3689  0.1139  118 LEU E CB  
12568 C CG  . LEU E 118 ? 2.2944 2.3016 1.8410 -0.0329 0.3457  0.1110  118 LEU E CG  
12569 C CD1 . LEU E 118 ? 2.3165 2.3195 1.8481 -0.0250 0.3382  0.1018  118 LEU E CD1 
12570 C CD2 . LEU E 118 ? 2.2579 2.2468 1.7873 -0.0350 0.3317  0.1204  118 LEU E CD2 
12571 N N   . LYS E 119 ? 2.3305 2.3592 1.8918 -0.0539 0.4179  0.1200  119 LYS E N   
12572 C CA  . LYS E 119 ? 2.3104 2.3383 1.8588 -0.0587 0.4411  0.1214  119 LYS E CA  
12573 C C   . LYS E 119 ? 2.3799 2.3982 1.9205 -0.0682 0.4493  0.1334  119 LYS E C   
12574 O O   . LYS E 119 ? 2.3900 2.3898 1.8949 -0.0716 0.4589  0.1392  119 LYS E O   
12575 C CB  . LYS E 119 ? 2.1933 2.2481 1.7778 -0.0581 0.4548  0.1132  119 LYS E CB  
12576 C CG  . LYS E 119 ? 2.1078 2.1714 1.6986 -0.0489 0.4495  0.1012  119 LYS E CG  
12577 C CD  . LYS E 119 ? 2.0085 2.0869 1.6095 -0.0482 0.4701  0.0939  119 LYS E CD  
12578 C CE  . LYS E 119 ? 1.9967 2.0591 1.5598 -0.0517 0.4872  0.0972  119 LYS E CE  
12579 N NZ  . LYS E 119 ? 2.0831 2.1212 1.6022 -0.0470 0.4775  0.0965  119 LYS E NZ  
12580 N N   . GLU E 120 ? 2.4534 2.4837 2.0268 -0.0727 0.4458  0.1373  120 GLU E N   
12581 C CA  . GLU E 120 ? 2.5037 2.5265 2.0746 -0.0821 0.4535  0.1484  120 GLU E CA  
12582 C C   . GLU E 120 ? 2.5223 2.5194 2.0643 -0.0830 0.4386  0.1578  120 GLU E C   
12583 O O   . GLU E 120 ? 2.5306 2.5204 2.0726 -0.0905 0.4416  0.1674  120 GLU E O   
12584 C CB  . GLU E 120 ? 2.4934 2.5389 2.1112 -0.0866 0.4551  0.1484  120 GLU E CB  
12585 C CG  . GLU E 120 ? 2.4814 2.5528 2.1296 -0.0866 0.4709  0.1402  120 GLU E CG  
12586 C CD  . GLU E 120 ? 2.5405 2.6342 2.2344 -0.0912 0.4718  0.1403  120 GLU E CD  
12587 O OE1 . GLU E 120 ? 2.5235 2.6124 2.2253 -0.0943 0.4600  0.1463  120 GLU E OE1 
12588 O OE2 . GLU E 120 ? 2.5738 2.6898 2.2957 -0.0915 0.4841  0.1341  120 GLU E OE2 
12589 N N   . MET E 121 ? 2.4932 2.4767 2.0112 -0.0757 0.4227  0.1552  121 MET E N   
12590 C CA  . MET E 121 ? 2.5232 2.4809 2.0096 -0.0759 0.4091  0.1639  121 MET E CA  
12591 C C   . MET E 121 ? 2.5732 2.5077 2.0115 -0.0769 0.4182  0.1684  121 MET E C   
12592 O O   . MET E 121 ? 2.6132 2.5265 2.0258 -0.0810 0.4157  0.1790  121 MET E O   
12593 C CB  . MET E 121 ? 2.5062 2.4615 1.9936 -0.0675 0.3853  0.1589  121 MET E CB  
12594 C CG  . MET E 121 ? 2.5830 2.5155 2.0473 -0.0674 0.3685  0.1677  121 MET E CG  
12595 S SD  . MET E 121 ? 2.6227 2.5532 2.0876 -0.0574 0.3416  0.1610  121 MET E SD  
12596 C CE  . MET E 121 ? 2.5789 2.5427 2.0982 -0.0552 0.3404  0.1511  121 MET E CE  
12597 N N   . LEU E 122 ? 2.5481 2.4858 1.9731 -0.0733 0.4286  0.1607  122 LEU E N   
12598 C CA  . LEU E 122 ? 2.5793 2.4964 1.9589 -0.0747 0.4397  0.1645  122 LEU E CA  
12599 C C   . LEU E 122 ? 2.6370 2.5514 2.0131 -0.0847 0.4600  0.1738  122 LEU E C   
12600 O O   . LEU E 122 ? 2.7059 2.5973 2.0449 -0.0885 0.4636  0.1832  122 LEU E O   
12601 C CB  . LEU E 122 ? 2.5351 2.4588 1.9054 -0.0688 0.4481  0.1532  122 LEU E CB  
12602 C CG  . LEU E 122 ? 2.4815 2.3968 1.8336 -0.0593 0.4303  0.1456  122 LEU E CG  
12603 C CD1 . LEU E 122 ? 2.4194 2.3515 1.8090 -0.0541 0.4130  0.1391  122 LEU E CD1 
12604 C CD2 . LEU E 122 ? 2.4748 2.3912 1.8088 -0.0551 0.4426  0.1362  122 LEU E CD2 
12605 N N   . GLU E 123 ? 2.6649 2.6025 2.0793 -0.0893 0.4735  0.1714  123 GLU E N   
12606 C CA  . GLU E 123 ? 2.7549 2.6916 2.1714 -0.0996 0.4918  0.1805  123 GLU E CA  
12607 C C   . GLU E 123 ? 2.7737 2.6955 2.1873 -0.1049 0.4811  0.1924  123 GLU E C   
12608 O O   . GLU E 123 ? 2.8380 2.7446 2.2308 -0.1124 0.4917  0.2029  123 GLU E O   
12609 C CB  . GLU E 123 ? 2.7722 2.7385 2.2344 -0.1029 0.5060  0.1748  123 GLU E CB  
12610 C CG  . GLU E 123 ? 2.8477 2.8155 2.3126 -0.1136 0.5283  0.1823  123 GLU E CG  
12611 C CD  . GLU E 123 ? 2.8681 2.8664 2.3787 -0.1163 0.5421  0.1757  123 GLU E CD  
12612 O OE1 . GLU E 123 ? 2.8481 2.8656 2.3928 -0.1112 0.5313  0.1676  123 GLU E OE1 
12613 O OE2 . GLU E 123 ? 2.8752 2.8783 2.3875 -0.1237 0.5637  0.1787  123 GLU E OE2 
12614 N N   . PHE E 124 ? 2.6548 2.5805 2.0891 -0.1010 0.4602  0.1911  124 PHE E N   
12615 C CA  . PHE E 124 ? 2.6607 2.5698 2.0886 -0.1044 0.4474  0.2017  124 PHE E CA  
12616 C C   . PHE E 124 ? 2.7214 2.6002 2.0999 -0.1016 0.4378  0.2082  124 PHE E C   
12617 O O   . PHE E 124 ? 2.7393 2.5999 2.1043 -0.1052 0.4306  0.2188  124 PHE E O   
12618 C CB  . PHE E 124 ? 2.6065 2.5287 2.0696 -0.1004 0.4278  0.1976  124 PHE E CB  
12619 C CG  . PHE E 124 ? 2.6014 2.5101 2.0653 -0.1043 0.4158  0.2077  124 PHE E CG  
12620 C CD1 . PHE E 124 ? 2.5939 2.5019 2.0687 -0.1141 0.4276  0.2162  124 PHE E CD1 
12621 C CD2 . PHE E 124 ? 2.5844 2.4812 2.0390 -0.0982 0.3930  0.2084  124 PHE E CD2 
12622 C CE1 . PHE E 124 ? 2.5812 2.4760 2.0570 -0.1175 0.4165  0.2251  124 PHE E CE1 
12623 C CE2 . PHE E 124 ? 2.5937 2.4781 2.0497 -0.1013 0.3820  0.2173  124 PHE E CE2 
12624 C CZ  . PHE E 124 ? 2.5794 2.4624 2.0457 -0.1109 0.3937  0.2256  124 PHE E CZ  
12625 N N   . HIS E 125 ? 2.7015 2.5744 2.0530 -0.0950 0.4371  0.2018  125 HIS E N   
12626 C CA  . HIS E 125 ? 2.7465 2.5911 2.0486 -0.0921 0.4291  0.2072  125 HIS E CA  
12627 C C   . HIS E 125 ? 2.8046 2.6352 2.0711 -0.0975 0.4498  0.2130  125 HIS E C   
12628 O O   . HIS E 125 ? 2.8102 2.6155 2.0405 -0.1002 0.4477  0.2237  125 HIS E O   
12629 C CB  . HIS E 125 ? 2.7131 2.5577 2.0040 -0.0817 0.4151  0.1966  125 HIS E CB  
12630 C CG  . HIS E 125 ? 2.7406 2.5571 1.9833 -0.0779 0.4034  0.2012  125 HIS E CG  
12631 N ND1 . HIS E 125 ? 2.7377 2.5384 1.9713 -0.0760 0.3828  0.2078  125 HIS E ND1 
12632 C CD2 . HIS E 125 ? 2.7355 2.5369 1.9364 -0.0755 0.4092  0.2000  125 HIS E CD2 
12633 C CE1 . HIS E 125 ? 2.7359 2.5131 1.9245 -0.0725 0.3760  0.2107  125 HIS E CE1 
12634 N NE2 . HIS E 125 ? 2.7330 2.5099 1.9004 -0.0722 0.3917  0.2060  125 HIS E NE2 
12635 N N   . LYS E 126 ? 2.8411 2.6879 2.1173 -0.0990 0.4699  0.2063  126 LYS E N   
12636 C CA  . LYS E 126 ? 2.9028 2.7392 2.1473 -0.1040 0.4915  0.2104  126 LYS E CA  
12637 C C   . LYS E 126 ? 3.0974 2.9358 2.3539 -0.1153 0.5092  0.2204  126 LYS E C   
12638 O O   . LYS E 126 ? 3.1367 2.9751 2.3799 -0.1204 0.5314  0.2221  126 LYS E O   
12639 C CB  . LYS E 126 ? 2.7973 2.6502 2.0462 -0.0998 0.5051  0.1978  126 LYS E CB  
12640 C CG  . LYS E 126 ? 2.6988 2.5457 1.9271 -0.0892 0.4905  0.1883  126 LYS E CG  
12641 C CD  . LYS E 126 ? 2.6370 2.4981 1.8669 -0.0856 0.5059  0.1763  126 LYS E CD  
12642 C CE  . LYS E 126 ? 2.5997 2.4530 1.8066 -0.0755 0.4919  0.1670  126 LYS E CE  
12643 N NZ  . LYS E 126 ? 2.6757 2.5408 1.8816 -0.0719 0.5074  0.1553  126 LYS E NZ  
12644 N N   . SER E 127 ? 3.5277 3.3678 2.8093 -0.1194 0.5001  0.2270  127 SER E N   
12645 C CA  . SER E 127 ? 3.5286 3.3698 2.8237 -0.1305 0.5149  0.2366  127 SER E CA  
12646 C C   . SER E 127 ? 3.5633 3.3752 2.8267 -0.1353 0.5089  0.2515  127 SER E C   
12647 O O   . SER E 127 ? 3.5921 3.3915 2.8334 -0.1431 0.5259  0.2607  127 SER E O   
12648 C CB  . SER E 127 ? 3.4882 3.3543 2.8381 -0.1327 0.5109  0.2329  127 SER E CB  
12649 O OG  . SER E 127 ? 3.5265 3.3946 2.8914 -0.1436 0.5255  0.2415  127 SER E OG  
12650 N N   . HIS E 128 ? 3.1794 2.9797 2.4403 -0.1307 0.4852  0.2542  128 HIS E N   
12651 C CA  . HIS E 128 ? 3.1211 2.8925 2.3517 -0.1338 0.4768  0.2679  128 HIS E CA  
12652 C C   . HIS E 128 ? 3.0720 2.8184 2.2512 -0.1275 0.4674  0.2700  128 HIS E C   
12653 O O   . HIS E 128 ? 3.0638 2.7837 2.2102 -0.1302 0.4632  0.2822  128 HIS E O   
12654 C CB  . HIS E 128 ? 3.0077 2.7803 2.2656 -0.1326 0.4561  0.2701  128 HIS E CB  
12655 C CG  . HIS E 128 ? 2.8943 2.6800 2.1709 -0.1223 0.4364  0.2586  128 HIS E CG  
12656 N ND1 . HIS E 128 ? 2.8685 2.6558 2.1273 -0.1140 0.4325  0.2493  128 HIS E ND1 
12657 C CD2 . HIS E 128 ? 2.7804 2.5785 2.0921 -0.1193 0.4198  0.2547  128 HIS E CD2 
12658 C CE1 . HIS E 128 ? 2.7821 2.5818 2.0644 -0.1065 0.4143  0.2406  128 HIS E CE1 
12659 N NE2 . HIS E 128 ? 2.7343 2.5410 2.0487 -0.1094 0.4066  0.2437  128 HIS E NE2 
12660 N N   . GLY E 129 ? 3.0135 2.7671 2.1850 -0.1190 0.4635  0.2585  129 GLY E N   
12661 C CA  . GLY E 129 ? 2.9984 2.7295 2.1216 -0.1128 0.4545  0.2592  129 GLY E CA  
12662 C C   . GLY E 129 ? 2.9862 2.7027 2.1003 -0.1062 0.4268  0.2614  129 GLY E C   
12663 O O   . GLY E 129 ? 3.0316 2.7222 2.1024 -0.1040 0.4187  0.2682  129 GLY E O   
12664 N N   . GLY E 130 ? 2.9389 2.6715 2.0927 -0.1028 0.4118  0.2559  130 GLY E N   
12665 C CA  . GLY E 130 ? 2.8945 2.6156 2.0432 -0.0961 0.3854  0.2570  130 GLY E CA  
12666 C C   . GLY E 130 ? 2.8782 2.5935 2.0011 -0.0865 0.3732  0.2487  130 GLY E C   
12667 O O   . GLY E 130 ? 2.8378 2.5594 1.9495 -0.0844 0.3844  0.2408  130 GLY E O   
12668 N N   . GLU E 131 ? 2.9299 2.6329 2.0442 -0.0804 0.3493  0.2501  131 GLU E N   
12669 C CA  . GLU E 131 ? 2.9482 2.6447 2.0392 -0.0712 0.3347  0.2424  131 GLU E CA  
12670 C C   . GLU E 131 ? 2.9095 2.6274 2.0372 -0.0642 0.3196  0.2302  131 GLU E C   
12671 O O   . GLU E 131 ? 2.8523 2.5779 1.9763 -0.0583 0.3179  0.2192  131 GLU E O   
12672 C CB  . GLU E 131 ? 2.9925 2.6595 2.0443 -0.0684 0.3176  0.2519  131 GLU E CB  
12673 C CG  . GLU E 131 ? 2.9737 2.6319 1.9974 -0.0593 0.3026  0.2445  131 GLU E CG  
12674 C CD  . GLU E 131 ? 2.9597 2.5945 1.9585 -0.0551 0.2797  0.2520  131 GLU E CD  
12675 O OE1 . GLU E 131 ? 3.0785 2.7042 2.0835 -0.0589 0.2750  0.2627  131 GLU E OE1 
12676 O OE2 . GLU E 131 ? 2.9083 2.5338 1.8818 -0.0479 0.2662  0.2469  131 GLU E OE2 
12677 N N   . ALA E 132 ? 2.8463 2.5737 2.0093 -0.0649 0.3089  0.2317  132 ALA E N   
12678 C CA  . ALA E 132 ? 2.7458 2.4925 1.9434 -0.0585 0.2937  0.2213  132 ALA E CA  
12679 C C   . ALA E 132 ? 2.6793 2.4497 1.9260 -0.0631 0.3006  0.2196  132 ALA E C   
12680 O O   . ALA E 132 ? 2.6973 2.4641 1.9520 -0.0702 0.3077  0.2288  132 ALA E O   
12681 C CB  . ALA E 132 ? 2.7095 2.4425 1.8989 -0.0527 0.2678  0.2239  132 ALA E CB  
12682 N N   . SER E 133 ? 2.7201 2.5143 1.9994 -0.0590 0.2980  0.2079  133 SER E N   
12683 C CA  . SER E 133 ? 2.7186 2.5376 2.0452 -0.0626 0.3042  0.2048  133 SER E CA  
12684 C C   . SER E 133 ? 2.7670 2.6015 2.1241 -0.0561 0.2858  0.1963  133 SER E C   
12685 O O   . SER E 133 ? 2.9026 2.7400 2.2536 -0.0491 0.2775  0.1877  133 SER E O   
12686 C CB  . SER E 133 ? 2.7299 2.5668 2.0692 -0.0657 0.3263  0.1986  133 SER E CB  
12687 O OG  . SER E 133 ? 2.6752 2.5357 2.0599 -0.0693 0.3321  0.1960  133 SER E OG  
12688 N N   . ILE E 134 ? 2.6178 2.4621 2.0076 -0.0584 0.2798  0.1987  134 ILE E N   
12689 C CA  . ILE E 134 ? 2.7124 2.5748 2.1366 -0.0534 0.2651  0.1908  134 ILE E CA  
12690 C C   . ILE E 134 ? 2.7133 2.5999 2.1804 -0.0582 0.2757  0.1884  134 ILE E C   
12691 O O   . ILE E 134 ? 2.6658 2.5529 2.1366 -0.0657 0.2915  0.1941  134 ILE E O   
12692 C CB  . ILE E 134 ? 2.7700 2.6202 2.1920 -0.0502 0.2433  0.1953  134 ILE E CB  
12693 C CG1 . ILE E 134 ? 2.7333 2.5778 2.1656 -0.0569 0.2457  0.2053  134 ILE E CG1 
12694 C CG2 . ILE E 134 ? 2.8464 2.6718 2.2249 -0.0456 0.2326  0.1985  134 ILE E CG2 
12695 C CD1 . ILE E 134 ? 2.7822 2.6172 2.2177 -0.0537 0.2249  0.2091  134 ILE E CD1 
12696 N N   . MET E 135 ? 2.7718 2.6788 2.2717 -0.0539 0.2667  0.1798  135 MET E N   
12697 C CA  . MET E 135 ? 2.7572 2.6883 2.2996 -0.0575 0.2736  0.1767  135 MET E CA  
12698 C C   . MET E 135 ? 2.7599 2.6946 2.3259 -0.0568 0.2574  0.1783  135 MET E C   
12699 O O   . MET E 135 ? 2.8027 2.7302 2.3619 -0.0509 0.2393  0.1771  135 MET E O   
12700 C CB  . MET E 135 ? 2.8487 2.8024 2.4125 -0.0535 0.2779  0.1652  135 MET E CB  
12701 C CG  . MET E 135 ? 2.8325 2.7865 2.3797 -0.0548 0.2965  0.1627  135 MET E CG  
12702 S SD  . MET E 135 ? 2.6618 2.6159 2.2108 -0.0653 0.3199  0.1706  135 MET E SD  
12703 C CE  . MET E 135 ? 2.7756 2.7601 2.3797 -0.0681 0.3226  0.1660  135 MET E CE  
12704 N N   . VAL E 136 ? 2.7810 2.7274 2.3754 -0.0627 0.2642  0.1808  136 VAL E N   
12705 C CA  . VAL E 136 ? 2.7495 2.6979 2.3653 -0.0633 0.2513  0.1834  136 VAL E CA  
12706 C C   . VAL E 136 ? 2.6873 2.6632 2.3469 -0.0652 0.2555  0.1773  136 VAL E C   
12707 O O   . VAL E 136 ? 2.7200 2.7082 2.3925 -0.0701 0.2723  0.1762  136 VAL E O   
12708 C CB  . VAL E 136 ? 2.6940 2.6225 2.2949 -0.0697 0.2541  0.1949  136 VAL E CB  
12709 C CG1 . VAL E 136 ? 2.8219 2.7547 2.4490 -0.0708 0.2427  0.1967  136 VAL E CG1 
12710 C CG2 . VAL E 136 ? 2.7052 2.6057 2.2624 -0.0671 0.2471  0.2013  136 VAL E CG2 
12711 N N   . THR E 137 ? 2.6201 2.6060 2.3029 -0.0612 0.2401  0.1732  137 THR E N   
12712 C CA  . THR E 137 ? 2.5114 2.5227 2.2354 -0.0625 0.2416  0.1676  137 THR E CA  
12713 C C   . THR E 137 ? 2.5459 2.5560 2.2868 -0.0641 0.2302  0.1710  137 THR E C   
12714 O O   . THR E 137 ? 2.7429 2.7378 2.4693 -0.0605 0.2155  0.1741  137 THR E O   
12715 C CB  . THR E 137 ? 2.4868 2.5161 2.2266 -0.0555 0.2347  0.1575  137 THR E CB  
12716 O OG1 . THR E 137 ? 2.3824 2.4352 2.1615 -0.0566 0.2343  0.1528  137 THR E OG1 
12717 C CG2 . THR E 137 ? 2.5773 2.5961 2.3034 -0.0483 0.2153  0.1561  137 THR E CG2 
12718 N N   . LYS E 138 ? 2.3711 2.3972 2.1426 -0.0693 0.2370  0.1703  138 LYS E N   
12719 C CA  . LYS E 138 ? 2.3425 2.3696 2.1333 -0.0711 0.2274  0.1725  138 LYS E CA  
12720 C C   . LYS E 138 ? 2.2511 2.2933 2.0641 -0.0645 0.2120  0.1649  138 LYS E C   
12721 O O   . LYS E 138 ? 2.2438 2.3052 2.0731 -0.0614 0.2137  0.1573  138 LYS E O   
12722 C CB  . LYS E 138 ? 2.2902 2.3294 2.1060 -0.0793 0.2404  0.1738  138 LYS E CB  
12723 C CG  . LYS E 138 ? 2.2029 2.2677 2.0430 -0.0797 0.2513  0.1663  138 LYS E CG  
12724 C CD  . LYS E 138 ? 2.1297 2.2101 2.0012 -0.0868 0.2596  0.1661  138 LYS E CD  
12725 C CE  . LYS E 138 ? 2.0333 2.1399 1.9301 -0.0862 0.2687  0.1582  138 LYS E CE  
12726 N NZ  . LYS E 138 ? 2.0677 2.1878 1.9763 -0.0780 0.2563  0.1503  138 LYS E NZ  
12727 N N   . VAL E 139 ? 2.2883 2.3217 2.1019 -0.0624 0.1972  0.1671  139 VAL E N   
12728 C CA  . VAL E 139 ? 2.2762 2.3230 2.1110 -0.0566 0.1824  0.1606  139 VAL E CA  
12729 C C   . VAL E 139 ? 2.2583 2.3074 2.1142 -0.0597 0.1766  0.1625  139 VAL E C   
12730 O O   . VAL E 139 ? 2.2722 2.3047 2.1175 -0.0641 0.1783  0.1699  139 VAL E O   
12731 C CB  . VAL E 139 ? 2.4598 2.4942 2.2734 -0.0490 0.1671  0.1598  139 VAL E CB  
12732 C CG1 . VAL E 139 ? 2.4992 2.5338 2.2952 -0.0456 0.1720  0.1563  139 VAL E CG1 
12733 C CG2 . VAL E 139 ? 2.5730 2.5808 2.3604 -0.0497 0.1608  0.1684  139 VAL E CG2 
12734 N N   . ASP E 140 ? 2.1427 2.2122 2.0283 -0.0573 0.1699  0.1557  140 ASP E N   
12735 C CA  . ASP E 140 ? 2.1223 2.1953 2.0291 -0.0595 0.1636  0.1562  140 ASP E CA  
12736 C C   . ASP E 140 ? 2.2789 2.3355 2.1735 -0.0551 0.1473  0.1588  140 ASP E C   
12737 O O   . ASP E 140 ? 2.2393 2.2888 2.1406 -0.0577 0.1432  0.1622  140 ASP E O   
12738 C CB  . ASP E 140 ? 2.0136 2.1139 1.9548 -0.0582 0.1616  0.1479  140 ASP E CB  
12739 C CG  . ASP E 140 ? 1.9519 2.0696 1.9071 -0.0620 0.1768  0.1449  140 ASP E CG  
12740 O OD1 . ASP E 140 ? 1.9649 2.0755 1.9111 -0.0680 0.1901  0.1496  140 ASP E OD1 
12741 O OD2 . ASP E 140 ? 1.8928 2.0313 1.8680 -0.0589 0.1755  0.1379  140 ASP E OD2 
12742 N N   . GLU E 141 ? 2.7777 2.8282 2.6553 -0.0483 0.1377  0.1572  141 GLU E N   
12743 C CA  . GLU E 141 ? 2.8070 2.8429 2.6730 -0.0431 0.1215  0.1591  141 GLU E CA  
12744 C C   . GLU E 141 ? 2.8391 2.8498 2.6676 -0.0421 0.1211  0.1659  141 GLU E C   
12745 O O   . GLU E 141 ? 2.8428 2.8511 2.6549 -0.0374 0.1178  0.1635  141 GLU E O   
12746 C CB  . GLU E 141 ? 2.7904 2.8405 2.6690 -0.0359 0.1090  0.1513  141 GLU E CB  
12747 N N   . PRO E 142 ? 2.5574 2.5482 2.3704 -0.0465 0.1242  0.1743  142 PRO E N   
12748 C CA  . PRO E 142 ? 2.5605 2.5263 2.3359 -0.0453 0.1231  0.1813  142 PRO E CA  
12749 C C   . PRO E 142 ? 2.5260 2.4777 2.2884 -0.0385 0.1045  0.1826  142 PRO E C   
12750 O O   . PRO E 142 ? 2.5055 2.4389 2.2367 -0.0359 0.1011  0.1866  142 PRO E O   
12751 C CB  . PRO E 142 ? 2.5068 2.4580 2.2740 -0.0532 0.1339  0.1902  142 PRO E CB  
12752 C CG  . PRO E 142 ? 2.4470 2.4093 2.2458 -0.0561 0.1318  0.1884  142 PRO E CG  
12753 C CD  . PRO E 142 ? 2.4651 2.4556 2.2937 -0.0532 0.1302  0.1781  142 PRO E CD  
12754 N N   . SER E 143 ? 2.5285 2.4883 2.3134 -0.0354 0.0924  0.1789  143 SER E N   
12755 C CA  . SER E 143 ? 2.4827 2.4298 2.2571 -0.0288 0.0746  0.1800  143 SER E CA  
12756 C C   . SER E 143 ? 2.4902 2.4436 2.2579 -0.0218 0.0661  0.1739  143 SER E C   
12757 O O   . SER E 143 ? 2.4553 2.3923 2.1992 -0.0172 0.0557  0.1765  143 SER E O   
12758 C CB  . SER E 143 ? 2.4315 2.3862 2.2331 -0.0275 0.0650  0.1775  143 SER E CB  
12759 O OG  . SER E 143 ? 2.4682 2.4495 2.2999 -0.0262 0.0648  0.1683  143 SER E OG  
12760 N N   . LYS E 144 ? 2.4809 2.4575 2.2691 -0.0211 0.0701  0.1658  144 LYS E N   
12761 C CA  . LYS E 144 ? 2.4931 2.4762 2.2767 -0.0149 0.0624  0.1597  144 LYS E CA  
12762 C C   . LYS E 144 ? 2.5306 2.5016 2.2830 -0.0148 0.0686  0.1618  144 LYS E C   
12763 O O   . LYS E 144 ? 2.5309 2.5029 2.2745 -0.0095 0.0612  0.1574  144 LYS E O   
12764 C CB  . LYS E 144 ? 2.4790 2.4898 2.2933 -0.0144 0.0652  0.1509  144 LYS E CB  
12765 C CG  . LYS E 144 ? 2.3913 2.4161 2.2368 -0.0141 0.0588  0.1477  144 LYS E CG  
12766 C CD  . LYS E 144 ? 2.2766 2.3281 2.1499 -0.0138 0.0625  0.1396  144 LYS E CD  
12767 C CE  . LYS E 144 ? 2.2285 2.2860 2.0978 -0.0078 0.0548  0.1340  144 LYS E CE  
12768 N NZ  . LYS E 144 ? 2.1288 2.2115 2.0248 -0.0073 0.0579  0.1265  144 LYS E NZ  
12769 N N   . TYR E 145 ? 2.5411 2.5004 2.2766 -0.0204 0.0820  0.1681  145 TYR E N   
12770 C CA  . TYR E 145 ? 2.6107 2.5581 2.3155 -0.0208 0.0898  0.1704  145 TYR E CA  
12771 C C   . TYR E 145 ? 2.5674 2.4870 2.2406 -0.0226 0.0889  0.1805  145 TYR E C   
12772 O O   . TYR E 145 ? 2.4812 2.3914 2.1580 -0.0236 0.0829  0.1857  145 TYR E O   
12773 C CB  . TYR E 145 ? 2.7418 2.7020 2.4544 -0.0262 0.1089  0.1685  145 TYR E CB  
12774 C CG  . TYR E 145 ? 2.7375 2.7252 2.4825 -0.0251 0.1110  0.1594  145 TYR E CG  
12775 C CD1 . TYR E 145 ? 2.6743 2.6716 2.4261 -0.0187 0.0997  0.1522  145 TYR E CD1 
12776 C CD2 . TYR E 145 ? 2.7232 2.7271 2.4921 -0.0306 0.1242  0.1581  145 TYR E CD2 
12777 C CE1 . TYR E 145 ? 2.6289 2.6505 2.4095 -0.0177 0.1018  0.1444  145 TYR E CE1 
12778 C CE2 . TYR E 145 ? 2.6153 2.6438 2.4129 -0.0294 0.1258  0.1502  145 TYR E CE2 
12779 C CZ  . TYR E 145 ? 2.5975 2.6345 2.4005 -0.0229 0.1147  0.1436  145 TYR E CZ  
12780 O OH  . TYR E 145 ? 2.5329 2.5936 2.3638 -0.0218 0.1163  0.1362  145 TYR E OH  
12781 N N   . GLY E 146 ? 2.6302 2.5362 2.2718 -0.0228 0.0951  0.1833  146 GLY E N   
12782 C CA  . GLY E 146 ? 2.5399 2.4193 2.1488 -0.0251 0.0965  0.1934  146 GLY E CA  
12783 C C   . GLY E 146 ? 2.7578 2.6348 2.3644 -0.0335 0.1159  0.1991  146 GLY E C   
12784 O O   . GLY E 146 ? 2.9843 2.8685 2.5866 -0.0362 0.1302  0.1967  146 GLY E O   
12785 N N   . VAL E 147 ? 2.6414 2.5081 2.2512 -0.0379 0.1167  0.2066  147 VAL E N   
12786 C CA  . VAL E 147 ? 2.8692 2.7356 2.4823 -0.0466 0.1348  0.2118  147 VAL E CA  
12787 C C   . VAL E 147 ? 3.0664 2.9096 2.6400 -0.0497 0.1438  0.2204  147 VAL E C   
12788 O O   . VAL E 147 ? 2.8261 2.6466 2.3712 -0.0466 0.1336  0.2266  147 VAL E O   
12789 C CB  . VAL E 147 ? 2.6669 2.5319 2.3010 -0.0504 0.1320  0.2159  147 VAL E CB  
12790 C CG1 . VAL E 147 ? 2.8726 2.7390 2.5131 -0.0599 0.1509  0.2206  147 VAL E CG1 
12791 C CG2 . VAL E 147 ? 2.5131 2.4008 2.1845 -0.0470 0.1228  0.2070  147 VAL E CG2 
12792 N N   . VAL E 148 ? 3.8481 3.6971 3.4197 -0.0557 0.1630  0.2209  148 VAL E N   
12793 C CA  . VAL E 148 ? 3.8721 3.7013 3.4083 -0.0599 0.1750  0.2291  148 VAL E CA  
12794 C C   . VAL E 148 ? 3.8739 3.6977 3.4175 -0.0690 0.1875  0.2372  148 VAL E C   
12795 O O   . VAL E 148 ? 3.8505 3.6934 3.4227 -0.0742 0.1994  0.2337  148 VAL E O   
12796 C CB  . VAL E 148 ? 3.8647 3.7040 3.3921 -0.0600 0.1885  0.2234  148 VAL E CB  
12797 C CG1 . VAL E 148 ? 3.8863 3.7059 3.3778 -0.0649 0.2026  0.2319  148 VAL E CG1 
12798 C CG2 . VAL E 148 ? 3.8650 3.7084 3.3848 -0.0511 0.1756  0.2154  148 VAL E CG2 
12799 N N   . VAL E 149 ? 3.4530 3.2507 2.9712 -0.0710 0.1845  0.2480  149 VAL E N   
12800 C CA  . VAL E 149 ? 3.4005 3.1894 2.9236 -0.0797 0.1945  0.2568  149 VAL E CA  
12801 C C   . VAL E 149 ? 3.2972 3.0754 2.7933 -0.0863 0.2139  0.2633  149 VAL E C   
12802 O O   . VAL E 149 ? 3.1631 2.9165 2.6213 -0.0859 0.2129  0.2717  149 VAL E O   
12803 C CB  . VAL E 149 ? 3.3140 3.0806 2.8276 -0.0783 0.1799  0.2650  149 VAL E CB  
12804 C CG1 . VAL E 149 ? 3.1531 2.9346 2.7036 -0.0751 0.1667  0.2588  149 VAL E CG1 
12805 C CG2 . VAL E 149 ? 3.2035 2.9494 2.6804 -0.0709 0.1662  0.2683  149 VAL E CG2 
12806 N N   . MET E 150 ? 3.4064 3.2037 2.9220 -0.0921 0.2315  0.2593  150 MET E N   
12807 C CA  . MET E 150 ? 3.3934 3.1843 2.8894 -0.0991 0.2522  0.2647  150 MET E CA  
12808 C C   . MET E 150 ? 3.3861 3.1779 2.9006 -0.1094 0.2649  0.2708  150 MET E C   
12809 O O   . MET E 150 ? 3.3726 3.1757 2.9201 -0.1108 0.2595  0.2683  150 MET E O   
12810 C CB  . MET E 150 ? 3.3726 3.1852 2.8760 -0.0979 0.2640  0.2550  150 MET E CB  
12811 C CG  . MET E 150 ? 3.3377 3.1810 2.8871 -0.0980 0.2652  0.2449  150 MET E CG  
12812 S SD  . MET E 150 ? 3.3873 3.2553 2.9457 -0.0948 0.2759  0.2330  150 MET E SD  
12813 C CE  . MET E 150 ? 3.3052 3.1701 2.8509 -0.1047 0.3029  0.2389  150 MET E CE  
12814 N N   . GLU E 151 ? 2.7044 2.4841 2.1971 -0.1167 0.2822  0.2788  151 GLU E N   
12815 C CA  . GLU E 151 ? 2.4509 2.2328 1.9609 -0.1273 0.2972  0.2843  151 GLU E CA  
12816 C C   . GLU E 151 ? 2.3504 2.1608 1.8880 -0.1311 0.3140  0.2758  151 GLU E C   
12817 O O   . GLU E 151 ? 2.3715 2.1910 1.8994 -0.1278 0.3206  0.2699  151 GLU E O   
12818 C CB  . GLU E 151 ? 2.2901 2.0446 1.7639 -0.1340 0.3082  0.2977  151 GLU E CB  
12819 C CG  . GLU E 151 ? 2.2510 2.0066 1.7029 -0.1372 0.3277  0.2982  151 GLU E CG  
12820 C CD  . GLU E 151 ? 2.3672 2.1134 1.7840 -0.1286 0.3206  0.2958  151 GLU E CD  
12821 O OE1 . GLU E 151 ? 2.4619 2.1886 1.8568 -0.1227 0.3031  0.2999  151 GLU E OE1 
12822 O OE2 . GLU E 151 ? 2.3653 2.1236 1.7770 -0.1277 0.3322  0.2895  151 GLU E OE2 
12823 N N   . GLU E 152 ? 2.1248 1.9496 1.6977 -0.1378 0.3202  0.2748  152 GLU E N   
12824 C CA  . GLU E 152 ? 2.0214 1.8750 1.6259 -0.1415 0.3345  0.2665  152 GLU E CA  
12825 C C   . GLU E 152 ? 1.9682 1.8196 1.5627 -0.1509 0.3582  0.2721  152 GLU E C   
12826 O O   . GLU E 152 ? 1.9626 1.8327 1.5872 -0.1576 0.3710  0.2693  152 GLU E O   
12827 C CB  . GLU E 152 ? 1.9675 1.8387 1.6155 -0.1440 0.3290  0.2620  152 GLU E CB  
12828 N N   . SER E 153 ? 1.9938 1.8232 1.5470 -0.1515 0.3646  0.2797  153 SER E N   
12829 C CA  . SER E 153 ? 1.9849 1.8110 1.5259 -0.1605 0.3878  0.2855  153 SER E CA  
12830 C C   . SER E 153 ? 1.9781 1.8029 1.4896 -0.1567 0.3971  0.2829  153 SER E C   
12831 O O   . SER E 153 ? 1.9162 1.7547 1.4345 -0.1615 0.4165  0.2803  153 SER E O   
12832 C CB  . SER E 153 ? 1.9337 1.7308 1.4511 -0.1679 0.3906  0.3001  153 SER E CB  
12833 O OG  . SER E 153 ? 1.9688 1.7391 1.4455 -0.1618 0.3779  0.3064  153 SER E OG  
12834 N N   . THR E 154 ? 2.0421 1.8514 1.5218 -0.1483 0.3838  0.2831  154 THR E N   
12835 C CA  . THR E 154 ? 2.0581 1.8640 1.5070 -0.1442 0.3913  0.2804  154 THR E CA  
12836 C C   . THR E 154 ? 2.1551 1.9707 1.6049 -0.1327 0.3758  0.2694  154 THR E C   
12837 O O   . THR E 154 ? 2.1486 1.9779 1.5977 -0.1296 0.3841  0.2612  154 THR E O   
12838 C CB  . THR E 154 ? 2.0241 1.7971 1.4234 -0.1460 0.3929  0.2926  154 THR E CB  
12839 O OG1 . THR E 154 ? 2.0949 1.8485 1.4819 -0.1412 0.3711  0.2978  154 THR E OG1 
12840 C CG2 . THR E 154 ? 1.9796 1.7437 1.3749 -0.1580 0.4122  0.3033  154 THR E CG2 
12841 N N   . GLY E 155 ? 2.3616 2.1703 1.8134 -0.1264 0.3536  0.2690  155 GLY E N   
12842 C CA  . GLY E 155 ? 2.4760 2.2947 1.9320 -0.1159 0.3382  0.2587  155 GLY E CA  
12843 C C   . GLY E 155 ? 2.5852 2.3799 2.0032 -0.1088 0.3217  0.2623  155 GLY E C   
12844 O O   . GLY E 155 ? 2.6840 2.4830 2.0938 -0.1006 0.3130  0.2544  155 GLY E O   
12845 N N   . ARG E 156 ? 2.5305 2.2996 1.9257 -0.1116 0.3168  0.2740  156 ARG E N   
12846 C CA  . ARG E 156 ? 2.6509 2.3956 2.0091 -0.1051 0.3006  0.2785  156 ARG E CA  
12847 C C   . ARG E 156 ? 2.7918 2.5361 2.1677 -0.0993 0.2775  0.2770  156 ARG E C   
12848 O O   . ARG E 156 ? 2.7461 2.4947 2.1490 -0.1032 0.2751  0.2795  156 ARG E O   
12849 C CB  . ARG E 156 ? 2.6030 2.3185 1.9234 -0.1110 0.3080  0.2928  156 ARG E CB  
12850 C CG  . ARG E 156 ? 2.6766 2.3660 1.9525 -0.1045 0.2943  0.2977  156 ARG E CG  
12851 C CD  . ARG E 156 ? 2.7212 2.3820 1.9602 -0.1109 0.3028  0.3125  156 ARG E CD  
12852 N NE  . ARG E 156 ? 2.6457 2.3109 1.8781 -0.1191 0.3285  0.3146  156 ARG E NE  
12853 C CZ  . ARG E 156 ? 2.5665 2.2110 1.7710 -0.1266 0.3413  0.3270  156 ARG E CZ  
12854 N NH1 . ARG E 156 ? 2.6330 2.2498 1.8127 -0.1268 0.3305  0.3389  156 ARG E NH1 
12855 N NH2 . ARG E 156 ? 2.4865 2.1377 1.6879 -0.1340 0.3651  0.3278  156 ARG E NH2 
12856 N N   . VAL E 157 ? 3.2014 2.9410 2.5624 -0.0900 0.2605  0.2724  157 VAL E N   
12857 C CA  . VAL E 157 ? 3.1980 2.9386 2.5751 -0.0835 0.2382  0.2697  157 VAL E CA  
12858 C C   . VAL E 157 ? 3.2320 2.9421 2.5771 -0.0819 0.2255  0.2808  157 VAL E C   
12859 O O   . VAL E 157 ? 3.2586 2.9472 2.5648 -0.0839 0.2317  0.2890  157 VAL E O   
12860 C CB  . VAL E 157 ? 3.2574 3.0131 2.6419 -0.0743 0.2262  0.2574  157 VAL E CB  
12861 C CG1 . VAL E 157 ? 3.1849 2.9659 2.5896 -0.0758 0.2416  0.2478  157 VAL E CG1 
12862 C CG2 . VAL E 157 ? 3.3249 3.0602 2.6671 -0.0680 0.2164  0.2592  157 VAL E CG2 
12863 N N   . GLU E 158 ? 2.9850 2.6931 2.3465 -0.0781 0.2075  0.2812  158 GLU E N   
12864 C CA  . GLU E 158 ? 2.8823 2.5621 2.2189 -0.0769 0.1952  0.2922  158 GLU E CA  
12865 C C   . GLU E 158 ? 2.8104 2.4864 2.1458 -0.0668 0.1705  0.2884  158 GLU E C   
12866 O O   . GLU E 158 ? 2.8470 2.5012 2.1471 -0.0623 0.1602  0.2936  158 GLU E O   
12867 C CB  . GLU E 158 ? 2.7607 2.4361 2.1169 -0.0843 0.1996  0.2998  158 GLU E CB  
12868 C CG  . GLU E 158 ? 2.6909 2.3681 2.0473 -0.0950 0.2239  0.3048  158 GLU E CG  
12869 C CD  . GLU E 158 ? 2.4713 2.1448 1.8491 -0.1026 0.2279  0.3117  158 GLU E CD  
12870 O OE1 . GLU E 158 ? 2.4040 2.0765 1.8003 -0.0993 0.2122  0.3113  158 GLU E OE1 
12871 O OE2 . GLU E 158 ? 2.4229 2.0946 1.7993 -0.1120 0.2471  0.3174  158 GLU E OE2 
12872 N N   . LYS E 159 ? 2.6791 2.3761 2.0523 -0.0631 0.1606  0.2793  159 LYS E N   
12873 C CA  . LYS E 159 ? 2.5256 2.2200 1.9020 -0.0541 0.1374  0.2759  159 LYS E CA  
12874 C C   . LYS E 159 ? 2.4882 2.2118 1.8988 -0.0495 0.1323  0.2622  159 LYS E C   
12875 O O   . LYS E 159 ? 2.6573 2.4024 2.0919 -0.0535 0.1459  0.2561  159 LYS E O   
12876 C CB  . LYS E 159 ? 2.4778 2.1598 1.8646 -0.0547 0.1267  0.2831  159 LYS E CB  
12877 C CG  . LYS E 159 ? 2.4045 2.0718 1.7781 -0.0459 0.1034  0.2846  159 LYS E CG  
12878 C CD  . LYS E 159 ? 2.4226 2.0637 1.7478 -0.0436 0.1003  0.2923  159 LYS E CD  
12879 C CE  . LYS E 159 ? 2.3704 1.9964 1.6837 -0.0349 0.0765  0.2944  159 LYS E CE  
12880 N NZ  . LYS E 159 ? 2.3736 2.0198 1.7093 -0.0270 0.0622  0.2819  159 LYS E NZ  
12881 N N   . PHE E 160 ? 2.3793 2.1033 1.7917 -0.0410 0.1124  0.2574  160 PHE E N   
12882 C CA  . PHE E 160 ? 2.2595 2.0096 1.7038 -0.0361 0.1053  0.2450  160 PHE E CA  
12883 C C   . PHE E 160 ? 2.1994 1.9531 1.6702 -0.0330 0.0897  0.2441  160 PHE E C   
12884 O O   . PHE E 160 ? 2.1961 1.9331 1.6526 -0.0280 0.0736  0.2483  160 PHE E O   
12885 C CB  . PHE E 160 ? 2.2792 2.0298 1.7050 -0.0288 0.0962  0.2384  160 PHE E CB  
12886 C CG  . PHE E 160 ? 2.3403 2.0691 1.7391 -0.0224 0.0773  0.2429  160 PHE E CG  
12887 C CD1 . PHE E 160 ? 2.3091 2.0449 1.7231 -0.0148 0.0579  0.2367  160 PHE E CD1 
12888 C CD2 . PHE E 160 ? 2.4368 2.1383 1.7949 -0.0237 0.0790  0.2532  160 PHE E CD2 
12889 C CE1 . PHE E 160 ? 2.3229 2.0396 1.7136 -0.0087 0.0401  0.2405  160 PHE E CE1 
12890 C CE2 . PHE E 160 ? 2.4799 2.1615 1.8133 -0.0175 0.0609  0.2574  160 PHE E CE2 
12891 C CZ  . PHE E 160 ? 2.4205 2.1100 1.7708 -0.0098 0.0412  0.2508  160 PHE E CZ  
12892 N N   . VAL E 161 ? 2.2656 2.0412 1.7751 -0.0358 0.0945  0.2386  161 VAL E N   
12893 C CA  . VAL E 161 ? 2.2534 2.0350 1.7912 -0.0335 0.0819  0.2370  161 VAL E CA  
12894 C C   . VAL E 161 ? 2.3050 2.1142 1.8740 -0.0292 0.0766  0.2246  161 VAL E C   
12895 O O   . VAL E 161 ? 2.3041 2.1345 1.8994 -0.0332 0.0880  0.2192  161 VAL E O   
12896 C CB  . VAL E 161 ? 2.1733 1.9546 1.7293 -0.0413 0.0919  0.2422  161 VAL E CB  
12897 C CG1 . VAL E 161 ? 2.1501 1.9360 1.7333 -0.0383 0.0779  0.2401  161 VAL E CG1 
12898 C CG2 . VAL E 161 ? 2.1685 1.9224 1.6926 -0.0465 0.0994  0.2549  161 VAL E CG2 
12899 N N   . GLU E 162 ? 2.2928 2.1021 1.8593 -0.0211 0.0593  0.2201  162 GLU E N   
12900 C CA  . GLU E 162 ? 2.3377 2.1719 1.9328 -0.0167 0.0528  0.2089  162 GLU E CA  
12901 C C   . GLU E 162 ? 2.3419 2.1845 1.9679 -0.0150 0.0425  0.2068  162 GLU E C   
12902 O O   . GLU E 162 ? 2.3375 2.1637 1.9563 -0.0128 0.0313  0.2124  162 GLU E O   
12903 C CB  . GLU E 162 ? 2.3443 2.1755 1.9221 -0.0091 0.0399  0.2044  162 GLU E CB  
12904 C CG  . GLU E 162 ? 2.3470 2.1610 1.9118 -0.0028 0.0203  0.2080  162 GLU E CG  
12905 C CD  . GLU E 162 ? 2.3708 2.1552 1.8980 -0.0043 0.0206  0.2194  162 GLU E CD  
12906 O OE1 . GLU E 162 ? 2.3280 2.1050 1.8375 -0.0102 0.0365  0.2243  162 GLU E OE1 
12907 O OE2 . GLU E 162 ? 2.3918 2.1604 1.9074 0.0006  0.0049  0.2235  162 GLU E OE2 
12908 N N   . LYS E 163 ? 2.2943 2.1626 1.9545 -0.0160 0.0463  0.1987  163 LYS E N   
12909 C CA  . LYS E 163 ? 2.2352 2.1151 1.9275 -0.0151 0.0389  0.1955  163 LYS E CA  
12910 C C   . LYS E 163 ? 2.1940 2.0576 1.8844 -0.0195 0.0407  0.2040  163 LYS E C   
12911 O O   . LYS E 163 ? 2.1612 2.0106 1.8465 -0.0156 0.0272  0.2076  163 LYS E O   
12912 C CB  . LYS E 163 ? 2.2217 2.1042 1.9195 -0.0066 0.0194  0.1906  163 LYS E CB  
12913 C CG  . LYS E 163 ? 2.2023 2.0989 1.9341 -0.0048 0.0113  0.1859  163 LYS E CG  
12914 C CD  . LYS E 163 ? 2.2177 2.1400 1.9806 -0.0090 0.0224  0.1793  163 LYS E CD  
12915 C CE  . LYS E 163 ? 2.1435 2.0778 1.9378 -0.0078 0.0152  0.1754  163 LYS E CE  
12916 N NZ  . LYS E 163 ? 1.9776 1.8944 1.7689 -0.0105 0.0138  0.1827  163 LYS E NZ  
12917 N N   . PRO E 164 ? 2.2057 2.0702 1.9000 -0.0275 0.0570  0.2077  164 PRO E N   
12918 C CA  . PRO E 164 ? 2.1240 1.9736 1.8190 -0.0323 0.0591  0.2156  164 PRO E CA  
12919 C C   . PRO E 164 ? 2.1059 1.9714 1.8377 -0.0323 0.0542  0.2101  164 PRO E C   
12920 O O   . PRO E 164 ? 2.1203 2.0087 1.8783 -0.0352 0.0623  0.2034  164 PRO E O   
12921 C CB  . PRO E 164 ? 2.0753 1.9230 1.7623 -0.0412 0.0794  0.2203  164 PRO E CB  
12922 C CG  . PRO E 164 ? 2.1306 1.9892 1.8081 -0.0401 0.0868  0.2154  164 PRO E CG  
12923 C CD  . PRO E 164 ? 2.2117 2.0886 1.9070 -0.0328 0.0746  0.2054  164 PRO E CD  
12924 N N   . LYS E 165 ? 2.0110 1.8641 1.7446 -0.0288 0.0409  0.2129  165 LYS E N   
12925 C CA  . LYS E 165 ? 1.9769 1.8431 1.7440 -0.0289 0.0363  0.2079  165 LYS E CA  
12926 C C   . LYS E 165 ? 1.9775 1.8445 1.7574 -0.0380 0.0503  0.2111  165 LYS E C   
12927 O O   . LYS E 165 ? 1.9637 1.8511 1.7743 -0.0403 0.0538  0.2045  165 LYS E O   
12928 C CB  . LYS E 165 ? 1.9396 1.7913 1.7047 -0.0226 0.0187  0.2101  165 LYS E CB  
12929 C CG  . LYS E 165 ? 1.8798 1.7380 1.6442 -0.0133 0.0034  0.2040  165 LYS E CG  
12930 C CD  . LYS E 165 ? 1.8014 1.6499 1.5719 -0.0074 -0.0133 0.2047  165 LYS E CD  
12931 C CE  . LYS E 165 ? 1.7842 1.6508 1.5914 -0.0080 -0.0144 0.1977  165 LYS E CE  
12932 N NZ  . LYS E 165 ? 1.7510 1.6012 1.5618 -0.0070 -0.0226 0.2021  165 LYS E NZ  
12933 N N   . LEU E 166 ? 2.0163 1.8615 1.7729 -0.0433 0.0583  0.2212  166 LEU E N   
12934 C CA  . LEU E 166 ? 2.0664 1.9119 1.8321 -0.0529 0.0737  0.2248  166 LEU E CA  
12935 C C   . LEU E 166 ? 2.1018 1.9536 1.8562 -0.0581 0.0906  0.2256  166 LEU E C   
12936 O O   . LEU E 166 ? 2.1073 1.9578 1.8412 -0.0543 0.0901  0.2250  166 LEU E O   
12937 C CB  . LEU E 166 ? 2.0977 1.9147 1.8469 -0.0563 0.0728  0.2359  166 LEU E CB  
12938 C CG  . LEU E 166 ? 2.0448 1.8644 1.8204 -0.0619 0.0757  0.2357  166 LEU E CG  
12939 C CD1 . LEU E 166 ? 2.0255 1.8523 1.8237 -0.0552 0.0594  0.2290  166 LEU E CD1 
12940 C CD2 . LEU E 166 ? 2.0343 1.8261 1.7912 -0.0681 0.0809  0.2478  166 LEU E CD2 
12941 N N   . TYR E 167 ? 2.1436 2.0025 1.9119 -0.0668 0.1056  0.2266  167 TYR E N   
12942 C CA  . TYR E 167 ? 2.2149 2.0836 1.9782 -0.0719 0.1226  0.2261  167 TYR E CA  
12943 C C   . TYR E 167 ? 2.2930 2.1365 2.0200 -0.0757 0.1308  0.2372  167 TYR E C   
12944 O O   . TYR E 167 ? 2.3016 2.1285 2.0228 -0.0820 0.1362  0.2455  167 TYR E O   
12945 C CB  . TYR E 167 ? 2.2270 2.1146 2.0210 -0.0797 0.1353  0.2226  167 TYR E CB  
12946 C CG  . TYR E 167 ? 2.3300 2.2277 2.1204 -0.0852 0.1535  0.2223  167 TYR E CG  
12947 C CD1 . TYR E 167 ? 2.3797 2.2993 2.1791 -0.0818 0.1561  0.2138  167 TYR E CD1 
12948 C CD2 . TYR E 167 ? 2.3114 2.1962 2.0893 -0.0939 0.1683  0.2307  167 TYR E CD2 
12949 C CE1 . TYR E 167 ? 2.4381 2.3670 2.2349 -0.0864 0.1726  0.2133  167 TYR E CE1 
12950 C CE2 . TYR E 167 ? 2.3377 2.2323 2.1130 -0.0988 0.1854  0.2302  167 TYR E CE2 
12951 C CZ  . TYR E 167 ? 2.4191 2.3358 2.2040 -0.0948 0.1873  0.2213  167 TYR E CZ  
12952 O OH  . TYR E 167 ? 2.4326 2.3591 2.2156 -0.0993 0.2043  0.2205  167 TYR E OH  
12953 N N   . VAL E 168 ? 2.3458 2.1859 2.0479 -0.0721 0.1319  0.2372  168 VAL E N   
12954 C CA  . VAL E 168 ? 2.4285 2.2485 2.0958 -0.0760 0.1425  0.2464  168 VAL E CA  
12955 C C   . VAL E 168 ? 2.5499 2.3849 2.2160 -0.0795 0.1593  0.2428  168 VAL E C   
12956 O O   . VAL E 168 ? 2.5971 2.4182 2.2370 -0.0840 0.1713  0.2499  168 VAL E O   
12957 C CB  . VAL E 168 ? 2.3521 2.1500 1.9843 -0.0688 0.1295  0.2510  168 VAL E CB  
12958 C CG1 . VAL E 168 ? 2.3007 2.0796 1.9304 -0.0662 0.1147  0.2568  168 VAL E CG1 
12959 C CG2 . VAL E 168 ? 2.3223 2.1353 1.9572 -0.0603 0.1196  0.2415  168 VAL E CG2 
12960 N N   . GLY E 169 ? 2.8266 2.6888 2.5196 -0.0776 0.1606  0.2323  169 GLY E N   
12961 C CA  . GLY E 169 ? 2.8225 2.7006 2.5179 -0.0804 0.1760  0.2280  169 GLY E CA  
12962 C C   . GLY E 169 ? 2.8296 2.7348 2.5510 -0.0751 0.1710  0.2162  169 GLY E C   
12963 O O   . GLY E 169 ? 2.7861 2.6973 2.5214 -0.0691 0.1557  0.2114  169 GLY E O   
12964 N N   . ASN E 170 ? 2.7615 2.6834 2.4898 -0.0774 0.1848  0.2115  170 ASN E N   
12965 C CA  . ASN E 170 ? 2.7415 2.6891 2.4930 -0.0728 0.1822  0.2007  170 ASN E CA  
12966 C C   . ASN E 170 ? 2.8735 2.8250 2.6082 -0.0702 0.1895  0.1973  170 ASN E C   
12967 O O   . ASN E 170 ? 2.8077 2.7797 2.5599 -0.0663 0.1882  0.1885  170 ASN E O   
12968 C CB  . ASN E 170 ? 2.6546 2.6253 2.4433 -0.0781 0.1909  0.1961  170 ASN E CB  
12969 C CG  . ASN E 170 ? 2.6614 2.6279 2.4487 -0.0877 0.2088  0.2022  170 ASN E CG  
12970 O OD1 . ASN E 170 ? 2.6172 2.5772 2.4135 -0.0932 0.2097  0.2069  170 ASN E OD1 
12971 N ND2 . ASN E 170 ? 2.6872 2.6574 2.4636 -0.0899 0.2233  0.2019  170 ASN E ND2 
12972 N N   . LYS E 171 ? 3.0464 2.9788 2.7476 -0.0721 0.1973  0.2039  171 LYS E N   
12973 C CA  . LYS E 171 ? 3.1388 3.0736 2.8224 -0.0705 0.2065  0.2009  171 LYS E CA  
12974 C C   . LYS E 171 ? 3.4061 3.3285 3.0635 -0.0623 0.1927  0.1996  171 LYS E C   
12975 O O   . LYS E 171 ? 3.3861 3.2857 3.0184 -0.0609 0.1838  0.2065  171 LYS E O   
12976 C CB  . LYS E 171 ? 3.0050 2.9266 2.6669 -0.0778 0.2244  0.2087  171 LYS E CB  
12977 C CG  . LYS E 171 ? 2.9340 2.8669 2.6217 -0.0866 0.2383  0.2105  171 LYS E CG  
12978 C CD  . LYS E 171 ? 2.9407 2.8510 2.6097 -0.0938 0.2449  0.2221  171 LYS E CD  
12979 C CE  . LYS E 171 ? 2.9574 2.8496 2.6192 -0.0911 0.2275  0.2274  171 LYS E CE  
12980 N NZ  . LYS E 171 ? 3.0274 2.8947 2.6672 -0.0976 0.2332  0.2395  171 LYS E NZ  
12981 N N   . ILE E 172 ? 4.0570 3.9944 3.7207 -0.0569 0.1905  0.1907  172 ILE E N   
12982 C CA  . ILE E 172 ? 4.0737 4.0024 3.7165 -0.0491 0.1769  0.1878  172 ILE E CA  
12983 C C   . ILE E 172 ? 4.0738 4.0036 3.6977 -0.0477 0.1872  0.1841  172 ILE E C   
12984 O O   . ILE E 172 ? 4.0569 3.9984 3.6897 -0.0520 0.2037  0.1822  172 ILE E O   
12985 C CB  . ILE E 172 ? 4.0558 4.0003 3.7241 -0.0428 0.1611  0.1799  172 ILE E CB  
12986 C CG1 . ILE E 172 ? 4.0223 3.9929 3.7163 -0.0420 0.1685  0.1705  172 ILE E CG1 
12987 C CG2 . ILE E 172 ? 4.0511 3.9974 3.7416 -0.0443 0.1528  0.1824  172 ILE E CG2 
12988 C CD1 . ILE E 172 ? 4.0072 3.9907 3.7164 -0.0348 0.1540  0.1623  172 ILE E CD1 
12989 N N   . ASN E 173 ? 3.4393 3.3570 3.0377 -0.0416 0.1767  0.1827  173 ASN E N   
12990 C CA  . ASN E 173 ? 3.1824 3.0995 2.7608 -0.0393 0.1840  0.1784  173 ASN E CA  
12991 C C   . ASN E 173 ? 3.1590 3.1016 2.7654 -0.0362 0.1856  0.1675  173 ASN E C   
12992 O O   . ASN E 173 ? 3.1489 3.1059 2.7828 -0.0333 0.1748  0.1627  173 ASN E O   
12993 C CB  . ASN E 173 ? 3.0024 2.8995 2.5467 -0.0334 0.1704  0.1795  173 ASN E CB  
12994 C CG  . ASN E 173 ? 2.9416 2.8318 2.4570 -0.0321 0.1795  0.1770  173 ASN E CG  
12995 O OD1 . ASN E 173 ? 2.9598 2.8664 2.4876 -0.0314 0.1884  0.1694  173 ASN E OD1 
12996 N ND2 . ASN E 173 ? 2.9134 2.7792 2.3898 -0.0316 0.1771  0.1834  173 ASN E ND2 
12997 N N   . ALA E 174 ? 3.1981 3.1460 2.7971 -0.0369 0.1995  0.1636  174 ALA E N   
12998 C CA  . ALA E 174 ? 3.1285 3.0993 2.7520 -0.0341 0.2029  0.1537  174 ALA E CA  
12999 C C   . ALA E 174 ? 3.1109 3.0781 2.7158 -0.0276 0.1975  0.1471  174 ALA E C   
13000 O O   . ALA E 174 ? 3.0801 3.0647 2.7031 -0.0249 0.2000  0.1387  174 ALA E O   
13001 C CB  . ALA E 174 ? 3.0812 3.0652 2.7181 -0.0398 0.2239  0.1530  174 ALA E CB  
13002 N N   . GLY E 175 ? 3.0570 3.0020 2.6263 -0.0251 0.1897  0.1505  175 GLY E N   
13003 C CA  . GLY E 175 ? 2.9628 2.9032 2.5136 -0.0189 0.1830  0.1440  175 GLY E CA  
13004 C C   . GLY E 175 ? 3.0326 2.9703 2.5631 -0.0195 0.1985  0.1410  175 GLY E C   
13005 O O   . GLY E 175 ? 2.8732 2.8082 2.3900 -0.0143 0.1936  0.1345  175 GLY E O   
13006 N N   . ILE E 176 ? 3.2500 3.1883 2.7784 -0.0255 0.2171  0.1451  176 ILE E N   
13007 C CA  . ILE E 176 ? 3.2549 3.1903 2.7633 -0.0264 0.2335  0.1427  176 ILE E CA  
13008 C C   . ILE E 176 ? 3.2834 3.1962 2.7565 -0.0311 0.2415  0.1525  176 ILE E C   
13009 O O   . ILE E 176 ? 3.2804 3.1901 2.7594 -0.0368 0.2457  0.1607  176 ILE E O   
13010 C CB  . ILE E 176 ? 3.2504 3.2089 2.7892 -0.0295 0.2504  0.1380  176 ILE E CB  
13011 C CG1 . ILE E 176 ? 3.2449 3.1976 2.7624 -0.0334 0.2712  0.1397  176 ILE E CG1 
13012 C CG2 . ILE E 176 ? 3.2832 3.2551 2.8560 -0.0342 0.2512  0.1418  176 ILE E CG2 
13013 C CD1 . ILE E 176 ? 3.2274 3.2025 2.7745 -0.0365 0.2885  0.1354  176 ILE E CD1 
13014 N N   . TYR E 177 ? 3.2344 3.1313 2.6705 -0.0286 0.2434  0.1516  177 TYR E N   
13015 C CA  . TYR E 177 ? 3.2632 3.1357 2.6600 -0.0320 0.2484  0.1610  177 TYR E CA  
13016 C C   . TYR E 177 ? 3.2722 3.1422 2.6476 -0.0340 0.2683  0.1591  177 TYR E C   
13017 O O   . TYR E 177 ? 3.2521 3.1370 2.6397 -0.0316 0.2758  0.1496  177 TYR E O   
13018 C CB  . TYR E 177 ? 3.2912 3.1427 2.6571 -0.0267 0.2291  0.1629  177 TYR E CB  
13019 C CG  . TYR E 177 ? 3.2939 3.1488 2.6806 -0.0233 0.2082  0.1631  177 TYR E CG  
13020 C CD1 . TYR E 177 ? 3.2785 3.1416 2.6938 -0.0273 0.2072  0.1681  177 TYR E CD1 
13021 C CD2 . TYR E 177 ? 3.3192 3.1694 2.6975 -0.0162 0.1896  0.1578  177 TYR E CD2 
13022 C CE1 . TYR E 177 ? 3.2798 3.1464 2.7141 -0.0240 0.1887  0.1677  177 TYR E CE1 
13023 C CE2 . TYR E 177 ? 3.3125 3.1666 2.7105 -0.0132 0.1710  0.1577  177 TYR E CE2 
13024 C CZ  . TYR E 177 ? 3.2779 3.1402 2.7037 -0.0170 0.1708  0.1626  177 TYR E CZ  
13025 O OH  . TYR E 177 ? 3.2509 3.1174 2.6963 -0.0138 0.1529  0.1621  177 TYR E OH  
13026 N N   . LEU E 178 ? 3.1064 2.9567 2.4493 -0.0385 0.2769  0.1683  178 LEU E N   
13027 C CA  . LEU E 178 ? 3.0592 2.9032 2.3749 -0.0405 0.2955  0.1676  178 LEU E CA  
13028 C C   . LEU E 178 ? 3.0464 2.8610 2.3150 -0.0417 0.2924  0.1772  178 LEU E C   
13029 O O   . LEU E 178 ? 3.0179 2.8219 2.2800 -0.0476 0.2966  0.1882  178 LEU E O   
13030 C CB  . LEU E 178 ? 3.0312 2.8898 2.3683 -0.0478 0.3179  0.1694  178 LEU E CB  
13031 C CG  . LEU E 178 ? 2.9776 2.8348 2.2943 -0.0504 0.3400  0.1677  178 LEU E CG  
13032 C CD1 . LEU E 178 ? 2.9060 2.7880 2.2599 -0.0547 0.3579  0.1639  178 LEU E CD1 
13033 C CD2 . LEU E 178 ? 2.9367 2.7698 2.2142 -0.0559 0.3486  0.1794  178 LEU E CD2 
13034 N N   . LEU E 179 ? 2.9615 2.7627 2.1976 -0.0359 0.2845  0.1730  179 LEU E N   
13035 C CA  . LEU E 179 ? 2.9102 2.6832 2.1010 -0.0353 0.2768  0.1812  179 LEU E CA  
13036 C C   . LEU E 179 ? 2.8918 2.6529 2.0433 -0.0356 0.2912  0.1798  179 LEU E C   
13037 O O   . LEU E 179 ? 2.9176 2.6879 2.0693 -0.0316 0.2954  0.1688  179 LEU E O   
13038 C CB  . LEU E 179 ? 2.8993 2.6644 2.0830 -0.0278 0.2511  0.1779  179 LEU E CB  
13039 C CG  . LEU E 179 ? 2.9036 2.6739 2.1163 -0.0268 0.2335  0.1811  179 LEU E CG  
13040 C CD1 . LEU E 179 ? 2.9371 2.7030 2.1446 -0.0188 0.2100  0.1753  179 LEU E CD1 
13041 C CD2 . LEU E 179 ? 2.9160 2.6688 2.1151 -0.0319 0.2331  0.1951  179 LEU E CD2 
13042 N N   . ASN E 180 ? 2.7012 2.4411 1.8181 -0.0402 0.2982  0.1909  180 ASN E N   
13043 C CA  . ASN E 180 ? 2.6132 2.3375 1.6859 -0.0401 0.3092  0.1908  180 ASN E CA  
13044 C C   . ASN E 180 ? 2.5182 2.2265 1.5593 -0.0323 0.2897  0.1867  180 ASN E C   
13045 O O   . ASN E 180 ? 2.4619 2.1656 1.5090 -0.0285 0.2681  0.1881  180 ASN E O   
13046 C CB  . ASN E 180 ? 2.6022 2.3076 1.6465 -0.0475 0.3217  0.2048  180 ASN E CB  
13047 C CG  . ASN E 180 ? 2.6760 2.3952 1.7380 -0.0553 0.3478  0.2064  180 ASN E CG  
13048 O OD1 . ASN E 180 ? 2.6628 2.4012 1.7434 -0.0544 0.3601  0.1963  180 ASN E OD1 
13049 N ND2 . ASN E 180 ? 2.7136 2.4228 1.7701 -0.0630 0.3564  0.2193  180 ASN E ND2 
13050 N N   . PRO E 181 ? 2.5189 2.2188 1.5266 -0.0298 0.2968  0.1812  181 PRO E N   
13051 C CA  . PRO E 181 ? 2.4613 2.1439 1.4349 -0.0228 0.2784  0.1778  181 PRO E CA  
13052 C C   . PRO E 181 ? 2.3762 2.0326 1.3166 -0.0234 0.2654  0.1905  181 PRO E C   
13053 O O   . PRO E 181 ? 2.3595 2.0028 1.2779 -0.0174 0.2459  0.1884  181 PRO E O   
13054 C CB  . PRO E 181 ? 2.4088 2.0871 1.3515 -0.0217 0.2937  0.1708  181 PRO E CB  
13055 C CG  . PRO E 181 ? 2.5226 2.2245 1.4986 -0.0255 0.3154  0.1653  181 PRO E CG  
13056 C CD  . PRO E 181 ? 2.5802 2.2888 1.5836 -0.0325 0.3213  0.1759  181 PRO E CD  
13057 N N   . SER E 182 ? 2.3642 2.0126 1.3009 -0.0305 0.2751  0.2035  182 SER E N   
13058 C CA  . SER E 182 ? 2.3148 1.9374 1.2201 -0.0314 0.2637  0.2166  182 SER E CA  
13059 C C   . SER E 182 ? 2.3155 1.9391 1.2451 -0.0284 0.2406  0.2195  182 SER E C   
13060 O O   . SER E 182 ? 2.3016 1.9052 1.2110 -0.0291 0.2303  0.2309  182 SER E O   
13061 C CB  . SER E 182 ? 2.3210 1.9346 1.2152 -0.0405 0.2833  0.2297  182 SER E CB  
13062 O OG  . SER E 182 ? 2.2299 1.8420 1.1000 -0.0434 0.3053  0.2274  182 SER E OG  
13063 N N   . VAL E 183 ? 2.3605 2.0068 1.3328 -0.0250 0.2323  0.2096  183 VAL E N   
13064 C CA  . VAL E 183 ? 2.3874 2.0364 1.3844 -0.0217 0.2106  0.2112  183 VAL E CA  
13065 C C   . VAL E 183 ? 2.4454 2.0934 1.4370 -0.0129 0.1886  0.2020  183 VAL E C   
13066 O O   . VAL E 183 ? 2.4196 2.0626 1.4182 -0.0094 0.1679  0.2047  183 VAL E O   
13067 C CB  . VAL E 183 ? 2.3966 2.0718 1.4480 -0.0247 0.2157  0.2082  183 VAL E CB  
13068 C CG1 . VAL E 183 ? 2.5088 2.2075 1.5881 -0.0204 0.2155  0.1932  183 VAL E CG1 
13069 C CG2 . VAL E 183 ? 2.2926 1.9661 1.3646 -0.0237 0.1975  0.2142  183 VAL E CG2 
13070 N N   . LEU E 184 ? 2.6902 2.3424 1.6697 -0.0094 0.1923  0.1910  184 LEU E N   
13071 C CA  . LEU E 184 ? 2.6949 2.3475 1.6715 -0.0014 0.1723  0.1811  184 LEU E CA  
13072 C C   . LEU E 184 ? 2.7228 2.3491 1.6574 0.0024  0.1545  0.1870  184 LEU E C   
13073 O O   . LEU E 184 ? 2.7258 2.3506 1.6560 0.0089  0.1362  0.1795  184 LEU E O   
13074 C CB  . LEU E 184 ? 2.7189 2.3811 1.6912 0.0010  0.1823  0.1681  184 LEU E CB  
13075 C CG  . LEU E 184 ? 2.7734 2.4638 1.7906 -0.0008 0.1958  0.1598  184 LEU E CG  
13076 C CD1 . LEU E 184 ? 2.8102 2.5065 1.8173 0.0017  0.2068  0.1478  184 LEU E CD1 
13077 C CD2 . LEU E 184 ? 2.7437 2.4514 1.8040 0.0025  0.1791  0.1549  184 LEU E CD2 
13078 N N   . ASP E 185 ? 2.4740 2.0796 1.3780 -0.0016 0.1594  0.2001  185 ASP E N   
13079 C CA  . ASP E 185 ? 2.4416 2.0211 1.3053 0.0019  0.1424  0.2071  185 ASP E CA  
13080 C C   . ASP E 185 ? 2.4078 1.9810 1.2852 0.0024  0.1257  0.2167  185 ASP E C   
13081 O O   . ASP E 185 ? 2.3692 1.9253 1.2233 0.0072  0.1059  0.2200  185 ASP E O   
13082 C CB  . ASP E 185 ? 2.4079 1.9655 1.2234 -0.0022 0.1574  0.2160  185 ASP E CB  
13083 C CG  . ASP E 185 ? 2.4203 1.9760 1.2435 -0.0105 0.1743  0.2285  185 ASP E CG  
13084 O OD1 . ASP E 185 ? 2.3817 1.9587 1.2489 -0.0140 0.1828  0.2265  185 ASP E OD1 
13085 O OD2 . ASP E 185 ? 2.5163 2.0492 1.3018 -0.0137 0.1790  0.2404  185 ASP E OD2 
13086 N N   . LYS E 186 ? 2.3965 1.9832 1.3115 -0.0023 0.1328  0.2209  186 LYS E N   
13087 C CA  . LYS E 186 ? 2.3730 1.9537 1.3021 -0.0023 0.1186  0.2301  186 LYS E CA  
13088 C C   . LYS E 186 ? 2.3684 1.9612 1.3270 0.0045  0.0958  0.2223  186 LYS E C   
13089 O O   . LYS E 186 ? 2.3501 1.9377 1.3198 0.0058  0.0813  0.2287  186 LYS E O   
13090 C CB  . LYS E 186 ? 2.3714 1.9626 1.3308 -0.0098 0.1346  0.2367  186 LYS E CB  
13091 C CG  . LYS E 186 ? 2.4876 2.0614 1.4408 -0.0123 0.1276  0.2510  186 LYS E CG  
13092 C CD  . LYS E 186 ? 2.7447 2.3310 1.7326 -0.0196 0.1420  0.2559  186 LYS E CD  
13093 C CE  . LYS E 186 ? 2.8866 2.4514 1.8605 -0.0231 0.1388  0.2713  186 LYS E CE  
13094 N NZ  . LYS E 186 ? 2.8921 2.4432 1.8577 -0.0162 0.1126  0.2742  186 LYS E NZ  
13095 N N   . ILE E 187 ? 2.4488 2.0573 1.4206 0.0086  0.0926  0.2087  187 ILE E N   
13096 C CA  . ILE E 187 ? 2.5950 2.2166 1.5962 0.0146  0.0724  0.2005  187 ILE E CA  
13097 C C   . ILE E 187 ? 2.8414 2.4452 1.8105 0.0213  0.0510  0.1995  187 ILE E C   
13098 O O   . ILE E 187 ? 2.7980 2.3843 1.7243 0.0221  0.0534  0.2005  187 ILE E O   
13099 C CB  . ILE E 187 ? 2.5347 2.1823 1.5681 0.0154  0.0794  0.1866  187 ILE E CB  
13100 C CG1 . ILE E 187 ? 2.4467 2.0918 1.4535 0.0144  0.0957  0.1810  187 ILE E CG1 
13101 C CG2 . ILE E 187 ? 2.5433 2.2124 1.6219 0.0107  0.0910  0.1871  187 ILE E CG2 
13102 C CD1 . ILE E 187 ? 2.4715 2.1049 1.4464 0.0205  0.0826  0.1739  187 ILE E CD1 
13103 N N   . GLU E 188 ? 3.6009 3.2095 2.5912 0.0262  0.0297  0.1973  188 GLU E N   
13104 C CA  . GLU E 188 ? 3.6091 3.2049 2.5770 0.0331  0.0070  0.1948  188 GLU E CA  
13105 C C   . GLU E 188 ? 3.5943 3.2074 2.5810 0.0376  -0.0008 0.1797  188 GLU E C   
13106 O O   . GLU E 188 ? 3.5749 3.2099 2.5936 0.0357  0.0102  0.1718  188 GLU E O   
13107 C CB  . GLU E 188 ? 3.6099 3.1988 2.5881 0.0359  -0.0123 0.2024  188 GLU E CB  
13108 C CG  . GLU E 188 ? 3.5827 3.1919 2.6109 0.0338  -0.0108 0.2024  188 GLU E CG  
13109 C CD  . GLU E 188 ? 3.5747 3.1821 2.6189 0.0386  -0.0338 0.2049  188 GLU E CD  
13110 O OE1 . GLU E 188 ? 3.5877 3.1750 2.6018 0.0429  -0.0496 0.2095  188 GLU E OE1 
13111 O OE2 . GLU E 188 ? 3.5503 3.1765 2.6371 0.0384  -0.0361 0.2021  188 GLU E OE2 
13112 N N   . LEU E 189 ? 3.1383 2.7411 2.1048 0.0437  -0.0206 0.1758  189 LEU E N   
13113 C CA  . LEU E 189 ? 2.9045 2.5220 1.8886 0.0482  -0.0308 0.1618  189 LEU E CA  
13114 C C   . LEU E 189 ? 2.9932 2.6305 2.0254 0.0501  -0.0430 0.1582  189 LEU E C   
13115 O O   . LEU E 189 ? 2.8930 2.5476 1.9497 0.0523  -0.0471 0.1467  189 LEU E O   
13116 C CB  . LEU E 189 ? 2.6549 2.2546 1.6017 0.0538  -0.0486 0.1588  189 LEU E CB  
13117 C CG  . LEU E 189 ? 2.6342 2.2107 1.5527 0.0560  -0.0636 0.1705  189 LEU E CG  
13118 C CD1 . LEU E 189 ? 2.4697 2.0475 1.3997 0.0626  -0.0907 0.1663  189 LEU E CD1 
13119 C CD2 . LEU E 189 ? 2.2930 1.8447 1.1558 0.0557  -0.0588 0.1751  189 LEU E CD2 
13120 N N   . ARG E 190 ? 3.2705 2.9052 2.3161 0.0493  -0.0486 0.1677  190 ARG E N   
13121 C CA  . ARG E 190 ? 3.2457 2.8980 2.3356 0.0511  -0.0599 0.1652  190 ARG E CA  
13122 C C   . ARG E 190 ? 3.2184 2.8941 2.3484 0.0463  -0.0428 0.1624  190 ARG E C   
13123 O O   . ARG E 190 ? 3.2240 2.8982 2.3489 0.0408  -0.0232 0.1678  190 ARG E O   
13124 C CB  . ARG E 190 ? 3.2718 2.9112 2.3592 0.0523  -0.0722 0.1765  190 ARG E CB  
13125 C CG  . ARG E 190 ? 3.2718 2.8868 2.3191 0.0571  -0.0897 0.1809  190 ARG E CG  
13126 C CD  . ARG E 190 ? 3.2618 2.8832 2.3152 0.0634  -0.1094 0.1701  190 ARG E CD  
13127 N NE  . ARG E 190 ? 3.2305 2.8755 2.3330 0.0647  -0.1162 0.1639  190 ARG E NE  
13128 C CZ  . ARG E 190 ? 3.2102 2.8754 2.3381 0.0653  -0.1152 0.1518  190 ARG E CZ  
13129 N NH1 . ARG E 190 ? 3.2203 2.8846 2.3294 0.0651  -0.1083 0.1443  190 ARG E NH1 
13130 N NH2 . ARG E 190 ? 3.1801 2.8659 2.3516 0.0662  -0.1212 0.1473  190 ARG E NH2 
13131 N N   . PRO E 191 ? 2.8741 2.5717 2.0443 0.0483  -0.0497 0.1539  191 PRO E N   
13132 C CA  . PRO E 191 ? 2.7919 2.5118 2.0027 0.0443  -0.0362 0.1521  191 PRO E CA  
13133 C C   . PRO E 191 ? 2.9175 2.6338 2.1366 0.0400  -0.0289 0.1633  191 PRO E C   
13134 O O   . PRO E 191 ? 2.9203 2.6326 2.1485 0.0420  -0.0425 0.1684  191 PRO E O   
13135 C CB  . PRO E 191 ? 2.6311 2.3694 1.8782 0.0483  -0.0517 0.1437  191 PRO E CB  
13136 C CG  . PRO E 191 ? 2.6481 2.3791 1.8741 0.0533  -0.0653 0.1366  191 PRO E CG  
13137 C CD  . PRO E 191 ? 2.8344 2.5380 2.0129 0.0541  -0.0688 0.1444  191 PRO E CD  
13138 N N   . THR E 192 ? 3.2009 2.9189 2.4177 0.0341  -0.0075 0.1668  192 THR E N   
13139 C CA  . THR E 192 ? 3.2038 2.9191 2.4291 0.0291  0.0019  0.1770  192 THR E CA  
13140 C C   . THR E 192 ? 3.1602 2.8998 2.4250 0.0247  0.0170  0.1730  192 THR E C   
13141 O O   . THR E 192 ? 3.1465 2.8976 2.4158 0.0233  0.0298  0.1659  192 THR E O   
13142 C CB  . THR E 192 ? 3.3187 3.0120 2.5037 0.0251  0.0145  0.1866  192 THR E CB  
13143 O OG1 . THR E 192 ? 3.4520 3.1484 2.6516 0.0186  0.0297  0.1943  192 THR E OG1 
13144 C CG2 . THR E 192 ? 3.2533 2.9462 2.4160 0.0243  0.0276  0.1805  192 THR E CG2 
13145 N N   . SER E 193 ? 2.8966 2.6438 2.1899 0.0229  0.0152  0.1773  193 SER E N   
13146 C CA  . SER E 193 ? 2.7072 2.4764 2.0373 0.0184  0.0292  0.1746  193 SER E CA  
13147 C C   . SER E 193 ? 2.8282 2.5899 2.1453 0.0114  0.0496  0.1827  193 SER E C   
13148 O O   . SER E 193 ? 3.0242 2.7698 2.3281 0.0090  0.0492  0.1931  193 SER E O   
13149 C CB  . SER E 193 ? 2.5702 2.3511 1.9364 0.0194  0.0187  0.1752  193 SER E CB  
13150 O OG  . SER E 193 ? 2.5189 2.2993 1.8881 0.0260  -0.0025 0.1709  193 SER E OG  
13151 N N   . ILE E 194 ? 2.7168 2.4897 2.0378 0.0082  0.0673  0.1778  194 ILE E N   
13152 C CA  . ILE E 194 ? 2.8265 2.5931 2.1344 0.0014  0.0878  0.1847  194 ILE E CA  
13153 C C   . ILE E 194 ? 2.8738 2.6458 2.2071 -0.0037 0.0929  0.1916  194 ILE E C   
13154 O O   . ILE E 194 ? 3.0562 2.8160 2.3747 -0.0092 0.1046  0.2008  194 ILE E O   
13155 C CB  . ILE E 194 ? 2.6600 2.4411 1.9729 -0.0005 0.1053  0.1769  194 ILE E CB  
13156 C CG1 . ILE E 194 ? 2.9540 2.7231 2.2403 -0.0064 0.1252  0.1837  194 ILE E CG1 
13157 C CG2 . ILE E 194 ? 2.5377 2.3461 1.8972 -0.0024 0.1114  0.1709  194 ILE E CG2 
13158 C CD1 . ILE E 194 ? 2.8891 2.6713 2.1784 -0.0080 0.1428  0.1761  194 ILE E CD1 
13159 N N   . GLU E 195 ? 2.6161 2.4053 1.9871 -0.0020 0.0840  0.1874  195 GLU E N   
13160 C CA  . GLU E 195 ? 2.5600 2.3559 1.9577 -0.0066 0.0883  0.1926  195 GLU E CA  
13161 C C   . GLU E 195 ? 2.6018 2.3789 1.9890 -0.0056 0.0750  0.2019  195 GLU E C   
13162 O O   . GLU E 195 ? 2.5460 2.3208 1.9439 -0.0105 0.0808  0.2088  195 GLU E O   
13163 C CB  . GLU E 195 ? 2.3193 2.1421 1.7618 -0.0053 0.0849  0.1840  195 GLU E CB  
13164 N N   . LYS E 196 ? 2.7124 2.4761 2.0795 0.0006  0.0570  0.2020  196 LYS E N   
13165 C CA  . LYS E 196 ? 2.8010 2.5480 2.1608 0.0027  0.0423  0.2099  196 LYS E CA  
13166 C C   . LYS E 196 ? 3.1039 2.8216 2.4175 0.0031  0.0397  0.2192  196 LYS E C   
13167 O O   . LYS E 196 ? 3.0550 2.7564 2.3603 0.0025  0.0336  0.2286  196 LYS E O   
13168 C CB  . LYS E 196 ? 2.6471 2.4020 2.0244 0.0101  0.0209  0.2033  196 LYS E CB  
13169 C CG  . LYS E 196 ? 2.4194 2.2032 1.8393 0.0106  0.0219  0.1932  196 LYS E CG  
13170 C CD  . LYS E 196 ? 2.2547 2.0453 1.6896 0.0177  0.0011  0.1870  196 LYS E CD  
13171 C CE  . LYS E 196 ? 1.8742 1.6932 1.3488 0.0182  0.0026  0.1769  196 LYS E CE  
13172 N NZ  . LYS E 196 ? 1.8037 1.6359 1.3086 0.0131  0.0131  0.1787  196 LYS E NZ  
13173 N N   . GLU E 197 ? 3.6775 3.3878 2.9607 0.0042  0.0440  0.2169  197 GLU E N   
13174 C CA  . GLU E 197 ? 3.7870 3.4694 3.0237 0.0053  0.0404  0.2250  197 GLU E CA  
13175 C C   . GLU E 197 ? 3.9649 3.6389 3.1733 -0.0002 0.0610  0.2285  197 GLU E C   
13176 O O   . GLU E 197 ? 3.9449 3.5973 3.1243 -0.0035 0.0658  0.2395  197 GLU E O   
13177 C CB  . GLU E 197 ? 3.7715 3.4483 2.9907 0.0133  0.0215  0.2190  197 GLU E CB  
13178 C CG  . GLU E 197 ? 3.7110 3.3893 2.9486 0.0192  -0.0011 0.2181  197 GLU E CG  
13179 C CD  . GLU E 197 ? 3.6250 3.3313 2.9074 0.0211  -0.0047 0.2073  197 GLU E CD  
13180 O OE1 . GLU E 197 ? 3.6128 3.3367 2.9100 0.0184  0.0089  0.2001  197 GLU E OE1 
13181 O OE2 . GLU E 197 ? 3.6065 3.3173 2.9095 0.0252  -0.0210 0.2060  197 GLU E OE2 
13182 N N   . THR E 198 ? 5.0256 4.7158 4.2415 -0.0013 0.0734  0.2195  198 THR E N   
13183 C CA  . THR E 198 ? 5.0386 4.7211 4.2260 -0.0058 0.0926  0.2217  198 THR E CA  
13184 C C   . THR E 198 ? 5.0299 4.7160 4.2295 -0.0144 0.1129  0.2285  198 THR E C   
13185 O O   . THR E 198 ? 5.0468 4.7149 4.2167 -0.0189 0.1239  0.2378  198 THR E O   
13186 C CB  . THR E 198 ? 5.0284 4.7266 4.2199 -0.0035 0.0986  0.2092  198 THR E CB  
13187 O OG1 . THR E 198 ? 5.0382 4.7317 4.2167 0.0041  0.0795  0.2031  198 THR E OG1 
13188 C CG2 . THR E 198 ? 5.0399 4.7304 4.2017 -0.0077 0.1188  0.2108  198 THR E CG2 
13189 N N   . PHE E 199 ? 3.9411 3.6505 3.1842 -0.0168 0.1181  0.2239  199 PHE E N   
13190 C CA  . PHE E 199 ? 3.6964 3.4110 2.9547 -0.0250 0.1367  0.2296  199 PHE E CA  
13191 C C   . PHE E 199 ? 3.6589 3.3526 2.9039 -0.0288 0.1346  0.2430  199 PHE E C   
13192 O O   . PHE E 199 ? 3.5737 3.2588 2.8051 -0.0358 0.1517  0.2507  199 PHE E O   
13193 C CB  . PHE E 199 ? 3.3844 3.1276 2.6927 -0.0261 0.1390  0.2219  199 PHE E CB  
13194 C CG  . PHE E 199 ? 3.2643 3.0286 2.5869 -0.0256 0.1500  0.2109  199 PHE E CG  
13195 C CD1 . PHE E 199 ? 3.3267 3.0851 2.6212 -0.0267 0.1632  0.2096  199 PHE E CD1 
13196 C CD2 . PHE E 199 ? 3.0542 2.8440 2.4181 -0.0239 0.1471  0.2019  199 PHE E CD2 
13197 C CE1 . PHE E 199 ? 3.1427 2.9201 2.4510 -0.0259 0.1732  0.1993  199 PHE E CE1 
13198 C CE2 . PHE E 199 ? 3.0289 2.8375 2.4061 -0.0232 0.1568  0.1921  199 PHE E CE2 
13199 C CZ  . PHE E 199 ? 3.0744 2.8767 2.4242 -0.0241 0.1698  0.1907  199 PHE E CZ  
13200 N N   . PRO E 200 ? 3.6387 3.3236 2.8876 -0.0247 0.1153  0.2466  200 PRO E N   
13201 C CA  . PRO E 200 ? 3.5342 3.1965 2.7671 -0.0281 0.1137  0.2600  200 PRO E CA  
13202 C C   . PRO E 200 ? 3.5951 3.2298 2.7772 -0.0289 0.1169  0.2690  200 PRO E C   
13203 O O   . PRO E 200 ? 3.5180 3.1349 2.6849 -0.0341 0.1230  0.2809  200 PRO E O   
13204 C CB  . PRO E 200 ? 3.3312 2.9913 2.5786 -0.0217 0.0902  0.2596  200 PRO E CB  
13205 C CG  . PRO E 200 ? 3.4695 3.1439 2.7253 -0.0143 0.0782  0.2475  200 PRO E CG  
13206 C CD  . PRO E 200 ? 3.4730 3.1695 2.7456 -0.0174 0.0952  0.2387  200 PRO E CD  
13207 N N   . LYS E 201 ? 3.6548 3.2849 2.8098 -0.0241 0.1129  0.2639  201 LYS E N   
13208 C CA  . LYS E 201 ? 3.5963 3.2002 2.7012 -0.0248 0.1163  0.2722  201 LYS E CA  
13209 C C   . LYS E 201 ? 3.5170 3.1197 2.6098 -0.0333 0.1423  0.2767  201 LYS E C   
13210 O O   . LYS E 201 ? 3.4055 2.9854 2.4650 -0.0373 0.1488  0.2882  201 LYS E O   
13211 C CB  . LYS E 201 ? 3.5984 3.1989 2.6783 -0.0174 0.1054  0.2645  201 LYS E CB  
13212 C CG  . LYS E 201 ? 3.5613 3.1518 2.6354 -0.0093 0.0788  0.2644  201 LYS E CG  
13213 C CD  . LYS E 201 ? 3.4032 2.9892 2.4502 -0.0027 0.0691  0.2569  201 LYS E CD  
13214 C CE  . LYS E 201 ? 3.3473 2.9226 2.3873 0.0052  0.0425  0.2573  201 LYS E CE  
13215 N NZ  . LYS E 201 ? 3.2608 2.8306 2.2730 0.0113  0.0326  0.2502  201 LYS E NZ  
13216 N N   . ILE E 202 ? 3.5949 3.2219 2.7146 -0.0363 0.1575  0.2678  202 ILE E N   
13217 C CA  . ILE E 202 ? 3.5319 3.1604 2.6446 -0.0445 0.1828  0.2712  202 ILE E CA  
13218 C C   . ILE E 202 ? 3.4722 3.1054 2.6118 -0.0525 0.1934  0.2784  202 ILE E C   
13219 O O   . ILE E 202 ? 3.3612 2.9872 2.4877 -0.0601 0.2123  0.2858  202 ILE E O   
13220 C CB  . ILE E 202 ? 3.5147 3.1667 2.6426 -0.0439 0.1951  0.2583  202 ILE E CB  
13221 C CG1 . ILE E 202 ? 3.5289 3.1816 2.6433 -0.0350 0.1802  0.2486  202 ILE E CG1 
13222 C CG2 . ILE E 202 ? 3.3820 3.0300 2.4880 -0.0505 0.2196  0.2616  202 ILE E CG2 
13223 C CD1 . ILE E 202 ? 3.4974 3.1726 2.6281 -0.0337 0.1904  0.2355  202 ILE E CD1 
13224 N N   . ALA E 203 ? 3.6962 3.3409 2.8727 -0.0510 0.1817  0.2763  203 ALA E N   
13225 C CA  . ALA E 203 ? 3.6732 3.3220 2.8759 -0.0584 0.1904  0.2826  203 ALA E CA  
13226 C C   . ALA E 203 ? 3.6988 3.3186 2.8734 -0.0621 0.1890  0.2977  203 ALA E C   
13227 O O   . ALA E 203 ? 3.6988 3.3143 2.8751 -0.0707 0.2051  0.3056  203 ALA E O   
13228 C CB  . ALA E 203 ? 3.6514 3.3191 2.8987 -0.0552 0.1771  0.2761  203 ALA E CB  
13229 N N   . ALA E 204 ? 3.4146 3.0140 2.5636 -0.0557 0.1698  0.3021  204 ALA E N   
13230 C CA  . ALA E 204 ? 3.3366 2.9063 2.4557 -0.0584 0.1671  0.3169  204 ALA E CA  
13231 C C   . ALA E 204 ? 3.2219 2.7746 2.2995 -0.0638 0.1847  0.3248  204 ALA E C   
13232 O O   . ALA E 204 ? 3.2134 2.7444 2.2710 -0.0692 0.1898  0.3380  204 ALA E O   
13233 C CB  . ALA E 204 ? 3.3788 2.9316 2.4797 -0.0495 0.1416  0.3190  204 ALA E CB  
13234 N N   . ALA E 205 ? 3.2727 2.8343 2.3370 -0.0626 0.1943  0.3170  205 ALA E N   
13235 C CA  . ALA E 205 ? 3.1382 2.6863 2.1650 -0.0679 0.2129  0.3231  205 ALA E CA  
13236 C C   . ALA E 205 ? 3.1522 2.7143 2.1995 -0.0779 0.2385  0.3241  205 ALA E C   
13237 O O   . ALA E 205 ? 3.0490 2.5992 2.0676 -0.0839 0.2560  0.3310  205 ALA E O   
13238 C CB  . ALA E 205 ? 3.0248 2.5755 2.0269 -0.0621 0.2122  0.3139  205 ALA E CB  
13239 N N   . GLN E 206 ? 3.0807 2.6679 2.1765 -0.0799 0.2409  0.3172  206 GLN E N   
13240 C CA  . GLN E 206 ? 3.0291 2.6322 2.1498 -0.0892 0.2638  0.3172  206 GLN E CA  
13241 C C   . GLN E 206 ? 3.0625 2.6742 2.1684 -0.0912 0.2836  0.3117  206 GLN E C   
13242 O O   . GLN E 206 ? 3.0075 2.6183 2.1084 -0.0997 0.3050  0.3171  206 GLN E O   
13243 C CB  . GLN E 206 ? 2.9942 2.5788 2.1073 -0.0980 0.2722  0.3320  206 GLN E CB  
13244 C CG  . GLN E 206 ? 3.0327 2.6057 2.1574 -0.0960 0.2531  0.3383  206 GLN E CG  
13245 C CD  . GLN E 206 ? 3.0515 2.6489 2.2296 -0.0968 0.2495  0.3310  206 GLN E CD  
13246 O OE1 . GLN E 206 ? 3.0276 2.6501 2.2329 -0.0927 0.2472  0.3181  206 GLN E OE1 
13247 N NE2 . GLN E 206 ? 3.0569 2.6465 2.2497 -0.1022 0.2490  0.3394  206 GLN E NE2 
13248 N N   . GLY E 207 ? 3.4488 3.0691 2.5483 -0.0834 0.2764  0.3007  207 GLY E N   
13249 C CA  . GLY E 207 ? 3.4492 3.0778 2.5348 -0.0841 0.2935  0.2941  207 GLY E CA  
13250 C C   . GLY E 207 ? 3.4021 3.0624 2.5271 -0.0812 0.2963  0.2792  207 GLY E C   
13251 O O   . GLY E 207 ? 3.3934 3.0622 2.5093 -0.0789 0.3050  0.2708  207 GLY E O   
13252 N N   . LEU E 208 ? 3.0573 2.7348 2.2260 -0.0813 0.2889  0.2759  208 LEU E N   
13253 C CA  . LEU E 208 ? 2.8813 2.5890 2.0905 -0.0786 0.2900  0.2625  208 LEU E CA  
13254 C C   . LEU E 208 ? 2.8321 2.5583 2.0817 -0.0864 0.3034  0.2633  208 LEU E C   
13255 O O   . LEU E 208 ? 2.8271 2.5427 2.0752 -0.0937 0.3102  0.2739  208 LEU E O   
13256 C CB  . LEU E 208 ? 2.8561 2.5700 2.0817 -0.0698 0.2655  0.2555  208 LEU E CB  
13257 C CG  . LEU E 208 ? 3.0164 2.7121 2.2354 -0.0675 0.2455  0.2636  208 LEU E CG  
13258 C CD1 . LEU E 208 ? 3.0547 2.7511 2.2980 -0.0747 0.2498  0.2716  208 LEU E CD1 
13259 C CD2 . LEU E 208 ? 3.0170 2.7224 2.2535 -0.0585 0.2234  0.2545  208 LEU E CD2 
13260 N N   . TYR E 209 ? 2.7424 2.4966 2.0284 -0.0847 0.3069  0.2518  209 TYR E N   
13261 C CA  . TYR E 209 ? 2.6641 2.4394 1.9920 -0.0911 0.3181  0.2505  209 TYR E CA  
13262 C C   . TYR E 209 ? 2.6126 2.4148 1.9798 -0.0856 0.3094  0.2378  209 TYR E C   
13263 O O   . TYR E 209 ? 2.5860 2.3916 1.9467 -0.0777 0.2993  0.2296  209 TYR E O   
13264 C CB  . TYR E 209 ? 2.6975 2.4788 2.0221 -0.0986 0.3442  0.2517  209 TYR E CB  
13265 C CG  . TYR E 209 ? 2.7053 2.4979 2.0223 -0.0942 0.3524  0.2413  209 TYR E CG  
13266 C CD1 . TYR E 209 ? 2.6631 2.4844 2.0172 -0.0928 0.3583  0.2302  209 TYR E CD1 
13267 C CD2 . TYR E 209 ? 2.6831 2.4573 1.9555 -0.0910 0.3536  0.2425  209 TYR E CD2 
13268 C CE1 . TYR E 209 ? 2.6518 2.4829 1.9996 -0.0885 0.3655  0.2206  209 TYR E CE1 
13269 C CE2 . TYR E 209 ? 2.6767 2.4607 1.9421 -0.0867 0.3608  0.2325  209 TYR E CE2 
13270 C CZ  . TYR E 209 ? 2.6733 2.4857 1.9769 -0.0855 0.3669  0.2216  209 TYR E CZ  
13271 O OH  . TYR E 209 ? 2.6492 2.4708 1.9465 -0.0810 0.3740  0.2115  209 TYR E OH  
13272 N N   . VAL E 212 ? 2.6442 2.6056 2.2629 -0.0905 0.3288  0.1941  212 VAL E N   
13273 C CA  . VAL E 212 ? 2.6893 2.6710 2.3468 -0.0880 0.3176  0.1879  212 VAL E CA  
13274 C C   . VAL E 212 ? 2.7730 2.7783 2.4509 -0.0833 0.3213  0.1767  212 VAL E C   
13275 O O   . VAL E 212 ? 2.7631 2.7767 2.4412 -0.0855 0.3382  0.1743  212 VAL E O   
13276 C CB  . VAL E 212 ? 2.6965 2.6864 2.3820 -0.0961 0.3236  0.1921  212 VAL E CB  
13277 C CG1 . VAL E 212 ? 2.6920 2.7014 2.4152 -0.0933 0.3110  0.1858  212 VAL E CG1 
13278 C CG2 . VAL E 212 ? 2.7227 2.6874 2.3863 -0.1011 0.3213  0.2036  212 VAL E CG2 
13279 N N   . LEU E 213 ? 3.0296 3.0456 2.7249 -0.0766 0.3055  0.1701  213 LEU E N   
13280 C CA  . LEU E 213 ? 2.9858 3.0234 2.7013 -0.0715 0.3067  0.1597  213 LEU E CA  
13281 C C   . LEU E 213 ? 2.9434 3.0063 2.7011 -0.0752 0.3130  0.1562  213 LEU E C   
13282 O O   . LEU E 213 ? 2.9312 3.0000 2.7106 -0.0760 0.3026  0.1569  213 LEU E O   
13283 C CB  . LEU E 213 ? 2.9878 3.0255 2.7030 -0.0630 0.2871  0.1544  213 LEU E CB  
13284 C CG  . LEU E 213 ? 2.9549 3.0148 2.6936 -0.0575 0.2861  0.1438  213 LEU E CG  
13285 C CD1 . LEU E 213 ? 2.9623 3.0225 2.6849 -0.0559 0.2996  0.1397  213 LEU E CD1 
13286 C CD2 . LEU E 213 ? 2.9529 3.0125 2.6934 -0.0501 0.2659  0.1396  213 LEU E CD2 
13287 N N   . PRO E 214 ? 2.6751 2.7534 2.4457 -0.0774 0.3295  0.1523  214 PRO E N   
13288 C CA  . PRO E 214 ? 2.5156 2.6186 2.3269 -0.0808 0.3349  0.1488  214 PRO E CA  
13289 C C   . PRO E 214 ? 2.3869 2.5108 2.2236 -0.0739 0.3267  0.1392  214 PRO E C   
13290 O O   . PRO E 214 ? 2.3376 2.4829 2.2007 -0.0746 0.3359  0.1340  214 PRO E O   
13291 C CB  . PRO E 214 ? 2.5091 2.6173 2.3198 -0.0864 0.3571  0.1496  214 PRO E CB  
13292 C CG  . PRO E 214 ? 2.6045 2.7005 2.3823 -0.0817 0.3613  0.1477  214 PRO E CG  
13293 C CD  . PRO E 214 ? 2.6911 2.7638 2.4386 -0.0778 0.3450  0.1516  214 PRO E CD  
13294 N N   . GLY E 215 ? 2.3915 2.5096 2.2209 -0.0672 0.3092  0.1369  215 GLY E N   
13295 C CA  . GLY E 215 ? 2.0874 2.2234 1.9382 -0.0606 0.3010  0.1283  215 GLY E CA  
13296 C C   . GLY E 215 ? 1.8682 2.0021 1.7243 -0.0562 0.2807  0.1275  215 GLY E C   
13297 O O   . GLY E 215 ? 1.8960 2.0188 1.7474 -0.0589 0.2730  0.1334  215 GLY E O   
13298 N N   . PHE E 216 ? 1.6742 1.8187 1.5403 -0.0493 0.2720  0.1204  216 PHE E N   
13299 C CA  . PHE E 216 ? 1.6314 1.7768 1.5053 -0.0449 0.2532  0.1188  216 PHE E CA  
13300 C C   . PHE E 216 ? 1.6842 1.8082 1.5254 -0.0403 0.2424  0.1202  216 PHE E C   
13301 O O   . PHE E 216 ? 1.6660 1.7791 1.4818 -0.0387 0.2483  0.1196  216 PHE E O   
13302 C CB  . PHE E 216 ? 1.5409 1.7083 1.4425 -0.0400 0.2489  0.1107  216 PHE E CB  
13303 C CG  . PHE E 216 ? 1.5252 1.6935 1.4160 -0.0347 0.2524  0.1049  216 PHE E CG  
13304 C CD1 . PHE E 216 ? 1.5307 1.7077 1.4258 -0.0360 0.2686  0.1022  216 PHE E CD1 
13305 C CD2 . PHE E 216 ? 1.5249 1.6854 1.4022 -0.0283 0.2393  0.1017  216 PHE E CD2 
13306 C CE1 . PHE E 216 ? 1.5111 1.6884 1.3965 -0.0308 0.2718  0.0964  216 PHE E CE1 
13307 C CE2 . PHE E 216 ? 1.4955 1.6562 1.3632 -0.0235 0.2423  0.0960  216 PHE E CE2 
13308 C CZ  . PHE E 216 ? 1.4715 1.6404 1.3431 -0.0246 0.2586  0.0933  216 PHE E CZ  
13309 N N   . TRP E 217 ? 1.7980 1.9165 1.6403 -0.0382 0.2262  0.1217  217 TRP E N   
13310 C CA  . TRP E 217 ? 1.8163 1.9161 1.6312 -0.0336 0.2134  0.1228  217 TRP E CA  
13311 C C   . TRP E 217 ? 1.7574 1.8660 1.5892 -0.0283 0.1964  0.1184  217 TRP E C   
13312 O O   . TRP E 217 ? 1.7386 1.8590 1.5958 -0.0298 0.1915  0.1184  217 TRP E O   
13313 C CB  . TRP E 217 ? 1.9075 1.9852 1.6989 -0.0371 0.2109  0.1316  217 TRP E CB  
13314 C CG  . TRP E 217 ? 1.9460 2.0046 1.7093 -0.0320 0.1972  0.1326  217 TRP E CG  
13315 C CD1 . TRP E 217 ? 2.0343 2.0764 1.7642 -0.0301 0.1995  0.1334  217 TRP E CD1 
13316 C CD2 . TRP E 217 ? 1.9712 2.0260 1.7378 -0.0282 0.1787  0.1327  217 TRP E CD2 
13317 N NE1 . TRP E 217 ? 2.0938 2.1219 1.8062 -0.0253 0.1831  0.1340  217 TRP E NE1 
13318 C CE2 . TRP E 217 ? 1.9924 2.0283 1.7274 -0.0241 0.1703  0.1336  217 TRP E CE2 
13319 C CE3 . TRP E 217 ? 1.9548 2.0206 1.7481 -0.0279 0.1686  0.1319  217 TRP E CE3 
13320 C CZ2 . TRP E 217 ? 1.9762 2.0044 1.7067 -0.0196 0.1521  0.1338  217 TRP E CZ2 
13321 C CZ3 . TRP E 217 ? 1.9789 2.0369 1.7673 -0.0234 0.1511  0.1320  217 TRP E CZ3 
13322 C CH2 . TRP E 217 ? 1.9787 2.0184 1.7366 -0.0193 0.1430  0.1330  217 TRP E CH2 
13323 N N   . MET E 218 ? 1.6979 1.8008 1.5154 -0.0224 0.1877  0.1144  218 MET E N   
13324 C CA  . MET E 218 ? 1.6451 1.7560 1.4770 -0.0172 0.1720  0.1099  218 MET E CA  
13325 C C   . MET E 218 ? 1.6395 1.7336 1.4438 -0.0122 0.1611  0.1089  218 MET E C   
13326 O O   . MET E 218 ? 1.6144 1.7020 1.3996 -0.0104 0.1667  0.1064  218 MET E O   
13327 C CB  . MET E 218 ? 1.5559 1.6894 1.4149 -0.0150 0.1752  0.1026  218 MET E CB  
13328 C CG  . MET E 218 ? 1.4679 1.6093 1.3398 -0.0095 0.1599  0.0977  218 MET E CG  
13329 S SD  . MET E 218 ? 1.4345 1.5825 1.3281 -0.0105 0.1470  0.1000  218 MET E SD  
13330 C CE  . MET E 218 ? 1.4136 1.5836 1.3399 -0.0153 0.1592  0.0996  218 MET E CE  
13331 N N   . ASP E 219 ? 1.5972 1.6846 1.3998 -0.0099 0.1454  0.1105  219 ASP E N   
13332 C CA  . ASP E 219 ? 1.5536 1.6272 1.3341 -0.0049 0.1327  0.1091  219 ASP E CA  
13333 C C   . ASP E 219 ? 1.5362 1.6252 1.3378 -0.0001 0.1228  0.1018  219 ASP E C   
13334 O O   . ASP E 219 ? 1.5030 1.6012 1.3255 0.0007  0.1130  0.1013  219 ASP E O   
13335 C CB  . ASP E 219 ? 1.5718 1.6285 1.3376 -0.0049 0.1212  0.1152  219 ASP E CB  
13336 C CG  . ASP E 219 ? 1.5875 1.6269 1.3251 -0.0002 0.1095  0.1146  219 ASP E CG  
13337 O OD1 . ASP E 219 ? 1.5687 1.6146 1.3112 0.0044  0.1018  0.1081  219 ASP E OD1 
13338 O OD2 . ASP E 219 ? 1.6483 1.6674 1.3587 -0.0011 0.1079  0.1207  219 ASP E OD2 
13339 N N   . ILE E 220 ? 1.5556 1.6472 1.3518 0.0029  0.1257  0.0960  220 ILE E N   
13340 C CA  . ILE E 220 ? 1.5177 1.6233 1.3329 0.0072  0.1176  0.0891  220 ILE E CA  
13341 C C   . ILE E 220 ? 1.5145 1.6072 1.3129 0.0115  0.1014  0.0880  220 ILE E C   
13342 O O   . ILE E 220 ? 1.5150 1.5943 1.2881 0.0137  0.1005  0.0863  220 ILE E O   
13343 C CB  . ILE E 220 ? 1.5224 1.6366 1.3411 0.0085  0.1281  0.0833  220 ILE E CB  
13344 C CG1 . ILE E 220 ? 1.5090 1.6366 1.3453 0.0042  0.1441  0.0845  220 ILE E CG1 
13345 C CG2 . ILE E 220 ? 1.5468 1.6739 1.3845 0.0128  0.1191  0.0767  220 ILE E CG2 
13346 C CD1 . ILE E 220 ? 1.5002 1.6159 1.3139 0.0008  0.1585  0.0880  220 ILE E CD1 
13347 N N   . GLY E 221 ? 1.5311 1.6281 1.3441 0.0127  0.0884  0.0888  221 GLY E N   
13348 C CA  . GLY E 221 ? 1.5819 1.6690 1.3831 0.0168  0.0722  0.0875  221 GLY E CA  
13349 C C   . GLY E 221 ? 1.5919 1.6948 1.4195 0.0196  0.0615  0.0827  221 GLY E C   
13350 O O   . GLY E 221 ? 1.6382 1.7361 1.4623 0.0228  0.0471  0.0816  221 GLY E O   
13351 N N   . GLN E 222 ? 1.5288 1.6512 1.3833 0.0185  0.0684  0.0798  222 GLN E N   
13352 C CA  . GLN E 222 ? 1.5241 1.6631 1.4049 0.0208  0.0600  0.0755  222 GLN E CA  
13353 C C   . GLN E 222 ? 1.5270 1.6826 1.4264 0.0204  0.0703  0.0715  222 GLN E C   
13354 O O   . GLN E 222 ? 1.5374 1.6962 1.4382 0.0174  0.0838  0.0731  222 GLN E O   
13355 C CB  . GLN E 222 ? 1.5607 1.7076 1.4609 0.0194  0.0539  0.0785  222 GLN E CB  
13356 C CG  . GLN E 222 ? 1.5882 1.7414 1.4990 0.0148  0.0655  0.0824  222 GLN E CG  
13357 C CD  . GLN E 222 ? 1.6113 1.7669 1.5348 0.0134  0.0588  0.0857  222 GLN E CD  
13358 O OE1 . GLN E 222 ? 1.6380 1.7860 1.5560 0.0158  0.0462  0.0864  222 GLN E OE1 
13359 N NE2 . GLN E 222 ? 1.6249 1.7912 1.5657 0.0097  0.0673  0.0875  222 GLN E NE2 
13360 N N   . PRO E 223 ? 1.5205 1.6867 1.4344 0.0233  0.0643  0.0662  223 PRO E N   
13361 C CA  . PRO E 223 ? 1.5081 1.6888 1.4384 0.0235  0.0737  0.0624  223 PRO E CA  
13362 C C   . PRO E 223 ? 1.4885 1.6860 1.4437 0.0205  0.0816  0.0643  223 PRO E C   
13363 O O   . PRO E 223 ? 1.4923 1.6996 1.4574 0.0199  0.0923  0.0624  223 PRO E O   
13364 C CB  . PRO E 223 ? 1.4516 1.6390 1.3931 0.0271  0.0630  0.0574  223 PRO E CB  
13365 C CG  . PRO E 223 ? 1.5028 1.6861 1.4441 0.0279  0.0489  0.0591  223 PRO E CG  
13366 C CD  . PRO E 223 ? 1.5220 1.6869 1.4377 0.0266  0.0489  0.0637  223 PRO E CD  
13367 N N   . ARG E 224 ? 1.5392 1.7406 1.5052 0.0187  0.0766  0.0676  224 ARG E N   
13368 C CA  . ARG E 224 ? 1.5121 1.7294 1.5014 0.0156  0.0836  0.0691  224 ARG E CA  
13369 C C   . ARG E 224 ? 1.5045 1.7168 1.4853 0.0116  0.0968  0.0728  224 ARG E C   
13370 O O   . ARG E 224 ? 1.4788 1.7047 1.4784 0.0089  0.1049  0.0733  224 ARG E O   
13371 C CB  . ARG E 224 ? 1.5247 1.7475 1.5281 0.0150  0.0738  0.0709  224 ARG E CB  
13372 C CG  . ARG E 224 ? 1.5616 1.7677 1.5471 0.0138  0.0690  0.0755  224 ARG E CG  
13373 C CD  . ARG E 224 ? 1.5638 1.7755 1.5640 0.0141  0.0585  0.0763  224 ARG E CD  
13374 N NE  . ARG E 224 ? 1.6510 1.8703 1.6615 0.0178  0.0476  0.0722  224 ARG E NE  
13375 C CZ  . ARG E 224 ? 1.7035 1.9118 1.7000 0.0209  0.0370  0.0712  224 ARG E CZ  
13376 N NH1 . ARG E 224 ? 1.6622 1.8510 1.6329 0.0211  0.0353  0.0740  224 ARG E NH1 
13377 N NH2 . ARG E 224 ? 1.7971 2.0139 1.8055 0.0238  0.0279  0.0673  224 ARG E NH2 
13378 N N   . ASP E 225 ? 1.5373 1.7306 1.4903 0.0110  0.0991  0.0754  225 ASP E N   
13379 C CA  . ASP E 225 ? 1.5444 1.7323 1.4879 0.0069  0.1127  0.0790  225 ASP E CA  
13380 C C   . ASP E 225 ? 1.5541 1.7488 1.4998 0.0070  0.1257  0.0758  225 ASP E C   
13381 O O   . ASP E 225 ? 1.5491 1.7430 1.4915 0.0035  0.1385  0.0782  225 ASP E O   
13382 C CB  . ASP E 225 ? 1.5233 1.6880 1.4347 0.0063  0.1113  0.0832  225 ASP E CB  
13383 C CG  . ASP E 225 ? 1.5389 1.6960 1.4484 0.0052  0.1015  0.0878  225 ASP E CG  
13384 O OD1 . ASP E 225 ? 1.5737 1.7440 1.5072 0.0044  0.0974  0.0877  225 ASP E OD1 
13385 O OD2 . ASP E 225 ? 1.5115 1.6494 1.3955 0.0053  0.0980  0.0915  225 ASP E OD2 
13386 N N   . TYR E 226 ? 1.6001 1.8018 1.5523 0.0110  0.1228  0.0703  226 TYR E N   
13387 C CA  . TYR E 226 ? 1.5904 1.7984 1.5454 0.0118  0.1347  0.0668  226 TYR E CA  
13388 C C   . TYR E 226 ? 1.5955 1.8237 1.5790 0.0095  0.1431  0.0665  226 TYR E C   
13389 O O   . TYR E 226 ? 1.6194 1.8520 1.6048 0.0083  0.1562  0.0656  226 TYR E O   
13390 C CB  . TYR E 226 ? 1.6053 1.8136 1.5589 0.0167  0.1284  0.0610  226 TYR E CB  
13391 C CG  . TYR E 226 ? 1.6911 1.8796 1.6135 0.0189  0.1261  0.0598  226 TYR E CG  
13392 C CD1 . TYR E 226 ? 1.7561 1.9315 1.6551 0.0169  0.1363  0.0620  226 TYR E CD1 
13393 C CD2 . TYR E 226 ? 1.7189 1.9018 1.6350 0.0227  0.1136  0.0563  226 TYR E CD2 
13394 C CE1 . TYR E 226 ? 1.7822 1.9392 1.6513 0.0189  0.1340  0.0607  226 TYR E CE1 
13395 C CE2 . TYR E 226 ? 1.7507 1.9156 1.6381 0.0247  0.1109  0.0547  226 TYR E CE2 
13396 C CZ  . TYR E 226 ? 1.7721 1.9240 1.6356 0.0229  0.1209  0.0569  226 TYR E CZ  
13397 O OH  . TYR E 226 ? 1.7447 1.8783 1.5782 0.0249  0.1180  0.0552  226 TYR E OH  
13398 N N   . ILE E 227 ? 1.7672 2.0083 1.7733 0.0091  0.1357  0.0671  227 ILE E N   
13399 C CA  . ILE E 227 ? 1.7263 1.9870 1.7596 0.0070  0.1427  0.0667  227 ILE E CA  
13400 C C   . ILE E 227 ? 1.7274 1.9871 1.7615 0.0016  0.1508  0.0713  227 ILE E C   
13401 O O   . ILE E 227 ? 1.7268 1.9983 1.7754 -0.0008 0.1616  0.0710  227 ILE E O   
13402 C CB  . ILE E 227 ? 1.6892 1.9647 1.7462 0.0087  0.1322  0.0651  227 ILE E CB  
13403 C CG1 . ILE E 227 ? 1.7139 1.9822 1.7665 0.0079  0.1205  0.0680  227 ILE E CG1 
13404 C CG2 . ILE E 227 ? 1.6729 1.9521 1.7332 0.0135  0.1269  0.0605  227 ILE E CG2 
13405 C CD1 . ILE E 227 ? 1.6802 1.9625 1.7545 0.0095  0.1102  0.0663  227 ILE E CD1 
13406 N N   . THR E 228 ? 1.5735 1.8193 1.5927 -0.0005 0.1456  0.0755  228 THR E N   
13407 C CA  . THR E 228 ? 1.5220 1.7648 1.5405 -0.0060 0.1534  0.0802  228 THR E CA  
13408 C C   . THR E 228 ? 1.5085 1.7376 1.5038 -0.0081 0.1653  0.0824  228 THR E C   
13409 O O   . THR E 228 ? 1.4937 1.7252 1.4930 -0.0129 0.1765  0.0852  228 THR E O   
13410 C CB  . THR E 228 ? 1.4513 1.6851 1.4653 -0.0074 0.1429  0.0841  228 THR E CB  
13411 O OG1 . THR E 228 ? 1.4502 1.6804 1.4639 -0.0130 0.1505  0.0888  228 THR E OG1 
13412 C CG2 . THR E 228 ? 1.4334 1.6469 1.4195 -0.0046 0.1344  0.0853  228 THR E CG2 
13413 N N   . GLY E 229 ? 1.5293 1.7441 1.5003 -0.0049 0.1633  0.0812  229 GLY E N   
13414 C CA  . GLY E 229 ? 1.5648 1.7672 1.5129 -0.0065 0.1752  0.0827  229 GLY E CA  
13415 C C   . GLY E 229 ? 1.5979 1.8128 1.5568 -0.0061 0.1884  0.0787  229 GLY E C   
13416 O O   . GLY E 229 ? 1.5572 1.7678 1.5062 -0.0091 0.2019  0.0803  229 GLY E O   
13417 N N   . LEU E 230 ? 1.7412 1.9715 1.7206 -0.0024 0.1850  0.0735  230 LEU E N   
13418 C CA  . LEU E 230 ? 1.7187 1.9621 1.7112 -0.0014 0.1968  0.0695  230 LEU E CA  
13419 C C   . LEU E 230 ? 1.6884 1.9468 1.7035 -0.0062 0.2068  0.0714  230 LEU E C   
13420 O O   . LEU E 230 ? 1.6896 1.9547 1.7096 -0.0071 0.2201  0.0697  230 LEU E O   
13421 C CB  . LEU E 230 ? 1.6954 1.9504 1.7039 0.0039  0.1894  0.0639  230 LEU E CB  
13422 C CG  . LEU E 230 ? 1.6933 1.9602 1.7141 0.0063  0.1998  0.0591  230 LEU E CG  
13423 C CD1 . LEU E 230 ? 1.6953 1.9551 1.7041 0.0119  0.1950  0.0542  230 LEU E CD1 
13424 C CD2 . LEU E 230 ? 1.6996 1.9891 1.7543 0.0063  0.1992  0.0579  230 LEU E CD2 
13425 N N   . ARG E 231 ? 1.5180 1.7820 1.5472 -0.0092 0.2006  0.0745  231 ARG E N   
13426 C CA  . ARG E 231 ? 1.4875 1.7645 1.5370 -0.0143 0.2095  0.0764  231 ARG E CA  
13427 C C   . ARG E 231 ? 1.4548 1.7203 1.4873 -0.0193 0.2223  0.0805  231 ARG E C   
13428 O O   . ARG E 231 ? 1.4145 1.6897 1.4577 -0.0221 0.2356  0.0799  231 ARG E O   
13429 C CB  . ARG E 231 ? 1.5076 1.7903 1.5726 -0.0164 0.1993  0.0787  231 ARG E CB  
13430 C CG  . ARG E 231 ? 1.5683 1.8619 1.6522 -0.0224 0.2071  0.0810  231 ARG E CG  
13431 C CD  . ARG E 231 ? 1.6866 1.9991 1.7919 -0.0225 0.2181  0.0775  231 ARG E CD  
13432 N NE  . ARG E 231 ? 1.7950 2.1262 1.9296 -0.0251 0.2170  0.0770  231 ARG E NE  
13433 C CZ  . ARG E 231 ? 1.8028 2.1528 1.9603 -0.0254 0.2246  0.0740  231 ARG E CZ  
13434 N NH1 . ARG E 231 ? 1.7658 2.1185 1.9210 -0.0229 0.2341  0.0713  231 ARG E NH1 
13435 N NH2 . ARG E 231 ? 1.7513 2.1175 1.9342 -0.0278 0.2224  0.0736  231 ARG E NH2 
13436 N N   . LEU E 232 ? 1.4415 1.6864 1.4476 -0.0207 0.2185  0.0848  232 LEU E N   
13437 C CA  . LEU E 232 ? 1.4046 1.6366 1.3916 -0.0256 0.2304  0.0894  232 LEU E CA  
13438 C C   . LEU E 232 ? 1.4122 1.6425 1.3873 -0.0240 0.2433  0.0865  232 LEU E C   
13439 O O   . LEU E 232 ? 1.4049 1.6349 1.3770 -0.0285 0.2577  0.0886  232 LEU E O   
13440 C CB  . LEU E 232 ? 1.3901 1.5991 1.3488 -0.0261 0.2222  0.0945  232 LEU E CB  
13441 C CG  . LEU E 232 ? 1.3702 1.5782 1.3380 -0.0275 0.2096  0.0977  232 LEU E CG  
13442 C CD1 . LEU E 232 ? 1.4134 1.5975 1.3517 -0.0277 0.2024  0.1029  232 LEU E CD1 
13443 C CD2 . LEU E 232 ? 1.4044 1.6238 1.3947 -0.0336 0.2164  0.1001  232 LEU E CD2 
13444 N N   . TYR E 233 ? 1.4109 1.6405 1.3797 -0.0178 0.2385  0.0813  233 TYR E N   
13445 C CA  . TYR E 233 ? 1.4101 1.6380 1.3677 -0.0157 0.2500  0.0776  233 TYR E CA  
13446 C C   . TYR E 233 ? 1.3939 1.6436 1.3799 -0.0161 0.2612  0.0739  233 TYR E C   
13447 O O   . TYR E 233 ? 1.3741 1.6250 1.3571 -0.0186 0.2765  0.0739  233 TYR E O   
13448 C CB  . TYR E 233 ? 1.4145 1.6349 1.3582 -0.0089 0.2406  0.0728  233 TYR E CB  
13449 C CG  . TYR E 233 ? 1.4122 1.6314 1.3457 -0.0058 0.2513  0.0678  233 TYR E CG  
13450 C CD1 . TYR E 233 ? 1.4592 1.6616 1.3626 -0.0073 0.2604  0.0694  233 TYR E CD1 
13451 C CD2 . TYR E 233 ? 1.3947 1.6290 1.3482 -0.0014 0.2523  0.0614  233 TYR E CD2 
13452 C CE1 . TYR E 233 ? 1.4687 1.6699 1.3624 -0.0042 0.2705  0.0642  233 TYR E CE1 
13453 C CE2 . TYR E 233 ? 1.3919 1.6249 1.3368 0.0018  0.2621  0.0564  233 TYR E CE2 
13454 C CZ  . TYR E 233 ? 1.4367 1.6533 1.3516 0.0004  0.2713  0.0575  233 TYR E CZ  
13455 O OH  . TYR E 233 ? 1.4600 1.6752 1.3659 0.0037  0.2814  0.0519  233 TYR E OH  
13456 N N   . LEU E 234 ? 1.3956 1.6628 1.4094 -0.0135 0.2538  0.0707  234 LEU E N   
13457 C CA  . LEU E 234 ? 1.4030 1.6915 1.4450 -0.0134 0.2629  0.0672  234 LEU E CA  
13458 C C   . LEU E 234 ? 1.3948 1.6917 1.4511 -0.0203 0.2728  0.0709  234 LEU E C   
13459 O O   . LEU E 234 ? 1.4270 1.7371 1.4988 -0.0214 0.2853  0.0688  234 LEU E O   
13460 C CB  . LEU E 234 ? 1.4628 1.7670 1.5299 -0.0091 0.2516  0.0637  234 LEU E CB  
13461 C CG  . LEU E 234 ? 1.4834 1.7840 1.5431 -0.0021 0.2448  0.0586  234 LEU E CG  
13462 C CD1 . LEU E 234 ? 1.6825 2.0010 1.7701 0.0014  0.2363  0.0556  234 LEU E CD1 
13463 C CD2 . LEU E 234 ? 1.4600 1.7577 1.5092 0.0002  0.2576  0.0547  234 LEU E CD2 
13464 N N   . ASP E 235 ? 1.3992 1.6888 1.4515 -0.0249 0.2674  0.0764  235 ASP E N   
13465 C CA  . ASP E 235 ? 1.3868 1.6820 1.4507 -0.0322 0.2769  0.0802  235 ASP E CA  
13466 C C   . ASP E 235 ? 1.3457 1.6311 1.3910 -0.0357 0.2931  0.0823  235 ASP E C   
13467 O O   . ASP E 235 ? 1.3067 1.6041 1.3674 -0.0396 0.3063  0.0820  235 ASP E O   
13468 C CB  . ASP E 235 ? 1.4361 1.7229 1.4972 -0.0360 0.2670  0.0855  235 ASP E CB  
13469 C CG  . ASP E 235 ? 1.5131 1.8071 1.5899 -0.0436 0.2752  0.0890  235 ASP E CG  
13470 O OD1 . ASP E 235 ? 1.5325 1.8424 1.6288 -0.0455 0.2866  0.0867  235 ASP E OD1 
13471 O OD2 . ASP E 235 ? 1.5849 1.8685 1.6552 -0.0476 0.2702  0.0940  235 ASP E OD2 
13472 N N   . SER E 236 ? 1.3525 1.6163 1.3642 -0.0346 0.2923  0.0845  236 SER E N   
13473 C CA  . SER E 236 ? 1.3579 1.6112 1.3487 -0.0376 0.3079  0.0863  236 SER E CA  
13474 C C   . SER E 236 ? 1.3405 1.6058 1.3395 -0.0341 0.3195  0.0800  236 SER E C   
13475 O O   . SER E 236 ? 1.3628 1.6291 1.3585 -0.0376 0.3356  0.0807  236 SER E O   
13476 C CB  . SER E 236 ? 1.4019 1.6295 1.3540 -0.0362 0.3029  0.0894  236 SER E CB  
13477 O OG  . SER E 236 ? 1.4574 1.6742 1.3874 -0.0392 0.3181  0.0915  236 SER E OG  
13478 N N   . LEU E 237 ? 1.3302 1.6046 1.3403 -0.0273 0.3117  0.0740  237 LEU E N   
13479 C CA  . LEU E 237 ? 1.3426 1.6288 1.3629 -0.0234 0.3220  0.0676  237 LEU E CA  
13480 C C   . LEU E 237 ? 1.3369 1.6463 1.3914 -0.0264 0.3313  0.0665  237 LEU E C   
13481 O O   . LEU E 237 ? 1.3276 1.6449 1.3879 -0.0263 0.3456  0.0633  237 LEU E O   
13482 C CB  . LEU E 237 ? 1.4030 1.6918 1.4264 -0.0154 0.3105  0.0618  237 LEU E CB  
13483 C CG  . LEU E 237 ? 1.3904 1.6623 1.3835 -0.0108 0.3115  0.0587  237 LEU E CG  
13484 C CD1 . LEU E 237 ? 1.3840 1.6321 1.3431 -0.0132 0.3064  0.0640  237 LEU E CD1 
13485 C CD2 . LEU E 237 ? 1.4134 1.6891 1.4130 -0.0033 0.3001  0.0528  237 LEU E CD2 
13486 N N   . ARG E 238 ? 1.2942 1.6149 1.3719 -0.0291 0.3232  0.0686  238 ARG E N   
13487 C CA  . ARG E 238 ? 1.2762 1.6182 1.3858 -0.0327 0.3314  0.0679  238 ARG E CA  
13488 C C   . ARG E 238 ? 1.2783 1.6173 1.3825 -0.0401 0.3477  0.0716  238 ARG E C   
13489 O O   . ARG E 238 ? 1.2554 1.6118 1.3832 -0.0426 0.3587  0.0698  238 ARG E O   
13490 C CB  . ARG E 238 ? 1.2812 1.6330 1.4125 -0.0347 0.3188  0.0697  238 ARG E CB  
13491 C CG  . ARG E 238 ? 1.3851 1.7598 1.5485 -0.0304 0.3142  0.0647  238 ARG E CG  
13492 C CD  . ARG E 238 ? 1.5066 1.8810 1.6647 -0.0222 0.3118  0.0593  238 ARG E CD  
13493 N NE  . ARG E 238 ? 1.5746 1.9654 1.7516 -0.0200 0.3234  0.0546  238 ARG E NE  
13494 C CZ  . ARG E 238 ? 1.6170 2.0254 1.8191 -0.0152 0.3191  0.0504  238 ARG E CZ  
13495 N NH1 . ARG E 238 ? 1.5674 1.9794 1.7780 -0.0123 0.3038  0.0503  238 ARG E NH1 
13496 N NH2 . ARG E 238 ? 1.6578 2.0803 1.8764 -0.0131 0.3301  0.0462  238 ARG E NH2 
13497 N N   . LYS E 239 ? 1.2493 1.5668 1.3234 -0.0437 0.3494  0.0769  239 LYS E N   
13498 C CA  . LYS E 239 ? 1.2571 1.5688 1.3219 -0.0510 0.3650  0.0814  239 LYS E CA  
13499 C C   . LYS E 239 ? 1.3242 1.6276 1.3670 -0.0491 0.3787  0.0791  239 LYS E C   
13500 O O   . LYS E 239 ? 1.3667 1.6792 1.4183 -0.0524 0.3951  0.0782  239 LYS E O   
13501 C CB  . LYS E 239 ? 1.2489 1.5410 1.2930 -0.0563 0.3590  0.0891  239 LYS E CB  
13502 C CG  . LYS E 239 ? 1.2572 1.5523 1.3150 -0.0558 0.3416  0.0904  239 LYS E CG  
13503 C CD  . LYS E 239 ? 1.3065 1.5790 1.3388 -0.0588 0.3335  0.0972  239 LYS E CD  
13504 C CE  . LYS E 239 ? 1.2898 1.5658 1.3364 -0.0578 0.3164  0.0978  239 LYS E CE  
13505 N NZ  . LYS E 239 ? 1.3803 1.6355 1.3999 -0.0548 0.3030  0.1006  239 LYS E NZ  
13506 N N   . LYS E 240 ? 1.3412 1.6278 1.3556 -0.0437 0.3721  0.0779  240 LYS E N   
13507 C CA  . LYS E 240 ? 1.3578 1.6343 1.3476 -0.0416 0.3842  0.0756  240 LYS E CA  
13508 C C   . LYS E 240 ? 1.3618 1.6570 1.3725 -0.0369 0.3931  0.0676  240 LYS E C   
13509 O O   . LYS E 240 ? 1.3993 1.7017 1.4149 -0.0396 0.4103  0.0665  240 LYS E O   
13510 C CB  . LYS E 240 ? 1.3819 1.6369 1.3382 -0.0366 0.3731  0.0753  240 LYS E CB  
13511 C CG  . LYS E 240 ? 1.4311 1.6659 1.3638 -0.0407 0.3646  0.0832  240 LYS E CG  
13512 C CD  . LYS E 240 ? 1.5165 1.7424 1.4352 -0.0487 0.3794  0.0897  240 LYS E CD  
13513 C CE  . LYS E 240 ? 1.6176 1.8196 1.5066 -0.0516 0.3710  0.0974  240 LYS E CE  
13514 N NZ  . LYS E 240 ? 1.7240 1.9118 1.5904 -0.0445 0.3562  0.0950  240 LYS E NZ  
13515 N N   . SER E 241 ? 1.4015 1.7048 1.4251 -0.0296 0.3817  0.0621  241 SER E N   
13516 C CA  . SER E 241 ? 1.4553 1.7759 1.4998 -0.0242 0.3880  0.0545  241 SER E CA  
13517 C C   . SER E 241 ? 1.4550 1.7926 1.5305 -0.0206 0.3746  0.0520  241 SER E C   
13518 O O   . SER E 241 ? 1.4754 1.8079 1.5457 -0.0149 0.3606  0.0498  241 SER E O   
13519 C CB  . SER E 241 ? 1.5636 1.8720 1.5836 -0.0176 0.3897  0.0492  241 SER E CB  
13520 O OG  . SER E 241 ? 1.6174 1.9079 1.6140 -0.0147 0.3742  0.0506  241 SER E OG  
13521 N N   . PRO E 242 ? 1.4272 1.7853 1.5354 -0.0238 0.3784  0.0523  242 PRO E N   
13522 C CA  . PRO E 242 ? 1.3992 1.7737 1.5364 -0.0207 0.3656  0.0503  242 PRO E CA  
13523 C C   . PRO E 242 ? 1.4781 1.8649 1.6307 -0.0126 0.3652  0.0431  242 PRO E C   
13524 O O   . PRO E 242 ? 1.5157 1.9136 1.6883 -0.0090 0.3532  0.0415  242 PRO E O   
13525 C CB  . PRO E 242 ? 1.3823 1.7739 1.5472 -0.0274 0.3715  0.0530  242 PRO E CB  
13526 C CG  . PRO E 242 ? 1.3973 1.7888 1.5568 -0.0314 0.3911  0.0531  242 PRO E CG  
13527 C CD  . PRO E 242 ? 1.4064 1.7732 1.5258 -0.0309 0.3943  0.0547  242 PRO E CD  
13528 N N   . ALA E 243 ? 1.5822 1.9672 1.7262 -0.0097 0.3779  0.0388  243 ALA E N   
13529 C CA  . ALA E 243 ? 1.6257 2.0206 1.7829 -0.0016 0.3781  0.0317  243 ALA E CA  
13530 C C   . ALA E 243 ? 1.8012 2.1801 1.9360 0.0048  0.3672  0.0290  243 ALA E C   
13531 O O   . ALA E 243 ? 1.7777 2.1623 1.9212 0.0118  0.3660  0.0231  243 ALA E O   
13532 C CB  . ALA E 243 ? 1.5092 1.9105 1.6693 -0.0011 0.3973  0.0275  243 ALA E CB  
13533 N N   . LYS E 244 ? 2.1368 2.4959 2.2437 0.0026  0.3590  0.0330  244 LYS E N   
13534 C CA  . LYS E 244 ? 2.1655 2.5096 2.2520 0.0082  0.3470  0.0307  244 LYS E CA  
13535 C C   . LYS E 244 ? 2.1495 2.4987 2.2504 0.0103  0.3289  0.0318  244 LYS E C   
13536 O O   . LYS E 244 ? 2.1593 2.4986 2.2480 0.0151  0.3180  0.0296  244 LYS E O   
13537 C CB  . LYS E 244 ? 2.2084 2.5282 2.2566 0.0052  0.3467  0.0344  244 LYS E CB  
13538 C CG  . LYS E 244 ? 2.2265 2.5388 2.2558 0.0028  0.3646  0.0338  244 LYS E CG  
13539 C CD  . LYS E 244 ? 2.2973 2.6022 2.3112 0.0095  0.3688  0.0266  244 LYS E CD  
13540 C CE  . LYS E 244 ? 2.3607 2.6811 2.3928 0.0113  0.3854  0.0213  244 LYS E CE  
13541 N NZ  . LYS E 244 ? 2.4671 2.7814 2.4874 0.0186  0.3885  0.0134  244 LYS E NZ  
13542 N N   . LEU E 245 ? 2.0617 2.4259 2.1878 0.0067  0.3255  0.0351  245 LEU E N   
13543 C CA  . LEU E 245 ? 2.0278 2.3984 2.1689 0.0083  0.3092  0.0363  245 LEU E CA  
13544 C C   . LEU E 245 ? 1.9672 2.3599 2.1416 0.0122  0.3091  0.0325  245 LEU E C   
13545 O O   . LEU E 245 ? 1.9630 2.3713 2.1581 0.0099  0.3192  0.0322  245 LEU E O   
13546 C CB  . LEU E 245 ? 2.0215 2.3921 2.1654 0.0015  0.3042  0.0427  245 LEU E CB  
13547 C CG  . LEU E 245 ? 2.0369 2.3859 2.1493 -0.0029 0.3044  0.0474  245 LEU E CG  
13548 C CD1 . LEU E 245 ? 2.0479 2.3955 2.1547 -0.0089 0.3209  0.0499  245 LEU E CD1 
13549 C CD2 . LEU E 245 ? 2.0331 2.3784 2.1458 -0.0059 0.2905  0.0522  245 LEU E CD2 
13550 N N   . THR E 246 ? 1.8546 2.2485 2.0342 0.0181  0.2976  0.0298  246 THR E N   
13551 C CA  . THR E 246 ? 1.7265 2.1394 1.9354 0.0228  0.2965  0.0264  246 THR E CA  
13552 C C   . THR E 246 ? 1.6585 2.0897 1.8949 0.0192  0.2927  0.0296  246 THR E C   
13553 O O   . THR E 246 ? 1.7078 2.1358 1.9406 0.0142  0.2863  0.0341  246 THR E O   
13554 C CB  . THR E 246 ? 1.6810 2.0891 1.8873 0.0293  0.2841  0.0236  246 THR E CB  
13555 O OG1 . THR E 246 ? 1.5816 2.0073 1.8156 0.0340  0.2837  0.0205  246 THR E OG1 
13556 C CG2 . THR E 246 ? 1.7957 2.1984 1.9973 0.0273  0.2686  0.0277  246 THR E CG2 
13557 N N   . SER E 247 ? 1.6193 2.0697 1.8834 0.0220  0.2965  0.0268  247 SER E N   
13558 C CA  . SER E 247 ? 1.5819 2.0517 1.8741 0.0191  0.2936  0.0289  247 SER E CA  
13559 C C   . SER E 247 ? 1.5345 2.0203 1.8517 0.0254  0.2883  0.0259  247 SER E C   
13560 O O   . SER E 247 ? 1.5488 2.0322 1.8641 0.0316  0.2901  0.0218  247 SER E O   
13561 C CB  . SER E 247 ? 1.6057 2.0850 1.9085 0.0136  0.3078  0.0296  247 SER E CB  
13562 O OG  . SER E 247 ? 1.6236 2.1224 1.9548 0.0110  0.3047  0.0310  247 SER E OG  
13563 N N   . GLY E 248 ? 1.2054 1.7071 1.5457 0.0237  0.2815  0.0279  248 GLY E N   
13564 C CA  . GLY E 248 ? 1.0292 1.5471 1.3941 0.0292  0.2759  0.0258  248 GLY E CA  
13565 C C   . GLY E 248 ? 0.9247 1.4555 1.3077 0.0270  0.2648  0.0289  248 GLY E C   
13566 O O   . GLY E 248 ? 0.9469 1.4748 1.3247 0.0210  0.2615  0.0323  248 GLY E O   
13567 N N   . PRO E 249 ? 0.8227 1.3679 1.2271 0.0320  0.2589  0.0276  249 PRO E N   
13568 C CA  . PRO E 249 ? 0.7698 1.3283 1.1916 0.0303  0.2482  0.0302  249 PRO E CA  
13569 C C   . PRO E 249 ? 0.8073 1.3549 1.2147 0.0299  0.2349  0.0330  249 PRO E C   
13570 O O   . PRO E 249 ? 0.8066 1.3608 1.2214 0.0264  0.2272  0.0355  249 PRO E O   
13571 C CB  . PRO E 249 ? 0.7566 1.3317 1.2028 0.0366  0.2463  0.0280  249 PRO E CB  
13572 C CG  . PRO E 249 ? 0.7544 1.3185 1.1891 0.0429  0.2498  0.0249  249 PRO E CG  
13573 C CD  . PRO E 249 ? 0.7907 1.3399 1.2036 0.0397  0.2611  0.0238  249 PRO E CD  
13574 N N   . HIS E 250 ? 0.8733 1.4045 1.2605 0.0333  0.2320  0.0322  250 HIS E N   
13575 C CA  . HIS E 250 ? 0.8496 1.3693 1.2220 0.0332  0.2199  0.0344  250 HIS E CA  
13576 C C   . HIS E 250 ? 0.8569 1.3584 1.2036 0.0286  0.2213  0.0360  250 HIS E C   
13577 O O   . HIS E 250 ? 0.8499 1.3395 1.1815 0.0288  0.2120  0.0374  250 HIS E O   
13578 C CB  . HIS E 250 ? 0.8396 1.3529 1.2071 0.0400  0.2148  0.0325  250 HIS E CB  
13579 C CG  . HIS E 250 ? 0.9218 1.4217 1.2728 0.0426  0.2237  0.0291  250 HIS E CG  
13580 N ND1 . HIS E 250 ? 0.9411 1.4476 1.3014 0.0447  0.2356  0.0259  250 HIS E ND1 
13581 C CD2 . HIS E 250 ? 0.9644 1.4447 1.2901 0.0433  0.2225  0.0282  250 HIS E CD2 
13582 C CE1 . HIS E 250 ? 0.9813 1.4727 1.3220 0.0468  0.2417  0.0231  250 HIS E CE1 
13583 N NE2 . HIS E 250 ? 1.0095 1.4847 1.3288 0.0459  0.2337  0.0244  250 HIS E NE2 
13584 N N   . ILE E 251 ? 0.9313 1.4303 1.2728 0.0245  0.2327  0.0360  251 ILE E N   
13585 C CA  . ILE E 251 ? 0.8758 1.3567 1.1918 0.0202  0.2353  0.0379  251 ILE E CA  
13586 C C   . ILE E 251 ? 0.8545 1.3400 1.1761 0.0132  0.2356  0.0412  251 ILE E C   
13587 O O   . ILE E 251 ? 0.7885 1.2891 1.1299 0.0106  0.2420  0.0409  251 ILE E O   
13588 C CB  . ILE E 251 ? 1.0016 1.4734 1.3038 0.0207  0.2489  0.0355  251 ILE E CB  
13589 C CG1 . ILE E 251 ? 1.0536 1.5202 1.3504 0.0279  0.2481  0.0316  251 ILE E CG1 
13590 C CG2 . ILE E 251 ? 1.2062 1.6590 1.4811 0.0161  0.2515  0.0380  251 ILE E CG2 
13591 C CD1 . ILE E 251 ? 1.0794 1.5307 1.3574 0.0301  0.2363  0.0321  251 ILE E CD1 
13592 N N   . VAL E 252 ? 0.9352 1.4078 1.2401 0.0101  0.2285  0.0441  252 VAL E N   
13593 C CA  . VAL E 252 ? 0.9438 1.4174 1.2509 0.0034  0.2279  0.0474  252 VAL E CA  
13594 C C   . VAL E 252 ? 1.0735 1.5258 1.3524 0.0001  0.2302  0.0499  252 VAL E C   
13595 O O   . VAL E 252 ? 1.1246 1.5621 1.3838 0.0028  0.2236  0.0500  252 VAL E O   
13596 C CB  . VAL E 252 ? 0.8699 1.3512 1.1885 0.0032  0.2145  0.0487  252 VAL E CB  
13597 C CG1 . VAL E 252 ? 0.8486 1.3525 1.1964 0.0047  0.2137  0.0470  252 VAL E CG1 
13598 C CG2 . VAL E 252 ? 0.8998 1.3712 1.2055 0.0076  0.2033  0.0485  252 VAL E CG2 
13599 N N   . GLY E 253 ? 1.2329 1.6835 1.5100 -0.0058 0.2395  0.0519  253 GLY E N   
13600 C CA  . GLY E 253 ? 1.3351 1.7656 1.5859 -0.0095 0.2425  0.0550  253 GLY E CA  
13601 C C   . GLY E 253 ? 1.4749 1.8927 1.7051 -0.0074 0.2520  0.0536  253 GLY E C   
13602 O O   . GLY E 253 ? 1.4922 1.9189 1.7317 -0.0057 0.2623  0.0507  253 GLY E O   
13603 N N   . ASN E 254 ? 1.6241 2.0214 1.8261 -0.0072 0.2485  0.0554  254 ASN E N   
13604 C CA  . ASN E 254 ? 1.8208 2.2034 1.9990 -0.0054 0.2566  0.0541  254 ASN E CA  
13605 C C   . ASN E 254 ? 2.0342 2.4098 2.2022 0.0013  0.2472  0.0510  254 ASN E C   
13606 O O   . ASN E 254 ? 1.9413 2.3086 2.1004 0.0022  0.2347  0.0525  254 ASN E O   
13607 C CB  . ASN E 254 ? 1.6842 2.0475 1.8361 -0.0103 0.2596  0.0586  254 ASN E CB  
13608 C CG  . ASN E 254 ? 1.6051 1.9740 1.7669 -0.0175 0.2684  0.0622  254 ASN E CG  
13609 O OD1 . ASN E 254 ? 1.5926 1.9794 1.7787 -0.0189 0.2755  0.0605  254 ASN E OD1 
13610 N ND2 . ASN E 254 ? 1.5156 1.8690 1.6588 -0.0222 0.2675  0.0671  254 ASN E ND2 
13611 N N   . VAL E 255 ? 2.9362 3.3153 3.1063 0.0060  0.2534  0.0465  255 VAL E N   
13612 C CA  . VAL E 255 ? 2.9440 3.3170 3.1062 0.0123  0.2454  0.0431  255 VAL E CA  
13613 C C   . VAL E 255 ? 2.9699 3.3316 3.1126 0.0149  0.2554  0.0397  255 VAL E C   
13614 O O   . VAL E 255 ? 2.9659 3.3352 3.1165 0.0147  0.2686  0.0377  255 VAL E O   
13615 C CB  . VAL E 255 ? 2.9078 3.2990 3.0974 0.0167  0.2403  0.0402  255 VAL E CB  
13616 C CG1 . VAL E 255 ? 2.9207 3.3043 3.1017 0.0229  0.2327  0.0367  255 VAL E CG1 
13617 C CG2 . VAL E 255 ? 2.8716 3.2740 3.0794 0.0142  0.2304  0.0432  255 VAL E CG2 
13618 N N   . LEU E 256 ? 2.0337 2.3775 2.1513 0.0174  0.2491  0.0388  256 LEU E N   
13619 C CA  . LEU E 256 ? 1.8039 2.1347 1.8997 0.0202  0.2568  0.0351  256 LEU E CA  
13620 C C   . LEU E 256 ? 1.6418 1.9722 1.7399 0.0269  0.2493  0.0300  256 LEU E C   
13621 O O   . LEU E 256 ? 1.5293 1.8491 1.6152 0.0286  0.2370  0.0301  256 LEU E O   
13622 C CB  . LEU E 256 ? 1.6308 1.9400 1.6935 0.0174  0.2559  0.0380  256 LEU E CB  
13623 C CG  . LEU E 256 ? 1.5245 1.8184 1.5608 0.0202  0.2629  0.0342  256 LEU E CG  
13624 C CD1 . LEU E 256 ? 1.5407 1.8426 1.5835 0.0200  0.2806  0.0315  256 LEU E CD1 
13625 C CD2 . LEU E 256 ? 1.4570 1.7295 1.4602 0.0173  0.2605  0.0378  256 LEU E CD2 
13626 N N   . VAL E 257 ? 1.6593 2.0012 1.7738 0.0307  0.2566  0.0256  257 VAL E N   
13627 C CA  . VAL E 257 ? 1.5725 1.9145 1.6915 0.0372  0.2508  0.0206  257 VAL E CA  
13628 C C   . VAL E 257 ? 1.6009 1.9304 1.6995 0.0405  0.2596  0.0154  257 VAL E C   
13629 O O   . VAL E 257 ? 1.6118 1.9409 1.7043 0.0388  0.2736  0.0146  257 VAL E O   
13630 C CB  . VAL E 257 ? 1.5769 1.9404 1.7296 0.0399  0.2512  0.0192  257 VAL E CB  
13631 C CG1 . VAL E 257 ? 1.6416 2.0084 1.7997 0.0453  0.2608  0.0132  257 VAL E CG1 
13632 C CG2 . VAL E 257 ? 1.5131 1.8808 1.6775 0.0420  0.2357  0.0203  257 VAL E CG2 
13633 N N   . ASP E 258 ? 1.3418 1.6609 1.4295 0.0450  0.2515  0.0116  258 ASP E N   
13634 C CA  . ASP E 258 ? 1.2369 1.5434 1.3050 0.0487  0.2584  0.0057  258 ASP E CA  
13635 C C   . ASP E 258 ? 1.2014 1.5200 1.2902 0.0540  0.2654  0.0003  258 ASP E C   
13636 O O   . ASP E 258 ? 1.2106 1.5438 1.3259 0.0561  0.2601  0.0007  258 ASP E O   
13637 C CB  . ASP E 258 ? 1.1787 1.4679 1.2256 0.0511  0.2460  0.0037  258 ASP E CB  
13638 C CG  . ASP E 258 ? 1.1471 1.4203 1.1679 0.0539  0.2528  -0.0021 258 ASP E CG  
13639 O OD1 . ASP E 258 ? 1.1257 1.4031 1.1544 0.0584  0.2604  -0.0079 258 ASP E OD1 
13640 O OD2 . ASP E 258 ? 1.2056 1.4618 1.1977 0.0518  0.2504  -0.0009 258 ASP E OD2 
13641 N N   . GLU E 259 ? 1.1459 1.4582 1.2221 0.0564  0.2775  -0.0049 259 GLU E N   
13642 C CA  . GLU E 259 ? 1.1030 1.4251 1.1972 0.0621  0.2846  -0.0107 259 GLU E CA  
13643 C C   . GLU E 259 ? 1.0864 1.4051 1.1857 0.0677  0.2729  -0.0145 259 GLU E C   
13644 O O   . GLU E 259 ? 1.0690 1.3994 1.1914 0.0723  0.2740  -0.0175 259 GLU E O   
13645 C CB  . GLU E 259 ? 1.0602 1.3746 1.1370 0.0635  0.3000  -0.0159 259 GLU E CB  
13646 C CG  . GLU E 259 ? 1.1046 1.3958 1.1454 0.0641  0.2970  -0.0187 259 GLU E CG  
13647 C CD  . GLU E 259 ? 1.1349 1.4184 1.1565 0.0648  0.3130  -0.0233 259 GLU E CD  
13648 O OE1 . GLU E 259 ? 1.2232 1.5199 1.2607 0.0650  0.3268  -0.0246 259 GLU E OE1 
13649 O OE2 . GLU E 259 ? 1.1488 1.4131 1.1392 0.0653  0.3118  -0.0259 259 GLU E OE2 
13650 N N   . THR E 260 ? 1.0749 1.3776 1.1534 0.0674  0.2614  -0.0144 260 THR E N   
13651 C CA  . THR E 260 ? 1.0564 1.3544 1.1385 0.0721  0.2498  -0.0178 260 THR E CA  
13652 C C   . THR E 260 ? 1.1249 1.4351 1.2305 0.0712  0.2374  -0.0129 260 THR E C   
13653 O O   . THR E 260 ? 1.1849 1.4989 1.3052 0.0755  0.2310  -0.0152 260 THR E O   
13654 C CB  . THR E 260 ? 1.0899 1.3662 1.1406 0.0719  0.2423  -0.0199 260 THR E CB  
13655 O OG1 . THR E 260 ? 1.1414 1.4064 1.1672 0.0712  0.2539  -0.0228 260 THR E OG1 
13656 C CG2 . THR E 260 ? 1.0985 1.3682 1.1506 0.0773  0.2343  -0.0257 260 THR E CG2 
13657 N N   . ALA E 261 ? 1.1586 1.4746 1.2675 0.0659  0.2340  -0.0063 261 ALA E N   
13658 C CA  . ALA E 261 ? 1.2279 1.5548 1.3568 0.0647  0.2223  -0.0018 261 ALA E CA  
13659 C C   . ALA E 261 ? 1.3502 1.6969 1.5108 0.0674  0.2257  -0.0017 261 ALA E C   
13660 O O   . ALA E 261 ? 1.3291 1.6857 1.4998 0.0673  0.2377  -0.0024 261 ALA E O   
13661 C CB  . ALA E 261 ? 1.1690 1.4971 1.2934 0.0585  0.2190  0.0047  261 ALA E CB  
13662 N N   . THR E 262 ? 1.7158 2.0686 1.8925 0.0696  0.2148  -0.0008 262 THR E N   
13663 C CA  . THR E 262 ? 1.6777 2.0487 1.8842 0.0725  0.2156  -0.0001 262 THR E CA  
13664 C C   . THR E 262 ? 1.6431 2.0259 1.8651 0.0692  0.2058  0.0060  262 THR E C   
13665 O O   . THR E 262 ? 1.6493 2.0251 1.8634 0.0676  0.1944  0.0082  262 THR E O   
13666 C CB  . THR E 262 ? 1.6877 2.0555 1.9005 0.0788  0.2122  -0.0046 262 THR E CB  
13667 O OG1 . THR E 262 ? 1.6485 2.0335 1.8900 0.0812  0.2094  -0.0025 262 THR E OG1 
13668 C CG2 . THR E 262 ? 1.7150 2.0678 1.9124 0.0789  0.1998  -0.0051 262 THR E CG2 
13669 N N   . ILE E 263 ? 1.2379 1.6387 1.4820 0.0682  0.2103  0.0085  263 ILE E N   
13670 C CA  . ILE E 263 ? 1.0094 1.4231 1.2696 0.0652  0.2024  0.0139  263 ILE E CA  
13671 C C   . ILE E 263 ? 0.9439 1.3731 1.2308 0.0694  0.1999  0.0140  263 ILE E C   
13672 O O   . ILE E 263 ? 1.0191 1.4559 1.3182 0.0729  0.2085  0.0112  263 ILE E O   
13673 C CB  . ILE E 263 ? 0.9102 1.3319 1.1732 0.0596  0.2088  0.0170  263 ILE E CB  
13674 C CG1 . ILE E 263 ? 0.9868 1.3921 1.2224 0.0554  0.2104  0.0177  263 ILE E CG1 
13675 C CG2 . ILE E 263 ? 0.9106 1.3467 1.1917 0.0569  0.2008  0.0218  263 ILE E CG2 
13676 C CD1 . ILE E 263 ? 0.9270 1.3382 1.1641 0.0495  0.2161  0.0213  263 ILE E CD1 
13677 N N   . GLY E 264 ? 0.8417 1.2755 1.1374 0.0692  0.1881  0.0174  264 GLY E N   
13678 C CA  . GLY E 264 ? 0.7579 1.2067 1.0784 0.0726  0.1847  0.0187  264 GLY E CA  
13679 C C   . GLY E 264 ? 0.7475 1.2153 1.0878 0.0704  0.1890  0.0213  264 GLY E C   
13680 O O   . GLY E 264 ? 0.7772 1.2467 1.1130 0.0661  0.1955  0.0219  264 GLY E O   
13681 N N   . GLU E 265 ? 0.6788 1.1608 1.0413 0.0734  0.1850  0.0229  265 GLU E N   
13682 C CA  . GLU E 265 ? 0.6627 1.1640 1.0462 0.0720  0.1879  0.0250  265 GLU E CA  
13683 C C   . GLU E 265 ? 0.6376 1.1463 1.0256 0.0676  0.1784  0.0298  265 GLU E C   
13684 O O   . GLU E 265 ? 0.6641 1.1664 1.0451 0.0672  0.1686  0.0318  265 GLU E O   
13685 C CB  . GLU E 265 ? 0.7002 1.2139 1.1060 0.0780  0.1889  0.0241  265 GLU E CB  
13686 C CG  . GLU E 265 ? 0.8047 1.3140 1.2100 0.0828  0.1993  0.0189  265 GLU E CG  
13687 C CD  . GLU E 265 ? 0.8511 1.3672 1.2596 0.0804  0.2120  0.0168  265 GLU E CD  
13688 O OE1 . GLU E 265 ? 0.8353 1.3624 1.2515 0.0755  0.2123  0.0197  265 GLU E OE1 
13689 O OE2 . GLU E 265 ? 0.9045 1.4151 1.3082 0.0833  0.2219  0.0122  265 GLU E OE2 
13690 N N   . GLY E 266 ? 0.6776 1.2002 1.0780 0.0642  0.1817  0.0314  266 GLY E N   
13691 C CA  . GLY E 266 ? 0.6918 1.2226 1.0978 0.0601  0.1734  0.0353  266 GLY E CA  
13692 C C   . GLY E 266 ? 0.7371 1.2552 1.1230 0.0551  0.1695  0.0367  266 GLY E C   
13693 O O   . GLY E 266 ? 0.7633 1.2833 1.1496 0.0532  0.1600  0.0396  266 GLY E O   
13694 N N   . CYS E 267 ? 0.8397 1.3447 1.2077 0.0530  0.1766  0.0348  267 CYS E N   
13695 C CA  . CYS E 267 ? 0.8062 1.2981 1.1542 0.0486  0.1731  0.0362  267 CYS E CA  
13696 C C   . CYS E 267 ? 0.8434 1.3400 1.1924 0.0428  0.1785  0.0376  267 CYS E C   
13697 O O   . CYS E 267 ? 0.8844 1.3938 1.2488 0.0421  0.1857  0.0371  267 CYS E O   
13698 C CB  . CYS E 267 ? 0.8434 1.3157 1.1681 0.0500  0.1763  0.0335  267 CYS E CB  
13699 S SG  . CYS E 267 ? 0.8637 1.3289 1.1871 0.0568  0.1717  0.0308  267 CYS E SG  
13700 N N   . LEU E 268 ? 0.7831 1.2691 1.1162 0.0387  0.1747  0.0394  268 LEU E N   
13701 C CA  . LEU E 268 ? 0.8181 1.3055 1.1496 0.0329  0.1795  0.0409  268 LEU E CA  
13702 C C   . LEU E 268 ? 0.7538 1.2215 1.0590 0.0303  0.1791  0.0416  268 LEU E C   
13703 O O   . LEU E 268 ? 0.7696 1.2296 1.0653 0.0299  0.1693  0.0429  268 LEU E O   
13704 C CB  . LEU E 268 ? 0.8865 1.3872 1.2332 0.0299  0.1724  0.0435  268 LEU E CB  
13705 C CG  . LEU E 268 ? 0.8976 1.4036 1.2490 0.0242  0.1786  0.0446  268 LEU E CG  
13706 C CD1 . LEU E 268 ? 0.8845 1.3983 1.2461 0.0244  0.1910  0.0426  268 LEU E CD1 
13707 C CD2 . LEU E 268 ? 0.9619 1.4822 1.3300 0.0218  0.1713  0.0462  268 LEU E CD2 
13708 N N   . ILE E 269 ? 0.7862 1.2460 1.0799 0.0286  0.1897  0.0406  269 ILE E N   
13709 C CA  . ILE E 269 ? 0.8201 1.2600 1.0869 0.0268  0.1905  0.0411  269 ILE E CA  
13710 C C   . ILE E 269 ? 0.8634 1.3014 1.1256 0.0207  0.1971  0.0435  269 ILE E C   
13711 O O   . ILE E 269 ? 0.8855 1.3329 1.1589 0.0189  0.2073  0.0431  269 ILE E O   
13712 C CB  . ILE E 269 ? 0.8733 1.3021 1.1259 0.0306  0.1974  0.0376  269 ILE E CB  
13713 C CG1 . ILE E 269 ? 0.7641 1.1935 1.0212 0.0364  0.1903  0.0352  269 ILE E CG1 
13714 C CG2 . ILE E 269 ? 1.0359 1.4442 1.2596 0.0285  0.1985  0.0382  269 ILE E CG2 
13715 C CD1 . ILE E 269 ? 0.7863 1.2307 1.0653 0.0405  0.1952  0.0328  269 ILE E CD1 
13716 N N   . GLY E 270 ? 0.8955 1.3216 1.1421 0.0176  0.1911  0.0462  270 GLY E N   
13717 C CA  . GLY E 270 ? 0.9283 1.3501 1.1687 0.0117  0.1963  0.0490  270 GLY E CA  
13718 C C   . GLY E 270 ? 0.9447 1.3702 1.1916 0.0083  0.1871  0.0518  270 GLY E C   
13719 O O   . GLY E 270 ? 0.8726 1.3080 1.1333 0.0103  0.1779  0.0515  270 GLY E O   
13720 N N   . PRO E 271 ? 0.9637 1.3808 1.2006 0.0032  0.1897  0.0547  271 PRO E N   
13721 C CA  . PRO E 271 ? 1.1739 1.5784 1.3932 0.0005  0.2008  0.0557  271 PRO E CA  
13722 C C   . PRO E 271 ? 1.2927 1.6755 1.4826 0.0020  0.1971  0.0564  271 PRO E C   
13723 O O   . PRO E 271 ? 1.2431 1.6204 1.4273 0.0040  0.1852  0.0567  271 PRO E O   
13724 C CB  . PRO E 271 ? 1.2042 1.6104 1.4284 -0.0061 0.2038  0.0591  271 PRO E CB  
13725 C CG  . PRO E 271 ? 1.1047 1.5262 1.3511 -0.0064 0.1945  0.0589  271 PRO E CG  
13726 C CD  . PRO E 271 ? 0.9865 1.4079 1.2318 -0.0009 0.1835  0.0571  271 PRO E CD  
13727 N N   . ASP E 272 ? 1.6518 2.0230 1.8238 0.0011  0.2073  0.0566  272 ASP E N   
13728 C CA  . ASP E 272 ? 1.6981 2.0477 1.8400 0.0020  0.2051  0.0574  272 ASP E CA  
13729 C C   . ASP E 272 ? 1.7021 2.0474 1.8380 0.0079  0.1958  0.0542  272 ASP E C   
13730 O O   . ASP E 272 ? 1.7098 2.0480 1.8384 0.0091  0.1837  0.0550  272 ASP E O   
13731 C CB  . ASP E 272 ? 1.7198 2.0579 1.8496 -0.0021 0.1989  0.0621  272 ASP E CB  
13732 C CG  . ASP E 272 ? 1.7581 2.0991 1.8936 -0.0084 0.2081  0.0654  272 ASP E CG  
13733 O OD1 . ASP E 272 ? 1.7954 2.1464 1.9483 -0.0112 0.2039  0.0669  272 ASP E OD1 
13734 O OD2 . ASP E 272 ? 1.7590 2.0928 1.8820 -0.0107 0.2200  0.0664  272 ASP E OD2 
13735 N N   . VAL E 273 ? 1.5976 1.9477 1.7376 0.0118  0.2019  0.0501  273 VAL E N   
13736 C CA  . VAL E 273 ? 1.4815 1.8275 1.6166 0.0174  0.1950  0.0465  273 VAL E CA  
13737 C C   . VAL E 273 ? 1.5494 1.8844 1.6661 0.0197  0.2043  0.0434  273 VAL E C   
13738 O O   . VAL E 273 ? 1.7414 2.0820 1.8630 0.0188  0.2172  0.0423  273 VAL E O   
13739 C CB  . VAL E 273 ? 1.3753 1.7398 1.5375 0.0207  0.1915  0.0441  273 VAL E CB  
13740 C CG1 . VAL E 273 ? 1.2923 1.6514 1.4492 0.0261  0.1838  0.0408  273 VAL E CG1 
13741 C CG2 . VAL E 273 ? 1.1959 1.5725 1.3765 0.0183  0.1834  0.0470  273 VAL E CG2 
13742 N N   . ALA E 274 ? 1.3532 1.6728 1.4490 0.0226  0.1978  0.0416  274 ALA E N   
13743 C CA  . ALA E 274 ? 1.3174 1.6245 1.3928 0.0251  0.2051  0.0380  274 ALA E CA  
13744 C C   . ALA E 274 ? 1.1983 1.5025 1.2728 0.0307  0.1970  0.0334  274 ALA E C   
13745 O O   . ALA E 274 ? 1.1653 1.4611 1.2309 0.0316  0.1846  0.0338  274 ALA E O   
13746 C CB  . ALA E 274 ? 1.3767 1.6638 1.4212 0.0223  0.2059  0.0406  274 ALA E CB  
13747 N N   . ILE E 275 ? 1.1951 1.5064 1.2797 0.0344  0.2039  0.0289  275 ILE E N   
13748 C CA  . ILE E 275 ? 1.1560 1.4653 1.2423 0.0397  0.1974  0.0243  275 ILE E CA  
13749 C C   . ILE E 275 ? 1.1541 1.4477 1.2161 0.0423  0.2037  0.0197  275 ILE E C   
13750 O O   . ILE E 275 ? 1.2094 1.5048 1.2699 0.0426  0.2171  0.0176  275 ILE E O   
13751 C CB  . ILE E 275 ? 1.1429 1.4708 1.2586 0.0427  0.1996  0.0223  275 ILE E CB  
13752 C CG1 . ILE E 275 ? 1.2076 1.5511 1.3463 0.0402  0.1933  0.0267  275 ILE E CG1 
13753 C CG2 . ILE E 275 ? 1.1452 1.4695 1.2619 0.0481  0.1931  0.0178  275 ILE E CG2 
13754 C CD1 . ILE E 275 ? 1.2532 1.6151 1.4204 0.0431  0.1947  0.0254  275 ILE E CD1 
13755 N N   . GLY E 276 ? 1.0869 1.3657 1.1304 0.0442  0.1940  0.0177  276 GLY E N   
13756 C CA  . GLY E 276 ? 1.1151 1.3783 1.1344 0.0468  0.1983  0.0128  276 GLY E CA  
13757 C C   . GLY E 276 ? 1.1087 1.3773 1.1392 0.0519  0.2040  0.0066  276 GLY E C   
13758 O O   . GLY E 276 ? 1.1345 1.4195 1.1922 0.0534  0.2049  0.0066  276 GLY E O   
13759 N N   . PRO E 277 ? 1.0844 1.3390 1.0937 0.0547  0.2079  0.0013  277 PRO E N   
13760 C CA  . PRO E 277 ? 1.0698 1.3274 1.0878 0.0599  0.2132  -0.0053 277 PRO E CA  
13761 C C   . PRO E 277 ? 1.0637 1.3200 1.0901 0.0635  0.2002  -0.0081 277 PRO E C   
13762 O O   . PRO E 277 ? 1.0875 1.3368 1.1065 0.0621  0.1873  -0.0062 277 PRO E O   
13763 C CB  . PRO E 277 ? 1.1673 1.4085 1.1560 0.0611  0.2218  -0.0100 277 PRO E CB  
13764 C CG  . PRO E 277 ? 1.2255 1.4510 1.1880 0.0579  0.2133  -0.0068 277 PRO E CG  
13765 C CD  . PRO E 277 ? 1.1677 1.4028 1.1431 0.0531  0.2085  0.0010  277 PRO E CD  
13766 N N   . GLY E 278 ? 1.0538 1.3171 1.0964 0.0681  0.2039  -0.0126 278 GLY E N   
13767 C CA  . GLY E 278 ? 1.0666 1.3286 1.1183 0.0715  0.1930  -0.0155 278 GLY E CA  
13768 C C   . GLY E 278 ? 1.0281 1.3023 1.1020 0.0700  0.1820  -0.0102 278 GLY E C   
13769 O O   . GLY E 278 ? 1.0195 1.2917 1.0996 0.0721  0.1719  -0.0118 278 GLY E O   
13770 N N   . CYS E 279 ? 1.0343 1.3211 1.1204 0.0663  0.1839  -0.0043 279 CYS E N   
13771 C CA  . CYS E 279 ? 1.1161 1.4149 1.2226 0.0647  0.1739  0.0006  279 CYS E CA  
13772 C C   . CYS E 279 ? 1.2420 1.5568 1.3769 0.0679  0.1762  0.0001  279 CYS E C   
13773 O O   . CYS E 279 ? 1.2653 1.5850 1.4071 0.0707  0.1869  -0.0029 279 CYS E O   
13774 C CB  . CYS E 279 ? 1.0527 1.3581 1.1607 0.0594  0.1747  0.0067  279 CYS E CB  
13775 S SG  . CYS E 279 ? 0.9905 1.2771 1.0652 0.0556  0.1736  0.0081  279 CYS E SG  
13776 N N   . ILE E 280 ? 1.4139 1.7371 1.5654 0.0677  0.1658  0.0032  280 ILE E N   
13777 C CA  . ILE E 280 ? 1.3799 1.7182 1.5583 0.0707  0.1658  0.0038  280 ILE E CA  
13778 C C   . ILE E 280 ? 1.3434 1.6962 1.5385 0.0672  0.1599  0.0101  280 ILE E C   
13779 O O   . ILE E 280 ? 1.3406 1.6923 1.5367 0.0659  0.1487  0.0124  280 ILE E O   
13780 C CB  . ILE E 280 ? 1.3988 1.7310 1.5803 0.0747  0.1584  0.0006  280 ILE E CB  
13781 C CG1 . ILE E 280 ? 1.4461 1.7614 1.6072 0.0777  0.1627  -0.0062 280 ILE E CG1 
13782 C CG2 . ILE E 280 ? 1.4045 1.7513 1.6126 0.0783  0.1598  0.0013  280 ILE E CG2 
13783 C CD1 . ILE E 280 ? 1.5256 1.8332 1.6887 0.0814  0.1555  -0.0100 280 ILE E CD1 
13784 N N   . VAL E 281 ? 1.1495 1.5161 1.3581 0.0658  0.1676  0.0124  281 VAL E N   
13785 C CA  . VAL E 281 ? 0.9827 1.3639 1.2077 0.0626  0.1630  0.0178  281 VAL E CA  
13786 C C   . VAL E 281 ? 0.9469 1.3436 1.1979 0.0660  0.1620  0.0185  281 VAL E C   
13787 O O   . VAL E 281 ? 1.0202 1.4236 1.2817 0.0690  0.1708  0.0163  281 VAL E O   
13788 C CB  . VAL E 281 ? 0.9356 1.3224 1.1596 0.0585  0.1712  0.0201  281 VAL E CB  
13789 C CG1 . VAL E 281 ? 0.8404 1.2443 1.0849 0.0558  0.1674  0.0247  281 VAL E CG1 
13790 C CG2 . VAL E 281 ? 0.9840 1.3552 1.1823 0.0548  0.1701  0.0207  281 VAL E CG2 
13791 N N   . GLU E 282 ? 0.7806 1.1830 1.0419 0.0656  0.1515  0.0217  282 GLU E N   
13792 C CA  . GLU E 282 ? 0.7014 1.1177 0.9860 0.0686  0.1491  0.0231  282 GLU E CA  
13793 C C   . GLU E 282 ? 0.6714 1.1059 0.9735 0.0662  0.1515  0.0268  282 GLU E C   
13794 O O   . GLU E 282 ? 0.6882 1.1240 0.9849 0.0623  0.1560  0.0278  282 GLU E O   
13795 C CB  . GLU E 282 ? 0.7087 1.1221 0.9952 0.0692  0.1371  0.0248  282 GLU E CB  
13796 C CG  . GLU E 282 ? 0.7535 1.1492 1.0244 0.0715  0.1342  0.0207  282 GLU E CG  
13797 C CD  . GLU E 282 ? 0.6988 1.0937 0.9765 0.0726  0.1236  0.0222  282 GLU E CD  
13798 O OE1 . GLU E 282 ? 0.6509 1.0583 0.9433 0.0712  0.1182  0.0268  282 GLU E OE1 
13799 O OE2 . GLU E 282 ? 0.7559 1.1375 1.0240 0.0747  0.1207  0.0188  282 GLU E OE2 
13800 N N   . SER E 283 ? 0.6543 1.1026 0.9774 0.0684  0.1483  0.0290  283 SER E N   
13801 C CA  . SER E 283 ? 0.6069 1.0735 0.9487 0.0670  0.1508  0.0317  283 SER E CA  
13802 C C   . SER E 283 ? 0.5754 1.0484 0.9199 0.0627  0.1425  0.0360  283 SER E C   
13803 O O   . SER E 283 ? 0.5762 1.0434 0.9148 0.0620  0.1334  0.0374  283 SER E O   
13804 C CB  . SER E 283 ? 0.5890 1.0675 0.9519 0.0720  0.1510  0.0320  283 SER E CB  
13805 O OG  . SER E 283 ? 0.6957 1.1728 1.0607 0.0758  0.1608  0.0280  283 SER E OG  
13806 N N   . GLY E 284 ? 0.5845 1.0699 0.9386 0.0596  0.1457  0.0377  284 GLY E N   
13807 C CA  . GLY E 284 ? 0.6458 1.1393 1.0049 0.0557  0.1385  0.0413  284 GLY E CA  
13808 C C   . GLY E 284 ? 0.7044 1.1871 1.0458 0.0511  0.1358  0.0419  284 GLY E C   
13809 O O   . GLY E 284 ? 0.7468 1.2340 1.0907 0.0484  0.1285  0.0444  284 GLY E O   
13810 N N   . VAL E 285 ? 0.6555 1.1239 0.9789 0.0503  0.1415  0.0396  285 VAL E N   
13811 C CA  . VAL E 285 ? 0.6927 1.1490 0.9977 0.0464  0.1383  0.0403  285 VAL E CA  
13812 C C   . VAL E 285 ? 0.8042 1.2659 1.1108 0.0418  0.1434  0.0417  285 VAL E C   
13813 O O   . VAL E 285 ? 0.8864 1.3585 1.2050 0.0415  0.1514  0.0413  285 VAL E O   
13814 C CB  . VAL E 285 ? 0.6506 1.0879 0.9334 0.0477  0.1409  0.0373  285 VAL E CB  
13815 C CG1 . VAL E 285 ? 0.6289 1.0606 0.9111 0.0521  0.1358  0.0354  285 VAL E CG1 
13816 C CG2 . VAL E 285 ? 0.7699 1.2049 1.0483 0.0479  0.1534  0.0350  285 VAL E CG2 
13817 N N   . ARG E 286 ? 0.7767 1.2311 1.0715 0.0381  0.1387  0.0434  286 ARG E N   
13818 C CA  . ARG E 286 ? 0.8308 1.2882 1.1259 0.0332  0.1425  0.0450  286 ARG E CA  
13819 C C   . ARG E 286 ? 0.7477 1.1868 1.0188 0.0308  0.1419  0.0453  286 ARG E C   
13820 O O   . ARG E 286 ? 0.7147 1.1478 0.9784 0.0298  0.1329  0.0465  286 ARG E O   
13821 C CB  . ARG E 286 ? 0.9712 1.4421 1.2814 0.0310  0.1356  0.0473  286 ARG E CB  
13822 C CG  . ARG E 286 ? 0.9769 1.4487 1.2860 0.0258  0.1381  0.0489  286 ARG E CG  
13823 C CD  . ARG E 286 ? 0.9003 1.3743 1.2117 0.0241  0.1503  0.0481  286 ARG E CD  
13824 N NE  . ARG E 286 ? 0.8435 1.3193 1.1560 0.0187  0.1529  0.0497  286 ARG E NE  
13825 C CZ  . ARG E 286 ? 0.8408 1.3122 1.1477 0.0157  0.1630  0.0498  286 ARG E CZ  
13826 N NH1 . ARG E 286 ? 0.8365 1.3018 1.1357 0.0178  0.1715  0.0481  286 ARG E NH1 
13827 N NH2 . ARG E 286 ? 0.8530 1.3257 1.1617 0.0105  0.1647  0.0515  286 ARG E NH2 
13828 N N   . LEU E 287 ? 0.7333 1.1638 0.9925 0.0300  0.1516  0.0442  287 LEU E N   
13829 C CA  . LEU E 287 ? 0.7486 1.1608 0.9834 0.0279  0.1521  0.0447  287 LEU E CA  
13830 C C   . LEU E 287 ? 0.7768 1.1897 1.0105 0.0227  0.1573  0.0472  287 LEU E C   
13831 O O   . LEU E 287 ? 0.7915 1.2152 1.0381 0.0211  0.1659  0.0473  287 LEU E O   
13832 C CB  . LEU E 287 ? 0.7871 1.1875 1.0065 0.0306  0.1593  0.0417  287 LEU E CB  
13833 C CG  . LEU E 287 ? 0.7207 1.1205 0.9429 0.0358  0.1544  0.0389  287 LEU E CG  
13834 C CD1 . LEU E 287 ? 0.8285 1.2156 1.0346 0.0386  0.1613  0.0353  287 LEU E CD1 
13835 C CD2 . LEU E 287 ? 0.7054 1.0999 0.9229 0.0362  0.1412  0.0398  287 LEU E CD2 
13836 N N   . SER E 288 ? 0.8016 1.2029 1.0204 0.0200  0.1518  0.0493  288 SER E N   
13837 C CA  . SER E 288 ? 0.8482 1.2487 1.0655 0.0149  0.1555  0.0521  288 SER E CA  
13838 C C   . SER E 288 ? 0.9025 1.2839 1.0958 0.0133  0.1510  0.0540  288 SER E C   
13839 O O   . SER E 288 ? 0.9429 1.3191 1.1310 0.0150  0.1401  0.0540  288 SER E O   
13840 C CB  . SER E 288 ? 0.8793 1.2955 1.1178 0.0128  0.1504  0.0534  288 SER E CB  
13841 O OG  . SER E 288 ? 0.8309 1.2483 1.0718 0.0150  0.1383  0.0533  288 SER E OG  
13842 N N   . ARG E 289 ? 1.0290 1.4000 1.2079 0.0101  0.1592  0.0556  289 ARG E N   
13843 C CA  . ARG E 289 ? 1.1087 1.4613 1.2645 0.0082  0.1558  0.0582  289 ARG E CA  
13844 C C   . ARG E 289 ? 1.1333 1.4715 1.2696 0.0121  0.1489  0.0565  289 ARG E C   
13845 O O   . ARG E 289 ? 1.2019 1.5259 1.3209 0.0115  0.1421  0.0583  289 ARG E O   
13846 C CB  . ARG E 289 ? 1.1349 1.4901 1.2978 0.0053  0.1474  0.0608  289 ARG E CB  
13847 C CG  . ARG E 289 ? 1.2940 1.6325 1.4373 0.0018  0.1473  0.0645  289 ARG E CG  
13848 C CD  . ARG E 289 ? 1.3084 1.6490 1.4593 -0.0001 0.1380  0.0664  289 ARG E CD  
13849 N NE  . ARG E 289 ? 1.5158 1.8376 1.6452 -0.0017 0.1342  0.0696  289 ARG E NE  
13850 C CZ  . ARG E 289 ? 1.6350 1.9488 1.7566 -0.0062 0.1405  0.0731  289 ARG E CZ  
13851 N NH1 . ARG E 289 ? 1.6781 2.0017 1.8125 -0.0098 0.1512  0.0736  289 ARG E NH1 
13852 N NH2 . ARG E 289 ? 1.6098 1.9058 1.7114 -0.0071 0.1360  0.0763  289 ARG E NH2 
13853 N N   . CYS E 290 ? 1.0185 1.3598 1.1575 0.0162  0.1501  0.0529  290 CYS E N   
13854 C CA  . CYS E 290 ? 0.9737 1.3027 1.0966 0.0199  0.1435  0.0506  290 CYS E CA  
13855 C C   . CYS E 290 ? 1.0080 1.3258 1.1127 0.0213  0.1528  0.0484  290 CYS E C   
13856 O O   . CYS E 290 ? 1.1375 1.4586 1.2440 0.0197  0.1650  0.0485  290 CYS E O   
13857 C CB  . CYS E 290 ? 0.9573 1.2976 1.0973 0.0237  0.1363  0.0479  290 CYS E CB  
13858 S SG  . CYS E 290 ? 0.8615 1.2204 1.0255 0.0255  0.1456  0.0457  290 CYS E SG  
13859 N N   . THR E 291 ? 0.9575 1.2619 1.0446 0.0244  0.1470  0.0460  291 THR E N   
13860 C CA  . THR E 291 ? 1.0369 1.3296 1.1050 0.0264  0.1544  0.0430  291 THR E CA  
13861 C C   . THR E 291 ? 1.0198 1.3104 1.0877 0.0312  0.1479  0.0384  291 THR E C   
13862 O O   . THR E 291 ? 1.0074 1.2946 1.0739 0.0323  0.1356  0.0383  291 THR E O   
13863 C CB  . THR E 291 ? 1.0822 1.3549 1.1205 0.0245  0.1544  0.0451  291 THR E CB  
13864 O OG1 . THR E 291 ? 1.0611 1.3224 1.0861 0.0268  0.1416  0.0439  291 THR E OG1 
13865 C CG2 . THR E 291 ? 1.1712 1.4437 1.2096 0.0196  0.1557  0.0505  291 THR E CG2 
13866 N N   . VAL E 292 ? 1.0556 1.3485 1.1257 0.0340  0.1564  0.0345  292 VAL E N   
13867 C CA  . VAL E 292 ? 1.0575 1.3483 1.1284 0.0386  0.1518  0.0297  292 VAL E CA  
13868 C C   . VAL E 292 ? 1.0736 1.3469 1.1177 0.0403  0.1563  0.0260  292 VAL E C   
13869 O O   . VAL E 292 ? 1.1230 1.3940 1.1592 0.0396  0.1687  0.0254  292 VAL E O   
13870 C CB  . VAL E 292 ? 1.0510 1.3586 1.1473 0.0411  0.1570  0.0276  292 VAL E CB  
13871 C CG1 . VAL E 292 ? 1.0267 1.3292 1.1204 0.0459  0.1552  0.0223  292 VAL E CG1 
13872 C CG2 . VAL E 292 ? 1.0194 1.3430 1.1402 0.0400  0.1497  0.0307  292 VAL E CG2 
13873 N N   . MET E 293 ? 1.0666 1.3279 1.0970 0.0425  0.1463  0.0234  293 MET E N   
13874 C CA  . MET E 293 ? 1.1297 1.3737 1.1338 0.0445  0.1490  0.0194  293 MET E CA  
13875 C C   . MET E 293 ? 1.1470 1.3931 1.1582 0.0490  0.1517  0.0132  293 MET E C   
13876 O O   . MET E 293 ? 1.1416 1.4026 1.1776 0.0505  0.1533  0.0128  293 MET E O   
13877 C CB  . MET E 293 ? 1.2299 1.4586 1.2136 0.0442  0.1363  0.0198  293 MET E CB  
13878 C CG  . MET E 293 ? 1.2679 1.4907 1.2396 0.0402  0.1344  0.0255  293 MET E CG  
13879 S SD  . MET E 293 ? 1.3356 1.5382 1.2796 0.0406  0.1205  0.0254  293 MET E SD  
13880 C CE  . MET E 293 ? 1.2257 1.4252 1.1628 0.0360  0.1196  0.0330  293 MET E CE  
13881 N N   . ARG E 294 ? 1.2429 1.4735 1.2318 0.0514  0.1521  0.0084  294 ARG E N   
13882 C CA  . ARG E 294 ? 1.2361 1.4667 1.2285 0.0557  0.1573  0.0020  294 ARG E CA  
13883 C C   . ARG E 294 ? 1.2244 1.4608 1.2349 0.0584  0.1469  -0.0001 294 ARG E C   
13884 O O   . ARG E 294 ? 1.2331 1.4670 1.2437 0.0574  0.1341  0.0015  294 ARG E O   
13885 C CB  . ARG E 294 ? 1.2977 1.5090 1.2596 0.0574  0.1595  -0.0029 294 ARG E CB  
13886 C CG  . ARG E 294 ? 1.3817 1.5853 1.3224 0.0548  0.1702  -0.0009 294 ARG E CG  
13887 C CD  . ARG E 294 ? 1.5013 1.6856 1.4110 0.0569  0.1716  -0.0062 294 ARG E CD  
13888 N NE  . ARG E 294 ? 1.5336 1.7178 1.4481 0.0616  0.1751  -0.0137 294 ARG E NE  
13889 C CZ  . ARG E 294 ? 1.6194 1.7886 1.5103 0.0642  0.1776  -0.0201 294 ARG E CZ  
13890 N NH1 . ARG E 294 ? 1.7051 1.8583 1.5652 0.0626  0.1770  -0.0194 294 ARG E NH1 
13891 N NH2 . ARG E 294 ? 1.6526 1.8225 1.5507 0.0686  0.1806  -0.0271 294 ARG E NH2 
13892 N N   . GLY E 295 ? 1.1726 1.4168 1.1990 0.0618  0.1529  -0.0037 295 GLY E N   
13893 C CA  . GLY E 295 ? 1.1959 1.4418 1.2351 0.0651  0.1450  -0.0070 295 GLY E CA  
13894 C C   . GLY E 295 ? 1.1216 1.3806 1.1844 0.0639  0.1354  -0.0027 295 GLY E C   
13895 O O   . GLY E 295 ? 1.1403 1.4026 1.2168 0.0664  0.1302  -0.0047 295 GLY E O   
13896 N N   . VAL E 296 ? 1.0764 1.3428 1.1443 0.0600  0.1329  0.0032  296 VAL E N   
13897 C CA  . VAL E 296 ? 1.1048 1.3836 1.1938 0.0588  0.1237  0.0072  296 VAL E CA  
13898 C C   . VAL E 296 ? 1.0782 1.3748 1.1936 0.0601  0.1300  0.0086  296 VAL E C   
13899 O O   . VAL E 296 ? 1.0349 1.3383 1.1545 0.0597  0.1409  0.0095  296 VAL E O   
13900 C CB  . VAL E 296 ? 1.1231 1.4027 1.2075 0.0545  0.1186  0.0125  296 VAL E CB  
13901 C CG1 . VAL E 296 ? 1.1235 1.4035 1.2001 0.0522  0.1294  0.0147  296 VAL E CG1 
13902 C CG2 . VAL E 296 ? 1.1240 1.4196 1.2327 0.0531  0.1121  0.0166  296 VAL E CG2 
13903 N N   . ARG E 297 ? 1.1600 1.4644 1.2936 0.0617  0.1229  0.0090  297 ARG E N   
13904 C CA  . ARG E 297 ? 1.1328 1.4543 1.2921 0.0631  0.1267  0.0109  297 ARG E CA  
13905 C C   . ARG E 297 ? 1.0751 1.4097 1.2498 0.0601  0.1200  0.0165  297 ARG E C   
13906 O O   . ARG E 297 ? 1.0753 1.4074 1.2490 0.0588  0.1093  0.0178  297 ARG E O   
13907 C CB  . ARG E 297 ? 1.1905 1.5113 1.3596 0.0674  0.1243  0.0075  297 ARG E CB  
13908 C CG  . ARG E 297 ? 1.1606 1.4990 1.3571 0.0688  0.1246  0.0106  297 ARG E CG  
13909 C CD  . ARG E 297 ? 1.2202 1.5566 1.4261 0.0725  0.1200  0.0083  297 ARG E CD  
13910 N NE  . ARG E 297 ? 1.4164 1.7419 1.6131 0.0765  0.1264  0.0022  297 ARG E NE  
13911 C CZ  . ARG E 297 ? 1.4692 1.7925 1.6745 0.0805  0.1251  -0.0006 297 ARG E CZ  
13912 N NH1 . ARG E 297 ? 1.5256 1.8567 1.7486 0.0808  0.1178  0.0027  297 ARG E NH1 
13913 N NH2 . ARG E 297 ? 1.4487 1.7614 1.6446 0.0842  0.1313  -0.0068 297 ARG E NH2 
13914 N N   . ILE E 298 ? 0.9234 1.2724 1.1127 0.0589  0.1263  0.0196  298 ILE E N   
13915 C CA  . ILE E 298 ? 0.8296 1.1927 1.0351 0.0563  0.1210  0.0245  298 ILE E CA  
13916 C C   . ILE E 298 ? 0.7835 1.1610 1.0128 0.0590  0.1212  0.0254  298 ILE E C   
13917 O O   . ILE E 298 ? 0.7971 1.1814 1.0357 0.0612  0.1300  0.0242  298 ILE E O   
13918 C CB  . ILE E 298 ? 0.8062 1.1751 1.0112 0.0526  0.1271  0.0273  298 ILE E CB  
13919 C CG1 . ILE E 298 ? 0.7970 1.1505 0.9775 0.0500  0.1263  0.0271  298 ILE E CG1 
13920 C CG2 . ILE E 298 ? 0.7306 1.1149 0.9539 0.0503  0.1219  0.0317  298 ILE E CG2 
13921 C CD1 . ILE E 298 ? 0.7586 1.1157 0.9372 0.0461  0.1323  0.0301  298 ILE E CD1 
13922 N N   . LYS E 299 ? 0.6990 1.0814 0.9384 0.0589  0.1116  0.0275  299 LYS E N   
13923 C CA  . LYS E 299 ? 0.6340 1.0281 0.8941 0.0616  0.1104  0.0288  299 LYS E CA  
13924 C C   . LYS E 299 ? 0.7073 1.1196 0.9852 0.0602  0.1135  0.0325  299 LYS E C   
13925 O O   . LYS E 299 ? 0.6052 1.0207 0.8799 0.0571  0.1172  0.0337  299 LYS E O   
13926 C CB  . LYS E 299 ? 0.6266 1.0189 0.8902 0.0616  0.0995  0.0300  299 LYS E CB  
13927 C CG  . LYS E 299 ? 0.6662 1.0417 0.9157 0.0635  0.0963  0.0258  299 LYS E CG  
13928 C CD  . LYS E 299 ? 0.6655 1.0407 0.9212 0.0631  0.0857  0.0272  299 LYS E CD  
13929 C CE  . LYS E 299 ? 0.6777 1.0361 0.9202 0.0646  0.0821  0.0227  299 LYS E CE  
13930 N NZ  . LYS E 299 ? 0.7565 1.1148 1.0061 0.0638  0.0721  0.0241  299 LYS E NZ  
13931 N N   . LYS E 300 ? 0.5929 1.0171 0.8898 0.0625  0.1116  0.0344  300 LYS E N   
13932 C CA  . LYS E 300 ? 0.5788 1.0206 0.8936 0.0620  0.1150  0.0372  300 LYS E CA  
13933 C C   . LYS E 300 ? 0.5652 1.0153 0.8836 0.0578  0.1090  0.0409  300 LYS E C   
13934 O O   . LYS E 300 ? 0.5617 1.0078 0.8755 0.0562  0.1005  0.0422  300 LYS E O   
13935 C CB  . LYS E 300 ? 0.5771 1.0285 0.9104 0.0661  0.1139  0.0384  300 LYS E CB  
13936 C CG  . LYS E 300 ? 0.6443 1.0919 0.9795 0.0708  0.1215  0.0348  300 LYS E CG  
13937 C CD  . LYS E 300 ? 0.7039 1.1602 1.0574 0.0750  0.1193  0.0365  300 LYS E CD  
13938 C CE  . LYS E 300 ? 0.7427 1.1882 1.0920 0.0767  0.1119  0.0362  300 LYS E CE  
13939 N NZ  . LYS E 300 ? 0.7833 1.2346 1.1490 0.0814  0.1107  0.0376  300 LYS E NZ  
13940 N N   . HIS E 301 ? 0.5969 1.0588 0.9241 0.0558  0.1137  0.0424  301 HIS E N   
13941 C CA  . HIS E 301 ? 0.5837 1.0564 0.9182 0.0523  0.1088  0.0456  301 HIS E CA  
13942 C C   . HIS E 301 ? 0.5481 1.0108 0.8668 0.0485  0.1044  0.0458  301 HIS E C   
13943 O O   . HIS E 301 ? 0.5374 1.0054 0.8597 0.0462  0.0975  0.0480  301 HIS E O   
13944 C CB  . HIS E 301 ? 0.5674 1.0505 0.9163 0.0537  0.1013  0.0484  301 HIS E CB  
13945 C CG  . HIS E 301 ? 0.5693 1.0605 0.9329 0.0580  0.1043  0.0486  301 HIS E CG  
13946 N ND1 . HIS E 301 ? 0.6269 1.1193 0.9976 0.0608  0.0988  0.0502  301 HIS E ND1 
13947 C CD2 . HIS E 301 ? 0.5852 1.0835 0.9581 0.0600  0.1122  0.0475  301 HIS E CD2 
13948 C CE1 . HIS E 301 ? 0.6083 1.1078 0.9917 0.0647  0.1028  0.0502  301 HIS E CE1 
13949 N NE2 . HIS E 301 ? 0.5902 1.0939 0.9757 0.0644  0.1109  0.0484  301 HIS E NE2 
13950 N N   . ALA E 302 ? 0.5646 1.0126 0.8654 0.0480  0.1083  0.0433  302 ALA E N   
13951 C CA  . ALA E 302 ? 0.5707 1.0083 0.8557 0.0447  0.1043  0.0436  302 ALA E CA  
13952 C C   . ALA E 302 ? 0.5705 1.0122 0.8551 0.0411  0.1094  0.0448  302 ALA E C   
13953 O O   . ALA E 302 ? 0.6820 1.1285 0.9714 0.0411  0.1184  0.0442  302 ALA E O   
13954 C CB  . ALA E 302 ? 0.5901 1.0090 0.8544 0.0459  0.1051  0.0406  302 ALA E CB  
13955 N N   . CYS E 303 ? 0.5674 1.0071 0.8469 0.0379  0.1037  0.0464  303 CYS E N   
13956 C CA  . CYS E 303 ? 0.5675 1.0097 0.8463 0.0341  0.1073  0.0477  303 CYS E CA  
13957 C C   . CYS E 303 ? 0.6040 1.0299 0.8620 0.0321  0.1045  0.0477  303 CYS E C   
13958 O O   . CYS E 303 ? 0.6671 1.0902 0.9219 0.0313  0.0956  0.0485  303 CYS E O   
13959 C CB  . CYS E 303 ? 0.6490 1.1069 0.9447 0.0322  0.1027  0.0498  303 CYS E CB  
13960 S SG  . CYS E 303 ? 0.7964 1.2573 1.0926 0.0272  0.1062  0.0512  303 CYS E SG  
13961 N N   . ILE E 304 ? 0.6109 1.0260 0.8547 0.0313  0.1122  0.0469  304 ILE E N   
13962 C CA  . ILE E 304 ? 0.7338 1.1318 0.9556 0.0297  0.1102  0.0471  304 ILE E CA  
13963 C C   . ILE E 304 ? 0.7654 1.1627 0.9840 0.0256  0.1163  0.0491  304 ILE E C   
13964 O O   . ILE E 304 ? 0.7769 1.1791 1.0005 0.0247  0.1263  0.0489  304 ILE E O   
13965 C CB  . ILE E 304 ? 0.6779 1.0612 0.8821 0.0322  0.1136  0.0444  304 ILE E CB  
13966 C CG1 . ILE E 304 ? 0.6772 1.0610 0.8857 0.0360  0.1076  0.0423  304 ILE E CG1 
13967 C CG2 . ILE E 304 ? 0.7630 1.1285 0.9435 0.0307  0.1110  0.0449  304 ILE E CG2 
13968 C CD1 . ILE E 304 ? 0.7652 1.1330 0.9551 0.0384  0.1085  0.0392  304 ILE E CD1 
13969 N N   . SER E 305 ? 0.9139 1.3053 1.1252 0.0232  0.1102  0.0510  305 SER E N   
13970 C CA  . SER E 305 ? 0.9247 1.3134 1.1319 0.0190  0.1149  0.0532  305 SER E CA  
13971 C C   . SER E 305 ? 0.9699 1.3400 1.1546 0.0181  0.1103  0.0544  305 SER E C   
13972 O O   . SER E 305 ? 0.9852 1.3518 1.1670 0.0192  0.0999  0.0543  305 SER E O   
13973 C CB  . SER E 305 ? 0.8865 1.2897 1.1124 0.0166  0.1118  0.0546  305 SER E CB  
13974 O OG  . SER E 305 ? 0.8692 1.2776 1.1024 0.0184  0.1011  0.0542  305 SER E OG  
13975 N N   . SER E 306 ? 0.9497 1.3087 1.1192 0.0159  0.1180  0.0556  306 SER E N   
13976 C CA  . SER E 306 ? 0.9746 1.3154 1.1216 0.0145  0.1148  0.0576  306 SER E CA  
13977 C C   . SER E 306 ? 0.8737 1.2032 1.0069 0.0179  0.1050  0.0560  306 SER E C   
13978 O O   . SER E 306 ? 0.8626 1.1881 0.9931 0.0180  0.0949  0.0570  306 SER E O   
13979 C CB  . SER E 306 ? 0.9975 1.3400 1.1498 0.0111  0.1108  0.0605  306 SER E CB  
13980 O OG  . SER E 306 ? 0.9489 1.3027 1.1173 0.0123  0.1013  0.0597  306 SER E OG  
13981 N N   . SER E 307 ? 0.8844 1.2089 1.0093 0.0208  0.1080  0.0533  307 SER E N   
13982 C CA  . SER E 307 ? 0.8301 1.1441 0.9424 0.0239  0.0991  0.0512  307 SER E CA  
13983 C C   . SER E 307 ? 0.8832 1.1834 0.9747 0.0254  0.1055  0.0492  307 SER E C   
13984 O O   . SER E 307 ? 1.0413 1.3414 1.1298 0.0242  0.1171  0.0494  307 SER E O   
13985 C CB  . SER E 307 ? 0.8413 1.1677 0.9717 0.0266  0.0929  0.0488  307 SER E CB  
13986 O OG  . SER E 307 ? 0.9773 1.3148 1.1238 0.0254  0.0861  0.0505  307 SER E OG  
13987 N N   . ILE E 308 ? 0.8827 1.1714 0.9601 0.0280  0.0979  0.0469  308 ILE E N   
13988 C CA  . ILE E 308 ? 0.9699 1.2438 1.0251 0.0297  0.1021  0.0444  308 ILE E CA  
13989 C C   . ILE E 308 ? 1.0325 1.3067 1.0907 0.0335  0.0967  0.0398  308 ILE E C   
13990 O O   . ILE E 308 ? 0.9711 1.2445 1.0317 0.0346  0.0851  0.0392  308 ILE E O   
13991 C CB  . ILE E 308 ? 0.9860 1.2410 1.0148 0.0288  0.0975  0.0462  308 ILE E CB  
13992 C CG1 . ILE E 308 ? 1.0828 1.3363 1.1085 0.0248  0.1029  0.0512  308 ILE E CG1 
13993 C CG2 . ILE E 308 ? 1.0867 1.3266 1.0918 0.0307  0.1016  0.0432  308 ILE E CG2 
13994 C CD1 . ILE E 308 ? 1.2216 1.4750 1.2428 0.0230  0.1180  0.0517  308 ILE E CD1 
13995 N N   . ILE E 309 ? 1.2968 1.5720 1.3552 0.0355  0.1052  0.0366  309 ILE E N   
13996 C CA  . ILE E 309 ? 1.3023 1.5776 1.3645 0.0391  0.1015  0.0321  309 ILE E CA  
13997 C C   . ILE E 309 ? 1.3526 1.6097 1.3887 0.0410  0.1029  0.0285  309 ILE E C   
13998 O O   . ILE E 309 ? 1.3675 1.6185 1.3905 0.0405  0.1135  0.0281  309 ILE E O   
13999 C CB  . ILE E 309 ? 1.2671 1.5574 1.3509 0.0407  0.1093  0.0307  309 ILE E CB  
14000 C CG1 . ILE E 309 ? 1.2539 1.5617 1.3608 0.0384  0.1098  0.0345  309 ILE E CG1 
14001 C CG2 . ILE E 309 ? 1.2666 1.5580 1.3577 0.0441  0.1033  0.0269  309 ILE E CG2 
14002 C CD1 . ILE E 309 ? 1.2034 1.5168 1.3209 0.0378  0.0974  0.0362  309 ILE E CD1 
14003 N N   . GLY E 310 ? 1.1955 1.4444 1.2242 0.0429  0.0924  0.0256  310 GLY E N   
14004 C CA  . GLY E 310 ? 1.1931 1.4245 1.1970 0.0449  0.0918  0.0215  310 GLY E CA  
14005 C C   . GLY E 310 ? 1.2283 1.4599 1.2341 0.0479  0.0993  0.0163  310 GLY E C   
14006 O O   . GLY E 310 ? 1.2629 1.5080 1.2888 0.0487  0.1062  0.0162  310 GLY E O   
14007 N N   . TRP E 311 ? 1.2984 1.5144 1.2825 0.0499  0.0976  0.0118  311 TRP E N   
14008 C CA  . TRP E 311 ? 1.3050 1.5185 1.2879 0.0532  0.1043  0.0060  311 TRP E CA  
14009 C C   . TRP E 311 ? 1.2927 1.5129 1.2946 0.0555  0.0970  0.0031  311 TRP E C   
14010 O O   . TRP E 311 ? 1.3026 1.5209 1.3065 0.0551  0.0845  0.0032  311 TRP E O   
14011 C CB  . TRP E 311 ? 1.3727 1.5664 1.3249 0.0547  0.1045  0.0015  311 TRP E CB  
14012 C CG  . TRP E 311 ? 1.4579 1.6422 1.3873 0.0528  0.1128  0.0037  311 TRP E CG  
14013 C CD1 . TRP E 311 ? 1.4497 1.6356 1.3765 0.0493  0.1139  0.0101  311 TRP E CD1 
14014 C CD2 . TRP E 311 ? 1.5582 1.7293 1.4634 0.0543  0.1215  -0.0004 311 TRP E CD2 
14015 N NE1 . TRP E 311 ? 1.5275 1.7018 1.4299 0.0483  0.1228  0.0106  311 TRP E NE1 
14016 C CE2 . TRP E 311 ? 1.5712 1.7365 1.4596 0.0513  0.1278  0.0042  311 TRP E CE2 
14017 C CE3 . TRP E 311 ? 1.5301 1.6934 1.4260 0.0579  0.1248  -0.0077 311 TRP E CE3 
14018 C CZ2 . TRP E 311 ? 1.5405 1.6930 1.4028 0.0517  0.1375  0.0021  311 TRP E CZ2 
14019 C CZ3 . TRP E 311 ? 1.5043 1.6550 1.3743 0.0585  0.1343  -0.0104 311 TRP E CZ3 
14020 C CH2 . TRP E 311 ? 1.5234 1.6690 1.3766 0.0553  0.1407  -0.0053 311 TRP E CH2 
14021 N N   . HIS E 312 ? 1.4352 1.6634 1.4515 0.0579  0.1051  0.0005  312 HIS E N   
14022 C CA  . HIS E 312 ? 1.4268 1.6586 1.4583 0.0606  0.1000  -0.0029 312 HIS E CA  
14023 C C   . HIS E 312 ? 1.3943 1.6371 1.4459 0.0590  0.0893  0.0009  312 HIS E C   
14024 O O   . HIS E 312 ? 1.3986 1.6392 1.4552 0.0599  0.0802  -0.0014 312 HIS E O   
14025 C CB  . HIS E 312 ? 1.4866 1.7012 1.4985 0.0628  0.0949  -0.0094 312 HIS E CB  
14026 C CG  . HIS E 312 ? 1.5121 1.7149 1.5018 0.0644  0.1052  -0.0136 312 HIS E CG  
14027 N ND1 . HIS E 312 ? 1.5376 1.7276 1.5007 0.0629  0.1056  -0.0132 312 HIS E ND1 
14028 C CD2 . HIS E 312 ? 1.5343 1.7363 1.5245 0.0676  0.1156  -0.0184 312 HIS E CD2 
14029 C CE1 . HIS E 312 ? 1.5551 1.7368 1.5023 0.0648  0.1162  -0.0174 312 HIS E CE1 
14030 N NE2 . HIS E 312 ? 1.5732 1.7622 1.5369 0.0678  0.1225  -0.0209 312 HIS E NE2 
14031 N N   . SER E 313 ? 1.2033 1.4581 1.2666 0.0563  0.0906  0.0066  313 SER E N   
14032 C CA  . SER E 313 ? 1.1401 1.4069 1.2232 0.0548  0.0818  0.0103  313 SER E CA  
14033 C C   . SER E 313 ? 1.0351 1.3175 1.1435 0.0563  0.0864  0.0112  313 SER E C   
14034 O O   . SER E 313 ? 1.0910 1.3744 1.2020 0.0588  0.0955  0.0086  313 SER E O   
14035 C CB  . SER E 313 ? 1.1189 1.3900 1.2012 0.0513  0.0798  0.0155  313 SER E CB  
14036 O OG  . SER E 313 ? 1.1185 1.3749 1.1781 0.0503  0.0738  0.0150  313 SER E OG  
14037 N N   . THR E 314 ? 0.9817 1.2766 1.1091 0.0549  0.0800  0.0149  314 THR E N   
14038 C CA  . THR E 314 ? 0.8660 1.1759 1.0173 0.0563  0.0830  0.0163  314 THR E CA  
14039 C C   . THR E 314 ? 0.8968 1.2212 1.0645 0.0537  0.0783  0.0216  314 THR E C   
14040 O O   . THR E 314 ? 0.9708 1.2950 1.1403 0.0523  0.0683  0.0226  314 THR E O   
14041 C CB  . THR E 314 ? 0.9688 1.2753 1.1261 0.0590  0.0784  0.0131  314 THR E CB  
14042 O OG1 . THR E 314 ? 1.0458 1.3396 1.1890 0.0618  0.0840  0.0077  314 THR E OG1 
14043 C CG2 . THR E 314 ? 0.9065 1.2285 1.0887 0.0603  0.0804  0.0156  314 THR E CG2 
14044 N N   . VAL E 315 ? 0.7981 1.1354 0.9781 0.0530  0.0855  0.0245  315 VAL E N   
14045 C CA  . VAL E 315 ? 0.7873 1.1395 0.9838 0.0507  0.0821  0.0290  315 VAL E CA  
14046 C C   . VAL E 315 ? 0.7318 1.0971 0.9500 0.0526  0.0818  0.0302  315 VAL E C   
14047 O O   . VAL E 315 ? 0.7646 1.1346 0.9904 0.0550  0.0897  0.0293  315 VAL E O   
14048 C CB  . VAL E 315 ? 0.7515 1.1100 0.9484 0.0484  0.0894  0.0315  315 VAL E CB  
14049 C CG1 . VAL E 315 ? 0.7272 1.1017 0.9423 0.0463  0.0859  0.0356  315 VAL E CG1 
14050 C CG2 . VAL E 315 ? 0.7620 1.1067 0.9368 0.0463  0.0892  0.0312  315 VAL E CG2 
14051 N N   . GLY E 316 ? 0.7405 1.1115 0.9688 0.0517  0.0730  0.0322  316 GLY E N   
14052 C CA  . GLY E 316 ? 0.6286 1.0112 0.8764 0.0534  0.0720  0.0339  316 GLY E CA  
14053 C C   . GLY E 316 ? 0.6538 1.0529 0.9174 0.0531  0.0776  0.0371  316 GLY E C   
14054 O O   . GLY E 316 ? 0.5901 0.9925 0.8511 0.0511  0.0819  0.0381  316 GLY E O   
14055 N N   . GLN E 317 ? 0.5799 0.9892 0.8605 0.0550  0.0772  0.0388  317 GLN E N   
14056 C CA  . GLN E 317 ? 0.5666 0.9923 0.8635 0.0552  0.0816  0.0417  317 GLN E CA  
14057 C C   . GLN E 317 ? 0.5523 0.9885 0.8553 0.0517  0.0768  0.0451  317 GLN E C   
14058 O O   . GLN E 317 ? 0.5689 1.0035 0.8701 0.0500  0.0689  0.0461  317 GLN E O   
14059 C CB  . GLN E 317 ? 0.5601 0.9930 0.8727 0.0585  0.0814  0.0430  317 GLN E CB  
14060 C CG  . GLN E 317 ? 0.5737 0.9974 0.8828 0.0625  0.0867  0.0394  317 GLN E CG  
14061 C CD  . GLN E 317 ? 0.5678 0.9979 0.8928 0.0660  0.0858  0.0410  317 GLN E CD  
14062 O OE1 . GLN E 317 ? 0.5870 1.0289 0.9253 0.0653  0.0813  0.0452  317 GLN E OE1 
14063 N NE2 . GLN E 317 ? 0.6813 1.1035 1.0047 0.0699  0.0900  0.0376  317 GLN E NE2 
14064 N N   . TRP E 318 ? 0.5450 0.9925 0.8559 0.0506  0.0818  0.0466  318 TRP E N   
14065 C CA  . TRP E 318 ? 0.5315 0.9903 0.8496 0.0474  0.0783  0.0494  318 TRP E CA  
14066 C C   . TRP E 318 ? 0.5357 0.9858 0.8402 0.0444  0.0735  0.0489  318 TRP E C   
14067 O O   . TRP E 318 ? 0.5377 0.9953 0.8473 0.0420  0.0687  0.0508  318 TRP E O   
14068 C CB  . TRP E 318 ? 0.5518 1.0225 0.8849 0.0480  0.0723  0.0524  318 TRP E CB  
14069 C CG  . TRP E 318 ? 0.5791 1.0620 0.9280 0.0506  0.0761  0.0539  318 TRP E CG  
14070 C CD1 . TRP E 318 ? 0.5771 1.0736 0.9372 0.0500  0.0799  0.0552  318 TRP E CD1 
14071 C CD2 . TRP E 318 ? 0.5234 1.0060 0.8792 0.0542  0.0759  0.0543  318 TRP E CD2 
14072 N NE1 . TRP E 318 ? 0.5688 1.0739 0.9423 0.0533  0.0819  0.0564  318 TRP E NE1 
14073 C CE2 . TRP E 318 ? 0.5921 1.0884 0.9631 0.0560  0.0796  0.0561  318 TRP E CE2 
14074 C CE3 . TRP E 318 ? 0.5711 1.0427 0.9219 0.0562  0.0728  0.0534  318 TRP E CE3 
14075 C CZ2 . TRP E 318 ? 0.5674 1.0666 0.9485 0.0600  0.0802  0.0572  318 TRP E CZ2 
14076 C CZ3 . TRP E 318 ? 0.5827 1.0567 0.9436 0.0598  0.0737  0.0543  318 TRP E CZ3 
14077 C CH2 . TRP E 318 ? 0.5898 1.0773 0.9655 0.0619  0.0773  0.0564  318 TRP E CH2 
14078 N N   . ALA E 319 ? 0.5517 0.9860 0.8388 0.0445  0.0746  0.0463  319 ALA E N   
14079 C CA  . ALA E 319 ? 0.5571 0.9824 0.8309 0.0420  0.0696  0.0460  319 ALA E CA  
14080 C C   . ALA E 319 ? 0.5587 0.9853 0.8287 0.0394  0.0743  0.0467  319 ALA E C   
14081 O O   . ALA E 319 ? 0.5649 0.9914 0.8335 0.0396  0.0829  0.0461  319 ALA E O   
14082 C CB  . ALA E 319 ? 0.5750 0.9823 0.8306 0.0432  0.0682  0.0429  319 ALA E CB  
14083 N N   . ARG E 320 ? 0.5536 0.9814 0.8223 0.0368  0.0687  0.0480  320 ARG E N   
14084 C CA  . ARG E 320 ? 0.5552 0.9835 0.8205 0.0340  0.0720  0.0490  320 ARG E CA  
14085 C C   . ARG E 320 ? 0.5824 0.9946 0.8282 0.0328  0.0688  0.0482  320 ARG E C   
14086 O O   . ARG E 320 ? 0.7342 1.1421 0.9763 0.0329  0.0602  0.0480  320 ARG E O   
14087 C CB  . ARG E 320 ? 0.5383 0.9812 0.8182 0.0320  0.0685  0.0509  320 ARG E CB  
14088 C CG  . ARG E 320 ? 0.5672 1.0096 0.8439 0.0289  0.0719  0.0517  320 ARG E CG  
14089 C CD  . ARG E 320 ? 0.6538 1.1098 0.9442 0.0269  0.0686  0.0529  320 ARG E CD  
14090 N NE  . ARG E 320 ? 0.7787 1.2323 1.0652 0.0238  0.0722  0.0534  320 ARG E NE  
14091 C CZ  . ARG E 320 ? 0.8363 1.2973 1.1305 0.0222  0.0797  0.0537  320 ARG E CZ  
14092 N NH1 . ARG E 320 ? 0.8348 1.3064 1.1410 0.0238  0.0841  0.0536  320 ARG E NH1 
14093 N NH2 . ARG E 320 ? 0.8408 1.2983 1.1309 0.0190  0.0827  0.0543  320 ARG E NH2 
14094 N N   . ILE E 321 ? 0.7590 1.1623 0.9926 0.0318  0.0757  0.0480  321 ILE E N   
14095 C CA  . ILE E 321 ? 0.7952 1.1820 1.0083 0.0308  0.0737  0.0477  321 ILE E CA  
14096 C C   . ILE E 321 ? 0.8101 1.1972 1.0211 0.0276  0.0784  0.0498  321 ILE E C   
14097 O O   . ILE E 321 ? 0.8323 1.2248 1.0484 0.0266  0.0875  0.0502  321 ILE E O   
14098 C CB  . ILE E 321 ? 0.8268 1.1996 1.0233 0.0328  0.0783  0.0454  321 ILE E CB  
14099 C CG1 . ILE E 321 ? 0.8228 1.1962 1.0238 0.0359  0.0746  0.0432  321 ILE E CG1 
14100 C CG2 . ILE E 321 ? 0.8790 1.2342 1.0530 0.0320  0.0749  0.0453  321 ILE E CG2 
14101 C CD1 . ILE E 321 ? 0.8339 1.2046 1.0343 0.0363  0.0630  0.0429  321 ILE E CD1 
14102 N N   . GLU E 322 ? 0.9669 1.3484 1.1715 0.0259  0.0721  0.0510  322 GLU E N   
14103 C CA  . GLU E 322 ? 0.9715 1.3523 1.1743 0.0226  0.0758  0.0530  322 GLU E CA  
14104 C C   . GLU E 322 ? 1.0075 1.3743 1.1946 0.0218  0.0690  0.0540  322 GLU E C   
14105 O O   . GLU E 322 ? 1.0217 1.3818 1.2020 0.0238  0.0607  0.0529  322 GLU E O   
14106 C CB  . GLU E 322 ? 0.9353 1.3336 1.1591 0.0209  0.0755  0.0539  322 GLU E CB  
14107 C CG  . GLU E 322 ? 0.9102 1.3142 1.1420 0.0214  0.0650  0.0538  322 GLU E CG  
14108 C CD  . GLU E 322 ? 0.8876 1.3081 1.1382 0.0196  0.0650  0.0544  322 GLU E CD  
14109 O OE1 . GLU E 322 ? 0.8525 1.2805 1.1110 0.0180  0.0727  0.0548  322 GLU E OE1 
14110 O OE2 . GLU E 322 ? 0.9352 1.3612 1.1927 0.0197  0.0574  0.0542  322 GLU E OE2 
14111 N N   . ASN E 323 ? 0.8917 1.2538 1.0735 0.0189  0.0726  0.0561  323 ASN E N   
14112 C CA  . ASN E 323 ? 0.8910 1.2416 1.0611 0.0179  0.0662  0.0577  323 ASN E CA  
14113 C C   . ASN E 323 ? 0.8527 1.1847 0.9996 0.0197  0.0629  0.0574  323 ASN E C   
14114 O O   . ASN E 323 ? 0.8322 1.1585 0.9739 0.0214  0.0529  0.0567  323 ASN E O   
14115 C CB  . ASN E 323 ? 0.8342 1.1941 1.0179 0.0184  0.0564  0.0572  323 ASN E CB  
14116 C CG  . ASN E 323 ? 0.8565 1.2065 1.0316 0.0173  0.0503  0.0588  323 ASN E CG  
14117 O OD1 . ASN E 323 ? 0.9379 1.2766 1.1004 0.0153  0.0545  0.0610  323 ASN E OD1 
14118 N ND2 . ASN E 323 ? 0.8273 1.1815 1.0096 0.0186  0.0406  0.0577  323 ASN E ND2 
14119 N N   . MET E 324 ? 0.8970 1.2197 1.0298 0.0192  0.0715  0.0578  324 MET E N   
14120 C CA  . MET E 324 ? 0.9401 1.2435 1.0478 0.0204  0.0699  0.0578  324 MET E CA  
14121 C C   . MET E 324 ? 0.9406 1.2410 1.0448 0.0239  0.0613  0.0547  324 MET E C   
14122 O O   . MET E 324 ? 0.9758 1.2642 1.0662 0.0251  0.0527  0.0546  324 MET E O   
14123 C CB  . MET E 324 ? 1.0852 1.3759 1.1794 0.0186  0.0657  0.0610  324 MET E CB  
14124 C CG  . MET E 324 ? 1.1583 1.4503 1.2549 0.0147  0.0744  0.0642  324 MET E CG  
14125 S SD  . MET E 324 ? 1.3956 1.6745 1.4811 0.0127  0.0681  0.0681  324 MET E SD  
14126 C CE  . MET E 324 ? 1.1766 1.4678 1.2817 0.0147  0.0553  0.0661  324 MET E CE  
14127 N N   . THR E 325 ? 0.9040 1.2154 1.0214 0.0256  0.0634  0.0522  325 THR E N   
14128 C CA  . THR E 325 ? 0.7858 1.0947 0.9014 0.0286  0.0563  0.0491  325 THR E CA  
14129 C C   . THR E 325 ? 0.7593 1.0531 0.8536 0.0301  0.0602  0.0472  325 THR E C   
14130 O O   . THR E 325 ? 0.8901 1.1845 0.9826 0.0300  0.0707  0.0466  325 THR E O   
14131 C CB  . THR E 325 ? 0.7792 1.1049 0.9169 0.0297  0.0571  0.0475  325 THR E CB  
14132 O OG1 . THR E 325 ? 0.8051 1.1449 0.9615 0.0282  0.0543  0.0493  325 THR E OG1 
14133 C CG2 . THR E 325 ? 0.7553 1.0783 0.8924 0.0324  0.0492  0.0446  325 THR E CG2 
14134 N N   . ILE E 326 ? 0.8096 1.0902 0.8880 0.0316  0.0515  0.0458  326 ILE E N   
14135 C CA  . ILE E 326 ? 0.7994 1.0635 0.8542 0.0330  0.0537  0.0438  326 ILE E CA  
14136 C C   . ILE E 326 ? 0.7762 1.0397 0.8328 0.0358  0.0481  0.0394  326 ILE E C   
14137 O O   . ILE E 326 ? 0.7970 1.0615 0.8586 0.0367  0.0370  0.0385  326 ILE E O   
14138 C CB  . ILE E 326 ? 0.8405 1.0878 0.8727 0.0325  0.0481  0.0458  326 ILE E CB  
14139 C CG1 . ILE E 326 ? 0.8596 1.1079 0.8925 0.0294  0.0526  0.0505  326 ILE E CG1 
14140 C CG2 . ILE E 326 ? 0.8735 1.1040 0.8798 0.0337  0.0518  0.0438  326 ILE E CG2 
14141 C CD1 . ILE E 326 ? 0.9095 1.1595 0.9409 0.0274  0.0671  0.0518  326 ILE E CD1 
14142 N N   . LEU E 327 ? 0.7673 1.0293 0.8208 0.0373  0.0557  0.0366  327 LEU E N   
14143 C CA  . LEU E 327 ? 0.8223 1.0827 0.8772 0.0399  0.0516  0.0321  327 LEU E CA  
14144 C C   . LEU E 327 ? 0.8683 1.1104 0.8970 0.0414  0.0526  0.0289  327 LEU E C   
14145 O O   . LEU E 327 ? 0.9016 1.1365 0.9157 0.0409  0.0620  0.0295  327 LEU E O   
14146 C CB  . LEU E 327 ? 0.8941 1.1681 0.9685 0.0409  0.0590  0.0309  327 LEU E CB  
14147 C CG  . LEU E 327 ? 0.8829 1.1756 0.9834 0.0397  0.0578  0.0337  327 LEU E CG  
14148 C CD1 . LEU E 327 ? 0.9522 1.2566 1.0702 0.0413  0.0636  0.0323  327 LEU E CD1 
14149 C CD2 . LEU E 327 ? 0.8032 1.0984 0.9105 0.0394  0.0450  0.0341  327 LEU E CD2 
14150 N N   . GLY E 328 ? 0.9307 1.1654 0.9533 0.0432  0.0429  0.0254  328 GLY E N   
14151 C CA  . GLY E 328 ? 0.9647 1.1823 0.9629 0.0449  0.0425  0.0215  328 GLY E CA  
14152 C C   . GLY E 328 ? 1.0022 1.2204 1.0027 0.0470  0.0503  0.0171  328 GLY E C   
14153 O O   . GLY E 328 ? 1.0020 1.2336 1.0223 0.0472  0.0571  0.0175  328 GLY E O   
14154 N N   . GLU E 329 ? 1.0563 1.2592 1.0356 0.0488  0.0493  0.0126  329 GLU E N   
14155 C CA  . GLU E 329 ? 1.1185 1.3198 1.0978 0.0512  0.0561  0.0075  329 GLU E CA  
14156 C C   . GLU E 329 ? 1.1009 1.3104 1.1007 0.0525  0.0495  0.0049  329 GLU E C   
14157 O O   . GLU E 329 ? 1.1089 1.3163 1.1106 0.0522  0.0373  0.0041  329 GLU E O   
14158 C CB  . GLU E 329 ? 1.1745 1.3566 1.1245 0.0529  0.0559  0.0029  329 GLU E CB  
14159 C CG  . GLU E 329 ? 1.1988 1.3776 1.1480 0.0558  0.0615  -0.0035 329 GLU E CG  
14160 C CD  . GLU E 329 ? 1.1894 1.3488 1.1091 0.0574  0.0598  -0.0088 329 GLU E CD  
14161 O OE1 . GLU E 329 ? 1.2709 1.4194 1.1696 0.0562  0.0552  -0.0070 329 GLU E OE1 
14162 O OE2 . GLU E 329 ? 1.1937 1.3486 1.1110 0.0600  0.0628  -0.0149 329 GLU E OE2 
14163 N N   . ASP E 330 ? 1.1351 1.3539 1.1508 0.0539  0.0576  0.0036  330 ASP E N   
14164 C CA  . ASP E 330 ? 1.1498 1.3753 1.1844 0.0553  0.0528  0.0013  330 ASP E CA  
14165 C C   . ASP E 330 ? 1.1394 1.3767 1.1930 0.0532  0.0434  0.0053  330 ASP E C   
14166 O O   . ASP E 330 ? 1.1818 1.4162 1.2371 0.0529  0.0324  0.0037  330 ASP E O   
14167 C CB  . ASP E 330 ? 1.1577 1.3685 1.1780 0.0573  0.0469  -0.0052 330 ASP E CB  
14168 C CG  . ASP E 330 ? 1.1987 1.4150 1.2381 0.0584  0.0423  -0.0076 330 ASP E CG  
14169 O OD1 . ASP E 330 ? 1.2214 1.4443 1.2736 0.0603  0.0502  -0.0085 330 ASP E OD1 
14170 O OD2 . ASP E 330 ? 1.2039 1.4177 1.2456 0.0575  0.0306  -0.0086 330 ASP E OD2 
14171 N N   . VAL E 331 ? 1.1514 1.4024 1.2195 0.0516  0.0480  0.0104  331 VAL E N   
14172 C CA  . VAL E 331 ? 1.1193 1.3834 1.2067 0.0497  0.0409  0.0143  331 VAL E CA  
14173 C C   . VAL E 331 ? 1.1896 1.4694 1.3010 0.0504  0.0463  0.0158  331 VAL E C   
14174 O O   . VAL E 331 ? 1.1662 1.4522 1.2820 0.0508  0.0566  0.0171  331 VAL E O   
14175 C CB  . VAL E 331 ? 1.0529 1.3198 1.1370 0.0473  0.0405  0.0189  331 VAL E CB  
14176 C CG1 . VAL E 331 ? 1.0842 1.3658 1.1894 0.0456  0.0342  0.0224  331 VAL E CG1 
14177 C CG2 . VAL E 331 ? 1.0410 1.2919 1.1012 0.0469  0.0342  0.0178  331 VAL E CG2 
14178 N N   . HIS E 332 ? 1.3947 1.6810 1.5217 0.0505  0.0393  0.0158  332 HIS E N   
14179 C CA  . HIS E 332 ? 1.3512 1.6507 1.5000 0.0514  0.0431  0.0171  332 HIS E CA  
14180 C C   . HIS E 332 ? 1.3029 1.6180 1.4697 0.0492  0.0393  0.0221  332 HIS E C   
14181 O O   . HIS E 332 ? 1.3071 1.6245 1.4802 0.0480  0.0300  0.0226  332 HIS E O   
14182 C CB  . HIS E 332 ? 1.3764 1.6708 1.5290 0.0532  0.0388  0.0135  332 HIS E CB  
14183 C CG  . HIS E 332 ? 1.4220 1.7011 1.5571 0.0556  0.0426  0.0080  332 HIS E CG  
14184 N ND1 . HIS E 332 ? 1.4276 1.7069 1.5668 0.0585  0.0512  0.0058  332 HIS E ND1 
14185 C CD2 . HIS E 332 ? 1.4719 1.7350 1.5850 0.0558  0.0389  0.0040  332 HIS E CD2 
14186 C CE1 . HIS E 332 ? 1.4801 1.7442 1.6005 0.0603  0.0530  0.0004  332 HIS E CE1 
14187 N NE2 . HIS E 332 ? 1.5032 1.7571 1.6070 0.0586  0.0456  -0.0008 332 HIS E NE2 
14188 N N   . VAL E 333 ? 1.0651 1.3912 1.2403 0.0486  0.0465  0.0253  333 VAL E N   
14189 C CA  . VAL E 333 ? 1.0166 1.3583 1.2089 0.0466  0.0441  0.0297  333 VAL E CA  
14190 C C   . VAL E 333 ? 0.9797 1.3336 1.1922 0.0479  0.0457  0.0310  333 VAL E C   
14191 O O   . VAL E 333 ? 0.9770 1.3334 1.1938 0.0499  0.0536  0.0305  333 VAL E O   
14192 C CB  . VAL E 333 ? 1.0512 1.3982 1.2423 0.0451  0.0506  0.0323  333 VAL E CB  
14193 C CG1 . VAL E 333 ? 1.0040 1.3668 1.2125 0.0431  0.0476  0.0362  333 VAL E CG1 
14194 C CG2 . VAL E 333 ? 1.1140 1.4473 1.2838 0.0439  0.0492  0.0315  333 VAL E CG2 
14195 N N   . SER E 334 ? 0.8687 1.2302 1.0937 0.0467  0.0382  0.0328  334 SER E N   
14196 C CA  . SER E 334 ? 0.7469 1.1198 0.9906 0.0477  0.0389  0.0349  334 SER E CA  
14197 C C   . SER E 334 ? 0.6827 1.0703 0.9387 0.0476  0.0455  0.0382  334 SER E C   
14198 O O   . SER E 334 ? 0.6663 1.0557 0.9176 0.0464  0.0492  0.0390  334 SER E O   
14199 C CB  . SER E 334 ? 0.7057 1.0838 0.9592 0.0460  0.0298  0.0365  334 SER E CB  
14200 O OG  . SER E 334 ? 0.7721 1.1373 1.0159 0.0459  0.0233  0.0331  334 SER E OG  
14201 N N   . ASP E 335 ? 0.6252 1.0231 0.8974 0.0489  0.0468  0.0403  335 ASP E N   
14202 C CA  . ASP E 335 ? 0.5630 0.9758 0.8483 0.0490  0.0520  0.0434  335 ASP E CA  
14203 C C   . ASP E 335 ? 0.5455 0.9692 0.8374 0.0460  0.0475  0.0464  335 ASP E C   
14204 O O   . ASP E 335 ? 0.5420 0.9651 0.8341 0.0444  0.0400  0.0469  335 ASP E O   
14205 C CB  . ASP E 335 ? 0.5524 0.9731 0.8530 0.0514  0.0534  0.0452  335 ASP E CB  
14206 C CG  . ASP E 335 ? 0.5876 0.9972 0.8831 0.0547  0.0572  0.0419  335 ASP E CG  
14207 O OD1 . ASP E 335 ? 0.6180 1.0174 0.8998 0.0554  0.0618  0.0384  335 ASP E OD1 
14208 O OD2 . ASP E 335 ? 0.5957 1.0067 0.9008 0.0566  0.0556  0.0428  335 ASP E OD2 
14209 N N   . GLU E 336 ? 0.5379 0.9719 0.8356 0.0452  0.0524  0.0481  336 GLU E N   
14210 C CA  . GLU E 336 ? 0.5238 0.9701 0.8301 0.0427  0.0491  0.0508  336 GLU E CA  
14211 C C   . GLU E 336 ? 0.5271 0.9666 0.8228 0.0403  0.0435  0.0498  336 GLU E C   
14212 O O   . GLU E 336 ? 0.5548 1.0025 0.8573 0.0385  0.0384  0.0514  336 GLU E O   
14213 C CB  . GLU E 336 ? 0.6003 1.0583 0.9219 0.0429  0.0449  0.0536  336 GLU E CB  
14214 C CG  . GLU E 336 ? 0.5670 1.0293 0.8982 0.0459  0.0489  0.0547  336 GLU E CG  
14215 C CD  . GLU E 336 ? 0.6210 1.0898 0.9633 0.0462  0.0438  0.0576  336 GLU E CD  
14216 O OE1 . GLU E 336 ? 0.6296 1.1046 0.9756 0.0438  0.0384  0.0592  336 GLU E OE1 
14217 O OE2 . GLU E 336 ? 0.5816 1.0489 0.9289 0.0488  0.0454  0.0581  336 GLU E OE2 
14218 N N   . ILE E 337 ? 0.5702 0.9949 0.8493 0.0404  0.0443  0.0472  337 ILE E N   
14219 C CA  . ILE E 337 ? 0.5648 0.9815 0.8328 0.0387  0.0384  0.0463  337 ILE E CA  
14220 C C   . ILE E 337 ? 0.5497 0.9666 0.8123 0.0370  0.0425  0.0469  337 ILE E C   
14221 O O   . ILE E 337 ? 0.5565 0.9709 0.8147 0.0374  0.0504  0.0466  337 ILE E O   
14222 C CB  . ILE E 337 ? 0.5650 0.9645 0.8168 0.0398  0.0356  0.0432  337 ILE E CB  
14223 C CG1 . ILE E 337 ? 0.5633 0.9624 0.8215 0.0410  0.0311  0.0424  337 ILE E CG1 
14224 C CG2 . ILE E 337 ? 0.5715 0.9627 0.8116 0.0382  0.0291  0.0424  337 ILE E CG2 
14225 C CD1 . ILE E 337 ? 0.5513 0.9583 0.8198 0.0394  0.0230  0.0440  337 ILE E CD1 
14226 N N   . TYR E 338 ? 0.5441 0.9639 0.8075 0.0350  0.0373  0.0478  338 TYR E N   
14227 C CA  . TYR E 338 ? 0.5454 0.9652 0.8049 0.0331  0.0400  0.0486  338 TYR E CA  
14228 C C   . TYR E 338 ? 0.5597 0.9644 0.8017 0.0326  0.0358  0.0475  338 TYR E C   
14229 O O   . TYR E 338 ? 0.5607 0.9613 0.8001 0.0329  0.0276  0.0466  338 TYR E O   
14230 C CB  . TYR E 338 ? 0.5287 0.9636 0.8029 0.0315  0.0376  0.0503  338 TYR E CB  
14231 C CG  . TYR E 338 ? 0.5392 0.9727 0.8092 0.0294  0.0386  0.0508  338 TYR E CG  
14232 C CD1 . TYR E 338 ? 0.6021 1.0373 0.8721 0.0282  0.0466  0.0515  338 TYR E CD1 
14233 C CD2 . TYR E 338 ? 0.5307 0.9611 0.7973 0.0285  0.0314  0.0505  338 TYR E CD2 
14234 C CE1 . TYR E 338 ? 0.6359 1.0690 0.9022 0.0259  0.0475  0.0521  338 TYR E CE1 
14235 C CE2 . TYR E 338 ? 0.5914 1.0195 0.8543 0.0266  0.0321  0.0510  338 TYR E CE2 
14236 C CZ  . TYR E 338 ? 0.6298 1.0589 0.8923 0.0252  0.0402  0.0519  338 TYR E CZ  
14237 O OH  . TYR E 338 ? 0.6869 1.1130 0.9459 0.0231  0.0409  0.0525  338 TYR E OH  
14238 N N   . SER E 339 ? 0.5907 0.9871 0.8209 0.0317  0.0412  0.0477  339 SER E N   
14239 C CA  . SER E 339 ? 0.5873 0.9683 0.7992 0.0312  0.0379  0.0472  339 SER E CA  
14240 C C   . SER E 339 ? 0.8958 1.2772 1.1060 0.0289  0.0406  0.0491  339 SER E C   
14241 O O   . SER E 339 ? 0.6089 0.9935 0.8210 0.0277  0.0492  0.0501  339 SER E O   
14242 C CB  . SER E 339 ? 0.6573 1.0234 0.8516 0.0326  0.0422  0.0456  339 SER E CB  
14243 O OG  . SER E 339 ? 0.6949 1.0581 0.8890 0.0347  0.0384  0.0433  339 SER E OG  
14244 N N   . ASN E 340 ? 0.5930 0.9712 0.8005 0.0282  0.0332  0.0495  340 ASN E N   
14245 C CA  . ASN E 340 ? 0.6834 1.0600 0.8884 0.0260  0.0346  0.0513  340 ASN E CA  
14246 C C   . ASN E 340 ? 0.6978 1.0562 0.8823 0.0262  0.0307  0.0516  340 ASN E C   
14247 O O   . ASN E 340 ? 0.7089 1.0648 0.8925 0.0260  0.0236  0.0520  340 ASN E O   
14248 C CB  . ASN E 340 ? 0.6306 1.0204 0.8518 0.0252  0.0295  0.0515  340 ASN E CB  
14249 C CG  . ASN E 340 ? 0.6674 1.0579 0.8897 0.0227  0.0323  0.0531  340 ASN E CG  
14250 O OD1 . ASN E 340 ? 0.7274 1.1153 0.9456 0.0211  0.0405  0.0542  340 ASN E OD1 
14251 N ND2 . ASN E 340 ? 0.6705 1.0647 0.8989 0.0224  0.0257  0.0529  340 ASN E ND2 
14252 N N   . GLY E 341 ? 0.7049 1.0504 0.8726 0.0267  0.0352  0.0514  341 GLY E N   
14253 C CA  . GLY E 341 ? 0.7319 1.0592 0.8780 0.0269  0.0318  0.0520  341 GLY E CA  
14254 C C   . GLY E 341 ? 0.7331 1.0513 0.8695 0.0294  0.0231  0.0497  341 GLY E C   
14255 O O   . GLY E 341 ? 0.7629 1.0715 0.8893 0.0300  0.0150  0.0499  341 GLY E O   
14256 N N   . GLY E 342 ? 0.7119 1.0330 0.8515 0.0310  0.0246  0.0473  342 GLY E N   
14257 C CA  . GLY E 342 ? 0.7376 1.0507 0.8693 0.0331  0.0165  0.0446  342 GLY E CA  
14258 C C   . GLY E 342 ? 0.7928 1.0884 0.9011 0.0341  0.0188  0.0434  342 GLY E C   
14259 O O   . GLY E 342 ? 0.8164 1.1110 0.9216 0.0346  0.0270  0.0422  342 GLY E O   
14260 N N   . VAL E 343 ? 0.7581 1.0397 0.8493 0.0346  0.0116  0.0435  343 VAL E N   
14261 C CA  . VAL E 343 ? 0.7606 1.0244 0.8271 0.0357  0.0124  0.0421  343 VAL E CA  
14262 C C   . VAL E 343 ? 0.8081 1.0691 0.8736 0.0378  0.0053  0.0379  343 VAL E C   
14263 O O   . VAL E 343 ? 0.7957 1.0538 0.8606 0.0387  -0.0059 0.0368  343 VAL E O   
14264 C CB  . VAL E 343 ? 0.7638 1.0134 0.8116 0.0354  0.0076  0.0445  343 VAL E CB  
14265 C CG1 . VAL E 343 ? 0.9122 1.1436 0.9329 0.0363  0.0103  0.0436  343 VAL E CG1 
14266 C CG2 . VAL E 343 ? 0.8166 1.0707 0.8697 0.0330  0.0133  0.0487  343 VAL E CG2 
14267 N N   . VAL E 344 ? 0.8124 1.0745 0.8788 0.0387  0.0118  0.0354  344 VAL E N   
14268 C CA  . VAL E 344 ? 0.8051 1.0661 0.8741 0.0404  0.0063  0.0313  344 VAL E CA  
14269 C C   . VAL E 344 ? 0.8602 1.1030 0.9041 0.0419  0.0057  0.0282  344 VAL E C   
14270 O O   . VAL E 344 ? 0.8765 1.1107 0.9044 0.0418  0.0142  0.0288  344 VAL E O   
14271 C CB  . VAL E 344 ? 0.8329 1.1073 0.9210 0.0406  0.0130  0.0304  344 VAL E CB  
14272 C CG1 . VAL E 344 ? 0.8844 1.1581 0.9775 0.0420  0.0065  0.0265  344 VAL E CG1 
14273 C CG2 . VAL E 344 ? 0.7914 1.0835 0.9021 0.0391  0.0144  0.0337  344 VAL E CG2 
14274 N N   . LEU E 345 ? 0.8836 1.1205 0.9238 0.0431  -0.0044 0.0247  345 LEU E N   
14275 C CA  . LEU E 345 ? 0.9334 1.1535 0.9507 0.0447  -0.0062 0.0208  345 LEU E CA  
14276 C C   . LEU E 345 ? 0.9469 1.1674 0.9660 0.0459  0.0019  0.0172  345 LEU E C   
14277 O O   . LEU E 345 ? 1.0293 1.2631 1.0697 0.0457  0.0051  0.0172  345 LEU E O   
14278 C CB  . LEU E 345 ? 0.9631 1.1776 0.9777 0.0455  -0.0205 0.0179  345 LEU E CB  
14279 C CG  . LEU E 345 ? 0.9187 1.1220 0.9165 0.0457  -0.0295 0.0193  345 LEU E CG  
14280 C CD1 . LEU E 345 ? 0.9078 1.1199 0.9165 0.0444  -0.0303 0.0245  345 LEU E CD1 
14281 C CD2 . LEU E 345 ? 0.9455 1.1436 0.9415 0.0468  -0.0434 0.0153  345 LEU E CD2 
14282 N N   . PRO E 346 ? 0.9790 1.1846 0.9756 0.0472  0.0053  0.0141  346 PRO E N   
14283 C CA  . PRO E 346 ? 1.0051 1.2100 1.0028 0.0488  0.0127  0.0099  346 PRO E CA  
14284 C C   . PRO E 346 ? 1.0372 1.2446 1.0471 0.0497  0.0044  0.0059  346 PRO E C   
14285 O O   . PRO E 346 ? 1.0266 1.2317 1.0370 0.0493  -0.0076 0.0050  346 PRO E O   
14286 C CB  . PRO E 346 ? 1.0736 1.2604 1.0414 0.0500  0.0162  0.0071  346 PRO E CB  
14287 C CG  . PRO E 346 ? 1.0758 1.2522 1.0273 0.0495  0.0057  0.0086  346 PRO E CG  
14288 C CD  . PRO E 346 ? 1.0182 1.2069 0.9866 0.0475  0.0032  0.0143  346 PRO E CD  
14289 N N   . HIS E 347 ? 1.0484 1.2604 1.0686 0.0509  0.0110  0.0034  347 HIS E N   
14290 C CA  . HIS E 347 ? 1.0663 1.2805 1.0993 0.0515  0.0049  -0.0003 347 HIS E CA  
14291 C C   . HIS E 347 ? 1.0984 1.3262 1.1537 0.0497  -0.0034 0.0029  347 HIS E C   
14292 O O   . HIS E 347 ? 1.1012 1.3263 1.1580 0.0491  -0.0145 0.0010  347 HIS E O   
14293 C CB  . HIS E 347 ? 1.1283 1.3258 1.1419 0.0527  -0.0026 -0.0063 347 HIS E CB  
14294 C CG  . HIS E 347 ? 1.1855 1.3692 1.1754 0.0546  0.0054  -0.0098 347 HIS E CG  
14295 N ND1 . HIS E 347 ? 1.1903 1.3748 1.1834 0.0565  0.0159  -0.0124 347 HIS E ND1 
14296 C CD2 . HIS E 347 ? 1.1823 1.3512 1.1449 0.0551  0.0047  -0.0111 347 HIS E CD2 
14297 C CE1 . HIS E 347 ? 1.1662 1.3373 1.1351 0.0579  0.0218  -0.0155 347 HIS E CE1 
14298 N NE2 . HIS E 347 ? 1.1852 1.3465 1.1347 0.0570  0.0151  -0.0146 347 HIS E NE2 
14299 N N   . LYS E 348 ? 1.1570 1.3997 1.2296 0.0486  0.0025  0.0077  348 LYS E N   
14300 C CA  . LYS E 348 ? 1.2239 1.4810 1.3179 0.0469  -0.0034 0.0111  348 LYS E CA  
14301 C C   . LYS E 348 ? 1.3371 1.6094 1.4525 0.0468  0.0044  0.0137  348 LYS E C   
14302 O O   . LYS E 348 ? 1.3134 1.5886 1.4279 0.0474  0.0146  0.0153  348 LYS E O   
14303 C CB  . LYS E 348 ? 1.1454 1.4048 1.2359 0.0454  -0.0063 0.0150  348 LYS E CB  
14304 C CG  . LYS E 348 ? 1.2093 1.4822 1.3198 0.0437  -0.0136 0.0176  348 LYS E CG  
14305 C CD  . LYS E 348 ? 1.2209 1.4899 1.3332 0.0436  -0.0253 0.0144  348 LYS E CD  
14306 C CE  . LYS E 348 ? 1.1691 1.4521 1.3015 0.0419  -0.0319 0.0169  348 LYS E CE  
14307 N NZ  . LYS E 348 ? 1.1433 1.4231 1.2782 0.0415  -0.0435 0.0138  348 LYS E NZ  
14308 N N   . GLU E 349 ? 1.8437 2.1255 1.9781 0.0461  -0.0006 0.0141  349 GLU E N   
14309 C CA  . GLU E 349 ? 1.7975 2.0942 1.9528 0.0461  0.0052  0.0171  349 GLU E CA  
14310 C C   . GLU E 349 ? 1.7501 2.0612 1.9197 0.0440  0.0027  0.0217  349 GLU E C   
14311 O O   . GLU E 349 ? 1.7388 2.0527 1.9142 0.0426  -0.0063 0.0220  349 GLU E O   
14312 C CB  . GLU E 349 ? 1.7962 2.0937 1.9630 0.0466  0.0021  0.0151  349 GLU E CB  
14313 C CG  . GLU E 349 ? 1.8426 2.1268 1.9976 0.0490  0.0053  0.0101  349 GLU E CG  
14314 C CD  . GLU E 349 ? 1.9053 2.1906 2.0736 0.0494  0.0028  0.0085  349 GLU E CD  
14315 O OE1 . GLU E 349 ? 1.9334 2.2264 2.1158 0.0474  -0.0042 0.0104  349 GLU E OE1 
14316 O OE2 . GLU E 349 ? 1.9484 2.2268 2.1131 0.0518  0.0079  0.0053  349 GLU E OE2 
14317 N N   . ILE E 350 ? 1.2879 1.6084 1.4635 0.0438  0.0106  0.0250  350 ILE E N   
14318 C CA  . ILE E 350 ? 1.1414 1.4754 1.3296 0.0420  0.0093  0.0291  350 ILE E CA  
14319 C C   . ILE E 350 ? 0.9744 1.3236 1.1845 0.0418  0.0109  0.0314  350 ILE E C   
14320 O O   . ILE E 350 ? 0.9421 1.2969 1.1586 0.0429  0.0188  0.0324  350 ILE E O   
14321 C CB  . ILE E 350 ? 1.0514 1.3866 1.2333 0.0415  0.0164  0.0312  350 ILE E CB  
14322 C CG1 . ILE E 350 ? 1.0946 1.4134 1.2532 0.0417  0.0151  0.0294  350 ILE E CG1 
14323 C CG2 . ILE E 350 ? 0.9379 1.2866 1.1330 0.0396  0.0145  0.0348  350 ILE E CG2 
14324 C CD1 . ILE E 350 ? 1.1411 1.4543 1.2941 0.0409  0.0038  0.0287  350 ILE E CD1 
14325 N N   . LYS E 351 ? 0.9434 1.2996 1.1651 0.0404  0.0033  0.0323  351 LYS E N   
14326 C CA  . LYS E 351 ? 0.8273 1.1980 1.0691 0.0399  0.0039  0.0351  351 LYS E CA  
14327 C C   . LYS E 351 ? 0.7104 1.0951 0.9638 0.0380  0.0017  0.0383  351 LYS E C   
14328 O O   . LYS E 351 ? 0.6047 1.0021 0.8743 0.0373  0.0014  0.0408  351 LYS E O   
14329 C CB  . LYS E 351 ? 0.8789 1.2464 1.1260 0.0397  -0.0020 0.0334  351 LYS E CB  
14330 C CG  . LYS E 351 ? 0.9264 1.2803 1.1635 0.0417  0.0002  0.0298  351 LYS E CG  
14331 C CD  . LYS E 351 ? 0.8896 1.2417 1.1350 0.0413  -0.0050 0.0287  351 LYS E CD  
14332 C CE  . LYS E 351 ? 0.9955 1.3343 1.2319 0.0436  -0.0023 0.0247  351 LYS E CE  
14333 N NZ  . LYS E 351 ? 1.0130 1.3498 1.2587 0.0430  -0.0069 0.0237  351 LYS E NZ  
14334 N N   . SER E 352 ? 0.7061 1.0885 0.9514 0.0372  0.0001  0.0383  352 SER E N   
14335 C CA  . SER E 352 ? 0.6493 1.0440 0.9046 0.0357  -0.0018 0.0407  352 SER E CA  
14336 C C   . SER E 352 ? 0.5596 0.9539 0.8081 0.0355  0.0040  0.0417  352 SER E C   
14337 O O   . SER E 352 ? 0.5845 0.9668 0.8178 0.0363  0.0073  0.0404  352 SER E O   
14338 C CB  . SER E 352 ? 0.7807 1.1734 1.0351 0.0347  -0.0114 0.0394  352 SER E CB  
14339 O OG  . SER E 352 ? 0.8534 1.2464 1.1145 0.0343  -0.0167 0.0383  352 SER E OG  
14340 N N   . ASN E 353 ? 0.5455 0.9530 0.8054 0.0344  0.0052  0.0441  353 ASN E N   
14341 C CA  . ASN E 353 ? 0.5462 0.9545 0.8020 0.0338  0.0106  0.0452  353 ASN E CA  
14342 C C   . ASN E 353 ? 0.5559 0.9542 0.7991 0.0332  0.0059  0.0443  353 ASN E C   
14343 O O   . ASN E 353 ? 0.5530 0.9524 0.7988 0.0329  -0.0019 0.0436  353 ASN E O   
14344 C CB  . ASN E 353 ? 0.5286 0.9542 0.8008 0.0326  0.0130  0.0475  353 ASN E CB  
14345 C CG  . ASN E 353 ? 0.5197 0.9553 0.8041 0.0334  0.0175  0.0489  353 ASN E CG  
14346 O OD1 . ASN E 353 ? 0.5274 0.9568 0.8074 0.0349  0.0216  0.0482  353 ASN E OD1 
14347 N ND2 . ASN E 353 ? 0.5043 0.9553 0.8037 0.0326  0.0169  0.0508  353 ASN E ND2 
14348 N N   . ILE E 354 ? 0.5680 0.9568 0.7978 0.0332  0.0108  0.0444  354 ILE E N   
14349 C CA  . ILE E 354 ? 0.6471 1.0263 0.8646 0.0326  0.0073  0.0444  354 ILE E CA  
14350 C C   . ILE E 354 ? 0.5743 0.9627 0.7996 0.0310  0.0109  0.0464  354 ILE E C   
14351 O O   . ILE E 354 ? 0.7507 1.1342 0.9683 0.0301  0.0171  0.0475  354 ILE E O   
14352 C CB  . ILE E 354 ? 0.6038 0.9656 0.8000 0.0333  0.0103  0.0435  354 ILE E CB  
14353 C CG1 . ILE E 354 ? 0.6241 0.9778 0.8138 0.0350  0.0079  0.0409  354 ILE E CG1 
14354 C CG2 . ILE E 354 ? 0.6182 0.9688 0.8010 0.0330  0.0047  0.0438  354 ILE E CG2 
14355 C CD1 . ILE E 354 ? 0.7395 1.0759 0.9071 0.0359  0.0107  0.0395  354 ILE E CD1 
14356 N N   . LEU E 355 ? 0.5730 0.9749 0.8140 0.0304  0.0071  0.0468  355 LEU E N   
14357 C CA  . LEU E 355 ? 0.6020 1.0149 0.8532 0.0288  0.0102  0.0482  355 LEU E CA  
14358 C C   . LEU E 355 ? 0.6455 1.0503 0.8877 0.0279  0.0086  0.0486  355 LEU E C   
14359 O O   . LEU E 355 ? 0.6805 1.0918 0.9288 0.0264  0.0122  0.0496  355 LEU E O   
14360 C CB  . LEU E 355 ? 0.5809 1.0096 0.8497 0.0286  0.0059  0.0481  355 LEU E CB  
14361 C CG  . LEU E 355 ? 0.5929 1.0197 0.8626 0.0296  -0.0025 0.0467  355 LEU E CG  
14362 C CD1 . LEU E 355 ? 0.6603 1.0798 0.9235 0.0298  -0.0097 0.0456  355 LEU E CD1 
14363 C CD2 . LEU E 355 ? 0.6479 1.0908 0.9351 0.0293  -0.0040 0.0471  355 LEU E CD2 
14364 N N   . LYS E 356 ? 0.6688 1.0592 0.8966 0.0288  0.0030  0.0479  356 LYS E N   
14365 C CA  . LYS E 356 ? 0.6724 1.0529 0.8898 0.0283  0.0008  0.0487  356 LYS E CA  
14366 C C   . LYS E 356 ? 0.6878 1.0494 0.8839 0.0293  -0.0006 0.0486  356 LYS E C   
14367 O O   . LYS E 356 ? 0.6786 1.0358 0.8698 0.0307  -0.0026 0.0470  356 LYS E O   
14368 C CB  . LYS E 356 ? 0.6933 1.0784 0.9187 0.0288  -0.0080 0.0477  356 LYS E CB  
14369 C CG  . LYS E 356 ? 0.7641 1.1664 1.0081 0.0276  -0.0063 0.0478  356 LYS E CG  
14370 C CD  . LYS E 356 ? 0.9465 1.3540 1.1988 0.0285  -0.0148 0.0462  356 LYS E CD  
14371 C CE  . LYS E 356 ? 1.0628 1.4570 1.3037 0.0290  -0.0193 0.0465  356 LYS E CE  
14372 N NZ  . LYS E 356 ? 1.0338 1.4256 1.2722 0.0271  -0.0133 0.0482  356 LYS E NZ  
14373 N N   . PRO E 357 ? 0.6858 1.0354 0.8683 0.0286  0.0007  0.0502  357 PRO E N   
14374 C CA  . PRO E 357 ? 0.7206 1.0515 0.8806 0.0296  -0.0005 0.0504  357 PRO E CA  
14375 C C   . PRO E 357 ? 0.7364 1.0614 0.8917 0.0319  -0.0114 0.0482  357 PRO E C   
14376 O O   . PRO E 357 ? 0.7634 1.0911 0.9251 0.0326  -0.0196 0.0478  357 PRO E O   
14377 C CB  . PRO E 357 ? 0.7453 1.0664 0.8948 0.0283  0.0009  0.0530  357 PRO E CB  
14378 C CG  . PRO E 357 ? 0.6924 1.0270 0.8577 0.0260  0.0076  0.0541  357 PRO E CG  
14379 C CD  . PRO E 357 ? 0.6920 1.0442 0.8782 0.0266  0.0042  0.0521  357 PRO E CD  
14380 N N   . GLU E 358 ? 0.7280 1.0449 0.8724 0.0330  -0.0114 0.0466  358 GLU E N   
14381 C CA  . GLU E 358 ? 0.6981 1.0105 0.8397 0.0349  -0.0213 0.0440  358 GLU E CA  
14382 C C   . GLU E 358 ? 0.7250 1.0232 0.8476 0.0359  -0.0197 0.0426  358 GLU E C   
14383 O O   . GLU E 358 ? 0.7522 1.0507 0.8724 0.0354  -0.0105 0.0426  358 GLU E O   
14384 C CB  . GLU E 358 ? 0.7312 1.0597 0.8941 0.0350  -0.0240 0.0423  358 GLU E CB  
14385 C CG  . GLU E 358 ? 0.7200 1.0453 0.8823 0.0364  -0.0336 0.0394  358 GLU E CG  
14386 C CD  . GLU E 358 ? 0.7679 1.1088 0.9509 0.0359  -0.0345 0.0382  358 GLU E CD  
14387 O OE1 . GLU E 358 ? 0.7819 1.1368 0.9800 0.0348  -0.0292 0.0397  358 GLU E OE1 
14388 O OE2 . GLU E 358 ? 0.8208 1.1599 1.0049 0.0366  -0.0406 0.0358  358 GLU E OE2 
14389 N N   . ILE E 359 ? 0.7412 1.0272 0.8506 0.0375  -0.0288 0.0410  359 ILE E N   
14390 C CA  . ILE E 359 ? 0.7873 1.0588 0.8772 0.0386  -0.0288 0.0389  359 ILE E CA  
14391 C C   . ILE E 359 ? 0.7913 1.0677 0.8904 0.0395  -0.0337 0.0352  359 ILE E C   
14392 O O   . ILE E 359 ? 0.8236 1.1031 0.9304 0.0401  -0.0438 0.0336  359 ILE E O   
14393 C CB  . ILE E 359 ? 0.8311 1.0852 0.8990 0.0398  -0.0361 0.0394  359 ILE E CB  
14394 C CG1 . ILE E 359 ? 0.8203 1.0678 0.8777 0.0387  -0.0302 0.0436  359 ILE E CG1 
14395 C CG2 . ILE E 359 ? 0.9180 1.1577 0.9660 0.0412  -0.0372 0.0366  359 ILE E CG2 
14396 C CD1 . ILE E 359 ? 0.8663 1.0964 0.9021 0.0399  -0.0376 0.0450  359 ILE E CD1 
14397 N N   . VAL E 360 ? 0.8265 1.1037 0.9255 0.0395  -0.0264 0.0337  360 VAL E N   
14398 C CA  . VAL E 360 ? 0.8015 1.0824 0.9091 0.0401  -0.0297 0.0303  360 VAL E CA  
14399 C C   . VAL E 360 ? 0.8580 1.1220 0.9443 0.0415  -0.0317 0.0269  360 VAL E C   
14400 O O   . VAL E 360 ? 0.8741 1.1277 0.9429 0.0419  -0.0247 0.0273  360 VAL E O   
14401 C CB  . VAL E 360 ? 0.7917 1.0858 0.9160 0.0394  -0.0206 0.0308  360 VAL E CB  
14402 C CG1 . VAL E 360 ? 0.8763 1.1739 1.0105 0.0399  -0.0245 0.0278  360 VAL E CG1 
14403 C CG2 . VAL E 360 ? 0.7466 1.0567 0.8896 0.0380  -0.0181 0.0341  360 VAL E CG2 
14404 N N   . MET E 361 ? 0.8764 1.1378 0.9642 0.0422  -0.0410 0.0235  361 MET E N   
14405 C CA  . MET E 361 ? 0.9681 1.2136 1.0362 0.0436  -0.0443 0.0195  361 MET E CA  
14406 C C   . MET E 361 ? 1.0305 1.2784 1.1068 0.0438  -0.0429 0.0158  361 MET E C   
14407 O O   . MET E 361 ? 1.0516 1.2912 1.1161 0.0447  -0.0365 0.0136  361 MET E O   
14408 C CB  . MET E 361 ? 1.0328 1.2700 1.0924 0.0443  -0.0578 0.0178  361 MET E CB  
14409 C CG  . MET E 361 ? 1.0194 1.2586 1.0800 0.0442  -0.0623 0.0214  361 MET E CG  
14410 S SD  . MET E 361 ? 0.9354 1.1635 0.9848 0.0458  -0.0786 0.0190  361 MET E SD  
14411 C CE  . MET E 361 ? 1.0429 1.2492 1.0600 0.0472  -0.0775 0.0162  361 MET E CE  
14412 O OXT . MET E 361 ? 1.0671 1.3252 1.1621 0.0430  -0.0479 0.0150  361 MET E OXT 
14413 N N   . MET F 1   ? 2.1591 2.1695 2.3486 -0.0096 -0.2458 -0.1753 1   MET F N   
14414 C CA  . MET F 1   ? 2.1400 2.1703 2.3473 -0.0103 -0.2371 -0.1619 1   MET F CA  
14415 C C   . MET F 1   ? 2.1161 2.1501 2.3020 -0.0034 -0.2273 -0.1568 1   MET F C   
14416 O O   . MET F 1   ? 2.0715 2.0988 2.2317 0.0004  -0.2317 -0.1619 1   MET F O   
14417 C CB  . MET F 1   ? 2.1009 2.1475 2.3281 -0.0160 -0.2470 -0.1584 1   MET F CB  
14418 C CG  . MET F 1   ? 2.0923 2.1598 2.3420 -0.0180 -0.2388 -0.1453 1   MET F CG  
14419 S SD  . MET F 1   ? 2.1402 2.2261 2.4171 -0.0254 -0.2505 -0.1425 1   MET F SD  
14420 C CE  . MET F 1   ? 2.1308 2.2063 2.4278 -0.0328 -0.2581 -0.1498 1   MET F CE  
14421 N N   . LYS F 2   ? 2.1614 2.2058 2.3578 -0.0019 -0.2143 -0.1467 2   LYS F N   
14422 C CA  . LYS F 2   ? 2.2075 2.2559 2.3867 0.0043  -0.2034 -0.1412 2   LYS F CA  
14423 C C   . LYS F 2   ? 2.1837 2.2533 2.3757 0.0030  -0.2013 -0.1303 2   LYS F C   
14424 O O   . LYS F 2   ? 2.1398 2.2214 2.3547 -0.0025 -0.2072 -0.1268 2   LYS F O   
14425 C CB  . LYS F 2   ? 2.2398 2.2826 2.4193 0.0078  -0.1896 -0.1389 2   LYS F CB  
14426 C CG  . LYS F 2   ? 2.2993 2.3206 2.4649 0.0100  -0.1903 -0.1500 2   LYS F CG  
14427 C CD  . LYS F 2   ? 2.3378 2.3473 2.4695 0.0155  -0.1912 -0.1575 2   LYS F CD  
14428 C CE  . LYS F 2   ? 2.3517 2.3402 2.4691 0.0182  -0.1901 -0.1685 2   LYS F CE  
14429 N NZ  . LYS F 2   ? 2.2872 2.2645 2.3703 0.0240  -0.1885 -0.1751 2   LYS F NZ  
14430 N N   . ALA F 3   ? 2.1411 2.2152 2.3183 0.0081  -0.1925 -0.1252 3   ALA F N   
14431 C CA  . ALA F 3   ? 2.0789 2.1722 2.2655 0.0077  -0.1895 -0.1153 3   ALA F CA  
14432 C C   . ALA F 3   ? 2.1641 2.2592 2.3355 0.0135  -0.1766 -0.1101 3   ALA F C   
14433 O O   . ALA F 3   ? 2.3079 2.3893 2.4561 0.0181  -0.1727 -0.1154 3   ALA F O   
14434 C CB  . ALA F 3   ? 2.0356 2.1335 2.2169 0.0063  -0.2018 -0.1173 3   ALA F CB  
14435 N N   . LEU F 4   ? 2.1008 2.2131 2.2858 0.0132  -0.1700 -0.1000 4   LEU F N   
14436 C CA  . LEU F 4   ? 2.1381 2.2551 2.3126 0.0180  -0.1579 -0.0940 4   LEU F CA  
14437 C C   . LEU F 4   ? 2.0469 2.1809 2.2269 0.0173  -0.1585 -0.0864 4   LEU F C   
14438 O O   . LEU F 4   ? 1.9901 2.1371 2.1921 0.0130  -0.1627 -0.0821 4   LEU F O   
14439 C CB  . LEU F 4   ? 2.0970 2.2172 2.2852 0.0188  -0.1458 -0.0889 4   LEU F CB  
14440 C CG  . LEU F 4   ? 2.0577 2.1857 2.2402 0.0232  -0.1331 -0.0818 4   LEU F CG  
14441 C CD1 . LEU F 4   ? 2.2222 2.3370 2.3758 0.0286  -0.1289 -0.0873 4   LEU F CD1 
14442 C CD2 . LEU F 4   ? 2.1941 2.3271 2.3945 0.0233  -0.1233 -0.0762 4   LEU F CD2 
14443 N N   . ILE F 5   ? 2.0045 2.1378 2.1645 0.0216  -0.1541 -0.0849 5   ILE F N   
14444 C CA  . ILE F 5   ? 1.7996 1.9471 1.9619 0.0217  -0.1545 -0.0782 5   ILE F CA  
14445 C C   . ILE F 5   ? 1.7608 1.9151 1.9201 0.0251  -0.1407 -0.0712 5   ILE F C   
14446 O O   . ILE F 5   ? 1.8342 1.9783 1.9735 0.0292  -0.1339 -0.0736 5   ILE F O   
14447 C CB  . ILE F 5   ? 1.7329 1.8734 1.8737 0.0232  -0.1640 -0.0828 5   ILE F CB  
14448 C CG1 . ILE F 5   ? 1.7924 1.9278 1.9384 0.0196  -0.1786 -0.0897 5   ILE F CG1 
14449 C CG2 . ILE F 5   ? 1.7057 1.8599 1.8482 0.0238  -0.1635 -0.0756 5   ILE F CG2 
14450 C CD1 . ILE F 5   ? 1.7479 1.8764 1.8736 0.0211  -0.1894 -0.0943 5   ILE F CD1 
14451 N N   . LEU F 6   ? 1.6591 1.8307 1.8383 0.0233  -0.1365 -0.0628 6   LEU F N   
14452 C CA  . LEU F 6   ? 1.5933 1.7735 1.7719 0.0261  -0.1243 -0.0558 6   LEU F CA  
14453 C C   . LEU F 6   ? 1.6830 1.8667 1.8473 0.0281  -0.1255 -0.0536 6   LEU F C   
14454 O O   . LEU F 6   ? 1.6892 1.8830 1.8624 0.0259  -0.1322 -0.0510 6   LEU F O   
14455 C CB  . LEU F 6   ? 1.4376 1.6346 1.6432 0.0233  -0.1198 -0.0480 6   LEU F CB  
14456 C CG  . LEU F 6   ? 1.4783 1.6719 1.6987 0.0215  -0.1175 -0.0487 6   LEU F CG  
14457 C CD1 . LEU F 6   ? 1.4902 1.7008 1.7363 0.0183  -0.1142 -0.0405 6   LEU F CD1 
14458 C CD2 . LEU F 6   ? 1.6424 1.8253 1.8510 0.0258  -0.1080 -0.0507 6   LEU F CD2 
14459 N N   . VAL F 7   ? 1.8654 2.0406 2.0076 0.0322  -0.1189 -0.0547 7   VAL F N   
14460 C CA  . VAL F 7   ? 1.8874 2.0641 2.0142 0.0342  -0.1190 -0.0524 7   VAL F CA  
14461 C C   . VAL F 7   ? 1.8339 2.0237 1.9680 0.0354  -0.1077 -0.0443 7   VAL F C   
14462 O O   . VAL F 7   ? 1.8069 2.0088 1.9489 0.0344  -0.1091 -0.0391 7   VAL F O   
14463 C CB  . VAL F 7   ? 1.9410 2.0999 2.0373 0.0377  -0.1189 -0.0584 7   VAL F CB  
14464 C CG1 . VAL F 7   ? 1.8915 2.0514 1.9718 0.0395  -0.1191 -0.0552 7   VAL F CG1 
14465 C CG2 . VAL F 7   ? 2.0124 2.1581 2.1009 0.0365  -0.1307 -0.0669 7   VAL F CG2 
14466 N N   . GLY F 8   ? 1.7801 1.9677 1.9123 0.0377  -0.0965 -0.0435 8   GLY F N   
14467 C CA  . GLY F 8   ? 1.8522 2.0512 1.9899 0.0390  -0.0856 -0.0365 8   GLY F CA  
14468 C C   . GLY F 8   ? 1.9292 2.1203 2.0435 0.0426  -0.0784 -0.0372 8   GLY F C   
14469 O O   . GLY F 8   ? 1.9125 2.0900 2.0111 0.0450  -0.0753 -0.0426 8   GLY F O   
14470 N N   . GLY F 9   ? 2.0967 2.2959 2.2084 0.0430  -0.0756 -0.0319 9   GLY F N   
14471 C CA  . GLY F 9   ? 2.1226 2.3154 2.2132 0.0458  -0.0685 -0.0316 9   GLY F CA  
14472 C C   . GLY F 9   ? 2.1441 2.3261 2.2128 0.0462  -0.0766 -0.0344 9   GLY F C   
14473 O O   . GLY F 9   ? 2.1523 2.3267 2.2167 0.0452  -0.0875 -0.0393 9   GLY F O   
14474 N N   . PHE F 10  ? 1.8643 2.0457 1.9191 0.0476  -0.0713 -0.0311 10  PHE F N   
14475 C CA  . PHE F 10  ? 1.7679 1.9384 1.7995 0.0484  -0.0777 -0.0327 10  PHE F CA  
14476 C C   . PHE F 10  ? 1.7008 1.8795 1.7407 0.0467  -0.0872 -0.0290 10  PHE F C   
14477 O O   . PHE F 10  ? 1.6316 1.8013 1.6547 0.0473  -0.0954 -0.0307 10  PHE F O   
14478 C CB  . PHE F 10  ? 1.7759 1.9410 1.7880 0.0506  -0.0669 -0.0305 10  PHE F CB  
14479 C CG  . PHE F 10  ? 1.7394 1.8863 1.7207 0.0523  -0.0702 -0.0350 10  PHE F CG  
14480 C CD1 . PHE F 10  ? 1.7841 1.9177 1.7509 0.0540  -0.0682 -0.0418 10  PHE F CD1 
14481 C CD2 . PHE F 10  ? 1.6635 1.8062 1.6298 0.0524  -0.0751 -0.0322 10  PHE F CD2 
14482 C CE1 . PHE F 10  ? 1.7682 1.8849 1.7052 0.0556  -0.0711 -0.0459 10  PHE F CE1 
14483 C CE2 . PHE F 10  ? 1.6755 1.8012 1.6123 0.0541  -0.0782 -0.0358 10  PHE F CE2 
14484 C CZ  . PHE F 10  ? 1.6982 1.8110 1.6198 0.0556  -0.0762 -0.0427 10  PHE F CZ  
14485 N N   . GLY F 11  ? 1.7848 1.9804 1.8498 0.0448  -0.0863 -0.0242 11  GLY F N   
14486 C CA  . GLY F 11  ? 1.7375 1.9422 1.8117 0.0435  -0.0939 -0.0207 11  GLY F CA  
14487 C C   . GLY F 11  ? 1.7000 1.9118 1.7730 0.0441  -0.0867 -0.0145 11  GLY F C   
14488 O O   . GLY F 11  ? 1.7021 1.9098 1.7631 0.0448  -0.0914 -0.0131 11  GLY F O   
14489 N N   . THR F 12  ? 1.5493 1.7715 1.6350 0.0438  -0.0757 -0.0107 12  THR F N   
14490 C CA  . THR F 12  ? 1.4347 1.6638 1.5200 0.0442  -0.0682 -0.0051 12  THR F CA  
14491 C C   . THR F 12  ? 1.3407 1.5804 1.4381 0.0429  -0.0750 -0.0016 12  THR F C   
14492 O O   . THR F 12  ? 1.2836 1.5227 1.3729 0.0434  -0.0739 0.0016  12  THR F O   
14493 C CB  . THR F 12  ? 1.4439 1.6836 1.5432 0.0441  -0.0562 -0.0022 12  THR F CB  
14494 O OG1 . THR F 12  ? 1.5241 1.7769 1.6481 0.0423  -0.0587 -0.0011 12  THR F OG1 
14495 C CG2 . THR F 12  ? 1.4422 1.6713 1.5294 0.0459  -0.0488 -0.0059 12  THR F CG2 
14496 N N   . ARG F 13  ? 1.3897 1.6390 1.5068 0.0411  -0.0819 -0.0022 13  ARG F N   
14497 C CA  . ARG F 13  ? 1.3991 1.6597 1.5299 0.0400  -0.0883 0.0005  13  ARG F CA  
14498 C C   . ARG F 13  ? 1.3564 1.6081 1.4759 0.0407  -0.1007 -0.0022 13  ARG F C   
14499 O O   . ARG F 13  ? 1.3381 1.5985 1.4693 0.0400  -0.1075 -0.0008 13  ARG F O   
14500 C CB  . ARG F 13  ? 1.4625 1.7379 1.6196 0.0376  -0.0899 0.0012  13  ARG F CB  
14501 C CG  . ARG F 13  ? 1.5247 1.7949 1.6850 0.0367  -0.0921 -0.0030 13  ARG F CG  
14502 C CD  . ARG F 13  ? 1.6049 1.8898 1.7899 0.0345  -0.0887 -0.0005 13  ARG F CD  
14503 N NE  . ARG F 13  ? 1.6640 1.9574 1.8543 0.0351  -0.0772 0.0041  13  ARG F NE  
14504 C CZ  . ARG F 13  ? 1.6901 1.9988 1.8955 0.0341  -0.0743 0.0087  13  ARG F CZ  
14505 N NH1 . ARG F 13  ? 1.6927 2.0103 1.9098 0.0326  -0.0817 0.0093  13  ARG F NH1 
14506 N NH2 . ARG F 13  ? 1.6741 1.9897 1.8834 0.0347  -0.0642 0.0125  13  ARG F NH2 
14507 N N   . LEU F 14  ? 1.3846 1.6194 1.4817 0.0421  -0.1039 -0.0061 14  LEU F N   
14508 C CA  . LEU F 14  ? 1.3853 1.6102 1.4693 0.0431  -0.1161 -0.0088 14  LEU F CA  
14509 C C   . LEU F 14  ? 1.3658 1.5771 1.4231 0.0454  -0.1141 -0.0074 14  LEU F C   
14510 O O   . LEU F 14  ? 1.4301 1.6298 1.4710 0.0467  -0.1237 -0.0098 14  LEU F O   
14511 C CB  . LEU F 14  ? 1.4323 1.6484 1.5126 0.0427  -0.1243 -0.0152 14  LEU F CB  
14512 C CG  . LEU F 14  ? 1.4732 1.7008 1.5789 0.0401  -0.1299 -0.0171 14  LEU F CG  
14513 C CD1 . LEU F 14  ? 1.4952 1.7310 1.6162 0.0386  -0.1197 -0.0158 14  LEU F CD1 
14514 C CD2 . LEU F 14  ? 1.6215 1.8386 1.7205 0.0398  -0.1417 -0.0237 14  LEU F CD2 
14515 N N   . ARG F 15  ? 1.2872 1.4997 1.3397 0.0457  -0.1019 -0.0035 15  ARG F N   
14516 C CA  . ARG F 15  ? 1.2821 1.4826 1.3105 0.0474  -0.0989 -0.0013 15  ARG F CA  
14517 C C   . ARG F 15  ? 1.2802 1.4824 1.3090 0.0479  -0.1071 0.0017  15  ARG F C   
14518 O O   . ARG F 15  ? 1.2963 1.5125 1.3471 0.0469  -0.1110 0.0032  15  ARG F O   
14519 C CB  . ARG F 15  ? 1.2201 1.4245 1.2480 0.0471  -0.0839 0.0025  15  ARG F CB  
14520 C CG  . ARG F 15  ? 1.2122 1.4126 1.2359 0.0473  -0.0748 -0.0005 15  ARG F CG  
14521 C CD  . ARG F 15  ? 1.1418 1.3440 1.1612 0.0474  -0.0607 0.0032  15  ARG F CD  
14522 N NE  . ARG F 15  ? 1.0975 1.2948 1.1106 0.0482  -0.0515 0.0002  15  ARG F NE  
14523 C CZ  . ARG F 15  ? 1.1134 1.3215 1.1444 0.0477  -0.0438 0.0005  15  ARG F CZ  
14524 N NH1 . ARG F 15  ? 1.1536 1.3782 1.2092 0.0463  -0.0441 0.0038  15  ARG F NH1 
14525 N NH2 . ARG F 15  ? 1.0924 1.2949 1.1166 0.0490  -0.0359 -0.0026 15  ARG F NH2 
14526 N N   . PRO F 16  ? 1.2926 1.4803 1.2969 0.0496  -0.1098 0.0028  16  PRO F N   
14527 C CA  . PRO F 16  ? 1.3511 1.5216 1.3267 0.0508  -0.1051 0.0015  16  PRO F CA  
14528 C C   . PRO F 16  ? 1.4556 1.6128 1.4157 0.0519  -0.1147 -0.0047 16  PRO F C   
14529 O O   . PRO F 16  ? 1.4746 1.6162 1.4083 0.0532  -0.1123 -0.0061 16  PRO F O   
14530 C CB  . PRO F 16  ? 1.3656 1.5284 1.3251 0.0518  -0.1053 0.0064  16  PRO F CB  
14531 C CG  . PRO F 16  ? 1.4209 1.5903 1.3938 0.0522  -0.1177 0.0073  16  PRO F CG  
14532 C CD  . PRO F 16  ? 1.3412 1.5294 1.3454 0.0505  -0.1175 0.0061  16  PRO F CD  
14533 N N   . LEU F 17  ? 1.6396 1.8029 1.6156 0.0513  -0.1252 -0.0084 17  LEU F N   
14534 C CA  . LEU F 17  ? 1.6593 1.8107 1.6222 0.0521  -0.1352 -0.0147 17  LEU F CA  
14535 C C   . LEU F 17  ? 1.6887 1.8346 1.6459 0.0518  -0.1276 -0.0192 17  LEU F C   
14536 O O   . LEU F 17  ? 1.7240 1.8553 1.6608 0.0529  -0.1321 -0.0243 17  LEU F O   
14537 C CB  . LEU F 17  ? 1.6608 1.8211 1.6443 0.0512  -0.1484 -0.0174 17  LEU F CB  
14538 C CG  . LEU F 17  ? 1.7153 1.8810 1.7058 0.0520  -0.1574 -0.0140 17  LEU F CG  
14539 C CD1 . LEU F 17  ? 1.8836 2.0594 1.8963 0.0510  -0.1696 -0.0174 17  LEU F CD1 
14540 C CD2 . LEU F 17  ? 1.8544 2.0032 1.8158 0.0547  -0.1636 -0.0132 17  LEU F CD2 
14541 N N   . THR F 18  ? 1.4917 1.6490 1.4664 0.0504  -0.1163 -0.0176 18  THR F N   
14542 C CA  . THR F 18  ? 1.4851 1.6382 1.4568 0.0504  -0.1084 -0.0216 18  THR F CA  
14543 C C   . THR F 18  ? 1.4779 1.6254 1.4337 0.0515  -0.0942 -0.0193 18  THR F C   
14544 O O   . THR F 18  ? 1.5047 1.6517 1.4619 0.0517  -0.0852 -0.0217 18  THR F O   
14545 C CB  . THR F 18  ? 1.4721 1.6407 1.4737 0.0484  -0.1056 -0.0217 18  THR F CB  
14546 O OG1 . THR F 18  ? 1.4287 1.6126 1.4481 0.0475  -0.0992 -0.0152 18  THR F OG1 
14547 C CG2 . THR F 18  ? 1.4780 1.6500 1.4936 0.0471  -0.1191 -0.0253 18  THR F CG2 
14548 N N   . LEU F 19  ? 1.4483 1.5915 1.3896 0.0522  -0.0919 -0.0147 19  LEU F N   
14549 C CA  . LEU F 19  ? 1.4608 1.5976 1.3853 0.0529  -0.0784 -0.0127 19  LEU F CA  
14550 C C   . LEU F 19  ? 1.5819 1.7004 1.4779 0.0547  -0.0780 -0.0180 19  LEU F C   
14551 O O   . LEU F 19  ? 1.5981 1.7124 1.4841 0.0553  -0.0658 -0.0187 19  LEU F O   
14552 C CB  . LEU F 19  ? 1.3960 1.5328 1.3132 0.0528  -0.0764 -0.0060 19  LEU F CB  
14553 C CG  . LEU F 19  ? 1.2943 1.4481 1.2347 0.0512  -0.0682 -0.0004 19  LEU F CG  
14554 C CD1 . LEU F 19  ? 1.2835 1.4349 1.2147 0.0510  -0.0671 0.0056  19  LEU F CD1 
14555 C CD2 . LEU F 19  ? 1.2404 1.3991 1.1862 0.0509  -0.0535 -0.0006 19  LEU F CD2 
14556 N N   . SER F 20  ? 1.6820 1.7897 1.5647 0.0555  -0.0912 -0.0221 20  SER F N   
14557 C CA  . SER F 20  ? 1.7408 1.8304 1.5951 0.0572  -0.0923 -0.0279 20  SER F CA  
14558 C C   . SER F 20  ? 1.7072 1.7949 1.5683 0.0572  -0.1000 -0.0357 20  SER F C   
14559 O O   . SER F 20  ? 1.7282 1.8115 1.5854 0.0578  -0.0927 -0.0404 20  SER F O   
14560 C CB  . SER F 20  ? 1.8334 1.9092 1.6614 0.0584  -0.1014 -0.0264 20  SER F CB  
14561 O OG  . SER F 20  ? 1.8756 1.9517 1.6961 0.0583  -0.0937 -0.0191 20  SER F OG  
14562 N N   . PHE F 21  ? 1.7987 1.8894 1.6706 0.0565  -0.1146 -0.0374 21  PHE F N   
14563 C CA  . PHE F 21  ? 1.7987 1.8882 1.6795 0.0559  -0.1222 -0.0446 21  PHE F CA  
14564 C C   . PHE F 21  ? 1.7682 1.8754 1.6833 0.0538  -0.1183 -0.0432 21  PHE F C   
14565 O O   . PHE F 21  ? 1.7388 1.8600 1.6731 0.0525  -0.1176 -0.0373 21  PHE F O   
14566 C CB  . PHE F 21  ? 1.7880 1.8729 1.6654 0.0559  -0.1400 -0.0476 21  PHE F CB  
14567 C CG  . PHE F 21  ? 1.8603 1.9264 1.7029 0.0581  -0.1459 -0.0499 21  PHE F CG  
14568 C CD1 . PHE F 21  ? 1.9200 1.9725 1.7367 0.0597  -0.1368 -0.0528 21  PHE F CD1 
14569 C CD2 . PHE F 21  ? 1.8140 1.8762 1.6495 0.0588  -0.1604 -0.0493 21  PHE F CD2 
14570 C CE1 . PHE F 21  ? 1.9158 1.9507 1.6990 0.0617  -0.1420 -0.0548 21  PHE F CE1 
14571 C CE2 . PHE F 21  ? 1.8320 1.8765 1.6344 0.0610  -0.1662 -0.0511 21  PHE F CE2 
14572 C CZ  . PHE F 21  ? 1.8675 1.8981 1.6431 0.0623  -0.1569 -0.0537 21  PHE F CZ  
14573 N N   . PRO F 22  ? 1.7021 1.8084 1.6250 0.0533  -0.1159 -0.0485 22  PRO F N   
14574 C CA  . PRO F 22  ? 1.6759 1.7982 1.6304 0.0513  -0.1119 -0.0467 22  PRO F CA  
14575 C C   . PRO F 22  ? 1.6114 1.7439 1.5874 0.0490  -0.1245 -0.0462 22  PRO F C   
14576 O O   . PRO F 22  ? 1.5900 1.7172 1.5578 0.0491  -0.1369 -0.0481 22  PRO F O   
14577 C CB  . PRO F 22  ? 1.7329 1.8481 1.6863 0.0518  -0.1079 -0.0533 22  PRO F CB  
14578 C CG  . PRO F 22  ? 1.7552 1.8512 1.6789 0.0536  -0.1138 -0.0601 22  PRO F CG  
14579 C CD  . PRO F 22  ? 1.7551 1.8455 1.6591 0.0545  -0.1194 -0.0569 22  PRO F CD  
14580 N N   . LYS F 23  ? 1.6069 1.7547 1.6112 0.0470  -0.1209 -0.0434 23  LYS F N   
14581 C CA  . LYS F 23  ? 1.5563 1.7164 1.5841 0.0445  -0.1307 -0.0421 23  LYS F CA  
14582 C C   . LYS F 23  ? 1.5522 1.7046 1.5781 0.0435  -0.1449 -0.0490 23  LYS F C   
14583 O O   . LYS F 23  ? 1.5297 1.6856 1.5598 0.0428  -0.1560 -0.0486 23  LYS F O   
14584 C CB  . LYS F 23  ? 1.5725 1.7483 1.6288 0.0424  -0.1235 -0.0388 23  LYS F CB  
14585 C CG  . LYS F 23  ? 1.5683 1.7576 1.6502 0.0394  -0.1323 -0.0376 23  LYS F CG  
14586 C CD  . LYS F 23  ? 1.5761 1.7814 1.6841 0.0374  -0.1241 -0.0329 23  LYS F CD  
14587 C CE  . LYS F 23  ? 1.6555 1.8564 1.7662 0.0374  -0.1169 -0.0355 23  LYS F CE  
14588 N NZ  . LYS F 23  ? 1.6317 1.8481 1.7678 0.0355  -0.1100 -0.0304 23  LYS F NZ  
14589 N N   . PRO F 24  ? 1.5837 1.7261 1.6044 0.0433  -0.1456 -0.0556 24  PRO F N   
14590 C CA  . PRO F 24  ? 1.5423 1.6786 1.5638 0.0419  -0.1599 -0.0622 24  PRO F CA  
14591 C C   . PRO F 24  ? 1.5217 1.6431 1.5156 0.0440  -0.1698 -0.0663 24  PRO F C   
14592 O O   . PRO F 24  ? 1.5028 1.6202 1.4977 0.0428  -0.1830 -0.0716 24  PRO F O   
14593 C CB  . PRO F 24  ? 1.5567 1.6863 1.5810 0.0412  -0.1559 -0.0678 24  PRO F CB  
14594 C CG  . PRO F 24  ? 1.5670 1.6908 1.5758 0.0440  -0.1418 -0.0664 24  PRO F CG  
14595 C CD  . PRO F 24  ? 1.5982 1.7349 1.6141 0.0444  -0.1340 -0.0576 24  PRO F CD  
14596 N N   . LEU F 25  ? 1.5627 1.6759 1.5322 0.0469  -0.1641 -0.0639 25  LEU F N   
14597 C CA  . LEU F 25  ? 1.5383 1.6362 1.4790 0.0491  -0.1730 -0.0672 25  LEU F CA  
14598 C C   . LEU F 25  ? 1.5371 1.6399 1.4770 0.0497  -0.1804 -0.0619 25  LEU F C   
14599 O O   . LEU F 25  ? 1.5259 1.6163 1.4411 0.0518  -0.1876 -0.0632 25  LEU F O   
14600 C CB  . LEU F 25  ? 1.5633 1.6469 1.4745 0.0518  -0.1625 -0.0682 25  LEU F CB  
14601 C CG  . LEU F 25  ? 1.5729 1.6462 1.4765 0.0522  -0.1583 -0.0757 25  LEU F CG  
14602 C CD1 . LEU F 25  ? 1.6235 1.6815 1.4943 0.0552  -0.1500 -0.0773 25  LEU F CD1 
14603 C CD2 . LEU F 25  ? 1.5801 1.6467 1.4849 0.0509  -0.1731 -0.0839 25  LEU F CD2 
14604 N N   . VAL F 26  ? 1.5450 1.6651 1.5108 0.0481  -0.1790 -0.0561 26  VAL F N   
14605 C CA  . VAL F 26  ? 1.5507 1.6765 1.5188 0.0489  -0.1861 -0.0514 26  VAL F CA  
14606 C C   . VAL F 26  ? 1.5395 1.6661 1.5157 0.0480  -0.2034 -0.0559 26  VAL F C   
14607 O O   . VAL F 26  ? 1.5037 1.6392 1.5031 0.0452  -0.2072 -0.0589 26  VAL F O   
14608 C CB  . VAL F 26  ? 1.6378 1.7820 1.6307 0.0476  -0.1779 -0.0441 26  VAL F CB  
14609 C CG1 . VAL F 26  ? 1.7074 1.8579 1.7051 0.0484  -0.1863 -0.0401 26  VAL F CG1 
14610 C CG2 . VAL F 26  ? 1.6292 1.7726 1.6135 0.0485  -0.1616 -0.0397 26  VAL F CG2 
14611 N N   . ASP F 27  ? 1.6498 1.7669 1.6070 0.0504  -0.2138 -0.0564 27  ASP F N   
14612 C CA  . ASP F 27  ? 1.5820 1.6998 1.5460 0.0500  -0.2311 -0.0606 27  ASP F CA  
14613 C C   . ASP F 27  ? 1.5505 1.6881 1.5466 0.0483  -0.2344 -0.0567 27  ASP F C   
14614 O O   . ASP F 27  ? 1.5920 1.7357 1.5903 0.0498  -0.2319 -0.0504 27  ASP F O   
14615 C CB  . ASP F 27  ? 1.5790 1.6820 1.5139 0.0534  -0.2410 -0.0610 27  ASP F CB  
14616 C CG  . ASP F 27  ? 1.6125 1.6955 1.5156 0.0549  -0.2410 -0.0667 27  ASP F CG  
14617 O OD1 . ASP F 27  ? 1.6520 1.7323 1.5538 0.0537  -0.2305 -0.0693 27  ASP F OD1 
14618 O OD2 . ASP F 27  ? 1.5778 1.6475 1.4566 0.0574  -0.2513 -0.0685 27  ASP F OD2 
14619 N N   . PHE F 28  ? 1.4822 1.6297 1.5032 0.0452  -0.2398 -0.0605 28  PHE F N   
14620 C CA  . PHE F 28  ? 1.4950 1.6612 1.5468 0.0434  -0.2443 -0.0580 28  PHE F CA  
14621 C C   . PHE F 28  ? 1.5169 1.6825 1.5739 0.0431  -0.2621 -0.0636 28  PHE F C   
14622 O O   . PHE F 28  ? 1.5251 1.6865 1.5851 0.0409  -0.2679 -0.0702 28  PHE F O   
14623 C CB  . PHE F 28  ? 1.5425 1.7230 1.6220 0.0395  -0.2351 -0.0570 28  PHE F CB  
14624 C CG  . PHE F 28  ? 1.5663 1.7659 1.6776 0.0371  -0.2403 -0.0555 28  PHE F CG  
14625 C CD1 . PHE F 28  ? 1.5210 1.7263 1.6520 0.0336  -0.2480 -0.0605 28  PHE F CD1 
14626 C CD2 . PHE F 28  ? 1.7006 1.9123 1.8223 0.0383  -0.2374 -0.0494 28  PHE F CD2 
14627 C CE1 . PHE F 28  ? 1.5795 1.8027 1.7399 0.0312  -0.2522 -0.0592 28  PHE F CE1 
14628 C CE2 . PHE F 28  ? 1.8154 2.0448 1.9661 0.0363  -0.2418 -0.0484 28  PHE F CE2 
14629 C CZ  . PHE F 28  ? 1.6759 1.9114 1.8460 0.0327  -0.2490 -0.0532 28  PHE F CZ  
14630 N N   . ALA F 29  ? 1.5039 1.6736 1.5628 0.0453  -0.2709 -0.0612 29  ALA F N   
14631 C CA  . ALA F 29  ? 1.4892 1.6579 1.5512 0.0459  -0.2888 -0.0662 29  ALA F CA  
14632 C C   . ALA F 29  ? 1.5104 1.6591 1.5444 0.0471  -0.2968 -0.0728 29  ALA F C   
14633 O O   . ALA F 29  ? 1.5277 1.6748 1.5684 0.0447  -0.3046 -0.0797 29  ALA F O   
14634 C CB  . ALA F 29  ? 1.5220 1.7078 1.6193 0.0418  -0.2936 -0.0690 29  ALA F CB  
14635 N N   . ASN F 30  ? 1.5605 1.6937 1.5623 0.0507  -0.2938 -0.0705 30  ASN F N   
14636 C CA  . ASN F 30  ? 1.5685 1.6811 1.5377 0.0527  -0.3001 -0.0757 30  ASN F CA  
14637 C C   . ASN F 30  ? 1.6307 1.7348 1.5903 0.0508  -0.2898 -0.0797 30  ASN F C   
14638 O O   . ASN F 30  ? 1.6782 1.7664 1.6073 0.0530  -0.2844 -0.0800 30  ASN F O   
14639 C CB  . ASN F 30  ? 1.5896 1.6998 1.5613 0.0528  -0.3197 -0.0826 30  ASN F CB  
14640 C CG  . ASN F 30  ? 1.5936 1.7056 1.5634 0.0563  -0.3316 -0.0793 30  ASN F CG  
14641 O OD1 . ASN F 30  ? 1.6039 1.7005 1.5451 0.0598  -0.3396 -0.0799 30  ASN F OD1 
14642 N ND2 . ASN F 30  ? 1.5529 1.6834 1.5529 0.0554  -0.3325 -0.0758 30  ASN F ND2 
14643 N N   . LYS F 31  ? 1.5850 1.6995 1.5703 0.0468  -0.2868 -0.0826 31  LYS F N   
14644 C CA  . LYS F 31  ? 1.5587 1.6652 1.5378 0.0450  -0.2788 -0.0873 31  LYS F CA  
14645 C C   . LYS F 31  ? 1.5468 1.6600 1.5333 0.0443  -0.2599 -0.0815 31  LYS F C   
14646 O O   . LYS F 31  ? 1.5418 1.6709 1.5503 0.0433  -0.2543 -0.0751 31  LYS F O   
14647 C CB  . LYS F 31  ? 1.5148 1.6268 1.5168 0.0410  -0.2869 -0.0941 31  LYS F CB  
14648 C CG  . LYS F 31  ? 1.6054 1.7073 1.5962 0.0415  -0.3050 -0.1019 31  LYS F CG  
14649 C CD  . LYS F 31  ? 1.6604 1.7743 1.6824 0.0372  -0.3153 -0.1065 31  LYS F CD  
14650 C CE  . LYS F 31  ? 1.7361 1.8435 1.7501 0.0383  -0.3350 -0.1129 31  LYS F CE  
14651 N NZ  . LYS F 31  ? 1.7229 1.8471 1.7710 0.0349  -0.3455 -0.1144 31  LYS F NZ  
14652 N N   . PRO F 32  ? 1.5339 1.6353 1.5022 0.0449  -0.2500 -0.0837 32  PRO F N   
14653 C CA  . PRO F 32  ? 1.5055 1.6136 1.4826 0.0442  -0.2325 -0.0788 32  PRO F CA  
14654 C C   . PRO F 32  ? 1.5036 1.6280 1.5160 0.0402  -0.2302 -0.0782 32  PRO F C   
14655 O O   . PRO F 32  ? 1.5452 1.6718 1.5721 0.0375  -0.2402 -0.0835 32  PRO F O   
14656 C CB  . PRO F 32  ? 1.5315 1.6227 1.4840 0.0455  -0.2257 -0.0839 32  PRO F CB  
14657 C CG  . PRO F 32  ? 1.5460 1.6207 1.4684 0.0481  -0.2370 -0.0884 32  PRO F CG  
14658 C CD  . PRO F 32  ? 1.5660 1.6470 1.5031 0.0468  -0.2541 -0.0906 32  PRO F CD  
14659 N N   . MET F 33  ? 1.4783 1.6141 1.5046 0.0396  -0.2167 -0.0716 33  MET F N   
14660 C CA  . MET F 33  ? 1.4714 1.6237 1.5307 0.0359  -0.2135 -0.0696 33  MET F CA  
14661 C C   . MET F 33  ? 1.5131 1.6601 1.5787 0.0334  -0.2125 -0.0756 33  MET F C   
14662 O O   . MET F 33  ? 1.5362 1.6938 1.6280 0.0297  -0.2151 -0.0761 33  MET F O   
14663 C CB  . MET F 33  ? 1.4603 1.6245 1.5299 0.0362  -0.1991 -0.0615 33  MET F CB  
14664 C CG  . MET F 33  ? 1.5157 1.6962 1.6035 0.0357  -0.2015 -0.0555 33  MET F CG  
14665 S SD  . MET F 33  ? 1.3642 1.5594 1.4847 0.0315  -0.2126 -0.0578 33  MET F SD  
14666 C CE  . MET F 33  ? 1.5054 1.7071 1.6460 0.0278  -0.2018 -0.0573 33  MET F CE  
14667 N N   . ILE F 34  ? 1.5346 1.6653 1.5767 0.0354  -0.2083 -0.0800 34  ILE F N   
14668 C CA  . ILE F 34  ? 1.5321 1.6566 1.5793 0.0335  -0.2066 -0.0859 34  ILE F CA  
14669 C C   . ILE F 34  ? 1.6221 1.7405 1.6715 0.0313  -0.2221 -0.0940 34  ILE F C   
14670 O O   . ILE F 34  ? 1.6781 1.7972 1.7437 0.0281  -0.2235 -0.0979 34  ILE F O   
14671 C CB  . ILE F 34  ? 1.5319 1.6415 1.5537 0.0367  -0.1963 -0.0884 34  ILE F CB  
14672 C CG1 . ILE F 34  ? 1.5799 1.6856 1.6116 0.0350  -0.1914 -0.0929 34  ILE F CG1 
14673 C CG2 . ILE F 34  ? 1.5987 1.6907 1.5879 0.0395  -0.2041 -0.0941 34  ILE F CG2 
14674 C CD1 . ILE F 34  ? 1.5872 1.7083 1.6470 0.0328  -0.1816 -0.0865 34  ILE F CD1 
14675 N N   . LEU F 35  ? 1.6371 1.7496 1.6713 0.0329  -0.2343 -0.0966 35  LEU F N   
14676 C CA  . LEU F 35  ? 1.6936 1.7998 1.7284 0.0311  -0.2500 -0.1048 35  LEU F CA  
14677 C C   . LEU F 35  ? 1.7595 1.8821 1.8274 0.0268  -0.2584 -0.1038 35  LEU F C   
14678 O O   . LEU F 35  ? 1.8645 1.9840 1.9387 0.0243  -0.2707 -0.1107 35  LEU F O   
14679 C CB  . LEU F 35  ? 1.6365 1.7304 1.6426 0.0345  -0.2606 -0.1077 35  LEU F CB  
14680 C CG  . LEU F 35  ? 1.7060 1.7816 1.6765 0.0384  -0.2540 -0.1101 35  LEU F CG  
14681 C CD1 . LEU F 35  ? 1.7042 1.7665 1.6466 0.0413  -0.2668 -0.1140 35  LEU F CD1 
14682 C CD2 . LEU F 35  ? 1.8548 1.9204 1.8225 0.0373  -0.2487 -0.1169 35  LEU F CD2 
14683 N N   . HIS F 36  ? 1.7326 1.8727 1.8218 0.0258  -0.2519 -0.0957 36  HIS F N   
14684 C CA  . HIS F 36  ? 1.7301 1.8868 1.8508 0.0218  -0.2590 -0.0946 36  HIS F CA  
14685 C C   . HIS F 36  ? 1.8356 1.9959 1.9786 0.0170  -0.2564 -0.0971 36  HIS F C   
14686 O O   . HIS F 36  ? 1.8600 2.0287 2.0254 0.0130  -0.2653 -0.0995 36  HIS F O   
14687 C CB  . HIS F 36  ? 1.7315 1.9054 1.8670 0.0224  -0.2523 -0.0855 36  HIS F CB  
14688 C CG  . HIS F 36  ? 1.7060 1.8780 1.8247 0.0265  -0.2573 -0.0830 36  HIS F CG  
14689 N ND1 . HIS F 36  ? 1.7215 1.8832 1.8133 0.0307  -0.2499 -0.0802 36  HIS F ND1 
14690 C CD2 . HIS F 36  ? 1.6843 1.8634 1.8099 0.0271  -0.2689 -0.0827 36  HIS F CD2 
14691 C CE1 . HIS F 36  ? 1.6954 1.8571 1.7775 0.0336  -0.2569 -0.0780 36  HIS F CE1 
14692 N NE2 . HIS F 36  ? 1.6675 1.8396 1.7697 0.0318  -0.2686 -0.0796 36  HIS F NE2 
14693 N N   . GLN F 37  ? 1.8681 2.0221 2.0062 0.0173  -0.2442 -0.0965 37  GLN F N   
14694 C CA  . GLN F 37  ? 1.9199 2.0755 2.0776 0.0130  -0.2412 -0.0984 37  GLN F CA  
14695 C C   . GLN F 37  ? 2.0315 2.1679 2.1726 0.0134  -0.2433 -0.1072 37  GLN F C   
14696 O O   . GLN F 37  ? 2.0775 2.2129 2.2344 0.0095  -0.2438 -0.1103 37  GLN F O   
14697 C CB  . GLN F 37  ? 1.8410 2.0064 2.0115 0.0128  -0.2252 -0.0905 37  GLN F CB  
14698 C CG  . GLN F 37  ? 1.7974 1.9827 1.9871 0.0119  -0.2219 -0.0820 37  GLN F CG  
14699 C CD  . GLN F 37  ? 1.7025 1.8886 1.8744 0.0167  -0.2168 -0.0771 37  GLN F CD  
14700 O OE1 . GLN F 37  ? 1.6419 1.8139 1.7869 0.0205  -0.2143 -0.0793 37  GLN F OE1 
14701 N NE2 . GLN F 37  ? 1.6905 1.8930 1.8774 0.0163  -0.2149 -0.0705 37  GLN F NE2 
14702 N N   . ILE F 38  ? 2.1788 2.2996 2.2883 0.0177  -0.2447 -0.1112 38  ILE F N   
14703 C CA  . ILE F 38  ? 2.2365 2.3387 2.3290 0.0182  -0.2481 -0.1206 38  ILE F CA  
14704 C C   . ILE F 38  ? 2.2936 2.3921 2.3908 0.0152  -0.2654 -0.1286 38  ILE F C   
14705 O O   . ILE F 38  ? 2.3157 2.4070 2.4197 0.0122  -0.2691 -0.1354 38  ILE F O   
14706 C CB  . ILE F 38  ? 2.2500 2.3370 2.3063 0.0237  -0.2434 -0.1224 38  ILE F CB  
14707 C CG1 . ILE F 38  ? 2.2756 2.3643 2.3293 0.0261  -0.2255 -0.1164 38  ILE F CG1 
14708 C CG2 . ILE F 38  ? 2.2994 2.3668 2.3352 0.0244  -0.2506 -0.1334 38  ILE F CG2 
14709 C CD1 . ILE F 38  ? 2.3128 2.3868 2.3324 0.0312  -0.2192 -0.1182 38  ILE F CD1 
14710 N N   . GLU F 39  ? 2.4812 2.5847 2.5756 0.0160  -0.2764 -0.1281 39  GLU F N   
14711 C CA  . GLU F 39  ? 2.4766 2.5790 2.5784 0.0130  -0.2935 -0.1352 39  GLU F CA  
14712 C C   . GLU F 39  ? 2.4646 2.5816 2.6038 0.0068  -0.2956 -0.1342 39  GLU F C   
14713 O O   . GLU F 39  ? 2.4885 2.6020 2.6371 0.0031  -0.3066 -0.1417 39  GLU F O   
14714 C CB  . GLU F 39  ? 2.4641 2.5699 2.5562 0.0158  -0.3042 -0.1338 39  GLU F CB  
14715 C CG  . GLU F 39  ? 2.5605 2.6620 2.6526 0.0142  -0.3233 -0.1423 39  GLU F CG  
14716 C CD  . GLU F 39  ? 2.5734 2.6929 2.7019 0.0091  -0.3310 -0.1414 39  GLU F CD  
14717 O OE1 . GLU F 39  ? 2.6142 2.7503 2.7654 0.0075  -0.3222 -0.1334 39  GLU F OE1 
14718 O OE2 . GLU F 39  ? 2.5575 2.6748 2.6918 0.0066  -0.3459 -0.1490 39  GLU F OE2 
14719 N N   . ALA F 40  ? 2.2912 2.4246 2.4518 0.0054  -0.2851 -0.1252 40  ALA F N   
14720 C CA  . ALA F 40  ? 2.2067 2.3536 2.4019 -0.0007 -0.2851 -0.1235 40  ALA F CA  
14721 C C   . ALA F 40  ? 2.1838 2.3213 2.3839 -0.0035 -0.2795 -0.1272 40  ALA F C   
14722 O O   . ALA F 40  ? 2.1960 2.3373 2.4189 -0.0090 -0.2846 -0.1300 40  ALA F O   
14723 C CB  . ALA F 40  ? 2.0366 2.2029 2.2512 -0.0011 -0.2748 -0.1129 40  ALA F CB  
14724 N N   . LEU F 41  ? 2.1857 2.3107 2.3651 0.0003  -0.2690 -0.1273 41  LEU F N   
14725 C CA  . LEU F 41  ? 2.1695 2.2831 2.3507 -0.0015 -0.2644 -0.1318 41  LEU F CA  
14726 C C   . LEU F 41  ? 2.1986 2.2954 2.3667 -0.0024 -0.2770 -0.1437 41  LEU F C   
14727 O O   . LEU F 41  ? 2.2109 2.2999 2.3877 -0.0056 -0.2772 -0.1487 41  LEU F O   
14728 C CB  . LEU F 41  ? 2.1233 2.2294 2.2870 0.0032  -0.2493 -0.1286 41  LEU F CB  
14729 C CG  . LEU F 41  ? 2.0620 2.1836 2.2420 0.0032  -0.2355 -0.1174 41  LEU F CG  
14730 C CD1 . LEU F 41  ? 1.9849 2.0991 2.1451 0.0085  -0.2218 -0.1149 41  LEU F CD1 
14731 C CD2 . LEU F 41  ? 2.0304 2.1600 2.2409 -0.0023 -0.2328 -0.1149 41  LEU F CD2 
14732 N N   . LYS F 42  ? 2.1892 2.2797 2.3365 0.0004  -0.2878 -0.1484 42  LYS F N   
14733 C CA  . LYS F 42  ? 2.1608 2.2370 2.2973 -0.0007 -0.3018 -0.1599 42  LYS F CA  
14734 C C   . LYS F 42  ? 2.2566 2.3428 2.4209 -0.0069 -0.3149 -0.1627 42  LYS F C   
14735 O O   . LYS F 42  ? 2.2676 2.3434 2.4314 -0.0096 -0.3255 -0.1723 42  LYS F O   
14736 C CB  . LYS F 42  ? 2.1227 2.1882 2.2257 0.0046  -0.3091 -0.1637 42  LYS F CB  
14737 C CG  . LYS F 42  ? 2.0507 2.0937 2.1231 0.0077  -0.3090 -0.1728 42  LYS F CG  
14738 C CD  . LYS F 42  ? 2.0078 2.0413 2.0883 0.0034  -0.3195 -0.1835 42  LYS F CD  
14739 C CE  . LYS F 42  ? 1.8967 1.9076 1.9462 0.0067  -0.3189 -0.1931 42  LYS F CE  
14740 N NZ  . LYS F 42  ? 1.8949 1.9005 1.9392 0.0092  -0.3012 -0.1901 42  LYS F NZ  
14741 N N   . ALA F 43  ? 2.3102 2.4164 2.4990 -0.0092 -0.3144 -0.1549 43  ALA F N   
14742 C CA  . ALA F 43  ? 2.3399 2.4576 2.5583 -0.0155 -0.3252 -0.1570 43  ALA F CA  
14743 C C   . ALA F 43  ? 2.5399 2.6566 2.7808 -0.0215 -0.3210 -0.1584 43  ALA F C   
14744 O O   . ALA F 43  ? 2.5762 2.6952 2.8363 -0.0271 -0.3314 -0.1637 43  ALA F O   
14745 C CB  . ALA F 43  ? 2.2111 2.3509 2.4501 -0.0163 -0.3239 -0.1480 43  ALA F CB  
14746 N N   . VAL F 44  ? 3.0001 3.1134 3.2395 -0.0204 -0.3059 -0.1536 44  VAL F N   
14747 C CA  . VAL F 44  ? 3.0066 3.1162 3.2640 -0.0253 -0.3011 -0.1548 44  VAL F CA  
14748 C C   . VAL F 44  ? 3.0521 3.1389 3.2869 -0.0228 -0.2998 -0.1632 44  VAL F C   
14749 O O   . VAL F 44  ? 3.0679 3.1487 3.3133 -0.0255 -0.2939 -0.1640 44  VAL F O   
14750 C CB  . VAL F 44  ? 2.9842 3.1069 3.2600 -0.0263 -0.2857 -0.1434 44  VAL F CB  
14751 C CG1 . VAL F 44  ? 2.9351 3.0801 3.2383 -0.0303 -0.2879 -0.1366 44  VAL F CG1 
14752 C CG2 . VAL F 44  ? 2.9953 3.1157 3.2489 -0.0193 -0.2733 -0.1378 44  VAL F CG2 
14753 N N   . GLY F 45  ? 2.5495 2.6233 2.7529 -0.0176 -0.3050 -0.1695 45  GLY F N   
14754 C CA  . GLY F 45  ? 2.3427 2.3946 2.5231 -0.0151 -0.3050 -0.1788 45  GLY F CA  
14755 C C   . GLY F 45  ? 2.1931 2.2383 2.3635 -0.0112 -0.2883 -0.1749 45  GLY F C   
14756 O O   . GLY F 45  ? 2.1002 2.1336 2.2725 -0.0123 -0.2848 -0.1797 45  GLY F O   
14757 N N   . VAL F 46  ? 2.1652 2.2178 2.3256 -0.0065 -0.2780 -0.1665 46  VAL F N   
14758 C CA  . VAL F 46  ? 2.0898 2.1368 2.2392 -0.0022 -0.2621 -0.1628 46  VAL F CA  
14759 C C   . VAL F 46  ? 2.0606 2.0908 2.1728 0.0040  -0.2617 -0.1694 46  VAL F C   
14760 O O   . VAL F 46  ? 2.0295 2.0606 2.1234 0.0070  -0.2666 -0.1690 46  VAL F O   
14761 C CB  . VAL F 46  ? 2.0772 2.1421 2.2376 -0.0009 -0.2505 -0.1500 46  VAL F CB  
14762 C CG1 . VAL F 46  ? 2.0416 2.1006 2.1881 0.0043  -0.2349 -0.1468 46  VAL F CG1 
14763 C CG2 . VAL F 46  ? 2.1375 2.2181 2.3338 -0.0070 -0.2494 -0.1435 46  VAL F CG2 
14764 N N   . ASP F 47  ? 2.1355 2.1500 2.2364 0.0060  -0.2558 -0.1755 47  ASP F N   
14765 C CA  . ASP F 47  ? 2.1346 2.1317 2.2002 0.0116  -0.2550 -0.1830 47  ASP F CA  
14766 C C   . ASP F 47  ? 2.0860 2.0845 2.1356 0.0174  -0.2394 -0.1764 47  ASP F C   
14767 O O   . ASP F 47  ? 2.0946 2.0873 2.1162 0.0217  -0.2394 -0.1777 47  ASP F O   
14768 C CB  . ASP F 47  ? 2.1504 2.1292 2.2112 0.0110  -0.2567 -0.1941 47  ASP F CB  
14769 C CG  . ASP F 47  ? 2.1594 2.1427 2.2533 0.0054  -0.2564 -0.1928 47  ASP F CG  
14770 O OD1 . ASP F 47  ? 2.1477 2.1443 2.2660 -0.0001 -0.2639 -0.1889 47  ASP F OD1 
14771 O OD2 . ASP F 47  ? 2.1726 2.1461 2.2684 0.0064  -0.2483 -0.1955 47  ASP F OD2 
14772 N N   . GLU F 48  ? 2.0704 2.0762 2.1370 0.0175  -0.2262 -0.1693 48  GLU F N   
14773 C CA  . GLU F 48  ? 2.0830 2.0901 2.1370 0.0228  -0.2109 -0.1636 48  GLU F CA  
14774 C C   . GLU F 48  ? 2.1403 2.1682 2.2139 0.0217  -0.2042 -0.1507 48  GLU F C   
14775 O O   . GLU F 48  ? 2.1567 2.1964 2.2590 0.0171  -0.2058 -0.1459 48  GLU F O   
14776 C CB  . GLU F 48  ? 2.0485 2.0455 2.1034 0.0249  -0.2003 -0.1668 48  GLU F CB  
14777 N N   . VAL F 49  ? 2.1437 2.1757 2.2012 0.0259  -0.1965 -0.1452 49  VAL F N   
14778 C CA  . VAL F 49  ? 2.2899 2.3408 2.3625 0.0256  -0.1895 -0.1335 49  VAL F CA  
14779 C C   . VAL F 49  ? 2.5164 2.5668 2.5762 0.0306  -0.1740 -0.1292 49  VAL F C   
14780 O O   . VAL F 49  ? 2.3516 2.3908 2.3833 0.0348  -0.1714 -0.1332 49  VAL F O   
14781 C CB  . VAL F 49  ? 2.1938 2.2531 2.2621 0.0248  -0.1987 -0.1304 49  VAL F CB  
14782 C CG1 . VAL F 49  ? 2.2514 2.3296 2.3348 0.0247  -0.1909 -0.1187 49  VAL F CG1 
14783 C CG2 . VAL F 49  ? 2.0699 2.1308 2.1524 0.0199  -0.2144 -0.1349 49  VAL F CG2 
14784 N N   . VAL F 50  ? 3.5108 3.5735 3.5911 0.0302  -0.1637 -0.1210 50  VAL F N   
14785 C CA  . VAL F 50  ? 3.5238 3.5885 3.5968 0.0346  -0.1487 -0.1162 50  VAL F CA  
14786 C C   . VAL F 50  ? 3.4862 3.5687 3.5677 0.0344  -0.1443 -0.1056 50  VAL F C   
14787 O O   . VAL F 50  ? 3.4470 3.5430 3.5498 0.0304  -0.1495 -0.1004 50  VAL F O   
14788 C CB  . VAL F 50  ? 3.5359 3.5992 3.6246 0.0349  -0.1397 -0.1158 50  VAL F CB  
14789 C CG1 . VAL F 50  ? 3.5535 3.6174 3.6327 0.0400  -0.1247 -0.1124 50  VAL F CG1 
14790 C CG2 . VAL F 50  ? 3.5684 3.6144 3.6522 0.0344  -0.1456 -0.1266 50  VAL F CG2 
14791 N N   . LEU F 51  ? 2.5231 2.6057 2.5879 0.0385  -0.1347 -0.1026 51  LEU F N   
14792 C CA  . LEU F 51  ? 2.2172 2.3151 2.2870 0.0387  -0.1298 -0.0931 51  LEU F CA  
14793 C C   . LEU F 51  ? 2.0800 2.1858 2.1598 0.0408  -0.1151 -0.0870 51  LEU F C   
14794 O O   . LEU F 51  ? 2.0308 2.1279 2.0959 0.0447  -0.1060 -0.0897 51  LEU F O   
14795 C CB  . LEU F 51  ? 2.0772 2.1692 2.1195 0.0415  -0.1313 -0.0940 51  LEU F CB  
14796 C CG  . LEU F 51  ? 2.0679 2.1517 2.0982 0.0400  -0.1465 -0.1000 51  LEU F CG  
14797 C CD1 . LEU F 51  ? 1.9194 1.9965 1.9211 0.0430  -0.1472 -0.1001 51  LEU F CD1 
14798 C CD2 . LEU F 51  ? 2.0448 2.1420 2.0994 0.0355  -0.1565 -0.0964 51  LEU F CD2 
14799 N N   . ALA F 52  ? 1.9505 2.0728 2.0552 0.0383  -0.1129 -0.0790 52  ALA F N   
14800 C CA  . ALA F 52  ? 1.8613 1.9932 1.9777 0.0401  -0.1000 -0.0724 52  ALA F CA  
14801 C C   . ALA F 52  ? 1.7974 1.9389 1.9065 0.0419  -0.0938 -0.0659 52  ALA F C   
14802 O O   . ALA F 52  ? 1.7657 1.9229 1.8908 0.0401  -0.0924 -0.0583 52  ALA F O   
14803 C CB  . ALA F 52  ? 1.8392 1.9831 1.9853 0.0364  -0.1007 -0.0671 52  ALA F CB  
14804 N N   . ILE F 53  ? 1.7391 1.8703 1.8228 0.0454  -0.0899 -0.0693 53  ILE F N   
14805 C CA  . ILE F 53  ? 1.7503 1.8876 1.8233 0.0471  -0.0838 -0.0640 53  ILE F CA  
14806 C C   . ILE F 53  ? 1.7724 1.9164 1.8513 0.0497  -0.0695 -0.0596 53  ILE F C   
14807 O O   . ILE F 53  ? 1.8437 1.9852 1.9311 0.0509  -0.0642 -0.0615 53  ILE F O   
14808 C CB  . ILE F 53  ? 1.8004 1.9232 1.8424 0.0493  -0.0864 -0.0693 53  ILE F CB  
14809 C CG1 . ILE F 53  ? 1.8331 1.9418 1.8589 0.0529  -0.0787 -0.0759 53  ILE F CG1 
14810 C CG2 . ILE F 53  ? 1.8169 1.9329 1.8534 0.0470  -0.1015 -0.0742 53  ILE F CG2 
14811 C CD1 . ILE F 53  ? 1.8427 1.9364 1.8364 0.0551  -0.0800 -0.0812 53  ILE F CD1 
14812 N N   . ASN F 54  ? 1.8360 1.9883 1.9107 0.0506  -0.0632 -0.0537 54  ASN F N   
14813 C CA  . ASN F 54  ? 1.8432 2.0021 1.9217 0.0531  -0.0497 -0.0498 54  ASN F CA  
14814 C C   . ASN F 54  ? 1.8749 2.0260 1.9288 0.0561  -0.0421 -0.0512 54  ASN F C   
14815 O O   . ASN F 54  ? 1.8609 2.0134 1.9147 0.0588  -0.0304 -0.0505 54  ASN F O   
14816 C CB  . ASN F 54  ? 1.8133 1.9914 1.9127 0.0513  -0.0470 -0.0407 54  ASN F CB  
14817 C CG  . ASN F 54  ? 1.9065 2.0928 2.0145 0.0536  -0.0341 -0.0367 54  ASN F CG  
14818 O OD1 . ASN F 54  ? 2.0878 2.2761 2.2103 0.0543  -0.0307 -0.0367 54  ASN F OD1 
14819 N ND2 . ASN F 54  ? 1.8433 2.0342 1.9429 0.0547  -0.0270 -0.0331 54  ASN F ND2 
14820 N N   . TYR F 55  ? 1.9422 2.0852 1.9754 0.0558  -0.0482 -0.0532 55  TYR F N   
14821 C CA  . TYR F 55  ? 1.9993 2.1335 2.0071 0.0583  -0.0414 -0.0545 55  TYR F CA  
14822 C C   . TYR F 55  ? 2.0181 2.1338 2.0047 0.0605  -0.0424 -0.0638 55  TYR F C   
14823 O O   . TYR F 55  ? 2.0010 2.1108 1.9936 0.0601  -0.0483 -0.0692 55  TYR F O   
14824 C CB  . TYR F 55  ? 1.9881 2.1231 1.9841 0.0569  -0.0472 -0.0508 55  TYR F CB  
14825 C CG  . TYR F 55  ? 1.9718 2.0995 1.9614 0.0552  -0.0623 -0.0545 55  TYR F CG  
14826 C CD1 . TYR F 55  ? 1.9318 2.0697 1.9428 0.0523  -0.0718 -0.0521 55  TYR F CD1 
14827 C CD2 . TYR F 55  ? 1.9973 2.1082 1.9592 0.0566  -0.0672 -0.0605 55  TYR F CD2 
14828 C CE1 . TYR F 55  ? 1.8952 2.0272 1.9017 0.0507  -0.0858 -0.0557 55  TYR F CE1 
14829 C CE2 . TYR F 55  ? 1.9360 2.0404 1.8924 0.0552  -0.0817 -0.0641 55  TYR F CE2 
14830 C CZ  . TYR F 55  ? 1.8686 1.9839 1.8480 0.0522  -0.0910 -0.0618 55  TYR F CZ  
14831 O OH  . TYR F 55  ? 1.8229 1.9326 1.7982 0.0508  -0.1056 -0.0656 55  TYR F OH  
14832 N N   . GLN F 56  ? 2.1168 2.2229 2.0779 0.0627  -0.0364 -0.0657 56  GLN F N   
14833 C CA  . GLN F 56  ? 2.1457 2.2339 2.0838 0.0651  -0.0365 -0.0747 56  GLN F CA  
14834 C C   . GLN F 56  ? 2.1465 2.2236 2.0684 0.0637  -0.0510 -0.0790 56  GLN F C   
14835 O O   . GLN F 56  ? 2.1337 2.2120 2.0463 0.0625  -0.0560 -0.0749 56  GLN F O   
14836 C CB  . GLN F 56  ? 2.1531 2.2354 2.0695 0.0680  -0.0236 -0.0752 56  GLN F CB  
14837 C CG  . GLN F 56  ? 2.1894 2.2707 2.0872 0.0672  -0.0235 -0.0703 56  GLN F CG  
14838 C CD  . GLN F 56  ? 2.2881 2.3866 2.2051 0.0650  -0.0215 -0.0606 56  GLN F CD  
14839 O OE1 . GLN F 56  ? 2.2633 2.3753 2.2052 0.0647  -0.0161 -0.0571 56  GLN F OE1 
14840 N NE2 . GLN F 56  ? 2.2819 2.3799 2.1873 0.0637  -0.0261 -0.0562 56  GLN F NE2 
14841 N N   . PRO F 57  ? 1.9717 2.0378 1.8902 0.0638  -0.0585 -0.0872 57  PRO F N   
14842 C CA  . PRO F 57  ? 1.9141 1.9701 1.8184 0.0625  -0.0733 -0.0917 57  PRO F CA  
14843 C C   . PRO F 57  ? 1.8522 1.8927 1.7207 0.0647  -0.0731 -0.0957 57  PRO F C   
14844 O O   . PRO F 57  ? 1.8269 1.8576 1.6808 0.0639  -0.0857 -0.0998 57  PRO F O   
14845 C CB  . PRO F 57  ? 1.8760 1.9256 1.7902 0.0619  -0.0796 -0.0995 57  PRO F CB  
14846 C CG  . PRO F 57  ? 1.8813 1.9286 1.7974 0.0648  -0.0661 -0.1021 57  PRO F CG  
14847 C CD  . PRO F 57  ? 1.9666 2.0288 1.8947 0.0654  -0.0539 -0.0930 57  PRO F CD  
14848 N N   . GLU F 58  ? 1.8593 1.8974 1.7135 0.0672  -0.0593 -0.0944 58  GLU F N   
14849 C CA  . GLU F 58  ? 1.8541 1.8767 1.6730 0.0693  -0.0574 -0.0983 58  GLU F CA  
14850 C C   . GLU F 58  ? 1.8706 1.8907 1.6738 0.0680  -0.0667 -0.0940 58  GLU F C   
14851 O O   . GLU F 58  ? 1.8519 1.8571 1.6250 0.0693  -0.0703 -0.0982 58  GLU F O   
14852 C CB  . GLU F 58  ? 1.8303 1.8541 1.6412 0.0718  -0.0396 -0.0962 58  GLU F CB  
14853 C CG  . GLU F 58  ? 1.8501 1.8785 1.6795 0.0735  -0.0295 -0.0992 58  GLU F CG  
14854 C CD  . GLU F 58  ? 1.8767 1.9177 1.7172 0.0743  -0.0141 -0.0923 58  GLU F CD  
14855 O OE1 . GLU F 58  ? 1.8818 1.9277 1.7155 0.0733  -0.0111 -0.0853 58  GLU F OE1 
14856 O OE2 . GLU F 58  ? 1.8618 1.9080 1.7185 0.0761  -0.0053 -0.0939 58  GLU F OE2 
14857 N N   . VAL F 59  ? 1.9084 1.9425 1.7311 0.0656  -0.0709 -0.0860 59  VAL F N   
14858 C CA  . VAL F 59  ? 1.9062 1.9387 1.7160 0.0647  -0.0793 -0.0813 59  VAL F CA  
14859 C C   . VAL F 59  ? 1.8713 1.8995 1.6819 0.0633  -0.0976 -0.0852 59  VAL F C   
14860 O O   . VAL F 59  ? 1.8813 1.9031 1.6742 0.0634  -0.1065 -0.0838 59  VAL F O   
14861 C CB  . VAL F 59  ? 1.8852 1.9345 1.7147 0.0631  -0.0748 -0.0710 59  VAL F CB  
14862 C CG1 . VAL F 59  ? 1.9425 1.9956 1.7692 0.0643  -0.0572 -0.0671 59  VAL F CG1 
14863 C CG2 . VAL F 59  ? 1.8425 1.9073 1.7073 0.0608  -0.0793 -0.0691 59  VAL F CG2 
14864 N N   . MET F 60  ? 1.8280 1.8596 1.6589 0.0619  -0.1037 -0.0899 60  MET F N   
14865 C CA  . MET F 60  ? 1.8040 1.8337 1.6401 0.0601  -0.1210 -0.0935 60  MET F CA  
14866 C C   . MET F 60  ? 1.8093 1.8247 1.6345 0.0607  -0.1270 -0.1044 60  MET F C   
14867 O O   . MET F 60  ? 1.7995 1.8138 1.6324 0.0588  -0.1412 -0.1086 60  MET F O   
14868 C CB  . MET F 60  ? 1.7914 1.8388 1.6640 0.0570  -0.1249 -0.0890 60  MET F CB  
14869 C CG  . MET F 60  ? 1.8109 1.8642 1.7055 0.0564  -0.1172 -0.0909 60  MET F CG  
14870 S SD  . MET F 60  ? 1.7978 1.8728 1.7336 0.0528  -0.1194 -0.0841 60  MET F SD  
14871 C CE  . MET F 60  ? 1.8532 1.9283 1.8064 0.0527  -0.1118 -0.0883 60  MET F CE  
14872 N N   . LEU F 61  ? 1.8221 1.8269 1.6302 0.0633  -0.1167 -0.1095 61  LEU F N   
14873 C CA  . LEU F 61  ? 1.8622 1.8527 1.6592 0.0641  -0.1221 -0.1206 61  LEU F CA  
14874 C C   . LEU F 61  ? 1.9259 1.9030 1.6975 0.0643  -0.1367 -0.1255 61  LEU F C   
14875 O O   . LEU F 61  ? 1.9804 1.9503 1.7525 0.0633  -0.1483 -0.1336 61  LEU F O   
14876 C CB  . LEU F 61  ? 1.8422 1.8239 1.6239 0.0673  -0.1073 -0.1250 61  LEU F CB  
14877 C CG  . LEU F 61  ? 1.8243 1.8169 1.6328 0.0674  -0.0950 -0.1229 61  LEU F CG  
14878 C CD1 . LEU F 61  ? 1.7768 1.7602 1.5696 0.0711  -0.0809 -0.1282 61  LEU F CD1 
14879 C CD2 . LEU F 61  ? 1.8122 1.8090 1.6478 0.0649  -0.1037 -0.1263 61  LEU F CD2 
14880 N N   . ASN F 62  ? 1.9227 1.8962 1.6719 0.0655  -0.1367 -0.1208 62  ASN F N   
14881 C CA  . ASN F 62  ? 1.9637 1.9248 1.6885 0.0660  -0.1513 -0.1246 62  ASN F CA  
14882 C C   . ASN F 62  ? 1.9798 1.9495 1.7258 0.0631  -0.1679 -0.1233 62  ASN F C   
14883 O O   . ASN F 62  ? 1.9928 1.9534 1.7287 0.0628  -0.1826 -0.1300 62  ASN F O   
14884 C CB  . ASN F 62  ? 1.9844 1.9399 1.6814 0.0678  -0.1472 -0.1185 62  ASN F CB  
14885 C CG  . ASN F 62  ? 2.0674 2.0097 1.7350 0.0707  -0.1342 -0.1222 62  ASN F CG  
14886 O OD1 . ASN F 62  ? 2.1263 2.0574 1.7827 0.0719  -0.1343 -0.1319 62  ASN F OD1 
14887 N ND2 . ASN F 62  ? 2.0754 2.0188 1.7305 0.0717  -0.1227 -0.1147 62  ASN F ND2 
14888 N N   . PHE F 63  ? 1.9510 1.9386 1.7267 0.0610  -0.1658 -0.1152 63  PHE F N   
14889 C CA  . PHE F 63  ? 1.9373 1.9348 1.7354 0.0583  -0.1803 -0.1138 63  PHE F CA  
14890 C C   . PHE F 63  ? 1.9781 1.9777 1.7983 0.0558  -0.1863 -0.1208 63  PHE F C   
14891 O O   . PHE F 63  ? 2.0092 2.0069 1.8336 0.0541  -0.2018 -0.1255 63  PHE F O   
14892 C CB  . PHE F 63  ? 1.8542 1.8700 1.6760 0.0570  -0.1754 -0.1031 63  PHE F CB  
14893 C CG  . PHE F 63  ? 1.8045 1.8186 1.6073 0.0588  -0.1733 -0.0961 63  PHE F CG  
14894 C CD1 . PHE F 63  ? 1.7527 1.7676 1.5526 0.0587  -0.1870 -0.0936 63  PHE F CD1 
14895 C CD2 . PHE F 63  ? 1.8008 1.8124 1.5891 0.0607  -0.1578 -0.0919 63  PHE F CD2 
14896 C CE1 . PHE F 63  ? 1.6902 1.7025 1.4727 0.0605  -0.1853 -0.0868 63  PHE F CE1 
14897 C CE2 . PHE F 63  ? 1.8103 1.8197 1.5814 0.0620  -0.1557 -0.0852 63  PHE F CE2 
14898 C CZ  . PHE F 63  ? 1.7617 1.7709 1.5295 0.0620  -0.1695 -0.0825 63  PHE F CZ  
14899 N N   . LEU F 64  ? 1.9913 1.9948 1.8263 0.0554  -0.1745 -0.1215 64  LEU F N   
14900 C CA  . LEU F 64  ? 2.0301 2.0346 1.8862 0.0529  -0.1793 -0.1277 64  LEU F CA  
14901 C C   . LEU F 64  ? 2.0516 2.0375 1.8860 0.0539  -0.1867 -0.1395 64  LEU F C   
14902 O O   . LEU F 64  ? 2.0575 2.0419 1.9054 0.0514  -0.1969 -0.1457 64  LEU F O   
14903 C CB  . LEU F 64  ? 2.0252 2.0380 1.9017 0.0528  -0.1645 -0.1249 64  LEU F CB  
14904 C CG  . LEU F 64  ? 1.9835 2.0145 1.8802 0.0520  -0.1561 -0.1136 64  LEU F CG  
14905 C CD1 . LEU F 64  ? 1.9369 1.9749 1.8519 0.0522  -0.1422 -0.1114 64  LEU F CD1 
14906 C CD2 . LEU F 64  ? 1.9812 2.0257 1.9021 0.0484  -0.1676 -0.1095 64  LEU F CD2 
14907 N N   . LYS F 65  ? 2.2338 2.2053 2.0346 0.0575  -0.1816 -0.1428 65  LYS F N   
14908 C CA  . LYS F 65  ? 2.2581 2.2112 2.0353 0.0587  -0.1886 -0.1543 65  LYS F CA  
14909 C C   . LYS F 65  ? 2.2490 2.1960 2.0135 0.0579  -0.2073 -0.1577 65  LYS F C   
14910 O O   . LYS F 65  ? 2.2579 2.1936 2.0144 0.0574  -0.2178 -0.1677 65  LYS F O   
14911 C CB  . LYS F 65  ? 2.3145 2.2545 2.0592 0.0628  -0.1761 -0.1567 65  LYS F CB  
14912 C CG  . LYS F 65  ? 2.3824 2.3047 2.1082 0.0644  -0.1778 -0.1693 65  LYS F CG  
14913 C CD  . LYS F 65  ? 2.4698 2.3816 2.1667 0.0685  -0.1628 -0.1710 65  LYS F CD  
14914 C CE  . LYS F 65  ? 2.4736 2.3977 2.1882 0.0693  -0.1446 -0.1633 65  LYS F CE  
14915 N NZ  . LYS F 65  ? 2.5247 2.4402 2.2125 0.0731  -0.1295 -0.1643 65  LYS F NZ  
14916 N N   . ASP F 66  ? 2.1291 2.0834 1.8922 0.0579  -0.2120 -0.1497 66  ASP F N   
14917 C CA  . ASP F 66  ? 2.1452 2.0946 1.8976 0.0575  -0.2303 -0.1522 66  ASP F CA  
14918 C C   . ASP F 66  ? 2.1454 2.1066 1.9305 0.0535  -0.2434 -0.1533 66  ASP F C   
14919 O O   . ASP F 66  ? 2.1629 2.1197 1.9426 0.0528  -0.2600 -0.1578 66  ASP F O   
14920 C CB  . ASP F 66  ? 2.1330 2.0847 1.8705 0.0594  -0.2306 -0.1433 66  ASP F CB  
14921 C CG  . ASP F 66  ? 2.1218 2.0606 1.8239 0.0631  -0.2190 -0.1423 66  ASP F CG  
14922 O OD1 . ASP F 66  ? 2.1581 2.0822 1.8386 0.0647  -0.2165 -0.1509 66  ASP F OD1 
14923 O OD2 . ASP F 66  ? 2.0641 2.0074 1.7600 0.0643  -0.2122 -0.1331 66  ASP F OD2 
14924 N N   . PHE F 67  ? 2.2076 2.1837 2.0263 0.0508  -0.2363 -0.1490 67  PHE F N   
14925 C CA  . PHE F 67  ? 2.1766 2.1648 2.0281 0.0465  -0.2470 -0.1496 67  PHE F CA  
14926 C C   . PHE F 67  ? 2.1793 2.1617 2.0423 0.0440  -0.2496 -0.1588 67  PHE F C   
14927 O O   . PHE F 67  ? 2.1585 2.1478 2.0452 0.0402  -0.2606 -0.1612 67  PHE F O   
14928 C CB  . PHE F 67  ? 2.1813 2.1898 2.0634 0.0447  -0.2386 -0.1390 67  PHE F CB  
14929 C CG  . PHE F 67  ? 2.1809 2.1962 2.0559 0.0466  -0.2378 -0.1300 67  PHE F CG  
14930 C CD1 . PHE F 67  ? 2.1627 2.1698 2.0150 0.0486  -0.2497 -0.1313 67  PHE F CD1 
14931 C CD2 . PHE F 67  ? 2.1234 2.1528 2.0142 0.0465  -0.2254 -0.1203 67  PHE F CD2 
14932 C CE1 . PHE F 67  ? 2.1484 2.1607 1.9943 0.0504  -0.2491 -0.1230 67  PHE F CE1 
14933 C CE2 . PHE F 67  ? 2.0951 2.1302 1.9798 0.0482  -0.2247 -0.1124 67  PHE F CE2 
14934 C CZ  . PHE F 67  ? 2.1185 2.1447 1.9808 0.0502  -0.2365 -0.1136 67  PHE F CZ  
14935 N N   . GLU F 68  ? 2.1033 2.0735 1.9511 0.0461  -0.2397 -0.1642 68  GLU F N   
14936 C CA  . GLU F 68  ? 2.0362 1.9997 1.8946 0.0439  -0.2419 -0.1732 68  GLU F CA  
14937 C C   . GLU F 68  ? 2.0735 2.0236 1.9170 0.0432  -0.2591 -0.1841 68  GLU F C   
14938 O O   . GLU F 68  ? 2.0708 2.0207 1.9329 0.0395  -0.2674 -0.1903 68  GLU F O   
14939 C CB  . GLU F 68  ? 1.9951 1.9489 1.8410 0.0469  -0.2264 -0.1762 68  GLU F CB  
14940 C CG  . GLU F 68  ? 1.9501 1.9172 1.8181 0.0469  -0.2102 -0.1675 68  GLU F CG  
14941 C CD  . GLU F 68  ? 1.8745 1.8319 1.7329 0.0499  -0.1962 -0.1718 68  GLU F CD  
14942 O OE1 . GLU F 68  ? 1.8801 1.8248 1.7070 0.0538  -0.1913 -0.1755 68  GLU F OE1 
14943 O OE2 . GLU F 68  ? 1.8601 1.8222 1.7423 0.0484  -0.1902 -0.1715 68  GLU F OE2 
14944 N N   . THR F 69  ? 2.0703 2.0092 1.8805 0.0464  -0.2648 -0.1865 69  THR F N   
14945 C CA  . THR F 69  ? 2.0580 1.9838 1.8513 0.0460  -0.2817 -0.1969 69  THR F CA  
14946 C C   . THR F 69  ? 2.0263 1.9617 1.8328 0.0436  -0.2987 -0.1946 69  THR F C   
14947 O O   . THR F 69  ? 2.0208 1.9528 1.8340 0.0409  -0.3137 -0.2026 69  THR F O   
14948 C CB  . THR F 69  ? 2.0606 1.9685 1.8097 0.0508  -0.2801 -0.2011 69  THR F CB  
14949 O OG1 . THR F 69  ? 2.0806 1.9923 1.8186 0.0540  -0.2648 -0.1916 69  THR F OG1 
14950 C CG2 . THR F 69  ? 2.1127 2.0040 1.8466 0.0519  -0.2767 -0.2128 69  THR F CG2 
14951 N N   . LYS F 70  ? 2.0152 1.9625 1.8257 0.0446  -0.2967 -0.1840 70  LYS F N   
14952 C CA  . LYS F 70  ? 1.9961 1.9534 1.8203 0.0428  -0.3122 -0.1813 70  LYS F CA  
14953 C C   . LYS F 70  ? 1.9751 1.9471 1.8405 0.0374  -0.3172 -0.1817 70  LYS F C   
14954 O O   . LYS F 70  ? 1.9712 1.9461 1.8477 0.0349  -0.3335 -0.1859 70  LYS F O   
14955 C CB  . LYS F 70  ? 2.0239 1.9910 1.8455 0.0452  -0.3070 -0.1696 70  LYS F CB  
14956 C CG  . LYS F 70  ? 2.0391 2.0178 1.8764 0.0439  -0.3220 -0.1661 70  LYS F CG  
14957 C CD  . LYS F 70  ? 2.0413 2.0310 1.8808 0.0460  -0.3149 -0.1542 70  LYS F CD  
14958 C CE  . LYS F 70  ? 1.9633 1.9670 1.8279 0.0443  -0.2979 -0.1468 70  LYS F CE  
14959 N NZ  . LYS F 70  ? 1.9099 1.9237 1.7761 0.0462  -0.2909 -0.1356 70  LYS F NZ  
14960 N N   . LEU F 71  ? 1.9838 1.9651 1.8724 0.0355  -0.3033 -0.1772 71  LEU F N   
14961 C CA  . LEU F 71  ? 1.9347 1.9306 1.8626 0.0302  -0.3059 -0.1760 71  LEU F CA  
14962 C C   . LEU F 71  ? 1.9741 1.9622 1.9117 0.0272  -0.3053 -0.1846 71  LEU F C   
14963 O O   . LEU F 71  ? 1.9778 1.9760 1.9471 0.0223  -0.3089 -0.1847 71  LEU F O   
14964 C CB  . LEU F 71  ? 1.9191 1.9323 1.8691 0.0297  -0.2917 -0.1642 71  LEU F CB  
14965 C CG  . LEU F 71  ? 1.9145 1.9367 1.8587 0.0323  -0.2919 -0.1553 71  LEU F CG  
14966 C CD1 . LEU F 71  ? 1.9310 1.9693 1.8956 0.0319  -0.2773 -0.1445 71  LEU F CD1 
14967 C CD2 . LEU F 71  ? 1.8905 1.9199 1.8458 0.0305  -0.3096 -0.1565 71  LEU F CD2 
14968 N N   . GLU F 72  ? 2.0501 2.0201 1.9611 0.0301  -0.3009 -0.1920 72  GLU F N   
14969 C CA  . GLU F 72  ? 2.0583 2.0186 1.9757 0.0280  -0.2993 -0.2006 72  GLU F CA  
14970 C C   . GLU F 72  ? 2.0589 2.0313 2.0078 0.0253  -0.2865 -0.1942 72  GLU F C   
14971 O O   . GLU F 72  ? 2.0475 2.0253 2.0243 0.0203  -0.2910 -0.1961 72  GLU F O   
14972 C CB  . GLU F 72  ? 1.9950 1.9504 1.9196 0.0240  -0.3178 -0.2106 72  GLU F CB  
14973 C CG  . GLU F 72  ? 2.0524 1.9913 1.9418 0.0271  -0.3300 -0.2196 72  GLU F CG  
14974 C CD  . GLU F 72  ? 2.1898 2.1233 2.0869 0.0231  -0.3482 -0.2304 72  GLU F CD  
14975 O OE1 . GLU F 72  ? 2.2177 2.1639 2.1493 0.0177  -0.3538 -0.2290 72  GLU F OE1 
14976 O OE2 . GLU F 72  ? 2.2273 2.1440 2.0961 0.0252  -0.3570 -0.2403 72  GLU F OE2 
14977 N N   . ILE F 73  ? 1.9666 1.9428 1.9102 0.0286  -0.2703 -0.1864 73  ILE F N   
14978 C CA  . ILE F 73  ? 1.9364 1.9243 1.9067 0.0270  -0.2570 -0.1791 73  ILE F CA  
14979 C C   . ILE F 73  ? 1.9390 1.9195 1.8908 0.0318  -0.2404 -0.1777 73  ILE F C   
14980 O O   . ILE F 73  ? 1.9262 1.9016 1.8509 0.0361  -0.2365 -0.1763 73  ILE F O   
14981 C CB  . ILE F 73  ? 1.9053 1.9146 1.8989 0.0250  -0.2558 -0.1674 73  ILE F CB  
14982 C CG1 . ILE F 73  ? 1.9158 1.9353 1.9392 0.0191  -0.2683 -0.1683 73  ILE F CG1 
14983 C CG2 . ILE F 73  ? 1.9036 1.9232 1.9113 0.0259  -0.2386 -0.1582 73  ILE F CG2 
14984 C CD1 . ILE F 73  ? 1.9504 1.9914 1.9992 0.0169  -0.2661 -0.1574 73  ILE F CD1 
14985 N N   . LYS F 74  ? 1.9360 1.9160 1.9029 0.0312  -0.2305 -0.1780 74  LYS F N   
14986 C CA  . LYS F 74  ? 1.9229 1.8977 1.8771 0.0357  -0.2141 -0.1765 74  LYS F CA  
14987 C C   . LYS F 74  ? 1.9061 1.8984 1.8746 0.0363  -0.2024 -0.1636 74  LYS F C   
14988 O O   . LYS F 74  ? 1.9029 1.9094 1.9015 0.0328  -0.2015 -0.1573 74  LYS F O   
14989 C CB  . LYS F 74  ? 1.9034 1.8695 1.8679 0.0352  -0.2091 -0.1826 74  LYS F CB  
14990 C CG  . LYS F 74  ? 1.8950 1.8542 1.8452 0.0404  -0.1929 -0.1829 74  LYS F CG  
14991 C CD  . LYS F 74  ? 1.8894 1.8337 1.8009 0.0449  -0.1928 -0.1896 74  LYS F CD  
14992 C CE  . LYS F 74  ? 1.9185 1.8556 1.8163 0.0500  -0.1765 -0.1910 74  LYS F CE  
14993 N NZ  . LYS F 74  ? 1.9514 1.8799 1.8613 0.0499  -0.1735 -0.1980 74  LYS F NZ  
14994 N N   . ILE F 75  ? 1.9334 1.9246 1.8800 0.0407  -0.1934 -0.1599 75  ILE F N   
14995 C CA  . ILE F 75  ? 1.9359 1.9428 1.8928 0.0416  -0.1826 -0.1482 75  ILE F CA  
14996 C C   . ILE F 75  ? 1.9506 1.9527 1.8957 0.0460  -0.1660 -0.1475 75  ILE F C   
14997 O O   . ILE F 75  ? 1.9201 1.9101 1.8355 0.0497  -0.1626 -0.1517 75  ILE F O   
14998 C CB  . ILE F 75  ? 1.8564 1.8686 1.8004 0.0423  -0.1878 -0.1430 75  ILE F CB  
14999 C CG1 . ILE F 75  ? 1.8601 1.8780 1.8176 0.0383  -0.2045 -0.1440 75  ILE F CG1 
15000 C CG2 . ILE F 75  ? 1.8546 1.8822 1.8087 0.0433  -0.1760 -0.1315 75  ILE F CG2 
15001 C CD1 . ILE F 75  ? 1.8719 1.8940 1.8171 0.0393  -0.2112 -0.1396 75  ILE F CD1 
15002 N N   . THR F 76  ? 1.9995 2.0113 1.9678 0.0455  -0.1558 -0.1421 76  THR F N   
15003 C CA  . THR F 76  ? 2.0261 2.0363 1.9887 0.0495  -0.1397 -0.1405 76  THR F CA  
15004 C C   . THR F 76  ? 2.1621 2.1910 2.1445 0.0492  -0.1303 -0.1287 76  THR F C   
15005 O O   . THR F 76  ? 2.2408 2.2832 2.2472 0.0454  -0.1352 -0.1227 76  THR F O   
15006 C CB  . THR F 76  ? 2.0825 2.0834 2.0531 0.0502  -0.1360 -0.1473 76  THR F CB  
15007 O OG1 . THR F 76  ? 2.2832 2.2930 2.2853 0.0458  -0.1407 -0.1443 76  THR F OG1 
15008 C CG2 . THR F 76  ? 2.0136 1.9947 1.9614 0.0512  -0.1440 -0.1600 76  THR F CG2 
15009 N N   . CYS F 77  ? 2.0978 2.1278 2.0701 0.0530  -0.1166 -0.1254 77  CYS F N   
15010 C CA  . CYS F 77  ? 2.0433 2.0904 2.0310 0.0531  -0.1072 -0.1146 77  CYS F CA  
15011 C C   . CYS F 77  ? 1.9922 2.0440 1.9984 0.0544  -0.0958 -0.1125 77  CYS F C   
15012 O O   . CYS F 77  ? 1.9513 1.9916 1.9520 0.0568  -0.0917 -0.1194 77  CYS F O   
15013 C CB  . CYS F 77  ? 2.0163 2.0632 1.9812 0.0561  -0.0998 -0.1113 77  CYS F CB  
15014 S SG  . CYS F 77  ? 2.1203 2.1634 2.0642 0.0549  -0.1124 -0.1114 77  CYS F SG  
15015 N N   . SER F 78  ? 2.0331 2.1020 2.0615 0.0530  -0.0911 -0.1028 78  SER F N   
15016 C CA  . SER F 78  ? 2.0220 2.0978 2.0683 0.0546  -0.0798 -0.0989 78  SER F CA  
15017 C C   . SER F 78  ? 1.9899 2.0809 2.0407 0.0555  -0.0707 -0.0894 78  SER F C   
15018 O O   . SER F 78  ? 1.9394 2.0430 2.0009 0.0526  -0.0751 -0.0827 78  SER F O   
15019 C CB  . SER F 78  ? 2.0127 2.0942 2.0871 0.0509  -0.0850 -0.0970 78  SER F CB  
15020 O OG  . SER F 78  ? 1.9564 2.0532 2.0470 0.0469  -0.0905 -0.0893 78  SER F OG  
15021 N N   . GLN F 79  ? 2.0197 2.1097 2.0631 0.0596  -0.0579 -0.0890 79  GLN F N   
15022 C CA  . GLN F 79  ? 2.0476 2.1509 2.0937 0.0607  -0.0483 -0.0808 79  GLN F CA  
15023 C C   . GLN F 79  ? 2.1431 2.2558 2.2106 0.0623  -0.0386 -0.0765 79  GLN F C   
15024 O O   . GLN F 79  ? 2.1732 2.2779 2.2391 0.0656  -0.0324 -0.0814 79  GLN F O   
15025 C CB  . GLN F 79  ? 2.0067 2.1020 2.0252 0.0640  -0.0412 -0.0835 79  GLN F CB  
15026 C CG  . GLN F 79  ? 1.9970 2.1051 2.0171 0.0648  -0.0315 -0.0755 79  GLN F CG  
15027 C CD  . GLN F 79  ? 1.9719 2.0713 1.9647 0.0678  -0.0236 -0.0782 79  GLN F CD  
15028 O OE1 . GLN F 79  ? 1.9414 2.0250 1.9132 0.0696  -0.0250 -0.0863 79  GLN F OE1 
15029 N NE2 . GLN F 79  ? 1.9742 2.0837 1.9669 0.0681  -0.0152 -0.0715 79  GLN F NE2 
15030 N N   . GLU F 80  ? 2.3446 2.4743 2.4321 0.0602  -0.0374 -0.0675 80  GLU F N   
15031 C CA  . GLU F 80  ? 2.3600 2.5005 2.4683 0.0616  -0.0288 -0.0621 80  GLU F CA  
15032 C C   . GLU F 80  ? 2.3952 2.5451 2.4997 0.0640  -0.0176 -0.0571 80  GLU F C   
15033 O O   . GLU F 80  ? 2.3464 2.5004 2.4406 0.0629  -0.0183 -0.0542 80  GLU F O   
15034 C CB  . GLU F 80  ? 2.3392 2.4926 2.4729 0.0576  -0.0346 -0.0555 80  GLU F CB  
15035 C CG  . GLU F 80  ? 2.3562 2.5017 2.4992 0.0551  -0.0438 -0.0596 80  GLU F CG  
15036 C CD  . GLU F 80  ? 2.4018 2.5390 2.5325 0.0521  -0.0558 -0.0647 80  GLU F CD  
15037 O OE1 . GLU F 80  ? 2.3270 2.4655 2.4430 0.0520  -0.0575 -0.0641 80  GLU F OE1 
15038 O OE2 . GLU F 80  ? 2.4342 2.5633 2.5702 0.0499  -0.0637 -0.0694 80  GLU F OE2 
15039 N N   . THR F 81  ? 2.4194 2.5727 2.5329 0.0673  -0.0075 -0.0560 81  THR F N   
15040 C CA  . THR F 81  ? 2.4833 2.6468 2.5964 0.0695  0.0035  -0.0513 81  THR F CA  
15041 C C   . THR F 81  ? 2.5198 2.7010 2.6481 0.0664  0.0020  -0.0420 81  THR F C   
15042 O O   . THR F 81  ? 2.5214 2.7084 2.6415 0.0659  0.0050  -0.0387 81  THR F O   
15043 C CB  . THR F 81  ? 2.4819 2.6465 2.6051 0.0738  0.0137  -0.0521 81  THR F CB  
15044 O OG1 . THR F 81  ? 2.4549 2.6248 2.6014 0.0728  0.0101  -0.0489 81  THR F OG1 
15045 C CG2 . THR F 81  ? 2.4468 2.5941 2.5525 0.0774  0.0169  -0.0618 81  THR F CG2 
15046 N N   . GLU F 82  ? 2.5675 2.7573 2.7179 0.0643  -0.0024 -0.0376 82  GLU F N   
15047 C CA  . GLU F 82  ? 2.5582 2.7648 2.7238 0.0613  -0.0041 -0.0292 82  GLU F CA  
15048 C C   . GLU F 82  ? 2.5391 2.7470 2.7140 0.0569  -0.0159 -0.0282 82  GLU F C   
15049 O O   . GLU F 82  ? 2.4976 2.6960 2.6753 0.0563  -0.0212 -0.0325 82  GLU F O   
15050 C CB  . GLU F 82  ? 2.5248 2.7444 2.7108 0.0629  0.0032  -0.0232 82  GLU F CB  
15051 C CG  . GLU F 82  ? 2.5533 2.7767 2.7348 0.0667  0.0151  -0.0226 82  GLU F CG  
15052 C CD  . GLU F 82  ? 2.5554 2.7651 2.7259 0.0710  0.0209  -0.0299 82  GLU F CD  
15053 O OE1 . GLU F 82  ? 2.5358 2.7378 2.7130 0.0721  0.0183  -0.0332 82  GLU F OE1 
15054 O OE2 . GLU F 82  ? 2.5838 2.7902 2.7392 0.0733  0.0282  -0.0325 82  GLU F OE2 
15055 N N   . PRO F 83  ? 2.6286 2.8478 2.8087 0.0538  -0.0200 -0.0230 83  PRO F N   
15056 C CA  . PRO F 83  ? 2.6100 2.8338 2.8035 0.0495  -0.0299 -0.0211 83  PRO F CA  
15057 C C   . PRO F 83  ? 2.5826 2.8135 2.7984 0.0489  -0.0284 -0.0170 83  PRO F C   
15058 O O   . PRO F 83  ? 2.5451 2.7887 2.7730 0.0497  -0.0220 -0.0107 83  PRO F O   
15059 C CB  . PRO F 83  ? 2.6129 2.8494 2.8080 0.0473  -0.0319 -0.0157 83  PRO F CB  
15060 C CG  . PRO F 83  ? 2.5988 2.8312 2.7745 0.0499  -0.0260 -0.0171 83  PRO F CG  
15061 C CD  . PRO F 83  ? 2.6066 2.8340 2.7795 0.0539  -0.0161 -0.0192 83  PRO F CD  
15062 N N   . LEU F 84  ? 2.3258 2.5482 2.5470 0.0473  -0.0344 -0.0205 84  LEU F N   
15063 C CA  . LEU F 84  ? 2.1943 2.4203 2.4353 0.0467  -0.0333 -0.0169 84  LEU F CA  
15064 C C   . LEU F 84  ? 2.2247 2.4609 2.4822 0.0415  -0.0406 -0.0121 84  LEU F C   
15065 O O   . LEU F 84  ? 2.2805 2.5118 2.5474 0.0388  -0.0462 -0.0134 84  LEU F O   
15066 C CB  . LEU F 84  ? 2.0998 2.3092 2.3371 0.0484  -0.0342 -0.0238 84  LEU F CB  
15067 C CG  . LEU F 84  ? 2.0442 2.2421 2.2638 0.0535  -0.0273 -0.0299 84  LEU F CG  
15068 C CD1 . LEU F 84  ? 1.8933 2.0740 2.1093 0.0547  -0.0298 -0.0376 84  LEU F CD1 
15069 C CD2 . LEU F 84  ? 1.9869 2.1940 2.2127 0.0574  -0.0162 -0.0251 84  LEU F CD2 
15070 N N   . GLY F 85  ? 2.3303 2.5810 2.5916 0.0400  -0.0402 -0.0066 85  GLY F N   
15071 C CA  . GLY F 85  ? 2.3091 2.5707 2.5854 0.0352  -0.0465 -0.0022 85  GLY F CA  
15072 C C   . GLY F 85  ? 2.3725 2.6266 2.6425 0.0321  -0.0568 -0.0076 85  GLY F C   
15073 O O   . GLY F 85  ? 2.3968 2.6440 2.6493 0.0334  -0.0593 -0.0123 85  GLY F O   
15074 N N   . THR F 86  ? 2.3289 2.5846 2.6134 0.0280  -0.0630 -0.0069 86  THR F N   
15075 C CA  . THR F 86  ? 2.3455 2.5949 2.6273 0.0247  -0.0735 -0.0121 86  THR F CA  
15076 C C   . THR F 86  ? 2.5852 2.8192 2.8669 0.0238  -0.0777 -0.0182 86  THR F C   
15077 O O   . THR F 86  ? 2.4660 2.6899 2.7379 0.0227  -0.0856 -0.0250 86  THR F O   
15078 C CB  . THR F 86  ? 2.1859 2.4501 2.4852 0.0198  -0.0785 -0.0072 86  THR F CB  
15079 O OG1 . THR F 86  ? 2.1375 2.4175 2.4426 0.0206  -0.0723 -0.0001 86  THR F OG1 
15080 C CG2 . THR F 86  ? 2.0809 2.3430 2.3737 0.0177  -0.0884 -0.0120 86  THR F CG2 
15081 N N   . ALA F 87  ? 3.8610 4.0929 4.1534 0.0242  -0.0730 -0.0159 87  ALA F N   
15082 C CA  . ALA F 87  ? 3.8947 4.1116 4.1885 0.0234  -0.0765 -0.0214 87  ALA F CA  
15083 C C   . ALA F 87  ? 3.9356 4.1379 4.2147 0.0287  -0.0710 -0.0269 87  ALA F C   
15084 O O   . ALA F 87  ? 3.9701 4.1578 4.2468 0.0286  -0.0742 -0.0332 87  ALA F O   
15085 C CB  . ALA F 87  ? 3.8739 4.0960 4.1899 0.0201  -0.0757 -0.0154 87  ALA F CB  
15086 N N   . GLY F 88  ? 2.7745 2.9807 3.0443 0.0333  -0.0626 -0.0249 88  GLY F N   
15087 C CA  . GLY F 88  ? 2.5163 2.7104 2.7726 0.0386  -0.0562 -0.0299 88  GLY F CA  
15088 C C   . GLY F 88  ? 2.5007 2.6780 2.7363 0.0397  -0.0610 -0.0401 88  GLY F C   
15089 O O   . GLY F 88  ? 2.5185 2.6813 2.7494 0.0416  -0.0607 -0.0464 88  GLY F O   
15090 N N   . PRO F 89  ? 2.4046 2.5832 2.6265 0.0388  -0.0655 -0.0420 89  PRO F N   
15091 C CA  . PRO F 89  ? 2.4156 2.5782 2.6162 0.0399  -0.0709 -0.0515 89  PRO F CA  
15092 C C   . PRO F 89  ? 2.6133 2.7637 2.8179 0.0370  -0.0798 -0.0580 89  PRO F C   
15093 O O   . PRO F 89  ? 2.5665 2.7010 2.7543 0.0388  -0.0825 -0.0668 89  PRO F O   
15094 C CB  . PRO F 89  ? 2.1724 2.3416 2.3641 0.0382  -0.0762 -0.0501 89  PRO F CB  
15095 C CG  . PRO F 89  ? 2.1316 2.3175 2.3318 0.0390  -0.0686 -0.0413 89  PRO F CG  
15096 C CD  . PRO F 89  ? 2.3139 2.5078 2.5371 0.0378  -0.0647 -0.0356 89  PRO F CD  
15097 N N   . LEU F 90  ? 3.1121 3.2696 3.3385 0.0325  -0.0843 -0.0538 90  LEU F N   
15098 C CA  . LEU F 90  ? 3.1316 3.2778 3.3643 0.0293  -0.0922 -0.0596 90  LEU F CA  
15099 C C   . LEU F 90  ? 3.1581 3.2928 3.3935 0.0321  -0.0866 -0.0623 90  LEU F C   
15100 O O   . LEU F 90  ? 3.1912 3.3109 3.4230 0.0314  -0.0919 -0.0702 90  LEU F O   
15101 C CB  . LEU F 90  ? 3.0964 3.2541 3.3521 0.0231  -0.0984 -0.0541 90  LEU F CB  
15102 C CG  . LEU F 90  ? 3.0643 3.2306 3.3199 0.0195  -0.1072 -0.0537 90  LEU F CG  
15103 C CD1 . LEU F 90  ? 3.0337 3.2161 3.2887 0.0209  -0.1020 -0.0462 90  LEU F CD1 
15104 C CD2 . LEU F 90  ? 3.0415 3.2129 3.3184 0.0130  -0.1149 -0.0521 90  LEU F CD2 
15105 N N   . ALA F 91  ? 2.7018 2.8433 2.9441 0.0354  -0.0762 -0.0562 91  ALA F N   
15106 C CA  . ALA F 91  ? 2.5049 2.6358 2.7504 0.0388  -0.0706 -0.0586 91  ALA F CA  
15107 C C   . ALA F 91  ? 2.4779 2.5931 2.7005 0.0439  -0.0677 -0.0683 91  ALA F C   
15108 O O   . ALA F 91  ? 2.4119 2.5132 2.6338 0.0460  -0.0668 -0.0743 91  ALA F O   
15109 C CB  . ALA F 91  ? 2.3224 2.4655 2.5810 0.0414  -0.0606 -0.0495 91  ALA F CB  
15110 N N   . LEU F 92  ? 2.5021 2.6192 2.7057 0.0460  -0.0661 -0.0701 92  LEU F N   
15111 C CA  . LEU F 92  ? 2.5008 2.6035 2.6808 0.0506  -0.0629 -0.0790 92  LEU F CA  
15112 C C   . LEU F 92  ? 2.5014 2.5889 2.6684 0.0484  -0.0735 -0.0889 92  LEU F C   
15113 O O   . LEU F 92  ? 2.4516 2.5231 2.6054 0.0515  -0.0725 -0.0979 92  LEU F O   
15114 C CB  . LEU F 92  ? 2.4738 2.5838 2.6379 0.0533  -0.0568 -0.0766 92  LEU F CB  
15115 C CG  . LEU F 92  ? 2.4612 2.5586 2.5993 0.0581  -0.0516 -0.0845 92  LEU F CG  
15116 C CD1 . LEU F 92  ? 2.4817 2.5889 2.6163 0.0620  -0.0394 -0.0793 92  LEU F CD1 
15117 C CD2 . LEU F 92  ? 2.3884 2.4784 2.5055 0.0564  -0.0603 -0.0900 92  LEU F CD2 
15118 N N   . ALA F 93  ? 2.4971 2.5895 2.6678 0.0433  -0.0838 -0.0878 93  ALA F N   
15119 C CA  . ALA F 93  ? 2.4149 2.4944 2.5736 0.0410  -0.0952 -0.0968 93  ALA F CA  
15120 C C   . ALA F 93  ? 2.3243 2.3966 2.4993 0.0370  -0.1025 -0.1002 93  ALA F C   
15121 O O   . ALA F 93  ? 2.2891 2.3539 2.4598 0.0337  -0.1136 -0.1065 93  ALA F O   
15122 C CB  . ALA F 93  ? 2.4180 2.5065 2.5723 0.0378  -0.1032 -0.0943 93  ALA F CB  
15123 N N   . ARG F 94  ? 2.2923 2.3664 2.4861 0.0372  -0.0968 -0.0960 94  ARG F N   
15124 C CA  . ARG F 94  ? 2.2140 2.2803 2.4238 0.0333  -0.1032 -0.0988 94  ARG F CA  
15125 C C   . ARG F 94  ? 2.1269 2.1717 2.3219 0.0352  -0.1069 -0.1113 94  ARG F C   
15126 O O   . ARG F 94  ? 2.0612 2.0977 2.2645 0.0309  -0.1157 -0.1161 94  ARG F O   
15127 C CB  . ARG F 94  ? 2.1957 2.2679 2.4276 0.0336  -0.0958 -0.0908 94  ARG F CB  
15128 C CG  . ARG F 94  ? 2.1351 2.1990 2.3604 0.0403  -0.0853 -0.0931 94  ARG F CG  
15129 C CD  . ARG F 94  ? 2.0904 2.1487 2.3353 0.0399  -0.0836 -0.0912 94  ARG F CD  
15130 N NE  . ARG F 94  ? 2.1335 2.2081 2.4009 0.0370  -0.0810 -0.0789 94  ARG F NE  
15131 C CZ  . ARG F 94  ? 2.1994 2.2722 2.4862 0.0356  -0.0799 -0.0744 94  ARG F CZ  
15132 N NH1 . ARG F 94  ? 2.1409 2.1961 2.4284 0.0369  -0.0812 -0.0814 94  ARG F NH1 
15133 N NH2 . ARG F 94  ? 2.2769 2.3650 2.5819 0.0331  -0.0775 -0.0630 94  ARG F NH2 
15134 N N   . ASP F 95  ? 2.1605 2.1965 2.3342 0.0413  -0.1001 -0.1170 95  ASP F N   
15135 C CA  . ASP F 95  ? 2.1605 2.1759 2.3187 0.0436  -0.1029 -0.1295 95  ASP F CA  
15136 C C   . ASP F 95  ? 2.2282 2.2362 2.3699 0.0407  -0.1149 -0.1375 95  ASP F C   
15137 O O   . ASP F 95  ? 2.1629 2.1554 2.3002 0.0395  -0.1221 -0.1473 95  ASP F O   
15138 C CB  . ASP F 95  ? 2.1493 2.1586 2.2894 0.0510  -0.0912 -0.1330 95  ASP F CB  
15139 C CG  . ASP F 95  ? 2.2072 2.2281 2.3335 0.0534  -0.0854 -0.1278 95  ASP F CG  
15140 O OD1 . ASP F 95  ? 2.2688 2.3018 2.3988 0.0495  -0.0908 -0.1219 95  ASP F OD1 
15141 O OD2 . ASP F 95  ? 2.1156 2.1335 2.2278 0.0591  -0.0752 -0.1297 95  ASP F OD2 
15142 N N   . LYS F 96  ? 2.4065 2.4248 2.5391 0.0397  -0.1176 -0.1337 96  LYS F N   
15143 C CA  . LYS F 96  ? 2.4164 2.4290 2.5336 0.0373  -0.1296 -0.1403 96  LYS F CA  
15144 C C   . LYS F 96  ? 2.3595 2.3793 2.4965 0.0302  -0.1416 -0.1379 96  LYS F C   
15145 O O   . LYS F 96  ? 2.3712 2.3867 2.4985 0.0277  -0.1529 -0.1436 96  LYS F O   
15146 C CB  . LYS F 96  ? 2.4872 2.5065 2.5842 0.0399  -0.1270 -0.1373 96  LYS F CB  
15147 C CG  . LYS F 96  ? 2.4691 2.4808 2.5434 0.0466  -0.1156 -0.1405 96  LYS F CG  
15148 C CD  . LYS F 96  ? 2.4827 2.4734 2.5357 0.0489  -0.1191 -0.1537 96  LYS F CD  
15149 C CE  . LYS F 96  ? 2.5363 2.5208 2.5708 0.0468  -0.1320 -0.1596 96  LYS F CE  
15150 N NZ  . LYS F 96  ? 2.6020 2.5657 2.6135 0.0491  -0.1356 -0.1729 96  LYS F NZ  
15151 N N   . LEU F 97  ? 2.1279 2.1587 2.2925 0.0268  -0.1393 -0.1297 97  LEU F N   
15152 C CA  . LEU F 97  ? 2.0649 2.1041 2.2502 0.0198  -0.1494 -0.1268 97  LEU F CA  
15153 C C   . LEU F 97  ? 1.9442 1.9728 2.1449 0.0158  -0.1549 -0.1318 97  LEU F C   
15154 O O   . LEU F 97  ? 1.9294 1.9601 2.1422 0.0098  -0.1657 -0.1333 97  LEU F O   
15155 C CB  . LEU F 97  ? 2.0576 2.1177 2.2638 0.0177  -0.1438 -0.1136 97  LEU F CB  
15156 C CG  . LEU F 97  ? 2.0687 2.1426 2.2657 0.0195  -0.1416 -0.1076 97  LEU F CG  
15157 C CD1 . LEU F 97  ? 2.0948 2.1881 2.3131 0.0178  -0.1350 -0.0953 97  LEU F CD1 
15158 C CD2 . LEU F 97  ? 2.0882 2.1631 2.2783 0.0164  -0.1543 -0.1117 97  LEU F CD2 
15159 N N   . LEU F 98  ? 1.9384 1.9557 2.1398 0.0189  -0.1479 -0.1345 98  LEU F N   
15160 C CA  . LEU F 98  ? 1.8582 1.8639 2.0744 0.0154  -0.1524 -0.1390 98  LEU F CA  
15161 C C   . LEU F 98  ? 1.9161 1.9016 2.1124 0.0167  -0.1597 -0.1534 98  LEU F C   
15162 O O   . LEU F 98  ? 1.8846 1.8579 2.0628 0.0227  -0.1534 -0.1596 98  LEU F O   
15163 C CB  . LEU F 98  ? 1.7834 1.7873 2.0121 0.0182  -0.1414 -0.1340 98  LEU F CB  
15164 C CG  . LEU F 98  ? 1.7331 1.7566 1.9808 0.0173  -0.1338 -0.1198 98  LEU F CG  
15165 C CD1 . LEU F 98  ? 1.5160 1.5359 1.7776 0.0197  -0.1248 -0.1154 98  LEU F CD1 
15166 C CD2 . LEU F 98  ? 1.8286 1.8650 2.0960 0.0095  -0.1418 -0.1140 98  LEU F CD2 
15167 N N   . ASP F 99  ? 1.9726 1.9547 2.1725 0.0110  -0.1729 -0.1591 99  ASP F N   
15168 C CA  . ASP F 99  ? 2.0012 1.9640 2.1839 0.0114  -0.1815 -0.1732 99  ASP F CA  
15169 C C   . ASP F 99  ? 1.9943 1.9429 2.1913 0.0088  -0.1838 -0.1788 99  ASP F C   
15170 O O   . ASP F 99  ? 2.0488 1.9792 2.2310 0.0102  -0.1887 -0.1912 99  ASP F O   
15171 C CB  . ASP F 99  ? 2.0572 2.0232 2.2353 0.0069  -0.1957 -0.1773 99  ASP F CB  
15172 C CG  . ASP F 99  ? 2.0598 2.0383 2.2676 -0.0011 -0.2028 -0.1712 99  ASP F CG  
15173 O OD1 . ASP F 99  ? 2.0589 2.0500 2.2875 -0.0027 -0.1952 -0.1602 99  ASP F OD1 
15174 O OD2 . ASP F 99  ? 2.0497 2.0256 2.2599 -0.0060 -0.2160 -0.1776 99  ASP F OD2 
15175 N N   . GLY F 100 ? 1.9018 1.8577 2.1265 0.0050  -0.1805 -0.1701 100 GLY F N   
15176 C CA  . GLY F 100 ? 1.8842 1.8273 2.1250 0.0019  -0.1823 -0.1738 100 GLY F CA  
15177 C C   . GLY F 100 ? 1.8738 1.8222 2.1388 -0.0074 -0.1927 -0.1718 100 GLY F C   
15178 O O   . GLY F 100 ? 1.8514 1.7957 2.1377 -0.0111 -0.1917 -0.1690 100 GLY F O   
15179 N N   . SER F 101 ? 1.9637 1.9210 2.2263 -0.0113 -0.2025 -0.1730 101 SER F N   
15180 C CA  . SER F 101 ? 1.9483 1.9119 2.2344 -0.0203 -0.2126 -0.1716 101 SER F CA  
15181 C C   . SER F 101 ? 2.0352 2.0185 2.3467 -0.0242 -0.2067 -0.1569 101 SER F C   
15182 O O   . SER F 101 ? 2.0137 2.0019 2.3487 -0.0319 -0.2124 -0.1542 101 SER F O   
15183 C CB  . SER F 101 ? 1.8993 1.8668 2.1749 -0.0226 -0.2253 -0.1779 101 SER F CB  
15184 O OG  . SER F 101 ? 1.8529 1.8285 2.1528 -0.0314 -0.2348 -0.1764 101 SER F OG  
15185 N N   . GLY F 102 ? 2.1660 2.1607 2.4735 -0.0192 -0.1954 -0.1474 102 GLY F N   
15186 C CA  . GLY F 102 ? 2.2119 2.2254 2.5413 -0.0223 -0.1893 -0.1335 102 GLY F CA  
15187 C C   . GLY F 102 ? 2.3727 2.4038 2.7129 -0.0280 -0.1968 -0.1296 102 GLY F C   
15188 O O   . GLY F 102 ? 2.4186 2.4601 2.7836 -0.0346 -0.1978 -0.1225 102 GLY F O   
15189 N N   . GLU F 103 ? 2.4547 2.4894 2.7764 -0.0254 -0.2020 -0.1340 103 GLU F N   
15190 C CA  . GLU F 103 ? 2.4430 2.4944 2.7736 -0.0298 -0.2094 -0.1308 103 GLU F CA  
15191 C C   . GLU F 103 ? 2.4225 2.4920 2.7505 -0.0263 -0.2009 -0.1204 103 GLU F C   
15192 O O   . GLU F 103 ? 2.4393 2.5060 2.7488 -0.0193 -0.1927 -0.1193 103 GLU F O   
15193 C CB  . GLU F 103 ? 2.4255 2.4696 2.7386 -0.0296 -0.2221 -0.1422 103 GLU F CB  
15194 C CG  . GLU F 103 ? 2.4072 2.4379 2.7282 -0.0352 -0.2334 -0.1523 103 GLU F CG  
15195 C CD  . GLU F 103 ? 2.3905 2.4343 2.7393 -0.0440 -0.2413 -0.1491 103 GLU F CD  
15196 O OE1 . GLU F 103 ? 2.3700 2.4335 2.7295 -0.0453 -0.2391 -0.1400 103 GLU F OE1 
15197 O OE2 . GLU F 103 ? 2.3792 2.4138 2.7398 -0.0497 -0.2494 -0.1557 103 GLU F OE2 
15198 N N   . PRO F 104 ? 2.2831 2.3714 2.6297 -0.0310 -0.2027 -0.1127 104 PRO F N   
15199 C CA  . PRO F 104 ? 2.1592 2.2651 2.5043 -0.0279 -0.1950 -0.1030 104 PRO F CA  
15200 C C   . PRO F 104 ? 2.0945 2.2001 2.4144 -0.0225 -0.1980 -0.1073 104 PRO F C   
15201 O O   . PRO F 104 ? 2.1260 2.2261 2.4370 -0.0236 -0.2093 -0.1156 104 PRO F O   
15202 C CB  . PRO F 104 ? 2.1225 2.2468 2.4935 -0.0349 -0.1985 -0.0963 104 PRO F CB  
15203 C CG  . PRO F 104 ? 2.1822 2.2991 2.5621 -0.0410 -0.2112 -0.1049 104 PRO F CG  
15204 C CD  . PRO F 104 ? 2.2712 2.3661 2.6425 -0.0396 -0.2111 -0.1125 104 PRO F CD  
15205 N N   . PHE F 105 ? 2.0558 2.1673 2.3644 -0.0169 -0.1879 -0.1013 105 PHE F N   
15206 C CA  . PHE F 105 ? 1.9960 2.1081 2.2810 -0.0117 -0.1888 -0.1035 105 PHE F CA  
15207 C C   . PHE F 105 ? 1.9188 2.0516 2.2116 -0.0120 -0.1862 -0.0942 105 PHE F C   
15208 O O   . PHE F 105 ? 1.9191 2.0654 2.2324 -0.0146 -0.1803 -0.0852 105 PHE F O   
15209 C CB  . PHE F 105 ? 2.0121 2.1126 2.2746 -0.0045 -0.1792 -0.1052 105 PHE F CB  
15210 C CG  . PHE F 105 ? 1.9985 2.1055 2.2710 -0.0025 -0.1658 -0.0962 105 PHE F CG  
15211 C CD1 . PHE F 105 ? 2.0959 2.1940 2.3790 -0.0033 -0.1617 -0.0965 105 PHE F CD1 
15212 C CD2 . PHE F 105 ? 1.9834 2.1048 2.2545 0.0004  -0.1577 -0.0876 105 PHE F CD2 
15213 C CE1 . PHE F 105 ? 2.1282 2.2322 2.4203 -0.0012 -0.1500 -0.0881 105 PHE F CE1 
15214 C CE2 . PHE F 105 ? 2.0257 2.1532 2.3058 0.0023  -0.1461 -0.0795 105 PHE F CE2 
15215 C CZ  . PHE F 105 ? 2.0601 2.1790 2.3506 0.0017  -0.1423 -0.0796 105 PHE F CZ  
15216 N N   . PHE F 106 ? 1.9020 2.0366 2.1778 -0.0091 -0.1907 -0.0965 106 PHE F N   
15217 C CA  . PHE F 106 ? 1.9082 2.0609 2.1887 -0.0087 -0.1893 -0.0890 106 PHE F CA  
15218 C C   . PHE F 106 ? 1.9525 2.1071 2.2171 -0.0026 -0.1779 -0.0839 106 PHE F C   
15219 O O   . PHE F 106 ? 1.9993 2.1402 2.2418 0.0022  -0.1745 -0.0886 106 PHE F O   
15220 C CB  . PHE F 106 ? 1.9118 2.0657 2.1843 -0.0093 -0.2019 -0.0941 106 PHE F CB  
15221 C CG  . PHE F 106 ? 1.8765 2.0346 2.1694 -0.0158 -0.2133 -0.0974 106 PHE F CG  
15222 C CD1 . PHE F 106 ? 1.8418 2.0191 2.1580 -0.0199 -0.2145 -0.0909 106 PHE F CD1 
15223 C CD2 . PHE F 106 ? 1.9039 2.0471 2.1928 -0.0180 -0.2228 -0.1073 106 PHE F CD2 
15224 C CE1 . PHE F 106 ? 1.8102 1.9923 2.1462 -0.0262 -0.2245 -0.0940 106 PHE F CE1 
15225 C CE2 . PHE F 106 ? 1.8904 2.0379 2.1991 -0.0243 -0.2334 -0.1104 106 PHE F CE2 
15226 C CZ  . PHE F 106 ? 1.8172 1.9845 2.1499 -0.0285 -0.2341 -0.1037 106 PHE F CZ  
15227 N N   . VAL F 107 ? 1.9991 2.1712 2.2756 -0.0028 -0.1717 -0.0746 107 VAL F N   
15228 C CA  . VAL F 107 ? 1.9920 2.1687 2.2561 0.0024  -0.1615 -0.0691 107 VAL F CA  
15229 C C   . VAL F 107 ? 1.9695 2.1610 2.2355 0.0022  -0.1646 -0.0649 107 VAL F C   
15230 O O   . VAL F 107 ? 2.0137 2.2208 2.3012 -0.0016 -0.1652 -0.0593 107 VAL F O   
15231 C CB  . VAL F 107 ? 2.0262 2.2095 2.3030 0.0028  -0.1492 -0.0614 107 VAL F CB  
15232 C CG1 . VAL F 107 ? 2.0205 2.2084 2.2843 0.0082  -0.1392 -0.0565 107 VAL F CG1 
15233 C CG2 . VAL F 107 ? 2.0615 2.2299 2.3384 0.0030  -0.1467 -0.0656 107 VAL F CG2 
15234 N N   . LEU F 108 ? 1.7773 1.9637 2.0209 0.0063  -0.1665 -0.0675 108 LEU F N   
15235 C CA  . LEU F 108 ? 1.6754 1.8730 1.9182 0.0067  -0.1708 -0.0646 108 LEU F CA  
15236 C C   . LEU F 108 ? 1.6284 1.8297 1.8578 0.0114  -0.1609 -0.0592 108 LEU F C   
15237 O O   . LEU F 108 ? 1.6670 1.8580 1.8798 0.0152  -0.1535 -0.0605 108 LEU F O   
15238 C CB  . LEU F 108 ? 1.7033 1.8914 1.9312 0.0071  -0.1839 -0.0724 108 LEU F CB  
15239 C CG  . LEU F 108 ? 1.7662 1.9492 2.0050 0.0025  -0.1953 -0.0792 108 LEU F CG  
15240 C CD1 . LEU F 108 ? 1.7334 1.9065 1.9543 0.0038  -0.2081 -0.0869 108 LEU F CD1 
15241 C CD2 . LEU F 108 ? 1.7382 1.9385 2.0074 -0.0029 -0.1978 -0.0746 108 LEU F CD2 
15242 N N   . ASN F 109 ? 1.6174 1.8338 1.8550 0.0111  -0.1607 -0.0534 109 ASN F N   
15243 C CA  . ASN F 109 ? 1.6253 1.8464 1.8517 0.0150  -0.1526 -0.0483 109 ASN F CA  
15244 C C   . ASN F 109 ? 1.6697 1.8864 1.8780 0.0174  -0.1604 -0.0511 109 ASN F C   
15245 O O   . ASN F 109 ? 1.6216 1.8421 1.8366 0.0153  -0.1713 -0.0533 109 ASN F O   
15246 C CB  . ASN F 109 ? 1.5703 1.8111 1.8177 0.0134  -0.1465 -0.0398 109 ASN F CB  
15247 C CG  . ASN F 109 ? 1.5201 1.7652 1.7579 0.0172  -0.1360 -0.0343 109 ASN F CG  
15248 O OD1 . ASN F 109 ? 1.5759 1.8122 1.7920 0.0207  -0.1354 -0.0363 109 ASN F OD1 
15249 N ND2 . ASN F 109 ? 1.4281 1.6870 1.6822 0.0162  -0.1278 -0.0274 109 ASN F ND2 
15250 N N   . SER F 110 ? 1.9744 2.1832 2.1602 0.0217  -0.1546 -0.0508 110 SER F N   
15251 C CA  . SER F 110 ? 1.9834 2.1859 2.1492 0.0243  -0.1613 -0.0529 110 SER F CA  
15252 C C   . SER F 110 ? 1.9483 2.1656 2.1232 0.0242  -0.1624 -0.0470 110 SER F C   
15253 O O   . SER F 110 ? 1.9532 2.1672 2.1164 0.0258  -0.1704 -0.0484 110 SER F O   
15254 C CB  . SER F 110 ? 2.0178 2.2069 2.1564 0.0286  -0.1538 -0.0541 110 SER F CB  
15255 O OG  . SER F 110 ? 2.0248 2.2065 2.1424 0.0310  -0.1603 -0.0557 110 SER F OG  
15256 N N   . ASP F 111 ? 1.6825 1.9156 1.8774 0.0227  -0.1549 -0.0404 111 ASP F N   
15257 C CA  . ASP F 111 ? 1.6308 1.8782 1.8346 0.0229  -0.1546 -0.0349 111 ASP F CA  
15258 C C   . ASP F 111 ? 1.6796 1.9399 1.9065 0.0193  -0.1633 -0.0349 111 ASP F C   
15259 O O   . ASP F 111 ? 1.7582 2.0333 1.9984 0.0188  -0.1615 -0.0300 111 ASP F O   
15260 C CB  . ASP F 111 ? 1.6054 1.8632 1.8168 0.0235  -0.1413 -0.0280 111 ASP F CB  
15261 C CG  . ASP F 111 ? 1.5633 1.8099 1.7545 0.0269  -0.1319 -0.0280 111 ASP F CG  
15262 O OD1 . ASP F 111 ? 1.5948 1.8253 1.7667 0.0285  -0.1349 -0.0336 111 ASP F OD1 
15263 O OD2 . ASP F 111 ? 1.4847 1.7389 1.6795 0.0279  -0.1214 -0.0227 111 ASP F OD2 
15264 N N   . VAL F 112 ? 1.6845 1.9398 1.9169 0.0167  -0.1724 -0.0404 112 VAL F N   
15265 C CA  . VAL F 112 ? 1.7309 1.9986 1.9871 0.0127  -0.1803 -0.0408 112 VAL F CA  
15266 C C   . VAL F 112 ? 1.7667 2.0258 2.0157 0.0126  -0.1947 -0.0479 112 VAL F C   
15267 O O   . VAL F 112 ? 1.7637 2.0062 1.9943 0.0139  -0.1984 -0.0535 112 VAL F O   
15268 C CB  . VAL F 112 ? 1.7277 2.0008 2.0046 0.0083  -0.1763 -0.0399 112 VAL F CB  
15269 C CG1 . VAL F 112 ? 1.8828 2.1711 2.1858 0.0039  -0.1826 -0.0392 112 VAL F CG1 
15270 C CG2 . VAL F 112 ? 1.6990 1.9781 1.9799 0.0090  -0.1622 -0.0333 112 VAL F CG2 
15271 N N   . ILE F 113 ? 1.8732 2.1437 2.1367 0.0113  -0.2031 -0.0478 113 ILE F N   
15272 C CA  . ILE F 113 ? 1.9180 2.1834 2.1798 0.0107  -0.2179 -0.0543 113 ILE F CA  
15273 C C   . ILE F 113 ? 1.9218 2.2016 2.2135 0.0056  -0.2233 -0.0550 113 ILE F C   
15274 O O   . ILE F 113 ? 1.9571 2.2534 2.2692 0.0036  -0.2169 -0.0495 113 ILE F O   
15275 C CB  . ILE F 113 ? 1.9631 2.2271 2.2110 0.0149  -0.2246 -0.0541 113 ILE F CB  
15276 C CG1 . ILE F 113 ? 1.9299 2.2116 2.1929 0.0154  -0.2194 -0.0475 113 ILE F CG1 
15277 C CG2 . ILE F 113 ? 2.0188 2.2655 2.2347 0.0194  -0.2212 -0.0547 113 ILE F CG2 
15278 C CD1 . ILE F 113 ? 1.9400 2.2216 2.1933 0.0193  -0.2267 -0.0472 113 ILE F CD1 
15279 N N   . SER F 114 ? 1.7782 2.0519 2.0723 0.0034  -0.2350 -0.0618 114 SER F N   
15280 C CA  . SER F 114 ? 1.7583 2.0443 2.0806 -0.0019 -0.2412 -0.0635 114 SER F CA  
15281 C C   . SER F 114 ? 1.7250 2.0010 2.0423 -0.0027 -0.2565 -0.0722 114 SER F C   
15282 O O   . SER F 114 ? 1.7431 2.0041 2.0350 0.0012  -0.2622 -0.0761 114 SER F O   
15283 C CB  . SER F 114 ? 1.8079 2.0978 2.1468 -0.0066 -0.2320 -0.0609 114 SER F CB  
15284 O OG  . SER F 114 ? 1.8345 2.1071 2.1603 -0.0071 -0.2324 -0.0657 114 SER F OG  
15285 N N   . GLU F 115 ? 1.6362 1.9208 1.9778 -0.0080 -0.2631 -0.0750 115 GLU F N   
15286 C CA  . GLU F 115 ? 1.6166 1.8932 1.9572 -0.0096 -0.2780 -0.0836 115 GLU F CA  
15287 C C   . GLU F 115 ? 1.6525 1.9130 1.9849 -0.0120 -0.2781 -0.0889 115 GLU F C   
15288 O O   . GLU F 115 ? 1.6703 1.9194 1.9935 -0.0122 -0.2902 -0.0968 115 GLU F O   
15289 C CB  . GLU F 115 ? 1.6183 1.9123 1.9903 -0.0144 -0.2855 -0.0847 115 GLU F CB  
15290 C CG  . GLU F 115 ? 1.6684 1.9803 2.0525 -0.0123 -0.2845 -0.0796 115 GLU F CG  
15291 C CD  . GLU F 115 ? 1.6950 2.0228 2.1075 -0.0162 -0.2941 -0.0823 115 GLU F CD  
15292 O OE1 . GLU F 115 ? 1.6968 2.0255 2.1256 -0.0220 -0.2979 -0.0860 115 GLU F OE1 
15293 O OE2 . GLU F 115 ? 1.6657 2.0051 2.0850 -0.0136 -0.2978 -0.0807 115 GLU F OE2 
15294 N N   . TYR F 116 ? 1.6526 1.9116 1.9880 -0.0137 -0.2654 -0.0849 116 TYR F N   
15295 C CA  . TYR F 116 ? 1.6696 1.9131 1.9974 -0.0154 -0.2634 -0.0891 116 TYR F CA  
15296 C C   . TYR F 116 ? 1.6693 1.9102 2.0119 -0.0209 -0.2748 -0.0965 116 TYR F C   
15297 O O   . TYR F 116 ? 1.6889 1.9155 2.0159 -0.0198 -0.2853 -0.1046 116 TYR F O   
15298 C CB  . TYR F 116 ? 1.7147 1.9387 2.0079 -0.0097 -0.2632 -0.0927 116 TYR F CB  
15299 C CG  . TYR F 116 ? 1.7577 1.9833 2.0369 -0.0048 -0.2507 -0.0855 116 TYR F CG  
15300 C CD1 . TYR F 116 ? 1.7658 1.9905 2.0460 -0.0049 -0.2368 -0.0808 116 TYR F CD1 
15301 C CD2 . TYR F 116 ? 1.7591 1.9873 2.0252 -0.0003 -0.2529 -0.0833 116 TYR F CD2 
15302 C CE1 . TYR F 116 ? 1.7207 1.9475 1.9893 -0.0007 -0.2256 -0.0745 116 TYR F CE1 
15303 C CE2 . TYR F 116 ? 1.7294 1.9591 1.9836 0.0037  -0.2415 -0.0768 116 TYR F CE2 
15304 C CZ  . TYR F 116 ? 1.7177 1.9470 1.9735 0.0034  -0.2278 -0.0726 116 TYR F CZ  
15305 O OH  . TYR F 116 ? 1.6957 1.9270 1.9407 0.0071  -0.2167 -0.0665 116 TYR F OH  
15306 N N   . PRO F 117 ? 1.6519 1.9063 2.0243 -0.0270 -0.2731 -0.0939 117 PRO F N   
15307 C CA  . PRO F 117 ? 1.7080 1.9594 2.0963 -0.0331 -0.2824 -0.1005 117 PRO F CA  
15308 C C   . PRO F 117 ? 1.7826 2.0207 2.1689 -0.0356 -0.2757 -0.1017 117 PRO F C   
15309 O O   . PRO F 117 ? 1.8409 2.0855 2.2498 -0.0412 -0.2706 -0.0985 117 PRO F O   
15310 C CB  . PRO F 117 ? 1.7030 1.9767 2.1244 -0.0383 -0.2823 -0.0960 117 PRO F CB  
15311 C CG  . PRO F 117 ? 1.7453 2.0295 2.1694 -0.0365 -0.2673 -0.0859 117 PRO F CG  
15312 C CD  . PRO F 117 ? 1.6581 1.9324 2.0518 -0.0288 -0.2635 -0.0848 117 PRO F CD  
15313 N N   . LEU F 118 ? 1.8523 2.0711 2.2107 -0.0312 -0.2754 -0.1062 118 LEU F N   
15314 C CA  . LEU F 118 ? 1.9392 2.1443 2.2932 -0.0322 -0.2681 -0.1074 118 LEU F CA  
15315 C C   . LEU F 118 ? 2.1037 2.3019 2.4717 -0.0385 -0.2769 -0.1147 118 LEU F C   
15316 O O   . LEU F 118 ? 2.0785 2.2714 2.4556 -0.0417 -0.2705 -0.1137 118 LEU F O   
15317 C CB  . LEU F 118 ? 1.9672 2.1540 2.2872 -0.0256 -0.2652 -0.1108 118 LEU F CB  
15318 C CG  . LEU F 118 ? 1.8553 2.0468 2.1596 -0.0195 -0.2557 -0.1038 118 LEU F CG  
15319 C CD1 . LEU F 118 ? 1.9364 2.1092 2.2075 -0.0135 -0.2535 -0.1082 118 LEU F CD1 
15320 C CD2 . LEU F 118 ? 1.7528 1.9561 2.0727 -0.0205 -0.2412 -0.0940 118 LEU F CD2 
15321 N N   . LYS F 119 ? 2.2472 2.4453 2.6177 -0.0402 -0.2918 -0.1221 119 LYS F N   
15322 C CA  . LYS F 119 ? 2.2940 2.4848 2.6772 -0.0463 -0.3012 -0.1300 119 LYS F CA  
15323 C C   . LYS F 119 ? 2.2649 2.4697 2.6827 -0.0540 -0.2970 -0.1248 119 LYS F C   
15324 O O   . LYS F 119 ? 2.2039 2.4004 2.6305 -0.0582 -0.2938 -0.1260 119 LYS F O   
15325 C CB  . LYS F 119 ? 2.3646 2.5548 2.7447 -0.0465 -0.3185 -0.1385 119 LYS F CB  
15326 C CG  . LYS F 119 ? 2.4424 2.6162 2.7871 -0.0395 -0.3243 -0.1447 119 LYS F CG  
15327 C CD  . LYS F 119 ? 2.4870 2.6504 2.8276 -0.0416 -0.3413 -0.1564 119 LYS F CD  
15328 C CE  . LYS F 119 ? 2.5473 2.6995 2.8980 -0.0472 -0.3416 -0.1620 119 LYS F CE  
15329 N NZ  . LYS F 119 ? 2.6680 2.8038 2.9987 -0.0438 -0.3299 -0.1617 119 LYS F NZ  
15330 N N   . GLU F 120 ? 2.6070 2.8327 3.0446 -0.0559 -0.2967 -0.1189 120 GLU F N   
15331 C CA  . GLU F 120 ? 2.5790 2.8197 3.0497 -0.0635 -0.2928 -0.1138 120 GLU F CA  
15332 C C   . GLU F 120 ? 2.5686 2.8135 3.0444 -0.0636 -0.2762 -0.1036 120 GLU F C   
15333 O O   . GLU F 120 ? 2.5401 2.7992 3.0418 -0.0693 -0.2711 -0.0974 120 GLU F O   
15334 C CB  . GLU F 120 ? 2.6382 2.9002 3.1278 -0.0652 -0.2987 -0.1120 120 GLU F CB  
15335 C CG  . GLU F 120 ? 2.6747 2.9339 3.1629 -0.0656 -0.3163 -0.1220 120 GLU F CG  
15336 C CD  . GLU F 120 ? 2.7490 3.0296 3.2575 -0.0669 -0.3224 -0.1205 120 GLU F CD  
15337 O OE1 . GLU F 120 ? 2.7890 3.0865 3.3117 -0.0674 -0.3125 -0.1118 120 GLU F OE1 
15338 O OE2 . GLU F 120 ? 2.7378 3.0183 3.2479 -0.0672 -0.3372 -0.1283 120 GLU F OE2 
15339 N N   . MET F 121 ? 2.1584 2.3915 2.6102 -0.0575 -0.2677 -0.1016 121 MET F N   
15340 C CA  . MET F 121 ? 2.0057 2.2402 2.4609 -0.0573 -0.2528 -0.0928 121 MET F CA  
15341 C C   . MET F 121 ? 1.9953 2.2129 2.4507 -0.0600 -0.2505 -0.0958 121 MET F C   
15342 O O   . MET F 121 ? 1.9377 2.1587 2.4079 -0.0633 -0.2411 -0.0888 121 MET F O   
15343 C CB  . MET F 121 ? 1.9296 2.1620 2.3608 -0.0492 -0.2441 -0.0886 121 MET F CB  
15344 C CG  . MET F 121 ? 1.8501 2.0886 2.2868 -0.0485 -0.2289 -0.0784 121 MET F CG  
15345 S SD  . MET F 121 ? 1.6633 1.8984 2.0718 -0.0393 -0.2192 -0.0745 121 MET F SD  
15346 C CE  . MET F 121 ? 1.6800 1.9241 2.0799 -0.0361 -0.2286 -0.0771 121 MET F CE  
15347 N N   . LEU F 122 ? 1.9938 2.1927 2.4327 -0.0586 -0.2589 -0.1059 122 LEU F N   
15348 C CA  . LEU F 122 ? 1.9501 2.1324 2.3907 -0.0615 -0.2582 -0.1100 122 LEU F CA  
15349 C C   . LEU F 122 ? 1.9685 2.1573 2.4399 -0.0708 -0.2622 -0.1097 122 LEU F C   
15350 O O   . LEU F 122 ? 1.9504 2.1341 2.4335 -0.0745 -0.2557 -0.1063 122 LEU F O   
15351 C CB  . LEU F 122 ? 1.9107 2.0724 2.3274 -0.0582 -0.2677 -0.1220 122 LEU F CB  
15352 C CG  . LEU F 122 ? 1.8924 2.0400 2.2775 -0.0498 -0.2614 -0.1236 122 LEU F CG  
15353 C CD1 . LEU F 122 ? 1.9415 2.0986 2.3110 -0.0438 -0.2598 -0.1199 122 LEU F CD1 
15354 C CD2 . LEU F 122 ? 1.9013 2.0272 2.2673 -0.0484 -0.2705 -0.1361 122 LEU F CD2 
15355 N N   . GLU F 123 ? 2.0017 2.2017 2.4870 -0.0748 -0.2730 -0.1131 123 GLU F N   
15356 C CA  . GLU F 123 ? 1.9703 2.1796 2.4871 -0.0841 -0.2761 -0.1120 123 GLU F CA  
15357 C C   . GLU F 123 ? 1.9297 2.1560 2.4661 -0.0870 -0.2634 -0.0994 123 GLU F C   
15358 O O   . GLU F 123 ? 1.9338 2.1618 2.4920 -0.0941 -0.2602 -0.0960 123 GLU F O   
15359 C CB  . GLU F 123 ? 2.0005 2.2202 2.5281 -0.0871 -0.2901 -0.1182 123 GLU F CB  
15360 C CG  . GLU F 123 ? 1.9884 2.2154 2.5478 -0.0971 -0.2954 -0.1195 123 GLU F CG  
15361 C CD  . GLU F 123 ? 2.0055 2.2424 2.5754 -0.0995 -0.3101 -0.1266 123 GLU F CD  
15362 O OE1 . GLU F 123 ? 1.9997 2.2432 2.5566 -0.0936 -0.3141 -0.1274 123 GLU F OE1 
15363 O OE2 . GLU F 123 ? 2.0740 2.3118 2.6653 -0.1074 -0.3178 -0.1314 123 GLU F OE2 
15364 N N   . PHE F 124 ? 1.9328 2.1712 2.4614 -0.0816 -0.2560 -0.0924 124 PHE F N   
15365 C CA  . PHE F 124 ? 1.8831 2.1359 2.4260 -0.0833 -0.2430 -0.0804 124 PHE F CA  
15366 C C   . PHE F 124 ? 1.8844 2.1243 2.4199 -0.0817 -0.2321 -0.0757 124 PHE F C   
15367 O O   . PHE F 124 ? 1.8680 2.1168 2.4175 -0.0844 -0.2219 -0.0661 124 PHE F O   
15368 C CB  . PHE F 124 ? 1.8374 2.1054 2.3724 -0.0776 -0.2386 -0.0750 124 PHE F CB  
15369 C CG  . PHE F 124 ? 1.7814 2.0667 2.3321 -0.0795 -0.2265 -0.0633 124 PHE F CG  
15370 C CD1 . PHE F 124 ? 1.7563 2.0567 2.3355 -0.0873 -0.2263 -0.0596 124 PHE F CD1 
15371 C CD2 . PHE F 124 ? 1.7709 2.0575 2.3077 -0.0736 -0.2152 -0.0562 124 PHE F CD2 
15372 C CE1 . PHE F 124 ? 1.7301 2.0463 2.3224 -0.0891 -0.2151 -0.0489 124 PHE F CE1 
15373 C CE2 . PHE F 124 ? 1.7108 2.0132 2.2611 -0.0753 -0.2046 -0.0458 124 PHE F CE2 
15374 C CZ  . PHE F 124 ? 1.6719 1.9888 2.2493 -0.0830 -0.2044 -0.0421 124 PHE F CZ  
15375 N N   . HIS F 125 ? 1.9232 2.1424 2.4371 -0.0773 -0.2340 -0.0824 125 HIS F N   
15376 C CA  . HIS F 125 ? 1.9477 2.1528 2.4547 -0.0755 -0.2249 -0.0795 125 HIS F CA  
15377 C C   . HIS F 125 ? 1.9152 2.1062 2.4343 -0.0817 -0.2290 -0.0841 125 HIS F C   
15378 O O   . HIS F 125 ? 1.8853 2.0726 2.4141 -0.0841 -0.2208 -0.0780 125 HIS F O   
15379 C CB  . HIS F 125 ? 2.0068 2.1974 2.4827 -0.0665 -0.2232 -0.0841 125 HIS F CB  
15380 C CG  . HIS F 125 ? 2.0324 2.2103 2.5007 -0.0634 -0.2129 -0.0807 125 HIS F CG  
15381 N ND1 . HIS F 125 ? 2.0017 2.1884 2.4719 -0.0608 -0.2004 -0.0700 125 HIS F ND1 
15382 C CD2 . HIS F 125 ? 2.0490 2.2061 2.5081 -0.0623 -0.2136 -0.0869 125 HIS F CD2 
15383 C CE1 . HIS F 125 ? 2.0286 2.2008 2.4916 -0.0581 -0.1939 -0.0695 125 HIS F CE1 
15384 N NE2 . HIS F 125 ? 2.0620 2.2160 2.5183 -0.0589 -0.2015 -0.0798 125 HIS F NE2 
15385 N N   . LYS F 126 ? 1.9401 2.1229 2.4588 -0.0845 -0.2419 -0.0950 126 LYS F N   
15386 C CA  . LYS F 126 ? 1.9466 2.1147 2.4758 -0.0904 -0.2472 -0.1009 126 LYS F CA  
15387 C C   . LYS F 126 ? 1.8927 2.0734 2.4543 -0.1006 -0.2497 -0.0974 126 LYS F C   
15388 O O   . LYS F 126 ? 1.8714 2.0424 2.4443 -0.1067 -0.2574 -0.1040 126 LYS F O   
15389 C CB  . LYS F 126 ? 1.9419 2.0945 2.4545 -0.0886 -0.2602 -0.1149 126 LYS F CB  
15390 C CG  . LYS F 126 ? 1.9329 2.0692 2.4133 -0.0793 -0.2573 -0.1193 126 LYS F CG  
15391 C CD  . LYS F 126 ? 1.8926 2.0124 2.3566 -0.0781 -0.2703 -0.1334 126 LYS F CD  
15392 C CE  . LYS F 126 ? 1.9036 2.0066 2.3355 -0.0692 -0.2663 -0.1379 126 LYS F CE  
15393 N NZ  . LYS F 126 ? 1.9814 2.0672 2.3959 -0.0680 -0.2786 -0.1519 126 LYS F NZ  
15394 N N   . SER F 127 ? 1.8622 2.0642 2.4390 -0.1026 -0.2432 -0.0874 127 SER F N   
15395 C CA  . SER F 127 ? 1.8701 2.0860 2.4778 -0.1122 -0.2439 -0.0831 127 SER F CA  
15396 C C   . SER F 127 ? 1.8579 2.0767 2.4794 -0.1157 -0.2312 -0.0713 127 SER F C   
15397 O O   . SER F 127 ? 1.8495 2.0634 2.4897 -0.1234 -0.2316 -0.0705 127 SER F O   
15398 C CB  . SER F 127 ? 1.8606 2.0999 2.4776 -0.1127 -0.2469 -0.0811 127 SER F CB  
15399 O OG  . SER F 127 ? 1.8420 2.0956 2.4896 -0.1221 -0.2475 -0.0776 127 SER F OG  
15400 N N   . HIS F 128 ? 1.8495 2.0764 2.4623 -0.1102 -0.2199 -0.0620 128 HIS F N   
15401 C CA  . HIS F 128 ? 1.8966 2.1262 2.5199 -0.1126 -0.2077 -0.0503 128 HIS F CA  
15402 C C   . HIS F 128 ? 1.9358 2.1454 2.5428 -0.1074 -0.2017 -0.0495 128 HIS F C   
15403 O O   . HIS F 128 ? 1.9319 2.1396 2.5481 -0.1097 -0.1931 -0.0408 128 HIS F O   
15404 C CB  . HIS F 128 ? 1.9110 2.1622 2.5362 -0.1100 -0.1988 -0.0401 128 HIS F CB  
15405 C CG  . HIS F 128 ? 1.8900 2.1425 2.4906 -0.1002 -0.1975 -0.0418 128 HIS F CG  
15406 N ND1 . HIS F 128 ? 1.9076 2.1422 2.4844 -0.0936 -0.2014 -0.0499 128 HIS F ND1 
15407 C CD2 . HIS F 128 ? 1.8557 2.1252 2.4519 -0.0961 -0.1926 -0.0364 128 HIS F CD2 
15408 C CE1 . HIS F 128 ? 1.8992 2.1397 2.4582 -0.0861 -0.1987 -0.0491 128 HIS F CE1 
15409 N NE2 . HIS F 128 ? 1.8903 2.1516 2.4608 -0.0875 -0.1936 -0.0410 128 HIS F NE2 
15410 N N   . GLY F 129 ? 1.9367 2.1315 2.5199 -0.1003 -0.2059 -0.0582 129 GLY F N   
15411 C CA  . GLY F 129 ? 1.9350 2.1108 2.5030 -0.0950 -0.2004 -0.0586 129 GLY F CA  
15412 C C   . GLY F 129 ? 1.9047 2.0859 2.4614 -0.0880 -0.1882 -0.0493 129 GLY F C   
15413 O O   . GLY F 129 ? 1.9149 2.0854 2.4697 -0.0861 -0.1810 -0.0450 129 GLY F O   
15414 N N   . GLY F 130 ? 1.8837 2.0812 2.4334 -0.0841 -0.1859 -0.0461 130 GLY F N   
15415 C CA  . GLY F 130 ? 1.9037 2.1071 2.4426 -0.0775 -0.1749 -0.0378 130 GLY F CA  
15416 C C   . GLY F 130 ? 1.9769 2.1631 2.4912 -0.0691 -0.1728 -0.0430 130 GLY F C   
15417 O O   . GLY F 130 ? 2.0114 2.1812 2.5146 -0.0678 -0.1799 -0.0535 130 GLY F O   
15418 N N   . GLU F 131 ? 1.9996 2.1902 2.5052 -0.0632 -0.1625 -0.0356 131 GLU F N   
15419 C CA  . GLU F 131 ? 1.9756 2.1526 2.4589 -0.0548 -0.1586 -0.0393 131 GLU F CA  
15420 C C   . GLU F 131 ? 2.0140 2.1982 2.4779 -0.0483 -0.1581 -0.0413 131 GLU F C   
15421 O O   . GLU F 131 ? 2.0482 2.2196 2.4920 -0.0432 -0.1609 -0.0497 131 GLU F O   
15422 C CB  . GLU F 131 ? 1.8734 2.0485 2.3596 -0.0521 -0.1475 -0.0301 131 GLU F CB  
15423 C CG  . GLU F 131 ? 1.8008 1.9619 2.2661 -0.0435 -0.1429 -0.0339 131 GLU F CG  
15424 C CD  . GLU F 131 ? 1.7151 1.8807 2.1820 -0.0395 -0.1315 -0.0237 131 GLU F CD  
15425 O OE1 . GLU F 131 ? 1.7207 1.9005 2.2033 -0.0433 -0.1273 -0.0135 131 GLU F OE1 
15426 O OE2 . GLU F 131 ? 1.7283 1.8837 2.1808 -0.0325 -0.1267 -0.0260 131 GLU F OE2 
15427 N N   . ALA F 132 ? 1.9870 2.1910 2.4563 -0.0485 -0.1544 -0.0339 132 ALA F N   
15428 C CA  . ALA F 132 ? 2.1092 2.3206 2.5614 -0.0425 -0.1531 -0.0346 132 ALA F CA  
15429 C C   . ALA F 132 ? 2.2592 2.4883 2.7208 -0.0461 -0.1584 -0.0335 132 ALA F C   
15430 O O   . ALA F 132 ? 2.1453 2.3869 2.6279 -0.0521 -0.1579 -0.0278 132 ALA F O   
15431 C CB  . ALA F 132 ? 1.9730 2.1908 2.4196 -0.0372 -0.1413 -0.0260 132 ALA F CB  
15432 N N   . SER F 133 ? 2.9712 3.2011 3.4169 -0.0422 -0.1633 -0.0390 133 SER F N   
15433 C CA  . SER F 133 ? 2.9403 3.1856 3.3932 -0.0446 -0.1694 -0.0393 133 SER F CA  
15434 C C   . SER F 133 ? 2.9293 3.1814 3.3652 -0.0381 -0.1665 -0.0380 133 SER F C   
15435 O O   . SER F 133 ? 2.9568 3.1966 3.3705 -0.0324 -0.1660 -0.0426 133 SER F O   
15436 C CB  . SER F 133 ? 2.9549 3.1924 3.4081 -0.0478 -0.1826 -0.0494 133 SER F CB  
15437 O OG  . SER F 133 ? 2.9242 3.1773 3.3863 -0.0500 -0.1887 -0.0496 133 SER F OG  
15438 N N   . ILE F 134 ? 3.1505 3.4217 3.5968 -0.0393 -0.1644 -0.0320 134 ILE F N   
15439 C CA  . ILE F 134 ? 3.1385 3.4177 3.5716 -0.0341 -0.1631 -0.0310 134 ILE F CA  
15440 C C   . ILE F 134 ? 3.1024 3.3949 3.5464 -0.0371 -0.1714 -0.0328 134 ILE F C   
15441 O O   . ILE F 134 ? 3.0839 3.3828 3.5480 -0.0433 -0.1760 -0.0330 134 ILE F O   
15442 C CB  . ILE F 134 ? 3.1027 3.3931 3.5366 -0.0313 -0.1511 -0.0215 134 ILE F CB  
15443 C CG1 . ILE F 134 ? 3.0594 3.3682 3.5174 -0.0367 -0.1479 -0.0140 134 ILE F CG1 
15444 C CG2 . ILE F 134 ? 3.1201 3.3983 3.5458 -0.0284 -0.1430 -0.0195 134 ILE F CG2 
15445 C CD1 . ILE F 134 ? 3.0151 3.3365 3.4739 -0.0341 -0.1372 -0.0049 134 ILE F CD1 
15446 N N   . MET F 135 ? 2.3967 2.6934 2.8275 -0.0325 -0.1733 -0.0340 135 MET F N   
15447 C CA  . MET F 135 ? 2.0448 2.3546 2.4844 -0.0339 -0.1807 -0.0353 135 MET F CA  
15448 C C   . MET F 135 ? 1.8964 2.2241 2.3416 -0.0323 -0.1730 -0.0275 135 MET F C   
15449 O O   . MET F 135 ? 1.9049 2.2316 2.3376 -0.0278 -0.1644 -0.0233 135 MET F O   
15450 C CB  . MET F 135 ? 1.8979 2.1980 2.3182 -0.0299 -0.1905 -0.0432 135 MET F CB  
15451 C CG  . MET F 135 ? 1.8421 2.1267 2.2587 -0.0321 -0.2007 -0.0522 135 MET F CG  
15452 S SD  . MET F 135 ? 1.8169 2.1112 2.2643 -0.0409 -0.2085 -0.0539 135 MET F SD  
15453 C CE  . MET F 135 ? 1.8876 2.1995 2.3425 -0.0401 -0.2160 -0.0543 135 MET F CE  
15454 N N   . VAL F 136 ? 1.7999 2.1443 2.2644 -0.0359 -0.1760 -0.0258 136 VAL F N   
15455 C CA  . VAL F 136 ? 1.6816 2.0445 2.1552 -0.0354 -0.1687 -0.0186 136 VAL F CA  
15456 C C   . VAL F 136 ? 1.7027 2.0770 2.1818 -0.0349 -0.1765 -0.0215 136 VAL F C   
15457 O O   . VAL F 136 ? 1.7964 2.1718 2.2862 -0.0383 -0.1862 -0.0267 136 VAL F O   
15458 C CB  . VAL F 136 ? 1.6207 1.9949 2.1166 -0.0412 -0.1617 -0.0119 136 VAL F CB  
15459 C CG1 . VAL F 136 ? 1.6021 1.9965 2.1083 -0.0410 -0.1554 -0.0054 136 VAL F CG1 
15460 C CG2 . VAL F 136 ? 1.7919 2.1551 2.2817 -0.0408 -0.1535 -0.0081 136 VAL F CG2 
15461 N N   . THR F 137 ? 1.7152 2.0982 2.1877 -0.0305 -0.1725 -0.0183 137 THR F N   
15462 C CA  . THR F 137 ? 1.7727 2.1669 2.2501 -0.0292 -0.1789 -0.0204 137 THR F CA  
15463 C C   . THR F 137 ? 1.8586 2.2723 2.3490 -0.0295 -0.1707 -0.0136 137 THR F C   
15464 O O   . THR F 137 ? 1.8103 2.2258 2.2957 -0.0280 -0.1603 -0.0077 137 THR F O   
15465 C CB  . THR F 137 ? 1.8683 2.2517 2.3218 -0.0228 -0.1839 -0.0244 137 THR F CB  
15466 O OG1 . THR F 137 ? 1.8410 2.2361 2.3003 -0.0211 -0.1894 -0.0254 137 THR F OG1 
15467 C CG2 . THR F 137 ? 1.9940 2.3719 2.4294 -0.0182 -0.1737 -0.0198 137 THR F CG2 
15468 N N   . LYS F 138 ? 2.1361 2.5648 2.6437 -0.0315 -0.1755 -0.0148 138 LYS F N   
15469 C CA  . LYS F 138 ? 2.1126 2.5606 2.6329 -0.0317 -0.1684 -0.0094 138 LYS F CA  
15470 C C   . LYS F 138 ? 2.1148 2.5638 2.6199 -0.0252 -0.1671 -0.0088 138 LYS F C   
15471 O O   . LYS F 138 ? 2.1530 2.5938 2.6456 -0.0214 -0.1754 -0.0138 138 LYS F O   
15472 C CB  . LYS F 138 ? 2.1094 2.5734 2.6545 -0.0361 -0.1737 -0.0114 138 LYS F CB  
15473 C CG  . LYS F 138 ? 2.1287 2.5893 2.6732 -0.0346 -0.1873 -0.0192 138 LYS F CG  
15474 C CD  . LYS F 138 ? 2.1457 2.6256 2.7152 -0.0376 -0.1911 -0.0205 138 LYS F CD  
15475 C CE  . LYS F 138 ? 2.2147 2.6919 2.7838 -0.0354 -0.2052 -0.0282 138 LYS F CE  
15476 N NZ  . LYS F 138 ? 2.2582 2.7267 2.8046 -0.0279 -0.2083 -0.0295 138 LYS F NZ  
15477 N N   . VAL F 139 ? 1.8774 2.3361 2.3833 -0.0240 -0.1567 -0.0026 139 VAL F N   
15478 C CA  . VAL F 139 ? 1.7623 2.2233 2.2558 -0.0184 -0.1542 -0.0014 139 VAL F CA  
15479 C C   . VAL F 139 ? 1.7028 2.1846 2.2128 -0.0194 -0.1487 0.0024  139 VAL F C   
15480 O O   . VAL F 139 ? 1.7581 2.2508 2.2839 -0.0238 -0.1427 0.0063  139 VAL F O   
15481 C CB  . VAL F 139 ? 1.7704 2.2199 2.2437 -0.0150 -0.1464 0.0019  139 VAL F CB  
15482 C CG1 . VAL F 139 ? 1.8051 2.2338 2.2601 -0.0133 -0.1519 -0.0026 139 VAL F CG1 
15483 C CG2 . VAL F 139 ? 1.8004 2.2556 2.2821 -0.0182 -0.1360 0.0082  139 VAL F CG2 
15484 N N   . ASP F 140 ? 1.6179 2.1048 2.1237 -0.0151 -0.1508 0.0011  140 ASP F N   
15485 C CA  . ASP F 140 ? 1.5807 2.0869 2.1006 -0.0153 -0.1456 0.0039  140 ASP F CA  
15486 C C   . ASP F 140 ? 1.7120 2.2221 2.2262 -0.0144 -0.1336 0.0103  140 ASP F C   
15487 O O   . ASP F 140 ? 1.6908 2.2172 2.2187 -0.0163 -0.1273 0.0138  140 ASP F O   
15488 C CB  . ASP F 140 ? 1.5108 2.0203 2.0283 -0.0107 -0.1521 0.0002  140 ASP F CB  
15489 C CG  . ASP F 140 ? 1.3896 1.8960 1.9131 -0.0111 -0.1647 -0.0062 140 ASP F CG  
15490 O OD1 . ASP F 140 ? 1.3515 1.8612 1.8898 -0.0161 -0.1674 -0.0075 140 ASP F OD1 
15491 O OD2 . ASP F 140 ? 1.2976 1.7980 1.8111 -0.0065 -0.1721 -0.0097 140 ASP F OD2 
15492 N N   . GLU F 141 ? 1.9136 2.4096 2.4081 -0.0114 -0.1306 0.0117  141 GLU F N   
15493 C CA  . GLU F 141 ? 1.8906 2.3892 2.3786 -0.0102 -0.1199 0.0174  141 GLU F CA  
15494 C C   . GLU F 141 ? 1.8581 2.3477 2.3429 -0.0127 -0.1153 0.0204  141 GLU F C   
15495 O O   . GLU F 141 ? 1.8401 2.3139 2.3081 -0.0102 -0.1157 0.0194  141 GLU F O   
15496 C CB  . GLU F 141 ? 1.8962 2.3869 2.3650 -0.0046 -0.1192 0.0168  141 GLU F CB  
15497 C CG  . GLU F 141 ? 1.9397 2.4390 2.4114 -0.0017 -0.1228 0.0145  141 GLU F CG  
15498 C CD  . GLU F 141 ? 1.9915 2.5085 2.4740 -0.0021 -0.1151 0.0183  141 GLU F CD  
15499 O OE1 . GLU F 141 ? 1.9520 2.4730 2.4360 -0.0039 -0.1066 0.0232  141 GLU F OE1 
15500 O OE2 . GLU F 141 ? 2.0273 2.5539 2.5165 -0.0004 -0.1177 0.0162  141 GLU F OE2 
15501 N N   . PRO F 142 ? 1.7424 2.2412 2.2424 -0.0174 -0.1106 0.0244  142 PRO F N   
15502 C CA  . PRO F 142 ? 1.7874 2.2771 2.2846 -0.0194 -0.1063 0.0277  142 PRO F CA  
15503 C C   . PRO F 142 ? 1.7578 2.2476 2.2458 -0.0170 -0.0968 0.0332  142 PRO F C   
15504 O O   . PRO F 142 ? 1.7682 2.2473 2.2497 -0.0170 -0.0937 0.0352  142 PRO F O   
15505 C CB  . PRO F 142 ? 1.8443 2.3447 2.3624 -0.0257 -0.1052 0.0301  142 PRO F CB  
15506 C CG  . PRO F 142 ? 1.7704 2.2898 2.3006 -0.0260 -0.1036 0.0309  142 PRO F CG  
15507 C CD  . PRO F 142 ? 1.6995 2.2168 2.2205 -0.0212 -0.1097 0.0257  142 PRO F CD  
15508 N N   . SER F 143 ? 1.8033 2.3045 2.2907 -0.0146 -0.0924 0.0354  143 SER F N   
15509 C CA  . SER F 143 ? 1.7125 2.2146 2.1920 -0.0123 -0.0838 0.0404  143 SER F CA  
15510 C C   . SER F 143 ? 1.7952 2.2818 2.2547 -0.0076 -0.0842 0.0382  143 SER F C   
15511 O O   . SER F 143 ? 1.7619 2.2420 2.2140 -0.0064 -0.0788 0.0412  143 SER F O   
15512 C CB  . SER F 143 ? 1.5995 2.1185 2.0846 -0.0114 -0.0792 0.0429  143 SER F CB  
15513 O OG  . SER F 143 ? 1.6840 2.2035 2.1634 -0.0081 -0.0836 0.0384  143 SER F OG  
15514 N N   . LYS F 144 ? 2.0682 2.5488 2.5191 -0.0050 -0.0906 0.0330  144 LYS F N   
15515 C CA  . LYS F 144 ? 2.1003 2.5661 2.5315 -0.0007 -0.0909 0.0308  144 LYS F CA  
15516 C C   . LYS F 144 ? 2.1363 2.5853 2.5594 -0.0011 -0.0933 0.0286  144 LYS F C   
15517 O O   . LYS F 144 ? 2.1952 2.6317 2.6017 0.0022  -0.0919 0.0273  144 LYS F O   
15518 C CB  . LYS F 144 ? 2.1246 2.5879 2.5483 0.0021  -0.0974 0.0262  144 LYS F CB  
15519 C CG  . LYS F 144 ? 2.1714 2.6496 2.6017 0.0031  -0.0956 0.0275  144 LYS F CG  
15520 C CD  . LYS F 144 ? 2.2122 2.6859 2.6353 0.0060  -0.1032 0.0228  144 LYS F CD  
15521 C CE  . LYS F 144 ? 2.2775 2.7349 2.6789 0.0098  -0.1032 0.0215  144 LYS F CE  
15522 N NZ  . LYS F 144 ? 2.3252 2.7770 2.7180 0.0127  -0.1107 0.0176  144 LYS F NZ  
15523 N N   . TYR F 145 ? 1.8529 2.3012 2.2871 -0.0051 -0.0966 0.0279  145 TYR F N   
15524 C CA  . TYR F 145 ? 1.7742 2.2064 2.2020 -0.0058 -0.0995 0.0251  145 TYR F CA  
15525 C C   . TYR F 145 ? 1.7363 2.1701 2.1746 -0.0091 -0.0941 0.0298  145 TYR F C   
15526 O O   . TYR F 145 ? 1.6936 2.1412 2.1439 -0.0110 -0.0886 0.0352  145 TYR F O   
15527 C CB  . TYR F 145 ? 1.7507 2.1775 2.1813 -0.0077 -0.1100 0.0190  145 TYR F CB  
15528 C CG  . TYR F 145 ? 1.7937 2.2197 2.2156 -0.0045 -0.1164 0.0147  145 TYR F CG  
15529 C CD1 . TYR F 145 ? 1.8545 2.2727 2.2576 0.0002  -0.1144 0.0142  145 TYR F CD1 
15530 C CD2 . TYR F 145 ? 1.7763 2.2092 2.2092 -0.0064 -0.1245 0.0114  145 TYR F CD2 
15531 C CE1 . TYR F 145 ? 1.8728 2.2892 2.2675 0.0031  -0.1203 0.0109  145 TYR F CE1 
15532 C CE2 . TYR F 145 ? 1.8147 2.2464 2.2399 -0.0032 -0.1308 0.0078  145 TYR F CE2 
15533 C CZ  . TYR F 145 ? 1.8504 2.2734 2.2561 0.0015  -0.1288 0.0077  145 TYR F CZ  
15534 O OH  . TYR F 145 ? 1.8028 2.2236 2.2003 0.0047  -0.1351 0.0046  145 TYR F OH  
15535 N N   . GLY F 146 ? 1.8255 2.2446 2.2589 -0.0096 -0.0959 0.0275  146 GLY F N   
15536 C CA  . GLY F 146 ? 1.8848 2.3031 2.3283 -0.0129 -0.0921 0.0315  146 GLY F CA  
15537 C C   . GLY F 146 ? 2.0521 2.4729 2.5114 -0.0185 -0.0979 0.0300  146 GLY F C   
15538 O O   . GLY F 146 ? 1.9920 2.4020 2.4485 -0.0194 -0.1055 0.0239  146 GLY F O   
15539 N N   . VAL F 147 ? 2.4855 2.9207 2.9617 -0.0225 -0.0942 0.0354  147 VAL F N   
15540 C CA  . VAL F 147 ? 2.4776 2.9182 2.9711 -0.0283 -0.0989 0.0345  147 VAL F CA  
15541 C C   . VAL F 147 ? 2.5009 2.9304 2.9992 -0.0318 -0.0987 0.0356  147 VAL F C   
15542 O O   . VAL F 147 ? 2.5146 2.9406 3.0108 -0.0310 -0.0920 0.0408  147 VAL F O   
15543 C CB  . VAL F 147 ? 2.4425 2.9037 2.9516 -0.0313 -0.0945 0.0398  147 VAL F CB  
15544 C CG1 . VAL F 147 ? 2.4360 2.9037 2.9638 -0.0375 -0.0992 0.0385  147 VAL F CG1 
15545 C CG2 . VAL F 147 ? 2.4191 2.8903 2.9231 -0.0275 -0.0944 0.0385  147 VAL F CG2 
15546 N N   . VAL F 148 ? 2.1312 2.5549 2.6365 -0.0355 -0.1065 0.0305  148 VAL F N   
15547 C CA  . VAL F 148 ? 2.1023 2.5157 2.6147 -0.0397 -0.1075 0.0308  148 VAL F CA  
15548 C C   . VAL F 148 ? 2.1008 2.5277 2.6357 -0.0467 -0.1073 0.0343  148 VAL F C   
15549 O O   . VAL F 148 ? 2.0511 2.4860 2.5954 -0.0493 -0.1134 0.0303  148 VAL F O   
15550 C CB  . VAL F 148 ? 1.9690 2.3652 2.4730 -0.0393 -0.1165 0.0221  148 VAL F CB  
15551 C CG1 . VAL F 148 ? 1.9661 2.3519 2.4793 -0.0441 -0.1177 0.0221  148 VAL F CG1 
15552 C CG2 . VAL F 148 ? 1.9079 2.2910 2.3890 -0.0324 -0.1157 0.0188  148 VAL F CG2 
15553 N N   . VAL F 149 ? 2.2115 2.6409 2.7549 -0.0498 -0.1003 0.0418  149 VAL F N   
15554 C CA  . VAL F 149 ? 2.1574 2.6001 2.7214 -0.0566 -0.0983 0.0465  149 VAL F CA  
15555 C C   . VAL F 149 ? 2.1674 2.5984 2.7410 -0.0622 -0.1029 0.0444  149 VAL F C   
15556 O O   . VAL F 149 ? 2.1527 2.5737 2.7263 -0.0634 -0.0992 0.0485  149 VAL F O   
15557 C CB  . VAL F 149 ? 2.1694 2.6223 2.7368 -0.0570 -0.0881 0.0565  149 VAL F CB  
15558 C CG1 . VAL F 149 ? 2.1120 2.5816 2.6769 -0.0537 -0.0846 0.0581  149 VAL F CG1 
15559 C CG2 . VAL F 149 ? 2.1168 2.5561 2.6716 -0.0530 -0.0835 0.0599  149 VAL F CG2 
15560 N N   . MET F 150 ? 2.0751 2.5071 2.6570 -0.0655 -0.1113 0.0377  150 MET F N   
15561 C CA  . MET F 150 ? 1.9652 2.3878 2.5584 -0.0714 -0.1168 0.0346  150 MET F CA  
15562 C C   . MET F 150 ? 1.9075 2.3462 2.5241 -0.0791 -0.1166 0.0373  150 MET F C   
15563 O O   . MET F 150 ? 1.8989 2.3557 2.5222 -0.0791 -0.1141 0.0393  150 MET F O   
15564 C CB  . MET F 150 ? 1.9083 2.3184 2.4929 -0.0695 -0.1278 0.0239  150 MET F CB  
15565 C CG  . MET F 150 ? 1.9020 2.3237 2.4868 -0.0675 -0.1337 0.0187  150 MET F CG  
15566 S SD  . MET F 150 ? 1.8072 2.2132 2.3776 -0.0640 -0.1465 0.0068  150 MET F SD  
15567 C CE  . MET F 150 ? 1.9227 2.3231 2.5121 -0.0725 -0.1543 0.0024  150 MET F CE  
15568 N N   . ARG F 156 ? 1.4316 1.7919 2.0346 -0.0842 -0.1392 0.0160  156 ARG F N   
15569 C CA  . ARG F 156 ? 1.5497 1.8996 2.1403 -0.0798 -0.1314 0.0214  156 ARG F CA  
15570 C C   . ARG F 156 ? 1.6268 1.9904 2.2100 -0.0747 -0.1230 0.0282  156 ARG F C   
15571 O O   . ARG F 156 ? 1.6647 2.0469 2.2596 -0.0775 -0.1197 0.0332  156 ARG F O   
15572 C CB  . ARG F 156 ? 1.6254 1.9700 2.2300 -0.0858 -0.1270 0.0279  156 ARG F CB  
15573 C CG  . ARG F 156 ? 1.8240 2.1539 2.4169 -0.0814 -0.1208 0.0319  156 ARG F CG  
15574 C CD  . ARG F 156 ? 1.9404 2.2650 2.5484 -0.0878 -0.1171 0.0388  156 ARG F CD  
15575 N NE  . ARG F 156 ? 1.8689 2.1861 2.4902 -0.0949 -0.1250 0.0329  156 ARG F NE  
15576 C CZ  . ARG F 156 ? 1.7973 2.1098 2.4346 -0.1021 -0.1235 0.0376  156 ARG F CZ  
15577 N NH1 . ARG F 156 ? 1.9239 2.2380 2.5648 -0.1028 -0.1145 0.0486  156 ARG F NH1 
15578 N NH2 . ARG F 156 ? 1.6879 1.9938 2.3373 -0.1086 -0.1312 0.0313  156 ARG F NH2 
15579 N N   . VAL F 157 ? 1.6809 2.0355 2.2449 -0.0674 -0.1196 0.0281  157 VAL F N   
15580 C CA  . VAL F 157 ? 1.7094 2.0753 2.2647 -0.0621 -0.1123 0.0336  157 VAL F CA  
15581 C C   . VAL F 157 ? 1.7176 2.0832 2.2757 -0.0621 -0.1029 0.0434  157 VAL F C   
15582 O O   . VAL F 157 ? 1.7295 2.0823 2.2912 -0.0643 -0.1023 0.0449  157 VAL F O   
15583 C CB  . VAL F 157 ? 1.6493 2.0070 2.1822 -0.0541 -0.1139 0.0278  157 VAL F CB  
15584 C CG1 . VAL F 157 ? 1.7033 2.0550 2.2317 -0.0542 -0.1246 0.0174  157 VAL F CG1 
15585 C CG2 . VAL F 157 ? 1.5968 1.9376 2.1171 -0.0497 -0.1101 0.0282  157 VAL F CG2 
15586 N N   . GLU F 158 ? 1.7642 2.1441 2.3205 -0.0596 -0.0957 0.0502  158 GLU F N   
15587 C CA  . GLU F 158 ? 1.7780 2.1606 2.3384 -0.0600 -0.0871 0.0603  158 GLU F CA  
15588 C C   . GLU F 158 ? 1.7926 2.1773 2.3383 -0.0526 -0.0808 0.0638  158 GLU F C   
15589 O O   . GLU F 158 ? 1.8210 2.1958 2.3615 -0.0497 -0.0767 0.0674  158 GLU F O   
15590 C CB  . GLU F 158 ? 1.7863 2.1870 2.3641 -0.0663 -0.0836 0.0674  158 GLU F CB  
15591 C CG  . GLU F 158 ? 1.7879 2.1881 2.3830 -0.0745 -0.0888 0.0652  158 GLU F CG  
15592 C CD  . GLU F 158 ? 1.7692 2.1883 2.3813 -0.0807 -0.0845 0.0721  158 GLU F CD  
15593 O OE1 . GLU F 158 ? 1.8153 2.2486 2.4249 -0.0783 -0.0782 0.0777  158 GLU F OE1 
15594 O OE2 . GLU F 158 ? 1.7395 2.1596 2.3678 -0.0881 -0.0872 0.0718  158 GLU F OE2 
15595 N N   . LYS F 159 ? 1.7947 2.1920 2.3344 -0.0493 -0.0802 0.0625  159 LYS F N   
15596 C CA  . LYS F 159 ? 1.7092 2.1109 2.2372 -0.0431 -0.0738 0.0663  159 LYS F CA  
15597 C C   . LYS F 159 ? 1.7553 2.1600 2.2709 -0.0384 -0.0768 0.0597  159 LYS F C   
15598 O O   . LYS F 159 ? 1.8745 2.2803 2.3918 -0.0401 -0.0835 0.0533  159 LYS F O   
15599 C CB  . LYS F 159 ? 1.5816 2.0004 2.1186 -0.0451 -0.0668 0.0759  159 LYS F CB  
15600 C CG  . LYS F 159 ? 1.4955 1.9153 2.0234 -0.0397 -0.0597 0.0819  159 LYS F CG  
15601 C CD  . LYS F 159 ? 1.4414 1.8446 1.9671 -0.0384 -0.0582 0.0841  159 LYS F CD  
15602 C CE  . LYS F 159 ? 1.3085 1.7138 1.8271 -0.0331 -0.0514 0.0905  159 LYS F CE  
15603 N NZ  . LYS F 159 ? 1.3044 1.7119 1.8089 -0.0267 -0.0507 0.0860  159 LYS F NZ  
15604 N N   . PHE F 160 ? 1.6535 2.0590 2.1566 -0.0324 -0.0720 0.0614  160 PHE F N   
15605 C CA  . PHE F 160 ? 1.6730 2.0812 2.1635 -0.0277 -0.0736 0.0563  160 PHE F CA  
15606 C C   . PHE F 160 ? 1.6565 2.0824 2.1483 -0.0262 -0.0678 0.0619  160 PHE F C   
15607 O O   . PHE F 160 ? 1.6402 2.0687 2.1302 -0.0240 -0.0612 0.0680  160 PHE F O   
15608 C CB  . PHE F 160 ? 1.7298 2.1222 2.2030 -0.0218 -0.0733 0.0520  160 PHE F CB  
15609 N N   . VAL F 161 ? 1.6914 2.1293 2.1867 -0.0273 -0.0705 0.0597  161 VAL F N   
15610 C CA  . VAL F 161 ? 1.6274 2.0825 2.1245 -0.0262 -0.0657 0.0639  161 VAL F CA  
15611 C C   . VAL F 161 ? 1.6492 2.1044 2.1341 -0.0217 -0.0685 0.0581  161 VAL F C   
15612 O O   . VAL F 161 ? 1.7176 2.1758 2.2050 -0.0229 -0.0744 0.0532  161 VAL F O   
15613 C CB  . VAL F 161 ? 1.5798 2.0507 2.0938 -0.0318 -0.0657 0.0668  161 VAL F CB  
15614 C CG1 . VAL F 161 ? 1.5345 2.0227 2.0493 -0.0302 -0.0603 0.0708  161 VAL F CG1 
15615 C CG2 . VAL F 161 ? 1.5590 2.0281 2.0848 -0.0369 -0.0633 0.0725  161 VAL F CG2 
15616 N N   . GLU F 162 ? 1.5758 2.0276 2.0478 -0.0165 -0.0643 0.0589  162 GLU F N   
15617 C CA  . GLU F 162 ? 1.5323 1.9836 1.9920 -0.0123 -0.0659 0.0544  162 GLU F CA  
15618 C C   . GLU F 162 ? 1.5088 1.9778 1.9725 -0.0117 -0.0621 0.0577  162 GLU F C   
15619 O O   . GLU F 162 ? 1.4820 1.9601 1.9506 -0.0121 -0.0559 0.0640  162 GLU F O   
15620 C CB  . GLU F 162 ? 1.5265 1.9650 1.9705 -0.0072 -0.0630 0.0532  162 GLU F CB  
15621 C CG  . GLU F 162 ? 1.5593 2.0035 2.0025 -0.0048 -0.0548 0.0595  162 GLU F CG  
15622 C CD  . GLU F 162 ? 1.6153 2.0575 2.0675 -0.0071 -0.0517 0.0650  162 GLU F CD  
15623 O OE1 . GLU F 162 ? 1.6590 2.0943 2.1177 -0.0107 -0.0557 0.0636  162 GLU F OE1 
15624 O OE2 . GLU F 162 ? 1.5707 2.0185 2.0238 -0.0054 -0.0456 0.0708  162 GLU F OE2 
15625 N N   . LYS F 163 ? 1.5047 1.9781 1.9661 -0.0107 -0.0663 0.0533  163 LYS F N   
15626 C CA  . LYS F 163 ? 1.5065 1.9961 1.9721 -0.0102 -0.0638 0.0551  163 LYS F CA  
15627 C C   . LYS F 163 ? 1.4942 1.9983 1.9758 -0.0146 -0.0602 0.0605  163 LYS F C   
15628 O O   . LYS F 163 ? 1.4445 1.9565 1.9272 -0.0140 -0.0536 0.0662  163 LYS F O   
15629 C CB  . LYS F 163 ? 1.5005 1.9909 1.9548 -0.0057 -0.0582 0.0569  163 LYS F CB  
15630 C CG  . LYS F 163 ? 1.4711 1.9769 1.9282 -0.0047 -0.0560 0.0578  163 LYS F CG  
15631 C CD  . LYS F 163 ? 1.4860 1.9941 1.9448 -0.0049 -0.0626 0.0523  163 LYS F CD  
15632 C CE  . LYS F 163 ? 1.4594 1.9835 1.9234 -0.0043 -0.0604 0.0531  163 LYS F CE  
15633 N NZ  . LYS F 163 ? 1.4533 1.9924 1.9314 -0.0079 -0.0560 0.0580  163 LYS F NZ  
15634 N N   . PRO F 164 ? 1.5081 2.0162 2.0023 -0.0190 -0.0643 0.0592  164 PRO F N   
15635 C CA  . PRO F 164 ? 1.5307 2.0532 2.0401 -0.0235 -0.0604 0.0645  164 PRO F CA  
15636 C C   . PRO F 164 ? 1.5731 2.1128 2.0871 -0.0229 -0.0586 0.0644  164 PRO F C   
15637 O O   . PRO F 164 ? 1.5536 2.0965 2.0701 -0.0224 -0.0638 0.0590  164 PRO F O   
15638 C CB  . PRO F 164 ? 1.5101 2.0295 2.0312 -0.0285 -0.0659 0.0621  164 PRO F CB  
15639 C CG  . PRO F 164 ? 1.5341 2.0359 2.0448 -0.0263 -0.0727 0.0557  164 PRO F CG  
15640 C CD  . PRO F 164 ? 1.5528 2.0517 2.0483 -0.0205 -0.0726 0.0530  164 PRO F CD  
15641 N N   . LYS F 165 ? 1.6260 2.1766 2.1412 -0.0226 -0.0515 0.0701  165 LYS F N   
15642 C CA  . LYS F 165 ? 1.6259 2.1932 2.1459 -0.0222 -0.0493 0.0699  165 LYS F CA  
15643 C C   . LYS F 165 ? 1.6134 2.1926 2.1501 -0.0272 -0.0504 0.0697  165 LYS F C   
15644 O O   . LYS F 165 ? 1.6001 2.1893 2.1422 -0.0267 -0.0526 0.0657  165 LYS F O   
15645 C CB  . LYS F 165 ? 1.6335 2.2092 2.1501 -0.0208 -0.0417 0.0759  165 LYS F CB  
15646 C CG  . LYS F 165 ? 1.6285 2.1969 2.1302 -0.0155 -0.0403 0.0752  165 LYS F CG  
15647 C CD  . LYS F 165 ? 1.7223 2.3019 2.2224 -0.0142 -0.0336 0.0802  165 LYS F CD  
15648 C CE  . LYS F 165 ? 1.7625 2.3576 2.2670 -0.0139 -0.0328 0.0780  165 LYS F CE  
15649 N NZ  . LYS F 165 ? 1.8164 2.4264 2.3263 -0.0157 -0.0266 0.0837  165 LYS F NZ  
15650 N N   . LEU F 166 ? 1.5938 2.1721 2.1394 -0.0319 -0.0489 0.0738  166 LEU F N   
15651 C CA  . LEU F 166 ? 1.6503 2.2378 2.2124 -0.0374 -0.0503 0.0734  166 LEU F CA  
15652 C C   . LEU F 166 ? 1.6898 2.2645 2.2551 -0.0393 -0.0580 0.0686  166 LEU F C   
15653 O O   . LEU F 166 ? 1.6455 2.2037 2.1999 -0.0370 -0.0610 0.0669  166 LEU F O   
15654 C CB  . LEU F 166 ? 1.6482 2.2436 2.2190 -0.0421 -0.0435 0.0814  166 LEU F CB  
15655 C CG  . LEU F 166 ? 1.6692 2.2848 2.2523 -0.0452 -0.0391 0.0832  166 LEU F CG  
15656 C CD1 . LEU F 166 ? 1.6845 2.3104 2.2597 -0.0409 -0.0344 0.0842  166 LEU F CD1 
15657 C CD2 . LEU F 166 ? 1.6367 2.2570 2.2300 -0.0513 -0.0339 0.0906  166 LEU F CD2 
15658 N N   . TYR F 167 ? 1.7900 2.3726 2.3705 -0.0437 -0.0611 0.0661  167 TYR F N   
15659 C CA  . TYR F 167 ? 1.7257 2.2979 2.3103 -0.0456 -0.0694 0.0606  167 TYR F CA  
15660 C C   . TYR F 167 ? 1.6969 2.2597 2.2864 -0.0504 -0.0684 0.0646  167 TYR F C   
15661 O O   . TYR F 167 ? 1.6501 2.2222 2.2534 -0.0559 -0.0643 0.0693  167 TYR F O   
15662 C CB  . TYR F 167 ? 1.7271 2.3118 2.3273 -0.0481 -0.0738 0.0558  167 TYR F CB  
15663 C CG  . TYR F 167 ? 1.7862 2.3609 2.3918 -0.0504 -0.0830 0.0500  167 TYR F CG  
15664 C CD1 . TYR F 167 ? 1.8507 2.4138 2.4451 -0.0459 -0.0911 0.0432  167 TYR F CD1 
15665 C CD2 . TYR F 167 ? 1.8059 2.3825 2.4274 -0.0572 -0.0836 0.0513  167 TYR F CD2 
15666 C CE1 . TYR F 167 ? 1.9392 2.4931 2.5376 -0.0479 -0.1001 0.0376  167 TYR F CE1 
15667 C CE2 . TYR F 167 ? 1.8813 2.4488 2.5081 -0.0594 -0.0925 0.0455  167 TYR F CE2 
15668 C CZ  . TYR F 167 ? 1.9832 2.5396 2.5982 -0.0546 -0.1009 0.0385  167 TYR F CZ  
15669 O OH  . TYR F 167 ? 2.0801 2.6274 2.6996 -0.0567 -0.1103 0.0326  167 TYR F OH  
15670 N N   . VAL F 168 ? 1.7822 2.3266 2.3606 -0.0484 -0.0720 0.0627  168 VAL F N   
15671 C CA  . VAL F 168 ? 1.7613 2.2940 2.3444 -0.0527 -0.0732 0.0644  168 VAL F CA  
15672 C C   . VAL F 168 ? 1.8231 2.3441 2.4070 -0.0536 -0.0829 0.0565  168 VAL F C   
15673 O O   . VAL F 168 ? 1.7673 2.2788 2.3571 -0.0578 -0.0851 0.0567  168 VAL F O   
15674 C CB  . VAL F 168 ? 1.6621 2.1821 2.2324 -0.0501 -0.0686 0.0693  168 VAL F CB  
15675 C CG1 . VAL F 168 ? 1.5456 2.0772 2.1176 -0.0504 -0.0594 0.0779  168 VAL F CG1 
15676 C CG2 . VAL F 168 ? 1.6477 2.1566 2.1995 -0.0431 -0.0711 0.0647  168 VAL F CG2 
15677 N N   . GLY F 169 ? 1.9477 2.4685 2.5255 -0.0497 -0.0890 0.0497  169 GLY F N   
15678 C CA  . GLY F 169 ? 1.9980 2.5084 2.5755 -0.0501 -0.0990 0.0419  169 GLY F CA  
15679 C C   . GLY F 169 ? 2.0769 2.5846 2.6412 -0.0440 -0.1042 0.0361  169 GLY F C   
15680 O O   . GLY F 169 ? 2.0406 2.5530 2.5954 -0.0395 -0.0998 0.0380  169 GLY F O   
15681 N N   . ASN F 170 ? 2.3117 2.8112 2.8753 -0.0440 -0.1140 0.0288  170 ASN F N   
15682 C CA  . ASN F 170 ? 2.3143 2.8088 2.8644 -0.0384 -0.1203 0.0230  170 ASN F CA  
15683 C C   . ASN F 170 ? 2.3493 2.8233 2.8855 -0.0367 -0.1277 0.0174  170 ASN F C   
15684 O O   . ASN F 170 ? 2.3575 2.8251 2.8807 -0.0322 -0.1336 0.0125  170 ASN F O   
15685 C CB  . ASN F 170 ? 2.2934 2.8015 2.8568 -0.0391 -0.1263 0.0189  170 ASN F CB  
15686 C CG  . ASN F 170 ? 2.2932 2.8076 2.8778 -0.0459 -0.1301 0.0175  170 ASN F CG  
15687 O OD1 . ASN F 170 ? 2.3478 2.8787 2.9498 -0.0498 -0.1254 0.0209  170 ASN F OD1 
15688 N ND2 . ASN F 170 ? 2.3152 2.8164 2.8985 -0.0475 -0.1384 0.0123  170 ASN F ND2 
15689 N N   . LYS F 171 ? 2.0735 2.5370 2.6117 -0.0401 -0.1275 0.0179  171 LYS F N   
15690 C CA  . LYS F 171 ? 1.9339 2.3783 2.4606 -0.0392 -0.1349 0.0119  171 LYS F CA  
15691 C C   . LYS F 171 ? 1.9284 2.3585 2.4348 -0.0346 -0.1297 0.0135  171 LYS F C   
15692 O O   . LYS F 171 ? 2.0090 2.4393 2.5167 -0.0354 -0.1213 0.0196  171 LYS F O   
15693 C CB  . LYS F 171 ? 1.8415 2.2821 2.3830 -0.0458 -0.1380 0.0109  171 LYS F CB  
15694 C CG  . LYS F 171 ? 1.7811 2.2371 2.3452 -0.0511 -0.1423 0.0096  171 LYS F CG  
15695 C CD  . LYS F 171 ? 1.7050 2.1675 2.2878 -0.0580 -0.1367 0.0153  171 LYS F CD  
15696 C CE  . LYS F 171 ? 1.8018 2.2733 2.3842 -0.0572 -0.1247 0.0242  171 LYS F CE  
15697 N NZ  . LYS F 171 ? 1.7588 2.2343 2.3568 -0.0638 -0.1190 0.0305  171 LYS F NZ  
15698 N N   . ILE F 172 ? 1.7485 2.1664 2.2361 -0.0297 -0.1346 0.0082  172 ILE F N   
15699 C CA  . ILE F 172 ? 1.7273 2.1319 2.1947 -0.0249 -0.1298 0.0089  172 ILE F CA  
15700 C C   . ILE F 172 ? 1.6493 2.0343 2.1043 -0.0241 -0.1367 0.0020  172 ILE F C   
15701 O O   . ILE F 172 ? 1.6295 2.0114 2.0891 -0.0265 -0.1462 -0.0037 172 ILE F O   
15702 C CB  . ILE F 172 ? 1.6977 2.1059 2.1513 -0.0193 -0.1272 0.0096  172 ILE F CB  
15703 C CG1 . ILE F 172 ? 1.6482 2.0500 2.0914 -0.0167 -0.1371 0.0026  172 ILE F CG1 
15704 C CG2 . ILE F 172 ? 1.7554 2.1837 2.2223 -0.0202 -0.1219 0.0150  172 ILE F CG2 
15705 C CD1 . ILE F 172 ? 1.7263 2.1239 2.1500 -0.0107 -0.1350 0.0025  172 ILE F CD1 
15706 N N   . ASN F 173 ? 1.7315 2.1033 2.1704 -0.0206 -0.1319 0.0023  173 ASN F N   
15707 C CA  . ASN F 173 ? 1.6896 2.0420 2.1144 -0.0192 -0.1374 -0.0044 173 ASN F CA  
15708 C C   . ASN F 173 ? 1.7192 2.0659 2.1280 -0.0155 -0.1450 -0.0104 173 ASN F C   
15709 O O   . ASN F 173 ? 1.7517 2.1059 2.1545 -0.0123 -0.1431 -0.0085 173 ASN F O   
15710 C CB  . ASN F 173 ? 1.5710 1.9120 1.9832 -0.0160 -0.1294 -0.0024 173 ASN F CB  
15711 C CG  . ASN F 173 ? 1.6290 1.9503 2.0307 -0.0157 -0.1340 -0.0091 173 ASN F CG  
15712 O OD1 . ASN F 173 ? 1.6488 1.9611 2.0394 -0.0145 -0.1423 -0.0161 173 ASN F OD1 
15713 N ND2 . ASN F 173 ? 1.6907 2.0048 2.0955 -0.0165 -0.1287 -0.0070 173 ASN F ND2 
15714 N N   . ALA F 174 ? 1.8798 2.2128 2.2814 -0.0160 -0.1539 -0.0177 174 ALA F N   
15715 C CA  . ALA F 174 ? 1.9833 2.3095 2.3693 -0.0128 -0.1625 -0.0237 174 ALA F CA  
15716 C C   . ALA F 174 ? 2.0244 2.3316 2.3847 -0.0083 -0.1618 -0.0278 174 ALA F C   
15717 O O   . ALA F 174 ? 2.0710 2.3703 2.4154 -0.0054 -0.1689 -0.0328 174 ALA F O   
15718 C CB  . ALA F 174 ? 2.0319 2.3582 2.4287 -0.0167 -0.1748 -0.0297 174 ALA F CB  
15719 N N   . GLY F 175 ? 1.7793 2.0789 2.1350 -0.0073 -0.1535 -0.0259 175 GLY F N   
15720 C CA  . GLY F 175 ? 1.7172 1.9997 2.0491 -0.0029 -0.1513 -0.0296 175 GLY F CA  
15721 C C   . GLY F 175 ? 1.7282 1.9935 2.0515 -0.0037 -0.1591 -0.0378 175 GLY F C   
15722 O O   . GLY F 175 ? 1.7188 1.9693 2.0209 0.0002  -0.1577 -0.0418 175 GLY F O   
15723 N N   . ILE F 176 ? 1.8408 2.1075 2.1799 -0.0087 -0.1671 -0.0409 176 ILE F N   
15724 C CA  . ILE F 176 ? 1.8753 2.1260 2.2083 -0.0101 -0.1751 -0.0491 176 ILE F CA  
15725 C C   . ILE F 176 ? 1.9855 2.2354 2.3369 -0.0148 -0.1722 -0.0477 176 ILE F C   
15726 O O   . ILE F 176 ? 2.1049 2.3689 2.4790 -0.0193 -0.1713 -0.0427 176 ILE F O   
15727 C CB  . ILE F 176 ? 1.7629 2.0143 2.0975 -0.0120 -0.1889 -0.0551 176 ILE F CB  
15728 N N   . TYR F 177 ? 1.9968 2.2301 2.3382 -0.0136 -0.1706 -0.0519 177 TYR F N   
15729 C CA  . TYR F 177 ? 2.0667 2.2966 2.4227 -0.0171 -0.1667 -0.0502 177 TYR F CA  
15730 C C   . TYR F 177 ? 2.0230 2.2366 2.3766 -0.0195 -0.1756 -0.0594 177 TYR F C   
15731 O O   . TYR F 177 ? 1.9836 2.1872 2.3209 -0.0176 -0.1838 -0.0673 177 TYR F O   
15732 C CB  . TYR F 177 ? 2.0632 2.2883 2.4113 -0.0128 -0.1544 -0.0458 177 TYR F CB  
15733 C CG  . TYR F 177 ? 1.9887 2.2280 2.3359 -0.0097 -0.1455 -0.0376 177 TYR F CG  
15734 C CD1 . TYR F 177 ? 1.9755 2.2338 2.3397 -0.0128 -0.1450 -0.0312 177 TYR F CD1 
15735 C CD2 . TYR F 177 ? 1.9294 2.1634 2.2590 -0.0038 -0.1373 -0.0367 177 TYR F CD2 
15736 C CE1 . TYR F 177 ? 1.9212 2.1920 2.2843 -0.0099 -0.1371 -0.0243 177 TYR F CE1 
15737 C CE2 . TYR F 177 ? 1.8954 2.1421 2.2246 -0.0013 -0.1295 -0.0296 177 TYR F CE2 
15738 C CZ  . TYR F 177 ? 1.8712 2.1360 2.2169 -0.0043 -0.1296 -0.0235 177 TYR F CZ  
15739 O OH  . TYR F 177 ? 1.7956 2.0727 2.1407 -0.0018 -0.1221 -0.0170 177 TYR F OH  
15740 N N   . LEU F 178 ? 2.1429 2.3535 2.5128 -0.0238 -0.1740 -0.0582 178 LEU F N   
15741 C CA  . LEU F 178 ? 2.1110 2.3051 2.4804 -0.0264 -0.1812 -0.0666 178 LEU F CA  
15742 C C   . LEU F 178 ? 2.1130 2.3009 2.4920 -0.0275 -0.1731 -0.0629 178 LEU F C   
15743 O O   . LEU F 178 ? 2.1725 2.3700 2.5738 -0.0326 -0.1707 -0.0566 178 LEU F O   
15744 C CB  . LEU F 178 ? 2.1050 2.3046 2.4912 -0.0330 -0.1927 -0.0702 178 LEU F CB  
15745 C CG  . LEU F 178 ? 1.9686 2.1524 2.3554 -0.0364 -0.2026 -0.0800 178 LEU F CG  
15746 C CD1 . LEU F 178 ? 1.9084 2.0984 2.3030 -0.0404 -0.2157 -0.0852 178 LEU F CD1 
15747 C CD2 . LEU F 178 ? 2.0742 2.2541 2.4802 -0.0415 -0.1990 -0.0774 178 LEU F CD2 
15748 N N   . LEU F 179 ? 2.0128 2.1847 2.3747 -0.0227 -0.1688 -0.0668 179 LEU F N   
15749 C CA  . LEU F 179 ? 2.0144 2.1803 2.3827 -0.0219 -0.1600 -0.0628 179 LEU F CA  
15750 C C   . LEU F 179 ? 2.0615 2.2067 2.4257 -0.0226 -0.1643 -0.0716 179 LEU F C   
15751 O O   . LEU F 179 ? 2.0530 2.1850 2.3976 -0.0195 -0.1694 -0.0810 179 LEU F O   
15752 C CB  . LEU F 179 ? 2.0099 2.1767 2.3636 -0.0148 -0.1489 -0.0585 179 LEU F CB  
15753 C CG  . LEU F 179 ? 1.9666 2.1537 2.3270 -0.0141 -0.1424 -0.0485 179 LEU F CG  
15754 C CD1 . LEU F 179 ? 1.9277 2.1142 2.2714 -0.0070 -0.1328 -0.0461 179 LEU F CD1 
15755 C CD2 . LEU F 179 ? 2.0057 2.2037 2.3908 -0.0189 -0.1383 -0.0394 179 LEU F CD2 
15756 N N   . ASN F 180 ? 2.0876 2.2297 2.4699 -0.0266 -0.1621 -0.0684 180 ASN F N   
15757 C CA  . ASN F 180 ? 2.1771 2.2990 2.5571 -0.0269 -0.1645 -0.0758 180 ASN F CA  
15758 C C   . ASN F 180 ? 2.2473 2.3579 2.6105 -0.0192 -0.1555 -0.0769 180 ASN F C   
15759 O O   . ASN F 180 ? 2.2235 2.3435 2.5835 -0.0150 -0.1461 -0.0695 180 ASN F O   
15760 C CB  . ASN F 180 ? 2.1305 2.2527 2.5358 -0.0336 -0.1642 -0.0710 180 ASN F CB  
15761 C CG  . ASN F 180 ? 2.1067 2.2306 2.5264 -0.0415 -0.1756 -0.0753 180 ASN F CG  
15762 O OD1 . ASN F 180 ? 2.1399 2.2570 2.5487 -0.0416 -0.1851 -0.0851 180 ASN F OD1 
15763 N ND2 . ASN F 180 ? 2.0426 2.1755 2.4868 -0.0483 -0.1747 -0.0680 180 ASN F ND2 
15764 N N   . PRO F 181 ? 2.4849 2.5754 2.8374 -0.0173 -0.1581 -0.0865 181 PRO F N   
15765 C CA  . PRO F 181 ? 2.5154 2.5949 2.8541 -0.0100 -0.1490 -0.0878 181 PRO F CA  
15766 C C   . PRO F 181 ? 2.5065 2.5897 2.8612 -0.0094 -0.1394 -0.0782 181 PRO F C   
15767 O O   . PRO F 181 ? 2.5250 2.6039 2.8705 -0.0029 -0.1306 -0.0771 181 PRO F O   
15768 C CB  . PRO F 181 ? 2.5599 2.6173 2.8883 -0.0096 -0.1554 -0.1006 181 PRO F CB  
15769 C CG  . PRO F 181 ? 2.5666 2.6247 2.8938 -0.0145 -0.1681 -0.1071 181 PRO F CG  
15770 C CD  . PRO F 181 ? 2.5168 2.5940 2.8670 -0.0210 -0.1698 -0.0976 181 PRO F CD  
15771 N N   . SER F 182 ? 2.3122 2.4031 2.6904 -0.0160 -0.1408 -0.0710 182 SER F N   
15772 C CA  . SER F 182 ? 2.2461 2.3402 2.6396 -0.0159 -0.1324 -0.0611 182 SER F CA  
15773 C C   . SER F 182 ? 2.2866 2.3996 2.6814 -0.0130 -0.1237 -0.0503 182 SER F C   
15774 O O   . SER F 182 ? 2.2674 2.3857 2.6756 -0.0132 -0.1171 -0.0409 182 SER F O   
15775 C CB  . SER F 182 ? 2.0899 2.1851 2.5074 -0.0244 -0.1369 -0.0572 182 SER F CB  
15776 O OG  . SER F 182 ? 2.0025 2.0797 2.4201 -0.0273 -0.1449 -0.0673 182 SER F OG  
15777 N N   . VAL F 183 ? 2.2585 2.3814 2.6399 -0.0104 -0.1239 -0.0513 183 VAL F N   
15778 C CA  . VAL F 183 ? 2.2916 2.4321 2.6735 -0.0077 -0.1160 -0.0417 183 VAL F CA  
15779 C C   . VAL F 183 ? 2.4096 2.5464 2.7726 0.0007  -0.1083 -0.0435 183 VAL F C   
15780 O O   . VAL F 183 ? 2.3866 2.5355 2.7518 0.0037  -0.1002 -0.0353 183 VAL F O   
15781 C CB  . VAL F 183 ? 2.1676 2.3243 2.5508 -0.0111 -0.1209 -0.0400 183 VAL F CB  
15782 C CG1 . VAL F 183 ? 2.1978 2.3500 2.5583 -0.0072 -0.1247 -0.0484 183 VAL F CG1 
15783 C CG2 . VAL F 183 ? 2.0961 2.2726 2.4881 -0.0107 -0.1136 -0.0285 183 VAL F CG2 
15784 N N   . LEU F 184 ? 2.5492 2.6701 2.8942 0.0045  -0.1104 -0.0539 184 LEU F N   
15785 C CA  . LEU F 184 ? 2.5830 2.7003 2.9090 0.0123  -0.1029 -0.0564 184 LEU F CA  
15786 C C   . LEU F 184 ? 2.5931 2.7072 2.9246 0.0169  -0.0933 -0.0520 184 LEU F C   
15787 O O   . LEU F 184 ? 2.5380 2.6506 2.8561 0.0233  -0.0861 -0.0535 184 LEU F O   
15788 C CB  . LEU F 184 ? 2.5522 2.6522 2.8572 0.0148  -0.1078 -0.0692 184 LEU F CB  
15789 C CG  . LEU F 184 ? 2.4584 2.5604 2.7519 0.0122  -0.1169 -0.0745 184 LEU F CG  
15790 C CD1 . LEU F 184 ? 2.4753 2.5581 2.7483 0.0147  -0.1218 -0.0873 184 LEU F CD1 
15791 C CD2 . LEU F 184 ? 2.4523 2.5692 2.7369 0.0148  -0.1127 -0.0692 184 LEU F CD2 
15792 N N   . ASP F 185 ? 2.8635 2.9765 3.2143 0.0138  -0.0929 -0.0467 185 ASP F N   
15793 C CA  . ASP F 185 ? 2.8667 2.9767 3.2240 0.0183  -0.0845 -0.0419 185 ASP F CA  
15794 C C   . ASP F 185 ? 2.8136 2.9422 3.1842 0.0180  -0.0783 -0.0289 185 ASP F C   
15795 O O   . ASP F 185 ? 2.8086 2.9380 3.1813 0.0231  -0.0705 -0.0246 185 ASP F O   
15796 C CB  . ASP F 185 ? 2.8988 2.9934 3.2682 0.0157  -0.0877 -0.0441 185 ASP F CB  
15797 C CG  . ASP F 185 ? 2.8779 2.9794 3.2676 0.0074  -0.0930 -0.0374 185 ASP F CG  
15798 O OD1 . ASP F 185 ? 2.8468 2.9603 3.2379 0.0027  -0.0977 -0.0360 185 ASP F OD1 
15799 O OD2 . ASP F 185 ? 2.9619 3.0568 3.3662 0.0055  -0.0923 -0.0335 185 ASP F OD2 
15800 N N   . LYS F 186 ? 2.3592 2.5028 2.7387 0.0123  -0.0817 -0.0230 186 LYS F N   
15801 C CA  . LYS F 186 ? 2.1424 2.3037 2.5347 0.0114  -0.0765 -0.0109 186 LYS F CA  
15802 C C   . LYS F 186 ? 1.9981 2.1717 2.3798 0.0167  -0.0697 -0.0081 186 LYS F C   
15803 O O   . LYS F 186 ? 1.9079 2.0962 2.2986 0.0169  -0.0647 0.0015  186 LYS F O   
15804 C CB  . LYS F 186 ? 2.0160 2.1892 2.4214 0.0035  -0.0822 -0.0063 186 LYS F CB  
15805 C CG  . LYS F 186 ? 1.7497 1.9349 2.1737 0.0004  -0.0785 0.0058  186 LYS F CG  
15806 C CD  . LYS F 186 ? 1.6205 1.8190 2.0560 -0.0072 -0.0834 0.0096  186 LYS F CD  
15807 C CE  . LYS F 186 ? 1.5684 1.7755 2.0228 -0.0113 -0.0804 0.0209  186 LYS F CE  
15808 N NZ  . LYS F 186 ? 1.5659 1.7809 2.0202 -0.0061 -0.0717 0.0292  186 LYS F NZ  
15809 N N   . ILE F 187 ? 2.0333 2.2013 2.3960 0.0208  -0.0694 -0.0161 187 ILE F N   
15810 C CA  . ILE F 187 ? 1.9136 2.0924 2.2656 0.0254  -0.0631 -0.0140 187 ILE F CA  
15811 C C   . ILE F 187 ? 1.8693 2.0437 2.2185 0.0323  -0.0543 -0.0132 187 ILE F C   
15812 O O   . ILE F 187 ? 1.8655 2.0249 2.2147 0.0347  -0.0537 -0.0178 187 ILE F O   
15813 C CB  . ILE F 187 ? 1.8773 2.0524 2.2097 0.0263  -0.0669 -0.0224 187 ILE F CB  
15814 C CG1 . ILE F 187 ? 2.0268 2.1817 2.3493 0.0264  -0.0724 -0.0334 187 ILE F CG1 
15815 C CG2 . ILE F 187 ? 1.9604 2.1484 2.2963 0.0210  -0.0729 -0.0197 187 ILE F CG2 
15816 C CD1 . ILE F 187 ? 2.0047 2.1463 2.3153 0.0332  -0.0661 -0.0391 187 ILE F CD1 
15817 N N   . GLU F 188 ? 1.7721 1.9602 2.1200 0.0355  -0.0475 -0.0075 188 GLU F N   
15818 C CA  . GLU F 188 ? 1.7797 1.9669 2.1249 0.0423  -0.0388 -0.0067 188 GLU F CA  
15819 C C   . GLU F 188 ? 1.7909 1.9748 2.1158 0.0467  -0.0354 -0.0138 188 GLU F C   
15820 O O   . GLU F 188 ? 1.7930 1.9766 2.1059 0.0446  -0.0397 -0.0182 188 GLU F O   
15821 C CB  . GLU F 188 ? 1.7430 1.9479 2.1006 0.0429  -0.0335 0.0044  188 GLU F CB  
15822 C CG  . GLU F 188 ? 1.7399 1.9615 2.0988 0.0386  -0.0358 0.0092  188 GLU F CG  
15823 C CD  . GLU F 188 ? 1.7348 1.9735 2.0994 0.0408  -0.0293 0.0177  188 GLU F CD  
15824 O OE1 . GLU F 188 ? 1.7123 1.9513 2.0836 0.0448  -0.0239 0.0215  188 GLU F OE1 
15825 O OE2 . GLU F 188 ? 1.7664 2.0184 2.1291 0.0386  -0.0300 0.0205  188 GLU F OE2 
15826 N N   . LEU F 189 ? 1.8124 1.9937 2.1336 0.0531  -0.0273 -0.0148 189 LEU F N   
15827 C CA  . LEU F 189 ? 1.8345 2.0142 2.1374 0.0574  -0.0223 -0.0205 189 LEU F CA  
15828 C C   . LEU F 189 ? 1.8460 2.0434 2.1471 0.0572  -0.0186 -0.0145 189 LEU F C   
15829 O O   . LEU F 189 ? 1.8614 2.0582 2.1462 0.0590  -0.0162 -0.0187 189 LEU F O   
15830 C CB  . LEU F 189 ? 1.8653 2.0363 2.1659 0.0643  -0.0146 -0.0242 189 LEU F CB  
15831 C CG  . LEU F 189 ? 1.8320 2.0085 2.1512 0.0668  -0.0102 -0.0168 189 LEU F CG  
15832 C CD1 . LEU F 189 ? 1.8054 1.9969 2.1263 0.0708  -0.0018 -0.0114 189 LEU F CD1 
15833 C CD2 . LEU F 189 ? 1.7628 1.9224 2.0836 0.0710  -0.0087 -0.0227 189 LEU F CD2 
15834 N N   . ARG F 190 ? 1.8518 2.0642 2.1686 0.0551  -0.0181 -0.0049 190 ARG F N   
15835 C CA  . ARG F 190 ? 1.8460 2.0754 2.1622 0.0547  -0.0149 0.0006  190 ARG F CA  
15836 C C   . ARG F 190 ? 1.8745 2.1079 2.1850 0.0495  -0.0220 -0.0001 190 ARG F C   
15837 O O   . ARG F 190 ? 1.8703 2.0996 2.1862 0.0450  -0.0295 -0.0008 190 ARG F O   
15838 C CB  . ARG F 190 ? 1.8335 2.0775 2.1679 0.0544  -0.0121 0.0108  190 ARG F CB  
15839 C CG  . ARG F 190 ? 1.8723 2.1128 2.2149 0.0595  -0.0062 0.0125  190 ARG F CG  
15840 C CD  . ARG F 190 ? 1.9309 2.1709 2.2636 0.0657  0.0020  0.0086  190 ARG F CD  
15841 N NE  . ARG F 190 ? 1.9510 2.2046 2.2777 0.0653  0.0051  0.0110  190 ARG F NE  
15842 C CZ  . ARG F 190 ? 1.9453 2.1955 2.2552 0.0663  0.0071  0.0052  190 ARG F CZ  
15843 N NH1 . ARG F 190 ? 1.9343 2.1682 2.2307 0.0679  0.0064  -0.0036 190 ARG F NH1 
15844 N NH2 . ARG F 190 ? 1.9257 2.1885 2.2317 0.0657  0.0099  0.0081  190 ARG F NH2 
15845 N N   . PRO F 191 ? 1.8920 2.1331 2.1920 0.0500  -0.0198 -0.0001 191 PRO F N   
15846 C CA  . PRO F 191 ? 1.9151 2.1613 2.2110 0.0455  -0.0265 -0.0001 191 PRO F CA  
15847 C C   . PRO F 191 ? 1.8906 2.1480 2.2041 0.0404  -0.0314 0.0067  191 PRO F C   
15848 O O   . PRO F 191 ? 1.8406 2.1125 2.1651 0.0402  -0.0277 0.0143  191 PRO F O   
15849 C CB  . PRO F 191 ? 1.9082 2.1641 2.1951 0.0475  -0.0212 0.0018  191 PRO F CB  
15850 C CG  . PRO F 191 ? 1.8912 2.1395 2.1689 0.0531  -0.0132 -0.0020 191 PRO F CG  
15851 C CD  . PRO F 191 ? 1.8812 2.1248 2.1716 0.0549  -0.0112 -0.0010 191 PRO F CD  
15852 N N   . THR F 192 ? 1.9850 2.2358 2.3008 0.0362  -0.0396 0.0037  192 THR F N   
15853 C CA  . THR F 192 ? 1.9805 2.2411 2.3129 0.0309  -0.0445 0.0093  192 THR F CA  
15854 C C   . THR F 192 ? 2.1489 2.4127 2.4770 0.0270  -0.0520 0.0068  192 THR F C   
15855 O O   . THR F 192 ? 2.2494 2.5015 2.5647 0.0270  -0.0571 -0.0008 192 THR F O   
15856 C CB  . THR F 192 ? 1.9696 2.2203 2.3129 0.0287  -0.0476 0.0087  192 THR F CB  
15857 O OG1 . THR F 192 ? 2.0012 2.2591 2.3579 0.0226  -0.0537 0.0123  192 THR F OG1 
15858 C CG2 . THR F 192 ? 2.0798 2.3110 2.4105 0.0300  -0.0512 -0.0012 192 THR F CG2 
15859 N N   . SER F 193 ? 2.1166 2.3966 2.4553 0.0238  -0.0529 0.0130  193 SER F N   
15860 C CA  . SER F 193 ? 2.0923 2.3777 2.4303 0.0201  -0.0600 0.0115  193 SER F CA  
15861 C C   . SER F 193 ? 2.0138 2.2972 2.3647 0.0147  -0.0673 0.0109  193 SER F C   
15862 O O   . SER F 193 ? 1.9496 2.2403 2.3169 0.0120  -0.0658 0.0171  193 SER F O   
15863 C CB  . SER F 193 ? 1.9561 2.2600 2.2998 0.0195  -0.0572 0.0180  193 SER F CB  
15864 O OG  . SER F 193 ? 2.0076 2.3150 2.3446 0.0241  -0.0490 0.0203  193 SER F OG  
15865 N N   . ILE F 194 ? 2.0239 2.2972 2.3674 0.0131  -0.0752 0.0036  194 ILE F N   
15866 C CA  . ILE F 194 ? 1.8709 2.1413 2.2266 0.0077  -0.0826 0.0021  194 ILE F CA  
15867 C C   . ILE F 194 ? 1.6500 1.9379 2.0225 0.0030  -0.0845 0.0082  194 ILE F C   
15868 O O   . ILE F 194 ? 1.6631 1.9529 2.0512 -0.0018 -0.0873 0.0103  194 ILE F O   
15869 C CB  . ILE F 194 ? 1.8272 2.0845 2.1707 0.0071  -0.0915 -0.0075 194 ILE F CB  
15870 C CG1 . ILE F 194 ? 1.6599 1.9098 2.0153 0.0022  -0.0982 -0.0103 194 ILE F CG1 
15871 C CG2 . ILE F 194 ? 1.7187 1.9846 2.0575 0.0062  -0.0968 -0.0086 194 ILE F CG2 
15872 C CD1 . ILE F 194 ? 1.6624 1.8992 2.0065 0.0015  -0.1076 -0.0201 194 ILE F CD1 
15873 N N   . GLU F 195 ? 1.5533 1.8543 1.9233 0.0041  -0.0827 0.0112  195 GLU F N   
15874 C CA  . GLU F 195 ? 1.4639 1.7819 1.8491 0.0000  -0.0843 0.0163  195 GLU F CA  
15875 C C   . GLU F 195 ? 1.4859 1.8160 1.8842 -0.0007 -0.0767 0.0253  195 GLU F C   
15876 O O   . GLU F 195 ? 1.4537 1.7961 1.8671 -0.0050 -0.0777 0.0298  195 GLU F O   
15877 C CB  . GLU F 195 ? 1.4060 1.7324 1.7832 0.0015  -0.0862 0.0151  195 GLU F CB  
15878 C CG  . GLU F 195 ? 1.3698 1.6854 1.7342 0.0019  -0.0947 0.0068  195 GLU F CG  
15879 C CD  . GLU F 195 ? 1.3790 1.6970 1.7558 -0.0034 -0.1038 0.0042  195 GLU F CD  
15880 O OE1 . GLU F 195 ? 1.3567 1.6868 1.7520 -0.0075 -0.1029 0.0092  195 GLU F OE1 
15881 O OE2 . GLU F 195 ? 1.4118 1.7198 1.7798 -0.0035 -0.1119 -0.0030 195 GLU F OE2 
15882 N N   . LYS F 196 ? 1.5685 1.8958 1.9614 0.0036  -0.0693 0.0280  196 LYS F N   
15883 C CA  . LYS F 196 ? 1.6000 1.9390 2.0037 0.0036  -0.0624 0.0367  196 LYS F CA  
15884 C C   . LYS F 196 ? 1.6665 1.9973 2.0771 0.0036  -0.0594 0.0397  196 LYS F C   
15885 O O   . LYS F 196 ? 1.6884 2.0285 2.1113 0.0019  -0.0559 0.0473  196 LYS F O   
15886 C CB  . LYS F 196 ? 1.5482 1.8939 1.9427 0.0085  -0.0559 0.0389  196 LYS F CB  
15887 C CG  . LYS F 196 ? 1.4447 1.7962 1.8302 0.0093  -0.0583 0.0358  196 LYS F CG  
15888 C CD  . LYS F 196 ? 1.3015 1.6589 1.6786 0.0138  -0.0515 0.0379  196 LYS F CD  
15889 C CE  . LYS F 196 ? 1.1900 1.5504 1.5567 0.0147  -0.0540 0.0346  196 LYS F CE  
15890 N NZ  . LYS F 196 ? 1.0782 1.4510 1.4550 0.0108  -0.0587 0.0361  196 LYS F NZ  
15891 N N   . GLU F 197 ? 1.6740 1.9875 2.0768 0.0057  -0.0609 0.0338  197 GLU F N   
15892 C CA  . GLU F 197 ? 1.7530 2.0571 2.1617 0.0065  -0.0580 0.0361  197 GLU F CA  
15893 C C   . GLU F 197 ? 1.8235 2.1130 2.2357 0.0031  -0.0642 0.0310  197 GLU F C   
15894 O O   . GLU F 197 ? 1.8391 2.1265 2.2641 0.0001  -0.0640 0.0353  197 GLU F O   
15895 C CB  . GLU F 197 ? 1.7845 2.0807 2.1814 0.0133  -0.0519 0.0342  197 GLU F CB  
15896 C CG  . GLU F 197 ? 1.7261 2.0360 2.1228 0.0168  -0.0447 0.0404  197 GLU F CG  
15897 C CD  . GLU F 197 ? 1.7369 2.0544 2.1226 0.0182  -0.0446 0.0378  197 GLU F CD  
15898 O OE1 . GLU F 197 ? 1.7671 2.0780 2.1437 0.0171  -0.0500 0.0311  197 GLU F OE1 
15899 O OE2 . GLU F 197 ? 1.7009 2.0305 2.0868 0.0203  -0.0394 0.0425  197 GLU F OE2 
15900 N N   . THR F 198 ? 1.9221 2.2011 2.3228 0.0034  -0.0699 0.0220  198 THR F N   
15901 C CA  . THR F 198 ? 1.9460 2.2094 2.3485 0.0007  -0.0759 0.0161  198 THR F CA  
15902 C C   . THR F 198 ? 1.9451 2.2147 2.3628 -0.0067 -0.0824 0.0175  198 THR F C   
15903 O O   . THR F 198 ? 1.9494 2.2128 2.3789 -0.0105 -0.0841 0.0188  198 THR F O   
15904 C CB  . THR F 198 ? 1.9772 2.2272 2.3611 0.0036  -0.0800 0.0057  198 THR F CB  
15905 O OG1 . THR F 198 ? 2.0362 2.2806 2.4069 0.0103  -0.0732 0.0044  198 THR F OG1 
15906 C CG2 . THR F 198 ? 1.9932 2.2267 2.3786 0.0009  -0.0867 -0.0012 198 THR F CG2 
15907 N N   . PHE F 199 ? 1.8097 2.0912 2.2277 -0.0089 -0.0860 0.0171  199 PHE F N   
15908 C CA  . PHE F 199 ? 1.7304 2.0194 2.1637 -0.0158 -0.0918 0.0182  199 PHE F CA  
15909 C C   . PHE F 199 ? 1.8090 2.1080 2.2608 -0.0198 -0.0873 0.0278  199 PHE F C   
15910 O O   . PHE F 199 ? 1.7713 2.0675 2.2363 -0.0255 -0.0912 0.0281  199 PHE F O   
15911 C CB  . PHE F 199 ? 1.6058 1.9075 2.0366 -0.0164 -0.0955 0.0166  199 PHE F CB  
15912 C CG  . PHE F 199 ? 1.5081 1.7995 1.9254 -0.0152 -0.1034 0.0068  199 PHE F CG  
15913 C CD1 . PHE F 199 ? 1.5029 1.7767 1.9157 -0.0159 -0.1085 -0.0003 199 PHE F CD1 
15914 C CD2 . PHE F 199 ? 1.4394 1.7383 1.8480 -0.0134 -0.1060 0.0047  199 PHE F CD2 
15915 C CE1 . PHE F 199 ? 1.5156 1.7798 1.9149 -0.0147 -0.1162 -0.0094 199 PHE F CE1 
15916 C CE2 . PHE F 199 ? 1.5323 1.8213 1.9275 -0.0121 -0.1137 -0.0039 199 PHE F CE2 
15917 C CZ  . PHE F 199 ? 1.6027 1.8745 1.9929 -0.0128 -0.1188 -0.0109 199 PHE F CZ  
15918 N N   . PRO F 200 ? 2.0299 2.3402 2.4835 -0.0174 -0.0796 0.0358  200 PRO F N   
15919 C CA  . PRO F 200 ? 2.0399 2.3578 2.5096 -0.0211 -0.0756 0.0452  200 PRO F CA  
15920 C C   . PRO F 200 ? 2.0380 2.3409 2.5124 -0.0216 -0.0746 0.0464  200 PRO F C   
15921 O O   . PRO F 200 ? 2.0312 2.3370 2.5201 -0.0264 -0.0736 0.0528  200 PRO F O   
15922 C CB  . PRO F 200 ? 2.0255 2.3568 2.4922 -0.0171 -0.0680 0.0521  200 PRO F CB  
15923 C CG  . PRO F 200 ? 2.0020 2.3275 2.4509 -0.0106 -0.0669 0.0464  200 PRO F CG  
15924 C CD  . PRO F 200 ? 2.0155 2.3338 2.4575 -0.0118 -0.0747 0.0371  200 PRO F CD  
15925 N N   . LYS F 201 ? 1.7741 2.0607 2.2365 -0.0167 -0.0746 0.0404  201 LYS F N   
15926 C CA  . LYS F 201 ? 1.6746 1.9459 2.1415 -0.0168 -0.0740 0.0409  201 LYS F CA  
15927 C C   . LYS F 201 ? 1.6353 1.8977 2.1118 -0.0234 -0.0813 0.0368  201 LYS F C   
15928 O O   . LYS F 201 ? 1.5871 1.8432 2.0754 -0.0268 -0.0808 0.0409  201 LYS F O   
15929 C CB  . LYS F 201 ? 1.6817 1.9382 2.1332 -0.0097 -0.0720 0.0347  201 LYS F CB  
15930 C CG  . LYS F 201 ? 1.6879 1.9505 2.1347 -0.0034 -0.0637 0.0403  201 LYS F CG  
15931 C CD  . LYS F 201 ? 1.6702 1.9181 2.1033 0.0034  -0.0613 0.0338  201 LYS F CD  
15932 C CE  . LYS F 201 ? 1.6244 1.8790 2.0550 0.0095  -0.0531 0.0395  201 LYS F CE  
15933 N NZ  . LYS F 201 ? 1.6101 1.8511 2.0287 0.0163  -0.0501 0.0332  201 LYS F NZ  
15934 N N   . ILE F 202 ? 1.6628 1.9244 2.1347 -0.0254 -0.0883 0.0287  202 ILE F N   
15935 C CA  . ILE F 202 ? 1.6115 1.8663 2.0935 -0.0321 -0.0959 0.0244  202 ILE F CA  
15936 C C   . ILE F 202 ? 1.6853 1.9567 2.1844 -0.0392 -0.0972 0.0302  202 ILE F C   
15937 O O   . ILE F 202 ? 1.7356 2.0033 2.2485 -0.0458 -0.1012 0.0302  202 ILE F O   
15938 C CB  . ILE F 202 ? 1.5307 1.7760 2.0000 -0.0310 -0.1039 0.0125  202 ILE F CB  
15939 C CG1 . ILE F 202 ? 1.5581 1.7919 2.0071 -0.0229 -0.1010 0.0072  202 ILE F CG1 
15940 C CG2 . ILE F 202 ? 1.6078 1.8399 2.0853 -0.0365 -0.1115 0.0066  202 ILE F CG2 
15941 C CD1 . ILE F 202 ? 1.5444 1.7690 1.9784 -0.0214 -0.1083 -0.0040 202 ILE F CD1 
15942 N N   . ALA F 203 ? 1.7039 1.9935 2.2028 -0.0382 -0.0937 0.0351  203 ALA F N   
15943 C CA  . ALA F 203 ? 1.7286 2.0350 2.2437 -0.0446 -0.0941 0.0406  203 ALA F CA  
15944 C C   . ALA F 203 ? 1.8201 2.1290 2.3494 -0.0484 -0.0885 0.0507  203 ALA F C   
15945 O O   . ALA F 203 ? 1.9613 2.2746 2.5066 -0.0557 -0.0905 0.0533  203 ALA F O   
15946 C CB  . ALA F 203 ? 1.6949 2.0193 2.2052 -0.0419 -0.0913 0.0428  203 ALA F CB  
15947 N N   . ALA F 204 ? 1.6921 1.9985 2.2162 -0.0437 -0.0816 0.0566  204 ALA F N   
15948 C CA  . ALA F 204 ? 1.7008 2.0074 2.2368 -0.0467 -0.0767 0.0664  204 ALA F CA  
15949 C C   . ALA F 204 ? 1.8061 2.0945 2.3492 -0.0504 -0.0803 0.0642  204 ALA F C   
15950 O O   . ALA F 204 ? 1.8788 2.1672 2.4352 -0.0553 -0.0780 0.0719  204 ALA F O   
15951 C CB  . ALA F 204 ? 1.7004 2.0078 2.2283 -0.0399 -0.0693 0.0727  204 ALA F CB  
15952 N N   . ALA F 205 ? 1.9141 2.1868 2.4486 -0.0483 -0.0859 0.0538  205 ALA F N   
15953 C CA  . ALA F 205 ? 1.9802 2.2349 2.5212 -0.0520 -0.0903 0.0500  205 ALA F CA  
15954 C C   . ALA F 205 ? 2.2270 2.4846 2.7808 -0.0604 -0.0974 0.0462  205 ALA F C   
15955 O O   . ALA F 205 ? 2.2310 2.4757 2.7940 -0.0652 -0.1009 0.0443  205 ALA F O   
15956 C CB  . ALA F 205 ? 1.8143 2.0504 2.3396 -0.0459 -0.0932 0.0398  205 ALA F CB  
15957 N N   . GLN F 206 ? 2.8597 3.1339 3.4151 -0.0623 -0.0995 0.0449  206 GLN F N   
15958 C CA  . GLN F 206 ? 2.8518 3.1313 3.4204 -0.0700 -0.1063 0.0412  206 GLN F CA  
15959 C C   . GLN F 206 ? 2.8839 3.1454 3.4492 -0.0711 -0.1152 0.0298  206 GLN F C   
15960 O O   . GLN F 206 ? 2.8906 3.1483 3.4701 -0.0784 -0.1203 0.0276  206 GLN F O   
15961 C CB  . GLN F 206 ? 2.8402 3.1269 3.4294 -0.0781 -0.1030 0.0505  206 GLN F CB  
15962 C CG  . GLN F 206 ? 2.8167 3.1203 3.4087 -0.0773 -0.0941 0.0623  206 GLN F CG  
15963 C CD  . GLN F 206 ? 2.7836 3.1089 3.3777 -0.0780 -0.0940 0.0624  206 GLN F CD  
15964 O OE1 . GLN F 206 ? 2.7760 3.1037 3.3593 -0.0739 -0.0980 0.0548  206 GLN F OE1 
15965 N NE2 . GLN F 206 ? 2.7686 3.1095 3.3764 -0.0833 -0.0893 0.0711  206 GLN F NE2 
15966 N N   . GLY F 207 ? 2.1723 2.4228 2.7186 -0.0639 -0.1170 0.0222  207 GLY F N   
15967 C CA  . GLY F 207 ? 2.0929 2.3256 2.6328 -0.0639 -0.1252 0.0107  207 GLY F CA  
15968 C C   . GLY F 207 ? 2.0661 2.3024 2.5934 -0.0612 -0.1318 0.0018  207 GLY F C   
15969 O O   . GLY F 207 ? 2.0526 2.2741 2.5677 -0.0588 -0.1379 -0.0083 207 GLY F O   
15970 N N   . LEU F 208 ? 1.9648 2.2205 2.4945 -0.0614 -0.1306 0.0054  208 LEU F N   
15971 C CA  . LEU F 208 ? 1.8454 2.1063 2.3641 -0.0587 -0.1366 -0.0017 208 LEU F CA  
15972 C C   . LEU F 208 ? 1.7859 2.0631 2.3214 -0.0652 -0.1416 -0.0012 208 LEU F C   
15973 O O   . LEU F 208 ? 1.7991 2.0851 2.3540 -0.0716 -0.1391 0.0053  208 LEU F O   
15974 C CB  . LEU F 208 ? 1.7563 2.0246 2.2590 -0.0511 -0.1302 0.0012  208 LEU F CB  
15975 C CG  . LEU F 208 ? 1.6336 1.9127 2.1407 -0.0496 -0.1195 0.0126  208 LEU F CG  
15976 C CD1 . LEU F 208 ? 1.7339 2.0312 2.2614 -0.0561 -0.1176 0.0203  208 LEU F CD1 
15977 C CD2 . LEU F 208 ? 1.5228 1.8078 2.0132 -0.0421 -0.1148 0.0134  208 LEU F CD2 
15978 N N   . TYR F 209 ? 1.8041 2.0851 2.3317 -0.0634 -0.1487 -0.0082 209 TYR F N   
15979 C CA  . TYR F 209 ? 1.7286 2.0259 2.2710 -0.0683 -0.1540 -0.0088 209 TYR F CA  
15980 C C   . TYR F 209 ? 1.8100 2.1134 2.3376 -0.0628 -0.1576 -0.0131 209 TYR F C   
15981 O O   . TYR F 209 ? 2.0789 2.3714 2.5851 -0.0562 -0.1576 -0.0171 209 TYR F O   
15982 C CB  . TYR F 209 ? 1.7577 2.0483 2.3133 -0.0752 -0.1636 -0.0155 209 TYR F CB  
15983 C CG  . TYR F 209 ? 1.9032 2.1762 2.4426 -0.0722 -0.1729 -0.0270 209 TYR F CG  
15984 C CD1 . TYR F 209 ? 1.9182 2.1948 2.4519 -0.0710 -0.1824 -0.0344 209 TYR F CD1 
15985 C CD2 . TYR F 209 ? 1.9550 2.2074 2.4841 -0.0702 -0.1723 -0.0305 209 TYR F CD2 
15986 C CE1 . TYR F 209 ? 1.9677 2.2279 2.4851 -0.0681 -0.1910 -0.0448 209 TYR F CE1 
15987 C CE2 . TYR F 209 ? 2.0188 2.2549 2.5317 -0.0673 -0.1805 -0.0413 209 TYR F CE2 
15988 C CZ  . TYR F 209 ? 2.0216 2.2616 2.5283 -0.0664 -0.1899 -0.0484 209 TYR F CZ  
15989 O OH  . TYR F 209 ? 2.0383 2.2620 2.5277 -0.0635 -0.1983 -0.0591 209 TYR F OH  
15990 N N   . MET F 211 ? 1.7309 2.0628 2.2532 -0.0590 -0.1817 -0.0280 211 MET F N   
15991 C CA  . MET F 211 ? 1.6880 2.0259 2.2173 -0.0609 -0.1932 -0.0346 211 MET F CA  
15992 C C   . MET F 211 ? 1.7227 2.0739 2.2464 -0.0562 -0.1929 -0.0330 211 MET F C   
15993 O O   . MET F 211 ? 1.7512 2.1003 2.2576 -0.0502 -0.1866 -0.0300 211 MET F O   
15994 C CB  . MET F 211 ? 1.6720 1.9909 2.1865 -0.0594 -0.2041 -0.0449 211 MET F CB  
15995 C CG  . MET F 211 ? 1.6228 1.9465 2.1450 -0.0615 -0.2174 -0.0523 211 MET F CG  
15996 S SD  . MET F 211 ? 1.6376 1.9385 2.1372 -0.0584 -0.2300 -0.0644 211 MET F SD  
15997 C CE  . MET F 211 ? 1.6707 1.9830 2.1813 -0.0600 -0.2447 -0.0707 211 MET F CE  
15998 N N   . VAL F 212 ? 1.7849 2.1500 2.3243 -0.0590 -0.1997 -0.0351 212 VAL F N   
15999 C CA  . VAL F 212 ? 1.8619 2.2405 2.3989 -0.0549 -0.2004 -0.0340 212 VAL F CA  
16000 C C   . VAL F 212 ? 2.1142 2.4826 2.6336 -0.0501 -0.2118 -0.0423 212 VAL F C   
16001 O O   . VAL F 212 ? 2.1163 2.4761 2.6373 -0.0525 -0.2224 -0.0496 212 VAL F O   
16002 C CB  . VAL F 212 ? 1.7566 2.1567 2.3210 -0.0600 -0.2011 -0.0317 212 VAL F CB  
16003 C CG1 . VAL F 212 ? 1.8063 2.2203 2.3687 -0.0553 -0.2010 -0.0305 212 VAL F CG1 
16004 C CG2 . VAL F 212 ? 1.6220 2.0308 2.2032 -0.0653 -0.1901 -0.0236 212 VAL F CG2 
16005 N N   . LEU F 213 ? 2.7787 3.1476 3.2808 -0.0435 -0.2098 -0.0410 213 LEU F N   
16006 C CA  . LEU F 213 ? 2.8117 3.1703 3.2944 -0.0385 -0.2199 -0.0477 213 LEU F CA  
16007 C C   . LEU F 213 ? 2.7987 3.1713 3.2946 -0.0388 -0.2291 -0.0504 213 LEU F C   
16008 O O   . LEU F 213 ? 2.7686 3.1567 3.2724 -0.0374 -0.2243 -0.0456 213 LEU F O   
16009 C CB  . LEU F 213 ? 2.8137 3.1656 3.2715 -0.0315 -0.2134 -0.0449 213 LEU F CB  
16010 C CG  . LEU F 213 ? 2.8352 3.1769 3.2712 -0.0259 -0.2227 -0.0506 213 LEU F CG  
16011 C CD1 . LEU F 213 ? 2.8642 3.1869 3.2877 -0.0265 -0.2315 -0.0585 213 LEU F CD1 
16012 C CD2 . LEU F 213 ? 2.8306 3.1680 3.2448 -0.0196 -0.2147 -0.0466 213 LEU F CD2 
16013 N N   . PRO F 214 ? 2.8451 3.2128 3.3440 -0.0405 -0.2423 -0.0582 214 PRO F N   
16014 C CA  . PRO F 214 ? 2.8227 3.2041 3.3352 -0.0404 -0.2518 -0.0610 214 PRO F CA  
16015 C C   . PRO F 214 ? 2.7743 3.1495 3.2651 -0.0331 -0.2586 -0.0638 214 PRO F C   
16016 O O   . PRO F 214 ? 2.7611 3.1368 3.2543 -0.0323 -0.2716 -0.0698 214 PRO F O   
16017 C CB  . PRO F 214 ? 2.8151 3.1936 3.3420 -0.0461 -0.2629 -0.0681 214 PRO F CB  
16018 C CG  . PRO F 214 ? 2.8005 3.1563 3.3064 -0.0454 -0.2641 -0.0719 214 PRO F CG  
16019 C CD  . PRO F 214 ? 2.7953 3.1464 3.2891 -0.0432 -0.2493 -0.0647 214 PRO F CD  
16020 N N   . GLY F 215 ? 2.7141 3.0833 3.1840 -0.0277 -0.2504 -0.0595 215 GLY F N   
16021 C CA  . GLY F 215 ? 2.6688 3.0306 3.1164 -0.0210 -0.2560 -0.0615 215 GLY F CA  
16022 C C   . GLY F 215 ? 2.6523 3.0188 3.0898 -0.0163 -0.2454 -0.0547 215 GLY F C   
16023 O O   . GLY F 215 ? 2.6683 3.0482 3.1202 -0.0183 -0.2349 -0.0486 215 GLY F O   
16024 N N   . PHE F 216 ? 2.1552 2.5104 2.5677 -0.0103 -0.2481 -0.0557 216 PHE F N   
16025 C CA  . PHE F 216 ? 2.0794 2.4380 2.4813 -0.0057 -0.2391 -0.0498 216 PHE F CA  
16026 C C   . PHE F 216 ? 2.2290 2.5764 2.6136 -0.0046 -0.2275 -0.0464 216 PHE F C   
16027 O O   . PHE F 216 ? 2.1475 2.4797 2.5199 -0.0053 -0.2286 -0.0498 216 PHE F O   
16028 C CB  . PHE F 216 ? 1.8265 2.1788 2.2108 0.0001  -0.2476 -0.0520 216 PHE F CB  
16029 C CG  . PHE F 216 ? 1.7819 2.1126 2.1386 0.0028  -0.2541 -0.0568 216 PHE F CG  
16030 C CD1 . PHE F 216 ? 1.7417 2.0652 2.0984 0.0014  -0.2675 -0.0640 216 PHE F CD1 
16031 C CD2 . PHE F 216 ? 1.8352 2.1528 2.1659 0.0068  -0.2467 -0.0543 216 PHE F CD2 
16032 C CE1 . PHE F 216 ? 1.7126 2.0159 2.0427 0.0040  -0.2735 -0.0688 216 PHE F CE1 
16033 C CE2 . PHE F 216 ? 1.7963 2.0941 2.1008 0.0094  -0.2521 -0.0589 216 PHE F CE2 
16034 C CZ  . PHE F 216 ? 1.7491 2.0395 2.0527 0.0081  -0.2655 -0.0661 216 PHE F CZ  
16035 N N   . TRP F 217 ? 2.8298 3.1851 3.2140 -0.0028 -0.2163 -0.0398 217 TRP F N   
16036 C CA  . TRP F 217 ? 2.8488 3.1958 3.2183 -0.0013 -0.2047 -0.0360 217 TRP F CA  
16037 C C   . TRP F 217 ? 2.8440 3.1922 3.1997 0.0037  -0.1992 -0.0319 217 TRP F C   
16038 O O   . TRP F 217 ? 2.8177 3.1800 3.1848 0.0044  -0.1987 -0.0292 217 TRP F O   
16039 C CB  . TRP F 217 ? 2.8329 3.1899 3.2208 -0.0056 -0.1945 -0.0312 217 TRP F CB  
16040 C CG  . TRP F 217 ? 2.8453 3.1944 3.2201 -0.0040 -0.1829 -0.0273 217 TRP F CG  
16041 C CD1 . TRP F 217 ? 2.8771 3.2115 3.2415 -0.0044 -0.1809 -0.0295 217 TRP F CD1 
16042 C CD2 . TRP F 217 ? 2.8376 3.1938 3.2093 -0.0015 -0.1718 -0.0209 217 TRP F CD2 
16043 N NE1 . TRP F 217 ? 2.8897 3.2219 3.2452 -0.0022 -0.1693 -0.0248 217 TRP F NE1 
16044 C CE2 . TRP F 217 ? 2.8595 3.2050 3.2193 -0.0005 -0.1637 -0.0194 217 TRP F CE2 
16045 C CE3 . TRP F 217 ? 2.8172 3.1877 3.1954 0.0000  -0.1682 -0.0167 217 TRP F CE3 
16046 C CZ2 . TRP F 217 ? 2.8517 3.2009 3.2064 0.0018  -0.1524 -0.0137 217 TRP F CZ2 
16047 C CZ3 . TRP F 217 ? 2.7961 3.1696 3.1685 0.0021  -0.1570 -0.0112 217 TRP F CZ3 
16048 C CH2 . TRP F 217 ? 2.8215 3.1847 3.1826 0.0029  -0.1494 -0.0097 217 TRP F CH2 
16049 N N   . MET F 218 ? 2.3520 2.6853 2.6835 0.0071  -0.1948 -0.0318 218 MET F N   
16050 C CA  . MET F 218 ? 2.1652 2.4976 2.4818 0.0116  -0.1893 -0.0281 218 MET F CA  
16051 C C   . MET F 218 ? 2.0959 2.4162 2.3942 0.0134  -0.1795 -0.0264 218 MET F C   
16052 O O   . MET F 218 ? 1.9672 2.2719 2.2505 0.0138  -0.1823 -0.0307 218 MET F O   
16053 C CB  . MET F 218 ? 1.9435 2.2681 2.2449 0.0154  -0.1998 -0.0314 218 MET F CB  
16054 C CG  . MET F 218 ? 1.8906 2.2110 2.1738 0.0199  -0.1944 -0.0277 218 MET F CG  
16055 S SD  . MET F 218 ? 1.8174 2.1583 2.1186 0.0202  -0.1868 -0.0213 218 MET F SD  
16056 C CE  . MET F 218 ? 1.6438 1.9959 1.9633 0.0197  -0.2000 -0.0245 218 MET F CE  
16057 N N   . ASP F 219 ? 2.0308 2.3586 2.3305 0.0144  -0.1683 -0.0206 219 ASP F N   
16058 C CA  . ASP F 219 ? 1.9859 2.3044 2.2698 0.0164  -0.1582 -0.0185 219 ASP F CA  
16059 C C   . ASP F 219 ? 1.9513 2.2622 2.2137 0.0208  -0.1575 -0.0178 219 ASP F C   
16060 O O   . ASP F 219 ? 1.9515 2.2720 2.2175 0.0221  -0.1537 -0.0136 219 ASP F O   
16061 C CB  . ASP F 219 ? 2.0559 2.3871 2.3545 0.0148  -0.1467 -0.0125 219 ASP F CB  
16062 C CG  . ASP F 219 ? 1.9936 2.3156 2.2796 0.0164  -0.1368 -0.0110 219 ASP F CG  
16063 O OD1 . ASP F 219 ? 1.8589 2.1702 2.1239 0.0199  -0.1346 -0.0118 219 ASP F OD1 
16064 O OD2 . ASP F 219 ? 2.1055 2.4312 2.4028 0.0141  -0.1310 -0.0090 219 ASP F OD2 
16065 N N   . ILE F 220 ? 1.8408 2.1341 2.0806 0.0230  -0.1611 -0.0219 220 ILE F N   
16066 C CA  . ILE F 220 ? 1.8279 2.1118 2.0449 0.0270  -0.1608 -0.0213 220 ILE F CA  
16067 C C   . ILE F 220 ? 1.7742 2.0544 1.9806 0.0285  -0.1475 -0.0179 220 ILE F C   
16068 O O   . ILE F 220 ? 1.7012 1.9695 1.8953 0.0290  -0.1441 -0.0204 220 ILE F O   
16069 C CB  . ILE F 220 ? 1.8274 2.0941 2.0239 0.0286  -0.1711 -0.0272 220 ILE F CB  
16070 C CG1 . ILE F 220 ? 1.8551 2.1265 2.0639 0.0272  -0.1849 -0.0308 220 ILE F CG1 
16071 C CG2 . ILE F 220 ? 2.0146 2.2708 2.1864 0.0326  -0.1699 -0.0258 220 ILE F CG2 
16072 C CD1 . ILE F 220 ? 1.7940 2.0649 2.0153 0.0235  -0.1899 -0.0355 220 ILE F CD1 
16073 N N   . GLY F 221 ? 1.7252 2.0158 1.9370 0.0292  -0.1401 -0.0124 221 GLY F N   
16074 C CA  . GLY F 221 ? 1.6955 1.9844 1.8989 0.0306  -0.1278 -0.0090 221 GLY F CA  
16075 C C   . GLY F 221 ? 1.6133 1.9016 1.8049 0.0332  -0.1248 -0.0057 221 GLY F C   
16076 O O   . GLY F 221 ? 1.6182 1.9077 1.8053 0.0341  -0.1143 -0.0023 221 GLY F O   
16077 N N   . GLN F 222 ? 1.5989 1.8851 1.7857 0.0343  -0.1341 -0.0068 222 GLN F N   
16078 C CA  . GLN F 222 ? 1.5985 1.8831 1.7744 0.0366  -0.1327 -0.0037 222 GLN F CA  
16079 C C   . GLN F 222 ? 1.6370 1.9102 1.7982 0.0385  -0.1446 -0.0068 222 GLN F C   
16080 O O   . GLN F 222 ? 1.6776 1.9516 1.8464 0.0376  -0.1550 -0.0105 222 GLN F O   
16081 C CB  . GLN F 222 ? 1.6454 1.9479 1.8415 0.0358  -0.1301 0.0004  222 GLN F CB  
16082 C CG  . GLN F 222 ? 1.6862 2.0001 1.9027 0.0342  -0.1393 -0.0013 222 GLN F CG  
16083 C CD  . GLN F 222 ? 1.6973 2.0300 1.9351 0.0331  -0.1347 0.0025  222 GLN F CD  
16084 O OE1 . GLN F 222 ? 1.6962 2.0347 1.9366 0.0328  -0.1243 0.0062  222 GLN F OE1 
16085 N NE2 . GLN F 222 ? 1.7117 2.0544 1.9651 0.0325  -0.1425 0.0013  222 GLN F NE2 
16086 N N   . PRO F 223 ? 1.6438 1.9062 1.7839 0.0411  -0.1436 -0.0052 223 PRO F N   
16087 C CA  . PRO F 223 ? 1.7546 2.0042 1.8778 0.0433  -0.1553 -0.0078 223 PRO F CA  
16088 C C   . PRO F 223 ? 1.8506 2.1093 1.9887 0.0436  -0.1662 -0.0081 223 PRO F C   
16089 O O   . PRO F 223 ? 1.9987 2.2492 2.1285 0.0450  -0.1782 -0.0115 223 PRO F O   
16090 C CB  . PRO F 223 ? 1.6718 1.9100 1.7716 0.0455  -0.1495 -0.0045 223 PRO F CB  
16091 C CG  . PRO F 223 ? 1.5758 1.8256 1.6870 0.0445  -0.1367 0.0003  223 PRO F CG  
16092 C CD  . PRO F 223 ? 1.5725 1.8328 1.7022 0.0420  -0.1318 -0.0009 223 PRO F CD  
16093 N N   . ARG F 224 ? 1.7449 2.0203 1.9045 0.0427  -0.1627 -0.0049 224 ARG F N   
16094 C CA  . ARG F 224 ? 1.7752 2.0600 1.9499 0.0433  -0.1725 -0.0055 224 ARG F CA  
16095 C C   . ARG F 224 ? 1.9272 2.2200 2.1205 0.0410  -0.1806 -0.0098 224 ARG F C   
16096 O O   . ARG F 224 ? 2.0451 2.3433 2.2487 0.0418  -0.1909 -0.0116 224 ARG F O   
16097 C CB  . ARG F 224 ? 1.7068 2.0069 1.8978 0.0431  -0.1657 -0.0012 224 ARG F CB  
16098 C CG  . ARG F 224 ? 1.7192 2.0342 1.9299 0.0399  -0.1560 0.0004  224 ARG F CG  
16099 C CD  . ARG F 224 ? 1.6811 2.0098 1.9048 0.0400  -0.1494 0.0044  224 ARG F CD  
16100 N NE  . ARG F 224 ? 1.6748 1.9948 1.8810 0.0421  -0.1440 0.0076  224 ARG F NE  
16101 C CZ  . ARG F 224 ? 1.7396 2.0556 1.9362 0.0416  -0.1330 0.0102  224 ARG F CZ  
16102 N NH1 . ARG F 224 ? 1.7695 2.0894 1.9720 0.0395  -0.1265 0.0099  224 ARG F NH1 
16103 N NH2 . ARG F 224 ? 1.7313 2.0396 1.9129 0.0432  -0.1287 0.0131  224 ARG F NH2 
16104 N N   . ASP F 225 ? 1.9797 2.2734 2.1783 0.0383  -0.1763 -0.0115 225 ASP F N   
16105 C CA  . ASP F 225 ? 2.0612 2.3614 2.2772 0.0357  -0.1839 -0.0156 225 ASP F CA  
16106 C C   . ASP F 225 ? 2.3143 2.6008 2.5169 0.0367  -0.1966 -0.0211 225 ASP F C   
16107 O O   . ASP F 225 ? 2.2553 2.5466 2.4722 0.0345  -0.2045 -0.0250 225 ASP F O   
16108 C CB  . ASP F 225 ? 1.9077 2.2125 2.1339 0.0323  -0.1753 -0.0154 225 ASP F CB  
16109 C CG  . ASP F 225 ? 1.8326 2.1549 2.0788 0.0306  -0.1656 -0.0106 225 ASP F CG  
16110 O OD1 . ASP F 225 ? 1.8100 2.1420 2.0642 0.0317  -0.1661 -0.0082 225 ASP F OD1 
16111 O OD2 . ASP F 225 ? 1.7649 2.0911 2.0186 0.0282  -0.1577 -0.0094 225 ASP F OD2 
16112 N N   . TYR F 226 ? 3.1491 3.4187 3.3245 0.0398  -0.1988 -0.0214 226 TYR F N   
16113 C CA  . TYR F 226 ? 3.1800 3.4357 3.3405 0.0409  -0.2111 -0.0268 226 TYR F CA  
16114 C C   . TYR F 226 ? 3.1615 3.4222 3.3312 0.0423  -0.2250 -0.0286 226 TYR F C   
16115 O O   . TYR F 226 ? 3.1631 3.4196 3.3333 0.0419  -0.2366 -0.0338 226 TYR F O   
16116 C CB  . TYR F 226 ? 3.2278 3.4639 3.3553 0.0438  -0.2090 -0.0263 226 TYR F CB  
16117 C CG  . TYR F 226 ? 3.2587 3.4851 3.3736 0.0426  -0.2006 -0.0282 226 TYR F CG  
16118 C CD1 . TYR F 226 ? 3.2583 3.4857 3.3835 0.0398  -0.2027 -0.0329 226 TYR F CD1 
16119 C CD2 . TYR F 226 ? 3.2877 3.5037 3.3809 0.0443  -0.1904 -0.0254 226 TYR F CD2 
16120 C CE1 . TYR F 226 ? 3.2847 3.5028 3.3988 0.0391  -0.1952 -0.0349 226 TYR F CE1 
16121 C CE2 . TYR F 226 ? 3.3129 3.5204 3.3953 0.0436  -0.1825 -0.0274 226 TYR F CE2 
16122 C CZ  . TYR F 226 ? 3.3094 3.5179 3.4023 0.0412  -0.1851 -0.0323 226 TYR F CZ  
16123 O OH  . TYR F 226 ? 3.3347 3.5344 3.4174 0.0408  -0.1774 -0.0346 226 TYR F OH  
16124 N N   . ILE F 227 ? 2.6973 2.9667 2.8748 0.0442  -0.2242 -0.0246 227 ILE F N   
16125 C CA  . ILE F 227 ? 2.6433 2.9176 2.8303 0.0460  -0.2374 -0.0264 227 ILE F CA  
16126 C C   . ILE F 227 ? 2.5804 2.8738 2.7998 0.0429  -0.2403 -0.0285 227 ILE F C   
16127 O O   . ILE F 227 ? 2.5310 2.8273 2.7600 0.0431  -0.2530 -0.0326 227 ILE F O   
16128 C CB  . ILE F 227 ? 2.5923 2.8675 2.7747 0.0496  -0.2363 -0.0217 227 ILE F CB  
16129 C CG1 . ILE F 227 ? 2.5559 2.8454 2.7538 0.0481  -0.2227 -0.0170 227 ILE F CG1 
16130 C CG2 . ILE F 227 ? 2.5524 2.8072 2.7017 0.0527  -0.2358 -0.0198 227 ILE F CG2 
16131 C CD1 . ILE F 227 ? 2.4744 2.7645 2.6682 0.0512  -0.2207 -0.0126 227 ILE F CD1 
16132 N N   . THR F 228 ? 2.3051 2.6117 2.5419 0.0397  -0.2289 -0.0259 228 THR F N   
16133 C CA  . THR F 228 ? 2.1386 2.4631 2.4054 0.0362  -0.2304 -0.0276 228 THR F CA  
16134 C C   . THR F 228 ? 2.0461 2.3672 2.3166 0.0324  -0.2326 -0.0318 228 THR F C   
16135 O O   . THR F 228 ? 1.9345 2.2660 2.2261 0.0297  -0.2391 -0.0349 228 THR F O   
16136 C CB  . THR F 228 ? 2.0047 2.3452 2.2884 0.0345  -0.2176 -0.0227 228 THR F CB  
16137 O OG1 . THR F 228 ? 1.9188 2.2766 2.2310 0.0309  -0.2188 -0.0241 228 THR F OG1 
16138 C CG2 . THR F 228 ? 1.9723 2.3071 2.2452 0.0330  -0.2047 -0.0198 228 THR F CG2 
16139 N N   . GLY F 229 ? 2.1252 2.4322 2.3763 0.0321  -0.2270 -0.0320 229 GLY F N   
16140 C CA  . GLY F 229 ? 1.9866 2.2879 2.2389 0.0289  -0.2300 -0.0366 229 GLY F CA  
16141 C C   . GLY F 229 ? 1.9798 2.2697 2.2216 0.0302  -0.2451 -0.0428 229 GLY F C   
16142 O O   . GLY F 229 ? 1.9007 2.1907 2.1521 0.0270  -0.2514 -0.0476 229 GLY F O   
16143 N N   . LEU F 230 ? 2.0689 2.3487 2.2909 0.0346  -0.2515 -0.0426 230 LEU F N   
16144 C CA  . LEU F 230 ? 1.9916 2.2610 2.2031 0.0362  -0.2670 -0.0482 230 LEU F CA  
16145 C C   . LEU F 230 ? 1.9986 2.2826 2.2362 0.0352  -0.2782 -0.0509 230 LEU F C   
16146 O O   . LEU F 230 ? 1.9078 2.1876 2.1463 0.0345  -0.2909 -0.0567 230 LEU F O   
16147 C CB  . LEU F 230 ? 1.9526 2.2071 2.1355 0.0414  -0.2705 -0.0464 230 LEU F CB  
16148 C CG  . LEU F 230 ? 1.6884 1.9287 1.8536 0.0438  -0.2862 -0.0517 230 LEU F CG  
16149 C CD1 . LEU F 230 ? 1.6193 1.8382 1.7489 0.0461  -0.2831 -0.0517 230 LEU F CD1 
16150 C CD2 . LEU F 230 ? 1.5836 1.8282 1.7527 0.0476  -0.2969 -0.0505 230 LEU F CD2 
16151 N N   . ARG F 231 ? 2.3765 2.6780 2.6356 0.0350  -0.2737 -0.0470 231 ARG F N   
16152 C CA  . ARG F 231 ? 2.3404 2.6580 2.6273 0.0336  -0.2827 -0.0496 231 ARG F CA  
16153 C C   . ARG F 231 ? 2.3294 2.6543 2.6362 0.0279  -0.2831 -0.0533 231 ARG F C   
16154 O O   . ARG F 231 ? 2.3219 2.6489 2.6394 0.0265  -0.2954 -0.0587 231 ARG F O   
16155 C CB  . ARG F 231 ? 2.3076 2.6424 2.6127 0.0345  -0.2758 -0.0448 231 ARG F CB  
16156 C CG  . ARG F 231 ? 2.2738 2.6278 2.6105 0.0328  -0.2826 -0.0472 231 ARG F CG  
16157 C CD  . ARG F 231 ? 2.3502 2.6994 2.6856 0.0350  -0.3001 -0.0528 231 ARG F CD  
16158 N NE  . ARG F 231 ? 2.4307 2.7940 2.7854 0.0376  -0.3070 -0.0531 231 ARG F NE  
16159 C CZ  . ARG F 231 ? 2.3551 2.7170 2.7121 0.0402  -0.3226 -0.0575 231 ARG F CZ  
16160 N NH1 . ARG F 231 ? 2.2764 2.6231 2.6168 0.0405  -0.3331 -0.0619 231 ARG F NH1 
16161 N NH2 . ARG F 231 ? 2.3397 2.7152 2.7156 0.0428  -0.3278 -0.0577 231 ARG F NH2 
16162 N N   . LEU F 232 ? 2.0040 2.3327 2.3164 0.0244  -0.2699 -0.0504 232 LEU F N   
16163 C CA  . LEU F 232 ? 1.8591 2.1935 2.1898 0.0187  -0.2694 -0.0533 232 LEU F CA  
16164 C C   . LEU F 232 ? 1.8800 2.1979 2.1963 0.0178  -0.2790 -0.0597 232 LEU F C   
16165 O O   . LEU F 232 ? 1.8588 2.1812 2.1919 0.0137  -0.2856 -0.0642 232 LEU F O   
16166 C CB  . LEU F 232 ? 1.6818 2.0201 2.0166 0.0158  -0.2535 -0.0484 232 LEU F CB  
16167 C CG  . LEU F 232 ? 1.5344 1.8897 1.8843 0.0160  -0.2432 -0.0422 232 LEU F CG  
16168 C CD1 . LEU F 232 ? 1.5742 1.9321 1.9273 0.0130  -0.2288 -0.0379 232 LEU F CD1 
16169 C CD2 . LEU F 232 ? 1.4257 1.8002 1.8049 0.0138  -0.2486 -0.0433 232 LEU F CD2 
16170 N N   . TYR F 233 ? 1.9841 2.2831 2.2696 0.0215  -0.2796 -0.0604 233 TYR F N   
16171 C CA  . TYR F 233 ? 2.0261 2.3086 2.2955 0.0212  -0.2890 -0.0670 233 TYR F CA  
16172 C C   . TYR F 233 ? 2.0190 2.3012 2.2905 0.0228  -0.3065 -0.0721 233 TYR F C   
16173 O O   . TYR F 233 ? 2.0026 2.2840 2.2834 0.0197  -0.3161 -0.0783 233 TYR F O   
16174 C CB  . TYR F 233 ? 2.0769 2.3397 2.3118 0.0248  -0.2838 -0.0661 233 TYR F CB  
16175 C CG  . TYR F 233 ? 2.1437 2.3884 2.3586 0.0251  -0.2938 -0.0733 233 TYR F CG  
16176 C CD1 . TYR F 233 ? 2.1829 2.4224 2.4011 0.0212  -0.2924 -0.0776 233 TYR F CD1 
16177 C CD2 . TYR F 233 ? 2.1171 2.3494 2.3093 0.0295  -0.3049 -0.0757 233 TYR F CD2 
16178 C CE1 . TYR F 233 ? 2.1740 2.3968 2.3738 0.0215  -0.3017 -0.0848 233 TYR F CE1 
16179 C CE2 . TYR F 233 ? 2.1151 2.3308 2.2879 0.0299  -0.3144 -0.0825 233 TYR F CE2 
16180 C CZ  . TYR F 233 ? 2.1235 2.3347 2.3003 0.0259  -0.3126 -0.0873 233 TYR F CZ  
16181 O OH  . TYR F 233 ? 2.1256 2.3200 2.2827 0.0263  -0.3221 -0.0947 233 TYR F OH  
16182 N N   . LEU F 234 ? 1.9915 2.2737 2.2546 0.0277  -0.3112 -0.0698 234 LEU F N   
16183 C CA  . LEU F 234 ? 1.9265 2.2084 2.1915 0.0300  -0.3284 -0.0743 234 LEU F CA  
16184 C C   . LEU F 234 ? 1.9637 2.2659 2.2648 0.0264  -0.3341 -0.0766 234 LEU F C   
16185 O O   . LEU F 234 ? 1.9140 2.2166 2.2220 0.0262  -0.3489 -0.0824 234 LEU F O   
16186 C CB  . LEU F 234 ? 1.7679 2.0454 2.0168 0.0362  -0.3314 -0.0705 234 LEU F CB  
16187 C CG  . LEU F 234 ? 1.6490 1.9041 1.8593 0.0402  -0.3308 -0.0696 234 LEU F CG  
16188 C CD1 . LEU F 234 ? 1.5361 1.7875 1.7339 0.0460  -0.3369 -0.0663 234 LEU F CD1 
16189 C CD2 . LEU F 234 ? 1.6492 1.8888 1.8429 0.0394  -0.3410 -0.0767 234 LEU F CD2 
16190 N N   . ASP F 235 ? 2.1243 2.4438 2.4488 0.0237  -0.3228 -0.0721 235 ASP F N   
16191 C CA  . ASP F 235 ? 2.0966 2.4360 2.4559 0.0197  -0.3265 -0.0741 235 ASP F CA  
16192 C C   . ASP F 235 ? 2.0924 2.4300 2.4620 0.0138  -0.3305 -0.0796 235 ASP F C   
16193 O O   . ASP F 235 ? 2.0769 2.4218 2.4645 0.0118  -0.3424 -0.0849 235 ASP F O   
16194 C CB  . ASP F 235 ? 2.1283 2.4853 2.5075 0.0178  -0.3121 -0.0679 235 ASP F CB  
16195 C CG  . ASP F 235 ? 2.1898 2.5686 2.6047 0.0142  -0.3152 -0.0694 235 ASP F CG  
16196 O OD1 . ASP F 235 ? 2.1395 2.5210 2.5643 0.0142  -0.3293 -0.0749 235 ASP F OD1 
16197 O OD2 . ASP F 235 ? 2.2502 2.6437 2.6832 0.0113  -0.3034 -0.0651 235 ASP F OD2 
16198 N N   . SER F 236 ? 1.9793 2.3073 2.3382 0.0111  -0.3208 -0.0787 236 SER F N   
16199 C CA  . SER F 236 ? 1.8852 2.2090 2.2516 0.0057  -0.3244 -0.0841 236 SER F CA  
16200 C C   . SER F 236 ? 1.8589 2.1678 2.2092 0.0074  -0.3405 -0.0918 236 SER F C   
16201 O O   . SER F 236 ? 1.7889 2.0985 2.1524 0.0030  -0.3488 -0.0978 236 SER F O   
16202 C CB  . SER F 236 ? 1.8206 2.1354 2.1763 0.0036  -0.3107 -0.0814 236 SER F CB  
16203 O OG  . SER F 236 ? 1.6888 1.9987 2.0521 -0.0017 -0.3139 -0.0865 236 SER F OG  
16204 N N   . LEU F 237 ? 1.9619 2.2570 2.2836 0.0134  -0.3453 -0.0917 237 LEU F N   
16205 C CA  . LEU F 237 ? 1.9534 2.2341 2.2579 0.0154  -0.3612 -0.0988 237 LEU F CA  
16206 C C   . LEU F 237 ? 1.9175 2.2103 2.2429 0.0155  -0.3767 -0.1028 237 LEU F C   
16207 O O   . LEU F 237 ? 1.9164 2.2035 2.2418 0.0142  -0.3904 -0.1101 237 LEU F O   
16208 C CB  . LEU F 237 ? 1.9867 2.2495 2.2543 0.0219  -0.3617 -0.0969 237 LEU F CB  
16209 C CG  . LEU F 237 ? 2.0478 2.2894 2.2858 0.0221  -0.3576 -0.0994 237 LEU F CG  
16210 C CD1 . LEU F 237 ? 2.1051 2.3492 2.3493 0.0185  -0.3403 -0.0957 237 LEU F CD1 
16211 C CD2 . LEU F 237 ? 2.0814 2.3067 2.2838 0.0284  -0.3583 -0.0972 237 LEU F CD2 
16212 N N   . ARG F 238 ? 1.7905 2.1000 2.1341 0.0173  -0.3750 -0.0984 238 ARG F N   
16213 C CA  . ARG F 238 ? 1.6834 2.0071 2.0514 0.0173  -0.3886 -0.1021 238 ARG F CA  
16214 C C   . ARG F 238 ? 1.6787 2.0142 2.0768 0.0099  -0.3912 -0.1069 238 ARG F C   
16215 O O   . ARG F 238 ? 1.5877 1.9309 2.0029 0.0091  -0.4052 -0.1123 238 ARG F O   
16216 C CB  . ARG F 238 ? 1.6130 1.9533 1.9964 0.0203  -0.3838 -0.0964 238 ARG F CB  
16217 C CG  . ARG F 238 ? 1.4722 1.8111 1.8491 0.0268  -0.3980 -0.0977 238 ARG F CG  
16218 C CD  . ARG F 238 ? 1.5104 1.8249 1.8476 0.0317  -0.4038 -0.0984 238 ARG F CD  
16219 N NE  . ARG F 238 ? 1.4552 1.7629 1.7870 0.0339  -0.4235 -0.1051 238 ARG F NE  
16220 C CZ  . ARG F 238 ? 1.3664 1.6664 1.6815 0.0405  -0.4344 -0.1046 238 ARG F CZ  
16221 N NH1 . ARG F 238 ? 1.3528 1.6501 1.6547 0.0454  -0.4271 -0.0977 238 ARG F NH1 
16222 N NH2 . ARG F 238 ? 1.3118 1.6060 1.6229 0.0423  -0.4528 -0.1109 238 ARG F NH2 
16223 N N   . LYS F 239 ? 1.7534 2.0903 2.1585 0.0045  -0.3783 -0.1048 239 LYS F N   
16224 C CA  . LYS F 239 ? 1.7010 2.0477 2.1338 -0.0031 -0.3794 -0.1086 239 LYS F CA  
16225 C C   . LYS F 239 ? 1.7137 2.0426 2.1322 -0.0058 -0.3861 -0.1154 239 LYS F C   
16226 O O   . LYS F 239 ? 1.7178 2.0497 2.1517 -0.0095 -0.3982 -0.1222 239 LYS F O   
16227 C CB  . LYS F 239 ? 1.6828 2.0411 2.1325 -0.0075 -0.3616 -0.1022 239 LYS F CB  
16228 C CG  . LYS F 239 ? 1.7330 2.1031 2.1858 -0.0038 -0.3512 -0.0945 239 LYS F CG  
16229 C CD  . LYS F 239 ? 1.8067 2.1830 2.2670 -0.0075 -0.3331 -0.0880 239 LYS F CD  
16230 C CE  . LYS F 239 ? 1.9153 2.3028 2.3776 -0.0038 -0.3230 -0.0809 239 LYS F CE  
16231 N NZ  . LYS F 239 ? 1.9280 2.3089 2.3751 -0.0035 -0.3072 -0.0747 239 LYS F NZ  
16232 N N   . LYS F 240 ? 1.7140 2.0246 2.1037 -0.0041 -0.3784 -0.1140 240 LYS F N   
16233 C CA  . LYS F 240 ? 1.6746 1.9679 2.0503 -0.0067 -0.3831 -0.1206 240 LYS F CA  
16234 C C   . LYS F 240 ? 1.6975 1.9794 2.0575 -0.0035 -0.4019 -0.1283 240 LYS F C   
16235 O O   . LYS F 240 ? 1.6079 1.8909 1.9814 -0.0075 -0.4137 -0.1357 240 LYS F O   
16236 C CB  . LYS F 240 ? 1.6252 1.9022 1.9731 -0.0047 -0.3699 -0.1172 240 LYS F CB  
16237 C CG  . LYS F 240 ? 1.5416 1.8282 1.9040 -0.0080 -0.3519 -0.1100 240 LYS F CG  
16238 C CD  . LYS F 240 ? 1.4532 1.7498 1.8460 -0.0159 -0.3513 -0.1122 240 LYS F CD  
16239 C CE  . LYS F 240 ? 1.4169 1.7186 1.8186 -0.0190 -0.3336 -0.1053 240 LYS F CE  
16240 N NZ  . LYS F 240 ? 1.4471 1.7333 1.8187 -0.0145 -0.3234 -0.1020 240 LYS F NZ  
16241 N N   . SER F 241 ? 1.7866 2.0574 2.1178 0.0035  -0.4050 -0.1268 241 SER F N   
16242 C CA  . SER F 241 ? 1.7377 1.9964 2.0499 0.0073  -0.4228 -0.1332 241 SER F CA  
16243 C C   . SER F 241 ? 1.7659 2.0280 2.0693 0.0142  -0.4267 -0.1286 241 SER F C   
16244 O O   . SER F 241 ? 1.8573 2.1082 2.1332 0.0191  -0.4194 -0.1237 241 SER F O   
16245 C CB  . SER F 241 ? 1.8124 2.0465 2.0890 0.0089  -0.4230 -0.1372 241 SER F CB  
16246 O OG  . SER F 241 ? 1.9428 2.1694 2.2002 0.0111  -0.4062 -0.1306 241 SER F OG  
16247 N N   . PRO F 242 ? 1.6253 1.9025 1.9518 0.0147  -0.4380 -0.1301 242 PRO F N   
16248 C CA  . PRO F 242 ? 1.5808 1.8622 1.9018 0.0214  -0.4415 -0.1255 242 PRO F CA  
16249 C C   . PRO F 242 ? 1.6050 1.8678 1.8928 0.0278  -0.4550 -0.1281 242 PRO F C   
16250 O O   . PRO F 242 ? 1.5836 1.8458 1.8609 0.0337  -0.4565 -0.1233 242 PRO F O   
16251 C CB  . PRO F 242 ? 1.5044 1.8087 1.8641 0.0194  -0.4497 -0.1274 242 PRO F CB  
16252 C CG  . PRO F 242 ? 1.5081 1.8132 1.8828 0.0133  -0.4589 -0.1357 242 PRO F CG  
16253 C CD  . PRO F 242 ? 1.5829 1.8749 1.9435 0.0091  -0.4474 -0.1360 242 PRO F CD  
16254 N N   . ALA F 243 ? 1.6744 1.9218 1.9450 0.0267  -0.4649 -0.1353 243 ALA F N   
16255 C CA  . ALA F 243 ? 1.6972 1.9258 1.9339 0.0325  -0.4779 -0.1380 243 ALA F CA  
16256 C C   . ALA F 243 ? 1.8452 2.0537 2.0429 0.0358  -0.4668 -0.1338 243 ALA F C   
16257 O O   . ALA F 243 ? 1.8094 2.0007 1.9751 0.0406  -0.4756 -0.1352 243 ALA F O   
16258 C CB  . ALA F 243 ? 1.6037 1.8247 1.8388 0.0299  -0.4943 -0.1484 243 ALA F CB  
16259 N N   . LYS F 244 ? 2.1461 2.3566 2.3456 0.0332  -0.4477 -0.1287 244 LYS F N   
16260 C CA  . LYS F 244 ? 2.1785 2.3721 2.3440 0.0362  -0.4356 -0.1243 244 LYS F CA  
16261 C C   . LYS F 244 ? 2.1711 2.3675 2.3289 0.0413  -0.4284 -0.1153 244 LYS F C   
16262 O O   . LYS F 244 ? 2.1965 2.3789 2.3251 0.0442  -0.4192 -0.1112 244 LYS F O   
16263 C CB  . LYS F 244 ? 2.1868 2.3807 2.3579 0.0312  -0.4187 -0.1234 244 LYS F CB  
16264 C CG  . LYS F 244 ? 2.1954 2.3858 2.3751 0.0258  -0.4243 -0.1321 244 LYS F CG  
16265 C CD  . LYS F 244 ? 2.2412 2.4076 2.3844 0.0277  -0.4285 -0.1377 244 LYS F CD  
16266 C CE  . LYS F 244 ? 2.2865 2.4476 2.4278 0.0275  -0.4494 -0.1470 244 LYS F CE  
16267 N NZ  . LYS F 244 ? 2.3557 2.4928 2.4582 0.0301  -0.4545 -0.1525 244 LYS F NZ  
16268 N N   . LEU F 245 ? 1.9085 2.1225 2.0919 0.0423  -0.4321 -0.1124 245 LEU F N   
16269 C CA  . LEU F 245 ? 1.8264 2.0440 2.0055 0.0470  -0.4262 -0.1043 245 LEU F CA  
16270 C C   . LEU F 245 ? 1.8546 2.0678 2.0241 0.0528  -0.4437 -0.1053 245 LEU F C   
16271 O O   . LEU F 245 ? 1.8111 2.0338 2.0011 0.0523  -0.4582 -0.1104 245 LEU F O   
16272 C CB  . LEU F 245 ? 1.6884 1.9294 1.9035 0.0444  -0.4165 -0.1000 245 LEU F CB  
16273 C CG  . LEU F 245 ? 1.6945 1.9425 1.9236 0.0384  -0.4000 -0.0987 245 LEU F CG  
16274 C CD1 . LEU F 245 ? 1.7264 1.9850 1.9834 0.0323  -0.4058 -0.1052 245 LEU F CD1 
16275 C CD2 . LEU F 245 ? 1.6214 1.8843 1.8667 0.0385  -0.3856 -0.0910 245 LEU F CD2 
16276 N N   . THR F 246 ? 1.9007 2.0993 2.0394 0.0583  -0.4424 -0.1003 246 THR F N   
16277 C CA  . THR F 246 ? 1.8950 2.0863 2.0202 0.0642  -0.4590 -0.1007 246 THR F CA  
16278 C C   . THR F 246 ? 1.9151 2.1259 2.0715 0.0662  -0.4646 -0.0985 246 THR F C   
16279 O O   . THR F 246 ? 1.8709 2.0978 2.0510 0.0643  -0.4524 -0.0943 246 THR F O   
16280 C CB  . THR F 246 ? 1.8668 2.0384 1.9528 0.0692  -0.4546 -0.0947 246 THR F CB  
16281 O OG1 . THR F 246 ? 1.8987 2.0618 1.9702 0.0750  -0.4719 -0.0950 246 THR F OG1 
16282 C CG2 . THR F 246 ? 1.8314 2.0104 1.9234 0.0701  -0.4382 -0.0859 246 THR F CG2 
16283 N N   . SER F 247 ? 2.0278 2.2371 2.1837 0.0703  -0.4835 -0.1016 247 SER F N   
16284 C CA  . SER F 247 ? 1.9787 2.2055 2.1632 0.0731  -0.4912 -0.1005 247 SER F CA  
16285 C C   . SER F 247 ? 1.9898 2.2040 2.1528 0.0806  -0.5070 -0.0992 247 SER F C   
16286 O O   . SER F 247 ? 2.0186 2.2127 2.1486 0.0827  -0.5151 -0.1010 247 SER F O   
16287 C CB  . SER F 247 ? 1.9535 2.1991 2.1752 0.0687  -0.5001 -0.1079 247 SER F CB  
16288 O OG  . SER F 247 ? 1.9350 2.1975 2.1841 0.0719  -0.5082 -0.1074 247 SER F OG  
16289 N N   . GLY F 248 ? 1.7375 1.9636 1.9192 0.0847  -0.5113 -0.0961 248 GLY F N   
16290 C CA  . GLY F 248 ? 1.6527 1.8684 1.8176 0.0922  -0.5266 -0.0943 248 GLY F CA  
16291 C C   . GLY F 248 ? 1.5848 1.8119 1.7672 0.0967  -0.5246 -0.0886 248 GLY F C   
16292 O O   . GLY F 248 ? 1.5804 1.8251 1.7897 0.0940  -0.5116 -0.0866 248 GLY F O   
16293 N N   . PRO F 249 ? 1.5696 1.7864 1.7364 0.1040  -0.5377 -0.0860 249 PRO F N   
16294 C CA  . PRO F 249 ? 1.5660 1.7922 1.7486 0.1090  -0.5368 -0.0808 249 PRO F CA  
16295 C C   . PRO F 249 ? 1.6468 1.8672 1.8157 0.1091  -0.5177 -0.0723 249 PRO F C   
16296 O O   . PRO F 249 ? 1.6385 1.8720 1.8286 0.1109  -0.5115 -0.0689 249 PRO F O   
16297 C CB  . PRO F 249 ? 1.5491 1.7620 1.7139 0.1166  -0.5572 -0.0805 249 PRO F CB  
16298 C CG  . PRO F 249 ? 1.6325 1.8218 1.7571 0.1160  -0.5616 -0.0815 249 PRO F CG  
16299 C CD  . PRO F 249 ? 1.5939 1.7894 1.7274 0.1081  -0.5540 -0.0877 249 PRO F CD  
16300 N N   . HIS F 250 ? 1.8153 2.0171 1.9503 0.1072  -0.5081 -0.0692 250 HIS F N   
16301 C CA  . HIS F 250 ? 1.8241 2.0206 1.9462 0.1067  -0.4893 -0.0614 250 HIS F CA  
16302 C C   . HIS F 250 ? 1.8124 2.0193 1.9473 0.0994  -0.4709 -0.0623 250 HIS F C   
16303 O O   . HIS F 250 ? 1.8201 2.0226 1.9437 0.0981  -0.4544 -0.0565 250 HIS F O   
16304 C CB  . HIS F 250 ? 1.8666 2.0359 1.9426 0.1094  -0.4891 -0.0566 250 HIS F CB  
16305 C CG  . HIS F 250 ? 1.8938 2.0502 1.9464 0.1057  -0.4889 -0.0609 250 HIS F CG  
16306 N ND1 . HIS F 250 ? 1.8981 2.0507 1.9473 0.1060  -0.5058 -0.0681 250 HIS F ND1 
16307 C CD2 . HIS F 250 ? 1.9172 2.0639 1.9493 0.1017  -0.4737 -0.0593 250 HIS F CD2 
16308 C CE1 . HIS F 250 ? 1.9260 2.0664 1.9528 0.1023  -0.5010 -0.0709 250 HIS F CE1 
16309 N NE2 . HIS F 250 ? 1.9368 2.0735 1.9531 0.0998  -0.4815 -0.0657 250 HIS F NE2 
16310 N N   . ILE F 251 ? 1.6305 1.8509 1.7890 0.0946  -0.4734 -0.0692 251 ILE F N   
16311 C CA  . ILE F 251 ? 1.4945 1.7241 1.6655 0.0876  -0.4574 -0.0704 251 ILE F CA  
16312 C C   . ILE F 251 ? 1.3431 1.5992 1.5571 0.0853  -0.4533 -0.0716 251 ILE F C   
16313 O O   . ILE F 251 ? 1.3124 1.5809 1.5504 0.0863  -0.4664 -0.0763 251 ILE F O   
16314 C CB  . ILE F 251 ? 1.5929 1.8158 1.7557 0.0833  -0.4624 -0.0773 251 ILE F CB  
16315 C CG1 . ILE F 251 ? 1.6680 1.8643 1.7863 0.0858  -0.4658 -0.0762 251 ILE F CG1 
16316 C CG2 . ILE F 251 ? 1.5488 1.7818 1.7270 0.0762  -0.4464 -0.0783 251 ILE F CG2 
16317 C CD1 . ILE F 251 ? 1.5658 1.7508 1.6601 0.0854  -0.4477 -0.0693 251 ILE F CD1 
16318 N N   . VAL F 252 ? 1.2719 1.5369 1.4957 0.0820  -0.4350 -0.0675 252 VAL F N   
16319 C CA  . VAL F 252 ? 1.1677 1.4575 1.4300 0.0793  -0.4284 -0.0681 252 VAL F CA  
16320 C C   . VAL F 252 ? 1.1229 1.4189 1.3927 0.0723  -0.4123 -0.0681 252 VAL F C   
16321 O O   . VAL F 252 ? 1.1551 1.4398 1.4029 0.0712  -0.3998 -0.0639 252 VAL F O   
16322 C CB  . VAL F 252 ? 1.1288 1.4249 1.3980 0.0836  -0.4224 -0.0622 252 VAL F CB  
16323 C CG1 . VAL F 252 ? 1.1367 1.4324 1.4098 0.0903  -0.4396 -0.0634 252 VAL F CG1 
16324 C CG2 . VAL F 252 ? 1.1794 1.4588 1.4177 0.0849  -0.4103 -0.0553 252 VAL F CG2 
16325 N N   . GLY F 253 ? 1.0831 1.3970 1.3838 0.0675  -0.4129 -0.0727 253 GLY F N   
16326 C CA  . GLY F 253 ? 1.1278 1.4482 1.4377 0.0608  -0.3986 -0.0726 253 GLY F CA  
16327 C C   . GLY F 253 ? 1.2167 1.5212 1.5054 0.0577  -0.4000 -0.0759 253 GLY F C   
16328 O O   . GLY F 253 ? 1.2102 1.5073 1.4929 0.0583  -0.4149 -0.0815 253 GLY F O   
16329 N N   . ASN F 254 ? 1.3174 1.6165 1.5950 0.0544  -0.3847 -0.0729 254 ASN F N   
16330 C CA  . ASN F 254 ? 1.3442 1.6285 1.6024 0.0513  -0.3834 -0.0760 254 ASN F CA  
16331 C C   . ASN F 254 ? 1.3695 1.6324 1.5891 0.0550  -0.3787 -0.0720 254 ASN F C   
16332 O O   . ASN F 254 ? 1.3066 1.5694 1.5198 0.0557  -0.3649 -0.0658 254 ASN F O   
16333 C CB  . ASN F 254 ? 1.4412 1.7354 1.7165 0.0448  -0.3695 -0.0757 254 ASN F CB  
16334 C CG  . ASN F 254 ? 1.4449 1.7611 1.7589 0.0406  -0.3724 -0.0787 254 ASN F CG  
16335 O OD1 . ASN F 254 ? 1.3801 1.7026 1.7077 0.0419  -0.3868 -0.0830 254 ASN F OD1 
16336 N ND2 . ASN F 254 ? 1.6039 1.9320 1.9360 0.0357  -0.3588 -0.0765 254 ASN F ND2 
16337 N N   . VAL F 255 ? 1.5458 1.7905 1.7395 0.0571  -0.3900 -0.0757 255 VAL F N   
16338 C CA  . VAL F 255 ? 1.6092 1.8324 1.7642 0.0605  -0.3865 -0.0725 255 VAL F CA  
16339 C C   . VAL F 255 ? 1.6407 1.8482 1.7751 0.0584  -0.3898 -0.0781 255 VAL F C   
16340 O O   . VAL F 255 ? 1.6126 1.8190 1.7514 0.0576  -0.4042 -0.0849 255 VAL F O   
16341 C CB  . VAL F 255 ? 1.5593 1.7736 1.6979 0.0671  -0.3984 -0.0702 255 VAL F CB  
16342 C CG1 . VAL F 255 ? 1.5715 1.7629 1.6691 0.0700  -0.3942 -0.0666 255 VAL F CG1 
16343 C CG2 . VAL F 255 ? 1.4733 1.7027 1.6329 0.0695  -0.3953 -0.0650 255 VAL F CG2 
16344 N N   . LEU F 256 ? 1.5989 1.7947 1.7115 0.0574  -0.3765 -0.0757 256 LEU F N   
16345 C CA  . LEU F 256 ? 1.5590 1.7389 1.6499 0.0556  -0.3772 -0.0810 256 LEU F CA  
16346 C C   . LEU F 256 ? 1.5888 1.7467 1.6386 0.0601  -0.3774 -0.0786 256 LEU F C   
16347 O O   . LEU F 256 ? 1.5697 1.7219 1.6044 0.0608  -0.3631 -0.0731 256 LEU F O   
16348 C CB  . LEU F 256 ? 1.4856 1.6701 1.5860 0.0507  -0.3612 -0.0807 256 LEU F CB  
16349 C CG  . LEU F 256 ? 1.4637 1.6321 1.5431 0.0489  -0.3597 -0.0862 256 LEU F CG  
16350 C CD1 . LEU F 256 ? 1.5289 1.6945 1.6124 0.0475  -0.3769 -0.0950 256 LEU F CD1 
16351 C CD2 . LEU F 256 ? 1.5471 1.7220 1.6398 0.0444  -0.3438 -0.0852 256 LEU F CD2 
16352 N N   . VAL F 257 ? 1.6966 1.8424 1.7284 0.0631  -0.3938 -0.0827 257 VAL F N   
16353 C CA  . VAL F 257 ? 1.6856 1.8098 1.6769 0.0674  -0.3958 -0.0807 257 VAL F CA  
16354 C C   . VAL F 257 ? 1.7178 1.8258 1.6854 0.0659  -0.3977 -0.0874 257 VAL F C   
16355 O O   . VAL F 257 ? 1.7886 1.8999 1.7692 0.0629  -0.4060 -0.0951 257 VAL F O   
16356 C CB  . VAL F 257 ? 1.6654 1.7859 1.6498 0.0726  -0.4130 -0.0797 257 VAL F CB  
16357 C CG1 . VAL F 257 ? 1.6805 1.7816 1.6341 0.0749  -0.4273 -0.0852 257 VAL F CG1 
16358 C CG2 . VAL F 257 ? 1.6685 1.7857 1.6412 0.0765  -0.4060 -0.0705 257 VAL F CG2 
16359 N N   . ASP F 258 ? 1.6227 1.7130 1.5555 0.0679  -0.3894 -0.0848 258 ASP F N   
16360 C CA  . ASP F 258 ? 1.5658 1.6389 1.4719 0.0671  -0.3902 -0.0911 258 ASP F CA  
16361 C C   . ASP F 258 ? 1.5524 1.6102 1.4322 0.0710  -0.4086 -0.0948 258 ASP F C   
16362 O O   . ASP F 258 ? 1.5972 1.6523 1.4684 0.0752  -0.4163 -0.0900 258 ASP F O   
16363 C CB  . ASP F 258 ? 1.5214 1.5831 1.4024 0.0675  -0.3721 -0.0867 258 ASP F CB  
16364 C CG  . ASP F 258 ? 1.4638 1.5108 1.3228 0.0661  -0.3696 -0.0939 258 ASP F CG  
16365 O OD1 . ASP F 258 ? 1.4679 1.4995 1.3011 0.0682  -0.3820 -0.0988 258 ASP F OD1 
16366 O OD2 . ASP F 258 ? 1.4564 1.5069 1.3237 0.0629  -0.3555 -0.0947 258 ASP F OD2 
16367 N N   . GLU F 259 ? 1.4970 1.5443 1.3640 0.0696  -0.4158 -0.1035 259 GLU F N   
16368 C CA  . GLU F 259 ? 1.4607 1.4923 1.3003 0.0731  -0.4335 -0.1078 259 GLU F CA  
16369 C C   . GLU F 259 ? 1.4736 1.4856 1.2708 0.0774  -0.4287 -0.1024 259 GLU F C   
16370 O O   . GLU F 259 ? 1.4520 1.4528 1.2273 0.0815  -0.4428 -0.1020 259 GLU F O   
16371 C CB  . GLU F 259 ? 1.4583 1.4828 1.2930 0.0704  -0.4413 -0.1189 259 GLU F CB  
16372 C CG  . GLU F 259 ? 1.5388 1.5540 1.3588 0.0679  -0.4254 -0.1215 259 GLU F CG  
16373 C CD  . GLU F 259 ? 1.5643 1.5737 1.3839 0.0649  -0.4336 -0.1331 259 GLU F CD  
16374 O OE1 . GLU F 259 ? 1.5382 1.5508 1.3684 0.0646  -0.4520 -0.1389 259 GLU F OE1 
16375 O OE2 . GLU F 259 ? 1.6176 1.6193 1.4268 0.0629  -0.4220 -0.1365 259 GLU F OE2 
16376 N N   . THR F 260 ? 1.5091 1.5168 1.2945 0.0765  -0.4092 -0.0980 260 THR F N   
16377 C CA  . THR F 260 ? 1.4804 1.4700 1.2264 0.0800  -0.4031 -0.0924 260 THR F CA  
16378 C C   . THR F 260 ? 1.5132 1.5072 1.2622 0.0830  -0.4015 -0.0821 260 THR F C   
16379 O O   . THR F 260 ? 1.5454 1.5243 1.2632 0.0868  -0.4047 -0.0775 260 THR F O   
16380 C CB  . THR F 260 ? 1.4501 1.4339 1.1832 0.0778  -0.3826 -0.0919 260 THR F CB  
16381 O OG1 . THR F 260 ? 1.4348 1.4192 1.1760 0.0744  -0.3826 -0.1014 260 THR F OG1 
16382 C CG2 . THR F 260 ? 1.5106 1.4724 1.1978 0.0810  -0.3788 -0.0893 260 THR F CG2 
16383 N N   . ALA F 261 ? 1.5790 1.5931 1.3645 0.0813  -0.3966 -0.0784 261 ALA F N   
16384 C CA  . ALA F 261 ? 1.5824 1.6017 1.3737 0.0839  -0.3945 -0.0690 261 ALA F CA  
16385 C C   . ALA F 261 ? 1.5567 1.5727 1.3442 0.0882  -0.4150 -0.0688 261 ALA F C   
16386 O O   . ALA F 261 ? 1.5008 1.5226 1.3031 0.0880  -0.4305 -0.0757 261 ALA F O   
16387 C CB  . ALA F 261 ? 1.5814 1.6237 1.4137 0.0809  -0.3850 -0.0663 261 ALA F CB  
16388 N N   . THR F 262 ? 1.5237 1.5304 1.2917 0.0922  -0.4151 -0.0608 262 THR F N   
16389 C CA  . THR F 262 ? 1.5066 1.5092 1.2698 0.0971  -0.4336 -0.0590 262 THR F CA  
16390 C C   . THR F 262 ? 1.5069 1.5218 1.2923 0.0987  -0.4299 -0.0510 262 THR F C   
16391 O O   . THR F 262 ? 1.5892 1.6032 1.3699 0.0980  -0.4137 -0.0439 262 THR F O   
16392 C CB  . THR F 262 ? 1.5178 1.4952 1.2339 0.1008  -0.4391 -0.0565 262 THR F CB  
16393 O OG1 . THR F 262 ? 1.4603 1.4337 1.1718 0.1060  -0.4543 -0.0520 262 THR F OG1 
16394 C CG2 . THR F 262 ? 1.5794 1.5457 1.2705 0.1000  -0.4193 -0.0497 262 THR F CG2 
16395 N N   . ILE F 263 ? 1.4197 1.4462 1.2298 0.1009  -0.4449 -0.0524 263 ILE F N   
16396 C CA  . ILE F 263 ? 1.4231 1.4630 1.2581 0.1028  -0.4433 -0.0462 263 ILE F CA  
16397 C C   . ILE F 263 ? 1.4352 1.4639 1.2541 0.1091  -0.4593 -0.0422 263 ILE F C   
16398 O O   . ILE F 263 ? 1.4967 1.5196 1.3079 0.1116  -0.4776 -0.0471 263 ILE F O   
16399 C CB  . ILE F 263 ? 1.3957 1.4606 1.2767 0.1002  -0.4462 -0.0512 263 ILE F CB  
16400 C CG1 . ILE F 263 ? 1.4282 1.5035 1.3247 0.0940  -0.4297 -0.0542 263 ILE F CG1 
16401 C CG2 . ILE F 263 ? 1.4150 1.4934 1.3209 0.1028  -0.4457 -0.0454 263 ILE F CG2 
16402 C CD1 . ILE F 263 ? 1.4129 1.5127 1.3539 0.0909  -0.4306 -0.0583 263 ILE F CD1 
16403 N N   . GLY F 264 ? 1.4787 1.5041 1.2926 0.1116  -0.4527 -0.0333 264 GLY F N   
16404 C CA  . GLY F 264 ? 1.4813 1.4972 1.2835 0.1178  -0.4670 -0.0285 264 GLY F CA  
16405 C C   . GLY F 264 ? 1.4948 1.5286 1.3335 0.1204  -0.4811 -0.0314 264 GLY F C   
16406 O O   . GLY F 264 ? 1.4933 1.5473 1.3665 0.1172  -0.4804 -0.0372 264 GLY F O   
16407 N N   . GLU F 265 ? 1.5177 1.5437 1.3482 0.1264  -0.4942 -0.0268 265 GLU F N   
16408 C CA  . GLU F 265 ? 1.5450 1.5860 1.4074 0.1301  -0.5089 -0.0290 265 GLU F CA  
16409 C C   . GLU F 265 ? 1.5539 1.6070 1.4402 0.1310  -0.4988 -0.0230 265 GLU F C   
16410 O O   . GLU F 265 ? 1.5784 1.6231 1.4496 0.1303  -0.4844 -0.0156 265 GLU F O   
16411 C CB  . GLU F 265 ? 1.6296 1.6554 1.4708 0.1367  -0.5306 -0.0280 265 GLU F CB  
16412 C CG  . GLU F 265 ? 1.7003 1.7148 1.5190 0.1363  -0.5431 -0.0349 265 GLU F CG  
16413 C CD  . GLU F 265 ? 1.7585 1.7922 1.6103 0.1338  -0.5530 -0.0453 265 GLU F CD  
16414 O OE1 . GLU F 265 ? 1.7754 1.8307 1.6672 0.1336  -0.5532 -0.0469 265 GLU F OE1 
16415 O OE2 . GLU F 265 ? 1.8167 1.8437 1.6543 0.1319  -0.5603 -0.0521 265 GLU F OE2 
16416 N N   . GLY F 266 ? 1.5834 1.6567 1.5079 0.1324  -0.5065 -0.0264 266 GLY F N   
16417 C CA  . GLY F 266 ? 1.6166 1.7028 1.5661 0.1337  -0.4984 -0.0218 266 GLY F CA  
16418 C C   . GLY F 266 ? 1.6148 1.7135 1.5797 0.1275  -0.4764 -0.0211 266 GLY F C   
16419 O O   . GLY F 266 ? 1.6233 1.7246 1.5939 0.1280  -0.4651 -0.0151 266 GLY F O   
16420 N N   . CYS F 267 ? 1.5768 1.6833 1.5489 0.1219  -0.4706 -0.0271 267 CYS F N   
16421 C CA  . CYS F 267 ? 1.5211 1.6400 1.5084 0.1160  -0.4506 -0.0269 267 CYS F CA  
16422 C C   . CYS F 267 ? 1.4599 1.6054 1.4916 0.1135  -0.4512 -0.0326 267 CYS F C   
16423 O O   . CYS F 267 ? 1.4563 1.6104 1.5063 0.1159  -0.4668 -0.0375 267 CYS F O   
16424 C CB  . CYS F 267 ? 1.4837 1.5922 1.4480 0.1113  -0.4422 -0.0293 267 CYS F CB  
16425 S SG  . CYS F 267 ? 1.4972 1.5740 1.4074 0.1139  -0.4430 -0.0239 267 CYS F SG  
16426 N N   . LEU F 268 ? 1.4246 1.5830 1.4733 0.1087  -0.4337 -0.0317 268 LEU F N   
16427 C CA  . LEU F 268 ? 1.3748 1.5583 1.4638 0.1054  -0.4314 -0.0367 268 LEU F CA  
16428 C C   . LEU F 268 ? 1.3322 1.5209 1.4238 0.0988  -0.4132 -0.0370 268 LEU F C   
16429 O O   . LEU F 268 ? 1.3583 1.5464 1.4454 0.0977  -0.3979 -0.0315 268 LEU F O   
16430 C CB  . LEU F 268 ? 1.3701 1.5685 1.4858 0.1083  -0.4303 -0.0340 268 LEU F CB  
16431 C CG  . LEU F 268 ? 1.3243 1.5487 1.4823 0.1062  -0.4325 -0.0397 268 LEU F CG  
16432 C CD1 . LEU F 268 ? 1.3696 1.5961 1.5347 0.1067  -0.4504 -0.0470 268 LEU F CD1 
16433 C CD2 . LEU F 268 ? 1.3639 1.6011 1.5453 0.1100  -0.4326 -0.0374 268 LEU F CD2 
16434 N N   . ILE F 269 ? 1.3190 1.5125 1.4180 0.0946  -0.4152 -0.0433 269 ILE F N   
16435 C CA  . ILE F 269 ? 1.3208 1.5162 1.4185 0.0887  -0.3997 -0.0440 269 ILE F CA  
16436 C C   . ILE F 269 ? 1.2603 1.4792 1.3966 0.0842  -0.3969 -0.0485 269 ILE F C   
16437 O O   . ILE F 269 ? 1.2642 1.4915 1.4182 0.0840  -0.4099 -0.0544 269 ILE F O   
16438 C CB  . ILE F 269 ? 1.3543 1.5316 1.4227 0.0873  -0.4031 -0.0475 269 ILE F CB  
16439 C CG1 . ILE F 269 ? 1.3742 1.5279 1.4028 0.0915  -0.4047 -0.0425 269 ILE F CG1 
16440 C CG2 . ILE F 269 ? 1.3817 1.5619 1.4518 0.0814  -0.3873 -0.0486 269 ILE F CG2 
16441 C CD1 . ILE F 269 ? 1.4538 1.5963 1.4682 0.0965  -0.4250 -0.0444 269 ILE F CD1 
16442 N N   . GLY F 270 ? 1.2147 1.4442 1.3638 0.0806  -0.3799 -0.0456 270 GLY F N   
16443 C CA  . GLY F 270 ? 1.1839 1.4353 1.3679 0.0761  -0.3750 -0.0488 270 GLY F CA  
16444 C C   . GLY F 270 ? 1.1666 1.4344 1.3731 0.0765  -0.3655 -0.0446 270 GLY F C   
16445 O O   . GLY F 270 ? 1.1874 1.4510 1.3866 0.0810  -0.3659 -0.0402 270 GLY F O   
16446 N N   . PRO F 271 ? 1.1107 1.3973 1.3450 0.0718  -0.3566 -0.0460 271 PRO F N   
16447 C CA  . PRO F 271 ? 1.1648 1.4551 1.4074 0.0663  -0.3559 -0.0508 271 PRO F CA  
16448 C C   . PRO F 271 ? 1.2573 1.5382 1.4820 0.0628  -0.3414 -0.0484 271 PRO F C   
16449 O O   . PRO F 271 ? 1.3238 1.6008 1.5369 0.0638  -0.3296 -0.0428 271 PRO F O   
16450 C CB  . PRO F 271 ? 1.1581 1.4735 1.4396 0.0631  -0.3525 -0.0525 271 PRO F CB  
16451 C CG  . PRO F 271 ? 1.1169 1.4413 1.4099 0.0676  -0.3532 -0.0494 271 PRO F CG  
16452 C CD  . PRO F 271 ? 1.0888 1.3953 1.3511 0.0716  -0.3494 -0.0439 271 PRO F CD  
16453 N N   . ASP F 272 ? 1.2968 1.5746 1.5204 0.0588  -0.3426 -0.0530 272 ASP F N   
16454 C CA  . ASP F 272 ? 1.3564 1.6275 1.5681 0.0551  -0.3293 -0.0518 272 ASP F CA  
16455 C C   . ASP F 272 ? 1.3642 1.6149 1.5399 0.0581  -0.3240 -0.0479 272 ASP F C   
16456 O O   . ASP F 272 ? 1.3465 1.5972 1.5164 0.0581  -0.3104 -0.0425 272 ASP F O   
16457 C CB  . ASP F 272 ? 1.4892 1.7781 1.7250 0.0514  -0.3145 -0.0486 272 ASP F CB  
16458 C CG  . ASP F 272 ? 1.6086 1.9178 1.8796 0.0482  -0.3190 -0.0520 272 ASP F CG  
16459 O OD1 . ASP F 272 ? 1.6290 1.9533 1.9201 0.0495  -0.3183 -0.0501 272 ASP F OD1 
16460 O OD2 . ASP F 272 ? 1.6692 1.9788 1.9475 0.0444  -0.3235 -0.0570 272 ASP F OD2 
16461 N N   . VAL F 273 ? 1.3689 1.6025 1.5204 0.0606  -0.3354 -0.0510 273 VAL F N   
16462 C CA  . VAL F 273 ? 1.3618 1.5743 1.4767 0.0633  -0.3321 -0.0481 273 VAL F CA  
16463 C C   . VAL F 273 ? 1.4064 1.6045 1.5021 0.0617  -0.3366 -0.0537 273 VAL F C   
16464 O O   . VAL F 273 ? 1.4468 1.6453 1.5490 0.0613  -0.3503 -0.0598 273 VAL F O   
16465 C CB  . VAL F 273 ? 1.3226 1.5259 1.4218 0.0691  -0.3422 -0.0452 273 VAL F CB  
16466 C CG1 . VAL F 273 ? 1.3638 1.5455 1.4248 0.0713  -0.3370 -0.0414 273 VAL F CG1 
16467 C CG2 . VAL F 273 ? 1.3192 1.5374 1.4397 0.0707  -0.3388 -0.0405 273 VAL F CG2 
16468 N N   . ALA F 274 ? 1.3999 1.5854 1.4725 0.0610  -0.3251 -0.0520 274 ALA F N   
16469 C CA  . ALA F 274 ? 1.4237 1.5944 1.4759 0.0597  -0.3274 -0.0574 274 ALA F CA  
16470 C C   . ALA F 274 ? 1.4357 1.5855 1.4491 0.0630  -0.3240 -0.0544 274 ALA F C   
16471 O O   . ALA F 274 ? 1.4195 1.5670 1.4239 0.0629  -0.3093 -0.0491 274 ALA F O   
16472 C CB  . ALA F 274 ? 1.4478 1.6250 1.5131 0.0548  -0.3152 -0.0592 274 ALA F CB  
16473 N N   . ILE F 275 ? 1.5427 1.6775 1.5334 0.0658  -0.3377 -0.0578 275 ILE F N   
16474 C CA  . ILE F 275 ? 1.5921 1.7061 1.5440 0.0691  -0.3363 -0.0550 275 ILE F CA  
16475 C C   . ILE F 275 ? 1.6090 1.7087 1.5391 0.0677  -0.3352 -0.0610 275 ILE F C   
16476 O O   . ILE F 275 ? 1.5896 1.6864 1.5205 0.0670  -0.3479 -0.0683 275 ILE F O   
16477 C CB  . ILE F 275 ? 1.5761 1.6819 1.5146 0.0739  -0.3526 -0.0540 275 ILE F CB  
16478 C CG1 . ILE F 275 ? 1.5350 1.6550 1.4963 0.0757  -0.3535 -0.0484 275 ILE F CG1 
16479 C CG2 . ILE F 275 ? 1.5809 1.6641 1.4776 0.0770  -0.3507 -0.0508 275 ILE F CG2 
16480 C CD1 . ILE F 275 ? 1.5704 1.6832 1.5213 0.0808  -0.3697 -0.0470 275 ILE F CD1 
16481 N N   . GLY F 276 ? 1.7691 1.8595 1.6793 0.0672  -0.3201 -0.0583 276 GLY F N   
16482 C CA  . GLY F 276 ? 1.7989 1.8758 1.6881 0.0661  -0.3168 -0.0638 276 GLY F CA  
16483 C C   . GLY F 276 ? 1.8261 1.8829 1.6809 0.0693  -0.3294 -0.0671 276 GLY F C   
16484 O O   . GLY F 276 ? 1.8227 1.8760 1.6704 0.0726  -0.3418 -0.0649 276 GLY F O   
16485 N N   . PRO F 277 ? 1.5431 1.5863 1.3761 0.0686  -0.3264 -0.0725 277 PRO F N   
16486 C CA  . PRO F 277 ? 1.5052 1.5284 1.3027 0.0716  -0.3374 -0.0762 277 PRO F CA  
16487 C C   . PRO F 277 ? 1.4612 1.4698 1.2252 0.0747  -0.3299 -0.0693 277 PRO F C   
16488 O O   . PRO F 277 ? 1.4337 1.4456 1.1988 0.0741  -0.3138 -0.0629 277 PRO F O   
16489 C CB  . PRO F 277 ? 1.5178 1.5334 1.3072 0.0693  -0.3346 -0.0849 277 PRO F CB  
16490 C CG  . PRO F 277 ? 1.4777 1.5034 1.2843 0.0663  -0.3156 -0.0824 277 PRO F CG  
16491 C CD  . PRO F 277 ? 1.5491 1.5952 1.3903 0.0651  -0.3137 -0.0763 277 PRO F CD  
16492 N N   . GLY F 278 ? 1.4635 1.4555 1.1973 0.0779  -0.3423 -0.0707 278 GLY F N   
16493 C CA  . GLY F 278 ? 1.4571 1.4328 1.1554 0.0809  -0.3372 -0.0644 278 GLY F CA  
16494 C C   . GLY F 278 ? 1.4354 1.4166 1.1405 0.0827  -0.3353 -0.0544 278 GLY F C   
16495 O O   . GLY F 278 ? 1.4353 1.4039 1.1134 0.0847  -0.3288 -0.0480 278 GLY F O   
16496 N N   . CYS F 279 ? 1.4808 1.4802 1.2213 0.0821  -0.3403 -0.0529 279 CYS F N   
16497 C CA  . CYS F 279 ? 1.5279 1.5331 1.2772 0.0840  -0.3390 -0.0441 279 CYS F CA  
16498 C C   . CYS F 279 ? 1.6073 1.6030 1.3421 0.0885  -0.3576 -0.0426 279 CYS F C   
16499 O O   . CYS F 279 ? 1.5929 1.5840 1.3227 0.0897  -0.3736 -0.0491 279 CYS F O   
16500 C CB  . CYS F 279 ? 1.5071 1.5362 1.3004 0.0817  -0.3363 -0.0435 279 CYS F CB  
16501 S SG  . CYS F 279 ? 1.4643 1.5057 1.2778 0.0765  -0.3173 -0.0461 279 CYS F SG  
16502 N N   . ILE F 280 ? 1.7550 1.7477 1.4835 0.0910  -0.3555 -0.0339 280 ILE F N   
16503 C CA  . ILE F 280 ? 1.8004 1.7842 1.5163 0.0957  -0.3719 -0.0307 280 ILE F CA  
16504 C C   . ILE F 280 ? 1.8193 1.8162 1.5608 0.0968  -0.3703 -0.0239 280 ILE F C   
16505 O O   . ILE F 280 ? 1.9783 1.9723 1.7129 0.0967  -0.3574 -0.0162 280 ILE F O   
16506 C CB  . ILE F 280 ? 1.8845 1.8438 1.5544 0.0983  -0.3716 -0.0263 280 ILE F CB  
16507 C CG1 . ILE F 280 ? 1.7918 1.7386 1.4358 0.0968  -0.3697 -0.0333 280 ILE F CG1 
16508 C CG2 . ILE F 280 ? 1.9286 1.8785 1.5861 0.1034  -0.3912 -0.0238 280 ILE F CG2 
16509 C CD1 . ILE F 280 ? 1.8892 1.8119 1.4866 0.0991  -0.3684 -0.0296 280 ILE F CD1 
16510 N N   . VAL F 281 ? 1.8187 1.8304 1.5903 0.0979  -0.3832 -0.0269 281 VAL F N   
16511 C CA  . VAL F 281 ? 1.7694 1.7952 1.5685 0.0992  -0.3832 -0.0219 281 VAL F CA  
16512 C C   . VAL F 281 ? 1.7721 1.7868 1.5567 0.1049  -0.3987 -0.0177 281 VAL F C   
16513 O O   . VAL F 281 ? 1.7934 1.8031 1.5721 0.1075  -0.4166 -0.0223 281 VAL F O   
16514 C CB  . VAL F 281 ? 1.7151 1.7645 1.5571 0.0971  -0.3874 -0.0277 281 VAL F CB  
16515 C CG1 . VAL F 281 ? 1.6837 1.7465 1.5521 0.0994  -0.3905 -0.0234 281 VAL F CG1 
16516 C CG2 . VAL F 281 ? 1.7074 1.7681 1.5650 0.0916  -0.3707 -0.0303 281 VAL F CG2 
16517 N N   . GLU F 282 ? 1.6853 1.6956 1.4640 0.1068  -0.3923 -0.0090 282 GLU F N   
16518 C CA  . GLU F 282 ? 1.6425 1.6409 1.4066 0.1123  -0.4057 -0.0038 282 GLU F CA  
16519 C C   . GLU F 282 ? 1.5702 1.5859 1.3704 0.1150  -0.4168 -0.0048 282 GLU F C   
16520 O O   . GLU F 282 ? 1.5854 1.6219 1.4203 0.1124  -0.4149 -0.0099 282 GLU F O   
16521 C CB  . GLU F 282 ? 1.6364 1.6207 1.3767 0.1129  -0.3937 0.0060  282 GLU F CB  
16522 C CG  . GLU F 282 ? 1.8336 1.7993 1.5356 0.1108  -0.3833 0.0075  282 GLU F CG  
16523 C CD  . GLU F 282 ? 1.8699 1.8188 1.5448 0.1122  -0.3754 0.0176  282 GLU F CD  
16524 O OE1 . GLU F 282 ? 1.7053 1.6581 1.3938 0.1142  -0.3762 0.0235  282 GLU F OE1 
16525 O OE2 . GLU F 282 ? 2.1761 2.1077 1.8162 0.1111  -0.3684 0.0197  282 GLU F OE2 
16526 N N   . SER F 283 ? 1.5691 1.5760 1.3609 0.1203  -0.4282 0.0003  283 SER F N   
16527 C CA  . SER F 283 ? 1.5680 1.5884 1.3896 0.1241  -0.4422 -0.0012 283 SER F CA  
16528 C C   . SER F 283 ? 1.6324 1.6666 1.4809 0.1238  -0.4315 0.0034  283 SER F C   
16529 O O   . SER F 283 ? 1.5915 1.6191 1.4283 0.1224  -0.4168 0.0101  283 SER F O   
16530 C CB  . SER F 283 ? 1.5912 1.5945 1.3904 0.1306  -0.4609 0.0020  283 SER F CB  
16531 O OG  . SER F 283 ? 1.6087 1.6049 1.3933 0.1314  -0.4753 -0.0045 283 SER F OG  
16532 N N   . GLY F 284 ? 2.1341 2.1881 2.0195 0.1252  -0.4392 -0.0005 284 GLY F N   
16533 C CA  . GLY F 284 ? 2.1112 2.1792 2.0237 0.1257  -0.4314 0.0029  284 GLY F CA  
16534 C C   . GLY F 284 ? 2.0922 2.1771 2.0263 0.1197  -0.4125 0.0016  284 GLY F C   
16535 O O   . GLY F 284 ? 2.0771 2.1711 2.0283 0.1196  -0.4032 0.0053  284 GLY F O   
16536 N N   . VAL F 285 ? 1.6606 1.7495 1.5943 0.1149  -0.4066 -0.0036 285 VAL F N   
16537 C CA  . VAL F 285 ? 1.5903 1.6933 1.5411 0.1092  -0.3884 -0.0044 285 VAL F CA  
16538 C C   . VAL F 285 ? 1.5589 1.6873 1.5518 0.1077  -0.3909 -0.0101 285 VAL F C   
16539 O O   . VAL F 285 ? 1.5361 1.6708 1.5430 0.1101  -0.4065 -0.0150 285 VAL F O   
16540 C CB  . VAL F 285 ? 1.5403 1.6347 1.4702 0.1048  -0.3800 -0.0068 285 VAL F CB  
16541 C CG1 . VAL F 285 ? 1.5633 1.6325 1.4507 0.1064  -0.3777 -0.0014 285 VAL F CG1 
16542 C CG2 . VAL F 285 ? 1.4804 1.5789 1.4170 0.1040  -0.3922 -0.0153 285 VAL F CG2 
16543 N N   . ARG F 286 ? 1.5263 1.6697 1.5394 0.1036  -0.3751 -0.0095 286 ARG F N   
16544 C CA  . ARG F 286 ? 1.4139 1.5820 1.4666 0.1015  -0.3743 -0.0141 286 ARG F CA  
16545 C C   . ARG F 286 ? 1.3734 1.5504 1.4336 0.0952  -0.3577 -0.0154 286 ARG F C   
16546 O O   . ARG F 286 ? 1.4392 1.6197 1.5015 0.0934  -0.3427 -0.0110 286 ARG F O   
16547 C CB  . ARG F 286 ? 1.4535 1.6328 1.5278 0.1044  -0.3734 -0.0109 286 ARG F CB  
16548 C CG  . ARG F 286 ? 1.3990 1.6044 1.5131 0.1019  -0.3692 -0.0149 286 ARG F CG  
16549 C CD  . ARG F 286 ? 1.3516 1.5674 1.4835 0.1008  -0.3811 -0.0224 286 ARG F CD  
16550 N NE  . ARG F 286 ? 1.3235 1.5644 1.4940 0.0987  -0.3776 -0.0257 286 ARG F NE  
16551 C CZ  . ARG F 286 ? 1.2758 1.5303 1.4669 0.0950  -0.3804 -0.0318 286 ARG F CZ  
16552 N NH1 . ARG F 286 ? 1.2410 1.4863 1.4183 0.0933  -0.3872 -0.0356 286 ARG F NH1 
16553 N NH2 . ARG F 286 ? 1.2738 1.5510 1.4992 0.0930  -0.3762 -0.0341 286 ARG F NH2 
16554 N N   . LEU F 287 ? 1.3348 1.5152 1.3990 0.0920  -0.3607 -0.0214 287 LEU F N   
16555 C CA  . LEU F 287 ? 1.3168 1.5044 1.3877 0.0863  -0.3464 -0.0230 287 LEU F CA  
16556 C C   . LEU F 287 ? 1.3208 1.5325 1.4304 0.0833  -0.3455 -0.0271 287 LEU F C   
16557 O O   . LEU F 287 ? 1.3084 1.5283 1.4353 0.0844  -0.3588 -0.0318 287 LEU F O   
16558 C CB  . LEU F 287 ? 1.3214 1.4950 1.3691 0.0844  -0.3488 -0.0268 287 LEU F CB  
16559 C CG  . LEU F 287 ? 1.3467 1.4957 1.3536 0.0870  -0.3493 -0.0233 287 LEU F CG  
16560 C CD1 . LEU F 287 ? 1.3808 1.5179 1.3675 0.0849  -0.3511 -0.0282 287 LEU F CD1 
16561 C CD2 . LEU F 287 ? 1.3633 1.5078 1.3589 0.0863  -0.3325 -0.0161 287 LEU F CD2 
16562 N N   . SER F 288 ? 1.4732 1.6963 1.5963 0.0794  -0.3296 -0.0253 288 SER F N   
16563 C CA  . SER F 288 ? 1.4372 1.6833 1.5960 0.0762  -0.3266 -0.0283 288 SER F CA  
16564 C C   . SER F 288 ? 1.4352 1.6874 1.5983 0.0712  -0.3091 -0.0266 288 SER F C   
16565 O O   . SER F 288 ? 1.4582 1.7058 1.6099 0.0714  -0.2972 -0.0214 288 SER F O   
16566 C CB  . SER F 288 ? 1.4323 1.6921 1.6133 0.0791  -0.3287 -0.0264 288 SER F CB  
16567 O OG  . SER F 288 ? 1.4414 1.6945 1.6094 0.0811  -0.3198 -0.0201 288 SER F OG  
16568 N N   . ARG F 289 ? 1.3118 1.5739 1.4914 0.0669  -0.3078 -0.0309 289 ARG F N   
16569 C CA  . ARG F 289 ? 1.3246 1.5951 1.5133 0.0622  -0.2923 -0.0297 289 ARG F CA  
16570 C C   . ARG F 289 ? 1.3760 1.6300 1.5359 0.0615  -0.2820 -0.0269 289 ARG F C   
16571 O O   . ARG F 289 ? 1.5442 1.8034 1.7082 0.0587  -0.2679 -0.0244 289 ARG F O   
16572 C CB  . ARG F 289 ? 1.3870 1.6753 1.5987 0.0616  -0.2828 -0.0260 289 ARG F CB  
16573 C CG  . ARG F 289 ? 1.6069 1.9101 1.8384 0.0565  -0.2705 -0.0260 289 ARG F CG  
16574 C CD  . ARG F 289 ? 1.6966 2.0154 1.9462 0.0564  -0.2608 -0.0221 289 ARG F CD  
16575 N NE  . ARG F 289 ? 1.8951 2.2232 2.1542 0.0521  -0.2466 -0.0202 289 ARG F NE  
16576 C CZ  . ARG F 289 ? 1.9100 2.2541 2.1938 0.0482  -0.2442 -0.0221 289 ARG F CZ  
16577 N NH1 . ARG F 289 ? 1.8489 2.2025 2.1516 0.0478  -0.2546 -0.0263 289 ARG F NH1 
16578 N NH2 . ARG F 289 ? 1.8711 2.2218 2.1607 0.0447  -0.2312 -0.0197 289 ARG F NH2 
16579 N N   . CYS F 290 ? 1.3474 1.5816 1.4781 0.0642  -0.2887 -0.0272 290 CYS F N   
16580 C CA  . CYS F 290 ? 1.3506 1.5688 1.4528 0.0639  -0.2790 -0.0247 290 CYS F CA  
16581 C C   . CYS F 290 ? 1.3363 1.5434 1.4245 0.0622  -0.2831 -0.0301 290 CYS F C   
16582 O O   . CYS F 290 ? 1.3158 1.5264 1.4148 0.0614  -0.2945 -0.0357 290 CYS F O   
16583 C CB  . CYS F 290 ? 1.3336 1.5363 1.4099 0.0682  -0.2814 -0.0202 290 CYS F CB  
16584 S SG  . CYS F 290 ? 1.3034 1.4951 1.3680 0.0729  -0.3028 -0.0231 290 CYS F SG  
16585 N N   . THR F 291 ? 1.3311 1.5251 1.3956 0.0616  -0.2733 -0.0287 291 THR F N   
16586 C CA  . THR F 291 ? 1.2978 1.4786 1.3442 0.0605  -0.2759 -0.0337 291 THR F CA  
16587 C C   . THR F 291 ? 1.3292 1.4892 1.3388 0.0632  -0.2729 -0.0312 291 THR F C   
16588 O O   . THR F 291 ? 1.3392 1.4973 1.3404 0.0633  -0.2602 -0.0257 291 THR F O   
16589 C CB  . THR F 291 ? 1.2963 1.4839 1.3547 0.0562  -0.2645 -0.0357 291 THR F CB  
16590 O OG1 . THR F 291 ? 1.3028 1.4843 1.3460 0.0561  -0.2493 -0.0314 291 THR F OG1 
16591 C CG2 . THR F 291 ? 1.4884 1.6984 1.5834 0.0534  -0.2618 -0.0353 291 THR F CG2 
16592 N N   . VAL F 292 ? 1.3599 1.5047 1.3476 0.0651  -0.2846 -0.0352 292 VAL F N   
16593 C CA  . VAL F 292 ? 1.3603 1.4841 1.3107 0.0677  -0.2834 -0.0332 292 VAL F CA  
16594 C C   . VAL F 292 ? 1.3830 1.4955 1.3159 0.0660  -0.2801 -0.0385 292 VAL F C   
16595 O O   . VAL F 292 ? 1.4475 1.5603 1.3865 0.0648  -0.2896 -0.0454 292 VAL F O   
16596 C CB  . VAL F 292 ? 1.3874 1.5009 1.3229 0.0718  -0.3001 -0.0331 292 VAL F CB  
16597 C CG1 . VAL F 292 ? 1.4385 1.5290 1.3334 0.0740  -0.3005 -0.0325 292 VAL F CG1 
16598 C CG2 . VAL F 292 ? 1.3548 1.4763 1.3024 0.0741  -0.3009 -0.0268 292 VAL F CG2 
16599 N N   . MET F 293 ? 1.3663 1.4688 1.2779 0.0659  -0.2666 -0.0357 293 MET F N   
16600 C CA  . MET F 293 ? 1.3503 1.4413 1.2438 0.0647  -0.2618 -0.0407 293 MET F CA  
16601 C C   . MET F 293 ? 1.3710 1.4403 1.2267 0.0678  -0.2694 -0.0421 293 MET F C   
16602 O O   . MET F 293 ? 1.4253 1.4889 1.2710 0.0707  -0.2802 -0.0395 293 MET F O   
16603 C CB  . MET F 293 ? 1.3473 1.4412 1.2413 0.0628  -0.2422 -0.0374 293 MET F CB  
16604 C CG  . MET F 293 ? 1.3556 1.4697 1.2850 0.0596  -0.2350 -0.0370 293 MET F CG  
16605 S SD  . MET F 293 ? 1.4923 1.6086 1.4215 0.0576  -0.2136 -0.0348 293 MET F SD  
16606 C CE  . MET F 293 ? 1.5061 1.6472 1.4783 0.0543  -0.2094 -0.0335 293 MET F CE  
16607 N N   . ARG F 294 ? 1.3614 1.4180 1.1953 0.0673  -0.2637 -0.0461 294 ARG F N   
16608 C CA  . ARG F 294 ? 1.3496 1.3858 1.1483 0.0698  -0.2723 -0.0494 294 ARG F CA  
16609 C C   . ARG F 294 ? 1.3460 1.3695 1.1164 0.0726  -0.2688 -0.0421 294 ARG F C   
16610 O O   . ARG F 294 ? 1.3975 1.4242 1.1687 0.0720  -0.2546 -0.0357 294 ARG F O   
16611 C CB  . ARG F 294 ? 1.3737 1.4005 1.1575 0.0685  -0.2653 -0.0559 294 ARG F CB  
16612 C CG  . ARG F 294 ? 1.4526 1.4899 1.2627 0.0655  -0.2682 -0.0631 294 ARG F CG  
16613 C CD  . ARG F 294 ? 1.4781 1.5047 1.2724 0.0646  -0.2609 -0.0695 294 ARG F CD  
16614 N NE  . ARG F 294 ? 1.4440 1.4499 1.2004 0.0672  -0.2675 -0.0731 294 ARG F NE  
16615 C CZ  . ARG F 294 ? 1.4827 1.4760 1.2191 0.0672  -0.2637 -0.0797 294 ARG F CZ  
16616 N NH1 . ARG F 294 ? 1.5103 1.5094 1.2619 0.0649  -0.2534 -0.0834 294 ARG F NH1 
16617 N NH2 . ARG F 294 ? 1.5130 1.4877 1.2139 0.0697  -0.2703 -0.0827 294 ARG F NH2 
16618 N N   . GLY F 295 ? 1.3807 1.3894 1.1258 0.0756  -0.2824 -0.0432 295 GLY F N   
16619 C CA  . GLY F 295 ? 1.5155 1.5069 1.2255 0.0781  -0.2797 -0.0376 295 GLY F CA  
16620 C C   . GLY F 295 ? 1.6003 1.5952 1.3146 0.0794  -0.2767 -0.0280 295 GLY F C   
16621 O O   . GLY F 295 ? 1.7134 1.6930 1.3985 0.0816  -0.2766 -0.0229 295 GLY F O   
16622 N N   . VAL F 296 ? 1.6266 1.6404 1.3754 0.0781  -0.2743 -0.0253 296 VAL F N   
16623 C CA  . VAL F 296 ? 1.8172 1.8346 1.5712 0.0791  -0.2704 -0.0166 296 VAL F CA  
16624 C C   . VAL F 296 ? 2.1030 2.1155 1.8529 0.0828  -0.2885 -0.0148 296 VAL F C   
16625 O O   . VAL F 296 ? 1.9476 1.9663 1.7125 0.0837  -0.3032 -0.0201 296 VAL F O   
16626 C CB  . VAL F 296 ? 1.6617 1.7012 1.4538 0.0765  -0.2613 -0.0148 296 VAL F CB  
16627 C CG1 . VAL F 296 ? 1.5405 1.5949 1.3623 0.0753  -0.2709 -0.0215 296 VAL F CG1 
16628 C CG2 . VAL F 296 ? 1.7607 1.8049 1.5616 0.0780  -0.2611 -0.0071 296 VAL F CG2 
16629 N N   . ARG F 297 ? 3.0816 3.0828 2.8116 0.0851  -0.2874 -0.0073 297 ARG F N   
16630 C CA  . ARG F 297 ? 3.0739 3.0689 2.7980 0.0891  -0.3036 -0.0043 297 ARG F CA  
16631 C C   . ARG F 297 ? 3.0463 3.0544 2.7964 0.0896  -0.3013 0.0018  297 ARG F C   
16632 O O   . ARG F 297 ? 3.0525 3.0617 2.8022 0.0880  -0.2866 0.0078  297 ARG F O   
16633 C CB  . ARG F 297 ? 3.1088 3.0799 2.7903 0.0916  -0.3050 0.0005  297 ARG F CB  
16634 C CG  . ARG F 297 ? 3.1064 3.0705 2.7820 0.0958  -0.3183 0.0063  297 ARG F CG  
16635 C CD  . ARG F 297 ? 3.1456 3.0866 2.7800 0.0976  -0.3159 0.0132  297 ARG F CD  
16636 N NE  . ARG F 297 ? 3.1856 3.1100 2.7865 0.0981  -0.3198 0.0087  297 ARG F NE  
16637 C CZ  . ARG F 297 ? 3.2209 3.1235 2.7824 0.1001  -0.3213 0.0134  297 ARG F CZ  
16638 N NH1 . ARG F 297 ? 3.2252 3.1198 2.7768 0.1016  -0.3192 0.0230  297 ARG F NH1 
16639 N NH2 . ARG F 297 ? 3.2441 3.1326 2.7758 0.1006  -0.3248 0.0085  297 ARG F NH2 
16640 N N   . ILE F 298 ? 2.1452 2.1636 1.9181 0.0917  -0.3158 -0.0002 298 ILE F N   
16641 C CA  . ILE F 298 ? 1.8772 1.9073 1.6742 0.0930  -0.3163 0.0047  298 ILE F CA  
16642 C C   . ILE F 298 ? 1.7871 1.8038 1.5674 0.0980  -0.3311 0.0087  298 ILE F C   
16643 O O   . ILE F 298 ? 1.8119 1.8246 1.5880 0.1008  -0.3481 0.0045  298 ILE F O   
16644 C CB  . ILE F 298 ? 1.7647 1.8182 1.6029 0.0917  -0.3204 -0.0005 298 ILE F CB  
16645 C CG1 . ILE F 298 ? 1.7848 1.8507 1.6386 0.0867  -0.3052 -0.0037 298 ILE F CG1 
16646 C CG2 . ILE F 298 ? 1.6008 1.6656 1.4622 0.0935  -0.3216 0.0041  298 ILE F CG2 
16647 C CD1 . ILE F 298 ? 1.6216 1.7102 1.5147 0.0848  -0.3078 -0.0084 298 ILE F CD1 
16648 N N   . LYS F 299 ? 1.6540 1.6635 1.4246 0.0992  -0.3251 0.0170  299 LYS F N   
16649 C CA  . LYS F 299 ? 1.5387 1.5327 1.2897 0.1041  -0.3378 0.0221  299 LYS F CA  
16650 C C   . LYS F 299 ? 1.4838 1.4904 1.2639 0.1076  -0.3518 0.0211  299 LYS F C   
16651 O O   . LYS F 299 ? 1.4872 1.5147 1.3019 0.1061  -0.3520 0.0162  299 LYS F O   
16652 C CB  . LYS F 299 ? 1.5080 1.4888 1.2380 0.1037  -0.3257 0.0314  299 LYS F CB  
16653 C CG  . LYS F 299 ? 1.5912 1.5566 1.2875 0.1010  -0.3137 0.0326  299 LYS F CG  
16654 C CD  . LYS F 299 ? 1.5479 1.4999 1.2235 0.1004  -0.3021 0.0422  299 LYS F CD  
16655 C CE  . LYS F 299 ? 1.6667 1.6044 1.3097 0.0977  -0.2896 0.0430  299 LYS F CE  
16656 N NZ  . LYS F 299 ? 1.7559 1.6809 1.3789 0.0965  -0.2775 0.0524  299 LYS F NZ  
16657 N N   . LYS F 300 ? 1.4592 1.4531 1.2253 0.1124  -0.3636 0.0261  300 LYS F N   
16658 C CA  . LYS F 300 ? 1.4610 1.4640 1.2503 0.1168  -0.3799 0.0245  300 LYS F CA  
16659 C C   . LYS F 300 ? 1.4371 1.4568 1.2589 0.1165  -0.3727 0.0271  300 LYS F C   
16660 O O   . LYS F 300 ? 1.4355 1.4527 1.2534 0.1145  -0.3581 0.0330  300 LYS F O   
16661 C CB  . LYS F 300 ? 1.4847 1.4673 1.2471 0.1225  -0.3952 0.0293  300 LYS F CB  
16662 C CG  . LYS F 300 ? 1.4899 1.4594 1.2267 0.1241  -0.4085 0.0250  300 LYS F CG  
16663 C CD  . LYS F 300 ? 1.4682 1.4166 1.1764 0.1298  -0.4232 0.0306  300 LYS F CD  
16664 C CE  . LYS F 300 ? 1.4827 1.4086 1.1507 0.1287  -0.4122 0.0385  300 LYS F CE  
16665 N NZ  . LYS F 300 ? 1.3513 1.2545 0.9867 0.1340  -0.4272 0.0438  300 LYS F NZ  
16666 N N   . HIS F 301 ? 1.4946 1.5318 1.3491 0.1184  -0.3831 0.0223  301 HIS F N   
16667 C CA  . HIS F 301 ? 1.4980 1.5511 1.3842 0.1195  -0.3802 0.0239  301 HIS F CA  
16668 C C   . HIS F 301 ? 1.4852 1.5530 1.3895 0.1140  -0.3604 0.0238  301 HIS F C   
16669 O O   . HIS F 301 ? 1.4457 1.5208 1.3655 0.1140  -0.3529 0.0274  301 HIS F O   
16670 C CB  . HIS F 301 ? 1.5012 1.5399 1.3740 0.1240  -0.3839 0.0319  301 HIS F CB  
16671 C CG  . HIS F 301 ? 1.5377 1.5592 1.3883 0.1296  -0.4028 0.0331  301 HIS F CG  
16672 N ND1 . HIS F 301 ? 1.5851 1.5838 1.4044 0.1325  -0.4050 0.0413  301 HIS F ND1 
16673 C CD2 . HIS F 301 ? 1.5830 1.6067 1.4379 0.1327  -0.4207 0.0274  301 HIS F CD2 
16674 C CE1 . HIS F 301 ? 1.5949 1.5821 1.3995 0.1375  -0.4237 0.0406  301 HIS F CE1 
16675 N NE2 . HIS F 301 ? 1.5871 1.5895 1.4133 0.1377  -0.4337 0.0321  301 HIS F NE2 
16676 N N   . ALA F 302 ? 1.4970 1.5693 1.3996 0.1093  -0.3522 0.0196  302 ALA F N   
16677 C CA  . ALA F 302 ? 1.4827 1.5693 1.4025 0.1041  -0.3342 0.0191  302 ALA F CA  
16678 C C   . ALA F 302 ? 1.5810 1.6924 1.5399 0.1028  -0.3364 0.0128  302 ALA F C   
16679 O O   . ALA F 302 ? 1.5676 1.6842 1.5363 0.1041  -0.3497 0.0071  302 ALA F O   
16680 C CB  . ALA F 302 ? 1.4654 1.5439 1.3637 0.1000  -0.3236 0.0180  302 ALA F CB  
16681 N N   . CYS F 303 ? 1.7837 1.9105 1.7651 0.1000  -0.3232 0.0139  303 CYS F N   
16682 C CA  . CYS F 303 ? 1.7415 1.8926 1.7602 0.0983  -0.3229 0.0087  303 CYS F CA  
16683 C C   . CYS F 303 ? 1.7271 1.8882 1.7536 0.0925  -0.3059 0.0078  303 CYS F C   
16684 O O   . CYS F 303 ? 1.7236 1.8878 1.7528 0.0908  -0.2924 0.0120  303 CYS F O   
16685 C CB  . CYS F 303 ? 1.7173 1.8794 1.7590 0.1012  -0.3248 0.0106  303 CYS F CB  
16686 S SG  . CYS F 303 ? 1.6570 1.8496 1.7445 0.0991  -0.3230 0.0048  303 CYS F SG  
16687 N N   . ILE F 304 ? 1.4806 1.6465 1.5112 0.0897  -0.3070 0.0023  304 ILE F N   
16688 C CA  . ILE F 304 ? 1.3935 1.5681 1.4313 0.0845  -0.2923 0.0011  304 ILE F CA  
16689 C C   . ILE F 304 ? 1.3435 1.5402 1.4159 0.0823  -0.2942 -0.0043 304 ILE F C   
16690 O O   . ILE F 304 ? 1.3484 1.5480 1.4286 0.0832  -0.3071 -0.0093 304 ILE F O   
16691 C CB  . ILE F 304 ? 1.3840 1.5434 1.3947 0.0827  -0.2901 -0.0006 304 ILE F CB  
16692 C CG1 . ILE F 304 ? 1.4331 1.5705 1.4087 0.0848  -0.2879 0.0049  304 ILE F CG1 
16693 C CG2 . ILE F 304 ? 1.3664 1.5352 1.3863 0.0777  -0.2750 -0.0019 304 ILE F CG2 
16694 C CD1 . ILE F 304 ? 1.4786 1.6017 1.4269 0.0827  -0.2819 0.0039  304 ILE F CD1 
16695 N N   . SER F 305 ? 1.3498 1.5621 1.4426 0.0794  -0.2814 -0.0030 305 SER F N   
16696 C CA  . SER F 305 ? 1.3197 1.5537 1.4454 0.0768  -0.2811 -0.0072 305 SER F CA  
16697 C C   . SER F 305 ? 1.2692 1.5114 1.4016 0.0719  -0.2652 -0.0066 305 SER F C   
16698 O O   . SER F 305 ? 1.2626 1.5036 1.3892 0.0711  -0.2529 -0.0020 305 SER F O   
16699 C CB  . SER F 305 ? 1.3406 1.5890 1.4907 0.0792  -0.2839 -0.0064 305 SER F CB  
16700 O OG  . SER F 305 ? 1.3425 1.5857 1.4838 0.0807  -0.2762 -0.0008 305 SER F OG  
16701 N N   . SER F 306 ? 1.3015 1.5522 1.4469 0.0686  -0.2657 -0.0112 306 SER F N   
16702 C CA  . SER F 306 ? 1.3127 1.5731 1.4686 0.0640  -0.2521 -0.0111 306 SER F CA  
16703 C C   . SER F 306 ? 1.2439 1.4917 1.3760 0.0632  -0.2396 -0.0071 306 SER F C   
16704 O O   . SER F 306 ? 1.2083 1.4626 1.3457 0.0620  -0.2274 -0.0033 306 SER F O   
16705 C CB  . SER F 306 ? 1.2998 1.5816 1.4856 0.0627  -0.2459 -0.0100 306 SER F CB  
16706 O OG  . SER F 306 ? 1.1949 1.4765 1.3784 0.0653  -0.2422 -0.0055 306 SER F OG  
16707 N N   . SER F 307 ? 1.2671 1.4969 1.3729 0.0639  -0.2429 -0.0083 307 SER F N   
16708 C CA  . SER F 307 ? 1.2801 1.4965 1.3612 0.0634  -0.2317 -0.0049 307 SER F CA  
16709 C C   . SER F 307 ? 1.3171 1.5224 1.3822 0.0620  -0.2327 -0.0090 307 SER F C   
16710 O O   . SER F 307 ? 1.3247 1.5317 1.3968 0.0614  -0.2427 -0.0143 307 SER F O   
16711 C CB  . SER F 307 ? 1.2993 1.5007 1.3574 0.0669  -0.2341 -0.0004 307 SER F CB  
16712 O OG  . SER F 307 ? 1.2239 1.4350 1.2966 0.0680  -0.2314 0.0034  307 SER F OG  
16713 N N   . ILE F 308 ? 1.4197 1.6137 1.4635 0.0613  -0.2220 -0.0069 308 ILE F N   
16714 C CA  . ILE F 308 ? 1.4722 1.6547 1.4988 0.0602  -0.2207 -0.0107 308 ILE F CA  
16715 C C   . ILE F 308 ? 1.6295 1.7916 1.6214 0.0624  -0.2186 -0.0081 308 ILE F C   
16716 O O   . ILE F 308 ? 1.8625 2.0223 1.8464 0.0623  -0.2075 -0.0029 308 ILE F O   
16717 C CB  . ILE F 308 ? 1.4667 1.6580 1.5051 0.0567  -0.2071 -0.0112 308 ILE F CB  
16718 N N   . ILE F 309 ? 1.4902 1.6375 1.4613 0.0641  -0.2292 -0.0118 309 ILE F N   
16719 C CA  . ILE F 309 ? 1.5755 1.7023 1.5115 0.0663  -0.2288 -0.0096 309 ILE F CA  
16720 C C   . ILE F 309 ? 1.5831 1.6999 1.5016 0.0648  -0.2225 -0.0136 309 ILE F C   
16721 O O   . ILE F 309 ? 1.5304 1.6478 1.4538 0.0639  -0.2290 -0.0200 309 ILE F O   
16722 C CB  . ILE F 309 ? 1.5491 1.6653 1.4716 0.0698  -0.2460 -0.0105 309 ILE F CB  
16723 C CG1 . ILE F 309 ? 1.5113 1.6404 1.4578 0.0713  -0.2539 -0.0084 309 ILE F CG1 
16724 C CG2 . ILE F 309 ? 1.6234 1.7195 1.5108 0.0721  -0.2443 -0.0061 309 ILE F CG2 
16725 C CD1 . ILE F 309 ? 1.5899 1.7233 1.5407 0.0716  -0.2440 -0.0012 309 ILE F CD1 
16726 N N   . GLY F 310 ? 1.6582 1.7656 1.5565 0.0647  -0.2097 -0.0101 310 GLY F N   
16727 C CA  . GLY F 310 ? 1.5346 1.6326 1.4159 0.0636  -0.2019 -0.0137 310 GLY F CA  
16728 C C   . GLY F 310 ? 1.4360 1.5144 1.2862 0.0658  -0.2116 -0.0174 310 GLY F C   
16729 O O   . GLY F 310 ? 1.4541 1.5263 1.2964 0.0681  -0.2257 -0.0174 310 GLY F O   
16730 N N   . TRP F 311 ? 1.4134 1.4819 1.2454 0.0652  -0.2037 -0.0207 311 TRP F N   
16731 C CA  . TRP F 311 ? 1.3751 1.4246 1.1758 0.0670  -0.2114 -0.0250 311 TRP F CA  
16732 C C   . TRP F 311 ? 1.4411 1.4750 1.2106 0.0692  -0.2092 -0.0192 311 TRP F C   
16733 O O   . TRP F 311 ? 1.4747 1.5089 1.2399 0.0684  -0.1952 -0.0135 311 TRP F O   
16734 C CB  . TRP F 311 ? 1.4020 1.4463 1.1941 0.0657  -0.2028 -0.0310 311 TRP F CB  
16735 C CG  . TRP F 311 ? 1.4161 1.4737 1.2368 0.0634  -0.2041 -0.0365 311 TRP F CG  
16736 C CD1 . TRP F 311 ? 1.4260 1.4847 1.2558 0.0631  -0.2181 -0.0431 311 TRP F CD1 
16737 C CD2 . TRP F 311 ? 1.4328 1.5041 1.2767 0.0610  -0.1908 -0.0358 311 TRP F CD2 
16738 N NE1 . TRP F 311 ? 1.4743 1.5463 1.3315 0.0604  -0.2139 -0.0463 311 TRP F NE1 
16739 C CE2 . TRP F 311 ? 1.4576 1.5372 1.3233 0.0592  -0.1974 -0.0418 311 TRP F CE2 
16740 C CE3 . TRP F 311 ? 1.4136 1.4909 1.2620 0.0601  -0.1741 -0.0307 311 TRP F CE3 
16741 C CZ2 . TRP F 311 ? 1.4756 1.5686 1.3664 0.0567  -0.1880 -0.0423 311 TRP F CZ2 
16742 C CZ3 . TRP F 311 ? 1.4270 1.5181 1.3007 0.0579  -0.1653 -0.0315 311 TRP F CZ3 
16743 C CH2 . TRP F 311 ? 1.4459 1.5443 1.3400 0.0563  -0.1722 -0.0371 311 TRP F CH2 
16744 N N   . HIS F 312 ? 1.4858 1.5059 1.2335 0.0717  -0.2234 -0.0205 312 HIS F N   
16745 C CA  . HIS F 312 ? 1.5511 1.5528 1.2637 0.0739  -0.2229 -0.0156 312 HIS F CA  
16746 C C   . HIS F 312 ? 1.5912 1.5969 1.3089 0.0739  -0.2158 -0.0062 312 HIS F C   
16747 O O   . HIS F 312 ? 1.5766 1.5712 1.2712 0.0740  -0.2060 -0.0010 312 HIS F O   
16748 C CB  . HIS F 312 ? 1.5277 1.5161 1.2123 0.0734  -0.2111 -0.0180 312 HIS F CB  
16749 C CG  . HIS F 312 ? 1.5447 1.5282 1.2234 0.0734  -0.2172 -0.0277 312 HIS F CG  
16750 N ND1 . HIS F 312 ? 1.5453 1.5395 1.2446 0.0711  -0.2102 -0.0332 312 HIS F ND1 
16751 C CD2 . HIS F 312 ? 1.5417 1.5104 1.1962 0.0754  -0.2300 -0.0330 312 HIS F CD2 
16752 C CE1 . HIS F 312 ? 1.5398 1.5258 1.2283 0.0716  -0.2182 -0.0416 312 HIS F CE1 
16753 N NE2 . HIS F 312 ? 1.5331 1.5038 1.1943 0.0741  -0.2303 -0.0419 312 HIS F NE2 
16754 N N   . SER F 313 ? 1.5753 1.5969 1.3237 0.0737  -0.2206 -0.0042 313 SER F N   
16755 C CA  . SER F 313 ? 1.5368 1.5629 1.2928 0.0738  -0.2157 0.0040  313 SER F CA  
16756 C C   . SER F 313 ? 1.6346 1.6498 1.3765 0.0773  -0.2305 0.0075  313 SER F C   
16757 O O   . SER F 313 ? 1.7594 1.7627 1.4827 0.0796  -0.2435 0.0039  313 SER F O   
16758 C CB  . SER F 313 ? 1.4351 1.4840 1.2309 0.0719  -0.2121 0.0041  313 SER F CB  
16759 O OG  . SER F 313 ? 1.3983 1.4560 1.2051 0.0689  -0.1976 0.0021  313 SER F OG  
16760 N N   . THR F 314 ? 1.5845 1.6033 1.3348 0.0780  -0.2290 0.0144  314 THR F N   
16761 C CA  . THR F 314 ? 1.6135 1.6214 1.3507 0.0815  -0.2424 0.0185  314 THR F CA  
16762 C C   . THR F 314 ? 1.5224 1.5431 1.2859 0.0820  -0.2429 0.0233  314 THR F C   
16763 O O   . THR F 314 ? 1.4724 1.4963 1.2401 0.0801  -0.2294 0.0286  314 THR F O   
16764 C CB  . THR F 314 ? 1.6450 1.6308 1.3428 0.0824  -0.2379 0.0241  314 THR F CB  
16765 O OG1 . THR F 314 ? 1.7872 1.7601 1.4589 0.0827  -0.2399 0.0189  314 THR F OG1 
16766 C CG2 . THR F 314 ? 1.6100 1.5849 1.2962 0.0862  -0.2510 0.0297  314 THR F CG2 
16767 N N   . VAL F 315 ? 1.5441 1.5721 1.3254 0.0845  -0.2583 0.0210  315 VAL F N   
16768 C CA  . VAL F 315 ? 1.4905 1.5294 1.2956 0.0858  -0.2612 0.0248  315 VAL F CA  
16769 C C   . VAL F 315 ? 1.5081 1.5305 1.2922 0.0900  -0.2724 0.0301  315 VAL F C   
16770 O O   . VAL F 315 ? 1.6047 1.6183 1.3767 0.0931  -0.2879 0.0275  315 VAL F O   
16771 C CB  . VAL F 315 ? 1.5203 1.5791 1.3606 0.0861  -0.2704 0.0189  315 VAL F CB  
16772 C CG1 . VAL F 315 ? 1.4481 1.5171 1.3110 0.0880  -0.2741 0.0226  315 VAL F CG1 
16773 C CG2 . VAL F 315 ? 1.5687 1.6433 1.4295 0.0818  -0.2588 0.0145  315 VAL F CG2 
16774 N N   . GLY F 316 ? 1.4533 1.4713 1.2333 0.0900  -0.2649 0.0377  316 GLY F N   
16775 C CA  . GLY F 316 ? 1.5070 1.5081 1.2666 0.0938  -0.2745 0.0436  316 GLY F CA  
16776 C C   . GLY F 316 ? 1.4895 1.4975 1.2688 0.0981  -0.2919 0.0421  316 GLY F C   
16777 O O   . GLY F 316 ? 1.4407 1.4679 1.2515 0.0979  -0.2958 0.0366  316 GLY F O   
16778 N N   . GLN F 317 ? 1.5250 1.5168 1.2851 0.1022  -0.3025 0.0472  317 GLN F N   
16779 C CA  . GLN F 317 ? 1.4973 1.4938 1.2742 0.1070  -0.3197 0.0462  317 GLN F CA  
16780 C C   . GLN F 317 ? 1.5148 1.5273 1.3237 0.1069  -0.3145 0.0482  317 GLN F C   
16781 O O   . GLN F 317 ? 1.5316 1.5430 1.3394 0.1043  -0.3004 0.0535  317 GLN F O   
16782 C CB  . GLN F 317 ? 1.5295 1.5032 1.2761 0.1117  -0.3323 0.0518  317 GLN F CB  
16783 C CG  . GLN F 317 ? 1.5169 1.4747 1.2312 0.1126  -0.3400 0.0493  317 GLN F CG  
16784 C CD  . GLN F 317 ? 1.4650 1.3996 1.1476 0.1173  -0.3524 0.0555  317 GLN F CD  
16785 O OE1 . GLN F 317 ? 1.5249 1.4548 1.2104 0.1201  -0.3559 0.0618  317 GLN F OE1 
16786 N NE2 . GLN F 317 ? 1.3813 1.3007 1.0331 0.1182  -0.3593 0.0536  317 GLN F NE2 
16787 N N   . TRP F 318 ? 1.5229 1.5505 1.3608 0.1096  -0.3261 0.0437  318 TRP F N   
16788 C CA  . TRP F 318 ? 1.5034 1.5472 1.3735 0.1102  -0.3235 0.0443  318 TRP F CA  
16789 C C   . TRP F 318 ? 1.4768 1.5366 1.3657 0.1047  -0.3050 0.0434  318 TRP F C   
16790 O O   . TRP F 318 ? 1.4629 1.5333 1.3728 0.1045  -0.2993 0.0452  318 TRP F O   
16791 C CB  . TRP F 318 ? 1.5325 1.5630 1.3926 0.1136  -0.3262 0.0521  318 TRP F CB  
16792 C CG  . TRP F 318 ? 1.5803 1.5999 1.4319 0.1200  -0.3461 0.0528  318 TRP F CG  
16793 C CD1 . TRP F 318 ? 1.5772 1.6089 1.4546 0.1242  -0.3601 0.0487  318 TRP F CD1 
16794 C CD2 . TRP F 318 ? 1.6364 1.6308 1.4513 0.1229  -0.3542 0.0582  318 TRP F CD2 
16795 N NE1 . TRP F 318 ? 1.6091 1.6249 1.4688 0.1299  -0.3770 0.0510  318 TRP F NE1 
16796 C CE2 . TRP F 318 ? 1.6304 1.6228 1.4509 0.1292  -0.3739 0.0570  318 TRP F CE2 
16797 C CE3 . TRP F 318 ? 1.6450 1.6185 1.4225 0.1209  -0.3467 0.0639  318 TRP F CE3 
16798 C CZ2 . TRP F 318 ? 1.6345 1.6042 1.4241 0.1336  -0.3868 0.0616  318 TRP F CZ2 
16799 C CZ3 . TRP F 318 ? 1.6779 1.6289 1.4241 0.1250  -0.3588 0.0685  318 TRP F CZ3 
16800 C CH2 . TRP F 318 ? 1.7033 1.6523 1.4553 0.1313  -0.3789 0.0675  318 TRP F CH2 
16801 N N   . ALA F 319 ? 1.4459 1.5074 1.3275 0.1005  -0.2955 0.0405  319 ALA F N   
16802 C CA  . ALA F 319 ? 1.3926 1.4693 1.2920 0.0956  -0.2786 0.0396  319 ALA F CA  
16803 C C   . ALA F 319 ? 1.3690 1.4694 1.3042 0.0948  -0.2815 0.0329  319 ALA F C   
16804 O O   . ALA F 319 ? 1.3953 1.4992 1.3353 0.0959  -0.2925 0.0273  319 ALA F O   
16805 C CB  . ALA F 319 ? 1.4243 1.4932 1.3021 0.0917  -0.2670 0.0393  319 ALA F CB  
16806 N N   . ARG F 320 ? 1.3816 1.4983 1.3418 0.0927  -0.2714 0.0334  320 ARG F N   
16807 C CA  . ARG F 320 ? 1.3683 1.5082 1.3629 0.0916  -0.2724 0.0276  320 ARG F CA  
16808 C C   . ARG F 320 ? 1.2745 1.4256 1.2777 0.0863  -0.2570 0.0260  320 ARG F C   
16809 O O   . ARG F 320 ? 1.2093 1.3600 1.2091 0.0839  -0.2433 0.0301  320 ARG F O   
16810 C CB  . ARG F 320 ? 1.3237 1.4758 1.3434 0.0938  -0.2743 0.0286  320 ARG F CB  
16811 C CG  . ARG F 320 ? 1.3014 1.4778 1.3561 0.0926  -0.2752 0.0227  320 ARG F CG  
16812 C CD  . ARG F 320 ? 1.2931 1.4824 1.3728 0.0949  -0.2764 0.0230  320 ARG F CD  
16813 N NE  . ARG F 320 ? 1.3309 1.5435 1.4432 0.0936  -0.2769 0.0173  320 ARG F NE  
16814 C CZ  . ARG F 320 ? 1.3459 1.5665 1.4744 0.0964  -0.2903 0.0128  320 ARG F CZ  
16815 N NH1 . ARG F 320 ? 1.3939 1.6012 1.5091 0.1010  -0.3048 0.0131  320 ARG F NH1 
16816 N NH2 . ARG F 320 ? 1.3030 1.5453 1.4612 0.0946  -0.2891 0.0080  320 ARG F NH2 
16817 N N   . ILE F 321 ? 1.2825 1.4434 1.2971 0.0845  -0.2595 0.0202  321 ILE F N   
16818 C CA  . ILE F 321 ? 1.2116 1.3829 1.2350 0.0798  -0.2465 0.0182  321 ILE F CA  
16819 C C   . ILE F 321 ? 1.2164 1.4102 1.2742 0.0787  -0.2490 0.0133  321 ILE F C   
16820 O O   . ILE F 321 ? 1.2591 1.4566 1.3261 0.0803  -0.2619 0.0090  321 ILE F O   
16821 C CB  . ILE F 321 ? 1.2394 1.3987 1.2405 0.0783  -0.2462 0.0157  321 ILE F CB  
16822 C CG1 . ILE F 321 ? 1.3311 1.4673 1.2964 0.0798  -0.2452 0.0203  321 ILE F CG1 
16823 C CG2 . ILE F 321 ? 1.2312 1.4004 1.2413 0.0738  -0.2323 0.0140  321 ILE F CG2 
16824 C CD1 . ILE F 321 ? 1.3426 1.4759 1.3008 0.0779  -0.2298 0.0262  321 ILE F CD1 
16825 N N   . GLU F 322 ? 1.1953 1.4044 1.2724 0.0757  -0.2368 0.0142  322 GLU F N   
16826 C CA  . GLU F 322 ? 1.1459 1.3767 1.2553 0.0743  -0.2377 0.0102  322 GLU F CA  
16827 C C   . GLU F 322 ? 1.0616 1.3050 1.1832 0.0701  -0.2221 0.0110  322 GLU F C   
16828 O O   . GLU F 322 ? 1.0929 1.3293 1.2005 0.0686  -0.2109 0.0147  322 GLU F O   
16829 C CB  . GLU F 322 ? 1.1356 1.3758 1.2639 0.0775  -0.2445 0.0104  322 GLU F CB  
16830 C CG  . GLU F 322 ? 1.0741 1.3159 1.2043 0.0777  -0.2347 0.0152  322 GLU F CG  
16831 C CD  . GLU F 322 ? 1.1132 1.3653 1.2640 0.0809  -0.2410 0.0145  322 GLU F CD  
16832 O OE1 . GLU F 322 ? 1.1762 1.4337 1.3392 0.0834  -0.2534 0.0107  322 GLU F OE1 
16833 O OE2 . GLU F 322 ? 1.1282 1.3835 1.2839 0.0810  -0.2336 0.0176  322 GLU F OE2 
16834 N N   . ASN F 323 ? 1.0037 1.2658 1.1520 0.0681  -0.2218 0.0075  323 ASN F N   
16835 C CA  . ASN F 323 ? 0.9989 1.2764 1.1643 0.0645  -0.2086 0.0083  323 ASN F CA  
16836 C C   . ASN F 323 ? 1.0206 1.2915 1.1717 0.0613  -0.1982 0.0091  323 ASN F C   
16837 O O   . ASN F 323 ? 1.0469 1.3163 1.1916 0.0600  -0.1864 0.0127  323 ASN F O   
16838 C CB  . ASN F 323 ? 1.0084 1.2913 1.1803 0.0653  -0.2018 0.0121  323 ASN F CB  
16839 C CG  . ASN F 323 ? 0.9321 1.2334 1.1249 0.0620  -0.1901 0.0124  323 ASN F CG  
16840 O OD1 . ASN F 323 ? 0.8798 1.1927 1.0875 0.0595  -0.1890 0.0096  323 ASN F OD1 
16841 N ND2 . ASN F 323 ? 0.9607 1.2645 1.1545 0.0619  -0.1816 0.0158  323 ASN F ND2 
16842 N N   . MET F 324 ? 1.0357 1.3028 1.1829 0.0602  -0.2029 0.0054  324 MET F N   
16843 C CA  . MET F 324 ? 1.0767 1.3399 1.2150 0.0573  -0.1940 0.0049  324 MET F CA  
16844 C C   . MET F 324 ? 1.1594 1.4062 1.2704 0.0578  -0.1861 0.0086  324 MET F C   
16845 O O   . MET F 324 ? 1.2462 1.4952 1.3559 0.0557  -0.1734 0.0106  324 MET F O   
16846 C CB  . MET F 324 ? 1.0251 1.3065 1.1867 0.0539  -0.1837 0.0052  324 MET F CB  
16847 C CG  . MET F 324 ? 1.0750 1.3729 1.2635 0.0528  -0.1902 0.0017  324 MET F CG  
16848 S SD  . MET F 324 ? 1.1613 1.4813 1.3768 0.0492  -0.1782 0.0032  324 MET F SD  
16849 C CE  . MET F 324 ? 0.9335 1.2568 1.1487 0.0510  -0.1713 0.0078  324 MET F CE  
16850 N N   . THR F 325 ? 1.2479 1.4784 1.3371 0.0608  -0.1937 0.0095  325 THR F N   
16851 C CA  . THR F 325 ? 1.3518 1.5653 1.4129 0.0612  -0.1870 0.0130  325 THR F CA  
16852 C C   . THR F 325 ? 1.6352 1.8378 1.6790 0.0602  -0.1862 0.0098  325 THR F C   
16853 O O   . THR F 325 ? 1.6286 1.8253 1.6671 0.0613  -0.1975 0.0057  325 THR F O   
16854 C CB  . THR F 325 ? 1.2991 1.4986 1.3426 0.0648  -0.1955 0.0157  325 THR F CB  
16855 O OG1 . THR F 325 ? 1.2511 1.4609 1.3124 0.0660  -0.1972 0.0180  325 THR F OG1 
16856 C CG2 . THR F 325 ? 1.4971 1.6797 1.5122 0.0647  -0.1871 0.0201  325 THR F CG2 
16857 N N   . ILE F 326 ? 2.2108 2.4108 2.2462 0.0582  -0.1729 0.0113  326 ILE F N   
16858 C CA  . ILE F 326 ? 2.2420 2.4335 2.2636 0.0571  -0.1698 0.0080  326 ILE F CA  
16859 C C   . ILE F 326 ? 2.3125 2.4847 2.3019 0.0583  -0.1654 0.0105  326 ILE F C   
16860 O O   . ILE F 326 ? 2.3091 2.4804 2.2933 0.0576  -0.1544 0.0151  326 ILE F O   
16861 C CB  . ILE F 326 ? 2.2284 2.4326 2.2667 0.0541  -0.1579 0.0073  326 ILE F CB  
16862 C CG1 . ILE F 326 ? 2.1841 2.4081 2.2543 0.0527  -0.1611 0.0060  326 ILE F CG1 
16863 C CG2 . ILE F 326 ? 2.2553 2.4508 2.2815 0.0533  -0.1562 0.0030  326 ILE F CG2 
16864 C CD1 . ILE F 326 ? 2.1756 2.4006 2.2533 0.0530  -0.1746 0.0009  326 ILE F CD1 
16865 N N   . LEU F 327 ? 2.9864 3.1434 2.9543 0.0598  -0.1737 0.0074  327 LEU F N   
16866 C CA  . LEU F 327 ? 3.0305 3.1680 2.9654 0.0610  -0.1705 0.0094  327 LEU F CA  
16867 C C   . LEU F 327 ? 3.0519 3.1817 2.9731 0.0600  -0.1654 0.0049  327 LEU F C   
16868 O O   . LEU F 327 ? 3.0420 3.1745 2.9709 0.0596  -0.1721 -0.0008 327 LEU F O   
16869 C CB  . LEU F 327 ? 3.0438 3.1675 2.9604 0.0642  -0.1848 0.0098  327 LEU F CB  
16870 C CG  . LEU F 327 ? 3.0251 3.1531 2.9517 0.0659  -0.1911 0.0142  327 LEU F CG  
16871 C CD1 . LEU F 327 ? 3.0551 3.1665 2.9590 0.0694  -0.2046 0.0150  327 LEU F CD1 
16872 C CD2 . LEU F 327 ? 3.0258 3.1566 2.9539 0.0647  -0.1778 0.0204  327 LEU F CD2 
16873 N N   . GLY F 328 ? 2.1118 2.2321 2.0132 0.0596  -0.1534 0.0074  328 GLY F N   
16874 C CA  . GLY F 328 ? 1.7868 1.8982 1.6723 0.0591  -0.1478 0.0032  328 GLY F CA  
16875 C C   . GLY F 328 ? 1.6232 1.7147 1.4776 0.0613  -0.1569 0.0006  328 GLY F C   
16876 O O   . GLY F 328 ? 1.6391 1.7239 1.4850 0.0633  -0.1691 0.0019  328 GLY F O   
16877 N N   . GLU F 329 ? 1.5029 1.5848 1.3399 0.0611  -0.1510 -0.0033 329 GLU F N   
16878 C CA  . GLU F 329 ? 1.3897 1.4520 1.1946 0.0631  -0.1583 -0.0063 329 GLU F CA  
16879 C C   . GLU F 329 ? 1.3449 1.3936 1.1229 0.0642  -0.1541 0.0001  329 GLU F C   
16880 O O   . GLU F 329 ? 1.3807 1.4314 1.1575 0.0629  -0.1398 0.0047  329 GLU F O   
16881 C CB  . GLU F 329 ? 1.4036 1.4597 1.1976 0.0627  -0.1520 -0.0126 329 GLU F CB  
16882 C CG  . GLU F 329 ? 1.3797 1.4148 1.1378 0.0647  -0.1577 -0.0160 329 GLU F CG  
16883 C CD  . GLU F 329 ? 1.3973 1.4261 1.1442 0.0644  -0.1500 -0.0225 329 GLU F CD  
16884 O OE1 . GLU F 329 ? 1.3987 1.4395 1.1675 0.0628  -0.1416 -0.0246 329 GLU F OE1 
16885 O OE2 . GLU F 329 ? 1.4916 1.5031 1.2074 0.0660  -0.1524 -0.0255 329 GLU F OE2 
16886 N N   . ASP F 330 ? 1.3497 1.3845 1.1063 0.0666  -0.1669 0.0004  330 ASP F N   
16887 C CA  . ASP F 330 ? 1.3765 1.3955 1.1040 0.0678  -0.1647 0.0065  330 ASP F CA  
16888 C C   . ASP F 330 ? 1.3807 1.4079 1.1220 0.0668  -0.1583 0.0145  330 ASP F C   
16889 O O   . ASP F 330 ? 1.3770 1.4019 1.1103 0.0652  -0.1441 0.0192  330 ASP F O   
16890 C CB  . ASP F 330 ? 1.3523 1.3583 1.0518 0.0672  -0.1521 0.0054  330 ASP F CB  
16891 C CG  . ASP F 330 ? 1.4087 1.3976 1.0764 0.0680  -0.1492 0.0119  330 ASP F CG  
16892 O OD1 . ASP F 330 ? 1.5059 1.4809 1.1520 0.0704  -0.1622 0.0121  330 ASP F OD1 
16893 O OD2 . ASP F 330 ? 1.3763 1.3658 1.0409 0.0662  -0.1340 0.0170  330 ASP F OD2 
16894 N N   . VAL F 331 ? 1.3962 1.4335 1.1595 0.0676  -0.1690 0.0156  331 VAL F N   
16895 C CA  . VAL F 331 ? 1.4158 1.4606 1.1932 0.0672  -0.1658 0.0225  331 VAL F CA  
16896 C C   . VAL F 331 ? 1.4755 1.5093 1.2401 0.0702  -0.1801 0.0259  331 VAL F C   
16897 O O   . VAL F 331 ? 1.4794 1.5142 1.2497 0.0724  -0.1955 0.0220  331 VAL F O   
16898 C CB  . VAL F 331 ? 1.5129 1.5804 1.3294 0.0657  -0.1648 0.0210  331 VAL F CB  
16899 C CG1 . VAL F 331 ? 1.6237 1.6978 1.4533 0.0656  -0.1628 0.0275  331 VAL F CG1 
16900 C CG2 . VAL F 331 ? 1.5245 1.6022 1.3530 0.0629  -0.1506 0.0184  331 VAL F CG2 
16901 N N   . HIS F 332 ? 1.5138 1.5372 1.2618 0.0704  -0.1752 0.0331  332 HIS F N   
16902 C CA  . HIS F 332 ? 1.5476 1.5572 1.2785 0.0735  -0.1877 0.0373  332 HIS F CA  
16903 C C   . HIS F 332 ? 1.5181 1.5371 1.2706 0.0738  -0.1887 0.0426  332 HIS F C   
16904 O O   . HIS F 332 ? 1.5580 1.5763 1.3095 0.0718  -0.1769 0.0484  332 HIS F O   
16905 C CB  . HIS F 332 ? 1.5883 1.5762 1.2803 0.0736  -0.1821 0.0418  332 HIS F CB  
16906 C CG  . HIS F 332 ? 1.6132 1.5910 1.2822 0.0737  -0.1818 0.0362  332 HIS F CG  
16907 N ND1 . HIS F 332 ? 1.7538 1.7162 1.3981 0.0767  -0.1958 0.0340  332 HIS F ND1 
16908 C CD2 . HIS F 332 ? 1.6030 1.5839 1.2704 0.0714  -0.1695 0.0319  332 HIS F CD2 
16909 C CE1 . HIS F 332 ? 1.7716 1.7279 1.3993 0.0761  -0.1919 0.0284  332 HIS F CE1 
16910 N NE2 . HIS F 332 ? 1.7063 1.6735 1.3480 0.0730  -0.1759 0.0269  332 HIS F NE2 
16911 N N   . VAL F 333 ? 1.4667 1.4943 1.2390 0.0762  -0.2029 0.0402  333 VAL F N   
16912 C CA  . VAL F 333 ? 1.4897 1.5261 1.2832 0.0771  -0.2060 0.0441  333 VAL F CA  
16913 C C   . VAL F 333 ? 1.4704 1.4889 1.2418 0.0806  -0.2165 0.0496  333 VAL F C   
16914 O O   . VAL F 333 ? 1.4611 1.4696 1.2184 0.0838  -0.2309 0.0474  333 VAL F O   
16915 C CB  . VAL F 333 ? 1.4836 1.5392 1.3108 0.0781  -0.2155 0.0386  333 VAL F CB  
16916 C CG1 . VAL F 333 ? 1.4703 1.5352 1.3192 0.0793  -0.2180 0.0422  333 VAL F CG1 
16917 C CG2 . VAL F 333 ? 1.5524 1.6242 1.3993 0.0746  -0.2056 0.0336  333 VAL F CG2 
16918 N N   . SER F 334 ? 1.4881 1.5019 1.2564 0.0800  -0.2095 0.0568  334 SER F N   
16919 C CA  . SER F 334 ? 1.5323 1.5285 1.2803 0.0832  -0.2188 0.0628  334 SER F CA  
16920 C C   . SER F 334 ? 1.5359 1.5386 1.3030 0.0875  -0.2362 0.0609  334 SER F C   
16921 O O   . SER F 334 ? 1.5172 1.5390 1.3143 0.0875  -0.2397 0.0553  334 SER F O   
16922 C CB  . SER F 334 ? 1.5701 1.5611 1.3139 0.0811  -0.2069 0.0708  334 SER F CB  
16923 O OG  . SER F 334 ? 1.5955 1.5801 1.3211 0.0772  -0.1909 0.0727  334 SER F OG  
16924 N N   . ASP F 335 ? 1.6105 1.5970 1.3597 0.0912  -0.2471 0.0658  335 ASP F N   
16925 C CA  . ASP F 335 ? 1.6099 1.6014 1.3765 0.0958  -0.2637 0.0646  335 ASP F CA  
16926 C C   . ASP F 335 ? 1.6536 1.6601 1.4508 0.0953  -0.2588 0.0663  335 ASP F C   
16927 O O   . ASP F 335 ? 1.6468 1.6524 1.4434 0.0922  -0.2449 0.0711  335 ASP F O   
16928 C CB  . ASP F 335 ? 1.7066 1.6758 1.4449 0.1002  -0.2767 0.0699  335 ASP F CB  
16929 C CG  . ASP F 335 ? 1.7583 1.7112 1.4631 0.1008  -0.2816 0.0685  335 ASP F CG  
16930 O OD1 . ASP F 335 ? 1.7161 1.6772 1.4253 0.0992  -0.2810 0.0613  335 ASP F OD1 
16931 O OD2 . ASP F 335 ? 1.8269 1.7583 1.5004 0.1029  -0.2862 0.0745  335 ASP F OD2 
16932 N N   . GLU F 336 ? 1.6770 1.6974 1.5015 0.0983  -0.2704 0.0621  336 GLU F N   
16933 C CA  . GLU F 336 ? 1.6569 1.6910 1.5106 0.0989  -0.2688 0.0630  336 GLU F CA  
16934 C C   . GLU F 336 ? 1.6400 1.6914 1.5143 0.0938  -0.2516 0.0616  336 GLU F C   
16935 O O   . GLU F 336 ? 1.6301 1.6881 1.5202 0.0932  -0.2455 0.0642  336 GLU F O   
16936 C CB  . GLU F 336 ? 1.6787 1.6967 1.5190 0.1014  -0.2710 0.0710  336 GLU F CB  
16937 C CG  . GLU F 336 ? 1.7030 1.6998 1.5160 0.1062  -0.2863 0.0741  336 GLU F CG  
16938 C CD  . GLU F 336 ? 1.7276 1.7043 1.5193 0.1072  -0.2845 0.0834  336 GLU F CD  
16939 O OE1 . GLU F 336 ? 1.7227 1.7044 1.5284 0.1054  -0.2751 0.0866  336 GLU F OE1 
16940 O OE2 . GLU F 336 ? 1.7474 1.7030 1.5081 0.1096  -0.2924 0.0876  336 GLU F OE2 
16941 N N   . ILE F 337 ? 1.5226 1.5810 1.3969 0.0903  -0.2439 0.0574  337 ILE F N   
16942 C CA  . ILE F 337 ? 1.4689 1.5426 1.3604 0.0855  -0.2277 0.0562  337 ILE F CA  
16943 C C   . ILE F 337 ? 1.4518 1.5489 1.3774 0.0853  -0.2307 0.0494  337 ILE F C   
16944 O O   . ILE F 337 ? 1.4492 1.5499 1.3787 0.0868  -0.2409 0.0442  337 ILE F O   
16945 C CB  . ILE F 337 ? 1.4983 1.5650 1.3689 0.0818  -0.2161 0.0561  337 ILE F CB  
16946 C CG1 . ILE F 337 ? 1.5768 1.6206 1.4135 0.0817  -0.2119 0.0631  337 ILE F CG1 
16947 C CG2 . ILE F 337 ? 1.5391 1.6226 1.4292 0.0773  -0.2002 0.0546  337 ILE F CG2 
16948 C CD1 . ILE F 337 ? 1.5579 1.6008 1.3985 0.0799  -0.2017 0.0694  337 ILE F CD1 
16949 N N   . TYR F 338 ? 1.4487 1.5617 1.3988 0.0833  -0.2218 0.0495  338 TYR F N   
16950 C CA  . TYR F 338 ? 1.3450 1.4811 1.3281 0.0827  -0.2226 0.0439  338 TYR F CA  
16951 C C   . TYR F 338 ? 1.3549 1.5031 1.3470 0.0778  -0.2075 0.0424  338 TYR F C   
16952 O O   . TYR F 338 ? 1.4008 1.5462 1.3865 0.0751  -0.1947 0.0463  338 TYR F O   
16953 C CB  . TYR F 338 ? 1.3003 1.4464 1.3061 0.0847  -0.2253 0.0448  338 TYR F CB  
16954 C CG  . TYR F 338 ? 1.2706 1.4414 1.3102 0.0833  -0.2227 0.0398  338 TYR F CG  
16955 C CD1 . TYR F 338 ? 1.2685 1.4503 1.3247 0.0850  -0.2335 0.0341  338 TYR F CD1 
16956 C CD2 . TYR F 338 ? 1.2449 1.4282 1.2997 0.0801  -0.2095 0.0407  338 TYR F CD2 
16957 C CE1 . TYR F 338 ? 1.2250 1.4292 1.3115 0.0835  -0.2306 0.0299  338 TYR F CE1 
16958 C CE2 . TYR F 338 ? 1.1590 1.3644 1.2432 0.0788  -0.2070 0.0364  338 TYR F CE2 
16959 C CZ  . TYR F 338 ? 1.1308 1.3465 1.2305 0.0804  -0.2173 0.0312  338 TYR F CZ  
16960 O OH  . TYR F 338 ? 1.0902 1.3279 1.2186 0.0789  -0.2143 0.0273  338 TYR F OH  
16961 N N   . SER F 339 ? 1.3163 1.4777 1.3236 0.0766  -0.2091 0.0367  339 SER F N   
16962 C CA  . SER F 339 ? 1.2652 1.4385 1.2825 0.0723  -0.1962 0.0348  339 SER F CA  
16963 C C   . SER F 339 ? 1.2210 1.4169 1.2714 0.0716  -0.1978 0.0304  339 SER F C   
16964 O O   . SER F 339 ? 1.2024 1.4032 1.2625 0.0733  -0.2091 0.0262  339 SER F O   
16965 C CB  . SER F 339 ? 1.2617 1.4259 1.2603 0.0710  -0.1952 0.0325  339 SER F CB  
16966 O OG  . SER F 339 ? 1.4338 1.5781 1.4014 0.0711  -0.1910 0.0367  339 SER F OG  
16967 N N   . ASN F 340 ? 1.2045 1.4143 1.2721 0.0690  -0.1864 0.0314  340 ASN F N   
16968 C CA  . ASN F 340 ? 1.1036 1.3354 1.2019 0.0680  -0.1861 0.0278  340 ASN F CA  
16969 C C   . ASN F 340 ? 1.0519 1.2941 1.1582 0.0639  -0.1745 0.0264  340 ASN F C   
16970 O O   . ASN F 340 ? 1.0779 1.3329 1.1993 0.0618  -0.1649 0.0275  340 ASN F O   
16971 C CB  . ASN F 340 ? 1.0873 1.3285 1.2023 0.0689  -0.1842 0.0295  340 ASN F CB  
16972 C CG  . ASN F 340 ? 1.0614 1.3244 1.2071 0.0686  -0.1860 0.0255  340 ASN F CG  
16973 O OD1 . ASN F 340 ? 1.0282 1.2972 1.1832 0.0691  -0.1940 0.0215  340 ASN F OD1 
16974 N ND2 . ASN F 340 ? 1.1252 1.4005 1.2869 0.0675  -0.1783 0.0265  340 ASN F ND2 
16975 N N   . GLY F 341 ? 1.0911 1.3278 1.1871 0.0628  -0.1754 0.0240  341 GLY F N   
16976 C CA  . GLY F 341 ? 1.0493 1.2951 1.1530 0.0594  -0.1653 0.0226  341 GLY F CA  
16977 C C   . GLY F 341 ? 1.1191 1.3544 1.2032 0.0577  -0.1535 0.0257  341 GLY F C   
16978 O O   . GLY F 341 ? 1.1159 1.3606 1.2089 0.0551  -0.1418 0.0267  341 GLY F O   
16979 N N   . GLY F 342 ? 1.1864 1.4024 1.2434 0.0592  -0.1564 0.0271  342 GLY F N   
16980 C CA  . GLY F 342 ? 1.2355 1.4405 1.2722 0.0577  -0.1451 0.0299  342 GLY F CA  
16981 C C   . GLY F 342 ? 1.3917 1.5919 1.4183 0.0565  -0.1426 0.0266  342 GLY F C   
16982 O O   . GLY F 342 ? 1.5512 1.7393 1.5619 0.0582  -0.1515 0.0241  342 GLY F O   
16983 N N   . VAL F 343 ? 1.3195 1.5289 1.3553 0.0540  -0.1310 0.0262  343 VAL F N   
16984 C CA  . VAL F 343 ? 1.4304 1.6355 1.4579 0.0529  -0.1272 0.0229  343 VAL F CA  
16985 C C   . VAL F 343 ? 1.4358 1.6247 1.4359 0.0529  -0.1190 0.0255  343 VAL F C   
16986 O O   . VAL F 343 ? 1.3895 1.5816 1.3904 0.0513  -0.1065 0.0284  343 VAL F O   
16987 C CB  . VAL F 343 ? 1.3199 1.5418 1.3699 0.0505  -0.1188 0.0216  343 VAL F CB  
16988 C CG1 . VAL F 343 ? 1.3601 1.5770 1.4031 0.0499  -0.1170 0.0176  343 VAL F CG1 
16989 C CG2 . VAL F 343 ? 1.2730 1.5119 1.3505 0.0502  -0.1253 0.0203  343 VAL F CG2 
16990 N N   . VAL F 344 ? 1.5442 1.7158 1.5197 0.0548  -0.1262 0.0242  344 VAL F N   
16991 C CA  . VAL F 344 ? 1.5461 1.7005 1.4927 0.0550  -0.1200 0.0271  344 VAL F CA  
16992 C C   . VAL F 344 ? 1.6009 1.7480 1.5334 0.0545  -0.1145 0.0233  344 VAL F C   
16993 O O   . VAL F 344 ? 1.6515 1.7995 1.5877 0.0550  -0.1211 0.0180  344 VAL F O   
16994 C CB  . VAL F 344 ? 1.5876 1.7263 1.5138 0.0576  -0.1315 0.0290  344 VAL F CB  
16995 C CG1 . VAL F 344 ? 1.6289 1.7501 1.5252 0.0576  -0.1242 0.0331  344 VAL F CG1 
16996 C CG2 . VAL F 344 ? 1.5245 1.6714 1.4678 0.0586  -0.1382 0.0318  344 VAL F CG2 
16997 N N   . LEU F 345 ? 1.6869 1.8269 1.6038 0.0535  -0.1020 0.0258  345 LEU F N   
16998 C CA  . LEU F 345 ? 1.6737 1.8053 1.5746 0.0533  -0.0954 0.0224  345 LEU F CA  
16999 C C   . LEU F 345 ? 1.7013 1.8126 1.5710 0.0554  -0.1032 0.0209  345 LEU F C   
17000 O O   . LEU F 345 ? 1.7230 1.8248 1.5795 0.0567  -0.1104 0.0243  345 LEU F O   
17001 C CB  . LEU F 345 ? 1.7187 1.8516 1.6161 0.0515  -0.0786 0.0257  345 LEU F CB  
17002 C CG  . LEU F 345 ? 1.6435 1.7936 1.5657 0.0498  -0.0687 0.0243  345 LEU F CG  
17003 C CD1 . LEU F 345 ? 1.5684 1.7364 1.5202 0.0489  -0.0723 0.0260  345 LEU F CD1 
17004 C CD2 . LEU F 345 ? 1.6853 1.8346 1.6008 0.0483  -0.0528 0.0273  345 LEU F CD2 
17005 N N   . PRO F 346 ? 1.4982 1.6022 1.3554 0.0558  -0.1023 0.0156  346 PRO F N   
17006 C CA  . PRO F 346 ? 1.4421 1.5264 1.2681 0.0578  -0.1096 0.0136  346 PRO F CA  
17007 C C   . PRO F 346 ? 1.3868 1.4568 1.1853 0.0577  -0.1013 0.0186  346 PRO F C   
17008 O O   . PRO F 346 ? 1.4078 1.4823 1.2096 0.0559  -0.0874 0.0224  346 PRO F O   
17009 C CB  . PRO F 346 ? 1.4189 1.5010 1.2413 0.0579  -0.1075 0.0064  346 PRO F CB  
17010 C CG  . PRO F 346 ? 1.4213 1.5181 1.2654 0.0559  -0.0940 0.0066  346 PRO F CG  
17011 C CD  . PRO F 346 ? 1.4667 1.5797 1.3381 0.0548  -0.0954 0.0109  346 PRO F CD  
17012 N N   . HIS F 347 ? 1.3639 1.4163 1.1345 0.0597  -0.1102 0.0187  347 HIS F N   
17013 C CA  . HIS F 347 ? 1.3292 1.3652 1.0694 0.0598  -0.1042 0.0236  347 HIS F CA  
17014 C C   . HIS F 347 ? 1.3337 1.3742 1.0821 0.0584  -0.0987 0.0316  347 HIS F C   
17015 O O   . HIS F 347 ? 1.3098 1.3502 1.0540 0.0563  -0.0843 0.0354  347 HIS F O   
17016 C CB  . HIS F 347 ? 1.3033 1.3335 1.0275 0.0588  -0.0897 0.0211  347 HIS F CB  
17017 C CG  . HIS F 347 ? 1.3062 1.3322 1.0237 0.0602  -0.0944 0.0127  347 HIS F CG  
17018 N ND1 . HIS F 347 ? 1.3401 1.3507 1.0334 0.0624  -0.1069 0.0094  347 HIS F ND1 
17019 C CD2 . HIS F 347 ? 1.3154 1.3503 1.0474 0.0596  -0.0888 0.0067  347 HIS F CD2 
17020 C CE1 . HIS F 347 ? 1.3852 1.3954 1.0786 0.0630  -0.1086 0.0015  347 HIS F CE1 
17021 N NE2 . HIS F 347 ? 1.3822 1.4067 1.0989 0.0614  -0.0977 -0.0002 347 HIS F NE2 
17022 N N   . LYS F 348 ? 1.3445 1.3889 1.1053 0.0596  -0.1109 0.0337  348 LYS F N   
17023 C CA  . LYS F 348 ? 1.4310 1.4801 1.2023 0.0586  -0.1081 0.0406  348 LYS F CA  
17024 C C   . LYS F 348 ? 1.4733 1.5118 1.2339 0.0612  -0.1230 0.0437  348 LYS F C   
17025 O O   . LYS F 348 ? 1.4577 1.4971 1.2232 0.0636  -0.1375 0.0398  348 LYS F O   
17026 C CB  . LYS F 348 ? 1.4746 1.5462 1.2835 0.0571  -0.1056 0.0397  348 LYS F CB  
17027 C CG  . LYS F 348 ? 1.5102 1.5874 1.3305 0.0557  -0.1005 0.0462  348 LYS F CG  
17028 C CD  . LYS F 348 ? 1.5507 1.6222 1.3575 0.0531  -0.0843 0.0504  348 LYS F CD  
17029 C CE  . LYS F 348 ? 1.5668 1.6436 1.3854 0.0513  -0.0793 0.0566  348 LYS F CE  
17030 N NZ  . LYS F 348 ? 1.6218 1.6946 1.4296 0.0483  -0.0629 0.0604  348 LYS F NZ  
17031 N N   . GLU F 349 ? 1.4965 1.5248 1.2429 0.0608  -0.1194 0.0509  349 GLU F N   
17032 C CA  . GLU F 349 ? 1.5648 1.5823 1.3009 0.0634  -0.1325 0.0550  349 GLU F CA  
17033 C C   . GLU F 349 ? 1.6125 1.6432 1.3765 0.0630  -0.1338 0.0583  349 GLU F C   
17034 O O   . GLU F 349 ? 1.5967 1.6314 1.3672 0.0603  -0.1217 0.0627  349 GLU F O   
17035 C CB  . GLU F 349 ? 1.6295 1.6255 1.3304 0.0632  -0.1281 0.0612  349 GLU F CB  
17036 C CG  . GLU F 349 ? 1.7036 1.6849 1.3737 0.0639  -0.1278 0.0579  349 GLU F CG  
17037 C CD  . GLU F 349 ? 1.7670 1.7264 1.4007 0.0638  -0.1242 0.0644  349 GLU F CD  
17038 O OE1 . GLU F 349 ? 1.7387 1.6960 1.3722 0.0618  -0.1160 0.0716  349 GLU F OE1 
17039 O OE2 . GLU F 349 ? 1.8169 1.7612 1.4218 0.0656  -0.1292 0.0623  349 GLU F OE2 
17040 N N   . ILE F 350 ? 1.8959 1.9335 1.6766 0.0657  -0.1483 0.0557  350 ILE F N   
17041 C CA  . ILE F 350 ? 1.8700 1.9211 1.6785 0.0659  -0.1508 0.0577  350 ILE F CA  
17042 C C   . ILE F 350 ? 1.8804 1.9175 1.6757 0.0685  -0.1604 0.0634  350 ILE F C   
17043 O O   . ILE F 350 ? 1.8782 1.9073 1.6647 0.0721  -0.1755 0.0620  350 ILE F O   
17044 C CB  . ILE F 350 ? 1.8350 1.9039 1.6725 0.0670  -0.1599 0.0513  350 ILE F CB  
17045 C CG1 . ILE F 350 ? 1.8295 1.9105 1.6784 0.0644  -0.1505 0.0461  350 ILE F CG1 
17046 C CG2 . ILE F 350 ? 1.8045 1.8876 1.6700 0.0673  -0.1616 0.0530  350 ILE F CG2 
17047 C CD1 . ILE F 350 ? 1.8284 1.9184 1.6872 0.0608  -0.1333 0.0487  350 ILE F CD1 
17048 N N   . LYS F 351 ? 1.6931 1.7271 1.4873 0.0668  -0.1518 0.0697  351 LYS F N   
17049 C CA  . LYS F 351 ? 1.6326 1.6533 1.4161 0.0690  -0.1596 0.0758  351 LYS F CA  
17050 C C   . LYS F 351 ? 1.5981 1.6316 1.4099 0.0691  -0.1601 0.0774  351 LYS F C   
17051 O O   . LYS F 351 ? 1.5796 1.6028 1.3854 0.0709  -0.1656 0.0826  351 LYS F O   
17052 C CB  . LYS F 351 ? 1.6241 1.6256 1.3770 0.0670  -0.1499 0.0828  351 LYS F CB  
17053 C CG  . LYS F 351 ? 1.6015 1.5883 1.3229 0.0671  -0.1492 0.0816  351 LYS F CG  
17054 C CD  . LYS F 351 ? 1.5325 1.4990 1.2222 0.0654  -0.1410 0.0892  351 LYS F CD  
17055 C CE  . LYS F 351 ? 1.5799 1.5310 1.2364 0.0660  -0.1413 0.0877  351 LYS F CE  
17056 N NZ  . LYS F 351 ? 1.5912 1.5214 1.2147 0.0645  -0.1339 0.0955  351 LYS F NZ  
17057 N N   . SER F 352 ? 1.6143 1.6693 1.4560 0.0672  -0.1546 0.0731  352 SER F N   
17058 C CA  . SER F 352 ? 1.6069 1.6756 1.4763 0.0672  -0.1544 0.0737  352 SER F CA  
17059 C C   . SER F 352 ? 1.5850 1.6736 1.4831 0.0687  -0.1617 0.0668  352 SER F C   
17060 O O   . SER F 352 ? 1.5752 1.6696 1.4750 0.0683  -0.1625 0.0618  352 SER F O   
17061 C CB  . SER F 352 ? 1.6329 1.7091 1.5111 0.0626  -0.1375 0.0763  352 SER F CB  
17062 O OG  . SER F 352 ? 1.6783 1.7366 1.5308 0.0607  -0.1299 0.0827  352 SER F OG  
17063 N N   . ASN F 353 ? 1.6848 1.7835 1.6056 0.0702  -0.1668 0.0666  353 ASN F N   
17064 C CA  . ASN F 353 ? 1.6418 1.7598 1.5909 0.0716  -0.1736 0.0605  353 ASN F CA  
17065 C C   . ASN F 353 ? 1.6198 1.7572 1.5898 0.0677  -0.1612 0.0575  353 ASN F C   
17066 O O   . ASN F 353 ? 1.6379 1.7792 1.6128 0.0648  -0.1494 0.0604  353 ASN F O   
17067 C CB  . ASN F 353 ? 1.6181 1.7410 1.5846 0.0748  -0.1825 0.0611  353 ASN F CB  
17068 C CG  . ASN F 353 ? 1.6469 1.7512 1.5947 0.0792  -0.1959 0.0641  353 ASN F CG  
17069 O OD1 . ASN F 353 ? 1.7075 1.7993 1.6342 0.0807  -0.2027 0.0638  353 ASN F OD1 
17070 N ND2 . ASN F 353 ? 1.6365 1.7385 1.5917 0.0815  -0.2002 0.0669  353 ASN F ND2 
17071 N N   . ILE F 354 ? 1.5964 1.7456 1.5788 0.0676  -0.1642 0.0519  354 ILE F N   
17072 C CA  . ILE F 354 ? 1.5328 1.7019 1.5383 0.0646  -0.1549 0.0488  354 ILE F CA  
17073 C C   . ILE F 354 ? 1.4471 1.6333 1.4816 0.0662  -0.1619 0.0457  354 ILE F C   
17074 O O   . ILE F 354 ? 1.4067 1.6038 1.4553 0.0668  -0.1678 0.0409  354 ILE F O   
17075 C CB  . ILE F 354 ? 1.4923 1.6637 1.4939 0.0631  -0.1526 0.0448  354 ILE F CB  
17076 C CG1 . ILE F 354 ? 1.5961 1.7485 1.5663 0.0624  -0.1478 0.0473  354 ILE F CG1 
17077 C CG2 . ILE F 354 ? 1.3843 1.5742 1.4071 0.0598  -0.1413 0.0429  354 ILE F CG2 
17078 C CD1 . ILE F 354 ? 1.6480 1.8009 1.6128 0.0612  -0.1454 0.0430  354 ILE F CD1 
17079 N N   . LEU F 355 ? 1.3585 1.5467 1.4016 0.0670  -0.1612 0.0484  355 LEU F N   
17080 C CA  . LEU F 355 ? 1.2715 1.4736 1.3396 0.0693  -0.1687 0.0456  355 LEU F CA  
17081 C C   . LEU F 355 ? 1.2093 1.4344 1.3044 0.0670  -0.1631 0.0415  355 LEU F C   
17082 O O   . LEU F 355 ? 1.2212 1.4594 1.3377 0.0687  -0.1694 0.0384  355 LEU F O   
17083 C CB  . LEU F 355 ? 1.2659 1.4633 1.3353 0.0704  -0.1679 0.0494  355 LEU F CB  
17084 C CG  . LEU F 355 ? 1.2803 1.4676 1.3341 0.0672  -0.1554 0.0547  355 LEU F CG  
17085 C CD1 . LEU F 355 ? 1.2408 1.4449 1.3114 0.0631  -0.1421 0.0536  355 LEU F CD1 
17086 C CD2 . LEU F 355 ? 1.2624 1.4378 1.3099 0.0690  -0.1583 0.0591  355 LEU F CD2 
17087 N N   . LYS F 356 ? 1.1818 1.4121 1.2765 0.0632  -0.1515 0.0416  356 LYS F N   
17088 C CA  . LYS F 356 ? 1.1298 1.3809 1.2481 0.0609  -0.1457 0.0384  356 LYS F CA  
17089 C C   . LYS F 356 ? 1.0957 1.3459 1.2060 0.0583  -0.1394 0.0373  356 LYS F C   
17090 O O   . LYS F 356 ? 1.1112 1.3461 1.1983 0.0578  -0.1362 0.0396  356 LYS F O   
17091 C CB  . LYS F 356 ? 1.1661 1.4278 1.2978 0.0589  -0.1357 0.0401  356 LYS F CB  
17092 C CG  . LYS F 356 ? 1.2670 1.5341 1.4131 0.0614  -0.1416 0.0397  356 LYS F CG  
17093 C CD  . LYS F 356 ? 1.3369 1.6130 1.4941 0.0592  -0.1315 0.0412  356 LYS F CD  
17094 C CE  . LYS F 356 ? 1.3040 1.5997 1.4797 0.0562  -0.1236 0.0387  356 LYS F CE  
17095 N NZ  . LYS F 356 ? 1.2280 1.5390 1.4242 0.0577  -0.1307 0.0342  356 LYS F NZ  
17096 N N   . PRO F 357 ? 1.0524 1.3186 1.1812 0.0568  -0.1377 0.0339  357 PRO F N   
17097 C CA  . PRO F 357 ? 1.0488 1.3144 1.1715 0.0546  -0.1320 0.0326  357 PRO F CA  
17098 C C   . PRO F 357 ? 1.0998 1.3598 1.2100 0.0523  -0.1189 0.0360  357 PRO F C   
17099 O O   . PRO F 357 ? 1.0925 1.3612 1.2128 0.0507  -0.1106 0.0380  357 PRO F O   
17100 C CB  . PRO F 357 ? 1.0080 1.2941 1.1569 0.0530  -0.1307 0.0296  357 PRO F CB  
17101 C CG  . PRO F 357 ? 1.0156 1.3095 1.1800 0.0553  -0.1406 0.0277  357 PRO F CG  
17102 C CD  . PRO F 357 ? 1.0675 1.3524 1.2233 0.0572  -0.1416 0.0309  357 PRO F CD  
17103 N N   . GLU F 358 ? 1.1407 1.3863 1.2291 0.0521  -0.1172 0.0363  358 GLU F N   
17104 C CA  . GLU F 358 ? 1.1588 1.3966 1.2323 0.0503  -0.1054 0.0395  358 GLU F CA  
17105 C C   . GLU F 358 ? 1.1415 1.3683 1.1966 0.0501  -0.1039 0.0378  358 GLU F C   
17106 O O   . GLU F 358 ? 1.1696 1.3864 1.2131 0.0520  -0.1138 0.0357  358 GLU F O   
17107 C CB  . GLU F 358 ? 1.2179 1.4425 1.2760 0.0511  -0.1056 0.0439  358 GLU F CB  
17108 C CG  . GLU F 358 ? 1.2536 1.4684 1.2944 0.0490  -0.0937 0.0475  358 GLU F CG  
17109 C CD  . GLU F 358 ? 1.2816 1.4812 1.3055 0.0497  -0.0952 0.0521  358 GLU F CD  
17110 O OE1 . GLU F 358 ? 1.2930 1.4921 1.3225 0.0519  -0.1045 0.0526  358 GLU F OE1 
17111 O OE2 . GLU F 358 ? 1.3574 1.5454 1.3626 0.0482  -0.0869 0.0553  358 GLU F OE2 
17112 N N   . ILE F 359 ? 1.1080 1.3364 1.1604 0.0479  -0.0918 0.0385  359 ILE F N   
17113 C CA  . ILE F 359 ? 1.1499 1.3678 1.1847 0.0478  -0.0885 0.0367  359 ILE F CA  
17114 C C   . ILE F 359 ? 1.2304 1.4313 1.2392 0.0477  -0.0831 0.0403  359 ILE F C   
17115 O O   . ILE F 359 ? 1.2673 1.4705 1.2769 0.0459  -0.0725 0.0437  359 ILE F O   
17116 C CB  . ILE F 359 ? 1.0885 1.3183 1.1363 0.0459  -0.0786 0.0350  359 ILE F CB  
17117 C CG1 . ILE F 359 ? 1.0924 1.3375 1.1640 0.0458  -0.0844 0.0317  359 ILE F CG1 
17118 C CG2 . ILE F 359 ? 1.1426 1.3603 1.1708 0.0460  -0.0741 0.0331  359 ILE F CG2 
17119 C CD1 . ILE F 359 ? 0.9374 1.1948 1.0235 0.0440  -0.0753 0.0306  359 ILE F CD1 
17120 N N   . VAL F 360 ? 1.3170 1.5010 1.3027 0.0496  -0.0903 0.0396  360 VAL F N   
17121 C CA  . VAL F 360 ? 1.4589 1.6249 1.4171 0.0496  -0.0863 0.0432  360 VAL F CA  
17122 C C   . VAL F 360 ? 1.6194 1.7767 1.5600 0.0493  -0.0798 0.0408  360 VAL F C   
17123 O O   . VAL F 360 ? 1.5837 1.7409 1.5242 0.0503  -0.0854 0.0360  360 VAL F O   
17124 C CB  . VAL F 360 ? 1.5045 1.6564 1.4471 0.0523  -0.0994 0.0447  360 VAL F CB  
17125 C CG1 . VAL F 360 ? 1.6076 1.7405 1.5210 0.0521  -0.0947 0.0493  360 VAL F CG1 
17126 C CG2 . VAL F 360 ? 1.4142 1.5757 1.3765 0.0531  -0.1062 0.0462  360 VAL F CG2 
17127 N N   . MET F 361 ? 2.0375 2.1875 1.9632 0.0477  -0.0680 0.0440  361 MET F N   
17128 C CA  . MET F 361 ? 2.0713 2.2132 1.9800 0.0474  -0.0602 0.0416  361 MET F CA  
17129 C C   . MET F 361 ? 2.1155 2.2361 1.9908 0.0481  -0.0598 0.0442  361 MET F C   
17130 O O   . MET F 361 ? 2.1345 2.2434 1.9906 0.0496  -0.0641 0.0409  361 MET F O   
17131 C CB  . MET F 361 ? 2.0670 2.2202 1.9881 0.0449  -0.0447 0.0425  361 MET F CB  
17132 C CG  . MET F 361 ? 2.0235 2.1975 1.9768 0.0438  -0.0439 0.0424  361 MET F CG  
17133 S SD  . MET F 361 ? 2.0511 2.2386 2.0191 0.0413  -0.0270 0.0430  361 MET F SD  
17134 C CE  . MET F 361 ? 2.0599 2.2415 2.0167 0.0426  -0.0235 0.0376  361 MET F CE  
17135 O OXT . MET F 361 ? 2.1314 2.2458 1.9977 0.0469  -0.0552 0.0497  361 MET F OXT 
17136 S S   . SO4 G .   ? 2.1183 2.7082 2.6481 -0.0789 0.1237  0.0257  501 SO4 A S   
17137 O O1  . SO4 G .   ? 2.0689 2.6612 2.5968 -0.0751 0.1125  0.0221  501 SO4 A O1  
17138 O O2  . SO4 G .   ? 2.0459 2.6573 2.5938 -0.0784 0.1261  0.0235  501 SO4 A O2  
17139 O O3  . SO4 G .   ? 2.1040 2.6843 2.6374 -0.0867 0.1282  0.0258  501 SO4 A O3  
17140 O O4  . SO4 G .   ? 2.0969 2.6723 2.6071 -0.0752 0.1279  0.0311  501 SO4 A O4  
17141 S S   . SO4 H .   ? 1.7339 2.3092 2.1900 -0.0327 0.0565  0.0192  502 SO4 A S   
17142 O O1  . SO4 H .   ? 1.6040 2.1815 2.0651 -0.0335 0.0505  0.0140  502 SO4 A O1  
17143 O O2  . SO4 H .   ? 1.5806 2.1685 2.0380 -0.0280 0.0542  0.0199  502 SO4 A O2  
17144 O O3  . SO4 H .   ? 1.6747 2.2299 2.1149 -0.0318 0.0581  0.0234  502 SO4 A O3  
17145 O O4  . SO4 H .   ? 1.6216 2.2017 2.0871 -0.0373 0.0632  0.0196  502 SO4 A O4  
17146 S S   . SO4 I .   ? 1.5403 2.0760 1.9160 0.0220  -0.0137 0.0275  503 SO4 A S   
17147 O O1  . SO4 I .   ? 1.3323 1.8857 1.7187 0.0222  -0.0135 0.0264  503 SO4 A O1  
17148 O O2  . SO4 I .   ? 1.3437 1.8791 1.7197 0.0196  -0.0091 0.0274  503 SO4 A O2  
17149 O O3  . SO4 I .   ? 1.3999 1.9282 1.7743 0.0238  -0.0196 0.0249  503 SO4 A O3  
17150 O O4  . SO4 I .   ? 1.4280 1.9540 1.7944 0.0222  -0.0127 0.0312  503 SO4 A O4  
17151 S S   . SO4 J .   ? 0.5376 1.4292 1.0203 0.0620  -0.0515 0.1343  501 SO4 B S   
17152 O O1  . SO4 J .   ? 0.6038 1.5002 1.0730 0.0620  -0.0548 0.1405  501 SO4 B O1  
17153 O O2  . SO4 J .   ? 0.5294 1.4281 1.0143 0.0585  -0.0511 0.1238  501 SO4 B O2  
17154 O O3  . SO4 J .   ? 0.5205 1.4155 1.0150 0.0669  -0.0555 0.1372  501 SO4 B O3  
17155 O O4  . SO4 J .   ? 0.6668 1.5431 1.1493 0.0608  -0.0447 0.1358  501 SO4 B O4  
17156 S S   . SO4 K .   ? 1.5939 2.1772 2.2582 0.1366  -0.2877 -0.0728 401 SO4 D S   
17157 O O1  . SO4 K .   ? 1.4578 2.0441 2.1137 0.1313  -0.2718 -0.0703 401 SO4 D O1  
17158 O O2  . SO4 K .   ? 1.5425 2.1512 2.2393 0.1374  -0.2884 -0.0798 401 SO4 D O2  
17159 O O3  . SO4 K .   ? 1.4489 2.0165 2.1061 0.1447  -0.2967 -0.0726 401 SO4 D O3  
17160 O O4  . SO4 K .   ? 1.4989 2.0698 2.1463 0.1330  -0.2941 -0.0685 401 SO4 D O4  
17161 S S   . SO4 L .   ? 1.4458 1.8221 1.9492 0.1064  -0.1358 -0.0799 402 SO4 D S   
17162 O O1  . SO4 L .   ? 1.3555 1.7587 1.8731 0.1084  -0.1327 -0.0883 402 SO4 D O1  
17163 O O2  . SO4 L .   ? 1.5019 1.8758 1.9951 0.0979  -0.1280 -0.0758 402 SO4 D O2  
17164 O O3  . SO4 L .   ? 1.4790 1.8397 1.9885 0.1112  -0.1414 -0.0843 402 SO4 D O3  
17165 O O4  . SO4 L .   ? 1.4174 1.7848 1.9106 0.1082  -0.1412 -0.0712 402 SO4 D O4  
17166 S S   . SO4 M .   ? 1.5295 2.0368 2.1501 0.1323  -0.1174 -0.1736 403 SO4 D S   
17167 O O1  . SO4 M .   ? 1.4089 1.9354 2.0453 0.1388  -0.1168 -0.1836 403 SO4 D O1  
17168 O O2  . SO4 M .   ? 1.4410 1.9546 2.0560 0.1254  -0.1103 -0.1764 403 SO4 D O2  
17169 O O3  . SO4 M .   ? 1.5698 2.0510 2.1900 0.1357  -0.1248 -0.1725 403 SO4 D O3  
17170 O O4  . SO4 M .   ? 1.4296 1.9375 2.0406 0.1291  -0.1178 -0.1619 403 SO4 D O4  
17171 S S   . SO4 N .   ? 1.4358 2.2721 2.0479 0.0900  -0.0120 -0.1800 404 SO4 D S   
17172 O O1  . SO4 N .   ? 1.3970 2.2526 2.0065 0.0890  -0.0045 -0.1864 404 SO4 D O1  
17173 O O2  . SO4 N .   ? 1.2904 2.1206 1.9160 0.0966  -0.0163 -0.1881 404 SO4 D O2  
17174 O O3  . SO4 N .   ? 1.2913 2.1114 1.8921 0.0869  -0.0158 -0.1762 404 SO4 D O3  
17175 O O4  . SO4 N .   ? 1.2588 2.0981 1.8715 0.0874  -0.0115 -0.1695 404 SO4 D O4  
17176 S S   . SO4 O .   ? 1.7638 1.7620 1.4172 0.0381  0.0109  0.0730  401 SO4 E S   
17177 O O1  . SO4 O .   ? 1.7510 1.7429 1.4032 0.0400  -0.0054 0.0764  401 SO4 E O1  
17178 O O2  . SO4 O .   ? 1.6784 1.6961 1.3639 0.0353  0.0204  0.0738  401 SO4 E O2  
17179 O O3  . SO4 O .   ? 1.8242 1.8063 1.4465 0.0361  0.0219  0.0774  401 SO4 E O3  
17180 O O4  . SO4 O .   ? 1.8266 1.8279 1.4802 0.0411  0.0067  0.0645  401 SO4 E O4  
17181 S S   . SO4 P .   ? 1.7217 2.0610 1.9268 0.0380  -0.0237 0.0273  402 SO4 E S   
17182 O O1  . SO4 P .   ? 1.7398 2.0875 1.9598 0.0365  -0.0314 0.0274  402 SO4 E O1  
17183 O O2  . SO4 P .   ? 1.6965 2.0426 1.9102 0.0386  -0.0147 0.0290  402 SO4 E O2  
17184 O O3  . SO4 P .   ? 1.7149 2.0564 1.9156 0.0377  -0.0224 0.0295  402 SO4 E O3  
17185 O O4  . SO4 P .   ? 1.7684 2.0904 1.9548 0.0393  -0.0263 0.0233  402 SO4 E O4  
17186 S S   . SO4 Q .   ? 1.9481 2.1840 2.0808 0.0402  -0.0768 -0.0147 401 SO4 F S   
17187 O O1  . SO4 Q .   ? 1.7957 2.0376 1.9303 0.0392  -0.0840 -0.0123 401 SO4 F O1  
17188 O O2  . SO4 Q .   ? 2.0249 2.2748 2.1799 0.0390  -0.0702 -0.0104 401 SO4 F O2  
17189 O O3  . SO4 Q .   ? 1.9201 2.1467 2.0324 0.0429  -0.0684 -0.0151 401 SO4 F O3  
17190 O O4  . SO4 Q .   ? 1.9030 2.1282 2.0322 0.0395  -0.0848 -0.0209 401 SO4 F O4  
17191 S S   . SO4 R .   ? 2.1459 2.1728 1.8738 0.0623  -0.0904 -0.0231 402 SO4 F S   
17192 O O1  . SO4 R .   ? 2.0242 2.0595 1.7668 0.0615  -0.0978 -0.0165 402 SO4 F O1  
17193 O O2  . SO4 R .   ? 2.1333 2.1700 1.8741 0.0612  -0.0732 -0.0214 402 SO4 F O2  
17194 O O3  . SO4 R .   ? 2.1925 2.1998 1.8823 0.0638  -0.0905 -0.0235 402 SO4 F O3  
17195 O O4  . SO4 R .   ? 2.0865 2.1150 1.8254 0.0627  -0.1003 -0.0309 402 SO4 F O4  
17196 O O   . HOH S .   ? 0.5366 1.3049 1.0576 -0.0139 -0.0028 -0.0261 601 HOH A O   
17197 O O   . HOH T .   ? 0.6316 1.1839 1.0358 0.0203  -0.0314 0.0498  601 HOH B O   
# 
