data_8K6F
# 
_entry.id   8K6F 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8K6F         pdb_00008k6f 10.2210/pdb8k6f/pdb 
WWPDB D_1300039652 ?            ?                   
# 
_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       2025-01-29 
# 
_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                        8K6F 
_pdbx_database_status.recvd_initial_deposition_date   2023-07-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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                 2 
_pdbx_contact_author.email              ouyangsy@fjnu.edu.cn 
_pdbx_contact_author.name_first         Songying 
_pdbx_contact_author.name_last          Ouyang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1120-1524 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chen, T.T.'   1 ? 
'Ouyang, S.Y.' 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                     'Complex structure of Legionella effector LnaB with host Actin and PR-Ub' 
_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 'Chen, T.T.' 1 ? 
primary 'Ouyang, S.' 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     nat 'Actin gamma 1' 41838.766 2 ? ? ? ? 
2 polymer     man 'Legionella effector LnaB' 40622.980 2 ? ? ? ? 
3 polymer     man Ubiquitin 8576.831  2 ? ? ? ? 
4 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE" 507.181   2 ? ? ? ? 
5 non-polymer syn 
;[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE
;
559.316   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 
;MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD
DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT
HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL
APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
;
;MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD
DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT
HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL
APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
;
A,B ? 
2 'polypeptide(L)' no no 
;MSYQKIELSISLSLDSPKLDESDFILLSVKYLEKSLGKKKEFSGFFEDIEKLYFKQNYKEAIEKILDFCKKNESLLSEQV
VQRLAEVAPRLKSNPKDNESRRLYETLYADHLESVIKQESDLSVFNELRDSYNAVKPEYAVTHETEIKTLDEAKQFILSF
VMLNDNVELPLKAQSERYPKKDRSREELGNTPSANPGIMKPNSPNFTDNLVPVRDVPKIAINEKVAGGYSKTKPTTPFVA
SLSGTTYSLMVVLTDYIEKHKTDKDIEKKVNQIINLWISSYIKEGYHSYSEVVDVLTEPFLQSIFDKANIKLNYGVLDDT
HAEFRKAQDYVFGLTIQSAMHHELQERFKNKE
;
;MSYQKIELSISLSLDSPKLDESDFILLSVKYLEKSLGKKKEFSGFFEDIEKLYFKQNYKEAIEKILDFCKKNESLLSEQV
VQRLAEVAPRLKSNPKDNESRRLYETLYADHLESVIKQESDLSVFNELRDSYNAVKPEYAVTHETEIKTLDEAKQFILSF
VMLNDNVELPLKAQSERYPKKDRSREELGNTPSANPGIMKPNSPNFTDNLVPVRDVPKIAINEKVAGGYSKTKPTTPFVA
SLSGTTYSLMVVLTDYIEKHKTDKDIEKKVNQIINLWISSYIKEGYHSYSEVVDVLTEPFLQSIFDKANIKLNYGVLDDT
HAEFRKAQDYVFGLTIQSAMHHELQERFKNKE
;
C,D ? 
3 'polypeptide(L)' no no MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG E,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
5 
;[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE
;
AR6 
# 
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   GLU n 
1 3   GLU n 
1 4   GLU n 
1 5   ILE n 
1 6   ALA n 
1 7   ALA n 
1 8   LEU n 
1 9   VAL n 
1 10  ILE n 
1 11  ASP n 
1 12  ASN n 
1 13  GLY n 
1 14  SER n 
1 15  GLY n 
1 16  MET n 
1 17  CYS n 
1 18  LYS n 
1 19  ALA n 
1 20  GLY n 
1 21  PHE n 
1 22  ALA n 
1 23  GLY n 
1 24  ASP n 
1 25  ASP n 
1 26  ALA n 
1 27  PRO n 
1 28  ARG n 
1 29  ALA n 
1 30  VAL n 
1 31  PHE n 
1 32  PRO n 
1 33  SER n 
1 34  ILE n 
1 35  VAL n 
1 36  GLY n 
1 37  ARG n 
1 38  PRO n 
1 39  ARG n 
1 40  HIS n 
1 41  GLN n 
1 42  GLY n 
1 43  VAL n 
1 44  MET n 
1 45  VAL n 
1 46  GLY n 
1 47  MET n 
1 48  GLY n 
1 49  GLN n 
1 50  LYS n 
1 51  ASP n 
1 52  SER n 
1 53  TYR n 
1 54  VAL n 
1 55  GLY n 
1 56  ASP n 
1 57  GLU n 
1 58  ALA n 
1 59  GLN n 
1 60  SER n 
1 61  LYS n 
1 62  ARG n 
1 63  GLY n 
1 64  ILE n 
1 65  LEU n 
1 66  THR n 
1 67  LEU n 
1 68  LYS n 
1 69  TYR n 
1 70  PRO n 
1 71  ILE n 
1 72  GLU n 
1 73  HIS n 
1 74  GLY n 
1 75  ILE n 
1 76  VAL n 
1 77  THR n 
1 78  ASN n 
1 79  TRP n 
1 80  ASP n 
1 81  ASP n 
1 82  MET n 
1 83  GLU n 
1 84  LYS n 
1 85  ILE n 
1 86  TRP n 
1 87  HIS n 
1 88  HIS n 
1 89  THR n 
1 90  PHE n 
1 91  TYR n 
1 92  ASN n 
1 93  GLU n 
1 94  LEU n 
1 95  ARG n 
1 96  VAL n 
1 97  ALA n 
1 98  PRO n 
1 99  GLU n 
1 100 GLU n 
1 101 HIS n 
1 102 PRO n 
1 103 VAL n 
1 104 LEU n 
1 105 LEU n 
1 106 THR n 
1 107 GLU n 
1 108 ALA n 
1 109 PRO n 
1 110 LEU n 
1 111 ASN n 
1 112 PRO n 
1 113 LYS n 
1 114 ALA n 
1 115 ASN n 
1 116 ARG n 
1 117 GLU n 
1 118 LYS n 
1 119 MET n 
1 120 THR n 
1 121 GLN n 
1 122 ILE n 
1 123 MET n 
1 124 PHE n 
1 125 GLU n 
1 126 THR n 
1 127 PHE n 
1 128 ASN n 
1 129 THR n 
1 130 PRO n 
1 131 ALA n 
1 132 MET n 
1 133 TYR n 
1 134 VAL n 
1 135 ALA n 
1 136 ILE n 
1 137 GLN n 
1 138 ALA n 
1 139 VAL n 
1 140 LEU n 
1 141 SER n 
1 142 LEU n 
1 143 TYR n 
1 144 ALA n 
1 145 SER n 
1 146 GLY n 
1 147 ARG n 
1 148 THR n 
1 149 THR n 
1 150 GLY n 
1 151 ILE n 
1 152 VAL n 
1 153 MET n 
1 154 ASP n 
1 155 SER n 
1 156 GLY n 
1 157 ASP n 
1 158 GLY n 
1 159 VAL n 
1 160 THR n 
1 161 HIS n 
1 162 THR n 
1 163 VAL n 
1 164 PRO n 
1 165 ILE n 
1 166 TYR n 
1 167 GLU n 
1 168 GLY n 
1 169 TYR n 
1 170 ALA n 
1 171 LEU n 
1 172 PRO n 
1 173 HIS n 
1 174 ALA n 
1 175 ILE n 
1 176 LEU n 
1 177 ARG n 
1 178 LEU n 
1 179 ASP n 
1 180 LEU n 
1 181 ALA n 
1 182 GLY n 
1 183 ARG n 
1 184 ASP n 
1 185 LEU n 
1 186 THR n 
1 187 ASP n 
1 188 TYR n 
1 189 LEU n 
1 190 MET n 
1 191 LYS n 
1 192 ILE n 
1 193 LEU n 
1 194 THR n 
1 195 GLU n 
1 196 ARG n 
1 197 GLY n 
1 198 TYR n 
1 199 SER n 
1 200 PHE n 
1 201 THR n 
1 202 THR n 
1 203 THR n 
1 204 ALA n 
1 205 GLU n 
1 206 ARG n 
1 207 GLU n 
1 208 ILE n 
1 209 VAL n 
1 210 ARG n 
1 211 ASP n 
1 212 ILE n 
1 213 LYS n 
1 214 GLU n 
1 215 LYS n 
1 216 LEU n 
1 217 CYS n 
1 218 TYR n 
1 219 VAL n 
1 220 ALA n 
1 221 LEU n 
1 222 ASP n 
1 223 PHE n 
1 224 GLU n 
1 225 GLN n 
1 226 GLU n 
1 227 MET n 
1 228 ALA n 
1 229 THR n 
1 230 ALA n 
1 231 ALA n 
1 232 SER n 
1 233 SER n 
1 234 SER n 
1 235 SER n 
1 236 LEU n 
1 237 GLU n 
1 238 LYS n 
1 239 SER n 
1 240 TYR n 
1 241 GLU n 
1 242 LEU n 
1 243 PRO n 
1 244 ASP n 
1 245 GLY n 
1 246 GLN n 
1 247 VAL n 
1 248 ILE n 
1 249 THR n 
1 250 ILE n 
1 251 GLY n 
1 252 ASN n 
1 253 GLU n 
1 254 ARG n 
1 255 PHE n 
1 256 ARG n 
1 257 CYS n 
1 258 PRO n 
1 259 GLU n 
1 260 ALA n 
1 261 LEU n 
1 262 PHE n 
1 263 GLN n 
1 264 PRO n 
1 265 SER n 
1 266 PHE n 
1 267 LEU n 
1 268 GLY n 
1 269 MET n 
1 270 GLU n 
1 271 SER n 
1 272 CYS n 
1 273 GLY n 
1 274 ILE n 
1 275 HIS n 
1 276 GLU n 
1 277 THR n 
1 278 THR n 
1 279 PHE n 
1 280 ASN n 
1 281 SER n 
1 282 ILE n 
1 283 MET n 
1 284 LYS n 
1 285 CYS n 
1 286 ASP n 
1 287 VAL n 
1 288 ASP n 
1 289 ILE n 
1 290 ARG n 
1 291 LYS n 
1 292 ASP n 
1 293 LEU n 
1 294 TYR n 
1 295 ALA n 
1 296 ASN n 
1 297 THR n 
1 298 VAL n 
1 299 LEU n 
1 300 SER n 
1 301 GLY n 
1 302 GLY n 
1 303 THR n 
1 304 THR n 
1 305 MET n 
1 306 TYR n 
1 307 PRO n 
1 308 GLY n 
1 309 ILE n 
1 310 ALA n 
1 311 ASP n 
1 312 ARG n 
1 313 MET n 
1 314 GLN n 
1 315 LYS n 
1 316 GLU n 
1 317 ILE n 
1 318 THR n 
1 319 ALA n 
1 320 LEU n 
1 321 ALA n 
1 322 PRO n 
1 323 SER n 
1 324 THR n 
1 325 MET n 
1 326 LYS n 
1 327 ILE n 
1 328 LYS n 
1 329 ILE n 
1 330 ILE n 
1 331 ALA n 
1 332 PRO n 
1 333 PRO n 
1 334 GLU n 
1 335 ARG n 
1 336 LYS n 
1 337 TYR n 
1 338 SER n 
1 339 VAL n 
1 340 TRP n 
1 341 ILE n 
1 342 GLY n 
1 343 GLY n 
1 344 SER n 
1 345 ILE n 
1 346 LEU n 
1 347 ALA n 
1 348 SER n 
1 349 LEU n 
1 350 SER n 
1 351 THR n 
1 352 PHE n 
1 353 GLN n 
1 354 GLN n 
1 355 MET n 
1 356 TRP n 
1 357 ILE n 
1 358 SER n 
1 359 LYS n 
1 360 GLN n 
1 361 GLU n 
1 362 TYR n 
1 363 ASP n 
1 364 GLU n 
1 365 SER n 
1 366 GLY n 
1 367 PRO n 
1 368 SER n 
1 369 ILE n 
1 370 VAL n 
1 371 HIS n 
1 372 ARG n 
1 373 LYS n 
1 374 CYS n 
1 375 PHE n 
2 1   MET n 
2 2   SER n 
2 3   TYR n 
2 4   GLN n 
2 5   LYS n 
2 6   ILE n 
2 7   GLU n 
2 8   LEU n 
2 9   SER n 
2 10  ILE n 
2 11  SER n 
2 12  LEU n 
2 13  SER n 
2 14  LEU n 
2 15  ASP n 
2 16  SER n 
2 17  PRO n 
2 18  LYS n 
2 19  LEU n 
2 20  ASP n 
2 21  GLU n 
2 22  SER n 
2 23  ASP n 
2 24  PHE n 
2 25  ILE n 
2 26  LEU n 
2 27  LEU n 
2 28  SER n 
2 29  VAL n 
2 30  LYS n 
2 31  TYR n 
2 32  LEU n 
2 33  GLU n 
2 34  LYS n 
2 35  SER n 
2 36  LEU n 
2 37  GLY n 
2 38  LYS n 
2 39  LYS n 
2 40  LYS n 
2 41  GLU n 
2 42  PHE n 
2 43  SER n 
2 44  GLY n 
2 45  PHE n 
2 46  PHE n 
2 47  GLU n 
2 48  ASP n 
2 49  ILE n 
2 50  GLU n 
2 51  LYS n 
2 52  LEU n 
2 53  TYR n 
2 54  PHE n 
2 55  LYS n 
2 56  GLN n 
2 57  ASN n 
2 58  TYR n 
2 59  LYS n 
2 60  GLU n 
2 61  ALA n 
2 62  ILE n 
2 63  GLU n 
2 64  LYS n 
2 65  ILE n 
2 66  LEU n 
2 67  ASP n 
2 68  PHE n 
2 69  CYS n 
2 70  LYS n 
2 71  LYS n 
2 72  ASN n 
2 73  GLU n 
2 74  SER n 
2 75  LEU n 
2 76  LEU n 
2 77  SER n 
2 78  GLU n 
2 79  GLN n 
2 80  VAL n 
2 81  VAL n 
2 82  GLN n 
2 83  ARG n 
2 84  LEU n 
2 85  ALA n 
2 86  GLU n 
2 87  VAL n 
2 88  ALA n 
2 89  PRO n 
2 90  ARG n 
2 91  LEU n 
2 92  LYS n 
2 93  SER n 
2 94  ASN n 
2 95  PRO n 
2 96  LYS n 
2 97  ASP n 
2 98  ASN n 
2 99  GLU n 
2 100 SER n 
2 101 ARG n 
2 102 ARG n 
2 103 LEU n 
2 104 TYR n 
2 105 GLU n 
2 106 THR n 
2 107 LEU n 
2 108 TYR n 
2 109 ALA n 
2 110 ASP n 
2 111 HIS n 
2 112 LEU n 
2 113 GLU n 
2 114 SER n 
2 115 VAL n 
2 116 ILE n 
2 117 LYS n 
2 118 GLN n 
2 119 GLU n 
2 120 SER n 
2 121 ASP n 
2 122 LEU n 
2 123 SER n 
2 124 VAL n 
2 125 PHE n 
2 126 ASN n 
2 127 GLU n 
2 128 LEU n 
2 129 ARG n 
2 130 ASP n 
2 131 SER n 
2 132 TYR n 
2 133 ASN n 
2 134 ALA n 
2 135 VAL n 
2 136 LYS n 
2 137 PRO n 
2 138 GLU n 
2 139 TYR n 
2 140 ALA n 
2 141 VAL n 
2 142 THR n 
2 143 HIS n 
2 144 GLU n 
2 145 THR n 
2 146 GLU n 
2 147 ILE n 
2 148 LYS n 
2 149 THR n 
2 150 LEU n 
2 151 ASP n 
2 152 GLU n 
2 153 ALA n 
2 154 LYS n 
2 155 GLN n 
2 156 PHE n 
2 157 ILE n 
2 158 LEU n 
2 159 SER n 
2 160 PHE n 
2 161 VAL n 
2 162 MET n 
2 163 LEU n 
2 164 ASN n 
2 165 ASP n 
2 166 ASN n 
2 167 VAL n 
2 168 GLU n 
2 169 LEU n 
2 170 PRO n 
2 171 LEU n 
2 172 LYS n 
2 173 ALA n 
2 174 GLN n 
2 175 SER n 
2 176 GLU n 
2 177 ARG n 
2 178 TYR n 
2 179 PRO n 
2 180 LYS n 
2 181 LYS n 
2 182 ASP n 
2 183 ARG n 
2 184 SER n 
2 185 ARG n 
2 186 GLU n 
2 187 GLU n 
2 188 LEU n 
2 189 GLY n 
2 190 ASN n 
2 191 THR n 
2 192 PRO n 
2 193 SER n 
2 194 ALA n 
2 195 ASN n 
2 196 PRO n 
2 197 GLY n 
2 198 ILE n 
2 199 MET n 
2 200 LYS n 
2 201 PRO n 
2 202 ASN n 
2 203 SER n 
2 204 PRO n 
2 205 ASN n 
2 206 PHE n 
2 207 THR n 
2 208 ASP n 
2 209 ASN n 
2 210 LEU n 
2 211 VAL n 
2 212 PRO n 
2 213 VAL n 
2 214 ARG n 
2 215 ASP n 
2 216 VAL n 
2 217 PRO n 
2 218 LYS n 
2 219 ILE n 
2 220 ALA n 
2 221 ILE n 
2 222 ASN n 
2 223 GLU n 
2 224 LYS n 
2 225 VAL n 
2 226 ALA n 
2 227 GLY n 
2 228 GLY n 
2 229 TYR n 
2 230 SER n 
2 231 LYS n 
2 232 THR n 
2 233 LYS n 
2 234 PRO n 
2 235 THR n 
2 236 THR n 
2 237 PRO n 
2 238 PHE n 
2 239 VAL n 
2 240 ALA n 
2 241 SER n 
2 242 LEU n 
2 243 SER n 
2 244 GLY n 
2 245 THR n 
2 246 THR n 
2 247 TYR n 
2 248 SER n 
2 249 LEU n 
2 250 MET n 
2 251 VAL n 
2 252 VAL n 
2 253 LEU n 
2 254 THR n 
2 255 ASP n 
2 256 TYR n 
2 257 ILE n 
2 258 GLU n 
2 259 LYS n 
2 260 HIS n 
2 261 LYS n 
2 262 THR n 
2 263 ASP n 
2 264 LYS n 
2 265 ASP n 
2 266 ILE n 
2 267 GLU n 
2 268 LYS n 
2 269 LYS n 
2 270 VAL n 
2 271 ASN n 
2 272 GLN n 
2 273 ILE n 
2 274 ILE n 
2 275 ASN n 
2 276 LEU n 
2 277 TRP n 
2 278 ILE n 
2 279 SER n 
2 280 SER n 
2 281 TYR n 
2 282 ILE n 
2 283 LYS n 
2 284 GLU n 
2 285 GLY n 
2 286 TYR n 
2 287 HIS n 
2 288 SER n 
2 289 TYR n 
2 290 SER n 
2 291 GLU n 
2 292 VAL n 
2 293 VAL n 
2 294 ASP n 
2 295 VAL n 
2 296 LEU n 
2 297 THR n 
2 298 GLU n 
2 299 PRO n 
2 300 PHE n 
2 301 LEU n 
2 302 GLN n 
2 303 SER n 
2 304 ILE n 
2 305 PHE n 
2 306 ASP n 
2 307 LYS n 
2 308 ALA n 
2 309 ASN n 
2 310 ILE n 
2 311 LYS n 
2 312 LEU n 
2 313 ASN n 
2 314 TYR n 
2 315 GLY n 
2 316 VAL n 
2 317 LEU n 
2 318 ASP n 
2 319 ASP n 
2 320 THR n 
2 321 HIS n 
2 322 ALA n 
2 323 GLU n 
2 324 PHE n 
2 325 ARG n 
2 326 LYS n 
2 327 ALA n 
2 328 GLN n 
2 329 ASP n 
2 330 TYR n 
2 331 VAL n 
2 332 PHE n 
2 333 GLY n 
2 334 LEU n 
2 335 THR n 
2 336 ILE n 
2 337 GLN n 
2 338 SER n 
2 339 ALA n 
2 340 MET n 
2 341 HIS n 
2 342 HIS n 
2 343 GLU n 
2 344 LEU n 
2 345 GLN n 
2 346 GLU n 
2 347 ARG n 
2 348 PHE n 
2 349 LYS n 
2 350 ASN n 
2 351 LYS n 
2 352 GLU n 
3 1   MET n 
3 2   GLN n 
3 3   ILE n 
3 4   PHE n 
3 5   VAL n 
3 6   LYS n 
3 7   THR n 
3 8   LEU n 
3 9   THR n 
3 10  GLY n 
3 11  LYS n 
3 12  THR n 
3 13  ILE n 
3 14  THR n 
3 15  LEU n 
3 16  GLU n 
3 17  VAL n 
3 18  GLU n 
3 19  PRO n 
3 20  SER n 
3 21  ASP n 
3 22  THR n 
3 23  ILE n 
3 24  GLU n 
3 25  ASN n 
3 26  VAL n 
3 27  LYS n 
3 28  ALA n 
3 29  LYS n 
3 30  ILE n 
3 31  GLN n 
3 32  ASP n 
3 33  LYS n 
3 34  GLU n 
3 35  GLY n 
3 36  ILE n 
3 37  PRO n 
3 38  PRO n 
3 39  ASP n 
3 40  GLN n 
3 41  GLN n 
3 42  ARG n 
3 43  LEU n 
3 44  ILE n 
3 45  PHE n 
3 46  ALA n 
3 47  GLY n 
3 48  LYS n 
3 49  GLN n 
3 50  LEU n 
3 51  GLU n 
3 52  ASP n 
3 53  GLY n 
3 54  ARG n 
3 55  THR n 
3 56  LEU n 
3 57  SER n 
3 58  ASP n 
3 59  TYR n 
3 60  ASN n 
3 61  ILE n 
3 62  GLN n 
3 63  LYS n 
3 64  GLU n 
3 65  SER n 
3 66  THR n 
3 67  LEU n 
3 68  HIS n 
3 69  LEU n 
3 70  VAL n 
3 71  LEU n 
3 72  ARG n 
3 73  LEU n 
3 74  ARG n 
3 75  GLY n 
3 76  GLY 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 
2 1 sample 'Biological sequence' 1 352 ?     ? ?   ? ? ? ? ? ? Legionella     445  ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 76  human ? UBB ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           375 
_entity_src_nat.common_name                rabbit 
_entity_src_nat.pdbx_organism_scientific   'Oryctolagus cuniculus' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9986 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
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  
AR6 non-polymer         . 
;[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE
;
Adenosine-5-Diphosphoribose 'C15 H23 N5 O14 P2' 559.316 
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 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ?                           'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE ?                           'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                           'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                           'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ?                           'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE ?                           'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE ?                           'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ?                           'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ?                           'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ?                           'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                           'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ?                           'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?                           'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?                           'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                           'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?                           'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?                           'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   GLU 4   4   ?   ?   ?   A . n 
A 1 5   ILE 5   5   ?   ?   ?   A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   LEU 8   8   8   LEU LEU 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  ASP 11  11  11  ASP ASP A . n 
A 1 12  ASN 12  12  12  ASN ASN A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  MET 16  16  16  MET MET A . n 
A 1 17  CYS 17  17  17  CYS CYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  MET 44  44  44  MET MET A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  MET 47  47  47  MET MET A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  GLN 59  59  59  GLN GLN A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  HIS 73  73  73  HIS HIS A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  ASN 78  78  78  ASN ASN A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  LYS 84  84  84  LYS LYS A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  TRP 86  86  86  TRP TRP A . n 
A 1 87  HIS 87  87  87  HIS HIS A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  ARG 95  95  95  ARG ARG A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 PRO 109 109 109 PRO PRO A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 GLN 121 121 121 GLN GLN A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 MET 123 123 123 MET MET A . n 
A 1 124 PHE 124 124 124 PHE PHE A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 MET 132 132 132 MET MET A . n 
A 1 133 TYR 133 133 133 TYR TYR A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 GLN 137 137 137 GLN GLN A . n 
A 1 138 ALA 138 138 138 ALA ALA A . n 
A 1 139 VAL 139 139 139 VAL VAL A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 TYR 143 143 143 TYR TYR A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 THR 148 148 148 THR THR A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 MET 153 153 153 MET MET A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 PRO 164 164 164 PRO PRO A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 ILE 175 175 175 ILE ILE A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 THR 186 186 186 THR THR A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 MET 190 190 190 MET MET A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 ARG 206 206 206 ARG ARG A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 ARG 210 210 210 ARG ARG A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 LYS 213 213 213 LYS LYS A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 CYS 217 217 217 CYS CYS A . n 
A 1 218 TYR 218 218 218 TYR TYR A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 GLN 225 225 225 GLN GLN A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 MET 227 227 227 MET MET A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 THR 229 229 229 THR THR A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 ASP 244 244 244 ASP ASP A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 GLN 246 246 246 GLN GLN A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ILE 248 248 248 ILE ILE A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 GLU 253 253 253 GLU GLU A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 PHE 255 255 255 PHE PHE A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 CYS 257 257 257 CYS CYS A . n 
A 1 258 PRO 258 258 258 PRO PRO A . n 
A 1 259 GLU 259 259 259 GLU GLU A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
A 1 264 PRO 264 264 264 PRO PRO A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 MET 269 269 269 MET MET A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 CYS 272 272 272 CYS CYS A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 ILE 274 274 274 ILE ILE A . n 
A 1 275 HIS 275 275 275 HIS HIS A . n 
A 1 276 GLU 276 276 276 GLU GLU A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 ASN 280 280 280 ASN ASN A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 MET 283 283 283 MET MET A . n 
A 1 284 LYS 284 284 284 LYS LYS A . n 
A 1 285 CYS 285 285 285 CYS CYS A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 ASP 288 288 288 ASP ASP A . n 
A 1 289 ILE 289 289 289 ILE ILE A . n 
A 1 290 ARG 290 290 290 ARG ARG A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 TYR 294 294 294 TYR TYR A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 ASN 296 296 296 ASN ASN A . n 
A 1 297 THR 297 297 297 THR THR A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 SER 300 300 300 SER SER A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 MET 305 305 305 MET MET A . n 
A 1 306 TYR 306 306 306 TYR TYR A . n 
A 1 307 PRO 307 307 307 PRO PRO A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 ILE 309 309 309 ILE ILE A . n 
A 1 310 ALA 310 310 310 ALA ALA A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 ARG 312 312 312 ARG ARG A . n 
A 1 313 MET 313 313 313 MET MET A . n 
A 1 314 GLN 314 314 314 GLN GLN A . n 
A 1 315 LYS 315 315 315 LYS LYS A . n 
A 1 316 GLU 316 316 316 GLU GLU A . n 
A 1 317 ILE 317 317 317 ILE ILE A . n 
A 1 318 THR 318 318 318 THR THR A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 PRO 322 322 322 PRO PRO A . n 
A 1 323 SER 323 323 323 SER SER A . n 
A 1 324 THR 324 324 324 THR THR A . n 
A 1 325 MET 325 325 325 MET MET A . n 
A 1 326 LYS 326 326 326 LYS LYS A . n 
A 1 327 ILE 327 327 327 ILE ILE A . n 
A 1 328 LYS 328 328 328 LYS LYS A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 ILE 330 330 330 ILE ILE A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 PRO 332 332 332 PRO PRO A . n 
A 1 333 PRO 333 333 333 PRO PRO A . n 
A 1 334 GLU 334 334 334 GLU GLU A . n 
A 1 335 ARG 335 335 335 ARG ARG A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 TYR 337 337 337 TYR TYR A . n 
A 1 338 SER 338 338 338 SER SER A . n 
A 1 339 VAL 339 339 339 VAL VAL A . n 
A 1 340 TRP 340 340 340 TRP TRP A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 GLY 343 343 343 GLY GLY 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 LEU 346 346 346 LEU LEU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 SER 348 348 348 SER SER A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 SER 350 350 350 SER SER A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 PHE 352 352 352 PHE PHE A . n 
A 1 353 GLN 353 353 353 GLN GLN A . n 
A 1 354 GLN 354 354 354 GLN GLN A . n 
A 1 355 MET 355 355 355 MET MET A . n 
A 1 356 TRP 356 356 356 TRP TRP A . n 
A 1 357 ILE 357 357 357 ILE ILE A . n 
A 1 358 SER 358 358 358 SER SER A . n 
A 1 359 LYS 359 359 359 LYS LYS A . n 
A 1 360 GLN 360 360 360 GLN GLN A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 TYR 362 362 362 TYR TYR A . n 
A 1 363 ASP 363 363 363 ASP ASP A . n 
A 1 364 GLU 364 364 364 GLU GLU A . n 
A 1 365 SER 365 365 365 SER SER A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 PRO 367 367 367 PRO PRO A . n 
A 1 368 SER 368 368 368 SER SER A . n 
A 1 369 ILE 369 369 369 ILE ILE A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 HIS 371 371 371 HIS HIS A . n 
A 1 372 ARG 372 372 372 ARG ARG A . n 
A 1 373 LYS 373 373 373 LYS LYS A . n 
A 1 374 CYS 374 374 374 CYS CYS A . n 
A 1 375 PHE 375 375 375 PHE PHE A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLU 2   2   ?   ?   ?   B . n 
B 1 3   GLU 3   3   ?   ?   ?   B . n 
B 1 4   GLU 4   4   ?   ?   ?   B . n 
B 1 5   ILE 5   5   5   ILE ILE B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   LEU 8   8   8   LEU LEU 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  ASP 11  11  11  ASP ASP B . n 
B 1 12  ASN 12  12  12  ASN ASN B . n 
B 1 13  GLY 13  13  13  GLY GLY B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  MET 16  16  16  MET MET B . n 
B 1 17  CYS 17  17  17  CYS CYS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  GLY 20  20  20  GLY GLY B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  ASP 24  24  24  ASP ASP B . n 
B 1 25  ASP 25  25  25  ASP ASP B . n 
B 1 26  ALA 26  26  26  ALA ALA B . n 
B 1 27  PRO 27  27  27  PRO PRO B . n 
B 1 28  ARG 28  28  28  ARG ARG B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  SER 33  33  33  SER SER B . n 
B 1 34  ILE 34  34  34  ILE ILE B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  GLY 36  36  36  GLY GLY B . n 
B 1 37  ARG 37  37  37  ARG ARG B . n 
B 1 38  PRO 38  38  38  PRO PRO B . n 
B 1 39  ARG 39  39  39  ARG ARG B . n 
B 1 40  HIS 40  40  40  HIS HIS B . n 
B 1 41  GLN 41  41  41  GLN GLN B . n 
B 1 42  GLY 42  42  42  GLY GLY B . n 
B 1 43  VAL 43  43  43  VAL VAL B . n 
B 1 44  MET 44  44  44  MET MET B . n 
B 1 45  VAL 45  45  45  VAL VAL B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  MET 47  47  47  MET MET B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  ASP 51  51  51  ASP ASP B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  TYR 53  53  53  TYR TYR B . n 
B 1 54  VAL 54  54  54  VAL VAL B . n 
B 1 55  GLY 55  55  55  GLY GLY B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  GLU 57  57  57  GLU GLU B . n 
B 1 58  ALA 58  58  58  ALA ALA B . n 
B 1 59  GLN 59  59  59  GLN GLN B . n 
B 1 60  SER 60  60  60  SER SER B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  ARG 62  62  62  ARG ARG B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  ILE 64  64  64  ILE ILE B . n 
B 1 65  LEU 65  65  65  LEU LEU B . n 
B 1 66  THR 66  66  66  THR THR B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  LYS 68  68  68  LYS LYS B . n 
B 1 69  TYR 69  69  69  TYR TYR B . n 
B 1 70  PRO 70  70  70  PRO PRO B . n 
B 1 71  ILE 71  71  71  ILE ILE B . n 
B 1 72  GLU 72  72  72  GLU GLU B . n 
B 1 73  HIS 73  73  73  HIS HIS B . n 
B 1 74  GLY 74  74  74  GLY GLY B . n 
B 1 75  ILE 75  75  75  ILE ILE B . n 
B 1 76  VAL 76  76  76  VAL VAL B . n 
B 1 77  THR 77  77  77  THR THR B . n 
B 1 78  ASN 78  78  78  ASN ASN B . n 
B 1 79  TRP 79  79  79  TRP TRP B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  ASP 81  81  81  ASP ASP B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  GLU 83  83  83  GLU GLU B . n 
B 1 84  LYS 84  84  84  LYS LYS B . n 
B 1 85  ILE 85  85  85  ILE ILE B . n 
B 1 86  TRP 86  86  86  TRP TRP B . n 
B 1 87  HIS 87  87  87  HIS HIS B . n 
B 1 88  HIS 88  88  88  HIS HIS B . n 
B 1 89  THR 89  89  89  THR THR B . n 
B 1 90  PHE 90  90  90  PHE PHE B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  ASN 92  92  92  ASN ASN B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  LEU 94  94  94  LEU LEU B . n 
B 1 95  ARG 95  95  95  ARG ARG B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  GLU 99  99  99  GLU GLU B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 PRO 102 102 102 PRO PRO B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 GLU 107 107 107 GLU GLU B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 PRO 109 109 109 PRO PRO B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 ASN 111 111 111 ASN ASN B . n 
B 1 112 PRO 112 112 112 PRO PRO B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 ARG 116 116 116 ARG ARG B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 LYS 118 118 118 LYS LYS B . n 
B 1 119 MET 119 119 119 MET MET B . n 
B 1 120 THR 120 120 120 THR THR B . n 
B 1 121 GLN 121 121 121 GLN GLN B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 MET 123 123 123 MET MET B . n 
B 1 124 PHE 124 124 124 PHE PHE B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 THR 126 126 126 THR THR B . n 
B 1 127 PHE 127 127 127 PHE PHE B . n 
B 1 128 ASN 128 128 128 ASN ASN B . n 
B 1 129 THR 129 129 129 THR THR B . n 
B 1 130 PRO 130 130 130 PRO PRO B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 MET 132 132 132 MET MET B . n 
B 1 133 TYR 133 133 133 TYR TYR B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 GLN 137 137 137 GLN GLN B . n 
B 1 138 ALA 138 138 138 ALA ALA B . n 
B 1 139 VAL 139 139 139 VAL VAL B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 SER 141 141 141 SER SER B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 TYR 143 143 143 TYR TYR B . n 
B 1 144 ALA 144 144 144 ALA ALA B . n 
B 1 145 SER 145 145 145 SER SER B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 ARG 147 147 147 ARG ARG B . n 
B 1 148 THR 148 148 148 THR THR B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 MET 153 153 153 MET MET B . n 
B 1 154 ASP 154 154 154 ASP ASP B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 GLY 158 158 158 GLY GLY B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 THR 160 160 160 THR THR B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 THR 162 162 162 THR THR B . n 
B 1 163 VAL 163 163 163 VAL VAL B . n 
B 1 164 PRO 164 164 164 PRO PRO B . n 
B 1 165 ILE 165 165 165 ILE ILE B . n 
B 1 166 TYR 166 166 166 TYR TYR B . n 
B 1 167 GLU 167 167 167 GLU GLU B . n 
B 1 168 GLY 168 168 168 GLY GLY B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 ALA 170 170 170 ALA ALA B . n 
B 1 171 LEU 171 171 171 LEU LEU B . n 
B 1 172 PRO 172 172 172 PRO PRO B . n 
B 1 173 HIS 173 173 173 HIS HIS B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 ILE 175 175 175 ILE ILE B . n 
B 1 176 LEU 176 176 176 LEU LEU B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 LEU 178 178 178 LEU LEU B . n 
B 1 179 ASP 179 179 179 ASP ASP B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 ALA 181 181 181 ALA ALA B . n 
B 1 182 GLY 182 182 182 GLY GLY B . n 
B 1 183 ARG 183 183 183 ARG ARG B . n 
B 1 184 ASP 184 184 184 ASP ASP B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 THR 186 186 186 THR THR B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 TYR 188 188 188 TYR TYR B . n 
B 1 189 LEU 189 189 189 LEU LEU B . n 
B 1 190 MET 190 190 190 MET MET B . n 
B 1 191 LYS 191 191 191 LYS LYS B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 LEU 193 193 193 LEU LEU B . n 
B 1 194 THR 194 194 194 THR THR B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 ARG 196 196 196 ARG ARG B . n 
B 1 197 GLY 197 197 197 GLY GLY B . n 
B 1 198 TYR 198 198 198 TYR TYR B . n 
B 1 199 SER 199 199 199 SER SER B . n 
B 1 200 PHE 200 200 200 PHE PHE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 THR 202 202 202 THR THR B . n 
B 1 203 THR 203 203 203 THR THR B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 GLU 205 205 205 GLU GLU B . n 
B 1 206 ARG 206 206 206 ARG ARG B . n 
B 1 207 GLU 207 207 207 GLU GLU B . n 
B 1 208 ILE 208 208 208 ILE ILE B . n 
B 1 209 VAL 209 209 209 VAL VAL B . n 
B 1 210 ARG 210 210 210 ARG ARG B . n 
B 1 211 ASP 211 211 211 ASP ASP B . n 
B 1 212 ILE 212 212 212 ILE ILE B . n 
B 1 213 LYS 213 213 213 LYS LYS B . n 
B 1 214 GLU 214 214 214 GLU GLU B . n 
B 1 215 LYS 215 215 215 LYS LYS B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 CYS 217 217 217 CYS CYS B . n 
B 1 218 TYR 218 218 218 TYR TYR B . n 
B 1 219 VAL 219 219 219 VAL VAL B . n 
B 1 220 ALA 220 220 220 ALA ALA B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 ASP 222 222 222 ASP ASP B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 GLU 224 224 224 GLU GLU B . n 
B 1 225 GLN 225 225 225 GLN GLN B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 MET 227 227 227 MET MET B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 THR 229 229 229 THR THR B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 ALA 231 231 231 ALA ALA B . n 
B 1 232 SER 232 232 232 SER SER B . n 
B 1 233 SER 233 233 233 SER SER B . n 
B 1 234 SER 234 234 234 SER SER B . n 
B 1 235 SER 235 235 235 SER SER B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 GLU 237 237 237 GLU GLU B . n 
B 1 238 LYS 238 238 238 LYS LYS B . n 
B 1 239 SER 239 239 239 SER SER B . n 
B 1 240 TYR 240 240 240 TYR TYR B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 PRO 243 243 243 PRO PRO B . n 
B 1 244 ASP 244 244 244 ASP ASP B . n 
B 1 245 GLY 245 245 245 GLY GLY B . n 
B 1 246 GLN 246 246 246 GLN GLN B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ILE 248 248 248 ILE ILE B . n 
B 1 249 THR 249 249 249 THR THR B . n 
B 1 250 ILE 250 250 250 ILE ILE B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 ASN 252 252 252 ASN ASN B . n 
B 1 253 GLU 253 253 253 GLU GLU B . n 
B 1 254 ARG 254 254 254 ARG ARG B . n 
B 1 255 PHE 255 255 255 PHE PHE B . n 
B 1 256 ARG 256 256 256 ARG ARG B . n 
B 1 257 CYS 257 257 257 CYS CYS B . n 
B 1 258 PRO 258 258 258 PRO PRO B . n 
B 1 259 GLU 259 259 259 GLU GLU B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 LEU 261 261 261 LEU LEU B . n 
B 1 262 PHE 262 262 262 PHE PHE B . n 
B 1 263 GLN 263 263 263 GLN GLN B . n 
B 1 264 PRO 264 264 264 PRO PRO B . n 
B 1 265 SER 265 265 265 SER SER B . n 
B 1 266 PHE 266 266 266 PHE PHE B . n 
B 1 267 LEU 267 267 267 LEU LEU B . n 
B 1 268 GLY 268 268 268 GLY GLY B . n 
B 1 269 MET 269 269 269 MET MET B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 SER 271 271 271 SER SER B . n 
B 1 272 CYS 272 272 272 CYS CYS B . n 
B 1 273 GLY 273 273 273 GLY GLY B . n 
B 1 274 ILE 274 274 274 ILE ILE B . n 
B 1 275 HIS 275 275 275 HIS HIS B . n 
B 1 276 GLU 276 276 276 GLU GLU B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 THR 278 278 278 THR THR B . n 
B 1 279 PHE 279 279 279 PHE PHE B . n 
B 1 280 ASN 280 280 280 ASN ASN B . n 
B 1 281 SER 281 281 281 SER SER B . n 
B 1 282 ILE 282 282 282 ILE ILE B . n 
B 1 283 MET 283 283 283 MET MET B . n 
B 1 284 LYS 284 284 284 LYS LYS B . n 
B 1 285 CYS 285 285 285 CYS CYS B . n 
B 1 286 ASP 286 286 286 ASP ASP B . n 
B 1 287 VAL 287 287 287 VAL VAL B . n 
B 1 288 ASP 288 288 288 ASP ASP B . n 
B 1 289 ILE 289 289 289 ILE ILE B . n 
B 1 290 ARG 290 290 290 ARG ARG B . n 
B 1 291 LYS 291 291 291 LYS LYS B . n 
B 1 292 ASP 292 292 292 ASP ASP B . n 
B 1 293 LEU 293 293 293 LEU LEU B . n 
B 1 294 TYR 294 294 294 TYR TYR B . n 
B 1 295 ALA 295 295 295 ALA ALA B . n 
B 1 296 ASN 296 296 296 ASN ASN B . n 
B 1 297 THR 297 297 297 THR THR B . n 
B 1 298 VAL 298 298 298 VAL VAL B . n 
B 1 299 LEU 299 299 299 LEU LEU B . n 
B 1 300 SER 300 300 300 SER SER B . n 
B 1 301 GLY 301 301 301 GLY GLY B . n 
B 1 302 GLY 302 302 302 GLY GLY B . n 
B 1 303 THR 303 303 303 THR THR B . n 
B 1 304 THR 304 304 304 THR THR B . n 
B 1 305 MET 305 305 305 MET MET B . n 
B 1 306 TYR 306 306 306 TYR TYR B . n 
B 1 307 PRO 307 307 307 PRO PRO B . n 
B 1 308 GLY 308 308 308 GLY GLY B . n 
B 1 309 ILE 309 309 309 ILE ILE B . n 
B 1 310 ALA 310 310 310 ALA ALA B . n 
B 1 311 ASP 311 311 311 ASP ASP B . n 
B 1 312 ARG 312 312 312 ARG ARG B . n 
B 1 313 MET 313 313 313 MET MET B . n 
B 1 314 GLN 314 314 314 GLN GLN B . n 
B 1 315 LYS 315 315 315 LYS LYS B . n 
B 1 316 GLU 316 316 316 GLU GLU B . n 
B 1 317 ILE 317 317 317 ILE ILE B . n 
B 1 318 THR 318 318 318 THR THR B . n 
B 1 319 ALA 319 319 319 ALA ALA B . n 
B 1 320 LEU 320 320 320 LEU LEU B . n 
B 1 321 ALA 321 321 321 ALA ALA B . n 
B 1 322 PRO 322 322 322 PRO PRO B . n 
B 1 323 SER 323 323 323 SER SER B . n 
B 1 324 THR 324 324 324 THR THR B . n 
B 1 325 MET 325 325 325 MET MET B . n 
B 1 326 LYS 326 326 326 LYS LYS B . n 
B 1 327 ILE 327 327 327 ILE ILE B . n 
B 1 328 LYS 328 328 328 LYS LYS B . n 
B 1 329 ILE 329 329 329 ILE ILE B . n 
B 1 330 ILE 330 330 330 ILE ILE B . n 
B 1 331 ALA 331 331 331 ALA ALA B . n 
B 1 332 PRO 332 332 332 PRO PRO B . n 
B 1 333 PRO 333 333 333 PRO PRO B . n 
B 1 334 GLU 334 334 334 GLU GLU B . n 
B 1 335 ARG 335 335 335 ARG ARG B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 TYR 337 337 337 TYR TYR B . n 
B 1 338 SER 338 338 338 SER SER B . n 
B 1 339 VAL 339 339 339 VAL VAL B . n 
B 1 340 TRP 340 340 340 TRP TRP B . n 
B 1 341 ILE 341 341 341 ILE ILE B . n 
B 1 342 GLY 342 342 342 GLY GLY B . n 
B 1 343 GLY 343 343 343 GLY GLY 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 LEU 346 346 346 LEU LEU B . n 
B 1 347 ALA 347 347 347 ALA ALA B . n 
B 1 348 SER 348 348 348 SER SER B . n 
B 1 349 LEU 349 349 349 LEU LEU B . n 
B 1 350 SER 350 350 350 SER SER B . n 
B 1 351 THR 351 351 351 THR THR B . n 
B 1 352 PHE 352 352 352 PHE PHE B . n 
B 1 353 GLN 353 353 353 GLN GLN B . n 
B 1 354 GLN 354 354 354 GLN GLN B . n 
B 1 355 MET 355 355 355 MET MET B . n 
B 1 356 TRP 356 356 356 TRP TRP B . n 
B 1 357 ILE 357 357 357 ILE ILE B . n 
B 1 358 SER 358 358 358 SER SER B . n 
B 1 359 LYS 359 359 359 LYS LYS B . n 
B 1 360 GLN 360 360 360 GLN GLN B . n 
B 1 361 GLU 361 361 361 GLU GLU B . n 
B 1 362 TYR 362 362 362 TYR TYR B . n 
B 1 363 ASP 363 363 363 ASP ASP B . n 
B 1 364 GLU 364 364 364 GLU GLU B . n 
B 1 365 SER 365 365 365 SER SER B . n 
B 1 366 GLY 366 366 366 GLY GLY B . n 
B 1 367 PRO 367 367 367 PRO PRO B . n 
B 1 368 SER 368 368 368 SER SER B . n 
B 1 369 ILE 369 369 369 ILE ILE B . n 
B 1 370 VAL 370 370 370 VAL VAL B . n 
B 1 371 HIS 371 371 371 HIS HIS B . n 
B 1 372 ARG 372 372 372 ARG ARG B . n 
B 1 373 LYS 373 373 373 LYS LYS B . n 
B 1 374 CYS 374 374 374 CYS CYS B . n 
B 1 375 PHE 375 375 375 PHE PHE B . n 
C 2 1   MET 1   19  ?   ?   ?   C . n 
C 2 2   SER 2   20  ?   ?   ?   C . n 
C 2 3   TYR 3   21  ?   ?   ?   C . n 
C 2 4   GLN 4   22  ?   ?   ?   C . n 
C 2 5   LYS 5   23  ?   ?   ?   C . n 
C 2 6   ILE 6   24  24  ILE ILE C . n 
C 2 7   GLU 7   25  25  GLU GLU C . n 
C 2 8   LEU 8   26  26  LEU LEU C . n 
C 2 9   SER 9   27  27  SER SER C . n 
C 2 10  ILE 10  28  28  ILE ILE C . n 
C 2 11  SER 11  29  29  SER SER C . n 
C 2 12  LEU 12  30  30  LEU LEU C . n 
C 2 13  SER 13  31  31  SER SER C . n 
C 2 14  LEU 14  32  32  LEU LEU C . n 
C 2 15  ASP 15  33  33  ASP ASP C . n 
C 2 16  SER 16  34  34  SER SER C . n 
C 2 17  PRO 17  35  35  PRO PRO C . n 
C 2 18  LYS 18  36  36  LYS LYS C . n 
C 2 19  LEU 19  37  37  LEU LEU C . n 
C 2 20  ASP 20  38  38  ASP ASP C . n 
C 2 21  GLU 21  39  39  GLU GLU C . n 
C 2 22  SER 22  40  40  SER SER C . n 
C 2 23  ASP 23  41  41  ASP ASP C . n 
C 2 24  PHE 24  42  42  PHE PHE C . n 
C 2 25  ILE 25  43  43  ILE ILE C . n 
C 2 26  LEU 26  44  44  LEU LEU C . n 
C 2 27  LEU 27  45  45  LEU LEU C . n 
C 2 28  SER 28  46  46  SER SER C . n 
C 2 29  VAL 29  47  47  VAL VAL C . n 
C 2 30  LYS 30  48  48  LYS LYS C . n 
C 2 31  TYR 31  49  49  TYR TYR C . n 
C 2 32  LEU 32  50  50  LEU LEU C . n 
C 2 33  GLU 33  51  51  GLU GLU C . n 
C 2 34  LYS 34  52  52  LYS LYS C . n 
C 2 35  SER 35  53  53  SER SER C . n 
C 2 36  LEU 36  54  54  LEU LEU C . n 
C 2 37  GLY 37  55  55  GLY GLY C . n 
C 2 38  LYS 38  56  56  LYS LYS C . n 
C 2 39  LYS 39  57  57  LYS LYS C . n 
C 2 40  LYS 40  58  58  LYS LYS C . n 
C 2 41  GLU 41  59  59  GLU GLU C . n 
C 2 42  PHE 42  60  60  PHE PHE C . n 
C 2 43  SER 43  61  61  SER SER C . n 
C 2 44  GLY 44  62  62  GLY GLY C . n 
C 2 45  PHE 45  63  63  PHE PHE C . n 
C 2 46  PHE 46  64  64  PHE PHE C . n 
C 2 47  GLU 47  65  65  GLU GLU C . n 
C 2 48  ASP 48  66  66  ASP ASP C . n 
C 2 49  ILE 49  67  67  ILE ILE C . n 
C 2 50  GLU 50  68  68  GLU GLU C . n 
C 2 51  LYS 51  69  69  LYS LYS C . n 
C 2 52  LEU 52  70  70  LEU LEU C . n 
C 2 53  TYR 53  71  71  TYR TYR C . n 
C 2 54  PHE 54  72  72  PHE PHE C . n 
C 2 55  LYS 55  73  73  LYS LYS C . n 
C 2 56  GLN 56  74  74  GLN GLN C . n 
C 2 57  ASN 57  75  75  ASN ASN C . n 
C 2 58  TYR 58  76  76  TYR TYR C . n 
C 2 59  LYS 59  77  77  LYS LYS C . n 
C 2 60  GLU 60  78  78  GLU GLU C . n 
C 2 61  ALA 61  79  79  ALA ALA C . n 
C 2 62  ILE 62  80  80  ILE ILE C . n 
C 2 63  GLU 63  81  81  GLU GLU C . n 
C 2 64  LYS 64  82  82  LYS LYS C . n 
C 2 65  ILE 65  83  83  ILE ILE C . n 
C 2 66  LEU 66  84  84  LEU LEU C . n 
C 2 67  ASP 67  85  85  ASP ASP C . n 
C 2 68  PHE 68  86  86  PHE PHE C . n 
C 2 69  CYS 69  87  87  CYS CYS C . n 
C 2 70  LYS 70  88  88  LYS LYS C . n 
C 2 71  LYS 71  89  89  LYS LYS C . n 
C 2 72  ASN 72  90  90  ASN ASN C . n 
C 2 73  GLU 73  91  91  GLU GLU C . n 
C 2 74  SER 74  92  92  SER SER C . n 
C 2 75  LEU 75  93  93  LEU LEU C . n 
C 2 76  LEU 76  94  94  LEU LEU C . n 
C 2 77  SER 77  95  95  SER SER C . n 
C 2 78  GLU 78  96  96  GLU GLU C . n 
C 2 79  GLN 79  97  97  GLN GLN C . n 
C 2 80  VAL 80  98  98  VAL VAL C . n 
C 2 81  VAL 81  99  99  VAL VAL C . n 
C 2 82  GLN 82  100 100 GLN GLN C . n 
C 2 83  ARG 83  101 101 ARG ARG C . n 
C 2 84  LEU 84  102 102 LEU LEU C . n 
C 2 85  ALA 85  103 103 ALA ALA C . n 
C 2 86  GLU 86  104 104 GLU GLU C . n 
C 2 87  VAL 87  105 105 VAL VAL C . n 
C 2 88  ALA 88  106 106 ALA ALA C . n 
C 2 89  PRO 89  107 107 PRO PRO C . n 
C 2 90  ARG 90  108 108 ARG ARG C . n 
C 2 91  LEU 91  109 109 LEU LEU C . n 
C 2 92  LYS 92  110 110 LYS LYS C . n 
C 2 93  SER 93  111 111 SER SER C . n 
C 2 94  ASN 94  112 112 ASN ASN C . n 
C 2 95  PRO 95  113 113 PRO PRO C . n 
C 2 96  LYS 96  114 114 LYS LYS C . n 
C 2 97  ASP 97  115 115 ASP ASP C . n 
C 2 98  ASN 98  116 116 ASN ASN C . n 
C 2 99  GLU 99  117 117 GLU GLU C . n 
C 2 100 SER 100 118 118 SER SER C . n 
C 2 101 ARG 101 119 119 ARG ARG C . n 
C 2 102 ARG 102 120 120 ARG ARG C . n 
C 2 103 LEU 103 121 121 LEU LEU C . n 
C 2 104 TYR 104 122 122 TYR TYR C . n 
C 2 105 GLU 105 123 123 GLU GLU C . n 
C 2 106 THR 106 124 124 THR THR C . n 
C 2 107 LEU 107 125 125 LEU LEU C . n 
C 2 108 TYR 108 126 126 TYR TYR C . n 
C 2 109 ALA 109 127 127 ALA ALA C . n 
C 2 110 ASP 110 128 128 ASP ASP C . n 
C 2 111 HIS 111 129 129 HIS HIS C . n 
C 2 112 LEU 112 130 130 LEU LEU C . n 
C 2 113 GLU 113 131 131 GLU GLU C . n 
C 2 114 SER 114 132 132 SER SER C . n 
C 2 115 VAL 115 133 133 VAL VAL C . n 
C 2 116 ILE 116 134 134 ILE ILE C . n 
C 2 117 LYS 117 135 135 LYS LYS C . n 
C 2 118 GLN 118 136 136 GLN GLN C . n 
C 2 119 GLU 119 137 137 GLU GLU C . n 
C 2 120 SER 120 138 138 SER SER C . n 
C 2 121 ASP 121 139 139 ASP ASP C . n 
C 2 122 LEU 122 140 140 LEU LEU C . n 
C 2 123 SER 123 141 141 SER SER C . n 
C 2 124 VAL 124 142 142 VAL VAL C . n 
C 2 125 PHE 125 143 143 PHE PHE C . n 
C 2 126 ASN 126 144 144 ASN ASN C . n 
C 2 127 GLU 127 145 145 GLU GLU C . n 
C 2 128 LEU 128 146 146 LEU LEU C . n 
C 2 129 ARG 129 147 147 ARG ARG C . n 
C 2 130 ASP 130 148 148 ASP ASP C . n 
C 2 131 SER 131 149 149 SER SER C . n 
C 2 132 TYR 132 150 150 TYR TYR C . n 
C 2 133 ASN 133 151 151 ASN ASN C . n 
C 2 134 ALA 134 152 152 ALA ALA C . n 
C 2 135 VAL 135 153 153 VAL VAL C . n 
C 2 136 LYS 136 154 154 LYS LYS C . n 
C 2 137 PRO 137 155 155 PRO PRO C . n 
C 2 138 GLU 138 156 156 GLU GLU C . n 
C 2 139 TYR 139 157 157 TYR TYR C . n 
C 2 140 ALA 140 158 158 ALA ALA C . n 
C 2 141 VAL 141 159 159 VAL VAL C . n 
C 2 142 THR 142 160 160 THR THR C . n 
C 2 143 HIS 143 161 161 HIS HIS C . n 
C 2 144 GLU 144 162 162 GLU GLU C . n 
C 2 145 THR 145 163 163 THR THR C . n 
C 2 146 GLU 146 164 164 GLU GLU C . n 
C 2 147 ILE 147 165 165 ILE ILE C . n 
C 2 148 LYS 148 166 166 LYS LYS C . n 
C 2 149 THR 149 167 167 THR THR C . n 
C 2 150 LEU 150 168 168 LEU LEU C . n 
C 2 151 ASP 151 169 169 ASP ASP C . n 
C 2 152 GLU 152 170 170 GLU GLU C . n 
C 2 153 ALA 153 171 171 ALA ALA C . n 
C 2 154 LYS 154 172 172 LYS LYS C . n 
C 2 155 GLN 155 173 173 GLN GLN C . n 
C 2 156 PHE 156 174 174 PHE PHE C . n 
C 2 157 ILE 157 175 175 ILE ILE C . n 
C 2 158 LEU 158 176 176 LEU LEU C . n 
C 2 159 SER 159 177 177 SER SER C . n 
C 2 160 PHE 160 178 178 PHE PHE C . n 
C 2 161 VAL 161 179 179 VAL VAL C . n 
C 2 162 MET 162 180 180 MET MET C . n 
C 2 163 LEU 163 181 181 LEU LEU C . n 
C 2 164 ASN 164 182 182 ASN ASN C . n 
C 2 165 ASP 165 183 183 ASP ASP C . n 
C 2 166 ASN 166 184 184 ASN ASN C . n 
C 2 167 VAL 167 185 185 VAL VAL C . n 
C 2 168 GLU 168 186 186 GLU GLU C . n 
C 2 169 LEU 169 187 187 LEU LEU C . n 
C 2 170 PRO 170 188 188 PRO PRO C . n 
C 2 171 LEU 171 189 189 LEU LEU C . n 
C 2 172 LYS 172 190 190 LYS LYS C . n 
C 2 173 ALA 173 191 191 ALA ALA C . n 
C 2 174 GLN 174 192 192 GLN GLN C . n 
C 2 175 SER 175 193 193 SER SER C . n 
C 2 176 GLU 176 194 194 GLU GLU C . n 
C 2 177 ARG 177 195 195 ARG ARG C . n 
C 2 178 TYR 178 196 196 TYR TYR C . n 
C 2 179 PRO 179 197 197 PRO PRO C . n 
C 2 180 LYS 180 198 198 LYS LYS C . n 
C 2 181 LYS 181 199 199 LYS LYS C . n 
C 2 182 ASP 182 200 200 ASP ASP C . n 
C 2 183 ARG 183 201 201 ARG ARG C . n 
C 2 184 SER 184 202 202 SER SER C . n 
C 2 185 ARG 185 203 203 ARG ARG C . n 
C 2 186 GLU 186 204 204 GLU GLU C . n 
C 2 187 GLU 187 205 205 GLU GLU C . n 
C 2 188 LEU 188 206 206 LEU LEU C . n 
C 2 189 GLY 189 207 207 GLY GLY C . n 
C 2 190 ASN 190 208 208 ASN ASN C . n 
C 2 191 THR 191 209 209 THR THR C . n 
C 2 192 PRO 192 210 210 PRO PRO C . n 
C 2 193 SER 193 211 211 SER SER C . n 
C 2 194 ALA 194 212 212 ALA ALA C . n 
C 2 195 ASN 195 213 213 ASN ASN C . n 
C 2 196 PRO 196 214 214 PRO PRO C . n 
C 2 197 GLY 197 215 215 GLY GLY C . n 
C 2 198 ILE 198 216 216 ILE ILE C . n 
C 2 199 MET 199 217 217 MET MET C . n 
C 2 200 LYS 200 218 218 LYS LYS C . n 
C 2 201 PRO 201 219 219 PRO PRO C . n 
C 2 202 ASN 202 220 220 ASN ASN C . n 
C 2 203 SER 203 221 221 SER SER C . n 
C 2 204 PRO 204 222 222 PRO PRO C . n 
C 2 205 ASN 205 223 223 ASN ASN C . n 
C 2 206 PHE 206 224 224 PHE PHE C . n 
C 2 207 THR 207 225 225 THR THR C . n 
C 2 208 ASP 208 226 226 ASP ASP C . n 
C 2 209 ASN 209 227 227 ASN ASN C . n 
C 2 210 LEU 210 228 228 LEU LEU C . n 
C 2 211 VAL 211 229 229 VAL VAL C . n 
C 2 212 PRO 212 230 230 PRO PRO C . n 
C 2 213 VAL 213 231 231 VAL VAL C . n 
C 2 214 ARG 214 232 232 ARG ARG C . n 
C 2 215 ASP 215 233 233 ASP ASP C . n 
C 2 216 VAL 216 234 234 VAL VAL C . n 
C 2 217 PRO 217 235 235 PRO PRO C . n 
C 2 218 LYS 218 236 236 LYS LYS C . n 
C 2 219 ILE 219 237 237 ILE ILE C . n 
C 2 220 ALA 220 238 238 ALA ALA C . n 
C 2 221 ILE 221 239 239 ILE ILE C . n 
C 2 222 ASN 222 240 240 ASN ASN C . n 
C 2 223 GLU 223 241 241 GLU GLU C . n 
C 2 224 LYS 224 242 242 LYS LYS C . n 
C 2 225 VAL 225 243 243 VAL VAL C . n 
C 2 226 ALA 226 244 244 ALA ALA C . n 
C 2 227 GLY 227 245 245 GLY GLY C . n 
C 2 228 GLY 228 246 246 GLY GLY C . n 
C 2 229 TYR 229 247 247 TYR TYR C . n 
C 2 230 SER 230 248 248 SER SER C . n 
C 2 231 LYS 231 249 249 LYS LYS C . n 
C 2 232 THR 232 250 250 THR THR C . n 
C 2 233 LYS 233 251 251 LYS LYS C . n 
C 2 234 PRO 234 252 252 PRO PRO C . n 
C 2 235 THR 235 253 253 THR THR C . n 
C 2 236 THR 236 254 254 THR THR C . n 
C 2 237 PRO 237 255 255 PRO PRO C . n 
C 2 238 PHE 238 256 256 PHE PHE C . n 
C 2 239 VAL 239 257 257 VAL VAL C . n 
C 2 240 ALA 240 258 258 ALA ALA C . n 
C 2 241 SER 241 259 259 SER SER C . n 
C 2 242 LEU 242 260 260 LEU LEU C . n 
C 2 243 SER 243 261 261 SER SER C . n 
C 2 244 GLY 244 262 262 GLY GLY C . n 
C 2 245 THR 245 263 263 THR THR C . n 
C 2 246 THR 246 264 264 THR THR C . n 
C 2 247 TYR 247 265 265 TYR TYR C . n 
C 2 248 SER 248 266 266 SER SER C . n 
C 2 249 LEU 249 267 267 LEU LEU C . n 
C 2 250 MET 250 268 268 MET MET C . n 
C 2 251 VAL 251 269 269 VAL VAL C . n 
C 2 252 VAL 252 270 270 VAL VAL C . n 
C 2 253 LEU 253 271 271 LEU LEU C . n 
C 2 254 THR 254 272 272 THR THR C . n 
C 2 255 ASP 255 273 273 ASP ASP C . n 
C 2 256 TYR 256 274 274 TYR TYR C . n 
C 2 257 ILE 257 275 275 ILE ILE C . n 
C 2 258 GLU 258 276 276 GLU GLU C . n 
C 2 259 LYS 259 277 277 LYS LYS C . n 
C 2 260 HIS 260 278 278 HIS HIS C . n 
C 2 261 LYS 261 279 279 LYS LYS C . n 
C 2 262 THR 262 280 280 THR THR C . n 
C 2 263 ASP 263 281 281 ASP ASP C . n 
C 2 264 LYS 264 282 282 LYS LYS C . n 
C 2 265 ASP 265 283 283 ASP ASP C . n 
C 2 266 ILE 266 284 284 ILE ILE C . n 
C 2 267 GLU 267 285 285 GLU GLU C . n 
C 2 268 LYS 268 286 286 LYS LYS C . n 
C 2 269 LYS 269 287 287 LYS LYS C . n 
C 2 270 VAL 270 288 288 VAL VAL C . n 
C 2 271 ASN 271 289 289 ASN ASN C . n 
C 2 272 GLN 272 290 290 GLN GLN C . n 
C 2 273 ILE 273 291 291 ILE ILE C . n 
C 2 274 ILE 274 292 292 ILE ILE C . n 
C 2 275 ASN 275 293 293 ASN ASN C . n 
C 2 276 LEU 276 294 294 LEU LEU C . n 
C 2 277 TRP 277 295 295 TRP TRP C . n 
C 2 278 ILE 278 296 296 ILE ILE C . n 
C 2 279 SER 279 297 297 SER SER C . n 
C 2 280 SER 280 298 298 SER SER C . n 
C 2 281 TYR 281 299 299 TYR TYR C . n 
C 2 282 ILE 282 300 300 ILE ILE C . n 
C 2 283 LYS 283 301 301 LYS LYS C . n 
C 2 284 GLU 284 302 302 GLU GLU C . n 
C 2 285 GLY 285 303 303 GLY GLY C . n 
C 2 286 TYR 286 304 304 TYR TYR C . n 
C 2 287 HIS 287 305 305 HIS HIS C . n 
C 2 288 SER 288 306 306 SER SER C . n 
C 2 289 TYR 289 307 307 TYR TYR C . n 
C 2 290 SER 290 308 308 SER SER C . n 
C 2 291 GLU 291 309 309 GLU GLU C . n 
C 2 292 VAL 292 310 310 VAL VAL C . n 
C 2 293 VAL 293 311 311 VAL VAL C . n 
C 2 294 ASP 294 312 312 ASP ASP C . n 
C 2 295 VAL 295 313 313 VAL VAL C . n 
C 2 296 LEU 296 314 314 LEU LEU C . n 
C 2 297 THR 297 315 315 THR THR C . n 
C 2 298 GLU 298 316 316 GLU GLU C . n 
C 2 299 PRO 299 317 317 PRO PRO C . n 
C 2 300 PHE 300 318 318 PHE PHE C . n 
C 2 301 LEU 301 319 319 LEU LEU C . n 
C 2 302 GLN 302 320 320 GLN GLN C . n 
C 2 303 SER 303 321 321 SER SER C . n 
C 2 304 ILE 304 322 322 ILE ILE C . n 
C 2 305 PHE 305 323 323 PHE PHE C . n 
C 2 306 ASP 306 324 324 ASP ASP C . n 
C 2 307 LYS 307 325 325 LYS LYS C . n 
C 2 308 ALA 308 326 326 ALA ALA C . n 
C 2 309 ASN 309 327 327 ASN ASN C . n 
C 2 310 ILE 310 328 328 ILE ILE C . n 
C 2 311 LYS 311 329 329 LYS LYS C . n 
C 2 312 LEU 312 330 330 LEU LEU C . n 
C 2 313 ASN 313 331 331 ASN ASN C . n 
C 2 314 TYR 314 332 332 TYR TYR C . n 
C 2 315 GLY 315 333 333 GLY GLY C . n 
C 2 316 VAL 316 334 334 VAL VAL C . n 
C 2 317 LEU 317 335 335 LEU LEU C . n 
C 2 318 ASP 318 336 336 ASP ASP C . n 
C 2 319 ASP 319 337 337 ASP ASP C . n 
C 2 320 THR 320 338 338 THR THR C . n 
C 2 321 HIS 321 339 339 HIS HIS C . n 
C 2 322 ALA 322 340 340 ALA ALA C . n 
C 2 323 GLU 323 341 341 GLU GLU C . n 
C 2 324 PHE 324 342 342 PHE PHE C . n 
C 2 325 ARG 325 343 343 ARG ARG C . n 
C 2 326 LYS 326 344 344 LYS LYS C . n 
C 2 327 ALA 327 345 345 ALA ALA C . n 
C 2 328 GLN 328 346 346 GLN GLN C . n 
C 2 329 ASP 329 347 347 ASP ASP C . n 
C 2 330 TYR 330 348 348 TYR TYR C . n 
C 2 331 VAL 331 349 349 VAL VAL C . n 
C 2 332 PHE 332 350 350 PHE PHE C . n 
C 2 333 GLY 333 351 351 GLY GLY C . n 
C 2 334 LEU 334 352 352 LEU LEU C . n 
C 2 335 THR 335 353 353 THR THR C . n 
C 2 336 ILE 336 354 354 ILE ILE C . n 
C 2 337 GLN 337 355 355 GLN GLN C . n 
C 2 338 SER 338 356 356 SER SER C . n 
C 2 339 ALA 339 357 357 ALA ALA C . n 
C 2 340 MET 340 358 358 MET MET C . n 
C 2 341 HIS 341 359 359 HIS HIS C . n 
C 2 342 HIS 342 360 360 HIS HIS C . n 
C 2 343 GLU 343 361 361 GLU GLU C . n 
C 2 344 LEU 344 362 362 LEU LEU C . n 
C 2 345 GLN 345 363 363 GLN GLN C . n 
C 2 346 GLU 346 364 364 GLU GLU C . n 
C 2 347 ARG 347 365 365 ARG ARG C . n 
C 2 348 PHE 348 366 366 PHE PHE C . n 
C 2 349 LYS 349 367 367 LYS LYS C . n 
C 2 350 ASN 350 368 368 ASN ASN C . n 
C 2 351 LYS 351 369 369 LYS LYS C . n 
C 2 352 GLU 352 370 370 GLU GLU C . n 
D 2 1   MET 1   19  ?   ?   ?   D . n 
D 2 2   SER 2   20  ?   ?   ?   D . n 
D 2 3   TYR 3   21  ?   ?   ?   D . n 
D 2 4   GLN 4   22  ?   ?   ?   D . n 
D 2 5   LYS 5   23  23  LYS LYS D . n 
D 2 6   ILE 6   24  24  ILE ILE D . n 
D 2 7   GLU 7   25  25  GLU GLU D . n 
D 2 8   LEU 8   26  26  LEU LEU D . n 
D 2 9   SER 9   27  27  SER SER D . n 
D 2 10  ILE 10  28  28  ILE ILE D . n 
D 2 11  SER 11  29  29  SER SER D . n 
D 2 12  LEU 12  30  30  LEU LEU D . n 
D 2 13  SER 13  31  31  SER SER D . n 
D 2 14  LEU 14  32  32  LEU LEU D . n 
D 2 15  ASP 15  33  33  ASP ASP D . n 
D 2 16  SER 16  34  34  SER SER D . n 
D 2 17  PRO 17  35  35  PRO PRO D . n 
D 2 18  LYS 18  36  36  LYS LYS D . n 
D 2 19  LEU 19  37  37  LEU LEU D . n 
D 2 20  ASP 20  38  38  ASP ASP D . n 
D 2 21  GLU 21  39  39  GLU GLU D . n 
D 2 22  SER 22  40  40  SER SER D . n 
D 2 23  ASP 23  41  41  ASP ASP D . n 
D 2 24  PHE 24  42  42  PHE PHE D . n 
D 2 25  ILE 25  43  43  ILE ILE D . n 
D 2 26  LEU 26  44  44  LEU LEU D . n 
D 2 27  LEU 27  45  45  LEU LEU D . n 
D 2 28  SER 28  46  46  SER SER D . n 
D 2 29  VAL 29  47  47  VAL VAL D . n 
D 2 30  LYS 30  48  48  LYS LYS D . n 
D 2 31  TYR 31  49  49  TYR TYR D . n 
D 2 32  LEU 32  50  50  LEU LEU D . n 
D 2 33  GLU 33  51  51  GLU GLU D . n 
D 2 34  LYS 34  52  52  LYS LYS D . n 
D 2 35  SER 35  53  53  SER SER D . n 
D 2 36  LEU 36  54  54  LEU LEU D . n 
D 2 37  GLY 37  55  55  GLY GLY D . n 
D 2 38  LYS 38  56  56  LYS LYS D . n 
D 2 39  LYS 39  57  57  LYS LYS D . n 
D 2 40  LYS 40  58  58  LYS LYS D . n 
D 2 41  GLU 41  59  59  GLU GLU D . n 
D 2 42  PHE 42  60  60  PHE PHE D . n 
D 2 43  SER 43  61  61  SER SER D . n 
D 2 44  GLY 44  62  62  GLY GLY D . n 
D 2 45  PHE 45  63  63  PHE PHE D . n 
D 2 46  PHE 46  64  64  PHE PHE D . n 
D 2 47  GLU 47  65  65  GLU GLU D . n 
D 2 48  ASP 48  66  66  ASP ASP D . n 
D 2 49  ILE 49  67  67  ILE ILE D . n 
D 2 50  GLU 50  68  68  GLU GLU D . n 
D 2 51  LYS 51  69  69  LYS LYS D . n 
D 2 52  LEU 52  70  70  LEU LEU D . n 
D 2 53  TYR 53  71  71  TYR TYR D . n 
D 2 54  PHE 54  72  72  PHE PHE D . n 
D 2 55  LYS 55  73  73  LYS LYS D . n 
D 2 56  GLN 56  74  74  GLN GLN D . n 
D 2 57  ASN 57  75  75  ASN ASN D . n 
D 2 58  TYR 58  76  76  TYR TYR D . n 
D 2 59  LYS 59  77  77  LYS LYS D . n 
D 2 60  GLU 60  78  78  GLU GLU D . n 
D 2 61  ALA 61  79  79  ALA ALA D . n 
D 2 62  ILE 62  80  80  ILE ILE D . n 
D 2 63  GLU 63  81  81  GLU GLU D . n 
D 2 64  LYS 64  82  82  LYS LYS D . n 
D 2 65  ILE 65  83  83  ILE ILE D . n 
D 2 66  LEU 66  84  84  LEU LEU D . n 
D 2 67  ASP 67  85  85  ASP ASP D . n 
D 2 68  PHE 68  86  86  PHE PHE D . n 
D 2 69  CYS 69  87  87  CYS CYS D . n 
D 2 70  LYS 70  88  88  LYS LYS D . n 
D 2 71  LYS 71  89  89  LYS LYS D . n 
D 2 72  ASN 72  90  90  ASN ASN D . n 
D 2 73  GLU 73  91  91  GLU GLU D . n 
D 2 74  SER 74  92  92  SER SER D . n 
D 2 75  LEU 75  93  93  LEU LEU D . n 
D 2 76  LEU 76  94  94  LEU LEU D . n 
D 2 77  SER 77  95  95  SER SER D . n 
D 2 78  GLU 78  96  96  GLU GLU D . n 
D 2 79  GLN 79  97  97  GLN GLN D . n 
D 2 80  VAL 80  98  98  VAL VAL D . n 
D 2 81  VAL 81  99  99  VAL VAL D . n 
D 2 82  GLN 82  100 100 GLN GLN D . n 
D 2 83  ARG 83  101 101 ARG ARG D . n 
D 2 84  LEU 84  102 102 LEU LEU D . n 
D 2 85  ALA 85  103 103 ALA ALA D . n 
D 2 86  GLU 86  104 104 GLU GLU D . n 
D 2 87  VAL 87  105 105 VAL VAL D . n 
D 2 88  ALA 88  106 106 ALA ALA D . n 
D 2 89  PRO 89  107 107 PRO PRO D . n 
D 2 90  ARG 90  108 108 ARG ARG D . n 
D 2 91  LEU 91  109 109 LEU LEU D . n 
D 2 92  LYS 92  110 110 LYS LYS D . n 
D 2 93  SER 93  111 111 SER SER D . n 
D 2 94  ASN 94  112 112 ASN ASN D . n 
D 2 95  PRO 95  113 113 PRO PRO D . n 
D 2 96  LYS 96  114 114 LYS LYS D . n 
D 2 97  ASP 97  115 115 ASP ASP D . n 
D 2 98  ASN 98  116 116 ASN ASN D . n 
D 2 99  GLU 99  117 117 GLU GLU D . n 
D 2 100 SER 100 118 118 SER SER D . n 
D 2 101 ARG 101 119 119 ARG ARG D . n 
D 2 102 ARG 102 120 120 ARG ARG D . n 
D 2 103 LEU 103 121 121 LEU LEU D . n 
D 2 104 TYR 104 122 122 TYR TYR D . n 
D 2 105 GLU 105 123 123 GLU GLU D . n 
D 2 106 THR 106 124 124 THR THR D . n 
D 2 107 LEU 107 125 125 LEU LEU D . n 
D 2 108 TYR 108 126 126 TYR TYR D . n 
D 2 109 ALA 109 127 127 ALA ALA D . n 
D 2 110 ASP 110 128 128 ASP ASP D . n 
D 2 111 HIS 111 129 129 HIS HIS D . n 
D 2 112 LEU 112 130 130 LEU LEU D . n 
D 2 113 GLU 113 131 131 GLU GLU D . n 
D 2 114 SER 114 132 132 SER SER D . n 
D 2 115 VAL 115 133 133 VAL VAL D . n 
D 2 116 ILE 116 134 134 ILE ILE D . n 
D 2 117 LYS 117 135 135 LYS LYS D . n 
D 2 118 GLN 118 136 136 GLN GLN D . n 
D 2 119 GLU 119 137 137 GLU GLU D . n 
D 2 120 SER 120 138 138 SER SER D . n 
D 2 121 ASP 121 139 139 ASP ASP D . n 
D 2 122 LEU 122 140 140 LEU LEU D . n 
D 2 123 SER 123 141 141 SER SER D . n 
D 2 124 VAL 124 142 142 VAL VAL D . n 
D 2 125 PHE 125 143 143 PHE PHE D . n 
D 2 126 ASN 126 144 144 ASN ASN D . n 
D 2 127 GLU 127 145 145 GLU GLU D . n 
D 2 128 LEU 128 146 146 LEU LEU D . n 
D 2 129 ARG 129 147 147 ARG ARG D . n 
D 2 130 ASP 130 148 148 ASP ASP D . n 
D 2 131 SER 131 149 149 SER SER D . n 
D 2 132 TYR 132 150 150 TYR TYR D . n 
D 2 133 ASN 133 151 151 ASN ASN D . n 
D 2 134 ALA 134 152 152 ALA ALA D . n 
D 2 135 VAL 135 153 153 VAL VAL D . n 
D 2 136 LYS 136 154 154 LYS LYS D . n 
D 2 137 PRO 137 155 155 PRO PRO D . n 
D 2 138 GLU 138 156 156 GLU GLU D . n 
D 2 139 TYR 139 157 157 TYR TYR D . n 
D 2 140 ALA 140 158 158 ALA ALA D . n 
D 2 141 VAL 141 159 159 VAL VAL D . n 
D 2 142 THR 142 160 160 THR THR D . n 
D 2 143 HIS 143 161 161 HIS HIS D . n 
D 2 144 GLU 144 162 162 GLU GLU D . n 
D 2 145 THR 145 163 163 THR THR D . n 
D 2 146 GLU 146 164 164 GLU GLU D . n 
D 2 147 ILE 147 165 165 ILE ILE D . n 
D 2 148 LYS 148 166 166 LYS LYS D . n 
D 2 149 THR 149 167 167 THR THR D . n 
D 2 150 LEU 150 168 168 LEU LEU D . n 
D 2 151 ASP 151 169 169 ASP ASP D . n 
D 2 152 GLU 152 170 170 GLU GLU D . n 
D 2 153 ALA 153 171 171 ALA ALA D . n 
D 2 154 LYS 154 172 172 LYS LYS D . n 
D 2 155 GLN 155 173 173 GLN GLN D . n 
D 2 156 PHE 156 174 174 PHE PHE D . n 
D 2 157 ILE 157 175 175 ILE ILE D . n 
D 2 158 LEU 158 176 176 LEU LEU D . n 
D 2 159 SER 159 177 177 SER SER D . n 
D 2 160 PHE 160 178 178 PHE PHE D . n 
D 2 161 VAL 161 179 179 VAL VAL D . n 
D 2 162 MET 162 180 180 MET MET D . n 
D 2 163 LEU 163 181 181 LEU LEU D . n 
D 2 164 ASN 164 182 182 ASN ASN D . n 
D 2 165 ASP 165 183 183 ASP ASP D . n 
D 2 166 ASN 166 184 184 ASN ASN D . n 
D 2 167 VAL 167 185 185 VAL VAL D . n 
D 2 168 GLU 168 186 186 GLU GLU D . n 
D 2 169 LEU 169 187 187 LEU LEU D . n 
D 2 170 PRO 170 188 188 PRO PRO D . n 
D 2 171 LEU 171 189 189 LEU LEU D . n 
D 2 172 LYS 172 190 190 LYS LYS D . n 
D 2 173 ALA 173 191 191 ALA ALA D . n 
D 2 174 GLN 174 192 192 GLN GLN D . n 
D 2 175 SER 175 193 193 SER SER D . n 
D 2 176 GLU 176 194 194 GLU GLU D . n 
D 2 177 ARG 177 195 195 ARG ARG D . n 
D 2 178 TYR 178 196 196 TYR TYR D . n 
D 2 179 PRO 179 197 197 PRO PRO D . n 
D 2 180 LYS 180 198 198 LYS LYS D . n 
D 2 181 LYS 181 199 199 LYS LYS D . n 
D 2 182 ASP 182 200 200 ASP ASP D . n 
D 2 183 ARG 183 201 201 ARG ARG D . n 
D 2 184 SER 184 202 202 SER SER D . n 
D 2 185 ARG 185 203 203 ARG ARG D . n 
D 2 186 GLU 186 204 204 GLU GLU D . n 
D 2 187 GLU 187 205 205 GLU GLU D . n 
D 2 188 LEU 188 206 206 LEU LEU D . n 
D 2 189 GLY 189 207 207 GLY GLY D . n 
D 2 190 ASN 190 208 208 ASN ASN D . n 
D 2 191 THR 191 209 209 THR THR D . n 
D 2 192 PRO 192 210 210 PRO PRO D . n 
D 2 193 SER 193 211 211 SER SER D . n 
D 2 194 ALA 194 212 212 ALA ALA D . n 
D 2 195 ASN 195 213 213 ASN ASN D . n 
D 2 196 PRO 196 214 214 PRO PRO D . n 
D 2 197 GLY 197 215 215 GLY GLY D . n 
D 2 198 ILE 198 216 216 ILE ILE D . n 
D 2 199 MET 199 217 217 MET MET D . n 
D 2 200 LYS 200 218 218 LYS LYS D . n 
D 2 201 PRO 201 219 219 PRO PRO D . n 
D 2 202 ASN 202 220 220 ASN ASN D . n 
D 2 203 SER 203 221 221 SER SER D . n 
D 2 204 PRO 204 222 222 PRO PRO D . n 
D 2 205 ASN 205 223 223 ASN ASN D . n 
D 2 206 PHE 206 224 224 PHE PHE D . n 
D 2 207 THR 207 225 225 THR THR D . n 
D 2 208 ASP 208 226 226 ASP ASP D . n 
D 2 209 ASN 209 227 227 ASN ASN D . n 
D 2 210 LEU 210 228 228 LEU LEU D . n 
D 2 211 VAL 211 229 229 VAL VAL D . n 
D 2 212 PRO 212 230 230 PRO PRO D . n 
D 2 213 VAL 213 231 231 VAL VAL D . n 
D 2 214 ARG 214 232 232 ARG ARG D . n 
D 2 215 ASP 215 233 233 ASP ASP D . n 
D 2 216 VAL 216 234 234 VAL VAL D . n 
D 2 217 PRO 217 235 235 PRO PRO D . n 
D 2 218 LYS 218 236 236 LYS LYS D . n 
D 2 219 ILE 219 237 237 ILE ILE D . n 
D 2 220 ALA 220 238 238 ALA ALA D . n 
D 2 221 ILE 221 239 239 ILE ILE D . n 
D 2 222 ASN 222 240 240 ASN ASN D . n 
D 2 223 GLU 223 241 241 GLU GLU D . n 
D 2 224 LYS 224 242 242 LYS LYS D . n 
D 2 225 VAL 225 243 243 VAL VAL D . n 
D 2 226 ALA 226 244 244 ALA ALA D . n 
D 2 227 GLY 227 245 245 GLY GLY D . n 
D 2 228 GLY 228 246 246 GLY GLY D . n 
D 2 229 TYR 229 247 247 TYR TYR D . n 
D 2 230 SER 230 248 248 SER SER D . n 
D 2 231 LYS 231 249 249 LYS LYS D . n 
D 2 232 THR 232 250 250 THR THR D . n 
D 2 233 LYS 233 251 251 LYS LYS D . n 
D 2 234 PRO 234 252 252 PRO PRO D . n 
D 2 235 THR 235 253 253 THR THR D . n 
D 2 236 THR 236 254 254 THR THR D . n 
D 2 237 PRO 237 255 255 PRO PRO D . n 
D 2 238 PHE 238 256 256 PHE PHE D . n 
D 2 239 VAL 239 257 257 VAL VAL D . n 
D 2 240 ALA 240 258 258 ALA ALA D . n 
D 2 241 SER 241 259 259 SER SER D . n 
D 2 242 LEU 242 260 260 LEU LEU D . n 
D 2 243 SER 243 261 261 SER SER D . n 
D 2 244 GLY 244 262 262 GLY GLY D . n 
D 2 245 THR 245 263 263 THR THR D . n 
D 2 246 THR 246 264 264 THR THR D . n 
D 2 247 TYR 247 265 265 TYR TYR D . n 
D 2 248 SER 248 266 266 SER SER D . n 
D 2 249 LEU 249 267 267 LEU LEU D . n 
D 2 250 MET 250 268 268 MET MET D . n 
D 2 251 VAL 251 269 269 VAL VAL D . n 
D 2 252 VAL 252 270 270 VAL VAL D . n 
D 2 253 LEU 253 271 271 LEU LEU D . n 
D 2 254 THR 254 272 272 THR THR D . n 
D 2 255 ASP 255 273 273 ASP ASP D . n 
D 2 256 TYR 256 274 274 TYR TYR D . n 
D 2 257 ILE 257 275 275 ILE ILE D . n 
D 2 258 GLU 258 276 276 GLU GLU D . n 
D 2 259 LYS 259 277 277 LYS LYS D . n 
D 2 260 HIS 260 278 278 HIS HIS D . n 
D 2 261 LYS 261 279 279 LYS LYS D . n 
D 2 262 THR 262 280 280 THR THR D . n 
D 2 263 ASP 263 281 281 ASP ASP D . n 
D 2 264 LYS 264 282 282 LYS LYS D . n 
D 2 265 ASP 265 283 283 ASP ASP D . n 
D 2 266 ILE 266 284 284 ILE ILE D . n 
D 2 267 GLU 267 285 285 GLU GLU D . n 
D 2 268 LYS 268 286 286 LYS LYS D . n 
D 2 269 LYS 269 287 287 LYS LYS D . n 
D 2 270 VAL 270 288 288 VAL VAL D . n 
D 2 271 ASN 271 289 289 ASN ASN D . n 
D 2 272 GLN 272 290 290 GLN GLN D . n 
D 2 273 ILE 273 291 291 ILE ILE D . n 
D 2 274 ILE 274 292 292 ILE ILE D . n 
D 2 275 ASN 275 293 293 ASN ASN D . n 
D 2 276 LEU 276 294 294 LEU LEU D . n 
D 2 277 TRP 277 295 295 TRP TRP D . n 
D 2 278 ILE 278 296 296 ILE ILE D . n 
D 2 279 SER 279 297 297 SER SER D . n 
D 2 280 SER 280 298 298 SER SER D . n 
D 2 281 TYR 281 299 299 TYR TYR D . n 
D 2 282 ILE 282 300 300 ILE ILE D . n 
D 2 283 LYS 283 301 301 LYS LYS D . n 
D 2 284 GLU 284 302 302 GLU GLU D . n 
D 2 285 GLY 285 303 303 GLY GLY D . n 
D 2 286 TYR 286 304 304 TYR TYR D . n 
D 2 287 HIS 287 305 305 HIS HIS D . n 
D 2 288 SER 288 306 306 SER SER D . n 
D 2 289 TYR 289 307 307 TYR TYR D . n 
D 2 290 SER 290 308 308 SER SER D . n 
D 2 291 GLU 291 309 309 GLU GLU D . n 
D 2 292 VAL 292 310 310 VAL VAL D . n 
D 2 293 VAL 293 311 311 VAL VAL D . n 
D 2 294 ASP 294 312 312 ASP ASP D . n 
D 2 295 VAL 295 313 313 VAL VAL D . n 
D 2 296 LEU 296 314 314 LEU LEU D . n 
D 2 297 THR 297 315 315 THR THR D . n 
D 2 298 GLU 298 316 316 GLU GLU D . n 
D 2 299 PRO 299 317 317 PRO PRO D . n 
D 2 300 PHE 300 318 318 PHE PHE D . n 
D 2 301 LEU 301 319 319 LEU LEU D . n 
D 2 302 GLN 302 320 320 GLN GLN D . n 
D 2 303 SER 303 321 321 SER SER D . n 
D 2 304 ILE 304 322 322 ILE ILE D . n 
D 2 305 PHE 305 323 323 PHE PHE D . n 
D 2 306 ASP 306 324 324 ASP ASP D . n 
D 2 307 LYS 307 325 325 LYS LYS D . n 
D 2 308 ALA 308 326 326 ALA ALA D . n 
D 2 309 ASN 309 327 327 ASN ASN D . n 
D 2 310 ILE 310 328 328 ILE ILE D . n 
D 2 311 LYS 311 329 329 LYS LYS D . n 
D 2 312 LEU 312 330 330 LEU LEU D . n 
D 2 313 ASN 313 331 331 ASN ASN D . n 
D 2 314 TYR 314 332 332 TYR TYR D . n 
D 2 315 GLY 315 333 333 GLY GLY D . n 
D 2 316 VAL 316 334 334 VAL VAL D . n 
D 2 317 LEU 317 335 335 LEU LEU D . n 
D 2 318 ASP 318 336 336 ASP ASP D . n 
D 2 319 ASP 319 337 337 ASP ASP D . n 
D 2 320 THR 320 338 338 THR THR D . n 
D 2 321 HIS 321 339 339 HIS HIS D . n 
D 2 322 ALA 322 340 340 ALA ALA D . n 
D 2 323 GLU 323 341 341 GLU GLU D . n 
D 2 324 PHE 324 342 342 PHE PHE D . n 
D 2 325 ARG 325 343 343 ARG ARG D . n 
D 2 326 LYS 326 344 344 LYS LYS D . n 
D 2 327 ALA 327 345 345 ALA ALA D . n 
D 2 328 GLN 328 346 346 GLN GLN D . n 
D 2 329 ASP 329 347 347 ASP ASP D . n 
D 2 330 TYR 330 348 348 TYR TYR D . n 
D 2 331 VAL 331 349 349 VAL VAL D . n 
D 2 332 PHE 332 350 350 PHE PHE D . n 
D 2 333 GLY 333 351 351 GLY GLY D . n 
D 2 334 LEU 334 352 352 LEU LEU D . n 
D 2 335 THR 335 353 353 THR THR D . n 
D 2 336 ILE 336 354 354 ILE ILE D . n 
D 2 337 GLN 337 355 355 GLN GLN D . n 
D 2 338 SER 338 356 356 SER SER D . n 
D 2 339 ALA 339 357 357 ALA ALA D . n 
D 2 340 MET 340 358 358 MET MET D . n 
D 2 341 HIS 341 359 359 HIS HIS D . n 
D 2 342 HIS 342 360 360 HIS HIS D . n 
D 2 343 GLU 343 361 361 GLU GLU D . n 
D 2 344 LEU 344 362 362 LEU LEU D . n 
D 2 345 GLN 345 363 363 GLN GLN D . n 
D 2 346 GLU 346 364 364 GLU GLU D . n 
D 2 347 ARG 347 365 365 ARG ARG D . n 
D 2 348 PHE 348 366 366 PHE PHE D . n 
D 2 349 LYS 349 367 367 LYS LYS D . n 
D 2 350 ASN 350 368 368 ASN ASN D . n 
D 2 351 LYS 351 369 369 LYS LYS D . n 
D 2 352 GLU 352 370 370 GLU GLU D . n 
E 3 1   MET 1   1   1   MET MET E . n 
E 3 2   GLN 2   2   2   GLN GLN E . n 
E 3 3   ILE 3   3   3   ILE ILE E . n 
E 3 4   PHE 4   4   4   PHE PHE E . n 
E 3 5   VAL 5   5   5   VAL VAL E . n 
E 3 6   LYS 6   6   6   LYS LYS E . n 
E 3 7   THR 7   7   7   THR THR E . n 
E 3 8   LEU 8   8   8   LEU LEU E . n 
E 3 9   THR 9   9   9   THR THR E . n 
E 3 10  GLY 10  10  10  GLY GLY E . n 
E 3 11  LYS 11  11  11  LYS LYS E . n 
E 3 12  THR 12  12  12  THR THR E . n 
E 3 13  ILE 13  13  13  ILE ILE E . n 
E 3 14  THR 14  14  14  THR THR E . n 
E 3 15  LEU 15  15  15  LEU LEU E . n 
E 3 16  GLU 16  16  16  GLU GLU E . n 
E 3 17  VAL 17  17  17  VAL VAL E . n 
E 3 18  GLU 18  18  18  GLU GLU E . n 
E 3 19  PRO 19  19  19  PRO PRO E . n 
E 3 20  SER 20  20  20  SER SER E . n 
E 3 21  ASP 21  21  21  ASP ASP E . n 
E 3 22  THR 22  22  22  THR THR E . n 
E 3 23  ILE 23  23  23  ILE ILE E . n 
E 3 24  GLU 24  24  24  GLU GLU E . n 
E 3 25  ASN 25  25  25  ASN ASN E . n 
E 3 26  VAL 26  26  26  VAL VAL E . n 
E 3 27  LYS 27  27  27  LYS LYS E . n 
E 3 28  ALA 28  28  28  ALA ALA E . n 
E 3 29  LYS 29  29  29  LYS LYS E . n 
E 3 30  ILE 30  30  30  ILE ILE E . n 
E 3 31  GLN 31  31  31  GLN GLN E . n 
E 3 32  ASP 32  32  32  ASP ASP E . n 
E 3 33  LYS 33  33  33  LYS LYS E . n 
E 3 34  GLU 34  34  34  GLU GLU E . n 
E 3 35  GLY 35  35  35  GLY GLY E . n 
E 3 36  ILE 36  36  36  ILE ILE E . n 
E 3 37  PRO 37  37  37  PRO PRO E . n 
E 3 38  PRO 38  38  38  PRO PRO E . n 
E 3 39  ASP 39  39  39  ASP ASP E . n 
E 3 40  GLN 40  40  40  GLN GLN E . n 
E 3 41  GLN 41  41  41  GLN GLN E . n 
E 3 42  ARG 42  42  42  ARG ARG E . n 
E 3 43  LEU 43  43  43  LEU LEU E . n 
E 3 44  ILE 44  44  44  ILE ILE E . n 
E 3 45  PHE 45  45  45  PHE PHE E . n 
E 3 46  ALA 46  46  46  ALA ALA E . n 
E 3 47  GLY 47  47  47  GLY GLY E . n 
E 3 48  LYS 48  48  48  LYS LYS E . n 
E 3 49  GLN 49  49  49  GLN GLN E . n 
E 3 50  LEU 50  50  50  LEU LEU E . n 
E 3 51  GLU 51  51  51  GLU GLU E . n 
E 3 52  ASP 52  52  52  ASP ASP E . n 
E 3 53  GLY 53  53  53  GLY GLY E . n 
E 3 54  ARG 54  54  54  ARG ARG E . n 
E 3 55  THR 55  55  55  THR THR E . n 
E 3 56  LEU 56  56  56  LEU LEU E . n 
E 3 57  SER 57  57  57  SER SER E . n 
E 3 58  ASP 58  58  58  ASP ASP E . n 
E 3 59  TYR 59  59  59  TYR TYR E . n 
E 3 60  ASN 60  60  60  ASN ASN E . n 
E 3 61  ILE 61  61  61  ILE ILE E . n 
E 3 62  GLN 62  62  62  GLN GLN E . n 
E 3 63  LYS 63  63  63  LYS LYS E . n 
E 3 64  GLU 64  64  64  GLU GLU E . n 
E 3 65  SER 65  65  65  SER SER E . n 
E 3 66  THR 66  66  66  THR THR E . n 
E 3 67  LEU 67  67  67  LEU LEU E . n 
E 3 68  HIS 68  68  68  HIS HIS E . n 
E 3 69  LEU 69  69  69  LEU LEU E . n 
E 3 70  VAL 70  70  70  VAL VAL E . n 
E 3 71  LEU 71  71  71  LEU LEU E . n 
E 3 72  ARG 72  72  72  ARG ARG E . n 
E 3 73  LEU 73  73  73  LEU LEU E . n 
E 3 74  ARG 74  74  74  ARG ARG E . n 
E 3 75  GLY 75  75  75  GLY GLY E . n 
E 3 76  GLY 76  76  76  GLY GLY E . n 
F 3 1   MET 1   1   1   MET MET F . n 
F 3 2   GLN 2   2   2   GLN GLN F . n 
F 3 3   ILE 3   3   3   ILE ILE F . n 
F 3 4   PHE 4   4   4   PHE PHE F . n 
F 3 5   VAL 5   5   5   VAL VAL F . n 
F 3 6   LYS 6   6   6   LYS LYS F . n 
F 3 7   THR 7   7   7   THR THR F . n 
F 3 8   LEU 8   8   8   LEU LEU F . n 
F 3 9   THR 9   9   9   THR THR F . n 
F 3 10  GLY 10  10  10  GLY GLY F . n 
F 3 11  LYS 11  11  11  LYS LYS F . n 
F 3 12  THR 12  12  12  THR THR F . n 
F 3 13  ILE 13  13  13  ILE ILE F . n 
F 3 14  THR 14  14  14  THR THR F . n 
F 3 15  LEU 15  15  15  LEU LEU F . n 
F 3 16  GLU 16  16  16  GLU GLU F . n 
F 3 17  VAL 17  17  17  VAL VAL F . n 
F 3 18  GLU 18  18  18  GLU GLU F . n 
F 3 19  PRO 19  19  19  PRO PRO F . n 
F 3 20  SER 20  20  20  SER SER F . n 
F 3 21  ASP 21  21  21  ASP ASP F . n 
F 3 22  THR 22  22  22  THR THR F . n 
F 3 23  ILE 23  23  23  ILE ILE F . n 
F 3 24  GLU 24  24  24  GLU GLU F . n 
F 3 25  ASN 25  25  25  ASN ASN F . n 
F 3 26  VAL 26  26  26  VAL VAL F . n 
F 3 27  LYS 27  27  27  LYS LYS F . n 
F 3 28  ALA 28  28  28  ALA ALA F . n 
F 3 29  LYS 29  29  29  LYS LYS F . n 
F 3 30  ILE 30  30  30  ILE ILE F . n 
F 3 31  GLN 31  31  31  GLN GLN F . n 
F 3 32  ASP 32  32  32  ASP ASP F . n 
F 3 33  LYS 33  33  33  LYS LYS F . n 
F 3 34  GLU 34  34  34  GLU GLU F . n 
F 3 35  GLY 35  35  35  GLY GLY F . n 
F 3 36  ILE 36  36  36  ILE ILE F . n 
F 3 37  PRO 37  37  37  PRO PRO F . n 
F 3 38  PRO 38  38  38  PRO PRO F . n 
F 3 39  ASP 39  39  39  ASP ASP F . n 
F 3 40  GLN 40  40  40  GLN GLN F . n 
F 3 41  GLN 41  41  41  GLN GLN F . n 
F 3 42  ARG 42  42  42  ARG ARG F . n 
F 3 43  LEU 43  43  43  LEU LEU F . n 
F 3 44  ILE 44  44  44  ILE ILE F . n 
F 3 45  PHE 45  45  45  PHE PHE F . n 
F 3 46  ALA 46  46  46  ALA ALA F . n 
F 3 47  GLY 47  47  47  GLY GLY F . n 
F 3 48  LYS 48  48  48  LYS LYS F . n 
F 3 49  GLN 49  49  49  GLN GLN F . n 
F 3 50  LEU 50  50  50  LEU LEU F . n 
F 3 51  GLU 51  51  51  GLU GLU F . n 
F 3 52  ASP 52  52  52  ASP ASP F . n 
F 3 53  GLY 53  53  53  GLY GLY F . n 
F 3 54  ARG 54  54  54  ARG ARG F . n 
F 3 55  THR 55  55  55  THR THR F . n 
F 3 56  LEU 56  56  56  LEU LEU F . n 
F 3 57  SER 57  57  57  SER SER F . n 
F 3 58  ASP 58  58  58  ASP ASP F . n 
F 3 59  TYR 59  59  59  TYR TYR F . n 
F 3 60  ASN 60  60  60  ASN ASN F . n 
F 3 61  ILE 61  61  61  ILE ILE F . n 
F 3 62  GLN 62  62  62  GLN GLN F . n 
F 3 63  LYS 63  63  63  LYS LYS F . n 
F 3 64  GLU 64  64  64  GLU GLU F . n 
F 3 65  SER 65  65  65  SER SER F . n 
F 3 66  THR 66  66  66  THR THR F . n 
F 3 67  LEU 67  67  67  LEU LEU F . n 
F 3 68  HIS 68  68  68  HIS HIS F . n 
F 3 69  LEU 69  69  69  LEU LEU F . n 
F 3 70  VAL 70  70  70  VAL VAL F . n 
F 3 71  LEU 71  71  71  LEU LEU F . n 
F 3 72  ARG 72  72  72  ARG ARG F . n 
F 3 73  LEU 73  73  73  LEU LEU F . n 
F 3 74  ARG 74  74  74  ARG ARG F . n 
F 3 75  GLY 75  75  75  GLY GLY F . n 
F 3 76  GLY 76  76  76  GLY GLY F . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 AR6 ? ? AR6 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 4 ATP 1 401 402 ATP ATP A . 
H 4 ATP 1 401 402 ATP ATP B . 
I 5 AR6 1 401 401 AR6 AR6 D . 
# 
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 N 1 D AR6 401 ? N1    ? I AR6 1 N1    
2  1 N 1 D AR6 401 ? C2    ? I AR6 1 C2    
3  1 N 1 D AR6 401 ? N3    ? I AR6 1 N3    
4  1 N 1 D AR6 401 ? C4    ? I AR6 1 C4    
5  1 N 1 D AR6 401 ? C5    ? I AR6 1 C5    
6  1 N 1 D AR6 401 ? C6    ? I AR6 1 C6    
7  1 N 1 D AR6 401 ? N6    ? I AR6 1 N6    
8  1 N 1 D AR6 401 ? N7    ? I AR6 1 N7    
9  1 N 1 D AR6 401 ? C8    ? I AR6 1 C8    
10 1 N 1 D AR6 401 ? N9    ? I AR6 1 N9    
11 1 N 1 D AR6 401 ? PA    ? I AR6 1 PA    
12 1 N 1 D AR6 401 ? "C1'" ? I AR6 1 "C1'" 
13 1 N 1 D AR6 401 ? O1A   ? I AR6 1 O1A   
14 1 N 1 D AR6 401 ? "C2'" ? I AR6 1 "C2'" 
15 1 N 1 D AR6 401 ? "O2'" ? I AR6 1 "O2'" 
16 1 N 1 D AR6 401 ? O2A   ? I AR6 1 O2A   
17 1 N 1 D AR6 401 ? "C3'" ? I AR6 1 "C3'" 
18 1 N 1 D AR6 401 ? "O3'" ? I AR6 1 "O3'" 
19 1 N 1 D AR6 401 ? "C4'" ? I AR6 1 "C4'" 
20 1 N 1 D AR6 401 ? "O4'" ? I AR6 1 "O4'" 
21 1 N 1 D AR6 401 ? "C5'" ? I AR6 1 "C5'" 
22 1 N 1 D AR6 401 ? "O5'" ? I AR6 1 "O5'" 
# 
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   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.30 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8K6F 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.690 
_cell.length_a_esd                 ? 
_cell.length_b                     214.227 
_cell.length_b_esd                 ? 
_cell.length_c                     79.563 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8K6F 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   8K6F 
_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             2.56 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.95 
_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          EVAPORATION 
_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    'PEG8000, Sodium Choride, Sodium HEPES' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-02 
_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   0.978565 
_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 BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978565 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8K6F 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.41 
_reflns.d_resolution_low                               37.29 
_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                                     24455 
_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                           97 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.54 
_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                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.961 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1299 
_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                                    3.41 
_reflns_shell.d_res_low                                     3.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1967 
_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                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.678 
_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                                  ? 
_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                                 8K6F 
_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                            3.41 
_refine.ls_d_res_low                             37.29 
_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                     24054 
_refine.ls_number_reflns_R_free                  1967 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.98 
_refine.ls_percent_reflns_R_free                 8.18 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2236 
_refine.ls_R_factor_R_free                       0.2434 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2218 
_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                          0.14 
_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       ML 
_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             1.10 
_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                 25.82 
_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                            0.32 
_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        12627 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         76 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               12703 
_refine_hist.d_res_high                       3.41 
_refine_hist.d_res_low                        37.29 
# 
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' ? 0.017  ? 12955 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.881  ? 17523 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.823 ? 4901  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.117  ? 1963  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 2242  ? 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' 3.41 3.50  . . 137 1535 96.00 . . . . 0.2771 . . . . . . . . . . . 0.2965 
'X-RAY DIFFRACTION' 3.50 3.59  . . 137 1595 97.00 . . . . 0.2624 . . . . . . . . . . . 0.2779 
'X-RAY DIFFRACTION' 3.59 3.70  . . 143 1570 96.00 . . . . 0.2547 . . . . . . . . . . . 0.2928 
'X-RAY DIFFRACTION' 3.70 3.82  . . 139 1546 97.00 . . . . 0.2449 . . . . . . . . . . . 0.2734 
'X-RAY DIFFRACTION' 3.82 3.95  . . 148 1597 97.00 . . . . 0.2347 . . . . . . . . . . . 0.2700 
'X-RAY DIFFRACTION' 3.96 4.11  . . 134 1569 98.00 . . . . 0.2225 . . . . . . . . . . . 0.2391 
'X-RAY DIFFRACTION' 4.11 4.30  . . 139 1578 97.00 . . . . 0.2153 . . . . . . . . . . . 0.2655 
'X-RAY DIFFRACTION' 4.30 4.53  . . 138 1600 97.00 . . . . 0.1947 . . . . . . . . . . . 0.2288 
'X-RAY DIFFRACTION' 4.53 4.81  . . 143 1562 97.00 . . . . 0.2007 . . . . . . . . . . . 0.2630 
'X-RAY DIFFRACTION' 4.81 5.18  . . 137 1568 97.00 . . . . 0.2045 . . . . . . . . . . . 0.1971 
'X-RAY DIFFRACTION' 5.18 5.70  . . 143 1602 97.00 . . . . 0.2401 . . . . . . . . . . . 0.2600 
'X-RAY DIFFRACTION' 5.70 6.52  . . 140 1606 98.00 . . . . 0.2419 . . . . . . . . . . . 0.2272 
'X-RAY DIFFRACTION' 6.52 8.20  . . 142 1585 98.00 . . . . 0.2259 . . . . . . . . . . . 0.2019 
'X-RAY DIFFRACTION' 8.20 37.29 . . 147 1574 96.00 . . . . 0.1791 . . . . . . . . . . . 0.2008 
# 
_struct.entry_id                     8K6F 
_struct.title                        'LnaB-Actin-PRUb ternary complex' 
_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        8K6F 
_struct_keywords.text            'AMPylation, Legionella effector, TOXIN' 
_struct_keywords.pdbx_keywords   TOXIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
# 
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 A0A8C6VAB1_NAJNA A0A8C6VAB1 ? 1 
;MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD
DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT
HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL
APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
;
1 
2 PDB 8K6F             8K6F       ? 2 ? 1 
3 UNP UBB_HUMAN        P0CG47     ? 3 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 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 8K6F A 1 ? 375 ? A0A8C6VAB1 1  ? 375 ? 1  375 
2 1 8K6F B 1 ? 375 ? A0A8C6VAB1 1  ? 375 ? 1  375 
3 2 8K6F C 1 ? 352 ? 8K6F       19 ? 370 ? 19 370 
4 2 8K6F D 1 ? 352 ? 8K6F       19 ? 370 ? 19 370 
5 3 8K6F E 1 ? 76  ? P0CG47     1  ? 76  ? 1  76  
6 3 8K6F F 1 ? 76  ? P0CG47     1  ? 76  ? 1  76  
# 
_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 
# 
_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 GLY A 55  ? LYS A 61  ? GLY A 55  LYS A 61  1 ? 7  
HELX_P HELX_P2  AA2 ILE A 71  ? ILE A 75  ? ILE A 71  ILE A 75  5 ? 5  
HELX_P HELX_P3  AA3 ASN A 78  ? TYR A 91  ? ASN A 78  TYR A 91  1 ? 14 
HELX_P HELX_P4  AA4 ALA A 97  ? HIS A 101 ? ALA A 97  HIS A 101 5 ? 5  
HELX_P HELX_P5  AA5 PRO A 112 ? PHE A 127 ? PRO A 112 PHE A 127 1 ? 16 
HELX_P HELX_P6  AA6 GLN A 137 ? GLY A 146 ? GLN A 137 GLY A 146 1 ? 10 
HELX_P HELX_P7  AA7 ALA A 181 ? ARG A 196 ? ALA A 181 ARG A 196 1 ? 16 
HELX_P HELX_P8  AA8 THR A 202 ? LYS A 215 ? THR A 202 LYS A 215 1 ? 14 
HELX_P HELX_P9  AA9 ASP A 222 ? SER A 233 ? ASP A 222 SER A 233 1 ? 12 
HELX_P HELX_P10 AB1 ASN A 252 ? GLN A 263 ? ASN A 252 GLN A 263 1 ? 12 
HELX_P HELX_P11 AB2 PRO A 264 ? GLY A 268 ? PRO A 264 GLY A 268 5 ? 5  
HELX_P HELX_P12 AB3 GLY A 273 ? MET A 283 ? GLY A 273 MET A 283 1 ? 11 
HELX_P HELX_P13 AB4 ASP A 286 ? ALA A 295 ? ASP A 286 ALA A 295 1 ? 10 
HELX_P HELX_P14 AB5 GLY A 308 ? LEU A 320 ? GLY A 308 LEU A 320 1 ? 13 
HELX_P HELX_P15 AB6 TYR A 337 ? SER A 348 ? TYR A 337 SER A 348 1 ? 12 
HELX_P HELX_P16 AB7 SER A 350 ? GLN A 354 ? SER A 350 GLN A 354 5 ? 5  
HELX_P HELX_P17 AB8 LYS A 359 ? GLY A 366 ? LYS A 359 GLY A 366 1 ? 8  
HELX_P HELX_P18 AB9 SER A 368 ? CYS A 374 ? SER A 368 CYS A 374 1 ? 7  
HELX_P HELX_P19 AC1 GLY B 42  ? GLY B 46  ? GLY B 42  GLY B 46  5 ? 5  
HELX_P HELX_P20 AC2 GLY B 55  ? LYS B 61  ? GLY B 55  LYS B 61  1 ? 7  
HELX_P HELX_P21 AC3 TRP B 79  ? TYR B 91  ? TRP B 79  TYR B 91  1 ? 13 
HELX_P HELX_P22 AC4 ALA B 97  ? HIS B 101 ? ALA B 97  HIS B 101 5 ? 5  
HELX_P HELX_P23 AC5 PRO B 112 ? ASN B 128 ? PRO B 112 ASN B 128 1 ? 17 
HELX_P HELX_P24 AC6 GLN B 137 ? GLY B 146 ? GLN B 137 GLY B 146 1 ? 10 
HELX_P HELX_P25 AC7 ALA B 181 ? GLU B 195 ? ALA B 181 GLU B 195 1 ? 15 
HELX_P HELX_P26 AC8 THR B 202 ? CYS B 217 ? THR B 202 CYS B 217 1 ? 16 
HELX_P HELX_P27 AC9 ASP B 222 ? SER B 233 ? ASP B 222 SER B 233 1 ? 12 
HELX_P HELX_P28 AD1 ASN B 252 ? ALA B 260 ? ASN B 252 ALA B 260 1 ? 9  
HELX_P HELX_P29 AD2 LEU B 261 ? PHE B 262 ? LEU B 261 PHE B 262 5 ? 2  
HELX_P HELX_P30 AD3 GLN B 263 ? GLY B 268 ? GLN B 263 GLY B 268 5 ? 6  
HELX_P HELX_P31 AD4 GLY B 273 ? MET B 283 ? GLY B 273 MET B 283 1 ? 11 
HELX_P HELX_P32 AD5 ASP B 286 ? ALA B 295 ? ASP B 286 ALA B 295 1 ? 10 
HELX_P HELX_P33 AD6 GLY B 308 ? THR B 318 ? GLY B 308 THR B 318 1 ? 11 
HELX_P HELX_P34 AD7 GLU B 334 ? LYS B 336 ? GLU B 334 LYS B 336 5 ? 3  
HELX_P HELX_P35 AD8 TYR B 337 ? LEU B 349 ? TYR B 337 LEU B 349 1 ? 13 
HELX_P HELX_P36 AD9 SER B 350 ? MET B 355 ? SER B 350 MET B 355 5 ? 6  
HELX_P HELX_P37 AE1 LYS B 359 ? GLY B 366 ? LYS B 359 GLY B 366 1 ? 8  
HELX_P HELX_P38 AE2 SER B 368 ? CYS B 374 ? SER B 368 CYS B 374 1 ? 7  
HELX_P HELX_P39 AE3 LEU C 8   ? ASP C 15  ? LEU C 26  ASP C 33  1 ? 8  
HELX_P HELX_P40 AE4 ASP C 20  ? GLY C 37  ? ASP C 38  GLY C 55  1 ? 18 
HELX_P HELX_P41 AE5 PHE C 42  ? LYS C 55  ? PHE C 60  LYS C 73  1 ? 14 
HELX_P HELX_P42 AE6 ASN C 57  ? ASN C 72  ? ASN C 75  ASN C 90  1 ? 16 
HELX_P HELX_P43 AE7 GLU C 73  ? LEU C 76  ? GLU C 91  LEU C 94  5 ? 4  
HELX_P HELX_P44 AE8 SER C 77  ? ALA C 88  ? SER C 95  ALA C 106 1 ? 12 
HELX_P HELX_P45 AE9 PRO C 89  ? LEU C 91  ? PRO C 107 LEU C 109 5 ? 3  
HELX_P HELX_P46 AF1 ASN C 94  ? ASP C 97  ? ASN C 112 ASP C 115 5 ? 4  
HELX_P HELX_P47 AF2 ASN C 98  ? SER C 120 ? ASN C 116 SER C 138 1 ? 23 
HELX_P HELX_P48 AF3 LEU C 122 ? LYS C 136 ? LEU C 140 LYS C 154 1 ? 15 
HELX_P HELX_P49 AF4 THR C 149 ? LEU C 158 ? THR C 167 LEU C 176 1 ? 10 
HELX_P HELX_P50 AF5 SER C 159 ? ASN C 164 ? SER C 177 ASN C 182 5 ? 6  
HELX_P HELX_P51 AF6 GLU C 168 ? ALA C 173 ? GLU C 186 ALA C 191 1 ? 6  
HELX_P HELX_P52 AF7 ARG C 177 ? LYS C 181 ? ARG C 195 LYS C 199 5 ? 5  
HELX_P HELX_P53 AF8 GLY C 228 ? LYS C 233 ? GLY C 246 LYS C 251 1 ? 6  
HELX_P HELX_P54 AF9 GLY C 244 ? HIS C 260 ? GLY C 262 HIS C 278 1 ? 17 
HELX_P HELX_P55 AG1 ASP C 265 ? GLY C 285 ? ASP C 283 GLY C 303 1 ? 21 
HELX_P HELX_P56 AG2 SER C 288 ? THR C 297 ? SER C 306 THR C 315 1 ? 10 
HELX_P HELX_P57 AG3 GLU C 298 ? ALA C 308 ? GLU C 316 ALA C 326 1 ? 11 
HELX_P HELX_P58 AG4 THR C 320 ? GLU C 352 ? THR C 338 GLU C 370 1 ? 33 
HELX_P HELX_P59 AG5 ILE D 6   ? SER D 16  ? ILE D 24  SER D 34  1 ? 11 
HELX_P HELX_P60 AG6 ASP D 20  ? GLY D 37  ? ASP D 38  GLY D 55  1 ? 18 
HELX_P HELX_P61 AG7 PHE D 42  ? TYR D 53  ? PHE D 60  TYR D 71  1 ? 12 
HELX_P HELX_P62 AG8 ASN D 57  ? ASN D 72  ? ASN D 75  ASN D 90  1 ? 16 
HELX_P HELX_P63 AG9 SER D 77  ? ALA D 88  ? SER D 95  ALA D 106 1 ? 12 
HELX_P HELX_P64 AH1 PRO D 89  ? LEU D 91  ? PRO D 107 LEU D 109 5 ? 3  
HELX_P HELX_P65 AH2 ASN D 94  ? ASP D 97  ? ASN D 112 ASP D 115 5 ? 4  
HELX_P HELX_P66 AH3 ASN D 98  ? SER D 120 ? ASN D 116 SER D 138 1 ? 23 
HELX_P HELX_P67 AH4 LEU D 122 ? LYS D 136 ? LEU D 140 LYS D 154 1 ? 15 
HELX_P HELX_P68 AH5 LEU D 150 ? LEU D 158 ? LEU D 168 LEU D 176 1 ? 9  
HELX_P HELX_P69 AH6 SER D 159 ? ASN D 164 ? SER D 177 ASN D 182 5 ? 6  
HELX_P HELX_P70 AH7 VAL D 167 ? ALA D 173 ? VAL D 185 ALA D 191 1 ? 7  
HELX_P HELX_P71 AH8 ARG D 177 ? LYS D 181 ? ARG D 195 LYS D 199 5 ? 5  
HELX_P HELX_P72 AH9 GLY D 228 ? LYS D 233 ? GLY D 246 LYS D 251 1 ? 6  
HELX_P HELX_P73 AI1 GLY D 244 ? HIS D 260 ? GLY D 262 HIS D 278 1 ? 17 
HELX_P HELX_P74 AI2 ASP D 265 ? GLU D 284 ? ASP D 283 GLU D 302 1 ? 20 
HELX_P HELX_P75 AI3 VAL D 292 ? THR D 297 ? VAL D 310 THR D 315 1 ? 6  
HELX_P HELX_P76 AI4 GLU D 298 ? LYS D 307 ? GLU D 316 LYS D 325 1 ? 10 
HELX_P HELX_P77 AI5 THR D 320 ? LEU D 344 ? THR D 338 LEU D 362 1 ? 25 
HELX_P HELX_P78 AI6 GLN D 345 ? ARG D 347 ? GLN D 363 ARG D 365 5 ? 3  
HELX_P HELX_P79 AI7 THR E 22  ? GLU E 34  ? THR E 22  GLU E 34  1 ? 13 
HELX_P HELX_P80 AI8 THR E 55  ? ASN E 60  ? THR E 55  ASN E 60  5 ? 6  
HELX_P HELX_P81 AI9 THR F 22  ? GLY F 35  ? THR F 22  GLY F 35  1 ? 14 
HELX_P HELX_P82 AJ1 THR F 55  ? ASN F 60  ? THR F 55  ASN F 60  5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 6 ? 
AA7 ? 3 ? 
AA8 ? 3 ? 
AA9 ? 5 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 5 ? 
AB5 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? parallel      
AA9 4 5 ? parallel      
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? parallel      
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? parallel      
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 29  ? PRO A 32  ? ALA A 29  PRO A 32  
AA1 2 MET A 16  ? PHE A 21  ? MET A 16  PHE A 21  
AA1 3 LEU A 8   ? ASN A 12  ? LEU A 8   ASN A 12  
AA1 4 VAL A 103 ? GLU A 107 ? VAL A 103 GLU A 107 
AA1 5 ALA A 131 ? ILE A 136 ? ALA A 131 ILE A 136 
AA1 6 ILE A 357 ? SER A 358 ? ILE A 357 SER A 358 
AA2 1 TYR A 53  ? VAL A 54  ? TYR A 53  VAL A 54  
AA2 2 VAL A 35  ? PRO A 38  ? VAL A 35  PRO A 38  
AA2 3 LEU A 65  ? LYS A 68  ? LEU A 65  LYS A 68  
AA3 1 TYR A 169 ? ALA A 170 ? TYR A 169 ALA A 170 
AA3 2 THR A 160 ? TYR A 166 ? THR A 160 TYR A 166 
AA3 3 LEU A 176 ? LEU A 178 ? LEU A 176 LEU A 178 
AA4 1 TYR A 169 ? ALA A 170 ? TYR A 169 ALA A 170 
AA4 2 THR A 160 ? TYR A 166 ? THR A 160 TYR A 166 
AA4 3 GLY A 150 ? SER A 155 ? GLY A 150 SER A 155 
AA4 4 THR A 297 ? GLY A 301 ? THR A 297 GLY A 301 
AA4 5 ILE A 329 ? ILE A 330 ? ILE A 329 ILE A 330 
AA5 1 LYS A 238 ? LEU A 242 ? LYS A 238 LEU A 242 
AA5 2 GLN A 246 ? ILE A 250 ? GLN A 246 ILE A 250 
AA6 1 ALA B 29  ? PRO B 32  ? ALA B 29  PRO B 32  
AA6 2 MET B 16  ? PHE B 21  ? MET B 16  PHE B 21  
AA6 3 LEU B 8   ? ASP B 11  ? LEU B 8   ASP B 11  
AA6 4 VAL B 103 ? GLU B 107 ? VAL B 103 GLU B 107 
AA6 5 ALA B 131 ? ILE B 136 ? ALA B 131 ILE B 136 
AA6 6 ILE B 357 ? SER B 358 ? ILE B 357 SER B 358 
AA7 1 TYR B 53  ? VAL B 54  ? TYR B 53  VAL B 54  
AA7 2 VAL B 35  ? PRO B 38  ? VAL B 35  PRO B 38  
AA7 3 LEU B 65  ? LYS B 68  ? LEU B 65  LYS B 68  
AA8 1 TYR B 169 ? ALA B 170 ? TYR B 169 ALA B 170 
AA8 2 THR B 160 ? TYR B 166 ? THR B 160 TYR B 166 
AA8 3 LEU B 176 ? LEU B 178 ? LEU B 176 LEU B 178 
AA9 1 TYR B 169 ? ALA B 170 ? TYR B 169 ALA B 170 
AA9 2 THR B 160 ? TYR B 166 ? THR B 160 TYR B 166 
AA9 3 GLY B 150 ? SER B 155 ? GLY B 150 SER B 155 
AA9 4 THR B 297 ? GLY B 301 ? THR B 297 GLY B 301 
AA9 5 ILE B 329 ? ILE B 330 ? ILE B 329 ILE B 330 
AB1 1 LYS B 238 ? GLU B 241 ? LYS B 238 GLU B 241 
AB1 2 VAL B 247 ? ILE B 250 ? VAL B 247 ILE B 250 
AB2 1 GLY C 189 ? SER C 193 ? GLY C 207 SER C 211 
AB2 2 ARG C 214 ? LYS C 218 ? ARG C 232 LYS C 236 
AB3 1 THR D 191 ? SER D 193 ? THR D 209 SER D 211 
AB3 2 ARG D 214 ? VAL D 216 ? ARG D 232 VAL D 234 
AB4 1 THR E 12  ? GLU E 16  ? THR E 12  GLU E 16  
AB4 2 GLN E 2   ? LYS E 6   ? GLN E 2   LYS E 6   
AB4 3 THR E 66  ? LEU E 71  ? THR E 66  LEU E 71  
AB4 4 GLN E 41  ? PHE E 45  ? GLN E 41  PHE E 45  
AB4 5 LYS E 48  ? GLN E 49  ? LYS E 48  GLN E 49  
AB5 1 THR F 12  ? THR F 14  ? THR F 12  THR F 14  
AB5 2 PHE F 4   ? LYS F 6   ? PHE F 4   LYS F 6   
AB5 3 THR F 66  ? LEU F 71  ? THR F 66  LEU F 71  
AB5 4 GLN F 41  ? PHE F 45  ? GLN F 41  PHE F 45  
AB5 5 LYS F 48  ? GLN F 49  ? LYS F 48  GLN F 49  
# 
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 PHE A 31  ? O PHE A 31  N CYS A 17  ? N CYS A 17  
AA1 2 3 O GLY A 20  ? O GLY A 20  N VAL A 9   ? N VAL A 9   
AA1 3 4 N LEU A 8   ? N LEU A 8   O LEU A 104 ? O LEU A 104 
AA1 4 5 N LEU A 105 ? N LEU A 105 O TYR A 133 ? O TYR A 133 
AA1 5 6 N MET A 132 ? N MET A 132 O ILE A 357 ? O ILE A 357 
AA2 1 2 O TYR A 53  ? O TYR A 53  N GLY A 36  ? N GLY A 36  
AA2 2 3 N VAL A 35  ? N VAL A 35  O LYS A 68  ? O LYS A 68  
AA3 1 2 O TYR A 169 ? O TYR A 169 N TYR A 166 ? N TYR A 166 
AA3 2 3 N THR A 160 ? N THR A 160 O LEU A 178 ? O LEU A 178 
AA4 1 2 O TYR A 169 ? O TYR A 169 N TYR A 166 ? N TYR A 166 
AA4 2 3 O ILE A 165 ? O ILE A 165 N GLY A 150 ? N GLY A 150 
AA4 3 4 N SER A 155 ? N SER A 155 O SER A 300 ? O SER A 300 
AA4 4 5 N THR A 297 ? N THR A 297 O ILE A 330 ? O ILE A 330 
AA5 1 2 N TYR A 240 ? N TYR A 240 O ILE A 248 ? O ILE A 248 
AA6 1 2 O ALA B 29  ? O ALA B 29  N ALA B 19  ? N ALA B 19  
AA6 2 3 O LYS B 18  ? O LYS B 18  N ASP B 11  ? N ASP B 11  
AA6 3 4 N LEU B 8   ? N LEU B 8   O LEU B 104 ? O LEU B 104 
AA6 4 5 N GLU B 107 ? N GLU B 107 O ALA B 135 ? O ALA B 135 
AA6 5 6 N MET B 132 ? N MET B 132 O ILE B 357 ? O ILE B 357 
AA7 1 2 O TYR B 53  ? O TYR B 53  N GLY B 36  ? N GLY B 36  
AA7 2 3 N ARG B 37  ? N ARG B 37  O THR B 66  ? O THR B 66  
AA8 1 2 O TYR B 169 ? O TYR B 169 N TYR B 166 ? N TYR B 166 
AA8 2 3 N THR B 160 ? N THR B 160 O LEU B 178 ? O LEU B 178 
AA9 1 2 O TYR B 169 ? O TYR B 169 N TYR B 166 ? N TYR B 166 
AA9 2 3 O ILE B 165 ? O ILE B 165 N GLY B 150 ? N GLY B 150 
AA9 3 4 N MET B 153 ? N MET B 153 O VAL B 298 ? O VAL B 298 
AA9 4 5 N LEU B 299 ? N LEU B 299 O ILE B 330 ? O ILE B 330 
AB1 1 2 N LYS B 238 ? N LYS B 238 O ILE B 250 ? O ILE B 250 
AB2 1 2 N THR C 191 ? N THR C 209 O VAL C 216 ? O VAL C 234 
AB3 1 2 N THR D 191 ? N THR D 209 O VAL D 216 ? O VAL D 234 
AB4 1 2 O ILE E 13  ? O ILE E 13  N VAL E 5   ? N VAL E 5   
AB4 2 3 N LYS E 6   ? N LYS E 6   O LEU E 69  ? O LEU E 69  
AB4 3 4 O HIS E 68  ? O HIS E 68  N ILE E 44  ? N ILE E 44  
AB4 4 5 N PHE E 45  ? N PHE E 45  O LYS E 48  ? O LYS E 48  
AB5 1 2 O ILE F 13  ? O ILE F 13  N VAL F 5   ? N VAL F 5   
AB5 2 3 N PHE F 4   ? N PHE F 4   O LEU F 67  ? O LEU F 67  
AB5 3 4 O HIS F 68  ? O HIS F 68  N ILE F 44  ? N ILE F 44  
AB5 4 5 N PHE F 45  ? N PHE F 45  O LYS F 48  ? O LYS F 48  
# 
_pdbx_entry_details.entry_id                   8K6F 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA C LEU 181 ? ? CB C LEU 181 ? ? CG C LEU 181 ? ? 130.37 115.30 15.07  2.30 N 
2 1 N  D VAL 257 ? ? CA D VAL 257 ? ? C  D VAL 257 ? ? 77.48  111.00 -33.52 2.70 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 LYS A 50  ? ? -101.38 73.07   
2  1 TYR A 91  ? ? -94.33  -66.30  
3  1 ASN A 128 ? ? 49.35   19.44   
4  1 ASP A 179 ? ? -108.41 44.68   
5  1 ILE B 71  ? ? 34.85   49.42   
6  1 ASP B 179 ? ? -85.24  49.13   
7  1 ALA B 181 ? ? -158.13 -156.75 
8  1 GLU C 25  ? ? 83.97   -7.28   
9  1 LEU C 26  ? ? -122.69 -52.33  
10 1 LYS C 58  ? ? 64.40   -4.21   
11 1 ASN C 75  ? ? -100.72 73.35   
12 1 ASN C 184 ? ? -138.09 -67.54  
13 1 THR C 225 ? ? 72.85   -5.36   
14 1 SER C 259 ? ? 73.61   -63.19  
15 1 HIS C 278 ? ? -141.42 43.79   
16 1 ASP C 283 ? ? -92.14  37.24   
17 1 LYS D 36  ? ? -88.68  44.85   
18 1 LEU D 168 ? ? 83.47   -6.41   
19 1 ASN D 184 ? ? -133.66 -70.02  
20 1 VAL D 257 ? ? -125.44 -168.89 
21 1 GLN E 62  ? ? -125.48 -162.36 
22 1 GLU F 64  ? ? 59.02   14.71   
# 
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 GLU 2  ? A GLU 2 
3  1 Y 1 A GLU 3  ? A GLU 3 
4  1 Y 1 A GLU 4  ? A GLU 4 
5  1 Y 1 A ILE 5  ? A ILE 5 
6  1 Y 1 B MET 1  ? B MET 1 
7  1 Y 1 B GLU 2  ? B GLU 2 
8  1 Y 1 B GLU 3  ? B GLU 3 
9  1 Y 1 B GLU 4  ? B GLU 4 
10 1 Y 1 C MET 19 ? C MET 1 
11 1 Y 1 C SER 20 ? C SER 2 
12 1 Y 1 C TYR 21 ? C TYR 3 
13 1 Y 1 C GLN 22 ? C GLN 4 
14 1 Y 1 C LYS 23 ? C LYS 5 
15 1 Y 1 D MET 19 ? D MET 1 
16 1 Y 1 D SER 20 ? D SER 2 
17 1 Y 1 D TYR 21 ? D TYR 3 
18 1 Y 1 D GLN 22 ? D GLN 4 
# 
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  
AR6 N1     N Y N 14  
AR6 C2     C Y N 15  
AR6 N3     N Y N 16  
AR6 C4     C Y N 17  
AR6 C5     C Y N 18  
AR6 C6     C Y N 19  
AR6 N6     N N N 20  
AR6 N7     N Y N 21  
AR6 C8     C Y N 22  
AR6 N9     N Y N 23  
AR6 PA     P N N 24  
AR6 PB     P N N 25  
AR6 "C1'"  C N R 26  
AR6 O1A    O N N 27  
AR6 O1B    O N N 28  
AR6 C1D    C N S 29  
AR6 O1D    O N N 30  
AR6 "C2'"  C N R 31  
AR6 "O2'"  O N N 32  
AR6 O2A    O N N 33  
AR6 O2B    O N N 34  
AR6 C2D    C N R 35  
AR6 O2D    O N N 36  
AR6 "C3'"  C N S 37  
AR6 "O3'"  O N N 38  
AR6 O3A    O N N 39  
AR6 C3D    C N S 40  
AR6 O3D    O N N 41  
AR6 "C4'"  C N R 42  
AR6 "O4'"  O N N 43  
AR6 C4D    C N R 44  
AR6 O4D    O N N 45  
AR6 "C5'"  C N N 46  
AR6 "O5'"  O N N 47  
AR6 C5D    C N N 48  
AR6 O5D    O N N 49  
AR6 H2     H N N 50  
AR6 HN6    H N N 51  
AR6 HN6A   H N N 52  
AR6 H8     H N N 53  
AR6 "H1'"  H N N 54  
AR6 H1D    H N N 55  
AR6 "H2'"  H N N 56  
AR6 "HO2'" H N N 57  
AR6 H2D    H N N 58  
AR6 HO2D   H N N 59  
AR6 "H3'"  H N N 60  
AR6 "HO3'" H N N 61  
AR6 H3D    H N N 62  
AR6 HO3D   H N N 63  
AR6 "H4'"  H N N 64  
AR6 H4D    H N N 65  
AR6 "H5'"  H N N 66  
AR6 "H5'A" H N N 67  
AR6 H5D    H N N 68  
AR6 H5DA   H N N 69  
AR6 H1A    H N N 70  
AR6 H1B    H N N 71  
AR6 HD1    H N N 72  
ARG N      N N N 73  
ARG CA     C N S 74  
ARG C      C N N 75  
ARG O      O N N 76  
ARG CB     C N N 77  
ARG CG     C N N 78  
ARG CD     C N N 79  
ARG NE     N N N 80  
ARG CZ     C N N 81  
ARG NH1    N N N 82  
ARG NH2    N N N 83  
ARG OXT    O N N 84  
ARG H      H N N 85  
ARG H2     H N N 86  
ARG HA     H N N 87  
ARG HB2    H N N 88  
ARG HB3    H N N 89  
ARG HG2    H N N 90  
ARG HG3    H N N 91  
ARG HD2    H N N 92  
ARG HD3    H N N 93  
ARG HE     H N N 94  
ARG HH11   H N N 95  
ARG HH12   H N N 96  
ARG HH21   H N N 97  
ARG HH22   H N N 98  
ARG HXT    H N N 99  
ASN N      N N N 100 
ASN CA     C N S 101 
ASN C      C N N 102 
ASN O      O N N 103 
ASN CB     C N N 104 
ASN CG     C N N 105 
ASN OD1    O N N 106 
ASN ND2    N N N 107 
ASN OXT    O N N 108 
ASN H      H N N 109 
ASN H2     H N N 110 
ASN HA     H N N 111 
ASN HB2    H N N 112 
ASN HB3    H N N 113 
ASN HD21   H N N 114 
ASN HD22   H N N 115 
ASN HXT    H N N 116 
ASP N      N N N 117 
ASP CA     C N S 118 
ASP C      C N N 119 
ASP O      O N N 120 
ASP CB     C N N 121 
ASP CG     C N N 122 
ASP OD1    O N N 123 
ASP OD2    O N N 124 
ASP OXT    O N N 125 
ASP H      H N N 126 
ASP H2     H N N 127 
ASP HA     H N N 128 
ASP HB2    H N N 129 
ASP HB3    H N N 130 
ASP HD2    H N N 131 
ASP HXT    H N N 132 
ATP PG     P N N 133 
ATP O1G    O N N 134 
ATP O2G    O N N 135 
ATP O3G    O N N 136 
ATP PB     P N R 137 
ATP O1B    O N N 138 
ATP O2B    O N N 139 
ATP O3B    O N N 140 
ATP PA     P N R 141 
ATP O1A    O N N 142 
ATP O2A    O N N 143 
ATP O3A    O N N 144 
ATP "O5'"  O N N 145 
ATP "C5'"  C N N 146 
ATP "C4'"  C N R 147 
ATP "O4'"  O N N 148 
ATP "C3'"  C N S 149 
ATP "O3'"  O N N 150 
ATP "C2'"  C N R 151 
ATP "O2'"  O N N 152 
ATP "C1'"  C N R 153 
ATP N9     N Y N 154 
ATP C8     C Y N 155 
ATP N7     N Y N 156 
ATP C5     C Y N 157 
ATP C6     C Y N 158 
ATP N6     N N N 159 
ATP N1     N Y N 160 
ATP C2     C Y N 161 
ATP N3     N Y N 162 
ATP C4     C Y N 163 
ATP HOG2   H N N 164 
ATP HOG3   H N N 165 
ATP HOB2   H N N 166 
ATP HOA2   H N N 167 
ATP "H5'1" H N N 168 
ATP "H5'2" H N N 169 
ATP "H4'"  H N N 170 
ATP "H3'"  H N N 171 
ATP "HO3'" H N N 172 
ATP "H2'"  H N N 173 
ATP "HO2'" H N N 174 
ATP "H1'"  H N N 175 
ATP H8     H N N 176 
ATP HN61   H N N 177 
ATP HN62   H N N 178 
ATP H2     H N N 179 
CYS N      N N N 180 
CYS CA     C N R 181 
CYS C      C N N 182 
CYS O      O N N 183 
CYS CB     C N N 184 
CYS SG     S N N 185 
CYS OXT    O N N 186 
CYS H      H N N 187 
CYS H2     H N N 188 
CYS HA     H N N 189 
CYS HB2    H N N 190 
CYS HB3    H N N 191 
CYS HG     H N N 192 
CYS HXT    H N N 193 
GLN N      N N N 194 
GLN CA     C N S 195 
GLN C      C N N 196 
GLN O      O N N 197 
GLN CB     C N N 198 
GLN CG     C N N 199 
GLN CD     C N N 200 
GLN OE1    O N N 201 
GLN NE2    N N N 202 
GLN OXT    O N N 203 
GLN H      H N N 204 
GLN H2     H N N 205 
GLN HA     H N N 206 
GLN HB2    H N N 207 
GLN HB3    H N N 208 
GLN HG2    H N N 209 
GLN HG3    H N N 210 
GLN HE21   H N N 211 
GLN HE22   H N N 212 
GLN HXT    H N N 213 
GLU N      N N N 214 
GLU CA     C N S 215 
GLU C      C N N 216 
GLU O      O N N 217 
GLU CB     C N N 218 
GLU CG     C N N 219 
GLU CD     C N N 220 
GLU OE1    O N N 221 
GLU OE2    O N N 222 
GLU OXT    O N N 223 
GLU H      H N N 224 
GLU H2     H N N 225 
GLU HA     H N N 226 
GLU HB2    H N N 227 
GLU HB3    H N N 228 
GLU HG2    H N N 229 
GLU HG3    H N N 230 
GLU HE2    H N N 231 
GLU HXT    H N N 232 
GLY N      N N N 233 
GLY CA     C N N 234 
GLY C      C N N 235 
GLY O      O N N 236 
GLY OXT    O N N 237 
GLY H      H N N 238 
GLY H2     H N N 239 
GLY HA2    H N N 240 
GLY HA3    H N N 241 
GLY HXT    H N N 242 
HIS N      N N N 243 
HIS CA     C N S 244 
HIS C      C N N 245 
HIS O      O N N 246 
HIS CB     C N N 247 
HIS CG     C Y N 248 
HIS ND1    N Y N 249 
HIS CD2    C Y N 250 
HIS CE1    C Y N 251 
HIS NE2    N Y N 252 
HIS OXT    O N N 253 
HIS H      H N N 254 
HIS H2     H N N 255 
HIS HA     H N N 256 
HIS HB2    H N N 257 
HIS HB3    H N N 258 
HIS HD1    H N N 259 
HIS HD2    H N N 260 
HIS HE1    H N N 261 
HIS HE2    H N N 262 
HIS HXT    H N N 263 
ILE N      N N N 264 
ILE CA     C N S 265 
ILE C      C N N 266 
ILE O      O N N 267 
ILE CB     C N S 268 
ILE CG1    C N N 269 
ILE CG2    C N N 270 
ILE CD1    C N N 271 
ILE OXT    O N N 272 
ILE H      H N N 273 
ILE H2     H N N 274 
ILE HA     H N N 275 
ILE HB     H N N 276 
ILE HG12   H N N 277 
ILE HG13   H N N 278 
ILE HG21   H N N 279 
ILE HG22   H N N 280 
ILE HG23   H N N 281 
ILE HD11   H N N 282 
ILE HD12   H N N 283 
ILE HD13   H N N 284 
ILE HXT    H N N 285 
LEU N      N N N 286 
LEU CA     C N S 287 
LEU C      C N N 288 
LEU O      O N N 289 
LEU CB     C N N 290 
LEU CG     C N N 291 
LEU CD1    C N N 292 
LEU CD2    C N N 293 
LEU OXT    O N N 294 
LEU H      H N N 295 
LEU H2     H N N 296 
LEU HA     H N N 297 
LEU HB2    H N N 298 
LEU HB3    H N N 299 
LEU HG     H N N 300 
LEU HD11   H N N 301 
LEU HD12   H N N 302 
LEU HD13   H N N 303 
LEU HD21   H N N 304 
LEU HD22   H N N 305 
LEU HD23   H N N 306 
LEU HXT    H N N 307 
LYS N      N N N 308 
LYS CA     C N S 309 
LYS C      C N N 310 
LYS O      O N N 311 
LYS CB     C N N 312 
LYS CG     C N N 313 
LYS CD     C N N 314 
LYS CE     C N N 315 
LYS NZ     N N N 316 
LYS OXT    O N N 317 
LYS H      H N N 318 
LYS H2     H N N 319 
LYS HA     H N N 320 
LYS HB2    H N N 321 
LYS HB3    H N N 322 
LYS HG2    H N N 323 
LYS HG3    H N N 324 
LYS HD2    H N N 325 
LYS HD3    H N N 326 
LYS HE2    H N N 327 
LYS HE3    H N N 328 
LYS HZ1    H N N 329 
LYS HZ2    H N N 330 
LYS HZ3    H N N 331 
LYS HXT    H N N 332 
MET N      N N N 333 
MET CA     C N S 334 
MET C      C N N 335 
MET O      O N N 336 
MET CB     C N N 337 
MET CG     C N N 338 
MET SD     S N N 339 
MET CE     C N N 340 
MET OXT    O N N 341 
MET H      H N N 342 
MET H2     H N N 343 
MET HA     H N N 344 
MET HB2    H N N 345 
MET HB3    H N N 346 
MET HG2    H N N 347 
MET HG3    H N N 348 
MET HE1    H N N 349 
MET HE2    H N N 350 
MET HE3    H N N 351 
MET HXT    H N N 352 
PHE N      N N N 353 
PHE CA     C N S 354 
PHE C      C N N 355 
PHE O      O N N 356 
PHE CB     C N N 357 
PHE CG     C Y N 358 
PHE CD1    C Y N 359 
PHE CD2    C Y N 360 
PHE CE1    C Y N 361 
PHE CE2    C Y N 362 
PHE CZ     C Y N 363 
PHE OXT    O N N 364 
PHE H      H N N 365 
PHE H2     H N N 366 
PHE HA     H N N 367 
PHE HB2    H N N 368 
PHE HB3    H N N 369 
PHE HD1    H N N 370 
PHE HD2    H N N 371 
PHE HE1    H N N 372 
PHE HE2    H N N 373 
PHE HZ     H N N 374 
PHE HXT    H N N 375 
PRO N      N N N 376 
PRO CA     C N S 377 
PRO C      C N N 378 
PRO O      O N N 379 
PRO CB     C N N 380 
PRO CG     C N N 381 
PRO CD     C N N 382 
PRO OXT    O N N 383 
PRO H      H N N 384 
PRO HA     H N N 385 
PRO HB2    H N N 386 
PRO HB3    H N N 387 
PRO HG2    H N N 388 
PRO HG3    H N N 389 
PRO HD2    H N N 390 
PRO HD3    H N N 391 
PRO HXT    H N N 392 
SER N      N N N 393 
SER CA     C N S 394 
SER C      C N N 395 
SER O      O N N 396 
SER CB     C N N 397 
SER OG     O N N 398 
SER OXT    O N N 399 
SER H      H N N 400 
SER H2     H N N 401 
SER HA     H N N 402 
SER HB2    H N N 403 
SER HB3    H N N 404 
SER HG     H N N 405 
SER HXT    H N N 406 
THR N      N N N 407 
THR CA     C N S 408 
THR C      C N N 409 
THR O      O N N 410 
THR CB     C N R 411 
THR OG1    O N N 412 
THR CG2    C N N 413 
THR OXT    O N N 414 
THR H      H N N 415 
THR H2     H N N 416 
THR HA     H N N 417 
THR HB     H N N 418 
THR HG1    H N N 419 
THR HG21   H N N 420 
THR HG22   H N N 421 
THR HG23   H N N 422 
THR HXT    H N N 423 
TRP N      N N N 424 
TRP CA     C N S 425 
TRP C      C N N 426 
TRP O      O N N 427 
TRP CB     C N N 428 
TRP CG     C Y N 429 
TRP CD1    C Y N 430 
TRP CD2    C Y N 431 
TRP NE1    N Y N 432 
TRP CE2    C Y N 433 
TRP CE3    C Y N 434 
TRP CZ2    C Y N 435 
TRP CZ3    C Y N 436 
TRP CH2    C Y N 437 
TRP OXT    O N N 438 
TRP H      H N N 439 
TRP H2     H N N 440 
TRP HA     H N N 441 
TRP HB2    H N N 442 
TRP HB3    H N N 443 
TRP HD1    H N N 444 
TRP HE1    H N N 445 
TRP HE3    H N N 446 
TRP HZ2    H N N 447 
TRP HZ3    H N N 448 
TRP HH2    H N N 449 
TRP HXT    H N N 450 
TYR N      N N N 451 
TYR CA     C N S 452 
TYR C      C N N 453 
TYR O      O N N 454 
TYR CB     C N N 455 
TYR CG     C Y N 456 
TYR CD1    C Y N 457 
TYR CD2    C Y N 458 
TYR CE1    C Y N 459 
TYR CE2    C Y N 460 
TYR CZ     C Y N 461 
TYR OH     O N N 462 
TYR OXT    O N N 463 
TYR H      H N N 464 
TYR H2     H N N 465 
TYR HA     H N N 466 
TYR HB2    H N N 467 
TYR HB3    H N N 468 
TYR HD1    H N N 469 
TYR HD2    H N N 470 
TYR HE1    H N N 471 
TYR HE2    H N N 472 
TYR HH     H N N 473 
TYR HXT    H N N 474 
VAL N      N N N 475 
VAL CA     C N S 476 
VAL C      C N N 477 
VAL O      O N N 478 
VAL CB     C N N 479 
VAL CG1    C N N 480 
VAL CG2    C N N 481 
VAL OXT    O N N 482 
VAL H      H N N 483 
VAL H2     H N N 484 
VAL HA     H N N 485 
VAL HB     H N N 486 
VAL HG11   H N N 487 
VAL HG12   H N N 488 
VAL HG13   H N N 489 
VAL HG21   H N N 490 
VAL HG22   H N N 491 
VAL HG23   H N N 492 
VAL HXT    H N N 493 
# 
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  
AR6 N1    C2     doub Y N 13  
AR6 N1    C6     sing Y N 14  
AR6 C2    N3     sing Y N 15  
AR6 N3    C4     doub Y N 16  
AR6 C4    C5     sing Y N 17  
AR6 C4    N9     sing Y N 18  
AR6 C5    C6     doub Y N 19  
AR6 C5    N7     sing Y N 20  
AR6 C6    N6     sing N N 21  
AR6 N7    C8     doub Y N 22  
AR6 C8    N9     sing Y N 23  
AR6 N9    "C1'"  sing N N 24  
AR6 PA    O1A    sing N N 25  
AR6 PA    O2A    doub N N 26  
AR6 PA    O3A    sing N N 27  
AR6 PA    "O5'"  sing N N 28  
AR6 PB    O1B    sing N N 29  
AR6 PB    O2B    doub N N 30  
AR6 PB    O3A    sing N N 31  
AR6 PB    O5D    sing N N 32  
AR6 "C1'" "C2'"  sing N N 33  
AR6 "C1'" "O4'"  sing N N 34  
AR6 C1D   O1D    sing N N 35  
AR6 C1D   C2D    sing N N 36  
AR6 C1D   O4D    sing N N 37  
AR6 "C2'" "O2'"  sing N N 38  
AR6 "C2'" "C3'"  sing N N 39  
AR6 C2D   O2D    sing N N 40  
AR6 C2D   C3D    sing N N 41  
AR6 "C3'" "O3'"  sing N N 42  
AR6 "C3'" "C4'"  sing N N 43  
AR6 C3D   O3D    sing N N 44  
AR6 C3D   C4D    sing N N 45  
AR6 "C4'" "O4'"  sing N N 46  
AR6 "C4'" "C5'"  sing N N 47  
AR6 C4D   O4D    sing N N 48  
AR6 C4D   C5D    sing N N 49  
AR6 "C5'" "O5'"  sing N N 50  
AR6 C5D   O5D    sing N N 51  
AR6 C2    H2     sing N N 52  
AR6 N6    HN6    sing N N 53  
AR6 N6    HN6A   sing N N 54  
AR6 C8    H8     sing N N 55  
AR6 "C1'" "H1'"  sing N N 56  
AR6 C1D   H1D    sing N N 57  
AR6 "C2'" "H2'"  sing N N 58  
AR6 "O2'" "HO2'" sing N N 59  
AR6 C2D   H2D    sing N N 60  
AR6 O2D   HO2D   sing N N 61  
AR6 "C3'" "H3'"  sing N N 62  
AR6 "O3'" "HO3'" sing N N 63  
AR6 C3D   H3D    sing N N 64  
AR6 O3D   HO3D   sing N N 65  
AR6 "C4'" "H4'"  sing N N 66  
AR6 C4D   H4D    sing N N 67  
AR6 "C5'" "H5'"  sing N N 68  
AR6 "C5'" "H5'A" sing N N 69  
AR6 C5D   H5D    sing N N 70  
AR6 C5D   H5DA   sing N N 71  
AR6 O1A   H1A    sing N N 72  
AR6 O1B   H1B    sing N N 73  
AR6 O1D   HD1    sing N N 74  
ARG N     CA     sing N N 75  
ARG N     H      sing N N 76  
ARG N     H2     sing N N 77  
ARG CA    C      sing N N 78  
ARG CA    CB     sing N N 79  
ARG CA    HA     sing N N 80  
ARG C     O      doub N N 81  
ARG C     OXT    sing N N 82  
ARG CB    CG     sing N N 83  
ARG CB    HB2    sing N N 84  
ARG CB    HB3    sing N N 85  
ARG CG    CD     sing N N 86  
ARG CG    HG2    sing N N 87  
ARG CG    HG3    sing N N 88  
ARG CD    NE     sing N N 89  
ARG CD    HD2    sing N N 90  
ARG CD    HD3    sing N N 91  
ARG NE    CZ     sing N N 92  
ARG NE    HE     sing N N 93  
ARG CZ    NH1    sing N N 94  
ARG CZ    NH2    doub N N 95  
ARG NH1   HH11   sing N N 96  
ARG NH1   HH12   sing N N 97  
ARG NH2   HH21   sing N N 98  
ARG NH2   HH22   sing N N 99  
ARG OXT   HXT    sing N N 100 
ASN N     CA     sing N N 101 
ASN N     H      sing N N 102 
ASN N     H2     sing N N 103 
ASN CA    C      sing N N 104 
ASN CA    CB     sing N N 105 
ASN CA    HA     sing N N 106 
ASN C     O      doub N N 107 
ASN C     OXT    sing N N 108 
ASN CB    CG     sing N N 109 
ASN CB    HB2    sing N N 110 
ASN CB    HB3    sing N N 111 
ASN CG    OD1    doub N N 112 
ASN CG    ND2    sing N N 113 
ASN ND2   HD21   sing N N 114 
ASN ND2   HD22   sing N N 115 
ASN OXT   HXT    sing N N 116 
ASP N     CA     sing N N 117 
ASP N     H      sing N N 118 
ASP N     H2     sing N N 119 
ASP CA    C      sing N N 120 
ASP CA    CB     sing N N 121 
ASP CA    HA     sing N N 122 
ASP C     O      doub N N 123 
ASP C     OXT    sing N N 124 
ASP CB    CG     sing N N 125 
ASP CB    HB2    sing N N 126 
ASP CB    HB3    sing N N 127 
ASP CG    OD1    doub N N 128 
ASP CG    OD2    sing N N 129 
ASP OD2   HD2    sing N N 130 
ASP OXT   HXT    sing N N 131 
ATP PG    O1G    doub N N 132 
ATP PG    O2G    sing N N 133 
ATP PG    O3G    sing N N 134 
ATP PG    O3B    sing N N 135 
ATP O2G   HOG2   sing N N 136 
ATP O3G   HOG3   sing N N 137 
ATP PB    O1B    doub N N 138 
ATP PB    O2B    sing N N 139 
ATP PB    O3B    sing N N 140 
ATP PB    O3A    sing N N 141 
ATP O2B   HOB2   sing N N 142 
ATP PA    O1A    doub N N 143 
ATP PA    O2A    sing N N 144 
ATP PA    O3A    sing N N 145 
ATP PA    "O5'"  sing N N 146 
ATP O2A   HOA2   sing N N 147 
ATP "O5'" "C5'"  sing N N 148 
ATP "C5'" "C4'"  sing N N 149 
ATP "C5'" "H5'1" sing N N 150 
ATP "C5'" "H5'2" sing N N 151 
ATP "C4'" "O4'"  sing N N 152 
ATP "C4'" "C3'"  sing N N 153 
ATP "C4'" "H4'"  sing N N 154 
ATP "O4'" "C1'"  sing N N 155 
ATP "C3'" "O3'"  sing N N 156 
ATP "C3'" "C2'"  sing N N 157 
ATP "C3'" "H3'"  sing N N 158 
ATP "O3'" "HO3'" sing N N 159 
ATP "C2'" "O2'"  sing N N 160 
ATP "C2'" "C1'"  sing N N 161 
ATP "C2'" "H2'"  sing N N 162 
ATP "O2'" "HO2'" sing N N 163 
ATP "C1'" N9     sing N N 164 
ATP "C1'" "H1'"  sing N N 165 
ATP N9    C8     sing Y N 166 
ATP N9    C4     sing Y N 167 
ATP C8    N7     doub Y N 168 
ATP C8    H8     sing N N 169 
ATP N7    C5     sing Y N 170 
ATP C5    C6     sing Y N 171 
ATP C5    C4     doub Y N 172 
ATP C6    N6     sing N N 173 
ATP C6    N1     doub Y N 174 
ATP N6    HN61   sing N N 175 
ATP N6    HN62   sing N N 176 
ATP N1    C2     sing Y N 177 
ATP C2    N3     doub Y N 178 
ATP C2    H2     sing N N 179 
ATP N3    C4     sing Y N 180 
CYS N     CA     sing N N 181 
CYS N     H      sing N N 182 
CYS N     H2     sing N N 183 
CYS CA    C      sing N N 184 
CYS CA    CB     sing N N 185 
CYS CA    HA     sing N N 186 
CYS C     O      doub N N 187 
CYS C     OXT    sing N N 188 
CYS CB    SG     sing N N 189 
CYS CB    HB2    sing N N 190 
CYS CB    HB3    sing N N 191 
CYS SG    HG     sing N N 192 
CYS OXT   HXT    sing N N 193 
GLN N     CA     sing N N 194 
GLN N     H      sing N N 195 
GLN N     H2     sing N N 196 
GLN CA    C      sing N N 197 
GLN CA    CB     sing N N 198 
GLN CA    HA     sing N N 199 
GLN C     O      doub N N 200 
GLN C     OXT    sing N N 201 
GLN CB    CG     sing N N 202 
GLN CB    HB2    sing N N 203 
GLN CB    HB3    sing N N 204 
GLN CG    CD     sing N N 205 
GLN CG    HG2    sing N N 206 
GLN CG    HG3    sing N N 207 
GLN CD    OE1    doub N N 208 
GLN CD    NE2    sing N N 209 
GLN NE2   HE21   sing N N 210 
GLN NE2   HE22   sing N N 211 
GLN OXT   HXT    sing N N 212 
GLU N     CA     sing N N 213 
GLU N     H      sing N N 214 
GLU N     H2     sing N N 215 
GLU CA    C      sing N N 216 
GLU CA    CB     sing N N 217 
GLU CA    HA     sing N N 218 
GLU C     O      doub N N 219 
GLU C     OXT    sing N N 220 
GLU CB    CG     sing N N 221 
GLU CB    HB2    sing N N 222 
GLU CB    HB3    sing N N 223 
GLU CG    CD     sing N N 224 
GLU CG    HG2    sing N N 225 
GLU CG    HG3    sing N N 226 
GLU CD    OE1    doub N N 227 
GLU CD    OE2    sing N N 228 
GLU OE2   HE2    sing N N 229 
GLU OXT   HXT    sing N N 230 
GLY N     CA     sing N N 231 
GLY N     H      sing N N 232 
GLY N     H2     sing N N 233 
GLY CA    C      sing N N 234 
GLY CA    HA2    sing N N 235 
GLY CA    HA3    sing N N 236 
GLY C     O      doub N N 237 
GLY C     OXT    sing N N 238 
GLY OXT   HXT    sing N N 239 
HIS N     CA     sing N N 240 
HIS N     H      sing N N 241 
HIS N     H2     sing N N 242 
HIS CA    C      sing N N 243 
HIS CA    CB     sing N N 244 
HIS CA    HA     sing N N 245 
HIS C     O      doub N N 246 
HIS C     OXT    sing N N 247 
HIS CB    CG     sing N N 248 
HIS CB    HB2    sing N N 249 
HIS CB    HB3    sing N N 250 
HIS CG    ND1    sing Y N 251 
HIS CG    CD2    doub Y N 252 
HIS ND1   CE1    doub Y N 253 
HIS ND1   HD1    sing N N 254 
HIS CD2   NE2    sing Y N 255 
HIS CD2   HD2    sing N N 256 
HIS CE1   NE2    sing Y N 257 
HIS CE1   HE1    sing N N 258 
HIS NE2   HE2    sing N N 259 
HIS OXT   HXT    sing N N 260 
ILE N     CA     sing N N 261 
ILE N     H      sing N N 262 
ILE N     H2     sing N N 263 
ILE CA    C      sing N N 264 
ILE CA    CB     sing N N 265 
ILE CA    HA     sing N N 266 
ILE C     O      doub N N 267 
ILE C     OXT    sing N N 268 
ILE CB    CG1    sing N N 269 
ILE CB    CG2    sing N N 270 
ILE CB    HB     sing N N 271 
ILE CG1   CD1    sing N N 272 
ILE CG1   HG12   sing N N 273 
ILE CG1   HG13   sing N N 274 
ILE CG2   HG21   sing N N 275 
ILE CG2   HG22   sing N N 276 
ILE CG2   HG23   sing N N 277 
ILE CD1   HD11   sing N N 278 
ILE CD1   HD12   sing N N 279 
ILE CD1   HD13   sing N N 280 
ILE OXT   HXT    sing N N 281 
LEU N     CA     sing N N 282 
LEU N     H      sing N N 283 
LEU N     H2     sing N N 284 
LEU CA    C      sing N N 285 
LEU CA    CB     sing N N 286 
LEU CA    HA     sing N N 287 
LEU C     O      doub N N 288 
LEU C     OXT    sing N N 289 
LEU CB    CG     sing N N 290 
LEU CB    HB2    sing N N 291 
LEU CB    HB3    sing N N 292 
LEU CG    CD1    sing N N 293 
LEU CG    CD2    sing N N 294 
LEU CG    HG     sing N N 295 
LEU CD1   HD11   sing N N 296 
LEU CD1   HD12   sing N N 297 
LEU CD1   HD13   sing N N 298 
LEU CD2   HD21   sing N N 299 
LEU CD2   HD22   sing N N 300 
LEU CD2   HD23   sing N N 301 
LEU OXT   HXT    sing N N 302 
LYS N     CA     sing N N 303 
LYS N     H      sing N N 304 
LYS N     H2     sing N N 305 
LYS CA    C      sing N N 306 
LYS CA    CB     sing N N 307 
LYS CA    HA     sing N N 308 
LYS C     O      doub N N 309 
LYS C     OXT    sing N N 310 
LYS CB    CG     sing N N 311 
LYS CB    HB2    sing N N 312 
LYS CB    HB3    sing N N 313 
LYS CG    CD     sing N N 314 
LYS CG    HG2    sing N N 315 
LYS CG    HG3    sing N N 316 
LYS CD    CE     sing N N 317 
LYS CD    HD2    sing N N 318 
LYS CD    HD3    sing N N 319 
LYS CE    NZ     sing N N 320 
LYS CE    HE2    sing N N 321 
LYS CE    HE3    sing N N 322 
LYS NZ    HZ1    sing N N 323 
LYS NZ    HZ2    sing N N 324 
LYS NZ    HZ3    sing N N 325 
LYS OXT   HXT    sing N N 326 
MET N     CA     sing N N 327 
MET N     H      sing N N 328 
MET N     H2     sing N N 329 
MET CA    C      sing N N 330 
MET CA    CB     sing N N 331 
MET CA    HA     sing N N 332 
MET C     O      doub N N 333 
MET C     OXT    sing N N 334 
MET CB    CG     sing N N 335 
MET CB    HB2    sing N N 336 
MET CB    HB3    sing N N 337 
MET CG    SD     sing N N 338 
MET CG    HG2    sing N N 339 
MET CG    HG3    sing N N 340 
MET SD    CE     sing N N 341 
MET CE    HE1    sing N N 342 
MET CE    HE2    sing N N 343 
MET CE    HE3    sing N N 344 
MET OXT   HXT    sing N N 345 
PHE N     CA     sing N N 346 
PHE N     H      sing N N 347 
PHE N     H2     sing N N 348 
PHE CA    C      sing N N 349 
PHE CA    CB     sing N N 350 
PHE CA    HA     sing N N 351 
PHE C     O      doub N N 352 
PHE C     OXT    sing N N 353 
PHE CB    CG     sing N N 354 
PHE CB    HB2    sing N N 355 
PHE CB    HB3    sing N N 356 
PHE CG    CD1    doub Y N 357 
PHE CG    CD2    sing Y N 358 
PHE CD1   CE1    sing Y N 359 
PHE CD1   HD1    sing N N 360 
PHE CD2   CE2    doub Y N 361 
PHE CD2   HD2    sing N N 362 
PHE CE1   CZ     doub Y N 363 
PHE CE1   HE1    sing N N 364 
PHE CE2   CZ     sing Y N 365 
PHE CE2   HE2    sing N N 366 
PHE CZ    HZ     sing N N 367 
PHE OXT   HXT    sing N N 368 
PRO N     CA     sing N N 369 
PRO N     CD     sing N N 370 
PRO N     H      sing N N 371 
PRO CA    C      sing N N 372 
PRO CA    CB     sing N N 373 
PRO CA    HA     sing N N 374 
PRO C     O      doub N N 375 
PRO C     OXT    sing N N 376 
PRO CB    CG     sing N N 377 
PRO CB    HB2    sing N N 378 
PRO CB    HB3    sing N N 379 
PRO CG    CD     sing N N 380 
PRO CG    HG2    sing N N 381 
PRO CG    HG3    sing N N 382 
PRO CD    HD2    sing N N 383 
PRO CD    HD3    sing N N 384 
PRO OXT   HXT    sing N N 385 
SER N     CA     sing N N 386 
SER N     H      sing N N 387 
SER N     H2     sing N N 388 
SER CA    C      sing N N 389 
SER CA    CB     sing N N 390 
SER CA    HA     sing N N 391 
SER C     O      doub N N 392 
SER C     OXT    sing N N 393 
SER CB    OG     sing N N 394 
SER CB    HB2    sing N N 395 
SER CB    HB3    sing N N 396 
SER OG    HG     sing N N 397 
SER OXT   HXT    sing N N 398 
THR N     CA     sing N N 399 
THR N     H      sing N N 400 
THR N     H2     sing N N 401 
THR CA    C      sing N N 402 
THR CA    CB     sing N N 403 
THR CA    HA     sing N N 404 
THR C     O      doub N N 405 
THR C     OXT    sing N N 406 
THR CB    OG1    sing N N 407 
THR CB    CG2    sing N N 408 
THR CB    HB     sing N N 409 
THR OG1   HG1    sing N N 410 
THR CG2   HG21   sing N N 411 
THR CG2   HG22   sing N N 412 
THR CG2   HG23   sing N N 413 
THR OXT   HXT    sing N N 414 
TRP N     CA     sing N N 415 
TRP N     H      sing N N 416 
TRP N     H2     sing N N 417 
TRP CA    C      sing N N 418 
TRP CA    CB     sing N N 419 
TRP CA    HA     sing N N 420 
TRP C     O      doub N N 421 
TRP C     OXT    sing N N 422 
TRP CB    CG     sing N N 423 
TRP CB    HB2    sing N N 424 
TRP CB    HB3    sing N N 425 
TRP CG    CD1    doub Y N 426 
TRP CG    CD2    sing Y N 427 
TRP CD1   NE1    sing Y N 428 
TRP CD1   HD1    sing N N 429 
TRP CD2   CE2    doub Y N 430 
TRP CD2   CE3    sing Y N 431 
TRP NE1   CE2    sing Y N 432 
TRP NE1   HE1    sing N N 433 
TRP CE2   CZ2    sing Y N 434 
TRP CE3   CZ3    doub Y N 435 
TRP CE3   HE3    sing N N 436 
TRP CZ2   CH2    doub Y N 437 
TRP CZ2   HZ2    sing N N 438 
TRP CZ3   CH2    sing Y N 439 
TRP CZ3   HZ3    sing N N 440 
TRP CH2   HH2    sing N N 441 
TRP OXT   HXT    sing N N 442 
TYR N     CA     sing N N 443 
TYR N     H      sing N N 444 
TYR N     H2     sing N N 445 
TYR CA    C      sing N N 446 
TYR CA    CB     sing N N 447 
TYR CA    HA     sing N N 448 
TYR C     O      doub N N 449 
TYR C     OXT    sing N N 450 
TYR CB    CG     sing N N 451 
TYR CB    HB2    sing N N 452 
TYR CB    HB3    sing N N 453 
TYR CG    CD1    doub Y N 454 
TYR CG    CD2    sing Y N 455 
TYR CD1   CE1    sing Y N 456 
TYR CD1   HD1    sing N N 457 
TYR CD2   CE2    doub Y N 458 
TYR CD2   HD2    sing N N 459 
TYR CE1   CZ     doub Y N 460 
TYR CE1   HE1    sing N N 461 
TYR CE2   CZ     sing Y N 462 
TYR CE2   HE2    sing N N 463 
TYR CZ    OH     sing N N 464 
TYR OH    HH     sing N N 465 
TYR OXT   HXT    sing N N 466 
VAL N     CA     sing N N 467 
VAL N     H      sing N N 468 
VAL N     H2     sing N N 469 
VAL CA    C      sing N N 470 
VAL CA    CB     sing N N 471 
VAL CA    HA     sing N N 472 
VAL C     O      doub N N 473 
VAL C     OXT    sing N N 474 
VAL CB    CG1    sing N N 475 
VAL CB    CG2    sing N N 476 
VAL CB    HB     sing N N 477 
VAL CG1   HG11   sing N N 478 
VAL CG1   HG12   sing N N 479 
VAL CG1   HG13   sing N N 480 
VAL CG2   HG21   sing N N 481 
VAL CG2   HG22   sing N N 482 
VAL CG2   HG23   sing N N 483 
VAL OXT   HXT    sing N N 484 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_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   8J9B 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8K6F 
_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.fract_transf_matrix[1][1]   0.018285 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000096 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.004668 
_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]   0.012569 
_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 
H 
N 
O 
P 
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      . ALA A 1 6   ? -11.725 17.118  12.696 1.00 37.42  ? 6   ALA A N      1 
ATOM   2     C CA     . ALA A 1 6   ? -11.136 15.820  12.471 1.00 34.11  ? 6   ALA A CA     1 
ATOM   3     C C      . ALA A 1 6   ? -9.940  15.606  13.354 1.00 38.93  ? 6   ALA A C      1 
ATOM   4     O O      . ALA A 1 6   ? -8.961  16.315  13.241 1.00 36.86  ? 6   ALA A O      1 
ATOM   5     C CB     . ALA A 1 6   ? -10.769 15.648  11.021 1.00 29.29  ? 6   ALA A CB     1 
ATOM   6     N N      . ALA A 1 7   ? -9.999  14.605  14.218 1.00 42.83  ? 7   ALA A N      1 
ATOM   7     C CA     . ALA A 1 7   ? -8.934  14.353  15.165 1.00 29.20  ? 7   ALA A CA     1 
ATOM   8     C C      . ALA A 1 7   ? -7.738  13.811  14.491 1.00 33.27  ? 7   ALA A C      1 
ATOM   9     O O      . ALA A 1 7   ? -7.843  13.171  13.464 1.00 41.71  ? 7   ALA A O      1 
ATOM   10    C CB     . ALA A 1 7   ? -9.404  13.391  16.217 1.00 23.20  ? 7   ALA A CB     1 
ATOM   11    N N      . LEU A 1 8   ? -6.580  14.059  15.072 1.00 28.65  ? 8   LEU A N      1 
ATOM   12    C CA     . LEU A 1 8   ? -5.359  13.603  14.471 1.00 33.40  ? 8   LEU A CA     1 
ATOM   13    C C      . LEU A 1 8   ? -4.671  12.730  15.462 1.00 33.59  ? 8   LEU A C      1 
ATOM   14    O O      . LEU A 1 8   ? -4.665  13.044  16.628 1.00 39.64  ? 8   LEU A O      1 
ATOM   15    C CB     . LEU A 1 8   ? -4.524  14.773  14.002 1.00 34.84  ? 8   LEU A CB     1 
ATOM   16    C CG     . LEU A 1 8   ? -3.648  15.623  14.895 1.00 39.87  ? 8   LEU A CG     1 
ATOM   17    C CD1    . LEU A 1 8   ? -2.245  15.055  14.800 1.00 41.48  ? 8   LEU A CD1    1 
ATOM   18    C CD2    . LEU A 1 8   ? -3.677  17.040  14.352 1.00 45.23  ? 8   LEU A CD2    1 
ATOM   19    N N      . VAL A 1 9   ? -4.101  11.619  15.027 1.00 36.04  ? 9   VAL A N      1 
ATOM   20    C CA     . VAL A 1 9   ? -3.503  10.665  15.945 1.00 36.43  ? 9   VAL A CA     1 
ATOM   21    C C      . VAL A 1 9   ? -1.986  10.604  15.792 1.00 36.72  ? 9   VAL A C      1 
ATOM   22    O O      . VAL A 1 9   ? -1.492  10.629  14.684 1.00 36.53  ? 9   VAL A O      1 
ATOM   23    C CB     . VAL A 1 9   ? -4.111  9.283   15.691 1.00 35.30  ? 9   VAL A CB     1 
ATOM   24    C CG1    . VAL A 1 9   ? -3.659  8.300   16.752 1.00 40.13  ? 9   VAL A CG1    1 
ATOM   25    C CG2    . VAL A 1 9   ? -5.623  9.369   15.658 1.00 35.17  ? 9   VAL A CG2    1 
ATOM   26    N N      . ILE A 1 10  ? -1.238  10.538  16.889 1.00 32.60  ? 10  ILE A N      1 
ATOM   27    C CA     . ILE A 1 10  ? 0.208   10.516  16.798 1.00 32.27  ? 10  ILE A CA     1 
ATOM   28    C C      . ILE A 1 10  ? 0.853   9.459   17.646 1.00 35.46  ? 10  ILE A C      1 
ATOM   29    O O      . ILE A 1 10  ? 0.510   9.320   18.798 1.00 36.57  ? 10  ILE A O      1 
ATOM   30    C CB     . ILE A 1 10  ? 0.821   11.861  17.144 1.00 25.74  ? 10  ILE A CB     1 
ATOM   31    C CG1    . ILE A 1 10  ? 2.340   11.779  17.047 1.00 32.05  ? 10  ILE A CG1    1 
ATOM   32    C CG2    . ILE A 1 10  ? 0.386   12.312  18.523 1.00 34.63  ? 10  ILE A CG2    1 
ATOM   33    C CD1    . ILE A 1 10  ? 2.992   13.092  16.691 1.00 35.42  ? 10  ILE A CD1    1 
ATOM   34    N N      . ASP A 1 11  ? 1.769   8.685   17.067 1.00 39.35  ? 11  ASP A N      1 
ATOM   35    C CA     . ASP A 1 11  ? 2.452   7.623   17.800 1.00 42.75  ? 11  ASP A CA     1 
ATOM   36    C C      . ASP A 1 11  ? 3.820   8.101   18.032 1.00 46.61  ? 11  ASP A C      1 
ATOM   37    O O      . ASP A 1 11  ? 4.597   8.210   17.107 1.00 43.49  ? 11  ASP A O      1 
ATOM   38    C CB     . ASP A 1 11  ? 2.506   6.323   17.039 1.00 39.31  ? 11  ASP A CB     1 
ATOM   39    C CG     . ASP A 1 11  ? 2.614   5.128   17.943 1.00 42.75  ? 11  ASP A CG     1 
ATOM   40    O OD1    . ASP A 1 11  ? 2.502   5.304   19.164 1.00 45.47  ? 11  ASP A OD1    1 
ATOM   41    O OD2    . ASP A 1 11  ? 2.802   4.009   17.436 1.00 49.59  ? 11  ASP A OD2    1 
ATOM   42    N N      . ASN A 1 12  ? 4.127   8.393   19.280 1.00 51.08  ? 12  ASN A N      1 
ATOM   43    C CA     . ASN A 1 12  ? 5.405   8.919   19.638 1.00 48.66  ? 12  ASN A CA     1 
ATOM   44    C C      . ASN A 1 12  ? 6.289   7.724   19.744 1.00 49.09  ? 12  ASN A C      1 
ATOM   45    O O      . ASN A 1 12  ? 6.633   7.284   20.829 1.00 48.31  ? 12  ASN A O      1 
ATOM   46    C CB     . ASN A 1 12  ? 5.246   9.625   20.963 1.00 38.88  ? 12  ASN A CB     1 
ATOM   47    C CG     . ASN A 1 12  ? 4.268   10.771  20.892 1.00 45.87  ? 12  ASN A CG     1 
ATOM   48    O OD1    . ASN A 1 12  ? 4.666   11.917  20.770 1.00 46.83  ? 12  ASN A OD1    1 
ATOM   49    N ND2    . ASN A 1 12  ? 2.983   10.468  20.962 1.00 39.39  ? 12  ASN A ND2    1 
ATOM   50    N N      . GLY A 1 13  ? 6.637   7.169   18.607 1.00 45.56  ? 13  GLY A N      1 
ATOM   51    C CA     . GLY A 1 13  ? 7.389   5.958   18.628 1.00 43.85  ? 13  GLY A CA     1 
ATOM   52    C C      . GLY A 1 13  ? 8.829   6.178   18.835 1.00 45.03  ? 13  GLY A C      1 
ATOM   53    O O      . GLY A 1 13  ? 9.357   7.190   18.421 1.00 44.14  ? 13  GLY A O      1 
ATOM   54    N N      . SER A 1 14  ? 9.486   5.200   19.419 1.00 51.68  ? 14  SER A N      1 
ATOM   55    C CA     . SER A 1 14  ? 10.894  5.317   19.700 1.00 57.55  ? 14  SER A CA     1 
ATOM   56    C C      . SER A 1 14  ? 11.728  5.522   18.465 1.00 56.42  ? 14  SER A C      1 
ATOM   57    O O      . SER A 1 14  ? 12.712  6.242   18.486 1.00 61.95  ? 14  SER A O      1 
ATOM   58    C CB     . SER A 1 14  ? 11.347  4.070   20.422 1.00 57.40  ? 14  SER A CB     1 
ATOM   59    O OG     . SER A 1 14  ? 12.738  4.102   20.649 1.00 61.46  ? 14  SER A OG     1 
ATOM   60    N N      . GLY A 1 15  ? 11.313  4.932   17.369 1.00 52.75  ? 15  GLY A N      1 
ATOM   61    C CA     . GLY A 1 15  ? 12.091  5.017   16.159 1.00 52.41  ? 15  GLY A CA     1 
ATOM   62    C C      . GLY A 1 15  ? 11.368  5.662   15.018 1.00 52.17  ? 15  GLY A C      1 
ATOM   63    O O      . GLY A 1 15  ? 12.005  6.224   14.143 1.00 56.18  ? 15  GLY A O      1 
ATOM   64    N N      . MET A 1 16  ? 10.055  5.584   14.996 1.00 46.43  ? 16  MET A N      1 
ATOM   65    C CA     . MET A 1 16  ? 9.326   6.257   13.962 1.00 44.59  ? 16  MET A CA     1 
ATOM   66    C C      . MET A 1 16  ? 8.076   6.917   14.503 1.00 48.41  ? 16  MET A C      1 
ATOM   67    O O      . MET A 1 16  ? 7.433   6.382   15.388 1.00 47.58  ? 16  MET A O      1 
ATOM   68    C CB     . MET A 1 16  ? 8.985   5.283   12.855 1.00 44.23  ? 16  MET A CB     1 
ATOM   69    C CG     . MET A 1 16  ? 10.167  4.615   12.202 1.00 48.82  ? 16  MET A CG     1 
ATOM   70    S SD     . MET A 1 16  ? 9.580   3.479   10.948 1.00 79.04  ? 16  MET A SD     1 
ATOM   71    C CE     . MET A 1 16  ? 11.135  2.822   10.353 1.00 76.77  ? 16  MET A CE     1 
ATOM   72    N N      . CYS A 1 17  ? 7.765   8.103   14.006 1.00 51.33  ? 17  CYS A N      1 
ATOM   73    C CA     . CYS A 1 17  ? 6.604   8.822   14.446 1.00 44.01  ? 17  CYS A CA     1 
ATOM   74    C C      . CYS A 1 17  ? 5.583   8.536   13.428 1.00 45.59  ? 17  CYS A C      1 
ATOM   75    O O      . CYS A 1 17  ? 5.736   8.896   12.279 1.00 44.01  ? 17  CYS A O      1 
ATOM   76    C CB     . CYS A 1 17  ? 6.876   10.297  14.478 1.00 39.06  ? 17  CYS A CB     1 
ATOM   77    S SG     . CYS A 1 17  ? 5.659   11.248  15.399 1.00 68.52  ? 17  CYS A SG     1 
ATOM   78    N N      . LYS A 1 18  ? 4.533   7.859   13.844 1.00 45.70  ? 18  LYS A N      1 
ATOM   79    C CA     . LYS A 1 18  ? 3.506   7.452   12.940 1.00 40.68  ? 18  LYS A CA     1 
ATOM   80    C C      . LYS A 1 18  ? 2.316   8.272   13.249 1.00 36.98  ? 18  LYS A C      1 
ATOM   81    O O      . LYS A 1 18  ? 1.744   8.152   14.306 1.00 36.34  ? 18  LYS A O      1 
ATOM   82    C CB     . LYS A 1 18  ? 3.238   5.979   13.167 1.00 39.87  ? 18  LYS A CB     1 
ATOM   83    C CG     . LYS A 1 18  ? 4.446   5.116   12.866 1.00 35.50  ? 18  LYS A CG     1 
ATOM   84    C CD     . LYS A 1 18  ? 4.216   3.672   13.249 1.00 42.91  ? 18  LYS A CD     1 
ATOM   85    C CE     . LYS A 1 18  ? 4.260   3.528   14.749 1.00 47.57  ? 18  LYS A CE     1 
ATOM   86    N NZ     . LYS A 1 18  ? 5.505   4.154   15.258 1.00 42.40  ? 18  LYS A NZ     1 
ATOM   87    N N      . ALA A 1 19  ? 1.942   9.120   12.311 1.00 37.84  ? 19  ALA A N      1 
ATOM   88    C CA     . ALA A 1 19  ? 0.856   10.025  12.554 1.00 35.12  ? 19  ALA A CA     1 
ATOM   89    C C      . ALA A 1 19  ? -0.066  10.175  11.402 1.00 36.20  ? 19  ALA A C      1 
ATOM   90    O O      . ALA A 1 19  ? 0.264   9.829   10.282 1.00 36.26  ? 19  ALA A O      1 
ATOM   91    C CB     . ALA A 1 19  ? 1.415   11.369  12.904 1.00 36.57  ? 19  ALA A CB     1 
ATOM   92    N N      . GLY A 1 20  ? -1.218  10.735  11.664 1.00 31.36  ? 20  GLY A N      1 
ATOM   93    C CA     . GLY A 1 20  ? -2.178  10.862  10.638 1.00 31.64  ? 20  GLY A CA     1 
ATOM   94    C C      . GLY A 1 20  ? -3.494  11.292  11.140 1.00 30.43  ? 20  GLY A C      1 
ATOM   95    O O      . GLY A 1 20  ? -3.596  11.837  12.205 1.00 30.79  ? 20  GLY A O      1 
ATOM   96    N N      . PHE A 1 21  ? -4.523  10.970  10.402 1.00 37.57  ? 21  PHE A N      1 
ATOM   97    C CA     . PHE A 1 21  ? -5.811  11.470  10.719 1.00 43.38  ? 21  PHE A CA     1 
ATOM   98    C C      . PHE A 1 21  ? -6.735  10.358  11.066 1.00 44.12  ? 21  PHE A C      1 
ATOM   99    O O      . PHE A 1 21  ? -6.577  9.265   10.573 1.00 47.56  ? 21  PHE A O      1 
ATOM   100   C CB     . PHE A 1 21  ? -6.371  12.138  9.465  1.00 48.49  ? 21  PHE A CB     1 
ATOM   101   C CG     . PHE A 1 21  ? -5.519  13.240  8.905  1.00 47.93  ? 21  PHE A CG     1 
ATOM   102   C CD1    . PHE A 1 21  ? -5.703  14.543  9.310  1.00 49.38  ? 21  PHE A CD1    1 
ATOM   103   C CD2    . PHE A 1 21  ? -4.568  12.976  7.945  1.00 40.59  ? 21  PHE A CD2    1 
ATOM   104   C CE1    . PHE A 1 21  ? -4.934  15.556  8.789  1.00 44.48  ? 21  PHE A CE1    1 
ATOM   105   C CE2    . PHE A 1 21  ? -3.791  13.984  7.422  1.00 37.56  ? 21  PHE A CE2    1 
ATOM   106   C CZ     . PHE A 1 21  ? -3.976  15.277  7.844  1.00 40.71  ? 21  PHE A CZ     1 
ATOM   107   N N      . ALA A 1 22  ? -7.717  10.633  11.903 1.00 45.59  ? 22  ALA A N      1 
ATOM   108   C CA     . ALA A 1 22  ? -8.644  9.613   12.324 1.00 49.73  ? 22  ALA A CA     1 
ATOM   109   C C      . ALA A 1 22  ? -9.656  9.220   11.294 1.00 52.89  ? 22  ALA A C      1 
ATOM   110   O O      . ALA A 1 22  ? -10.170 10.056  10.591 1.00 66.03  ? 22  ALA A O      1 
ATOM   111   C CB     . ALA A 1 22  ? -9.336  10.064  13.563 1.00 44.32  ? 22  ALA A CB     1 
ATOM   112   N N      . GLY A 1 23  ? -9.996  7.954   11.239 1.00 44.97  ? 23  GLY A N      1 
ATOM   113   C CA     . GLY A 1 23  ? -10.926 7.467   10.253 1.00 56.74  ? 23  GLY A CA     1 
ATOM   114   C C      . GLY A 1 23  ? -10.187 6.874   9.097  1.00 70.18  ? 23  GLY A C      1 
ATOM   115   O O      . GLY A 1 23  ? -10.731 6.125   8.312  1.00 77.48  ? 23  GLY A O      1 
ATOM   116   N N      . ASP A 1 24  ? -8.929  7.188   8.982  1.00 67.87  ? 24  ASP A N      1 
ATOM   117   C CA     . ASP A 1 24  ? -8.163  6.586   7.955  1.00 61.50  ? 24  ASP A CA     1 
ATOM   118   C C      . ASP A 1 24  ? -7.720  5.339   8.635  1.00 60.51  ? 24  ASP A C      1 
ATOM   119   O O      . ASP A 1 24  ? -7.855  5.227   9.832  1.00 62.43  ? 24  ASP A O      1 
ATOM   120   C CB     . ASP A 1 24  ? -6.949  7.451   7.629  1.00 54.91  ? 24  ASP A CB     1 
ATOM   121   C CG     . ASP A 1 24  ? -7.305  8.859   7.190  1.00 63.01  ? 24  ASP A CG     1 
ATOM   122   O OD1    . ASP A 1 24  ? -6.377  9.597   6.810  1.00 72.49  ? 24  ASP A OD1    1 
ATOM   123   O OD2    . ASP A 1 24  ? -8.488  9.245   7.215  1.00 56.17  ? 24  ASP A OD2    1 
ATOM   124   N N      . ASP A 1 25  ? -7.191  4.381   7.907  1.00 59.34  ? 25  ASP A N      1 
ATOM   125   C CA     . ASP A 1 25  ? -6.636  3.191   8.514  1.00 51.36  ? 25  ASP A CA     1 
ATOM   126   C C      . ASP A 1 25  ? -5.160  3.116   8.354  1.00 46.23  ? 25  ASP A C      1 
ATOM   127   O O      . ASP A 1 25  ? -4.572  2.087   8.587  1.00 51.49  ? 25  ASP A O      1 
ATOM   128   C CB     . ASP A 1 25  ? -7.237  1.932   7.915  1.00 58.93  ? 25  ASP A CB     1 
ATOM   129   C CG     . ASP A 1 25  ? -8.260  1.288   8.816  1.00 70.13  ? 25  ASP A CG     1 
ATOM   130   O OD1    . ASP A 1 25  ? -8.710  1.940   9.782  1.00 75.98  ? 25  ASP A OD1    1 
ATOM   131   O OD2    . ASP A 1 25  ? -8.613  0.121   8.553  1.00 74.86  ? 25  ASP A OD2    1 
ATOM   132   N N      . ALA A 1 26  ? -4.539  4.164   7.896  1.00 38.77  ? 26  ALA A N      1 
ATOM   133   C CA     . ALA A 1 26  ? -3.115  4.100   7.836  1.00 37.19  ? 26  ALA A CA     1 
ATOM   134   C C      . ALA A 1 26  ? -2.430  5.389   8.110  1.00 41.51  ? 26  ALA A C      1 
ATOM   135   O O      . ALA A 1 26  ? -2.944  6.452   7.812  1.00 42.49  ? 26  ALA A O      1 
ATOM   136   C CB     . ALA A 1 26  ? -2.678  3.574   6.520  1.00 46.27  ? 26  ALA A CB     1 
ATOM   137   N N      . PRO A 1 27  ? -1.241  5.288   8.674  1.00 40.39  ? 27  PRO A N      1 
ATOM   138   C CA     . PRO A 1 27  ? -0.619  6.525   9.017  1.00 39.87  ? 27  PRO A CA     1 
ATOM   139   C C      . PRO A 1 27  ? -0.385  7.240   7.752  1.00 40.22  ? 27  PRO A C      1 
ATOM   140   O O      . PRO A 1 27  ? 0.194   6.675   6.848  1.00 42.13  ? 27  PRO A O      1 
ATOM   141   C CB     . PRO A 1 27  ? 0.689   6.057   9.573  1.00 37.46  ? 27  PRO A CB     1 
ATOM   142   C CG     . PRO A 1 27  ? 0.338   4.818   10.294 1.00 37.17  ? 27  PRO A CG     1 
ATOM   143   C CD     . PRO A 1 27  ? -0.609  4.149   9.350  1.00 39.13  ? 27  PRO A CD     1 
ATOM   144   N N      . ARG A 1 28  ? -0.828  8.474   7.659  1.00 37.65  ? 28  ARG A N      1 
ATOM   145   C CA     . ARG A 1 28  ? -0.530  9.235   6.489  1.00 40.35  ? 28  ARG A CA     1 
ATOM   146   C C      . ARG A 1 28  ? 0.938   9.487   6.454  1.00 43.48  ? 28  ARG A C      1 
ATOM   147   O O      . ARG A 1 28  ? 1.560   9.365   5.424  1.00 47.52  ? 28  ARG A O      1 
ATOM   148   C CB     . ARG A 1 28  ? -1.310  10.522  6.499  1.00 34.65  ? 28  ARG A CB     1 
ATOM   149   C CG     . ARG A 1 28  ? -2.806  10.315  6.589  1.00 40.85  ? 28  ARG A CG     1 
ATOM   150   C CD     . ARG A 1 28  ? -3.351  9.777   5.286  1.00 41.71  ? 28  ARG A CD     1 
ATOM   151   N NE     . ARG A 1 28  ? -3.168  10.737  4.210  1.00 38.14  ? 28  ARG A NE     1 
ATOM   152   C CZ     . ARG A 1 28  ? -4.081  11.628  3.855  1.00 50.71  ? 28  ARG A CZ     1 
ATOM   153   N NH1    . ARG A 1 28  ? -5.239  11.669  4.489  1.00 53.59  ? 28  ARG A NH1    1 
ATOM   154   N NH2    . ARG A 1 28  ? -3.840  12.474  2.867  1.00 53.24  ? 28  ARG A NH2    1 
ATOM   155   N N      . ALA A 1 29  ? 1.513   9.800   7.599  1.00 42.18  ? 29  ALA A N      1 
ATOM   156   C CA     . ALA A 1 29  ? 2.913   10.124  7.638  1.00 38.72  ? 29  ALA A CA     1 
ATOM   157   C C      . ALA A 1 29  ? 3.686   9.473   8.714  1.00 39.47  ? 29  ALA A C      1 
ATOM   158   O O      . ALA A 1 29  ? 3.399   9.651   9.868  1.00 35.22  ? 29  ALA A O      1 
ATOM   159   C CB     . ALA A 1 29  ? 3.080   11.590  7.754  1.00 44.82  ? 29  ALA A CB     1 
ATOM   160   N N      . VAL A 1 30  ? 4.693   8.729   8.330  1.00 45.59  ? 30  VAL A N      1 
ATOM   161   C CA     . VAL A 1 30  ? 5.555   8.031   9.251  1.00 35.44  ? 30  VAL A CA     1 
ATOM   162   C C      . VAL A 1 30  ? 6.930   8.558   8.946  1.00 35.59  ? 30  VAL A C      1 
ATOM   163   O O      . VAL A 1 30  ? 7.339   8.593   7.796  1.00 40.33  ? 30  VAL A O      1 
ATOM   164   C CB     . VAL A 1 30  ? 5.597   6.547   8.920  1.00 34.25  ? 30  VAL A CB     1 
ATOM   165   C CG1    . VAL A 1 30  ? 6.495   5.799   9.882  1.00 46.02  ? 30  VAL A CG1    1 
ATOM   166   C CG2    . VAL A 1 30  ? 4.209   5.950   8.891  1.00 37.98  ? 30  VAL A CG2    1 
ATOM   167   N N      . PHE A 1 31  ? 7.659   8.964   9.966  1.00 38.53  ? 31  PHE A N      1 
ATOM   168   C CA     . PHE A 1 31  ? 8.996   9.445   9.761  1.00 43.94  ? 31  PHE A CA     1 
ATOM   169   C C      . PHE A 1 31  ? 9.830   9.124   10.964 1.00 43.86  ? 31  PHE A C      1 
ATOM   170   O O      . PHE A 1 31  ? 9.313   8.926   12.033 1.00 43.06  ? 31  PHE A O      1 
ATOM   171   C CB     . PHE A 1 31  ? 9.003   10.941  9.448  1.00 50.27  ? 31  PHE A CB     1 
ATOM   172   C CG     . PHE A 1 31  ? 8.492   11.825  10.552 1.00 48.07  ? 31  PHE A CG     1 
ATOM   173   C CD1    . PHE A 1 31  ? 7.142   12.060  10.706 1.00 43.68  ? 31  PHE A CD1    1 
ATOM   174   C CD2    . PHE A 1 31  ? 9.371   12.472  11.394 1.00 46.69  ? 31  PHE A CD2    1 
ATOM   175   C CE1    . PHE A 1 31  ? 6.679   12.884  11.704 1.00 41.60  ? 31  PHE A CE1    1 
ATOM   176   C CE2    . PHE A 1 31  ? 8.917   13.297  12.393 1.00 41.32  ? 31  PHE A CE2    1 
ATOM   177   C CZ     . PHE A 1 31  ? 7.569   13.504  12.548 1.00 40.69  ? 31  PHE A CZ     1 
ATOM   178   N N      . PRO A 1 32  ? 11.162  9.049   10.783 1.00 48.53  ? 32  PRO A N      1 
ATOM   179   C CA     . PRO A 1 32  ? 11.916  8.802   11.992 1.00 50.41  ? 32  PRO A CA     1 
ATOM   180   C C      . PRO A 1 32  ? 11.888  9.888   13.005 1.00 48.44  ? 32  PRO A C      1 
ATOM   181   O O      . PRO A 1 32  ? 11.945  11.047  12.659 1.00 51.39  ? 32  PRO A O      1 
ATOM   182   C CB     . PRO A 1 32  ? 13.327  8.696   11.473 1.00 56.61  ? 32  PRO A CB     1 
ATOM   183   C CG     . PRO A 1 32  ? 13.175  8.086   10.141 1.00 59.29  ? 32  PRO A CG     1 
ATOM   184   C CD     . PRO A 1 32  ? 12.035  8.874   9.599  1.00 55.55  ? 32  PRO A CD     1 
ATOM   185   N N      . SER A 1 33  ? 11.864  9.512   14.266 1.00 45.85  ? 33  SER A N      1 
ATOM   186   C CA     . SER A 1 33  ? 11.859  10.466  15.331 1.00 43.57  ? 33  SER A CA     1 
ATOM   187   C C      . SER A 1 33  ? 13.253  10.852  15.652 1.00 48.83  ? 33  SER A C      1 
ATOM   188   O O      . SER A 1 33  ? 13.744  10.527  16.714 1.00 50.46  ? 33  SER A O      1 
ATOM   189   C CB     . SER A 1 33  ? 11.246  9.847   16.567 1.00 44.91  ? 33  SER A CB     1 
ATOM   190   O OG     . SER A 1 33  ? 11.918  8.662   16.933 1.00 59.58  ? 33  SER A OG     1 
ATOM   191   N N      . ILE A 1 34  ? 13.916  11.549  14.741 1.00 53.10  ? 34  ILE A N      1 
ATOM   192   C CA     . ILE A 1 34  ? 15.253  12.052  15.012 1.00 51.03  ? 34  ILE A CA     1 
ATOM   193   C C      . ILE A 1 34  ? 15.325  13.526  14.686 1.00 51.43  ? 34  ILE A C      1 
ATOM   194   O O      . ILE A 1 34  ? 14.682  13.986  13.764 1.00 56.85  ? 34  ILE A O      1 
ATOM   195   C CB     . ILE A 1 34  ? 16.331  11.300  14.235 1.00 53.58  ? 34  ILE A CB     1 
ATOM   196   C CG1    . ILE A 1 34  ? 16.249  11.582  12.750 1.00 55.28  ? 34  ILE A CG1    1 
ATOM   197   C CG2    . ILE A 1 34  ? 16.211  9.805   14.440 1.00 59.92  ? 34  ILE A CG2    1 
ATOM   198   C CD1    . ILE A 1 34  ? 17.471  11.090  12.028 1.00 60.71  ? 34  ILE A CD1    1 
ATOM   199   N N      . VAL A 1 35  ? 16.046  14.292  15.480 1.00 49.60  ? 35  VAL A N      1 
ATOM   200   C CA     . VAL A 1 35  ? 16.131  15.717  15.266 1.00 51.68  ? 35  VAL A CA     1 
ATOM   201   C C      . VAL A 1 35  ? 17.569  16.115  15.182 1.00 55.93  ? 35  VAL A C      1 
ATOM   202   O O      . VAL A 1 35  ? 18.377  15.692  15.985 1.00 54.11  ? 35  VAL A O      1 
ATOM   203   C CB     . VAL A 1 35  ? 15.539  16.499  16.426 1.00 47.65  ? 35  VAL A CB     1 
ATOM   204   C CG1    . VAL A 1 35  ? 15.237  17.924  16.005 1.00 55.64  ? 35  VAL A CG1    1 
ATOM   205   C CG2    . VAL A 1 35  ? 14.294  15.829  16.962 1.00 46.71  ? 35  VAL A CG2    1 
ATOM   206   N N      . GLY A 1 36  ? 17.897  16.937  14.209 1.00 66.45  ? 36  GLY A N      1 
ATOM   207   C CA     . GLY A 1 36  ? 19.270  17.310  14.017 1.00 67.98  ? 36  GLY A CA     1 
ATOM   208   C C      . GLY A 1 36  ? 19.542  18.769  14.175 1.00 68.39  ? 36  GLY A C      1 
ATOM   209   O O      . GLY A 1 36  ? 18.704  19.597  13.867 1.00 71.60  ? 36  GLY A O      1 
ATOM   210   N N      . ARG A 1 37  ? 20.708  19.084  14.690 1.00 66.39  ? 37  ARG A N      1 
ATOM   211   C CA     . ARG A 1 37  ? 21.074  20.440  14.886 1.00 65.67  ? 37  ARG A CA     1 
ATOM   212   C C      . ARG A 1 37  ? 22.422  20.402  14.267 1.00 65.58  ? 37  ARG A C      1 
ATOM   213   O O      . ARG A 1 37  ? 23.096  19.390  14.333 1.00 69.05  ? 37  ARG A O      1 
ATOM   214   C CB     . ARG A 1 37  ? 21.180  20.691  16.369 1.00 65.40  ? 37  ARG A CB     1 
ATOM   215   C CG     . ARG A 1 37  ? 19.922  20.346  17.142 1.00 69.05  ? 37  ARG A CG     1 
ATOM   216   C CD     . ARG A 1 37  ? 20.060  20.667  18.617 1.00 76.04  ? 37  ARG A CD     1 
ATOM   217   N NE     . ARG A 1 37  ? 18.798  20.471  19.318 1.00 79.80  ? 37  ARG A NE     1 
ATOM   218   C CZ     . ARG A 1 37  ? 17.865  21.406  19.441 1.00 69.23  ? 37  ARG A CZ     1 
ATOM   219   N NH1    . ARG A 1 37  ? 18.050  22.605  18.910 1.00 58.78  ? 37  ARG A NH1    1 
ATOM   220   N NH2    . ARG A 1 37  ? 16.747  21.144  20.098 1.00 66.46  ? 37  ARG A NH2    1 
ATOM   221   N N      . PRO A 1 38  ? 22.839  21.492  13.589 1.00 60.65  ? 38  PRO A N      1 
ATOM   222   C CA     . PRO A 1 38  ? 24.129  21.310  12.944 1.00 60.78  ? 38  PRO A CA     1 
ATOM   223   C C      . PRO A 1 38  ? 25.247  21.048  13.919 1.00 62.59  ? 38  PRO A C      1 
ATOM   224   O O      . PRO A 1 38  ? 25.124  21.291  15.113 1.00 64.19  ? 38  PRO A O      1 
ATOM   225   C CB     . PRO A 1 38  ? 24.329  22.617  12.195 1.00 54.52  ? 38  PRO A CB     1 
ATOM   226   C CG     . PRO A 1 38  ? 22.963  23.141  11.975 1.00 50.88  ? 38  PRO A CG     1 
ATOM   227   C CD     . PRO A 1 38  ? 22.297  22.832  13.271 1.00 55.89  ? 38  PRO A CD     1 
ATOM   228   N N      . ARG A 1 39  ? 26.355  20.549  13.414 1.00 59.44  ? 39  ARG A N      1 
ATOM   229   C CA     . ARG A 1 39  ? 27.483  20.297  14.262 1.00 63.98  ? 39  ARG A CA     1 
ATOM   230   C C      . ARG A 1 39  ? 28.330  21.522  14.245 1.00 65.53  ? 39  ARG A C      1 
ATOM   231   O O      . ARG A 1 39  ? 28.716  22.023  15.290 1.00 70.01  ? 39  ARG A O      1 
ATOM   232   C CB     . ARG A 1 39  ? 28.274  19.153  13.687 1.00 68.90  ? 39  ARG A CB     1 
ATOM   233   C CG     . ARG A 1 39  ? 29.185  18.436  14.661 1.00 74.82  ? 39  ARG A CG     1 
ATOM   234   C CD     . ARG A 1 39  ? 29.810  17.241  13.969 1.00 81.37  ? 39  ARG A CD     1 
ATOM   235   N NE     . ARG A 1 39  ? 28.793  16.336  13.446 1.00 78.95  ? 39  ARG A NE     1 
ATOM   236   C CZ     . ARG A 1 39  ? 29.044  15.322  12.628 1.00 68.28  ? 39  ARG A CZ     1 
ATOM   237   N NH1    . ARG A 1 39  ? 30.282  15.090  12.223 1.00 57.66  ? 39  ARG A NH1    1 
ATOM   238   N NH2    . ARG A 1 39  ? 28.056  14.549  12.208 1.00 66.53  ? 39  ARG A NH2    1 
ATOM   239   N N      . HIS A 1 40  ? 28.619  22.017  13.052 1.00 71.47  ? 40  HIS A N      1 
ATOM   240   C CA     . HIS A 1 40  ? 29.425  23.226  12.921 1.00 74.99  ? 40  HIS A CA     1 
ATOM   241   C C      . HIS A 1 40  ? 28.568  24.388  12.467 1.00 69.15  ? 40  HIS A C      1 
ATOM   242   O O      . HIS A 1 40  ? 27.561  24.193  11.812 1.00 72.50  ? 40  HIS A O      1 
ATOM   243   C CB     . HIS A 1 40  ? 30.586  23.014  11.951 1.00 73.36  ? 40  HIS A CB     1 
ATOM   244   C CG     . HIS A 1 40  ? 31.515  21.913  12.348 1.00 79.45  ? 40  HIS A CG     1 
ATOM   245   N ND1    . HIS A 1 40  ? 31.813  20.857  11.517 1.00 79.41  ? 40  HIS A ND1    1 
ATOM   246   C CD2    . HIS A 1 40  ? 32.208  21.702  13.491 1.00 74.04  ? 40  HIS A CD2    1 
ATOM   247   C CE1    . HIS A 1 40  ? 32.654  20.043  12.129 1.00 76.00  ? 40  HIS A CE1    1 
ATOM   248   N NE2    . HIS A 1 40  ? 32.908  20.533  13.329 1.00 82.69  ? 40  HIS A NE2    1 
ATOM   249   N N      . GLN A 1 41  ? 28.970  25.610  12.788 1.00 59.16  ? 41  GLN A N      1 
ATOM   250   C CA     . GLN A 1 41  ? 28.150  26.775  12.480 1.00 59.63  ? 41  GLN A CA     1 
ATOM   251   C C      . GLN A 1 41  ? 28.156  27.221  11.046 1.00 62.84  ? 41  GLN A C      1 
ATOM   252   O O      . GLN A 1 41  ? 27.381  28.077  10.665 1.00 62.76  ? 41  GLN A O      1 
ATOM   253   C CB     . GLN A 1 41  ? 28.568  27.929  13.375 1.00 53.70  ? 41  GLN A CB     1 
ATOM   254   C CG     . GLN A 1 41  ? 28.231  27.704  14.836 1.00 65.03  ? 41  GLN A CG     1 
ATOM   255   C CD     . GLN A 1 41  ? 28.747  28.810  15.722 1.00 55.38  ? 41  GLN A CD     1 
ATOM   256   O OE1    . GLN A 1 41  ? 29.469  29.682  15.266 1.00 48.49  ? 41  GLN A OE1    1 
ATOM   257   N NE2    . GLN A 1 41  ? 28.384  28.777  16.993 1.00 49.47  ? 41  GLN A NE2    1 
ATOM   258   N N      . GLY A 1 42  ? 29.009  26.646  10.229 1.00 64.22  ? 42  GLY A N      1 
ATOM   259   C CA     . GLY A 1 42  ? 29.108  27.075  8.852  1.00 60.04  ? 42  GLY A CA     1 
ATOM   260   C C      . GLY A 1 42  ? 27.894  26.709  8.041  1.00 62.65  ? 42  GLY A C      1 
ATOM   261   O O      . GLY A 1 42  ? 27.599  27.336  7.042  1.00 63.72  ? 42  GLY A O      1 
ATOM   262   N N      . VAL A 1 43  ? 27.159  25.702  8.467  1.00 63.03  ? 43  VAL A N      1 
ATOM   263   C CA     . VAL A 1 43  ? 26.024  25.265  7.690  1.00 60.77  ? 43  VAL A CA     1 
ATOM   264   C C      . VAL A 1 43  ? 24.975  26.296  7.856  1.00 65.63  ? 43  VAL A C      1 
ATOM   265   O O      . VAL A 1 43  ? 24.419  26.777  6.880  1.00 63.50  ? 43  VAL A O      1 
ATOM   266   C CB     . VAL A 1 43  ? 25.447  23.978  8.257  1.00 64.56  ? 43  VAL A CB     1 
ATOM   267   C CG1    . VAL A 1 43  ? 24.336  23.459  7.367  1.00 58.52  ? 43  VAL A CG1    1 
ATOM   268   C CG2    . VAL A 1 43  ? 26.541  22.938  8.413  1.00 69.81  ? 43  VAL A CG2    1 
ATOM   269   N N      . MET A 1 44  ? 24.720  26.667  9.100  1.00 71.67  ? 44  MET A N      1 
ATOM   270   C CA     . MET A 1 44  ? 23.651  27.610  9.398  1.00 67.12  ? 44  MET A CA     1 
ATOM   271   C C      . MET A 1 44  ? 23.844  28.927  8.708  1.00 63.35  ? 44  MET A C      1 
ATOM   272   O O      . MET A 1 44  ? 22.916  29.708  8.589  1.00 62.07  ? 44  MET A O      1 
ATOM   273   C CB     . MET A 1 44  ? 23.576  27.828  10.905 1.00 53.28  ? 44  MET A CB     1 
ATOM   274   C CG     . MET A 1 44  ? 24.102  26.672  11.719 1.00 59.78  ? 44  MET A CG     1 
ATOM   275   S SD     . MET A 1 44  ? 23.752  26.966  13.449 1.00 77.85  ? 44  MET A SD     1 
ATOM   276   C CE     . MET A 1 44  ? 22.029  27.409  13.324 1.00 59.18  ? 44  MET A CE     1 
ATOM   277   N N      . VAL A 1 45  ? 25.036  29.148  8.200  1.00 59.34  ? 45  VAL A N      1 
ATOM   278   C CA     . VAL A 1 45  ? 25.332  30.393  7.568  1.00 55.08  ? 45  VAL A CA     1 
ATOM   279   C C      . VAL A 1 45  ? 24.429  30.566  6.408  1.00 59.03  ? 45  VAL A C      1 
ATOM   280   O O      . VAL A 1 45  ? 24.535  29.858  5.428  1.00 69.59  ? 45  VAL A O      1 
ATOM   281   C CB     . VAL A 1 45  ? 26.784  30.448  7.129  1.00 54.22  ? 45  VAL A CB     1 
ATOM   282   C CG1    . VAL A 1 45  ? 27.029  31.645  6.238  1.00 55.84  ? 45  VAL A CG1    1 
ATOM   283   C CG2    . VAL A 1 45  ? 27.683  30.514  8.346  1.00 54.57  ? 45  VAL A CG2    1 
ATOM   284   N N      . GLY A 1 46  ? 23.506  31.491  6.518  1.00 55.52  ? 46  GLY A N      1 
ATOM   285   C CA     . GLY A 1 46  ? 22.634  31.809  5.414  1.00 61.78  ? 46  GLY A CA     1 
ATOM   286   C C      . GLY A 1 46  ? 21.277  31.202  5.395  1.00 62.53  ? 46  GLY A C      1 
ATOM   287   O O      . GLY A 1 46  ? 20.395  31.653  4.677  1.00 61.87  ? 46  GLY A O      1 
ATOM   288   N N      . MET A 1 47  ? 21.087  30.197  6.209  1.00 67.90  ? 47  MET A N      1 
ATOM   289   C CA     . MET A 1 47  ? 19.810  29.543  6.262  1.00 70.74  ? 47  MET A CA     1 
ATOM   290   C C      . MET A 1 47  ? 18.935  30.358  7.142  1.00 68.92  ? 47  MET A C      1 
ATOM   291   O O      . MET A 1 47  ? 19.411  31.273  7.775  1.00 71.24  ? 47  MET A O      1 
ATOM   292   C CB     . MET A 1 47  ? 19.964  28.125  6.755  1.00 76.86  ? 47  MET A CB     1 
ATOM   293   C CG     . MET A 1 47  ? 20.772  27.277  5.803  1.00 71.85  ? 47  MET A CG     1 
ATOM   294   S SD     . MET A 1 47  ? 20.921  25.590  6.378  1.00 95.47  ? 47  MET A SD     1 
ATOM   295   C CE     . MET A 1 47  ? 21.751  24.870  4.965  1.00 81.46  ? 47  MET A CE     1 
ATOM   296   N N      . GLY A 1 48  ? 17.654  30.052  7.162  1.00 63.35  ? 48  GLY A N      1 
ATOM   297   C CA     . GLY A 1 48  ? 16.723  30.858  7.906  1.00 73.85  ? 48  GLY A CA     1 
ATOM   298   C C      . GLY A 1 48  ? 16.265  30.272  9.198  1.00 80.44  ? 48  GLY A C      1 
ATOM   299   O O      . GLY A 1 48  ? 15.300  29.521  9.219  1.00 86.71  ? 48  GLY A O      1 
ATOM   300   N N      . GLN A 1 49  ? 16.970  30.582  10.269 1.00 83.57  ? 49  GLN A N      1 
ATOM   301   C CA     . GLN A 1 49  ? 16.615  30.086  11.591 1.00 89.60  ? 49  GLN A CA     1 
ATOM   302   C C      . GLN A 1 49  ? 16.510  28.571  11.573 1.00 100.85 ? 49  GLN A C      1 
ATOM   303   O O      . GLN A 1 49  ? 15.697  27.994  12.286 1.00 105.90 ? 49  GLN A O      1 
ATOM   304   C CB     . GLN A 1 49  ? 15.362  30.768  12.119 1.00 87.83  ? 49  GLN A CB     1 
ATOM   305   C CG     . GLN A 1 49  ? 15.377  31.013  13.616 1.00 90.16  ? 49  GLN A CG     1 
ATOM   306   C CD     . GLN A 1 49  ? 16.553  31.857  14.055 1.00 88.31  ? 49  GLN A CD     1 
ATOM   307   O OE1    . GLN A 1 49  ? 16.885  32.861  13.425 1.00 74.86  ? 49  GLN A OE1    1 
ATOM   308   N NE2    . GLN A 1 49  ? 17.186  31.457  15.151 1.00 87.65  ? 49  GLN A NE2    1 
ATOM   309   N N      . LYS A 1 50  ? 17.373  27.918  10.801 1.00 97.28  ? 50  LYS A N      1 
ATOM   310   C CA     . LYS A 1 50  ? 17.289  26.478  10.656 1.00 93.42  ? 50  LYS A CA     1 
ATOM   311   C C      . LYS A 1 50  ? 18.334  25.847  11.523 1.00 93.96  ? 50  LYS A C      1 
ATOM   312   O O      . LYS A 1 50  ? 19.337  25.344  11.031 1.00 97.21  ? 50  LYS A O      1 
ATOM   313   C CB     . LYS A 1 50  ? 17.507  26.072  9.201  1.00 82.63  ? 50  LYS A CB     1 
ATOM   314   C CG     . LYS A 1 50  ? 16.914  24.735  8.808  1.00 76.61  ? 50  LYS A CG     1 
ATOM   315   C CD     . LYS A 1 50  ? 15.402  24.772  8.828  1.00 74.62  ? 50  LYS A CD     1 
ATOM   316   C CE     . LYS A 1 50  ? 14.839  23.473  8.293  1.00 69.30  ? 50  LYS A CE     1 
ATOM   317   N NZ     . LYS A 1 50  ? 13.356  23.453  8.328  1.00 75.95  ? 50  LYS A NZ     1 
ATOM   318   N N      . ASP A 1 51  ? 18.104  25.871  12.823 1.00 89.19  ? 51  ASP A N      1 
ATOM   319   C CA     . ASP A 1 51  ? 19.047  25.277  13.729 1.00 87.72  ? 51  ASP A CA     1 
ATOM   320   C C      . ASP A 1 51  ? 18.569  23.891  13.830 1.00 84.58  ? 51  ASP A C      1 
ATOM   321   O O      . ASP A 1 51  ? 19.151  23.092  14.536 1.00 80.61  ? 51  ASP A O      1 
ATOM   322   C CB     . ASP A 1 51  ? 18.976  25.922  15.107 1.00 88.87  ? 51  ASP A CB     1 
ATOM   323   C CG     . ASP A 1 51  ? 17.579  25.880  15.724 1.00 94.78  ? 51  ASP A CG     1 
ATOM   324   O OD1    . ASP A 1 51  ? 16.569  25.906  14.989 1.00 97.43  ? 51  ASP A OD1    1 
ATOM   325   O OD2    . ASP A 1 51  ? 17.492  25.847  16.969 1.00 84.26  ? 51  ASP A OD2    1 
ATOM   326   N N      . SER A 1 52  ? 17.468  23.602  13.156 1.00 82.18  ? 52  SER A N      1 
ATOM   327   C CA     . SER A 1 52  ? 16.906  22.283  13.280 1.00 79.05  ? 52  SER A CA     1 
ATOM   328   C C      . SER A 1 52  ? 16.379  21.647  12.039 1.00 71.91  ? 52  SER A C      1 
ATOM   329   O O      . SER A 1 52  ? 15.462  22.155  11.419 1.00 76.81  ? 52  SER A O      1 
ATOM   330   C CB     . SER A 1 52  ? 15.795  22.331  14.307 1.00 80.21  ? 52  SER A CB     1 
ATOM   331   O OG     . SER A 1 52  ? 15.126  23.571  14.249 1.00 81.48  ? 52  SER A OG     1 
ATOM   332   N N      . TYR A 1 53  ? 16.940  20.509  11.682 1.00 66.49  ? 53  TYR A N      1 
ATOM   333   C CA     . TYR A 1 53  ? 16.424  19.770  10.570 1.00 67.24  ? 53  TYR A CA     1 
ATOM   334   C C      . TYR A 1 53  ? 15.891  18.548  11.276 1.00 69.07  ? 53  TYR A C      1 
ATOM   335   O O      . TYR A 1 53  ? 16.610  17.945  12.047 1.00 68.26  ? 53  TYR A O      1 
ATOM   336   C CB     . TYR A 1 53  ? 17.563  19.379  9.667  1.00 64.81  ? 53  TYR A CB     1 
ATOM   337   C CG     . TYR A 1 53  ? 17.985  20.369  8.625  1.00 62.83  ? 53  TYR A CG     1 
ATOM   338   C CD1    . TYR A 1 53  ? 17.205  20.593  7.512  1.00 69.28  ? 53  TYR A CD1    1 
ATOM   339   C CD2    . TYR A 1 53  ? 19.197  21.028  8.719  1.00 61.40  ? 53  TYR A CD2    1 
ATOM   340   C CE1    . TYR A 1 53  ? 17.596  21.479  6.536  1.00 77.49  ? 53  TYR A CE1    1 
ATOM   341   C CE2    . TYR A 1 53  ? 19.599  21.917  7.746  1.00 69.29  ? 53  TYR A CE2    1 
ATOM   342   C CZ     . TYR A 1 53  ? 18.790  22.136  6.656  1.00 77.31  ? 53  TYR A CZ     1 
ATOM   343   O OH     . TYR A 1 53  ? 19.164  23.016  5.675  1.00 76.52  ? 53  TYR A OH     1 
ATOM   344   N N      . VAL A 1 54  ? 14.653  18.142  11.016 1.00 65.06  ? 54  VAL A N      1 
ATOM   345   C CA     . VAL A 1 54  ? 14.037  17.009  11.710 1.00 59.12  ? 54  VAL A CA     1 
ATOM   346   C C      . VAL A 1 54  ? 13.634  15.900  10.749 1.00 60.85  ? 54  VAL A C      1 
ATOM   347   O O      . VAL A 1 54  ? 13.492  16.151  9.566  1.00 62.36  ? 54  VAL A O      1 
ATOM   348   C CB     . VAL A 1 54  ? 12.770  17.475  12.451 1.00 56.15  ? 54  VAL A CB     1 
ATOM   349   C CG1    . VAL A 1 54  ? 12.400  16.541  13.582 1.00 55.63  ? 54  VAL A CG1    1 
ATOM   350   C CG2    . VAL A 1 54  ? 12.937  18.885  12.985 1.00 60.98  ? 54  VAL A CG2    1 
ATOM   351   N N      . GLY A 1 55  ? 13.462  14.675  11.225 1.00 55.49  ? 55  GLY A N      1 
ATOM   352   C CA     . GLY A 1 55  ? 12.968  13.598  10.379 1.00 53.00  ? 55  GLY A CA     1 
ATOM   353   C C      . GLY A 1 55  ? 13.883  13.019  9.341  1.00 56.00  ? 55  GLY A C      1 
ATOM   354   O O      . GLY A 1 55  ? 15.040  12.774  9.607  1.00 56.91  ? 55  GLY A O      1 
ATOM   355   N N      . ASP A 1 56  ? 13.355  12.727  8.161  1.00 56.21  ? 56  ASP A N      1 
ATOM   356   C CA     . ASP A 1 56  ? 14.151  12.094  7.117  1.00 58.99  ? 56  ASP A CA     1 
ATOM   357   C C      . ASP A 1 56  ? 15.048  13.111  6.538  1.00 61.18  ? 56  ASP A C      1 
ATOM   358   O O      . ASP A 1 56  ? 15.984  12.778  5.841  1.00 60.48  ? 56  ASP A O      1 
ATOM   359   C CB     . ASP A 1 56  ? 13.275  11.500  6.026  1.00 56.73  ? 56  ASP A CB     1 
ATOM   360   C CG     . ASP A 1 56  ? 12.931  10.050  6.276  1.00 66.37  ? 56  ASP A CG     1 
ATOM   361   O OD1    . ASP A 1 56  ? 13.834  9.288   6.672  1.00 70.20  ? 56  ASP A OD1    1 
ATOM   362   O OD2    . ASP A 1 56  ? 11.765  9.666   6.059  1.00 64.52  ? 56  ASP A OD2    1 
ATOM   363   N N      . GLU A 1 57  ? 14.786  14.367  6.813  1.00 61.82  ? 57  GLU A N      1 
ATOM   364   C CA     . GLU A 1 57  ? 15.687  15.407  6.361  1.00 65.71  ? 57  GLU A CA     1 
ATOM   365   C C      . GLU A 1 57  ? 16.958  15.302  7.173  1.00 64.25  ? 57  GLU A C      1 
ATOM   366   O O      . GLU A 1 57  ? 18.040  15.445  6.641  1.00 63.88  ? 57  GLU A O      1 
ATOM   367   C CB     . GLU A 1 57  ? 15.024  16.762  6.561  1.00 70.92  ? 57  GLU A CB     1 
ATOM   368   C CG     . GLU A 1 57  ? 15.443  17.853  5.603  1.00 62.22  ? 57  GLU A CG     1 
ATOM   369   C CD     . GLU A 1 57  ? 14.590  19.088  5.774  1.00 60.82  ? 57  GLU A CD     1 
ATOM   370   O OE1    . GLU A 1 57  ? 13.709  19.072  6.657  1.00 56.45  ? 57  GLU A OE1    1 
ATOM   371   O OE2    . GLU A 1 57  ? 14.795  20.068  5.034  1.00 69.88  ? 57  GLU A OE2    1 
ATOM   372   N N      . ALA A 1 58  ? 16.845  15.008  8.453  1.00 54.69  ? 58  ALA A N      1 
ATOM   373   C CA     . ALA A 1 58  ? 18.009  14.870  9.286  1.00 56.07  ? 58  ALA A CA     1 
ATOM   374   C C      . ALA A 1 58  ? 18.741  13.600  9.003  1.00 65.74  ? 58  ALA A C      1 
ATOM   375   O O      . ALA A 1 58  ? 19.948  13.551  9.158  1.00 68.24  ? 58  ALA A O      1 
ATOM   376   C CB     . ALA A 1 58  ? 17.618  14.907  10.714 1.00 58.25  ? 58  ALA A CB     1 
ATOM   377   N N      . GLN A 1 59  ? 18.052  12.552  8.589  1.00 61.78  ? 59  GLN A N      1 
ATOM   378   C CA     . GLN A 1 59  ? 18.758  11.346  8.208  1.00 58.53  ? 59  GLN A CA     1 
ATOM   379   C C      . GLN A 1 59  ? 19.513  11.670  6.979  1.00 59.49  ? 59  GLN A C      1 
ATOM   380   O O      . GLN A 1 59  ? 20.630  11.242  6.795  1.00 62.10  ? 59  GLN A O      1 
ATOM   381   C CB     . GLN A 1 59  ? 17.812  10.226  7.843  1.00 65.74  ? 59  GLN A CB     1 
ATOM   382   C CG     . GLN A 1 59  ? 17.130  9.499   8.991  1.00 71.68  ? 59  GLN A CG     1 
ATOM   383   C CD     . GLN A 1 59  ? 18.010  8.471   9.684  1.00 69.26  ? 59  GLN A CD     1 
ATOM   384   O OE1    . GLN A 1 59  ? 19.230  8.461   9.530  1.00 67.55  ? 59  GLN A OE1    1 
ATOM   385   N NE2    . GLN A 1 59  ? 17.386  7.601   10.466 1.00 59.50  ? 59  GLN A NE2    1 
ATOM   386   N N      . SER A 1 60  ? 18.882  12.399  6.089  1.00 60.01  ? 60  SER A N      1 
ATOM   387   C CA     . SER A 1 60  ? 19.523  12.727  4.846  1.00 60.97  ? 60  SER A CA     1 
ATOM   388   C C      . SER A 1 60  ? 20.774  13.460  5.185  1.00 68.09  ? 60  SER A C      1 
ATOM   389   O O      . SER A 1 60  ? 21.869  13.019  4.850  1.00 66.28  ? 60  SER A O      1 
ATOM   390   C CB     . SER A 1 60  ? 18.620  13.619  4.015  1.00 65.69  ? 60  SER A CB     1 
ATOM   391   O OG     . SER A 1 60  ? 19.342  14.225  2.959  1.00 77.66  ? 60  SER A OG     1 
ATOM   392   N N      . LYS A 1 61  ? 20.635  14.560  5.906  1.00 67.14  ? 61  LYS A N      1 
ATOM   393   C CA     . LYS A 1 61  ? 21.771  15.389  6.241  1.00 59.12  ? 61  LYS A CA     1 
ATOM   394   C C      . LYS A 1 61  ? 22.403  14.966  7.531  1.00 60.14  ? 61  LYS A C      1 
ATOM   395   O O      . LYS A 1 61  ? 22.614  15.758  8.414  1.00 65.55  ? 61  LYS A O      1 
ATOM   396   C CB     . LYS A 1 61  ? 21.297  16.822  6.316  1.00 53.40  ? 61  LYS A CB     1 
ATOM   397   C CG     . LYS A 1 61  ? 20.816  17.356  4.984  1.00 57.82  ? 61  LYS A CG     1 
ATOM   398   C CD     . LYS A 1 61  ? 19.638  18.302  5.130  1.00 70.22  ? 61  LYS A CD     1 
ATOM   399   C CE     . LYS A 1 61  ? 19.126  18.712  3.758  1.00 76.55  ? 61  LYS A CE     1 
ATOM   400   N NZ     . LYS A 1 61  ? 17.879  19.518  3.806  1.00 68.18  ? 61  LYS A NZ     1 
ATOM   401   N N      . ARG A 1 62  ? 22.706  13.698  7.646  1.00 62.55  ? 62  ARG A N      1 
ATOM   402   C CA     . ARG A 1 62  ? 23.327  13.197  8.846  1.00 66.83  ? 62  ARG A CA     1 
ATOM   403   C C      . ARG A 1 62  ? 24.687  13.756  9.104  1.00 66.35  ? 62  ARG A C      1 
ATOM   404   O O      . ARG A 1 62  ? 25.023  14.082  10.223 1.00 69.88  ? 62  ARG A O      1 
ATOM   405   C CB     . ARG A 1 62  ? 23.511  11.692  8.714  1.00 71.45  ? 62  ARG A CB     1 
ATOM   406   C CG     . ARG A 1 62  ? 22.514  10.845  9.473  1.00 64.55  ? 62  ARG A CG     1 
ATOM   407   C CD     . ARG A 1 62  ? 22.793  9.366   9.277  1.00 62.52  ? 62  ARG A CD     1 
ATOM   408   N NE     . ARG A 1 62  ? 22.018  8.785   8.184  1.00 78.11  ? 62  ARG A NE     1 
ATOM   409   C CZ     . ARG A 1 62  ? 22.469  8.615   6.947  1.00 86.78  ? 62  ARG A CZ     1 
ATOM   410   N NH1    . ARG A 1 62  ? 23.701  8.981   6.632  1.00 79.27  ? 62  ARG A NH1    1 
ATOM   411   N NH2    . ARG A 1 62  ? 21.686  8.077   6.024  1.00 90.39  ? 62  ARG A NH2    1 
ATOM   412   N N      . GLY A 1 63  ? 25.503  13.846  8.081  1.00 61.54  ? 63  GLY A N      1 
ATOM   413   C CA     . GLY A 1 63  ? 26.862  14.266  8.309  1.00 58.86  ? 63  GLY A CA     1 
ATOM   414   C C      . GLY A 1 63  ? 26.973  15.660  8.822  1.00 70.56  ? 63  GLY A C      1 
ATOM   415   O O      . GLY A 1 63  ? 27.733  15.913  9.741  1.00 73.41  ? 63  GLY A O      1 
ATOM   416   N N      . ILE A 1 64  ? 26.197  16.572  8.254  1.00 69.09  ? 64  ILE A N      1 
ATOM   417   C CA     . ILE A 1 64  ? 26.217  17.959  8.686  1.00 59.09  ? 64  ILE A CA     1 
ATOM   418   C C      . ILE A 1 64  ? 25.560  18.184  10.044 1.00 57.32  ? 64  ILE A C      1 
ATOM   419   O O      . ILE A 1 64  ? 25.730  19.231  10.638 1.00 58.89  ? 64  ILE A O      1 
ATOM   420   C CB     . ILE A 1 64  ? 25.643  18.884  7.617  1.00 46.19  ? 64  ILE A CB     1 
ATOM   421   C CG1    . ILE A 1 64  ? 24.125  18.851  7.602  1.00 52.49  ? 64  ILE A CG1    1 
ATOM   422   C CG2    . ILE A 1 64  ? 26.194  18.504  6.258  1.00 47.73  ? 64  ILE A CG2    1 
ATOM   423   C CD1    . ILE A 1 64  ? 23.520  19.827  6.619  1.00 50.82  ? 64  ILE A CD1    1 
ATOM   424   N N      . LEU A 1 65  ? 24.820  17.205  10.540 1.00 60.15  ? 65  LEU A N      1 
ATOM   425   C CA     . LEU A 1 65  ? 24.141  17.347  11.815 1.00 61.07  ? 65  LEU A CA     1 
ATOM   426   C C      . LEU A 1 65  ? 24.485  16.337  12.920 1.00 66.88  ? 65  LEU A C      1 
ATOM   427   O O      . LEU A 1 65  ? 25.289  15.443  12.706 1.00 67.68  ? 65  LEU A O      1 
ATOM   428   C CB     . LEU A 1 65  ? 22.632  17.284  11.585 1.00 56.49  ? 65  LEU A CB     1 
ATOM   429   C CG     . LEU A 1 65  ? 21.924  18.054  10.479 1.00 53.45  ? 65  LEU A CG     1 
ATOM   430   C CD1    . LEU A 1 65  ? 20.521  17.512  10.343 1.00 57.81  ? 65  LEU A CD1    1 
ATOM   431   C CD2    . LEU A 1 65  ? 21.886  19.545  10.720 1.00 63.01  ? 65  LEU A CD2    1 
ATOM   432   N N      . THR A 1 66  ? 23.872  16.489  14.100 1.00 63.93  ? 66  THR A N      1 
ATOM   433   C CA     . THR A 1 66  ? 24.077  15.576  15.230 1.00 65.70  ? 66  THR A CA     1 
ATOM   434   C C      . THR A 1 66  ? 22.695  15.188  15.623 1.00 62.88  ? 66  THR A C      1 
ATOM   435   O O      . THR A 1 66  ? 21.909  16.046  15.989 1.00 58.21  ? 66  THR A O      1 
ATOM   436   C CB     . THR A 1 66  ? 24.665  16.283  16.433 1.00 68.56  ? 66  THR A CB     1 
ATOM   437   O OG1    . THR A 1 66  ? 25.840  16.998  16.039 1.00 76.40  ? 66  THR A OG1    1 
ATOM   438   C CG2    . THR A 1 66  ? 25.029  15.278  17.506 1.00 61.97  ? 66  THR A CG2    1 
ATOM   439   N N      . LEU A 1 67  ? 22.383  13.907  15.609 1.00 65.29  ? 67  LEU A N      1 
ATOM   440   C CA     . LEU A 1 67  ? 21.009  13.500  15.805 1.00 60.56  ? 67  LEU A CA     1 
ATOM   441   C C      . LEU A 1 67  ? 20.664  13.131  17.215 1.00 59.67  ? 67  LEU A C      1 
ATOM   442   O O      . LEU A 1 67  ? 21.472  12.546  17.920 1.00 58.26  ? 67  LEU A O      1 
ATOM   443   C CB     . LEU A 1 67  ? 20.663  12.353  14.866 1.00 55.54  ? 67  LEU A CB     1 
ATOM   444   C CG     . LEU A 1 67  ? 20.740  12.507  13.346 1.00 55.40  ? 67  LEU A CG     1 
ATOM   445   C CD1    . LEU A 1 67  ? 20.305  13.894  12.923 1.00 67.89  ? 67  LEU A CD1    1 
ATOM   446   C CD2    . LEU A 1 67  ? 22.115  12.185  12.784 1.00 57.05  ? 67  LEU A CD2    1 
ATOM   447   N N      . LYS A 1 68  ? 19.452  13.467  17.635 1.00 57.67  ? 68  LYS A N      1 
ATOM   448   C CA     . LYS A 1 68  ? 19.004  13.142  18.964 1.00 47.24  ? 68  LYS A CA     1 
ATOM   449   C C      . LYS A 1 68  ? 17.697  12.442  18.805 1.00 45.01  ? 68  LYS A C      1 
ATOM   450   O O      . LYS A 1 68  ? 16.906  12.815  17.972 1.00 47.03  ? 68  LYS A O      1 
ATOM   451   C CB     . LYS A 1 68  ? 18.815  14.403  19.782 1.00 50.68  ? 68  LYS A CB     1 
ATOM   452   C CG     . LYS A 1 68  ? 19.849  15.486  19.524 1.00 59.37  ? 68  LYS A CG     1 
ATOM   453   C CD     . LYS A 1 68  ? 20.483  15.979  20.811 1.00 56.77  ? 68  LYS A CD     1 
ATOM   454   C CE     . LYS A 1 68  ? 19.456  16.619  21.726 1.00 47.31  ? 68  LYS A CE     1 
ATOM   455   N NZ     . LYS A 1 68  ? 20.088  17.140  22.966 1.00 40.24  ? 68  LYS A NZ     1 
ATOM   456   N N      . TYR A 1 69  ? 17.470  11.422  19.604 1.00 52.48  ? 69  TYR A N      1 
ATOM   457   C CA     . TYR A 1 69  ? 16.269  10.641  19.523 1.00 48.68  ? 69  TYR A CA     1 
ATOM   458   C C      . TYR A 1 69  ? 15.523  11.006  20.742 1.00 47.98  ? 69  TYR A C      1 
ATOM   459   O O      . TYR A 1 69  ? 15.787  10.485  21.813 1.00 54.08  ? 69  TYR A O      1 
ATOM   460   C CB     . TYR A 1 69  ? 16.634  9.174   19.572 1.00 48.51  ? 69  TYR A CB     1 
ATOM   461   C CG     . TYR A 1 69  ? 17.744  8.824   18.609 1.00 61.23  ? 69  TYR A CG     1 
ATOM   462   C CD1    . TYR A 1 69  ? 19.078  8.914   18.983 1.00 68.41  ? 69  TYR A CD1    1 
ATOM   463   C CD2    . TYR A 1 69  ? 17.457  8.422   17.322 1.00 65.15  ? 69  TYR A CD2    1 
ATOM   464   C CE1    . TYR A 1 69  ? 20.090  8.617   18.094 1.00 77.69  ? 69  TYR A CE1    1 
ATOM   465   C CE2    . TYR A 1 69  ? 18.463  8.114   16.428 1.00 75.78  ? 69  TYR A CE2    1 
ATOM   466   C CZ     . TYR A 1 69  ? 19.775  8.215   16.818 1.00 87.01  ? 69  TYR A CZ     1 
ATOM   467   O OH     . TYR A 1 69  ? 20.774  7.910   15.925 1.00 92.50  ? 69  TYR A OH     1 
ATOM   468   N N      . PRO A 1 70  ? 14.545  11.924  20.619 1.00 42.57  ? 70  PRO A N      1 
ATOM   469   C CA     . PRO A 1 70  ? 13.945  12.292  21.894 1.00 44.77  ? 70  PRO A CA     1 
ATOM   470   C C      . PRO A 1 70  ? 13.122  11.217  22.534 1.00 46.79  ? 70  PRO A C      1 
ATOM   471   O O      . PRO A 1 70  ? 13.008  11.227  23.747 1.00 44.69  ? 70  PRO A O      1 
ATOM   472   C CB     . PRO A 1 70  ? 13.069  13.458  21.522 1.00 42.90  ? 70  PRO A CB     1 
ATOM   473   C CG     . PRO A 1 70  ? 12.672  13.217  20.121 1.00 45.28  ? 70  PRO A CG     1 
ATOM   474   C CD     . PRO A 1 70  ? 13.891  12.642  19.497 1.00 44.48  ? 70  PRO A CD     1 
ATOM   475   N N      . ILE A 1 71  ? 12.614  10.264  21.769 1.00 46.36  ? 71  ILE A N      1 
ATOM   476   C CA     . ILE A 1 71  ? 11.712  9.269   22.320 1.00 44.68  ? 71  ILE A CA     1 
ATOM   477   C C      . ILE A 1 71  ? 12.317  7.870   22.272 1.00 53.17  ? 71  ILE A C      1 
ATOM   478   O O      . ILE A 1 71  ? 11.634  6.866   22.271 1.00 48.50  ? 71  ILE A O      1 
ATOM   479   C CB     . ILE A 1 71  ? 10.343  9.455   21.657 1.00 39.86  ? 71  ILE A CB     1 
ATOM   480   C CG1    . ILE A 1 71  ? 9.271   8.471   22.127 1.00 46.56  ? 71  ILE A CG1    1 
ATOM   481   C CG2    . ILE A 1 71  ? 10.500  9.484   20.153 1.00 44.54  ? 71  ILE A CG2    1 
ATOM   482   C CD1    . ILE A 1 71  ? 8.813   8.665   23.546 1.00 49.02  ? 71  ILE A CD1    1 
ATOM   483   N N      . GLU A 1 72  ? 13.637  7.778   22.330 1.00 60.39  ? 72  GLU A N      1 
ATOM   484   C CA     . GLU A 1 72  ? 14.264  6.462   22.383 1.00 59.82  ? 72  GLU A CA     1 
ATOM   485   C C      . GLU A 1 72  ? 13.951  5.772   23.669 1.00 59.98  ? 72  GLU A C      1 
ATOM   486   O O      . GLU A 1 72  ? 13.854  6.419   24.708 1.00 63.37  ? 72  GLU A O      1 
ATOM   487   C CB     . GLU A 1 72  ? 15.774  6.536   22.210 1.00 63.25  ? 72  GLU A CB     1 
ATOM   488   C CG     . GLU A 1 72  ? 16.530  7.238   23.321 1.00 74.66  ? 72  GLU A CG     1 
ATOM   489   C CD     . GLU A 1 72  ? 17.958  6.749   23.450 1.00 80.49  ? 72  GLU A CD     1 
ATOM   490   O OE1    . GLU A 1 72  ? 18.410  5.991   22.571 1.00 75.76  ? 72  GLU A OE1    1 
ATOM   491   O OE2    . GLU A 1 72  ? 18.629  7.119   24.434 1.00 87.36  ? 72  GLU A OE2    1 
ATOM   492   N N      . HIS A 1 73  ? 13.781  4.467   23.605 1.00 57.14  ? 73  HIS A N      1 
ATOM   493   C CA     . HIS A 1 73  ? 13.459  3.681   24.788 1.00 58.45  ? 73  HIS A CA     1 
ATOM   494   C C      . HIS A 1 73  ? 12.131  4.045   25.413 1.00 52.44  ? 73  HIS A C      1 
ATOM   495   O O      . HIS A 1 73  ? 11.897  3.771   26.578 1.00 49.31  ? 73  HIS A O      1 
ATOM   496   C CB     . HIS A 1 73  ? 14.606  3.687   25.784 1.00 63.00  ? 73  HIS A CB     1 
ATOM   497   C CG     . HIS A 1 73  ? 15.812  2.936   25.316 1.00 73.71  ? 73  HIS A CG     1 
ATOM   498   N ND1    . HIS A 1 73  ? 15.820  1.566   25.165 1.00 68.37  ? 73  HIS A ND1    1 
ATOM   499   C CD2    . HIS A 1 73  ? 17.050  3.359   24.973 1.00 74.26  ? 73  HIS A CD2    1 
ATOM   500   C CE1    . HIS A 1 73  ? 17.010  1.178   24.745 1.00 66.18  ? 73  HIS A CE1    1 
ATOM   501   N NE2    . HIS A 1 73  ? 17.775  2.247   24.621 1.00 76.99  ? 73  HIS A NE2    1 
ATOM   502   N N      . GLY A 1 74  ? 11.238  4.647   24.654 1.00 52.69  ? 74  GLY A N      1 
ATOM   503   C CA     . GLY A 1 74  ? 9.907   4.896   25.171 1.00 48.84  ? 74  GLY A CA     1 
ATOM   504   C C      . GLY A 1 74  ? 9.510   6.174   25.842 1.00 54.84  ? 74  GLY A C      1 
ATOM   505   O O      . GLY A 1 74  ? 8.400   6.615   25.668 1.00 67.35  ? 74  GLY A O      1 
ATOM   506   N N      . ILE A 1 75  ? 10.364  6.775   26.635 1.00 43.16  ? 75  ILE A N      1 
ATOM   507   C CA     . ILE A 1 75  ? 9.951   7.940   27.358 1.00 42.25  ? 75  ILE A CA     1 
ATOM   508   C C      . ILE A 1 75  ? 10.620  9.123   26.754 1.00 45.76  ? 75  ILE A C      1 
ATOM   509   O O      . ILE A 1 75  ? 11.748  9.030   26.297 1.00 44.99  ? 75  ILE A O      1 
ATOM   510   C CB     . ILE A 1 75  ? 10.279  7.819   28.848 1.00 38.92  ? 75  ILE A CB     1 
ATOM   511   C CG1    . ILE A 1 75  ? 11.787  7.736   29.077 1.00 50.50  ? 75  ILE A CG1    1 
ATOM   512   C CG2    . ILE A 1 75  ? 9.623   6.589   29.446 1.00 31.53  ? 75  ILE A CG2    1 
ATOM   513   C CD1    . ILE A 1 75  ? 12.184  7.776   30.535 1.00 54.47  ? 75  ILE A CD1    1 
ATOM   514   N N      . VAL A 1 76  ? 9.949   10.269  26.765 1.00 47.25  ? 76  VAL A N      1 
ATOM   515   C CA     . VAL A 1 76  ? 10.487  11.469  26.148 1.00 38.89  ? 76  VAL A CA     1 
ATOM   516   C C      . VAL A 1 76  ? 11.516  12.199  26.975 1.00 39.09  ? 76  VAL A C      1 
ATOM   517   O O      . VAL A 1 76  ? 11.184  12.845  27.946 1.00 39.40  ? 76  VAL A O      1 
ATOM   518   C CB     . VAL A 1 76  ? 9.366   12.431  25.794 1.00 39.33  ? 76  VAL A CB     1 
ATOM   519   C CG1    . VAL A 1 76  ? 9.779   13.283  24.614 1.00 46.09  ? 76  VAL A CG1    1 
ATOM   520   C CG2    . VAL A 1 76  ? 8.091   11.674  25.479 1.00 31.38  ? 76  VAL A CG2    1 
ATOM   521   N N      . THR A 1 77  ? 12.766  12.146  26.561 1.00 39.85  ? 77  THR A N      1 
ATOM   522   C CA     . THR A 1 77  ? 13.833  12.774  27.306 1.00 41.63  ? 77  THR A CA     1 
ATOM   523   C C      . THR A 1 77  ? 13.920  14.272  27.111 1.00 49.54  ? 77  THR A C      1 
ATOM   524   O O      . THR A 1 77  ? 14.054  15.010  28.073 1.00 56.54  ? 77  THR A O      1 
ATOM   525   C CB     . THR A 1 77  ? 15.167  12.165  26.883 1.00 40.95  ? 77  THR A CB     1 
ATOM   526   O OG1    . THR A 1 77  ? 15.214  12.066  25.457 1.00 39.89  ? 77  THR A OG1    1 
ATOM   527   C CG2    . THR A 1 77  ? 15.314  10.781  27.464 1.00 46.66  ? 77  THR A CG2    1 
ATOM   528   N N      . ASN A 1 78  ? 13.887  14.736  25.869 1.00 54.66  ? 78  ASN A N      1 
ATOM   529   C CA     . ASN A 1 78  ? 14.014  16.155  25.576 1.00 54.56  ? 78  ASN A CA     1 
ATOM   530   C C      . ASN A 1 78  ? 12.682  16.675  25.209 1.00 56.75  ? 78  ASN A C      1 
ATOM   531   O O      . ASN A 1 78  ? 12.057  16.182  24.292 1.00 56.32  ? 78  ASN A O      1 
ATOM   532   C CB     . ASN A 1 78  ? 14.932  16.376  24.389 1.00 47.75  ? 78  ASN A CB     1 
ATOM   533   C CG     . ASN A 1 78  ? 15.597  17.731  24.417 1.00 61.39  ? 78  ASN A CG     1 
ATOM   534   O OD1    . ASN A 1 78  ? 15.358  18.530  25.316 1.00 74.47  ? 78  ASN A OD1    1 
ATOM   535   N ND2    . ASN A 1 78  ? 16.444  17.993  23.437 1.00 56.65  ? 78  ASN A ND2    1 
ATOM   536   N N      . TRP A 1 79  ? 12.231  17.692  25.904 1.00 52.67  ? 79  TRP A N      1 
ATOM   537   C CA     . TRP A 1 79  ? 10.968  18.277  25.558 1.00 54.76  ? 79  TRP A CA     1 
ATOM   538   C C      . TRP A 1 79  ? 11.176  19.407  24.594 1.00 59.01  ? 79  TRP A C      1 
ATOM   539   O O      . TRP A 1 79  ? 10.267  19.775  23.872 1.00 57.93  ? 79  TRP A O      1 
ATOM   540   C CB     . TRP A 1 79  ? 10.240  18.704  26.806 1.00 55.07  ? 79  TRP A CB     1 
ATOM   541   C CG     . TRP A 1 79  ? 9.661   17.556  27.540 1.00 53.99  ? 79  TRP A CG     1 
ATOM   542   C CD1    . TRP A 1 79  ? 10.098  17.029  28.712 1.00 51.03  ? 79  TRP A CD1    1 
ATOM   543   C CD2    . TRP A 1 79  ? 8.538   16.773  27.142 1.00 50.60  ? 79  TRP A CD2    1 
ATOM   544   N NE1    . TRP A 1 79  ? 9.308   15.972  29.078 1.00 47.07  ? 79  TRP A NE1    1 
ATOM   545   C CE2    . TRP A 1 79  ? 8.343   15.795  28.125 1.00 48.11  ? 79  TRP A CE2    1 
ATOM   546   C CE3    . TRP A 1 79  ? 7.673   16.810  26.050 1.00 48.36  ? 79  TRP A CE3    1 
ATOM   547   C CZ2    . TRP A 1 79  ? 7.323   14.861  28.048 1.00 49.83  ? 79  TRP A CZ2    1 
ATOM   548   C CZ3    . TRP A 1 79  ? 6.665   15.887  25.977 1.00 44.85  ? 79  TRP A CZ3    1 
ATOM   549   C CH2    . TRP A 1 79  ? 6.496   14.926  26.968 1.00 49.30  ? 79  TRP A CH2    1 
ATOM   550   N N      . ASP A 1 80  ? 12.378  19.943  24.541 1.00 62.06  ? 80  ASP A N      1 
ATOM   551   C CA     . ASP A 1 80  ? 12.676  20.982  23.575 1.00 66.58  ? 80  ASP A CA     1 
ATOM   552   C C      . ASP A 1 80  ? 12.602  20.371  22.206 1.00 66.65  ? 80  ASP A C      1 
ATOM   553   O O      . ASP A 1 80  ? 11.983  20.930  21.319 1.00 66.81  ? 80  ASP A O      1 
ATOM   554   C CB     . ASP A 1 80  ? 14.073  21.530  23.819 1.00 65.55  ? 80  ASP A CB     1 
ATOM   555   C CG     . ASP A 1 80  ? 14.243  22.944  23.332 1.00 80.75  ? 80  ASP A CG     1 
ATOM   556   O OD1    . ASP A 1 80  ? 13.300  23.487  22.723 1.00 87.01  ? 80  ASP A OD1    1 
ATOM   557   O OD2    . ASP A 1 80  ? 15.327  23.517  23.566 1.00 76.68  ? 80  ASP A OD2    1 
ATOM   558   N N      . ASP A 1 81  ? 13.200  19.207  22.023 1.00 58.97  ? 81  ASP A N      1 
ATOM   559   C CA     . ASP A 1 81  ? 13.209  18.551  20.729 1.00 58.55  ? 81  ASP A CA     1 
ATOM   560   C C      . ASP A 1 81  ? 11.897  17.916  20.299 1.00 51.87  ? 81  ASP A C      1 
ATOM   561   O O      . ASP A 1 81  ? 11.601  17.856  19.126 1.00 50.05  ? 81  ASP A O      1 
ATOM   562   C CB     . ASP A 1 81  ? 14.306  17.515  20.707 1.00 52.64  ? 81  ASP A CB     1 
ATOM   563   C CG     . ASP A 1 81  ? 15.536  18.000  20.009 1.00 58.68  ? 81  ASP A CG     1 
ATOM   564   O OD1    . ASP A 1 81  ? 15.435  19.014  19.303 1.00 72.56  ? 81  ASP A OD1    1 
ATOM   565   O OD2    . ASP A 1 81  ? 16.598  17.370  20.148 1.00 50.99  ? 81  ASP A OD2    1 
ATOM   566   N N      . MET A 1 82  ? 11.083  17.470  21.234 1.00 46.61  ? 82  MET A N      1 
ATOM   567   C CA     . MET A 1 82  ? 9.834   16.830  20.883 1.00 42.59  ? 82  MET A CA     1 
ATOM   568   C C      . MET A 1 82  ? 8.865   17.873  20.462 1.00 41.85  ? 82  MET A C      1 
ATOM   569   O O      . MET A 1 82  ? 7.889   17.586  19.805 1.00 44.46  ? 82  MET A O      1 
ATOM   570   C CB     . MET A 1 82  ? 9.264   16.021  22.020 1.00 48.98  ? 82  MET A CB     1 
ATOM   571   C CG     . MET A 1 82  ? 8.273   14.957  21.593 1.00 45.40  ? 82  MET A CG     1 
ATOM   572   S SD     . MET A 1 82  ? 9.103   13.603  20.759 1.00 44.94  ? 82  MET A SD     1 
ATOM   573   C CE     . MET A 1 82  ? 7.739   12.853  19.892 1.00 49.72  ? 82  MET A CE     1 
ATOM   574   N N      . GLU A 1 83  ? 9.115   19.107  20.815 1.00 48.96  ? 83  GLU A N      1 
ATOM   575   C CA     . GLU A 1 83  ? 8.262   20.165  20.312 1.00 53.92  ? 83  GLU A CA     1 
ATOM   576   C C      . GLU A 1 83  ? 8.502   20.226  18.842 1.00 47.35  ? 83  GLU A C      1 
ATOM   577   O O      . GLU A 1 83  ? 7.585   20.377  18.057 1.00 44.07  ? 83  GLU A O      1 
ATOM   578   C CB     . GLU A 1 83  ? 8.644   21.503  20.911 1.00 54.76  ? 83  GLU A CB     1 
ATOM   579   C CG     . GLU A 1 83  ? 7.835   21.898  22.131 1.00 52.48  ? 83  GLU A CG     1 
ATOM   580   C CD     . GLU A 1 83  ? 8.294   23.210  22.727 1.00 54.96  ? 83  GLU A CD     1 
ATOM   581   O OE1    . GLU A 1 83  ? 9.457   23.597  22.491 1.00 56.38  ? 83  GLU A OE1    1 
ATOM   582   O OE2    . GLU A 1 83  ? 7.495   23.852  23.436 1.00 50.26  ? 83  GLU A OE2    1 
ATOM   583   N N      . LYS A 1 84  ? 9.745   20.065  18.453 1.00 44.11  ? 84  LYS A N      1 
ATOM   584   C CA     . LYS A 1 84  ? 10.080  20.135  17.068 1.00 43.48  ? 84  LYS A CA     1 
ATOM   585   C C      . LYS A 1 84  ? 9.581   18.936  16.313 1.00 43.62  ? 84  LYS A C      1 
ATOM   586   O O      . LYS A 1 84  ? 9.205   19.058  15.162 1.00 52.96  ? 84  LYS A O      1 
ATOM   587   C CB     . LYS A 1 84  ? 11.572  20.241  16.947 1.00 48.71  ? 84  LYS A CB     1 
ATOM   588   C CG     . LYS A 1 84  ? 12.168  21.447  17.649 1.00 54.03  ? 84  LYS A CG     1 
ATOM   589   C CD     . LYS A 1 84  ? 13.672  21.507  17.448 1.00 58.38  ? 84  LYS A CD     1 
ATOM   590   C CE     . LYS A 1 84  ? 14.240  22.839  17.907 1.00 71.42  ? 84  LYS A CE     1 
ATOM   591   N NZ     . LYS A 1 84  ? 13.963  23.108  19.343 1.00 68.46  ? 84  LYS A NZ     1 
ATOM   592   N N      . ILE A 1 85  ? 9.554   17.769  16.935 1.00 39.70  ? 85  ILE A N      1 
ATOM   593   C CA     . ILE A 1 85  ? 9.000   16.600  16.267 1.00 38.59  ? 85  ILE A CA     1 
ATOM   594   C C      . ILE A 1 85  ? 7.536   16.833  16.034 1.00 41.87  ? 85  ILE A C      1 
ATOM   595   O O      . ILE A 1 85  ? 7.036   16.593  14.951 1.00 48.05  ? 85  ILE A O      1 
ATOM   596   C CB     . ILE A 1 85  ? 9.189   15.317  17.069 1.00 31.66  ? 85  ILE A CB     1 
ATOM   597   C CG1    . ILE A 1 85  ? 10.663  14.969  17.179 1.00 34.51  ? 85  ILE A CG1    1 
ATOM   598   C CG2    . ILE A 1 85  ? 8.483   14.157  16.401 1.00 32.72  ? 85  ILE A CG2    1 
ATOM   599   C CD1    . ILE A 1 85  ? 11.148  14.117  16.036 1.00 37.46  ? 85  ILE A CD1    1 
ATOM   600   N N      . TRP A 1 86  ? 6.844   17.380  17.017 1.00 39.03  ? 86  TRP A N      1 
ATOM   601   C CA     . TRP A 1 86  ? 5.415   17.581  16.880 1.00 38.47  ? 86  TRP A CA     1 
ATOM   602   C C      . TRP A 1 86  ? 5.071   18.680  15.907 1.00 44.54  ? 86  TRP A C      1 
ATOM   603   O O      . TRP A 1 86  ? 4.052   18.629  15.255 1.00 46.71  ? 86  TRP A O      1 
ATOM   604   C CB     . TRP A 1 86  ? 4.780   17.842  18.218 1.00 40.38  ? 86  TRP A CB     1 
ATOM   605   C CG     . TRP A 1 86  ? 4.649   16.648  19.067 1.00 45.07  ? 86  TRP A CG     1 
ATOM   606   C CD1    . TRP A 1 86  ? 4.441   15.378  18.654 1.00 48.69  ? 86  TRP A CD1    1 
ATOM   607   C CD2    . TRP A 1 86  ? 4.692   16.605  20.490 1.00 41.80  ? 86  TRP A CD2    1 
ATOM   608   N NE1    . TRP A 1 86  ? 4.360   14.536  19.728 1.00 45.83  ? 86  TRP A NE1    1 
ATOM   609   C CE2    . TRP A 1 86  ? 4.509   15.271  20.871 1.00 47.33  ? 86  TRP A CE2    1 
ATOM   610   C CE3    . TRP A 1 86  ? 4.870   17.568  21.480 1.00 41.37  ? 86  TRP A CE3    1 
ATOM   611   C CZ2    . TRP A 1 86  ? 4.505   14.875  22.196 1.00 52.93  ? 86  TRP A CZ2    1 
ATOM   612   C CZ3    . TRP A 1 86  ? 4.860   17.171  22.791 1.00 45.09  ? 86  TRP A CZ3    1 
ATOM   613   C CH2    . TRP A 1 86  ? 4.681   15.840  23.137 1.00 50.08  ? 86  TRP A CH2    1 
ATOM   614   N N      . HIS A 1 87  ? 5.909   19.682  15.796 1.00 43.96  ? 87  HIS A N      1 
ATOM   615   C CA     . HIS A 1 87  ? 5.682   20.731  14.820 1.00 44.11  ? 87  HIS A CA     1 
ATOM   616   C C      . HIS A 1 87  ? 5.747   20.181  13.445 1.00 44.12  ? 87  HIS A C      1 
ATOM   617   O O      . HIS A 1 87  ? 4.911   20.478  12.626 1.00 46.42  ? 87  HIS A O      1 
ATOM   618   C CB     . HIS A 1 87  ? 6.804   21.762  14.940 1.00 43.69  ? 87  HIS A CB     1 
ATOM   619   C CG     . HIS A 1 87  ? 6.573   23.029  14.181 1.00 50.60  ? 87  HIS A CG     1 
ATOM   620   N ND1    . HIS A 1 87  ? 6.817   23.145  12.831 1.00 56.86  ? 87  HIS A ND1    1 
ATOM   621   C CD2    . HIS A 1 87  ? 6.166   24.250  14.594 1.00 46.84  ? 87  HIS A CD2    1 
ATOM   622   C CE1    . HIS A 1 87  ? 6.544   24.375  12.440 1.00 52.47  ? 87  HIS A CE1    1 
ATOM   623   N NE2    . HIS A 1 87  ? 6.147   25.066  13.491 1.00 55.12  ? 87  HIS A NE2    1 
ATOM   624   N N      . HIS A 1 88  ? 6.725   19.344  13.188 1.00 42.96  ? 88  HIS A N      1 
ATOM   625   C CA     . HIS A 1 88  ? 6.915   18.836  11.861 1.00 46.29  ? 88  HIS A CA     1 
ATOM   626   C C      . HIS A 1 88  ? 5.691   18.096  11.543 1.00 48.03  ? 88  HIS A C      1 
ATOM   627   O O      . HIS A 1 88  ? 5.140   18.220  10.474 1.00 46.58  ? 88  HIS A O      1 
ATOM   628   C CB     . HIS A 1 88  ? 8.041   17.826  11.914 1.00 45.57  ? 88  HIS A CB     1 
ATOM   629   C CG     . HIS A 1 88  ? 8.848   17.721  10.666 1.00 52.82  ? 88  HIS A CG     1 
ATOM   630   N ND1    . HIS A 1 88  ? 9.031   16.527  10.007 1.00 52.80  ? 88  HIS A ND1    1 
ATOM   631   C CD2    . HIS A 1 88  ? 9.559   18.644  9.980  1.00 61.98  ? 88  HIS A CD2    1 
ATOM   632   C CE1    . HIS A 1 88  ? 9.806   16.722  8.957  1.00 60.39  ? 88  HIS A CE1    1 
ATOM   633   N NE2    . HIS A 1 88  ? 10.140  17.999  8.918  1.00 73.25  ? 88  HIS A NE2    1 
ATOM   634   N N      . THR A 1 89  ? 5.238   17.315  12.493 1.00 42.74  ? 89  THR A N      1 
ATOM   635   C CA     . THR A 1 89  ? 4.117   16.498  12.211 1.00 40.45  ? 89  THR A CA     1 
ATOM   636   C C      . THR A 1 89  ? 2.893   17.294  11.939 1.00 45.35  ? 89  THR A C      1 
ATOM   637   O O      . THR A 1 89  ? 2.252   17.104  10.928 1.00 47.66  ? 89  THR A O      1 
ATOM   638   C CB     . THR A 1 89  ? 3.825   15.648  13.425 1.00 39.07  ? 89  THR A CB     1 
ATOM   639   O OG1    . THR A 1 89  ? 5.028   15.007  13.850 1.00 40.39  ? 89  THR A OG1    1 
ATOM   640   C CG2    . THR A 1 89  ? 2.802   14.609  13.103 1.00 42.58  ? 89  THR A CG2    1 
ATOM   641   N N      . PHE A 1 90  ? 2.575   18.239  12.798 1.00 45.76  ? 90  PHE A N      1 
ATOM   642   C CA     . PHE A 1 90  ? 1.329   18.950  12.624 1.00 45.52  ? 90  PHE A CA     1 
ATOM   643   C C      . PHE A 1 90  ? 1.330   19.843  11.439 1.00 48.27  ? 90  PHE A C      1 
ATOM   644   O O      . PHE A 1 90  ? 0.436   19.809  10.631 1.00 44.23  ? 90  PHE A O      1 
ATOM   645   C CB     . PHE A 1 90  ? 1.021   19.799  13.846 1.00 39.56  ? 90  PHE A CB     1 
ATOM   646   C CG     . PHE A 1 90  ? 0.831   19.023  15.101 1.00 44.57  ? 90  PHE A CG     1 
ATOM   647   C CD1    . PHE A 1 90  ? 0.380   17.726  15.073 1.00 50.38  ? 90  PHE A CD1    1 
ATOM   648   C CD2    . PHE A 1 90  ? 1.083   19.611  16.314 1.00 41.12  ? 90  PHE A CD2    1 
ATOM   649   C CE1    . PHE A 1 90  ? 0.208   17.019  16.237 1.00 44.45  ? 90  PHE A CE1    1 
ATOM   650   C CE2    . PHE A 1 90  ? 0.909   18.913  17.480 1.00 35.89  ? 90  PHE A CE2    1 
ATOM   651   C CZ     . PHE A 1 90  ? 0.470   17.615  17.442 1.00 35.18  ? 90  PHE A CZ     1 
ATOM   652   N N      . TYR A 1 91  ? 2.383   20.601  11.274 1.00 50.77  ? 91  TYR A N      1 
ATOM   653   C CA     . TYR A 1 91  ? 2.367   21.572  10.232 1.00 46.78  ? 91  TYR A CA     1 
ATOM   654   C C      . TYR A 1 91  ? 2.985   21.050  8.993  1.00 44.95  ? 91  TYR A C      1 
ATOM   655   O O      . TYR A 1 91  ? 2.313   20.869  8.011  1.00 50.58  ? 91  TYR A O      1 
ATOM   656   C CB     . TYR A 1 91  ? 3.181   22.769  10.678 1.00 47.98  ? 91  TYR A CB     1 
ATOM   657   C CG     . TYR A 1 91  ? 2.647   23.560  11.842 1.00 46.13  ? 91  TYR A CG     1 
ATOM   658   C CD1    . TYR A 1 91  ? 1.701   24.550  11.659 1.00 54.62  ? 91  TYR A CD1    1 
ATOM   659   C CD2    . TYR A 1 91  ? 3.129   23.353  13.118 1.00 45.29  ? 91  TYR A CD2    1 
ATOM   660   C CE1    . TYR A 1 91  ? 1.233   25.291  12.723 1.00 57.25  ? 91  TYR A CE1    1 
ATOM   661   C CE2    . TYR A 1 91  ? 2.668   24.088  14.188 1.00 44.93  ? 91  TYR A CE2    1 
ATOM   662   C CZ     . TYR A 1 91  ? 1.721   25.056  13.984 1.00 49.44  ? 91  TYR A CZ     1 
ATOM   663   O OH     . TYR A 1 91  ? 1.260   25.783  15.050 1.00 50.86  ? 91  TYR A OH     1 
ATOM   664   N N      . ASN A 1 92  ? 4.272   20.787  9.015  1.00 44.67  ? 92  ASN A N      1 
ATOM   665   C CA     . ASN A 1 92  ? 4.923   20.381  7.787  1.00 54.23  ? 92  ASN A CA     1 
ATOM   666   C C      . ASN A 1 92  ? 4.513   19.040  7.149  1.00 51.25  ? 92  ASN A C      1 
ATOM   667   O O      . ASN A 1 92  ? 4.263   18.977  5.956  1.00 41.78  ? 92  ASN A O      1 
ATOM   668   C CB     . ASN A 1 92  ? 6.427   20.380  8.030  1.00 53.72  ? 92  ASN A CB     1 
ATOM   669   C CG     . ASN A 1 92  ? 6.913   21.655  8.663  1.00 53.24  ? 92  ASN A CG     1 
ATOM   670   O OD1    . ASN A 1 92  ? 6.236   22.674  8.626  1.00 55.38  ? 92  ASN A OD1    1 
ATOM   671   N ND2    . ASN A 1 92  ? 8.098   21.605  9.244  1.00 53.60  ? 92  ASN A ND2    1 
ATOM   672   N N      . GLU A 1 93  ? 4.455   17.973  7.927  1.00 47.81  ? 93  GLU A N      1 
ATOM   673   C CA     . GLU A 1 93  ? 4.053   16.677  7.410  1.00 44.60  ? 93  GLU A CA     1 
ATOM   674   C C      . GLU A 1 93  ? 2.603   16.463  7.051  1.00 44.59  ? 93  GLU A C      1 
ATOM   675   O O      . GLU A 1 93  ? 2.304   15.899  6.013  1.00 48.49  ? 93  GLU A O      1 
ATOM   676   C CB     . GLU A 1 93  ? 4.468   15.602  8.399  1.00 45.71  ? 93  GLU A CB     1 
ATOM   677   C CG     . GLU A 1 93  ? 5.965   15.468  8.585  1.00 53.23  ? 93  GLU A CG     1 
ATOM   678   C CD     . GLU A 1 93  ? 6.559   14.352  7.760  1.00 51.42  ? 93  GLU A CD     1 
ATOM   679   O OE1    . GLU A 1 93  ? 5.802   13.466  7.327  1.00 48.00  ? 93  GLU A OE1    1 
ATOM   680   O OE2    . GLU A 1 93  ? 7.786   14.353  7.553  1.00 51.68  ? 93  GLU A OE2    1 
ATOM   681   N N      . LEU A 1 94  ? 1.693   16.892  7.908  1.00 44.95  ? 94  LEU A N      1 
ATOM   682   C CA     . LEU A 1 94  ? 0.280   16.640  7.690  1.00 44.22  ? 94  LEU A CA     1 
ATOM   683   C C      . LEU A 1 94  ? -0.415  17.846  7.151  1.00 43.89  ? 94  LEU A C      1 
ATOM   684   O O      . LEU A 1 94  ? -1.571  17.778  6.769  1.00 39.23  ? 94  LEU A O      1 
ATOM   685   C CB     . LEU A 1 94  ? -0.357  16.247  9.015  1.00 42.85  ? 94  LEU A CB     1 
ATOM   686   C CG     . LEU A 1 94  ? -0.420  14.827  9.571  1.00 37.15  ? 94  LEU A CG     1 
ATOM   687   C CD1    . LEU A 1 94  ? 0.942   14.169  9.649  1.00 41.56  ? 94  LEU A CD1    1 
ATOM   688   C CD2    . LEU A 1 94  ? -1.054  14.882  10.948 1.00 34.06  ? 94  LEU A CD2    1 
ATOM   689   N N      . ARG A 1 95  ? 0.287   18.956  7.113  1.00 48.02  ? 95  ARG A N      1 
ATOM   690   C CA     . ARG A 1 95  ? -0.275  20.199  6.626  1.00 52.00  ? 95  ARG A CA     1 
ATOM   691   C C      . ARG A 1 95  ? -1.544  20.634  7.327  1.00 53.99  ? 95  ARG A C      1 
ATOM   692   O O      . ARG A 1 95  ? -2.470  21.123  6.694  1.00 59.23  ? 95  ARG A O      1 
ATOM   693   C CB     . ARG A 1 95  ? -0.356  20.206  5.112  1.00 47.39  ? 95  ARG A CB     1 
ATOM   694   C CG     . ARG A 1 95  ? 1.009   20.390  4.474  1.00 45.19  ? 95  ARG A CG     1 
ATOM   695   C CD     . ARG A 1 95  ? 0.912   20.580  2.976  1.00 41.11  ? 95  ARG A CD     1 
ATOM   696   N NE     . ARG A 1 95  ? 2.070   21.294  2.454  1.00 47.66  ? 95  ARG A NE     1 
ATOM   697   C CZ     . ARG A 1 95  ? 2.106   22.606  2.248  1.00 60.27  ? 95  ARG A CZ     1 
ATOM   698   N NH1    . ARG A 1 95  ? 1.045   23.352  2.514  1.00 60.84  ? 95  ARG A NH1    1 
ATOM   699   N NH2    . ARG A 1 95  ? 3.201   23.174  1.772  1.00 59.68  ? 95  ARG A NH2    1 
ATOM   700   N N      . VAL A 1 96  ? -1.571  20.495  8.646  1.00 48.61  ? 96  VAL A N      1 
ATOM   701   C CA     . VAL A 1 96  ? -2.722  20.900  9.406  1.00 44.98  ? 96  VAL A CA     1 
ATOM   702   C C      . VAL A 1 96  ? -2.326  21.895  10.453 1.00 52.40  ? 96  VAL A C      1 
ATOM   703   O O      . VAL A 1 96  ? -1.170  22.006  10.810 1.00 52.48  ? 96  VAL A O      1 
ATOM   704   C CB     . VAL A 1 96  ? -3.403  19.723  10.095 1.00 40.39  ? 96  VAL A CB     1 
ATOM   705   C CG1    . VAL A 1 96  ? -3.885  18.722  9.072  1.00 44.63  ? 96  VAL A CG1    1 
ATOM   706   C CG2    . VAL A 1 96  ? -2.519  19.072  11.135 1.00 41.32  ? 96  VAL A CG2    1 
ATOM   707   N N      . ALA A 1 97  ? -3.278  22.681  10.910 1.00 52.57  ? 97  ALA A N      1 
ATOM   708   C CA     . ALA A 1 97  ? -3.018  23.605  11.970 1.00 42.50  ? 97  ALA A CA     1 
ATOM   709   C C      . ALA A 1 97  ? -3.577  22.947  13.176 1.00 41.29  ? 97  ALA A C      1 
ATOM   710   O O      . ALA A 1 97  ? -4.757  22.650  13.232 1.00 39.22  ? 97  ALA A O      1 
ATOM   711   C CB     . ALA A 1 97  ? -3.777  24.863  11.704 1.00 46.66  ? 97  ALA A CB     1 
ATOM   712   N N      . PRO A 1 98  ? -2.759  22.766  14.182 1.00 40.32  ? 98  PRO A N      1 
ATOM   713   C CA     . PRO A 1 98  ? -3.191  22.054  15.369 1.00 44.50  ? 98  PRO A CA     1 
ATOM   714   C C      . PRO A 1 98  ? -4.313  22.716  16.096 1.00 44.32  ? 98  PRO A C      1 
ATOM   715   O O      . PRO A 1 98  ? -5.034  22.043  16.802 1.00 46.80  ? 98  PRO A O      1 
ATOM   716   C CB     . PRO A 1 98  ? -1.952  22.072  16.235 1.00 47.38  ? 98  PRO A CB     1 
ATOM   717   C CG     . PRO A 1 98  ? -1.054  23.114  15.673 1.00 49.96  ? 98  PRO A CG     1 
ATOM   718   C CD     . PRO A 1 98  ? -1.332  23.091  14.215 1.00 45.49  ? 98  PRO A CD     1 
ATOM   719   N N      . GLU A 1 99  ? -4.467  24.009  15.947 1.00 40.65  ? 99  GLU A N      1 
ATOM   720   C CA     . GLU A 1 99  ? -5.475  24.757  16.645 1.00 37.96  ? 99  GLU A CA     1 
ATOM   721   C C      . GLU A 1 99  ? -6.843  24.304  16.288 1.00 42.04  ? 99  GLU A C      1 
ATOM   722   O O      . GLU A 1 99  ? -7.781  24.582  17.013 1.00 37.85  ? 99  GLU A O      1 
ATOM   723   C CB     . GLU A 1 99  ? -5.342  26.209  16.250 1.00 42.39  ? 99  GLU A CB     1 
ATOM   724   C CG     . GLU A 1 99  ? -3.999  26.829  16.614 1.00 55.01  ? 99  GLU A CG     1 
ATOM   725   C CD     . GLU A 1 99  ? -2.969  26.776  15.499 1.00 53.10  ? 99  GLU A CD     1 
ATOM   726   O OE1    . GLU A 1 99  ? -3.362  26.865  14.324 1.00 59.30  ? 99  GLU A OE1    1 
ATOM   727   O OE2    . GLU A 1 99  ? -1.763  26.668  15.799 1.00 43.04  ? 99  GLU A OE2    1 
ATOM   728   N N      . GLU A 1 100 ? -6.993  23.668  15.144 1.00 45.05  ? 100 GLU A N      1 
ATOM   729   C CA     . GLU A 1 100 ? -8.311  23.278  14.678 1.00 46.93  ? 100 GLU A CA     1 
ATOM   730   C C      . GLU A 1 100 ? -8.672  21.803  14.759 1.00 42.04  ? 100 GLU A C      1 
ATOM   731   O O      . GLU A 1 100 ? -9.767  21.423  14.368 1.00 40.17  ? 100 GLU A O      1 
ATOM   732   C CB     . GLU A 1 100 ? -8.445  23.733  13.234 1.00 50.85  ? 100 GLU A CB     1 
ATOM   733   C CG     . GLU A 1 100 ? -8.342  25.231  13.031 1.00 55.82  ? 100 GLU A CG     1 
ATOM   734   C CD     . GLU A 1 100 ? -8.204  25.602  11.574 1.00 62.25  ? 100 GLU A CD     1 
ATOM   735   O OE1    . GLU A 1 100 ? -7.808  24.730  10.779 1.00 60.42  ? 100 GLU A OE1    1 
ATOM   736   O OE2    . GLU A 1 100 ? -8.484  26.766  11.223 1.00 70.07  ? 100 GLU A OE2    1 
ATOM   737   N N      . HIS A 1 101 ? -7.772  20.966  15.254 1.00 42.62  ? 101 HIS A N      1 
ATOM   738   C CA     . HIS A 1 101 ? -8.018  19.541  15.304 1.00 43.79  ? 101 HIS A CA     1 
ATOM   739   C C      . HIS A 1 101 ? -7.704  19.002  16.677 1.00 39.34  ? 101 HIS A C      1 
ATOM   740   O O      . HIS A 1 101 ? -6.672  19.305  17.232 1.00 47.89  ? 101 HIS A O      1 
ATOM   741   C CB     . HIS A 1 101 ? -7.125  18.833  14.284 1.00 39.88  ? 101 HIS A CB     1 
ATOM   742   C CG     . HIS A 1 101 ? -7.224  19.381  12.899 1.00 41.92  ? 101 HIS A CG     1 
ATOM   743   N ND1    . HIS A 1 101 ? -8.279  19.098  12.060 1.00 38.62  ? 101 HIS A ND1    1 
ATOM   744   C CD2    . HIS A 1 101 ? -6.389  20.178  12.196 1.00 39.59  ? 101 HIS A CD2    1 
ATOM   745   C CE1    . HIS A 1 101 ? -8.094  19.707  10.904 1.00 33.50  ? 101 HIS A CE1    1 
ATOM   746   N NE2    . HIS A 1 101 ? -6.955  20.369  10.960 1.00 36.18  ? 101 HIS A NE2    1 
ATOM   747   N N      . PRO A 1 102 ? -8.613  18.185  17.255 1.00 33.63  ? 102 PRO A N      1 
ATOM   748   C CA     . PRO A 1 102 ? -8.221  17.623  18.531 1.00 31.21  ? 102 PRO A CA     1 
ATOM   749   C C      . PRO A 1 102 ? -7.133  16.621  18.316 1.00 30.81  ? 102 PRO A C      1 
ATOM   750   O O      . PRO A 1 102 ? -7.109  16.003  17.280 1.00 35.35  ? 102 PRO A O      1 
ATOM   751   C CB     . PRO A 1 102 ? -9.475  16.911  18.968 1.00 30.80  ? 102 PRO A CB     1 
ATOM   752   C CG     . PRO A 1 102 ? -10.584 17.651  18.338 1.00 32.24  ? 102 PRO A CG     1 
ATOM   753   C CD     . PRO A 1 102 ? -10.035 17.876  16.979 1.00 32.92  ? 102 PRO A CD     1 
ATOM   754   N N      . VAL A 1 103 ? -6.233  16.446  19.269 1.00 30.09  ? 103 VAL A N      1 
ATOM   755   C CA     . VAL A 1 103 ? -5.107  15.553  19.088 1.00 30.87  ? 103 VAL A CA     1 
ATOM   756   C C      . VAL A 1 103 ? -5.003  14.382  20.048 1.00 29.34  ? 103 VAL A C      1 
ATOM   757   O O      . VAL A 1 103 ? -4.963  14.575  21.239 1.00 30.14  ? 103 VAL A O      1 
ATOM   758   C CB     . VAL A 1 103 ? -3.792  16.324  19.142 1.00 27.43  ? 103 VAL A CB     1 
ATOM   759   C CG1    . VAL A 1 103 ? -2.619  15.412  18.837 1.00 28.27  ? 103 VAL A CG1    1 
ATOM   760   C CG2    . VAL A 1 103 ? -3.811  17.474  18.160 1.00 31.51  ? 103 VAL A CG2    1 
ATOM   761   N N      . LEU A 1 104 ? -4.953  13.162  19.531 1.00 30.98  ? 104 LEU A N      1 
ATOM   762   C CA     . LEU A 1 104 ? -4.751  11.995  20.365 1.00 36.72  ? 104 LEU A CA     1 
ATOM   763   C C      . LEU A 1 104 ? -3.294  11.671  20.317 1.00 37.69  ? 104 LEU A C      1 
ATOM   764   O O      . LEU A 1 104 ? -2.715  11.625  19.248 1.00 31.21  ? 104 LEU A O      1 
ATOM   765   C CB     . LEU A 1 104 ? -5.526  10.795  19.862 1.00 33.83  ? 104 LEU A CB     1 
ATOM   766   C CG     . LEU A 1 104 ? -5.643  9.608   20.827 1.00 35.08  ? 104 LEU A CG     1 
ATOM   767   C CD1    . LEU A 1 104 ? -7.016  8.971   20.777 1.00 36.15  ? 104 LEU A CD1    1 
ATOM   768   C CD2    . LEU A 1 104 ? -4.572  8.558   20.603 1.00 40.37  ? 104 LEU A CD2    1 
ATOM   769   N N      . LEU A 1 105 ? -2.691  11.440  21.469 1.00 36.99  ? 105 LEU A N      1 
ATOM   770   C CA     . LEU A 1 105 ? -1.280  11.194  21.539 1.00 34.98  ? 105 LEU A CA     1 
ATOM   771   C C      . LEU A 1 105 ? -1.082  9.875   22.197 1.00 35.01  ? 105 LEU A C      1 
ATOM   772   O O      . LEU A 1 105 ? -1.968  9.385   22.861 1.00 37.55  ? 105 LEU A O      1 
ATOM   773   C CB     . LEU A 1 105 ? -0.653  12.247  22.404 1.00 34.35  ? 105 LEU A CB     1 
ATOM   774   C CG     . LEU A 1 105 ? -0.395  13.630  21.866 1.00 37.27  ? 105 LEU A CG     1 
ATOM   775   C CD1    . LEU A 1 105 ? -0.977  14.589  22.875 1.00 35.32  ? 105 LEU A CD1    1 
ATOM   776   C CD2    . LEU A 1 105 ? 1.109   13.770  21.801 1.00 42.52  ? 105 LEU A CD2    1 
ATOM   777   N N      . THR A 1 106 ? 0.081   9.287   22.017 1.00 34.69  ? 106 THR A N      1 
ATOM   778   C CA     . THR A 1 106 ? 0.313   8.014   22.600 1.00 37.25  ? 106 THR A CA     1 
ATOM   779   C C      . THR A 1 106 ? 1.423   8.141   23.558 1.00 43.65  ? 106 THR A C      1 
ATOM   780   O O      . THR A 1 106 ? 2.370   8.863   23.322 1.00 47.60  ? 106 THR A O      1 
ATOM   781   C CB     . THR A 1 106 ? 0.699   6.984   21.580 1.00 36.83  ? 106 THR A CB     1 
ATOM   782   O OG1    . THR A 1 106 ? 1.868   7.430   20.895 1.00 43.06  ? 106 THR A OG1    1 
ATOM   783   C CG2    . THR A 1 106 ? -0.429  6.760   20.598 1.00 38.36  ? 106 THR A CG2    1 
ATOM   784   N N      . GLU A 1 107 ? 1.336   7.394   24.638 1.00 43.18  ? 107 GLU A N      1 
ATOM   785   C CA     . GLU A 1 107 ? 2.327   7.443   25.654 1.00 38.68  ? 107 GLU A CA     1 
ATOM   786   C C      . GLU A 1 107 ? 2.774   6.055   25.933 1.00 44.66  ? 107 GLU A C      1 
ATOM   787   O O      . GLU A 1 107 ? 1.999   5.120   25.899 1.00 43.74  ? 107 GLU A O      1 
ATOM   788   C CB     . GLU A 1 107 ? 1.708   8.020   26.912 1.00 47.19  ? 107 GLU A CB     1 
ATOM   789   C CG     . GLU A 1 107 ? 0.414   7.372   27.352 1.00 49.72  ? 107 GLU A CG     1 
ATOM   790   C CD     . GLU A 1 107 ? -0.012  7.825   28.725 1.00 50.85  ? 107 GLU A CD     1 
ATOM   791   O OE1    . GLU A 1 107 ? 0.814   8.440   29.422 1.00 49.07  ? 107 GLU A OE1    1 
ATOM   792   O OE2    . GLU A 1 107 ? -1.167  7.562   29.109 1.00 48.49  ? 107 GLU A OE2    1 
ATOM   793   N N      . ALA A 1 108 ? 4.043   5.904   26.226 1.00 47.25  ? 108 ALA A N      1 
ATOM   794   C CA     . ALA A 1 108 ? 4.573   4.596   26.469 1.00 45.00  ? 108 ALA A CA     1 
ATOM   795   C C      . ALA A 1 108 ? 4.033   4.027   27.724 1.00 40.96  ? 108 ALA A C      1 
ATOM   796   O O      . ALA A 1 108 ? 3.513   4.731   28.567 1.00 41.15  ? 108 ALA A O      1 
ATOM   797   C CB     . ALA A 1 108 ? 6.072   4.659   26.551 1.00 41.18  ? 108 ALA A CB     1 
ATOM   798   N N      . PRO A 1 109 ? 4.133   2.688   27.864 1.00 40.11  ? 109 PRO A N      1 
ATOM   799   C CA     . PRO A 1 109 ? 3.713   2.183   29.155 1.00 38.06  ? 109 PRO A CA     1 
ATOM   800   C C      . PRO A 1 109 ? 4.581   2.700   30.254 1.00 36.66  ? 109 PRO A C      1 
ATOM   801   O O      . PRO A 1 109 ? 5.773   2.846   30.044 1.00 36.76  ? 109 PRO A O      1 
ATOM   802   C CB     . PRO A 1 109 ? 3.941   0.708   29.003 1.00 37.79  ? 109 PRO A CB     1 
ATOM   803   C CG     . PRO A 1 109 ? 3.606   0.437   27.597 1.00 35.65  ? 109 PRO A CG     1 
ATOM   804   C CD     . PRO A 1 109 ? 4.275   1.564   26.901 1.00 39.61  ? 109 PRO A CD     1 
ATOM   805   N N      . LEU A 1 110 ? 3.997   2.951   31.414 1.00 36.02  ? 110 LEU A N      1 
ATOM   806   C CA     . LEU A 1 110 ? 4.736   3.410   32.581 1.00 34.94  ? 110 LEU A CA     1 
ATOM   807   C C      . LEU A 1 110 ? 5.432   4.746   32.412 1.00 41.86  ? 110 LEU A C      1 
ATOM   808   O O      . LEU A 1 110 ? 6.517   4.938   32.938 1.00 42.07  ? 110 LEU A O      1 
ATOM   809   C CB     . LEU A 1 110 ? 5.704   2.330   33.047 1.00 31.14  ? 110 LEU A CB     1 
ATOM   810   C CG     . LEU A 1 110 ? 5.181   0.921   33.313 1.00 33.34  ? 110 LEU A CG     1 
ATOM   811   C CD1    . LEU A 1 110 ? 6.317   0.014   33.748 1.00 30.04  ? 110 LEU A CD1    1 
ATOM   812   C CD2    . LEU A 1 110 ? 4.095   0.950   34.369 1.00 39.19  ? 110 LEU A CD2    1 
ATOM   813   N N      . ASN A 1 111 ? 4.803   5.677   31.696 1.00 43.04  ? 111 ASN A N      1 
ATOM   814   C CA     . ASN A 1 111 ? 5.384   6.994   31.464 1.00 41.80  ? 111 ASN A CA     1 
ATOM   815   C C      . ASN A 1 111 ? 5.170   7.668   32.768 1.00 47.83  ? 111 ASN A C      1 
ATOM   816   O O      . ASN A 1 111 ? 4.093   7.582   33.330 1.00 48.66  ? 111 ASN A O      1 
ATOM   817   C CB     . ASN A 1 111 ? 4.656   7.744   30.358 1.00 39.44  ? 111 ASN A CB     1 
ATOM   818   C CG     . ASN A 1 111 ? 5.593   8.459   29.420 1.00 41.86  ? 111 ASN A CG     1 
ATOM   819   O OD1    . ASN A 1 111 ? 6.784   8.194   29.409 1.00 46.77  ? 111 ASN A OD1    1 
ATOM   820   N ND2    . ASN A 1 111 ? 5.056   9.365   28.618 1.00 37.05  ? 111 ASN A ND2    1 
ATOM   821   N N      . PRO A 1 112 ? 6.208   8.364   33.272 1.00 43.51  ? 112 PRO A N      1 
ATOM   822   C CA     . PRO A 1 112 ? 5.948   8.899   34.583 1.00 41.46  ? 112 PRO A CA     1 
ATOM   823   C C      . PRO A 1 112 ? 4.848   9.906   34.568 1.00 44.55  ? 112 PRO A C      1 
ATOM   824   O O      . PRO A 1 112 ? 4.528   10.435  33.532 1.00 41.64  ? 112 PRO A O      1 
ATOM   825   C CB     . PRO A 1 112 ? 7.264   9.537   34.937 1.00 41.26  ? 112 PRO A CB     1 
ATOM   826   C CG     . PRO A 1 112 ? 8.283   8.766   34.198 1.00 34.60  ? 112 PRO A CG     1 
ATOM   827   C CD     . PRO A 1 112 ? 7.614   8.623   32.885 1.00 39.24  ? 112 PRO A CD     1 
ATOM   828   N N      . LYS A 1 113 ? 4.278   10.201  35.725 1.00 45.16  ? 113 LYS A N      1 
ATOM   829   C CA     . LYS A 1 113 ? 3.206   11.164  35.821 1.00 46.02  ? 113 LYS A CA     1 
ATOM   830   C C      . LYS A 1 113 ? 3.653   12.517  35.389 1.00 46.22  ? 113 LYS A C      1 
ATOM   831   O O      . LYS A 1 113 ? 2.844   13.323  34.993 1.00 45.64  ? 113 LYS A O      1 
ATOM   832   C CB     . LYS A 1 113 ? 2.669   11.215  37.223 1.00 47.22  ? 113 LYS A CB     1 
ATOM   833   C CG     . LYS A 1 113 ? 3.728   11.201  38.309 1.00 64.86  ? 113 LYS A CG     1 
ATOM   834   C CD     . LYS A 1 113 ? 3.120   11.501  39.668 1.00 76.37  ? 113 LYS A CD     1 
ATOM   835   C CE     . LYS A 1 113 ? 2.516   12.894  39.693 1.00 86.86  ? 113 LYS A CE     1 
ATOM   836   N NZ     . LYS A 1 113 ? 1.811   13.177  40.970 1.00 64.69  ? 113 LYS A NZ     1 
ATOM   837   N N      . ALA A 1 114 ? 4.934   12.799  35.480 1.00 50.06  ? 114 ALA A N      1 
ATOM   838   C CA     . ALA A 1 114 ? 5.475   14.037  34.977 1.00 46.55  ? 114 ALA A CA     1 
ATOM   839   C C      . ALA A 1 114 ? 5.425   14.184  33.492 1.00 48.51  ? 114 ALA A C      1 
ATOM   840   O O      . ALA A 1 114 ? 5.076   15.242  33.004 1.00 49.39  ? 114 ALA A O      1 
ATOM   841   C CB     . ALA A 1 114 ? 6.916   14.104  35.374 1.00 42.62  ? 114 ALA A CB     1 
ATOM   842   N N      . ASN A 1 115 ? 5.799   13.149  32.753 1.00 46.57  ? 115 ASN A N      1 
ATOM   843   C CA     . ASN A 1 115 ? 5.857   13.242  31.313 1.00 40.63  ? 115 ASN A CA     1 
ATOM   844   C C      . ASN A 1 115 ? 4.503   13.441  30.746 1.00 41.03  ? 115 ASN A C      1 
ATOM   845   O O      . ASN A 1 115 ? 4.333   14.157  29.786 1.00 43.11  ? 115 ASN A O      1 
ATOM   846   C CB     . ASN A 1 115 ? 6.520   12.044  30.707 1.00 38.11  ? 115 ASN A CB     1 
ATOM   847   C CG     . ASN A 1 115 ? 8.028   12.099  30.806 1.00 48.61  ? 115 ASN A CG     1 
ATOM   848   O OD1    . ASN A 1 115 ? 8.724   11.271  30.232 1.00 50.38  ? 115 ASN A OD1    1 
ATOM   849   N ND2    . ASN A 1 115 ? 8.541   13.081  31.526 1.00 53.45  ? 115 ASN A ND2    1 
ATOM   850   N N      . ARG A 1 116 ? 3.522   12.791  31.325 1.00 41.74  ? 116 ARG A N      1 
ATOM   851   C CA     . ARG A 1 116 ? 2.174   12.903  30.845 1.00 42.78  ? 116 ARG A CA     1 
ATOM   852   C C      . ARG A 1 116 ? 1.672   14.283  30.982 1.00 44.61  ? 116 ARG A C      1 
ATOM   853   O O      . ARG A 1 116 ? 1.048   14.798  30.087 1.00 47.61  ? 116 ARG A O      1 
ATOM   854   C CB     . ARG A 1 116 ? 1.316   12.005  31.672 1.00 46.64  ? 116 ARG A CB     1 
ATOM   855   C CG     . ARG A 1 116 ? 1.793   10.578  31.726 1.00 49.07  ? 116 ARG A CG     1 
ATOM   856   C CD     . ARG A 1 116 ? 1.075   9.860   32.841 1.00 51.71  ? 116 ARG A CD     1 
ATOM   857   N NE     . ARG A 1 116 ? -0.331  10.215  32.841 1.00 47.90  ? 116 ARG A NE     1 
ATOM   858   C CZ     . ARG A 1 116 ? -1.275  9.472   32.290 1.00 62.71  ? 116 ARG A CZ     1 
ATOM   859   N NH1    . ARG A 1 116 ? -0.957  8.326   31.718 1.00 68.78  ? 116 ARG A NH1    1 
ATOM   860   N NH2    . ARG A 1 116 ? -2.532  9.862   32.330 1.00 64.07  ? 116 ARG A NH2    1 
ATOM   861   N N      . GLU A 1 117 ? 1.948   14.900  32.105 1.00 44.54  ? 117 GLU A N      1 
ATOM   862   C CA     . GLU A 1 117 ? 1.548   16.266  32.323 1.00 47.57  ? 117 GLU A CA     1 
ATOM   863   C C      . GLU A 1 117 ? 2.202   17.247  31.386 1.00 48.10  ? 117 GLU A C      1 
ATOM   864   O O      . GLU A 1 117 ? 1.602   18.228  31.017 1.00 49.59  ? 117 GLU A O      1 
ATOM   865   C CB     . GLU A 1 117 ? 1.850   16.679  33.736 1.00 52.73  ? 117 GLU A CB     1 
ATOM   866   C CG     . GLU A 1 117 ? 1.000   16.021  34.792 1.00 57.20  ? 117 GLU A CG     1 
ATOM   867   C CD     . GLU A 1 117 ? 1.200   16.666  36.143 1.00 67.95  ? 117 GLU A CD     1 
ATOM   868   O OE1    . GLU A 1 117 ? 1.906   17.691  36.203 1.00 71.42  ? 117 GLU A OE1    1 
ATOM   869   O OE2    . GLU A 1 117 ? 0.651   16.158  37.140 1.00 74.08  ? 117 GLU A OE2    1 
ATOM   870   N N      . LYS A 1 118 ? 3.457   17.034  31.057 1.00 44.29  ? 118 LYS A N      1 
ATOM   871   C CA     . LYS A 1 118 ? 4.140   17.972  30.218 1.00 44.85  ? 118 LYS A CA     1 
ATOM   872   C C      . LYS A 1 118 ? 3.597   17.889  28.825 1.00 49.07  ? 118 LYS A C      1 
ATOM   873   O O      . LYS A 1 118 ? 3.591   18.853  28.099 1.00 48.80  ? 118 LYS A O      1 
ATOM   874   C CB     . LYS A 1 118 ? 5.628   17.714  30.226 1.00 38.18  ? 118 LYS A CB     1 
ATOM   875   C CG     . LYS A 1 118 ? 6.350   18.183  31.463 1.00 50.41  ? 118 LYS A CG     1 
ATOM   876   C CD     . LYS A 1 118 ? 7.565   18.996  31.064 1.00 58.17  ? 118 LYS A CD     1 
ATOM   877   C CE     . LYS A 1 118 ? 7.165   20.186  30.208 1.00 54.67  ? 118 LYS A CE     1 
ATOM   878   N NZ     . LYS A 1 118 ? 8.345   20.945  29.717 1.00 53.65  ? 118 LYS A NZ     1 
ATOM   879   N N      . MET A 1 119 ? 3.122   16.732  28.445 1.00 43.20  ? 119 MET A N      1 
ATOM   880   C CA     . MET A 1 119 ? 2.588   16.545  27.111 1.00 43.10  ? 119 MET A CA     1 
ATOM   881   C C      . MET A 1 119 ? 1.313   17.296  26.983 1.00 43.44  ? 119 MET A C      1 
ATOM   882   O O      . MET A 1 119 ? 1.087   17.947  25.990 1.00 44.83  ? 119 MET A O      1 
ATOM   883   C CB     . MET A 1 119 ? 2.312   15.071  26.898 1.00 49.35  ? 119 MET A CB     1 
ATOM   884   C CG     . MET A 1 119 ? 2.562   14.531  25.507 1.00 53.96  ? 119 MET A CG     1 
ATOM   885   S SD     . MET A 1 119 ? 2.507   12.729  25.469 1.00 51.67  ? 119 MET A SD     1 
ATOM   886   C CE     . MET A 1 119 ? 3.832   12.308  26.587 1.00 34.99  ? 119 MET A CE     1 
ATOM   887   N N      . THR A 1 120 ? 0.466   17.212  27.993 1.00 39.97  ? 120 THR A N      1 
ATOM   888   C CA     . THR A 1 120 ? -0.775  17.954  27.986 1.00 40.49  ? 120 THR A CA     1 
ATOM   889   C C      . THR A 1 120 ? -0.525  19.446  27.947 1.00 43.20  ? 120 THR A C      1 
ATOM   890   O O      . THR A 1 120 ? -1.248  20.172  27.294 1.00 42.20  ? 120 THR A O      1 
ATOM   891   C CB     . THR A 1 120 ? -1.621  17.596  29.193 1.00 35.27  ? 120 THR A CB     1 
ATOM   892   O OG1    . THR A 1 120 ? -0.960  18.028  30.380 1.00 47.28  ? 120 THR A OG1    1 
ATOM   893   C CG2    . THR A 1 120 ? -1.808  16.117  29.257 1.00 33.82  ? 120 THR A CG2    1 
ATOM   894   N N      . GLN A 1 121 ? 0.506   19.913  28.621 1.00 42.53  ? 121 GLN A N      1 
ATOM   895   C CA     . GLN A 1 121 ? 0.842   21.308  28.606 1.00 42.19  ? 121 GLN A CA     1 
ATOM   896   C C      . GLN A 1 121 ? 1.375   21.683  27.287 1.00 45.14  ? 121 GLN A C      1 
ATOM   897   O O      . GLN A 1 121 ? 0.877   22.590  26.675 1.00 49.27  ? 121 GLN A O      1 
ATOM   898   C CB     . GLN A 1 121 ? 1.912   21.542  29.644 1.00 47.30  ? 121 GLN A CB     1 
ATOM   899   C CG     . GLN A 1 121 ? 2.660   22.855  29.563 1.00 55.45  ? 121 GLN A CG     1 
ATOM   900   C CD     . GLN A 1 121 ? 3.826   22.903  30.529 1.00 61.91  ? 121 GLN A CD     1 
ATOM   901   O OE1    . GLN A 1 121 ? 3.807   22.253  31.572 1.00 60.27  ? 121 GLN A OE1    1 
ATOM   902   N NE2    . GLN A 1 121 ? 4.848   23.673  30.187 1.00 61.97  ? 121 GLN A NE2    1 
ATOM   903   N N      . ILE A 1 122 ? 2.383   20.987  26.815 1.00 43.12  ? 122 ILE A N      1 
ATOM   904   C CA     . ILE A 1 122 ? 2.993   21.366  25.562 1.00 44.74  ? 122 ILE A CA     1 
ATOM   905   C C      . ILE A 1 122 ? 1.952   21.437  24.466 1.00 40.03  ? 122 ILE A C      1 
ATOM   906   O O      . ILE A 1 122 ? 1.917   22.366  23.697 1.00 42.92  ? 122 ILE A O      1 
ATOM   907   C CB     . ILE A 1 122 ? 4.145   20.431  25.193 1.00 38.55  ? 122 ILE A CB     1 
ATOM   908   C CG1    . ILE A 1 122 ? 5.331   20.681  26.117 1.00 40.48  ? 122 ILE A CG1    1 
ATOM   909   C CG2    . ILE A 1 122 ? 4.583   20.647  23.759 1.00 36.77  ? 122 ILE A CG2    1 
ATOM   910   C CD1    . ILE A 1 122 ? 6.640   20.181  25.562 1.00 36.88  ? 122 ILE A CD1    1 
ATOM   911   N N      . MET A 1 123 ? 1.034   20.502  24.437 1.00 40.31  ? 123 MET A N      1 
ATOM   912   C CA     . MET A 1 123 ? -0.015  20.569  23.445 1.00 42.04  ? 123 MET A CA     1 
ATOM   913   C C      . MET A 1 123 ? -0.919  21.764  23.603 1.00 40.75  ? 123 MET A C      1 
ATOM   914   O O      . MET A 1 123 ? -1.001  22.578  22.711 1.00 46.60  ? 123 MET A O      1 
ATOM   915   C CB     . MET A 1 123 ? -0.826  19.291  23.407 1.00 46.23  ? 123 MET A CB     1 
ATOM   916   C CG     . MET A 1 123 ? -0.044  18.098  22.918 1.00 43.90  ? 123 MET A CG     1 
ATOM   917   S SD     . MET A 1 123 ? -0.173  17.970  21.142 1.00 35.32  ? 123 MET A SD     1 
ATOM   918   C CE     . MET A 1 123 ? 1.353   17.139  20.784 1.00 34.63  ? 123 MET A CE     1 
ATOM   919   N N      . PHE A 1 124 ? -1.616  21.880  24.711 1.00 36.69  ? 124 PHE A N      1 
ATOM   920   C CA     . PHE A 1 124 ? -2.543  22.978  24.832 1.00 43.08  ? 124 PHE A CA     1 
ATOM   921   C C      . PHE A 1 124 ? -1.852  24.339  24.810 1.00 44.82  ? 124 PHE A C      1 
ATOM   922   O O      . PHE A 1 124 ? -2.386  25.292  24.277 1.00 41.56  ? 124 PHE A O      1 
ATOM   923   C CB     . PHE A 1 124 ? -3.372  22.858  26.092 1.00 40.05  ? 124 PHE A CB     1 
ATOM   924   C CG     . PHE A 1 124 ? -4.454  21.826  26.039 1.00 39.96  ? 124 PHE A CG     1 
ATOM   925   C CD1    . PHE A 1 124 ? -5.641  22.091  25.405 1.00 41.16  ? 124 PHE A CD1    1 
ATOM   926   C CD2    . PHE A 1 124 ? -4.305  20.619  26.683 1.00 37.64  ? 124 PHE A CD2    1 
ATOM   927   C CE1    . PHE A 1 124 ? -6.647  21.159  25.377 1.00 34.69  ? 124 PHE A CE1    1 
ATOM   928   C CE2    . PHE A 1 124 ? -5.305  19.680  26.663 1.00 33.23  ? 124 PHE A CE2    1 
ATOM   929   C CZ     . PHE A 1 124 ? -6.478  19.953  26.007 1.00 35.29  ? 124 PHE A CZ     1 
ATOM   930   N N      . GLU A 1 125 ? -0.683  24.450  25.412 1.00 39.53  ? 125 GLU A N      1 
ATOM   931   C CA     . GLU A 1 125 ? 0.043   25.692  25.374 1.00 37.09  ? 125 GLU A CA     1 
ATOM   932   C C      . GLU A 1 125 ? 0.750   25.947  24.056 1.00 42.53  ? 125 GLU A C      1 
ATOM   933   O O      . GLU A 1 125 ? 0.388   26.873  23.351 1.00 52.13  ? 125 GLU A O      1 
ATOM   934   C CB     . GLU A 1 125 ? 1.008   25.778  26.540 1.00 42.44  ? 125 GLU A CB     1 
ATOM   935   C CG     . GLU A 1 125 ? 0.304   25.851  27.881 1.00 48.72  ? 125 GLU A CG     1 
ATOM   936   C CD     . GLU A 1 125 ? 1.237   26.214  29.010 1.00 52.20  ? 125 GLU A CD     1 
ATOM   937   O OE1    . GLU A 1 125 ? 2.441   26.403  28.746 1.00 53.73  ? 125 GLU A OE1    1 
ATOM   938   O OE2    . GLU A 1 125 ? 0.768   26.309  30.160 1.00 50.99  ? 125 GLU A OE2    1 
ATOM   939   N N      . THR A 1 126 ? 1.731   25.133  23.685 1.00 38.50  ? 126 THR A N      1 
ATOM   940   C CA     . THR A 1 126 ? 2.503   25.402  22.471 1.00 33.80  ? 126 THR A CA     1 
ATOM   941   C C      . THR A 1 126 ? 1.759   25.183  21.158 1.00 32.20  ? 126 THR A C      1 
ATOM   942   O O      . THR A 1 126 ? 1.970   25.918  20.207 1.00 39.64  ? 126 THR A O      1 
ATOM   943   C CB     . THR A 1 126 ? 3.838   24.663  22.490 1.00 33.08  ? 126 THR A CB     1 
ATOM   944   O OG1    . THR A 1 126 ? 4.432   24.789  23.785 1.00 29.43  ? 126 THR A OG1    1 
ATOM   945   C CG2    . THR A 1 126 ? 4.788   25.220  21.456 1.00 33.98  ? 126 THR A CG2    1 
ATOM   946   N N      . PHE A 1 127 ? 0.877   24.198  21.094 1.00 34.06  ? 127 PHE A N      1 
ATOM   947   C CA     . PHE A 1 127 ? 0.100   23.963  19.886 1.00 37.33  ? 127 PHE A CA     1 
ATOM   948   C C      . PHE A 1 127 ? -1.389  24.315  19.912 1.00 38.14  ? 127 PHE A C      1 
ATOM   949   O O      . PHE A 1 127 ? -2.086  24.031  18.962 1.00 41.09  ? 127 PHE A O      1 
ATOM   950   C CB     . PHE A 1 127 ? 0.308   22.536  19.440 1.00 36.03  ? 127 PHE A CB     1 
ATOM   951   C CG     . PHE A 1 127 ? 1.749   22.163  19.249 1.00 39.88  ? 127 PHE A CG     1 
ATOM   952   C CD1    . PHE A 1 127 ? 2.449   22.599  18.145 1.00 40.03  ? 127 PHE A CD1    1 
ATOM   953   C CD2    . PHE A 1 127 ? 2.395   21.362  20.167 1.00 38.65  ? 127 PHE A CD2    1 
ATOM   954   C CE1    . PHE A 1 127 ? 3.770   22.256  17.967 1.00 39.98  ? 127 PHE A CE1    1 
ATOM   955   C CE2    . PHE A 1 127 ? 3.715   21.015  19.996 1.00 36.25  ? 127 PHE A CE2    1 
ATOM   956   C CZ     . PHE A 1 127 ? 4.405   21.463  18.894 1.00 38.61  ? 127 PHE A CZ     1 
ATOM   957   N N      . ASN A 1 128 ? -1.875  24.930  20.972 1.00 37.60  ? 128 ASN A N      1 
ATOM   958   C CA     . ASN A 1 128 ? -3.281  25.348  21.102 1.00 36.32  ? 128 ASN A CA     1 
ATOM   959   C C      . ASN A 1 128 ? -4.354  24.344  20.794 1.00 39.81  ? 128 ASN A C      1 
ATOM   960   O O      . ASN A 1 128 ? -5.492  24.718  20.577 1.00 38.45  ? 128 ASN A O      1 
ATOM   961   C CB     . ASN A 1 128 ? -3.531  26.635  20.350 1.00 39.18  ? 128 ASN A CB     1 
ATOM   962   C CG     . ASN A 1 128 ? -4.571  27.507  21.017 1.00 49.17  ? 128 ASN A CG     1 
ATOM   963   O OD1    . ASN A 1 128 ? -4.926  27.289  22.172 1.00 57.72  ? 128 ASN A OD1    1 
ATOM   964   N ND2    . ASN A 1 128 ? -5.070  28.497  20.291 1.00 54.72  ? 128 ASN A ND2    1 
ATOM   965   N N      . THR A 1 129 ? -4.000  23.076  20.813 1.00 46.47  ? 129 THR A N      1 
ATOM   966   C CA     . THR A 1 129 ? -4.942  22.037  20.481 1.00 43.53  ? 129 THR A CA     1 
ATOM   967   C C      . THR A 1 129 ? -6.272  22.267  21.176 1.00 43.45  ? 129 THR A C      1 
ATOM   968   O O      . THR A 1 129 ? -6.296  22.538  22.359 1.00 49.36  ? 129 THR A O      1 
ATOM   969   C CB     . THR A 1 129 ? -4.376  20.651  20.786 1.00 40.46  ? 129 THR A CB     1 
ATOM   970   O OG1    . THR A 1 129 ? -4.153  20.521  22.189 1.00 47.65  ? 129 THR A OG1    1 
ATOM   971   C CG2    . THR A 1 129 ? -3.067  20.472  20.069 1.00 37.63  ? 129 THR A CG2    1 
ATOM   972   N N      . PRO A 1 130 ? -7.399  22.176  20.449 1.00 38.62  ? 130 PRO A N      1 
ATOM   973   C CA     . PRO A 1 130 ? -8.628  22.360  21.198 1.00 34.35  ? 130 PRO A CA     1 
ATOM   974   C C      . PRO A 1 130 ? -8.947  21.255  22.165 1.00 35.23  ? 130 PRO A C      1 
ATOM   975   O O      . PRO A 1 130 ? -9.689  21.507  23.096 1.00 36.51  ? 130 PRO A O      1 
ATOM   976   C CB     . PRO A 1 130 ? -9.674  22.368  20.108 1.00 39.02  ? 130 PRO A CB     1 
ATOM   977   C CG     . PRO A 1 130 ? -9.111  21.576  19.004 1.00 39.85  ? 130 PRO A CG     1 
ATOM   978   C CD     . PRO A 1 130 ? -7.695  22.020  19.005 1.00 41.53  ? 130 PRO A CD     1 
ATOM   979   N N      . ALA A 1 131 ? -8.432  20.055  21.945 1.00 33.46  ? 131 ALA A N      1 
ATOM   980   C CA     . ALA A 1 131 ? -8.705  18.931  22.816 1.00 34.37  ? 131 ALA A CA     1 
ATOM   981   C C      . ALA A 1 131 ? -7.625  17.903  22.717 1.00 39.34  ? 131 ALA A C      1 
ATOM   982   O O      . ALA A 1 131 ? -6.891  17.893  21.752 1.00 40.14  ? 131 ALA A O      1 
ATOM   983   C CB     . ALA A 1 131 ? -10.044 18.339  22.514 1.00 25.42  ? 131 ALA A CB     1 
ATOM   984   N N      . MET A 1 132 ? -7.501  17.046  23.719 1.00 39.66  ? 132 MET A N      1 
ATOM   985   C CA     . MET A 1 132 ? -6.404  16.109  23.743 1.00 37.03  ? 132 MET A CA     1 
ATOM   986   C C      . MET A 1 132 ? -6.700  14.856  24.489 1.00 40.38  ? 132 MET A C      1 
ATOM   987   O O      . MET A 1 132 ? -7.519  14.874  25.383 1.00 41.53  ? 132 MET A O      1 
ATOM   988   C CB     . MET A 1 132 ? -5.269  16.765  24.505 1.00 39.24  ? 132 MET A CB     1 
ATOM   989   C CG     . MET A 1 132 ? -3.893  16.568  23.943 1.00 46.95  ? 132 MET A CG     1 
ATOM   990   S SD     . MET A 1 132 ? -2.806  16.593  25.361 1.00 57.35  ? 132 MET A SD     1 
ATOM   991   C CE     . MET A 1 132 ? -3.258  15.047  26.126 1.00 61.29  ? 132 MET A CE     1 
ATOM   992   N N      . TYR A 1 133 ? -6.057  13.753  24.127 1.00 41.41  ? 133 TYR A N      1 
ATOM   993   C CA     . TYR A 1 133 ? -6.168  12.538  24.907 1.00 36.91  ? 133 TYR A CA     1 
ATOM   994   C C      . TYR A 1 133 ? -4.854  11.866  24.788 1.00 34.15  ? 133 TYR A C      1 
ATOM   995   O O      . TYR A 1 133 ? -4.277  11.833  23.728 1.00 32.47  ? 133 TYR A O      1 
ATOM   996   C CB     . TYR A 1 133 ? -7.264  11.617  24.441 1.00 35.17  ? 133 TYR A CB     1 
ATOM   997   C CG     . TYR A 1 133 ? -7.729  10.616  25.467 1.00 39.01  ? 133 TYR A CG     1 
ATOM   998   C CD1    . TYR A 1 133 ? -8.728  10.936  26.360 1.00 37.06  ? 133 TYR A CD1    1 
ATOM   999   C CD2    . TYR A 1 133 ? -7.187  9.345   25.526 1.00 42.40  ? 133 TYR A CD2    1 
ATOM   1000  C CE1    . TYR A 1 133 ? -9.166  10.028  27.297 1.00 42.61  ? 133 TYR A CE1    1 
ATOM   1001  C CE2    . TYR A 1 133 ? -7.616  8.430   26.460 1.00 38.25  ? 133 TYR A CE2    1 
ATOM   1002  C CZ     . TYR A 1 133 ? -8.608  8.780   27.343 1.00 49.97  ? 133 TYR A CZ     1 
ATOM   1003  O OH     . TYR A 1 133 ? -9.048  7.876   28.278 1.00 60.92  ? 133 TYR A OH     1 
ATOM   1004  N N      . VAL A 1 134 ? -4.386  11.314  25.882 1.00 33.18  ? 134 VAL A N      1 
ATOM   1005  C CA     . VAL A 1 134 ? -3.131  10.624  25.882 1.00 39.86  ? 134 VAL A CA     1 
ATOM   1006  C C      . VAL A 1 134 ? -3.480  9.193   26.223 1.00 38.94  ? 134 VAL A C      1 
ATOM   1007  O O      . VAL A 1 134 ? -4.328  8.961   27.066 1.00 46.14  ? 134 VAL A O      1 
ATOM   1008  C CB     . VAL A 1 134 ? -2.139  11.295  26.853 1.00 41.18  ? 134 VAL A CB     1 
ATOM   1009  C CG1    . VAL A 1 134 ? -2.376  10.899  28.297 1.00 45.63  ? 134 VAL A CG1    1 
ATOM   1010  C CG2    . VAL A 1 134 ? -0.700  11.064  26.432 1.00 37.28  ? 134 VAL A CG2    1 
ATOM   1011  N N      . ALA A 1 135 ? -2.894  8.221   25.532 1.00 32.94  ? 135 ALA A N      1 
ATOM   1012  C CA     . ALA A 1 135 ? -3.289  6.873   25.781 1.00 36.51  ? 135 ALA A CA     1 
ATOM   1013  C C      . ALA A 1 135 ? -2.215  5.869   25.546 1.00 38.62  ? 135 ALA A C      1 
ATOM   1014  O O      . ALA A 1 135 ? -1.449  6.007   24.615 1.00 38.08  ? 135 ALA A O      1 
ATOM   1015  C CB     . ALA A 1 135 ? -4.496  6.563   24.967 1.00 31.16  ? 135 ALA A CB     1 
ATOM   1016  N N      . ILE A 1 136 ? -2.163  4.846   26.387 1.00 41.38  ? 136 ILE A N      1 
ATOM   1017  C CA     . ILE A 1 136 ? -1.099  3.874   26.303 1.00 42.58  ? 136 ILE A CA     1 
ATOM   1018  C C      . ILE A 1 136 ? -1.120  3.221   24.972 1.00 38.95  ? 136 ILE A C      1 
ATOM   1019  O O      . ILE A 1 136 ? -2.161  2.831   24.492 1.00 37.58  ? 136 ILE A O      1 
ATOM   1020  C CB     . ILE A 1 136 ? -1.172  2.835   27.431 1.00 45.86  ? 136 ILE A CB     1 
ATOM   1021  C CG1    . ILE A 1 136 ? -1.067  3.512   28.797 1.00 44.17  ? 136 ILE A CG1    1 
ATOM   1022  C CG2    . ILE A 1 136 ? -0.075  1.798   27.287 1.00 42.82  ? 136 ILE A CG2    1 
ATOM   1023  C CD1    . ILE A 1 136 ? -2.373  4.074   29.314 1.00 52.69  ? 136 ILE A CD1    1 
ATOM   1024  N N      . GLN A 1 137 ? 0.033   3.098   24.366 1.00 37.75  ? 137 GLN A N      1 
ATOM   1025  C CA     . GLN A 1 137 ? 0.121   2.521   23.059 1.00 37.28  ? 137 GLN A CA     1 
ATOM   1026  C C      . GLN A 1 137 ? -0.474  1.142   22.981 1.00 36.21  ? 137 GLN A C      1 
ATOM   1027  O O      . GLN A 1 137 ? -1.237  0.855   22.085 1.00 36.50  ? 137 GLN A O      1 
ATOM   1028  C CB     . GLN A 1 137 ? 1.588   2.499   22.645 1.00 37.98  ? 137 GLN A CB     1 
ATOM   1029  C CG     . GLN A 1 137 ? 2.204   3.883   22.579 1.00 38.97  ? 137 GLN A CG     1 
ATOM   1030  C CD     . GLN A 1 137 ? 3.696   3.850   22.364 1.00 44.63  ? 137 GLN A CD     1 
ATOM   1031  O OE1    . GLN A 1 137 ? 4.348   2.854   22.653 1.00 50.64  ? 137 GLN A OE1    1 
ATOM   1032  N NE2    . GLN A 1 137 ? 4.246   4.944   21.866 1.00 45.79  ? 137 GLN A NE2    1 
ATOM   1033  N N      . ALA A 1 138 ? -0.216  0.290   23.934 1.00 32.79  ? 138 ALA A N      1 
ATOM   1034  C CA     . ALA A 1 138 ? -0.660  -1.067  23.809 1.00 30.96  ? 138 ALA A CA     1 
ATOM   1035  C C      . ALA A 1 138 ? -2.073  -1.345  24.056 1.00 31.23  ? 138 ALA A C      1 
ATOM   1036  O O      . ALA A 1 138 ? -2.587  -2.302  23.560 1.00 35.44  ? 138 ALA A O      1 
ATOM   1037  C CB     . ALA A 1 138 ? 0.139   -1.906  24.706 1.00 29.14  ? 138 ALA A CB     1 
ATOM   1038  N N      . VAL A 1 139 ? -2.733  -0.543  24.836 1.00 30.08  ? 139 VAL A N      1 
ATOM   1039  C CA     . VAL A 1 139 ? -4.128  -0.758  25.003 1.00 31.53  ? 139 VAL A CA     1 
ATOM   1040  C C      . VAL A 1 139 ? -4.723  -0.537  23.673 1.00 34.75  ? 139 VAL A C      1 
ATOM   1041  O O      . VAL A 1 139 ? -5.621  -1.235  23.278 1.00 38.89  ? 139 VAL A O      1 
ATOM   1042  C CB     . VAL A 1 139 ? -4.744  0.120   26.087 1.00 30.55  ? 139 VAL A CB     1 
ATOM   1043  C CG1    . VAL A 1 139 ? -4.118  -0.163  27.433 1.00 28.90  ? 139 VAL A CG1    1 
ATOM   1044  C CG2    . VAL A 1 139 ? -4.662  1.594   25.780 1.00 36.58  ? 139 VAL A CG2    1 
ATOM   1045  N N      . LEU A 1 140 ? -4.224  0.443   22.961 1.00 32.33  ? 140 LEU A N      1 
ATOM   1046  C CA     . LEU A 1 140 ? -4.732  0.758   21.661 1.00 32.67  ? 140 LEU A CA     1 
ATOM   1047  C C      . LEU A 1 140 ? -4.500  -0.375  20.691 1.00 36.73  ? 140 LEU A C      1 
ATOM   1048  O O      . LEU A 1 140 ? -5.338  -0.662  19.868 1.00 41.86  ? 140 LEU A O      1 
ATOM   1049  C CB     . LEU A 1 140 ? -4.155  2.073   21.150 1.00 34.21  ? 140 LEU A CB     1 
ATOM   1050  C CG     . LEU A 1 140 ? -4.361  3.392   21.881 1.00 30.86  ? 140 LEU A CG     1 
ATOM   1051  C CD1    . LEU A 1 140 ? -3.802  4.523   21.042 1.00 19.77  ? 140 LEU A CD1    1 
ATOM   1052  C CD2    . LEU A 1 140 ? -5.828  3.628   22.153 1.00 28.65  ? 140 LEU A CD2    1 
ATOM   1053  N N      . SER A 1 141 ? -3.379  -1.055  20.781 1.00 39.04  ? 141 SER A N      1 
ATOM   1054  C CA     . SER A 1 141 ? -3.091  -2.093  19.810 1.00 36.66  ? 141 SER A CA     1 
ATOM   1055  C C      . SER A 1 141 ? -4.037  -3.180  20.025 1.00 34.30  ? 141 SER A C      1 
ATOM   1056  O O      . SER A 1 141 ? -4.333  -3.911  19.116 1.00 46.09  ? 141 SER A O      1 
ATOM   1057  C CB     . SER A 1 141 ? -1.724  -2.646  20.003 1.00 34.99  ? 141 SER A CB     1 
ATOM   1058  O OG     . SER A 1 141 ? -0.763  -1.618  19.982 1.00 44.52  ? 141 SER A OG     1 
ATOM   1059  N N      . LEU A 1 142 ? -4.454  -3.361  21.253 1.00 34.44  ? 142 LEU A N      1 
ATOM   1060  C CA     . LEU A 1 142 ? -5.442  -4.359  21.587 1.00 39.61  ? 142 LEU A CA     1 
ATOM   1061  C C      . LEU A 1 142 ? -6.749  -3.936  21.040 1.00 39.33  ? 142 LEU A C      1 
ATOM   1062  O O      . LEU A 1 142 ? -7.533  -4.753  20.633 1.00 43.12  ? 142 LEU A O      1 
ATOM   1063  C CB     . LEU A 1 142 ? -5.526  -4.580  23.095 1.00 33.97  ? 142 LEU A CB     1 
ATOM   1064  C CG     . LEU A 1 142 ? -6.016  -5.872  23.723 1.00 32.78  ? 142 LEU A CG     1 
ATOM   1065  C CD1    . LEU A 1 142 ? -4.943  -6.930  23.683 1.00 28.51  ? 142 LEU A CD1    1 
ATOM   1066  C CD2    . LEU A 1 142 ? -6.351  -5.577  25.164 1.00 35.02  ? 142 LEU A CD2    1 
ATOM   1067  N N      . TYR A 1 143 ? -7.029  -2.658  21.051 1.00 34.26  ? 143 TYR A N      1 
ATOM   1068  C CA     . TYR A 1 143 ? -8.319  -2.212  20.638 1.00 31.15  ? 143 TYR A CA     1 
ATOM   1069  C C      . TYR A 1 143 ? -8.579  -2.547  19.213 1.00 34.83  ? 143 TYR A C      1 
ATOM   1070  O O      . TYR A 1 143 ? -9.684  -2.869  18.853 1.00 36.63  ? 143 TYR A O      1 
ATOM   1071  C CB     . TYR A 1 143 ? -8.435  -0.750  20.898 1.00 33.44  ? 143 TYR A CB     1 
ATOM   1072  C CG     . TYR A 1 143 ? -8.692  -0.411  22.340 1.00 36.87  ? 143 TYR A CG     1 
ATOM   1073  C CD1    . TYR A 1 143 ? -8.407  0.843   22.839 1.00 33.83  ? 143 TYR A CD1    1 
ATOM   1074  C CD2    . TYR A 1 143 ? -9.228  -1.347  23.199 1.00 35.51  ? 143 TYR A CD2    1 
ATOM   1075  C CE1    . TYR A 1 143 ? -8.648  1.152   24.156 1.00 33.06  ? 143 TYR A CE1    1 
ATOM   1076  C CE2    . TYR A 1 143 ? -9.470  -1.044  24.515 1.00 31.99  ? 143 TYR A CE2    1 
ATOM   1077  C CZ     . TYR A 1 143 ? -9.180  0.205   24.984 1.00 31.20  ? 143 TYR A CZ     1 
ATOM   1078  O OH     . TYR A 1 143 ? -9.426  0.500   26.296 1.00 37.25  ? 143 TYR A OH     1 
ATOM   1079  N N      . ALA A 1 144 ? -7.578  -2.459  18.376 1.00 35.73  ? 144 ALA A N      1 
ATOM   1080  C CA     . ALA A 1 144 ? -7.736  -2.852  17.000 1.00 37.34  ? 144 ALA A CA     1 
ATOM   1081  C C      . ALA A 1 144 ? -8.057  -4.299  16.911 1.00 38.98  ? 144 ALA A C      1 
ATOM   1082  O O      . ALA A 1 144 ? -8.872  -4.688  16.106 1.00 48.22  ? 144 ALA A O      1 
ATOM   1083  C CB     . ALA A 1 144 ? -6.458  -2.619  16.265 1.00 33.17  ? 144 ALA A CB     1 
ATOM   1084  N N      . SER A 1 145 ? -7.422  -5.116  17.727 1.00 36.64  ? 145 SER A N      1 
ATOM   1085  C CA     . SER A 1 145 ? -7.614  -6.542  17.704 1.00 38.07  ? 145 SER A CA     1 
ATOM   1086  C C      . SER A 1 145 ? -8.994  -6.872  18.094 1.00 38.82  ? 145 SER A C      1 
ATOM   1087  O O      . SER A 1 145 ? -9.471  -7.951  17.818 1.00 38.90  ? 145 SER A O      1 
ATOM   1088  C CB     . SER A 1 145 ? -6.702  -7.180  18.694 1.00 37.69  ? 145 SER A CB     1 
ATOM   1089  O OG     . SER A 1 145 ? -7.365  -7.354  19.921 1.00 37.45  ? 145 SER A OG     1 
ATOM   1090  N N      . GLY A 1 146 ? -9.653  -5.954  18.766 1.00 40.20  ? 146 GLY A N      1 
ATOM   1091  C CA     . GLY A 1 146 ? -11.025 -6.151  19.150 1.00 39.05  ? 146 GLY A CA     1 
ATOM   1092  C C      . GLY A 1 146 ? -11.197 -6.507  20.570 1.00 31.38  ? 146 GLY A C      1 
ATOM   1093  O O      . GLY A 1 146 ? -12.286 -6.861  20.975 1.00 33.81  ? 146 GLY A O      1 
ATOM   1094  N N      . ARG A 1 147 ? -10.145 -6.405  21.348 1.00 29.03  ? 147 ARG A N      1 
ATOM   1095  C CA     . ARG A 1 147 ? -10.235 -6.868  22.686 1.00 32.75  ? 147 ARG A CA     1 
ATOM   1096  C C      . ARG A 1 147 ? -10.016 -5.845  23.710 1.00 35.04  ? 147 ARG A C      1 
ATOM   1097  O O      . ARG A 1 147 ? -9.285  -4.913  23.485 1.00 38.01  ? 147 ARG A O      1 
ATOM   1098  C CB     . ARG A 1 147 ? -9.208  -7.950  22.860 1.00 36.56  ? 147 ARG A CB     1 
ATOM   1099  C CG     . ARG A 1 147 ? -9.505  -9.204  22.068 1.00 33.33  ? 147 ARG A CG     1 
ATOM   1100  C CD     . ARG A 1 147 ? -8.253  -9.971  21.707 1.00 32.62  ? 147 ARG A CD     1 
ATOM   1101  N NE     . ARG A 1 147 ? -8.609  -11.210 21.033 1.00 43.97  ? 147 ARG A NE     1 
ATOM   1102  C CZ     . ARG A 1 147 ? -8.708  -11.345 19.718 1.00 49.07  ? 147 ARG A CZ     1 
ATOM   1103  N NH1    . ARG A 1 147 ? -8.451  -10.324 18.927 1.00 52.70  ? 147 ARG A NH1    1 
ATOM   1104  N NH2    . ARG A 1 147 ? -9.049  -12.507 19.191 1.00 47.96  ? 147 ARG A NH2    1 
ATOM   1105  N N      . THR A 1 148 ? -10.654 -6.007  24.851 1.00 34.06  ? 148 THR A N      1 
ATOM   1106  C CA     . THR A 1 148 ? -10.445 -5.122  25.943 1.00 31.93  ? 148 THR A CA     1 
ATOM   1107  C C      . THR A 1 148 ? -9.551  -5.785  26.970 1.00 38.45  ? 148 THR A C      1 
ATOM   1108  O O      . THR A 1 148 ? -9.075  -5.108  27.855 1.00 41.70  ? 148 THR A O      1 
ATOM   1109  C CB     . THR A 1 148 ? -11.790 -4.721  26.554 1.00 31.11  ? 148 THR A CB     1 
ATOM   1110  O OG1    . THR A 1 148 ? -12.395 -5.853  27.175 1.00 42.62  ? 148 THR A OG1    1 
ATOM   1111  C CG2    . THR A 1 148 ? -12.713 -4.205  25.488 1.00 31.41  ? 148 THR A CG2    1 
ATOM   1112  N N      . THR A 1 149 ? -9.284  -7.088  26.849 1.00 35.69  ? 149 THR A N      1 
ATOM   1113  C CA     . THR A 1 149 ? -8.504  -7.829  27.850 1.00 33.33  ? 149 THR A CA     1 
ATOM   1114  C C      . THR A 1 149 ? -7.466  -8.689  27.217 1.00 30.18  ? 149 THR A C      1 
ATOM   1115  O O      . THR A 1 149 ? -7.779  -9.406  26.312 1.00 36.51  ? 149 THR A O      1 
ATOM   1116  C CB     . THR A 1 149 ? -9.398  -8.753  28.674 1.00 35.66  ? 149 THR A CB     1 
ATOM   1117  O OG1    . THR A 1 149 ? -10.455 -7.997  29.270 1.00 35.32  ? 149 THR A OG1    1 
ATOM   1118  C CG2    . THR A 1 149 ? -8.616  -9.435  29.767 1.00 34.31  ? 149 THR A CG2    1 
ATOM   1119  N N      . GLY A 1 150 ? -6.233  -8.633  27.675 1.00 23.99  ? 150 GLY A N      1 
ATOM   1120  C CA     . GLY A 1 150 ? -5.166  -9.365  27.057 1.00 25.79  ? 150 GLY A CA     1 
ATOM   1121  C C      . GLY A 1 150 ? -3.787  -8.886  27.336 1.00 25.52  ? 150 GLY A C      1 
ATOM   1122  O O      . GLY A 1 150 ? -3.598  -8.083  28.203 1.00 32.13  ? 150 GLY A O      1 
ATOM   1123  N N      . ILE A 1 151 ? -2.815  -9.374  26.598 1.00 24.49  ? 151 ILE A N      1 
ATOM   1124  C CA     . ILE A 1 151 ? -1.467  -8.905  26.762 1.00 27.41  ? 151 ILE A CA     1 
ATOM   1125  C C      . ILE A 1 151 ? -0.862  -8.591  25.417 1.00 36.14  ? 151 ILE A C      1 
ATOM   1126  O O      . ILE A 1 151 ? -0.968  -9.376  24.498 1.00 33.55  ? 151 ILE A O      1 
ATOM   1127  C CB     . ILE A 1 151 ? -0.614  -9.915  27.524 1.00 30.91  ? 151 ILE A CB     1 
ATOM   1128  C CG1    . ILE A 1 151 ? 0.867   -9.601  27.371 1.00 36.01  ? 151 ILE A CG1    1 
ATOM   1129  C CG2    . ILE A 1 151 ? -0.887  -11.326 27.053 1.00 37.32  ? 151 ILE A CG2    1 
ATOM   1130  C CD1    . ILE A 1 151 ? 1.750   -10.517 28.171 1.00 40.78  ? 151 ILE A CD1    1 
ATOM   1131  N N      . VAL A 1 152 ? -0.249  -7.427  25.270 1.00 36.30  ? 152 VAL A N      1 
ATOM   1132  C CA     . VAL A 1 152 ? 0.280   -7.018  23.983 1.00 34.34  ? 152 VAL A CA     1 
ATOM   1133  C C      . VAL A 1 152 ? 1.780   -6.992  23.982 1.00 38.16  ? 152 VAL A C      1 
ATOM   1134  O O      . VAL A 1 152 ? 2.364   -6.253  24.746 1.00 42.00  ? 152 VAL A O      1 
ATOM   1135  C CB     . VAL A 1 152 ? -0.189  -5.603  23.645 1.00 31.22  ? 152 VAL A CB     1 
ATOM   1136  C CG1    . VAL A 1 152 ? 0.538   -5.067  22.428 1.00 38.55  ? 152 VAL A CG1    1 
ATOM   1137  C CG2    . VAL A 1 152 ? -1.692  -5.572  23.444 1.00 29.09  ? 152 VAL A CG2    1 
ATOM   1138  N N      . MET A 1 153 ? 2.423   -7.799  23.150 1.00 37.89  ? 153 MET A N      1 
ATOM   1139  C CA     . MET A 1 153 ? 3.866   -7.718  23.040 1.00 38.82  ? 153 MET A CA     1 
ATOM   1140  C C      . MET A 1 153 ? 4.133   -6.616  22.073 1.00 50.46  ? 153 MET A C      1 
ATOM   1141  O O      . MET A 1 153 ? 3.927   -6.787  20.885 1.00 59.77  ? 153 MET A O      1 
ATOM   1142  C CB     . MET A 1 153 ? 4.491   -8.986  22.523 1.00 27.21  ? 153 MET A CB     1 
ATOM   1143  C CG     . MET A 1 153 ? 5.994   -8.902  22.514 1.00 27.94  ? 153 MET A CG     1 
ATOM   1144  S SD     . MET A 1 153 ? 6.578   -9.902  21.160 1.00 98.10  ? 153 MET A SD     1 
ATOM   1145  C CE     . MET A 1 153 ? 5.599   -11.363 21.457 1.00 59.02  ? 153 MET A CE     1 
ATOM   1146  N N      . ASP A 1 154 ? 4.559   -5.468  22.566 1.00 40.79  ? 154 ASP A N      1 
ATOM   1147  C CA     . ASP A 1 154 ? 4.787   -4.328  21.719 1.00 39.98  ? 154 ASP A CA     1 
ATOM   1148  C C      . ASP A 1 154 ? 6.235   -4.351  21.418 1.00 40.05  ? 154 ASP A C      1 
ATOM   1149  O O      . ASP A 1 154 ? 7.030   -4.351  22.319 1.00 42.93  ? 154 ASP A O      1 
ATOM   1150  C CB     . ASP A 1 154 ? 4.468   -3.084  22.518 1.00 46.89  ? 154 ASP A CB     1 
ATOM   1151  C CG     . ASP A 1 154 ? 4.102   -1.899  21.657 1.00 64.93  ? 154 ASP A CG     1 
ATOM   1152  O OD1    . ASP A 1 154 ? 4.340   -1.937  20.437 1.00 56.26  ? 154 ASP A OD1    1 
ATOM   1153  O OD2    . ASP A 1 154 ? 3.577   -0.914  22.216 1.00 55.05  ? 154 ASP A OD2    1 
ATOM   1154  N N      . SER A 1 155 ? 6.607   -4.382  20.156 1.00 34.03  ? 155 SER A N      1 
ATOM   1155  C CA     . SER A 1 155 ? 8.003   -4.301  19.824 1.00 36.91  ? 155 SER A CA     1 
ATOM   1156  C C      . SER A 1 155 ? 8.220   -3.073  19.022 1.00 39.12  ? 155 SER A C      1 
ATOM   1157  O O      . SER A 1 155 ? 7.279   -2.499  18.512 1.00 45.07  ? 155 SER A O      1 
ATOM   1158  C CB     . SER A 1 155 ? 8.448   -5.481  19.028 1.00 36.02  ? 155 SER A CB     1 
ATOM   1159  O OG     . SER A 1 155 ? 7.947   -5.348  17.723 1.00 35.94  ? 155 SER A OG     1 
ATOM   1160  N N      . GLY A 1 156 ? 9.461   -2.655  18.905 1.00 36.87  ? 156 GLY A N      1 
ATOM   1161  C CA     . GLY A 1 156 ? 9.744   -1.411  18.238 1.00 41.93  ? 156 GLY A CA     1 
ATOM   1162  C C      . GLY A 1 156 ? 11.202  -1.161  17.987 1.00 48.44  ? 156 GLY A C      1 
ATOM   1163  O O      . GLY A 1 156 ? 11.994  -2.048  18.155 1.00 46.60  ? 156 GLY A O      1 
ATOM   1164  N N      . ASP A 1 157 ? 11.550  0.024   17.514 1.00 48.17  ? 157 ASP A N      1 
ATOM   1165  C CA     . ASP A 1 157 ? 12.925  0.316   17.199 1.00 50.93  ? 157 ASP A CA     1 
ATOM   1166  C C      . ASP A 1 157 ? 13.713  0.330   18.445 1.00 56.45  ? 157 ASP A C      1 
ATOM   1167  O O      . ASP A 1 157 ? 14.841  -0.121  18.457 1.00 58.84  ? 157 ASP A O      1 
ATOM   1168  C CB     . ASP A 1 157 ? 13.083  1.660   16.535 1.00 53.26  ? 157 ASP A CB     1 
ATOM   1169  C CG     . ASP A 1 157 ? 14.460  1.854   15.955 1.00 62.20  ? 157 ASP A CG     1 
ATOM   1170  O OD1    . ASP A 1 157 ? 15.029  0.872   15.439 1.00 57.20  ? 157 ASP A OD1    1 
ATOM   1171  O OD2    . ASP A 1 157 ? 14.975  2.986   16.008 1.00 65.76  ? 157 ASP A OD2    1 
ATOM   1172  N N      . GLY A 1 158 ? 13.151  0.897   19.500 1.00 53.11  ? 158 GLY A N      1 
ATOM   1173  C CA     . GLY A 1 158 ? 13.874  1.012   20.747 1.00 47.36  ? 158 GLY A CA     1 
ATOM   1174  C C      . GLY A 1 158 ? 13.477  0.181   21.926 1.00 44.42  ? 158 GLY A C      1 
ATOM   1175  O O      . GLY A 1 158 ? 14.329  -0.380  22.587 1.00 50.65  ? 158 GLY A O      1 
ATOM   1176  N N      . VAL A 1 159 ? 12.194  0.115   22.219 1.00 41.00  ? 159 VAL A N      1 
ATOM   1177  C CA     . VAL A 1 159 ? 11.762  -0.581  23.404 1.00 46.32  ? 159 VAL A CA     1 
ATOM   1178  C C      . VAL A 1 159 ? 10.646  -1.554  23.165 1.00 44.26  ? 159 VAL A C      1 
ATOM   1179  O O      . VAL A 1 159 ? 9.733   -1.278  22.406 1.00 43.49  ? 159 VAL A O      1 
ATOM   1180  C CB     . VAL A 1 159 ? 11.334  0.399   24.498 1.00 43.64  ? 159 VAL A CB     1 
ATOM   1181  C CG1    . VAL A 1 159 ? 10.161  1.244   24.043 1.00 43.84  ? 159 VAL A CG1    1 
ATOM   1182  C CG2    . VAL A 1 159 ? 11.013  -0.331  25.787 1.00 41.98  ? 159 VAL A CG2    1 
ATOM   1183  N N      . THR A 1 160 ? 10.710  -2.699  23.826 1.00 42.01  ? 160 THR A N      1 
ATOM   1184  C CA     . THR A 1 160 ? 9.679   -3.702  23.699 1.00 38.20  ? 160 THR A CA     1 
ATOM   1185  C C      . THR A 1 160 ? 9.067   -3.898  25.060 1.00 36.25  ? 160 THR A C      1 
ATOM   1186  O O      . THR A 1 160 ? 9.769   -4.182  25.997 1.00 39.23  ? 160 THR A O      1 
ATOM   1187  C CB     . THR A 1 160 ? 10.268  -5.014  23.192 1.00 35.29  ? 160 THR A CB     1 
ATOM   1188  O OG1    . THR A 1 160 ? 10.677  -4.858  21.832 1.00 36.43  ? 160 THR A OG1    1 
ATOM   1189  C CG2    . THR A 1 160 ? 9.261   -6.138  23.285 1.00 32.85  ? 160 THR A CG2    1 
ATOM   1190  N N      . HIS A 1 161 ? 7.764   -3.737  25.184 1.00 33.22  ? 161 HIS A N      1 
ATOM   1191  C CA     . HIS A 1 161 ? 7.103   -3.836  26.453 1.00 33.51  ? 161 HIS A CA     1 
ATOM   1192  C C      . HIS A 1 161 ? 6.102   -4.931  26.341 1.00 38.20  ? 161 HIS A C      1 
ATOM   1193  O O      . HIS A 1 161 ? 5.449   -5.026  25.325 1.00 44.03  ? 161 HIS A O      1 
ATOM   1194  C CB     . HIS A 1 161 ? 6.278   -2.592  26.683 1.00 31.37  ? 161 HIS A CB     1 
ATOM   1195  C CG     . HIS A 1 161 ? 7.058   -1.334  26.843 1.00 33.88  ? 161 HIS A CG     1 
ATOM   1196  N ND1    . HIS A 1 161 ? 7.671   -0.986  28.024 1.00 39.82  ? 161 HIS A ND1    1 
ATOM   1197  C CD2    . HIS A 1 161 ? 7.261   -0.301  25.995 1.00 39.94  ? 161 HIS A CD2    1 
ATOM   1198  C CE1    . HIS A 1 161 ? 8.249   0.192   27.886 1.00 45.48  ? 161 HIS A CE1    1 
ATOM   1199  N NE2    . HIS A 1 161 ? 8.014   0.629   26.664 1.00 45.64  ? 161 HIS A NE2    1 
ATOM   1200  N N      . THR A 1 162 ? 5.944   -5.765  27.359 1.00 37.25  ? 162 THR A N      1 
ATOM   1201  C CA     . THR A 1 162 ? 4.888   -6.765  27.341 1.00 39.33  ? 162 THR A CA     1 
ATOM   1202  C C      . THR A 1 162 ? 3.846   -6.295  28.315 1.00 37.36  ? 162 THR A C      1 
ATOM   1203  O O      . THR A 1 162 ? 3.955   -6.539  29.497 1.00 40.39  ? 162 THR A O      1 
ATOM   1204  C CB     . THR A 1 162 ? 5.397   -8.147  27.696 1.00 39.96  ? 162 THR A CB     1 
ATOM   1205  O OG1    . THR A 1 162 ? 6.054   -8.092  28.960 1.00 50.65  ? 162 THR A OG1    1 
ATOM   1206  C CG2    . THR A 1 162 ? 6.371   -8.627  26.647 1.00 31.61  ? 162 THR A CG2    1 
ATOM   1207  N N      . VAL A 1 163 ? 2.835   -5.608  27.818 1.00 30.29  ? 163 VAL A N      1 
ATOM   1208  C CA     . VAL A 1 163 ? 1.834   -5.012  28.665 1.00 31.42  ? 163 VAL A CA     1 
ATOM   1209  C C      . VAL A 1 163 ? 0.582   -5.819  28.886 1.00 31.10  ? 163 VAL A C      1 
ATOM   1210  O O      . VAL A 1 163 ? -0.113  -6.119  27.939 1.00 30.78  ? 163 VAL A O      1 
ATOM   1211  C CB     . VAL A 1 163 ? 1.409   -3.730  27.973 1.00 26.76  ? 163 VAL A CB     1 
ATOM   1212  C CG1    . VAL A 1 163 ? 0.508   -2.891  28.856 1.00 30.98  ? 163 VAL A CG1    1 
ATOM   1213  C CG2    . VAL A 1 163 ? 2.627   -2.957  27.525 1.00 22.45  ? 163 VAL A CG2    1 
ATOM   1214  N N      . PRO A 1 164 ? 0.270   -6.190  30.159 1.00 27.79  ? 164 PRO A N      1 
ATOM   1215  C CA     . PRO A 1 164 ? -1.008  -6.862  30.392 1.00 29.70  ? 164 PRO A CA     1 
ATOM   1216  C C      . PRO A 1 164 ? -2.176  -5.968  30.631 1.00 27.16  ? 164 PRO A C      1 
ATOM   1217  O O      . PRO A 1 164 ? -2.113  -5.189  31.548 1.00 31.18  ? 164 PRO A O      1 
ATOM   1218  C CB     . PRO A 1 164 ? -0.762  -7.592  31.678 1.00 30.30  ? 164 PRO A CB     1 
ATOM   1219  C CG     . PRO A 1 164 ? 0.692   -7.829  31.695 1.00 32.86  ? 164 PRO A CG     1 
ATOM   1220  C CD     . PRO A 1 164 ? 1.165   -6.484  31.294 1.00 31.12  ? 164 PRO A CD     1 
ATOM   1221  N N      . ILE A 1 165 ? -3.258  -6.120  29.886 1.00 24.81  ? 165 ILE A N      1 
ATOM   1222  C CA     . ILE A 1 165 ? -4.396  -5.227  29.976 1.00 27.70  ? 165 ILE A CA     1 
ATOM   1223  C C      . ILE A 1 165 ? -5.630  -5.965  30.421 1.00 32.83  ? 165 ILE A C      1 
ATOM   1224  O O      . ILE A 1 165 ? -5.889  -7.041  29.936 1.00 38.49  ? 165 ILE A O      1 
ATOM   1225  C CB     . ILE A 1 165 ? -4.648  -4.582  28.594 1.00 26.31  ? 165 ILE A CB     1 
ATOM   1226  C CG1    . ILE A 1 165 ? -3.470  -3.711  28.182 1.00 30.55  ? 165 ILE A CG1    1 
ATOM   1227  C CG2    . ILE A 1 165 ? -5.906  -3.744  28.588 1.00 26.72  ? 165 ILE A CG2    1 
ATOM   1228  C CD1    . ILE A 1 165 ? -2.755  -4.210  26.956 1.00 32.31  ? 165 ILE A CD1    1 
ATOM   1229  N N      . TYR A 1 166 ? -6.390  -5.421  31.356 1.00 30.22  ? 166 TYR A N      1 
ATOM   1230  C CA     . TYR A 1 166 ? -7.615  -6.048  31.791 1.00 34.41  ? 166 TYR A CA     1 
ATOM   1231  C C      . TYR A 1 166 ? -8.693  -5.026  31.826 1.00 37.73  ? 166 TYR A C      1 
ATOM   1232  O O      . TYR A 1 166 ? -8.588  -4.073  32.575 1.00 41.36  ? 166 TYR A O      1 
ATOM   1233  C CB     . TYR A 1 166 ? -7.458  -6.631  33.172 1.00 37.22  ? 166 TYR A CB     1 
ATOM   1234  C CG     . TYR A 1 166 ? -8.736  -7.142  33.800 1.00 42.30  ? 166 TYR A CG     1 
ATOM   1235  C CD1    . TYR A 1 166 ? -9.274  -8.361  33.429 1.00 41.27  ? 166 TYR A CD1    1 
ATOM   1236  C CD2    . TYR A 1 166 ? -9.391  -6.413  34.780 1.00 41.75  ? 166 TYR A CD2    1 
ATOM   1237  C CE1    . TYR A 1 166 ? -10.438 -8.831  34.000 1.00 42.65  ? 166 TYR A CE1    1 
ATOM   1238  C CE2    . TYR A 1 166 ? -10.555 -6.876  35.355 1.00 43.60  ? 166 TYR A CE2    1 
ATOM   1239  C CZ     . TYR A 1 166 ? -11.072 -8.085  34.960 1.00 44.68  ? 166 TYR A CZ     1 
ATOM   1240  O OH     . TYR A 1 166 ? -12.229 -8.548  35.531 1.00 38.84  ? 166 TYR A OH     1 
ATOM   1241  N N      . GLU A 1 167 ? -9.748  -5.203  31.044 1.00 38.95  ? 167 GLU A N      1 
ATOM   1242  C CA     . GLU A 1 167 ? -10.850 -4.249  30.948 1.00 39.01  ? 167 GLU A CA     1 
ATOM   1243  C C      . GLU A 1 167 ? -10.424 -2.865  30.590 1.00 34.40  ? 167 GLU A C      1 
ATOM   1244  O O      . GLU A 1 167 ? -11.034 -1.907  31.003 1.00 36.50  ? 167 GLU A O      1 
ATOM   1245  C CB     . GLU A 1 167 ? -11.753 -4.289  32.164 1.00 39.80  ? 167 GLU A CB     1 
ATOM   1246  C CG     . GLU A 1 167 ? -12.590 -5.550  32.239 1.00 50.11  ? 167 GLU A CG     1 
ATOM   1247  C CD     . GLU A 1 167 ? -13.745 -5.426  33.204 1.00 60.73  ? 167 GLU A CD     1 
ATOM   1248  O OE1    . GLU A 1 167 ? -14.047 -4.297  33.627 1.00 57.78  ? 167 GLU A OE1    1 
ATOM   1249  O OE2    . GLU A 1 167 ? -14.358 -6.458  33.535 1.00 66.69  ? 167 GLU A OE2    1 
ATOM   1250  N N      . GLY A 1 168 ? -9.392  -2.764  29.791 1.00 31.81  ? 168 GLY A N      1 
ATOM   1251  C CA     . GLY A 1 168 ? -8.896  -1.481  29.373 1.00 30.99  ? 168 GLY A CA     1 
ATOM   1252  C C      . GLY A 1 168 ? -7.836  -0.820  30.218 1.00 40.77  ? 168 GLY A C      1 
ATOM   1253  O O      . GLY A 1 168 ? -7.292  0.189   29.813 1.00 43.24  ? 168 GLY A O      1 
ATOM   1254  N N      . TYR A 1 169 ? -7.504  -1.390  31.365 1.00 40.43  ? 169 TYR A N      1 
ATOM   1255  C CA     . TYR A 1 169 ? -6.491  -0.830  32.219 1.00 34.68  ? 169 TYR A CA     1 
ATOM   1256  C C      . TYR A 1 169 ? -5.238  -1.599  32.109 1.00 35.59  ? 169 TYR A C      1 
ATOM   1257  O O      . TYR A 1 169 ? -5.223  -2.774  32.369 1.00 40.13  ? 169 TYR A O      1 
ATOM   1258  C CB     . TYR A 1 169 ? -6.944  -0.873  33.639 1.00 34.62  ? 169 TYR A CB     1 
ATOM   1259  C CG     . TYR A 1 169 ? -6.007  -0.240  34.630 1.00 42.46  ? 169 TYR A CG     1 
ATOM   1260  C CD1    . TYR A 1 169 ? -5.597  1.070   34.489 1.00 43.60  ? 169 TYR A CD1    1 
ATOM   1261  C CD2    . TYR A 1 169 ? -5.564  -0.946  35.730 1.00 50.48  ? 169 TYR A CD2    1 
ATOM   1262  C CE1    . TYR A 1 169 ? -4.745  1.649   35.404 1.00 51.83  ? 169 TYR A CE1    1 
ATOM   1263  C CE2    . TYR A 1 169 ? -4.719  -0.374  36.650 1.00 47.54  ? 169 TYR A CE2    1 
ATOM   1264  C CZ     . TYR A 1 169 ? -4.314  0.921   36.481 1.00 48.39  ? 169 TYR A CZ     1 
ATOM   1265  O OH     . TYR A 1 169 ? -3.469  1.481   37.398 1.00 45.05  ? 169 TYR A OH     1 
ATOM   1266  N N      . ALA A 1 170 ? -4.175  -0.935  31.717 1.00 33.00  ? 170 ALA A N      1 
ATOM   1267  C CA     . ALA A 1 170 ? -2.907  -1.574  31.600 1.00 37.06  ? 170 ALA A CA     1 
ATOM   1268  C C      . ALA A 1 170 ? -2.408  -1.698  32.967 1.00 38.69  ? 170 ALA A C      1 
ATOM   1269  O O      . ALA A 1 170 ? -2.110  -0.698  33.587 1.00 41.56  ? 170 ALA A O      1 
ATOM   1270  C CB     . ALA A 1 170 ? -1.987  -0.694  30.840 1.00 35.02  ? 170 ALA A CB     1 
ATOM   1271  N N      . LEU A 1 171 ? -2.245  -2.912  33.442 1.00 36.25  ? 171 LEU A N      1 
ATOM   1272  C CA     . LEU A 1 171 ? -1.884  -3.095  34.809 1.00 39.34  ? 171 LEU A CA     1 
ATOM   1273  C C      . LEU A 1 171 ? -0.456  -2.724  35.023 1.00 42.82  ? 171 LEU A C      1 
ATOM   1274  O O      . LEU A 1 171 ? 0.416   -3.345  34.461 1.00 45.45  ? 171 LEU A O      1 
ATOM   1275  C CB     . LEU A 1 171 ? -2.105  -4.547  35.138 1.00 36.88  ? 171 LEU A CB     1 
ATOM   1276  C CG     . LEU A 1 171 ? -3.477  -5.083  34.749 1.00 39.32  ? 171 LEU A CG     1 
ATOM   1277  C CD1    . LEU A 1 171 ? -3.497  -6.594  34.829 1.00 41.52  ? 171 LEU A CD1    1 
ATOM   1278  C CD2    . LEU A 1 171 ? -4.570  -4.483  35.612 1.00 41.66  ? 171 LEU A CD2    1 
ATOM   1279  N N      . PRO A 1 172 ? -0.197  -1.749  35.895 1.00 39.50  ? 172 PRO A N      1 
ATOM   1280  C CA     . PRO A 1 172 ? 1.152   -1.278  36.193 1.00 33.95  ? 172 PRO A CA     1 
ATOM   1281  C C      . PRO A 1 172 ? 2.026   -2.301  36.849 1.00 37.25  ? 172 PRO A C      1 
ATOM   1282  O O      . PRO A 1 172 ? 3.227   -2.258  36.683 1.00 36.81  ? 172 PRO A O      1 
ATOM   1283  C CB     . PRO A 1 172 ? 0.907   -0.129  37.134 1.00 31.72  ? 172 PRO A CB     1 
ATOM   1284  C CG     . PRO A 1 172 ? -0.409  -0.397  37.764 1.00 34.34  ? 172 PRO A CG     1 
ATOM   1285  C CD     . PRO A 1 172 ? -1.213  -1.058  36.698 1.00 34.81  ? 172 PRO A CD     1 
ATOM   1286  N N      . HIS A 1 173 ? 1.426   -3.219  37.587 1.00 40.49  ? 173 HIS A N      1 
ATOM   1287  C CA     . HIS A 1 173 ? 2.174   -4.235  38.287 1.00 35.77  ? 173 HIS A CA     1 
ATOM   1288  C C      . HIS A 1 173 ? 2.818   -5.203  37.386 1.00 34.92  ? 173 HIS A C      1 
ATOM   1289  O O      . HIS A 1 173 ? 3.904   -5.668  37.663 1.00 36.51  ? 173 HIS A O      1 
ATOM   1290  C CB     . HIS A 1 173 ? 1.324   -5.016  39.273 1.00 34.50  ? 173 HIS A CB     1 
ATOM   1291  C CG     . HIS A 1 173 ? -0.127  -5.115  38.937 1.00 40.64  ? 173 HIS A CG     1 
ATOM   1292  N ND1    . HIS A 1 173 ? -1.014  -4.085  39.158 1.00 47.50  ? 173 HIS A ND1    1 
ATOM   1293  C CD2    . HIS A 1 173 ? -0.867  -6.160  38.501 1.00 42.56  ? 173 HIS A CD2    1 
ATOM   1294  C CE1    . HIS A 1 173 ? -2.228  -4.472  38.817 1.00 49.04  ? 173 HIS A CE1    1 
ATOM   1295  N NE2    . HIS A 1 173 ? -2.166  -5.728  38.417 1.00 50.05  ? 173 HIS A NE2    1 
ATOM   1296  N N      . ALA A 1 174 ? 2.158   -5.520  36.298 1.00 37.72  ? 174 ALA A N      1 
ATOM   1297  C CA     . ALA A 1 174 ? 2.691   -6.509  35.388 1.00 41.43  ? 174 ALA A CA     1 
ATOM   1298  C C      . ALA A 1 174 ? 3.438   -6.069  34.153 1.00 38.16  ? 174 ALA A C      1 
ATOM   1299  O O      . ALA A 1 174 ? 4.093   -6.869  33.513 1.00 37.17  ? 174 ALA A O      1 
ATOM   1300  C CB     . ALA A 1 174 ? 1.578   -7.419  34.986 1.00 39.17  ? 174 ALA A CB     1 
ATOM   1301  N N      . ILE A 1 175 ? 3.363   -4.808  33.809 1.00 33.97  ? 175 ILE A N      1 
ATOM   1302  C CA     . ILE A 1 175 ? 3.999   -4.387  32.603 1.00 35.38  ? 175 ILE A CA     1 
ATOM   1303  C C      . ILE A 1 175 ? 5.457   -4.665  32.795 1.00 41.74  ? 175 ILE A C      1 
ATOM   1304  O O      . ILE A 1 175 ? 5.994   -4.440  33.867 1.00 48.41  ? 175 ILE A O      1 
ATOM   1305  C CB     . ILE A 1 175 ? 3.760   -2.901  32.311 1.00 31.61  ? 175 ILE A CB     1 
ATOM   1306  C CG1    . ILE A 1 175 ? 2.279   -2.630  32.119 1.00 34.76  ? 175 ILE A CG1    1 
ATOM   1307  C CG2    . ILE A 1 175 ? 4.503   -2.468  31.063 1.00 29.62  ? 175 ILE A CG2    1 
ATOM   1308  C CD1    . ILE A 1 175 ? 1.949   -1.169  31.944 1.00 34.92  ? 175 ILE A CD1    1 
ATOM   1309  N N      . LEU A 1 176 ? 6.106   -5.185  31.770 1.00 35.29  ? 176 LEU A N      1 
ATOM   1310  C CA     . LEU A 1 176 ? 7.516   -5.415  31.840 1.00 34.52  ? 176 LEU A CA     1 
ATOM   1311  C C      . LEU A 1 176 ? 8.092   -4.709  30.673 1.00 36.17  ? 176 LEU A C      1 
ATOM   1312  O O      . LEU A 1 176 ? 7.378   -4.364  29.763 1.00 35.04  ? 176 LEU A O      1 
ATOM   1313  C CB     . LEU A 1 176 ? 7.830   -6.894  31.793 1.00 38.66  ? 176 LEU A CB     1 
ATOM   1314  C CG     . LEU A 1 176 ? 7.787   -7.655  33.116 1.00 37.94  ? 176 LEU A CG     1 
ATOM   1315  C CD1    . LEU A 1 176 ? 7.779   -9.149  32.882 1.00 33.07  ? 176 LEU A CD1    1 
ATOM   1316  C CD2    . LEU A 1 176 ? 8.977   -7.266  33.972 1.00 33.03  ? 176 LEU A CD2    1 
ATOM   1317  N N      . ARG A 1 177 ? 9.385   -4.479  30.700 1.00 42.61  ? 177 ARG A N      1 
ATOM   1318  C CA     . ARG A 1 177 ? 10.056  -3.745  29.649 1.00 43.14  ? 177 ARG A CA     1 
ATOM   1319  C C      . ARG A 1 177 ? 11.316  -4.459  29.247 1.00 49.02  ? 177 ARG A C      1 
ATOM   1320  O O      . ARG A 1 177 ? 12.025  -4.976  30.101 1.00 52.32  ? 177 ARG A O      1 
ATOM   1321  C CB     . ARG A 1 177 ? 10.402  -2.370  30.193 1.00 45.54  ? 177 ARG A CB     1 
ATOM   1322  C CG     . ARG A 1 177 ? 11.317  -1.516  29.347 1.00 51.86  ? 177 ARG A CG     1 
ATOM   1323  C CD     . ARG A 1 177 ? 11.439  -0.141  29.976 1.00 56.62  ? 177 ARG A CD     1 
ATOM   1324  N NE     . ARG A 1 177 ? 12.569  0.610   29.453 1.00 71.26  ? 177 ARG A NE     1 
ATOM   1325  C CZ     . ARG A 1 177 ? 13.783  0.588   29.990 1.00 77.23  ? 177 ARG A CZ     1 
ATOM   1326  N NH1    . ARG A 1 177 ? 14.022  -0.159  31.059 1.00 71.16  ? 177 ARG A NH1    1 
ATOM   1327  N NH2    . ARG A 1 177 ? 14.761  1.303   29.452 1.00 82.03  ? 177 ARG A NH2    1 
ATOM   1328  N N      . LEU A 1 178 ? 11.589  -4.514  27.950 1.00 46.54  ? 178 LEU A N      1 
ATOM   1329  C CA     . LEU A 1 178 ? 12.810  -5.130  27.451 1.00 49.82  ? 178 LEU A CA     1 
ATOM   1330  C C      . LEU A 1 178 ? 13.434  -4.095  26.572 1.00 49.14  ? 178 LEU A C      1 
ATOM   1331  O O      . LEU A 1 178 ? 12.737  -3.324  25.941 1.00 47.65  ? 178 LEU A O      1 
ATOM   1332  C CB     . LEU A 1 178 ? 12.506  -6.401  26.668 1.00 43.44  ? 178 LEU A CB     1 
ATOM   1333  C CG     . LEU A 1 178 ? 13.628  -7.228  26.063 1.00 47.67  ? 178 LEU A CG     1 
ATOM   1334  C CD1    . LEU A 1 178 ? 14.665  -7.571  27.110 1.00 49.49  ? 178 LEU A CD1    1 
ATOM   1335  C CD2    . LEU A 1 178 ? 13.033  -8.488  25.472 1.00 53.09  ? 178 LEU A CD2    1 
ATOM   1336  N N      . ASP A 1 179 ? 14.745  -4.067  26.536 1.00 48.65  ? 179 ASP A N      1 
ATOM   1337  C CA     . ASP A 1 179 ? 15.429  -3.084  25.743 1.00 54.47  ? 179 ASP A CA     1 
ATOM   1338  C C      . ASP A 1 179 ? 16.039  -3.758  24.562 1.00 56.51  ? 179 ASP A C      1 
ATOM   1339  O O      . ASP A 1 179 ? 17.189  -3.513  24.232 1.00 54.43  ? 179 ASP A O      1 
ATOM   1340  C CB     . ASP A 1 179 ? 16.474  -2.395  26.580 1.00 61.18  ? 179 ASP A CB     1 
ATOM   1341  C CG     . ASP A 1 179 ? 15.864  -1.574  27.696 1.00 71.62  ? 179 ASP A CG     1 
ATOM   1342  O OD1    . ASP A 1 179 ? 14.680  -1.202  27.575 1.00 65.26  ? 179 ASP A OD1    1 
ATOM   1343  O OD2    . ASP A 1 179 ? 16.565  -1.295  28.690 1.00 74.06  ? 179 ASP A OD2    1 
ATOM   1344  N N      . LEU A 1 180 ? 15.268  -4.626  23.933 1.00 58.98  ? 180 LEU A N      1 
ATOM   1345  C CA     . LEU A 1 180 ? 15.724  -5.325  22.758 1.00 53.89  ? 180 LEU A CA     1 
ATOM   1346  C C      . LEU A 1 180 ? 14.730  -4.906  21.759 1.00 46.80  ? 180 LEU A C      1 
ATOM   1347  O O      . LEU A 1 180 ? 13.539  -4.872  22.024 1.00 45.38  ? 180 LEU A O      1 
ATOM   1348  C CB     . LEU A 1 180 ? 15.656  -6.829  22.936 1.00 50.23  ? 180 LEU A CB     1 
ATOM   1349  C CG     . LEU A 1 180 ? 16.278  -7.684  21.848 1.00 52.50  ? 180 LEU A CG     1 
ATOM   1350  C CD1    . LEU A 1 180 ? 17.724  -7.278  21.649 1.00 64.19  ? 180 LEU A CD1    1 
ATOM   1351  C CD2    . LEU A 1 180 ? 16.188  -9.128  22.287 1.00 49.25  ? 180 LEU A CD2    1 
ATOM   1352  N N      . ALA A 1 181 ? 15.207  -4.576  20.594 1.00 43.24  ? 181 ALA A N      1 
ATOM   1353  C CA     . ALA A 1 181 ? 14.307  -4.051  19.647 1.00 45.95  ? 181 ALA A CA     1 
ATOM   1354  C C      . ALA A 1 181 ? 14.935  -4.082  18.317 1.00 48.81  ? 181 ALA A C      1 
ATOM   1355  O O      . ALA A 1 181 ? 16.010  -4.615  18.154 1.00 52.11  ? 181 ALA A O      1 
ATOM   1356  C CB     . ALA A 1 181 ? 14.003  -2.652  20.037 1.00 48.82  ? 181 ALA A CB     1 
ATOM   1357  N N      . GLY A 1 182 ? 14.275  -3.500  17.351 1.00 37.29  ? 182 GLY A N      1 
ATOM   1358  C CA     . GLY A 1 182 ? 14.764  -3.566  16.014 1.00 39.88  ? 182 GLY A CA     1 
ATOM   1359  C C      . GLY A 1 182 ? 16.110  -2.967  15.804 1.00 46.99  ? 182 GLY A C      1 
ATOM   1360  O O      . GLY A 1 182 ? 16.854  -3.488  15.010 1.00 54.55  ? 182 GLY A O      1 
ATOM   1361  N N      . ARG A 1 183 ? 16.431  -1.866  16.447 1.00 45.94  ? 183 ARG A N      1 
ATOM   1362  C CA     . ARG A 1 183 ? 17.691  -1.215  16.168 1.00 46.82  ? 183 ARG A CA     1 
ATOM   1363  C C      . ARG A 1 183 ? 18.784  -2.159  16.526 1.00 46.98  ? 183 ARG A C      1 
ATOM   1364  O O      . ARG A 1 183 ? 19.811  -2.186  15.882 1.00 46.28  ? 183 ARG A O      1 
ATOM   1365  C CB     . ARG A 1 183 ? 17.816  0.061   16.966 1.00 53.79  ? 183 ARG A CB     1 
ATOM   1366  C CG     . ARG A 1 183 ? 17.983  -0.137  18.458 1.00 65.40  ? 183 ARG A CG     1 
ATOM   1367  C CD     . ARG A 1 183 ? 18.232  1.183   19.160 1.00 57.92  ? 183 ARG A CD     1 
ATOM   1368  N NE     . ARG A 1 183 ? 17.064  2.048   19.106 1.00 56.57  ? 183 ARG A NE     1 
ATOM   1369  C CZ     . ARG A 1 183 ? 17.022  3.257   19.643 1.00 57.65  ? 183 ARG A CZ     1 
ATOM   1370  N NH1    . ARG A 1 183 ? 18.086  3.735   20.263 1.00 61.78  ? 183 ARG A NH1    1 
ATOM   1371  N NH2    . ARG A 1 183 ? 15.921  3.984   19.559 1.00 61.35  ? 183 ARG A NH2    1 
ATOM   1372  N N      . ASP A 1 184 ? 18.599  -2.897  17.595 1.00 49.87  ? 184 ASP A N      1 
ATOM   1373  C CA     . ASP A 1 184 ? 19.557  -3.894  17.997 1.00 51.04  ? 184 ASP A CA     1 
ATOM   1374  C C      . ASP A 1 184 ? 19.625  -5.004  16.979 1.00 44.83  ? 184 ASP A C      1 
ATOM   1375  O O      . ASP A 1 184 ? 20.678  -5.537  16.714 1.00 46.65  ? 184 ASP A O      1 
ATOM   1376  C CB     . ASP A 1 184 ? 19.175  -4.432  19.357 1.00 52.22  ? 184 ASP A CB     1 
ATOM   1377  C CG     . ASP A 1 184 ? 18.999  -3.336  20.379 1.00 59.61  ? 184 ASP A CG     1 
ATOM   1378  O OD1    . ASP A 1 184 ? 19.941  -2.545  20.569 1.00 59.42  ? 184 ASP A OD1    1 
ATOM   1379  O OD2    . ASP A 1 184 ? 17.920  -3.262  20.998 1.00 58.97  ? 184 ASP A OD2    1 
ATOM   1380  N N      . LEU A 1 185 ? 18.491  -5.371  16.423 1.00 41.19  ? 185 LEU A N      1 
ATOM   1381  C CA     . LEU A 1 185 ? 18.464  -6.422  15.442 1.00 43.85  ? 185 LEU A CA     1 
ATOM   1382  C C      . LEU A 1 185 ? 19.035  -5.996  14.109 1.00 49.49  ? 185 LEU A C      1 
ATOM   1383  O O      . LEU A 1 185 ? 19.474  -6.844  13.354 1.00 55.04  ? 185 LEU A O      1 
ATOM   1384  C CB     . LEU A 1 185 ? 17.062  -6.984  15.297 1.00 40.82  ? 185 LEU A CB     1 
ATOM   1385  C CG     . LEU A 1 185 ? 16.596  -8.074  16.267 1.00 41.84  ? 185 LEU A CG     1 
ATOM   1386  C CD1    . LEU A 1 185 ? 16.837  -7.701  17.717 1.00 45.91  ? 185 LEU A CD1    1 
ATOM   1387  C CD2    . LEU A 1 185 ? 15.132  -8.394  16.038 1.00 36.16  ? 185 LEU A CD2    1 
ATOM   1388  N N      . THR A 1 186 ? 19.011  -4.709  13.778 1.00 47.29  ? 186 THR A N      1 
ATOM   1389  C CA     . THR A 1 186 ? 19.650  -4.220  12.565 1.00 42.95  ? 186 THR A CA     1 
ATOM   1390  C C      . THR A 1 186 ? 21.108  -4.331  12.808 1.00 46.56  ? 186 THR A C      1 
ATOM   1391  O O      . THR A 1 186 ? 21.852  -4.691  11.920 1.00 52.77  ? 186 THR A O      1 
ATOM   1392  C CB     . THR A 1 186 ? 19.312  -2.761  12.298 1.00 42.53  ? 186 THR A CB     1 
ATOM   1393  O OG1    . THR A 1 186 ? 17.894  -2.617  12.177 1.00 41.10  ? 186 THR A OG1    1 
ATOM   1394  C CG2    . THR A 1 186 ? 19.967  -2.294  11.029 1.00 46.76  ? 186 THR A CG2    1 
ATOM   1395  N N      . ASP A 1 187 ? 21.532  -4.110  14.041 1.00 46.09  ? 187 ASP A N      1 
ATOM   1396  C CA     . ASP A 1 187 ? 22.952  -4.130  14.357 1.00 49.20  ? 187 ASP A CA     1 
ATOM   1397  C C      . ASP A 1 187 ? 23.509  -5.512  14.528 1.00 54.39  ? 187 ASP A C      1 
ATOM   1398  O O      . ASP A 1 187 ? 24.660  -5.744  14.205 1.00 57.61  ? 187 ASP A O      1 
ATOM   1399  C CB     . ASP A 1 187 ? 23.236  -3.288  15.570 1.00 52.26  ? 187 ASP A CB     1 
ATOM   1400  C CG     . ASP A 1 187 ? 22.996  -1.816  15.322 1.00 67.31  ? 187 ASP A CG     1 
ATOM   1401  O OD1    . ASP A 1 187 ? 23.198  -1.362  14.181 1.00 69.87  ? 187 ASP A OD1    1 
ATOM   1402  O OD2    . ASP A 1 187 ? 22.618  -1.107  16.273 1.00 68.59  ? 187 ASP A OD2    1 
ATOM   1403  N N      . TYR A 1 188 ? 22.724  -6.452  15.029 1.00 53.57  ? 188 TYR A N      1 
ATOM   1404  C CA     . TYR A 1 188 ? 23.204  -7.827  15.091 1.00 49.08  ? 188 TYR A CA     1 
ATOM   1405  C C      . TYR A 1 188 ? 23.332  -8.308  13.676 1.00 52.16  ? 188 TYR A C      1 
ATOM   1406  O O      . TYR A 1 188 ? 24.280  -8.986  13.350 1.00 55.84  ? 188 TYR A O      1 
ATOM   1407  C CB     . TYR A 1 188 ? 22.269  -8.733  15.877 1.00 44.26  ? 188 TYR A CB     1 
ATOM   1408  C CG     . TYR A 1 188 ? 22.770  -10.132 16.094 1.00 49.90  ? 188 TYR A CG     1 
ATOM   1409  C CD1    . TYR A 1 188 ? 23.961  -10.368 16.753 1.00 54.77  ? 188 TYR A CD1    1 
ATOM   1410  C CD2    . TYR A 1 188 ? 22.035  -11.222 15.664 1.00 50.07  ? 188 TYR A CD2    1 
ATOM   1411  C CE1    . TYR A 1 188 ? 24.417  -11.653 16.960 1.00 57.89  ? 188 TYR A CE1    1 
ATOM   1412  C CE2    . TYR A 1 188 ? 22.483  -12.510 15.865 1.00 46.34  ? 188 TYR A CE2    1 
ATOM   1413  C CZ     . TYR A 1 188 ? 23.675  -12.718 16.512 1.00 49.74  ? 188 TYR A CZ     1 
ATOM   1414  O OH     . TYR A 1 188 ? 24.124  -13.998 16.707 1.00 47.17  ? 188 TYR A OH     1 
ATOM   1415  N N      . LEU A 1 189 ? 22.400  -7.946  12.811 1.00 47.38  ? 189 LEU A N      1 
ATOM   1416  C CA     . LEU A 1 189 ? 22.425  -8.452  11.458 1.00 46.08  ? 189 LEU A CA     1 
ATOM   1417  C C      . LEU A 1 189 ? 23.646  -7.957  10.773 1.00 49.68  ? 189 LEU A C      1 
ATOM   1418  O O      . LEU A 1 189 ? 24.255  -8.661  10.004 1.00 53.60  ? 189 LEU A O      1 
ATOM   1419  C CB     . LEU A 1 189 ? 21.180  -8.069  10.681 1.00 41.34  ? 189 LEU A CB     1 
ATOM   1420  C CG     . LEU A 1 189 ? 20.960  -8.695  9.304  1.00 45.01  ? 189 LEU A CG     1 
ATOM   1421  C CD1    . LEU A 1 189 ? 21.031  -10.204 9.342  1.00 45.89  ? 189 LEU A CD1    1 
ATOM   1422  C CD2    . LEU A 1 189 ? 19.635  -8.260  8.715  1.00 49.26  ? 189 LEU A CD2    1 
ATOM   1423  N N      . MET A 1 190 ? 24.043  -6.747  11.069 1.00 51.38  ? 190 MET A N      1 
ATOM   1424  C CA     . MET A 1 190 ? 25.169  -6.189  10.376 1.00 52.38  ? 190 MET A CA     1 
ATOM   1425  C C      . MET A 1 190 ? 26.364  -6.981  10.750 1.00 50.35  ? 190 MET A C      1 
ATOM   1426  O O      . MET A 1 190 ? 27.163  -7.335  9.916  1.00 49.54  ? 190 MET A O      1 
ATOM   1427  C CB     . MET A 1 190 ? 25.409  -4.759  10.802 1.00 60.55  ? 190 MET A CB     1 
ATOM   1428  C CG     . MET A 1 190 ? 24.383  -3.757  10.339 1.00 60.52  ? 190 MET A CG     1 
ATOM   1429  S SD     . MET A 1 190 ? 24.970  -2.139  10.826 1.00 58.20  ? 190 MET A SD     1 
ATOM   1430  C CE     . MET A 1 190 ? 25.860  -2.548  12.319 1.00 61.47  ? 190 MET A CE     1 
ATOM   1431  N N      . LYS A 1 191 ? 26.513  -7.228  12.032 1.00 51.50  ? 191 LYS A N      1 
ATOM   1432  C CA     . LYS A 1 191 ? 27.671  -7.945  12.495 1.00 50.97  ? 191 LYS A CA     1 
ATOM   1433  C C      . LYS A 1 191 ? 27.704  -9.319  11.875 1.00 54.03  ? 191 LYS A C      1 
ATOM   1434  O O      . LYS A 1 191 ? 28.716  -9.729  11.336 1.00 53.70  ? 191 LYS A O      1 
ATOM   1435  C CB     . LYS A 1 191 ? 27.657  -8.051  14.003 1.00 50.14  ? 191 LYS A CB     1 
ATOM   1436  C CG     . LYS A 1 191 ? 29.041  -8.246  14.597 1.00 61.11  ? 191 LYS A CG     1 
ATOM   1437  C CD     . LYS A 1 191 ? 28.997  -8.495  16.096 1.00 59.30  ? 191 LYS A CD     1 
ATOM   1438  C CE     . LYS A 1 191 ? 28.497  -9.893  16.414 1.00 51.74  ? 191 LYS A CE     1 
ATOM   1439  N NZ     . LYS A 1 191 ? 28.667  -10.219 17.854 1.00 48.87  ? 191 LYS A NZ     1 
ATOM   1440  N N      . ILE A 1 192 ? 26.596  -10.039 11.942 1.00 50.41  ? 192 ILE A N      1 
ATOM   1441  C CA     . ILE A 1 192 ? 26.551  -11.378 11.387 1.00 46.96  ? 192 ILE A CA     1 
ATOM   1442  C C      . ILE A 1 192 ? 26.808  -11.404 9.887  1.00 51.41  ? 192 ILE A C      1 
ATOM   1443  O O      . ILE A 1 192 ? 27.544  -12.246 9.408  1.00 54.34  ? 192 ILE A O      1 
ATOM   1444  C CB     . ILE A 1 192 ? 25.311  -12.158 11.850 1.00 40.88  ? 192 ILE A CB     1 
ATOM   1445  C CG1    . ILE A 1 192 ? 24.014  -11.622 11.284 1.00 38.27  ? 192 ILE A CG1    1 
ATOM   1446  C CG2    . ILE A 1 192 ? 25.236  -12.123 13.360 1.00 48.71  ? 192 ILE A CG2    1 
ATOM   1447  C CD1    . ILE A 1 192 ? 22.808  -12.283 11.907 1.00 36.33  ? 192 ILE A CD1    1 
ATOM   1448  N N      . LEU A 1 193 ? 26.259  -10.465 9.141  1.00 53.00  ? 193 LEU A N      1 
ATOM   1449  C CA     . LEU A 1 193 ? 26.532  -10.397 7.721  1.00 53.21  ? 193 LEU A CA     1 
ATOM   1450  C C      . LEU A 1 193 ? 27.956  -9.950  7.459  1.00 61.45  ? 193 LEU A C      1 
ATOM   1451  O O      . LEU A 1 193 ? 28.510  -10.300 6.430  1.00 64.90  ? 193 LEU A O      1 
ATOM   1452  C CB     . LEU A 1 193 ? 25.548  -9.486  7.020  1.00 49.74  ? 193 LEU A CB     1 
ATOM   1453  C CG     . LEU A 1 193 ? 24.166  -10.029 6.698  1.00 47.91  ? 193 LEU A CG     1 
ATOM   1454  C CD1    . LEU A 1 193 ? 23.287  -8.883  6.240  1.00 46.30  ? 193 LEU A CD1    1 
ATOM   1455  C CD2    . LEU A 1 193 ? 24.282  -11.077 5.609  1.00 55.90  ? 193 LEU A CD2    1 
ATOM   1456  N N      . THR A 1 194 ? 28.579  -9.208  8.370  1.00 58.77  ? 194 THR A N      1 
ATOM   1457  C CA     . THR A 1 194 ? 29.980  -8.825  8.197  1.00 54.48  ? 194 THR A CA     1 
ATOM   1458  C C      . THR A 1 194 ? 30.874  -10.047 8.333  1.00 56.92  ? 194 THR A C      1 
ATOM   1459  O O      . THR A 1 194 ? 31.848  -10.188 7.610  1.00 59.03  ? 194 THR A O      1 
ATOM   1460  C CB     . THR A 1 194 ? 30.401  -7.709  9.157  1.00 47.82  ? 194 THR A CB     1 
ATOM   1461  O OG1    . THR A 1 194 ? 29.616  -6.542  8.904  1.00 53.39  ? 194 THR A OG1    1 
ATOM   1462  C CG2    . THR A 1 194 ? 31.863  -7.356  8.983  1.00 46.69  ? 194 THR A CG2    1 
ATOM   1463  N N      . GLU A 1 195 ? 30.528  -10.958 9.232  1.00 54.84  ? 195 GLU A N      1 
ATOM   1464  C CA     . GLU A 1 195 ? 31.320  -12.160 9.443  1.00 50.22  ? 195 GLU A CA     1 
ATOM   1465  C C      . GLU A 1 195 ? 31.264  -13.049 8.241  1.00 52.77  ? 195 GLU A C      1 
ATOM   1466  O O      . GLU A 1 195 ? 32.221  -13.739 7.954  1.00 60.24  ? 195 GLU A O      1 
ATOM   1467  C CB     . GLU A 1 195 ? 30.790  -12.943 10.635 1.00 48.91  ? 195 GLU A CB     1 
ATOM   1468  C CG     . GLU A 1 195 ? 30.827  -12.224 11.969 1.00 51.33  ? 195 GLU A CG     1 
ATOM   1469  C CD     . GLU A 1 195 ? 29.953  -12.901 13.008 1.00 48.13  ? 195 GLU A CD     1 
ATOM   1470  O OE1    . GLU A 1 195 ? 29.098  -13.718 12.620 1.00 47.98  ? 195 GLU A OE1    1 
ATOM   1471  O OE2    . GLU A 1 195 ? 30.110  -12.614 14.209 1.00 45.16  ? 195 GLU A OE2    1 
ATOM   1472  N N      . ARG A 1 196 ? 30.143  -13.049 7.528  1.00 55.08  ? 196 ARG A N      1 
ATOM   1473  C CA     . ARG A 1 196 ? 29.975  -13.916 6.363  1.00 56.45  ? 196 ARG A CA     1 
ATOM   1474  C C      . ARG A 1 196 ? 30.857  -13.388 5.283  1.00 58.15  ? 196 ARG A C      1 
ATOM   1475  O O      . ARG A 1 196 ? 31.095  -14.047 4.280  1.00 54.20  ? 196 ARG A O      1 
ATOM   1476  C CB     . ARG A 1 196 ? 28.526  -13.957 5.894  1.00 52.69  ? 196 ARG A CB     1 
ATOM   1477  C CG     . ARG A 1 196 ? 28.147  -15.125 4.999  1.00 54.50  ? 196 ARG A CG     1 
ATOM   1478  C CD     . ARG A 1 196 ? 26.753  -14.917 4.429  1.00 62.47  ? 196 ARG A CD     1 
ATOM   1479  N NE     . ARG A 1 196 ? 26.367  -15.928 3.449  1.00 84.96  ? 196 ARG A NE     1 
ATOM   1480  C CZ     . ARG A 1 196 ? 25.614  -16.990 3.718  1.00 82.91  ? 196 ARG A CZ     1 
ATOM   1481  N NH1    . ARG A 1 196 ? 25.160  -17.190 4.945  1.00 75.08  ? 196 ARG A NH1    1 
ATOM   1482  N NH2    . ARG A 1 196 ? 25.316  -17.854 2.761  1.00 73.32  ? 196 ARG A NH2    1 
ATOM   1483  N N      . GLY A 1 197 ? 31.337  -12.169 5.454  1.00 59.61  ? 197 GLY A N      1 
ATOM   1484  C CA     . GLY A 1 197 ? 32.272  -11.616 4.491  1.00 59.20  ? 197 GLY A CA     1 
ATOM   1485  C C      . GLY A 1 197 ? 31.935  -10.234 4.034  1.00 56.54  ? 197 GLY A C      1 
ATOM   1486  O O      . GLY A 1 197 ? 32.788  -9.505  3.554  1.00 57.84  ? 197 GLY A O      1 
ATOM   1487  N N      . TYR A 1 198 ? 30.692  -9.859  4.188  1.00 56.18  ? 198 TYR A N      1 
ATOM   1488  C CA     . TYR A 1 198 ? 30.268  -8.571  3.714  1.00 62.54  ? 198 TYR A CA     1 
ATOM   1489  C C      . TYR A 1 198 ? 30.762  -7.493  4.636  1.00 63.17  ? 198 TYR A C      1 
ATOM   1490  O O      . TYR A 1 198 ? 31.337  -7.780  5.667  1.00 65.11  ? 198 TYR A O      1 
ATOM   1491  C CB     . TYR A 1 198 ? 28.754  -8.572  3.604  1.00 66.65  ? 198 TYR A CB     1 
ATOM   1492  C CG     . TYR A 1 198 ? 28.270  -9.721  2.763  1.00 64.28  ? 198 TYR A CG     1 
ATOM   1493  C CD1    . TYR A 1 198 ? 28.779  -9.926  1.492  1.00 60.20  ? 198 TYR A CD1    1 
ATOM   1494  C CD2    . TYR A 1 198 ? 27.325  -10.609 3.238  1.00 59.58  ? 198 TYR A CD2    1 
ATOM   1495  C CE1    . TYR A 1 198 ? 28.360  -10.982 0.718  1.00 60.95  ? 198 TYR A CE1    1 
ATOM   1496  C CE2    . TYR A 1 198 ? 26.896  -11.667 2.465  1.00 61.13  ? 198 TYR A CE2    1 
ATOM   1497  C CZ     . TYR A 1 198 ? 27.419  -11.844 1.207  1.00 59.99  ? 198 TYR A CZ     1 
ATOM   1498  O OH     . TYR A 1 198 ? 27.006  -12.891 0.430  1.00 55.00  ? 198 TYR A OH     1 
ATOM   1499  N N      . SER A 1 199 ? 30.501  -6.241  4.306  1.00 62.11  ? 199 SER A N      1 
ATOM   1500  C CA     . SER A 1 199 ? 31.018  -5.175  5.123  1.00 73.59  ? 199 SER A CA     1 
ATOM   1501  C C      . SER A 1 199 ? 30.001  -4.130  5.379  1.00 77.73  ? 199 SER A C      1 
ATOM   1502  O O      . SER A 1 199 ? 29.956  -3.139  4.668  1.00 77.40  ? 199 SER A O      1 
ATOM   1503  C CB     . SER A 1 199 ? 32.206  -4.519  4.464  1.00 69.81  ? 199 SER A CB     1 
ATOM   1504  O OG     . SER A 1 199 ? 32.731  -3.499  5.292  1.00 78.32  ? 199 SER A OG     1 
ATOM   1505  N N      . PHE A 1 200 ? 29.199  -4.308  6.422  1.00 78.30  ? 200 PHE A N      1 
ATOM   1506  C CA     . PHE A 1 200 ? 28.189  -3.327  6.779  1.00 75.95  ? 200 PHE A CA     1 
ATOM   1507  C C      . PHE A 1 200 ? 28.493  -2.615  8.085  1.00 78.50  ? 200 PHE A C      1 
ATOM   1508  O O      . PHE A 1 200 ? 28.074  -3.054  9.141  1.00 75.55  ? 200 PHE A O      1 
ATOM   1509  C CB     . PHE A 1 200 ? 26.835  -3.992  6.838  1.00 64.95  ? 200 PHE A CB     1 
ATOM   1510  C CG     . PHE A 1 200 ? 26.369  -4.521  5.527  1.00 61.43  ? 200 PHE A CG     1 
ATOM   1511  C CD1    . PHE A 1 200 ? 26.006  -3.661  4.515  1.00 66.12  ? 200 PHE A CD1    1 
ATOM   1512  C CD2    . PHE A 1 200 ? 26.283  -5.878  5.314  1.00 64.28  ? 200 PHE A CD2    1 
ATOM   1513  C CE1    . PHE A 1 200 ? 25.571  -4.146  3.306  1.00 58.21  ? 200 PHE A CE1    1 
ATOM   1514  C CE2    . PHE A 1 200 ? 25.846  -6.371  4.107  1.00 69.42  ? 200 PHE A CE2    1 
ATOM   1515  C CZ     . PHE A 1 200 ? 25.491  -5.504  3.102  1.00 61.99  ? 200 PHE A CZ     1 
ATOM   1516  N N      . THR A 1 201 ? 29.205  -1.502  8.023  1.00 76.81  ? 201 THR A N      1 
ATOM   1517  C CA     . THR A 1 201 ? 29.593  -0.787  9.225  1.00 67.64  ? 201 THR A CA     1 
ATOM   1518  C C      . THR A 1 201 ? 29.108  0.652   9.247  1.00 79.37  ? 201 THR A C      1 
ATOM   1519  O O      . THR A 1 201 ? 28.805  1.178   10.315 1.00 82.32  ? 201 THR A O      1 
ATOM   1520  C CB     . THR A 1 201 ? 31.112  -0.746  9.332  1.00 66.08  ? 201 THR A CB     1 
ATOM   1521  O OG1    . THR A 1 201 ? 31.654  -0.194  8.126  1.00 59.65  ? 201 THR A OG1    1 
ATOM   1522  C CG2    . THR A 1 201 ? 31.671  -2.140  9.531  1.00 77.87  ? 201 THR A CG2    1 
ATOM   1523  N N      . THR A 1 202 ? 29.052  1.323   8.097  1.00 82.85  ? 202 THR A N      1 
ATOM   1524  C CA     . THR A 1 202 ? 28.668  2.736   8.097  1.00 78.65  ? 202 THR A CA     1 
ATOM   1525  C C      . THR A 1 202 ? 27.171  2.926   8.305  1.00 75.65  ? 202 THR A C      1 
ATOM   1526  O O      . THR A 1 202 ? 26.412  1.972   8.268  1.00 69.95  ? 202 THR A O      1 
ATOM   1527  C CB     . THR A 1 202 ? 29.119  3.485   6.833  1.00 81.37  ? 202 THR A CB     1 
ATOM   1528  O OG1    . THR A 1 202 ? 28.220  3.210   5.756  1.00 82.40  ? 202 THR A OG1    1 
ATOM   1529  C CG2    . THR A 1 202 ? 30.522  3.074   6.446  1.00 79.24  ? 202 THR A CG2    1 
ATOM   1530  N N      . THR A 1 203 ? 26.750  4.157   8.548  1.00 80.19  ? 203 THR A N      1 
ATOM   1531  C CA     . THR A 1 203 ? 25.351  4.429   8.790  1.00 79.01  ? 203 THR A CA     1 
ATOM   1532  C C      . THR A 1 203 ? 24.554  4.238   7.531  1.00 79.88  ? 203 THR A C      1 
ATOM   1533  O O      . THR A 1 203 ? 23.391  3.857   7.583  1.00 78.06  ? 203 THR A O      1 
ATOM   1534  C CB     . THR A 1 203 ? 25.140  5.833   9.327  1.00 74.99  ? 203 THR A CB     1 
ATOM   1535  O OG1    . THR A 1 203 ? 23.744  6.136   9.287  1.00 80.03  ? 203 THR A OG1    1 
ATOM   1536  C CG2    . THR A 1 203 ? 25.910  6.846   8.501  1.00 72.69  ? 203 THR A CG2    1 
ATOM   1537  N N      . ALA A 1 204 ? 25.152  4.483   6.380  1.00 79.39  ? 204 ALA A N      1 
ATOM   1538  C CA     . ALA A 1 204 ? 24.452  4.224   5.142  1.00 75.33  ? 204 ALA A CA     1 
ATOM   1539  C C      . ALA A 1 204 ? 24.332  2.754   5.114  1.00 73.21  ? 204 ALA A C      1 
ATOM   1540  O O      . ALA A 1 204 ? 23.334  2.215   4.668  1.00 79.77  ? 204 ALA A O      1 
ATOM   1541  C CB     . ALA A 1 204 ? 25.264  4.677   3.957  1.00 79.44  ? 204 ALA A CB     1 
ATOM   1542  N N      . GLU A 1 205 ? 25.348  2.081   5.619  1.00 73.31  ? 205 GLU A N      1 
ATOM   1543  C CA     . GLU A 1 205 ? 25.332  0.642   5.542  1.00 72.59  ? 205 GLU A CA     1 
ATOM   1544  C C      . GLU A 1 205 ? 24.306  0.074   6.479  1.00 66.19  ? 205 GLU A C      1 
ATOM   1545  O O      . GLU A 1 205 ? 23.668  -0.901  6.150  1.00 67.35  ? 205 GLU A O      1 
ATOM   1546  C CB     . GLU A 1 205 ? 26.731  0.069   5.712  1.00 70.16  ? 205 GLU A CB     1 
ATOM   1547  C CG     . GLU A 1 205 ? 27.524  0.185   4.420  1.00 73.60  ? 205 GLU A CG     1 
ATOM   1548  C CD     . GLU A 1 205 ? 28.988  -0.149  4.568  1.00 73.09  ? 205 GLU A CD     1 
ATOM   1549  O OE1    . GLU A 1 205 ? 29.497  -0.125  5.699  1.00 75.10  ? 205 GLU A OE1    1 
ATOM   1550  O OE2    . GLU A 1 205 ? 29.635  -0.426  3.541  1.00 71.21  ? 205 GLU A OE2    1 
ATOM   1551  N N      . ARG A 1 206 ? 24.088  0.710   7.617  1.00 64.44  ? 206 ARG A N      1 
ATOM   1552  C CA     . ARG A 1 206 ? 23.052  0.251   8.529  1.00 60.69  ? 206 ARG A CA     1 
ATOM   1553  C C      . ARG A 1 206 ? 21.703  0.461   7.911  1.00 62.36  ? 206 ARG A C      1 
ATOM   1554  O O      . ARG A 1 206 ? 20.774  -0.290  8.146  1.00 62.09  ? 206 ARG A O      1 
ATOM   1555  C CB     . ARG A 1 206 ? 23.126  1.013   9.838  1.00 57.93  ? 206 ARG A CB     1 
ATOM   1556  C CG     . ARG A 1 206 ? 22.273  0.430   10.943 1.00 64.21  ? 206 ARG A CG     1 
ATOM   1557  C CD     . ARG A 1 206 ? 22.047  1.413   12.074 1.00 63.56  ? 206 ARG A CD     1 
ATOM   1558  N NE     . ARG A 1 206 ? 20.913  1.004   12.897 1.00 71.26  ? 206 ARG A NE     1 
ATOM   1559  C CZ     . ARG A 1 206 ? 19.653  1.354   12.661 1.00 79.75  ? 206 ARG A CZ     1 
ATOM   1560  N NH1    . ARG A 1 206 ? 19.358  2.133   11.628 1.00 78.00  ? 206 ARG A NH1    1 
ATOM   1561  N NH2    . ARG A 1 206 ? 18.685  0.929   13.457 1.00 69.13  ? 206 ARG A NH2    1 
ATOM   1562  N N      . GLU A 1 207 ? 21.582  1.493   7.112  1.00 63.85  ? 207 GLU A N      1 
ATOM   1563  C CA     . GLU A 1 207 ? 20.316  1.791   6.494  1.00 65.38  ? 207 GLU A CA     1 
ATOM   1564  C C      . GLU A 1 207 ? 19.852  0.627   5.655  1.00 61.36  ? 207 GLU A C      1 
ATOM   1565  O O      . GLU A 1 207 ? 18.723  0.198   5.763  1.00 61.87  ? 207 GLU A O      1 
ATOM   1566  C CB     . GLU A 1 207 ? 20.460  3.052   5.653  1.00 71.11  ? 207 GLU A CB     1 
ATOM   1567  C CG     . GLU A 1 207 ? 19.403  3.245   4.580  1.00 85.03  ? 207 GLU A CG     1 
ATOM   1568  C CD     . GLU A 1 207 ? 19.740  4.380   3.632  1.00 93.71  ? 207 GLU A CD     1 
ATOM   1569  O OE1    . GLU A 1 207 ? 20.075  5.478   4.118  1.00 97.88  ? 207 GLU A OE1    1 
ATOM   1570  O OE2    . GLU A 1 207 ? 19.662  4.174   2.403  1.00 88.96  ? 207 GLU A OE2    1 
ATOM   1571  N N      . ILE A 1 208 ? 20.728  0.089   4.828  1.00 60.20  ? 208 ILE A N      1 
ATOM   1572  C CA     . ILE A 1 208 ? 20.345  -0.985  3.925  1.00 60.29  ? 208 ILE A CA     1 
ATOM   1573  C C      . ILE A 1 208 ? 20.200  -2.327  4.609  1.00 60.19  ? 208 ILE A C      1 
ATOM   1574  O O      . ILE A 1 208 ? 19.616  -3.233  4.052  1.00 58.64  ? 208 ILE A O      1 
ATOM   1575  C CB     . ILE A 1 208 ? 21.386  -1.152  2.813  1.00 58.55  ? 208 ILE A CB     1 
ATOM   1576  C CG1    . ILE A 1 208 ? 22.026  0.189   2.475  1.00 61.77  ? 208 ILE A CG1    1 
ATOM   1577  C CG2    . ILE A 1 208 ? 20.761  -1.780  1.579  1.00 47.90  ? 208 ILE A CG2    1 
ATOM   1578  C CD1    . ILE A 1 208 ? 23.126  0.081   1.447  1.00 59.95  ? 208 ILE A CD1    1 
ATOM   1579  N N      . VAL A 1 209 ? 20.765  -2.477  5.798  1.00 52.57  ? 209 VAL A N      1 
ATOM   1580  C CA     . VAL A 1 209 ? 20.683  -3.737  6.497  1.00 49.91  ? 209 VAL A CA     1 
ATOM   1581  C C      . VAL A 1 209 ? 19.373  -3.739  7.240  1.00 50.92  ? 209 VAL A C      1 
ATOM   1582  O O      . VAL A 1 209 ? 19.025  -4.699  7.907  1.00 50.80  ? 209 VAL A O      1 
ATOM   1583  C CB     . VAL A 1 209 ? 21.888  -3.987  7.406  1.00 46.40  ? 209 VAL A CB     1 
ATOM   1584  C CG1    . VAL A 1 209 ? 21.833  -5.375  8.015  1.00 52.56  ? 209 VAL A CG1    1 
ATOM   1585  C CG2    . VAL A 1 209 ? 23.169  -3.844  6.615  1.00 45.65  ? 209 VAL A CG2    1 
ATOM   1586  N N      . ARG A 1 210 ? 18.590  -2.695  7.059  1.00 44.62  ? 210 ARG A N      1 
ATOM   1587  C CA     . ARG A 1 210 ? 17.280  -2.700  7.647  1.00 44.75  ? 210 ARG A CA     1 
ATOM   1588  C C      . ARG A 1 210 ? 16.381  -3.264  6.605  1.00 49.30  ? 210 ARG A C      1 
ATOM   1589  O O      . ARG A 1 210 ? 15.391  -3.875  6.934  1.00 51.51  ? 210 ARG A O      1 
ATOM   1590  C CB     . ARG A 1 210 ? 16.834  -1.308  8.013  1.00 48.58  ? 210 ARG A CB     1 
ATOM   1591  C CG     . ARG A 1 210 ? 15.756  -1.251  9.073  1.00 51.83  ? 210 ARG A CG     1 
ATOM   1592  C CD     . ARG A 1 210 ? 15.293  0.176   9.305  1.00 56.30  ? 210 ARG A CD     1 
ATOM   1593  N NE     . ARG A 1 210 ? 14.700  0.749   8.104  1.00 56.67  ? 210 ARG A NE     1 
ATOM   1594  C CZ     . ARG A 1 210 ? 15.342  1.547   7.259  1.00 57.93  ? 210 ARG A CZ     1 
ATOM   1595  N NH1    . ARG A 1 210 ? 16.601  1.886   7.489  1.00 52.46  ? 210 ARG A NH1    1 
ATOM   1596  N NH2    . ARG A 1 210 ? 14.719  2.013   6.189  1.00 65.50  ? 210 ARG A NH2    1 
ATOM   1597  N N      . ASP A 1 211 ? 16.684  -3.054  5.336  1.00 48.83  ? 211 ASP A N      1 
ATOM   1598  C CA     . ASP A 1 211 ? 15.867  -3.641  4.280  1.00 51.33  ? 211 ASP A CA     1 
ATOM   1599  C C      . ASP A 1 211 ? 16.228  -5.075  3.963  1.00 57.58  ? 211 ASP A C      1 
ATOM   1600  O O      . ASP A 1 211 ? 15.491  -5.755  3.275  1.00 58.41  ? 211 ASP A O      1 
ATOM   1601  C CB     . ASP A 1 211 ? 15.868  -2.805  3.010  1.00 48.25  ? 211 ASP A CB     1 
ATOM   1602  C CG     . ASP A 1 211 ? 14.641  -3.046  2.158  1.00 57.57  ? 211 ASP A CG     1 
ATOM   1603  O OD1    . ASP A 1 211 ? 13.534  -2.691  2.606  1.00 69.99  ? 211 ASP A OD1    1 
ATOM   1604  O OD2    . ASP A 1 211 ? 14.776  -3.588  1.045  1.00 45.82  ? 211 ASP A OD2    1 
ATOM   1605  N N      . ILE A 1 212 ? 17.333  -5.564  4.493  1.00 54.59  ? 212 ILE A N      1 
ATOM   1606  C CA     . ILE A 1 212 ? 17.688  -6.940  4.295  1.00 48.72  ? 212 ILE A CA     1 
ATOM   1607  C C      . ILE A 1 212 ? 17.214  -7.530  5.565  1.00 48.99  ? 212 ILE A C      1 
ATOM   1608  O O      . ILE A 1 212 ? 17.459  -8.680  5.851  1.00 55.29  ? 212 ILE A O      1 
ATOM   1609  C CB     . ILE A 1 212 ? 19.203  -7.095  4.196  1.00 50.34  ? 212 ILE A CB     1 
ATOM   1610  C CG1    . ILE A 1 212 ? 19.775  -6.094  3.208  1.00 44.27  ? 212 ILE A CG1    1 
ATOM   1611  C CG2    . ILE A 1 212 ? 19.581  -8.494  3.752  1.00 59.03  ? 212 ILE A CG2    1 
ATOM   1612  C CD1    . ILE A 1 212 ? 21.270  -6.205  3.052  1.00 51.34  ? 212 ILE A CD1    1 
ATOM   1613  N N      . LYS A 1 213 ? 16.475  -6.754  6.318  1.00 49.39  ? 213 LYS A N      1 
ATOM   1614  C CA     . LYS A 1 213 ? 15.991  -7.227  7.586  1.00 49.64  ? 213 LYS A CA     1 
ATOM   1615  C C      . LYS A 1 213 ? 14.528  -7.327  7.446  1.00 53.14  ? 213 LYS A C      1 
ATOM   1616  O O      . LYS A 1 213 ? 13.934  -8.361  7.648  1.00 58.77  ? 213 LYS A O      1 
ATOM   1617  C CB     . LYS A 1 213 ? 16.301  -6.236  8.686  1.00 45.91  ? 213 LYS A CB     1 
ATOM   1618  C CG     . LYS A 1 213 ? 16.122  -6.798  10.075 1.00 47.15  ? 213 LYS A CG     1 
ATOM   1619  C CD     . LYS A 1 213 ? 16.392  -5.741  11.122 1.00 52.50  ? 213 LYS A CD     1 
ATOM   1620  C CE     . LYS A 1 213 ? 15.288  -4.709  11.143 1.00 55.67  ? 213 LYS A CE     1 
ATOM   1621  N NZ     . LYS A 1 213 ? 15.283  -4.002  12.445 1.00 45.17  ? 213 LYS A NZ     1 
ATOM   1622  N N      . GLU A 1 214 ? 13.924  -6.236  7.085  1.00 53.96  ? 214 GLU A N      1 
ATOM   1623  C CA     . GLU A 1 214 ? 12.519  -6.260  6.898  1.00 56.05  ? 214 GLU A CA     1 
ATOM   1624  C C      . GLU A 1 214 ? 12.189  -7.201  5.759  1.00 56.95  ? 214 GLU A C      1 
ATOM   1625  O O      . GLU A 1 214 ? 11.375  -8.095  5.925  1.00 60.48  ? 214 GLU A O      1 
ATOM   1626  C CB     . GLU A 1 214 ? 12.026  -4.840  6.640  1.00 57.56  ? 214 GLU A CB     1 
ATOM   1627  C CG     . GLU A 1 214 ? 12.433  -3.861  7.724  1.00 52.09  ? 214 GLU A CG     1 
ATOM   1628  C CD     . GLU A 1 214 ? 12.103  -2.437  7.360  1.00 59.39  ? 214 GLU A CD     1 
ATOM   1629  O OE1    . GLU A 1 214 ? 11.511  -2.223  6.287  1.00 69.34  ? 214 GLU A OE1    1 
ATOM   1630  O OE2    . GLU A 1 214 ? 12.437  -1.529  8.142  1.00 61.41  ? 214 GLU A OE2    1 
ATOM   1631  N N      . LYS A 1 215 ? 12.832  -7.062  4.618  1.00 54.97  ? 215 LYS A N      1 
ATOM   1632  C CA     . LYS A 1 215 ? 12.436  -7.888  3.488  1.00 57.24  ? 215 LYS A CA     1 
ATOM   1633  C C      . LYS A 1 215 ? 12.759  -9.342  3.674  1.00 56.80  ? 215 LYS A C      1 
ATOM   1634  O O      . LYS A 1 215 ? 11.869  -10.162 3.797  1.00 55.35  ? 215 LYS A O      1 
ATOM   1635  C CB     . LYS A 1 215 ? 13.038  -7.381  2.184  1.00 52.68  ? 215 LYS A CB     1 
ATOM   1636  C CG     . LYS A 1 215 ? 12.620  -8.189  0.971  1.00 55.12  ? 215 LYS A CG     1 
ATOM   1637  C CD     . LYS A 1 215 ? 13.515  -7.910  -0.224 1.00 59.24  ? 215 LYS A CD     1 
ATOM   1638  C CE     . LYS A 1 215 ? 13.214  -8.874  -1.360 1.00 58.83  ? 215 LYS A CE     1 
ATOM   1639  N NZ     . LYS A 1 215 ? 14.221  -8.779  -2.448 1.00 56.76  ? 215 LYS A NZ     1 
ATOM   1640  N N      . LEU A 1 216 ? 14.028  -9.676  3.755  1.00 52.10  ? 216 LEU A N      1 
ATOM   1641  C CA     . LEU A 1 216 ? 14.428  -11.066 3.815  1.00 46.33  ? 216 LEU A CA     1 
ATOM   1642  C C      . LEU A 1 216 ? 14.266  -11.869 5.107  1.00 45.17  ? 216 LEU A C      1 
ATOM   1643  O O      . LEU A 1 216 ? 13.973  -13.044 5.047  1.00 50.35  ? 216 LEU A O      1 
ATOM   1644  C CB     . LEU A 1 216 ? 15.861  -11.149 3.309  1.00 39.30  ? 216 LEU A CB     1 
ATOM   1645  C CG     . LEU A 1 216 ? 15.970  -10.664 1.872  1.00 45.07  ? 216 LEU A CG     1 
ATOM   1646  C CD1    . LEU A 1 216 ? 17.413  -10.636 1.432  1.00 48.74  ? 216 LEU A CD1    1 
ATOM   1647  C CD2    . LEU A 1 216 ? 15.153  -11.553 0.955  1.00 54.59  ? 216 LEU A CD2    1 
ATOM   1648  N N      . CYS A 1 217 ? 14.443  -11.268 6.264  1.00 43.36  ? 217 CYS A N      1 
ATOM   1649  C CA     . CYS A 1 217 ? 14.431  -12.028 7.508  1.00 39.51  ? 217 CYS A CA     1 
ATOM   1650  C C      . CYS A 1 217 ? 13.139  -12.642 7.957  1.00 41.63  ? 217 CYS A C      1 
ATOM   1651  O O      . CYS A 1 217 ? 12.076  -12.164 7.606  1.00 43.23  ? 217 CYS A O      1 
ATOM   1652  C CB     . CYS A 1 217 ? 15.060  -11.232 8.636  1.00 39.16  ? 217 CYS A CB     1 
ATOM   1653  S SG     . CYS A 1 217 ? 16.832  -10.947 8.507  1.00 45.46  ? 217 CYS A SG     1 
ATOM   1654  N N      . TYR A 1 218 ? 13.240  -13.693 8.762  1.00 41.44  ? 218 TYR A N      1 
ATOM   1655  C CA     . TYR A 1 218 ? 12.082  -14.415 9.232  1.00 39.24  ? 218 TYR A CA     1 
ATOM   1656  C C      . TYR A 1 218 ? 12.477  -15.115 10.480 1.00 36.77  ? 218 TYR A C      1 
ATOM   1657  O O      . TYR A 1 218 ? 13.643  -15.312 10.716 1.00 35.57  ? 218 TYR A O      1 
ATOM   1658  C CB     . TYR A 1 218 ? 11.676  -15.465 8.213  1.00 42.24  ? 218 TYR A CB     1 
ATOM   1659  C CG     . TYR A 1 218 ? 12.567  -16.675 8.090  1.00 40.03  ? 218 TYR A CG     1 
ATOM   1660  C CD1    . TYR A 1 218 ? 13.749  -16.619 7.382  1.00 38.55  ? 218 TYR A CD1    1 
ATOM   1661  C CD2    . TYR A 1 218 ? 12.198  -17.885 8.641  1.00 40.54  ? 218 TYR A CD2    1 
ATOM   1662  C CE1    . TYR A 1 218 ? 14.557  -17.724 7.258  1.00 39.14  ? 218 TYR A CE1    1 
ATOM   1663  C CE2    . TYR A 1 218 ? 13.001  -18.994 8.522  1.00 47.90  ? 218 TYR A CE2    1 
ATOM   1664  C CZ     . TYR A 1 218 ? 14.176  -18.903 7.825  1.00 46.86  ? 218 TYR A CZ     1 
ATOM   1665  O OH     . TYR A 1 218 ? 14.979  -20.000 7.698  1.00 51.20  ? 218 TYR A OH     1 
ATOM   1666  N N      . VAL A 1 219 ? 11.507  -15.530 11.276 1.00 36.23  ? 219 VAL A N      1 
ATOM   1667  C CA     . VAL A 1 219 ? 11.783  -16.250 12.496 1.00 37.30  ? 219 VAL A CA     1 
ATOM   1668  C C      . VAL A 1 219 ? 11.540  -17.708 12.248 1.00 39.73  ? 219 VAL A C      1 
ATOM   1669  O O      . VAL A 1 219 ? 10.493  -18.075 11.760 1.00 45.34  ? 219 VAL A O      1 
ATOM   1670  C CB     . VAL A 1 219 ? 10.844  -15.821 13.619 1.00 35.65  ? 219 VAL A CB     1 
ATOM   1671  C CG1    . VAL A 1 219 ? 11.258  -16.454 14.931 1.00 37.38  ? 219 VAL A CG1    1 
ATOM   1672  C CG2    . VAL A 1 219 ? 10.823  -14.314 13.753 1.00 36.49  ? 219 VAL A CG2    1 
ATOM   1673  N N      . ALA A 1 220 ? 12.477  -18.564 12.612 1.00 45.82  ? 220 ALA A N      1 
ATOM   1674  C CA     . ALA A 1 220 ? 12.352  -19.980 12.371 1.00 42.79  ? 220 ALA A CA     1 
ATOM   1675  C C      . ALA A 1 220 ? 11.633  -20.620 13.511 1.00 45.09  ? 220 ALA A C      1 
ATOM   1676  O O      . ALA A 1 220 ? 11.883  -20.245 14.627 1.00 51.59  ? 220 ALA A O      1 
ATOM   1677  C CB     . ALA A 1 220 ? 13.728  -20.543 12.292 1.00 36.57  ? 220 ALA A CB     1 
ATOM   1678  N N      . LEU A 1 221 ? 10.808  -21.641 13.300 1.00 40.60  ? 221 LEU A N      1 
ATOM   1679  C CA     . LEU A 1 221 ? 10.148  -22.347 14.431 1.00 42.63  ? 221 LEU A CA     1 
ATOM   1680  C C      . LEU A 1 221 ? 11.054  -23.147 15.334 1.00 50.82  ? 221 LEU A C      1 
ATOM   1681  O O      . LEU A 1 221 ? 10.868  -23.128 16.535 1.00 54.76  ? 221 LEU A O      1 
ATOM   1682  C CB     . LEU A 1 221 ? 8.964   -23.192 13.996 1.00 38.78  ? 221 LEU A CB     1 
ATOM   1683  C CG     . LEU A 1 221 ? 8.069   -23.949 14.962 1.00 36.48  ? 221 LEU A CG     1 
ATOM   1684  C CD1    . LEU A 1 221 ? 7.250   -22.968 15.763 1.00 38.38  ? 221 LEU A CD1    1 
ATOM   1685  C CD2    . LEU A 1 221 ? 7.138   -24.828 14.152 1.00 38.69  ? 221 LEU A CD2    1 
ATOM   1686  N N      . ASP A 1 222 ? 11.998  -23.899 14.801 1.00 52.09  ? 222 ASP A N      1 
ATOM   1687  C CA     . ASP A 1 222 ? 12.974  -24.555 15.657 1.00 51.79  ? 222 ASP A CA     1 
ATOM   1688  C C      . ASP A 1 222 ? 14.267  -24.151 15.066 1.00 51.95  ? 222 ASP A C      1 
ATOM   1689  O O      . ASP A 1 222 ? 14.560  -24.511 13.944 1.00 53.97  ? 222 ASP A O      1 
ATOM   1690  C CB     . ASP A 1 222 ? 12.827  -26.059 15.624 1.00 59.98  ? 222 ASP A CB     1 
ATOM   1691  C CG     . ASP A 1 222 ? 13.833  -26.776 16.504 1.00 70.28  ? 222 ASP A CG     1 
ATOM   1692  O OD1    . ASP A 1 222 ? 14.489  -26.131 17.342 1.00 64.41  ? 222 ASP A OD1    1 
ATOM   1693  O OD2    . ASP A 1 222 ? 13.962  -28.007 16.363 1.00 75.46  ? 222 ASP A OD2    1 
ATOM   1694  N N      . PHE A 1 223 ? 15.081  -23.445 15.815 1.00 47.54  ? 223 PHE A N      1 
ATOM   1695  C CA     . PHE A 1 223 ? 16.317  -22.919 15.277 1.00 45.57  ? 223 PHE A CA     1 
ATOM   1696  C C      . PHE A 1 223 ? 17.216  -24.021 14.861 1.00 47.08  ? 223 PHE A C      1 
ATOM   1697  O O      . PHE A 1 223 ? 17.786  -23.983 13.798 1.00 44.73  ? 223 PHE A O      1 
ATOM   1698  C CB     . PHE A 1 223 ? 16.982  -22.156 16.401 1.00 40.39  ? 223 PHE A CB     1 
ATOM   1699  C CG     . PHE A 1 223 ? 18.112  -21.273 16.006 1.00 35.29  ? 223 PHE A CG     1 
ATOM   1700  C CD1    . PHE A 1 223 ? 17.896  -20.144 15.266 1.00 41.34  ? 223 PHE A CD1    1 
ATOM   1701  C CD2    . PHE A 1 223 ? 19.376  -21.521 16.483 1.00 33.11  ? 223 PHE A CD2    1 
ATOM   1702  C CE1    . PHE A 1 223 ? 18.938  -19.311 14.950 1.00 42.42  ? 223 PHE A CE1    1 
ATOM   1703  C CE2    . PHE A 1 223 ? 20.424  -20.695 16.168 1.00 36.48  ? 223 PHE A CE2    1 
ATOM   1704  C CZ     . PHE A 1 223 ? 20.204  -19.587 15.397 1.00 40.46  ? 223 PHE A CZ     1 
ATOM   1705  N N      . GLU A 1 224 ? 17.314  -25.049 15.663 1.00 48.03  ? 224 GLU A N      1 
ATOM   1706  C CA     . GLU A 1 224 ? 18.277  -26.070 15.371 1.00 45.34  ? 224 GLU A CA     1 
ATOM   1707  C C      . GLU A 1 224 ? 18.029  -26.780 14.084 1.00 49.96  ? 224 GLU A C      1 
ATOM   1708  O O      . GLU A 1 224 ? 18.971  -27.107 13.377 1.00 51.59  ? 224 GLU A O      1 
ATOM   1709  C CB     . GLU A 1 224 ? 18.364  -27.033 16.529 1.00 57.60  ? 224 GLU A CB     1 
ATOM   1710  C CG     . GLU A 1 224 ? 18.975  -26.442 17.787 1.00 58.67  ? 224 GLU A CG     1 
ATOM   1711  C CD     . GLU A 1 224 ? 19.489  -27.496 18.748 1.00 71.71  ? 224 GLU A CD     1 
ATOM   1712  O OE1    . GLU A 1 224 ? 19.280  -28.703 18.505 1.00 81.30  ? 224 GLU A OE1    1 
ATOM   1713  O OE2    . GLU A 1 224 ? 20.108  -27.114 19.757 1.00 69.34  ? 224 GLU A OE2    1 
ATOM   1714  N N      . GLN A 1 225 ? 16.783  -27.073 13.774 1.00 54.01  ? 225 GLN A N      1 
ATOM   1715  C CA     . GLN A 1 225 ? 16.469  -27.654 12.493 1.00 50.90  ? 225 GLN A CA     1 
ATOM   1716  C C      . GLN A 1 225 ? 16.795  -26.659 11.421 1.00 44.40  ? 225 GLN A C      1 
ATOM   1717  O O      . GLN A 1 225 ? 17.296  -27.013 10.370 1.00 41.01  ? 225 GLN A O      1 
ATOM   1718  C CB     . GLN A 1 225 ? 15.002  -28.002 12.429 1.00 51.64  ? 225 GLN A CB     1 
ATOM   1719  C CG     . GLN A 1 225 ? 14.563  -28.592 11.111 1.00 59.71  ? 225 GLN A CG     1 
ATOM   1720  C CD     . GLN A 1 225 ? 13.101  -28.948 11.114 1.00 70.87  ? 225 GLN A CD     1 
ATOM   1721  O OE1    . GLN A 1 225 ? 12.421  -28.802 12.126 1.00 65.41  ? 225 GLN A OE1    1 
ATOM   1722  N NE2    . GLN A 1 225 ? 12.608  -29.422 9.980  1.00 84.47  ? 225 GLN A NE2    1 
ATOM   1723  N N      . GLU A 1 226 ? 16.478  -25.404 11.670 1.00 36.88  ? 226 GLU A N      1 
ATOM   1724  C CA     . GLU A 1 226 ? 16.726  -24.390 10.685 1.00 36.97  ? 226 GLU A CA     1 
ATOM   1725  C C      . GLU A 1 226 ? 18.173  -24.112 10.429 1.00 38.69  ? 226 GLU A C      1 
ATOM   1726  O O      . GLU A 1 226 ? 18.547  -23.789 9.322  1.00 42.23  ? 226 GLU A O      1 
ATOM   1727  C CB     . GLU A 1 226 ? 15.841  -23.186 10.871 1.00 40.78  ? 226 GLU A CB     1 
ATOM   1728  C CG     . GLU A 1 226 ? 14.370  -23.535 10.740 1.00 40.12  ? 226 GLU A CG     1 
ATOM   1729  C CD     . GLU A 1 226 ? 13.749  -22.993 9.477  1.00 45.17  ? 226 GLU A CD     1 
ATOM   1730  O OE1    . GLU A 1 226 ? 14.478  -22.395 8.672  1.00 39.11  ? 226 GLU A OE1    1 
ATOM   1731  O OE2    . GLU A 1 226 ? 12.530  -23.161 9.294  1.00 49.30  ? 226 GLU A OE2    1 
ATOM   1732  N N      . MET A 1 227 ? 19.000  -24.196 11.440 1.00 35.23  ? 227 MET A N      1 
ATOM   1733  C CA     . MET A 1 227 ? 20.411  -24.055 11.194 1.00 35.95  ? 227 MET A CA     1 
ATOM   1734  C C      . MET A 1 227 ? 20.856  -25.189 10.309 1.00 44.64  ? 227 MET A C      1 
ATOM   1735  O O      . MET A 1 227 ? 21.704  -25.004 9.464  1.00 51.27  ? 227 MET A O      1 
ATOM   1736  C CB     . MET A 1 227 ? 21.201  -24.018 12.470 1.00 35.17  ? 227 MET A CB     1 
ATOM   1737  C CG     . MET A 1 227 ? 21.041  -22.753 13.272 1.00 40.92  ? 227 MET A CG     1 
ATOM   1738  S SD     . MET A 1 227 ? 21.907  -21.384 12.508 1.00 47.32  ? 227 MET A SD     1 
ATOM   1739  C CE     . MET A 1 227 ? 23.587  -21.978 12.574 1.00 49.95  ? 227 MET A CE     1 
ATOM   1740  N N      . ALA A 1 228 ? 20.319  -26.376 10.504 1.00 42.90  ? 228 ALA A N      1 
ATOM   1741  C CA     . ALA A 1 228 ? 20.635  -27.504 9.652  1.00 40.85  ? 228 ALA A CA     1 
ATOM   1742  C C      . ALA A 1 228 ? 20.214  -27.380 8.212  1.00 48.27  ? 228 ALA A C      1 
ATOM   1743  O O      . ALA A 1 228 ? 20.953  -27.741 7.324  1.00 50.33  ? 228 ALA A O      1 
ATOM   1744  C CB     . ALA A 1 228 ? 19.982  -28.710 10.224 1.00 36.88  ? 228 ALA A CB     1 
ATOM   1745  N N      . THR A 1 229 ? 19.016  -26.882 7.973  1.00 48.90  ? 229 THR A N      1 
ATOM   1746  C CA     . THR A 1 229 ? 18.506  -26.767 6.640  1.00 41.86  ? 229 THR A CA     1 
ATOM   1747  C C      . THR A 1 229 ? 19.472  -25.918 5.917  1.00 44.10  ? 229 THR A C      1 
ATOM   1748  O O      . THR A 1 229 ? 19.795  -26.166 4.789  1.00 52.96  ? 229 THR A O      1 
ATOM   1749  C CB     . THR A 1 229 ? 17.136  -26.112 6.664  1.00 33.50  ? 229 THR A CB     1 
ATOM   1750  O OG1    . THR A 1 229 ? 16.307  -26.795 7.609  1.00 27.58  ? 229 THR A OG1    1 
ATOM   1751  C CG2    . THR A 1 229 ? 16.491  -26.184 5.317  1.00 46.01  ? 229 THR A CG2    1 
ATOM   1752  N N      . ALA A 1 230 ? 19.988  -24.925 6.579  1.00 43.05  ? 230 ALA A N      1 
ATOM   1753  C CA     . ALA A 1 230 ? 20.880  -24.001 5.909  1.00 53.78  ? 230 ALA A CA     1 
ATOM   1754  C C      . ALA A 1 230 ? 22.244  -24.572 5.650  1.00 55.93  ? 230 ALA A C      1 
ATOM   1755  O O      . ALA A 1 230 ? 22.932  -24.152 4.729  1.00 59.07  ? 230 ALA A O      1 
ATOM   1756  C CB     . ALA A 1 230 ? 21.006  -22.738 6.721  1.00 51.72  ? 230 ALA A CB     1 
ATOM   1757  N N      . ALA A 1 231 ? 22.663  -25.506 6.476  1.00 54.21  ? 231 ALA A N      1 
ATOM   1758  C CA     . ALA A 1 231 ? 23.985  -26.058 6.322  1.00 57.52  ? 231 ALA A CA     1 
ATOM   1759  C C      . ALA A 1 231 ? 23.906  -27.271 5.440  1.00 65.10  ? 231 ALA A C      1 
ATOM   1760  O O      . ALA A 1 231 ? 24.921  -27.837 5.071  1.00 65.50  ? 231 ALA A O      1 
ATOM   1761  C CB     . ALA A 1 231 ? 24.559  -26.426 7.665  1.00 42.35  ? 231 ALA A CB     1 
ATOM   1762  N N      . SER A 1 232 ? 22.706  -27.643 5.032  1.00 59.77  ? 232 SER A N      1 
ATOM   1763  C CA     . SER A 1 232 ? 22.539  -28.794 4.181  1.00 50.87  ? 232 SER A CA     1 
ATOM   1764  C C      . SER A 1 232 ? 21.891  -28.423 2.890  1.00 54.16  ? 232 SER A C      1 
ATOM   1765  O O      . SER A 1 232 ? 21.986  -29.154 1.920  1.00 63.09  ? 232 SER A O      1 
ATOM   1766  C CB     . SER A 1 232 ? 21.642  -29.773 4.881  1.00 56.02  ? 232 SER A CB     1 
ATOM   1767  O OG     . SER A 1 232 ? 22.066  -29.987 6.214  1.00 58.97  ? 232 SER A OG     1 
ATOM   1768  N N      . SER A 1 233 ? 21.243  -27.271 2.861  1.00 51.39  ? 233 SER A N      1 
ATOM   1769  C CA     . SER A 1 233 ? 20.550  -26.838 1.667  1.00 57.70  ? 233 SER A CA     1 
ATOM   1770  C C      . SER A 1 233 ? 20.700  -25.369 1.367  1.00 59.55  ? 233 SER A C      1 
ATOM   1771  O O      . SER A 1 233 ? 21.055  -24.595 2.233  1.00 60.56  ? 233 SER A O      1 
ATOM   1772  C CB     . SER A 1 233 ? 19.068  -27.143 1.788  1.00 58.24  ? 233 SER A CB     1 
ATOM   1773  O OG     . SER A 1 233 ? 18.397  -26.078 2.417  1.00 56.60  ? 233 SER A OG     1 
ATOM   1774  N N      . SER A 1 234 ? 20.473  -24.984 0.121  1.00 64.00  ? 234 SER A N      1 
ATOM   1775  C CA     . SER A 1 234 ? 20.559  -23.593 -0.267 1.00 59.66  ? 234 SER A CA     1 
ATOM   1776  C C      . SER A 1 234 ? 19.157  -23.137 -0.460 1.00 64.78  ? 234 SER A C      1 
ATOM   1777  O O      . SER A 1 234 ? 18.904  -22.181 -1.176 1.00 65.67  ? 234 SER A O      1 
ATOM   1778  C CB     . SER A 1 234 ? 21.289  -23.463 -1.577 1.00 55.46  ? 234 SER A CB     1 
ATOM   1779  O OG     . SER A 1 234 ? 22.544  -24.112 -1.518 1.00 63.94  ? 234 SER A OG     1 
ATOM   1780  N N      . SER A 1 235 ? 18.224  -23.822 0.173  1.00 63.79  ? 235 SER A N      1 
ATOM   1781  C CA     . SER A 1 235 ? 16.839  -23.450 0.057  1.00 59.57  ? 235 SER A CA     1 
ATOM   1782  C C      . SER A 1 235 ? 16.654  -22.153 0.765  1.00 59.48  ? 235 SER A C      1 
ATOM   1783  O O      . SER A 1 235 ? 15.951  -21.277 0.284  1.00 57.28  ? 235 SER A O      1 
ATOM   1784  C CB     . SER A 1 235 ? 15.968  -24.503 0.713  1.00 54.83  ? 235 SER A CB     1 
ATOM   1785  O OG     . SER A 1 235 ? 16.206  -24.583 2.101  1.00 59.31  ? 235 SER A OG     1 
ATOM   1786  N N      . LEU A 1 236 ? 17.308  -22.004 1.904  1.00 61.99  ? 236 LEU A N      1 
ATOM   1787  C CA     . LEU A 1 236 ? 17.127  -20.813 2.718  1.00 53.00  ? 236 LEU A CA     1 
ATOM   1788  C C      . LEU A 1 236 ? 17.723  -19.582 2.138  1.00 46.37  ? 236 LEU A C      1 
ATOM   1789  O O      . LEU A 1 236 ? 17.183  -18.509 2.278  1.00 49.94  ? 236 LEU A O      1 
ATOM   1790  C CB     . LEU A 1 236 ? 17.735  -21.065 4.093  1.00 50.12  ? 236 LEU A CB     1 
ATOM   1791  C CG     . LEU A 1 236 ? 16.976  -22.077 4.941  1.00 53.88  ? 236 LEU A CG     1 
ATOM   1792  C CD1    . LEU A 1 236 ? 17.425  -21.964 6.384  1.00 44.56  ? 236 LEU A CD1    1 
ATOM   1793  C CD2    . LEU A 1 236 ? 15.479  -21.830 4.840  1.00 47.24  ? 236 LEU A CD2    1 
ATOM   1794  N N      . GLU A 1 237 ? 18.844  -19.725 1.480  1.00 48.67  ? 237 GLU A N      1 
ATOM   1795  C CA     . GLU A 1 237 ? 19.540  -18.577 0.973  1.00 53.49  ? 237 GLU A CA     1 
ATOM   1796  C C      . GLU A 1 237 ? 18.725  -17.744 0.045  1.00 64.17  ? 237 GLU A C      1 
ATOM   1797  O O      . GLU A 1 237 ? 17.998  -18.268 -0.783 1.00 70.41  ? 237 GLU A O      1 
ATOM   1798  C CB     . GLU A 1 237 ? 20.804  -19.020 0.267  1.00 58.73  ? 237 GLU A CB     1 
ATOM   1799  C CG     . GLU A 1 237 ? 21.827  -19.663 1.179  1.00 74.25  ? 237 GLU A CG     1 
ATOM   1800  C CD     . GLU A 1 237 ? 23.160  -19.858 0.494  1.00 88.48  ? 237 GLU A CD     1 
ATOM   1801  O OE1    . GLU A 1 237 ? 23.206  -19.763 -0.749 1.00 84.38  ? 237 GLU A OE1    1 
ATOM   1802  O OE2    . GLU A 1 237 ? 24.162  -20.106 1.196  1.00 93.06  ? 237 GLU A OE2    1 
ATOM   1803  N N      . LYS A 1 238 ? 18.862  -16.433 0.147  1.00 60.23  ? 238 LYS A N      1 
ATOM   1804  C CA     . LYS A 1 238 ? 18.146  -15.541 -0.728 1.00 47.53  ? 238 LYS A CA     1 
ATOM   1805  C C      . LYS A 1 238 ? 19.124  -14.478 -1.133 1.00 48.10  ? 238 LYS A C      1 
ATOM   1806  O O      . LYS A 1 238 ? 20.146  -14.314 -0.494 1.00 52.03  ? 238 LYS A O      1 
ATOM   1807  C CB     . LYS A 1 238 ? 16.964  -14.953 0.007  1.00 46.33  ? 238 LYS A CB     1 
ATOM   1808  C CG     . LYS A 1 238 ? 15.606  -15.308 -0.570 1.00 48.58  ? 238 LYS A CG     1 
ATOM   1809  C CD     . LYS A 1 238 ? 15.040  -16.548 0.089  1.00 51.53  ? 238 LYS A CD     1 
ATOM   1810  C CE     . LYS A 1 238 ? 13.561  -16.706 -0.213 1.00 51.54  ? 238 LYS A CE     1 
ATOM   1811  N NZ     . LYS A 1 238 ? 12.970  -17.881 0.484  1.00 53.26  ? 238 LYS A NZ     1 
ATOM   1812  N N      . SER A 1 239 ? 18.825  -13.746 -2.191 1.00 49.95  ? 239 SER A N      1 
ATOM   1813  C CA     . SER A 1 239 ? 19.748  -12.753 -2.702 1.00 55.69  ? 239 SER A CA     1 
ATOM   1814  C C      . SER A 1 239 ? 19.266  -11.328 -2.560 1.00 53.86  ? 239 SER A C      1 
ATOM   1815  O O      . SER A 1 239 ? 18.105  -11.047 -2.809 1.00 58.17  ? 239 SER A O      1 
ATOM   1816  C CB     . SER A 1 239 ? 19.976  -13.027 -4.178 1.00 54.12  ? 239 SER A CB     1 
ATOM   1817  O OG     . SER A 1 239 ? 18.786  -12.823 -4.914 1.00 53.22  ? 239 SER A OG     1 
ATOM   1818  N N      . TYR A 1 240 ? 20.149  -10.411 -2.181 1.00 49.57  ? 240 TYR A N      1 
ATOM   1819  C CA     . TYR A 1 240 ? 19.766  -9.014  -2.109 1.00 49.69  ? 240 TYR A CA     1 
ATOM   1820  C C      . TYR A 1 240 ? 20.688  -8.206  -2.948 1.00 48.64  ? 240 TYR A C      1 
ATOM   1821  O O      . TYR A 1 240 ? 21.874  -8.435  -2.947 1.00 45.19  ? 240 TYR A O      1 
ATOM   1822  C CB     . TYR A 1 240 ? 19.809  -8.500  -0.690 1.00 50.30  ? 240 TYR A CB     1 
ATOM   1823  C CG     . TYR A 1 240 ? 19.201  -7.139  -0.487 1.00 50.73  ? 240 TYR A CG     1 
ATOM   1824  C CD1    . TYR A 1 240 ? 17.834  -6.983  -0.366 1.00 55.59  ? 240 TYR A CD1    1 
ATOM   1825  C CD2    . TYR A 1 240 ? 19.996  -6.014  -0.399 1.00 51.22  ? 240 TYR A CD2    1 
ATOM   1826  C CE1    . TYR A 1 240 ? 17.275  -5.739  -0.175 1.00 56.64  ? 240 TYR A CE1    1 
ATOM   1827  C CE2    . TYR A 1 240 ? 19.446  -4.768  -0.210 1.00 53.78  ? 240 TYR A CE2    1 
ATOM   1828  C CZ     . TYR A 1 240 ? 18.086  -4.637  -0.097 1.00 52.64  ? 240 TYR A CZ     1 
ATOM   1829  O OH     . TYR A 1 240 ? 17.544  -3.394  0.091  1.00 53.19  ? 240 TYR A OH     1 
ATOM   1830  N N      . GLU A 1 241 ? 20.133  -7.244  -3.669 1.00 50.34  ? 241 GLU A N      1 
ATOM   1831  C CA     . GLU A 1 241 ? 20.926  -6.396  -4.523 1.00 49.79  ? 241 GLU A CA     1 
ATOM   1832  C C      . GLU A 1 241 ? 21.222  -5.124  -3.818 1.00 53.98  ? 241 GLU A C      1 
ATOM   1833  O O      . GLU A 1 241 ? 20.380  -4.241  -3.735 1.00 58.35  ? 241 GLU A O      1 
ATOM   1834  C CB     . GLU A 1 241 ? 20.199  -6.077  -5.812 1.00 50.57  ? 241 GLU A CB     1 
ATOM   1835  C CG     . GLU A 1 241 ? 21.099  -5.409  -6.833 1.00 55.28  ? 241 GLU A CG     1 
ATOM   1836  C CD     . GLU A 1 241 ? 20.349  -4.912  -8.044 1.00 68.76  ? 241 GLU A CD     1 
ATOM   1837  O OE1    . GLU A 1 241 ? 19.189  -5.324  -8.249 1.00 72.61  ? 241 GLU A OE1    1 
ATOM   1838  O OE2    . GLU A 1 241 ? 20.931  -4.107  -8.796 1.00 66.84  ? 241 GLU A OE2    1 
ATOM   1839  N N      . LEU A 1 242 ? 22.428  -4.993  -3.314 1.00 55.61  ? 242 LEU A N      1 
ATOM   1840  C CA     . LEU A 1 242 ? 22.817  -3.778  -2.658 1.00 52.96  ? 242 LEU A CA     1 
ATOM   1841  C C      . LEU A 1 242 ? 22.739  -2.677  -3.676 1.00 55.71  ? 242 LEU A C      1 
ATOM   1842  O O      . LEU A 1 242 ? 22.945  -2.897  -4.855 1.00 62.56  ? 242 LEU A O      1 
ATOM   1843  C CB     . LEU A 1 242 ? 24.233  -3.912  -2.140 1.00 46.91  ? 242 LEU A CB     1 
ATOM   1844  C CG     . LEU A 1 242 ? 24.498  -4.843  -0.980 1.00 53.06  ? 242 LEU A CG     1 
ATOM   1845  C CD1    . LEU A 1 242 ? 25.942  -4.639  -0.564 1.00 57.89  ? 242 LEU A CD1    1 
ATOM   1846  C CD2    . LEU A 1 242 ? 23.553  -4.477  0.148  1.00 59.56  ? 242 LEU A CD2    1 
ATOM   1847  N N      . PRO A 1 243 ? 22.508  -1.432  -3.229 1.00 51.00  ? 243 PRO A N      1 
ATOM   1848  C CA     . PRO A 1 243 ? 22.434  -0.451  -4.296 1.00 47.13  ? 243 PRO A CA     1 
ATOM   1849  C C      . PRO A 1 243 ? 23.744  -0.044  -4.906 1.00 49.78  ? 243 PRO A C      1 
ATOM   1850  O O      . PRO A 1 243 ? 23.688  0.686   -5.881 1.00 50.83  ? 243 PRO A O      1 
ATOM   1851  C CB     . PRO A 1 243 ? 21.845  0.759   -3.607 1.00 54.87  ? 243 PRO A CB     1 
ATOM   1852  C CG     . PRO A 1 243 ? 21.155  0.238   -2.401 1.00 59.01  ? 243 PRO A CG     1 
ATOM   1853  C CD     . PRO A 1 243 ? 22.085  -0.827  -1.950 1.00 59.24  ? 243 PRO A CD     1 
ATOM   1854  N N      . ASP A 1 244 ? 24.877  -0.528  -4.416 1.00 55.43  ? 244 ASP A N      1 
ATOM   1855  C CA     . ASP A 1 244 ? 26.155  -0.227  -5.055 1.00 54.61  ? 244 ASP A CA     1 
ATOM   1856  C C      . ASP A 1 244 ? 26.336  -1.126  -6.231 1.00 57.74  ? 244 ASP A C      1 
ATOM   1857  O O      . ASP A 1 244 ? 27.428  -1.271  -6.743 1.00 63.80  ? 244 ASP A O      1 
ATOM   1858  C CB     . ASP A 1 244 ? 27.337  -0.362  -4.098 1.00 60.93  ? 244 ASP A CB     1 
ATOM   1859  C CG     . ASP A 1 244 ? 27.646  -1.785  -3.730 1.00 73.36  ? 244 ASP A CG     1 
ATOM   1860  O OD1    . ASP A 1 244 ? 26.706  -2.570  -3.544 1.00 79.98  ? 244 ASP A OD1    1 
ATOM   1861  O OD2    . ASP A 1 244 ? 28.840  -2.114  -3.603 1.00 74.99  ? 244 ASP A OD2    1 
ATOM   1862  N N      . GLY A 1 245 ? 25.253  -1.735  -6.669 1.00 59.25  ? 245 GLY A N      1 
ATOM   1863  C CA     . GLY A 1 245 ? 25.309  -2.605  -7.819 1.00 56.19  ? 245 GLY A CA     1 
ATOM   1864  C C      . GLY A 1 245 ? 25.826  -3.971  -7.475 1.00 61.18  ? 245 GLY A C      1 
ATOM   1865  O O      . GLY A 1 245 ? 26.311  -4.673  -8.349 1.00 63.33  ? 245 GLY A O      1 
ATOM   1866  N N      . GLN A 1 246 ? 25.759  -4.358  -6.214 1.00 52.36  ? 246 GLN A N      1 
ATOM   1867  C CA     . GLN A 1 246 ? 26.343  -5.620  -5.834 1.00 46.87  ? 246 GLN A CA     1 
ATOM   1868  C C      . GLN A 1 246 ? 25.289  -6.489  -5.254 1.00 48.38  ? 246 GLN A C      1 
ATOM   1869  O O      . GLN A 1 246 ? 24.386  -5.997  -4.633 1.00 48.67  ? 246 GLN A O      1 
ATOM   1870  C CB     . GLN A 1 246 ? 27.472  -5.399  -4.844 1.00 48.24  ? 246 GLN A CB     1 
ATOM   1871  C CG     . GLN A 1 246 ? 28.515  -6.493  -4.811 1.00 48.03  ? 246 GLN A CG     1 
ATOM   1872  C CD     . GLN A 1 246 ? 29.669  -6.142  -3.907 1.00 56.00  ? 246 GLN A CD     1 
ATOM   1873  O OE1    . GLN A 1 246 ? 29.758  -5.023  -3.410 1.00 58.98  ? 246 GLN A OE1    1 
ATOM   1874  N NE2    . GLN A 1 246 ? 30.564  -7.095  -3.691 1.00 59.80  ? 246 GLN A NE2    1 
ATOM   1875  N N      . VAL A 1 247 ? 25.388  -7.794  -5.473 1.00 53.87  ? 247 VAL A N      1 
ATOM   1876  C CA     . VAL A 1 247 ? 24.416  -8.744  -4.954 1.00 48.92  ? 247 VAL A CA     1 
ATOM   1877  C C      . VAL A 1 247 ? 25.035  -9.519  -3.827 1.00 49.39  ? 247 VAL A C      1 
ATOM   1878  O O      . VAL A 1 247 ? 26.210  -9.862  -3.877 1.00 47.67  ? 247 VAL A O      1 
ATOM   1879  C CB     . VAL A 1 247 ? 23.903  -9.697  -6.044 1.00 49.02  ? 247 VAL A CB     1 
ATOM   1880  C CG1    . VAL A 1 247 ? 25.044  -10.420 -6.733 1.00 60.27  ? 247 VAL A CG1    1 
ATOM   1881  C CG2    . VAL A 1 247 ? 22.870  -10.674 -5.509 1.00 49.06  ? 247 VAL A CG2    1 
ATOM   1882  N N      . ILE A 1 248 ? 24.273  -9.738  -2.771 1.00 50.77  ? 248 ILE A N      1 
ATOM   1883  C CA     . ILE A 1 248 ? 24.794  -10.444 -1.638 1.00 52.78  ? 248 ILE A CA     1 
ATOM   1884  C C      . ILE A 1 248 ? 23.923  -11.647 -1.390 1.00 55.27  ? 248 ILE A C      1 
ATOM   1885  O O      . ILE A 1 248 ? 22.779  -11.667 -1.811 1.00 59.17  ? 248 ILE A O      1 
ATOM   1886  C CB     . ILE A 1 248 ? 24.879  -9.535  -0.410 1.00 52.21  ? 248 ILE A CB     1 
ATOM   1887  C CG1    . ILE A 1 248 ? 23.535  -8.939  -0.055 1.00 53.93  ? 248 ILE A CG1    1 
ATOM   1888  C CG2    . ILE A 1 248 ? 25.878  -8.417  -0.641 1.00 48.66  ? 248 ILE A CG2    1 
ATOM   1889  C CD1    . ILE A 1 248 ? 23.568  -8.251  1.284  1.00 51.08  ? 248 ILE A CD1    1 
ATOM   1890  N N      . THR A 1 249 ? 24.457  -12.664 -0.728 1.00 56.46  ? 249 THR A N      1 
ATOM   1891  C CA     . THR A 1 249 ? 23.686  -13.858 -0.426 1.00 55.19  ? 249 THR A CA     1 
ATOM   1892  C C      . THR A 1 249 ? 23.490  -14.028 1.057  1.00 57.54  ? 249 THR A C      1 
ATOM   1893  O O      . THR A 1 249 ? 24.452  -14.127 1.798  1.00 57.83  ? 249 THR A O      1 
ATOM   1894  C CB     . THR A 1 249 ? 24.353  -15.097 -0.999 1.00 55.64  ? 249 THR A CB     1 
ATOM   1895  O OG1    . THR A 1 249 ? 24.829  -14.811 -2.318 1.00 53.60  ? 249 THR A OG1    1 
ATOM   1896  C CG2    . THR A 1 249 ? 23.366  -16.240 -1.066 1.00 60.97  ? 249 THR A CG2    1 
ATOM   1897  N N      . ILE A 1 250 ? 22.241  -14.076 1.500  1.00 54.90  ? 250 ILE A N      1 
ATOM   1898  C CA     . ILE A 1 250 ? 21.937  -14.144 2.920  1.00 60.57  ? 250 ILE A CA     1 
ATOM   1899  C C      . ILE A 1 250 ? 21.169  -15.389 3.284  1.00 58.79  ? 250 ILE A C      1 
ATOM   1900  O O      . ILE A 1 250 ? 20.074  -15.592 2.792  1.00 53.11  ? 250 ILE A O      1 
ATOM   1901  C CB     . ILE A 1 250 ? 21.040  -12.964 3.305  1.00 60.39  ? 250 ILE A CB     1 
ATOM   1902  C CG1    . ILE A 1 250 ? 21.617  -11.648 2.784  1.00 63.66  ? 250 ILE A CG1    1 
ATOM   1903  C CG2    . ILE A 1 250 ? 20.845  -12.888 4.809  1.00 53.23  ? 250 ILE A CG2    1 
ATOM   1904  C CD1    . ILE A 1 250 ? 20.980  -11.163 1.504  1.00 58.22  ? 250 ILE A CD1    1 
ATOM   1905  N N      . GLY A 1 251 ? 21.719  -16.213 4.164  1.00 51.97  ? 251 GLY A N      1 
ATOM   1906  C CA     . GLY A 1 251 ? 21.077  -17.461 4.504  1.00 44.99  ? 251 GLY A CA     1 
ATOM   1907  C C      . GLY A 1 251 ? 20.706  -17.712 5.934  1.00 45.86  ? 251 GLY A C      1 
ATOM   1908  O O      . GLY A 1 251 ? 19.568  -17.532 6.311  1.00 45.60  ? 251 GLY A O      1 
ATOM   1909  N N      . ASN A 1 252 ? 21.663  -18.151 6.737  1.00 51.53  ? 252 ASN A N      1 
ATOM   1910  C CA     . ASN A 1 252 ? 21.387  -18.471 8.124  1.00 43.39  ? 252 ASN A CA     1 
ATOM   1911  C C      . ASN A 1 252 ? 21.084  -17.218 8.857  1.00 43.09  ? 252 ASN A C      1 
ATOM   1912  O O      . ASN A 1 252 ? 20.358  -17.228 9.822  1.00 40.24  ? 252 ASN A O      1 
ATOM   1913  C CB     . ASN A 1 252 ? 22.542  -19.238 8.762  1.00 39.20  ? 252 ASN A CB     1 
ATOM   1914  C CG     . ASN A 1 252 ? 23.893  -18.786 8.271  1.00 51.22  ? 252 ASN A CG     1 
ATOM   1915  O OD1    . ASN A 1 252 ? 24.341  -17.691 8.583  1.00 53.30  ? 252 ASN A OD1    1 
ATOM   1916  N ND2    . ASN A 1 252 ? 24.567  -19.647 7.520  1.00 50.37  ? 252 ASN A ND2    1 
ATOM   1917  N N      . GLU A 1 253 ? 21.615  -16.112 8.369  1.00 44.22  ? 253 GLU A N      1 
ATOM   1918  C CA     . GLU A 1 253 ? 21.442  -14.833 9.018  1.00 38.65  ? 253 GLU A CA     1 
ATOM   1919  C C      . GLU A 1 253 ? 20.029  -14.385 9.018  1.00 37.02  ? 253 GLU A C      1 
ATOM   1920  O O      . GLU A 1 253 ? 19.662  -13.477 9.725  1.00 38.30  ? 253 GLU A O      1 
ATOM   1921  C CB     . GLU A 1 253 ? 22.304  -13.813 8.312  1.00 34.89  ? 253 GLU A CB     1 
ATOM   1922  C CG     . GLU A 1 253 ? 23.792  -14.041 8.467  1.00 43.17  ? 253 GLU A CG     1 
ATOM   1923  C CD     . GLU A 1 253 ? 24.379  -14.841 7.337  1.00 49.19  ? 253 GLU A CD     1 
ATOM   1924  O OE1    . GLU A 1 253 ? 23.677  -15.042 6.333  1.00 53.39  ? 253 GLU A OE1    1 
ATOM   1925  O OE2    . GLU A 1 253 ? 25.541  -15.271 7.454  1.00 49.61  ? 253 GLU A OE2    1 
ATOM   1926  N N      . ARG A 1 254 ? 19.201  -15.055 8.266  1.00 38.55  ? 254 ARG A N      1 
ATOM   1927  C CA     . ARG A 1 254 ? 17.852  -14.602 8.141  1.00 38.26  ? 254 ARG A CA     1 
ATOM   1928  C C      . ARG A 1 254 ? 17.061  -14.882 9.367  1.00 38.63  ? 254 ARG A C      1 
ATOM   1929  O O      . ARG A 1 254 ? 16.159  -14.147 9.684  1.00 39.62  ? 254 ARG A O      1 
ATOM   1930  C CB     . ARG A 1 254 ? 17.198  -15.277 6.957  1.00 42.44  ? 254 ARG A CB     1 
ATOM   1931  C CG     . ARG A 1 254 ? 17.723  -14.858 5.603  1.00 40.67  ? 254 ARG A CG     1 
ATOM   1932  C CD     . ARG A 1 254 ? 17.014  -15.643 4.520  1.00 40.75  ? 254 ARG A CD     1 
ATOM   1933  N NE     . ARG A 1 254 ? 15.616  -15.256 4.407  1.00 40.67  ? 254 ARG A NE     1 
ATOM   1934  C CZ     . ARG A 1 254 ? 14.665  -16.038 3.912  1.00 46.33  ? 254 ARG A CZ     1 
ATOM   1935  N NH1    . ARG A 1 254 ? 14.953  -17.262 3.511  1.00 51.14  ? 254 ARG A NH1    1 
ATOM   1936  N NH2    . ARG A 1 254 ? 13.418  -15.603 3.841  1.00 47.01  ? 254 ARG A NH2    1 
ATOM   1937  N N      . PHE A 1 255 ? 17.401  -15.930 10.082 1.00 37.08  ? 255 PHE A N      1 
ATOM   1938  C CA     . PHE A 1 255 ? 16.655  -16.295 11.267 1.00 36.96  ? 255 PHE A CA     1 
ATOM   1939  C C      . PHE A 1 255 ? 17.461  -16.136 12.508 1.00 38.69  ? 255 PHE A C      1 
ATOM   1940  O O      . PHE A 1 255 ? 16.912  -16.075 13.594 1.00 39.85  ? 255 PHE A O      1 
ATOM   1941  C CB     . PHE A 1 255 ? 16.163  -17.722 11.196 1.00 42.63  ? 255 PHE A CB     1 
ATOM   1942  C CG     . PHE A 1 255 ? 17.196  -18.715 10.792 1.00 42.82  ? 255 PHE A CG     1 
ATOM   1943  C CD1    . PHE A 1 255 ? 17.461  -18.951 9.466  1.00 44.58  ? 255 PHE A CD1    1 
ATOM   1944  C CD2    . PHE A 1 255 ? 17.856  -19.448 11.739 1.00 36.71  ? 255 PHE A CD2    1 
ATOM   1945  C CE1    . PHE A 1 255 ? 18.398  -19.877 9.097  1.00 44.36  ? 255 PHE A CE1    1 
ATOM   1946  C CE2    . PHE A 1 255 ? 18.796  -20.372 11.382 1.00 37.76  ? 255 PHE A CE2    1 
ATOM   1947  C CZ     . PHE A 1 255 ? 19.072  -20.587 10.058 1.00 43.13  ? 255 PHE A CZ     1 
ATOM   1948  N N      . ARG A 1 256 ? 18.769  -16.076 12.360 1.00 38.18  ? 256 ARG A N      1 
ATOM   1949  C CA     . ARG A 1 256 ? 19.600  -15.882 13.500 1.00 37.79  ? 256 ARG A CA     1 
ATOM   1950  C C      . ARG A 1 256 ? 19.300  -14.501 14.017 1.00 43.60  ? 256 ARG A C      1 
ATOM   1951  O O      . ARG A 1 256 ? 19.226  -14.288 15.215 1.00 41.90  ? 256 ARG A O      1 
ATOM   1952  C CB     . ARG A 1 256 ? 21.059  -16.020 13.117 1.00 31.04  ? 256 ARG A CB     1 
ATOM   1953  C CG     . ARG A 1 256 ? 21.517  -17.412 12.787 1.00 33.88  ? 256 ARG A CG     1 
ATOM   1954  C CD     . ARG A 1 256 ? 22.878  -17.323 12.147 1.00 33.83  ? 256 ARG A CD     1 
ATOM   1955  N NE     . ARG A 1 256 ? 23.801  -16.594 12.994 1.00 30.46  ? 256 ARG A NE     1 
ATOM   1956  C CZ     . ARG A 1 256 ? 24.958  -16.108 12.573 1.00 40.10  ? 256 ARG A CZ     1 
ATOM   1957  N NH1    . ARG A 1 256 ? 25.321  -16.260 11.310 1.00 44.48  ? 256 ARG A NH1    1 
ATOM   1958  N NH2    . ARG A 1 256 ? 25.746  -15.461 13.412 1.00 46.95  ? 256 ARG A NH2    1 
ATOM   1959  N N      . CYS A 1 257 ? 19.125  -13.547 13.118 1.00 39.16  ? 257 CYS A N      1 
ATOM   1960  C CA     . CYS A 1 257 ? 18.898  -12.170 13.518 1.00 36.06  ? 257 CYS A CA     1 
ATOM   1961  C C      . CYS A 1 257 ? 17.669  -11.993 14.379 1.00 42.23  ? 257 CYS A C      1 
ATOM   1962  O O      . CYS A 1 257 ? 17.776  -11.493 15.483 1.00 38.13  ? 257 CYS A O      1 
ATOM   1963  C CB     . CYS A 1 257 ? 18.886  -11.256 12.305 1.00 38.64  ? 257 CYS A CB     1 
ATOM   1964  S SG     . CYS A 1 257 ? 18.216  -9.601  12.539 1.00 60.20  ? 257 CYS A SG     1 
ATOM   1965  N N      . PRO A 1 258 ? 16.473  -12.429 13.908 1.00 43.00  ? 258 PRO A N      1 
ATOM   1966  C CA     . PRO A 1 258 ? 15.357  -12.243 14.830 1.00 43.82  ? 258 PRO A CA     1 
ATOM   1967  C C      . PRO A 1 258 ? 15.312  -13.189 15.979 1.00 38.38  ? 258 PRO A C      1 
ATOM   1968  O O      . PRO A 1 258 ? 14.431  -13.067 16.805 1.00 34.29  ? 258 PRO A O      1 
ATOM   1969  C CB     . PRO A 1 258 ? 14.159  -12.498 13.961 1.00 37.63  ? 258 PRO A CB     1 
ATOM   1970  C CG     . PRO A 1 258 ? 14.634  -13.421 12.934 1.00 41.56  ? 258 PRO A CG     1 
ATOM   1971  C CD     . PRO A 1 258 ? 15.949  -12.835 12.588 1.00 39.54  ? 258 PRO A CD     1 
ATOM   1972  N N      . GLU A 1 259 ? 16.246  -14.115 16.064 1.00 37.33  ? 259 GLU A N      1 
ATOM   1973  C CA     . GLU A 1 259 ? 16.288  -15.023 17.188 1.00 41.36  ? 259 GLU A CA     1 
ATOM   1974  C C      . GLU A 1 259 ? 16.762  -14.256 18.363 1.00 46.97  ? 259 GLU A C      1 
ATOM   1975  O O      . GLU A 1 259 ? 16.575  -14.661 19.494 1.00 47.19  ? 259 GLU A O      1 
ATOM   1976  C CB     . GLU A 1 259 ? 17.234  -16.179 16.912 1.00 41.72  ? 259 GLU A CB     1 
ATOM   1977  C CG     . GLU A 1 259 ? 17.617  -17.036 18.106 1.00 53.09  ? 259 GLU A CG     1 
ATOM   1978  C CD     . GLU A 1 259 ? 16.654  -18.163 18.352 1.00 56.11  ? 259 GLU A CD     1 
ATOM   1979  O OE1    . GLU A 1 259 ? 15.955  -18.533 17.397 1.00 49.25  ? 259 GLU A OE1    1 
ATOM   1980  O OE2    . GLU A 1 259 ? 16.613  -18.688 19.482 1.00 56.83  ? 259 GLU A OE2    1 
ATOM   1981  N N      . ALA A 1 260 ? 17.407  -13.134 18.107 1.00 48.22  ? 260 ALA A N      1 
ATOM   1982  C CA     . ALA A 1 260 ? 17.989  -12.392 19.194 1.00 41.01  ? 260 ALA A CA     1 
ATOM   1983  C C      . ALA A 1 260 ? 16.897  -12.086 20.132 1.00 40.90  ? 260 ALA A C      1 
ATOM   1984  O O      . ALA A 1 260 ? 17.142  -11.837 21.273 1.00 51.88  ? 260 ALA A O      1 
ATOM   1985  C CB     . ALA A 1 260 ? 18.627  -11.125 18.702 1.00 35.51  ? 260 ALA A CB     1 
ATOM   1986  N N      . LEU A 1 261 ? 15.661  -12.166 19.696 1.00 41.10  ? 261 LEU A N      1 
ATOM   1987  C CA     . LEU A 1 261 ? 14.563  -11.798 20.561 1.00 40.59  ? 261 LEU A CA     1 
ATOM   1988  C C      . LEU A 1 261 ? 14.395  -12.911 21.537 1.00 38.30  ? 261 LEU A C      1 
ATOM   1989  O O      . LEU A 1 261 ? 14.338  -12.696 22.730 1.00 38.98  ? 261 LEU A O      1 
ATOM   1990  C CB     . LEU A 1 261 ? 13.306  -11.602 19.740 1.00 35.43  ? 261 LEU A CB     1 
ATOM   1991  C CG     . LEU A 1 261 ? 13.341  -10.500 18.691 1.00 38.14  ? 261 LEU A CG     1 
ATOM   1992  C CD1    . LEU A 1 261 ? 12.199  -10.673 17.710 1.00 36.36  ? 261 LEU A CD1    1 
ATOM   1993  C CD2    . LEU A 1 261 ? 13.283  -9.138  19.355 1.00 43.05  ? 261 LEU A CD2    1 
ATOM   1994  N N      . PHE A 1 262 ? 14.353  -14.121 21.033 1.00 37.87  ? 262 PHE A N      1 
ATOM   1995  C CA     . PHE A 1 262 ? 14.125  -15.257 21.884 1.00 39.00  ? 262 PHE A CA     1 
ATOM   1996  C C      . PHE A 1 262 ? 15.361  -15.624 22.648 1.00 41.06  ? 262 PHE A C      1 
ATOM   1997  O O      . PHE A 1 262 ? 15.267  -16.096 23.766 1.00 43.72  ? 262 PHE A O      1 
ATOM   1998  C CB     . PHE A 1 262 ? 13.620  -16.405 21.049 1.00 36.30  ? 262 PHE A CB     1 
ATOM   1999  C CG     . PHE A 1 262 ? 12.273  -16.161 20.431 1.00 36.95  ? 262 PHE A CG     1 
ATOM   2000  C CD1    . PHE A 1 262 ? 11.119  -16.414 21.143 1.00 32.32  ? 262 PHE A CD1    1 
ATOM   2001  C CD2    . PHE A 1 262 ? 12.162  -15.693 19.140 1.00 33.11  ? 262 PHE A CD2    1 
ATOM   2002  C CE1    . PHE A 1 262 ? 9.882   -16.197 20.585 1.00 27.59  ? 262 PHE A CE1    1 
ATOM   2003  C CE2    . PHE A 1 262 ? 10.928  -15.471 18.576 1.00 28.96  ? 262 PHE A CE2    1 
ATOM   2004  C CZ     . PHE A 1 262 ? 9.787   -15.726 19.299 1.00 29.21  ? 262 PHE A CZ     1 
ATOM   2005  N N      . GLN A 1 263 ? 16.522  -15.419 22.058 1.00 45.03  ? 263 GLN A N      1 
ATOM   2006  C CA     . GLN A 1 263 ? 17.760  -15.661 22.760 1.00 45.94  ? 263 GLN A CA     1 
ATOM   2007  C C      . GLN A 1 263 ? 18.546  -14.411 22.663 1.00 43.28  ? 263 GLN A C      1 
ATOM   2008  O O      . GLN A 1 263 ? 19.281  -14.217 21.717 1.00 39.33  ? 263 GLN A O      1 
ATOM   2009  C CB     . GLN A 1 263 ? 18.524  -16.797 22.140 1.00 49.06  ? 263 GLN A CB     1 
ATOM   2010  C CG     . GLN A 1 263 ? 18.065  -18.163 22.611 1.00 58.35  ? 263 GLN A CG     1 
ATOM   2011  C CD     . GLN A 1 263 ? 18.993  -19.274 22.178 1.00 66.42  ? 263 GLN A CD     1 
ATOM   2012  O OE1    . GLN A 1 263 ? 19.186  -19.512 20.987 1.00 60.64  ? 263 GLN A OE1    1 
ATOM   2013  N NE2    . GLN A 1 263 ? 19.569  -19.972 23.149 1.00 59.56  ? 263 GLN A NE2    1 
ATOM   2014  N N      . PRO A 1 264 ? 18.402  -13.522 23.685 1.00 42.30  ? 264 PRO A N      1 
ATOM   2015  C CA     . PRO A 1 264 ? 19.086  -12.251 23.541 1.00 39.69  ? 264 PRO A CA     1 
ATOM   2016  C C      . PRO A 1 264 ? 20.526  -12.376 23.857 1.00 44.47  ? 264 PRO A C      1 
ATOM   2017  O O      . PRO A 1 264 ? 21.223  -11.385 23.829 1.00 49.81  ? 264 PRO A O      1 
ATOM   2018  C CB     . PRO A 1 264 ? 18.423  -11.396 24.598 1.00 38.14  ? 264 PRO A CB     1 
ATOM   2019  C CG     . PRO A 1 264 ? 17.180  -12.097 24.998 1.00 34.24  ? 264 PRO A CG     1 
ATOM   2020  C CD     . PRO A 1 264 ? 17.614  -13.510 24.938 1.00 37.87  ? 264 PRO A CD     1 
ATOM   2021  N N      . SER A 1 265 ? 20.962  -13.578 24.201 1.00 45.32  ? 265 SER A N      1 
ATOM   2022  C CA     . SER A 1 265 ? 22.334  -13.819 24.592 1.00 44.91  ? 265 SER A CA     1 
ATOM   2023  C C      . SER A 1 265 ? 23.167  -13.581 23.415 1.00 43.90  ? 265 SER A C      1 
ATOM   2024  O O      . SER A 1 265 ? 24.368  -13.415 23.511 1.00 47.60  ? 265 SER A O      1 
ATOM   2025  C CB     . SER A 1 265 ? 22.493  -15.271 24.965 1.00 42.59  ? 265 SER A CB     1 
ATOM   2026  O OG     . SER A 1 265 ? 22.468  -16.091 23.814 1.00 50.45  ? 265 SER A OG     1 
ATOM   2027  N N      . PHE A 1 266 ? 22.528  -13.564 22.275 1.00 38.60  ? 266 PHE A N      1 
ATOM   2028  C CA     . PHE A 1 266 ? 23.246  -13.382 21.056 1.00 45.26  ? 266 PHE A CA     1 
ATOM   2029  C C      . PHE A 1 266 ? 23.797  -12.004 21.139 1.00 51.96  ? 266 PHE A C      1 
ATOM   2030  O O      . PHE A 1 266 ? 24.835  -11.716 20.566 1.00 56.52  ? 266 PHE A O      1 
ATOM   2031  C CB     . PHE A 1 266 ? 22.282  -13.463 19.889 1.00 49.16  ? 266 PHE A CB     1 
ATOM   2032  C CG     . PHE A 1 266 ? 21.914  -14.863 19.480 1.00 52.90  ? 266 PHE A CG     1 
ATOM   2033  C CD1    . PHE A 1 266 ? 22.040  -15.926 20.353 1.00 51.24  ? 266 PHE A CD1    1 
ATOM   2034  C CD2    . PHE A 1 266 ? 21.430  -15.109 18.212 1.00 52.42  ? 266 PHE A CD2    1 
ATOM   2035  C CE1    . PHE A 1 266 ? 21.700  -17.203 19.966 1.00 48.04  ? 266 PHE A CE1    1 
ATOM   2036  C CE2    . PHE A 1 266 ? 21.093  -16.382 17.817 1.00 49.06  ? 266 PHE A CE2    1 
ATOM   2037  C CZ     . PHE A 1 266 ? 21.224  -17.431 18.696 1.00 48.48  ? 266 PHE A CZ     1 
ATOM   2038  N N      . LEU A 1 267 ? 23.132  -11.145 21.897 1.00 54.10  ? 267 LEU A N      1 
ATOM   2039  C CA     . LEU A 1 267 ? 23.541  -9.741  21.988 1.00 50.64  ? 267 LEU A CA     1 
ATOM   2040  C C      . LEU A 1 267 ? 24.206  -9.364  23.294 1.00 53.59  ? 267 LEU A C      1 
ATOM   2041  O O      . LEU A 1 267 ? 24.495  -8.200  23.523 1.00 59.43  ? 267 LEU A O      1 
ATOM   2042  C CB     . LEU A 1 267 ? 22.341  -8.837  21.755 1.00 43.68  ? 267 LEU A CB     1 
ATOM   2043  C CG     . LEU A 1 267 ? 22.009  -8.599  20.295 1.00 50.35  ? 267 LEU A CG     1 
ATOM   2044  C CD1    . LEU A 1 267 ? 20.813  -7.677  20.220 1.00 54.65  ? 267 LEU A CD1    1 
ATOM   2045  C CD2    . LEU A 1 267 ? 23.210  -7.964  19.614 1.00 55.41  ? 267 LEU A CD2    1 
ATOM   2046  N N      . GLY A 1 268 ? 24.443  -10.333 24.160 1.00 50.27  ? 268 GLY A N      1 
ATOM   2047  C CA     . GLY A 1 268 ? 25.130  -10.067 25.403 1.00 47.86  ? 268 GLY A CA     1 
ATOM   2048  C C      . GLY A 1 268 ? 24.174  -9.995  26.548 1.00 54.84  ? 268 GLY A C      1 
ATOM   2049  O O      . GLY A 1 268 ? 24.558  -10.170 27.694 1.00 72.67  ? 268 GLY A O      1 
ATOM   2050  N N      . MET A 1 269 ? 22.917  -9.758  26.243 1.00 52.55  ? 269 MET A N      1 
ATOM   2051  C CA     . MET A 1 269 ? 21.931  -9.606  27.280 1.00 55.47  ? 269 MET A CA     1 
ATOM   2052  C C      . MET A 1 269 ? 21.670  -10.870 28.041 1.00 57.75  ? 269 MET A C      1 
ATOM   2053  O O      . MET A 1 269 ? 21.567  -11.940 27.469 1.00 57.30  ? 269 MET A O      1 
ATOM   2054  C CB     . MET A 1 269 ? 20.656  -9.045  26.682 1.00 52.47  ? 269 MET A CB     1 
ATOM   2055  C CG     . MET A 1 269 ? 20.890  -7.759  25.913 1.00 53.94  ? 269 MET A CG     1 
ATOM   2056  S SD     . MET A 1 269 ? 19.373  -7.010  25.314 1.00 61.60  ? 269 MET A SD     1 
ATOM   2057  C CE     . MET A 1 269 ? 18.478  -6.781  26.841 1.00 51.70  ? 269 MET A CE     1 
ATOM   2058  N N      . GLU A 1 270 ? 21.600  -10.748 29.355 1.00 57.38  ? 270 GLU A N      1 
ATOM   2059  C CA     . GLU A 1 270 ? 21.337  -11.888 30.203 1.00 54.96  ? 270 GLU A CA     1 
ATOM   2060  C C      . GLU A 1 270 ? 19.869  -11.813 30.431 1.00 62.37  ? 270 GLU A C      1 
ATOM   2061  O O      . GLU A 1 270 ? 19.351  -12.324 31.416 1.00 68.62  ? 270 GLU A O      1 
ATOM   2062  C CB     . GLU A 1 270 ? 22.034  -11.696 31.534 1.00 53.76  ? 270 GLU A CB     1 
ATOM   2063  C CG     . GLU A 1 270 ? 22.328  -12.972 32.302 1.00 68.08  ? 270 GLU A CG     1 
ATOM   2064  C CD     . GLU A 1 270 ? 22.835  -12.700 33.705 1.00 72.73  ? 270 GLU A CD     1 
ATOM   2065  O OE1    . GLU A 1 270 ? 22.765  -11.536 34.147 1.00 75.34  ? 270 GLU A OE1    1 
ATOM   2066  O OE2    . GLU A 1 270 ? 23.298  -13.647 34.369 1.00 75.17  ? 270 GLU A OE2    1 
ATOM   2067  N N      . SER A 1 271 ? 19.171  -11.170 29.515 1.00 58.53  ? 271 SER A N      1 
ATOM   2068  C CA     . SER A 1 271 ? 17.761  -10.963 29.737 1.00 58.74  ? 271 SER A CA     1 
ATOM   2069  C C      . SER A 1 271 ? 16.859  -12.040 29.257 1.00 47.72  ? 271 SER A C      1 
ATOM   2070  O O      . SER A 1 271 ? 17.212  -12.830 28.404 1.00 47.06  ? 271 SER A O      1 
ATOM   2071  C CB     . SER A 1 271 ? 17.331  -9.664  29.100 1.00 64.38  ? 271 SER A CB     1 
ATOM   2072  O OG     . SER A 1 271 ? 16.007  -9.341  29.473 1.00 78.18  ? 271 SER A OG     1 
ATOM   2073  N N      . CYS A 1 272 ? 15.641  -12.012 29.744 1.00 46.14  ? 272 CYS A N      1 
ATOM   2074  C CA     . CYS A 1 272 ? 14.680  -12.988 29.346 1.00 51.05  ? 272 CYS A CA     1 
ATOM   2075  C C      . CYS A 1 272 ? 14.095  -12.640 28.019 1.00 39.93  ? 272 CYS A C      1 
ATOM   2076  O O      . CYS A 1 272 ? 13.896  -11.484 27.708 1.00 41.16  ? 272 CYS A O      1 
ATOM   2077  C CB     . CYS A 1 272 ? 13.596  -13.062 30.395 1.00 56.35  ? 272 CYS A CB     1 
ATOM   2078  S SG     . CYS A 1 272 ? 14.198  -13.260 32.087 1.00 91.88  ? 272 CYS A SG     1 
ATOM   2079  N N      . GLY A 1 273 ? 13.821  -13.644 27.225 1.00 41.93  ? 273 GLY A N      1 
ATOM   2080  C CA     . GLY A 1 273 ? 13.352  -13.392 25.893 1.00 44.31  ? 273 GLY A CA     1 
ATOM   2081  C C      . GLY A 1 273 ? 11.928  -12.992 25.828 1.00 39.43  ? 273 GLY A C      1 
ATOM   2082  O O      . GLY A 1 273 ? 11.266  -12.849 26.832 1.00 43.03  ? 273 GLY A O      1 
ATOM   2083  N N      . ILE A 1 274 ? 11.435  -12.823 24.627 1.00 31.16  ? 274 ILE A N      1 
ATOM   2084  C CA     . ILE A 1 274 ? 10.099  -12.356 24.507 1.00 35.43  ? 274 ILE A CA     1 
ATOM   2085  C C      . ILE A 1 274 ? 9.112   -13.400 24.964 1.00 42.06  ? 274 ILE A C      1 
ATOM   2086  O O      . ILE A 1 274 ? 8.026   -13.050 25.399 1.00 44.41  ? 274 ILE A O      1 
ATOM   2087  C CB     . ILE A 1 274 ? 9.831   -11.821 23.106 1.00 40.66  ? 274 ILE A CB     1 
ATOM   2088  C CG1    . ILE A 1 274 ? 9.981   -12.898 22.051 1.00 44.63  ? 274 ILE A CG1    1 
ATOM   2089  C CG2    . ILE A 1 274 ? 10.793  -10.691 22.790 1.00 37.07  ? 274 ILE A CG2    1 
ATOM   2090  C CD1    . ILE A 1 274 ? 9.748   -12.362 20.660 1.00 37.46  ? 274 ILE A CD1    1 
ATOM   2091  N N      . HIS A 1 275 ? 9.480   -14.674 24.971 1.00 41.29  ? 275 HIS A N      1 
ATOM   2092  C CA     . HIS A 1 275 ? 8.556   -15.684 25.495 1.00 40.35  ? 275 HIS A CA     1 
ATOM   2093  C C      . HIS A 1 275 ? 8.462   -15.668 26.993 1.00 46.42  ? 275 HIS A C      1 
ATOM   2094  O O      . HIS A 1 275 ? 7.381   -15.742 27.552 1.00 45.50  ? 275 HIS A O      1 
ATOM   2095  C CB     . HIS A 1 275 ? 8.858   -17.081 24.981 1.00 36.06  ? 275 HIS A CB     1 
ATOM   2096  C CG     . HIS A 1 275 ? 10.272  -17.522 25.157 1.00 43.53  ? 275 HIS A CG     1 
ATOM   2097  N ND1    . HIS A 1 275 ? 11.318  -16.972 24.454 1.00 47.69  ? 275 HIS A ND1    1 
ATOM   2098  C CD2    . HIS A 1 275 ? 10.805  -18.505 25.916 1.00 46.74  ? 275 HIS A CD2    1 
ATOM   2099  C CE1    . HIS A 1 275 ? 12.440  -17.577 24.795 1.00 50.39  ? 275 HIS A CE1    1 
ATOM   2100  N NE2    . HIS A 1 275 ? 12.156  -18.510 25.682 1.00 54.20  ? 275 HIS A NE2    1 
ATOM   2101  N N      . GLU A 1 276 ? 9.585   -15.517 27.659 1.00 42.43  ? 276 GLU A N      1 
ATOM   2102  C CA     . GLU A 1 276 ? 9.601   -15.575 29.087 1.00 36.91  ? 276 GLU A CA     1 
ATOM   2103  C C      . GLU A 1 276 ? 9.069   -14.314 29.663 1.00 36.44  ? 276 GLU A C      1 
ATOM   2104  O O      . GLU A 1 276 ? 8.428   -14.333 30.683 1.00 38.23  ? 276 GLU A O      1 
ATOM   2105  C CB     . GLU A 1 276 ? 11.016  -15.812 29.542 1.00 46.18  ? 276 GLU A CB     1 
ATOM   2106  C CG     . GLU A 1 276 ? 11.539  -17.203 29.243 1.00 52.65  ? 276 GLU A CG     1 
ATOM   2107  C CD     . GLU A 1 276 ? 13.008  -17.214 28.880 1.00 53.71  ? 276 GLU A CD     1 
ATOM   2108  O OE1    . GLU A 1 276 ? 13.472  -16.253 28.242 1.00 46.69  ? 276 GLU A OE1    1 
ATOM   2109  O OE2    . GLU A 1 276 ? 13.698  -18.194 29.215 1.00 67.27  ? 276 GLU A OE2    1 
ATOM   2110  N N      . THR A 1 277 ? 9.322   -13.200 29.015 1.00 35.51  ? 277 THR A N      1 
ATOM   2111  C CA     . THR A 1 277 ? 8.798   -11.949 29.491 1.00 36.51  ? 277 THR A CA     1 
ATOM   2112  C C      . THR A 1 277 ? 7.285   -11.998 29.466 1.00 40.36  ? 277 THR A C      1 
ATOM   2113  O O      . THR A 1 277 ? 6.636   -11.504 30.367 1.00 40.60  ? 277 THR A O      1 
ATOM   2114  C CB     . THR A 1 277 ? 9.358   -10.782 28.686 1.00 37.78  ? 277 THR A CB     1 
ATOM   2115  O OG1    . THR A 1 277 ? 10.783  -10.890 28.639 1.00 38.51  ? 277 THR A OG1    1 
ATOM   2116  C CG2    . THR A 1 277 ? 9.013   -9.479  29.326 1.00 40.42  ? 277 THR A CG2    1 
ATOM   2117  N N      . THR A 1 278 ? 6.710   -12.640 28.463 1.00 44.30  ? 278 THR A N      1 
ATOM   2118  C CA     . THR A 1 278 ? 5.268   -12.743 28.357 1.00 41.72  ? 278 THR A CA     1 
ATOM   2119  C C      . THR A 1 278 ? 4.764   -13.592 29.489 1.00 41.34  ? 278 THR A C      1 
ATOM   2120  O O      . THR A 1 278 ? 3.791   -13.260 30.120 1.00 43.87  ? 278 THR A O      1 
ATOM   2121  C CB     . THR A 1 278 ? 4.845   -13.311 27.005 1.00 36.88  ? 278 THR A CB     1 
ATOM   2122  O OG1    . THR A 1 278 ? 5.248   -12.407 25.973 1.00 38.32  ? 278 THR A OG1    1 
ATOM   2123  C CG2    . THR A 1 278 ? 3.358   -13.486 26.932 1.00 36.72  ? 278 THR A CG2    1 
ATOM   2124  N N      . PHE A 1 279 ? 5.445   -14.674 29.791 1.00 38.21  ? 279 PHE A N      1 
ATOM   2125  C CA     . PHE A 1 279 ? 5.053   -15.510 30.910 1.00 38.71  ? 279 PHE A CA     1 
ATOM   2126  C C      . PHE A 1 279 ? 5.151   -14.741 32.192 1.00 38.68  ? 279 PHE A C      1 
ATOM   2127  O O      . PHE A 1 279 ? 4.246   -14.779 32.989 1.00 37.07  ? 279 PHE A O      1 
ATOM   2128  C CB     . PHE A 1 279 ? 5.956   -16.731 30.956 1.00 34.03  ? 279 PHE A CB     1 
ATOM   2129  C CG     . PHE A 1 279 ? 5.692   -17.681 32.080 1.00 32.12  ? 279 PHE A CG     1 
ATOM   2130  C CD1    . PHE A 1 279 ? 4.536   -18.423 32.119 1.00 38.15  ? 279 PHE A CD1    1 
ATOM   2131  C CD2    . PHE A 1 279 ? 6.647   -17.889 33.053 1.00 31.23  ? 279 PHE A CD2    1 
ATOM   2132  C CE1    . PHE A 1 279 ? 4.311   -19.321 33.139 1.00 43.34  ? 279 PHE A CE1    1 
ATOM   2133  C CE2    . PHE A 1 279 ? 6.433   -18.784 34.076 1.00 32.05  ? 279 PHE A CE2    1 
ATOM   2134  C CZ     . PHE A 1 279 ? 5.263   -19.506 34.118 1.00 35.41  ? 279 PHE A CZ     1 
ATOM   2135  N N      . ASN A 1 280 ? 6.234   -14.013 32.398 1.00 37.72  ? 280 ASN A N      1 
ATOM   2136  C CA     . ASN A 1 280 ? 6.440   -13.341 33.669 1.00 36.71  ? 280 ASN A CA     1 
ATOM   2137  C C      . ASN A 1 280 ? 5.390   -12.332 33.976 1.00 36.24  ? 280 ASN A C      1 
ATOM   2138  O O      . ASN A 1 280 ? 4.958   -12.234 35.102 1.00 37.62  ? 280 ASN A O      1 
ATOM   2139  C CB     . ASN A 1 280 ? 7.798   -12.690 33.697 1.00 33.34  ? 280 ASN A CB     1 
ATOM   2140  C CG     . ASN A 1 280 ? 8.926   -13.693 33.619 1.00 38.78  ? 280 ASN A CG     1 
ATOM   2141  O OD1    . ASN A 1 280 ? 8.759   -14.860 33.957 1.00 41.90  ? 280 ASN A OD1    1 
ATOM   2142  N ND2    . ASN A 1 280 ? 10.087  -13.239 33.174 1.00 40.23  ? 280 ASN A ND2    1 
ATOM   2143  N N      . SER A 1 281 ? 4.974   -11.563 32.991 1.00 36.88  ? 281 SER A N      1 
ATOM   2144  C CA     . SER A 1 281 ? 3.925   -10.592 33.201 1.00 35.11  ? 281 SER A CA     1 
ATOM   2145  C C      . SER A 1 281 ? 2.656   -11.297 33.481 1.00 37.69  ? 281 SER A C      1 
ATOM   2146  O O      . SER A 1 281 ? 1.892   -10.880 34.324 1.00 37.40  ? 281 SER A O      1 
ATOM   2147  C CB     . SER A 1 281 ? 3.734   -9.763  31.976 1.00 39.77  ? 281 SER A CB     1 
ATOM   2148  O OG     . SER A 1 281 ? 3.575   -10.588 30.851 1.00 49.07  ? 281 SER A OG     1 
ATOM   2149  N N      . ILE A 1 282 ? 2.427   -12.405 32.797 1.00 39.82  ? 282 ILE A N      1 
ATOM   2150  C CA     . ILE A 1 282 ? 1.207   -13.170 32.989 1.00 39.74  ? 282 ILE A CA     1 
ATOM   2151  C C      . ILE A 1 282 ? 1.278   -13.825 34.336 1.00 41.74  ? 282 ILE A C      1 
ATOM   2152  O O      . ILE A 1 282 ? 0.265   -14.038 34.963 1.00 47.53  ? 282 ILE A O      1 
ATOM   2153  C CB     . ILE A 1 282 ? 0.957   -14.166 31.852 1.00 37.60  ? 282 ILE A CB     1 
ATOM   2154  C CG1    . ILE A 1 282 ? 0.716   -13.417 30.554 1.00 39.81  ? 282 ILE A CG1    1 
ATOM   2155  C CG2    . ILE A 1 282 ? -0.278  -14.998 32.111 1.00 38.76  ? 282 ILE A CG2    1 
ATOM   2156  C CD1    . ILE A 1 282 ? 0.568   -14.324 29.360 1.00 43.25  ? 282 ILE A CD1    1 
ATOM   2157  N N      . MET A 1 283 ? 2.472   -14.094 34.837 1.00 40.96  ? 283 MET A N      1 
ATOM   2158  C CA     . MET A 1 283 ? 2.592   -14.638 36.189 1.00 41.66  ? 283 MET A CA     1 
ATOM   2159  C C      . MET A 1 283 ? 2.730   -13.581 37.268 1.00 33.51  ? 283 MET A C      1 
ATOM   2160  O O      . MET A 1 283 ? 3.011   -13.894 38.409 1.00 30.10  ? 283 MET A O      1 
ATOM   2161  C CB     . MET A 1 283 ? 3.716   -15.643 36.272 1.00 36.55  ? 283 MET A CB     1 
ATOM   2162  C CG     . MET A 1 283 ? 3.465   -16.871 35.446 1.00 39.78  ? 283 MET A CG     1 
ATOM   2163  S SD     . MET A 1 283 ? 2.466   -18.071 36.321 1.00 63.83  ? 283 MET A SD     1 
ATOM   2164  C CE     . MET A 1 283 ? 3.538   -18.418 37.708 1.00 43.61  ? 283 MET A CE     1 
ATOM   2165  N N      . LYS A 1 284 ? 2.629   -12.321 36.916 1.00 33.46  ? 284 LYS A N      1 
ATOM   2166  C CA     . LYS A 1 284 ? 2.666   -11.291 37.921 1.00 35.27  ? 284 LYS A CA     1 
ATOM   2167  C C      . LYS A 1 284 ? 1.283   -10.761 37.899 1.00 38.63  ? 284 LYS A C      1 
ATOM   2168  O O      . LYS A 1 284 ? 1.059   -9.593  38.145 1.00 41.46  ? 284 LYS A O      1 
ATOM   2169  C CB     . LYS A 1 284 ? 3.675   -10.202 37.619 1.00 26.56  ? 284 LYS A CB     1 
ATOM   2170  C CG     . LYS A 1 284 ? 5.091   -10.553 38.001 1.00 26.59  ? 284 LYS A CG     1 
ATOM   2171  C CD     . LYS A 1 284 ? 5.936   -9.305  38.120 1.00 24.33  ? 284 LYS A CD     1 
ATOM   2172  C CE     . LYS A 1 284 ? 6.124   -8.632  36.779 1.00 27.43  ? 284 LYS A CE     1 
ATOM   2173  N NZ     . LYS A 1 284 ? 7.066   -7.489  36.895 1.00 26.39  ? 284 LYS A NZ     1 
ATOM   2174  N N      . CYS A 1 285 ? 0.336   -11.633 37.607 1.00 36.98  ? 285 CYS A N      1 
ATOM   2175  C CA     . CYS A 1 285 ? -1.050  -11.246 37.552 1.00 38.66  ? 285 CYS A CA     1 
ATOM   2176  C C      . CYS A 1 285 ? -1.914  -12.232 38.309 1.00 38.75  ? 285 CYS A C      1 
ATOM   2177  O O      . CYS A 1 285 ? -1.509  -13.354 38.543 1.00 40.31  ? 285 CYS A O      1 
ATOM   2178  C CB     . CYS A 1 285 ? -1.497  -11.146 36.113 1.00 35.47  ? 285 CYS A CB     1 
ATOM   2179  S SG     . CYS A 1 285 ? -1.097  -9.607  35.286 1.00 52.58  ? 285 CYS A SG     1 
ATOM   2180  N N      . ASP A 1 286 ? -3.099  -11.815 38.700 1.00 39.79  ? 286 ASP A N      1 
ATOM   2181  C CA     . ASP A 1 286 ? -3.989  -12.648 39.462 1.00 44.20  ? 286 ASP A CA     1 
ATOM   2182  C C      . ASP A 1 286 ? -4.325  -13.802 38.647 1.00 49.52  ? 286 ASP A C      1 
ATOM   2183  O O      . ASP A 1 286 ? -4.603  -13.663 37.491 1.00 49.18  ? 286 ASP A O      1 
ATOM   2184  C CB     . ASP A 1 286 ? -5.256  -11.889 39.738 1.00 50.13  ? 286 ASP A CB     1 
ATOM   2185  C CG     . ASP A 1 286 ? -5.985  -12.374 40.954 1.00 69.58  ? 286 ASP A CG     1 
ATOM   2186  O OD1    . ASP A 1 286 ? -6.982  -11.722 41.323 1.00 79.67  ? 286 ASP A OD1    1 
ATOM   2187  O OD2    . ASP A 1 286 ? -5.571  -13.388 41.547 1.00 68.20  ? 286 ASP A OD2    1 
ATOM   2188  N N      . VAL A 1 287 ? -4.420  -14.957 39.255 1.00 51.26  ? 287 VAL A N      1 
ATOM   2189  C CA     . VAL A 1 287 ? -4.603  -16.168 38.512 1.00 43.64  ? 287 VAL A CA     1 
ATOM   2190  C C      . VAL A 1 287 ? -5.853  -16.131 37.714 1.00 47.59  ? 287 VAL A C      1 
ATOM   2191  O O      . VAL A 1 287 ? -5.894  -16.634 36.610 1.00 49.54  ? 287 VAL A O      1 
ATOM   2192  C CB     . VAL A 1 287 ? -4.622  -17.339 39.475 1.00 41.06  ? 287 VAL A CB     1 
ATOM   2193  C CG1    . VAL A 1 287 ? -4.095  -18.584 38.793 1.00 36.58  ? 287 VAL A CG1    1 
ATOM   2194  C CG2    . VAL A 1 287 ? -3.773  -17.015 40.688 1.00 48.79  ? 287 VAL A CG2    1 
ATOM   2195  N N      . ASP A 1 288 ? -6.878  -15.509 38.244 1.00 48.46  ? 288 ASP A N      1 
ATOM   2196  C CA     . ASP A 1 288 ? -8.153  -15.519 37.598 1.00 45.07  ? 288 ASP A CA     1 
ATOM   2197  C C      . ASP A 1 288 ? -8.091  -14.904 36.242 1.00 45.65  ? 288 ASP A C      1 
ATOM   2198  O O      . ASP A 1 288 ? -8.784  -15.342 35.346 1.00 54.56  ? 288 ASP A O      1 
ATOM   2199  C CB     . ASP A 1 288 ? -9.117  -14.771 38.479 1.00 50.18  ? 288 ASP A CB     1 
ATOM   2200  C CG     . ASP A 1 288 ? -8.836  -14.976 39.944 1.00 55.57  ? 288 ASP A CG     1 
ATOM   2201  O OD1    . ASP A 1 288 ? -8.503  -16.108 40.342 1.00 49.35  ? 288 ASP A OD1    1 
ATOM   2202  O OD2    . ASP A 1 288 ? -8.960  -14.002 40.707 1.00 60.90  ? 288 ASP A OD2    1 
ATOM   2203  N N      . ILE A 1 289 ? -7.301  -13.860 36.089 1.00 41.76  ? 289 ILE A N      1 
ATOM   2204  C CA     . ILE A 1 289 ? -7.217  -13.168 34.825 1.00 42.36  ? 289 ILE A CA     1 
ATOM   2205  C C      . ILE A 1 289 ? -6.230  -13.749 33.856 1.00 42.34  ? 289 ILE A C      1 
ATOM   2206  O O      . ILE A 1 289 ? -6.300  -13.435 32.695 1.00 44.46  ? 289 ILE A O      1 
ATOM   2207  C CB     . ILE A 1 289 ? -6.919  -11.676 35.009 1.00 42.52  ? 289 ILE A CB     1 
ATOM   2208  C CG1    . ILE A 1 289 ? -5.457  -11.416 35.312 1.00 39.67  ? 289 ILE A CG1    1 
ATOM   2209  C CG2    . ILE A 1 289 ? -7.786  -11.093 36.108 1.00 45.14  ? 289 ILE A CG2    1 
ATOM   2210  C CD1    . ILE A 1 289 ? -5.172  -9.952  35.522 1.00 36.99  ? 289 ILE A CD1    1 
ATOM   2211  N N      . ARG A 1 290 ? -5.343  -14.628 34.294 1.00 38.86  ? 290 ARG A N      1 
ATOM   2212  C CA     . ARG A 1 290 ? -4.300  -15.172 33.434 1.00 34.84  ? 290 ARG A CA     1 
ATOM   2213  C C      . ARG A 1 290 ? -4.817  -15.981 32.300 1.00 40.55  ? 290 ARG A C      1 
ATOM   2214  O O      . ARG A 1 290 ? -4.254  -15.999 31.230 1.00 44.98  ? 290 ARG A O      1 
ATOM   2215  C CB     . ARG A 1 290 ? -3.398  -16.059 34.222 1.00 33.66  ? 290 ARG A CB     1 
ATOM   2216  C CG     . ARG A 1 290 ? -2.602  -15.370 35.302 1.00 39.58  ? 290 ARG A CG     1 
ATOM   2217  C CD     . ARG A 1 290 ? -1.727  -16.382 36.013 1.00 37.85  ? 290 ARG A CD     1 
ATOM   2218  N NE     . ARG A 1 290 ? -1.167  -15.842 37.239 1.00 38.61  ? 290 ARG A NE     1 
ATOM   2219  C CZ     . ARG A 1 290 ? -0.515  -16.567 38.132 1.00 40.64  ? 290 ARG A CZ     1 
ATOM   2220  N NH1    . ARG A 1 290 ? -0.346  -17.860 37.932 1.00 43.95  ? 290 ARG A NH1    1 
ATOM   2221  N NH2    . ARG A 1 290 ? -0.040  -16.001 39.226 1.00 42.15  ? 290 ARG A NH2    1 
ATOM   2222  N N      . LYS A 1 291 ? -5.852  -16.722 32.550 1.00 41.97  ? 291 LYS A N      1 
ATOM   2223  C CA     . LYS A 1 291 ? -6.427  -17.511 31.527 1.00 46.40  ? 291 LYS A CA     1 
ATOM   2224  C C      . LYS A 1 291 ? -6.796  -16.657 30.366 1.00 42.03  ? 291 LYS A C      1 
ATOM   2225  O O      . LYS A 1 291 ? -6.492  -16.989 29.240 1.00 44.97  ? 291 LYS A O      1 
ATOM   2226  C CB     . LYS A 1 291 ? -7.663  -18.157 32.109 1.00 49.00  ? 291 LYS A CB     1 
ATOM   2227  C CG     . LYS A 1 291 ? -8.596  -18.806 31.104 1.00 57.50  ? 291 LYS A CG     1 
ATOM   2228  C CD     . LYS A 1 291 ? -9.821  -19.371 31.800 1.00 63.23  ? 291 LYS A CD     1 
ATOM   2229  C CE     . LYS A 1 291 ? -10.913 -19.728 30.809 1.00 51.14  ? 291 LYS A CE     1 
ATOM   2230  N NZ     . LYS A 1 291 ? -11.485 -18.518 30.164 1.00 39.33  ? 291 LYS A NZ     1 
ATOM   2231  N N      . ASP A 1 292 ? -7.437  -15.542 30.615 1.00 37.85  ? 292 ASP A N      1 
ATOM   2232  C CA     . ASP A 1 292 ? -7.935  -14.718 29.542 1.00 41.29  ? 292 ASP A CA     1 
ATOM   2233  C C      . ASP A 1 292 ? -6.804  -14.015 28.828 1.00 41.31  ? 292 ASP A C      1 
ATOM   2234  O O      . ASP A 1 292 ? -6.926  -13.670 27.670 1.00 41.95  ? 292 ASP A O      1 
ATOM   2235  C CB     . ASP A 1 292 ? -8.938  -13.713 30.102 1.00 44.66  ? 292 ASP A CB     1 
ATOM   2236  C CG     . ASP A 1 292 ? -10.098 -14.366 30.812 1.00 49.03  ? 292 ASP A CG     1 
ATOM   2237  O OD1    . ASP A 1 292 ? -10.157 -15.605 30.869 1.00 51.23  ? 292 ASP A OD1    1 
ATOM   2238  O OD2    . ASP A 1 292 ? -10.963 -13.628 31.319 1.00 53.75  ? 292 ASP A OD2    1 
ATOM   2239  N N      . LEU A 1 293 ? -5.706  -13.799 29.516 1.00 37.49  ? 293 LEU A N      1 
ATOM   2240  C CA     . LEU A 1 293 ? -4.570  -13.134 28.937 1.00 33.09  ? 293 LEU A CA     1 
ATOM   2241  C C      . LEU A 1 293 ? -3.790  -14.047 28.059 1.00 36.11  ? 293 LEU A C      1 
ATOM   2242  O O      . LEU A 1 293 ? -3.180  -13.605 27.114 1.00 32.61  ? 293 LEU A O      1 
ATOM   2243  C CB     . LEU A 1 293 ? -3.663  -12.626 30.043 1.00 33.17  ? 293 LEU A CB     1 
ATOM   2244  C CG     . LEU A 1 293 ? -3.724  -11.208 30.599 1.00 37.23  ? 293 LEU A CG     1 
ATOM   2245  C CD1    . LEU A 1 293 ? -5.104  -10.832 31.100 1.00 39.84  ? 293 LEU A CD1    1 
ATOM   2246  C CD2    . LEU A 1 293 ? -2.700  -11.077 31.708 1.00 35.18  ? 293 LEU A CD2    1 
ATOM   2247  N N      . TYR A 1 294 ? -3.819  -15.341 28.341 1.00 39.08  ? 294 TYR A N      1 
ATOM   2248  C CA     . TYR A 1 294 ? -3.077  -16.319 27.546 1.00 38.64  ? 294 TYR A CA     1 
ATOM   2249  C C      . TYR A 1 294 ? -3.752  -16.507 26.219 1.00 42.53  ? 294 TYR A C      1 
ATOM   2250  O O      . TYR A 1 294 ? -3.132  -16.895 25.251 1.00 42.53  ? 294 TYR A O      1 
ATOM   2251  C CB     . TYR A 1 294 ? -3.005  -17.660 28.244 1.00 33.75  ? 294 TYR A CB     1 
ATOM   2252  C CG     . TYR A 1 294 ? -1.807  -17.891 29.115 1.00 37.84  ? 294 TYR A CG     1 
ATOM   2253  C CD1    . TYR A 1 294 ? -0.527  -17.796 28.606 1.00 39.57  ? 294 TYR A CD1    1 
ATOM   2254  C CD2    . TYR A 1 294 ? -1.958  -18.253 30.438 1.00 40.11  ? 294 TYR A CD2    1 
ATOM   2255  C CE1    . TYR A 1 294 ? 0.573   -18.024 29.405 1.00 44.15  ? 294 TYR A CE1    1 
ATOM   2256  C CE2    . TYR A 1 294 ? -0.868  -18.489 31.242 1.00 41.56  ? 294 TYR A CE2    1 
ATOM   2257  C CZ     . TYR A 1 294 ? 0.392   -18.370 30.720 1.00 43.26  ? 294 TYR A CZ     1 
ATOM   2258  O OH     . TYR A 1 294 ? 1.472   -18.602 31.521 1.00 38.90  ? 294 TYR A OH     1 
ATOM   2259  N N      . ALA A 1 295 ? -5.032  -16.206 26.155 1.00 39.52  ? 295 ALA A N      1 
ATOM   2260  C CA     . ALA A 1 295 ? -5.765  -16.383 24.933 1.00 38.75  ? 295 ALA A CA     1 
ATOM   2261  C C      . ALA A 1 295 ? -6.043  -15.095 24.249 1.00 43.31  ? 295 ALA A C      1 
ATOM   2262  O O      . ALA A 1 295 ? -6.817  -15.079 23.314 1.00 56.20  ? 295 ALA A O      1 
ATOM   2263  C CB     . ALA A 1 295 ? -7.055  -17.084 25.204 1.00 46.11  ? 295 ALA A CB     1 
ATOM   2264  N N      . ASN A 1 296 ? -5.462  -13.999 24.699 1.00 34.52  ? 296 ASN A N      1 
ATOM   2265  C CA     . ASN A 1 296 ? -5.621  -12.754 23.998 1.00 33.78  ? 296 ASN A CA     1 
ATOM   2266  C C      . ASN A 1 296 ? -4.278  -12.091 23.918 1.00 32.93  ? 296 ASN A C      1 
ATOM   2267  O O      . ASN A 1 296 ? -4.129  -10.945 24.268 1.00 34.54  ? 296 ASN A O      1 
ATOM   2268  C CB     . ASN A 1 296 ? -6.622  -11.885 24.703 1.00 31.44  ? 296 ASN A CB     1 
ATOM   2269  C CG     . ASN A 1 296 ? -8.030  -12.418 24.620 1.00 35.77  ? 296 ASN A CG     1 
ATOM   2270  O OD1    . ASN A 1 296 ? -8.543  -12.682 23.538 1.00 38.88  ? 296 ASN A OD1    1 
ATOM   2271  N ND2    . ASN A 1 296 ? -8.672  -12.558 25.767 1.00 38.85  ? 296 ASN A ND2    1 
ATOM   2272  N N      . THR A 1 297 ? -3.287  -12.813 23.430 1.00 32.06  ? 297 THR A N      1 
ATOM   2273  C CA     . THR A 1 297 ? -1.937  -12.289 23.322 1.00 36.26  ? 297 THR A CA     1 
ATOM   2274  C C      . THR A 1 297 ? -1.704  -11.592 22.008 1.00 40.96  ? 297 THR A C      1 
ATOM   2275  O O      . THR A 1 297 ? -1.138  -12.165 21.098 1.00 43.13  ? 297 THR A O      1 
ATOM   2276  C CB     . THR A 1 297 ? -0.888  -13.402 23.464 1.00 37.60  ? 297 THR A CB     1 
ATOM   2277  O OG1    . THR A 1 297 ? -1.253  -14.275 24.537 1.00 34.60  ? 297 THR A OG1    1 
ATOM   2278  C CG2    . THR A 1 297 ? 0.493   -12.822 23.736 1.00 33.49  ? 297 THR A CG2    1 
ATOM   2279  N N      . VAL A 1 298 ? -2.115  -10.336 21.896 1.00 37.85  ? 298 VAL A N      1 
ATOM   2280  C CA     . VAL A 1 298 ? -1.964  -9.581  20.657 1.00 32.33  ? 298 VAL A CA     1 
ATOM   2281  C C      . VAL A 1 298 ? -0.565  -9.067  20.509 1.00 33.74  ? 298 VAL A C      1 
ATOM   2282  O O      . VAL A 1 298 ? 0.021   -8.648  21.461 1.00 36.66  ? 298 VAL A O      1 
ATOM   2283  C CB     . VAL A 1 298 ? -2.961  -8.435  20.603 1.00 32.39  ? 298 VAL A CB     1 
ATOM   2284  C CG1    . VAL A 1 298 ? -2.874  -7.690  19.289 1.00 38.79  ? 298 VAL A CG1    1 
ATOM   2285  C CG2    . VAL A 1 298 ? -4.359  -8.976  20.795 1.00 33.48  ? 298 VAL A CG2    1 
ATOM   2286  N N      . LEU A 1 299 ? -0.006  -9.130  19.322 1.00 36.86  ? 299 LEU A N      1 
ATOM   2287  C CA     . LEU A 1 299 ? 1.339   -8.633  19.070 1.00 38.42  ? 299 LEU A CA     1 
ATOM   2288  C C      . LEU A 1 299 ? 1.282   -7.323  18.301 1.00 40.08  ? 299 LEU A C      1 
ATOM   2289  O O      . LEU A 1 299 ? 0.670   -7.250  17.250 1.00 42.90  ? 299 LEU A O      1 
ATOM   2290  C CB     . LEU A 1 299 ? 2.160   -9.663  18.291 1.00 35.31  ? 299 LEU A CB     1 
ATOM   2291  C CG     . LEU A 1 299 ? 2.717   -10.910 18.967 1.00 36.70  ? 299 LEU A CG     1 
ATOM   2292  C CD1    . LEU A 1 299 ? 1.587   -11.832 19.371 1.00 36.91  ? 299 LEU A CD1    1 
ATOM   2293  C CD2    . LEU A 1 299 ? 3.658   -11.627 18.020 1.00 30.16  ? 299 LEU A CD2    1 
ATOM   2294  N N      . SER A 1 300 ? 1.905   -6.287  18.830 1.00 36.17  ? 300 SER A N      1 
ATOM   2295  C CA     . SER A 1 300 ? 1.900   -4.996  18.179 1.00 39.81  ? 300 SER A CA     1 
ATOM   2296  C C      . SER A 1 300 ? 3.284   -4.594  17.934 1.00 37.69  ? 300 SER A C      1 
ATOM   2297  O O      . SER A 1 300 ? 4.081   -4.595  18.833 1.00 41.91  ? 300 SER A O      1 
ATOM   2298  C CB     . SER A 1 300 ? 1.338   -3.945  19.100 1.00 44.59  ? 300 SER A CB     1 
ATOM   2299  O OG     . SER A 1 300 ? 1.671   -2.647  18.653 1.00 48.09  ? 300 SER A OG     1 
ATOM   2300  N N      . GLY A 1 301 ? 3.600   -4.222  16.720 1.00 26.64  ? 301 GLY A N      1 
ATOM   2301  C CA     . GLY A 1 301 ? 4.916   -3.722  16.498 1.00 31.56  ? 301 GLY A CA     1 
ATOM   2302  C C      . GLY A 1 301 ? 5.469   -3.954  15.151 1.00 34.83  ? 301 GLY A C      1 
ATOM   2303  O O      . GLY A 1 301 ? 4.896   -4.655  14.358 1.00 43.36  ? 301 GLY A O      1 
ATOM   2304  N N      . GLY A 1 302 ? 6.613   -3.371  14.897 1.00 34.80  ? 302 GLY A N      1 
ATOM   2305  C CA     . GLY A 1 302 ? 7.238   -3.525  13.628 1.00 35.18  ? 302 GLY A CA     1 
ATOM   2306  C C      . GLY A 1 302 ? 8.299   -4.565  13.731 1.00 49.19  ? 302 GLY A C      1 
ATOM   2307  O O      . GLY A 1 302 ? 8.745   -5.049  12.716 1.00 54.85  ? 302 GLY A O      1 
ATOM   2308  N N      . THR A 1 303 ? 8.728   -4.915  14.932 1.00 49.04  ? 303 THR A N      1 
ATOM   2309  C CA     . THR A 1 303 ? 9.701   -5.980  15.086 1.00 47.29  ? 303 THR A CA     1 
ATOM   2310  C C      . THR A 1 303 ? 8.961   -7.283  15.229 1.00 41.14  ? 303 THR A C      1 
ATOM   2311  O O      . THR A 1 303 ? 9.557   -8.344  15.266 1.00 43.55  ? 303 THR A O      1 
ATOM   2312  C CB     . THR A 1 303 ? 10.602  -5.741  16.294 1.00 41.34  ? 303 THR A CB     1 
ATOM   2313  O OG1    . THR A 1 303 ? 10.965  -4.359  16.338 1.00 42.30  ? 303 THR A OG1    1 
ATOM   2314  C CG2    . THR A 1 303 ? 11.858  -6.573  16.204 1.00 41.30  ? 303 THR A CG2    1 
ATOM   2315  N N      . THR A 1 304 ? 7.649   -7.203  15.306 1.00 35.44  ? 304 THR A N      1 
ATOM   2316  C CA     . THR A 1 304 ? 6.852   -8.382  15.471 1.00 36.08  ? 304 THR A CA     1 
ATOM   2317  C C      . THR A 1 304 ? 6.260   -8.639  14.155 1.00 41.74  ? 304 THR A C      1 
ATOM   2318  O O      . THR A 1 304 ? 5.289   -9.352  14.053 1.00 43.14  ? 304 THR A O      1 
ATOM   2319  C CB     . THR A 1 304 ? 5.704   -8.140  16.431 1.00 37.95  ? 304 THR A CB     1 
ATOM   2320  O OG1    . THR A 1 304 ? 4.905   -7.060  15.954 1.00 49.52  ? 304 THR A OG1    1 
ATOM   2321  C CG2    . THR A 1 304 ? 6.224   -7.790  17.795 1.00 38.75  ? 304 THR A CG2    1 
ATOM   2322  N N      . MET A 1 305 ? 6.842   -8.050  13.127 1.00 42.72  ? 305 MET A N      1 
ATOM   2323  C CA     . MET A 1 305 ? 6.305   -8.197  11.788 1.00 43.45  ? 305 MET A CA     1 
ATOM   2324  C C      . MET A 1 305 ? 7.148   -9.184  11.035 1.00 45.12  ? 305 MET A C      1 
ATOM   2325  O O      . MET A 1 305 ? 6.975   -9.380  9.849  1.00 44.36  ? 305 MET A O      1 
ATOM   2326  C CB     . MET A 1 305 ? 6.263   -6.859  11.078 1.00 38.28  ? 305 MET A CB     1 
ATOM   2327  C CG     . MET A 1 305 ? 4.958   -6.104  11.194 1.00 40.86  ? 305 MET A CG     1 
ATOM   2328  S SD     . MET A 1 305 ? 3.881   -6.491  9.810  1.00 56.60  ? 305 MET A SD     1 
ATOM   2329  C CE     . MET A 1 305 ? 2.844   -5.039  9.764  1.00 51.06  ? 305 MET A CE     1 
ATOM   2330  N N      . TYR A 1 306 ? 8.080   -9.806  11.723 1.00 46.56  ? 306 TYR A N      1 
ATOM   2331  C CA     . TYR A 1 306 ? 8.900   -10.802 11.103 1.00 37.91  ? 306 TYR A CA     1 
ATOM   2332  C C      . TYR A 1 306 ? 7.961   -11.923 10.819 1.00 38.86  ? 306 TYR A C      1 
ATOM   2333  O O      . TYR A 1 306 ? 7.034   -12.154 11.568 1.00 39.78  ? 306 TYR A O      1 
ATOM   2334  C CB     . TYR A 1 306 ? 9.983   -11.255 12.060 1.00 38.86  ? 306 TYR A CB     1 
ATOM   2335  C CG     . TYR A 1 306 ? 11.091  -10.270 12.241 1.00 42.84  ? 306 TYR A CG     1 
ATOM   2336  C CD1    . TYR A 1 306 ? 11.838  -9.838  11.165 1.00 51.07  ? 306 TYR A CD1    1 
ATOM   2337  C CD2    . TYR A 1 306 ? 11.404  -9.788  13.489 1.00 37.70  ? 306 TYR A CD2    1 
ATOM   2338  C CE1    . TYR A 1 306 ? 12.861  -8.934  11.330 1.00 61.31  ? 306 TYR A CE1    1 
ATOM   2339  C CE2    . TYR A 1 306 ? 12.422  -8.882  13.666 1.00 47.41  ? 306 TYR A CE2    1 
ATOM   2340  C CZ     . TYR A 1 306 ? 13.148  -8.462  12.584 1.00 55.30  ? 306 TYR A CZ     1 
ATOM   2341  O OH     . TYR A 1 306 ? 14.164  -7.563  12.767 1.00 52.07  ? 306 TYR A OH     1 
ATOM   2342  N N      . PRO A 1 307 ? 8.179   -12.639 9.721  1.00 40.47  ? 307 PRO A N      1 
ATOM   2343  C CA     . PRO A 1 307 ? 7.337   -13.790 9.474  1.00 29.37  ? 307 PRO A CA     1 
ATOM   2344  C C      . PRO A 1 307 ? 7.633   -14.880 10.447 1.00 28.72  ? 307 PRO A C      1 
ATOM   2345  O O      . PRO A 1 307 ? 8.780   -15.139 10.702 1.00 30.40  ? 307 PRO A O      1 
ATOM   2346  C CB     . PRO A 1 307 ? 7.790   -14.236 8.101  1.00 24.82  ? 307 PRO A CB     1 
ATOM   2347  C CG     . PRO A 1 307 ? 8.333   -13.024 7.452  1.00 36.20  ? 307 PRO A CG     1 
ATOM   2348  C CD     . PRO A 1 307 ? 9.047   -12.346 8.569  1.00 47.74  ? 307 PRO A CD     1 
ATOM   2349  N N      . GLY A 1 308 ? 6.639   -15.511 11.023 1.00 28.64  ? 308 GLY A N      1 
ATOM   2350  C CA     . GLY A 1 308 ? 6.907   -16.659 11.862 1.00 33.16  ? 308 GLY A CA     1 
ATOM   2351  C C      . GLY A 1 308 ? 6.964   -16.477 13.347 1.00 40.88  ? 308 GLY A C      1 
ATOM   2352  O O      . GLY A 1 308 ? 7.040   -17.440 14.095 1.00 36.06  ? 308 GLY A O      1 
ATOM   2353  N N      . ILE A 1 309 ? 6.936   -15.241 13.791 1.00 42.41  ? 309 ILE A N      1 
ATOM   2354  C CA     . ILE A 1 309 ? 7.062   -14.986 15.189 1.00 39.71  ? 309 ILE A CA     1 
ATOM   2355  C C      . ILE A 1 309 ? 5.831   -15.538 15.789 1.00 45.21  ? 309 ILE A C      1 
ATOM   2356  O O      . ILE A 1 309 ? 5.862   -16.087 16.872 1.00 45.09  ? 309 ILE A O      1 
ATOM   2357  C CB     . ILE A 1 309 ? 7.212   -13.476 15.472 1.00 33.65  ? 309 ILE A CB     1 
ATOM   2358  C CG1    . ILE A 1 309 ? 7.388   -13.209 16.963 1.00 45.38  ? 309 ILE A CG1    1 
ATOM   2359  C CG2    . ILE A 1 309 ? 6.056   -12.668 14.911 1.00 30.87  ? 309 ILE A CG2    1 
ATOM   2360  C CD1    . ILE A 1 309 ? 7.739   -11.776 17.277 1.00 46.71  ? 309 ILE A CD1    1 
ATOM   2361  N N      . ALA A 1 310 ? 4.737   -15.478 15.065 1.00 40.97  ? 310 ALA A N      1 
ATOM   2362  C CA     . ALA A 1 310 ? 3.474   -15.888 15.640 1.00 39.08  ? 310 ALA A CA     1 
ATOM   2363  C C      . ALA A 1 310 ? 3.470   -17.316 16.103 1.00 45.33  ? 310 ALA A C      1 
ATOM   2364  O O      . ALA A 1 310 ? 3.183   -17.593 17.253 1.00 51.77  ? 310 ALA A O      1 
ATOM   2365  C CB     . ALA A 1 310 ? 2.372   -15.644 14.652 1.00 32.49  ? 310 ALA A CB     1 
ATOM   2366  N N      . ASP A 1 311 ? 3.820   -18.237 15.227 1.00 50.54  ? 311 ASP A N      1 
ATOM   2367  C CA     . ASP A 1 311 ? 3.776   -19.644 15.570 1.00 46.75  ? 311 ASP A CA     1 
ATOM   2368  C C      . ASP A 1 311 ? 4.802   -20.048 16.598 1.00 46.29  ? 311 ASP A C      1 
ATOM   2369  O O      . ASP A 1 311 ? 4.531   -20.890 17.427 1.00 47.11  ? 311 ASP A O      1 
ATOM   2370  C CB     . ASP A 1 311 ? 3.951   -20.485 14.319 1.00 52.97  ? 311 ASP A CB     1 
ATOM   2371  C CG     . ASP A 1 311 ? 2.831   -20.291 13.319 1.00 66.00  ? 311 ASP A CG     1 
ATOM   2372  O OD1    . ASP A 1 311 ? 1.852   -19.591 13.636 1.00 67.30  ? 311 ASP A OD1    1 
ATOM   2373  O OD2    . ASP A 1 311 ? 2.925   -20.850 12.209 1.00 72.19  ? 311 ASP A OD2    1 
ATOM   2374  N N      . ARG A 1 312 ? 5.972   -19.442 16.563 1.00 45.19  ? 312 ARG A N      1 
ATOM   2375  C CA     . ARG A 1 312 ? 7.009   -19.800 17.501 1.00 41.54  ? 312 ARG A CA     1 
ATOM   2376  C C      . ARG A 1 312 ? 6.612   -19.363 18.846 1.00 44.16  ? 312 ARG A C      1 
ATOM   2377  O O      . ARG A 1 312 ? 6.860   -20.032 19.825 1.00 42.59  ? 312 ARG A O      1 
ATOM   2378  C CB     . ARG A 1 312 ? 8.323   -19.141 17.177 1.00 37.43  ? 312 ARG A CB     1 
ATOM   2379  C CG     . ARG A 1 312 ? 9.423   -19.593 18.108 1.00 36.97  ? 312 ARG A CG     1 
ATOM   2380  C CD     . ARG A 1 312 ? 10.781  -19.402 17.494 1.00 36.49  ? 312 ARG A CD     1 
ATOM   2381  N NE     . ARG A 1 312 ? 11.816  -19.945 18.351 1.00 32.12  ? 312 ARG A NE     1 
ATOM   2382  C CZ     . ARG A 1 312 ? 13.099  -19.945 18.033 1.00 40.68  ? 312 ARG A CZ     1 
ATOM   2383  N NH1    . ARG A 1 312 ? 13.485  -19.437 16.878 1.00 46.09  ? 312 ARG A NH1    1 
ATOM   2384  N NH2    . ARG A 1 312 ? 13.990  -20.454 18.867 1.00 44.01  ? 312 ARG A NH2    1 
ATOM   2385  N N      . MET A 1 313 ? 5.978   -18.218 18.917 1.00 45.40  ? 313 MET A N      1 
ATOM   2386  C CA     . MET A 1 313 ? 5.656   -17.700 20.212 1.00 42.28  ? 313 MET A CA     1 
ATOM   2387  C C      . MET A 1 313 ? 4.808   -18.731 20.882 1.00 42.86  ? 313 MET A C      1 
ATOM   2388  O O      . MET A 1 313 ? 5.022   -19.065 22.017 1.00 50.68  ? 313 MET A O      1 
ATOM   2389  C CB     . MET A 1 313 ? 4.982   -16.357 20.100 1.00 37.25  ? 313 MET A CB     1 
ATOM   2390  C CG     . MET A 1 313 ? 5.945   -15.200 20.145 1.00 45.19  ? 313 MET A CG     1 
ATOM   2391  S SD     . MET A 1 313 ? 6.132   -14.757 21.864 1.00 59.49  ? 313 MET A SD     1 
ATOM   2392  C CE     . MET A 1 313 ? 4.415   -14.433 22.236 1.00 59.16  ? 313 MET A CE     1 
ATOM   2393  N N      . GLN A 1 314 ? 3.878   -19.290 20.155 1.00 36.63  ? 314 GLN A N      1 
ATOM   2394  C CA     . GLN A 1 314 ? 2.986   -20.244 20.749 1.00 39.18  ? 314 GLN A CA     1 
ATOM   2395  C C      . GLN A 1 314 ? 3.741   -21.457 21.190 1.00 43.18  ? 314 GLN A C      1 
ATOM   2396  O O      . GLN A 1 314 ? 3.485   -21.976 22.247 1.00 46.82  ? 314 GLN A O      1 
ATOM   2397  C CB     . GLN A 1 314 ? 1.922   -20.639 19.741 1.00 43.91  ? 314 GLN A CB     1 
ATOM   2398  C CG     . GLN A 1 314 ? 0.509   -20.696 20.277 1.00 42.69  ? 314 GLN A CG     1 
ATOM   2399  C CD     . GLN A 1 314 ? -0.506  -20.605 19.165 1.00 58.38  ? 314 GLN A CD     1 
ATOM   2400  O OE1    . GLN A 1 314 ? -0.161  -20.310 18.024 1.00 66.46  ? 314 GLN A OE1    1 
ATOM   2401  N NE2    . GLN A 1 314 ? -1.762  -20.852 19.487 1.00 62.68  ? 314 GLN A NE2    1 
ATOM   2402  N N      . LYS A 1 315 ? 4.672   -21.932 20.387 1.00 40.46  ? 315 LYS A N      1 
ATOM   2403  C CA     . LYS A 1 315 ? 5.428   -23.122 20.723 1.00 40.23  ? 315 LYS A CA     1 
ATOM   2404  C C      . LYS A 1 315 ? 6.058   -22.915 22.053 1.00 47.35  ? 315 LYS A C      1 
ATOM   2405  O O      . LYS A 1 315 ? 5.947   -23.754 22.932 1.00 51.18  ? 315 LYS A O      1 
ATOM   2406  C CB     . LYS A 1 315 ? 6.520   -23.353 19.699 1.00 39.02  ? 315 LYS A CB     1 
ATOM   2407  C CG     . LYS A 1 315 ? 7.598   -24.335 20.115 1.00 36.55  ? 315 LYS A CG     1 
ATOM   2408  C CD     . LYS A 1 315 ? 8.826   -24.179 19.239 1.00 38.72  ? 315 LYS A CD     1 
ATOM   2409  C CE     . LYS A 1 315 ? 10.057  -24.766 19.902 1.00 39.72  ? 315 LYS A CE     1 
ATOM   2410  N NZ     . LYS A 1 315 ? 11.297  -24.375 19.180 1.00 39.67  ? 315 LYS A NZ     1 
ATOM   2411  N N      . GLU A 1 316 ? 6.687   -21.765 22.239 1.00 43.73  ? 316 GLU A N      1 
ATOM   2412  C CA     . GLU A 1 316 ? 7.410   -21.511 23.473 1.00 43.41  ? 316 GLU A CA     1 
ATOM   2413  C C      . GLU A 1 316 ? 6.573   -21.168 24.693 1.00 41.55  ? 316 GLU A C      1 
ATOM   2414  O O      . GLU A 1 316 ? 6.972   -21.486 25.790 1.00 45.58  ? 316 GLU A O      1 
ATOM   2415  C CB     . GLU A 1 316 ? 8.448   -20.446 23.229 1.00 41.89  ? 316 GLU A CB     1 
ATOM   2416  C CG     . GLU A 1 316 ? 9.155   -20.552 21.891 1.00 39.63  ? 316 GLU A CG     1 
ATOM   2417  C CD     . GLU A 1 316 ? 10.623  -20.876 22.024 1.00 49.72  ? 316 GLU A CD     1 
ATOM   2418  O OE1    . GLU A 1 316 ? 11.015  -21.442 23.061 1.00 58.53  ? 316 GLU A OE1    1 
ATOM   2419  O OE2    . GLU A 1 316 ? 11.384  -20.576 21.084 1.00 42.59  ? 316 GLU A OE2    1 
ATOM   2420  N N      . ILE A 1 317 ? 5.421   -20.531 24.528 1.00 35.39  ? 317 ILE A N      1 
ATOM   2421  C CA     . ILE A 1 317 ? 4.550   -20.256 25.667 1.00 38.15  ? 317 ILE A CA     1 
ATOM   2422  C C      . ILE A 1 317 ? 3.535   -21.349 25.900 1.00 39.91  ? 317 ILE A C      1 
ATOM   2423  O O      . ILE A 1 317 ? 2.668   -21.228 26.742 1.00 43.37  ? 317 ILE A O      1 
ATOM   2424  C CB     . ILE A 1 317 ? 3.872   -18.884 25.598 1.00 35.78  ? 317 ILE A CB     1 
ATOM   2425  C CG1    . ILE A 1 317 ? 4.755   -17.881 24.899 1.00 39.30  ? 317 ILE A CG1    1 
ATOM   2426  C CG2    . ILE A 1 317 ? 3.610   -18.325 26.984 1.00 30.48  ? 317 ILE A CG2    1 
ATOM   2427  C CD1    . ILE A 1 317 ? 4.181   -16.498 24.986 1.00 36.73  ? 317 ILE A CD1    1 
ATOM   2428  N N      . THR A 1 318 ? 3.645   -22.451 25.194 1.00 42.06  ? 318 THR A N      1 
ATOM   2429  C CA     . THR A 1 318 ? 2.773   -23.568 25.485 1.00 46.35  ? 318 THR A CA     1 
ATOM   2430  C C      . THR A 1 318 ? 3.679   -24.489 26.262 1.00 47.58  ? 318 THR A C      1 
ATOM   2431  O O      . THR A 1 318 ? 3.225   -25.381 26.964 1.00 50.18  ? 318 THR A O      1 
ATOM   2432  C CB     . THR A 1 318 ? 2.250   -24.241 24.221 1.00 39.14  ? 318 THR A CB     1 
ATOM   2433  O OG1    . THR A 1 318 ? 1.637   -23.265 23.381 1.00 43.50  ? 318 THR A OG1    1 
ATOM   2434  C CG2    . THR A 1 318 ? 1.206   -25.283 24.560 1.00 36.48  ? 318 THR A CG2    1 
ATOM   2435  N N      . ALA A 1 319 ? 4.975   -24.230 26.200 1.00 44.77  ? 319 ALA A N      1 
ATOM   2436  C CA     . ALA A 1 319 ? 5.937   -25.054 26.906 1.00 47.25  ? 319 ALA A CA     1 
ATOM   2437  C C      . ALA A 1 319 ? 6.317   -24.419 28.197 1.00 47.85  ? 319 ALA A C      1 
ATOM   2438  O O      . ALA A 1 319 ? 6.851   -25.075 29.076 1.00 44.72  ? 319 ALA A O      1 
ATOM   2439  C CB     . ALA A 1 319 ? 7.162   -25.217 26.067 1.00 48.82  ? 319 ALA A CB     1 
ATOM   2440  N N      . LEU A 1 320 ? 6.051   -23.136 28.330 1.00 49.12  ? 320 LEU A N      1 
ATOM   2441  C CA     . LEU A 1 320 ? 6.356   -22.427 29.558 1.00 48.50  ? 320 LEU A CA     1 
ATOM   2442  C C      . LEU A 1 320 ? 5.136   -22.347 30.414 1.00 43.94  ? 320 LEU A C      1 
ATOM   2443  O O      . LEU A 1 320 ? 5.216   -21.997 31.573 1.00 46.29  ? 320 LEU A O      1 
ATOM   2444  C CB     . LEU A 1 320 ? 6.823   -21.011 29.236 1.00 42.49  ? 320 LEU A CB     1 
ATOM   2445  C CG     . LEU A 1 320 ? 8.302   -20.650 29.239 1.00 43.47  ? 320 LEU A CG     1 
ATOM   2446  C CD1    . LEU A 1 320 ? 9.125   -21.563 28.348 1.00 49.86  ? 320 LEU A CD1    1 
ATOM   2447  C CD2    . LEU A 1 320 ? 8.428   -19.216 28.781 1.00 40.33  ? 320 LEU A CD2    1 
ATOM   2448  N N      . ALA A 1 321 ? 3.996   -22.677 29.861 1.00 37.74  ? 321 ALA A N      1 
ATOM   2449  C CA     . ALA A 1 321 ? 2.781   -22.511 30.589 1.00 37.75  ? 321 ALA A CA     1 
ATOM   2450  C C      . ALA A 1 321 ? 2.076   -23.811 30.815 1.00 41.01  ? 321 ALA A C      1 
ATOM   2451  O O      . ALA A 1 321 ? 2.481   -24.826 30.277 1.00 44.14  ? 321 ALA A O      1 
ATOM   2452  C CB     . ALA A 1 321 ? 1.917   -21.576 29.812 1.00 40.91  ? 321 ALA A CB     1 
ATOM   2453  N N      . PRO A 1 322 ? 0.985   -23.796 31.636 1.00 41.75  ? 322 PRO A N      1 
ATOM   2454  C CA     . PRO A 1 322 ? 0.372   -25.084 31.927 1.00 46.27  ? 322 PRO A CA     1 
ATOM   2455  C C      . PRO A 1 322 ? -0.061  -25.906 30.750 1.00 53.80  ? 322 PRO A C      1 
ATOM   2456  O O      . PRO A 1 322 ? -0.394  -25.347 29.717 1.00 55.34  ? 322 PRO A O      1 
ATOM   2457  C CB     . PRO A 1 322 ? -0.856  -24.683 32.699 1.00 47.44  ? 322 PRO A CB     1 
ATOM   2458  C CG     . PRO A 1 322 ? -0.395  -23.547 33.510 1.00 50.14  ? 322 PRO A CG     1 
ATOM   2459  C CD     . PRO A 1 322 ? 0.381   -22.758 32.514 1.00 45.48  ? 322 PRO A CD     1 
ATOM   2460  N N      . SER A 1 323 ? -0.116  -27.225 30.912 1.00 57.88  ? 323 SER A N      1 
ATOM   2461  C CA     . SER A 1 323 ? -0.449  -28.121 29.810 1.00 56.27  ? 323 SER A CA     1 
ATOM   2462  C C      . SER A 1 323 ? -1.818  -27.923 29.242 1.00 54.49  ? 323 SER A C      1 
ATOM   2463  O O      . SER A 1 323 ? -1.987  -27.847 28.035 1.00 57.42  ? 323 SER A O      1 
ATOM   2464  C CB     . SER A 1 323 ? -0.319  -29.549 30.279 1.00 54.97  ? 323 SER A CB     1 
ATOM   2465  O OG     . SER A 1 323 ? 0.980   -29.787 30.790 1.00 71.25  ? 323 SER A OG     1 
ATOM   2466  N N      . THR A 1 324 ? -2.806  -27.805 30.102 1.00 54.93  ? 324 THR A N      1 
ATOM   2467  C CA     . THR A 1 324 ? -4.168  -27.686 29.635 1.00 57.43  ? 324 THR A CA     1 
ATOM   2468  C C      . THR A 1 324 ? -4.550  -26.301 29.204 1.00 66.96  ? 324 THR A C      1 
ATOM   2469  O O      . THR A 1 324 ? -5.672  -26.086 28.766 1.00 71.36  ? 324 THR A O      1 
ATOM   2470  C CB     . THR A 1 324 ? -5.109  -28.006 30.766 1.00 63.63  ? 324 THR A CB     1 
ATOM   2471  O OG1    . THR A 1 324 ? -4.899  -27.062 31.823 1.00 71.07  ? 324 THR A OG1    1 
ATOM   2472  C CG2    . THR A 1 324 ? -4.840  -29.400 31.287 1.00 71.23  ? 324 THR A CG2    1 
ATOM   2473  N N      . MET A 1 325 ? -3.648  -25.343 29.319 1.00 60.42  ? 325 MET A N      1 
ATOM   2474  C CA     . MET A 1 325 ? -4.000  -23.973 29.016 1.00 48.10  ? 325 MET A CA     1 
ATOM   2475  C C      . MET A 1 325 ? -4.416  -23.773 27.585 1.00 51.12  ? 325 MET A C      1 
ATOM   2476  O O      . MET A 1 325 ? -4.106  -24.580 26.728 1.00 63.41  ? 325 MET A O      1 
ATOM   2477  C CB     . MET A 1 325 ? -2.829  -23.074 29.342 1.00 51.61  ? 325 MET A CB     1 
ATOM   2478  C CG     . MET A 1 325 ? -3.148  -21.601 29.540 1.00 63.79  ? 325 MET A CG     1 
ATOM   2479  S SD     . MET A 1 325 ? -3.937  -21.203 31.109 1.00 71.46  ? 325 MET A SD     1 
ATOM   2480  C CE     . MET A 1 325 ? -5.670  -21.258 30.667 1.00 59.04  ? 325 MET A CE     1 
ATOM   2481  N N      . LYS A 1 326 ? -5.133  -22.699 27.316 1.00 45.41  ? 326 LYS A N      1 
ATOM   2482  C CA     . LYS A 1 326 ? -5.512  -22.377 25.964 1.00 48.37  ? 326 LYS A CA     1 
ATOM   2483  C C      . LYS A 1 326 ? -4.696  -21.183 25.593 1.00 49.71  ? 326 LYS A C      1 
ATOM   2484  O O      . LYS A 1 326 ? -4.754  -20.174 26.260 1.00 53.07  ? 326 LYS A O      1 
ATOM   2485  C CB     . LYS A 1 326 ? -6.983  -22.025 25.914 1.00 54.01  ? 326 LYS A CB     1 
ATOM   2486  C CG     . LYS A 1 326 ? -7.473  -21.549 24.557 1.00 62.32  ? 326 LYS A CG     1 
ATOM   2487  C CD     . LYS A 1 326 ? -8.976  -21.321 24.569 1.00 66.87  ? 326 LYS A CD     1 
ATOM   2488  C CE     . LYS A 1 326 ? -9.482  -20.811 23.230 1.00 67.00  ? 326 LYS A CE     1 
ATOM   2489  N NZ     . LYS A 1 326 ? -8.991  -19.442 22.920 1.00 54.88  ? 326 LYS A NZ     1 
ATOM   2490  N N      . ILE A 1 327 ? -3.938  -21.261 24.516 1.00 49.58  ? 327 ILE A N      1 
ATOM   2491  C CA     . ILE A 1 327 ? -3.049  -20.175 24.176 1.00 46.50  ? 327 ILE A CA     1 
ATOM   2492  C C      . ILE A 1 327 ? -3.200  -19.659 22.757 1.00 48.40  ? 327 ILE A C      1 
ATOM   2493  O O      . ILE A 1 327 ? -3.095  -20.415 21.811 1.00 53.28  ? 327 ILE A O      1 
ATOM   2494  C CB     . ILE A 1 327 ? -1.609  -20.617 24.442 1.00 45.03  ? 327 ILE A CB     1 
ATOM   2495  C CG1    . ILE A 1 327 ? -0.601  -19.620 23.888 1.00 44.66  ? 327 ILE A CG1    1 
ATOM   2496  C CG2    . ILE A 1 327 ? -1.376  -22.016 23.897 1.00 52.99  ? 327 ILE A CG2    1 
ATOM   2497  C CD1    . ILE A 1 327 ? -0.105  -18.640 24.924 1.00 50.51  ? 327 ILE A CD1    1 
ATOM   2498  N N      . LYS A 1 328 ? -3.473  -18.372 22.595 1.00 45.25  ? 328 LYS A N      1 
ATOM   2499  C CA     . LYS A 1 328 ? -3.550  -17.797 21.267 1.00 40.72  ? 328 LYS A CA     1 
ATOM   2500  C C      . LYS A 1 328 ? -2.679  -16.609 21.163 1.00 38.78  ? 328 LYS A C      1 
ATOM   2501  O O      . LYS A 1 328 ? -2.745  -15.725 21.986 1.00 40.36  ? 328 LYS A O      1 
ATOM   2502  C CB     . LYS A 1 328 ? -4.957  -17.394 20.898 1.00 41.68  ? 328 LYS A CB     1 
ATOM   2503  C CG     . LYS A 1 328 ? -5.749  -18.476 20.191 1.00 57.93  ? 328 LYS A CG     1 
ATOM   2504  C CD     . LYS A 1 328 ? -7.159  -18.004 19.886 1.00 61.25  ? 328 LYS A CD     1 
ATOM   2505  C CE     . LYS A 1 328 ? -7.150  -16.724 19.070 1.00 47.98  ? 328 LYS A CE     1 
ATOM   2506  N NZ     . LYS A 1 328 ? -6.519  -16.911 17.737 1.00 46.33  ? 328 LYS A NZ     1 
ATOM   2507  N N      . ILE A 1 329 ? -1.854  -16.580 20.141 1.00 40.42  ? 329 ILE A N      1 
ATOM   2508  C CA     . ILE A 1 329 ? -0.987  -15.471 19.904 1.00 37.14  ? 329 ILE A CA     1 
ATOM   2509  C C      . ILE A 1 329 ? -1.637  -14.854 18.697 1.00 39.38  ? 329 ILE A C      1 
ATOM   2510  O O      . ILE A 1 329 ? -1.807  -15.516 17.684 1.00 43.47  ? 329 ILE A O      1 
ATOM   2511  C CB     . ILE A 1 329 ? 0.432   -15.966 19.645 1.00 35.70  ? 329 ILE A CB     1 
ATOM   2512  C CG1    . ILE A 1 329 ? 1.260   -15.894 20.914 1.00 40.42  ? 329 ILE A CG1    1 
ATOM   2513  C CG2    . ILE A 1 329 ? 1.122   -15.139 18.586 1.00 45.78  ? 329 ILE A CG2    1 
ATOM   2514  C CD1    . ILE A 1 329 ? 1.085   -17.079 21.823 1.00 50.03  ? 329 ILE A CD1    1 
ATOM   2515  N N      . ILE A 1 330 ? -2.089  -13.613 18.820 1.00 39.56  ? 330 ILE A N      1 
ATOM   2516  C CA     . ILE A 1 330 ? -2.840  -12.976 17.748 1.00 37.91  ? 330 ILE A CA     1 
ATOM   2517  C C      . ILE A 1 330 ? -2.058  -11.889 17.128 1.00 37.81  ? 330 ILE A C      1 
ATOM   2518  O O      . ILE A 1 330 ? -1.804  -10.879 17.732 1.00 41.98  ? 330 ILE A O      1 
ATOM   2519  C CB     . ILE A 1 330 ? -4.129  -12.357 18.274 1.00 35.26  ? 330 ILE A CB     1 
ATOM   2520  C CG1    . ILE A 1 330 ? -4.875  -13.373 19.124 1.00 41.74  ? 330 ILE A CG1    1 
ATOM   2521  C CG2    . ILE A 1 330 ? -4.998  -11.879 17.127 1.00 30.41  ? 330 ILE A CG2    1 
ATOM   2522  C CD1    . ILE A 1 330 ? -5.609  -12.754 20.279 1.00 35.25  ? 330 ILE A CD1    1 
ATOM   2523  N N      . ALA A 1 331 ? -1.734  -12.058 15.873 1.00 37.06  ? 331 ALA A N      1 
ATOM   2524  C CA     . ALA A 1 331 ? -0.928  -11.100 15.203 1.00 41.06  ? 331 ALA A CA     1 
ATOM   2525  C C      . ALA A 1 331 ? -1.669  -10.569 14.031 1.00 42.49  ? 331 ALA A C      1 
ATOM   2526  O O      . ALA A 1 331 ? -1.765  -11.236 13.014 1.00 42.07  ? 331 ALA A O      1 
ATOM   2527  C CB     . ALA A 1 331 ? 0.284   -11.800 14.722 1.00 42.97  ? 331 ALA A CB     1 
ATOM   2528  N N      . PRO A 1 332 ? -2.209  -9.331  14.158 1.00 42.62  ? 332 PRO A N      1 
ATOM   2529  C CA     . PRO A 1 332 ? -2.886  -8.867  12.964 1.00 36.51  ? 332 PRO A CA     1 
ATOM   2530  C C      . PRO A 1 332 ? -1.925  -8.526  11.875 1.00 42.53  ? 332 PRO A C      1 
ATOM   2531  O O      . PRO A 1 332 ? -0.806  -8.149  12.152 1.00 45.45  ? 332 PRO A O      1 
ATOM   2532  C CB     . PRO A 1 332 ? -3.564  -7.603  13.441 1.00 35.25  ? 332 PRO A CB     1 
ATOM   2533  C CG     . PRO A 1 332 ? -3.739  -7.773  14.899 1.00 45.45  ? 332 PRO A CG     1 
ATOM   2534  C CD     . PRO A 1 332 ? -2.442  -8.389  15.276 1.00 44.06  ? 332 PRO A CD     1 
ATOM   2535  N N      . PRO A 1 333 ? -2.364  -8.626  10.596 1.00 43.06  ? 333 PRO A N      1 
ATOM   2536  C CA     . PRO A 1 333 ? -1.356  -8.396  9.569  1.00 43.06  ? 333 PRO A CA     1 
ATOM   2537  C C      . PRO A 1 333 ? -0.867  -6.991  9.485  1.00 47.45  ? 333 PRO A C      1 
ATOM   2538  O O      . PRO A 1 333 ? 0.260   -6.782  9.084  1.00 51.28  ? 333 PRO A O      1 
ATOM   2539  C CB     . PRO A 1 333 ? -2.089  -8.735  8.293  1.00 43.52  ? 333 PRO A CB     1 
ATOM   2540  C CG     . PRO A 1 333 ? -3.206  -9.620  8.698  1.00 43.95  ? 333 PRO A CG     1 
ATOM   2541  C CD     . PRO A 1 333 ? -3.653  -8.979  9.960  1.00 40.33  ? 333 PRO A CD     1 
ATOM   2542  N N      . GLU A 1 334 ? -1.687  -6.029  9.844  1.00 47.62  ? 334 GLU A N      1 
ATOM   2543  C CA     . GLU A 1 334 ? -1.261  -4.654  9.844  1.00 46.66  ? 334 GLU A CA     1 
ATOM   2544  C C      . GLU A 1 334 ? -0.966  -4.299  11.246 1.00 49.84  ? 334 GLU A C      1 
ATOM   2545  O O      . GLU A 1 334 ? -1.786  -3.679  11.901 1.00 50.78  ? 334 GLU A O      1 
ATOM   2546  C CB     . GLU A 1 334 ? -2.392  -3.792  9.353  1.00 50.45  ? 334 GLU A CB     1 
ATOM   2547  C CG     . GLU A 1 334 ? -2.996  -4.278  8.042  1.00 74.77  ? 334 GLU A CG     1 
ATOM   2548  C CD     . GLU A 1 334 ? -2.000  -4.328  6.890  1.00 75.21  ? 334 GLU A CD     1 
ATOM   2549  O OE1    . GLU A 1 334 ? -1.080  -3.485  6.844  1.00 75.79  ? 334 GLU A OE1    1 
ATOM   2550  O OE2    . GLU A 1 334 ? -2.144  -5.207  6.016  1.00 64.86  ? 334 GLU A OE2    1 
ATOM   2551  N N      . ARG A 1 335 ? 0.216   -4.633  11.721 1.00 44.35  ? 335 ARG A N      1 
ATOM   2552  C CA     . ARG A 1 335 ? 0.508   -4.419  13.114 1.00 39.72  ? 335 ARG A CA     1 
ATOM   2553  C C      . ARG A 1 335 ? 1.581   -3.400  13.331 1.00 39.66  ? 335 ARG A C      1 
ATOM   2554  O O      . ARG A 1 335 ? 1.797   -2.966  14.445 1.00 40.98  ? 335 ARG A O      1 
ATOM   2555  C CB     . ARG A 1 335 ? 0.882   -5.740  13.771 1.00 39.14  ? 335 ARG A CB     1 
ATOM   2556  C CG     . ARG A 1 335 ? 2.320   -6.170  13.587 1.00 42.92  ? 335 ARG A CG     1 
ATOM   2557  C CD     . ARG A 1 335 ? 2.483   -7.657  13.843 1.00 34.49  ? 335 ARG A CD     1 
ATOM   2558  N NE     . ARG A 1 335 ? 2.100   -8.420  12.667 1.00 43.07  ? 335 ARG A NE     1 
ATOM   2559  C CZ     . ARG A 1 335 ? 2.221   -9.734  12.555 1.00 43.56  ? 335 ARG A CZ     1 
ATOM   2560  N NH1    . ARG A 1 335 ? 2.718   -10.435 13.551 1.00 46.38  ? 335 ARG A NH1    1 
ATOM   2561  N NH2    . ARG A 1 335 ? 1.848   -10.344 11.442 1.00 45.91  ? 335 ARG A NH2    1 
ATOM   2562  N N      . LYS A 1 336 ? 2.229   -2.965  12.273 1.00 37.20  ? 336 LYS A N      1 
ATOM   2563  C CA     . LYS A 1 336 ? 3.251   -1.961  12.424 1.00 40.96  ? 336 LYS A CA     1 
ATOM   2564  C C      . LYS A 1 336 ? 2.574   -0.694  12.804 1.00 43.60  ? 336 LYS A C      1 
ATOM   2565  O O      . LYS A 1 336 ? 3.097   0.082   13.592 1.00 38.38  ? 336 LYS A O      1 
ATOM   2566  C CB     . LYS A 1 336 ? 4.007   -1.776  11.120 1.00 36.42  ? 336 LYS A CB     1 
ATOM   2567  C CG     . LYS A 1 336 ? 5.281   -0.967  11.257 1.00 45.59  ? 336 LYS A CG     1 
ATOM   2568  C CD     . LYS A 1 336 ? 5.923   -0.787  9.899  1.00 40.65  ? 336 LYS A CD     1 
ATOM   2569  C CE     . LYS A 1 336 ? 5.674   -2.018  9.051  1.00 43.18  ? 336 LYS A CE     1 
ATOM   2570  N NZ     . LYS A 1 336 ? 6.108   -1.822  7.643  1.00 65.74  ? 336 LYS A NZ     1 
ATOM   2571  N N      . TYR A 1 337 ? 1.371   -0.499  12.292 1.00 48.08  ? 337 TYR A N      1 
ATOM   2572  C CA     . TYR A 1 337 ? 0.631   0.713   12.537 1.00 41.29  ? 337 TYR A CA     1 
ATOM   2573  C C      . TYR A 1 337 ? -0.598  0.385   13.323 1.00 37.85  ? 337 TYR A C      1 
ATOM   2574  O O      . TYR A 1 337 ? -1.608  1.027   13.168 1.00 34.90  ? 337 TYR A O      1 
ATOM   2575  C CB     . TYR A 1 337 ? 0.257   1.283   11.193 1.00 37.56  ? 337 TYR A CB     1 
ATOM   2576  C CG     . TYR A 1 337 ? 1.447   1.474   10.284 1.00 40.57  ? 337 TYR A CG     1 
ATOM   2577  C CD1    . TYR A 1 337 ? 2.570   2.155   10.720 1.00 40.88  ? 337 TYR A CD1    1 
ATOM   2578  C CD2    . TYR A 1 337 ? 1.446   0.977   8.995  1.00 44.75  ? 337 TYR A CD2    1 
ATOM   2579  C CE1    . TYR A 1 337 ? 3.662   2.335   9.900  1.00 40.45  ? 337 TYR A CE1    1 
ATOM   2580  C CE2    . TYR A 1 337 ? 2.534   1.156   8.164  1.00 54.27  ? 337 TYR A CE2    1 
ATOM   2581  C CZ     . TYR A 1 337 ? 3.640   1.836   8.624  1.00 51.17  ? 337 TYR A CZ     1 
ATOM   2582  O OH     . TYR A 1 337 ? 4.726   2.012   7.803  1.00 42.76  ? 337 TYR A OH     1 
ATOM   2583  N N      . SER A 1 338 ? -0.500  -0.566  14.228 1.00 38.03  ? 338 SER A N      1 
ATOM   2584  C CA     . SER A 1 338 ? -1.645  -0.991  15.001 1.00 43.09  ? 338 SER A CA     1 
ATOM   2585  C C      . SER A 1 338 ? -1.960  -0.030  16.112 1.00 38.38  ? 338 SER A C      1 
ATOM   2586  O O      . SER A 1 338 ? -3.103  0.153   16.464 1.00 34.65  ? 338 SER A O      1 
ATOM   2587  C CB     . SER A 1 338 ? -1.377  -2.361  15.589 1.00 43.55  ? 338 SER A CB     1 
ATOM   2588  O OG     . SER A 1 338 ? -2.510  -2.863  16.268 1.00 45.18  ? 338 SER A OG     1 
ATOM   2589  N N      . VAL A 1 339 ? -0.955  0.587   16.678 1.00 33.19  ? 339 VAL A N      1 
ATOM   2590  C CA     . VAL A 1 339 ? -1.199  1.515   17.727 1.00 34.20  ? 339 VAL A CA     1 
ATOM   2591  C C      . VAL A 1 339 ? -2.041  2.565   17.146 1.00 36.47  ? 339 VAL A C      1 
ATOM   2592  O O      . VAL A 1 339 ? -3.070  2.904   17.658 1.00 41.19  ? 339 VAL A O      1 
ATOM   2593  C CB     . VAL A 1 339 ? 0.083   2.162   18.186 1.00 33.75  ? 339 VAL A CB     1 
ATOM   2594  C CG1    . VAL A 1 339 ? -0.190  3.095   19.342 1.00 32.88  ? 339 VAL A CG1    1 
ATOM   2595  C CG2    . VAL A 1 339 ? 1.084   1.096   18.586 1.00 39.77  ? 339 VAL A CG2    1 
ATOM   2596  N N      . TRP A 1 340 ? -1.620  3.089   16.040 1.00 34.37  ? 340 TRP A N      1 
ATOM   2597  C CA     . TRP A 1 340 ? -2.326  4.175   15.477 1.00 31.80  ? 340 TRP A CA     1 
ATOM   2598  C C      . TRP A 1 340 ? -3.721  3.781   15.109 1.00 36.95  ? 340 TRP A C      1 
ATOM   2599  O O      . TRP A 1 340 ? -4.627  4.512   15.398 1.00 36.20  ? 340 TRP A O      1 
ATOM   2600  C CB     . TRP A 1 340 ? -1.531  4.621   14.263 1.00 34.66  ? 340 TRP A CB     1 
ATOM   2601  C CG     . TRP A 1 340 ? -1.933  5.873   13.636 1.00 41.46  ? 340 TRP A CG     1 
ATOM   2602  C CD1    . TRP A 1 340 ? -1.492  7.112   13.941 1.00 37.68  ? 340 TRP A CD1    1 
ATOM   2603  C CD2    . TRP A 1 340 ? -2.832  6.019   12.551 1.00 34.68  ? 340 TRP A CD2    1 
ATOM   2604  N NE1    . TRP A 1 340 ? -2.081  8.030   13.127 1.00 36.68  ? 340 TRP A NE1    1 
ATOM   2605  C CE2    . TRP A 1 340 ? -2.913  7.377   12.262 1.00 34.09  ? 340 TRP A CE2    1 
ATOM   2606  C CE3    . TRP A 1 340 ? -3.593  5.127   11.807 1.00 33.48  ? 340 TRP A CE3    1 
ATOM   2607  C CZ2    . TRP A 1 340 ? -3.719  7.868   11.262 1.00 40.68  ? 340 TRP A CZ2    1 
ATOM   2608  C CZ3    . TRP A 1 340 ? -4.389  5.615   10.821 1.00 39.80  ? 340 TRP A CZ3    1 
ATOM   2609  C CH2    . TRP A 1 340 ? -4.448  6.971   10.551 1.00 48.23  ? 340 TRP A CH2    1 
ATOM   2610  N N      . ILE A 1 341 ? -3.921  2.628   14.496 1.00 40.25  ? 341 ILE A N      1 
ATOM   2611  C CA     . ILE A 1 341 ? -5.241  2.235   14.021 1.00 36.47  ? 341 ILE A CA     1 
ATOM   2612  C C      . ILE A 1 341 ? -6.120  1.966   15.203 1.00 39.06  ? 341 ILE A C      1 
ATOM   2613  O O      . ILE A 1 341 ? -7.330  1.975   15.094 1.00 36.29  ? 341 ILE A O      1 
ATOM   2614  C CB     . ILE A 1 341 ? -5.165  1.028   13.101 1.00 26.89  ? 341 ILE A CB     1 
ATOM   2615  C CG1    . ILE A 1 341 ? -4.237  1.330   11.943 1.00 29.55  ? 341 ILE A CG1    1 
ATOM   2616  C CG2    . ILE A 1 341 ? -6.534  0.673   12.561 1.00 29.41  ? 341 ILE A CG2    1 
ATOM   2617  C CD1    . ILE A 1 341 ? -3.901  0.112   11.121 1.00 47.46  ? 341 ILE A CD1    1 
ATOM   2618  N N      . GLY A 1 342 ? -5.517  1.725   16.349 1.00 39.65  ? 342 GLY A N      1 
ATOM   2619  C CA     . GLY A 1 342 ? -6.301  1.557   17.545 1.00 38.63  ? 342 GLY A CA     1 
ATOM   2620  C C      . GLY A 1 342 ? -6.772  2.913   17.898 1.00 37.72  ? 342 GLY A C      1 
ATOM   2621  O O      . GLY A 1 342 ? -7.882  3.086   18.344 1.00 38.72  ? 342 GLY A O      1 
ATOM   2622  N N      . GLY A 1 343 ? -5.943  3.887   17.663 1.00 37.41  ? 343 GLY A N      1 
ATOM   2623  C CA     . GLY A 1 343 ? -6.315  5.233   17.940 1.00 36.92  ? 343 GLY A CA     1 
ATOM   2624  C C      . GLY A 1 343 ? -7.330  5.712   16.963 1.00 42.20  ? 343 GLY A C      1 
ATOM   2625  O O      . GLY A 1 343 ? -8.267  6.358   17.353 1.00 48.07  ? 343 GLY A O      1 
ATOM   2626  N N      . SER A 1 344 ? -7.160  5.415   15.692 1.00 41.55  ? 344 SER A N      1 
ATOM   2627  C CA     . SER A 1 344 ? -8.083  5.944   14.722 1.00 42.41  ? 344 SER A CA     1 
ATOM   2628  C C      . SER A 1 344 ? -9.430  5.376   15.028 1.00 40.86  ? 344 SER A C      1 
ATOM   2629  O O      . SER A 1 344 ? -10.442 5.992   14.772 1.00 44.43  ? 344 SER A O      1 
ATOM   2630  C CB     . SER A 1 344 ? -7.641  5.611   13.325 1.00 40.85  ? 344 SER A CB     1 
ATOM   2631  O OG     . SER A 1 344 ? -6.468  6.320   13.011 1.00 39.90  ? 344 SER A OG     1 
ATOM   2632  N N      . ILE A 1 345 ? -9.454  4.170   15.543 1.00 38.29  ? 345 ILE A N      1 
ATOM   2633  C CA     . ILE A 1 345 ? -10.696 3.563   15.923 1.00 41.70  ? 345 ILE A CA     1 
ATOM   2634  C C      . ILE A 1 345 ? -11.263 4.307   17.072 1.00 40.61  ? 345 ILE A C      1 
ATOM   2635  O O      . ILE A 1 345 ? -12.403 4.673   17.031 1.00 46.61  ? 345 ILE A O      1 
ATOM   2636  C CB     . ILE A 1 345 ? -10.515 2.073   16.242 1.00 34.70  ? 345 ILE A CB     1 
ATOM   2637  C CG1    . ILE A 1 345 ? -10.424 1.281   14.947 1.00 34.42  ? 345 ILE A CG1    1 
ATOM   2638  C CG2    . ILE A 1 345 ? -11.663 1.540   17.074 1.00 32.93  ? 345 ILE A CG2    1 
ATOM   2639  C CD1    . ILE A 1 345 ? -10.081 -0.171  15.148 1.00 37.86  ? 345 ILE A CD1    1 
ATOM   2640  N N      . LEU A 1 346 ? -10.470 4.643   18.059 1.00 36.92  ? 346 LEU A N      1 
ATOM   2641  C CA     . LEU A 1 346 ? -11.025 5.248   19.242 1.00 40.63  ? 346 LEU A CA     1 
ATOM   2642  C C      . LEU A 1 346 ? -11.422 6.636   18.959 1.00 45.25  ? 346 LEU A C      1 
ATOM   2643  O O      . LEU A 1 346 ? -12.494 7.046   19.296 1.00 50.62  ? 346 LEU A O      1 
ATOM   2644  C CB     . LEU A 1 346 ? -10.027 5.213   20.384 1.00 43.96  ? 346 LEU A CB     1 
ATOM   2645  C CG     . LEU A 1 346 ? -10.417 5.592   21.802 1.00 44.02  ? 346 LEU A CG     1 
ATOM   2646  C CD1    . LEU A 1 346 ? -11.430 4.600   22.349 1.00 52.08  ? 346 LEU A CD1    1 
ATOM   2647  C CD2    . LEU A 1 346 ? -9.168  5.606   22.663 1.00 39.07  ? 346 LEU A CD2    1 
ATOM   2648  N N      . ALA A 1 347 ? -10.572 7.386   18.327 1.00 41.67  ? 347 ALA A N      1 
ATOM   2649  C CA     . ALA A 1 347 ? -10.867 8.787   18.112 1.00 38.40  ? 347 ALA A CA     1 
ATOM   2650  C C      . ALA A 1 347 ? -12.139 8.953   17.365 1.00 42.83  ? 347 ALA A C      1 
ATOM   2651  O O      . ALA A 1 347 ? -12.931 9.826   17.679 1.00 49.59  ? 347 ALA A O      1 
ATOM   2652  C CB     . ALA A 1 347 ? -9.749  9.441   17.348 1.00 35.05  ? 347 ALA A CB     1 
ATOM   2653  N N      . SER A 1 348 ? -12.366 8.109   16.376 1.00 41.25  ? 348 SER A N      1 
ATOM   2654  C CA     . SER A 1 348 ? -13.541 8.245   15.540 1.00 46.28  ? 348 SER A CA     1 
ATOM   2655  C C      . SER A 1 348 ? -14.801 7.871   16.261 1.00 48.43  ? 348 SER A C      1 
ATOM   2656  O O      . SER A 1 348 ? -15.894 8.076   15.757 1.00 48.55  ? 348 SER A O      1 
ATOM   2657  C CB     . SER A 1 348 ? -13.396 7.355   14.333 1.00 46.95  ? 348 SER A CB     1 
ATOM   2658  O OG     . SER A 1 348 ? -13.387 5.997   14.717 1.00 53.62  ? 348 SER A OG     1 
ATOM   2659  N N      . LEU A 1 349 ? -14.666 7.350   17.461 1.00 43.26  ? 349 LEU A N      1 
ATOM   2660  C CA     . LEU A 1 349 ? -15.840 6.882   18.134 1.00 44.88  ? 349 LEU A CA     1 
ATOM   2661  C C      . LEU A 1 349 ? -16.649 7.987   18.687 1.00 51.47  ? 349 LEU A C      1 
ATOM   2662  O O      . LEU A 1 349 ? -16.114 8.995   19.097 1.00 52.21  ? 349 LEU A O      1 
ATOM   2663  C CB     . LEU A 1 349 ? -15.509 5.876   19.222 1.00 49.98  ? 349 LEU A CB     1 
ATOM   2664  C CG     . LEU A 1 349 ? -14.927 4.522   18.834 1.00 48.53  ? 349 LEU A CG     1 
ATOM   2665  C CD1    . LEU A 1 349 ? -14.862 3.617   20.048 1.00 41.41  ? 349 LEU A CD1    1 
ATOM   2666  C CD2    . LEU A 1 349 ? -15.737 3.872   17.728 1.00 55.73  ? 349 LEU A CD2    1 
ATOM   2667  N N      . SER A 1 350 ? -17.955 7.796   18.718 1.00 57.21  ? 350 SER A N      1 
ATOM   2668  C CA     . SER A 1 350 ? -18.859 8.817   19.188 1.00 52.11  ? 350 SER A CA     1 
ATOM   2669  C C      . SER A 1 350 ? -18.774 8.963   20.674 1.00 52.56  ? 350 SER A C      1 
ATOM   2670  O O      . SER A 1 350 ? -18.903 10.048  21.200 1.00 58.17  ? 350 SER A O      1 
ATOM   2671  C CB     . SER A 1 350 ? -20.264 8.431   18.800 1.00 45.79  ? 350 SER A CB     1 
ATOM   2672  O OG     . SER A 1 350 ? -20.478 7.057   19.048 1.00 64.89  ? 350 SER A OG     1 
ATOM   2673  N N      . THR A 1 351 ? -18.546 7.864   21.366 1.00 48.60  ? 351 THR A N      1 
ATOM   2674  C CA     . THR A 1 351 ? -18.522 7.909   22.798 1.00 47.27  ? 351 THR A CA     1 
ATOM   2675  C C      . THR A 1 351 ? -17.297 8.602   23.249 1.00 47.91  ? 351 THR A C      1 
ATOM   2676  O O      . THR A 1 351 ? -17.272 9.185   24.306 1.00 52.11  ? 351 THR A O      1 
ATOM   2677  C CB     . THR A 1 351 ? -18.486 6.514   23.340 1.00 51.41  ? 351 THR A CB     1 
ATOM   2678  O OG1    . THR A 1 351 ? -17.259 5.893   22.957 1.00 56.10  ? 351 THR A OG1    1 
ATOM   2679  C CG2    . THR A 1 351 ? -19.632 5.721   22.762 1.00 53.14  ? 351 THR A CG2    1 
ATOM   2680  N N      . PHE A 1 352 ? -16.263 8.571   22.435 1.00 44.67  ? 352 PHE A N      1 
ATOM   2681  C CA     . PHE A 1 352 ? -14.999 9.148   22.810 1.00 45.03  ? 352 PHE A CA     1 
ATOM   2682  C C      . PHE A 1 352 ? -15.101 10.612  22.702 1.00 49.09  ? 352 PHE A C      1 
ATOM   2683  O O      . PHE A 1 352 ? -14.150 11.320  22.940 1.00 52.20  ? 352 PHE A O      1 
ATOM   2684  C CB     . PHE A 1 352 ? -13.921 8.677   21.859 1.00 44.58  ? 352 PHE A CB     1 
ATOM   2685  C CG     . PHE A 1 352 ? -12.531 9.056   22.262 1.00 44.91  ? 352 PHE A CG     1 
ATOM   2686  C CD1    . PHE A 1 352 ? -11.986 8.593   23.434 1.00 52.00  ? 352 PHE A CD1    1 
ATOM   2687  C CD2    . PHE A 1 352 ? -11.768 9.865   21.450 1.00 39.09  ? 352 PHE A CD2    1 
ATOM   2688  C CE1    . PHE A 1 352 ? -10.706 8.941   23.799 1.00 48.17  ? 352 PHE A CE1    1 
ATOM   2689  C CE2    . PHE A 1 352 ? -10.488 10.215  21.806 1.00 37.15  ? 352 PHE A CE2    1 
ATOM   2690  C CZ     . PHE A 1 352 ? -9.956  9.751   22.981 1.00 38.46  ? 352 PHE A CZ     1 
ATOM   2691  N N      . GLN A 1 353 ? -16.252 11.114  22.326 1.00 49.18  ? 353 GLN A N      1 
ATOM   2692  C CA     . GLN A 1 353 ? -16.299 12.542  22.122 1.00 49.06  ? 353 GLN A CA     1 
ATOM   2693  C C      . GLN A 1 353 ? -16.493 13.206  23.453 1.00 53.06  ? 353 GLN A C      1 
ATOM   2694  O O      . GLN A 1 353 ? -16.526 14.425  23.551 1.00 54.62  ? 353 GLN A O      1 
ATOM   2695  C CB     . GLN A 1 353 ? -17.344 12.936  21.094 1.00 48.23  ? 353 GLN A CB     1 
ATOM   2696  C CG     . GLN A 1 353 ? -17.125 12.322  19.714 1.00 56.49  ? 353 GLN A CG     1 
ATOM   2697  C CD     . GLN A 1 353 ? -15.792 12.680  19.075 1.00 59.24  ? 353 GLN A CD     1 
ATOM   2698  O OE1    . GLN A 1 353 ? -15.240 13.755  19.306 1.00 57.21  ? 353 GLN A OE1    1 
ATOM   2699  N NE2    . GLN A 1 353 ? -15.280 11.782  18.244 1.00 48.34  ? 353 GLN A NE2    1 
ATOM   2700  N N      . GLN A 1 354 ? -16.563 12.407  24.504 1.00 49.22  ? 354 GLN A N      1 
ATOM   2701  C CA     . GLN A 1 354 ? -16.730 12.953  25.837 1.00 48.54  ? 354 GLN A CA     1 
ATOM   2702  C C      . GLN A 1 354 ? -15.483 12.757  26.644 1.00 46.93  ? 354 GLN A C      1 
ATOM   2703  O O      . GLN A 1 354 ? -15.237 13.487  27.590 1.00 49.77  ? 354 GLN A O      1 
ATOM   2704  C CB     . GLN A 1 354 ? -17.923 12.311  26.520 1.00 46.42  ? 354 GLN A CB     1 
ATOM   2705  C CG     . GLN A 1 354 ? -19.217 13.092  26.392 1.00 54.39  ? 354 GLN A CG     1 
ATOM   2706  C CD     . GLN A 1 354 ? -19.817 13.011  25.008 1.00 60.23  ? 354 GLN A CD     1 
ATOM   2707  O OE1    . GLN A 1 354 ? -19.828 11.951  24.389 1.00 62.98  ? 354 GLN A OE1    1 
ATOM   2708  N NE2    . GLN A 1 354 ? -20.331 14.129  24.519 1.00 56.73  ? 354 GLN A NE2    1 
ATOM   2709  N N      . MET A 1 355 ? -14.647 11.821  26.242 1.00 42.27  ? 355 MET A N      1 
ATOM   2710  C CA     . MET A 1 355 ? -13.424 11.540  26.961 1.00 44.09  ? 355 MET A CA     1 
ATOM   2711  C C      . MET A 1 355 ? -12.311 12.496  26.657 1.00 38.98  ? 355 MET A C      1 
ATOM   2712  O O      . MET A 1 355 ? -11.288 12.472  27.302 1.00 42.30  ? 355 MET A O      1 
ATOM   2713  C CB     . MET A 1 355 ? -12.979 10.134  26.645 1.00 43.39  ? 355 MET A CB     1 
ATOM   2714  C CG     . MET A 1 355 ? -14.077 9.113   26.816 1.00 45.14  ? 355 MET A CG     1 
ATOM   2715  S SD     . MET A 1 355 ? -13.450 7.455   26.574 1.00 60.28  ? 355 MET A SD     1 
ATOM   2716  C CE     . MET A 1 355 ? -14.985 6.544   26.508 1.00 55.35  ? 355 MET A CE     1 
ATOM   2717  N N      . TRP A 1 356 ? -12.502 13.343  25.673 1.00 38.35  ? 356 TRP A N      1 
ATOM   2718  C CA     . TRP A 1 356 ? -11.502 14.320  25.339 1.00 35.35  ? 356 TRP A CA     1 
ATOM   2719  C C      . TRP A 1 356 ? -11.284 15.274  26.488 1.00 36.15  ? 356 TRP A C      1 
ATOM   2720  O O      . TRP A 1 356 ? -12.177 15.496  27.290 1.00 35.98  ? 356 TRP A O      1 
ATOM   2721  C CB     . TRP A 1 356 ? -11.926 15.124  24.120 1.00 30.26  ? 356 TRP A CB     1 
ATOM   2722  C CG     . TRP A 1 356 ? -11.867 14.477  22.792 1.00 30.45  ? 356 TRP A CG     1 
ATOM   2723  C CD1    . TRP A 1 356 ? -12.920 14.141  22.009 1.00 37.34  ? 356 TRP A CD1    1 
ATOM   2724  C CD2    . TRP A 1 356 ? -10.694 14.157  22.043 1.00 32.81  ? 356 TRP A CD2    1 
ATOM   2725  N NE1    . TRP A 1 356 ? -12.484 13.601  20.831 1.00 43.34  ? 356 TRP A NE1    1 
ATOM   2726  C CE2    . TRP A 1 356 ? -11.116 13.600  20.829 1.00 39.69  ? 356 TRP A CE2    1 
ATOM   2727  C CE3    . TRP A 1 356 ? -9.329  14.270  22.290 1.00 31.63  ? 356 TRP A CE3    1 
ATOM   2728  C CZ2    . TRP A 1 356 ? -10.225 13.158  19.865 1.00 35.63  ? 356 TRP A CZ2    1 
ATOM   2729  C CZ3    . TRP A 1 356 ? -8.450  13.830  21.334 1.00 35.93  ? 356 TRP A CZ3    1 
ATOM   2730  C CH2    . TRP A 1 356 ? -8.897  13.281  20.139 1.00 33.58  ? 356 TRP A CH2    1 
ATOM   2731  N N      . ILE A 1 357 ? -10.101 15.857  26.569 1.00 32.76  ? 357 ILE A N      1 
ATOM   2732  C CA     . ILE A 1 357 ? -9.826  16.830  27.588 1.00 35.50  ? 357 ILE A CA     1 
ATOM   2733  C C      . ILE A 1 357 ? -9.985  18.162  26.931 1.00 37.91  ? 357 ILE A C      1 
ATOM   2734  O O      . ILE A 1 357 ? -9.241  18.474  26.034 1.00 42.82  ? 357 ILE A O      1 
ATOM   2735  C CB     . ILE A 1 357 ? -8.380  16.771  28.027 1.00 36.98  ? 357 ILE A CB     1 
ATOM   2736  C CG1    . ILE A 1 357 ? -8.098  15.541  28.852 1.00 33.20  ? 357 ILE A CG1    1 
ATOM   2737  C CG2    . ILE A 1 357 ? -8.050  17.960  28.908 1.00 48.67  ? 357 ILE A CG2    1 
ATOM   2738  C CD1    . ILE A 1 357 ? -6.762  15.653  29.544 1.00 31.51  ? 357 ILE A CD1    1 
ATOM   2739  N N      . SER A 1 358 ? -10.944 18.962  27.354 1.00 40.23  ? 358 SER A N      1 
ATOM   2740  C CA     . SER A 1 358 ? -11.199 20.224  26.695 1.00 39.69  ? 358 SER A CA     1 
ATOM   2741  C C      . SER A 1 358 ? -10.235 21.274  27.150 1.00 40.98  ? 358 SER A C      1 
ATOM   2742  O O      . SER A 1 358 ? -9.581  21.103  28.153 1.00 45.39  ? 358 SER A O      1 
ATOM   2743  C CB     . SER A 1 358 ? -12.612 20.646  27.005 1.00 41.39  ? 358 SER A CB     1 
ATOM   2744  O OG     . SER A 1 358 ? -13.512 19.575  26.807 1.00 39.17  ? 358 SER A OG     1 
ATOM   2745  N N      . LYS A 1 359 ? -10.148 22.378  26.429 1.00 41.55  ? 359 LYS A N      1 
ATOM   2746  C CA     . LYS A 1 359 ? -9.251  23.454  26.795 1.00 43.08  ? 359 LYS A CA     1 
ATOM   2747  C C      . LYS A 1 359 ? -9.860  24.092  27.962 1.00 44.70  ? 359 LYS A C      1 
ATOM   2748  O O      . LYS A 1 359 ? -9.170  24.612  28.811 1.00 54.29  ? 359 LYS A O      1 
ATOM   2749  C CB     . LYS A 1 359 ? -9.166  24.482  25.690 1.00 48.54  ? 359 LYS A CB     1 
ATOM   2750  C CG     . LYS A 1 359 ? -8.343  25.723  26.001 1.00 50.64  ? 359 LYS A CG     1 
ATOM   2751  C CD     . LYS A 1 359 ? -6.860  25.415  26.093 1.00 54.21  ? 359 LYS A CD     1 
ATOM   2752  C CE     . LYS A 1 359 ? -6.040  26.672  26.337 1.00 60.66  ? 359 LYS A CE     1 
ATOM   2753  N NZ     . LYS A 1 359 ? -6.310  27.276  27.670 1.00 47.62  ? 359 LYS A NZ     1 
ATOM   2754  N N      . GLN A 1 360 ? -11.173 24.055  28.038 1.00 40.27  ? 360 GLN A N      1 
ATOM   2755  C CA     . GLN A 1 360 ? -11.867 24.645  29.158 1.00 48.56  ? 360 GLN A CA     1 
ATOM   2756  C C      . GLN A 1 360 ? -11.377 23.983  30.406 1.00 56.48  ? 360 GLN A C      1 
ATOM   2757  O O      . GLN A 1 360 ? -11.104 24.625  31.394 1.00 53.48  ? 360 GLN A O      1 
ATOM   2758  C CB     . GLN A 1 360 ? -13.358 24.414  29.017 1.00 49.82  ? 360 GLN A CB     1 
ATOM   2759  C CG     . GLN A 1 360 ? -14.208 25.205  29.991 1.00 59.58  ? 360 GLN A CG     1 
ATOM   2760  C CD     . GLN A 1 360 ? -15.669 24.841  29.886 1.00 68.57  ? 360 GLN A CD     1 
ATOM   2761  O OE1    . GLN A 1 360 ? -16.014 23.763  29.406 1.00 73.50  ? 360 GLN A OE1    1 
ATOM   2762  N NE2    . GLN A 1 360 ? -16.537 25.736  30.337 1.00 73.47  ? 360 GLN A NE2    1 
ATOM   2763  N N      . GLU A 1 361 ? -11.224 22.680  30.364 1.00 54.59  ? 361 GLU A N      1 
ATOM   2764  C CA     . GLU A 1 361 ? -10.835 21.961  31.554 1.00 44.57  ? 361 GLU A CA     1 
ATOM   2765  C C      . GLU A 1 361 ? -9.370  22.064  31.820 1.00 45.91  ? 361 GLU A C      1 
ATOM   2766  O O      . GLU A 1 361 ? -8.962  21.963  32.961 1.00 56.26  ? 361 GLU A O      1 
ATOM   2767  C CB     . GLU A 1 361 ? -11.266 20.517  31.457 1.00 42.97  ? 361 GLU A CB     1 
ATOM   2768  C CG     . GLU A 1 361 ? -12.756 20.337  31.652 1.00 49.42  ? 361 GLU A CG     1 
ATOM   2769  C CD     . GLU A 1 361 ? -13.170 18.890  31.593 1.00 52.24  ? 361 GLU A CD     1 
ATOM   2770  O OE1    . GLU A 1 361 ? -12.414 18.095  31.012 1.00 49.11  ? 361 GLU A OE1    1 
ATOM   2771  O OE2    . GLU A 1 361 ? -14.246 18.552  32.122 1.00 47.80  ? 361 GLU A OE2    1 
ATOM   2772  N N      . TYR A 1 362 ? -8.564  22.240  30.781 1.00 43.69  ? 362 TYR A N      1 
ATOM   2773  C CA     . TYR A 1 362 ? -7.137  22.412  30.972 1.00 42.35  ? 362 TYR A CA     1 
ATOM   2774  C C      . TYR A 1 362 ? -6.954  23.587  31.847 1.00 54.05  ? 362 TYR A C      1 
ATOM   2775  O O      . TYR A 1 362 ? -6.238  23.532  32.829 1.00 60.52  ? 362 TYR A O      1 
ATOM   2776  C CB     . TYR A 1 362 ? -6.403  22.690  29.693 1.00 36.92  ? 362 TYR A CB     1 
ATOM   2777  C CG     . TYR A 1 362 ? -4.936  22.966  29.891 1.00 40.10  ? 362 TYR A CG     1 
ATOM   2778  C CD1    . TYR A 1 362 ? -4.064  21.955  30.244 1.00 45.22  ? 362 TYR A CD1    1 
ATOM   2779  C CD2    . TYR A 1 362 ? -4.421  24.236  29.721 1.00 45.67  ? 362 TYR A CD2    1 
ATOM   2780  C CE1    . TYR A 1 362 ? -2.723  22.205  30.424 1.00 41.89  ? 362 TYR A CE1    1 
ATOM   2781  C CE2    . TYR A 1 362 ? -3.081  24.490  29.906 1.00 44.88  ? 362 TYR A CE2    1 
ATOM   2782  C CZ     . TYR A 1 362 ? -2.240  23.470  30.257 1.00 42.04  ? 362 TYR A CZ     1 
ATOM   2783  O OH     . TYR A 1 362 ? -0.910  23.727  30.437 1.00 45.79  ? 362 TYR A OH     1 
ATOM   2784  N N      . ASP A 1 363 ? -7.597  24.683  31.497 1.00 55.71  ? 363 ASP A N      1 
ATOM   2785  C CA     . ASP A 1 363 ? -7.388  25.894  32.256 1.00 53.50  ? 363 ASP A CA     1 
ATOM   2786  C C      . ASP A 1 363 ? -7.893  25.736  33.668 1.00 59.43  ? 363 ASP A C      1 
ATOM   2787  O O      . ASP A 1 363 ? -7.326  26.284  34.599 1.00 66.77  ? 363 ASP A O      1 
ATOM   2788  C CB     . ASP A 1 363 ? -7.955  27.118  31.537 1.00 49.37  ? 363 ASP A CB     1 
ATOM   2789  C CG     . ASP A 1 363 ? -9.444  27.092  31.388 1.00 62.23  ? 363 ASP A CG     1 
ATOM   2790  O OD1    . ASP A 1 363 ? -10.170 27.115  32.403 1.00 66.59  ? 363 ASP A OD1    1 
ATOM   2791  O OD2    . ASP A 1 363 ? -9.897  27.103  30.231 1.00 75.37  ? 363 ASP A OD2    1 
ATOM   2792  N N      . GLU A 1 364 ? -8.955  24.994  33.847 1.00 59.57  ? 364 GLU A N      1 
ATOM   2793  C CA     . GLU A 1 364 ? -9.480  24.876  35.171 1.00 61.20  ? 364 GLU A CA     1 
ATOM   2794  C C      . GLU A 1 364 ? -8.540  24.072  36.013 1.00 65.69  ? 364 GLU A C      1 
ATOM   2795  O O      . GLU A 1 364 ? -8.278  24.434  37.144 1.00 77.82  ? 364 GLU A O      1 
ATOM   2796  C CB     . GLU A 1 364 ? -10.847 24.208  35.181 1.00 65.32  ? 364 GLU A CB     1 
ATOM   2797  C CG     . GLU A 1 364 ? -11.967 24.988  34.520 1.00 68.55  ? 364 GLU A CG     1 
ATOM   2798  C CD     . GLU A 1 364 ? -13.275 24.223  34.543 1.00 81.50  ? 364 GLU A CD     1 
ATOM   2799  O OE1    . GLU A 1 364 ? -13.336 23.175  35.220 1.00 83.43  ? 364 GLU A OE1    1 
ATOM   2800  O OE2    . GLU A 1 364 ? -14.245 24.661  33.891 1.00 75.08  ? 364 GLU A OE2    1 
ATOM   2801  N N      . SER A 1 365 ? -8.038  22.964  35.502 1.00 53.93  ? 365 SER A N      1 
ATOM   2802  C CA     . SER A 1 365 ? -7.231  22.119  36.377 1.00 67.50  ? 365 SER A CA     1 
ATOM   2803  C C      . SER A 1 365 ? -5.761  21.991  36.159 1.00 62.04  ? 365 SER A C      1 
ATOM   2804  O O      . SER A 1 365 ? -5.063  21.375  36.948 1.00 60.77  ? 365 SER A O      1 
ATOM   2805  C CB     . SER A 1 365 ? -7.819  20.730  36.456 1.00 77.48  ? 365 SER A CB     1 
ATOM   2806  O OG     . SER A 1 365 ? -7.245  20.000  37.526 1.00 79.23  ? 365 SER A OG     1 
ATOM   2807  N N      . GLY A 1 366 ? -5.268  22.592  35.117 1.00 51.92  ? 366 GLY A N      1 
ATOM   2808  C CA     . GLY A 1 366 ? -3.858  22.569  34.934 1.00 52.91  ? 366 GLY A CA     1 
ATOM   2809  C C      . GLY A 1 366 ? -3.462  21.393  34.137 1.00 48.01  ? 366 GLY A C      1 
ATOM   2810  O O      . GLY A 1 366 ? -4.288  20.668  33.633 1.00 47.15  ? 366 GLY A O      1 
ATOM   2811  N N      . PRO A 1 367 ? -2.177  21.175  34.045 1.00 44.25  ? 367 PRO A N      1 
ATOM   2812  C CA     . PRO A 1 367 ? -1.697  20.098  33.228 1.00 49.69  ? 367 PRO A CA     1 
ATOM   2813  C C      . PRO A 1 367 ? -2.087  18.777  33.838 1.00 51.05  ? 367 PRO A C      1 
ATOM   2814  O O      . PRO A 1 367 ? -1.984  17.767  33.184 1.00 52.97  ? 367 PRO A O      1 
ATOM   2815  C CB     . PRO A 1 367 ? -0.199  20.320  33.260 1.00 47.39  ? 367 PRO A CB     1 
ATOM   2816  C CG     . PRO A 1 367 ? -0.010  21.756  33.551 1.00 43.43  ? 367 PRO A CG     1 
ATOM   2817  C CD     . PRO A 1 367 ? -1.089  22.027  34.537 1.00 43.86  ? 367 PRO A CD     1 
ATOM   2818  N N      . SER A 1 368 ? -2.553  18.771  35.061 1.00 47.73  ? 368 SER A N      1 
ATOM   2819  C CA     . SER A 1 368 ? -2.860  17.550  35.750 1.00 44.60  ? 368 SER A CA     1 
ATOM   2820  C C      . SER A 1 368 ? -4.256  17.024  35.556 1.00 48.74  ? 368 SER A C      1 
ATOM   2821  O O      . SER A 1 368 ? -4.683  16.156  36.293 1.00 50.46  ? 368 SER A O      1 
ATOM   2822  C CB     . SER A 1 368 ? -2.628  17.772  37.216 1.00 44.76  ? 368 SER A CB     1 
ATOM   2823  O OG     . SER A 1 368 ? -1.354  18.341  37.439 1.00 52.47  ? 368 SER A OG     1 
ATOM   2824  N N      . ILE A 1 369 ? -5.004  17.575  34.614 1.00 44.55  ? 369 ILE A N      1 
ATOM   2825  C CA     . ILE A 1 369 ? -6.333  17.065  34.308 1.00 43.44  ? 369 ILE A CA     1 
ATOM   2826  C C      . ILE A 1 369 ? -6.143  15.775  33.576 1.00 50.83  ? 369 ILE A C      1 
ATOM   2827  O O      . ILE A 1 369 ? -7.050  14.975  33.439 1.00 53.76  ? 369 ILE A O      1 
ATOM   2828  C CB     . ILE A 1 369 ? -7.134  18.056  33.475 1.00 36.69  ? 369 ILE A CB     1 
ATOM   2829  C CG1    . ILE A 1 369 ? -8.568  17.593  33.251 1.00 39.05  ? 369 ILE A CG1    1 
ATOM   2830  C CG2    . ILE A 1 369 ? -6.421  18.349  32.170 1.00 42.60  ? 369 ILE A CG2    1 
ATOM   2831  C CD1    . ILE A 1 369 ? -9.364  17.472  34.524 1.00 41.06  ? 369 ILE A CD1    1 
ATOM   2832  N N      . VAL A 1 370 ? -4.933  15.530  33.132 1.00 50.82  ? 370 VAL A N      1 
ATOM   2833  C CA     . VAL A 1 370 ? -4.695  14.360  32.368 1.00 49.19  ? 370 VAL A CA     1 
ATOM   2834  C C      . VAL A 1 370 ? -5.052  13.226  33.243 1.00 48.65  ? 370 VAL A C      1 
ATOM   2835  O O      . VAL A 1 370 ? -5.801  12.368  32.857 1.00 54.61  ? 370 VAL A O      1 
ATOM   2836  C CB     . VAL A 1 370 ? -3.221  14.288  31.951 1.00 47.19  ? 370 VAL A CB     1 
ATOM   2837  C CG1    . VAL A 1 370 ? -2.269  14.626  33.076 1.00 44.58  ? 370 VAL A CG1    1 
ATOM   2838  C CG2    . VAL A 1 370 ? -2.893  12.954  31.327 1.00 56.07  ? 370 VAL A CG2    1 
ATOM   2839  N N      . HIS A 1 371 ? -4.644  13.265  34.480 1.00 46.84  ? 371 HIS A N      1 
ATOM   2840  C CA     . HIS A 1 371 ? -4.840  12.141  35.337 1.00 50.21  ? 371 HIS A CA     1 
ATOM   2841  C C      . HIS A 1 371 ? -6.273  11.820  35.569 1.00 48.82  ? 371 HIS A C      1 
ATOM   2842  O O      . HIS A 1 371 ? -6.642  10.671  35.633 1.00 51.93  ? 371 HIS A O      1 
ATOM   2843  C CB     . HIS A 1 371 ? -4.145  12.449  36.630 1.00 49.21  ? 371 HIS A CB     1 
ATOM   2844  C CG     . HIS A 1 371 ? -2.698  12.776  36.469 1.00 48.30  ? 371 HIS A CG     1 
ATOM   2845  N ND1    . HIS A 1 371 ? -1.875  12.091  35.608 1.00 54.70  ? 371 HIS A ND1    1 
ATOM   2846  C CD2    . HIS A 1 371 ? -1.922  13.701  37.075 1.00 46.18  ? 371 HIS A CD2    1 
ATOM   2847  C CE1    . HIS A 1 371 ? -0.655  12.585  35.682 1.00 51.68  ? 371 HIS A CE1    1 
ATOM   2848  N NE2    . HIS A 1 371 ? -0.657  13.562  36.566 1.00 47.00  ? 371 HIS A NE2    1 
ATOM   2849  N N      . ARG A 1 372 ? -7.087  12.828  35.746 1.00 49.69  ? 372 ARG A N      1 
ATOM   2850  C CA     . ARG A 1 372 ? -8.505  12.635  35.968 1.00 51.00  ? 372 ARG A CA     1 
ATOM   2851  C C      . ARG A 1 372 ? -9.281  12.090  34.820 1.00 49.73  ? 372 ARG A C      1 
ATOM   2852  O O      . ARG A 1 372 ? -10.229 11.367  35.016 1.00 52.72  ? 372 ARG A O      1 
ATOM   2853  C CB     . ARG A 1 372 ? -9.146  13.929  36.407 1.00 55.45  ? 372 ARG A CB     1 
ATOM   2854  C CG     . ARG A 1 372 ? -8.405  14.644  37.518 1.00 54.20  ? 372 ARG A CG     1 
ATOM   2855  C CD     . ARG A 1 372 ? -9.392  15.323  38.445 1.00 61.93  ? 372 ARG A CD     1 
ATOM   2856  N NE     . ARG A 1 372 ? -8.762  16.349  39.263 1.00 76.79  ? 372 ARG A NE     1 
ATOM   2857  C CZ     . ARG A 1 372 ? -8.815  17.649  38.998 1.00 91.26  ? 372 ARG A CZ     1 
ATOM   2858  N NH1    . ARG A 1 372 ? -9.482  18.086  37.942 1.00 72.63  ? 372 ARG A NH1    1 
ATOM   2859  N NH2    . ARG A 1 372 ? -8.213  18.514  39.798 1.00 101.55 ? 372 ARG A NH2    1 
ATOM   2860  N N      . LYS A 1 373 ? -8.956  12.515  33.619 1.00 48.18  ? 373 LYS A N      1 
ATOM   2861  C CA     . LYS A 1 373 ? -9.710  12.074  32.471 1.00 50.91  ? 373 LYS A CA     1 
ATOM   2862  C C      . LYS A 1 373 ? -9.073  10.973  31.678 1.00 49.60  ? 373 LYS A C      1 
ATOM   2863  O O      . LYS A 1 373 ? -9.700  9.969   31.388 1.00 48.91  ? 373 LYS A O      1 
ATOM   2864  C CB     . LYS A 1 373 ? -9.939  13.257  31.540 1.00 48.73  ? 373 LYS A CB     1 
ATOM   2865  C CG     . LYS A 1 373 ? -10.643 14.431  32.170 1.00 46.53  ? 373 LYS A CG     1 
ATOM   2866  C CD     . LYS A 1 373 ? -11.562 15.070  31.155 1.00 42.43  ? 373 LYS A CD     1 
ATOM   2867  C CE     . LYS A 1 373 ? -12.838 14.269  31.000 1.00 49.15  ? 373 LYS A CE     1 
ATOM   2868  N NZ     . LYS A 1 373 ? -13.614 14.260  32.270 1.00 43.42  ? 373 LYS A NZ     1 
ATOM   2869  N N      . CYS A 1 374 ? -7.820  11.161  31.321 1.00 52.52  ? 374 CYS A N      1 
ATOM   2870  C CA     . CYS A 1 374 ? -7.133  10.193  30.521 1.00 60.42  ? 374 CYS A CA     1 
ATOM   2871  C C      . CYS A 1 374 ? -6.186  9.430   31.390 1.00 70.17  ? 374 CYS A C      1 
ATOM   2872  O O      . CYS A 1 374 ? -5.130  9.916   31.738 1.00 71.68  ? 374 CYS A O      1 
ATOM   2873  C CB     . CYS A 1 374 ? -6.277  10.895  29.502 1.00 52.74  ? 374 CYS A CB     1 
ATOM   2874  S SG     . CYS A 1 374 ? -7.005  12.358  28.807 1.00 64.05  ? 374 CYS A SG     1 
ATOM   2875  N N      . PHE A 1 375 ? -6.520  8.194   31.689 1.00 71.58  ? 375 PHE A N      1 
ATOM   2876  C CA     . PHE A 1 375 ? -5.658  7.404   32.502 1.00 69.86  ? 375 PHE A CA     1 
ATOM   2877  C C      . PHE A 1 375 ? -4.636  6.942   31.493 1.00 78.84  ? 375 PHE A C      1 
ATOM   2878  O O      . PHE A 1 375 ? -3.694  6.218   31.793 1.00 87.05  ? 375 PHE A O      1 
ATOM   2879  C CB     . PHE A 1 375 ? -6.415  6.230   33.121 1.00 63.62  ? 375 PHE A CB     1 
ATOM   2880  C CG     . PHE A 1 375 ? -7.706  6.604   33.787 1.00 56.37  ? 375 PHE A CG     1 
ATOM   2881  C CD1    . PHE A 1 375 ? -7.712  7.243   35.007 1.00 51.96  ? 375 PHE A CD1    1 
ATOM   2882  C CD2    . PHE A 1 375 ? -8.915  6.273   33.206 1.00 57.63  ? 375 PHE A CD2    1 
ATOM   2883  C CE1    . PHE A 1 375 ? -8.899  7.571   35.625 1.00 51.15  ? 375 PHE A CE1    1 
ATOM   2884  C CE2    . PHE A 1 375 ? -10.105 6.598   33.819 1.00 52.27  ? 375 PHE A CE2    1 
ATOM   2885  C CZ     . PHE A 1 375 ? -10.097 7.246   35.033 1.00 41.70  ? 375 PHE A CZ     1 
ATOM   2886  O OXT    . PHE A 1 375 ? -4.739  7.292   30.333 1.00 63.01  ? 375 PHE A OXT    1 
ATOM   2887  N N      . ILE B 1 5   ? 39.209  36.560  11.547 1.00 45.64  ? 5   ILE B N      1 
ATOM   2888  C CA     . ILE B 1 5   ? 40.111  37.306  12.399 1.00 57.49  ? 5   ILE B CA     1 
ATOM   2889  C C      . ILE B 1 5   ? 39.469  38.617  12.727 1.00 52.55  ? 5   ILE B C      1 
ATOM   2890  O O      . ILE B 1 5   ? 39.827  39.273  13.690 1.00 58.57  ? 5   ILE B O      1 
ATOM   2891  C CB     . ILE B 1 5   ? 41.481  37.534  11.727 1.00 62.31  ? 5   ILE B CB     1 
ATOM   2892  C CG1    . ILE B 1 5   ? 42.604  37.534  12.768 1.00 63.08  ? 5   ILE B CG1    1 
ATOM   2893  C CG2    . ILE B 1 5   ? 41.506  38.807  10.892 1.00 48.39  ? 5   ILE B CG2    1 
ATOM   2894  C CD1    . ILE B 1 5   ? 43.988  37.670  12.176 1.00 50.78  ? 5   ILE B CD1    1 
ATOM   2895  N N      . ALA B 1 6   ? 38.473  38.986  11.960 1.00 51.53  ? 6   ALA B N      1 
ATOM   2896  C CA     . ALA B 1 6   ? 37.860  40.267  12.158 1.00 48.39  ? 6   ALA B CA     1 
ATOM   2897  C C      . ALA B 1 6   ? 36.936  40.220  13.314 1.00 43.21  ? 6   ALA B C      1 
ATOM   2898  O O      . ALA B 1 6   ? 36.496  39.167  13.718 1.00 44.62  ? 6   ALA B O      1 
ATOM   2899  C CB     . ALA B 1 6   ? 37.128  40.689  10.910 1.00 53.31  ? 6   ALA B CB     1 
ATOM   2900  N N      . ALA B 1 7   ? 36.638  41.377  13.860 1.00 35.89  ? 7   ALA B N      1 
ATOM   2901  C CA     . ALA B 1 7   ? 35.823  41.416  15.019 1.00 35.31  ? 7   ALA B CA     1 
ATOM   2902  C C      . ALA B 1 7   ? 34.519  41.982  14.643 1.00 37.82  ? 7   ALA B C      1 
ATOM   2903  O O      . ALA B 1 7   ? 34.440  43.066  14.103 1.00 39.26  ? 7   ALA B O      1 
ATOM   2904  C CB     . ALA B 1 7   ? 36.477  42.252  16.072 1.00 36.82  ? 7   ALA B CB     1 
ATOM   2905  N N      . LEU B 1 8   ? 33.471  41.252  14.919 1.00 31.45  ? 8   LEU B N      1 
ATOM   2906  C CA     . LEU B 1 8   ? 32.184  41.678  14.534 1.00 30.45  ? 8   LEU B CA     1 
ATOM   2907  C C      . LEU B 1 8   ? 31.776  42.712  15.518 1.00 31.71  ? 8   LEU B C      1 
ATOM   2908  O O      . LEU B 1 8   ? 32.103  42.600  16.673 1.00 40.40  ? 8   LEU B O      1 
ATOM   2909  C CB     . LEU B 1 8   ? 31.289  40.482  14.628 1.00 34.62  ? 8   LEU B CB     1 
ATOM   2910  C CG     . LEU B 1 8   ? 31.735  39.225  13.896 1.00 34.91  ? 8   LEU B CG     1 
ATOM   2911  C CD1    . LEU B 1 8   ? 30.820  38.068  14.252 1.00 32.87  ? 8   LEU B CD1    1 
ATOM   2912  C CD2    . LEU B 1 8   ? 31.730  39.471  12.400 1.00 36.01  ? 8   LEU B CD2    1 
ATOM   2913  N N      . VAL B 1 9   ? 31.051  43.724  15.078 1.00 31.08  ? 9   VAL B N      1 
ATOM   2914  C CA     . VAL B 1 9   ? 30.613  44.791  15.956 1.00 32.08  ? 9   VAL B CA     1 
ATOM   2915  C C      . VAL B 1 9   ? 29.106  44.841  15.815 1.00 33.15  ? 9   VAL B C      1 
ATOM   2916  O O      . VAL B 1 9   ? 28.601  44.495  14.770 1.00 36.65  ? 9   VAL B O      1 
ATOM   2917  C CB     . VAL B 1 9   ? 31.236  46.121  15.527 1.00 32.83  ? 9   VAL B CB     1 
ATOM   2918  C CG1    . VAL B 1 9   ? 30.941  47.203  16.548 1.00 33.16  ? 9   VAL B CG1    1 
ATOM   2919  C CG2    . VAL B 1 9   ? 32.733  45.970  15.331 1.00 33.85  ? 9   VAL B CG2    1 
ATOM   2920  N N      . ILE B 1 10  ? 28.363  45.208  16.844 1.00 29.59  ? 10  ILE B N      1 
ATOM   2921  C CA     . ILE B 1 10  ? 26.928  45.180  16.694 1.00 32.19  ? 10  ILE B CA     1 
ATOM   2922  C C      . ILE B 1 10  ? 26.212  46.117  17.595 1.00 40.22  ? 10  ILE B C      1 
ATOM   2923  O O      . ILE B 1 10  ? 26.368  46.048  18.793 1.00 43.34  ? 10  ILE B O      1 
ATOM   2924  C CB     . ILE B 1 10  ? 26.356  43.776  16.856 1.00 32.63  ? 10  ILE B CB     1 
ATOM   2925  C CG1    . ILE B 1 10  ? 24.841  43.795  16.691 1.00 31.33  ? 10  ILE B CG1    1 
ATOM   2926  C CG2    . ILE B 1 10  ? 26.752  43.179  18.194 1.00 38.36  ? 10  ILE B CG2    1 
ATOM   2927  C CD1    . ILE B 1 10  ? 24.239  42.417  16.571 1.00 27.43  ? 10  ILE B CD1    1 
ATOM   2928  N N      . ASP B 1 11  ? 25.404  46.995  17.018 1.00 42.93  ? 11  ASP B N      1 
ATOM   2929  C CA     . ASP B 1 11  ? 24.725  47.997  17.788 1.00 47.48  ? 11  ASP B CA     1 
ATOM   2930  C C      . ASP B 1 11  ? 23.389  47.388  17.948 1.00 46.41  ? 11  ASP B C      1 
ATOM   2931  O O      . ASP B 1 11  ? 22.648  47.278  16.997 1.00 42.38  ? 11  ASP B O      1 
ATOM   2932  C CB     . ASP B 1 11  ? 24.679  49.322  17.066 1.00 36.22  ? 11  ASP B CB     1 
ATOM   2933  C CG     . ASP B 1 11  ? 24.739  50.498  18.001 1.00 37.96  ? 11  ASP B CG     1 
ATOM   2934  O OD1    . ASP B 1 11  ? 24.739  50.289  19.221 1.00 38.38  ? 11  ASP B OD1    1 
ATOM   2935  O OD2    . ASP B 1 11  ? 24.787  51.640  17.514 1.00 51.15  ? 11  ASP B OD2    1 
ATOM   2936  N N      . ASN B 1 12  ? 23.110  46.928  19.149 1.00 50.37  ? 12  ASN B N      1 
ATOM   2937  C CA     . ASN B 1 12  ? 21.856  46.324  19.456 1.00 49.71  ? 12  ASN B CA     1 
ATOM   2938  C C      . ASN B 1 12  ? 20.982  47.499  19.643 1.00 48.45  ? 12  ASN B C      1 
ATOM   2939  O O      . ASN B 1 12  ? 20.679  47.876  20.761 1.00 53.70  ? 12  ASN B O      1 
ATOM   2940  C CB     . ASN B 1 12  ? 22.013  45.575  20.766 1.00 46.51  ? 12  ASN B CB     1 
ATOM   2941  C CG     . ASN B 1 12  ? 23.037  44.466  20.681 1.00 50.24  ? 12  ASN B CG     1 
ATOM   2942  O OD1    . ASN B 1 12  ? 23.308  43.948  19.607 1.00 52.39  ? 12  ASN B OD1    1 
ATOM   2943  N ND2    . ASN B 1 12  ? 23.598  44.087  21.816 1.00 47.43  ? 12  ASN B ND2    1 
ATOM   2944  N N      . GLY B 1 13  ? 20.573  48.102  18.559 1.00 42.70  ? 13  GLY B N      1 
ATOM   2945  C CA     . GLY B 1 13  ? 19.819  49.311  18.667 1.00 46.18  ? 13  GLY B CA     1 
ATOM   2946  C C      . GLY B 1 13  ? 18.362  49.224  18.942 1.00 49.21  ? 13  GLY B C      1 
ATOM   2947  O O      . GLY B 1 13  ? 17.772  48.169  18.830 1.00 49.29  ? 13  GLY B O      1 
ATOM   2948  N N      . SER B 1 14  ? 17.764  50.355  19.257 1.00 59.96  ? 14  SER B N      1 
ATOM   2949  C CA     . SER B 1 14  ? 16.359  50.396  19.580 1.00 61.70  ? 14  SER B CA     1 
ATOM   2950  C C      . SER B 1 14  ? 15.499  50.000  18.420 1.00 58.24  ? 14  SER B C      1 
ATOM   2951  O O      . SER B 1 14  ? 14.614  49.176  18.553 1.00 59.15  ? 14  SER B O      1 
ATOM   2952  C CB     . SER B 1 14  ? 15.986  51.796  20.038 1.00 55.88  ? 14  SER B CB     1 
ATOM   2953  O OG     . SER B 1 14  ? 14.659  51.820  20.529 1.00 58.44  ? 14  SER B OG     1 
ATOM   2954  N N      . GLY B 1 15  ? 15.780  50.555  17.262 1.00 53.92  ? 15  GLY B N      1 
ATOM   2955  C CA     . GLY B 1 15  ? 14.959  50.277  16.111 1.00 54.38  ? 15  GLY B CA     1 
ATOM   2956  C C      . GLY B 1 15  ? 15.719  49.669  14.979 1.00 52.54  ? 15  GLY B C      1 
ATOM   2957  O O      . GLY B 1 15  ? 15.150  48.968  14.161 1.00 51.71  ? 15  GLY B O      1 
ATOM   2958  N N      . MET B 1 16  ? 17.012  49.914  14.933 1.00 45.90  ? 16  MET B N      1 
ATOM   2959  C CA     . MET B 1 16  ? 17.801  49.318  13.893 1.00 47.90  ? 16  MET B CA     1 
ATOM   2960  C C      . MET B 1 16  ? 19.123  48.738  14.317 1.00 39.75  ? 16  MET B C      1 
ATOM   2961  O O      . MET B 1 16  ? 19.982  49.445  14.809 1.00 39.25  ? 16  MET B O      1 
ATOM   2962  C CB     . MET B 1 16  ? 17.987  50.296  12.737 1.00 48.82  ? 16  MET B CB     1 
ATOM   2963  C CG     . MET B 1 16  ? 16.729  50.559  11.945 1.00 48.16  ? 16  MET B CG     1 
ATOM   2964  S SD     . MET B 1 16  ? 17.127  50.909  10.232 1.00 96.44  ? 16  MET B SD     1 
ATOM   2965  C CE     . MET B 1 16  ? 15.493  50.884  9.499  1.00 73.43  ? 16  MET B CE     1 
ATOM   2966  N N      . CYS B 1 17  ? 19.284  47.444  14.122 1.00 40.40  ? 17  CYS B N      1 
ATOM   2967  C CA     . CYS B 1 17  ? 20.520  46.802  14.448 1.00 35.49  ? 17  CYS B CA     1 
ATOM   2968  C C      . CYS B 1 17  ? 21.485  47.146  13.396 1.00 35.70  ? 17  CYS B C      1 
ATOM   2969  O O      . CYS B 1 17  ? 21.186  47.048  12.229 1.00 42.87  ? 17  CYS B O      1 
ATOM   2970  C CB     . CYS B 1 17  ? 20.343  45.314  14.469 1.00 34.16  ? 17  CYS B CB     1 
ATOM   2971  S SG     . CYS B 1 17  ? 21.851  44.423  14.857 1.00 70.62  ? 17  CYS B SG     1 
ATOM   2972  N N      . LYS B 1 18  ? 22.681  47.502  13.808 1.00 32.95  ? 18  LYS B N      1 
ATOM   2973  C CA     . LYS B 1 18  ? 23.667  47.953  12.885 1.00 34.41  ? 18  LYS B CA     1 
ATOM   2974  C C      . LYS B 1 18  ? 24.901  47.188  13.141 1.00 32.48  ? 18  LYS B C      1 
ATOM   2975  O O      . LYS B 1 18  ? 25.504  47.359  14.173 1.00 32.97  ? 18  LYS B O      1 
ATOM   2976  C CB     . LYS B 1 18  ? 23.896  49.425  13.114 1.00 37.58  ? 18  LYS B CB     1 
ATOM   2977  C CG     . LYS B 1 18  ? 22.666  50.278  12.896 1.00 34.71  ? 18  LYS B CG     1 
ATOM   2978  C CD     . LYS B 1 18  ? 22.974  51.741  13.116 1.00 47.18  ? 18  LYS B CD     1 
ATOM   2979  C CE     . LYS B 1 18  ? 23.158  52.027  14.586 1.00 46.32  ? 18  LYS B CE     1 
ATOM   2980  N NZ     . LYS B 1 18  ? 21.905  51.706  15.310 1.00 43.80  ? 18  LYS B NZ     1 
ATOM   2981  N N      . ALA B 1 19  ? 25.315  46.368  12.190 1.00 34.09  ? 19  ALA B N      1 
ATOM   2982  C CA     . ALA B 1 19  ? 26.431  45.479  12.396 1.00 31.51  ? 19  ALA B CA     1 
ATOM   2983  C C      . ALA B 1 19  ? 27.416  45.418  11.301 1.00 30.51  ? 19  ALA B C      1 
ATOM   2984  O O      . ALA B 1 19  ? 27.147  45.809  10.202 1.00 37.96  ? 19  ALA B O      1 
ATOM   2985  C CB     . ALA B 1 19  ? 25.909  44.105  12.610 1.00 26.55  ? 19  ALA B CB     1 
ATOM   2986  N N      . GLY B 1 20  ? 28.575  44.893  11.595 1.00 25.65  ? 20  GLY B N      1 
ATOM   2987  C CA     . GLY B 1 20  ? 29.596  44.885  10.616 1.00 33.12  ? 20  GLY B CA     1 
ATOM   2988  C C      . GLY B 1 20  ? 30.914  44.400  11.088 1.00 35.68  ? 20  GLY B C      1 
ATOM   2989  O O      . GLY B 1 20  ? 31.014  43.801  12.131 1.00 33.71  ? 20  GLY B O      1 
ATOM   2990  N N      . PHE B 1 21  ? 31.932  44.641  10.296 1.00 37.24  ? 21  PHE B N      1 
ATOM   2991  C CA     . PHE B 1 21  ? 33.240  44.173  10.607 1.00 37.41  ? 21  PHE B CA     1 
ATOM   2992  C C      . PHE B 1 21  ? 34.124  45.301  11.048 1.00 48.80  ? 21  PHE B C      1 
ATOM   2993  O O      . PHE B 1 21  ? 33.829  46.443  10.769 1.00 55.71  ? 21  PHE B O      1 
ATOM   2994  C CB     . PHE B 1 21  ? 33.785  43.488  9.390  1.00 41.40  ? 21  PHE B CB     1 
ATOM   2995  C CG     . PHE B 1 21  ? 32.925  42.359  8.910  1.00 50.08  ? 21  PHE B CG     1 
ATOM   2996  C CD1    . PHE B 1 21  ? 33.107  41.085  9.401  1.00 44.77  ? 21  PHE B CD1    1 
ATOM   2997  C CD2    . PHE B 1 21  ? 31.926  42.577  7.985  1.00 43.31  ? 21  PHE B CD2    1 
ATOM   2998  C CE1    . PHE B 1 21  ? 32.315  40.047  8.972  1.00 36.86  ? 21  PHE B CE1    1 
ATOM   2999  C CE2    . PHE B 1 21  ? 31.129  41.544  7.552  1.00 39.23  ? 21  PHE B CE2    1 
ATOM   3000  C CZ     . PHE B 1 21  ? 31.324  40.277  8.047  1.00 36.23  ? 21  PHE B CZ     1 
ATOM   3001  N N      . ALA B 1 22  ? 35.212  45.006  11.732 1.00 48.41  ? 22  ALA B N      1 
ATOM   3002  C CA     . ALA B 1 22  ? 36.045  46.042  12.315 1.00 47.10  ? 22  ALA B CA     1 
ATOM   3003  C C      . ALA B 1 22  ? 36.759  47.082  11.485 1.00 53.69  ? 22  ALA B C      1 
ATOM   3004  O O      . ALA B 1 22  ? 36.754  48.244  11.834 1.00 60.90  ? 22  ALA B O      1 
ATOM   3005  C CB     . ALA B 1 22  ? 37.055  45.371  13.181 1.00 38.44  ? 22  ALA B CB     1 
ATOM   3006  N N      . GLY B 1 23  ? 37.387  46.696  10.408 1.00 53.29  ? 23  GLY B N      1 
ATOM   3007  C CA     . GLY B 1 23  ? 38.100  47.635  9.574  1.00 59.71  ? 23  GLY B CA     1 
ATOM   3008  C C      . GLY B 1 23  ? 37.166  48.595  8.925  1.00 70.89  ? 23  GLY B C      1 
ATOM   3009  O O      . GLY B 1 23  ? 37.515  49.704  8.588  1.00 76.56  ? 23  GLY B O      1 
ATOM   3010  N N      . ASP B 1 24  ? 35.960  48.156  8.727  1.00 64.70  ? 24  ASP B N      1 
ATOM   3011  C CA     . ASP B 1 24  ? 34.999  48.958  8.051  1.00 64.50  ? 24  ASP B CA     1 
ATOM   3012  C C      . ASP B 1 24  ? 34.696  50.241  8.750  1.00 62.63  ? 24  ASP B C      1 
ATOM   3013  O O      . ASP B 1 24  ? 34.671  50.291  9.963  1.00 56.57  ? 24  ASP B O      1 
ATOM   3014  C CB     . ASP B 1 24  ? 33.699  48.166  7.930  1.00 58.82  ? 24  ASP B CB     1 
ATOM   3015  C CG     . ASP B 1 24  ? 33.804  46.990  6.998  1.00 63.22  ? 24  ASP B CG     1 
ATOM   3016  O OD1    . ASP B 1 24  ? 34.847  46.824  6.346  1.00 65.88  ? 24  ASP B OD1    1 
ATOM   3017  O OD2    . ASP B 1 24  ? 32.826  46.229  6.911  1.00 58.71  ? 24  ASP B OD2    1 
ATOM   3018  N N      . ASP B 1 25  ? 34.464  51.291  7.984  1.00 63.09  ? 25  ASP B N      1 
ATOM   3019  C CA     . ASP B 1 25  ? 34.110  52.574  8.530  1.00 64.47  ? 25  ASP B CA     1 
ATOM   3020  C C      . ASP B 1 25  ? 32.643  52.690  8.285  1.00 56.67  ? 25  ASP B C      1 
ATOM   3021  O O      . ASP B 1 25  ? 32.084  53.770  8.276  1.00 56.69  ? 25  ASP B O      1 
ATOM   3022  C CB     . ASP B 1 25  ? 34.852  53.681  7.798  1.00 66.29  ? 25  ASP B CB     1 
ATOM   3023  C CG     . ASP B 1 25  ? 34.748  55.019  8.495  1.00 71.38  ? 25  ASP B CG     1 
ATOM   3024  O OD1    . ASP B 1 25  ? 34.869  55.051  9.731  1.00 61.93  ? 25  ASP B OD1    1 
ATOM   3025  O OD2    . ASP B 1 25  ? 34.549  56.040  7.806  1.00 74.14  ? 25  ASP B OD2    1 
ATOM   3026  N N      . ALA B 1 26  ? 32.015  51.583  7.986  1.00 48.73  ? 26  ALA B N      1 
ATOM   3027  C CA     . ALA B 1 26  ? 30.598  51.624  7.826  1.00 44.09  ? 26  ALA B CA     1 
ATOM   3028  C C      . ALA B 1 26  ? 29.918  50.395  8.345  1.00 44.80  ? 26  ALA B C      1 
ATOM   3029  O O      . ALA B 1 26  ? 30.419  49.297  8.201  1.00 44.83  ? 26  ALA B O      1 
ATOM   3030  C CB     . ALA B 1 26  ? 30.287  51.777  6.388  1.00 47.72  ? 26  ALA B CB     1 
ATOM   3031  N N      . PRO B 1 27  ? 28.730  50.568  8.893  1.00 39.83  ? 27  PRO B N      1 
ATOM   3032  C CA     . PRO B 1 27  ? 28.079  49.358  9.308  1.00 36.04  ? 27  PRO B CA     1 
ATOM   3033  C C      . PRO B 1 27  ? 27.695  48.631  8.073  1.00 40.93  ? 27  PRO B C      1 
ATOM   3034  O O      . PRO B 1 27  ? 26.873  49.146  7.352  1.00 43.11  ? 27  PRO B O      1 
ATOM   3035  C CB     . PRO B 1 27  ? 26.826  49.893  9.933  1.00 32.68  ? 27  PRO B CB     1 
ATOM   3036  C CG     . PRO B 1 27  ? 27.247  51.163  10.554 1.00 40.16  ? 27  PRO B CG     1 
ATOM   3037  C CD     . PRO B 1 27  ? 28.145  51.758  9.519  1.00 40.27  ? 27  PRO B CD     1 
ATOM   3038  N N      . ARG B 1 28  ? 28.201  47.434  7.843  1.00 41.87  ? 28  ARG B N      1 
ATOM   3039  C CA     . ARG B 1 28  ? 27.930  46.752  6.604  1.00 42.49  ? 28  ARG B CA     1 
ATOM   3040  C C      . ARG B 1 28  ? 26.468  46.462  6.471  1.00 39.53  ? 28  ARG B C      1 
ATOM   3041  O O      . ARG B 1 28  ? 25.909  46.601  5.408  1.00 46.67  ? 28  ARG B O      1 
ATOM   3042  C CB     . ARG B 1 28  ? 28.730  45.472  6.524  1.00 39.84  ? 28  ARG B CB     1 
ATOM   3043  C CG     . ARG B 1 28  ? 28.984  44.958  5.119  1.00 53.03  ? 28  ARG B CG     1 
ATOM   3044  C CD     . ARG B 1 28  ? 30.275  45.517  4.544  1.00 55.20  ? 28  ARG B CD     1 
ATOM   3045  N NE     . ARG B 1 28  ? 31.408  44.609  4.709  1.00 63.18  ? 28  ARG B NE     1 
ATOM   3046  C CZ     . ARG B 1 28  ? 31.841  43.778  3.767  1.00 69.78  ? 28  ARG B CZ     1 
ATOM   3047  N NH1    . ARG B 1 28  ? 31.243  43.740  2.592  1.00 69.34  ? 28  ARG B NH1    1 
ATOM   3048  N NH2    . ARG B 1 28  ? 32.875  42.986  3.994  1.00 74.46  ? 28  ARG B NH2    1 
ATOM   3049  N N      . ALA B 1 29  ? 25.834  46.047  7.545  1.00 37.47  ? 29  ALA B N      1 
ATOM   3050  C CA     . ALA B 1 29  ? 24.438  45.684  7.477  1.00 37.40  ? 29  ALA B CA     1 
ATOM   3051  C C      . ALA B 1 29  ? 23.589  46.181  8.579  1.00 38.11  ? 29  ALA B C      1 
ATOM   3052  O O      . ALA B 1 29  ? 23.917  46.039  9.723  1.00 40.25  ? 29  ALA B O      1 
ATOM   3053  C CB     . ALA B 1 29  ? 24.319  44.215  7.426  1.00 40.42  ? 29  ALA B CB     1 
ATOM   3054  N N      . VAL B 1 30  ? 22.449  46.711  8.233  1.00 36.31  ? 30  VAL B N      1 
ATOM   3055  C CA     . VAL B 1 30  ? 21.565  47.251  9.205  1.00 35.50  ? 30  VAL B CA     1 
ATOM   3056  C C      . VAL B 1 30  ? 20.219  46.703  8.842  1.00 39.52  ? 30  VAL B C      1 
ATOM   3057  O O      . VAL B 1 30  ? 19.930  46.485  7.680  1.00 44.53  ? 30  VAL B O      1 
ATOM   3058  C CB     . VAL B 1 30  ? 21.539  48.768  9.096  1.00 37.66  ? 30  VAL B CB     1 
ATOM   3059  C CG1    . VAL B 1 30  ? 20.560  49.375  10.080 1.00 37.72  ? 30  VAL B CG1    1 
ATOM   3060  C CG2    . VAL B 1 30  ? 22.925  49.343  9.295  1.00 43.33  ? 30  VAL B CG2    1 
ATOM   3061  N N      . PHE B 1 31  ? 19.390  46.470  9.833  1.00 37.75  ? 31  PHE B N      1 
ATOM   3062  C CA     . PHE B 1 31  ? 18.098  45.954  9.577  1.00 44.61  ? 31  PHE B CA     1 
ATOM   3063  C C      . PHE B 1 31  ? 17.227  46.320  10.719 1.00 44.68  ? 31  PHE B C      1 
ATOM   3064  O O      . PHE B 1 31  ? 17.722  46.640  11.759 1.00 46.36  ? 31  PHE B O      1 
ATOM   3065  C CB     . PHE B 1 31  ? 18.158  44.449  9.428  1.00 48.70  ? 31  PHE B CB     1 
ATOM   3066  C CG     . PHE B 1 31  ? 18.830  43.729  10.559 1.00 45.45  ? 31  PHE B CG     1 
ATOM   3067  C CD1    . PHE B 1 31  ? 20.197  43.560  10.575 1.00 43.76  ? 31  PHE B CD1    1 
ATOM   3068  C CD2    . PHE B 1 31  ? 18.086  43.163  11.569 1.00 42.32  ? 31  PHE B CD2    1 
ATOM   3069  C CE1    . PHE B 1 31  ? 20.812  42.883  11.601 1.00 44.81  ? 31  PHE B CE1    1 
ATOM   3070  C CE2    . PHE B 1 31  ? 18.694  42.485  12.596 1.00 42.34  ? 31  PHE B CE2    1 
ATOM   3071  C CZ     . PHE B 1 31  ? 20.058  42.344  12.611 1.00 39.18  ? 31  PHE B CZ     1 
ATOM   3072  N N      . PRO B 1 32  ? 15.920  46.299  10.534 1.00 50.36  ? 32  PRO B N      1 
ATOM   3073  C CA     . PRO B 1 32  ? 15.091  46.558  11.698 1.00 46.37  ? 32  PRO B CA     1 
ATOM   3074  C C      . PRO B 1 32  ? 15.248  45.543  12.780 1.00 51.19  ? 32  PRO B C      1 
ATOM   3075  O O      . PRO B 1 32  ? 15.272  44.363  12.496 1.00 54.83  ? 32  PRO B O      1 
ATOM   3076  C CB     . PRO B 1 32  ? 13.694  46.402  11.147 1.00 48.63  ? 32  PRO B CB     1 
ATOM   3077  C CG     . PRO B 1 32  ? 13.794  46.920  9.772  1.00 58.51  ? 32  PRO B CG     1 
ATOM   3078  C CD     . PRO B 1 32  ? 15.096  46.363  9.298  1.00 61.03  ? 32  PRO B CD     1 
ATOM   3079  N N      . SER B 1 33  ? 15.341  45.988  14.023 1.00 55.42  ? 33  SER B N      1 
ATOM   3080  C CA     . SER B 1 33  ? 15.414  45.077  15.144 1.00 53.36  ? 33  SER B CA     1 
ATOM   3081  C C      . SER B 1 33  ? 14.020  44.714  15.518 1.00 59.75  ? 33  SER B C      1 
ATOM   3082  O O      . SER B 1 33  ? 13.470  45.271  16.456 1.00 60.01  ? 33  SER B O      1 
ATOM   3083  C CB     . SER B 1 33  ? 16.087  45.717  16.338 1.00 42.92  ? 33  SER B CB     1 
ATOM   3084  O OG     . SER B 1 33  ? 17.491  45.724  16.180 1.00 39.53  ? 33  SER B OG     1 
ATOM   3085  N N      . ILE B 1 34  ? 13.454  43.751  14.812 1.00 57.06  ? 34  ILE B N      1 
ATOM   3086  C CA     . ILE B 1 34  ? 12.092  43.361  15.054 1.00 57.68  ? 34  ILE B CA     1 
ATOM   3087  C C      . ILE B 1 34  ? 11.986  41.892  14.713 1.00 64.02  ? 34  ILE B C      1 
ATOM   3088  O O      . ILE B 1 34  ? 12.776  41.385  13.935 1.00 62.42  ? 34  ILE B O      1 
ATOM   3089  C CB     . ILE B 1 34  ? 11.199  44.215  14.171 1.00 61.09  ? 34  ILE B CB     1 
ATOM   3090  C CG1    . ILE B 1 34  ? 9.774   44.243  14.660 1.00 71.01  ? 34  ILE B CG1    1 
ATOM   3091  C CG2    . ILE B 1 34  ? 11.262  43.788  12.714 1.00 62.94  ? 34  ILE B CG2    1 
ATOM   3092  C CD1    . ILE B 1 34  ? 8.995   45.193  13.802 1.00 73.46  ? 34  ILE B CD1    1 
ATOM   3093  N N      . VAL B 1 35  ? 11.055  41.184  15.325 1.00 59.39  ? 35  VAL B N      1 
ATOM   3094  C CA     . VAL B 1 35  ? 10.952  39.766  15.103 1.00 50.37  ? 35  VAL B CA     1 
ATOM   3095  C C      . VAL B 1 35  ? 9.518   39.386  15.216 1.00 55.83  ? 35  VAL B C      1 
ATOM   3096  O O      . VAL B 1 35  ? 8.825   39.796  16.129 1.00 58.54  ? 35  VAL B O      1 
ATOM   3097  C CB     . VAL B 1 35  ? 11.789  38.989  16.114 1.00 53.30  ? 35  VAL B CB     1 
ATOM   3098  C CG1    . VAL B 1 35  ? 11.585  39.508  17.520 1.00 59.79  ? 35  VAL B CG1    1 
ATOM   3099  C CG2    . VAL B 1 35  ? 11.526  37.498  16.034 1.00 62.88  ? 35  VAL B CG2    1 
ATOM   3100  N N      . GLY B 1 36  ? 9.047   38.615  14.260 1.00 60.72  ? 36  GLY B N      1 
ATOM   3101  C CA     . GLY B 1 36  ? 7.657   38.252  14.262 1.00 60.75  ? 36  GLY B CA     1 
ATOM   3102  C C      . GLY B 1 36  ? 7.414   36.793  14.069 1.00 59.64  ? 36  GLY B C      1 
ATOM   3103  O O      . GLY B 1 36  ? 8.201   36.120  13.445 1.00 57.10  ? 36  GLY B O      1 
ATOM   3104  N N      . ARG B 1 37  ? 6.315   36.307  14.600 1.00 62.71  ? 37  ARG B N      1 
ATOM   3105  C CA     . ARG B 1 37  ? 5.993   34.920  14.487 1.00 63.74  ? 37  ARG B CA     1 
ATOM   3106  C C      . ARG B 1 37  ? 4.629   34.956  13.936 1.00 61.56  ? 37  ARG B C      1 
ATOM   3107  O O      . ARG B 1 37  ? 3.910   35.907  14.160 1.00 63.17  ? 37  ARG B O      1 
ATOM   3108  C CB     . ARG B 1 37  ? 5.973   34.291  15.856 1.00 62.02  ? 37  ARG B CB     1 
ATOM   3109  C CG     . ARG B 1 37  ? 7.325   34.258  16.537 1.00 61.18  ? 37  ARG B CG     1 
ATOM   3110  C CD     . ARG B 1 37  ? 7.242   33.561  17.879 1.00 60.40  ? 37  ARG B CD     1 
ATOM   3111  N NE     . ARG B 1 37  ? 8.566   33.273  18.407 1.00 57.05  ? 37  ARG B NE     1 
ATOM   3112  C CZ     . ARG B 1 37  ? 9.283   34.131  19.116 1.00 53.75  ? 37  ARG B CZ     1 
ATOM   3113  N NH1    . ARG B 1 37  ? 8.807   35.334  19.383 1.00 54.21  ? 37  ARG B NH1    1 
ATOM   3114  N NH2    . ARG B 1 37  ? 10.478  33.783  19.557 1.00 53.49  ? 37  ARG B NH2    1 
ATOM   3115  N N      . PRO B 1 38  ? 4.241   33.914  13.219 1.00 70.06  ? 38  PRO B N      1 
ATOM   3116  C CA     . PRO B 1 38  ? 2.943   34.071  12.606 1.00 70.96  ? 38  PRO B CA     1 
ATOM   3117  C C      . PRO B 1 38  ? 1.885   34.334  13.608 1.00 65.22  ? 38  PRO B C      1 
ATOM   3118  O O      . PRO B 1 38  ? 1.841   33.746  14.675 1.00 67.65  ? 38  PRO B O      1 
ATOM   3119  C CB     . PRO B 1 38  ? 2.750   32.762  11.879 1.00 67.94  ? 38  PRO B CB     1 
ATOM   3120  C CG     . PRO B 1 38  ? 4.125   32.420  11.439 1.00 70.57  ? 38  PRO B CG     1 
ATOM   3121  C CD     . PRO B 1 38  ? 4.996   32.819  12.595 1.00 74.53  ? 38  PRO B CD     1 
ATOM   3122  N N      . ARG B 1 39  ? 1.018   35.245  13.258 1.00 59.91  ? 39  ARG B N      1 
ATOM   3123  C CA     . ARG B 1 39  ? 0.008   35.658  14.174 1.00 67.66  ? 39  ARG B CA     1 
ATOM   3124  C C      . ARG B 1 39  ? -1.082  34.673  14.276 1.00 70.59  ? 39  ARG B C      1 
ATOM   3125  O O      . ARG B 1 39  ? -1.414  34.210  15.359 1.00 69.55  ? 39  ARG B O      1 
ATOM   3126  C CB     . ARG B 1 39  ? -0.585  36.929  13.575 1.00 72.99  ? 39  ARG B CB     1 
ATOM   3127  C CG     . ARG B 1 39  ? -1.586  37.678  14.428 1.00 80.09  ? 39  ARG B CG     1 
ATOM   3128  C CD     . ARG B 1 39  ? -2.048  38.912  13.676 1.00 70.41  ? 39  ARG B CD     1 
ATOM   3129  N NE     . ARG B 1 39  ? -0.953  39.850  13.452 1.00 71.42  ? 39  ARG B NE     1 
ATOM   3130  C CZ     . ARG B 1 39  ? -1.060  40.960  12.731 1.00 80.74  ? 39  ARG B CZ     1 
ATOM   3131  N NH1    . ARG B 1 39  ? -2.209  41.263  12.149 1.00 83.03  ? 39  ARG B NH1    1 
ATOM   3132  N NH2    . ARG B 1 39  ? -0.017  41.764  12.583 1.00 74.55  ? 39  ARG B NH2    1 
ATOM   3133  N N      . HIS B 1 40  ? -1.642  34.319  13.141 1.00 76.87  ? 40  HIS B N      1 
ATOM   3134  C CA     . HIS B 1 40  ? -2.819  33.481  13.156 1.00 81.88  ? 40  HIS B CA     1 
ATOM   3135  C C      . HIS B 1 40  ? -2.842  32.453  12.075 1.00 82.02  ? 40  HIS B C      1 
ATOM   3136  O O      . HIS B 1 40  ? -2.077  32.544  11.124 1.00 78.90  ? 40  HIS B O      1 
ATOM   3137  C CB     . HIS B 1 40  ? -4.072  34.340  12.920 1.00 81.82  ? 40  HIS B CB     1 
ATOM   3138  C CG     . HIS B 1 40  ? -4.655  34.940  14.160 1.00 91.72  ? 40  HIS B CG     1 
ATOM   3139  N ND1    . HIS B 1 40  ? -5.015  36.267  14.242 1.00 95.14  ? 40  HIS B ND1    1 
ATOM   3140  C CD2    . HIS B 1 40  ? -4.958  34.394  15.361 1.00 98.97  ? 40  HIS B CD2    1 
ATOM   3141  C CE1    . HIS B 1 40  ? -5.504  36.516  15.441 1.00 95.68  ? 40  HIS B CE1    1 
ATOM   3142  N NE2    . HIS B 1 40  ? -5.482  35.396  16.140 1.00 104.96 ? 40  HIS B NE2    1 
ATOM   3143  N N      . GLN B 1 41  ? -3.768  31.514  12.182 1.00 88.60  ? 41  GLN B N      1 
ATOM   3144  C CA     . GLN B 1 41  ? -3.971  30.510  11.141 1.00 96.90  ? 41  GLN B CA     1 
ATOM   3145  C C      . GLN B 1 41  ? -2.862  29.523  10.837 1.00 87.20  ? 41  GLN B C      1 
ATOM   3146  O O      . GLN B 1 41  ? -2.981  28.767  9.874  1.00 80.09  ? 41  GLN B O      1 
ATOM   3147  C CB     . GLN B 1 41  ? -4.540  31.140  9.857  1.00 90.39  ? 41  GLN B CB     1 
ATOM   3148  C CG     . GLN B 1 41  ? -5.972  31.627  10.012 1.00 86.98  ? 41  GLN B CG     1 
ATOM   3149  C CD     . GLN B 1 41  ? -6.455  32.430  8.822  1.00 91.82  ? 41  GLN B CD     1 
ATOM   3150  O OE1    . GLN B 1 41  ? -5.752  32.565  7.823  1.00 100.51 ? 41  GLN B OE1    1 
ATOM   3151  N NE2    . GLN B 1 41  ? -7.663  32.971  8.925  1.00 85.81  ? 41  GLN B NE2    1 
ATOM   3152  N N      . GLY B 1 42  ? -1.810  29.486  11.644 1.00 73.40  ? 42  GLY B N      1 
ATOM   3153  C CA     . GLY B 1 42  ? -0.823  28.466  11.396 1.00 70.65  ? 42  GLY B CA     1 
ATOM   3154  C C      . GLY B 1 42  ? -0.373  28.469  9.958  1.00 74.92  ? 42  GLY B C      1 
ATOM   3155  O O      . GLY B 1 42  ? -0.481  27.461  9.284  1.00 80.54  ? 42  GLY B O      1 
ATOM   3156  N N      . VAL B 1 43  ? 0.147   29.587  9.476  1.00 80.08  ? 43  VAL B N      1 
ATOM   3157  C CA     . VAL B 1 43  ? 0.600   29.712  8.094  1.00 73.68  ? 43  VAL B CA     1 
ATOM   3158  C C      . VAL B 1 43  ? 1.941   29.064  8.016  1.00 75.14  ? 43  VAL B C      1 
ATOM   3159  O O      . VAL B 1 43  ? 2.583   29.089  6.982  1.00 74.18  ? 43  VAL B O      1 
ATOM   3160  C CB     . VAL B 1 43  ? 0.765   31.175  7.680  1.00 69.51  ? 43  VAL B CB     1 
ATOM   3161  C CG1    . VAL B 1 43  ? -0.549  31.920  7.832  1.00 64.90  ? 43  VAL B CG1    1 
ATOM   3162  C CG2    . VAL B 1 43  ? 1.843   31.844  8.506  1.00 69.16  ? 43  VAL B CG2    1 
ATOM   3163  N N      . MET B 1 44  ? 2.363   28.453  9.108  1.00 74.89  ? 44  MET B N      1 
ATOM   3164  C CA     . MET B 1 44  ? 3.645   27.806  9.179  1.00 71.92  ? 44  MET B CA     1 
ATOM   3165  C C      . MET B 1 44  ? 3.448   26.433  8.642  1.00 65.37  ? 44  MET B C      1 
ATOM   3166  O O      . MET B 1 44  ? 4.316   25.594  8.784  1.00 63.22  ? 44  MET B O      1 
ATOM   3167  C CB     . MET B 1 44  ? 4.093   27.686  10.625 1.00 69.80  ? 44  MET B CB     1 
ATOM   3168  C CG     . MET B 1 44  ? 3.444   28.660  11.581 1.00 72.67  ? 44  MET B CG     1 
ATOM   3169  S SD     . MET B 1 44  ? 4.166   28.486  13.216 1.00 68.08  ? 44  MET B SD     1 
ATOM   3170  C CE     . MET B 1 44  ? 3.075   29.522  14.181 1.00 79.59  ? 44  MET B CE     1 
ATOM   3171  N N      . VAL B 1 45  ? 2.289   26.232  8.036  1.00 66.11  ? 45  VAL B N      1 
ATOM   3172  C CA     . VAL B 1 45  ? 1.936   24.944  7.486  1.00 62.52  ? 45  VAL B CA     1 
ATOM   3173  C C      . VAL B 1 45  ? 3.046   24.296  6.685  1.00 61.00  ? 45  VAL B C      1 
ATOM   3174  O O      . VAL B 1 45  ? 3.402   23.166  6.930  1.00 67.33  ? 45  VAL B O      1 
ATOM   3175  C CB     . VAL B 1 45  ? 0.623   25.060  6.688  1.00 61.71  ? 45  VAL B CB     1 
ATOM   3176  C CG1    . VAL B 1 45  ? 0.628   26.281  5.783  1.00 68.35  ? 45  VAL B CG1    1 
ATOM   3177  C CG2    . VAL B 1 45  ? 0.339   23.803  5.900  1.00 63.35  ? 45  VAL B CG2    1 
ATOM   3178  N N      . GLY B 1 46  ? 3.616   24.991  5.736  1.00 56.90  ? 46  GLY B N      1 
ATOM   3179  C CA     . GLY B 1 46  ? 4.629   24.351  4.950  1.00 59.00  ? 46  GLY B CA     1 
ATOM   3180  C C      . GLY B 1 46  ? 5.941   24.889  5.394  1.00 64.12  ? 46  GLY B C      1 
ATOM   3181  O O      . GLY B 1 46  ? 6.987   24.413  4.959  1.00 63.75  ? 46  GLY B O      1 
ATOM   3182  N N      . MET B 1 47  ? 5.905   25.874  6.273  1.00 64.37  ? 47  MET B N      1 
ATOM   3183  C CA     . MET B 1 47  ? 7.134   26.519  6.648  1.00 71.20  ? 47  MET B CA     1 
ATOM   3184  C C      . MET B 1 47  ? 7.845   25.656  7.623  1.00 74.18  ? 47  MET B C      1 
ATOM   3185  O O      . MET B 1 47  ? 7.459   25.569  8.779  1.00 72.98  ? 47  MET B O      1 
ATOM   3186  C CB     . MET B 1 47  ? 6.832   27.857  7.284  1.00 76.73  ? 47  MET B CB     1 
ATOM   3187  C CG     . MET B 1 47  ? 6.191   28.875  6.362  1.00 77.99  ? 47  MET B CG     1 
ATOM   3188  S SD     . MET B 1 47  ? 5.749   30.365  7.271  1.00 99.28  ? 47  MET B SD     1 
ATOM   3189  C CE     . MET B 1 47  ? 4.969   31.327  5.977  1.00 87.46  ? 47  MET B CE     1 
ATOM   3190  N N      . GLY B 1 48  ? 8.921   25.043  7.170  1.00 73.77  ? 48  GLY B N      1 
ATOM   3191  C CA     . GLY B 1 48  ? 9.643   24.132  8.017  1.00 67.40  ? 48  GLY B CA     1 
ATOM   3192  C C      . GLY B 1 48  ? 10.447  24.900  9.013  1.00 79.96  ? 48  GLY B C      1 
ATOM   3193  O O      . GLY B 1 48  ? 11.388  25.594  8.642  1.00 87.31  ? 48  GLY B O      1 
ATOM   3194  N N      . GLN B 1 49  ? 10.101  24.758  10.272 1.00 70.16  ? 49  GLN B N      1 
ATOM   3195  C CA     . GLN B 1 49  ? 10.788  25.484  11.298 1.00 77.96  ? 49  GLN B CA     1 
ATOM   3196  C C      . GLN B 1 49  ? 10.939  26.916  10.903 1.00 85.69  ? 49  GLN B C      1 
ATOM   3197  O O      . GLN B 1 49  ? 12.027  27.467  10.977 1.00 91.09  ? 49  GLN B O      1 
ATOM   3198  C CB     . GLN B 1 49  ? 12.143  24.884  11.592 1.00 78.13  ? 49  GLN B CB     1 
ATOM   3199  C CG     . GLN B 1 49  ? 12.533  25.013  13.059 1.00 85.87  ? 49  GLN B CG     1 
ATOM   3200  C CD     . GLN B 1 49  ? 11.581  24.287  13.999 1.00 78.16  ? 49  GLN B CD     1 
ATOM   3201  O OE1    . GLN B 1 49  ? 11.012  24.885  14.914 1.00 63.76  ? 49  GLN B OE1    1 
ATOM   3202  N NE2    . GLN B 1 49  ? 11.405  22.992  13.775 1.00 70.35  ? 49  GLN B NE2    1 
ATOM   3203  N N      . LYS B 1 50  ? 9.858   27.535  10.468 1.00 81.29  ? 50  LYS B N      1 
ATOM   3204  C CA     . LYS B 1 50  ? 9.926   28.947  10.197 1.00 82.94  ? 50  LYS B CA     1 
ATOM   3205  C C      . LYS B 1 50  ? 8.756   29.492  10.947 1.00 89.03  ? 50  LYS B C      1 
ATOM   3206  O O      . LYS B 1 50  ? 7.755   29.884  10.365 1.00 89.89  ? 50  LYS B O      1 
ATOM   3207  C CB     . LYS B 1 50  ? 9.858   29.266  8.719  1.00 80.76  ? 50  LYS B CB     1 
ATOM   3208  C CG     . LYS B 1 50  ? 10.377  30.643  8.350  1.00 75.49  ? 50  LYS B CG     1 
ATOM   3209  C CD     . LYS B 1 50  ? 11.741  30.912  8.956  1.00 72.53  ? 50  LYS B CD     1 
ATOM   3210  C CE     . LYS B 1 50  ? 12.295  32.230  8.449  1.00 73.80  ? 50  LYS B CE     1 
ATOM   3211  N NZ     . LYS B 1 50  ? 13.396  32.756  9.299  1.00 76.95  ? 50  LYS B NZ     1 
ATOM   3212  N N      . ASP B 1 51  ? 8.882   29.511  12.260 1.00 82.38  ? 51  ASP B N      1 
ATOM   3213  C CA     . ASP B 1 51  ? 7.833   30.018  13.093 1.00 78.81  ? 51  ASP B CA     1 
ATOM   3214  C C      . ASP B 1 51  ? 8.168   31.397  13.424 1.00 77.30  ? 51  ASP B C      1 
ATOM   3215  O O      . ASP B 1 51  ? 7.495   32.009  14.215 1.00 76.24  ? 51  ASP B O      1 
ATOM   3216  C CB     . ASP B 1 51  ? 7.833   29.264  14.407 1.00 90.36  ? 51  ASP B CB     1 
ATOM   3217  C CG     . ASP B 1 51  ? 9.127   29.427  15.200 1.00 98.01  ? 51  ASP B CG     1 
ATOM   3218  O OD1    . ASP B 1 51  ? 10.221  29.460  14.603 1.00 97.07  ? 51  ASP B OD1    1 
ATOM   3219  O OD2    . ASP B 1 51  ? 9.046   29.493  16.444 1.00 91.58  ? 51  ASP B OD2    1 
ATOM   3220  N N      . SER B 1 52  ? 9.265   31.875  12.888 1.00 74.95  ? 52  SER B N      1 
ATOM   3221  C CA     . SER B 1 52  ? 9.708   33.208  13.224 1.00 67.88  ? 52  SER B CA     1 
ATOM   3222  C C      . SER B 1 52  ? 10.338  33.897  12.062 1.00 68.54  ? 52  SER B C      1 
ATOM   3223  O O      . SER B 1 52  ? 11.192  33.330  11.405 1.00 75.68  ? 52  SER B O      1 
ATOM   3224  C CB     . SER B 1 52  ? 10.737  33.126  14.332 1.00 68.05  ? 52  SER B CB     1 
ATOM   3225  O OG     . SER B 1 52  ? 11.275  34.399  14.615 1.00 63.69  ? 52  SER B OG     1 
ATOM   3226  N N      . TYR B 1 53  ? 9.956   35.137  11.806 1.00 68.48  ? 53  TYR B N      1 
ATOM   3227  C CA     . TYR B 1 53  ? 10.589  35.897  10.754 1.00 66.08  ? 53  TYR B CA     1 
ATOM   3228  C C      . TYR B 1 53  ? 11.218  37.091  11.398 1.00 60.84  ? 53  TYR B C      1 
ATOM   3229  O O      . TYR B 1 53  ? 10.558  37.801  12.129 1.00 59.27  ? 53  TYR B O      1 
ATOM   3230  C CB     . TYR B 1 53  ? 9.568   36.353  9.750  1.00 65.21  ? 53  TYR B CB     1 
ATOM   3231  C CG     . TYR B 1 53  ? 9.195   35.363  8.684  1.00 62.15  ? 53  TYR B CG     1 
ATOM   3232  C CD1    . TYR B 1 53  ? 10.000  35.182  7.576  1.00 71.03  ? 53  TYR B CD1    1 
ATOM   3233  C CD2    . TYR B 1 53  ? 8.017   34.647  8.763  1.00 62.61  ? 53  TYR B CD2    1 
ATOM   3234  C CE1    . TYR B 1 53  ? 9.656   34.291  6.584  1.00 81.06  ? 53  TYR B CE1    1 
ATOM   3235  C CE2    . TYR B 1 53  ? 7.662   33.753  7.776  1.00 80.50  ? 53  TYR B CE2    1 
ATOM   3236  C CZ     . TYR B 1 53  ? 8.487   33.580  6.689  1.00 85.95  ? 53  TYR B CZ     1 
ATOM   3237  O OH     . TYR B 1 53  ? 8.143   32.690  5.702  1.00 86.27  ? 53  TYR B OH     1 
ATOM   3238  N N      . VAL B 1 54  ? 12.499  37.313  11.142 1.00 61.72  ? 54  VAL B N      1 
ATOM   3239  C CA     . VAL B 1 54  ? 13.222  38.404  11.775 1.00 61.32  ? 54  VAL B CA     1 
ATOM   3240  C C      . VAL B 1 54  ? 13.838  39.349  10.779 1.00 53.57  ? 54  VAL B C      1 
ATOM   3241  O O      . VAL B 1 54  ? 14.449  38.916  9.819  1.00 52.96  ? 54  VAL B O      1 
ATOM   3242  C CB     . VAL B 1 54  ? 14.388  37.860  12.615 1.00 54.20  ? 54  VAL B CB     1 
ATOM   3243  C CG1    . VAL B 1 54  ? 14.927  38.909  13.564 1.00 54.56  ? 54  VAL B CG1    1 
ATOM   3244  C CG2    . VAL B 1 54  ? 14.002  36.588  13.347 1.00 50.15  ? 54  VAL B CG2    1 
ATOM   3245  N N      . GLY B 1 55  ? 13.685  40.639  10.988 1.00 52.26  ? 55  GLY B N      1 
ATOM   3246  C CA     . GLY B 1 55  ? 14.359  41.587  10.138 1.00 58.88  ? 55  GLY B CA     1 
ATOM   3247  C C      . GLY B 1 55  ? 13.571  42.274  9.067  1.00 61.81  ? 55  GLY B C      1 
ATOM   3248  O O      . GLY B 1 55  ? 12.445  42.688  9.280  1.00 61.13  ? 55  GLY B O      1 
ATOM   3249  N N      . ASP B 1 56  ? 14.180  42.421  7.901  1.00 64.27  ? 56  ASP B N      1 
ATOM   3250  C CA     . ASP B 1 56  ? 13.509  43.071  6.797  1.00 69.71  ? 56  ASP B CA     1 
ATOM   3251  C C      . ASP B 1 56  ? 12.319  42.290  6.333  1.00 70.97  ? 56  ASP B C      1 
ATOM   3252  O O      . ASP B 1 56  ? 11.425  42.846  5.715  1.00 75.15  ? 56  ASP B O      1 
ATOM   3253  C CB     . ASP B 1 56  ? 14.478  43.221  5.641  1.00 69.20  ? 56  ASP B CB     1 
ATOM   3254  C CG     . ASP B 1 56  ? 15.637  44.130  5.972  1.00 79.21  ? 56  ASP B CG     1 
ATOM   3255  O OD1    . ASP B 1 56  ? 15.485  45.362  5.837  1.00 78.89  ? 56  ASP B OD1    1 
ATOM   3256  O OD2    . ASP B 1 56  ? 16.698  43.612  6.372  1.00 75.40  ? 56  ASP B OD2    1 
ATOM   3257  N N      . GLU B 1 57  ? 12.291  41.001  6.622  1.00 66.33  ? 57  GLU B N      1 
ATOM   3258  C CA     . GLU B 1 57  ? 11.175  40.159  6.220  1.00 68.81  ? 57  GLU B CA     1 
ATOM   3259  C C      . GLU B 1 57  ? 10.113  40.115  7.280  1.00 66.44  ? 57  GLU B C      1 
ATOM   3260  O O      . GLU B 1 57  ? 9.128   39.416  7.143  1.00 67.35  ? 57  GLU B O      1 
ATOM   3261  C CB     . GLU B 1 57  ? 11.668  38.761  5.895  1.00 78.26  ? 57  GLU B CB     1 
ATOM   3262  C CG     . GLU B 1 57  ? 12.724  38.246  6.850  1.00 87.18  ? 57  GLU B CG     1 
ATOM   3263  C CD     . GLU B 1 57  ? 13.078  36.801  6.592  1.00 84.86  ? 57  GLU B CD     1 
ATOM   3264  O OE1    . GLU B 1 57  ? 12.713  36.284  5.517  1.00 84.13  ? 57  GLU B OE1    1 
ATOM   3265  O OE2    . GLU B 1 57  ? 13.708  36.180  7.472  1.00 81.07  ? 57  GLU B OE2    1 
ATOM   3266  N N      . ALA B 1 58  ? 10.318  40.857  8.348  1.00 63.95  ? 58  ALA B N      1 
ATOM   3267  C CA     . ALA B 1 58  ? 9.328   40.933  9.388  1.00 65.53  ? 58  ALA B CA     1 
ATOM   3268  C C      . ALA B 1 58  ? 8.449   42.116  9.141  1.00 75.89  ? 58  ALA B C      1 
ATOM   3269  O O      . ALA B 1 58  ? 7.362   42.195  9.689  1.00 76.27  ? 58  ALA B O      1 
ATOM   3270  C CB     . ALA B 1 58  ? 9.988   41.053  10.725 1.00 60.43  ? 58  ALA B CB     1 
ATOM   3271  N N      . GLN B 1 59  ? 8.895   43.062  8.330  1.00 73.30  ? 59  GLN B N      1 
ATOM   3272  C CA     . GLN B 1 59  ? 8.016   44.154  7.991  1.00 65.65  ? 59  GLN B CA     1 
ATOM   3273  C C      . GLN B 1 59  ? 7.494   43.886  6.621  1.00 62.24  ? 59  GLN B C      1 
ATOM   3274  O O      . GLN B 1 59  ? 6.454   44.393  6.244  1.00 62.79  ? 59  GLN B O      1 
ATOM   3275  C CB     . GLN B 1 59  ? 8.703   45.500  8.111  1.00 66.67  ? 59  GLN B CB     1 
ATOM   3276  C CG     . GLN B 1 59  ? 8.491   46.161  9.459  1.00 68.09  ? 59  GLN B CG     1 
ATOM   3277  C CD     . GLN B 1 59  ? 9.115   47.535  9.542  1.00 73.74  ? 59  GLN B CD     1 
ATOM   3278  O OE1    . GLN B 1 59  ? 9.967   47.892  8.729  1.00 69.57  ? 59  GLN B OE1    1 
ATOM   3279  N NE2    . GLN B 1 59  ? 8.699   48.312  10.531 1.00 71.35  ? 59  GLN B NE2    1 
ATOM   3280  N N      . SER B 1 60  ? 8.196   43.062  5.868  1.00 64.94  ? 60  SER B N      1 
ATOM   3281  C CA     . SER B 1 60  ? 7.686   42.673  4.569  1.00 76.35  ? 60  SER B CA     1 
ATOM   3282  C C      . SER B 1 60  ? 6.449   41.860  4.828  1.00 82.34  ? 60  SER B C      1 
ATOM   3283  O O      . SER B 1 60  ? 5.426   42.062  4.180  1.00 91.87  ? 60  SER B O      1 
ATOM   3284  C CB     . SER B 1 60  ? 8.704   41.840  3.803  1.00 75.06  ? 60  SER B CB     1 
ATOM   3285  O OG     . SER B 1 60  ? 8.155   41.336  2.601  1.00 78.20  ? 60  SER B OG     1 
ATOM   3286  N N      . LYS B 1 61  ? 6.513   40.980  5.819  1.00 72.36  ? 61  LYS B N      1 
ATOM   3287  C CA     . LYS B 1 61  ? 5.364   40.181  6.189  1.00 64.76  ? 61  LYS B CA     1 
ATOM   3288  C C      . LYS B 1 61  ? 4.875   40.717  7.486  1.00 70.74  ? 61  LYS B C      1 
ATOM   3289  O O      . LYS B 1 61  ? 5.427   40.396  8.506  1.00 77.58  ? 61  LYS B O      1 
ATOM   3290  C CB     . LYS B 1 61  ? 5.809   38.756  6.381  1.00 64.15  ? 61  LYS B CB     1 
ATOM   3291  C CG     . LYS B 1 61  ? 6.154   38.051  5.079  1.00 78.42  ? 61  LYS B CG     1 
ATOM   3292  C CD     . LYS B 1 61  ? 7.563   37.487  5.092  1.00 79.22  ? 61  LYS B CD     1 
ATOM   3293  C CE     . LYS B 1 61  ? 7.993   37.038  3.706  1.00 80.36  ? 61  LYS B CE     1 
ATOM   3294  N NZ     . LYS B 1 61  ? 9.424   36.626  3.663  1.00 75.45  ? 61  LYS B NZ     1 
ATOM   3295  N N      . ARG B 1 62  ? 3.834   41.524  7.475  1.00 69.78  ? 62  ARG B N      1 
ATOM   3296  C CA     . ARG B 1 62  ? 3.411   42.159  8.707  1.00 70.82  ? 62  ARG B CA     1 
ATOM   3297  C C      . ARG B 1 62  ? 2.065   41.689  9.176  1.00 68.08  ? 62  ARG B C      1 
ATOM   3298  O O      . ARG B 1 62  ? 1.870   41.445  10.344 1.00 67.79  ? 62  ARG B O      1 
ATOM   3299  C CB     . ARG B 1 62  ? 3.402   43.666  8.522  1.00 62.48  ? 62  ARG B CB     1 
ATOM   3300  C CG     . ARG B 1 62  ? 3.734   44.454  9.770  1.00 67.62  ? 62  ARG B CG     1 
ATOM   3301  C CD     . ARG B 1 62  ? 3.724   45.952  9.513  1.00 68.67  ? 62  ARG B CD     1 
ATOM   3302  N NE     . ARG B 1 62  ? 4.684   46.356  8.493  1.00 71.02  ? 62  ARG B NE     1 
ATOM   3303  C CZ     . ARG B 1 62  ? 4.358   46.718  7.257  1.00 70.45  ? 62  ARG B CZ     1 
ATOM   3304  N NH1    . ARG B 1 62  ? 3.089   46.733  6.881  1.00 71.61  ? 62  ARG B NH1    1 
ATOM   3305  N NH2    . ARG B 1 62  ? 5.301   47.069  6.397  1.00 65.82  ? 62  ARG B NH2    1 
ATOM   3306  N N      . GLY B 1 63  ? 1.122   41.556  8.268  1.00 63.10  ? 63  GLY B N      1 
ATOM   3307  C CA     . GLY B 1 63  ? -0.214  41.148  8.636  1.00 56.98  ? 63  GLY B CA     1 
ATOM   3308  C C      . GLY B 1 63  ? -0.121  39.716  9.027  1.00 70.01  ? 63  GLY B C      1 
ATOM   3309  O O      . GLY B 1 63  ? -0.825  39.278  9.923  1.00 80.37  ? 63  GLY B O      1 
ATOM   3310  N N      . ILE B 1 64  ? 0.783   38.979  8.400  1.00 71.14  ? 64  ILE B N      1 
ATOM   3311  C CA     . ILE B 1 64  ? 0.966   37.568  8.706  1.00 63.29  ? 64  ILE B CA     1 
ATOM   3312  C C      . ILE B 1 64  ? 1.621   37.388  10.066 1.00 65.25  ? 64  ILE B C      1 
ATOM   3313  O O      . ILE B 1 64  ? 1.473   36.350  10.686 1.00 54.39  ? 64  ILE B O      1 
ATOM   3314  C CB     . ILE B 1 64  ? 1.811   36.928  7.606  1.00 50.00  ? 64  ILE B CB     1 
ATOM   3315  C CG1    . ILE B 1 64  ? 1.136   37.134  6.254  1.00 58.77  ? 64  ILE B CG1    1 
ATOM   3316  C CG2    . ILE B 1 64  ? 2.006   35.445  7.833  1.00 62.28  ? 64  ILE B CG2    1 
ATOM   3317  C CD1    . ILE B 1 64  ? 1.940   37.964  5.278  1.00 79.72  ? 64  ILE B CD1    1 
ATOM   3318  N N      . LEU B 1 65  ? 2.285   38.423  10.575 1.00 67.39  ? 65  LEU B N      1 
ATOM   3319  C CA     . LEU B 1 65  ? 3.024   38.300  11.835 1.00 65.13  ? 65  LEU B CA     1 
ATOM   3320  C C      . LEU B 1 65  ? 2.715   39.278  12.969 1.00 65.72  ? 65  LEU B C      1 
ATOM   3321  O O      . LEU B 1 65  ? 2.399   40.422  12.735 1.00 65.98  ? 65  LEU B O      1 
ATOM   3322  C CB     . LEU B 1 65  ? 4.514   38.410  11.544 1.00 63.07  ? 65  LEU B CB     1 
ATOM   3323  C CG     . LEU B 1 65  ? 5.197   37.701  10.384 1.00 61.35  ? 65  LEU B CG     1 
ATOM   3324  C CD1    . LEU B 1 65  ? 6.635   38.164  10.370 1.00 71.69  ? 65  LEU B CD1    1 
ATOM   3325  C CD2    . LEU B 1 65  ? 5.150   36.196  10.515 1.00 60.89  ? 65  LEU B CD2    1 
ATOM   3326  N N      . THR B 1 66  ? 2.834   38.835  14.219 1.00 63.31  ? 66  THR B N      1 
ATOM   3327  C CA     . THR B 1 66  ? 2.653   39.718  15.366 1.00 65.76  ? 66  THR B CA     1 
ATOM   3328  C C      . THR B 1 66  ? 4.050   40.081  15.747 1.00 71.36  ? 66  THR B C      1 
ATOM   3329  O O      . THR B 1 66  ? 4.834   39.200  16.068 1.00 63.79  ? 66  THR B O      1 
ATOM   3330  C CB     . THR B 1 66  ? 2.057   39.007  16.568 1.00 60.49  ? 66  THR B CB     1 
ATOM   3331  O OG1    . THR B 1 66  ? 0.742   38.555  16.256 1.00 72.61  ? 66  THR B OG1    1 
ATOM   3332  C CG2    . THR B 1 66  ? 1.964   39.954  17.747 1.00 65.20  ? 66  THR B CG2    1 
ATOM   3333  N N      . LEU B 1 67  ? 4.380   41.364  15.752 1.00 79.35  ? 67  LEU B N      1 
ATOM   3334  C CA     . LEU B 1 67  ? 5.762   41.754  15.967 1.00 71.33  ? 67  LEU B CA     1 
ATOM   3335  C C      . LEU B 1 67  ? 6.045   42.264  17.335 1.00 73.52  ? 67  LEU B C      1 
ATOM   3336  O O      . LEU B 1 67  ? 5.301   43.080  17.857 1.00 80.38  ? 67  LEU B O      1 
ATOM   3337  C CB     . LEU B 1 67  ? 6.163   42.823  14.953 1.00 65.48  ? 67  LEU B CB     1 
ATOM   3338  C CG     . LEU B 1 67  ? 5.826   42.534  13.494 1.00 72.68  ? 67  LEU B CG     1 
ATOM   3339  C CD1    . LEU B 1 67  ? 5.869   43.802  12.662 1.00 70.64  ? 67  LEU B CD1    1 
ATOM   3340  C CD2    . LEU B 1 67  ? 6.762   41.487  12.927 1.00 72.49  ? 67  LEU B CD2    1 
ATOM   3341  N N      . LYS B 1 68  ? 7.123   41.779  17.925 1.00 73.27  ? 68  LYS B N      1 
ATOM   3342  C CA     . LYS B 1 68  ? 7.520   42.235  19.227 1.00 65.53  ? 68  LYS B CA     1 
ATOM   3343  C C      . LYS B 1 68  ? 8.852   42.888  19.012 1.00 62.88  ? 68  LYS B C      1 
ATOM   3344  O O      . LYS B 1 68  ? 9.799   42.221  18.670 1.00 66.18  ? 68  LYS B O      1 
ATOM   3345  C CB     . LYS B 1 68  ? 7.658   41.043  20.156 1.00 57.64  ? 68  LYS B CB     1 
ATOM   3346  C CG     . LYS B 1 68  ? 7.647   41.394  21.636 1.00 77.43  ? 68  LYS B CG     1 
ATOM   3347  C CD     . LYS B 1 68  ? 9.048   41.499  22.221 1.00 76.76  ? 68  LYS B CD     1 
ATOM   3348  C CE     . LYS B 1 68  ? 9.012   42.022  23.645 1.00 58.21  ? 68  LYS B CE     1 
ATOM   3349  N NZ     . LYS B 1 68  ? 8.436   43.393  23.695 1.00 53.26  ? 68  LYS B NZ     1 
ATOM   3350  N N      . TYR B 1 69  ? 8.922   44.194  19.182 1.00 62.46  ? 69  TYR B N      1 
ATOM   3351  C CA     . TYR B 1 69  ? 10.166  44.911  19.037 1.00 66.09  ? 69  TYR B CA     1 
ATOM   3352  C C      . TYR B 1 69  ? 10.942  44.677  20.277 1.00 65.38  ? 69  TYR B C      1 
ATOM   3353  O O      . TYR B 1 69  ? 10.611  45.217  21.317 1.00 65.49  ? 69  TYR B O      1 
ATOM   3354  C CB     . TYR B 1 69  ? 9.906   46.410  18.971 1.00 68.83  ? 69  TYR B CB     1 
ATOM   3355  C CG     . TYR B 1 69  ? 9.145   46.903  17.763 1.00 76.84  ? 69  TYR B CG     1 
ATOM   3356  C CD1    . TYR B 1 69  ? 7.796   46.623  17.596 1.00 85.53  ? 69  TYR B CD1    1 
ATOM   3357  C CD2    . TYR B 1 69  ? 9.770   47.683  16.804 1.00 79.89  ? 69  TYR B CD2    1 
ATOM   3358  C CE1    . TYR B 1 69  ? 7.097   47.076  16.495 1.00 96.61  ? 69  TYR B CE1    1 
ATOM   3359  C CE2    . TYR B 1 69  ? 9.078   48.151  15.703 1.00 97.20  ? 69  TYR B CE2    1 
ATOM   3360  C CZ     . TYR B 1 69  ? 7.740   47.845  15.553 1.00 100.74 ? 69  TYR B CZ     1 
ATOM   3361  O OH     . TYR B 1 69  ? 7.045   48.301  14.453 1.00 88.23  ? 69  TYR B OH     1 
ATOM   3362  N N      . PRO B 1 70  ? 12.020  43.856  20.199 1.00 65.30  ? 70  PRO B N      1 
ATOM   3363  C CA     . PRO B 1 70  ? 12.755  43.760  21.450 1.00 62.90  ? 70  PRO B CA     1 
ATOM   3364  C C      . PRO B 1 70  ? 13.627  44.955  21.451 1.00 68.41  ? 70  PRO B C      1 
ATOM   3365  O O      . PRO B 1 70  ? 13.512  45.778  20.545 1.00 69.39  ? 70  PRO B O      1 
ATOM   3366  C CB     . PRO B 1 70  ? 13.642  42.543  21.264 1.00 52.63  ? 70  PRO B CB     1 
ATOM   3367  C CG     . PRO B 1 70  ? 13.327  41.973  19.929 1.00 54.59  ? 70  PRO B CG     1 
ATOM   3368  C CD     . PRO B 1 70  ? 12.710  43.076  19.148 1.00 58.01  ? 70  PRO B CD     1 
ATOM   3369  N N      . ILE B 1 71  ? 14.556  45.031  22.383 1.00 60.29  ? 71  ILE B N      1 
ATOM   3370  C CA     . ILE B 1 71  ? 15.441  46.184  22.469 1.00 59.94  ? 71  ILE B CA     1 
ATOM   3371  C C      . ILE B 1 71  ? 14.705  47.461  22.074 1.00 61.58  ? 71  ILE B C      1 
ATOM   3372  O O      . ILE B 1 71  ? 15.141  48.207  21.236 1.00 60.51  ? 71  ILE B O      1 
ATOM   3373  C CB     . ILE B 1 71  ? 16.801  45.932  21.761 1.00 53.42  ? 71  ILE B CB     1 
ATOM   3374  C CG1    . ILE B 1 71  ? 17.798  47.048  22.048 1.00 57.85  ? 71  ILE B CG1    1 
ATOM   3375  C CG2    . ILE B 1 71  ? 16.661  45.620  20.275 1.00 53.39  ? 71  ILE B CG2    1 
ATOM   3376  C CD1    . ILE B 1 71  ? 18.729  46.731  23.187 1.00 62.98  ? 71  ILE B CD1    1 
ATOM   3377  N N      . GLU B 1 72  ? 13.531  47.682  22.648 1.00 64.67  ? 72  GLU B N      1 
ATOM   3378  C CA     . GLU B 1 72  ? 12.804  48.917  22.405 1.00 60.79  ? 72  GLU B CA     1 
ATOM   3379  C C      . GLU B 1 72  ? 13.066  49.623  23.680 1.00 63.56  ? 72  GLU B C      1 
ATOM   3380  O O      . GLU B 1 72  ? 13.099  48.966  24.717 1.00 64.07  ? 72  GLU B O      1 
ATOM   3381  C CB     . GLU B 1 72  ? 11.323  48.649  22.248 1.00 61.09  ? 72  GLU B CB     1 
ATOM   3382  C CG     . GLU B 1 72  ? 10.392  49.799  22.571 1.00 55.46  ? 72  GLU B CG     1 
ATOM   3383  C CD     . GLU B 1 72  ? 8.962   49.330  22.768 1.00 65.27  ? 72  GLU B CD     1 
ATOM   3384  O OE1    . GLU B 1 72  ? 8.712   48.117  22.629 1.00 68.66  ? 72  GLU B OE1    1 
ATOM   3385  O OE2    . GLU B 1 72  ? 8.087   50.166  23.065 1.00 56.33  ? 72  GLU B OE2    1 
ATOM   3386  N N      . HIS B 1 73  ? 13.246  50.931  23.631 1.00 57.34  ? 73  HIS B N      1 
ATOM   3387  C CA     . HIS B 1 73  ? 13.595  51.720  24.807 1.00 55.83  ? 73  HIS B CA     1 
ATOM   3388  C C      . HIS B 1 73  ? 15.050  51.515  25.175 1.00 52.84  ? 73  HIS B C      1 
ATOM   3389  O O      . HIS B 1 73  ? 15.525  52.092  26.133 1.00 52.56  ? 73  HIS B O      1 
ATOM   3390  C CB     . HIS B 1 73  ? 12.663  51.507  25.988 1.00 58.45  ? 73  HIS B CB     1 
ATOM   3391  C CG     . HIS B 1 73  ? 11.254  51.946  25.752 1.00 59.67  ? 73  HIS B CG     1 
ATOM   3392  N ND1    . HIS B 1 73  ? 10.172  51.145  26.040 1.00 51.37  ? 73  HIS B ND1    1 
ATOM   3393  C CD2    . HIS B 1 73  ? 10.748  53.107  25.278 1.00 69.03  ? 73  HIS B CD2    1 
ATOM   3394  C CE1    . HIS B 1 73  ? 9.058   51.792  25.748 1.00 60.67  ? 73  HIS B CE1    1 
ATOM   3395  N NE2    . HIS B 1 73  ? 9.380   52.983  25.281 1.00 72.26  ? 73  HIS B NE2    1 
ATOM   3396  N N      . GLY B 1 74  ? 15.776  50.721  24.410 1.00 52.12  ? 74  GLY B N      1 
ATOM   3397  C CA     . GLY B 1 74  ? 17.205  50.587  24.633 1.00 46.74  ? 74  GLY B CA     1 
ATOM   3398  C C      . GLY B 1 74  ? 17.728  49.444  25.447 1.00 46.14  ? 74  GLY B C      1 
ATOM   3399  O O      . GLY B 1 74  ? 18.903  49.141  25.400 1.00 48.20  ? 74  GLY B O      1 
ATOM   3400  N N      . ILE B 1 75  ? 16.873  48.823  26.225 1.00 47.15  ? 75  ILE B N      1 
ATOM   3401  C CA     . ILE B 1 75  ? 17.310  47.754  27.079 1.00 49.74  ? 75  ILE B CA     1 
ATOM   3402  C C      . ILE B 1 75  ? 16.640  46.490  26.641 1.00 52.30  ? 75  ILE B C      1 
ATOM   3403  O O      . ILE B 1 75  ? 15.437  46.466  26.425 1.00 55.41  ? 75  ILE B O      1 
ATOM   3404  C CB     . ILE B 1 75  ? 17.043  48.055  28.563 1.00 53.11  ? 75  ILE B CB     1 
ATOM   3405  C CG1    . ILE B 1 75  ? 15.656  48.656  28.762 1.00 63.73  ? 75  ILE B CG1    1 
ATOM   3406  C CG2    . ILE B 1 75  ? 18.086  49.017  29.109 1.00 43.26  ? 75  ILE B CG2    1 
ATOM   3407  C CD1    . ILE B 1 75  ? 15.427  49.176  30.161 1.00 60.15  ? 75  ILE B CD1    1 
ATOM   3408  N N      . VAL B 1 76  ? 17.393  45.405  26.528 1.00 45.40  ? 76  VAL B N      1 
ATOM   3409  C CA     . VAL B 1 76  ? 16.852  44.167  26.004 1.00 40.95  ? 76  VAL B CA     1 
ATOM   3410  C C      . VAL B 1 76  ? 15.781  43.519  26.833 1.00 42.98  ? 76  VAL B C      1 
ATOM   3411  O O      . VAL B 1 76  ? 16.072  42.850  27.803 1.00 47.96  ? 76  VAL B O      1 
ATOM   3412  C CB     . VAL B 1 76  ? 17.960  43.163  25.792 1.00 44.76  ? 76  VAL B CB     1 
ATOM   3413  C CG1    . VAL B 1 76  ? 17.528  42.141  24.763 1.00 51.82  ? 76  VAL B CG1    1 
ATOM   3414  C CG2    . VAL B 1 76  ? 19.230  43.860  25.349 1.00 41.22  ? 76  VAL B CG2    1 
ATOM   3415  N N      . THR B 1 77  ? 14.541  43.638  26.409 1.00 45.26  ? 77  THR B N      1 
ATOM   3416  C CA     . THR B 1 77  ? 13.432  43.032  27.118 1.00 49.07  ? 77  THR B CA     1 
ATOM   3417  C C      . THR B 1 77  ? 13.386  41.519  27.038 1.00 53.02  ? 77  THR B C      1 
ATOM   3418  O O      . THR B 1 77  ? 13.506  40.843  28.046 1.00 55.92  ? 77  THR B O      1 
ATOM   3419  C CB     . THR B 1 77  ? 12.127  43.553  26.529 1.00 45.48  ? 77  THR B CB     1 
ATOM   3420  O OG1    . THR B 1 77  ? 12.312  44.901  26.090 1.00 58.65  ? 77  THR B OG1    1 
ATOM   3421  C CG2    . THR B 1 77  ? 11.017  43.498  27.555 1.00 44.41  ? 77  THR B CG2    1 
ATOM   3422  N N      . ASN B 1 78  ? 13.195  40.974  25.845 1.00 55.14  ? 78  ASN B N      1 
ATOM   3423  C CA     . ASN B 1 78  ? 13.051  39.535  25.681 1.00 57.67  ? 78  ASN B CA     1 
ATOM   3424  C C      . ASN B 1 78  ? 14.306  38.954  25.179 1.00 58.25  ? 78  ASN B C      1 
ATOM   3425  O O      . ASN B 1 78  ? 14.700  39.204  24.058 1.00 61.06  ? 78  ASN B O      1 
ATOM   3426  C CB     . ASN B 1 78  ? 11.984  39.227  24.649 1.00 55.24  ? 78  ASN B CB     1 
ATOM   3427  C CG     . ASN B 1 78  ? 11.372  37.860  24.839 1.00 63.47  ? 78  ASN B CG     1 
ATOM   3428  O OD1    . ASN B 1 78  ? 11.780  37.101  25.714 1.00 64.66  ? 78  ASN B OD1    1 
ATOM   3429  N ND2    . ASN B 1 78  ? 10.378  37.543  24.027 1.00 67.40  ? 78  ASN B ND2    1 
ATOM   3430  N N      . TRP B 1 79  ? 14.916  38.097  25.969 1.00 47.40  ? 79  TRP B N      1 
ATOM   3431  C CA     . TRP B 1 79  ? 16.186  37.567  25.569 1.00 45.07  ? 79  TRP B CA     1 
ATOM   3432  C C      . TRP B 1 79  ? 16.045  36.533  24.485 1.00 48.57  ? 79  TRP B C      1 
ATOM   3433  O O      . TRP B 1 79  ? 16.915  36.401  23.646 1.00 45.36  ? 79  TRP B O      1 
ATOM   3434  C CB     . TRP B 1 79  ? 16.929  37.056  26.776 1.00 42.54  ? 79  TRP B CB     1 
ATOM   3435  C CG     . TRP B 1 79  ? 17.510  38.140  27.577 1.00 44.23  ? 79  TRP B CG     1 
ATOM   3436  C CD1    . TRP B 1 79  ? 17.098  38.561  28.795 1.00 48.29  ? 79  TRP B CD1    1 
ATOM   3437  C CD2    . TRP B 1 79  ? 18.613  38.966  27.214 1.00 44.10  ? 79  TRP B CD2    1 
ATOM   3438  N NE1    . TRP B 1 79  ? 17.883  39.595  29.225 1.00 48.59  ? 79  TRP B NE1    1 
ATOM   3439  C CE2    . TRP B 1 79  ? 18.822  39.862  28.266 1.00 46.21  ? 79  TRP B CE2    1 
ATOM   3440  C CE3    . TRP B 1 79  ? 19.449  39.028  26.101 1.00 46.72  ? 79  TRP B CE3    1 
ATOM   3441  C CZ2    . TRP B 1 79  ? 19.828  40.810  28.239 1.00 47.43  ? 79  TRP B CZ2    1 
ATOM   3442  C CZ3    . TRP B 1 79  ? 20.443  39.964  26.079 1.00 43.41  ? 79  TRP B CZ3    1 
ATOM   3443  C CH2    . TRP B 1 79  ? 20.628  40.843  27.138 1.00 42.10  ? 79  TRP B CH2    1 
ATOM   3444  N N      . ASP B 1 80  ? 14.919  35.843  24.442 1.00 54.79  ? 80  ASP B N      1 
ATOM   3445  C CA     . ASP B 1 80  ? 14.686  34.814  23.425 1.00 58.56  ? 80  ASP B CA     1 
ATOM   3446  C C      . ASP B 1 80  ? 14.439  35.372  22.046 1.00 54.01  ? 80  ASP B C      1 
ATOM   3447  O O      . ASP B 1 80  ? 14.708  34.716  21.057 1.00 49.46  ? 80  ASP B O      1 
ATOM   3448  C CB     . ASP B 1 80  ? 13.508  33.920  23.810 1.00 58.18  ? 80  ASP B CB     1 
ATOM   3449  C CG     . ASP B 1 80  ? 13.869  32.889  24.852 1.00 66.61  ? 80  ASP B CG     1 
ATOM   3450  O OD1    . ASP B 1 80  ? 14.789  33.136  25.655 1.00 67.01  ? 80  ASP B OD1    1 
ATOM   3451  O OD2    . ASP B 1 80  ? 13.219  31.825  24.870 1.00 66.70  ? 80  ASP B OD2    1 
ATOM   3452  N N      . ASP B 1 81  ? 13.922  36.581  21.972 1.00 55.82  ? 81  ASP B N      1 
ATOM   3453  C CA     . ASP B 1 81  ? 13.641  37.183  20.698 1.00 54.89  ? 81  ASP B CA     1 
ATOM   3454  C C      . ASP B 1 81  ? 14.800  38.034  20.297 1.00 51.68  ? 81  ASP B C      1 
ATOM   3455  O O      . ASP B 1 81  ? 14.762  38.648  19.254 1.00 56.18  ? 81  ASP B O      1 
ATOM   3456  C CB     . ASP B 1 81  ? 12.392  38.026  20.769 1.00 54.36  ? 81  ASP B CB     1 
ATOM   3457  C CG     . ASP B 1 81  ? 11.144  37.208  20.907 1.00 66.46  ? 81  ASP B CG     1 
ATOM   3458  O OD1    . ASP B 1 81  ? 11.253  35.991  21.133 1.00 67.03  ? 81  ASP B OD1    1 
ATOM   3459  O OD2    . ASP B 1 81  ? 10.045  37.785  20.798 1.00 67.75  ? 81  ASP B OD2    1 
ATOM   3460  N N      . MET B 1 82  ? 15.840  38.079  21.113 1.00 48.17  ? 82  MET B N      1 
ATOM   3461  C CA     . MET B 1 82  ? 17.039  38.842  20.778 1.00 50.36  ? 82  MET B CA     1 
ATOM   3462  C C      . MET B 1 82  ? 18.119  37.933  20.280 1.00 48.56  ? 82  MET B C      1 
ATOM   3463  O O      . MET B 1 82  ? 18.981  38.342  19.530 1.00 51.74  ? 82  MET B O      1 
ATOM   3464  C CB     . MET B 1 82  ? 17.551  39.639  21.964 1.00 52.29  ? 82  MET B CB     1 
ATOM   3465  C CG     . MET B 1 82  ? 18.698  40.577  21.656 1.00 50.11  ? 82  MET B CG     1 
ATOM   3466  S SD     . MET B 1 82  ? 18.113  41.979  20.711 1.00 60.03  ? 82  MET B SD     1 
ATOM   3467  C CE     . MET B 1 82  ? 19.631  42.530  19.952 1.00 56.75  ? 82  MET B CE     1 
ATOM   3468  N N      . GLU B 1 83  ? 18.088  36.681  20.678 1.00 46.77  ? 83  GLU B N      1 
ATOM   3469  C CA     . GLU B 1 83  ? 19.060  35.752  20.158 1.00 48.48  ? 83  GLU B CA     1 
ATOM   3470  C C      . GLU B 1 83  ? 18.793  35.602  18.714 1.00 42.69  ? 83  GLU B C      1 
ATOM   3471  O O      . GLU B 1 83  ? 19.687  35.410  17.924 1.00 39.62  ? 83  GLU B O      1 
ATOM   3472  C CB     . GLU B 1 83  ? 18.923  34.398  20.816 1.00 51.26  ? 83  GLU B CB     1 
ATOM   3473  C CG     . GLU B 1 83  ? 19.069  34.428  22.324 1.00 56.03  ? 83  GLU B CG     1 
ATOM   3474  C CD     . GLU B 1 83  ? 18.994  33.052  22.951 1.00 57.96  ? 83  GLU B CD     1 
ATOM   3475  O OE1    . GLU B 1 83  ? 19.572  32.106  22.385 1.00 52.42  ? 83  GLU B OE1    1 
ATOM   3476  O OE2    . GLU B 1 83  ? 18.367  32.922  24.021 1.00 63.05  ? 83  GLU B OE2    1 
ATOM   3477  N N      . LYS B 1 84  ? 17.543  35.712  18.352 1.00 42.06  ? 84  LYS B N      1 
ATOM   3478  C CA     . LYS B 1 84  ? 17.184  35.531  16.983 1.00 42.67  ? 84  LYS B CA     1 
ATOM   3479  C C      . LYS B 1 84  ? 17.662  36.695  16.183 1.00 47.02  ? 84  LYS B C      1 
ATOM   3480  O O      . LYS B 1 84  ? 18.068  36.539  15.045 1.00 53.93  ? 84  LYS B O      1 
ATOM   3481  C CB     . LYS B 1 84  ? 15.691  35.385  16.872 1.00 43.92  ? 84  LYS B CB     1 
ATOM   3482  C CG     . LYS B 1 84  ? 15.170  34.109  17.496 1.00 46.80  ? 84  LYS B CG     1 
ATOM   3483  C CD     . LYS B 1 84  ? 13.672  33.986  17.323 1.00 50.25  ? 84  LYS B CD     1 
ATOM   3484  C CE     . LYS B 1 84  ? 13.194  32.657  17.870 1.00 47.18  ? 84  LYS B CE     1 
ATOM   3485  N NZ     . LYS B 1 84  ? 13.705  32.455  19.250 1.00 49.94  ? 84  LYS B NZ     1 
ATOM   3486  N N      . ILE B 1 85  ? 17.637  37.879  16.762 1.00 43.55  ? 85  ILE B N      1 
ATOM   3487  C CA     . ILE B 1 85  ? 18.155  39.029  16.063 1.00 41.07  ? 85  ILE B CA     1 
ATOM   3488  C C      . ILE B 1 85  ? 19.626  38.792  15.878 1.00 47.35  ? 85  ILE B C      1 
ATOM   3489  O O      . ILE B 1 85  ? 20.151  39.010  14.800 1.00 47.09  ? 85  ILE B O      1 
ATOM   3490  C CB     . ILE B 1 85  ? 17.880  40.327  16.802 1.00 34.63  ? 85  ILE B CB     1 
ATOM   3491  C CG1    . ILE B 1 85  ? 16.384  40.599  16.801 1.00 38.75  ? 85  ILE B CG1    1 
ATOM   3492  C CG2    . ILE B 1 85  ? 18.598  41.487  16.148 1.00 33.46  ? 85  ILE B CG2    1 
ATOM   3493  C CD1    . ILE B 1 85  ? 16.012  41.943  17.366 1.00 39.28  ? 85  ILE B CD1    1 
ATOM   3494  N N      . TRP B 1 86  ? 20.278  38.188  16.864 1.00 46.97  ? 86  TRP B N      1 
ATOM   3495  C CA     . TRP B 1 86  ? 21.706  37.948  16.772 1.00 38.97  ? 86  TRP B CA     1 
ATOM   3496  C C      . TRP B 1 86  ? 21.998  36.832  15.832 1.00 42.70  ? 86  TRP B C      1 
ATOM   3497  O O      . TRP B 1 86  ? 23.012  36.826  15.186 1.00 43.26  ? 86  TRP B O      1 
ATOM   3498  C CB     . TRP B 1 86  ? 22.313  37.697  18.112 1.00 40.02  ? 86  TRP B CB     1 
ATOM   3499  C CG     . TRP B 1 86  ? 22.454  38.890  18.947 1.00 48.55  ? 86  TRP B CG     1 
ATOM   3500  C CD1    . TRP B 1 86  ? 22.660  40.153  18.526 1.00 59.47  ? 86  TRP B CD1    1 
ATOM   3501  C CD2    . TRP B 1 86  ? 22.429  38.937  20.368 1.00 43.70  ? 86  TRP B CD2    1 
ATOM   3502  N NE1    . TRP B 1 86  ? 22.757  40.999  19.595 1.00 57.81  ? 86  TRP B NE1    1 
ATOM   3503  C CE2    . TRP B 1 86  ? 22.621  40.269  20.742 1.00 50.36  ? 86  TRP B CE2    1 
ATOM   3504  C CE3    . TRP B 1 86  ? 22.262  37.979  21.362 1.00 46.33  ? 86  TRP B CE3    1 
ATOM   3505  C CZ2    . TRP B 1 86  ? 22.646  40.668  22.062 1.00 54.81  ? 86  TRP B CZ2    1 
ATOM   3506  C CZ3    . TRP B 1 86  ? 22.289  38.377  22.666 1.00 53.03  ? 86  TRP B CZ3    1 
ATOM   3507  C CH2    . TRP B 1 86  ? 22.476  39.706  23.007 1.00 54.63  ? 86  TRP B CH2    1 
ATOM   3508  N N      . HIS B 1 87  ? 21.127  35.864  15.729 1.00 43.32  ? 87  HIS B N      1 
ATOM   3509  C CA     . HIS B 1 87  ? 21.340  34.846  14.730 1.00 45.37  ? 87  HIS B CA     1 
ATOM   3510  C C      . HIS B 1 87  ? 21.237  35.488  13.416 1.00 44.67  ? 87  HIS B C      1 
ATOM   3511  O O      . HIS B 1 87  ? 22.070  35.295  12.568 1.00 44.35  ? 87  HIS B O      1 
ATOM   3512  C CB     . HIS B 1 87  ? 20.204  33.845  14.794 1.00 50.35  ? 87  HIS B CB     1 
ATOM   3513  C CG     . HIS B 1 87  ? 20.439  32.584  14.032 1.00 56.78  ? 87  HIS B CG     1 
ATOM   3514  N ND1    . HIS B 1 87  ? 20.234  32.485  12.674 1.00 58.85  ? 87  HIS B ND1    1 
ATOM   3515  C CD2    . HIS B 1 87  ? 20.805  31.350  14.447 1.00 56.09  ? 87  HIS B CD2    1 
ATOM   3516  C CE1    . HIS B 1 87  ? 20.493  31.253  12.280 1.00 61.80  ? 87  HIS B CE1    1 
ATOM   3517  N NE2    . HIS B 1 87  ? 20.842  30.544  13.338 1.00 61.80  ? 87  HIS B NE2    1 
ATOM   3518  N N      . HIS B 1 88  ? 20.225  36.303  13.247 1.00 41.87  ? 88  HIS B N      1 
ATOM   3519  C CA     . HIS B 1 88  ? 20.004  36.853  11.952 1.00 44.32  ? 88  HIS B CA     1 
ATOM   3520  C C      . HIS B 1 88  ? 21.226  37.585  11.640 1.00 42.40  ? 88  HIS B C      1 
ATOM   3521  O O      . HIS B 1 88  ? 21.690  37.582  10.525 1.00 46.47  ? 88  HIS B O      1 
ATOM   3522  C CB     . HIS B 1 88  ? 18.815  37.785  11.963 1.00 42.77  ? 88  HIS B CB     1 
ATOM   3523  C CG     . HIS B 1 88  ? 18.275  38.108  10.610 1.00 46.15  ? 88  HIS B CG     1 
ATOM   3524  N ND1    . HIS B 1 88  ? 18.507  39.312  9.987  1.00 44.45  ? 88  HIS B ND1    1 
ATOM   3525  C CD2    . HIS B 1 88  ? 17.493  37.395  9.771  1.00 48.70  ? 88  HIS B CD2    1 
ATOM   3526  C CE1    . HIS B 1 88  ? 17.901  39.323  8.816  1.00 50.11  ? 88  HIS B CE1    1 
ATOM   3527  N NE2    . HIS B 1 88  ? 17.279  38.171  8.660  1.00 54.20  ? 88  HIS B NE2    1 
ATOM   3528  N N      . THR B 1 89  ? 21.781  38.217  12.637 1.00 34.93  ? 89  THR B N      1 
ATOM   3529  C CA     . THR B 1 89  ? 22.911  39.039  12.349 1.00 37.84  ? 89  THR B CA     1 
ATOM   3530  C C      . THR B 1 89  ? 24.081  38.226  11.937 1.00 42.04  ? 89  THR B C      1 
ATOM   3531  O O      . THR B 1 89  ? 24.570  38.366  10.836 1.00 46.43  ? 89  THR B O      1 
ATOM   3532  C CB     . THR B 1 89  ? 23.306  39.888  13.539 1.00 38.06  ? 89  THR B CB     1 
ATOM   3533  O OG1    . THR B 1 89  ? 22.150  40.518  14.087 1.00 38.46  ? 89  THR B OG1    1 
ATOM   3534  C CG2    . THR B 1 89  ? 24.282  40.939  13.111 1.00 35.51  ? 89  THR B CG2    1 
ATOM   3535  N N      . PHE B 1 90  ? 24.538  37.334  12.779 1.00 42.85  ? 90  PHE B N      1 
ATOM   3536  C CA     . PHE B 1 90  ? 25.753  36.625  12.469 1.00 41.75  ? 90  PHE B CA     1 
ATOM   3537  C C      . PHE B 1 90  ? 25.616  35.776  11.244 1.00 44.06  ? 90  PHE B C      1 
ATOM   3538  O O      . PHE B 1 90  ? 26.235  36.040  10.231 1.00 44.75  ? 90  PHE B O      1 
ATOM   3539  C CB     . PHE B 1 90  ? 26.191  35.801  13.669 1.00 36.11  ? 90  PHE B CB     1 
ATOM   3540  C CG     . PHE B 1 90  ? 26.409  36.606  14.905 1.00 40.58  ? 90  PHE B CG     1 
ATOM   3541  C CD1    . PHE B 1 90  ? 27.128  37.778  14.859 1.00 47.19  ? 90  PHE B CD1    1 
ATOM   3542  C CD2    . PHE B 1 90  ? 25.907  36.185  16.110 1.00 39.01  ? 90  PHE B CD2    1 
ATOM   3543  C CE1    . PHE B 1 90  ? 27.330  38.526  15.995 1.00 49.84  ? 90  PHE B CE1    1 
ATOM   3544  C CE2    . PHE B 1 90  ? 26.103  36.925  17.249 1.00 42.84  ? 90  PHE B CE2    1 
ATOM   3545  C CZ     . PHE B 1 90  ? 26.816  38.096  17.193 1.00 49.07  ? 90  PHE B CZ     1 
ATOM   3546  N N      . TYR B 1 91  ? 24.751  34.802  11.264 1.00 44.95  ? 91  TYR B N      1 
ATOM   3547  C CA     . TYR B 1 91  ? 24.627  33.918  10.149 1.00 45.65  ? 91  TYR B CA     1 
ATOM   3548  C C      . TYR B 1 91  ? 23.988  34.529  8.917  1.00 40.62  ? 91  TYR B C      1 
ATOM   3549  O O      . TYR B 1 91  ? 24.615  34.652  7.895  1.00 41.78  ? 91  TYR B O      1 
ATOM   3550  C CB     . TYR B 1 91  ? 23.820  32.744  10.625 1.00 45.74  ? 91  TYR B CB     1 
ATOM   3551  C CG     . TYR B 1 91  ? 24.362  32.033  11.824 1.00 38.71  ? 91  TYR B CG     1 
ATOM   3552  C CD1    . TYR B 1 91  ? 25.387  31.124  11.708 1.00 42.84  ? 91  TYR B CD1    1 
ATOM   3553  C CD2    . TYR B 1 91  ? 23.816  32.244  13.067 1.00 42.77  ? 91  TYR B CD2    1 
ATOM   3554  C CE1    . TYR B 1 91  ? 25.865  30.455  12.810 1.00 55.30  ? 91  TYR B CE1    1 
ATOM   3555  C CE2    . TYR B 1 91  ? 24.288  31.585  14.176 1.00 50.51  ? 91  TYR B CE2    1 
ATOM   3556  C CZ     . TYR B 1 91  ? 25.312  30.693  14.043 1.00 54.29  ? 91  TYR B CZ     1 
ATOM   3557  O OH     . TYR B 1 91  ? 25.770  30.047  15.160 1.00 47.34  ? 91  TYR B OH     1 
ATOM   3558  N N      . ASN B 1 92  ? 22.726  34.882  8.998  1.00 39.91  ? 92  ASN B N      1 
ATOM   3559  C CA     . ASN B 1 92  ? 22.001  35.406  7.850  1.00 48.58  ? 92  ASN B CA     1 
ATOM   3560  C C      . ASN B 1 92  ? 22.405  36.738  7.206  1.00 51.76  ? 92  ASN B C      1 
ATOM   3561  O O      . ASN B 1 92  ? 22.437  36.830  5.990  1.00 52.23  ? 92  ASN B O      1 
ATOM   3562  C CB     . ASN B 1 92  ? 20.520  35.499  8.203  1.00 47.21  ? 92  ASN B CB     1 
ATOM   3563  C CG     . ASN B 1 92  ? 19.943  34.214  8.733  1.00 51.49  ? 92  ASN B CG     1 
ATOM   3564  O OD1    . ASN B 1 92  ? 20.568  33.497  9.501  1.00 54.46  ? 92  ASN B OD1    1 
ATOM   3565  N ND2    . ASN B 1 92  ? 18.711  33.940  8.352  1.00 53.66  ? 92  ASN B ND2    1 
ATOM   3566  N N      . GLU B 1 93  ? 22.702  37.766  7.989  1.00 45.66  ? 93  GLU B N      1 
ATOM   3567  C CA     . GLU B 1 93  ? 23.024  39.061  7.435  1.00 40.64  ? 93  GLU B CA     1 
ATOM   3568  C C      . GLU B 1 93  ? 24.486  39.241  7.159  1.00 40.06  ? 93  GLU B C      1 
ATOM   3569  O O      . GLU B 1 93  ? 24.861  39.676  6.087  1.00 38.25  ? 93  GLU B O      1 
ATOM   3570  C CB     . GLU B 1 93  ? 22.591  40.136  8.386  1.00 41.03  ? 93  GLU B CB     1 
ATOM   3571  C CG     . GLU B 1 93  ? 21.125  40.497  8.314  1.00 50.34  ? 93  GLU B CG     1 
ATOM   3572  C CD     . GLU B 1 93  ? 20.805  41.497  7.222  1.00 64.50  ? 93  GLU B CD     1 
ATOM   3573  O OE1    . GLU B 1 93  ? 21.733  41.976  6.543  1.00 61.26  ? 93  GLU B OE1    1 
ATOM   3574  O OE2    . GLU B 1 93  ? 19.614  41.811  7.044  1.00 62.94  ? 93  GLU B OE2    1 
ATOM   3575  N N      . LEU B 1 94  ? 25.319  38.924  8.125  1.00 40.89  ? 94  LEU B N      1 
ATOM   3576  C CA     . LEU B 1 94  ? 26.762  39.088  7.973  1.00 41.35  ? 94  LEU B CA     1 
ATOM   3577  C C      . LEU B 1 94  ? 27.477  37.889  7.397  1.00 41.12  ? 94  LEU B C      1 
ATOM   3578  O O      . LEU B 1 94  ? 28.654  37.970  7.081  1.00 36.41  ? 94  LEU B O      1 
ATOM   3579  C CB     . LEU B 1 94  ? 27.379  39.438  9.319  1.00 39.26  ? 94  LEU B CB     1 
ATOM   3580  C CG     . LEU B 1 94  ? 27.617  40.883  9.735  1.00 37.98  ? 94  LEU B CG     1 
ATOM   3581  C CD1    . LEU B 1 94  ? 26.360  41.717  9.589  1.00 42.66  ? 94  LEU B CD1    1 
ATOM   3582  C CD2    . LEU B 1 94  ? 28.106  40.894  11.171 1.00 31.75  ? 94  LEU B CD2    1 
ATOM   3583  N N      . ARG B 1 95  ? 26.792  36.770  7.277  1.00 43.14  ? 95  ARG B N      1 
ATOM   3584  C CA     . ARG B 1 95  ? 27.374  35.547  6.727  1.00 42.44  ? 95  ARG B CA     1 
ATOM   3585  C C      . ARG B 1 95  ? 28.631  35.160  7.411  1.00 38.42  ? 95  ARG B C      1 
ATOM   3586  O O      . ARG B 1 95  ? 29.645  34.959  6.771  1.00 33.83  ? 95  ARG B O      1 
ATOM   3587  C CB     . ARG B 1 95  ? 27.563  35.651  5.234  1.00 46.26  ? 95  ARG B CB     1 
ATOM   3588  C CG     . ARG B 1 95  ? 26.267  35.921  4.488  1.00 49.82  ? 95  ARG B CG     1 
ATOM   3589  C CD     . ARG B 1 95  ? 26.377  35.536  3.026  1.00 52.70  ? 95  ARG B CD     1 
ATOM   3590  N NE     . ARG B 1 95  ? 26.397  34.089  2.859  1.00 45.76  ? 95  ARG B NE     1 
ATOM   3591  C CZ     . ARG B 1 95  ? 25.320  33.356  2.617  1.00 49.30  ? 95  ARG B CZ     1 
ATOM   3592  N NH1    . ARG B 1 95  ? 24.137  33.935  2.500  1.00 50.91  ? 95  ARG B NH1    1 
ATOM   3593  N NH2    . ARG B 1 95  ? 25.424  32.045  2.483  1.00 58.90  ? 95  ARG B NH2    1 
ATOM   3594  N N      . VAL B 1 96  ? 28.563  35.034  8.718  1.00 39.80  ? 96  VAL B N      1 
ATOM   3595  C CA     . VAL B 1 96  ? 29.729  34.719  9.475  1.00 38.43  ? 96  VAL B CA     1 
ATOM   3596  C C      . VAL B 1 96  ? 29.399  33.630  10.430 1.00 40.35  ? 96  VAL B C      1 
ATOM   3597  O O      . VAL B 1 96  ? 28.243  33.298  10.633 1.00 42.40  ? 96  VAL B O      1 
ATOM   3598  C CB     . VAL B 1 96  ? 30.194  35.939  10.252 1.00 32.26  ? 96  VAL B CB     1 
ATOM   3599  C CG1    . VAL B 1 96  ? 29.509  36.056  11.597 1.00 32.25  ? 96  VAL B CG1    1 
ATOM   3600  C CG2    . VAL B 1 96  ? 31.696  35.959  10.377 1.00 28.84  ? 96  VAL B CG2    1 
ATOM   3601  N N      . ALA B 1 97  ? 30.422  33.031  10.993 1.00 39.45  ? 97  ALA B N      1 
ATOM   3602  C CA     . ALA B 1 97  ? 30.230  32.019  11.975 1.00 37.36  ? 97  ALA B CA     1 
ATOM   3603  C C      . ALA B 1 97  ? 30.688  32.710  13.209 1.00 38.16  ? 97  ALA B C      1 
ATOM   3604  O O      . ALA B 1 97  ? 31.811  33.181  13.276 1.00 35.96  ? 97  ALA B O      1 
ATOM   3605  C CB     . ALA B 1 97  ? 31.154  30.880  11.676 1.00 39.05  ? 97  ALA B CB     1 
ATOM   3606  N N      . PRO B 1 98  ? 29.795  32.826  14.214 1.00 36.16  ? 98  PRO B N      1 
ATOM   3607  C CA     . PRO B 1 98  ? 30.273  33.568  15.362 1.00 33.10  ? 98  PRO B CA     1 
ATOM   3608  C C      . PRO B 1 98  ? 31.474  32.986  16.022 1.00 38.16  ? 98  PRO B C      1 
ATOM   3609  O O      . PRO B 1 98  ? 32.240  33.736  16.578 1.00 44.71  ? 98  PRO B O      1 
ATOM   3610  C CB     . PRO B 1 98  ? 29.138  33.418  16.340 1.00 34.74  ? 98  PRO B CB     1 
ATOM   3611  C CG     . PRO B 1 98  ? 27.927  33.319  15.521 1.00 37.46  ? 98  PRO B CG     1 
ATOM   3612  C CD     . PRO B 1 98  ? 28.353  32.506  14.357 1.00 39.00  ? 98  PRO B CD     1 
ATOM   3613  N N      . GLU B 1 99  ? 31.649  31.682  15.998 1.00 44.40  ? 99  GLU B N      1 
ATOM   3614  C CA     . GLU B 1 99  ? 32.733  31.049  16.710 1.00 36.31  ? 99  GLU B CA     1 
ATOM   3615  C C      . GLU B 1 99  ? 34.094  31.447  16.275 1.00 40.31  ? 99  GLU B C      1 
ATOM   3616  O O      . GLU B 1 99  ? 35.052  31.090  16.919 1.00 45.69  ? 99  GLU B O      1 
ATOM   3617  C CB     . GLU B 1 99  ? 32.639  29.555  16.554 1.00 42.51  ? 99  GLU B CB     1 
ATOM   3618  C CG     . GLU B 1 99  ? 32.712  29.072  15.118 1.00 67.93  ? 99  GLU B CG     1 
ATOM   3619  C CD     . GLU B 1 99  ? 32.865  27.570  15.013 1.00 76.80  ? 99  GLU B CD     1 
ATOM   3620  O OE1    . GLU B 1 99  ? 32.897  26.898  16.062 1.00 64.92  ? 99  GLU B OE1    1 
ATOM   3621  O OE2    . GLU B 1 99  ? 32.959  27.061  13.878 1.00 79.57  ? 99  GLU B OE2    1 
ATOM   3622  N N      . GLU B 1 100 ? 34.218  32.203  15.201 1.00 41.80  ? 100 GLU B N      1 
ATOM   3623  C CA     . GLU B 1 100 ? 35.539  32.517  14.685 1.00 42.35  ? 100 GLU B CA     1 
ATOM   3624  C C      . GLU B 1 100 ? 35.893  33.963  14.780 1.00 42.43  ? 100 GLU B C      1 
ATOM   3625  O O      . GLU B 1 100 ? 37.041  34.330  14.578 1.00 41.43  ? 100 GLU B O      1 
ATOM   3626  C CB     . GLU B 1 100 ? 35.624  32.118  13.230 1.00 50.34  ? 100 GLU B CB     1 
ATOM   3627  C CG     . GLU B 1 100 ? 35.499  30.628  12.980 1.00 68.35  ? 100 GLU B CG     1 
ATOM   3628  C CD     . GLU B 1 100 ? 35.588  30.276  11.511 1.00 74.84  ? 100 GLU B CD     1 
ATOM   3629  O OE1    . GLU B 1 100 ? 35.674  31.203  10.681 1.00 72.07  ? 100 GLU B OE1    1 
ATOM   3630  O OE2    . GLU B 1 100 ? 35.573  29.071  11.189 1.00 64.96  ? 100 GLU B OE2    1 
ATOM   3631  N N      . HIS B 1 101 ? 34.917  34.796  15.086 1.00 45.36  ? 101 HIS B N      1 
ATOM   3632  C CA     . HIS B 1 101 ? 35.145  36.228  15.127 1.00 45.24  ? 101 HIS B CA     1 
ATOM   3633  C C      . HIS B 1 101 ? 34.753  36.815  16.473 1.00 43.14  ? 101 HIS B C      1 
ATOM   3634  O O      . HIS B 1 101 ? 33.666  36.572  16.963 1.00 41.56  ? 101 HIS B O      1 
ATOM   3635  C CB     . HIS B 1 101 ? 34.356  36.907  14.011 1.00 42.24  ? 101 HIS B CB     1 
ATOM   3636  C CG     . HIS B 1 101 ? 34.772  36.519  12.630 1.00 46.38  ? 101 HIS B CG     1 
ATOM   3637  N ND1    . HIS B 1 101 ? 35.439  37.381  11.788 1.00 47.33  ? 101 HIS B ND1    1 
ATOM   3638  C CD2    . HIS B 1 101 ? 34.597  35.375  11.931 1.00 49.15  ? 101 HIS B CD2    1 
ATOM   3639  C CE1    . HIS B 1 101 ? 35.669  36.779  10.635 1.00 48.64  ? 101 HIS B CE1    1 
ATOM   3640  N NE2    . HIS B 1 101 ? 35.167  35.561  10.696 1.00 48.46  ? 101 HIS B NE2    1 
ATOM   3641  N N      . PRO B 1 102 ? 35.674  37.595  17.103 1.00 37.53  ? 102 PRO B N      1 
ATOM   3642  C CA     . PRO B 1 102 ? 35.281  38.190  18.363 1.00 32.08  ? 102 PRO B CA     1 
ATOM   3643  C C      . PRO B 1 102 ? 34.171  39.167  18.226 1.00 33.43  ? 102 PRO B C      1 
ATOM   3644  O O      . PRO B 1 102 ? 34.081  39.814  17.216 1.00 37.05  ? 102 PRO B O      1 
ATOM   3645  C CB     . PRO B 1 102 ? 36.529  38.925  18.768 1.00 31.29  ? 102 PRO B CB     1 
ATOM   3646  C CG     . PRO B 1 102 ? 37.637  38.140  18.206 1.00 29.91  ? 102 PRO B CG     1 
ATOM   3647  C CD     . PRO B 1 102 ? 37.111  37.863  16.849 1.00 35.34  ? 102 PRO B CD     1 
ATOM   3648  N N      . VAL B 1 103 ? 33.329  39.301  19.236 1.00 31.68  ? 103 VAL B N      1 
ATOM   3649  C CA     . VAL B 1 103 ? 32.160  40.161  19.124 1.00 32.84  ? 103 VAL B CA     1 
ATOM   3650  C C      . VAL B 1 103 ? 32.000  41.327  20.080 1.00 35.67  ? 103 VAL B C      1 
ATOM   3651  O O      . VAL B 1 103 ? 31.704  41.129  21.236 1.00 38.16  ? 103 VAL B O      1 
ATOM   3652  C CB     . VAL B 1 103 ? 30.880  39.331  19.197 1.00 34.87  ? 103 VAL B CB     1 
ATOM   3653  C CG1    . VAL B 1 103 ? 29.676  40.205  18.907 1.00 42.01  ? 103 VAL B CG1    1 
ATOM   3654  C CG2    . VAL B 1 103 ? 30.921  38.215  18.175 1.00 36.89  ? 103 VAL B CG2    1 
ATOM   3655  N N      . LEU B 1 104 ? 32.174  42.552  19.595 1.00 31.78  ? 104 LEU B N      1 
ATOM   3656  C CA     . LEU B 1 104 ? 31.935  43.718  20.408 1.00 28.72  ? 104 LEU B CA     1 
ATOM   3657  C C      . LEU B 1 104 ? 30.472  43.941  20.322 1.00 32.75  ? 104 LEU B C      1 
ATOM   3658  O O      . LEU B 1 104 ? 29.890  43.802  19.265 1.00 32.67  ? 104 LEU B O      1 
ATOM   3659  C CB     . LEU B 1 104 ? 32.648  44.932  19.854 1.00 29.68  ? 104 LEU B CB     1 
ATOM   3660  C CG     . LEU B 1 104 ? 32.781  46.184  20.722 1.00 33.23  ? 104 LEU B CG     1 
ATOM   3661  C CD1    . LEU B 1 104 ? 34.110  46.863  20.466 1.00 38.91  ? 104 LEU B CD1    1 
ATOM   3662  C CD2    . LEU B 1 104 ? 31.646  47.162  20.494 1.00 30.17  ? 104 LEU B CD2    1 
ATOM   3663  N N      . LEU B 1 105 ? 29.853  44.271  21.435 1.00 33.33  ? 105 LEU B N      1 
ATOM   3664  C CA     . LEU B 1 105 ? 28.446  44.502  21.452 1.00 35.69  ? 105 LEU B CA     1 
ATOM   3665  C C      . LEU B 1 105 ? 28.269  45.838  22.084 1.00 35.01  ? 105 LEU B C      1 
ATOM   3666  O O      . LEU B 1 105 ? 29.203  46.415  22.592 1.00 31.09  ? 105 LEU B O      1 
ATOM   3667  C CB     . LEU B 1 105 ? 27.757  43.462  22.299 1.00 34.49  ? 105 LEU B CB     1 
ATOM   3668  C CG     . LEU B 1 105 ? 27.803  41.967  22.050 1.00 42.93  ? 105 LEU B CG     1 
ATOM   3669  C CD1    . LEU B 1 105 ? 27.454  41.288  23.357 1.00 45.76  ? 105 LEU B CD1    1 
ATOM   3670  C CD2    . LEU B 1 105 ? 26.784  41.604  20.993 1.00 47.76  ? 105 LEU B CD2    1 
ATOM   3671  N N      . THR B 1 106 ? 27.060  46.350  22.044 1.00 37.21  ? 106 THR B N      1 
ATOM   3672  C CA     . THR B 1 106 ? 26.795  47.615  22.631 1.00 31.53  ? 106 THR B CA     1 
ATOM   3673  C C      . THR B 1 106 ? 25.686  47.479  23.574 1.00 37.31  ? 106 THR B C      1 
ATOM   3674  O O      . THR B 1 106 ? 24.783  46.703  23.365 1.00 45.03  ? 106 THR B O      1 
ATOM   3675  C CB     . THR B 1 106 ? 26.325  48.613  21.621 1.00 37.75  ? 106 THR B CB     1 
ATOM   3676  O OG1    . THR B 1 106 ? 25.197  48.081  20.930 1.00 40.40  ? 106 THR B OG1    1 
ATOM   3677  C CG2    . THR B 1 106 ? 27.436  48.951  20.649 1.00 38.24  ? 106 THR B CG2    1 
ATOM   3678  N N      . GLU B 1 107 ? 25.758  48.250  24.634 1.00 43.23  ? 107 GLU B N      1 
ATOM   3679  C CA     . GLU B 1 107 ? 24.747  48.216  25.625 1.00 43.19  ? 107 GLU B CA     1 
ATOM   3680  C C      . GLU B 1 107 ? 24.391  49.632  25.812 1.00 43.52  ? 107 GLU B C      1 
ATOM   3681  O O      . GLU B 1 107 ? 25.164  50.521  25.526 1.00 43.49  ? 107 GLU B O      1 
ATOM   3682  C CB     . GLU B 1 107 ? 25.279  47.613  26.915 1.00 41.21  ? 107 GLU B CB     1 
ATOM   3683  C CG     . GLU B 1 107 ? 26.396  48.360  27.600 1.00 48.71  ? 107 GLU B CG     1 
ATOM   3684  C CD     . GLU B 1 107 ? 26.744  47.716  28.913 1.00 51.69  ? 107 GLU B CD     1 
ATOM   3685  O OE1    . GLU B 1 107 ? 26.096  46.706  29.237 1.00 53.91  ? 107 GLU B OE1    1 
ATOM   3686  O OE2    . GLU B 1 107 ? 27.647  48.209  29.614 1.00 50.85  ? 107 GLU B OE2    1 
ATOM   3687  N N      . ALA B 1 108 ? 23.190  49.857  26.259 1.00 40.65  ? 108 ALA B N      1 
ATOM   3688  C CA     . ALA B 1 108 ? 22.732  51.187  26.419 1.00 36.95  ? 108 ALA B CA     1 
ATOM   3689  C C      . ALA B 1 108 ? 23.218  51.762  27.668 1.00 36.03  ? 108 ALA B C      1 
ATOM   3690  O O      . ALA B 1 108 ? 23.725  51.078  28.531 1.00 42.70  ? 108 ALA B O      1 
ATOM   3691  C CB     . ALA B 1 108 ? 21.232  51.191  26.446 1.00 36.31  ? 108 ALA B CB     1 
ATOM   3692  N N      . PRO B 1 109 ? 23.074  53.050  27.778 1.00 33.85  ? 109 PRO B N      1 
ATOM   3693  C CA     . PRO B 1 109 ? 23.400  53.606  29.055 1.00 35.19  ? 109 PRO B CA     1 
ATOM   3694  C C      . PRO B 1 109 ? 22.460  53.039  30.081 1.00 36.64  ? 109 PRO B C      1 
ATOM   3695  O O      . PRO B 1 109 ? 21.303  52.817  29.764 1.00 35.66  ? 109 PRO B O      1 
ATOM   3696  C CB     . PRO B 1 109 ? 23.082  55.057  28.840 1.00 38.83  ? 109 PRO B CB     1 
ATOM   3697  C CG     . PRO B 1 109 ? 23.493  55.307  27.439 1.00 41.34  ? 109 PRO B CG     1 
ATOM   3698  C CD     . PRO B 1 109 ? 23.155  54.051  26.704 1.00 43.31  ? 109 PRO B CD     1 
ATOM   3699  N N      . LEU B 1 110 ? 22.942  52.805  31.290 1.00 33.58  ? 110 LEU B N      1 
ATOM   3700  C CA     . LEU B 1 110 ? 22.132  52.285  32.383 1.00 31.52  ? 110 LEU B CA     1 
ATOM   3701  C C      . LEU B 1 110 ? 21.507  50.920  32.204 1.00 36.33  ? 110 LEU B C      1 
ATOM   3702  O O      . LEU B 1 110 ? 20.393  50.697  32.645 1.00 34.16  ? 110 LEU B O      1 
ATOM   3703  C CB     . LEU B 1 110 ? 21.098  53.314  32.798 1.00 30.19  ? 110 LEU B CB     1 
ATOM   3704  C CG     . LEU B 1 110 ? 21.597  54.711  33.157 1.00 26.76  ? 110 LEU B CG     1 
ATOM   3705  C CD1    . LEU B 1 110 ? 20.431  55.601  33.540 1.00 26.31  ? 110 LEU B CD1    1 
ATOM   3706  C CD2    . LEU B 1 110 ? 22.614  54.649  34.279 1.00 35.16  ? 110 LEU B CD2    1 
ATOM   3707  N N      . ASN B 1 111 ? 22.229  49.996  31.582 1.00 42.61  ? 111 ASN B N      1 
ATOM   3708  C CA     . ASN B 1 111 ? 21.738  48.640  31.374 1.00 42.26  ? 111 ASN B CA     1 
ATOM   3709  C C      . ASN B 1 111 ? 21.789  48.024  32.730 1.00 44.13  ? 111 ASN B C      1 
ATOM   3710  O O      . ASN B 1 111 ? 22.832  48.086  33.357 1.00 44.26  ? 111 ASN B O      1 
ATOM   3711  C CB     . ASN B 1 111 ? 22.671  47.868  30.473 1.00 38.42  ? 111 ASN B CB     1 
ATOM   3712  C CG     . ASN B 1 111 ? 21.942  46.936  29.535 1.00 50.24  ? 111 ASN B CG     1 
ATOM   3713  O OD1    . ASN B 1 111 ? 20.720  46.927  29.482 1.00 54.57  ? 111 ASN B OD1    1 
ATOM   3714  N ND2    . ASN B 1 111 ? 22.695  46.150  28.785 1.00 57.03  ? 111 ASN B ND2    1 
ATOM   3715  N N      . PRO B 1 112 ? 20.682  47.414  33.207 1.00 41.52  ? 112 PRO B N      1 
ATOM   3716  C CA     . PRO B 1 112 ? 20.819  46.928  34.563 1.00 41.34  ? 112 PRO B CA     1 
ATOM   3717  C C      . PRO B 1 112 ? 21.960  45.970  34.700 1.00 50.11  ? 112 PRO B C      1 
ATOM   3718  O O      . PRO B 1 112 ? 22.341  45.327  33.733 1.00 49.10  ? 112 PRO B O      1 
ATOM   3719  C CB     . PRO B 1 112 ? 19.498  46.254  34.817 1.00 38.83  ? 112 PRO B CB     1 
ATOM   3720  C CG     . PRO B 1 112 ? 18.534  47.004  33.989 1.00 38.70  ? 112 PRO B CG     1 
ATOM   3721  C CD     . PRO B 1 112 ? 19.298  47.200  32.724 1.00 43.04  ? 112 PRO B CD     1 
ATOM   3722  N N      . LYS B 1 113 ? 22.513  45.869  35.896 1.00 54.82  ? 113 LYS B N      1 
ATOM   3723  C CA     . LYS B 1 113 ? 23.634  44.993  36.150 1.00 51.80  ? 113 LYS B CA     1 
ATOM   3724  C C      . LYS B 1 113 ? 23.360  43.680  35.530 1.00 56.97  ? 113 LYS B C      1 
ATOM   3725  O O      . LYS B 1 113 ? 24.215  43.097  34.889 1.00 56.68  ? 113 LYS B O      1 
ATOM   3726  C CB     . LYS B 1 113 ? 23.728  44.803  37.649 1.00 49.64  ? 113 LYS B CB     1 
ATOM   3727  C CG     . LYS B 1 113 ? 24.898  43.983  38.143 1.00 62.97  ? 113 LYS B CG     1 
ATOM   3728  C CD     . LYS B 1 113 ? 24.439  42.753  38.912 1.00 69.72  ? 113 LYS B CD     1 
ATOM   3729  C CE     . LYS B 1 113 ? 23.663  43.137  40.158 1.00 68.85  ? 113 LYS B CE     1 
ATOM   3730  N NZ     . LYS B 1 113 ? 24.492  43.920  41.111 1.00 69.83  ? 113 LYS B NZ     1 
ATOM   3731  N N      . ALA B 1 114 ? 22.137  43.217  35.659 1.00 56.04  ? 114 ALA B N      1 
ATOM   3732  C CA     . ALA B 1 114 ? 21.798  41.896  35.183 1.00 54.13  ? 114 ALA B CA     1 
ATOM   3733  C C      . ALA B 1 114 ? 21.764  41.673  33.702 1.00 47.24  ? 114 ALA B C      1 
ATOM   3734  O O      . ALA B 1 114 ? 22.153  40.617  33.242 1.00 45.16  ? 114 ALA B O      1 
ATOM   3735  C CB     . ALA B 1 114 ? 20.465  41.527  35.766 1.00 54.69  ? 114 ALA B CB     1 
ATOM   3736  N N      . ASN B 1 115 ? 21.262  42.628  32.945 1.00 42.18  ? 115 ASN B N      1 
ATOM   3737  C CA     . ASN B 1 115 ? 21.102  42.409  31.527 1.00 41.66  ? 115 ASN B CA     1 
ATOM   3738  C C      . ASN B 1 115 ? 22.416  42.191  30.866 1.00 44.14  ? 115 ASN B C      1 
ATOM   3739  O O      . ASN B 1 115 ? 22.511  41.466  29.898 1.00 45.79  ? 115 ASN B O      1 
ATOM   3740  C CB     . ASN B 1 115 ? 20.383  43.573  30.892 1.00 43.59  ? 115 ASN B CB     1 
ATOM   3741  C CG     . ASN B 1 115 ? 18.909  43.580  31.208 1.00 53.32  ? 115 ASN B CG     1 
ATOM   3742  O OD1    . ASN B 1 115 ? 18.434  42.780  32.009 1.00 54.67  ? 115 ASN B OD1    1 
ATOM   3743  N ND2    . ASN B 1 115 ? 18.173  44.481  30.574 1.00 53.60  ? 115 ASN B ND2    1 
ATOM   3744  N N      . ARG B 1 116 ? 23.453  42.798  31.395 1.00 47.37  ? 116 ARG B N      1 
ATOM   3745  C CA     . ARG B 1 116 ? 24.758  42.693  30.781 1.00 50.52  ? 116 ARG B CA     1 
ATOM   3746  C C      . ARG B 1 116 ? 25.228  41.280  30.834 1.00 50.25  ? 116 ARG B C      1 
ATOM   3747  O O      . ARG B 1 116 ? 25.789  40.770  29.883 1.00 49.53  ? 116 ARG B O      1 
ATOM   3748  C CB     . ARG B 1 116 ? 25.750  43.519  31.563 1.00 55.75  ? 116 ARG B CB     1 
ATOM   3749  C CG     . ARG B 1 116 ? 25.276  44.866  32.057 1.00 54.20  ? 116 ARG B CG     1 
ATOM   3750  C CD     . ARG B 1 116 ? 26.464  45.621  32.628 1.00 56.07  ? 116 ARG B CD     1 
ATOM   3751  N NE     . ARG B 1 116 ? 27.430  45.939  31.584 1.00 58.98  ? 116 ARG B NE     1 
ATOM   3752  C CZ     . ARG B 1 116 ? 28.748  45.916  31.736 1.00 60.40  ? 116 ARG B CZ     1 
ATOM   3753  N NH1    . ARG B 1 116 ? 29.278  45.576  32.894 1.00 57.78  ? 116 ARG B NH1    1 
ATOM   3754  N NH2    . ARG B 1 116 ? 29.537  46.223  30.719 1.00 51.86  ? 116 ARG B NH2    1 
ATOM   3755  N N      . GLU B 1 117 ? 25.028  40.647  31.972 1.00 47.25  ? 117 GLU B N      1 
ATOM   3756  C CA     . GLU B 1 117 ? 25.482  39.293  32.159 1.00 47.25  ? 117 GLU B CA     1 
ATOM   3757  C C      . GLU B 1 117 ? 24.834  38.295  31.243 1.00 49.09  ? 117 GLU B C      1 
ATOM   3758  O O      . GLU B 1 117 ? 25.480  37.363  30.808 1.00 50.28  ? 117 GLU B O      1 
ATOM   3759  C CB     . GLU B 1 117 ? 25.209  38.864  33.579 1.00 49.49  ? 117 GLU B CB     1 
ATOM   3760  C CG     . GLU B 1 117 ? 26.067  39.522  34.638 1.00 52.37  ? 117 GLU B CG     1 
ATOM   3761  C CD     . GLU B 1 117 ? 25.826  38.919  36.005 1.00 54.08  ? 117 GLU B CD     1 
ATOM   3762  O OE1    . GLU B 1 117 ? 25.004  37.992  36.103 1.00 61.10  ? 117 GLU B OE1    1 
ATOM   3763  O OE2    . GLU B 1 117 ? 26.453  39.362  36.983 1.00 52.07  ? 117 GLU B OE2    1 
ATOM   3764  N N      . LYS B 1 118 ? 23.554  38.448  30.971 1.00 46.23  ? 118 LYS B N      1 
ATOM   3765  C CA     . LYS B 1 118 ? 22.866  37.470  30.163 1.00 44.04  ? 118 LYS B CA     1 
ATOM   3766  C C      . LYS B 1 118 ? 23.361  37.600  28.753 1.00 46.38  ? 118 LYS B C      1 
ATOM   3767  O O      . LYS B 1 118 ? 23.329  36.658  27.995 1.00 51.09  ? 118 LYS B O      1 
ATOM   3768  C CB     . LYS B 1 118 ? 21.371  37.666  30.289 1.00 38.52  ? 118 LYS B CB     1 
ATOM   3769  C CG     . LYS B 1 118 ? 20.512  36.592  29.650 1.00 56.35  ? 118 LYS B CG     1 
ATOM   3770  C CD     . LYS B 1 118 ? 20.686  35.249  30.328 1.00 57.17  ? 118 LYS B CD     1 
ATOM   3771  C CE     . LYS B 1 118 ? 19.608  34.275  29.886 1.00 55.69  ? 118 LYS B CE     1 
ATOM   3772  N NZ     . LYS B 1 118 ? 19.544  34.128  28.407 1.00 48.80  ? 118 LYS B NZ     1 
ATOM   3773  N N      . MET B 1 119 ? 23.875  38.757  28.406 1.00 42.12  ? 119 MET B N      1 
ATOM   3774  C CA     . MET B 1 119 ? 24.386  38.989  27.061 1.00 47.26  ? 119 MET B CA     1 
ATOM   3775  C C      . MET B 1 119 ? 25.683  38.284  26.943 1.00 46.51  ? 119 MET B C      1 
ATOM   3776  O O      . MET B 1 119 ? 25.987  37.692  25.930 1.00 48.83  ? 119 MET B O      1 
ATOM   3777  C CB     . MET B 1 119 ? 24.649  40.474  26.876 1.00 54.83  ? 119 MET B CB     1 
ATOM   3778  C CG     . MET B 1 119 ? 24.456  41.029  25.486 1.00 55.94  ? 119 MET B CG     1 
ATOM   3779  S SD     . MET B 1 119 ? 24.649  42.819  25.479 1.00 58.22  ? 119 MET B SD     1 
ATOM   3780  C CE     . MET B 1 119 ? 23.422  43.313  26.678 1.00 41.79  ? 119 MET B CE     1 
ATOM   3781  N N      . THR B 1 120 ? 26.473  38.368  27.986 1.00 44.38  ? 120 THR B N      1 
ATOM   3782  C CA     . THR B 1 120 ? 27.726  37.685  27.992 1.00 45.45  ? 120 THR B CA     1 
ATOM   3783  C C      . THR B 1 120 ? 27.435  36.214  27.882 1.00 45.90  ? 120 THR B C      1 
ATOM   3784  O O      . THR B 1 120 ? 28.116  35.491  27.182 1.00 44.41  ? 120 THR B O      1 
ATOM   3785  C CB     . THR B 1 120 ? 28.468  37.999  29.280 1.00 44.55  ? 120 THR B CB     1 
ATOM   3786  O OG1    . THR B 1 120 ? 28.465  39.414  29.482 1.00 39.85  ? 120 THR B OG1    1 
ATOM   3787  C CG2    . THR B 1 120 ? 29.899  37.509  29.220 1.00 47.74  ? 120 THR B CG2    1 
ATOM   3788  N N      . GLN B 1 121 ? 26.387  35.764  28.534 1.00 42.14  ? 121 GLN B N      1 
ATOM   3789  C CA     . GLN B 1 121 ? 26.072  34.356  28.536 1.00 41.81  ? 121 GLN B CA     1 
ATOM   3790  C C      . GLN B 1 121 ? 25.668  33.887  27.177 1.00 49.02  ? 121 GLN B C      1 
ATOM   3791  O O      . GLN B 1 121 ? 26.189  32.911  26.697 1.00 53.19  ? 121 GLN B O      1 
ATOM   3792  C CB     . GLN B 1 121 ? 24.961  34.084  29.531 1.00 42.63  ? 121 GLN B CB     1 
ATOM   3793  C CG     . GLN B 1 121 ? 24.580  32.634  29.699 1.00 48.88  ? 121 GLN B CG     1 
ATOM   3794  C CD     . GLN B 1 121 ? 23.656  32.426  30.875 1.00 58.77  ? 121 GLN B CD     1 
ATOM   3795  O OE1    . GLN B 1 121 ? 23.372  33.356  31.623 1.00 68.77  ? 121 GLN B OE1    1 
ATOM   3796  N NE2    . GLN B 1 121 ? 23.185  31.200  31.049 1.00 54.92  ? 121 GLN B NE2    1 
ATOM   3797  N N      . ILE B 1 122 ? 24.766  34.587  26.517 1.00 49.20  ? 122 ILE B N      1 
ATOM   3798  C CA     . ILE B 1 122 ? 24.266  34.144  25.226 1.00 41.58  ? 122 ILE B CA     1 
ATOM   3799  C C      . ILE B 1 122 ? 25.351  34.038  24.184 1.00 39.07  ? 122 ILE B C      1 
ATOM   3800  O O      . ILE B 1 122 ? 25.429  33.076  23.467 1.00 41.30  ? 122 ILE B O      1 
ATOM   3801  C CB     . ILE B 1 122 ? 23.145  35.054  24.753 1.00 37.78  ? 122 ILE B CB     1 
ATOM   3802  C CG1    . ILE B 1 122 ? 21.958  34.927  25.698 1.00 41.30  ? 122 ILE B CG1    1 
ATOM   3803  C CG2    . ILE B 1 122 ? 22.703  34.695  23.352 1.00 46.56  ? 122 ILE B CG2    1 
ATOM   3804  C CD1    . ILE B 1 122 ? 20.815  35.849  25.362 1.00 40.51  ? 122 ILE B CD1    1 
ATOM   3805  N N      . MET B 1 123 ? 26.226  35.009  24.114 1.00 38.89  ? 123 MET B N      1 
ATOM   3806  C CA     . MET B 1 123 ? 27.257  34.955  23.119 1.00 41.76  ? 123 MET B CA     1 
ATOM   3807  C C      . MET B 1 123 ? 28.122  33.765  23.362 1.00 43.16  ? 123 MET B C      1 
ATOM   3808  O O      . MET B 1 123 ? 28.256  32.922  22.508 1.00 45.29  ? 123 MET B O      1 
ATOM   3809  C CB     . MET B 1 123 ? 28.103  36.204  23.128 1.00 40.10  ? 123 MET B CB     1 
ATOM   3810  C CG     . MET B 1 123 ? 27.355  37.453  22.732 1.00 51.19  ? 123 MET B CG     1 
ATOM   3811  S SD     . MET B 1 123 ? 27.327  37.621  20.951 1.00 62.38  ? 123 MET B SD     1 
ATOM   3812  C CE     . MET B 1 123 ? 25.694  38.273  20.722 1.00 43.97  ? 123 MET B CE     1 
ATOM   3813  N N      . PHE B 1 124 ? 28.713  33.661  24.527 1.00 41.58  ? 124 PHE B N      1 
ATOM   3814  C CA     . PHE B 1 124 ? 29.621  32.566  24.736 1.00 41.34  ? 124 PHE B CA     1 
ATOM   3815  C C      . PHE B 1 124 ? 28.913  31.235  24.732 1.00 42.67  ? 124 PHE B C      1 
ATOM   3816  O O      . PHE B 1 124 ? 29.346  30.312  24.085 1.00 44.45  ? 124 PHE B O      1 
ATOM   3817  C CB     . PHE B 1 124 ? 30.361  32.738  26.021 1.00 38.82  ? 124 PHE B CB     1 
ATOM   3818  C CG     . PHE B 1 124 ? 31.513  33.672  25.939 1.00 36.97  ? 124 PHE B CG     1 
ATOM   3819  C CD1    . PHE B 1 124 ? 32.546  33.427  25.072 1.00 33.61  ? 124 PHE B CD1    1 
ATOM   3820  C CD2    . PHE B 1 124 ? 31.582  34.768  26.765 1.00 38.66  ? 124 PHE B CD2    1 
ATOM   3821  C CE1    . PHE B 1 124 ? 33.619  34.276  25.008 1.00 36.54  ? 124 PHE B CE1    1 
ATOM   3822  C CE2    . PHE B 1 124 ? 32.654  35.621  26.712 1.00 45.67  ? 124 PHE B CE2    1 
ATOM   3823  C CZ     . PHE B 1 124 ? 33.671  35.374  25.829 1.00 46.58  ? 124 PHE B CZ     1 
ATOM   3824  N N      . GLU B 1 125 ? 27.796  31.120  25.413 1.00 41.56  ? 125 GLU B N      1 
ATOM   3825  C CA     . GLU B 1 125 ? 27.052  29.876  25.373 1.00 37.80  ? 125 GLU B CA     1 
ATOM   3826  C C      . GLU B 1 125 ? 26.347  29.530  24.056 1.00 36.29  ? 125 GLU B C      1 
ATOM   3827  O O      . GLU B 1 125 ? 26.660  28.515  23.468 1.00 36.53  ? 125 GLU B O      1 
ATOM   3828  C CB     . GLU B 1 125 ? 26.112  29.813  26.559 1.00 40.17  ? 125 GLU B CB     1 
ATOM   3829  C CG     . GLU B 1 125 ? 26.850  29.809  27.888 1.00 47.12  ? 125 GLU B CG     1 
ATOM   3830  C CD     . GLU B 1 125 ? 25.994  29.336  29.044 1.00 57.45  ? 125 GLU B CD     1 
ATOM   3831  O OE1    . GLU B 1 125 ? 24.825  28.970  28.814 1.00 61.68  ? 125 GLU B OE1    1 
ATOM   3832  O OE2    . GLU B 1 125 ? 26.492  29.328  30.187 1.00 53.06  ? 125 GLU B OE2    1 
ATOM   3833  N N      . THR B 1 126 ? 25.429  30.358  23.571 1.00 40.91  ? 126 THR B N      1 
ATOM   3834  C CA     . THR B 1 126 ? 24.734  30.104  22.305 1.00 40.08  ? 126 THR B CA     1 
ATOM   3835  C C      . THR B 1 126 ? 25.610  30.231  21.072 1.00 39.25  ? 126 THR B C      1 
ATOM   3836  O O      . THR B 1 126 ? 25.569  29.374  20.199 1.00 42.10  ? 126 THR B O      1 
ATOM   3837  C CB     . THR B 1 126 ? 23.500  30.995  22.123 1.00 31.86  ? 126 THR B CB     1 
ATOM   3838  O OG1    . THR B 1 126 ? 22.726  30.999  23.324 1.00 41.73  ? 126 THR B OG1    1 
ATOM   3839  C CG2    . THR B 1 126 ? 22.638  30.498  20.986 1.00 27.63  ? 126 THR B CG2    1 
ATOM   3840  N N      . PHE B 1 127 ? 26.441  31.258  20.994 1.00 33.61  ? 127 PHE B N      1 
ATOM   3841  C CA     . PHE B 1 127 ? 27.222  31.472  19.791 1.00 34.81  ? 127 PHE B CA     1 
ATOM   3842  C C      . PHE B 1 127 ? 28.680  31.086  19.861 1.00 37.38  ? 127 PHE B C      1 
ATOM   3843  O O      . PHE B 1 127 ? 29.345  31.037  18.843 1.00 35.95  ? 127 PHE B O      1 
ATOM   3844  C CB     . PHE B 1 127 ? 27.098  32.922  19.387 1.00 38.76  ? 127 PHE B CB     1 
ATOM   3845  C CG     . PHE B 1 127 ? 25.681  33.384  19.197 1.00 42.10  ? 127 PHE B CG     1 
ATOM   3846  C CD1    . PHE B 1 127 ? 24.929  32.930  18.135 1.00 41.24  ? 127 PHE B CD1    1 
ATOM   3847  C CD2    . PHE B 1 127 ? 25.110  34.282  20.074 1.00 38.63  ? 127 PHE B CD2    1 
ATOM   3848  C CE1    . PHE B 1 127 ? 23.630  33.353  17.959 1.00 41.26  ? 127 PHE B CE1    1 
ATOM   3849  C CE2    . PHE B 1 127 ? 23.813  34.709  19.905 1.00 33.94  ? 127 PHE B CE2    1 
ATOM   3850  C CZ     . PHE B 1 127 ? 23.071  34.243  18.847 1.00 35.88  ? 127 PHE B CZ     1 
ATOM   3851  N N      . ASN B 1 128 ? 29.188  30.805  21.045 1.00 38.96  ? 128 ASN B N      1 
ATOM   3852  C CA     . ASN B 1 128 ? 30.591  30.421  21.243 1.00 38.93  ? 128 ASN B CA     1 
ATOM   3853  C C      . ASN B 1 128 ? 31.564  31.384  20.666 1.00 39.70  ? 128 ASN B C      1 
ATOM   3854  O O      . ASN B 1 128 ? 32.520  30.998  20.021 1.00 36.85  ? 128 ASN B O      1 
ATOM   3855  C CB     . ASN B 1 128 ? 30.874  28.997  20.807 1.00 41.36  ? 128 ASN B CB     1 
ATOM   3856  C CG     . ASN B 1 128 ? 30.599  27.991  21.901 1.00 42.63  ? 128 ASN B CG     1 
ATOM   3857  O OD1    . ASN B 1 128 ? 31.055  28.148  23.030 1.00 47.40  ? 128 ASN B OD1    1 
ATOM   3858  N ND2    . ASN B 1 128 ? 29.858  26.946  21.571 1.00 42.26  ? 128 ASN B ND2    1 
ATOM   3859  N N      . THR B 1 129 ? 31.329  32.655  20.922 1.00 44.54  ? 129 THR B N      1 
ATOM   3860  C CA     . THR B 1 129 ? 32.188  33.680  20.412 1.00 41.26  ? 129 THR B CA     1 
ATOM   3861  C C      . THR B 1 129 ? 33.534  33.492  21.037 1.00 41.39  ? 129 THR B C      1 
ATOM   3862  O O      . THR B 1 129 ? 33.634  33.123  22.189 1.00 41.95  ? 129 THR B O      1 
ATOM   3863  C CB     . THR B 1 129 ? 31.629  35.046  20.747 1.00 31.86  ? 129 THR B CB     1 
ATOM   3864  O OG1    . THR B 1 129 ? 31.471  35.155  22.159 1.00 41.72  ? 129 THR B OG1    1 
ATOM   3865  C CG2    . THR B 1 129 ? 30.288  35.206  20.100 1.00 33.44  ? 129 THR B CG2    1 
ATOM   3866  N N      . PRO B 1 130 ? 34.619  33.690  20.254 1.00 36.94  ? 130 PRO B N      1 
ATOM   3867  C CA     . PRO B 1 130 ? 35.876  33.437  20.933 1.00 31.86  ? 130 PRO B CA     1 
ATOM   3868  C C      . PRO B 1 130 ? 36.067  34.395  22.053 1.00 35.71  ? 130 PRO B C      1 
ATOM   3869  O O      . PRO B 1 130 ? 36.588  34.014  23.085 1.00 34.94  ? 130 PRO B O      1 
ATOM   3870  C CB     . PRO B 1 130 ? 36.894  33.772  19.873 1.00 34.36  ? 130 PRO B CB     1 
ATOM   3871  C CG     . PRO B 1 130 ? 36.217  33.589  18.585 1.00 36.81  ? 130 PRO B CG     1 
ATOM   3872  C CD     . PRO B 1 130 ? 34.852  34.098  18.852 1.00 36.75  ? 130 PRO B CD     1 
ATOM   3873  N N      . ALA B 1 131 ? 35.638  35.631  21.858 1.00 38.68  ? 131 ALA B N      1 
ATOM   3874  C CA     . ALA B 1 131 ? 35.812  36.666  22.848 1.00 34.22  ? 131 ALA B CA     1 
ATOM   3875  C C      . ALA B 1 131 ? 34.676  37.650  22.782 1.00 36.18  ? 131 ALA B C      1 
ATOM   3876  O O      . ALA B 1 131 ? 33.851  37.564  21.899 1.00 40.94  ? 131 ALA B O      1 
ATOM   3877  C CB     . ALA B 1 131 ? 37.106  37.366  22.591 1.00 31.87  ? 131 ALA B CB     1 
ATOM   3878  N N      . MET B 1 132 ? 34.638  38.601  23.702 1.00 33.71  ? 132 MET B N      1 
ATOM   3879  C CA     . MET B 1 132 ? 33.547  39.546  23.741 1.00 36.76  ? 132 MET B CA     1 
ATOM   3880  C C      . MET B 1 132 ? 33.823  40.829  24.470 1.00 36.43  ? 132 MET B C      1 
ATOM   3881  O O      . MET B 1 132 ? 34.711  40.865  25.286 1.00 43.07  ? 132 MET B O      1 
ATOM   3882  C CB     . MET B 1 132 ? 32.354  38.902  24.431 1.00 36.15  ? 132 MET B CB     1 
ATOM   3883  C CG     . MET B 1 132 ? 31.074  39.692  24.293 1.00 55.95  ? 132 MET B CG     1 
ATOM   3884  S SD     . MET B 1 132 ? 30.097  39.344  25.731 1.00 59.53  ? 132 MET B SD     1 
ATOM   3885  C CE     . MET B 1 132 ? 30.155  37.584  25.532 1.00 41.23  ? 132 MET B CE     1 
ATOM   3886  N N      . TYR B 1 133 ? 33.080  41.891  24.174 1.00 32.18  ? 133 TYR B N      1 
ATOM   3887  C CA     . TYR B 1 133 ? 33.180  43.132  24.916 1.00 34.77  ? 133 TYR B CA     1 
ATOM   3888  C C      . TYR B 1 133 ? 31.838  43.783  24.840 1.00 32.63  ? 133 TYR B C      1 
ATOM   3889  O O      . TYR B 1 133 ? 31.204  43.733  23.813 1.00 35.69  ? 133 TYR B O      1 
ATOM   3890  C CB     . TYR B 1 133 ? 34.237  44.046  24.348 1.00 38.54  ? 133 TYR B CB     1 
ATOM   3891  C CG     . TYR B 1 133 ? 34.692  45.157  25.262 1.00 37.15  ? 133 TYR B CG     1 
ATOM   3892  C CD1    . TYR B 1 133 ? 34.043  46.380  25.276 1.00 36.54  ? 133 TYR B CD1    1 
ATOM   3893  C CD2    . TYR B 1 133 ? 35.790  44.994  26.084 1.00 33.02  ? 133 TYR B CD2    1 
ATOM   3894  C CE1    . TYR B 1 133 ? 34.459  47.398  26.104 1.00 38.95  ? 133 TYR B CE1    1 
ATOM   3895  C CE2    . TYR B 1 133 ? 36.214  46.007  26.915 1.00 36.06  ? 133 TYR B CE2    1 
ATOM   3896  C CZ     . TYR B 1 133 ? 35.544  47.206  26.919 1.00 40.80  ? 133 TYR B CZ     1 
ATOM   3897  O OH     . TYR B 1 133 ? 35.961  48.223  27.739 1.00 31.95  ? 133 TYR B OH     1 
ATOM   3898  N N      . VAL B 1 134 ? 31.394  44.399  25.926 1.00 27.96  ? 134 VAL B N      1 
ATOM   3899  C CA     . VAL B 1 134 ? 30.125  45.114  25.947 1.00 33.80  ? 134 VAL B CA     1 
ATOM   3900  C C      . VAL B 1 134 ? 30.381  46.575  26.300 1.00 30.68  ? 134 VAL B C      1 
ATOM   3901  O O      . VAL B 1 134 ? 30.996  46.863  27.309 1.00 37.65  ? 134 VAL B O      1 
ATOM   3902  C CB     . VAL B 1 134 ? 29.122  44.491  26.924 1.00 34.25  ? 134 VAL B CB     1 
ATOM   3903  C CG1    . VAL B 1 134 ? 27.705  44.758  26.464 1.00 38.80  ? 134 VAL B CG1    1 
ATOM   3904  C CG2    . VAL B 1 134 ? 29.338  42.995  27.041 1.00 32.17  ? 134 VAL B CG2    1 
ATOM   3905  N N      . ALA B 1 135 ? 29.915  47.502  25.481 1.00 31.83  ? 135 ALA B N      1 
ATOM   3906  C CA     . ALA B 1 135 ? 30.220  48.894  25.700 1.00 31.45  ? 135 ALA B CA     1 
ATOM   3907  C C      . ALA B 1 135 ? 29.062  49.834  25.618 1.00 36.18  ? 135 ALA B C      1 
ATOM   3908  O O      . ALA B 1 135 ? 28.103  49.577  24.941 1.00 40.85  ? 135 ALA B O      1 
ATOM   3909  C CB     . ALA B 1 135 ? 31.229  49.310  24.686 1.00 33.04  ? 135 ALA B CB     1 
ATOM   3910  N N      . ILE B 1 136 ? 29.173  50.958  26.308 1.00 37.11  ? 136 ILE B N      1 
ATOM   3911  C CA     . ILE B 1 136 ? 28.112  51.937  26.315 1.00 39.76  ? 136 ILE B CA     1 
ATOM   3912  C C      . ILE B 1 136 ? 28.203  52.657  25.012 1.00 45.07  ? 136 ILE B C      1 
ATOM   3913  O O      . ILE B 1 136 ? 29.230  53.224  24.700 1.00 50.36  ? 136 ILE B O      1 
ATOM   3914  C CB     . ILE B 1 136 ? 28.248  52.908  27.484 1.00 36.57  ? 136 ILE B CB     1 
ATOM   3915  C CG1    . ILE B 1 136 ? 28.342  52.151  28.802 1.00 37.29  ? 136 ILE B CG1    1 
ATOM   3916  C CG2    . ILE B 1 136 ? 27.078  53.867  27.522 1.00 37.90  ? 136 ILE B CG2    1 
ATOM   3917  C CD1    . ILE B 1 136 ? 26.999  51.804  29.399 1.00 37.96  ? 136 ILE B CD1    1 
ATOM   3918  N N      . GLN B 1 137 ? 27.139  52.649  24.242 1.00 44.61  ? 137 GLN B N      1 
ATOM   3919  C CA     . GLN B 1 137 ? 27.150  53.220  22.924 1.00 38.80  ? 137 GLN B CA     1 
ATOM   3920  C C      . GLN B 1 137 ? 27.682  54.607  22.938 1.00 36.22  ? 137 GLN B C      1 
ATOM   3921  O O      . GLN B 1 137 ? 28.415  54.997  22.063 1.00 32.88  ? 137 GLN B O      1 
ATOM   3922  C CB     . GLN B 1 137 ? 25.716  53.242  22.452 1.00 39.03  ? 137 GLN B CB     1 
ATOM   3923  C CG     . GLN B 1 137 ? 25.047  51.881  22.504 1.00 42.73  ? 137 GLN B CG     1 
ATOM   3924  C CD     . GLN B 1 137 ? 23.544  51.971  22.401 1.00 46.14  ? 137 GLN B CD     1 
ATOM   3925  O OE1    . GLN B 1 137 ? 22.970  53.042  22.553 1.00 52.85  ? 137 GLN B OE1    1 
ATOM   3926  N NE2    . GLN B 1 137 ? 22.896  50.842  22.151 1.00 44.21  ? 137 GLN B NE2    1 
ATOM   3927  N N      . ALA B 1 138 ? 27.349  55.370  23.944 1.00 36.72  ? 138 ALA B N      1 
ATOM   3928  C CA     . ALA B 1 138 ? 27.742  56.752  23.933 1.00 40.24  ? 138 ALA B CA     1 
ATOM   3929  C C      . ALA B 1 138 ? 29.193  56.978  24.136 1.00 43.59  ? 138 ALA B C      1 
ATOM   3930  O O      . ALA B 1 138 ? 29.747  57.923  23.607 1.00 50.65  ? 138 ALA B O      1 
ATOM   3931  C CB     . ALA B 1 138 ? 26.976  57.500  24.956 1.00 40.83  ? 138 ALA B CB     1 
ATOM   3932  N N      . VAL B 1 139 ? 29.833  56.133  24.913 1.00 37.85  ? 139 VAL B N      1 
ATOM   3933  C CA     . VAL B 1 139 ? 31.254  56.262  25.100 1.00 36.91  ? 139 VAL B CA     1 
ATOM   3934  C C      . VAL B 1 139 ? 31.857  56.006  23.768 1.00 40.60  ? 139 VAL B C      1 
ATOM   3935  O O      . VAL B 1 139 ? 32.765  56.698  23.359 1.00 43.45  ? 139 VAL B O      1 
ATOM   3936  C CB     . VAL B 1 139 ? 31.762  55.261  26.106 1.00 32.27  ? 139 VAL B CB     1 
ATOM   3937  C CG1    . VAL B 1 139 ? 33.197  55.562  26.443 1.00 32.13  ? 139 VAL B CG1    1 
ATOM   3938  C CG2    . VAL B 1 139 ? 30.938  55.362  27.372 1.00 37.06  ? 139 VAL B CG2    1 
ATOM   3939  N N      . LEU B 1 140 ? 31.326  55.027  23.055 1.00 40.24  ? 140 LEU B N      1 
ATOM   3940  C CA     . LEU B 1 140 ? 31.870  54.659  21.764 1.00 36.83  ? 140 LEU B CA     1 
ATOM   3941  C C      . LEU B 1 140 ? 31.763  55.797  20.815 1.00 35.28  ? 140 LEU B C      1 
ATOM   3942  O O      . LEU B 1 140 ? 32.651  56.031  20.029 1.00 41.45  ? 140 LEU B O      1 
ATOM   3943  C CB     . LEU B 1 140 ? 31.156  53.450  21.183 1.00 33.09  ? 140 LEU B CB     1 
ATOM   3944  C CG     . LEU B 1 140 ? 31.294  52.100  21.862 1.00 33.33  ? 140 LEU B CG     1 
ATOM   3945  C CD1    . LEU B 1 140 ? 30.594  51.057  21.017 1.00 25.80  ? 140 LEU B CD1    1 
ATOM   3946  C CD2    . LEU B 1 140 ? 32.760  51.756  22.011 1.00 37.77  ? 140 LEU B CD2    1 
ATOM   3947  N N      . SER B 1 141 ? 30.680  56.533  20.873 1.00 33.52  ? 141 SER B N      1 
ATOM   3948  C CA     . SER B 1 141 ? 30.476  57.583  19.902 1.00 38.19  ? 141 SER B CA     1 
ATOM   3949  C C      . SER B 1 141 ? 31.460  58.656  20.108 1.00 34.76  ? 141 SER B C      1 
ATOM   3950  O O      . SER B 1 141 ? 31.956  59.246  19.171 1.00 41.17  ? 141 SER B O      1 
ATOM   3951  C CB     . SER B 1 141 ? 29.102  58.172  20.062 1.00 38.21  ? 141 SER B CB     1 
ATOM   3952  O OG     . SER B 1 141 ? 28.100  57.186  19.957 1.00 45.60  ? 141 SER B OG     1 
ATOM   3953  N N      . LEU B 1 142 ? 31.763  58.918  21.357 1.00 37.35  ? 142 LEU B N      1 
ATOM   3954  C CA     . LEU B 1 142 ? 32.655  60.003  21.667 1.00 42.59  ? 142 LEU B CA     1 
ATOM   3955  C C      . LEU B 1 142 ? 33.992  59.597  21.165 1.00 44.10  ? 142 LEU B C      1 
ATOM   3956  O O      . LEU B 1 142 ? 34.799  60.427  20.809 1.00 49.40  ? 142 LEU B O      1 
ATOM   3957  C CB     . LEU B 1 142 ? 32.683  60.248  23.172 1.00 34.34  ? 142 LEU B CB     1 
ATOM   3958  C CG     . LEU B 1 142 ? 33.112  61.581  23.754 1.00 35.86  ? 142 LEU B CG     1 
ATOM   3959  C CD1    . LEU B 1 142 ? 31.937  62.524  23.827 1.00 37.42  ? 142 LEU B CD1    1 
ATOM   3960  C CD2    . LEU B 1 142 ? 33.605  61.306  25.152 1.00 39.44  ? 142 LEU B CD2    1 
ATOM   3961  N N      . TYR B 1 143 ? 34.227  58.307  21.087 1.00 36.30  ? 143 TYR B N      1 
ATOM   3962  C CA     . TYR B 1 143 ? 35.514  57.828  20.676 1.00 34.99  ? 143 TYR B CA     1 
ATOM   3963  C C      . TYR B 1 143 ? 35.789  58.128  19.231 1.00 38.96  ? 143 TYR B C      1 
ATOM   3964  O O      . TYR B 1 143 ? 36.916  58.370  18.861 1.00 38.59  ? 143 TYR B O      1 
ATOM   3965  C CB     . TYR B 1 143 ? 35.578  56.346  20.908 1.00 38.63  ? 143 TYR B CB     1 
ATOM   3966  C CG     . TYR B 1 143 ? 35.803  55.938  22.338 1.00 42.61  ? 143 TYR B CG     1 
ATOM   3967  C CD1    . TYR B 1 143 ? 36.351  56.814  23.253 1.00 40.45  ? 143 TYR B CD1    1 
ATOM   3968  C CD2    . TYR B 1 143 ? 35.494  54.662  22.760 1.00 37.80  ? 143 TYR B CD2    1 
ATOM   3969  C CE1    . TYR B 1 143 ? 36.572  56.432  24.555 1.00 39.74  ? 143 TYR B CE1    1 
ATOM   3970  C CE2    . TYR B 1 143 ? 35.712  54.274  24.058 1.00 31.34  ? 143 TYR B CE2    1 
ATOM   3971  C CZ     . TYR B 1 143 ? 36.254  55.164  24.946 1.00 31.21  ? 143 TYR B CZ     1 
ATOM   3972  O OH     . TYR B 1 143 ? 36.464  54.779  26.241 1.00 41.34  ? 143 TYR B OH     1 
ATOM   3973  N N      . ALA B 1 144 ? 34.760  58.151  18.407 1.00 41.67  ? 144 ALA B N      1 
ATOM   3974  C CA     . ALA B 1 144 ? 34.924  58.497  17.005 1.00 40.02  ? 144 ALA B CA     1 
ATOM   3975  C C      . ALA B 1 144 ? 35.204  59.951  16.857 1.00 44.69  ? 144 ALA B C      1 
ATOM   3976  O O      . ALA B 1 144 ? 35.828  60.347  15.905 1.00 49.35  ? 144 ALA B O      1 
ATOM   3977  C CB     . ALA B 1 144 ? 33.680  58.175  16.247 1.00 34.37  ? 144 ALA B CB     1 
ATOM   3978  N N      . SER B 1 145 ? 34.693  60.777  17.753 1.00 43.58  ? 145 SER B N      1 
ATOM   3979  C CA     . SER B 1 145 ? 35.008  62.191  17.725 1.00 46.34  ? 145 SER B CA     1 
ATOM   3980  C C      . SER B 1 145 ? 36.480  62.341  18.004 1.00 47.49  ? 145 SER B C      1 
ATOM   3981  O O      . SER B 1 145 ? 37.118  63.247  17.496 1.00 45.82  ? 145 SER B O      1 
ATOM   3982  C CB     . SER B 1 145 ? 34.159  62.963  18.696 1.00 37.49  ? 145 SER B CB     1 
ATOM   3983  O OG     . SER B 1 145 ? 34.625  62.823  20.010 1.00 40.24  ? 145 SER B OG     1 
ATOM   3984  N N      . GLY B 1 146 ? 37.022  61.484  18.852 1.00 44.57  ? 146 GLY B N      1 
ATOM   3985  C CA     . GLY B 1 146 ? 38.439  61.509  19.144 1.00 40.45  ? 146 GLY B CA     1 
ATOM   3986  C C      . GLY B 1 146 ? 38.545  62.018  20.534 1.00 41.62  ? 146 GLY B C      1 
ATOM   3987  O O      . GLY B 1 146 ? 39.586  62.518  20.924 1.00 48.41  ? 146 GLY B O      1 
ATOM   3988  N N      . ARG B 1 147 ? 37.483  61.868  21.303 1.00 39.23  ? 147 ARG B N      1 
ATOM   3989  C CA     . ARG B 1 147 ? 37.456  62.463  22.615 1.00 38.42  ? 147 ARG B CA     1 
ATOM   3990  C C      . ARG B 1 147 ? 37.183  61.463  23.662 1.00 40.73  ? 147 ARG B C      1 
ATOM   3991  O O      . ARG B 1 147 ? 36.378  60.574  23.471 1.00 46.18  ? 147 ARG B O      1 
ATOM   3992  C CB     . ARG B 1 147 ? 36.362  63.515  22.662 1.00 39.42  ? 147 ARG B CB     1 
ATOM   3993  C CG     . ARG B 1 147 ? 36.694  64.774  21.891 1.00 38.62  ? 147 ARG B CG     1 
ATOM   3994  C CD     . ARG B 1 147 ? 35.463  65.581  21.532 1.00 32.70  ? 147 ARG B CD     1 
ATOM   3995  N NE     . ARG B 1 147 ? 35.855  66.815  20.864 1.00 42.01  ? 147 ARG B NE     1 
ATOM   3996  C CZ     . ARG B 1 147 ? 35.999  66.946  19.551 1.00 46.03  ? 147 ARG B CZ     1 
ATOM   3997  N NH1    . ARG B 1 147 ? 35.766  65.926  18.750 1.00 48.95  ? 147 ARG B NH1    1 
ATOM   3998  N NH2    . ARG B 1 147 ? 36.365  68.108  19.035 1.00 45.03  ? 147 ARG B NH2    1 
ATOM   3999  N N      . THR B 1 148 ? 37.809  61.622  24.806 1.00 41.35  ? 148 THR B N      1 
ATOM   4000  C CA     . THR B 1 148 ? 37.577  60.730  25.900 1.00 40.23  ? 148 THR B CA     1 
ATOM   4001  C C      . THR B 1 148 ? 36.634  61.400  26.897 1.00 40.79  ? 148 THR B C      1 
ATOM   4002  O O      . THR B 1 148 ? 36.099  60.742  27.765 1.00 39.16  ? 148 THR B O      1 
ATOM   4003  C CB     . THR B 1 148 ? 38.917  60.368  26.519 1.00 36.76  ? 148 THR B CB     1 
ATOM   4004  O OG1    . THR B 1 148 ? 39.574  61.561  26.948 1.00 54.61  ? 148 THR B OG1    1 
ATOM   4005  C CG2    . THR B 1 148 ? 39.782  59.700  25.486 1.00 35.78  ? 148 THR B CG2    1 
ATOM   4006  N N      . THR B 1 149 ? 36.390  62.697  26.744 1.00 42.61  ? 149 THR B N      1 
ATOM   4007  C CA     . THR B 1 149 ? 35.554  63.442  27.690 1.00 43.77  ? 149 THR B CA     1 
ATOM   4008  C C      . THR B 1 149 ? 34.565  64.380  27.034 1.00 33.78  ? 149 THR B C      1 
ATOM   4009  O O      . THR B 1 149 ? 34.946  65.203  26.232 1.00 33.91  ? 149 THR B O      1 
ATOM   4010  C CB     . THR B 1 149 ? 36.431  64.279  28.635 1.00 51.43  ? 149 THR B CB     1 
ATOM   4011  O OG1    . THR B 1 149 ? 37.293  63.414  29.384 1.00 55.38  ? 149 THR B OG1    1 
ATOM   4012  C CG2    . THR B 1 149 ? 35.592  65.094  29.602 1.00 43.14  ? 149 THR B CG2    1 
ATOM   4013  N N      . GLY B 1 150 ? 33.296  64.274  27.396 1.00 27.89  ? 150 GLY B N      1 
ATOM   4014  C CA     . GLY B 1 150 ? 32.284  65.130  26.835 1.00 27.18  ? 150 GLY B CA     1 
ATOM   4015  C C      . GLY B 1 150 ? 30.898  64.670  27.154 1.00 29.04  ? 150 GLY B C      1 
ATOM   4016  O O      . GLY B 1 150 ? 30.734  63.865  28.024 1.00 35.56  ? 150 GLY B O      1 
ATOM   4017  N N      . ILE B 1 151 ? 29.894  65.185  26.472 1.00 27.67  ? 151 ILE B N      1 
ATOM   4018  C CA     . ILE B 1 151 ? 28.551  64.709  26.669 1.00 28.95  ? 151 ILE B CA     1 
ATOM   4019  C C      . ILE B 1 151 ? 27.946  64.369  25.332 1.00 37.99  ? 151 ILE B C      1 
ATOM   4020  O O      . ILE B 1 151 ? 28.004  65.154  24.418 1.00 40.54  ? 151 ILE B O      1 
ATOM   4021  C CB     . ILE B 1 151 ? 27.691  65.713  27.449 1.00 26.73  ? 151 ILE B CB     1 
ATOM   4022  C CG1    . ILE B 1 151 ? 26.209  65.373  27.327 1.00 32.78  ? 151 ILE B CG1    1 
ATOM   4023  C CG2    . ILE B 1 151 ? 27.962  67.131  27.000 1.00 34.68  ? 151 ILE B CG2    1 
ATOM   4024  C CD1    . ILE B 1 151 ? 25.358  65.985  28.409 1.00 34.97  ? 151 ILE B CD1    1 
ATOM   4025  N N      . VAL B 1 152 ? 27.413  63.168  25.184 1.00 34.94  ? 152 VAL B N      1 
ATOM   4026  C CA     . VAL B 1 152 ? 26.832  62.748  23.931 1.00 34.59  ? 152 VAL B CA     1 
ATOM   4027  C C      . VAL B 1 152 ? 25.349  62.752  24.045 1.00 38.83  ? 152 VAL B C      1 
ATOM   4028  O O      . VAL B 1 152 ? 24.814  62.244  25.007 1.00 42.27  ? 152 VAL B O      1 
ATOM   4029  C CB     . VAL B 1 152 ? 27.254  61.320  23.579 1.00 37.12  ? 152 VAL B CB     1 
ATOM   4030  C CG1    . VAL B 1 152 ? 26.403  60.730  22.475 1.00 36.07  ? 152 VAL B CG1    1 
ATOM   4031  C CG2    . VAL B 1 152 ? 28.711  61.271  23.193 1.00 39.57  ? 152 VAL B CG2    1 
ATOM   4032  N N      . MET B 1 153 ? 24.668  63.336  23.084 1.00 39.99  ? 153 MET B N      1 
ATOM   4033  C CA     . MET B 1 153 ? 23.237  63.258  23.086 1.00 42.35  ? 153 MET B CA     1 
ATOM   4034  C C      . MET B 1 153 ? 22.914  62.186  22.098 1.00 47.72  ? 153 MET B C      1 
ATOM   4035  O O      . MET B 1 153 ? 22.949  62.432  20.909 1.00 53.85  ? 153 MET B O      1 
ATOM   4036  C CB     . MET B 1 153 ? 22.623  64.542  22.600 1.00 33.39  ? 153 MET B CB     1 
ATOM   4037  C CG     . MET B 1 153 ? 21.118  64.529  22.698 1.00 41.28  ? 153 MET B CG     1 
ATOM   4038  S SD     . MET B 1 153 ? 20.418  65.742  21.585 1.00 87.46  ? 153 MET B SD     1 
ATOM   4039  C CE     . MET B 1 153 ? 20.868  65.047  20.004 1.00 58.85  ? 153 MET B CE     1 
ATOM   4040  N N      . ASP B 1 154 ? 22.627  60.983  22.591 1.00 41.42  ? 154 ASP B N      1 
ATOM   4041  C CA     . ASP B 1 154 ? 22.364  59.849  21.714 1.00 40.84  ? 154 ASP B CA     1 
ATOM   4042  C C      . ASP B 1 154 ? 20.879  59.684  21.423 1.00 43.46  ? 154 ASP B C      1 
ATOM   4043  O O      . ASP B 1 154 ? 20.149  59.126  22.239 1.00 46.11  ? 154 ASP B O      1 
ATOM   4044  C CB     . ASP B 1 154 ? 22.918  58.568  22.344 1.00 48.57  ? 154 ASP B CB     1 
ATOM   4045  C CG     . ASP B 1 154 ? 23.040  57.429  21.348 1.00 62.36  ? 154 ASP B CG     1 
ATOM   4046  O OD1    . ASP B 1 154 ? 23.003  57.690  20.127 1.00 59.13  ? 154 ASP B OD1    1 
ATOM   4047  O OD2    . ASP B 1 154 ? 23.186  56.270  21.790 1.00 62.88  ? 154 ASP B OD2    1 
ATOM   4048  N N      . SER B 1 155 ? 20.431  60.154  20.259 1.00 42.24  ? 155 SER B N      1 
ATOM   4049  C CA     . SER B 1 155 ? 19.014  60.066  19.943 1.00 43.94  ? 155 SER B CA     1 
ATOM   4050  C C      . SER B 1 155 ? 18.751  59.069  18.848 1.00 42.98  ? 155 SER B C      1 
ATOM   4051  O O      . SER B 1 155 ? 19.411  59.083  17.829 1.00 38.33  ? 155 SER B O      1 
ATOM   4052  C CB     . SER B 1 155 ? 18.414  61.428  19.625 1.00 38.73  ? 155 SER B CB     1 
ATOM   4053  O OG     . SER B 1 155 ? 17.020  61.345  19.432 1.00 34.09  ? 155 SER B OG     1 
ATOM   4054  N N      . GLY B 1 156 ? 17.780  58.197  19.062 1.00 42.70  ? 156 GLY B N      1 
ATOM   4055  C CA     . GLY B 1 156 ? 17.461  57.181  18.092 1.00 50.02  ? 156 GLY B CA     1 
ATOM   4056  C C      . GLY B 1 156 ? 15.999  56.876  17.977 1.00 51.94  ? 156 GLY B C      1 
ATOM   4057  O O      . GLY B 1 156 ? 15.185  57.757  18.087 1.00 52.34  ? 156 GLY B O      1 
ATOM   4058  N N      . ASP B 1 157 ? 15.639  55.625  17.787 1.00 48.76  ? 157 ASP B N      1 
ATOM   4059  C CA     . ASP B 1 157 ? 14.247  55.328  17.534 1.00 49.16  ? 157 ASP B CA     1 
ATOM   4060  C C      . ASP B 1 157 ? 13.383  55.460  18.723 1.00 51.29  ? 157 ASP B C      1 
ATOM   4061  O O      . ASP B 1 157 ? 12.310  56.005  18.616 1.00 54.48  ? 157 ASP B O      1 
ATOM   4062  C CB     . ASP B 1 157 ? 14.080  53.936  16.957 1.00 55.28  ? 157 ASP B CB     1 
ATOM   4063  C CG     . ASP B 1 157 ? 12.791  53.771  16.194 1.00 62.87  ? 157 ASP B CG     1 
ATOM   4064  O OD1    . ASP B 1 157 ? 12.355  54.740  15.551 1.00 65.91  ? 157 ASP B OD1    1 
ATOM   4065  O OD2    . ASP B 1 157 ? 12.220  52.664  16.223 1.00 66.61  ? 157 ASP B OD2    1 
ATOM   4066  N N      . GLY B 1 158 ? 13.799  54.943  19.863 1.00 49.92  ? 158 GLY B N      1 
ATOM   4067  C CA     . GLY B 1 158 ? 12.915  54.936  21.011 1.00 44.23  ? 158 GLY B CA     1 
ATOM   4068  C C      . GLY B 1 158 ? 13.444  55.514  22.278 1.00 42.08  ? 158 GLY B C      1 
ATOM   4069  O O      . GLY B 1 158 ? 12.698  55.738  23.214 1.00 49.17  ? 158 GLY B O      1 
ATOM   4070  N N      . VAL B 1 159 ? 14.733  55.783  22.309 1.00 37.84  ? 159 VAL B N      1 
ATOM   4071  C CA     . VAL B 1 159 ? 15.319  56.282  23.511 1.00 42.49  ? 159 VAL B CA     1 
ATOM   4072  C C      . VAL B 1 159 ? 16.377  57.317  23.250 1.00 44.36  ? 159 VAL B C      1 
ATOM   4073  O O      . VAL B 1 159 ? 17.217  57.157  22.380 1.00 44.90  ? 159 VAL B O      1 
ATOM   4074  C CB     . VAL B 1 159 ? 15.854  55.129  24.354 1.00 44.31  ? 159 VAL B CB     1 
ATOM   4075  C CG1    . VAL B 1 159 ? 17.075  54.470  23.738 1.00 42.84  ? 159 VAL B CG1    1 
ATOM   4076  C CG2    . VAL B 1 159 ? 16.092  55.572  25.778 1.00 50.53  ? 159 VAL B CG2    1 
ATOM   4077  N N      . THR B 1 160 ? 16.320  58.414  23.984 1.00 39.50  ? 160 THR B N      1 
ATOM   4078  C CA     . THR B 1 160 ? 17.323  59.428  23.844 1.00 37.17  ? 160 THR B CA     1 
ATOM   4079  C C      . THR B 1 160 ? 17.956  59.536  25.187 1.00 41.84  ? 160 THR B C      1 
ATOM   4080  O O      . THR B 1 160 ? 17.267  59.694  26.171 1.00 43.40  ? 160 THR B O      1 
ATOM   4081  C CB     . THR B 1 160 ? 16.724  60.758  23.417 1.00 40.77  ? 160 THR B CB     1 
ATOM   4082  O OG1    . THR B 1 160 ? 16.172  60.628  22.104 1.00 35.06  ? 160 THR B OG1    1 
ATOM   4083  C CG2    . THR B 1 160 ? 17.777  61.848  23.407 1.00 42.01  ? 160 THR B CG2    1 
ATOM   4084  N N      . HIS B 1 161 ? 19.269  59.410  25.247 1.00 42.98  ? 161 HIS B N      1 
ATOM   4085  C CA     . HIS B 1 161 ? 19.974  59.455  26.496 1.00 45.31  ? 161 HIS B CA     1 
ATOM   4086  C C      . HIS B 1 161 ? 20.955  60.563  26.388 1.00 44.25  ? 161 HIS B C      1 
ATOM   4087  O O      . HIS B 1 161 ? 21.389  60.879  25.298 1.00 45.40  ? 161 HIS B O      1 
ATOM   4088  C CB     . HIS B 1 161 ? 20.806  58.199  26.656 1.00 42.86  ? 161 HIS B CB     1 
ATOM   4089  C CG     . HIS B 1 161 ? 20.022  56.959  26.917 1.00 39.46  ? 161 HIS B CG     1 
ATOM   4090  N ND1    . HIS B 1 161 ? 19.349  56.740  28.096 1.00 42.89  ? 161 HIS B ND1    1 
ATOM   4091  C CD2    . HIS B 1 161 ? 19.859  55.842  26.175 1.00 38.13  ? 161 HIS B CD2    1 
ATOM   4092  C CE1    . HIS B 1 161 ? 18.778  55.552  28.057 1.00 47.67  ? 161 HIS B CE1    1 
ATOM   4093  N NE2    . HIS B 1 161 ? 19.073  54.986  26.902 1.00 47.49  ? 161 HIS B NE2    1 
ATOM   4094  N N      . THR B 1 162 ? 21.327  61.165  27.502 1.00 42.89  ? 162 THR B N      1 
ATOM   4095  C CA     . THR B 1 162 ? 22.369  62.162  27.470 1.00 45.05  ? 162 THR B CA     1 
ATOM   4096  C C      . THR B 1 162 ? 23.429  61.654  28.392 1.00 35.35  ? 162 THR B C      1 
ATOM   4097  O O      . THR B 1 162 ? 23.244  61.638  29.587 1.00 41.16  ? 162 THR B O      1 
ATOM   4098  C CB     . THR B 1 162 ? 21.858  63.530  27.910 1.00 48.35  ? 162 THR B CB     1 
ATOM   4099  O OG1    . THR B 1 162 ? 21.012  63.368  29.049 1.00 51.64  ? 162 THR B OG1    1 
ATOM   4100  C CG2    . THR B 1 162 ? 21.074  64.185  26.795 1.00 34.62  ? 162 THR B CG2    1 
ATOM   4101  N N      . VAL B 1 163 ? 24.541  61.223  27.834 1.00 25.89  ? 163 VAL B N      1 
ATOM   4102  C CA     . VAL B 1 163 ? 25.556  60.599  28.626 1.00 33.16  ? 163 VAL B CA     1 
ATOM   4103  C C      . VAL B 1 163 ? 26.833  61.383  28.827 1.00 32.75  ? 163 VAL B C      1 
ATOM   4104  O O      . VAL B 1 163 ? 27.661  61.417  27.933 1.00 29.99  ? 163 VAL B O      1 
ATOM   4105  C CB     . VAL B 1 163 ? 25.952  59.312  27.942 1.00 38.08  ? 163 VAL B CB     1 
ATOM   4106  C CG1    . VAL B 1 163 ? 26.734  58.422  28.887 1.00 40.06  ? 163 VAL B CG1    1 
ATOM   4107  C CG2    . VAL B 1 163 ? 24.710  58.598  27.454 1.00 34.75  ? 163 VAL B CG2    1 
ATOM   4108  N N      . PRO B 1 164 ? 27.017  62.027  30.000 1.00 35.03  ? 164 PRO B N      1 
ATOM   4109  C CA     . PRO B 1 164 ? 28.308  62.662  30.188 1.00 33.06  ? 164 PRO B CA     1 
ATOM   4110  C C      . PRO B 1 164 ? 29.406  61.698  30.404 1.00 32.26  ? 164 PRO B C      1 
ATOM   4111  O O      . PRO B 1 164 ? 29.299  60.872  31.280 1.00 38.64  ? 164 PRO B O      1 
ATOM   4112  C CB     . PRO B 1 164 ? 28.098  63.426  31.453 1.00 30.81  ? 164 PRO B CB     1 
ATOM   4113  C CG     . PRO B 1 164 ? 26.727  63.916  31.304 1.00 36.27  ? 164 PRO B CG     1 
ATOM   4114  C CD     . PRO B 1 164 ? 26.042  62.648  30.920 1.00 33.69  ? 164 PRO B CD     1 
ATOM   4115  N N      . ILE B 1 165 ? 30.481  61.823  29.651 1.00 29.34  ? 165 ILE B N      1 
ATOM   4116  C CA     . ILE B 1 165 ? 31.565  60.889  29.729 1.00 32.77  ? 165 ILE B CA     1 
ATOM   4117  C C      . ILE B 1 165 ? 32.805  61.581  30.206 1.00 38.78  ? 165 ILE B C      1 
ATOM   4118  O O      . ILE B 1 165 ? 33.179  62.586  29.655 1.00 41.20  ? 165 ILE B O      1 
ATOM   4119  C CB     . ILE B 1 165 ? 31.801  60.289  28.345 1.00 27.99  ? 165 ILE B CB     1 
ATOM   4120  C CG1    . ILE B 1 165 ? 30.546  59.571  27.875 1.00 34.21  ? 165 ILE B CG1    1 
ATOM   4121  C CG2    . ILE B 1 165 ? 32.958  59.317  28.361 1.00 34.21  ? 165 ILE B CG2    1 
ATOM   4122  C CD1    . ILE B 1 165 ? 30.263  59.763  26.410 1.00 40.13  ? 165 ILE B CD1    1 
ATOM   4123  N N      . TYR B 1 166 ? 33.429  61.075  31.258 1.00 41.08  ? 166 TYR B N      1 
ATOM   4124  C CA     . TYR B 1 166 ? 34.664  61.643  31.758 1.00 42.64  ? 166 TYR B CA     1 
ATOM   4125  C C      . TYR B 1 166 ? 35.673  60.551  31.837 1.00 47.23  ? 166 TYR B C      1 
ATOM   4126  O O      . TYR B 1 166 ? 35.471  59.594  32.566 1.00 49.52  ? 166 TYR B O      1 
ATOM   4127  C CB     . TYR B 1 166 ? 34.478  62.240  33.136 1.00 40.79  ? 166 TYR B CB     1 
ATOM   4128  C CG     . TYR B 1 166 ? 35.710  62.916  33.675 1.00 50.56  ? 166 TYR B CG     1 
ATOM   4129  C CD1    . TYR B 1 166 ? 36.185  64.080  33.101 1.00 56.31  ? 166 TYR B CD1    1 
ATOM   4130  C CD2    . TYR B 1 166 ? 36.395  62.396  34.758 1.00 51.15  ? 166 TYR B CD2    1 
ATOM   4131  C CE1    . TYR B 1 166 ? 37.312  64.705  33.584 1.00 61.24  ? 166 TYR B CE1    1 
ATOM   4132  C CE2    . TYR B 1 166 ? 37.525  63.016  35.248 1.00 55.83  ? 166 TYR B CE2    1 
ATOM   4133  C CZ     . TYR B 1 166 ? 37.977  64.171  34.653 1.00 60.60  ? 166 TYR B CZ     1 
ATOM   4134  O OH     . TYR B 1 166 ? 39.101  64.798  35.129 1.00 59.68  ? 166 TYR B OH     1 
ATOM   4135  N N      . GLU B 1 167 ? 36.740  60.656  31.060 1.00 45.83  ? 167 GLU B N      1 
ATOM   4136  C CA     . GLU B 1 167 ? 37.765  59.629  31.014 1.00 49.66  ? 167 GLU B CA     1 
ATOM   4137  C C      . GLU B 1 167 ? 37.242  58.266  30.678 1.00 48.87  ? 167 GLU B C      1 
ATOM   4138  O O      . GLU B 1 167 ? 37.657  57.289  31.270 1.00 55.83  ? 167 GLU B O      1 
ATOM   4139  C CB     . GLU B 1 167 ? 38.557  59.598  32.303 1.00 59.69  ? 167 GLU B CB     1 
ATOM   4140  C CG     . GLU B 1 167 ? 39.430  60.827  32.497 1.00 66.76  ? 167 GLU B CG     1 
ATOM   4141  C CD     . GLU B 1 167 ? 40.227  60.787  33.784 1.00 81.07  ? 167 GLU B CD     1 
ATOM   4142  O OE1    . GLU B 1 167 ? 39.919  59.944  34.652 1.00 90.26  ? 167 GLU B OE1    1 
ATOM   4143  O OE2    . GLU B 1 167 ? 41.158  61.606  33.929 1.00 71.53  ? 167 GLU B OE2    1 
ATOM   4144  N N      . GLY B 1 168 ? 36.320  58.188  29.740 1.00 46.79  ? 168 GLY B N      1 
ATOM   4145  C CA     . GLY B 1 168 ? 35.789  56.914  29.309 1.00 39.70  ? 168 GLY B CA     1 
ATOM   4146  C C      . GLY B 1 168 ? 34.689  56.330  30.147 1.00 44.40  ? 168 GLY B C      1 
ATOM   4147  O O      . GLY B 1 168 ? 34.223  55.241  29.861 1.00 46.05  ? 168 GLY B O      1 
ATOM   4148  N N      . TYR B 1 169 ? 34.307  57.008  31.213 1.00 45.83  ? 169 TYR B N      1 
ATOM   4149  C CA     . TYR B 1 169 ? 33.322  56.443  32.112 1.00 46.52  ? 169 TYR B CA     1 
ATOM   4150  C C      . TYR B 1 169 ? 32.045  57.191  31.997 1.00 44.47  ? 169 TYR B C      1 
ATOM   4151  O O      . TYR B 1 169 ? 31.998  58.376  32.237 1.00 42.67  ? 169 TYR B O      1 
ATOM   4152  C CB     . TYR B 1 169 ? 33.823  56.466  33.551 1.00 46.13  ? 169 TYR B CB     1 
ATOM   4153  C CG     . TYR B 1 169 ? 32.915  55.816  34.555 1.00 42.66  ? 169 TYR B CG     1 
ATOM   4154  C CD1    . TYR B 1 169 ? 32.542  54.494  34.425 1.00 49.57  ? 169 TYR B CD1    1 
ATOM   4155  C CD2    . TYR B 1 169 ? 32.454  56.520  35.650 1.00 41.75  ? 169 TYR B CD2    1 
ATOM   4156  C CE1    . TYR B 1 169 ? 31.712  53.897  35.348 1.00 58.29  ? 169 TYR B CE1    1 
ATOM   4157  C CE2    . TYR B 1 169 ? 31.630  55.932  36.579 1.00 42.02  ? 169 TYR B CE2    1 
ATOM   4158  C CZ     . TYR B 1 169 ? 31.264  54.621  36.419 1.00 50.52  ? 169 TYR B CZ     1 
ATOM   4159  O OH     . TYR B 1 169 ? 30.438  54.030  37.338 1.00 49.55  ? 169 TYR B OH     1 
ATOM   4160  N N      . ALA B 1 170 ? 30.998  56.491  31.617 1.00 40.75  ? 170 ALA B N      1 
ATOM   4161  C CA     . ALA B 1 170 ? 29.713  57.100  31.521 1.00 40.81  ? 170 ALA B CA     1 
ATOM   4162  C C      . ALA B 1 170 ? 29.309  57.282  32.909 1.00 39.96  ? 170 ALA B C      1 
ATOM   4163  O O      . ALA B 1 170 ? 29.102  56.310  33.606 1.00 40.84  ? 170 ALA B O      1 
ATOM   4164  C CB     . ALA B 1 170 ? 28.772  56.140  30.886 1.00 41.15  ? 170 ALA B CB     1 
ATOM   4165  N N      . LEU B 1 171 ? 29.214  58.523  33.330 1.00 37.99  ? 171 LEU B N      1 
ATOM   4166  C CA     . LEU B 1 171 ? 28.897  58.814  34.694 1.00 39.81  ? 171 LEU B CA     1 
ATOM   4167  C C      . LEU B 1 171 ? 27.463  58.474  34.935 1.00 39.94  ? 171 LEU B C      1 
ATOM   4168  O O      . LEU B 1 171 ? 26.591  59.110  34.384 1.00 44.24  ? 171 LEU B O      1 
ATOM   4169  C CB     . LEU B 1 171 ? 29.180  60.280  34.939 1.00 32.46  ? 171 LEU B CB     1 
ATOM   4170  C CG     . LEU B 1 171 ? 30.562  60.691  34.451 1.00 32.36  ? 171 LEU B CG     1 
ATOM   4171  C CD1    . LEU B 1 171 ? 30.686  62.194  34.340 1.00 35.70  ? 171 LEU B CD1    1 
ATOM   4172  C CD2    . LEU B 1 171 ? 31.640  60.126  35.350 1.00 38.44  ? 171 LEU B CD2    1 
ATOM   4173  N N      . PRO B 1 172 ? 27.194  57.459  35.803 1.00 36.79  ? 172 PRO B N      1 
ATOM   4174  C CA     . PRO B 1 172 ? 25.800  57.063  35.944 1.00 33.23  ? 172 PRO B CA     1 
ATOM   4175  C C      . PRO B 1 172 ? 24.914  58.080  36.606 1.00 35.90  ? 172 PRO B C      1 
ATOM   4176  O O      . PRO B 1 172 ? 23.703  58.017  36.484 1.00 31.86  ? 172 PRO B O      1 
ATOM   4177  C CB     . PRO B 1 172 ? 25.888  55.861  36.861 1.00 29.07  ? 172 PRO B CB     1 
ATOM   4178  C CG     . PRO B 1 172 ? 27.279  55.366  36.755 1.00 32.92  ? 172 PRO B CG     1 
ATOM   4179  C CD     . PRO B 1 172 ? 28.032  56.642  36.709 1.00 35.89  ? 172 PRO B CD     1 
ATOM   4180  N N      . HIS B 1 173 ? 25.501  59.049  37.273 1.00 36.22  ? 173 HIS B N      1 
ATOM   4181  C CA     . HIS B 1 173 ? 24.698  59.998  38.001 1.00 33.73  ? 173 HIS B CA     1 
ATOM   4182  C C      . HIS B 1 173 ? 24.066  60.982  37.090 1.00 38.98  ? 173 HIS B C      1 
ATOM   4183  O O      . HIS B 1 173 ? 22.963  61.420  37.345 1.00 41.93  ? 173 HIS B O      1 
ATOM   4184  C CB     . HIS B 1 173 ? 25.479  60.706  39.095 1.00 35.47  ? 173 HIS B CB     1 
ATOM   4185  C CG     . HIS B 1 173 ? 26.926  60.923  38.804 1.00 38.54  ? 173 HIS B CG     1 
ATOM   4186  N ND1    . HIS B 1 173 ? 27.877  59.947  38.993 1.00 38.78  ? 173 HIS B ND1    1 
ATOM   4187  C CD2    . HIS B 1 173 ? 27.596  62.031  38.413 1.00 39.11  ? 173 HIS B CD2    1 
ATOM   4188  C CE1    . HIS B 1 173 ? 29.066  60.431  38.691 1.00 35.82  ? 173 HIS B CE1    1 
ATOM   4189  N NE2    . HIS B 1 173 ? 28.922  61.694  38.336 1.00 37.01  ? 173 HIS B NE2    1 
ATOM   4190  N N      . ALA B 1 174 ? 24.750  61.332  36.022 1.00 42.33  ? 174 ALA B N      1 
ATOM   4191  C CA     . ALA B 1 174 ? 24.233  62.291  35.065 1.00 43.99  ? 174 ALA B CA     1 
ATOM   4192  C C      . ALA B 1 174 ? 23.339  61.791  33.972 1.00 41.76  ? 174 ALA B C      1 
ATOM   4193  O O      . ALA B 1 174 ? 22.535  62.533  33.446 1.00 39.11  ? 174 ALA B O      1 
ATOM   4194  C CB     . ALA B 1 174 ? 25.398  62.986  34.438 1.00 40.27  ? 174 ALA B CB     1 
ATOM   4195  N N      . ILE B 1 175 ? 23.494  60.548  33.579 1.00 44.55  ? 175 ILE B N      1 
ATOM   4196  C CA     . ILE B 1 175 ? 22.717  60.016  32.488 1.00 43.00  ? 175 ILE B CA     1 
ATOM   4197  C C      . ILE B 1 175 ? 21.248  60.273  32.680 1.00 45.72  ? 175 ILE B C      1 
ATOM   4198  O O      . ILE B 1 175 ? 20.671  59.852  33.665 1.00 49.97  ? 175 ILE B O      1 
ATOM   4199  C CB     . ILE B 1 175 ? 22.993  58.526  32.258 1.00 37.80  ? 175 ILE B CB     1 
ATOM   4200  C CG1    . ILE B 1 175 ? 24.488  58.283  32.120 1.00 33.84  ? 175 ILE B CG1    1 
ATOM   4201  C CG2    . ILE B 1 175 ? 22.281  58.051  31.007 1.00 45.64  ? 175 ILE B CG2    1 
ATOM   4202  C CD1    . ILE B 1 175 ? 24.850  56.826  31.984 1.00 32.32  ? 175 ILE B CD1    1 
ATOM   4203  N N      . LEU B 1 176 ? 20.645  60.977  31.736 1.00 45.98  ? 176 LEU B N      1 
ATOM   4204  C CA     . LEU B 1 176 ? 19.232  61.257  31.786 1.00 45.85  ? 176 LEU B CA     1 
ATOM   4205  C C      . LEU B 1 176 ? 18.621  60.644  30.567 1.00 44.14  ? 176 LEU B C      1 
ATOM   4206  O O      . LEU B 1 176 ? 19.240  60.603  29.524 1.00 40.22  ? 176 LEU B O      1 
ATOM   4207  C CB     . LEU B 1 176 ? 18.968  62.755  31.844 1.00 42.54  ? 176 LEU B CB     1 
ATOM   4208  C CG     . LEU B 1 176 ? 19.314  63.506  33.128 1.00 38.62  ? 176 LEU B CG     1 
ATOM   4209  C CD1    . LEU B 1 176 ? 18.899  64.959  33.017 1.00 32.42  ? 176 LEU B CD1    1 
ATOM   4210  C CD2    . LEU B 1 176 ? 18.619  62.860  34.309 1.00 44.80  ? 176 LEU B CD2    1 
ATOM   4211  N N      . ARG B 1 177 ? 17.393  60.175  30.691 1.00 46.81  ? 177 ARG B N      1 
ATOM   4212  C CA     . ARG B 1 177 ? 16.719  59.483  29.608 1.00 50.62  ? 177 ARG B CA     1 
ATOM   4213  C C      . ARG B 1 177 ? 15.488  60.234  29.213 1.00 57.30  ? 177 ARG B C      1 
ATOM   4214  O O      . ARG B 1 177 ? 14.671  60.572  30.060 1.00 55.86  ? 177 ARG B O      1 
ATOM   4215  C CB     . ARG B 1 177 ? 16.303  58.111  30.123 1.00 44.17  ? 177 ARG B CB     1 
ATOM   4216  C CG     . ARG B 1 177 ? 15.633  57.152  29.165 1.00 44.77  ? 177 ARG B CG     1 
ATOM   4217  C CD     . ARG B 1 177 ? 14.994  56.057  30.005 1.00 52.90  ? 177 ARG B CD     1 
ATOM   4218  N NE     . ARG B 1 177 ? 14.775  54.793  29.309 1.00 64.48  ? 177 ARG B NE     1 
ATOM   4219  C CZ     . ARG B 1 177 ? 15.561  53.728  29.430 1.00 57.32  ? 177 ARG B CZ     1 
ATOM   4220  N NH1    . ARG B 1 177 ? 16.627  53.767  30.214 1.00 56.78  ? 177 ARG B NH1    1 
ATOM   4221  N NH2    . ARG B 1 177 ? 15.277  52.616  28.774 1.00 43.01  ? 177 ARG B NH2    1 
ATOM   4222  N N      . LEU B 1 178 ? 15.355  60.536  27.931 1.00 54.79  ? 178 LEU B N      1 
ATOM   4223  C CA     . LEU B 1 178 ? 14.156  61.169  27.442 1.00 49.37  ? 178 LEU B CA     1 
ATOM   4224  C C      . LEU B 1 178 ? 13.610  60.082  26.571 1.00 53.91  ? 178 LEU B C      1 
ATOM   4225  O O      . LEU B 1 178 ? 14.262  59.661  25.632 1.00 51.06  ? 178 LEU B O      1 
ATOM   4226  C CB     . LEU B 1 178 ? 14.499  62.383  26.613 1.00 40.19  ? 178 LEU B CB     1 
ATOM   4227  C CG     . LEU B 1 178 ? 13.337  63.221  26.106 1.00 51.16  ? 178 LEU B CG     1 
ATOM   4228  C CD1    . LEU B 1 178 ? 12.533  63.754  27.273 1.00 56.62  ? 178 LEU B CD1    1 
ATOM   4229  C CD2    . LEU B 1 178 ? 13.863  64.359  25.254 1.00 65.00  ? 178 LEU B CD2    1 
ATOM   4230  N N      . ASP B 1 179 ? 12.445  59.570  26.910 1.00 57.05  ? 179 ASP B N      1 
ATOM   4231  C CA     . ASP B 1 179 ? 11.876  58.477  26.157 1.00 54.06  ? 179 ASP B CA     1 
ATOM   4232  C C      . ASP B 1 179 ? 11.132  59.059  24.992 1.00 58.91  ? 179 ASP B C      1 
ATOM   4233  O O      . ASP B 1 179 ? 9.980   58.722  24.746 1.00 57.26  ? 179 ASP B O      1 
ATOM   4234  C CB     . ASP B 1 179 ? 10.951  57.649  27.029 1.00 57.92  ? 179 ASP B CB     1 
ATOM   4235  C CG     . ASP B 1 179 ? 11.642  57.078  28.237 1.00 64.14  ? 179 ASP B CG     1 
ATOM   4236  O OD1    . ASP B 1 179 ? 11.860  57.830  29.207 1.00 67.06  ? 179 ASP B OD1    1 
ATOM   4237  O OD2    . ASP B 1 179 ? 11.947  55.870  28.227 1.00 67.41  ? 179 ASP B OD2    1 
ATOM   4238  N N      . LEU B 1 180 ? 11.778  59.954  24.269 1.00 58.54  ? 180 LEU B N      1 
ATOM   4239  C CA     . LEU B 1 180 ? 11.171  60.592  23.128 1.00 47.44  ? 180 LEU B CA     1 
ATOM   4240  C C      . LEU B 1 180 ? 12.195  60.362  22.084 1.00 41.71  ? 180 LEU B C      1 
ATOM   4241  O O      . LEU B 1 180 ? 13.366  60.598  22.294 1.00 42.24  ? 180 LEU B O      1 
ATOM   4242  C CB     . LEU B 1 180 ? 11.018  62.092  23.382 1.00 45.00  ? 180 LEU B CB     1 
ATOM   4243  C CG     . LEU B 1 180 ? 10.277  63.022  22.428 1.00 50.50  ? 180 LEU B CG     1 
ATOM   4244  C CD1    . LEU B 1 180 ? 10.001  64.330  23.141 1.00 50.28  ? 180 LEU B CD1    1 
ATOM   4245  C CD2    . LEU B 1 180 ? 11.068  63.277  21.159 1.00 53.78  ? 180 LEU B CD2    1 
ATOM   4246  N N      . ALA B 1 181 ? 11.743  59.930  20.935 1.00 40.58  ? 181 ALA B N      1 
ATOM   4247  C CA     . ALA B 1 181 ? 12.659  59.723  19.889 1.00 41.27  ? 181 ALA B CA     1 
ATOM   4248  C C      . ALA B 1 181 ? 12.075  59.734  18.540 1.00 43.08  ? 181 ALA B C      1 
ATOM   4249  O O      . ALA B 1 181 ? 10.999  60.234  18.338 1.00 47.79  ? 181 ALA B O      1 
ATOM   4250  C CB     . ALA B 1 181 ? 13.288  58.423  20.114 1.00 47.96  ? 181 ALA B CB     1 
ATOM   4251  N N      . GLY B 1 182 ? 12.745  59.104  17.610 1.00 39.37  ? 182 GLY B N      1 
ATOM   4252  C CA     . GLY B 1 182 ? 12.333  59.157  16.235 1.00 44.71  ? 182 GLY B CA     1 
ATOM   4253  C C      . GLY B 1 182 ? 11.009  58.625  15.870 1.00 45.95  ? 182 GLY B C      1 
ATOM   4254  O O      . GLY B 1 182 ? 10.368  59.155  15.016 1.00 49.87  ? 182 GLY B O      1 
ATOM   4255  N N      . ARG B 1 183 ? 10.607  57.552  16.476 1.00 43.28  ? 183 ARG B N      1 
ATOM   4256  C CA     . ARG B 1 183 ? 9.340   56.965  16.191 1.00 45.61  ? 183 ARG B CA     1 
ATOM   4257  C C      . ARG B 1 183 ? 8.264   57.934  16.543 1.00 47.53  ? 183 ARG B C      1 
ATOM   4258  O O      . ARG B 1 183 ? 7.235   57.963  15.909 1.00 44.76  ? 183 ARG B O      1 
ATOM   4259  C CB     . ARG B 1 183 ? 9.181   55.714  17.015 1.00 48.23  ? 183 ARG B CB     1 
ATOM   4260  C CG     . ARG B 1 183 ? 9.210   55.951  18.510 1.00 51.70  ? 183 ARG B CG     1 
ATOM   4261  C CD     . ARG B 1 183 ? 8.949   54.671  19.273 1.00 57.82  ? 183 ARG B CD     1 
ATOM   4262  N NE     . ARG B 1 183 ? 10.005  53.691  19.062 1.00 58.44  ? 183 ARG B NE     1 
ATOM   4263  C CZ     . ARG B 1 183 ? 10.024  52.498  19.637 1.00 53.61  ? 183 ARG B CZ     1 
ATOM   4264  N NH1    . ARG B 1 183 ? 9.043   52.144  20.448 1.00 46.01  ? 183 ARG B NH1    1 
ATOM   4265  N NH2    . ARG B 1 183 ? 11.020  51.663  19.400 1.00 52.58  ? 183 ARG B NH2    1 
ATOM   4266  N N      . ASP B 1 184 ? 8.459   58.693  17.593 1.00 48.54  ? 184 ASP B N      1 
ATOM   4267  C CA     . ASP B 1 184 ? 7.457   59.608  18.037 1.00 45.76  ? 184 ASP B CA     1 
ATOM   4268  C C      . ASP B 1 184 ? 7.408   60.752  17.077 1.00 44.35  ? 184 ASP B C      1 
ATOM   4269  O O      . ASP B 1 184 ? 6.393   61.399  16.940 1.00 46.55  ? 184 ASP B O      1 
ATOM   4270  C CB     . ASP B 1 184 ? 7.818   60.071  19.423 1.00 45.22  ? 184 ASP B CB     1 
ATOM   4271  C CG     . ASP B 1 184 ? 7.927   58.932  20.412 1.00 55.91  ? 184 ASP B CG     1 
ATOM   4272  O OD1    . ASP B 1 184 ? 7.238   57.913  20.233 1.00 51.96  ? 184 ASP B OD1    1 
ATOM   4273  O OD2    . ASP B 1 184 ? 8.690   59.060  21.386 1.00 64.49  ? 184 ASP B OD2    1 
ATOM   4274  N N      . LEU B 1 185 ? 8.502   61.019  16.408 1.00 38.46  ? 185 LEU B N      1 
ATOM   4275  C CA     . LEU B 1 185 ? 8.535   62.048  15.398 1.00 37.93  ? 185 LEU B CA     1 
ATOM   4276  C C      . LEU B 1 185 ? 7.933   61.590  14.072 1.00 43.24  ? 185 LEU B C      1 
ATOM   4277  O O      . LEU B 1 185 ? 7.259   62.360  13.423 1.00 41.45  ? 185 LEU B O      1 
ATOM   4278  C CB     . LEU B 1 185 ? 9.949   62.576  15.235 1.00 34.64  ? 185 LEU B CB     1 
ATOM   4279  C CG     . LEU B 1 185 ? 10.420  63.670  16.193 1.00 31.92  ? 185 LEU B CG     1 
ATOM   4280  C CD1    . LEU B 1 185 ? 10.247  63.272  17.647 1.00 34.47  ? 185 LEU B CD1    1 
ATOM   4281  C CD2    . LEU B 1 185 ? 11.866  64.029  15.912 1.00 36.73  ? 185 LEU B CD2    1 
ATOM   4282  N N      . THR B 1 186 ? 8.169   60.358  13.639 1.00 43.50  ? 186 THR B N      1 
ATOM   4283  C CA     . THR B 1 186 ? 7.554   59.853  12.425 1.00 36.58  ? 186 THR B CA     1 
ATOM   4284  C C      . THR B 1 186 ? 6.088   59.805  12.646 1.00 42.79  ? 186 THR B C      1 
ATOM   4285  O O      . THR B 1 186 ? 5.322   60.004  11.726 1.00 46.60  ? 186 THR B O      1 
ATOM   4286  C CB     . THR B 1 186 ? 8.018   58.445  12.085 1.00 37.68  ? 186 THR B CB     1 
ATOM   4287  O OG1    . THR B 1 186 ? 7.428   57.498  12.977 1.00 55.79  ? 186 THR B OG1    1 
ATOM   4288  C CG2    . THR B 1 186 ? 9.511   58.339  12.177 1.00 40.48  ? 186 THR B CG2    1 
ATOM   4289  N N      . ASP B 1 187 ? 5.667   59.575  13.874 1.00 45.66  ? 187 ASP B N      1 
ATOM   4290  C CA     . ASP B 1 187 ? 4.249   59.507  14.184 1.00 44.76  ? 187 ASP B CA     1 
ATOM   4291  C C      . ASP B 1 187 ? 3.700   60.883  14.318 1.00 48.04  ? 187 ASP B C      1 
ATOM   4292  O O      . ASP B 1 187 ? 2.543   61.107  14.030 1.00 55.39  ? 187 ASP B O      1 
ATOM   4293  C CB     . ASP B 1 187 ? 3.997   58.718  15.445 1.00 52.79  ? 187 ASP B CB     1 
ATOM   4294  C CG     . ASP B 1 187 ? 4.380   57.259  15.312 1.00 59.70  ? 187 ASP B CG     1 
ATOM   4295  O OD1    . ASP B 1 187 ? 4.753   56.836  14.206 1.00 61.35  ? 187 ASP B OD1    1 
ATOM   4296  O OD2    . ASP B 1 187 ? 4.319   56.534  16.322 1.00 55.47  ? 187 ASP B OD2    1 
ATOM   4297  N N      . TYR B 1 188 ? 4.519   61.829  14.741 1.00 46.64  ? 188 TYR B N      1 
ATOM   4298  C CA     . TYR B 1 188 ? 4.060   63.212  14.791 1.00 45.92  ? 188 TYR B CA     1 
ATOM   4299  C C      . TYR B 1 188 ? 3.934   63.739  13.393 1.00 42.06  ? 188 TYR B C      1 
ATOM   4300  O O      . TYR B 1 188 ? 2.998   64.439  13.096 1.00 46.66  ? 188 TYR B O      1 
ATOM   4301  C CB     . TYR B 1 188 ? 4.985   64.094  15.612 1.00 40.06  ? 188 TYR B CB     1 
ATOM   4302  C CG     . TYR B 1 188 ? 4.575   65.531  15.771 1.00 38.86  ? 188 TYR B CG     1 
ATOM   4303  C CD1    . TYR B 1 188 ? 3.374   65.870  16.362 1.00 43.69  ? 188 TYR B CD1    1 
ATOM   4304  C CD2    . TYR B 1 188 ? 5.416   66.552  15.373 1.00 38.58  ? 188 TYR B CD2    1 
ATOM   4305  C CE1    . TYR B 1 188 ? 3.010   67.191  16.525 1.00 49.48  ? 188 TYR B CE1    1 
ATOM   4306  C CE2    . TYR B 1 188 ? 5.062   67.874  15.529 1.00 40.65  ? 188 TYR B CE2    1 
ATOM   4307  C CZ     . TYR B 1 188 ? 3.858   68.187  16.106 1.00 44.30  ? 188 TYR B CZ     1 
ATOM   4308  O OH     . TYR B 1 188 ? 3.500   69.502  16.256 1.00 40.60  ? 188 TYR B OH     1 
ATOM   4309  N N      . LEU B 1 189 ? 4.841   63.397  12.506 1.00 33.47  ? 189 LEU B N      1 
ATOM   4310  C CA     . LEU B 1 189 ? 4.764   63.979  11.196 1.00 37.05  ? 189 LEU B CA     1 
ATOM   4311  C C      . LEU B 1 189 ? 3.533   63.477  10.537 1.00 42.30  ? 189 LEU B C      1 
ATOM   4312  O O      . LEU B 1 189 ? 2.920   64.174  9.768  1.00 44.79  ? 189 LEU B O      1 
ATOM   4313  C CB     . LEU B 1 189 ? 5.975   63.654  10.361 1.00 35.71  ? 189 LEU B CB     1 
ATOM   4314  C CG     . LEU B 1 189 ? 6.122   64.363  9.022  1.00 36.68  ? 189 LEU B CG     1 
ATOM   4315  C CD1    . LEU B 1 189 ? 6.083   65.861  9.199  1.00 44.44  ? 189 LEU B CD1    1 
ATOM   4316  C CD2    . LEU B 1 189 ? 7.415   63.962  8.355  1.00 37.95  ? 189 LEU B CD2    1 
ATOM   4317  N N      . MET B 1 190 ? 3.128   62.274  10.860 1.00 43.90  ? 190 MET B N      1 
ATOM   4318  C CA     . MET B 1 190 ? 1.924   61.731  10.283 1.00 48.53  ? 190 MET B CA     1 
ATOM   4319  C C      . MET B 1 190 ? 0.797   62.560  10.762 1.00 47.54  ? 190 MET B C      1 
ATOM   4320  O O      . MET B 1 190 ? -0.101  62.881  10.010 1.00 47.07  ? 190 MET B O      1 
ATOM   4321  C CB     . MET B 1 190 ? 1.663   60.313  10.767 1.00 59.33  ? 190 MET B CB     1 
ATOM   4322  C CG     . MET B 1 190 ? 2.640   59.245  10.342 1.00 54.96  ? 190 MET B CG     1 
ATOM   4323  S SD     . MET B 1 190 ? 2.345   57.813  11.379 1.00 52.68  ? 190 MET B SD     1 
ATOM   4324  C CE     . MET B 1 190 ? 1.332   56.810  10.310 1.00 57.96  ? 190 MET B CE     1 
ATOM   4325  N N      . LYS B 1 191 ? 0.822   62.896  12.039 1.00 43.33  ? 191 LYS B N      1 
ATOM   4326  C CA     . LYS B 1 191 ? -0.281  63.641  12.605 1.00 48.61  ? 191 LYS B CA     1 
ATOM   4327  C C      . LYS B 1 191 ? -0.391  64.994  11.959 1.00 52.21  ? 191 LYS B C      1 
ATOM   4328  O O      . LYS B 1 191 ? -1.444  65.358  11.461 1.00 54.68  ? 191 LYS B O      1 
ATOM   4329  C CB     . LYS B 1 191 ? -0.141  63.790  14.106 1.00 39.64  ? 191 LYS B CB     1 
ATOM   4330  C CG     . LYS B 1 191 ? -1.271  64.587  14.733 1.00 41.86  ? 191 LYS B CG     1 
ATOM   4331  C CD     . LYS B 1 191 ? -0.941  65.024  16.148 1.00 54.08  ? 191 LYS B CD     1 
ATOM   4332  C CE     . LYS B 1 191 ? -2.013  65.951  16.693 1.00 57.64  ? 191 LYS B CE     1 
ATOM   4333  N NZ     . LYS B 1 191 ? -1.737  66.332  18.106 1.00 54.70  ? 191 LYS B NZ     1 
ATOM   4334  N N      . ILE B 1 192 ? 0.696   65.740  11.928 1.00 44.13  ? 192 ILE B N      1 
ATOM   4335  C CA     . ILE B 1 192 ? 0.663   67.056  11.344 1.00 46.01  ? 192 ILE B CA     1 
ATOM   4336  C C      . ILE B 1 192 ? 0.382   67.056  9.844  1.00 52.45  ? 192 ILE B C      1 
ATOM   4337  O O      . ILE B 1 192 ? -0.302  67.938  9.354  1.00 53.04  ? 192 ILE B O      1 
ATOM   4338  C CB     . ILE B 1 192 ? 1.905   67.856  11.737 1.00 38.05  ? 192 ILE B CB     1 
ATOM   4339  C CG1    . ILE B 1 192 ? 3.183   67.245  11.196 1.00 36.27  ? 192 ILE B CG1    1 
ATOM   4340  C CG2    . ILE B 1 192 ? 1.999   67.919  13.240 1.00 40.87  ? 192 ILE B CG2    1 
ATOM   4341  C CD1    . ILE B 1 192 ? 4.419   67.915  11.739 1.00 37.88  ? 192 ILE B CD1    1 
ATOM   4342  N N      . LEU B 1 193 ? 0.853   66.055  9.117  1.00 47.37  ? 193 LEU B N      1 
ATOM   4343  C CA     . LEU B 1 193 ? 0.607   65.979  7.692  1.00 44.40  ? 193 LEU B CA     1 
ATOM   4344  C C      . LEU B 1 193 ? -0.812  65.564  7.427  1.00 51.90  ? 193 LEU B C      1 
ATOM   4345  O O      . LEU B 1 193 ? -1.358  65.903  6.396  1.00 56.96  ? 193 LEU B O      1 
ATOM   4346  C CB     . LEU B 1 193 ? 1.577   65.028  7.022  1.00 40.77  ? 193 LEU B CB     1 
ATOM   4347  C CG     . LEU B 1 193 ? 2.964   65.549  6.682  1.00 39.01  ? 193 LEU B CG     1 
ATOM   4348  C CD1    . LEU B 1 193 ? 3.775   64.430  6.060  1.00 38.61  ? 193 LEU B CD1    1 
ATOM   4349  C CD2    . LEU B 1 193 ? 2.856   66.715  5.720  1.00 44.70  ? 193 LEU B CD2    1 
ATOM   4350  N N      . THR B 1 194 ? -1.420  64.822  8.341  1.00 52.32  ? 194 THR B N      1 
ATOM   4351  C CA     . THR B 1 194 ? -2.810  64.421  8.176  1.00 53.80  ? 194 THR B CA     1 
ATOM   4352  C C      . THR B 1 194 ? -3.719  65.620  8.264  1.00 60.18  ? 194 THR B C      1 
ATOM   4353  O O      . THR B 1 194 ? -4.679  65.724  7.521  1.00 63.95  ? 194 THR B O      1 
ATOM   4354  C CB     . THR B 1 194 ? -3.255  63.337  9.171  1.00 53.35  ? 194 THR B CB     1 
ATOM   4355  O OG1    . THR B 1 194 ? -2.419  62.187  9.032  1.00 56.55  ? 194 THR B OG1    1 
ATOM   4356  C CG2    . THR B 1 194 ? -4.688  62.913  8.914  1.00 50.84  ? 194 THR B CG2    1 
ATOM   4357  N N      . GLU B 1 195 ? -3.417  66.542  9.170  1.00 58.96  ? 195 GLU B N      1 
ATOM   4358  C CA     . GLU B 1 195 ? -4.237  67.734  9.355  1.00 56.28  ? 195 GLU B CA     1 
ATOM   4359  C C      . GLU B 1 195 ? -4.089  68.686  8.204  1.00 62.88  ? 195 GLU B C      1 
ATOM   4360  O O      . GLU B 1 195 ? -4.708  69.740  8.202  1.00 67.80  ? 195 GLU B O      1 
ATOM   4361  C CB     . GLU B 1 195 ? -3.815  68.481  10.610 1.00 58.26  ? 195 GLU B CB     1 
ATOM   4362  C CG     . GLU B 1 195 ? -3.946  67.724  11.921 1.00 69.53  ? 195 GLU B CG     1 
ATOM   4363  C CD     . GLU B 1 195 ? -3.298  68.464  13.081 1.00 69.19  ? 195 GLU B CD     1 
ATOM   4364  O OE1    . GLU B 1 195 ? -2.299  69.173  12.856 1.00 60.72  ? 195 GLU B OE1    1 
ATOM   4365  O OE2    . GLU B 1 195 ? -3.776  68.329  14.224 1.00 67.67  ? 195 GLU B OE2    1 
ATOM   4366  N N      . ARG B 1 196 ? -3.297  68.310  7.205  1.00 61.66  ? 196 ARG B N      1 
ATOM   4367  C CA     . ARG B 1 196 ? -3.092  69.152  6.031  1.00 61.98  ? 196 ARG B CA     1 
ATOM   4368  C C      . ARG B 1 196 ? -3.813  68.398  4.968  1.00 67.74  ? 196 ARG B C      1 
ATOM   4369  O O      . ARG B 1 196 ? -3.650  68.652  3.781  1.00 77.92  ? 196 ARG B O      1 
ATOM   4370  C CB     . ARG B 1 196 ? -1.609  69.303  5.711  1.00 53.68  ? 196 ARG B CB     1 
ATOM   4371  C CG     . ARG B 1 196 ? -1.198  70.505  4.879  1.00 47.21  ? 196 ARG B CG     1 
ATOM   4372  C CD     . ARG B 1 196 ? 0.285   70.388  4.560  1.00 52.04  ? 196 ARG B CD     1 
ATOM   4373  N NE     . ARG B 1 196 ? 0.735   71.294  3.510  1.00 66.53  ? 196 ARG B NE     1 
ATOM   4374  C CZ     . ARG B 1 196 ? 1.431   72.406  3.723  1.00 67.98  ? 196 ARG B CZ     1 
ATOM   4375  N NH1    . ARG B 1 196 ? 1.762   72.757  4.954  1.00 58.36  ? 196 ARG B NH1    1 
ATOM   4376  N NH2    . ARG B 1 196 ? 1.798   73.167  2.703  1.00 73.53  ? 196 ARG B NH2    1 
ATOM   4377  N N      . GLY B 1 197 ? -4.603  67.424  5.377  1.00 60.82  ? 197 GLY B N      1 
ATOM   4378  C CA     . GLY B 1 197 ? -5.415  66.710  4.411  1.00 58.78  ? 197 GLY B CA     1 
ATOM   4379  C C      . GLY B 1 197 ? -4.900  65.399  3.880  1.00 64.67  ? 197 GLY B C      1 
ATOM   4380  O O      . GLY B 1 197 ? -5.669  64.592  3.380  1.00 70.20  ? 197 GLY B O      1 
ATOM   4381  N N      . TYR B 1 198 ? -3.607  65.176  3.962  1.00 64.62  ? 198 TYR B N      1 
ATOM   4382  C CA     . TYR B 1 198 ? -3.064  63.921  3.517  1.00 62.94  ? 198 TYR B CA     1 
ATOM   4383  C C      . TYR B 1 198 ? -3.495  62.874  4.501  1.00 59.02  ? 198 TYR B C      1 
ATOM   4384  O O      . TYR B 1 198 ? -3.891  63.196  5.600  1.00 60.90  ? 198 TYR B O      1 
ATOM   4385  C CB     . TYR B 1 198 ? -1.550  64.025  3.457  1.00 63.41  ? 198 TYR B CB     1 
ATOM   4386  C CG     . TYR B 1 198 ? -1.051  65.203  2.664  1.00 59.44  ? 198 TYR B CG     1 
ATOM   4387  C CD1    . TYR B 1 198 ? -1.489  65.422  1.372  1.00 59.46  ? 198 TYR B CD1    1 
ATOM   4388  C CD2    . TYR B 1 198 ? -0.136  66.088  3.199  1.00 56.75  ? 198 TYR B CD2    1 
ATOM   4389  C CE1    . TYR B 1 198 ? -1.039  66.500  0.638  1.00 59.70  ? 198 TYR B CE1    1 
ATOM   4390  C CE2    . TYR B 1 198 ? 0.322   67.164  2.471  1.00 65.09  ? 198 TYR B CE2    1 
ATOM   4391  C CZ     . TYR B 1 198 ? -0.134  67.364  1.190  1.00 62.65  ? 198 TYR B CZ     1 
ATOM   4392  O OH     . TYR B 1 198 ? 0.313   68.432  0.454  1.00 57.65  ? 198 TYR B OH     1 
ATOM   4393  N N      . SER B 1 199 ? -3.423  61.610  4.139  1.00 61.70  ? 199 SER B N      1 
ATOM   4394  C CA     . SER B 1 199 ? -3.777  60.580  5.088  1.00 64.84  ? 199 SER B CA     1 
ATOM   4395  C C      . SER B 1 199 ? -2.724  59.559  5.314  1.00 63.49  ? 199 SER B C      1 
ATOM   4396  O O      . SER B 1 199 ? -2.629  58.596  4.569  1.00 62.68  ? 199 SER B O      1 
ATOM   4397  C CB     . SER B 1 199 ? -5.043  59.862  4.666  1.00 63.37  ? 199 SER B CB     1 
ATOM   4398  O OG     . SER B 1 199 ? -5.388  58.865  5.610  1.00 64.42  ? 199 SER B OG     1 
ATOM   4399  N N      . PHE B 1 200 ? -1.947  59.737  6.365  1.00 61.07  ? 200 PHE B N      1 
ATOM   4400  C CA     . PHE B 1 200 ? -0.919  58.794  6.689  1.00 62.25  ? 200 PHE B CA     1 
ATOM   4401  C C      . PHE B 1 200 ? -1.243  58.173  8.016  1.00 66.99  ? 200 PHE B C      1 
ATOM   4402  O O      . PHE B 1 200 ? -0.804  58.667  9.032  1.00 67.70  ? 200 PHE B O      1 
ATOM   4403  C CB     . PHE B 1 200 ? 0.376   59.532  6.811  1.00 60.52  ? 200 PHE B CB     1 
ATOM   4404  C CG     . PHE B 1 200 ? 0.791   60.240  5.568  1.00 60.15  ? 200 PHE B CG     1 
ATOM   4405  C CD1    . PHE B 1 200 ? 1.139   59.533  4.442  1.00 58.21  ? 200 PHE B CD1    1 
ATOM   4406  C CD2    . PHE B 1 200 ? 0.861   61.612  5.538  1.00 55.30  ? 200 PHE B CD2    1 
ATOM   4407  C CE1    . PHE B 1 200 ? 1.532   60.185  3.299  1.00 54.23  ? 200 PHE B CE1    1 
ATOM   4408  C CE2    . PHE B 1 200 ? 1.258   62.269  4.400  1.00 52.84  ? 200 PHE B CE2    1 
ATOM   4409  C CZ     . PHE B 1 200 ? 1.593   61.555  3.278  1.00 51.93  ? 200 PHE B CZ     1 
ATOM   4410  N N      . THR B 1 201 ? -1.983  57.071  8.021  1.00 68.84  ? 201 THR B N      1 
ATOM   4411  C CA     . THR B 1 201 ? -2.379  56.414  9.263  1.00 67.12  ? 201 THR B CA     1 
ATOM   4412  C C      . THR B 1 201 ? -1.983  54.951  9.309  1.00 68.17  ? 201 THR B C      1 
ATOM   4413  O O      . THR B 1 201 ? -1.819  54.389  10.384 1.00 63.50  ? 201 THR B O      1 
ATOM   4414  C CB     . THR B 1 201 ? -3.888  56.483  9.455  1.00 64.56  ? 201 THR B CB     1 
ATOM   4415  O OG1    . THR B 1 201 ? -4.536  55.982  8.282  1.00 66.95  ? 201 THR B OG1    1 
ATOM   4416  C CG2    . THR B 1 201 ? -4.331  57.914  9.690  1.00 69.90  ? 201 THR B CG2    1 
ATOM   4417  N N      . THR B 1 202 ? -1.822  54.335  8.149  1.00 65.11  ? 202 THR B N      1 
ATOM   4418  C CA     . THR B 1 202 ? -1.485  52.929  8.101  1.00 64.89  ? 202 THR B CA     1 
ATOM   4419  C C      . THR B 1 202 ? -0.038  52.709  8.481  1.00 68.54  ? 202 THR B C      1 
ATOM   4420  O O      . THR B 1 202 ? 0.774   53.613  8.384  1.00 60.43  ? 202 THR B O      1 
ATOM   4421  C CB     . THR B 1 202 ? -1.751  52.357  6.710  1.00 66.15  ? 202 THR B CB     1 
ATOM   4422  O OG1    . THR B 1 202 ? -2.902  52.997  6.149  1.00 68.93  ? 202 THR B OG1    1 
ATOM   4423  C CG2    . THR B 1 202 ? -1.996  50.858  6.769  1.00 71.84  ? 202 THR B CG2    1 
ATOM   4424  N N      . THR B 1 203 ? 0.289   51.512  8.955  1.00 74.84  ? 203 THR B N      1 
ATOM   4425  C CA     . THR B 1 203 ? 1.646   51.202  9.372  1.00 68.03  ? 203 THR B CA     1 
ATOM   4426  C C      . THR B 1 203 ? 2.496   51.259  8.155  1.00 69.60  ? 203 THR B C      1 
ATOM   4427  O O      . THR B 1 203 ? 3.681   51.529  8.235  1.00 67.25  ? 203 THR B O      1 
ATOM   4428  C CB     . THR B 1 203 ? 1.732   49.815  9.995  1.00 59.59  ? 203 THR B CB     1 
ATOM   4429  O OG1    . THR B 1 203 ? 1.298   48.840  9.042  1.00 72.80  ? 203 THR B OG1    1 
ATOM   4430  C CG2    . THR B 1 203 ? 0.849   49.742  11.222 1.00 51.33  ? 203 THR B CG2    1 
ATOM   4431  N N      . ALA B 1 204 ? 1.898   51.040  7.003  1.00 64.38  ? 204 ALA B N      1 
ATOM   4432  C CA     . ALA B 1 204 ? 2.647   51.126  5.776  1.00 61.77  ? 204 ALA B CA     1 
ATOM   4433  C C      . ALA B 1 204 ? 2.903   52.564  5.526  1.00 59.97  ? 204 ALA B C      1 
ATOM   4434  O O      . ALA B 1 204 ? 3.950   52.949  5.026  1.00 59.70  ? 204 ALA B O      1 
ATOM   4435  C CB     . ALA B 1 204 ? 1.855   50.541  4.637  1.00 67.41  ? 204 ALA B CB     1 
ATOM   4436  N N      . GLU B 1 205 ? 1.937   53.382  5.894  1.00 60.55  ? 205 GLU B N      1 
ATOM   4437  C CA     . GLU B 1 205 ? 2.063   54.791  5.619  1.00 63.93  ? 205 GLU B CA     1 
ATOM   4438  C C      . GLU B 1 205 ? 3.043   55.455  6.547  1.00 60.63  ? 205 GLU B C      1 
ATOM   4439  O O      . GLU B 1 205 ? 3.517   56.529  6.269  1.00 57.57  ? 205 GLU B O      1 
ATOM   4440  C CB     . GLU B 1 205 ? 0.686   55.435  5.644  1.00 63.93  ? 205 GLU B CB     1 
ATOM   4441  C CG     . GLU B 1 205 ? -0.120  55.124  4.395  1.00 62.96  ? 205 GLU B CG     1 
ATOM   4442  C CD     . GLU B 1 205 ? -1.561  55.569  4.491  1.00 66.22  ? 205 GLU B CD     1 
ATOM   4443  O OE1    . GLU B 1 205 ? -2.053  55.761  5.615  1.00 65.87  ? 205 GLU B OE1    1 
ATOM   4444  O OE2    . GLU B 1 205 ? -2.210  55.716  3.438  1.00 61.24  ? 205 GLU B OE2    1 
ATOM   4445  N N      . ARG B 1 206 ? 3.368   54.823  7.658  1.00 57.31  ? 206 ARG B N      1 
ATOM   4446  C CA     . ARG B 1 206 ? 4.360   55.382  8.555  1.00 55.19  ? 206 ARG B CA     1 
ATOM   4447  C C      . ARG B 1 206 ? 5.714   55.324  7.907  1.00 62.11  ? 206 ARG B C      1 
ATOM   4448  O O      . ARG B 1 206 ? 6.550   56.181  8.135  1.00 65.61  ? 206 ARG B O      1 
ATOM   4449  C CB     . ARG B 1 206 ? 4.381   54.607  9.857  1.00 57.37  ? 206 ARG B CB     1 
ATOM   4450  C CG     . ARG B 1 206 ? 5.165   55.250  10.982 1.00 55.00  ? 206 ARG B CG     1 
ATOM   4451  C CD     . ARG B 1 206 ? 5.421   54.244  12.090 1.00 56.20  ? 206 ARG B CD     1 
ATOM   4452  N NE     . ARG B 1 206 ? 6.241   53.139  11.610 1.00 70.92  ? 206 ARG B NE     1 
ATOM   4453  C CZ     . ARG B 1 206 ? 7.566   53.099  11.693 1.00 72.90  ? 206 ARG B CZ     1 
ATOM   4454  N NH1    . ARG B 1 206 ? 8.232   54.099  12.255 1.00 66.72  ? 206 ARG B NH1    1 
ATOM   4455  N NH2    . ARG B 1 206 ? 8.228   52.053  11.218 1.00 71.66  ? 206 ARG B NH2    1 
ATOM   4456  N N      . GLU B 1 207 ? 5.936   54.342  7.054  1.00 61.06  ? 207 GLU B N      1 
ATOM   4457  C CA     . GLU B 1 207 ? 7.254   54.158  6.460  1.00 60.75  ? 207 GLU B CA     1 
ATOM   4458  C C      . GLU B 1 207 ? 7.641   55.130  5.368  1.00 61.94  ? 207 GLU B C      1 
ATOM   4459  O O      . GLU B 1 207 ? 8.809   55.245  5.037  1.00 64.47  ? 207 GLU B O      1 
ATOM   4460  C CB     . GLU B 1 207 ? 7.376   52.727  5.976  1.00 59.22  ? 207 GLU B CB     1 
ATOM   4461  C CG     . GLU B 1 207 ? 7.278   51.727  7.106  1.00 69.81  ? 207 GLU B CG     1 
ATOM   4462  C CD     . GLU B 1 207 ? 6.437   50.533  6.735  1.00 81.64  ? 207 GLU B CD     1 
ATOM   4463  O OE1    . GLU B 1 207 ? 6.099   50.407  5.543  1.00 83.11  ? 207 GLU B OE1    1 
ATOM   4464  O OE2    . GLU B 1 207 ? 6.115   49.727  7.632  1.00 89.56  ? 207 GLU B OE2    1 
ATOM   4465  N N      . ILE B 1 208 ? 6.685   55.861  4.825  1.00 61.68  ? 208 ILE B N      1 
ATOM   4466  C CA     . ILE B 1 208 ? 6.996   56.876  3.839  1.00 59.24  ? 208 ILE B CA     1 
ATOM   4467  C C      . ILE B 1 208 ? 6.984   58.206  4.541  1.00 53.85  ? 208 ILE B C      1 
ATOM   4468  O O      . ILE B 1 208 ? 7.439   59.192  3.997  1.00 54.16  ? 208 ILE B O      1 
ATOM   4469  C CB     . ILE B 1 208 ? 5.987   56.876  2.695  1.00 56.15  ? 208 ILE B CB     1 
ATOM   4470  C CG1    . ILE B 1 208 ? 4.567   56.750  3.237  1.00 62.03  ? 208 ILE B CG1    1 
ATOM   4471  C CG2    . ILE B 1 208 ? 6.272   55.729  1.745  1.00 52.91  ? 208 ILE B CG2    1 
ATOM   4472  C CD1    . ILE B 1 208 ? 3.517   56.607  2.161  1.00 55.36  ? 208 ILE B CD1    1 
ATOM   4473  N N      . VAL B 1 209 ? 6.456   58.245  5.750  1.00 48.71  ? 209 VAL B N      1 
ATOM   4474  C CA     . VAL B 1 209 ? 6.481   59.466  6.524  1.00 51.87  ? 209 VAL B CA     1 
ATOM   4475  C C      . VAL B 1 209 ? 7.818   59.474  7.215  1.00 49.84  ? 209 VAL B C      1 
ATOM   4476  O O      . VAL B 1 209 ? 8.236   60.475  7.763  1.00 48.42  ? 209 VAL B O      1 
ATOM   4477  C CB     . VAL B 1 209 ? 5.316   59.540  7.518  1.00 52.53  ? 209 VAL B CB     1 
ATOM   4478  C CG1    . VAL B 1 209 ? 5.386   60.799  8.360  1.00 47.33  ? 209 VAL B CG1    1 
ATOM   4479  C CG2    . VAL B 1 209 ? 3.997   59.496  6.773  1.00 52.25  ? 209 VAL B CG2    1 
ATOM   4480  N N      . ARG B 1 210 ? 8.530   58.372  7.133  1.00 45.67  ? 210 ARG B N      1 
ATOM   4481  C CA     . ARG B 1 210 ? 9.865   58.353  7.671  1.00 48.26  ? 210 ARG B CA     1 
ATOM   4482  C C      . ARG B 1 210 ? 10.799  58.788  6.576  1.00 49.22  ? 210 ARG B C      1 
ATOM   4483  O O      . ARG B 1 210 ? 11.834  59.348  6.851  1.00 51.13  ? 210 ARG B O      1 
ATOM   4484  C CB     . ARG B 1 210 ? 10.210  56.976  8.182  1.00 56.85  ? 210 ARG B CB     1 
ATOM   4485  C CG     . ARG B 1 210 ? 11.396  56.929  9.125  1.00 57.44  ? 210 ARG B CG     1 
ATOM   4486  C CD     . ARG B 1 210 ? 11.506  55.562  9.775  1.00 56.03  ? 210 ARG B CD     1 
ATOM   4487  N NE     . ARG B 1 210 ? 11.376  54.496  8.787  1.00 63.19  ? 210 ARG B NE     1 
ATOM   4488  C CZ     . ARG B 1 210 ? 12.398  53.932  8.156  1.00 66.31  ? 210 ARG B CZ     1 
ATOM   4489  N NH1    . ARG B 1 210 ? 13.636  54.319  8.420  1.00 71.91  ? 210 ARG B NH1    1 
ATOM   4490  N NH2    . ARG B 1 210 ? 12.181  52.974  7.270  1.00 59.67  ? 210 ARG B NH2    1 
ATOM   4491  N N      . ASP B 1 211 ? 10.467  58.528  5.328  1.00 48.74  ? 211 ASP B N      1 
ATOM   4492  C CA     . ASP B 1 211 ? 11.299  59.011  4.260  1.00 46.04  ? 211 ASP B CA     1 
ATOM   4493  C C      . ASP B 1 211 ? 11.089  60.496  4.145  1.00 55.20  ? 211 ASP B C      1 
ATOM   4494  O O      . ASP B 1 211 ? 12.041  61.240  4.077  1.00 58.32  ? 211 ASP B O      1 
ATOM   4495  C CB     . ASP B 1 211 ? 10.996  58.346  2.947  1.00 41.16  ? 211 ASP B CB     1 
ATOM   4496  C CG     . ASP B 1 211 ? 11.652  57.004  2.825  1.00 57.29  ? 211 ASP B CG     1 
ATOM   4497  O OD1    . ASP B 1 211 ? 11.994  56.423  3.873  1.00 64.97  ? 211 ASP B OD1    1 
ATOM   4498  O OD2    . ASP B 1 211 ? 11.829  56.525  1.687  1.00 64.77  ? 211 ASP B OD2    1 
ATOM   4499  N N      . ILE B 1 212 ? 9.849   60.942  4.152  1.00 52.23  ? 212 ILE B N      1 
ATOM   4500  C CA     . ILE B 1 212 ? 9.619   62.357  4.058  1.00 44.67  ? 212 ILE B CA     1 
ATOM   4501  C C      . ILE B 1 212 ? 10.401  62.974  5.178  1.00 51.23  ? 212 ILE B C      1 
ATOM   4502  O O      . ILE B 1 212 ? 11.076  63.963  4.989  1.00 51.79  ? 212 ILE B O      1 
ATOM   4503  C CB     . ILE B 1 212 ? 8.138   62.671  4.224  1.00 42.76  ? 212 ILE B CB     1 
ATOM   4504  C CG1    . ILE B 1 212 ? 7.358   62.197  3.007  1.00 43.52  ? 212 ILE B CG1    1 
ATOM   4505  C CG2    . ILE B 1 212 ? 7.928   64.157  4.433  1.00 52.10  ? 212 ILE B CG2    1 
ATOM   4506  C CD1    . ILE B 1 212 ? 5.865   62.351  3.154  1.00 46.08  ? 212 ILE B CD1    1 
ATOM   4507  N N      . LYS B 1 213 ? 10.384  62.359  6.343  1.00 51.97  ? 213 LYS B N      1 
ATOM   4508  C CA     . LYS B 1 213 ? 11.046  62.945  7.500  1.00 49.05  ? 213 LYS B CA     1 
ATOM   4509  C C      . LYS B 1 213 ? 12.513  63.058  7.304  1.00 51.39  ? 213 LYS B C      1 
ATOM   4510  O O      . LYS B 1 213 ? 13.092  64.103  7.481  1.00 61.47  ? 213 LYS B O      1 
ATOM   4511  C CB     . LYS B 1 213 ? 10.794  62.117  8.740  1.00 46.01  ? 213 LYS B CB     1 
ATOM   4512  C CG     . LYS B 1 213 ? 11.278  62.747  10.025 1.00 47.12  ? 213 LYS B CG     1 
ATOM   4513  C CD     . LYS B 1 213 ? 10.852  61.896  11.203 1.00 48.61  ? 213 LYS B CD     1 
ATOM   4514  C CE     . LYS B 1 213 ? 11.450  60.510  11.097 1.00 48.00  ? 213 LYS B CE     1 
ATOM   4515  N NZ     . LYS B 1 213 ? 12.923  60.586  10.964 1.00 55.19  ? 213 LYS B NZ     1 
ATOM   4516  N N      . GLU B 1 214 ? 13.145  61.979  6.945  1.00 47.57  ? 214 GLU B N      1 
ATOM   4517  C CA     . GLU B 1 214 ? 14.558  62.014  6.820  1.00 50.03  ? 214 GLU B CA     1 
ATOM   4518  C C      . GLU B 1 214 ? 14.945  62.896  5.678  1.00 47.57  ? 214 GLU B C      1 
ATOM   4519  O O      . GLU B 1 214 ? 15.805  63.739  5.828  1.00 52.78  ? 214 GLU B O      1 
ATOM   4520  C CB     . GLU B 1 214 ? 15.061  60.606  6.587  1.00 55.68  ? 214 GLU B CB     1 
ATOM   4521  C CG     . GLU B 1 214 ? 14.719  59.640  7.708  1.00 59.25  ? 214 GLU B CG     1 
ATOM   4522  C CD     . GLU B 1 214 ? 15.070  58.206  7.374  1.00 57.93  ? 214 GLU B CD     1 
ATOM   4523  O OE1    . GLU B 1 214 ? 15.776  57.977  6.374  1.00 61.28  ? 214 GLU B OE1    1 
ATOM   4524  O OE2    . GLU B 1 214 ? 14.642  57.304  8.117  1.00 53.41  ? 214 GLU B OE2    1 
ATOM   4525  N N      . LYS B 1 215 ? 14.293  62.766  4.542  1.00 46.78  ? 215 LYS B N      1 
ATOM   4526  C CA     . LYS B 1 215 ? 14.730  63.506  3.358  1.00 52.42  ? 215 LYS B CA     1 
ATOM   4527  C C      . LYS B 1 215 ? 14.453  64.993  3.340  1.00 51.54  ? 215 LYS B C      1 
ATOM   4528  O O      . LYS B 1 215 ? 15.250  65.761  2.822  1.00 48.53  ? 215 LYS B O      1 
ATOM   4529  C CB     . LYS B 1 215 ? 14.153  62.880  2.085  1.00 55.35  ? 215 LYS B CB     1 
ATOM   4530  C CG     . LYS B 1 215 ? 14.243  61.370  1.986  1.00 53.58  ? 215 LYS B CG     1 
ATOM   4531  C CD     . LYS B 1 215 ? 15.666  60.882  1.838  1.00 64.73  ? 215 LYS B CD     1 
ATOM   4532  C CE     . LYS B 1 215 ? 15.665  59.384  1.607  1.00 68.69  ? 215 LYS B CE     1 
ATOM   4533  N NZ     . LYS B 1 215 ? 14.744  59.038  0.490  1.00 67.05  ? 215 LYS B NZ     1 
ATOM   4534  N N      . LEU B 1 216 ? 13.343  65.411  3.915  1.00 50.39  ? 216 LEU B N      1 
ATOM   4535  C CA     . LEU B 1 216 ? 12.969  66.803  3.861  1.00 43.21  ? 216 LEU B CA     1 
ATOM   4536  C C      . LEU B 1 216 ? 13.134  67.520  5.168  1.00 39.63  ? 216 LEU B C      1 
ATOM   4537  O O      . LEU B 1 216 ? 13.684  68.602  5.200  1.00 40.70  ? 216 LEU B O      1 
ATOM   4538  C CB     . LEU B 1 216 ? 11.517  66.894  3.429  1.00 36.49  ? 216 LEU B CB     1 
ATOM   4539  C CG     . LEU B 1 216 ? 11.172  66.204  2.117  1.00 38.92  ? 216 LEU B CG     1 
ATOM   4540  C CD1    . LEU B 1 216 ? 9.674   66.221  1.889  1.00 44.19  ? 216 LEU B CD1    1 
ATOM   4541  C CD2    . LEU B 1 216 ? 11.897  66.881  0.970  1.00 47.43  ? 216 LEU B CD2    1 
ATOM   4542  N N      . CYS B 1 217 ? 12.688  66.924  6.256  1.00 39.61  ? 217 CYS B N      1 
ATOM   4543  C CA     . CYS B 1 217 ? 12.706  67.612  7.543  1.00 39.29  ? 217 CYS B CA     1 
ATOM   4544  C C      . CYS B 1 217 ? 13.999  68.178  8.051  1.00 36.68  ? 217 CYS B C      1 
ATOM   4545  O O      . CYS B 1 217 ? 15.056  67.634  7.802  1.00 34.70  ? 217 CYS B O      1 
ATOM   4546  C CB     . CYS B 1 217 ? 12.018  66.794  8.625  1.00 33.18  ? 217 CYS B CB     1 
ATOM   4547  S SG     . CYS B 1 217 ? 10.230  66.951  8.694  1.00 40.26  ? 217 CYS B SG     1 
ATOM   4548  N N      . TYR B 1 218 ? 13.898  69.287  8.774  1.00 37.99  ? 218 TYR B N      1 
ATOM   4549  C CA     . TYR B 1 218 ? 15.056  69.964  9.285  1.00 34.60  ? 218 TYR B CA     1 
ATOM   4550  C C      . TYR B 1 218 ? 14.678  70.705  10.523 1.00 37.69  ? 218 TYR B C      1 
ATOM   4551  O O      . TYR B 1 218 ? 13.519  70.907  10.770 1.00 37.80  ? 218 TYR B O      1 
ATOM   4552  C CB     . TYR B 1 218 ? 15.531  70.954  8.255  1.00 37.71  ? 218 TYR B CB     1 
ATOM   4553  C CG     . TYR B 1 218 ? 14.724  72.218  8.115  1.00 44.52  ? 218 TYR B CG     1 
ATOM   4554  C CD1    . TYR B 1 218 ? 13.538  72.232  7.414  1.00 42.58  ? 218 TYR B CD1    1 
ATOM   4555  C CD2    . TYR B 1 218 ? 15.179  73.411  8.645  1.00 49.92  ? 218 TYR B CD2    1 
ATOM   4556  C CE1    . TYR B 1 218 ? 12.812  73.392  7.276  1.00 47.22  ? 218 TYR B CE1    1 
ATOM   4557  C CE2    . TYR B 1 218 ? 14.457  74.572  8.513  1.00 46.16  ? 218 TYR B CE2    1 
ATOM   4558  C CZ     . TYR B 1 218 ? 13.278  74.553  7.826  1.00 47.87  ? 218 TYR B CZ     1 
ATOM   4559  O OH     . TYR B 1 218 ? 12.559  75.705  7.689  1.00 51.57  ? 218 TYR B OH     1 
ATOM   4560  N N      . VAL B 1 219 ? 15.657  71.110  11.316 1.00 40.96  ? 219 VAL B N      1 
ATOM   4561  C CA     . VAL B 1 219 ? 15.402  71.837  12.546 1.00 43.58  ? 219 VAL B CA     1 
ATOM   4562  C C      . VAL B 1 219 ? 15.657  73.275  12.288 1.00 43.43  ? 219 VAL B C      1 
ATOM   4563  O O      . VAL B 1 219 ? 16.723  73.652  11.851 1.00 46.63  ? 219 VAL B O      1 
ATOM   4564  C CB     . VAL B 1 219 ? 16.340  71.434  13.683 1.00 41.37  ? 219 VAL B CB     1 
ATOM   4565  C CG1    . VAL B 1 219 ? 16.013  72.206  14.943 1.00 37.87  ? 219 VAL B CG1    1 
ATOM   4566  C CG2    . VAL B 1 219 ? 16.258  69.949  13.949 1.00 41.33  ? 219 VAL B CG2    1 
ATOM   4567  N N      . ALA B 1 220 ? 14.701  74.109  12.603 1.00 46.99  ? 220 ALA B N      1 
ATOM   4568  C CA     . ALA B 1 220 ? 14.844  75.499  12.328 1.00 50.15  ? 220 ALA B CA     1 
ATOM   4569  C C      . ALA B 1 220 ? 15.551  76.146  13.471 1.00 50.07  ? 220 ALA B C      1 
ATOM   4570  O O      . ALA B 1 220 ? 15.351  75.743  14.592 1.00 52.67  ? 220 ALA B O      1 
ATOM   4571  C CB     . ALA B 1 220 ? 13.475  76.069  12.196 1.00 49.82  ? 220 ALA B CB     1 
ATOM   4572  N N      . LEU B 1 221 ? 16.367  77.158  13.210 1.00 42.77  ? 221 LEU B N      1 
ATOM   4573  C CA     . LEU B 1 221 ? 17.049  77.877  14.276 1.00 39.52  ? 221 LEU B CA     1 
ATOM   4574  C C      . LEU B 1 221 ? 16.043  78.542  15.171 1.00 48.46  ? 221 LEU B C      1 
ATOM   4575  O O      . LEU B 1 221 ? 16.120  78.404  16.385 1.00 54.28  ? 221 LEU B O      1 
ATOM   4576  C CB     . LEU B 1 221 ? 18.022  78.897  13.729 1.00 32.03  ? 221 LEU B CB     1 
ATOM   4577  C CG     . LEU B 1 221 ? 18.924  79.668  14.679 1.00 33.81  ? 221 LEU B CG     1 
ATOM   4578  C CD1    . LEU B 1 221 ? 19.746  78.677  15.455 1.00 46.40  ? 221 LEU B CD1    1 
ATOM   4579  C CD2    . LEU B 1 221 ? 19.841  80.588  13.897 1.00 26.56  ? 221 LEU B CD2    1 
ATOM   4580  N N      . ASP B 1 222 ? 15.111  79.287  14.601 1.00 43.82  ? 222 ASP B N      1 
ATOM   4581  C CA     . ASP B 1 222 ? 14.069  79.867  15.419 1.00 46.61  ? 222 ASP B CA     1 
ATOM   4582  C C      . ASP B 1 222 ? 12.786  79.434  14.843 1.00 45.60  ? 222 ASP B C      1 
ATOM   4583  O O      . ASP B 1 222 ? 12.437  79.835  13.758 1.00 49.84  ? 222 ASP B O      1 
ATOM   4584  C CB     . ASP B 1 222 ? 14.142  81.379  15.446 1.00 52.52  ? 222 ASP B CB     1 
ATOM   4585  C CG     . ASP B 1 222 ? 13.389  81.977  16.616 1.00 60.66  ? 222 ASP B CG     1 
ATOM   4586  O OD1    . ASP B 1 222 ? 12.870  81.210  17.447 1.00 57.03  ? 222 ASP B OD1    1 
ATOM   4587  O OD2    . ASP B 1 222 ? 13.321  83.216  16.714 1.00 67.26  ? 222 ASP B OD2    1 
ATOM   4588  N N      . PHE B 1 223 ? 12.092  78.564  15.542 1.00 48.09  ? 223 PHE B N      1 
ATOM   4589  C CA     . PHE B 1 223 ? 10.813  78.084  15.094 1.00 46.74  ? 223 PHE B CA     1 
ATOM   4590  C C      . PHE B 1 223 ? 9.966   79.266  14.770 1.00 47.85  ? 223 PHE B C      1 
ATOM   4591  O O      . PHE B 1 223 ? 9.272   79.276  13.781 1.00 54.95  ? 223 PHE B O      1 
ATOM   4592  C CB     . PHE B 1 223 ? 10.178  77.341  16.243 1.00 45.38  ? 223 PHE B CB     1 
ATOM   4593  C CG     . PHE B 1 223 ? 8.957   76.565  15.895 1.00 37.94  ? 223 PHE B CG     1 
ATOM   4594  C CD1    . PHE B 1 223 ? 9.030   75.488  15.049 1.00 44.60  ? 223 PHE B CD1    1 
ATOM   4595  C CD2    . PHE B 1 223 ? 7.752   76.870  16.486 1.00 36.10  ? 223 PHE B CD2    1 
ATOM   4596  C CE1    . PHE B 1 223 ? 7.906   74.754  14.757 1.00 48.67  ? 223 PHE B CE1    1 
ATOM   4597  C CE2    . PHE B 1 223 ? 6.625   76.141  16.201 1.00 44.14  ? 223 PHE B CE2    1 
ATOM   4598  C CZ     . PHE B 1 223 ? 6.702   75.078  15.334 1.00 46.32  ? 223 PHE B CZ     1 
ATOM   4599  N N      . GLU B 1 224 ? 10.037  80.306  15.565 1.00 47.53  ? 224 GLU B N      1 
ATOM   4600  C CA     . GLU B 1 224 ? 9.150   81.429  15.353 1.00 48.60  ? 224 GLU B CA     1 
ATOM   4601  C C      . GLU B 1 224 ? 9.421   82.186  14.070 1.00 51.33  ? 224 GLU B C      1 
ATOM   4602  O O      . GLU B 1 224 ? 8.497   82.525  13.352 1.00 51.04  ? 224 GLU B O      1 
ATOM   4603  C CB     . GLU B 1 224 ? 9.192   82.335  16.568 1.00 57.84  ? 224 GLU B CB     1 
ATOM   4604  C CG     . GLU B 1 224 ? 8.653   81.681  17.825 1.00 54.32  ? 224 GLU B CG     1 
ATOM   4605  C CD     . GLU B 1 224 ? 7.812   82.626  18.651 1.00 60.67  ? 224 GLU B CD     1 
ATOM   4606  O OE1    . GLU B 1 224 ? 7.902   83.850  18.432 1.00 67.48  ? 224 GLU B OE1    1 
ATOM   4607  O OE2    . GLU B 1 224 ? 7.062   82.148  19.521 1.00 59.72  ? 224 GLU B OE2    1 
ATOM   4608  N N      . GLN B 1 225 ? 10.674  82.454  13.751 1.00 52.67  ? 225 GLN B N      1 
ATOM   4609  C CA     . GLN B 1 225 ? 10.992  83.101  12.496 1.00 47.17  ? 225 GLN B CA     1 
ATOM   4610  C C      . GLN B 1 225 ? 10.625  82.187  11.374 1.00 47.74  ? 225 GLN B C      1 
ATOM   4611  O O      . GLN B 1 225 ? 10.104  82.624  10.367 1.00 52.41  ? 225 GLN B O      1 
ATOM   4612  C CB     . GLN B 1 225 ? 12.469  83.402  12.400 1.00 47.51  ? 225 GLN B CB     1 
ATOM   4613  C CG     . GLN B 1 225 ? 12.861  84.816  12.751 1.00 73.16  ? 225 GLN B CG     1 
ATOM   4614  C CD     . GLN B 1 225 ? 14.220  85.163  12.191 1.00 89.74  ? 225 GLN B CD     1 
ATOM   4615  O OE1    . GLN B 1 225 ? 15.162  84.378  12.291 1.00 88.06  ? 225 GLN B OE1    1 
ATOM   4616  N NE2    . GLN B 1 225 ? 14.330  86.339  11.588 1.00 94.02  ? 225 GLN B NE2    1 
ATOM   4617  N N      . GLU B 1 226 ? 10.887  80.901  11.538 1.00 40.68  ? 226 GLU B N      1 
ATOM   4618  C CA     . GLU B 1 226 ? 10.647  79.985  10.451 1.00 35.97  ? 226 GLU B CA     1 
ATOM   4619  C C      . GLU B 1 226 ? 9.205   79.606  10.285 1.00 41.09  ? 226 GLU B C      1 
ATOM   4620  O O      . GLU B 1 226 ? 8.798   79.266  9.194  1.00 51.47  ? 226 GLU B O      1 
ATOM   4621  C CB     . GLU B 1 226 ? 11.570  78.795  10.534 1.00 38.92  ? 226 GLU B CB     1 
ATOM   4622  C CG     . GLU B 1 226 ? 13.039  79.180  10.509 1.00 39.94  ? 226 GLU B CG     1 
ATOM   4623  C CD     . GLU B 1 226 ? 13.764  78.661  9.288  1.00 48.14  ? 226 GLU B CD     1 
ATOM   4624  O OE1    . GLU B 1 226 ? 13.094  78.327  8.298  1.00 50.43  ? 226 GLU B OE1    1 
ATOM   4625  O OE2    . GLU B 1 226 ? 15.007  78.596  9.316  1.00 44.29  ? 226 GLU B OE2    1 
ATOM   4626  N N      . MET B 1 227 ? 8.393   79.710  11.320 1.00 38.20  ? 227 MET B N      1 
ATOM   4627  C CA     . MET B 1 227 ? 6.975   79.461  11.126 1.00 42.51  ? 227 MET B CA     1 
ATOM   4628  C C      . MET B 1 227 ? 6.485   80.595  10.274 1.00 52.69  ? 227 MET B C      1 
ATOM   4629  O O      . MET B 1 227 ? 5.609   80.423  9.443  1.00 58.74  ? 227 MET B O      1 
ATOM   4630  C CB     . MET B 1 227 ? 6.199   79.436  12.429 1.00 38.39  ? 227 MET B CB     1 
ATOM   4631  C CG     . MET B 1 227 ? 6.290   78.156  13.224 1.00 47.30  ? 227 MET B CG     1 
ATOM   4632  S SD     . MET B 1 227 ? 5.584   76.749  12.366 1.00 55.37  ? 227 MET B SD     1 
ATOM   4633  C CE     . MET B 1 227 ? 4.034   77.434  11.820 1.00 60.47  ? 227 MET B CE     1 
ATOM   4634  N N      . ALA B 1 228 ? 7.070   81.762  10.465 1.00 49.80  ? 228 ALA B N      1 
ATOM   4635  C CA     . ALA B 1 228 ? 6.633   82.936  9.750  1.00 41.67  ? 228 ALA B CA     1 
ATOM   4636  C C      . ALA B 1 228 ? 7.027   82.901  8.323  1.00 47.18  ? 228 ALA B C      1 
ATOM   4637  O O      . ALA B 1 228 ? 6.271   83.304  7.474  1.00 50.35  ? 228 ALA B O      1 
ATOM   4638  C CB     . ALA B 1 228 ? 7.237   84.143  10.388 1.00 34.56  ? 228 ALA B CB     1 
ATOM   4639  N N      . THR B 1 229 ? 8.245   82.468  8.051  1.00 49.67  ? 229 THR B N      1 
ATOM   4640  C CA     . THR B 1 229 ? 8.745   82.440  6.699  1.00 47.38  ? 229 THR B CA     1 
ATOM   4641  C C      . THR B 1 229 ? 7.859   81.551  5.912  1.00 50.69  ? 229 THR B C      1 
ATOM   4642  O O      . THR B 1 229 ? 7.849   81.589  4.699  1.00 60.06  ? 229 THR B O      1 
ATOM   4643  C CB     . THR B 1 229 ? 10.173  81.908  6.661  1.00 45.09  ? 229 THR B CB     1 
ATOM   4644  O OG1    . THR B 1 229 ? 10.942  82.542  7.689  1.00 37.78  ? 229 THR B OG1    1 
ATOM   4645  C CG2    . THR B 1 229 ? 10.828  82.191  5.328  1.00 53.57  ? 229 THR B CG2    1 
ATOM   4646  N N      . ALA B 1 230 ? 7.072   80.753  6.591  1.00 50.05  ? 230 ALA B N      1 
ATOM   4647  C CA     . ALA B 1 230 ? 6.260   79.787  5.876  1.00 54.58  ? 230 ALA B CA     1 
ATOM   4648  C C      . ALA B 1 230 ? 4.923   80.359  5.557  1.00 54.19  ? 230 ALA B C      1 
ATOM   4649  O O      . ALA B 1 230 ? 4.204   79.840  4.719  1.00 55.67  ? 230 ALA B O      1 
ATOM   4650  C CB     . ALA B 1 230 ? 6.107   78.528  6.692  1.00 51.40  ? 230 ALA B CB     1 
ATOM   4651  N N      . ALA B 1 231 ? 4.579   81.438  6.214  1.00 47.82  ? 231 ALA B N      1 
ATOM   4652  C CA     . ALA B 1 231 ? 3.321   82.064  5.950  1.00 52.42  ? 231 ALA B CA     1 
ATOM   4653  C C      . ALA B 1 231 ? 3.589   83.317  5.183  1.00 53.37  ? 231 ALA B C      1 
ATOM   4654  O O      . ALA B 1 231 ? 2.713   83.851  4.528  1.00 51.30  ? 231 ALA B O      1 
ATOM   4655  C CB     . ALA B 1 231 ? 2.648   82.383  7.249  1.00 45.46  ? 231 ALA B CB     1 
ATOM   4656  N N      . SER B 1 232 ? 4.812   83.791  5.239  1.00 52.32  ? 232 SER B N      1 
ATOM   4657  C CA     . SER B 1 232 ? 5.157   85.008  4.563  1.00 49.14  ? 232 SER B CA     1 
ATOM   4658  C C      . SER B 1 232 ? 5.771   84.674  3.237  1.00 52.33  ? 232 SER B C      1 
ATOM   4659  O O      . SER B 1 232 ? 5.948   85.539  2.394  1.00 57.86  ? 232 SER B O      1 
ATOM   4660  C CB     . SER B 1 232 ? 6.131   85.795  5.418  1.00 47.71  ? 232 SER B CB     1 
ATOM   4661  O OG     . SER B 1 232 ? 5.602   86.013  6.713  1.00 45.12  ? 232 SER B OG     1 
ATOM   4662  N N      . SER B 1 233 ? 6.080   83.403  3.038  1.00 51.58  ? 233 SER B N      1 
ATOM   4663  C CA     . SER B 1 233 ? 6.656   82.956  1.785  1.00 57.05  ? 233 SER B CA     1 
ATOM   4664  C C      . SER B 1 233 ? 6.406   81.479  1.602  1.00 60.20  ? 233 SER B C      1 
ATOM   4665  O O      . SER B 1 233 ? 6.064   80.788  2.537  1.00 65.66  ? 233 SER B O      1 
ATOM   4666  C CB     . SER B 1 233 ? 8.152   83.201  1.773  1.00 61.44  ? 233 SER B CB     1 
ATOM   4667  O OG     . SER B 1 233 ? 8.861   82.017  2.075  1.00 64.01  ? 233 SER B OG     1 
ATOM   4668  N N      . SER B 1 234 ? 6.577   80.980  0.395  1.00 62.62  ? 234 SER B N      1 
ATOM   4669  C CA     . SER B 1 234 ? 6.338   79.581  0.128  1.00 67.40  ? 234 SER B CA     1 
ATOM   4670  C C      . SER B 1 234 ? 7.641   78.907  -0.150 1.00 70.06  ? 234 SER B C      1 
ATOM   4671  O O      . SER B 1 234 ? 7.668   77.854  -0.767 1.00 72.31  ? 234 SER B O      1 
ATOM   4672  C CB     . SER B 1 234 ? 5.463   79.442  -1.103 1.00 67.04  ? 234 SER B CB     1 
ATOM   4673  O OG     . SER B 1 234 ? 6.162   79.853  -2.261 1.00 73.16  ? 234 SER B OG     1 
ATOM   4674  N N      . SER B 1 235 ? 8.740   79.479  0.311  1.00 64.04  ? 235 SER B N      1 
ATOM   4675  C CA     . SER B 1 235 ? 10.043  78.936  -0.035 1.00 62.83  ? 235 SER B CA     1 
ATOM   4676  C C      . SER B 1 235 ? 10.358  77.636  0.617  1.00 57.40  ? 235 SER B C      1 
ATOM   4677  O O      . SER B 1 235 ? 10.994  76.782  0.018  1.00 60.12  ? 235 SER B O      1 
ATOM   4678  C CB     . SER B 1 235 ? 11.109  79.925  0.366  1.00 66.86  ? 235 SER B CB     1 
ATOM   4679  O OG     . SER B 1 235 ? 10.993  80.259  1.733  1.00 68.29  ? 235 SER B OG     1 
ATOM   4680  N N      . LEU B 1 236 ? 9.931   77.476  1.853  1.00 56.06  ? 236 LEU B N      1 
ATOM   4681  C CA     . LEU B 1 236 ? 10.269  76.284  2.600  1.00 52.48  ? 236 LEU B CA     1 
ATOM   4682  C C      . LEU B 1 236 ? 9.600   75.059  2.070  1.00 54.98  ? 236 LEU B C      1 
ATOM   4683  O O      . LEU B 1 236 ? 10.083  73.962  2.262  1.00 59.69  ? 236 LEU B O      1 
ATOM   4684  C CB     . LEU B 1 236 ? 9.863   76.496  4.045  1.00 50.60  ? 236 LEU B CB     1 
ATOM   4685  C CG     . LEU B 1 236 ? 10.487  77.724  4.701  1.00 58.90  ? 236 LEU B CG     1 
ATOM   4686  C CD1    . LEU B 1 236 ? 9.935   77.928  6.099  1.00 47.56  ? 236 LEU B CD1    1 
ATOM   4687  C CD2    . LEU B 1 236 ? 12.002  77.602  4.730  1.00 57.09  ? 236 LEU B CD2    1 
ATOM   4688  N N      . GLU B 1 237 ? 8.478   75.233  1.410  1.00 57.24  ? 237 GLU B N      1 
ATOM   4689  C CA     . GLU B 1 237 ? 7.725   74.107  0.922  1.00 54.62  ? 237 GLU B CA     1 
ATOM   4690  C C      . GLU B 1 237 ? 8.545   73.243  0.018  1.00 56.56  ? 237 GLU B C      1 
ATOM   4691  O O      . GLU B 1 237 ? 9.283   73.742  -0.815 1.00 56.84  ? 237 GLU B O      1 
ATOM   4692  C CB     . GLU B 1 237 ? 6.502   74.604  0.168  1.00 60.17  ? 237 GLU B CB     1 
ATOM   4693  C CG     . GLU B 1 237 ? 5.372   75.098  1.046  1.00 62.72  ? 237 GLU B CG     1 
ATOM   4694  C CD     . GLU B 1 237 ? 4.075   75.220  0.276  1.00 76.11  ? 237 GLU B CD     1 
ATOM   4695  O OE1    . GLU B 1 237 ? 4.110   75.088  -0.964 1.00 76.58  ? 237 GLU B OE1    1 
ATOM   4696  O OE2    . GLU B 1 237 ? 3.022   75.443  0.906  1.00 79.05  ? 237 GLU B OE2    1 
ATOM   4697  N N      . LYS B 1 238 ? 8.406   71.935  0.162  1.00 55.67  ? 238 LYS B N      1 
ATOM   4698  C CA     . LYS B 1 238 ? 9.115   71.020  -0.706 1.00 52.38  ? 238 LYS B CA     1 
ATOM   4699  C C      . LYS B 1 238 ? 8.140   69.961  -1.136 1.00 45.09  ? 238 LYS B C      1 
ATOM   4700  O O      . LYS B 1 238 ? 7.116   69.797  -0.516 1.00 46.08  ? 238 LYS B O      1 
ATOM   4701  C CB     . LYS B 1 238 ? 10.346  70.453  -0.000 1.00 47.40  ? 238 LYS B CB     1 
ATOM   4702  C CG     . LYS B 1 238 ? 11.534  70.219  -0.918 1.00 44.10  ? 238 LYS B CG     1 
ATOM   4703  C CD     . LYS B 1 238 ? 12.817  70.725  -0.290 1.00 43.13  ? 238 LYS B CD     1 
ATOM   4704  C CE     . LYS B 1 238 ? 12.772  72.231  -0.100 1.00 52.68  ? 238 LYS B CE     1 
ATOM   4705  N NZ     . LYS B 1 238 ? 14.087  72.778  0.335  1.00 51.37  ? 238 LYS B NZ     1 
ATOM   4706  N N      . SER B 1 239 ? 8.438   69.242  -2.198 1.00 43.95  ? 239 SER B N      1 
ATOM   4707  C CA     . SER B 1 239 ? 7.510   68.273  -2.720 1.00 46.46  ? 239 SER B CA     1 
ATOM   4708  C C      . SER B 1 239 ? 8.025   66.855  -2.636 1.00 45.81  ? 239 SER B C      1 
ATOM   4709  O O      . SER B 1 239 ? 9.192   66.613  -2.899 1.00 49.35  ? 239 SER B O      1 
ATOM   4710  C CB     . SER B 1 239 ? 7.222   68.622  -4.165 1.00 47.02  ? 239 SER B CB     1 
ATOM   4711  O OG     . SER B 1 239 ? 6.683   69.924  -4.275 1.00 45.52  ? 239 SER B OG     1 
ATOM   4712  N N      . TYR B 1 240 ? 7.171   65.918  -2.253 1.00 40.38  ? 240 TYR B N      1 
ATOM   4713  C CA     . TYR B 1 240 ? 7.578   64.540  -2.177 1.00 40.66  ? 240 TYR B CA     1 
ATOM   4714  C C      . TYR B 1 240 ? 6.705   63.691  -3.009 1.00 40.82  ? 240 TYR B C      1 
ATOM   4715  O O      . TYR B 1 240 ? 5.508   63.836  -2.975 1.00 40.81  ? 240 TYR B O      1 
ATOM   4716  C CB     . TYR B 1 240 ? 7.522   64.039  -0.758 1.00 43.12  ? 240 TYR B CB     1 
ATOM   4717  C CG     . TYR B 1 240 ? 8.025   62.630  -0.557 1.00 43.94  ? 240 TYR B CG     1 
ATOM   4718  C CD1    . TYR B 1 240 ? 9.379   62.350  -0.553 1.00 42.24  ? 240 TYR B CD1    1 
ATOM   4719  C CD2    . TYR B 1 240 ? 7.144   61.584  -0.349 1.00 39.87  ? 240 TYR B CD2    1 
ATOM   4720  C CE1    . TYR B 1 240 ? 9.840   61.065  -0.363 1.00 40.27  ? 240 TYR B CE1    1 
ATOM   4721  C CE2    . TYR B 1 240 ? 7.595   60.299  -0.156 1.00 36.37  ? 240 TYR B CE2    1 
ATOM   4722  C CZ     . TYR B 1 240 ? 8.942   60.046  -0.165 1.00 37.90  ? 240 TYR B CZ     1 
ATOM   4723  O OH     . TYR B 1 240 ? 9.385   58.764  0.023  1.00 42.25  ? 240 TYR B OH     1 
ATOM   4724  N N      . GLU B 1 241 ? 7.323   62.792  -3.763 1.00 43.34  ? 241 GLU B N      1 
ATOM   4725  C CA     . GLU B 1 241 ? 6.593   61.873  -4.610 1.00 47.20  ? 241 GLU B CA     1 
ATOM   4726  C C      . GLU B 1 241 ? 6.203   60.640  -3.851 1.00 43.26  ? 241 GLU B C      1 
ATOM   4727  O O      . GLU B 1 241 ? 7.006   59.734  -3.664 1.00 39.36  ? 241 GLU B O      1 
ATOM   4728  C CB     . GLU B 1 241 ? 7.460   61.467  -5.790 1.00 54.96  ? 241 GLU B CB     1 
ATOM   4729  C CG     . GLU B 1 241 ? 6.822   60.444  -6.717 1.00 57.18  ? 241 GLU B CG     1 
ATOM   4730  C CD     . GLU B 1 241 ? 6.355   61.042  -8.021 1.00 60.47  ? 241 GLU B CD     1 
ATOM   4731  O OE1    . GLU B 1 241 ? 6.792   62.159  -8.356 1.00 57.81  ? 241 GLU B OE1    1 
ATOM   4732  O OE2    . GLU B 1 241 ? 5.559   60.385  -8.716 1.00 69.98  ? 241 GLU B OE2    1 
ATOM   4733  N N      . LEU B 1 242 ? 4.958   60.585  -3.421 1.00 38.87  ? 242 LEU B N      1 
ATOM   4734  C CA     . LEU B 1 242 ? 4.506   59.458  -2.668 1.00 36.62  ? 242 LEU B CA     1 
ATOM   4735  C C      . LEU B 1 242 ? 4.604   58.330  -3.632 1.00 43.77  ? 242 LEU B C      1 
ATOM   4736  O O      . LEU B 1 242 ? 4.541   58.536  -4.831 1.00 52.33  ? 242 LEU B O      1 
ATOM   4737  C CB     . LEU B 1 242 ? 3.076   59.677  -2.235 1.00 33.54  ? 242 LEU B CB     1 
ATOM   4738  C CG     . LEU B 1 242 ? 2.678   59.489  -0.784 1.00 38.47  ? 242 LEU B CG     1 
ATOM   4739  C CD1    . LEU B 1 242 ? 3.539   60.376  0.091  1.00 50.14  ? 242 LEU B CD1    1 
ATOM   4740  C CD2    . LEU B 1 242 ? 1.206   59.824  -0.625 1.00 31.98  ? 242 LEU B CD2    1 
ATOM   4741  N N      . PRO B 1 243 ? 4.760   57.086  -3.122 1.00 40.74  ? 243 PRO B N      1 
ATOM   4742  C CA     . PRO B 1 243 ? 4.962   56.043  -4.116 1.00 40.34  ? 243 PRO B CA     1 
ATOM   4743  C C      . PRO B 1 243 ? 3.783   55.841  -5.041 1.00 50.99  ? 243 PRO B C      1 
ATOM   4744  O O      . PRO B 1 243 ? 3.976   55.301  -6.123 1.00 49.47  ? 243 PRO B O      1 
ATOM   4745  C CB     . PRO B 1 243 ? 5.164   54.807  -3.268 1.00 38.23  ? 243 PRO B CB     1 
ATOM   4746  C CG     . PRO B 1 243 ? 4.397   55.064  -2.033 1.00 41.54  ? 243 PRO B CG     1 
ATOM   4747  C CD     . PRO B 1 243 ? 4.724   56.491  -1.764 1.00 44.00  ? 243 PRO B CD     1 
ATOM   4748  N N      . ASP B 1 244 ? 2.588   56.270  -4.646 1.00 53.76  ? 244 ASP B N      1 
ATOM   4749  C CA     . ASP B 1 244 ? 1.399   56.129  -5.469 1.00 49.23  ? 244 ASP B CA     1 
ATOM   4750  C C      . ASP B 1 244 ? 1.559   57.025  -6.637 1.00 55.04  ? 244 ASP B C      1 
ATOM   4751  O O      . ASP B 1 244 ? 0.776   56.971  -7.567 1.00 59.52  ? 244 ASP B O      1 
ATOM   4752  C CB     . ASP B 1 244 ? 0.172   56.579  -4.703 1.00 47.73  ? 244 ASP B CB     1 
ATOM   4753  C CG     . ASP B 1 244 ? -0.118  55.721  -3.502 1.00 64.35  ? 244 ASP B CG     1 
ATOM   4754  O OD1    . ASP B 1 244 ? 0.571   54.700  -3.317 1.00 74.30  ? 244 ASP B OD1    1 
ATOM   4755  O OD2    . ASP B 1 244 ? -1.044  56.062  -2.740 1.00 62.05  ? 244 ASP B OD2    1 
ATOM   4756  N N      . GLY B 1 245 ? 2.544   57.896  -6.594 1.00 52.52  ? 245 GLY B N      1 
ATOM   4757  C CA     . GLY B 1 245 ? 2.727   58.854  -7.660 1.00 46.77  ? 245 GLY B CA     1 
ATOM   4758  C C      . GLY B 1 245 ? 2.258   60.224  -7.241 1.00 51.36  ? 245 GLY B C      1 
ATOM   4759  O O      . GLY B 1 245 ? 2.614   61.213  -7.860 1.00 57.70  ? 245 GLY B O      1 
ATOM   4760  N N      . GLN B 1 246 ? 1.455   60.301  -6.195 1.00 46.68  ? 246 GLN B N      1 
ATOM   4761  C CA     . GLN B 1 246 ? 0.919   61.572  -5.801 1.00 40.35  ? 246 GLN B CA     1 
ATOM   4762  C C      . GLN B 1 246 ? 2.070   62.391  -5.316 1.00 39.15  ? 246 GLN B C      1 
ATOM   4763  O O      . GLN B 1 246 ? 2.890   61.902  -4.574 1.00 41.07  ? 246 GLN B O      1 
ATOM   4764  C CB     . GLN B 1 246 ? -0.114  61.403  -4.704 1.00 32.34  ? 246 GLN B CB     1 
ATOM   4765  C CG     . GLN B 1 246 ? -0.951  60.154  -4.817 1.00 41.99  ? 246 GLN B CG     1 
ATOM   4766  C CD     . GLN B 1 246 ? -1.965  60.078  -3.707 1.00 48.58  ? 246 GLN B CD     1 
ATOM   4767  O OE1    . GLN B 1 246 ? -2.410  61.100  -3.200 1.00 47.43  ? 246 GLN B OE1    1 
ATOM   4768  N NE2    . GLN B 1 246 ? -2.340  58.866  -3.323 1.00 47.34  ? 246 GLN B NE2    1 
ATOM   4769  N N      . VAL B 1 247 ? 2.160   63.638  -5.750 1.00 39.55  ? 247 VAL B N      1 
ATOM   4770  C CA     . VAL B 1 247 ? 3.198   64.525  -5.279 1.00 40.47  ? 247 VAL B CA     1 
ATOM   4771  C C      . VAL B 1 247 ? 2.604   65.370  -4.207 1.00 44.68  ? 247 VAL B C      1 
ATOM   4772  O O      . VAL B 1 247 ? 1.646   66.086  -4.453 1.00 41.55  ? 247 VAL B O      1 
ATOM   4773  C CB     . VAL B 1 247 ? 3.717   65.446  -6.364 1.00 34.39  ? 247 VAL B CB     1 
ATOM   4774  C CG1    . VAL B 1 247 ? 4.732   66.417  -5.799 1.00 31.65  ? 247 VAL B CG1    1 
ATOM   4775  C CG2    . VAL B 1 247 ? 4.342   64.632  -7.480 1.00 50.24  ? 247 VAL B CG2    1 
ATOM   4776  N N      . ILE B 1 248 ? 3.135   65.268  -2.996 1.00 49.56  ? 248 ILE B N      1 
ATOM   4777  C CA     . ILE B 1 248 ? 2.612   66.013  -1.876 1.00 46.67  ? 248 ILE B CA     1 
ATOM   4778  C C      . ILE B 1 248 ? 3.543   67.150  -1.520 1.00 47.66  ? 248 ILE B C      1 
ATOM   4779  O O      . ILE B 1 248 ? 4.715   67.086  -1.828 1.00 46.56  ? 248 ILE B O      1 
ATOM   4780  C CB     . ILE B 1 248 ? 2.387   65.093  -0.677 1.00 41.08  ? 248 ILE B CB     1 
ATOM   4781  C CG1    . ILE B 1 248 ? 3.686   64.544  -0.135 1.00 39.52  ? 248 ILE B CG1    1 
ATOM   4782  C CG2    . ILE B 1 248 ? 1.474   63.942  -1.057 1.00 39.55  ? 248 ILE B CG2    1 
ATOM   4783  C CD1    . ILE B 1 248 ? 3.503   63.987  1.248  1.00 41.56  ? 248 ILE B CD1    1 
ATOM   4784  N N      . THR B 1 249 ? 3.026   68.203  -0.900 1.00 45.05  ? 249 THR B N      1 
ATOM   4785  C CA     . THR B 1 249 ? 3.836   69.356  -0.570 1.00 43.84  ? 249 THR B CA     1 
ATOM   4786  C C      . THR B 1 249 ? 3.980   69.507  0.905  1.00 49.69  ? 249 THR B C      1 
ATOM   4787  O O      . THR B 1 249 ? 2.992   69.625  1.601  1.00 60.09  ? 249 THR B O      1 
ATOM   4788  C CB     . THR B 1 249 ? 3.189   70.627  -1.066 1.00 47.84  ? 249 THR B CB     1 
ATOM   4789  O OG1    . THR B 1 249 ? 1.813   70.641  -0.676 1.00 53.82  ? 249 THR B OG1    1 
ATOM   4790  C CG2    . THR B 1 249 ? 3.269   70.701  -2.574 1.00 52.54  ? 249 THR B CG2    1 
ATOM   4791  N N      . ILE B 1 250 ? 5.209   69.535  1.400  1.00 46.36  ? 250 ILE B N      1 
ATOM   4792  C CA     . ILE B 1 250 ? 5.460   69.624  2.828  1.00 49.84  ? 250 ILE B CA     1 
ATOM   4793  C C      . ILE B 1 250 ? 6.196   70.899  3.143  1.00 50.76  ? 250 ILE B C      1 
ATOM   4794  O O      . ILE B 1 250 ? 7.284   71.117  2.648  1.00 48.23  ? 250 ILE B O      1 
ATOM   4795  C CB     . ILE B 1 250 ? 6.327   68.445  3.298  1.00 46.21  ? 250 ILE B CB     1 
ATOM   4796  C CG1    . ILE B 1 250 ? 5.671   67.115  2.955  1.00 48.39  ? 250 ILE B CG1    1 
ATOM   4797  C CG2    . ILE B 1 250 ? 6.555   68.503  4.796  1.00 45.57  ? 250 ILE B CG2    1 
ATOM   4798  C CD1    . ILE B 1 250 ? 6.227   66.468  1.715  1.00 47.70  ? 250 ILE B CD1    1 
ATOM   4799  N N      . GLY B 1 251 ? 5.620   71.750  3.976  1.00 47.85  ? 251 GLY B N      1 
ATOM   4800  C CA     . GLY B 1 251 ? 6.237   73.023  4.288  1.00 47.76  ? 251 GLY B CA     1 
ATOM   4801  C C      . GLY B 1 251 ? 6.574   73.335  5.725  1.00 51.12  ? 251 GLY B C      1 
ATOM   4802  O O      . GLY B 1 251 ? 7.702   73.166  6.142  1.00 50.42  ? 251 GLY B O      1 
ATOM   4803  N N      . ASN B 1 252 ? 5.598   73.796  6.491  1.00 57.94  ? 252 ASN B N      1 
ATOM   4804  C CA     . ASN B 1 252 ? 5.843   74.121  7.882  1.00 49.40  ? 252 ASN B CA     1 
ATOM   4805  C C      . ASN B 1 252 ? 6.013   72.855  8.633  1.00 45.55  ? 252 ASN B C      1 
ATOM   4806  O O      . ASN B 1 252 ? 6.485   72.856  9.739  1.00 48.34  ? 252 ASN B O      1 
ATOM   4807  C CB     . ASN B 1 252 ? 4.762   75.018  8.514  1.00 41.32  ? 252 ASN B CB     1 
ATOM   4808  C CG     . ASN B 1 252 ? 3.358   74.487  8.349  1.00 46.42  ? 252 ASN B CG     1 
ATOM   4809  O OD1    . ASN B 1 252 ? 3.052   73.770  7.407  1.00 56.71  ? 252 ASN B OD1    1 
ATOM   4810  N ND2    . ASN B 1 252 ? 2.480   74.878  9.259  1.00 40.69  ? 252 ASN B ND2    1 
ATOM   4811  N N      . GLU B 1 253 ? 5.658   71.748  8.020  1.00 41.56  ? 253 GLU B N      1 
ATOM   4812  C CA     . GLU B 1 253 ? 5.739   70.488  8.700  1.00 40.12  ? 253 GLU B CA     1 
ATOM   4813  C C      . GLU B 1 253 ? 7.144   70.012  8.709  1.00 38.19  ? 253 GLU B C      1 
ATOM   4814  O O      . GLU B 1 253 ? 7.472   69.051  9.370  1.00 33.32  ? 253 GLU B O      1 
ATOM   4815  C CB     . GLU B 1 253 ? 4.842   69.473  8.041  1.00 38.79  ? 253 GLU B CB     1 
ATOM   4816  C CG     . GLU B 1 253 ? 3.388   69.594  8.427  1.00 41.32  ? 253 GLU B CG     1 
ATOM   4817  C CD     . GLU B 1 253 ? 2.650   70.568  7.558  1.00 50.42  ? 253 GLU B CD     1 
ATOM   4818  O OE1    . GLU B 1 253 ? 3.152   70.853  6.457  1.00 57.99  ? 253 GLU B OE1    1 
ATOM   4819  O OE2    . GLU B 1 253 ? 1.573   71.036  7.972  1.00 52.25  ? 253 GLU B OE2    1 
ATOM   4820  N N      . ARG B 1 254 ? 8.007   70.718  8.027  1.00 40.84  ? 254 ARG B N      1 
ATOM   4821  C CA     . ARG B 1 254 ? 9.363   70.266  7.917  1.00 38.09  ? 254 ARG B CA     1 
ATOM   4822  C C      . ARG B 1 254 ? 10.129  70.536  9.157  1.00 45.41  ? 254 ARG B C      1 
ATOM   4823  O O      . ARG B 1 254 ? 11.015  69.796  9.498  1.00 44.83  ? 254 ARG B O      1 
ATOM   4824  C CB     . ARG B 1 254 ? 10.053  70.941  6.756  1.00 40.67  ? 254 ARG B CB     1 
ATOM   4825  C CG     . ARG B 1 254 ? 9.635   70.454  5.390  1.00 40.74  ? 254 ARG B CG     1 
ATOM   4826  C CD     . ARG B 1 254 ? 10.395  71.225  4.336  1.00 36.90  ? 254 ARG B CD     1 
ATOM   4827  N NE     . ARG B 1 254 ? 11.800  70.860  4.322  1.00 35.94  ? 254 ARG B NE     1 
ATOM   4828  C CZ     . ARG B 1 254 ? 12.759  71.639  3.846  1.00 38.14  ? 254 ARG B CZ     1 
ATOM   4829  N NH1    . ARG B 1 254 ? 12.457  72.834  3.378  1.00 45.78  ? 254 ARG B NH1    1 
ATOM   4830  N NH2    . ARG B 1 254 ? 14.017  71.236  3.860  1.00 44.28  ? 254 ARG B NH2    1 
ATOM   4831  N N      . PHE B 1 255 ? 9.795   71.597  9.856  1.00 45.05  ? 255 PHE B N      1 
ATOM   4832  C CA     . PHE B 1 255 ? 10.495  71.939  11.076 1.00 40.82  ? 255 PHE B CA     1 
ATOM   4833  C C      . PHE B 1 255 ? 9.676   71.692  12.294 1.00 41.07  ? 255 PHE B C      1 
ATOM   4834  O O      . PHE B 1 255 ? 10.206  71.614  13.387 1.00 42.56  ? 255 PHE B O      1 
ATOM   4835  C CB     . PHE B 1 255 ? 10.960  73.381  11.070 1.00 48.10  ? 255 PHE B CB     1 
ATOM   4836  C CG     . PHE B 1 255 ? 10.005  74.336  10.451 1.00 51.83  ? 255 PHE B CG     1 
ATOM   4837  C CD1    . PHE B 1 255 ? 9.991   74.529  9.089  1.00 49.40  ? 255 PHE B CD1    1 
ATOM   4838  C CD2    . PHE B 1 255 ? 9.163   75.076  11.237 1.00 46.22  ? 255 PHE B CD2    1 
ATOM   4839  C CE1    . PHE B 1 255 ? 9.123   75.416  8.514  1.00 48.76  ? 255 PHE B CE1    1 
ATOM   4840  C CE2    . PHE B 1 255 ? 8.295   75.969  10.672 1.00 45.15  ? 255 PHE B CE2    1 
ATOM   4841  C CZ     . PHE B 1 255 ? 8.273   76.141  9.309  1.00 52.32  ? 255 PHE B CZ     1 
ATOM   4842  N N      . ARG B 1 256 ? 8.381   71.569  12.113 1.00 36.88  ? 256 ARG B N      1 
ATOM   4843  C CA     . ARG B 1 256 ? 7.532   71.372  13.230 1.00 38.41  ? 256 ARG B CA     1 
ATOM   4844  C C      . ARG B 1 256 ? 7.915   70.061  13.833 1.00 47.20  ? 256 ARG B C      1 
ATOM   4845  O O      . ARG B 1 256 ? 8.093   69.969  15.033 1.00 45.68  ? 256 ARG B O      1 
ATOM   4846  C CB     . ARG B 1 256 ? 6.093   71.375  12.776 1.00 31.46  ? 256 ARG B CB     1 
ATOM   4847  C CG     . ARG B 1 256 ? 5.457   72.739  12.705 1.00 40.47  ? 256 ARG B CG     1 
ATOM   4848  C CD     . ARG B 1 256 ? 4.132   72.653  11.985 1.00 39.57  ? 256 ARG B CD     1 
ATOM   4849  N NE     . ARG B 1 256 ? 3.103   72.043  12.805 1.00 35.22  ? 256 ARG B NE     1 
ATOM   4850  C CZ     . ARG B 1 256 ? 1.884   71.770  12.365 1.00 45.50  ? 256 ARG B CZ     1 
ATOM   4851  N NH1    . ARG B 1 256 ? 1.561   72.045  11.114 1.00 50.59  ? 256 ARG B NH1    1 
ATOM   4852  N NH2    . ARG B 1 256 ? 0.992   71.223  13.172 1.00 53.84  ? 256 ARG B NH2    1 
ATOM   4853  N N      . CYS B 1 257 ? 8.019   69.025  13.015 1.00 49.81  ? 257 CYS B N      1 
ATOM   4854  C CA     . CYS B 1 257 ? 8.318   67.679  13.508 1.00 44.25  ? 257 CYS B CA     1 
ATOM   4855  C C      . CYS B 1 257 ? 9.632   67.576  14.238 1.00 46.13  ? 257 CYS B C      1 
ATOM   4856  O O      . CYS B 1 257 ? 9.676   67.071  15.348 1.00 41.19  ? 257 CYS B O      1 
ATOM   4857  C CB     . CYS B 1 257 ? 8.230   66.660  12.385 1.00 36.12  ? 257 CYS B CB     1 
ATOM   4858  S SG     . CYS B 1 257 ? 9.069   65.094  12.654 1.00 50.65  ? 257 CYS B SG     1 
ATOM   4859  N N      . PRO B 1 258 ? 10.737  68.071  13.634 1.00 43.66  ? 258 PRO B N      1 
ATOM   4860  C CA     . PRO B 1 258 ? 11.944  67.994  14.433 1.00 42.75  ? 258 PRO B CA     1 
ATOM   4861  C C      . PRO B 1 258 ? 11.926  68.863  15.643 1.00 46.91  ? 258 PRO B C      1 
ATOM   4862  O O      . PRO B 1 258 ? 12.763  68.656  16.496 1.00 49.79  ? 258 PRO B O      1 
ATOM   4863  C CB     . PRO B 1 258 ? 12.979  68.527  13.496 1.00 39.54  ? 258 PRO B CB     1 
ATOM   4864  C CG     . PRO B 1 258 ? 12.546  68.043  12.185 1.00 47.08  ? 258 PRO B CG     1 
ATOM   4865  C CD     . PRO B 1 258 ? 11.105  68.398  12.239 1.00 43.64  ? 258 PRO B CD     1 
ATOM   4866  N N      . GLU B 1 259 ? 11.030  69.829  15.744 1.00 44.21  ? 259 GLU B N      1 
ATOM   4867  C CA     . GLU B 1 259 ? 10.964  70.643  16.949 1.00 48.31  ? 259 GLU B CA     1 
ATOM   4868  C C      . GLU B 1 259 ? 10.412  69.903  18.126 1.00 49.04  ? 259 GLU B C      1 
ATOM   4869  O O      . GLU B 1 259 ? 10.631  70.288  19.264 1.00 42.00  ? 259 GLU B O      1 
ATOM   4870  C CB     . GLU B 1 259 ? 10.183  71.928  16.705 1.00 44.58  ? 259 GLU B CB     1 
ATOM   4871  C CG     . GLU B 1 259 ? 9.522   72.581  17.908 1.00 49.30  ? 259 GLU B CG     1 
ATOM   4872  C CD     . GLU B 1 259 ? 10.316  73.719  18.491 1.00 54.55  ? 259 GLU B CD     1 
ATOM   4873  O OE1    . GLU B 1 259 ? 11.261  74.154  17.823 1.00 59.13  ? 259 GLU B OE1    1 
ATOM   4874  O OE2    . GLU B 1 259 ? 9.984   74.189  19.596 1.00 45.03  ? 259 GLU B OE2    1 
ATOM   4875  N N      . ALA B 1 260 ? 9.726   68.801  17.878 1.00 46.47  ? 260 ALA B N      1 
ATOM   4876  C CA     . ALA B 1 260 ? 9.096   68.103  18.969 1.00 36.23  ? 260 ALA B CA     1 
ATOM   4877  C C      . ALA B 1 260 ? 10.190  67.780  19.900 1.00 38.52  ? 260 ALA B C      1 
ATOM   4878  O O      . ALA B 1 260 ? 9.962   67.570  21.061 1.00 48.53  ? 260 ALA B O      1 
ATOM   4879  C CB     . ALA B 1 260 ? 8.430   66.858  18.486 1.00 33.14  ? 260 ALA B CB     1 
ATOM   4880  N N      . LEU B 1 261 ? 11.410  67.788  19.411 1.00 38.40  ? 261 LEU B N      1 
ATOM   4881  C CA     . LEU B 1 261 ? 12.552  67.445  20.236 1.00 38.25  ? 261 LEU B CA     1 
ATOM   4882  C C      . LEU B 1 261 ? 12.861  68.546  21.229 1.00 44.70  ? 261 LEU B C      1 
ATOM   4883  O O      . LEU B 1 261 ? 13.136  68.268  22.387 1.00 41.76  ? 261 LEU B O      1 
ATOM   4884  C CB     . LEU B 1 261 ? 13.764  67.167  19.352 1.00 30.41  ? 261 LEU B CB     1 
ATOM   4885  C CG     . LEU B 1 261 ? 13.764  65.968  18.425 1.00 35.90  ? 261 LEU B CG     1 
ATOM   4886  C CD1    . LEU B 1 261 ? 14.848  66.162  17.384 1.00 34.74  ? 261 LEU B CD1    1 
ATOM   4887  C CD2    . LEU B 1 261 ? 14.003  64.706  19.228 1.00 38.94  ? 261 LEU B CD2    1 
ATOM   4888  N N      . PHE B 1 262 ? 12.825  69.794  20.786 1.00 40.93  ? 262 PHE B N      1 
ATOM   4889  C CA     . PHE B 1 262 ? 13.177  70.895  21.647 1.00 32.95  ? 262 PHE B CA     1 
ATOM   4890  C C      . PHE B 1 262 ? 12.011  71.365  22.463 1.00 34.33  ? 262 PHE B C      1 
ATOM   4891  O O      . PHE B 1 262 ? 12.196  72.066  23.435 1.00 37.13  ? 262 PHE B O      1 
ATOM   4892  C CB     . PHE B 1 262 ? 13.710  72.008  20.810 1.00 33.30  ? 262 PHE B CB     1 
ATOM   4893  C CG     . PHE B 1 262 ? 15.040  71.723  20.193 1.00 34.20  ? 262 PHE B CG     1 
ATOM   4894  C CD1    . PHE B 1 262 ? 16.200  72.032  20.866 1.00 33.49  ? 262 PHE B CD1    1 
ATOM   4895  C CD2    . PHE B 1 262 ? 15.128  71.178  18.932 1.00 37.83  ? 262 PHE B CD2    1 
ATOM   4896  C CE1    . PHE B 1 262 ? 17.428  71.789  20.300 1.00 34.90  ? 262 PHE B CE1    1 
ATOM   4897  C CE2    . PHE B 1 262 ? 16.352  70.926  18.361 1.00 39.71  ? 262 PHE B CE2    1 
ATOM   4898  C CZ     . PHE B 1 262 ? 17.504  71.236  19.044 1.00 39.37  ? 262 PHE B CZ     1 
ATOM   4899  N N      . GLN B 1 263 ? 10.804  70.993  22.085 1.00 36.15  ? 263 GLN B N      1 
ATOM   4900  C CA     . GLN B 1 263 ? 9.639   71.326  22.876 1.00 38.80  ? 263 GLN B CA     1 
ATOM   4901  C C      . GLN B 1 263 ? 8.743   70.163  22.742 1.00 37.88  ? 263 GLN B C      1 
ATOM   4902  O O      . GLN B 1 263 ? 7.992   70.065  21.795 1.00 36.41  ? 263 GLN B O      1 
ATOM   4903  C CB     . GLN B 1 263 ? 8.955   72.548  22.341 1.00 48.20  ? 263 GLN B CB     1 
ATOM   4904  C CG     . GLN B 1 263 ? 8.038   73.245  23.321 1.00 47.05  ? 263 GLN B CG     1 
ATOM   4905  C CD     . GLN B 1 263 ? 7.608   74.602  22.816 1.00 53.01  ? 263 GLN B CD     1 
ATOM   4906  O OE1    . GLN B 1 263 ? 7.908   74.976  21.682 1.00 47.85  ? 263 GLN B OE1    1 
ATOM   4907  N NE2    . GLN B 1 263 ? 6.906   75.351  23.654 1.00 52.54  ? 263 GLN B NE2    1 
ATOM   4908  N N      . PRO B 1 264 ? 8.789   69.241  23.729 1.00 41.53  ? 264 PRO B N      1 
ATOM   4909  C CA     . PRO B 1 264 ? 7.990   68.046  23.521 1.00 45.81  ? 264 PRO B CA     1 
ATOM   4910  C C      . PRO B 1 264 ? 6.569   68.205  23.934 1.00 51.49  ? 264 PRO B C      1 
ATOM   4911  O O      . PRO B 1 264 ? 5.916   67.203  24.158 1.00 54.16  ? 264 PRO B O      1 
ATOM   4912  C CB     . PRO B 1 264 ? 8.613   67.056  24.479 1.00 45.24  ? 264 PRO B CB     1 
ATOM   4913  C CG     . PRO B 1 264 ? 9.891   67.654  24.952 1.00 44.02  ? 264 PRO B CG     1 
ATOM   4914  C CD     . PRO B 1 264 ? 9.562   69.096  24.980 1.00 44.84  ? 264 PRO B CD     1 
ATOM   4915  N N      . SER B 1 265 ? 6.094   69.429  24.055 1.00 50.77  ? 265 SER B N      1 
ATOM   4916  C CA     . SER B 1 265 ? 4.719   69.680  24.441 1.00 53.26  ? 265 SER B CA     1 
ATOM   4917  C C      . SER B 1 265 ? 3.920   69.348  23.240 1.00 46.42  ? 265 SER B C      1 
ATOM   4918  O O      . SER B 1 265 ? 2.714   69.169  23.305 1.00 42.84  ? 265 SER B O      1 
ATOM   4919  C CB     . SER B 1 265 ? 4.539   71.139  24.777 1.00 49.41  ? 265 SER B CB     1 
ATOM   4920  O OG     . SER B 1 265 ? 4.657   71.941  23.619 1.00 47.39  ? 265 SER B OG     1 
ATOM   4921  N N      . PHE B 1 266 ? 4.603   69.195  22.133 1.00 44.70  ? 266 PHE B N      1 
ATOM   4922  C CA     . PHE B 1 266 ? 3.937   68.900  20.889 1.00 51.00  ? 266 PHE B CA     1 
ATOM   4923  C C      . PHE B 1 266 ? 3.373   67.497  20.876 1.00 53.83  ? 266 PHE B C      1 
ATOM   4924  O O      . PHE B 1 266 ? 2.417   67.229  20.165 1.00 54.69  ? 266 PHE B O      1 
ATOM   4925  C CB     . PHE B 1 266 ? 4.946   69.052  19.761 1.00 46.29  ? 266 PHE B CB     1 
ATOM   4926  C CG     . PHE B 1 266 ? 5.268   70.478  19.398 1.00 49.21  ? 266 PHE B CG     1 
ATOM   4927  C CD1    . PHE B 1 266 ? 4.925   71.529  20.226 1.00 49.57  ? 266 PHE B CD1    1 
ATOM   4928  C CD2    . PHE B 1 266 ? 5.920   70.761  18.217 1.00 47.48  ? 266 PHE B CD2    1 
ATOM   4929  C CE1    . PHE B 1 266 ? 5.224   72.830  19.885 1.00 40.07  ? 266 PHE B CE1    1 
ATOM   4930  C CE2    . PHE B 1 266 ? 6.215   72.059  17.866 1.00 41.86  ? 266 PHE B CE2    1 
ATOM   4931  C CZ     . PHE B 1 266 ? 5.873   73.095  18.704 1.00 37.55  ? 266 PHE B CZ     1 
ATOM   4932  N N      . LEU B 1 267 ? 3.925   66.608  21.691 1.00 58.55  ? 267 LEU B N      1 
ATOM   4933  C CA     . LEU B 1 267 ? 3.500   65.215  21.715 1.00 53.84  ? 267 LEU B CA     1 
ATOM   4934  C C      . LEU B 1 267 ? 2.817   64.881  23.012 1.00 56.89  ? 267 LEU B C      1 
ATOM   4935  O O      . LEU B 1 267 ? 2.510   63.728  23.268 1.00 59.84  ? 267 LEU B O      1 
ATOM   4936  C CB     . LEU B 1 267 ? 4.717   64.317  21.616 1.00 54.23  ? 267 LEU B CB     1 
ATOM   4937  C CG     . LEU B 1 267 ? 5.811   64.640  20.615 1.00 62.08  ? 267 LEU B CG     1 
ATOM   4938  C CD1    . LEU B 1 267 ? 6.983   63.712  20.852 1.00 55.05  ? 267 LEU B CD1    1 
ATOM   4939  C CD2    . LEU B 1 267 ? 5.270   64.448  19.217 1.00 62.82  ? 267 LEU B CD2    1 
ATOM   4940  N N      . GLY B 1 268 ? 2.621   65.873  23.862 1.00 55.77  ? 268 GLY B N      1 
ATOM   4941  C CA     . GLY B 1 268 ? 1.925   65.656  25.112 1.00 55.28  ? 268 GLY B CA     1 
ATOM   4942  C C      . GLY B 1 268 ? 2.850   65.264  26.210 1.00 54.07  ? 268 GLY B C      1 
ATOM   4943  O O      . GLY B 1 268 ? 2.452   64.617  27.162 1.00 65.00  ? 268 GLY B O      1 
ATOM   4944  N N      . MET B 1 269 ? 4.098   65.648  26.069 1.00 52.68  ? 269 MET B N      1 
ATOM   4945  C CA     . MET B 1 269 ? 5.067   65.314  27.070 1.00 57.96  ? 269 MET B CA     1 
ATOM   4946  C C      . MET B 1 269 ? 5.417   66.559  27.834 1.00 64.02  ? 269 MET B C      1 
ATOM   4947  O O      . MET B 1 269 ? 5.643   67.604  27.241 1.00 62.44  ? 269 MET B O      1 
ATOM   4948  C CB     . MET B 1 269 ? 6.291   64.659  26.444 1.00 52.86  ? 269 MET B CB     1 
ATOM   4949  C CG     . MET B 1 269 ? 6.013   63.274  25.898 1.00 56.52  ? 269 MET B CG     1 
ATOM   4950  S SD     . MET B 1 269 ? 7.478   62.502  25.215 1.00 56.61  ? 269 MET B SD     1 
ATOM   4951  C CE     . MET B 1 269 ? 8.590   62.595  26.609 1.00 51.73  ? 269 MET B CE     1 
ATOM   4952  N N      . GLU B 1 270 ? 5.466   66.454  29.156 1.00 64.60  ? 270 GLU B N      1 
ATOM   4953  C CA     . GLU B 1 270 ? 5.758   67.595  30.001 1.00 55.53  ? 270 GLU B CA     1 
ATOM   4954  C C      . GLU B 1 270 ? 7.236   67.596  30.244 1.00 51.83  ? 270 GLU B C      1 
ATOM   4955  O O      . GLU B 1 270 ? 7.741   68.380  31.031 1.00 56.29  ? 270 GLU B O      1 
ATOM   4956  C CB     . GLU B 1 270 ? 4.988   67.462  31.295 1.00 59.22  ? 270 GLU B CB     1 
ATOM   4957  C CG     . GLU B 1 270 ? 3.504   67.224  31.089 1.00 65.99  ? 270 GLU B CG     1 
ATOM   4958  C CD     . GLU B 1 270 ? 2.813   68.394  30.418 1.00 77.59  ? 270 GLU B CD     1 
ATOM   4959  O OE1    . GLU B 1 270 ? 2.606   69.427  31.088 1.00 76.53  ? 270 GLU B OE1    1 
ATOM   4960  O OE2    . GLU B 1 270 ? 2.467   68.282  29.225 1.00 84.82  ? 270 GLU B OE2    1 
ATOM   4961  N N      . SER B 1 271 ? 7.932   66.707  29.564 1.00 52.70  ? 271 SER B N      1 
ATOM   4962  C CA     . SER B 1 271 ? 9.363   66.591  29.730 1.00 55.49  ? 271 SER B CA     1 
ATOM   4963  C C      . SER B 1 271 ? 10.159  67.707  29.143 1.00 51.19  ? 271 SER B C      1 
ATOM   4964  O O      . SER B 1 271 ? 9.672   68.466  28.328 1.00 52.35  ? 271 SER B O      1 
ATOM   4965  C CB     . SER B 1 271 ? 9.851   65.286  29.130 1.00 54.85  ? 271 SER B CB     1 
ATOM   4966  O OG     . SER B 1 271 ? 9.280   64.176  29.796 1.00 57.25  ? 271 SER B OG     1 
ATOM   4967  N N      . CYS B 1 272 ? 11.386  67.835  29.592 1.00 53.10  ? 272 CYS B N      1 
ATOM   4968  C CA     . CYS B 1 272 ? 12.242  68.866  29.096 1.00 52.53  ? 272 CYS B CA     1 
ATOM   4969  C C      . CYS B 1 272 ? 12.755  68.520  27.726 1.00 52.94  ? 272 CYS B C      1 
ATOM   4970  O O      . CYS B 1 272 ? 12.782  67.364  27.352 1.00 56.75  ? 272 CYS B O      1 
ATOM   4971  C CB     . CYS B 1 272 ? 13.400  69.022  30.049 1.00 50.92  ? 272 CYS B CB     1 
ATOM   4972  S SG     . CYS B 1 272 ? 12.939  68.988  31.792 1.00 99.56  ? 272 CYS B SG     1 
ATOM   4973  N N      . GLY B 1 273 ? 13.173  69.520  26.975 1.00 46.18  ? 273 GLY B N      1 
ATOM   4974  C CA     . GLY B 1 273 ? 13.671  69.286  25.649 1.00 41.96  ? 273 GLY B CA     1 
ATOM   4975  C C      . GLY B 1 273 ? 15.065  68.784  25.658 1.00 39.40  ? 273 GLY B C      1 
ATOM   4976  O O      . GLY B 1 273 ? 15.662  68.646  26.702 1.00 40.49  ? 273 GLY B O      1 
ATOM   4977  N N      . ILE B 1 274 ? 15.606  68.528  24.489 1.00 35.10  ? 274 ILE B N      1 
ATOM   4978  C CA     . ILE B 1 274 ? 16.905  67.953  24.433 1.00 37.85  ? 274 ILE B CA     1 
ATOM   4979  C C      . ILE B 1 274 ? 17.897  68.969  24.918 1.00 38.81  ? 274 ILE B C      1 
ATOM   4980  O O      . ILE B 1 274 ? 18.927  68.613  25.459 1.00 46.73  ? 274 ILE B O      1 
ATOM   4981  C CB     . ILE B 1 274 ? 17.230  67.430  23.033 1.00 38.82  ? 274 ILE B CB     1 
ATOM   4982  C CG1    . ILE B 1 274 ? 17.117  68.512  21.973 1.00 44.28  ? 274 ILE B CG1    1 
ATOM   4983  C CG2    . ILE B 1 274 ? 16.301  66.285  22.677 1.00 38.32  ? 274 ILE B CG2    1 
ATOM   4984  C CD1    . ILE B 1 274 ? 17.404  67.976  20.593 1.00 39.35  ? 274 ILE B CD1    1 
ATOM   4985  N N      . HIS B 1 275 ? 17.554  70.236  24.838 1.00 36.31  ? 275 HIS B N      1 
ATOM   4986  C CA     . HIS B 1 275 ? 18.475  71.270  25.265 1.00 38.47  ? 275 HIS B CA     1 
ATOM   4987  C C      . HIS B 1 275 ? 18.539  71.391  26.761 1.00 40.70  ? 275 HIS B C      1 
ATOM   4988  O O      . HIS B 1 275 ? 19.609  71.479  27.328 1.00 40.63  ? 275 HIS B O      1 
ATOM   4989  C CB     . HIS B 1 275 ? 18.158  72.603  24.608 1.00 40.05  ? 275 HIS B CB     1 
ATOM   4990  C CG     . HIS B 1 275 ? 16.813  73.164  24.943 1.00 43.21  ? 275 HIS B CG     1 
ATOM   4991  N ND1    . HIS B 1 275 ? 15.640  72.635  24.459 1.00 43.55  ? 275 HIS B ND1    1 
ATOM   4992  C CD2    . HIS B 1 275 ? 16.462  74.243  25.679 1.00 45.86  ? 275 HIS B CD2    1 
ATOM   4993  C CE1    . HIS B 1 275 ? 14.622  73.344  24.905 1.00 46.39  ? 275 HIS B CE1    1 
ATOM   4994  N NE2    . HIS B 1 275 ? 15.094  74.328  25.647 1.00 50.15  ? 275 HIS B NE2    1 
ATOM   4995  N N      . GLU B 1 276 ? 17.399  71.335  27.417 1.00 39.27  ? 276 GLU B N      1 
ATOM   4996  C CA     . GLU B 1 276 ? 17.370  71.463  28.843 1.00 39.81  ? 276 GLU B CA     1 
ATOM   4997  C C      . GLU B 1 276 ? 17.903  70.221  29.434 1.00 40.23  ? 276 GLU B C      1 
ATOM   4998  O O      . GLU B 1 276 ? 18.604  70.276  30.411 1.00 44.07  ? 276 GLU B O      1 
ATOM   4999  C CB     . GLU B 1 276 ? 15.966  71.669  29.338 1.00 45.46  ? 276 GLU B CB     1 
ATOM   5000  C CG     . GLU B 1 276 ? 15.270  72.877  28.752 1.00 50.82  ? 276 GLU B CG     1 
ATOM   5001  C CD     . GLU B 1 276 ? 13.817  72.955  29.153 1.00 58.21  ? 276 GLU B CD     1 
ATOM   5002  O OE1    . GLU B 1 276 ? 13.472  72.433  30.230 1.00 55.43  ? 276 GLU B OE1    1 
ATOM   5003  O OE2    . GLU B 1 276 ? 13.021  73.540  28.395 1.00 72.52  ? 276 GLU B OE2    1 
ATOM   5004  N N      . THR B 1 277 ? 17.552  69.078  28.879 1.00 41.73  ? 277 THR B N      1 
ATOM   5005  C CA     . THR B 1 277 ? 17.989  67.816  29.445 1.00 37.28  ? 277 THR B CA     1 
ATOM   5006  C C      . THR B 1 277 ? 19.503  67.769  29.466 1.00 36.05  ? 277 THR B C      1 
ATOM   5007  O O      . THR B 1 277 ? 20.093  67.340  30.434 1.00 40.80  ? 277 THR B O      1 
ATOM   5008  C CB     . THR B 1 277 ? 17.364  66.612  28.731 1.00 33.19  ? 277 THR B CB     1 
ATOM   5009  O OG1    . THR B 1 277 ? 16.004  66.472  29.148 1.00 34.97  ? 277 THR B OG1    1 
ATOM   5010  C CG2    . THR B 1 277 ? 18.091  65.341  29.060 1.00 32.36  ? 277 THR B CG2    1 
ATOM   5011  N N      . THR B 1 278 ? 20.144  68.237  28.418 1.00 34.64  ? 278 THR B N      1 
ATOM   5012  C CA     . THR B 1 278 ? 21.585  68.261  28.393 1.00 34.86  ? 278 THR B CA     1 
ATOM   5013  C C      . THR B 1 278 ? 22.068  69.029  29.581 1.00 35.24  ? 278 THR B C      1 
ATOM   5014  O O      . THR B 1 278 ? 22.869  68.545  30.341 1.00 37.15  ? 278 THR B O      1 
ATOM   5015  C CB     . THR B 1 278 ? 22.128  68.836  27.090 1.00 32.86  ? 278 THR B CB     1 
ATOM   5016  O OG1    . THR B 1 278 ? 21.788  67.953  26.020 1.00 33.45  ? 278 THR B OG1    1 
ATOM   5017  C CG2    . THR B 1 278 ? 23.618  68.966  27.139 1.00 32.40  ? 278 THR B CG2    1 
ATOM   5018  N N      . PHE B 1 279 ? 21.578  70.232  29.761 1.00 36.10  ? 279 PHE B N      1 
ATOM   5019  C CA     . PHE B 1 279 ? 22.035  71.079  30.854 1.00 35.23  ? 279 PHE B CA     1 
ATOM   5020  C C      . PHE B 1 279 ? 21.768  70.429  32.166 1.00 34.04  ? 279 PHE B C      1 
ATOM   5021  O O      . PHE B 1 279 ? 22.610  70.436  33.036 1.00 33.54  ? 279 PHE B O      1 
ATOM   5022  C CB     . PHE B 1 279 ? 21.331  72.427  30.747 1.00 30.28  ? 279 PHE B CB     1 
ATOM   5023  C CG     . PHE B 1 279 ? 21.467  73.323  31.936 1.00 27.36  ? 279 PHE B CG     1 
ATOM   5024  C CD1    . PHE B 1 279 ? 22.596  74.083  32.117 1.00 29.90  ? 279 PHE B CD1    1 
ATOM   5025  C CD2    . PHE B 1 279 ? 20.415  73.478  32.815 1.00 26.94  ? 279 PHE B CD2    1 
ATOM   5026  C CE1    . PHE B 1 279 ? 22.701  74.940  33.189 1.00 29.37  ? 279 PHE B CE1    1 
ATOM   5027  C CE2    . PHE B 1 279 ? 20.513  74.330  33.892 1.00 26.49  ? 279 PHE B CE2    1 
ATOM   5028  C CZ     . PHE B 1 279 ? 21.657  75.066  34.078 1.00 26.43  ? 279 PHE B CZ     1 
ATOM   5029  N N      . ASN B 1 280 ? 20.609  69.817  32.305 1.00 36.53  ? 280 ASN B N      1 
ATOM   5030  C CA     . ASN B 1 280 ? 20.218  69.243  33.574 1.00 36.65  ? 280 ASN B CA     1 
ATOM   5031  C C      . ASN B 1 280 ? 21.071  68.080  33.911 1.00 38.59  ? 280 ASN B C      1 
ATOM   5032  O O      . ASN B 1 280 ? 21.011  67.570  35.004 1.00 44.20  ? 280 ASN B O      1 
ATOM   5033  C CB     . ASN B 1 280 ? 18.762  68.796  33.526 1.00 35.62  ? 280 ASN B CB     1 
ATOM   5034  C CG     . ASN B 1 280 ? 17.799  69.943  33.332 1.00 37.01  ? 280 ASN B CG     1 
ATOM   5035  O OD1    . ASN B 1 280 ? 18.187  71.104  33.338 1.00 40.89  ? 280 ASN B OD1    1 
ATOM   5036  N ND2    . ASN B 1 280 ? 16.528  69.617  33.156 1.00 35.40  ? 280 ASN B ND2    1 
ATOM   5037  N N      . SER B 1 281 ? 21.873  67.643  32.971 1.00 35.77  ? 281 SER B N      1 
ATOM   5038  C CA     . SER B 1 281 ? 22.753  66.522  33.204 1.00 36.59  ? 281 SER B CA     1 
ATOM   5039  C C      . SER B 1 281 ? 24.137  67.027  33.397 1.00 42.09  ? 281 SER B C      1 
ATOM   5040  O O      . SER B 1 281 ? 24.882  66.470  34.177 1.00 42.85  ? 281 SER B O      1 
ATOM   5041  C CB     . SER B 1 281 ? 22.739  65.609  32.022 1.00 41.36  ? 281 SER B CB     1 
ATOM   5042  O OG     . SER B 1 281 ? 23.750  64.648  32.140 1.00 47.39  ? 281 SER B OG     1 
ATOM   5043  N N      . ILE B 1 282 ? 24.503  68.091  32.692 1.00 41.64  ? 282 ILE B N      1 
ATOM   5044  C CA     . ILE B 1 282 ? 25.819  68.678  32.835 1.00 38.62  ? 282 ILE B CA     1 
ATOM   5045  C C      . ILE B 1 282 ? 25.813  69.348  34.172 1.00 40.91  ? 282 ILE B C      1 
ATOM   5046  O O      . ILE B 1 282 ? 26.841  69.487  34.790 1.00 44.14  ? 282 ILE B O      1 
ATOM   5047  C CB     . ILE B 1 282 ? 26.125  69.657  31.711 1.00 33.51  ? 282 ILE B CB     1 
ATOM   5048  C CG1    . ILE B 1 282 ? 26.110  68.943  30.375 1.00 33.14  ? 282 ILE B CG1    1 
ATOM   5049  C CG2    . ILE B 1 282 ? 27.497  70.265  31.874 1.00 44.02  ? 282 ILE B CG2    1 
ATOM   5050  C CD1    . ILE B 1 282 ? 26.571  69.816  29.237 1.00 39.12  ? 282 ILE B CD1    1 
ATOM   5051  N N      . MET B 1 283 ? 24.644  69.738  34.655 1.00 40.89  ? 283 MET B N      1 
ATOM   5052  C CA     . MET B 1 283 ? 24.531  70.326  35.993 1.00 43.73  ? 283 MET B CA     1 
ATOM   5053  C C      . MET B 1 283 ? 24.342  69.271  37.066 1.00 47.68  ? 283 MET B C      1 
ATOM   5054  O O      . MET B 1 283 ? 24.009  69.589  38.197 1.00 51.72  ? 283 MET B O      1 
ATOM   5055  C CB     . MET B 1 283 ? 23.407  71.337  36.066 1.00 34.59  ? 283 MET B CB     1 
ATOM   5056  C CG     . MET B 1 283 ? 23.777  72.670  35.474 1.00 38.01  ? 283 MET B CG     1 
ATOM   5057  S SD     . MET B 1 283 ? 24.972  73.533  36.491 1.00 58.89  ? 283 MET B SD     1 
ATOM   5058  C CE     . MET B 1 283 ? 25.499  74.834  35.382 1.00 49.35  ? 283 MET B CE     1 
ATOM   5059  N N      . LYS B 1 284 ? 24.580  68.013  36.738 1.00 43.92  ? 284 LYS B N      1 
ATOM   5060  C CA     . LYS B 1 284 ? 24.500  66.953  37.719 1.00 40.30  ? 284 LYS B CA     1 
ATOM   5061  C C      . LYS B 1 284 ? 25.884  66.391  37.732 1.00 39.61  ? 284 LYS B C      1 
ATOM   5062  O O      . LYS B 1 284 ? 26.070  65.201  37.905 1.00 42.99  ? 284 LYS B O      1 
ATOM   5063  C CB     . LYS B 1 284 ? 23.464  65.918  37.322 1.00 37.13  ? 284 LYS B CB     1 
ATOM   5064  C CG     . LYS B 1 284 ? 22.053  66.302  37.719 1.00 32.86  ? 284 LYS B CG     1 
ATOM   5065  C CD     . LYS B 1 284 ? 21.263  65.108  38.214 1.00 27.85  ? 284 LYS B CD     1 
ATOM   5066  C CE     . LYS B 1 284 ? 21.022  64.099  37.113 1.00 31.09  ? 284 LYS B CE     1 
ATOM   5067  N NZ     . LYS B 1 284 ? 20.367  62.876  37.649 1.00 37.77  ? 284 LYS B NZ     1 
ATOM   5068  N N      . CYS B 1 285 ? 26.863  67.258  37.520 1.00 34.48  ? 285 CYS B N      1 
ATOM   5069  C CA     . CYS B 1 285 ? 28.255  66.852  37.551 1.00 38.03  ? 285 CYS B CA     1 
ATOM   5070  C C      . CYS B 1 285 ? 29.016  67.889  38.351 1.00 44.75  ? 285 CYS B C      1 
ATOM   5071  O O      . CYS B 1 285 ? 28.462  68.904  38.732 1.00 45.43  ? 285 CYS B O      1 
ATOM   5072  C CB     . CYS B 1 285 ? 28.827  66.749  36.147 1.00 34.32  ? 285 CYS B CB     1 
ATOM   5073  S SG     . CYS B 1 285 ? 28.305  65.328  35.179 1.00 42.43  ? 285 CYS B SG     1 
ATOM   5074  N N      . ASP B 1 286 ? 30.279  67.637  38.625 1.00 48.16  ? 286 ASP B N      1 
ATOM   5075  C CA     . ASP B 1 286 ? 31.062  68.533  39.446 1.00 53.87  ? 286 ASP B CA     1 
ATOM   5076  C C      . ASP B 1 286 ? 31.360  69.746  38.669 1.00 57.19  ? 286 ASP B C      1 
ATOM   5077  O O      . ASP B 1 286 ? 31.529  69.666  37.474 1.00 60.30  ? 286 ASP B O      1 
ATOM   5078  C CB     . ASP B 1 286 ? 32.373  67.862  39.803 1.00 59.33  ? 286 ASP B CB     1 
ATOM   5079  C CG     . ASP B 1 286 ? 33.073  68.521  40.968 1.00 82.56  ? 286 ASP B CG     1 
ATOM   5080  O OD1    . ASP B 1 286 ? 32.444  69.344  41.667 1.00 84.61  ? 286 ASP B OD1    1 
ATOM   5081  O OD2    . ASP B 1 286 ? 34.257  68.204  41.192 1.00 90.41  ? 286 ASP B OD2    1 
ATOM   5082  N N      . VAL B 1 287 ? 31.434  70.886  39.336 1.00 54.64  ? 287 VAL B N      1 
ATOM   5083  C CA     . VAL B 1 287 ? 31.644  72.132  38.647 1.00 47.20  ? 287 VAL B CA     1 
ATOM   5084  C C      . VAL B 1 287 ? 32.881  72.010  37.814 1.00 52.98  ? 287 VAL B C      1 
ATOM   5085  O O      . VAL B 1 287 ? 32.955  72.555  36.731 1.00 52.24  ? 287 VAL B O      1 
ATOM   5086  C CB     . VAL B 1 287 ? 31.822  73.247  39.653 1.00 42.72  ? 287 VAL B CB     1 
ATOM   5087  C CG1    . VAL B 1 287 ? 31.357  74.567  39.071 1.00 43.62  ? 287 VAL B CG1    1 
ATOM   5088  C CG2    . VAL B 1 287 ? 31.069  72.921  40.928 1.00 49.43  ? 287 VAL B CG2    1 
ATOM   5089  N N      . ASP B 1 288 ? 33.845  71.242  38.277 1.00 57.23  ? 288 ASP B N      1 
ATOM   5090  C CA     . ASP B 1 288 ? 35.117  71.161  37.586 1.00 53.79  ? 288 ASP B CA     1 
ATOM   5091  C C      . ASP B 1 288 ? 35.023  70.527  36.241 1.00 54.77  ? 288 ASP B C      1 
ATOM   5092  O O      . ASP B 1 288 ? 35.753  70.906  35.340 1.00 62.93  ? 288 ASP B O      1 
ATOM   5093  C CB     . ASP B 1 288 ? 36.117  70.373  38.414 1.00 59.48  ? 288 ASP B CB     1 
ATOM   5094  C CG     . ASP B 1 288 ? 36.190  70.840  39.848 1.00 74.21  ? 288 ASP B CG     1 
ATOM   5095  O OD1    . ASP B 1 288 ? 35.951  72.036  40.108 1.00 80.76  ? 288 ASP B OD1    1 
ATOM   5096  O OD2    . ASP B 1 288 ? 36.505  70.008  40.722 1.00 68.58  ? 288 ASP B OD2    1 
ATOM   5097  N N      . ILE B 1 289 ? 34.151  69.542  36.081 1.00 51.65  ? 289 ILE B N      1 
ATOM   5098  C CA     . ILE B 1 289 ? 34.106  68.813  34.817 1.00 50.26  ? 289 ILE B CA     1 
ATOM   5099  C C      . ILE B 1 289 ? 33.094  69.340  33.824 1.00 46.28  ? 289 ILE B C      1 
ATOM   5100  O O      . ILE B 1 289 ? 33.154  68.995  32.666 1.00 50.04  ? 289 ILE B O      1 
ATOM   5101  C CB     . ILE B 1 289 ? 33.948  67.295  35.016 1.00 44.60  ? 289 ILE B CB     1 
ATOM   5102  C CG1    . ILE B 1 289 ? 32.503  66.911  35.281 1.00 45.13  ? 289 ILE B CG1    1 
ATOM   5103  C CG2    . ILE B 1 289 ? 34.845  66.805  36.137 1.00 46.35  ? 289 ILE B CG2    1 
ATOM   5104  C CD1    . ILE B 1 289 ? 32.296  65.419  35.229 1.00 36.88  ? 289 ILE B CD1    1 
ATOM   5105  N N      . ARG B 1 290 ? 32.183  70.197  34.252 1.00 40.79  ? 290 ARG B N      1 
ATOM   5106  C CA     . ARG B 1 290 ? 31.161  70.698  33.365 1.00 39.18  ? 290 ARG B CA     1 
ATOM   5107  C C      . ARG B 1 290 ? 31.798  71.512  32.286 1.00 42.92  ? 290 ARG B C      1 
ATOM   5108  O O      . ARG B 1 290 ? 31.248  71.671  31.211 1.00 39.04  ? 290 ARG B O      1 
ATOM   5109  C CB     . ARG B 1 290 ? 30.202  71.605  34.106 1.00 32.00  ? 290 ARG B CB     1 
ATOM   5110  C CG     . ARG B 1 290 ? 29.545  71.067  35.351 1.00 36.77  ? 290 ARG B CG     1 
ATOM   5111  C CD     . ARG B 1 290 ? 28.373  71.970  35.696 1.00 41.40  ? 290 ARG B CD     1 
ATOM   5112  N NE     . ARG B 1 290 ? 28.514  72.687  36.955 1.00 55.08  ? 290 ARG B NE     1 
ATOM   5113  C CZ     . ARG B 1 290 ? 27.924  72.329  38.088 1.00 50.59  ? 290 ARG B CZ     1 
ATOM   5114  N NH1    . ARG B 1 290 ? 27.150  71.261  38.128 1.00 43.27  ? 290 ARG B NH1    1 
ATOM   5115  N NH2    . ARG B 1 290 ? 28.098  73.049  39.182 1.00 50.22  ? 290 ARG B NH2    1 
ATOM   5116  N N      . LYS B 1 291 ? 32.972  72.035  32.543 1.00 43.96  ? 291 LYS B N      1 
ATOM   5117  C CA     . LYS B 1 291 ? 33.596  72.913  31.589 1.00 47.63  ? 291 LYS B CA     1 
ATOM   5118  C C      . LYS B 1 291 ? 33.883  72.187  30.333 1.00 46.83  ? 291 LYS B C      1 
ATOM   5119  O O      . LYS B 1 291 ? 33.490  72.604  29.262 1.00 45.95  ? 291 LYS B O      1 
ATOM   5120  C CB     . LYS B 1 291 ? 34.893  73.414  32.166 1.00 47.97  ? 291 LYS B CB     1 
ATOM   5121  C CG     . LYS B 1 291 ? 34.771  73.887  33.602 1.00 55.25  ? 291 LYS B CG     1 
ATOM   5122  C CD     . LYS B 1 291 ? 33.947  75.157  33.697 1.00 55.50  ? 291 LYS B CD     1 
ATOM   5123  C CE     . LYS B 1 291 ? 33.394  75.350  35.096 1.00 56.66  ? 291 LYS B CE     1 
ATOM   5124  N NZ     . LYS B 1 291 ? 34.462  75.246  36.127 1.00 62.25  ? 291 LYS B NZ     1 
ATOM   5125  N N      . ASP B 1 292 ? 34.568  71.077  30.449 1.00 46.39  ? 292 ASP B N      1 
ATOM   5126  C CA     . ASP B 1 292 ? 34.958  70.337  29.275 1.00 46.99  ? 292 ASP B CA     1 
ATOM   5127  C C      . ASP B 1 292 ? 33.782  69.723  28.608 1.00 40.31  ? 292 ASP B C      1 
ATOM   5128  O O      . ASP B 1 292 ? 33.771  69.546  27.410 1.00 38.28  ? 292 ASP B O      1 
ATOM   5129  C CB     . ASP B 1 292 ? 35.907  69.247  29.694 1.00 56.89  ? 292 ASP B CB     1 
ATOM   5130  C CG     . ASP B 1 292 ? 37.038  69.760  30.560 1.00 64.69  ? 292 ASP B CG     1 
ATOM   5131  O OD1    . ASP B 1 292 ? 37.378  70.952  30.454 1.00 63.16  ? 292 ASP B OD1    1 
ATOM   5132  O OD2    . ASP B 1 292 ? 37.595  68.965  31.343 1.00 71.93  ? 292 ASP B OD2    1 
ATOM   5133  N N      . LEU B 1 293 ? 32.772  69.409  29.386 1.00 39.38  ? 293 LEU B N      1 
ATOM   5134  C CA     . LEU B 1 293 ? 31.584  68.791  28.844 1.00 39.96  ? 293 LEU B CA     1 
ATOM   5135  C C      . LEU B 1 293 ? 30.849  69.733  27.932 1.00 40.55  ? 293 LEU B C      1 
ATOM   5136  O O      . LEU B 1 293 ? 30.390  69.332  26.883 1.00 34.87  ? 293 LEU B O      1 
ATOM   5137  C CB     . LEU B 1 293 ? 30.668  68.304  29.960 1.00 33.81  ? 293 LEU B CB     1 
ATOM   5138  C CG     . LEU B 1 293 ? 30.732  66.863  30.445 1.00 35.11  ? 293 LEU B CG     1 
ATOM   5139  C CD1    . LEU B 1 293 ? 32.145  66.424  30.778 1.00 34.66  ? 293 LEU B CD1    1 
ATOM   5140  C CD2    . LEU B 1 293 ? 29.829  66.723  31.650 1.00 36.36  ? 293 LEU B CD2    1 
ATOM   5141  N N      . TYR B 1 294 ? 30.754  71.000  28.302 1.00 41.40  ? 294 TYR B N      1 
ATOM   5142  C CA     . TYR B 1 294 ? 30.100  71.984  27.449 1.00 36.92  ? 294 TYR B CA     1 
ATOM   5143  C C      . TYR B 1 294 ? 30.898  72.156  26.182 1.00 36.09  ? 294 TYR B C      1 
ATOM   5144  O O      . TYR B 1 294 ? 30.334  72.347  25.125 1.00 36.28  ? 294 TYR B O      1 
ATOM   5145  C CB     . TYR B 1 294 ? 29.982  73.319  28.147 1.00 33.46  ? 294 TYR B CB     1 
ATOM   5146  C CG     . TYR B 1 294 ? 28.860  73.488  29.136 1.00 34.38  ? 294 TYR B CG     1 
ATOM   5147  C CD1    . TYR B 1 294 ? 27.542  73.303  28.767 1.00 32.39  ? 294 TYR B CD1    1 
ATOM   5148  C CD2    . TYR B 1 294 ? 29.119  73.902  30.427 1.00 37.08  ? 294 TYR B CD2    1 
ATOM   5149  C CE1    . TYR B 1 294 ? 26.518  73.490  29.671 1.00 35.08  ? 294 TYR B CE1    1 
ATOM   5150  C CE2    . TYR B 1 294 ? 28.105  74.093  31.335 1.00 38.31  ? 294 TYR B CE2    1 
ATOM   5151  C CZ     . TYR B 1 294 ? 26.809  73.885  30.950 1.00 38.77  ? 294 TYR B CZ     1 
ATOM   5152  O OH     . TYR B 1 294 ? 25.806  74.074  31.859 1.00 39.87  ? 294 TYR B OH     1 
ATOM   5153  N N      . ALA B 1 295 ? 32.216  72.082  26.279 1.00 35.99  ? 295 ALA B N      1 
ATOM   5154  C CA     . ALA B 1 295 ? 33.089  72.245  25.126 1.00 33.14  ? 295 ALA B CA     1 
ATOM   5155  C C      . ALA B 1 295 ? 33.244  70.996  24.340 1.00 35.96  ? 295 ALA B C      1 
ATOM   5156  O O      . ALA B 1 295 ? 33.913  71.014  23.329 1.00 38.64  ? 295 ALA B O      1 
ATOM   5157  C CB     . ALA B 1 295 ? 34.440  72.706  25.568 1.00 33.54  ? 295 ALA B CB     1 
ATOM   5158  N N      . ASN B 1 296 ? 32.645  69.904  24.779 1.00 34.93  ? 296 ASN B N      1 
ATOM   5159  C CA     . ASN B 1 296 ? 32.690  68.678  24.020 1.00 31.14  ? 296 ASN B CA     1 
ATOM   5160  C C      . ASN B 1 296 ? 31.353  67.939  23.962 1.00 33.32  ? 296 ASN B C      1 
ATOM   5161  O O      . ASN B 1 296 ? 31.295  66.785  24.301 1.00 37.61  ? 296 ASN B O      1 
ATOM   5162  C CB     . ASN B 1 296 ? 33.736  67.765  24.609 1.00 30.54  ? 296 ASN B CB     1 
ATOM   5163  C CG     . ASN B 1 296 ? 35.131  68.346  24.564 1.00 35.14  ? 296 ASN B CG     1 
ATOM   5164  O OD1    . ASN B 1 296 ? 35.826  68.382  25.574 1.00 38.03  ? 296 ASN B OD1    1 
ATOM   5165  N ND2    . ASN B 1 296 ? 35.551  68.798  23.396 1.00 38.38  ? 296 ASN B ND2    1 
ATOM   5166  N N      . THR B 1 297 ? 30.282  68.580  23.488 1.00 37.50  ? 297 THR B N      1 
ATOM   5167  C CA     . THR B 1 297 ? 28.952  67.953  23.377 1.00 33.44  ? 297 THR B CA     1 
ATOM   5168  C C      . THR B 1 297 ? 28.708  67.276  22.057 1.00 35.48  ? 297 THR B C      1 
ATOM   5169  O O      . THR B 1 297 ? 28.157  67.875  21.156 1.00 35.65  ? 297 THR B O      1 
ATOM   5170  C CB     . THR B 1 297 ? 27.811  68.965  23.556 1.00 34.20  ? 297 THR B CB     1 
ATOM   5171  O OG1    . THR B 1 297 ? 28.093  69.824  24.664 1.00 37.81  ? 297 THR B OG1    1 
ATOM   5172  C CG2    . THR B 1 297 ? 26.478  68.269  23.790 1.00 26.77  ? 297 THR B CG2    1 
ATOM   5173  N N      . VAL B 1 298 ? 29.091  66.014  21.935 1.00 38.30  ? 298 VAL B N      1 
ATOM   5174  C CA     . VAL B 1 298 ? 28.952  65.283  20.681 1.00 35.93  ? 298 VAL B CA     1 
ATOM   5175  C C      . VAL B 1 298 ? 27.526  64.895  20.443 1.00 37.23  ? 298 VAL B C      1 
ATOM   5176  O O      . VAL B 1 298 ? 26.855  64.467  21.352 1.00 36.16  ? 298 VAL B O      1 
ATOM   5177  C CB     . VAL B 1 298 ? 29.838  64.038  20.685 1.00 27.31  ? 298 VAL B CB     1 
ATOM   5178  C CG1    . VAL B 1 298 ? 29.657  63.225  19.420 1.00 35.77  ? 298 VAL B CG1    1 
ATOM   5179  C CG2    . VAL B 1 298 ? 31.288  64.443  20.835 1.00 29.54  ? 298 VAL B CG2    1 
ATOM   5180  N N      . LEU B 1 299 ? 27.043  65.064  19.225 1.00 36.00  ? 299 LEU B N      1 
ATOM   5181  C CA     . LEU B 1 299 ? 25.704  64.646  18.891 1.00 35.61  ? 299 LEU B CA     1 
ATOM   5182  C C      . LEU B 1 299 ? 25.823  63.358  18.103 1.00 37.68  ? 299 LEU B C      1 
ATOM   5183  O O      . LEU B 1 299 ? 26.373  63.349  17.017 1.00 40.96  ? 299 LEU B O      1 
ATOM   5184  C CB     . LEU B 1 299 ? 24.968  65.726  18.095 1.00 30.37  ? 299 LEU B CB     1 
ATOM   5185  C CG     . LEU B 1 299 ? 24.541  67.016  18.783 1.00 28.82  ? 299 LEU B CG     1 
ATOM   5186  C CD1    . LEU B 1 299 ? 23.695  67.830  17.830 1.00 23.92  ? 299 LEU B CD1    1 
ATOM   5187  C CD2    . LEU B 1 299 ? 23.739  66.698  20.024 1.00 45.21  ? 299 LEU B CD2    1 
ATOM   5188  N N      . SER B 1 300 ? 25.356  62.257  18.670 1.00 35.56  ? 300 SER B N      1 
ATOM   5189  C CA     . SER B 1 300 ? 25.386  60.986  17.977 1.00 35.76  ? 300 SER B CA     1 
ATOM   5190  C C      . SER B 1 300 ? 24.033  60.408  17.992 1.00 35.53  ? 300 SER B C      1 
ATOM   5191  O O      . SER B 1 300 ? 23.292  60.585  18.928 1.00 35.83  ? 300 SER B O      1 
ATOM   5192  C CB     . SER B 1 300 ? 26.335  60.005  18.608 1.00 41.35  ? 300 SER B CB     1 
ATOM   5193  O OG     . SER B 1 300 ? 27.656  60.283  18.200 1.00 49.02  ? 300 SER B OG     1 
ATOM   5194  N N      . GLY B 1 301 ? 23.700  59.698  16.941 1.00 35.26  ? 301 GLY B N      1 
ATOM   5195  C CA     . GLY B 1 301 ? 22.379  59.170  16.826 1.00 36.41  ? 301 GLY B CA     1 
ATOM   5196  C C      . GLY B 1 301 ? 21.924  59.535  15.451 1.00 38.92  ? 301 GLY B C      1 
ATOM   5197  O O      . GLY B 1 301 ? 22.707  60.004  14.652 1.00 35.50  ? 301 GLY B O      1 
ATOM   5198  N N      . GLY B 1 302 ? 20.653  59.331  15.178 1.00 38.37  ? 302 GLY B N      1 
ATOM   5199  C CA     . GLY B 1 302 ? 20.143  59.588  13.866 1.00 36.81  ? 302 GLY B CA     1 
ATOM   5200  C C      . GLY B 1 302 ? 19.062  60.611  13.920 1.00 41.72  ? 302 GLY B C      1 
ATOM   5201  O O      . GLY B 1 302 ? 18.745  61.207  12.915 1.00 48.73  ? 302 GLY B O      1 
ATOM   5202  N N      . THR B 1 303 ? 18.486  60.836  15.082 1.00 34.74  ? 303 THR B N      1 
ATOM   5203  C CA     . THR B 1 303 ? 17.513  61.888  15.187 1.00 38.84  ? 303 THR B CA     1 
ATOM   5204  C C      . THR B 1 303 ? 18.312  63.134  15.420 1.00 37.82  ? 303 THR B C      1 
ATOM   5205  O O      . THR B 1 303 ? 17.767  64.196  15.675 1.00 37.20  ? 303 THR B O      1 
ATOM   5206  C CB     . THR B 1 303 ? 16.521  61.614  16.310 1.00 36.26  ? 303 THR B CB     1 
ATOM   5207  O OG1    . THR B 1 303 ? 15.996  60.294  16.159 1.00 39.83  ? 303 THR B OG1    1 
ATOM   5208  C CG2    . THR B 1 303 ? 15.368  62.588  16.275 1.00 37.01  ? 303 THR B CG2    1 
ATOM   5209  N N      . THR B 1 304 ? 19.622  63.016  15.323 1.00 33.33  ? 304 THR B N      1 
ATOM   5210  C CA     . THR B 1 304 ? 20.490  64.137  15.530 1.00 31.28  ? 304 THR B CA     1 
ATOM   5211  C C      . THR B 1 304 ? 20.963  64.515  14.187 1.00 34.97  ? 304 THR B C      1 
ATOM   5212  O O      . THR B 1 304 ? 21.773  65.400  14.058 1.00 35.36  ? 304 THR B O      1 
ATOM   5213  C CB     . THR B 1 304 ? 21.719  63.716  16.289 1.00 32.47  ? 304 THR B CB     1 
ATOM   5214  O OG1    . THR B 1 304 ? 22.566  62.957  15.424 1.00 30.86  ? 304 THR B OG1    1 
ATOM   5215  C CG2    . THR B 1 304 ? 21.339  62.883  17.482 1.00 37.79  ? 304 THR B CG2    1 
ATOM   5216  N N      . MET B 1 305 ? 20.429  63.876  13.163 1.00 42.24  ? 305 MET B N      1 
ATOM   5217  C CA     . MET B 1 305 ? 20.892  64.111  11.807 1.00 43.14  ? 305 MET B CA     1 
ATOM   5218  C C      . MET B 1 305 ? 20.077  65.170  11.115 1.00 45.86  ? 305 MET B C      1 
ATOM   5219  O O      . MET B 1 305 ? 20.351  65.532  9.984  1.00 47.35  ? 305 MET B O      1 
ATOM   5220  C CB     . MET B 1 305 ? 20.868  62.811  11.001 1.00 30.87  ? 305 MET B CB     1 
ATOM   5221  C CG     . MET B 1 305 ? 21.913  61.801  11.400 1.00 38.54  ? 305 MET B CG     1 
ATOM   5222  S SD     . MET B 1 305 ? 23.238  61.808  10.196 1.00 35.86  ? 305 MET B SD     1 
ATOM   5223  C CE     . MET B 1 305 ? 22.328  61.393  8.721  1.00 47.75  ? 305 MET B CE     1 
ATOM   5224  N N      . TYR B 1 306 ? 19.043  65.638  11.779 1.00 39.29  ? 306 TYR B N      1 
ATOM   5225  C CA     . TYR B 1 306 ? 18.221  66.651  11.198 1.00 39.41  ? 306 TYR B CA     1 
ATOM   5226  C C      . TYR B 1 306 ? 19.118  67.816  10.929 1.00 43.28  ? 306 TYR B C      1 
ATOM   5227  O O      . TYR B 1 306 ? 19.976  68.132  11.726 1.00 42.37  ? 306 TYR B O      1 
ATOM   5228  C CB     . TYR B 1 306 ? 17.105  67.040  12.145 1.00 34.88  ? 306 TYR B CB     1 
ATOM   5229  C CG     . TYR B 1 306 ? 16.050  65.999  12.305 1.00 38.10  ? 306 TYR B CG     1 
ATOM   5230  C CD1    . TYR B 1 306 ? 15.348  65.526  11.215 1.00 49.69  ? 306 TYR B CD1    1 
ATOM   5231  C CD2    . TYR B 1 306 ? 15.740  65.501  13.547 1.00 43.51  ? 306 TYR B CD2    1 
ATOM   5232  C CE1    . TYR B 1 306 ? 14.369  64.570  11.364 1.00 55.64  ? 306 TYR B CE1    1 
ATOM   5233  C CE2    . TYR B 1 306 ? 14.764  64.548  13.706 1.00 49.91  ? 306 TYR B CE2    1 
ATOM   5234  C CZ     . TYR B 1 306 ? 14.086  64.089  12.612 1.00 48.86  ? 306 TYR B CZ     1 
ATOM   5235  O OH     . TYR B 1 306 ? 13.123  63.140  12.792 1.00 51.50  ? 306 TYR B OH     1 
ATOM   5236  N N      . PRO B 1 307 ? 18.949  68.462  9.776  1.00 48.44  ? 307 PRO B N      1 
ATOM   5237  C CA     . PRO B 1 307 ? 19.718  69.659  9.498  1.00 38.75  ? 307 PRO B CA     1 
ATOM   5238  C C      . PRO B 1 307 ? 19.370  70.746  10.467 1.00 32.86  ? 307 PRO B C      1 
ATOM   5239  O O      . PRO B 1 307 ? 18.219  71.049  10.622 1.00 32.46  ? 307 PRO B O      1 
ATOM   5240  C CB     . PRO B 1 307 ? 19.209  70.055  8.131  1.00 35.26  ? 307 PRO B CB     1 
ATOM   5241  C CG     . PRO B 1 307 ? 18.826  68.780  7.486  1.00 39.21  ? 307 PRO B CG     1 
ATOM   5242  C CD     . PRO B 1 307 ? 18.170  68.038  8.599  1.00 51.01  ? 307 PRO B CD     1 
ATOM   5243  N N      . GLY B 1 308 ? 20.344  71.328  11.130 1.00 31.44  ? 308 GLY B N      1 
ATOM   5244  C CA     . GLY B 1 308 ? 20.081  72.434  12.022 1.00 35.61  ? 308 GLY B CA     1 
ATOM   5245  C C      . GLY B 1 308 ? 20.055  72.064  13.479 1.00 44.31  ? 308 GLY B C      1 
ATOM   5246  O O      . GLY B 1 308 ? 19.845  72.920  14.324 1.00 42.40  ? 308 GLY B O      1 
ATOM   5247  N N      . ILE B 1 309 ? 20.293  70.804  13.790 1.00 44.46  ? 309 ILE B N      1 
ATOM   5248  C CA     . ILE B 1 309 ? 20.259  70.352  15.161 1.00 33.65  ? 309 ILE B CA     1 
ATOM   5249  C C      . ILE B 1 309 ? 21.361  71.050  15.898 1.00 41.70  ? 309 ILE B C      1 
ATOM   5250  O O      . ILE B 1 309 ? 21.142  71.572  16.980 1.00 39.69  ? 309 ILE B O      1 
ATOM   5251  C CB     . ILE B 1 309 ? 20.382  68.816  15.244 1.00 28.38  ? 309 ILE B CB     1 
ATOM   5252  C CG1    . ILE B 1 309 ? 20.059  68.307  16.643 1.00 34.20  ? 309 ILE B CG1    1 
ATOM   5253  C CG2    . ILE B 1 309 ? 21.723  68.315  14.744 1.00 27.79  ? 309 ILE B CG2    1 
ATOM   5254  C CD1    . ILE B 1 309 ? 18.601  67.956  16.821 1.00 34.81  ? 309 ILE B CD1    1 
ATOM   5255  N N      . ALA B 1 310 ? 22.536  71.138  15.298 1.00 39.98  ? 310 ALA B N      1 
ATOM   5256  C CA     . ALA B 1 310 ? 23.680  71.685  15.992 1.00 32.40  ? 310 ALA B CA     1 
ATOM   5257  C C      . ALA B 1 310 ? 23.590  73.149  16.223 1.00 39.29  ? 310 ALA B C      1 
ATOM   5258  O O      . ALA B 1 310 ? 23.776  73.621  17.326 1.00 41.51  ? 310 ALA B O      1 
ATOM   5259  C CB     . ALA B 1 310 ? 24.907  71.380  15.193 1.00 26.34  ? 310 ALA B CB     1 
ATOM   5260  N N      . ASP B 1 311 ? 23.322  73.891  15.175 1.00 43.96  ? 311 ASP B N      1 
ATOM   5261  C CA     . ASP B 1 311 ? 23.288  75.317  15.300 1.00 39.49  ? 311 ASP B CA     1 
ATOM   5262  C C      . ASP B 1 311 ? 22.266  75.735  16.303 1.00 38.42  ? 311 ASP B C      1 
ATOM   5263  O O      . ASP B 1 311 ? 22.515  76.620  17.094 1.00 46.46  ? 311 ASP B O      1 
ATOM   5264  C CB     . ASP B 1 311 ? 23.009  75.941  13.953 1.00 50.18  ? 311 ASP B CB     1 
ATOM   5265  C CG     . ASP B 1 311 ? 24.197  75.865  13.018 1.00 58.51  ? 311 ASP B CG     1 
ATOM   5266  O OD1    . ASP B 1 311 ? 25.120  75.075  13.286 1.00 59.27  ? 311 ASP B OD1    1 
ATOM   5267  O OD2    . ASP B 1 311 ? 24.208  76.599  12.011 1.00 64.28  ? 311 ASP B OD2    1 
ATOM   5268  N N      . ARG B 1 312 ? 21.123  75.086  16.323 1.00 35.95  ? 312 ARG B N      1 
ATOM   5269  C CA     . ARG B 1 312 ? 20.121  75.414  17.317 1.00 33.54  ? 312 ARG B CA     1 
ATOM   5270  C C      . ARG B 1 312 ? 20.533  75.008  18.686 1.00 42.94  ? 312 ARG B C      1 
ATOM   5271  O O      . ARG B 1 312 ? 20.271  75.714  19.639 1.00 45.09  ? 312 ARG B O      1 
ATOM   5272  C CB     . ARG B 1 312 ? 18.785  74.798  17.022 1.00 30.45  ? 312 ARG B CB     1 
ATOM   5273  C CG     . ARG B 1 312 ? 17.744  75.165  18.050 1.00 32.63  ? 312 ARG B CG     1 
ATOM   5274  C CD     . ARG B 1 312 ? 16.356  74.922  17.536 1.00 33.76  ? 312 ARG B CD     1 
ATOM   5275  N NE     . ARG B 1 312 ? 15.359  75.366  18.488 1.00 31.46  ? 312 ARG B NE     1 
ATOM   5276  C CZ     . ARG B 1 312 ? 14.067  75.387  18.221 1.00 38.02  ? 312 ARG B CZ     1 
ATOM   5277  N NH1    . ARG B 1 312 ? 13.645  74.998  17.030 1.00 46.85  ? 312 ARG B NH1    1 
ATOM   5278  N NH2    . ARG B 1 312 ? 13.205  75.802  19.132 1.00 36.54  ? 312 ARG B NH2    1 
ATOM   5279  N N      . MET B 1 313 ? 21.205  73.885  18.833 1.00 45.01  ? 313 MET B N      1 
ATOM   5280  C CA     . MET B 1 313 ? 21.496  73.464  20.181 1.00 41.45  ? 313 MET B CA     1 
ATOM   5281  C C      . MET B 1 313 ? 22.477  74.394  20.803 1.00 38.04  ? 313 MET B C      1 
ATOM   5282  O O      . MET B 1 313 ? 22.380  74.696  21.962 1.00 41.68  ? 313 MET B O      1 
ATOM   5283  C CB     . MET B 1 313 ? 21.936  72.024  20.253 1.00 35.06  ? 313 MET B CB     1 
ATOM   5284  C CG     . MET B 1 313 ? 21.624  71.377  21.573 1.00 29.89  ? 313 MET B CG     1 
ATOM   5285  S SD     . MET B 1 313 ? 21.574  69.608  21.348 1.00 66.00  ? 313 MET B SD     1 
ATOM   5286  C CE     . MET B 1 313 ? 21.146  69.107  23.001 1.00 49.62  ? 313 MET B CE     1 
ATOM   5287  N N      . GLN B 1 314 ? 23.416  74.901  20.043 1.00 36.57  ? 314 GLN B N      1 
ATOM   5288  C CA     . GLN B 1 314 ? 24.297  75.876  20.626 1.00 38.09  ? 314 GLN B CA     1 
ATOM   5289  C C      . GLN B 1 314 ? 23.450  76.981  21.097 1.00 38.79  ? 314 GLN B C      1 
ATOM   5290  O O      . GLN B 1 314 ? 23.530  77.370  22.236 1.00 43.68  ? 314 GLN B O      1 
ATOM   5291  C CB     . GLN B 1 314 ? 25.266  76.462  19.621 1.00 38.40  ? 314 GLN B CB     1 
ATOM   5292  C CG     . GLN B 1 314 ? 26.379  75.538  19.191 1.00 35.92  ? 314 GLN B CG     1 
ATOM   5293  C CD     . GLN B 1 314 ? 27.703  76.253  19.162 1.00 48.09  ? 314 GLN B CD     1 
ATOM   5294  O OE1    . GLN B 1 314 ? 27.890  77.248  19.855 1.00 59.12  ? 314 GLN B OE1    1 
ATOM   5295  N NE2    . GLN B 1 314 ? 28.632  75.751  18.361 1.00 46.64  ? 314 GLN B NE2    1 
ATOM   5296  N N      . LYS B 1 315 ? 22.623  77.507  20.226 1.00 37.49  ? 315 LYS B N      1 
ATOM   5297  C CA     . LYS B 1 315 ? 21.833  78.662  20.586 1.00 41.35  ? 315 LYS B CA     1 
ATOM   5298  C C      . LYS B 1 315 ? 21.070  78.400  21.850 1.00 43.72  ? 315 LYS B C      1 
ATOM   5299  O O      . LYS B 1 315 ? 21.041  79.231  22.744 1.00 50.17  ? 315 LYS B O      1 
ATOM   5300  C CB     . LYS B 1 315 ? 20.861  78.987  19.470 1.00 39.40  ? 315 LYS B CB     1 
ATOM   5301  C CG     . LYS B 1 315 ? 19.938  80.156  19.750 1.00 42.99  ? 315 LYS B CG     1 
ATOM   5302  C CD     . LYS B 1 315 ? 18.764  80.163  18.791 1.00 41.32  ? 315 LYS B CD     1 
ATOM   5303  C CE     . LYS B 1 315 ? 17.984  81.459  18.896 1.00 56.65  ? 315 LYS B CE     1 
ATOM   5304  N NZ     . LYS B 1 315 ? 18.844  82.629  18.570 1.00 56.07  ? 315 LYS B NZ     1 
ATOM   5305  N N      . GLU B 1 316 ? 20.500  77.219  21.977 1.00 34.76  ? 316 GLU B N      1 
ATOM   5306  C CA     . GLU B 1 316 ? 19.671  76.932  23.130 1.00 38.04  ? 316 GLU B CA     1 
ATOM   5307  C C      . GLU B 1 316 ? 20.411  76.682  24.426 1.00 40.26  ? 316 GLU B C      1 
ATOM   5308  O O      . GLU B 1 316 ? 19.931  77.053  25.478 1.00 40.54  ? 316 GLU B O      1 
ATOM   5309  C CB     . GLU B 1 316 ? 18.759  75.775  22.805 1.00 40.68  ? 316 GLU B CB     1 
ATOM   5310  C CG     . GLU B 1 316 ? 17.794  76.025  21.657 1.00 42.16  ? 316 GLU B CG     1 
ATOM   5311  C CD     . GLU B 1 316 ? 16.479  76.653  22.082 1.00 48.07  ? 316 GLU B CD     1 
ATOM   5312  O OE1    . GLU B 1 316 ? 16.387  77.190  23.202 1.00 50.76  ? 316 GLU B OE1    1 
ATOM   5313  O OE2    . GLU B 1 316 ? 15.523  76.608  21.286 1.00 43.18  ? 316 GLU B OE2    1 
ATOM   5314  N N      . ILE B 1 317 ? 21.584  76.070  24.367 1.00 38.95  ? 317 ILE B N      1 
ATOM   5315  C CA     . ILE B 1 317 ? 22.370  75.778  25.561 1.00 35.24  ? 317 ILE B CA     1 
ATOM   5316  C C      . ILE B 1 317 ? 23.330  76.892  25.879 1.00 34.47  ? 317 ILE B C      1 
ATOM   5317  O O      . ILE B 1 317 ? 23.947  76.888  26.911 1.00 37.06  ? 317 ILE B O      1 
ATOM   5318  C CB     . ILE B 1 317 ? 23.105  74.437  25.443 1.00 35.80  ? 317 ILE B CB     1 
ATOM   5319  C CG1    . ILE B 1 317 ? 22.172  73.374  24.899 1.00 39.33  ? 317 ILE B CG1    1 
ATOM   5320  C CG2    . ILE B 1 317 ? 23.585  73.925  26.788 1.00 39.64  ? 317 ILE B CG2    1 
ATOM   5321  C CD1    . ILE B 1 317 ? 22.730  71.987  25.062 1.00 37.72  ? 317 ILE B CD1    1 
ATOM   5322  N N      . THR B 1 318 ? 23.424  77.895  25.035 1.00 36.37  ? 318 THR B N      1 
ATOM   5323  C CA     . THR B 1 318 ? 24.248  79.027  25.371 1.00 33.13  ? 318 THR B CA     1 
ATOM   5324  C C      . THR B 1 318 ? 23.311  79.951  26.098 1.00 38.59  ? 318 THR B C      1 
ATOM   5325  O O      . THR B 1 318 ? 23.724  80.935  26.690 1.00 41.21  ? 318 THR B O      1 
ATOM   5326  C CB     . THR B 1 318 ? 24.860  79.679  24.142 1.00 28.48  ? 318 THR B CB     1 
ATOM   5327  O OG1    . THR B 1 318 ? 25.493  78.680  23.347 1.00 37.78  ? 318 THR B OG1    1 
ATOM   5328  C CG2    . THR B 1 318 ? 25.922  80.676  24.536 1.00 26.01  ? 318 THR B CG2    1 
ATOM   5329  N N      . ALA B 1 319 ? 22.041  79.588  26.153 1.00 41.09  ? 319 ALA B N      1 
ATOM   5330  C CA     . ALA B 1 319 ? 21.044  80.440  26.794 1.00 41.11  ? 319 ALA B CA     1 
ATOM   5331  C C      . ALA B 1 319 ? 20.608  79.919  28.113 1.00 38.89  ? 319 ALA B C      1 
ATOM   5332  O O      . ALA B 1 319 ? 19.982  80.622  28.884 1.00 34.46  ? 319 ALA B O      1 
ATOM   5333  C CB     . ALA B 1 319 ? 19.844  80.561  25.910 1.00 39.13  ? 319 ALA B CB     1 
ATOM   5334  N N      . LEU B 1 320 ? 20.991  78.692  28.401 1.00 41.01  ? 320 LEU B N      1 
ATOM   5335  C CA     . LEU B 1 320 ? 20.676  78.083  29.669 1.00 42.19  ? 320 LEU B CA     1 
ATOM   5336  C C      . LEU B 1 320 ? 21.949  78.016  30.456 1.00 33.99  ? 320 LEU B C      1 
ATOM   5337  O O      . LEU B 1 320 ? 21.962  77.500  31.547 1.00 30.50  ? 320 LEU B O      1 
ATOM   5338  C CB     . LEU B 1 320 ? 20.192  76.656  29.421 1.00 36.30  ? 320 LEU B CB     1 
ATOM   5339  C CG     . LEU B 1 320 ? 18.851  76.342  28.787 1.00 34.73  ? 320 LEU B CG     1 
ATOM   5340  C CD1    . LEU B 1 320 ? 18.941  74.947  28.207 1.00 36.66  ? 320 LEU B CD1    1 
ATOM   5341  C CD2    . LEU B 1 320 ? 17.754  76.413  29.833 1.00 34.53  ? 320 LEU B CD2    1 
ATOM   5342  N N      . ALA B 1 321 ? 23.024  78.569  29.942 1.00 33.23  ? 321 ALA B N      1 
ATOM   5343  C CA     . ALA B 1 321 ? 24.302  78.415  30.585 1.00 32.96  ? 321 ALA B CA     1 
ATOM   5344  C C      . ALA B 1 321 ? 25.060  79.701  30.821 1.00 44.70  ? 321 ALA B C      1 
ATOM   5345  O O      . ALA B 1 321 ? 24.634  80.755  30.363 1.00 51.38  ? 321 ALA B O      1 
ATOM   5346  C CB     . ALA B 1 321 ? 25.125  77.497  29.739 1.00 34.72  ? 321 ALA B CB     1 
ATOM   5347  N N      . PRO B 1 322 ? 26.190  79.633  31.598 1.00 50.96  ? 322 PRO B N      1 
ATOM   5348  C CA     . PRO B 1 322 ? 26.989  80.841  31.798 1.00 50.78  ? 322 PRO B CA     1 
ATOM   5349  C C      . PRO B 1 322 ? 27.462  81.558  30.569 1.00 54.18  ? 322 PRO B C      1 
ATOM   5350  O O      . PRO B 1 322 ? 27.795  80.915  29.584 1.00 58.17  ? 322 PRO B O      1 
ATOM   5351  C CB     . PRO B 1 322 ? 28.199  80.314  32.523 1.00 48.76  ? 322 PRO B CB     1 
ATOM   5352  C CG     . PRO B 1 322 ? 27.637  79.297  33.419 1.00 50.78  ? 322 PRO B CG     1 
ATOM   5353  C CD     . PRO B 1 322 ? 26.666  78.581  32.540 1.00 54.58  ? 322 PRO B CD     1 
ATOM   5354  N N      . SER B 1 323 ? 27.553  82.879  30.639 1.00 51.42  ? 323 SER B N      1 
ATOM   5355  C CA     . SER B 1 323 ? 27.915  83.672  29.477 1.00 55.80  ? 323 SER B CA     1 
ATOM   5356  C C      . SER B 1 323 ? 29.371  83.654  29.145 1.00 54.10  ? 323 SER B C      1 
ATOM   5357  O O      . SER B 1 323 ? 29.787  84.216  28.146 1.00 62.83  ? 323 SER B O      1 
ATOM   5358  C CB     . SER B 1 323 ? 27.525  85.104  29.721 1.00 60.82  ? 323 SER B CB     1 
ATOM   5359  O OG     . SER B 1 323 ? 26.228  85.175  30.282 1.00 76.08  ? 323 SER B OG     1 
ATOM   5360  N N      . THR B 1 324 ? 30.163  82.995  29.959 1.00 47.85  ? 324 THR B N      1 
ATOM   5361  C CA     . THR B 1 324 ? 31.562  82.904  29.656 1.00 52.22  ? 324 THR B CA     1 
ATOM   5362  C C      . THR B 1 324 ? 31.893  81.535  29.143 1.00 62.84  ? 324 THR B C      1 
ATOM   5363  O O      . THR B 1 324 ? 33.014  81.286  28.718 1.00 75.99  ? 324 THR B O      1 
ATOM   5364  C CB     . THR B 1 324 ? 32.389  83.164  30.901 1.00 62.65  ? 324 THR B CB     1 
ATOM   5365  O OG1    . THR B 1 324 ? 33.780  83.010  30.597 1.00 74.05  ? 324 THR B OG1    1 
ATOM   5366  C CG2    . THR B 1 324 ? 32.003  82.195  32.009 1.00 62.07  ? 324 THR B CG2    1 
ATOM   5367  N N      . MET B 1 325 ? 30.931  80.631  29.152 1.00 53.72  ? 325 MET B N      1 
ATOM   5368  C CA     . MET B 1 325 ? 31.239  79.267  28.778 1.00 45.37  ? 325 MET B CA     1 
ATOM   5369  C C      . MET B 1 325 ? 31.516  79.044  27.306 1.00 48.37  ? 325 MET B C      1 
ATOM   5370  O O      . MET B 1 325 ? 30.967  79.726  26.460 1.00 55.99  ? 325 MET B O      1 
ATOM   5371  C CB     . MET B 1 325 ? 30.122  78.368  29.252 1.00 45.22  ? 325 MET B CB     1 
ATOM   5372  C CG     . MET B 1 325 ? 30.497  76.905  29.299 1.00 55.69  ? 325 MET B CG     1 
ATOM   5373  S SD     . MET B 1 325 ? 31.878  76.606  30.404 1.00 49.57  ? 325 MET B SD     1 
ATOM   5374  C CE     . MET B 1 325 ? 31.099  77.005  31.961 1.00 62.18  ? 325 MET B CE     1 
ATOM   5375  N N      . LYS B 1 326 ? 32.355  78.069  26.987 1.00 43.92  ? 326 LYS B N      1 
ATOM   5376  C CA     . LYS B 1 326 ? 32.620  77.740  25.609 1.00 44.63  ? 326 LYS B CA     1 
ATOM   5377  C C      . LYS B 1 326 ? 31.717  76.624  25.232 1.00 40.81  ? 326 LYS B C      1 
ATOM   5378  O O      . LYS B 1 326 ? 32.120  75.485  25.272 1.00 43.84  ? 326 LYS B O      1 
ATOM   5379  C CB     . LYS B 1 326 ? 34.045  77.235  25.443 1.00 43.95  ? 326 LYS B CB     1 
ATOM   5380  C CG     . LYS B 1 326 ? 34.513  77.199  23.995 1.00 47.05  ? 326 LYS B CG     1 
ATOM   5381  C CD     . LYS B 1 326 ? 35.567  76.132  23.772 1.00 41.69  ? 326 LYS B CD     1 
ATOM   5382  C CE     . LYS B 1 326 ? 36.854  76.451  24.509 1.00 45.98  ? 326 LYS B CE     1 
ATOM   5383  N NZ     . LYS B 1 326 ? 37.655  77.492  23.811 1.00 53.91  ? 326 LYS B NZ     1 
ATOM   5384  N N      . ILE B 1 327 ? 30.495  76.918  24.843 1.00 37.20  ? 327 ILE B N      1 
ATOM   5385  C CA     . ILE B 1 327 ? 29.618  75.866  24.410 1.00 40.72  ? 327 ILE B CA     1 
ATOM   5386  C C      . ILE B 1 327 ? 29.943  75.444  23.004 1.00 42.12  ? 327 ILE B C      1 
ATOM   5387  O O      . ILE B 1 327 ? 29.931  76.266  22.115 1.00 45.67  ? 327 ILE B O      1 
ATOM   5388  C CB     . ILE B 1 327 ? 28.159  76.291  24.480 1.00 38.28  ? 327 ILE B CB     1 
ATOM   5389  C CG1    . ILE B 1 327 ? 27.928  77.182  25.690 1.00 41.45  ? 327 ILE B CG1    1 
ATOM   5390  C CG2    . ILE B 1 327 ? 27.252  75.076  24.534 1.00 31.34  ? 327 ILE B CG2    1 
ATOM   5391  C CD1    . ILE B 1 327 ? 27.620  76.416  26.950 1.00 40.92  ? 327 ILE B CD1    1 
ATOM   5392  N N      . LYS B 1 328 ? 30.217  74.163  22.787 1.00 42.91  ? 328 LYS B N      1 
ATOM   5393  C CA     . LYS B 1 328 ? 30.493  73.646  21.452 1.00 40.31  ? 328 LYS B CA     1 
ATOM   5394  C C      . LYS B 1 328 ? 29.763  72.351  21.222 1.00 36.67  ? 328 LYS B C      1 
ATOM   5395  O O      . LYS B 1 328 ? 29.982  71.384  21.923 1.00 33.73  ? 328 LYS B O      1 
ATOM   5396  C CB     . LYS B 1 328 ? 31.984  73.457  21.244 1.00 35.19  ? 328 LYS B CB     1 
ATOM   5397  C CG     . LYS B 1 328 ? 32.415  73.093  19.840 1.00 33.67  ? 328 LYS B CG     1 
ATOM   5398  C CD     . LYS B 1 328 ? 33.930  73.086  19.773 1.00 35.21  ? 328 LYS B CD     1 
ATOM   5399  C CE     . LYS B 1 328 ? 34.434  72.809  18.371 1.00 40.64  ? 328 LYS B CE     1 
ATOM   5400  N NZ     . LYS B 1 328 ? 35.908  72.997  18.303 1.00 43.93  ? 328 LYS B NZ     1 
ATOM   5401  N N      . ILE B 1 329 ? 28.850  72.353  20.269 1.00 36.81  ? 329 ILE B N      1 
ATOM   5402  C CA     . ILE B 1 329 ? 28.100  71.164  19.950 1.00 38.71  ? 329 ILE B CA     1 
ATOM   5403  C C      . ILE B 1 329 ? 28.777  70.572  18.749 1.00 36.23  ? 329 ILE B C      1 
ATOM   5404  O O      . ILE B 1 329 ? 28.981  71.247  17.749 1.00 30.57  ? 329 ILE B O      1 
ATOM   5405  C CB     . ILE B 1 329 ? 26.622  71.465  19.703 1.00 34.32  ? 329 ILE B CB     1 
ATOM   5406  C CG1    . ILE B 1 329 ? 25.839  71.476  21.009 1.00 39.72  ? 329 ILE B CG1    1 
ATOM   5407  C CG2    . ILE B 1 329 ? 26.008  70.406  18.821 1.00 35.82  ? 329 ILE B CG2    1 
ATOM   5408  C CD1    . ILE B 1 329 ? 26.024  72.719  21.843 1.00 42.73  ? 329 ILE B CD1    1 
ATOM   5409  N N      . ILE B 1 330 ? 29.195  69.326  18.863 1.00 37.46  ? 330 ILE B N      1 
ATOM   5410  C CA     . ILE B 1 330 ? 29.966  68.714  17.807 1.00 35.62  ? 330 ILE B CA     1 
ATOM   5411  C C      . ILE B 1 330 ? 29.172  67.636  17.173 1.00 36.95  ? 330 ILE B C      1 
ATOM   5412  O O      . ILE B 1 330 ? 28.955  66.603  17.752 1.00 39.18  ? 330 ILE B O      1 
ATOM   5413  C CB     . ILE B 1 330 ? 31.218  68.059  18.390 1.00 39.09  ? 330 ILE B CB     1 
ATOM   5414  C CG1    . ILE B 1 330 ? 31.893  69.020  19.357 1.00 37.55  ? 330 ILE B CG1    1 
ATOM   5415  C CG2    . ILE B 1 330 ? 32.168  67.639  17.285 1.00 41.21  ? 330 ILE B CG2    1 
ATOM   5416  C CD1    . ILE B 1 330 ? 32.939  68.370  20.214 1.00 34.92  ? 330 ILE B CD1    1 
ATOM   5417  N N      . ALA B 1 331 ? 28.796  67.846  15.935 1.00 42.39  ? 331 ALA B N      1 
ATOM   5418  C CA     . ALA B 1 331 ? 28.025  66.871  15.226 1.00 45.24  ? 331 ALA B CA     1 
ATOM   5419  C C      . ALA B 1 331 ? 28.836  66.305  14.100 1.00 42.75  ? 331 ALA B C      1 
ATOM   5420  O O      . ALA B 1 331 ? 29.053  66.963  13.099 1.00 39.25  ? 331 ALA B O      1 
ATOM   5421  C CB     . ALA B 1 331 ? 26.795  67.527  14.679 1.00 37.82  ? 331 ALA B CB     1 
ATOM   5422  N N      . PRO B 1 332 ? 29.303  65.038  14.256 1.00 47.29  ? 332 PRO B N      1 
ATOM   5423  C CA     . PRO B 1 332 ? 30.043  64.517  13.128 1.00 44.01  ? 332 PRO B CA     1 
ATOM   5424  C C      . PRO B 1 332 ? 29.141  64.284  11.960 1.00 43.27  ? 332 PRO B C      1 
ATOM   5425  O O      . PRO B 1 332 ? 27.957  64.122  12.122 1.00 40.79  ? 332 PRO B O      1 
ATOM   5426  C CB     . PRO B 1 332 ? 30.558  63.180  13.654 1.00 41.75  ? 332 PRO B CB     1 
ATOM   5427  C CG     . PRO B 1 332 ? 30.545  63.288  15.127 1.00 47.12  ? 332 PRO B CG     1 
ATOM   5428  C CD     . PRO B 1 332 ? 29.291  64.048  15.359 1.00 52.07  ? 332 PRO B CD     1 
ATOM   5429  N N      . PRO B 1 333 ? 29.709  64.222  10.740 1.00 38.99  ? 333 PRO B N      1 
ATOM   5430  C CA     . PRO B 1 333 ? 28.769  64.073  9.649  1.00 31.79  ? 333 PRO B CA     1 
ATOM   5431  C C      . PRO B 1 333 ? 28.169  62.701  9.576  1.00 41.64  ? 333 PRO B C      1 
ATOM   5432  O O      . PRO B 1 333 ? 27.068  62.553  9.070  1.00 44.88  ? 333 PRO B O      1 
ATOM   5433  C CB     . PRO B 1 333 ? 29.657  64.242  8.435  1.00 31.17  ? 333 PRO B CB     1 
ATOM   5434  C CG     . PRO B 1 333 ? 30.881  64.934  8.901  1.00 37.93  ? 333 PRO B CG     1 
ATOM   5435  C CD     . PRO B 1 333 ? 31.091  64.296  10.217 1.00 39.39  ? 333 PRO B CD     1 
ATOM   5436  N N      . GLU B 1 334 ? 28.868  61.704  10.087 1.00 48.80  ? 334 GLU B N      1 
ATOM   5437  C CA     . GLU B 1 334 ? 28.416  60.321  10.012 1.00 41.84  ? 334 GLU B CA     1 
ATOM   5438  C C      . GLU B 1 334 ? 27.806  59.872  11.283 1.00 48.69  ? 334 GLU B C      1 
ATOM   5439  O O      . GLU B 1 334 ? 27.945  58.726  11.645 1.00 55.89  ? 334 GLU B O      1 
ATOM   5440  C CB     . GLU B 1 334 ? 29.629  59.438  9.770  1.00 36.28  ? 334 GLU B CB     1 
ATOM   5441  C CG     . GLU B 1 334 ? 30.904  59.949  10.410 1.00 45.79  ? 334 GLU B CG     1 
ATOM   5442  C CD     . GLU B 1 334 ? 31.155  59.352  11.776 1.00 63.86  ? 334 GLU B CD     1 
ATOM   5443  O OE1    . GLU B 1 334 ? 30.829  58.167  11.971 1.00 62.04  ? 334 GLU B OE1    1 
ATOM   5444  O OE2    . GLU B 1 334 ? 31.696  60.057  12.649 1.00 69.45  ? 334 GLU B OE2    1 
ATOM   5445  N N      . ARG B 1 335 ? 27.134  60.758  11.986 1.00 49.22  ? 335 ARG B N      1 
ATOM   5446  C CA     . ARG B 1 335 ? 26.636  60.415  13.299 1.00 40.57  ? 335 ARG B CA     1 
ATOM   5447  C C      . ARG B 1 335 ? 25.642  59.295  13.354 1.00 41.21  ? 335 ARG B C      1 
ATOM   5448  O O      . ARG B 1 335 ? 25.414  58.730  14.404 1.00 40.30  ? 335 ARG B O      1 
ATOM   5449  C CB     . ARG B 1 335 ? 26.126  61.664  14.021 1.00 38.30  ? 335 ARG B CB     1 
ATOM   5450  C CG     . ARG B 1 335 ? 25.282  62.612  13.200 1.00 42.24  ? 335 ARG B CG     1 
ATOM   5451  C CD     . ARG B 1 335 ? 25.362  64.007  13.787 1.00 29.20  ? 335 ARG B CD     1 
ATOM   5452  N NE     . ARG B 1 335 ? 24.363  64.900  13.225 1.00 33.64  ? 335 ARG B NE     1 
ATOM   5453  C CZ     . ARG B 1 335 ? 24.513  65.595  12.105 1.00 44.70  ? 335 ARG B CZ     1 
ATOM   5454  N NH1    . ARG B 1 335 ? 25.626  65.501  11.405 1.00 48.42  ? 335 ARG B NH1    1 
ATOM   5455  N NH2    . ARG B 1 335 ? 23.542  66.384  11.674 1.00 42.03  ? 335 ARG B NH2    1 
ATOM   5456  N N      . LYS B 1 336 ? 25.050  58.935  12.237 1.00 39.57  ? 336 LYS B N      1 
ATOM   5457  C CA     . LYS B 1 336 ? 24.014  57.932  12.303 1.00 43.25  ? 336 LYS B CA     1 
ATOM   5458  C C      . LYS B 1 336 ? 24.654  56.645  12.702 1.00 50.32  ? 336 LYS B C      1 
ATOM   5459  O O      . LYS B 1 336 ? 24.072  55.849  13.430 1.00 45.01  ? 336 LYS B O      1 
ATOM   5460  C CB     . LYS B 1 336 ? 23.327  57.800  10.953 1.00 38.27  ? 336 LYS B CB     1 
ATOM   5461  C CG     . LYS B 1 336 ? 22.026  57.022  10.966 1.00 50.72  ? 336 LYS B CG     1 
ATOM   5462  C CD     . LYS B 1 336 ? 21.376  57.044  9.594  1.00 45.51  ? 336 LYS B CD     1 
ATOM   5463  C CE     . LYS B 1 336 ? 20.045  56.307  9.588  1.00 52.91  ? 336 LYS B CE     1 
ATOM   5464  N NZ     . LYS B 1 336 ? 20.177  54.848  9.853  1.00 48.32  ? 336 LYS B NZ     1 
ATOM   5465  N N      . TYR B 1 337 ? 25.891  56.452  12.286 1.00 52.90  ? 337 TYR B N      1 
ATOM   5466  C CA     . TYR B 1 337 ? 26.565  55.195  12.546 1.00 46.90  ? 337 TYR B CA     1 
ATOM   5467  C C      . TYR B 1 337 ? 27.779  55.357  13.416 1.00 39.76  ? 337 TYR B C      1 
ATOM   5468  O O      . TYR B 1 337 ? 28.618  54.489  13.447 1.00 40.85  ? 337 TYR B O      1 
ATOM   5469  C CB     . TYR B 1 337 ? 26.950  54.555  11.215 1.00 41.54  ? 337 TYR B CB     1 
ATOM   5470  C CG     . TYR B 1 337 ? 25.773  54.244  10.329 1.00 40.45  ? 337 TYR B CG     1 
ATOM   5471  C CD1    . TYR B 1 337 ? 24.618  53.689  10.848 1.00 39.98  ? 337 TYR B CD1    1 
ATOM   5472  C CD2    . TYR B 1 337 ? 25.823  54.488  8.970  1.00 48.42  ? 337 TYR B CD2    1 
ATOM   5473  C CE1    . TYR B 1 337 ? 23.540  53.400  10.043 1.00 42.37  ? 337 TYR B CE1    1 
ATOM   5474  C CE2    . TYR B 1 337 ? 24.749  54.199  8.156  1.00 52.92  ? 337 TYR B CE2    1 
ATOM   5475  C CZ     . TYR B 1 337 ? 23.612  53.653  8.700  1.00 51.91  ? 337 TYR B CZ     1 
ATOM   5476  O OH     . TYR B 1 337 ? 22.541  53.365  7.893  1.00 46.87  ? 337 TYR B OH     1 
ATOM   5477  N N      . SER B 1 338 ? 27.846  56.449  14.154 1.00 35.84  ? 338 SER B N      1 
ATOM   5478  C CA     . SER B 1 338 ? 29.002  56.745  14.983 1.00 46.49  ? 338 SER B CA     1 
ATOM   5479  C C      . SER B 1 338 ? 29.234  55.784  16.094 1.00 43.00  ? 338 SER B C      1 
ATOM   5480  O O      . SER B 1 338 ? 30.357  55.532  16.464 1.00 37.55  ? 338 SER B O      1 
ATOM   5481  C CB     . SER B 1 338 ? 28.810  58.106  15.610 1.00 47.25  ? 338 SER B CB     1 
ATOM   5482  O OG     . SER B 1 338 ? 27.605  58.141  16.336 1.00 49.77  ? 338 SER B OG     1 
ATOM   5483  N N      . VAL B 1 339 ? 28.177  55.280  16.681 1.00 38.22  ? 339 VAL B N      1 
ATOM   5484  C CA     . VAL B 1 339 ? 28.340  54.391  17.773 1.00 31.65  ? 339 VAL B CA     1 
ATOM   5485  C C      . VAL B 1 339 ? 29.163  53.276  17.228 1.00 36.46  ? 339 VAL B C      1 
ATOM   5486  O O      . VAL B 1 339 ? 30.153  52.886  17.809 1.00 44.70  ? 339 VAL B O      1 
ATOM   5487  C CB     . VAL B 1 339 ? 26.993  53.861  18.205 1.00 31.00  ? 339 VAL B CB     1 
ATOM   5488  C CG1    . VAL B 1 339 ? 27.136  53.025  19.458 1.00 36.22  ? 339 VAL B CG1    1 
ATOM   5489  C CG2    . VAL B 1 339 ? 26.022  55.006  18.421 1.00 35.92  ? 339 VAL B CG2    1 
ATOM   5490  N N      . TRP B 1 340 ? 28.756  52.752  16.099 1.00 35.38  ? 340 TRP B N      1 
ATOM   5491  C CA     . TRP B 1 340 ? 29.445  51.632  15.512 1.00 38.10  ? 340 TRP B CA     1 
ATOM   5492  C C      . TRP B 1 340 ? 30.853  51.938  15.071 1.00 42.61  ? 340 TRP B C      1 
ATOM   5493  O O      . TRP B 1 340 ? 31.735  51.147  15.281 1.00 41.01  ? 340 TRP B O      1 
ATOM   5494  C CB     . TRP B 1 340 ? 28.618  51.126  14.344 1.00 39.75  ? 340 TRP B CB     1 
ATOM   5495  C CG     . TRP B 1 340 ? 29.093  49.866  13.737 1.00 42.23  ? 340 TRP B CG     1 
ATOM   5496  C CD1    . TRP B 1 340 ? 28.669  48.613  14.024 1.00 36.83  ? 340 TRP B CD1    1 
ATOM   5497  C CD2    . TRP B 1 340 ? 30.077  49.736  12.719 1.00 38.58  ? 340 TRP B CD2    1 
ATOM   5498  N NE1    . TRP B 1 340 ? 29.338  47.705  13.255 1.00 33.87  ? 340 TRP B NE1    1 
ATOM   5499  C CE2    . TRP B 1 340 ? 30.211  48.374  12.444 1.00 36.86  ? 340 TRP B CE2    1 
ATOM   5500  C CE3    . TRP B 1 340 ? 30.866  50.644  12.020 1.00 39.71  ? 340 TRP B CE3    1 
ATOM   5501  C CZ2    . TRP B 1 340 ? 31.098  47.898  11.501 1.00 42.93  ? 340 TRP B CZ2    1 
ATOM   5502  C CZ3    . TRP B 1 340 ? 31.742  50.170  11.090 1.00 43.96  ? 340 TRP B CZ3    1 
ATOM   5503  C CH2    . TRP B 1 340 ? 31.854  48.813  10.834 1.00 44.34  ? 340 TRP B CH2    1 
ATOM   5504  N N      . ILE B 1 341 ? 31.074  53.089  14.462 1.00 42.94  ? 341 ILE B N      1 
ATOM   5505  C CA     . ILE B 1 341 ? 32.386  53.438  13.961 1.00 43.11  ? 341 ILE B CA     1 
ATOM   5506  C C      . ILE B 1 341 ? 33.333  53.513  15.113 1.00 45.96  ? 341 ILE B C      1 
ATOM   5507  O O      . ILE B 1 341 ? 34.478  53.143  14.991 1.00 49.62  ? 341 ILE B O      1 
ATOM   5508  C CB     . ILE B 1 341 ? 32.413  54.800  13.271 1.00 35.29  ? 341 ILE B CB     1 
ATOM   5509  C CG1    . ILE B 1 341 ? 31.334  54.899  12.201 1.00 38.28  ? 341 ILE B CG1    1 
ATOM   5510  C CG2    . ILE B 1 341 ? 33.784  55.070  12.685 1.00 35.75  ? 341 ILE B CG2    1 
ATOM   5511  C CD1    . ILE B 1 341 ? 31.476  53.887  11.098 1.00 49.77  ? 341 ILE B CD1    1 
ATOM   5512  N N      . GLY B 1 342 ? 32.872  54.028  16.234 1.00 43.92  ? 342 GLY B N      1 
ATOM   5513  C CA     . GLY B 1 342 ? 33.718  54.096  17.402 1.00 44.96  ? 342 GLY B CA     1 
ATOM   5514  C C      . GLY B 1 342 ? 34.087  52.711  17.807 1.00 42.98  ? 342 GLY B C      1 
ATOM   5515  O O      . GLY B 1 342 ? 35.208  52.451  18.173 1.00 42.90  ? 342 GLY B O      1 
ATOM   5516  N N      . GLY B 1 343 ? 33.136  51.816  17.758 1.00 39.26  ? 343 GLY B N      1 
ATOM   5517  C CA     . GLY B 1 343 ? 33.408  50.442  18.049 1.00 39.28  ? 343 GLY B CA     1 
ATOM   5518  C C      . GLY B 1 343 ? 34.320  49.767  17.064 1.00 49.91  ? 343 GLY B C      1 
ATOM   5519  O O      . GLY B 1 343 ? 35.151  48.977  17.465 1.00 56.06  ? 343 GLY B O      1 
ATOM   5520  N N      . SER B 1 344 ? 34.125  50.019  15.774 1.00 49.19  ? 344 SER B N      1 
ATOM   5521  C CA     . SER B 1 344 ? 34.967  49.414  14.754 1.00 46.20  ? 344 SER B CA     1 
ATOM   5522  C C      . SER B 1 344 ? 36.370  49.901  15.015 1.00 49.82  ? 344 SER B C      1 
ATOM   5523  O O      . SER B 1 344 ? 37.337  49.171  14.802 1.00 51.63  ? 344 SER B O      1 
ATOM   5524  C CB     . SER B 1 344 ? 34.505  49.815  13.357 1.00 43.58  ? 344 SER B CB     1 
ATOM   5525  O OG     . SER B 1 344 ? 34.876  51.146  13.047 1.00 44.88  ? 344 SER B OG     1 
ATOM   5526  N N      . ILE B 1 345 ? 36.476  51.107  15.526 1.00 47.12  ? 345 ILE B N      1 
ATOM   5527  C CA     . ILE B 1 345 ? 37.769  51.651  15.814 1.00 46.41  ? 345 ILE B CA     1 
ATOM   5528  C C      . ILE B 1 345 ? 38.361  50.900  16.956 1.00 43.91  ? 345 ILE B C      1 
ATOM   5529  O O      . ILE B 1 345 ? 39.457  50.390  16.844 1.00 42.62  ? 345 ILE B O      1 
ATOM   5530  C CB     . ILE B 1 345 ? 37.676  53.139  16.143 1.00 41.21  ? 345 ILE B CB     1 
ATOM   5531  C CG1    . ILE B 1 345 ? 37.469  53.947  14.867 1.00 44.34  ? 345 ILE B CG1    1 
ATOM   5532  C CG2    . ILE B 1 345 ? 38.946  53.628  16.808 1.00 44.31  ? 345 ILE B CG2    1 
ATOM   5533  C CD1    . ILE B 1 345 ? 37.334  55.432  15.107 1.00 45.66  ? 345 ILE B CD1    1 
ATOM   5534  N N      . LEU B 1 346 ? 37.632  50.759  18.036 1.00 41.22  ? 346 LEU B N      1 
ATOM   5535  C CA     . LEU B 1 346 ? 38.211  50.171  19.210 1.00 42.28  ? 346 LEU B CA     1 
ATOM   5536  C C      . LEU B 1 346 ? 38.626  48.794  18.885 1.00 44.75  ? 346 LEU B C      1 
ATOM   5537  O O      . LEU B 1 346 ? 39.675  48.363  19.304 1.00 48.25  ? 346 LEU B O      1 
ATOM   5538  C CB     . LEU B 1 346 ? 37.226  50.146  20.363 1.00 38.33  ? 346 LEU B CB     1 
ATOM   5539  C CG     . LEU B 1 346 ? 37.584  50.844  21.657 1.00 36.94  ? 346 LEU B CG     1 
ATOM   5540  C CD1    . LEU B 1 346 ? 37.885  52.297  21.347 1.00 46.15  ? 346 LEU B CD1    1 
ATOM   5541  C CD2    . LEU B 1 346 ? 36.406  50.724  22.608 1.00 29.68  ? 346 LEU B CD2    1 
ATOM   5542  N N      . ALA B 1 347 ? 37.825  48.078  18.131 1.00 43.10  ? 347 ALA B N      1 
ATOM   5543  C CA     . ALA B 1 347 ? 38.119  46.687  17.877 1.00 38.83  ? 347 ALA B CA     1 
ATOM   5544  C C      . ALA B 1 347 ? 39.400  46.547  17.133 1.00 42.70  ? 347 ALA B C      1 
ATOM   5545  O O      . ALA B 1 347 ? 40.154  45.615  17.375 1.00 41.26  ? 347 ALA B O      1 
ATOM   5546  C CB     . ALA B 1 347 ? 37.000  46.046  17.117 1.00 38.69  ? 347 ALA B CB     1 
ATOM   5547  N N      . SER B 1 348 ? 39.654  47.464  16.214 1.00 44.92  ? 348 SER B N      1 
ATOM   5548  C CA     . SER B 1 348 ? 40.875  47.431  15.427 1.00 42.69  ? 348 SER B CA     1 
ATOM   5549  C C      . SER B 1 348 ? 42.052  47.986  16.182 1.00 41.80  ? 348 SER B C      1 
ATOM   5550  O O      . SER B 1 348 ? 43.162  47.956  15.688 1.00 39.10  ? 348 SER B O      1 
ATOM   5551  C CB     . SER B 1 348 ? 40.690  48.190  14.134 1.00 48.39  ? 348 SER B CB     1 
ATOM   5552  O OG     . SER B 1 348 ? 40.377  49.545  14.377 1.00 58.80  ? 348 SER B OG     1 
ATOM   5553  N N      . LEU B 1 349 ? 41.823  48.528  17.362 1.00 43.03  ? 349 LEU B N      1 
ATOM   5554  C CA     . LEU B 1 349 ? 42.936  48.976  18.153 1.00 44.80  ? 349 LEU B CA     1 
ATOM   5555  C C      . LEU B 1 349 ? 43.676  47.786  18.698 1.00 46.52  ? 349 LEU B C      1 
ATOM   5556  O O      . LEU B 1 349 ? 43.065  46.807  19.074 1.00 44.70  ? 349 LEU B O      1 
ATOM   5557  C CB     . LEU B 1 349 ? 42.507  49.898  19.279 1.00 41.99  ? 349 LEU B CB     1 
ATOM   5558  C CG     . LEU B 1 349 ? 41.990  51.288  18.936 1.00 46.19  ? 349 LEU B CG     1 
ATOM   5559  C CD1    . LEU B 1 349 ? 41.909  52.121  20.201 1.00 40.66  ? 349 LEU B CD1    1 
ATOM   5560  C CD2    . LEU B 1 349 ? 42.911  51.949  17.933 1.00 56.19  ? 349 LEU B CD2    1 
ATOM   5561  N N      . SER B 1 350 ? 44.994  47.864  18.741 1.00 47.45  ? 350 SER B N      1 
ATOM   5562  C CA     . SER B 1 350 ? 45.811  46.774  19.197 1.00 39.85  ? 350 SER B CA     1 
ATOM   5563  C C      . SER B 1 350 ? 45.718  46.605  20.668 1.00 38.42  ? 350 SER B C      1 
ATOM   5564  O O      . SER B 1 350 ? 45.663  45.507  21.162 1.00 39.95  ? 350 SER B O      1 
ATOM   5565  C CB     . SER B 1 350 ? 47.241  47.086  18.827 1.00 37.91  ? 350 SER B CB     1 
ATOM   5566  O OG     . SER B 1 350 ? 47.352  47.344  17.444 1.00 43.68  ? 350 SER B OG     1 
ATOM   5567  N N      . THR B 1 351 ? 45.743  47.703  21.390 1.00 41.18  ? 351 THR B N      1 
ATOM   5568  C CA     . THR B 1 351 ? 45.696  47.653  22.826 1.00 43.26  ? 351 THR B CA     1 
ATOM   5569  C C      . THR B 1 351 ? 44.462  46.935  23.248 1.00 44.83  ? 351 THR B C      1 
ATOM   5570  O O      . THR B 1 351 ? 44.429  46.301  24.287 1.00 47.83  ? 351 THR B O      1 
ATOM   5571  C CB     . THR B 1 351 ? 45.628  49.063  23.381 1.00 44.85  ? 351 THR B CB     1 
ATOM   5572  O OG1    . THR B 1 351 ? 46.556  49.893  22.678 1.00 47.33  ? 351 THR B OG1    1 
ATOM   5573  C CG2    . THR B 1 351 ? 45.969  49.065  24.847 1.00 48.77  ? 351 THR B CG2    1 
ATOM   5574  N N      . PHE B 1 352 ? 43.433  47.000  22.426 1.00 41.76  ? 352 PHE B N      1 
ATOM   5575  C CA     . PHE B 1 352 ? 42.155  46.424  22.787 1.00 41.48  ? 352 PHE B CA     1 
ATOM   5576  C C      . PHE B 1 352 ? 42.226  44.944  22.770 1.00 47.58  ? 352 PHE B C      1 
ATOM   5577  O O      . PHE B 1 352 ? 41.373  44.280  23.319 1.00 51.52  ? 352 PHE B O      1 
ATOM   5578  C CB     . PHE B 1 352 ? 41.089  46.887  21.807 1.00 34.89  ? 352 PHE B CB     1 
ATOM   5579  C CG     . PHE B 1 352 ? 39.683  46.642  22.249 1.00 31.15  ? 352 PHE B CG     1 
ATOM   5580  C CD1    . PHE B 1 352 ? 39.103  47.439  23.200 1.00 38.25  ? 352 PHE B CD1    1 
ATOM   5581  C CD2    . PHE B 1 352 ? 38.928  45.648  21.668 1.00 32.10  ? 352 PHE B CD2    1 
ATOM   5582  C CE1    . PHE B 1 352 ? 37.804  47.228  23.594 1.00 38.47  ? 352 PHE B CE1    1 
ATOM   5583  C CE2    . PHE B 1 352 ? 37.628  45.431  22.056 1.00 30.96  ? 352 PHE B CE2    1 
ATOM   5584  C CZ     . PHE B 1 352 ? 37.065  46.224  23.018 1.00 32.48  ? 352 PHE B CZ     1 
ATOM   5585  N N      . GLN B 1 353 ? 43.232  44.388  22.132 1.00 46.96  ? 353 GLN B N      1 
ATOM   5586  C CA     . GLN B 1 353 ? 43.252  42.945  22.002 1.00 43.34  ? 353 GLN B CA     1 
ATOM   5587  C C      . GLN B 1 353 ? 43.352  42.353  23.377 1.00 49.74  ? 353 GLN B C      1 
ATOM   5588  O O      . GLN B 1 353 ? 43.042  41.187  23.587 1.00 49.66  ? 353 GLN B O      1 
ATOM   5589  C CB     . GLN B 1 353 ? 44.389  42.499  21.088 1.00 44.27  ? 353 GLN B CB     1 
ATOM   5590  C CG     . GLN B 1 353 ? 45.771  42.492  21.711 1.00 55.88  ? 353 GLN B CG     1 
ATOM   5591  C CD     . GLN B 1 353 ? 46.865  42.708  20.687 1.00 49.70  ? 353 GLN B CD     1 
ATOM   5592  O OE1    . GLN B 1 353 ? 46.619  42.668  19.485 1.00 43.27  ? 353 GLN B OE1    1 
ATOM   5593  N NE2    . GLN B 1 353 ? 48.079  42.951  21.159 1.00 45.19  ? 353 GLN B NE2    1 
ATOM   5594  N N      . GLN B 1 354 ? 43.764  43.163  24.340 1.00 52.52  ? 354 GLN B N      1 
ATOM   5595  C CA     . GLN B 1 354 ? 43.974  42.657  25.684 1.00 48.43  ? 354 GLN B CA     1 
ATOM   5596  C C      . GLN B 1 354 ? 42.818  43.044  26.559 1.00 46.02  ? 354 GLN B C      1 
ATOM   5597  O O      . GLN B 1 354 ? 42.761  42.654  27.710 1.00 61.37  ? 354 GLN B O      1 
ATOM   5598  C CB     . GLN B 1 354 ? 45.279  43.197  26.266 1.00 42.12  ? 354 GLN B CB     1 
ATOM   5599  C CG     . GLN B 1 354 ? 46.451  43.262  25.307 1.00 45.05  ? 354 GLN B CG     1 
ATOM   5600  C CD     . GLN B 1 354 ? 47.143  41.930  25.137 1.00 57.60  ? 354 GLN B CD     1 
ATOM   5601  O OE1    . GLN B 1 354 ? 46.736  40.931  25.715 1.00 59.84  ? 354 GLN B OE1    1 
ATOM   5602  N NE2    . GLN B 1 354 ? 48.202  41.911  24.344 1.00 61.74  ? 354 GLN B NE2    1 
ATOM   5603  N N      . MET B 1 355 ? 41.876  43.789  26.016 1.00 35.57  ? 355 MET B N      1 
ATOM   5604  C CA     . MET B 1 355 ? 40.735  44.199  26.789 1.00 37.54  ? 355 MET B CA     1 
ATOM   5605  C C      . MET B 1 355 ? 39.551  43.290  26.575 1.00 37.30  ? 355 MET B C      1 
ATOM   5606  O O      . MET B 1 355 ? 38.509  43.481  27.178 1.00 37.38  ? 355 MET B O      1 
ATOM   5607  C CB     . MET B 1 355 ? 40.373  45.627  26.456 1.00 44.22  ? 355 MET B CB     1 
ATOM   5608  C CG     . MET B 1 355 ? 41.512  46.611  26.567 1.00 45.91  ? 355 MET B CG     1 
ATOM   5609  S SD     . MET B 1 355 ? 40.866  48.277  26.433 1.00 55.91  ? 355 MET B SD     1 
ATOM   5610  C CE     . MET B 1 355 ? 39.488  48.188  27.563 1.00 47.23  ? 355 MET B CE     1 
ATOM   5611  N N      . TRP B 1 356 ? 39.706  42.292  25.727 1.00 39.47  ? 356 TRP B N      1 
ATOM   5612  C CA     . TRP B 1 356 ? 38.635  41.346  25.451 1.00 35.77  ? 356 TRP B CA     1 
ATOM   5613  C C      . TRP B 1 356 ? 38.385  40.359  26.571 1.00 34.75  ? 356 TRP B C      1 
ATOM   5614  O O      . TRP B 1 356 ? 39.297  40.003  27.296 1.00 36.66  ? 356 TRP B O      1 
ATOM   5615  C CB     . TRP B 1 356 ? 38.976  40.531  24.212 1.00 31.09  ? 356 TRP B CB     1 
ATOM   5616  C CG     . TRP B 1 356 ? 38.930  41.179  22.885 1.00 31.09  ? 356 TRP B CG     1 
ATOM   5617  C CD1    . TRP B 1 356 ? 39.989  41.493  22.105 1.00 33.86  ? 356 TRP B CD1    1 
ATOM   5618  C CD2    . TRP B 1 356 ? 37.766  41.519  22.136 1.00 31.71  ? 356 TRP B CD2    1 
ATOM   5619  N NE1    . TRP B 1 356 ? 39.564  42.038  20.926 1.00 37.66  ? 356 TRP B NE1    1 
ATOM   5620  C CE2    . TRP B 1 356 ? 38.198  42.065  20.922 1.00 33.34  ? 356 TRP B CE2    1 
ATOM   5621  C CE3    . TRP B 1 356 ? 36.401  41.432  22.383 1.00 33.62  ? 356 TRP B CE3    1 
ATOM   5622  C CZ2    . TRP B 1 356 ? 37.316  42.525  19.960 1.00 39.33  ? 356 TRP B CZ2    1 
ATOM   5623  C CZ3    . TRP B 1 356 ? 35.530  41.886  21.430 1.00 40.95  ? 356 TRP B CZ3    1 
ATOM   5624  C CH2    . TRP B 1 356 ? 35.987  42.427  20.233 1.00 45.12  ? 356 TRP B CH2    1 
ATOM   5625  N N      . ILE B 1 357 ? 37.156  39.870  26.683 1.00 31.55  ? 357 ILE B N      1 
ATOM   5626  C CA     . ILE B 1 357 ? 36.825  38.855  27.663 1.00 34.62  ? 357 ILE B CA     1 
ATOM   5627  C C      . ILE B 1 357 ? 36.943  37.517  26.986 1.00 35.63  ? 357 ILE B C      1 
ATOM   5628  O O      . ILE B 1 357 ? 36.064  37.135  26.249 1.00 36.71  ? 357 ILE B O      1 
ATOM   5629  C CB     . ILE B 1 357 ? 35.372  38.949  28.097 1.00 30.42  ? 357 ILE B CB     1 
ATOM   5630  C CG1    . ILE B 1 357 ? 35.059  40.273  28.751 1.00 25.22  ? 357 ILE B CG1    1 
ATOM   5631  C CG2    . ILE B 1 357 ? 35.049  37.841  29.076 1.00 42.91  ? 357 ILE B CG2    1 
ATOM   5632  C CD1    . ILE B 1 357 ? 33.637  40.294  29.244 1.00 29.31  ? 357 ILE B CD1    1 
ATOM   5633  N N      . SER B 1 358 ? 38.021  36.791  27.212 1.00 35.62  ? 358 SER B N      1 
ATOM   5634  C CA     . SER B 1 358 ? 38.243  35.533  26.526 1.00 36.11  ? 358 SER B CA     1 
ATOM   5635  C C      . SER B 1 358 ? 37.357  34.435  27.040 1.00 42.33  ? 358 SER B C      1 
ATOM   5636  O O      . SER B 1 358 ? 36.797  34.552  28.104 1.00 47.64  ? 358 SER B O      1 
ATOM   5637  C CB     . SER B 1 358 ? 39.692  35.139  26.646 1.00 36.55  ? 358 SER B CB     1 
ATOM   5638  O OG     . SER B 1 358 ? 40.052  34.964  27.997 1.00 45.44  ? 358 SER B OG     1 
ATOM   5639  N N      . LYS B 1 359 ? 37.193  33.370  26.278 1.00 44.06  ? 359 LYS B N      1 
ATOM   5640  C CA     . LYS B 1 359 ? 36.325  32.265  26.670 1.00 48.01  ? 359 LYS B CA     1 
ATOM   5641  C C      . LYS B 1 359 ? 36.844  31.640  27.896 1.00 48.47  ? 359 LYS B C      1 
ATOM   5642  O O      . LYS B 1 359 ? 36.091  31.182  28.730 1.00 46.56  ? 359 LYS B O      1 
ATOM   5643  C CB     . LYS B 1 359 ? 36.277  31.213  25.583 1.00 48.15  ? 359 LYS B CB     1 
ATOM   5644  C CG     . LYS B 1 359 ? 35.243  30.125  25.789 1.00 49.58  ? 359 LYS B CG     1 
ATOM   5645  C CD     . LYS B 1 359 ? 34.983  29.389  24.486 1.00 50.71  ? 359 LYS B CD     1 
ATOM   5646  C CE     . LYS B 1 359 ? 36.279  28.919  23.846 1.00 45.41  ? 359 LYS B CE     1 
ATOM   5647  N NZ     . LYS B 1 359 ? 36.952  27.869  24.657 1.00 47.64  ? 359 LYS B NZ     1 
ATOM   5648  N N      . GLN B 1 360 ? 38.153  31.584  28.000 1.00 52.15  ? 360 GLN B N      1 
ATOM   5649  C CA     . GLN B 1 360 ? 38.771  30.974  29.141 1.00 53.22  ? 360 GLN B CA     1 
ATOM   5650  C C      . GLN B 1 360 ? 38.359  31.716  30.369 1.00 52.36  ? 360 GLN B C      1 
ATOM   5651  O O      . GLN B 1 360 ? 38.034  31.112  31.371 1.00 57.71  ? 360 GLN B O      1 
ATOM   5652  C CB     . GLN B 1 360 ? 40.279  31.064  28.991 1.00 50.62  ? 360 GLN B CB     1 
ATOM   5653  C CG     . GLN B 1 360 ? 40.894  30.016  28.076 1.00 57.04  ? 360 GLN B CG     1 
ATOM   5654  C CD     . GLN B 1 360 ? 40.478  30.163  26.626 1.00 61.90  ? 360 GLN B CD     1 
ATOM   5655  O OE1    . GLN B 1 360 ? 40.739  31.180  25.990 1.00 57.69  ? 360 GLN B OE1    1 
ATOM   5656  N NE2    . GLN B 1 360 ? 39.830  29.137  26.097 1.00 70.67  ? 360 GLN B NE2    1 
ATOM   5657  N N      . GLU B 1 361 ? 38.343  33.030  30.294 1.00 41.38  ? 361 GLU B N      1 
ATOM   5658  C CA     . GLU B 1 361 ? 37.925  33.828  31.420 1.00 38.93  ? 361 GLU B CA     1 
ATOM   5659  C C      . GLU B 1 361 ? 36.485  33.606  31.782 1.00 40.11  ? 361 GLU B C      1 
ATOM   5660  O O      . GLU B 1 361 ? 36.134  33.621  32.945 1.00 42.20  ? 361 GLU B O      1 
ATOM   5661  C CB     . GLU B 1 361 ? 38.228  35.286  31.190 1.00 43.42  ? 361 GLU B CB     1 
ATOM   5662  C CG     . GLU B 1 361 ? 39.641  35.657  31.602 1.00 53.39  ? 361 GLU B CG     1 
ATOM   5663  C CD     . GLU B 1 361 ? 40.133  36.928  30.952 1.00 55.98  ? 361 GLU B CD     1 
ATOM   5664  O OE1    . GLU B 1 361 ? 39.586  37.304  29.902 1.00 53.75  ? 361 GLU B OE1    1 
ATOM   5665  O OE2    . GLU B 1 361 ? 41.079  37.542  31.480 1.00 57.06  ? 361 GLU B OE2    1 
ATOM   5666  N N      . TYR B 1 362 ? 35.637  33.412  30.796 1.00 44.08  ? 362 TYR B N      1 
ATOM   5667  C CA     . TYR B 1 362 ? 34.251  33.129  31.076 1.00 41.61  ? 362 TYR B CA     1 
ATOM   5668  C C      . TYR B 1 362 ? 34.148  31.852  31.841 1.00 53.08  ? 362 TYR B C      1 
ATOM   5669  O O      . TYR B 1 362 ? 33.391  31.761  32.784 1.00 56.46  ? 362 TYR B O      1 
ATOM   5670  C CB     . TYR B 1 362 ? 33.465  32.984  29.785 1.00 32.32  ? 362 TYR B CB     1 
ATOM   5671  C CG     . TYR B 1 362 ? 32.006  32.670  29.963 1.00 30.55  ? 362 TYR B CG     1 
ATOM   5672  C CD1    . TYR B 1 362 ? 31.108  33.651  30.322 1.00 37.30  ? 362 TYR B CD1    1 
ATOM   5673  C CD2    . TYR B 1 362 ? 31.522  31.395  29.748 1.00 36.97  ? 362 TYR B CD2    1 
ATOM   5674  C CE1    . TYR B 1 362 ? 29.771  33.370  30.477 1.00 37.86  ? 362 TYR B CE1    1 
ATOM   5675  C CE2    . TYR B 1 362 ? 30.187  31.106  29.907 1.00 42.78  ? 362 TYR B CE2    1 
ATOM   5676  C CZ     . TYR B 1 362 ? 29.320  32.100  30.270 1.00 39.38  ? 362 TYR B CZ     1 
ATOM   5677  O OH     . TYR B 1 362 ? 27.991  31.820  30.428 1.00 41.61  ? 362 TYR B OH     1 
ATOM   5678  N N      . ASP B 1 363 ? 34.904  30.844  31.449 1.00 59.73  ? 363 ASP B N      1 
ATOM   5679  C CA     . ASP B 1 363 ? 34.780  29.562  32.094 1.00 48.71  ? 363 ASP B CA     1 
ATOM   5680  C C      . ASP B 1 363 ? 35.185  29.696  33.525 1.00 49.05  ? 363 ASP B C      1 
ATOM   5681  O O      . ASP B 1 363 ? 34.507  29.208  34.417 1.00 51.31  ? 363 ASP B O      1 
ATOM   5682  C CB     . ASP B 1 363 ? 35.660  28.553  31.385 1.00 48.93  ? 363 ASP B CB     1 
ATOM   5683  C CG     . ASP B 1 363 ? 35.185  28.248  29.989 1.00 61.88  ? 363 ASP B CG     1 
ATOM   5684  O OD1    . ASP B 1 363 ? 34.054  28.638  29.645 1.00 57.16  ? 363 ASP B OD1    1 
ATOM   5685  O OD2    . ASP B 1 363 ? 35.938  27.607  29.233 1.00 77.13  ? 363 ASP B OD2    1 
ATOM   5686  N N      . GLU B 1 364 ? 36.279  30.389  33.760 1.00 47.26  ? 364 GLU B N      1 
ATOM   5687  C CA     . GLU B 1 364 ? 36.753  30.582  35.108 1.00 51.40  ? 364 GLU B CA     1 
ATOM   5688  C C      . GLU B 1 364 ? 35.861  31.410  36.008 1.00 57.38  ? 364 GLU B C      1 
ATOM   5689  O O      . GLU B 1 364 ? 35.669  31.059  37.163 1.00 65.15  ? 364 GLU B O      1 
ATOM   5690  C CB     . GLU B 1 364 ? 38.132  31.220  35.058 1.00 53.24  ? 364 GLU B CB     1 
ATOM   5691  C CG     . GLU B 1 364 ? 39.152  30.412  34.286 1.00 52.68  ? 364 GLU B CG     1 
ATOM   5692  C CD     . GLU B 1 364 ? 40.429  31.185  34.051 1.00 66.09  ? 364 GLU B CD     1 
ATOM   5693  O OE1    . GLU B 1 364 ? 40.575  32.277  34.635 1.00 67.10  ? 364 GLU B OE1    1 
ATOM   5694  O OE2    . GLU B 1 364 ? 41.284  30.702  33.284 1.00 66.31  ? 364 GLU B OE2    1 
ATOM   5695  N N      . SER B 1 365 ? 35.298  32.499  35.504 1.00 53.44  ? 365 SER B N      1 
ATOM   5696  C CA     . SER B 1 365 ? 34.535  33.408  36.370 1.00 57.77  ? 365 SER B CA     1 
ATOM   5697  C C      . SER B 1 365 ? 33.049  33.476  36.143 1.00 54.00  ? 365 SER B C      1 
ATOM   5698  O O      . SER B 1 365 ? 32.315  34.028  36.953 1.00 54.66  ? 365 SER B O      1 
ATOM   5699  C CB     . SER B 1 365 ? 35.089  34.819  36.239 1.00 63.13  ? 365 SER B CB     1 
ATOM   5700  O OG     . SER B 1 365 ? 34.466  35.706  37.153 1.00 71.95  ? 365 SER B OG     1 
ATOM   5701  N N      . GLY B 1 366 ? 32.605  32.927  35.037 1.00 50.17  ? 366 GLY B N      1 
ATOM   5702  C CA     . GLY B 1 366 ? 31.200  32.915  34.763 1.00 50.51  ? 366 GLY B CA     1 
ATOM   5703  C C      . GLY B 1 366 ? 30.765  34.144  34.038 1.00 47.46  ? 366 GLY B C      1 
ATOM   5704  O O      . GLY B 1 366 ? 31.577  34.855  33.488 1.00 51.77  ? 366 GLY B O      1 
ATOM   5705  N N      . PRO B 1 367 ? 29.473  34.406  34.021 1.00 46.82  ? 367 PRO B N      1 
ATOM   5706  C CA     . PRO B 1 367 ? 28.934  35.550  33.308 1.00 48.62  ? 367 PRO B CA     1 
ATOM   5707  C C      . PRO B 1 367 ? 29.395  36.888  33.837 1.00 47.11  ? 367 PRO B C      1 
ATOM   5708  O O      . PRO B 1 367 ? 29.523  37.805  33.054 1.00 48.57  ? 367 PRO B O      1 
ATOM   5709  C CB     . PRO B 1 367 ? 27.443  35.387  33.524 1.00 49.02  ? 367 PRO B CB     1 
ATOM   5710  C CG     . PRO B 1 367 ? 27.231  33.937  33.751 1.00 46.24  ? 367 PRO B CG     1 
ATOM   5711  C CD     . PRO B 1 367 ? 28.416  33.543  34.564 1.00 46.39  ? 367 PRO B CD     1 
ATOM   5712  N N      . SER B 1 368 ? 29.701  37.007  35.110 1.00 46.74  ? 368 SER B N      1 
ATOM   5713  C CA     . SER B 1 368 ? 30.023  38.285  35.715 1.00 46.93  ? 368 SER B CA     1 
ATOM   5714  C C      . SER B 1 368 ? 31.395  38.777  35.422 1.00 45.27  ? 368 SER B C      1 
ATOM   5715  O O      . SER B 1 368 ? 31.835  39.739  36.012 1.00 47.88  ? 368 SER B O      1 
ATOM   5716  C CB     . SER B 1 368 ? 29.861  38.175  37.207 1.00 44.82  ? 368 SER B CB     1 
ATOM   5717  O OG     . SER B 1 368 ? 30.162  36.866  37.643 1.00 44.85  ? 368 SER B OG     1 
ATOM   5718  N N      . ILE B 1 369 ? 32.111  38.093  34.556 1.00 43.77  ? 369 ILE B N      1 
ATOM   5719  C CA     . ILE B 1 369 ? 33.423  38.534  34.160 1.00 44.77  ? 369 ILE B CA     1 
ATOM   5720  C C      . ILE B 1 369 ? 33.246  39.843  33.437 1.00 47.56  ? 369 ILE B C      1 
ATOM   5721  O O      . ILE B 1 369 ? 34.148  40.658  33.365 1.00 46.22  ? 369 ILE B O      1 
ATOM   5722  C CB     . ILE B 1 369 ? 34.101  37.485  33.286 1.00 38.74  ? 369 ILE B CB     1 
ATOM   5723  C CG1    . ILE B 1 369 ? 35.551  37.866  33.010 1.00 41.04  ? 369 ILE B CG1    1 
ATOM   5724  C CG2    . ILE B 1 369 ? 33.297  37.230  32.027 1.00 39.86  ? 369 ILE B CG2    1 
ATOM   5725  C CD1    . ILE B 1 369 ? 36.365  38.046  34.272 1.00 57.47  ? 369 ILE B CD1    1 
ATOM   5726  N N      . VAL B 1 370 ? 32.061  40.077  32.917 1.00 52.11  ? 370 VAL B N      1 
ATOM   5727  C CA     . VAL B 1 370 ? 31.824  41.275  32.157 1.00 51.29  ? 370 VAL B CA     1 
ATOM   5728  C C      . VAL B 1 370 ? 32.066  42.453  33.037 1.00 51.14  ? 370 VAL B C      1 
ATOM   5729  O O      . VAL B 1 370 ? 32.680  43.415  32.631 1.00 53.15  ? 370 VAL B O      1 
ATOM   5730  C CB     . VAL B 1 370 ? 30.393  41.287  31.584 1.00 48.26  ? 370 VAL B CB     1 
ATOM   5731  C CG1    . VAL B 1 370 ? 29.352  40.923  32.620 1.00 46.65  ? 370 VAL B CG1    1 
ATOM   5732  C CG2    . VAL B 1 370 ? 30.074  42.608  30.914 1.00 52.33  ? 370 VAL B CG2    1 
ATOM   5733  N N      . HIS B 1 371 ? 31.645  42.373  34.272 1.00 48.30  ? 371 HIS B N      1 
ATOM   5734  C CA     . HIS B 1 371 ? 31.757  43.489  35.163 1.00 45.57  ? 371 HIS B CA     1 
ATOM   5735  C C      . HIS B 1 371 ? 33.176  43.897  35.427 1.00 43.08  ? 371 HIS B C      1 
ATOM   5736  O O      . HIS B 1 371 ? 33.448  45.062  35.617 1.00 49.66  ? 371 HIS B O      1 
ATOM   5737  C CB     . HIS B 1 371 ? 31.027  43.142  36.432 1.00 43.72  ? 371 HIS B CB     1 
ATOM   5738  C CG     . HIS B 1 371 ? 29.568  42.919  36.236 1.00 44.11  ? 371 HIS B CG     1 
ATOM   5739  N ND1    . HIS B 1 371 ? 28.758  42.413  37.224 1.00 49.33  ? 371 HIS B ND1    1 
ATOM   5740  C CD2    . HIS B 1 371 ? 28.769  43.141  35.168 1.00 48.58  ? 371 HIS B CD2    1 
ATOM   5741  C CE1    . HIS B 1 371 ? 27.522  42.330  36.772 1.00 55.39  ? 371 HIS B CE1    1 
ATOM   5742  N NE2    . HIS B 1 371 ? 27.501  42.766  35.527 1.00 56.38  ? 371 HIS B NE2    1 
ATOM   5743  N N      . ARG B 1 372 ? 34.087  42.950  35.482 1.00 40.90  ? 372 ARG B N      1 
ATOM   5744  C CA     . ARG B 1 372 ? 35.457  43.268  35.834 1.00 40.92  ? 372 ARG B CA     1 
ATOM   5745  C C      . ARG B 1 372 ? 36.341  43.657  34.693 1.00 38.63  ? 372 ARG B C      1 
ATOM   5746  O O      . ARG B 1 372 ? 37.372  44.258  34.915 1.00 36.25  ? 372 ARG B O      1 
ATOM   5747  C CB     . ARG B 1 372 ? 36.088  42.067  36.508 1.00 51.12  ? 372 ARG B CB     1 
ATOM   5748  C CG     . ARG B 1 372 ? 35.117  41.279  37.366 1.00 60.35  ? 372 ARG B CG     1 
ATOM   5749  C CD     . ARG B 1 372 ? 35.338  41.568  38.837 1.00 67.40  ? 372 ARG B CD     1 
ATOM   5750  N NE     . ARG B 1 372 ? 36.689  41.200  39.238 1.00 67.94  ? 372 ARG B NE     1 
ATOM   5751  C CZ     . ARG B 1 372 ? 37.034  39.993  39.667 1.00 70.33  ? 372 ARG B CZ     1 
ATOM   5752  N NH1    . ARG B 1 372 ? 36.129  39.028  39.758 1.00 70.71  ? 372 ARG B NH1    1 
ATOM   5753  N NH2    . ARG B 1 372 ? 38.287  39.747  40.003 1.00 61.23  ? 372 ARG B NH2    1 
ATOM   5754  N N      . LYS B 1 373 ? 35.977  43.294  33.473 1.00 38.68  ? 373 LYS B N      1 
ATOM   5755  C CA     . LYS B 1 373 ? 36.825  43.570  32.343 1.00 41.85  ? 373 LYS B CA     1 
ATOM   5756  C C      . LYS B 1 373 ? 36.225  44.692  31.543 1.00 40.76  ? 373 LYS B C      1 
ATOM   5757  O O      . LYS B 1 373 ? 36.869  45.694  31.280 1.00 40.11  ? 373 LYS B O      1 
ATOM   5758  C CB     . LYS B 1 373 ? 36.973  42.307  31.507 1.00 35.16  ? 373 LYS B CB     1 
ATOM   5759  C CG     . LYS B 1 373 ? 37.599  41.146  32.241 1.00 37.76  ? 373 LYS B CG     1 
ATOM   5760  C CD     . LYS B 1 373 ? 38.278  40.218  31.258 1.00 42.77  ? 373 LYS B CD     1 
ATOM   5761  C CE     . LYS B 1 373 ? 39.401  40.937  30.532 1.00 48.94  ? 373 LYS B CE     1 
ATOM   5762  N NZ     . LYS B 1 373 ? 40.494  41.320  31.463 1.00 57.95  ? 373 LYS B NZ     1 
ATOM   5763  N N      . CYS B 1 374 ? 34.972  44.536  31.177 1.00 41.06  ? 374 CYS B N      1 
ATOM   5764  C CA     . CYS B 1 374 ? 34.278  45.540  30.425 1.00 44.39  ? 374 CYS B CA     1 
ATOM   5765  C C      . CYS B 1 374 ? 33.518  46.414  31.379 1.00 57.10  ? 374 CYS B C      1 
ATOM   5766  O O      . CYS B 1 374 ? 32.323  46.225  31.561 1.00 55.81  ? 374 CYS B O      1 
ATOM   5767  C CB     . CYS B 1 374 ? 33.263  44.861  29.544 1.00 40.34  ? 374 CYS B CB     1 
ATOM   5768  S SG     . CYS B 1 374 ? 33.924  43.625  28.443 1.00 47.77  ? 374 CYS B SG     1 
ATOM   5769  N N      . PHE B 1 375 ? 34.194  47.368  32.000 1.00 62.17  ? 375 PHE B N      1 
ATOM   5770  C CA     . PHE B 1 375 ? 33.529  48.288  32.896 1.00 63.61  ? 375 PHE B CA     1 
ATOM   5771  C C      . PHE B 1 375 ? 32.494  49.011  32.082 1.00 82.30  ? 375 PHE B C      1 
ATOM   5772  O O      . PHE B 1 375 ? 31.670  49.757  32.605 1.00 82.60  ? 375 PHE B O      1 
ATOM   5773  C CB     . PHE B 1 375 ? 34.489  49.338  33.412 1.00 60.68  ? 375 PHE B CB     1 
ATOM   5774  C CG     . PHE B 1 375 ? 35.745  48.792  33.990 1.00 58.62  ? 375 PHE B CG     1 
ATOM   5775  C CD1    . PHE B 1 375 ? 35.779  48.341  35.289 1.00 52.97  ? 375 PHE B CD1    1 
ATOM   5776  C CD2    . PHE B 1 375 ? 36.905  48.770  33.242 1.00 66.67  ? 375 PHE B CD2    1 
ATOM   5777  C CE1    . PHE B 1 375 ? 36.945  47.855  35.828 1.00 55.11  ? 375 PHE B CE1    1 
ATOM   5778  C CE2    . PHE B 1 375 ? 38.073  48.279  33.778 1.00 61.96  ? 375 PHE B CE2    1 
ATOM   5779  C CZ     . PHE B 1 375 ? 38.094  47.820  35.075 1.00 61.22  ? 375 PHE B CZ     1 
ATOM   5780  O OXT    . PHE B 1 375 ? 32.475  48.889  30.864 1.00 86.23  ? 375 PHE B OXT    1 
ATOM   5781  N N      . ILE C 2 6   ? 32.049  17.116  29.277 1.00 59.19  ? 24  ILE C N      1 
ATOM   5782  C CA     . ILE C 2 6   ? 31.168  16.740  30.353 1.00 61.65  ? 24  ILE C CA     1 
ATOM   5783  C C      . ILE C 2 6   ? 29.873  16.470  29.688 1.00 67.08  ? 24  ILE C C      1 
ATOM   5784  O O      . ILE C 2 6   ? 29.591  17.136  28.708 1.00 71.06  ? 24  ILE C O      1 
ATOM   5785  C CB     . ILE C 2 6   ? 31.026  17.851  31.394 1.00 64.25  ? 24  ILE C CB     1 
ATOM   5786  C CG1    . ILE C 2 6   ? 32.373  18.115  32.060 1.00 69.18  ? 24  ILE C CG1    1 
ATOM   5787  C CG2    . ILE C 2 6   ? 30.046  17.469  32.480 1.00 66.05  ? 24  ILE C CG2    1 
ATOM   5788  C CD1    . ILE C 2 6   ? 32.834  16.995  32.969 1.00 62.67  ? 24  ILE C CD1    1 
ATOM   5789  N N      . GLU C 2 7   ? 29.136  15.463  30.149 1.00 75.61  ? 25  GLU C N      1 
ATOM   5790  C CA     . GLU C 2 7   ? 27.846  15.043  29.583 1.00 74.97  ? 25  GLU C CA     1 
ATOM   5791  C C      . GLU C 2 7   ? 28.110  14.127  28.429 1.00 72.22  ? 25  GLU C C      1 
ATOM   5792  O O      . GLU C 2 7   ? 27.196  13.530  27.887 1.00 74.69  ? 25  GLU C O      1 
ATOM   5793  C CB     . GLU C 2 7   ? 26.916  16.197  29.214 1.00 78.75  ? 25  GLU C CB     1 
ATOM   5794  C CG     . GLU C 2 7   ? 26.469  17.033  30.397 1.00 78.21  ? 25  GLU C CG     1 
ATOM   5795  C CD     . GLU C 2 7   ? 26.684  18.518  30.185 1.00 78.91  ? 25  GLU C CD     1 
ATOM   5796  O OE1    . GLU C 2 7   ? 27.210  18.904  29.121 1.00 81.16  ? 25  GLU C OE1    1 
ATOM   5797  O OE2    . GLU C 2 7   ? 26.330  19.302  31.088 1.00 71.01  ? 25  GLU C OE2    1 
ATOM   5798  N N      . LEU C 2 8   ? 29.370  13.999  28.058 1.00 70.55  ? 26  LEU C N      1 
ATOM   5799  C CA     . LEU C 2 8   ? 29.741  13.082  27.018 1.00 67.48  ? 26  LEU C CA     1 
ATOM   5800  C C      . LEU C 2 8   ? 30.713  12.247  27.744 1.00 69.48  ? 26  LEU C C      1 
ATOM   5801  O O      . LEU C 2 8   ? 30.605  11.042  27.781 1.00 70.58  ? 26  LEU C O      1 
ATOM   5802  C CB     . LEU C 2 8   ? 30.489  13.800  25.915 1.00 65.44  ? 26  LEU C CB     1 
ATOM   5803  C CG     . LEU C 2 8   ? 29.749  14.620  24.856 1.00 73.92  ? 26  LEU C CG     1 
ATOM   5804  C CD1    . LEU C 2 8   ? 29.322  15.984  25.378 1.00 80.29  ? 26  LEU C CD1    1 
ATOM   5805  C CD2    . LEU C 2 8   ? 30.640  14.791  23.637 1.00 60.63  ? 26  LEU C CD2    1 
ATOM   5806  N N      . SER C 2 9   ? 31.674  12.903  28.358 1.00 72.46  ? 27  SER C N      1 
ATOM   5807  C CA     . SER C 2 9   ? 32.676  12.200  29.105 1.00 72.72  ? 27  SER C CA     1 
ATOM   5808  C C      . SER C 2 9   ? 32.068  11.505  30.273 1.00 69.15  ? 27  SER C C      1 
ATOM   5809  O O      . SER C 2 9   ? 32.464  10.406  30.613 1.00 71.46  ? 27  SER C O      1 
ATOM   5810  C CB     . SER C 2 9   ? 33.729  13.172  29.568 1.00 73.59  ? 27  SER C CB     1 
ATOM   5811  O OG     . SER C 2 9   ? 34.413  13.731  28.462 1.00 78.18  ? 27  SER C OG     1 
ATOM   5812  N N      . ILE C 2 10  ? 31.125  12.150  30.923 1.00 67.00  ? 28  ILE C N      1 
ATOM   5813  C CA     . ILE C 2 10  ? 30.442  11.508  32.019 1.00 71.59  ? 28  ILE C CA     1 
ATOM   5814  C C      . ILE C 2 10  ? 29.647  10.310  31.580 1.00 67.68  ? 28  ILE C C      1 
ATOM   5815  O O      . ILE C 2 10  ? 29.686  9.281   32.226 1.00 70.78  ? 28  ILE C O      1 
ATOM   5816  C CB     . ILE C 2 10  ? 29.509  12.480  32.737 1.00 75.27  ? 28  ILE C CB     1 
ATOM   5817  C CG1    . ILE C 2 10  ? 30.300  13.669  33.278 1.00 75.98  ? 28  ILE C CG1    1 
ATOM   5818  C CG2    . ILE C 2 10  ? 28.796  11.803  33.895 1.00 67.04  ? 28  ILE C CG2    1 
ATOM   5819  C CD1    . ILE C 2 10  ? 31.151  13.335  34.483 1.00 66.92  ? 28  ILE C CD1    1 
ATOM   5820  N N      . SER C 2 11  ? 28.950  10.402  30.466 1.00 61.73  ? 29  SER C N      1 
ATOM   5821  C CA     . SER C 2 11  ? 28.090  9.302   30.088 1.00 64.21  ? 29  SER C CA     1 
ATOM   5822  C C      . SER C 2 11  ? 28.877  8.159   29.546 1.00 61.62  ? 29  SER C C      1 
ATOM   5823  O O      . SER C 2 11  ? 28.563  7.014   29.811 1.00 59.99  ? 29  SER C O      1 
ATOM   5824  C CB     . SER C 2 11  ? 27.069  9.747   29.068 1.00 65.41  ? 29  SER C CB     1 
ATOM   5825  O OG     . SER C 2 11  ? 26.094  8.743   28.859 1.00 70.77  ? 29  SER C OG     1 
ATOM   5826  N N      . LEU C 2 12  ? 29.901  8.462   28.778 1.00 56.81  ? 30  LEU C N      1 
ATOM   5827  C CA     . LEU C 2 12  ? 30.734  7.424   28.225 1.00 56.31  ? 30  LEU C CA     1 
ATOM   5828  C C      . LEU C 2 12  ? 31.220  6.591   29.374 1.00 65.46  ? 30  LEU C C      1 
ATOM   5829  O O      . LEU C 2 12  ? 31.301  5.378   29.278 1.00 72.49  ? 30  LEU C O      1 
ATOM   5830  C CB     . LEU C 2 12  ? 31.892  8.008   27.435 1.00 45.34  ? 30  LEU C CB     1 
ATOM   5831  C CG     . LEU C 2 12  ? 31.545  8.539   26.053 1.00 43.55  ? 30  LEU C CG     1 
ATOM   5832  C CD1    . LEU C 2 12  ? 32.805  9.016   25.361 1.00 51.08  ? 30  LEU C CD1    1 
ATOM   5833  C CD2    . LEU C 2 12  ? 30.864  7.456   25.239 1.00 50.57  ? 30  LEU C CD2    1 
ATOM   5834  N N      . SER C 2 13  ? 31.534  7.244   30.474 1.00 61.99  ? 31  SER C N      1 
ATOM   5835  C CA     . SER C 2 13  ? 32.084  6.553   31.613 1.00 53.99  ? 31  SER C CA     1 
ATOM   5836  C C      . SER C 2 13  ? 31.080  5.714   32.313 1.00 56.64  ? 31  SER C C      1 
ATOM   5837  O O      . SER C 2 13  ? 31.372  4.601   32.702 1.00 61.57  ? 31  SER C O      1 
ATOM   5838  C CB     . SER C 2 13  ? 32.605  7.586   32.580 1.00 58.63  ? 31  SER C CB     1 
ATOM   5839  O OG     . SER C 2 13  ? 33.634  8.352   31.993 1.00 63.12  ? 31  SER C OG     1 
ATOM   5840  N N      . LEU C 2 14  ? 29.900  6.263   32.523 1.00 53.44  ? 32  LEU C N      1 
ATOM   5841  C CA     . LEU C 2 14  ? 28.870  5.564   33.257 1.00 58.34  ? 32  LEU C CA     1 
ATOM   5842  C C      . LEU C 2 14  ? 28.559  4.257   32.606 1.00 64.51  ? 32  LEU C C      1 
ATOM   5843  O O      . LEU C 2 14  ? 27.972  3.376   33.214 1.00 62.99  ? 32  LEU C O      1 
ATOM   5844  C CB     . LEU C 2 14  ? 27.616  6.414   33.296 1.00 58.24  ? 32  LEU C CB     1 
ATOM   5845  C CG     . LEU C 2 14  ? 27.225  7.186   34.550 1.00 55.75  ? 32  LEU C CG     1 
ATOM   5846  C CD1    . LEU C 2 14  ? 26.727  6.236   35.619 1.00 69.21  ? 32  LEU C CD1    1 
ATOM   5847  C CD2    . LEU C 2 14  ? 28.359  8.046   35.073 1.00 63.58  ? 32  LEU C CD2    1 
ATOM   5848  N N      . ASP C 2 15  ? 29.003  4.095   31.375 1.00 64.04  ? 33  ASP C N      1 
ATOM   5849  C CA     . ASP C 2 15  ? 28.695  2.888   30.641 1.00 60.73  ? 33  ASP C CA     1 
ATOM   5850  C C      . ASP C 2 15  ? 29.545  1.698   31.021 1.00 64.41  ? 33  ASP C C      1 
ATOM   5851  O O      . ASP C 2 15  ? 29.221  0.581   30.646 1.00 71.78  ? 33  ASP C O      1 
ATOM   5852  C CB     . ASP C 2 15  ? 28.835  3.128   29.145 1.00 67.27  ? 33  ASP C CB     1 
ATOM   5853  C CG     . ASP C 2 15  ? 27.759  4.019   28.593 1.00 76.10  ? 33  ASP C CG     1 
ATOM   5854  O OD1    . ASP C 2 15  ? 26.962  4.544   29.390 1.00 83.41  ? 33  ASP C OD1    1 
ATOM   5855  O OD2    . ASP C 2 15  ? 27.710  4.197   27.359 1.00 66.09  ? 33  ASP C OD2    1 
ATOM   5856  N N      . SER C 2 16  ? 30.637  1.909   31.737 1.00 60.44  ? 34  SER C N      1 
ATOM   5857  C CA     . SER C 2 16  ? 31.511  0.798   32.061 1.00 62.33  ? 34  SER C CA     1 
ATOM   5858  C C      . SER C 2 16  ? 30.741  -0.201  32.869 1.00 58.26  ? 34  SER C C      1 
ATOM   5859  O O      . SER C 2 16  ? 30.056  0.148   33.817 1.00 56.83  ? 34  SER C O      1 
ATOM   5860  C CB     . SER C 2 16  ? 32.731  1.240   32.843 1.00 55.88  ? 34  SER C CB     1 
ATOM   5861  O OG     . SER C 2 16  ? 33.580  0.142   33.122 1.00 54.99  ? 34  SER C OG     1 
ATOM   5862  N N      . PRO C 2 17  ? 30.834  -1.497  32.511 1.00 54.29  ? 35  PRO C N      1 
ATOM   5863  C CA     . PRO C 2 17  ? 30.004  -2.375  33.330 1.00 58.61  ? 35  PRO C CA     1 
ATOM   5864  C C      . PRO C 2 17  ? 30.632  -2.700  34.653 1.00 58.89  ? 35  PRO C C      1 
ATOM   5865  O O      . PRO C 2 17  ? 30.070  -3.465  35.417 1.00 60.96  ? 35  PRO C O      1 
ATOM   5866  C CB     . PRO C 2 17  ? 29.944  -3.638  32.495 1.00 66.07  ? 35  PRO C CB     1 
ATOM   5867  C CG     . PRO C 2 17  ? 31.268  -3.695  31.834 1.00 63.34  ? 35  PRO C CG     1 
ATOM   5868  C CD     . PRO C 2 17  ? 31.555  -2.273  31.471 1.00 59.79  ? 35  PRO C CD     1 
ATOM   5869  N N      . LYS C 2 18  ? 31.780  -2.127  34.934 1.00 55.85  ? 36  LYS C N      1 
ATOM   5870  C CA     . LYS C 2 18  ? 32.483  -2.430  36.156 1.00 57.61  ? 36  LYS C CA     1 
ATOM   5871  C C      . LYS C 2 18  ? 32.281  -1.323  37.139 1.00 52.90  ? 36  LYS C C      1 
ATOM   5872  O O      . LYS C 2 18  ? 33.054  -1.161  38.065 1.00 57.76  ? 36  LYS C O      1 
ATOM   5873  C CB     . LYS C 2 18  ? 33.957  -2.623  35.882 1.00 64.08  ? 36  LYS C CB     1 
ATOM   5874  C CG     . LYS C 2 18  ? 34.264  -3.757  34.922 1.00 62.37  ? 36  LYS C CG     1 
ATOM   5875  C CD     . LYS C 2 18  ? 35.622  -4.370  35.215 1.00 57.66  ? 36  LYS C CD     1 
ATOM   5876  C CE     . LYS C 2 18  ? 36.706  -3.308  35.258 1.00 63.47  ? 36  LYS C CE     1 
ATOM   5877  N NZ     . LYS C 2 18  ? 38.023  -3.866  35.668 1.00 49.54  ? 36  LYS C NZ     1 
ATOM   5878  N N      . LEU C 2 19  ? 31.269  -0.515  36.901 1.00 48.83  ? 37  LEU C N      1 
ATOM   5879  C CA     . LEU C 2 19  ? 30.996  0.582   37.782 1.00 53.79  ? 37  LEU C CA     1 
ATOM   5880  C C      . LEU C 2 19  ? 30.590  0.086   39.139 1.00 57.91  ? 37  LEU C C      1 
ATOM   5881  O O      . LEU C 2 19  ? 29.875  -0.900  39.249 1.00 56.05  ? 37  LEU C O      1 
ATOM   5882  C CB     . LEU C 2 19  ? 29.931  1.488   37.192 1.00 48.75  ? 37  LEU C CB     1 
ATOM   5883  C CG     . LEU C 2 19  ? 30.155  2.978   37.416 1.00 52.58  ? 37  LEU C CG     1 
ATOM   5884  C CD1    . LEU C 2 19  ? 31.200  3.485   36.443 1.00 50.83  ? 37  LEU C CD1    1 
ATOM   5885  C CD2    . LEU C 2 19  ? 28.856  3.732   37.232 1.00 53.83  ? 37  LEU C CD2    1 
ATOM   5886  N N      . ASP C 2 20  ? 31.028  0.783   40.182 1.00 58.71  ? 38  ASP C N      1 
ATOM   5887  C CA     . ASP C 2 20  ? 30.747  0.376   41.541 1.00 51.66  ? 38  ASP C CA     1 
ATOM   5888  C C      . ASP C 2 20  ? 30.147  1.547   42.228 1.00 52.07  ? 38  ASP C C      1 
ATOM   5889  O O      . ASP C 2 20  ? 30.200  2.649   41.716 1.00 54.38  ? 38  ASP C O      1 
ATOM   5890  C CB     . ASP C 2 20  ? 31.990  -0.160  42.270 1.00 54.59  ? 38  ASP C CB     1 
ATOM   5891  C CG     . ASP C 2 20  ? 33.212  0.689   42.083 1.00 57.31  ? 38  ASP C CG     1 
ATOM   5892  O OD1    . ASP C 2 20  ? 33.256  1.787   42.647 1.00 52.53  ? 38  ASP C OD1    1 
ATOM   5893  O OD2    . ASP C 2 20  ? 34.160  0.234   41.419 1.00 58.68  ? 38  ASP C OD2    1 
ATOM   5894  N N      . GLU C 2 21  ? 29.571  1.335   43.387 1.00 51.99  ? 39  GLU C N      1 
ATOM   5895  C CA     . GLU C 2 21  ? 28.873  2.406   44.043 1.00 55.23  ? 39  GLU C CA     1 
ATOM   5896  C C      . GLU C 2 21  ? 29.822  3.534   44.273 1.00 50.78  ? 39  GLU C C      1 
ATOM   5897  O O      . GLU C 2 21  ? 29.459  4.688   44.168 1.00 50.83  ? 39  GLU C O      1 
ATOM   5898  C CB     . GLU C 2 21  ? 28.281  1.918   45.352 1.00 52.91  ? 39  GLU C CB     1 
ATOM   5899  C CG     . GLU C 2 21  ? 27.130  0.955   45.167 1.00 53.40  ? 39  GLU C CG     1 
ATOM   5900  C CD     . GLU C 2 21  ? 26.449  0.608   46.467 1.00 61.05  ? 39  GLU C CD     1 
ATOM   5901  O OE1    . GLU C 2 21  ? 27.157  0.246   47.425 1.00 64.33  ? 39  GLU C OE1    1 
ATOM   5902  O OE2    . GLU C 2 21  ? 25.206  0.685   46.523 1.00 59.13  ? 39  GLU C OE2    1 
ATOM   5903  N N      . SER C 2 22  ? 31.049  3.212   44.585 1.00 51.23  ? 40  SER C N      1 
ATOM   5904  C CA     . SER C 2 22  ? 31.987  4.235   44.863 1.00 48.84  ? 40  SER C CA     1 
ATOM   5905  C C      . SER C 2 22  ? 32.155  5.076   43.642 1.00 57.55  ? 40  SER C C      1 
ATOM   5906  O O      . SER C 2 22  ? 32.175  6.287   43.738 1.00 64.62  ? 40  SER C O      1 
ATOM   5907  C CB     . SER C 2 22  ? 33.310  3.610   45.245 1.00 48.50  ? 40  SER C CB     1 
ATOM   5908  O OG     . SER C 2 22  ? 33.123  2.509   46.111 1.00 52.80  ? 40  SER C OG     1 
ATOM   5909  N N      . ASP C 2 23  ? 32.248  4.465   42.475 1.00 59.05  ? 41  ASP C N      1 
ATOM   5910  C CA     . ASP C 2 23  ? 32.510  5.227   41.266 1.00 53.47  ? 41  ASP C CA     1 
ATOM   5911  C C      . ASP C 2 23  ? 31.396  6.192   40.939 1.00 52.03  ? 41  ASP C C      1 
ATOM   5912  O O      . ASP C 2 23  ? 31.653  7.311   40.551 1.00 55.05  ? 41  ASP C O      1 
ATOM   5913  C CB     . ASP C 2 23  ? 32.781  4.299   40.096 1.00 57.73  ? 41  ASP C CB     1 
ATOM   5914  C CG     . ASP C 2 23  ? 34.063  3.522   40.252 1.00 66.08  ? 41  ASP C CG     1 
ATOM   5915  O OD1    . ASP C 2 23  ? 34.785  3.763   41.231 1.00 66.00  ? 41  ASP C OD1    1 
ATOM   5916  O OD2    . ASP C 2 23  ? 34.354  2.663   39.399 1.00 66.79  ? 41  ASP C OD2    1 
ATOM   5917  N N      . PHE C 2 24  ? 30.158  5.777   41.121 1.00 45.68  ? 42  PHE C N      1 
ATOM   5918  C CA     . PHE C 2 24  ? 29.039  6.620   40.799 1.00 42.11  ? 42  PHE C CA     1 
ATOM   5919  C C      . PHE C 2 24  ? 29.149  7.830   41.665 1.00 49.75  ? 42  PHE C C      1 
ATOM   5920  O O      . PHE C 2 24  ? 28.993  8.923   41.187 1.00 51.68  ? 42  PHE C O      1 
ATOM   5921  C CB     . PHE C 2 24  ? 27.782  5.862   41.137 1.00 39.02  ? 42  PHE C CB     1 
ATOM   5922  C CG     . PHE C 2 24  ? 26.513  6.607   40.931 1.00 37.89  ? 42  PHE C CG     1 
ATOM   5923  C CD1    . PHE C 2 24  ? 25.885  6.583   39.714 1.00 46.59  ? 42  PHE C CD1    1 
ATOM   5924  C CD2    . PHE C 2 24  ? 25.902  7.252   41.985 1.00 45.14  ? 42  PHE C CD2    1 
ATOM   5925  C CE1    . PHE C 2 24  ? 24.694  7.235   39.535 1.00 56.44  ? 42  PHE C CE1    1 
ATOM   5926  C CE2    . PHE C 2 24  ? 24.714  7.915   41.813 1.00 51.94  ? 42  PHE C CE2    1 
ATOM   5927  C CZ     . PHE C 2 24  ? 24.108  7.907   40.582 1.00 61.62  ? 42  PHE C CZ     1 
ATOM   5928  N N      . ILE C 2 25  ? 29.478  7.659   42.930 1.00 48.47  ? 43  ILE C N      1 
ATOM   5929  C CA     . ILE C 2 25  ? 29.517  8.787   43.840 1.00 44.80  ? 43  ILE C CA     1 
ATOM   5930  C C      . ILE C 2 25  ? 30.649  9.722   43.501 1.00 44.94  ? 43  ILE C C      1 
ATOM   5931  O O      . ILE C 2 25  ? 30.492  10.922  43.556 1.00 48.88  ? 43  ILE C O      1 
ATOM   5932  C CB     . ILE C 2 25  ? 29.605  8.307   45.284 1.00 39.33  ? 43  ILE C CB     1 
ATOM   5933  C CG1    . ILE C 2 25  ? 28.378  7.474   45.617 1.00 41.12  ? 43  ILE C CG1    1 
ATOM   5934  C CG2    . ILE C 2 25  ? 29.695  9.472   46.250 1.00 46.19  ? 43  ILE C CG2    1 
ATOM   5935  C CD1    . ILE C 2 25  ? 28.371  6.986   47.039 1.00 44.83  ? 43  ILE C CD1    1 
ATOM   5936  N N      . LEU C 2 26  ? 31.781  9.185   43.107 1.00 41.21  ? 44  LEU C N      1 
ATOM   5937  C CA     . LEU C 2 26  ? 32.892  10.013  42.711 1.00 40.66  ? 44  LEU C CA     1 
ATOM   5938  C C      . LEU C 2 26  ? 32.600  10.724  41.422 1.00 43.71  ? 44  LEU C C      1 
ATOM   5939  O O      . LEU C 2 26  ? 32.729  11.929  41.347 1.00 43.94  ? 44  LEU C O      1 
ATOM   5940  C CB     . LEU C 2 26  ? 34.131  9.167   42.590 1.00 40.61  ? 44  LEU C CB     1 
ATOM   5941  C CG     . LEU C 2 26  ? 34.784  8.762   43.894 1.00 41.60  ? 44  LEU C CG     1 
ATOM   5942  C CD1    . LEU C 2 26  ? 35.694  7.590   43.631 1.00 47.80  ? 44  LEU C CD1    1 
ATOM   5943  C CD2    . LEU C 2 26  ? 35.579  9.925   44.440 1.00 40.10  ? 44  LEU C CD2    1 
ATOM   5944  N N      . LEU C 2 27  ? 32.173  9.996   40.411 1.00 44.84  ? 45  LEU C N      1 
ATOM   5945  C CA     . LEU C 2 27  ? 31.811  10.592  39.129 1.00 47.62  ? 45  LEU C CA     1 
ATOM   5946  C C      . LEU C 2 27  ? 30.605  11.513  39.157 1.00 45.00  ? 45  LEU C C      1 
ATOM   5947  O O      . LEU C 2 27  ? 30.618  12.547  38.520 1.00 42.74  ? 45  LEU C O      1 
ATOM   5948  C CB     . LEU C 2 27  ? 31.520  9.492   38.116 1.00 48.08  ? 45  LEU C CB     1 
ATOM   5949  C CG     . LEU C 2 27  ? 32.645  8.692   37.473 1.00 53.92  ? 45  LEU C CG     1 
ATOM   5950  C CD1    . LEU C 2 27  ? 32.090  7.422   36.854 1.00 48.83  ? 45  LEU C CD1    1 
ATOM   5951  C CD2    . LEU C 2 27  ? 33.337  9.535   36.423 1.00 58.35  ? 45  LEU C CD2    1 
ATOM   5952  N N      . SER C 2 28  ? 29.536  11.122  39.834 1.00 38.08  ? 46  SER C N      1 
ATOM   5953  C CA     . SER C 2 28  ? 28.336  11.918  39.834 1.00 37.15  ? 46  SER C CA     1 
ATOM   5954  C C      . SER C 2 28  ? 28.636  13.256  40.365 1.00 45.39  ? 46  SER C C      1 
ATOM   5955  O O      . SER C 2 28  ? 28.285  14.253  39.770 1.00 48.82  ? 46  SER C O      1 
ATOM   5956  C CB     . SER C 2 28  ? 27.306  11.328  40.731 1.00 35.35  ? 46  SER C CB     1 
ATOM   5957  O OG     . SER C 2 28  ? 26.064  11.921  40.447 1.00 47.83  ? 46  SER C OG     1 
ATOM   5958  N N      . VAL C 2 29  ? 29.263  13.296  41.521 1.00 45.35  ? 47  VAL C N      1 
ATOM   5959  C CA     . VAL C 2 29  ? 29.587  14.554  42.138 1.00 39.94  ? 47  VAL C CA     1 
ATOM   5960  C C      . VAL C 2 29  ? 30.341  15.423  41.169 1.00 45.75  ? 47  VAL C C      1 
ATOM   5961  O O      . VAL C 2 29  ? 30.163  16.613  41.154 1.00 52.39  ? 47  VAL C O      1 
ATOM   5962  C CB     . VAL C 2 29  ? 30.347  14.340  43.434 1.00 35.84  ? 47  VAL C CB     1 
ATOM   5963  C CG1    . VAL C 2 29  ? 31.006  15.619  43.912 1.00 43.71  ? 47  VAL C CG1    1 
ATOM   5964  C CG2    . VAL C 2 29  ? 29.409  13.812  44.500 1.00 42.07  ? 47  VAL C CG2    1 
ATOM   5965  N N      . LYS C 2 30  ? 31.143  14.840  40.303 1.00 48.90  ? 48  LYS C N      1 
ATOM   5966  C CA     . LYS C 2 30  ? 31.968  15.653  39.416 1.00 49.67  ? 48  LYS C CA     1 
ATOM   5967  C C      . LYS C 2 30  ? 31.106  16.406  38.478 1.00 53.10  ? 48  LYS C C      1 
ATOM   5968  O O      . LYS C 2 30  ? 31.304  17.587  38.257 1.00 56.80  ? 48  LYS C O      1 
ATOM   5969  C CB     . LYS C 2 30  ? 32.942  14.807  38.610 1.00 47.47  ? 48  LYS C CB     1 
ATOM   5970  C CG     . LYS C 2 30  ? 33.956  15.614  37.824 1.00 49.23  ? 48  LYS C CG     1 
ATOM   5971  C CD     . LYS C 2 30  ? 34.945  14.720  37.101 1.00 63.32  ? 48  LYS C CD     1 
ATOM   5972  C CE     . LYS C 2 30  ? 35.977  15.556  36.364 1.00 68.23  ? 48  LYS C CE     1 
ATOM   5973  N NZ     . LYS C 2 30  ? 36.970  14.730  35.629 1.00 64.64  ? 48  LYS C NZ     1 
ATOM   5974  N N      . TYR C 2 31  ? 30.179  15.704  37.865 1.00 52.44  ? 49  TYR C N      1 
ATOM   5975  C CA     . TYR C 2 31  ? 29.358  16.331  36.874 1.00 53.66  ? 49  TYR C CA     1 
ATOM   5976  C C      . TYR C 2 31  ? 28.712  17.379  37.657 1.00 52.89  ? 49  TYR C C      1 
ATOM   5977  O O      . TYR C 2 31  ? 28.677  18.522  37.252 1.00 57.92  ? 49  TYR C O      1 
ATOM   5978  C CB     . TYR C 2 31  ? 28.337  15.338  36.335 1.00 51.32  ? 49  TYR C CB     1 
ATOM   5979  C CG     . TYR C 2 31  ? 27.175  15.939  35.611 1.00 50.93  ? 49  TYR C CG     1 
ATOM   5980  C CD1    . TYR C 2 31  ? 27.370  16.785  34.546 1.00 58.58  ? 49  TYR C CD1    1 
ATOM   5981  C CD2    . TYR C 2 31  ? 25.878  15.638  35.982 1.00 49.97  ? 49  TYR C CD2    1 
ATOM   5982  C CE1    . TYR C 2 31  ? 26.308  17.338  33.879 1.00 71.39  ? 49  TYR C CE1    1 
ATOM   5983  C CE2    . TYR C 2 31  ? 24.807  16.183  35.315 1.00 60.66  ? 49  TYR C CE2    1 
ATOM   5984  C CZ     . TYR C 2 31  ? 25.035  17.033  34.262 1.00 76.76  ? 49  TYR C CZ     1 
ATOM   5985  O OH     . TYR C 2 31  ? 23.988  17.592  33.585 1.00 86.66  ? 49  TYR C OH     1 
ATOM   5986  N N      . LEU C 2 32  ? 28.234  17.015  38.820 1.00 47.31  ? 50  LEU C N      1 
ATOM   5987  C CA     . LEU C 2 32  ? 27.481  17.974  39.562 1.00 49.82  ? 50  LEU C CA     1 
ATOM   5988  C C      . LEU C 2 32  ? 28.343  19.139  39.911 1.00 52.33  ? 50  LEU C C      1 
ATOM   5989  O O      . LEU C 2 32  ? 27.893  20.258  39.882 1.00 55.97  ? 50  LEU C O      1 
ATOM   5990  C CB     . LEU C 2 32  ? 26.830  17.348  40.780 1.00 52.93  ? 50  LEU C CB     1 
ATOM   5991  C CG     . LEU C 2 32  ? 25.768  16.298  40.492 1.00 49.77  ? 50  LEU C CG     1 
ATOM   5992  C CD1    . LEU C 2 32  ? 25.172  15.787  41.789 1.00 51.47  ? 50  LEU C CD1    1 
ATOM   5993  C CD2    . LEU C 2 32  ? 24.695  16.892  39.605 1.00 49.87  ? 50  LEU C CD2    1 
ATOM   5994  N N      . GLU C 2 33  ? 29.581  18.906  40.268 1.00 51.59  ? 51  GLU C N      1 
ATOM   5995  C CA     . GLU C 2 33  ? 30.370  20.026  40.688 1.00 57.06  ? 51  GLU C CA     1 
ATOM   5996  C C      . GLU C 2 33  ? 30.586  20.992  39.568 1.00 68.53  ? 51  GLU C C      1 
ATOM   5997  O O      . GLU C 2 33  ? 30.408  22.182  39.741 1.00 77.98  ? 51  GLU C O      1 
ATOM   5998  C CB     . GLU C 2 33  ? 31.727  19.566  41.190 1.00 61.25  ? 51  GLU C CB     1 
ATOM   5999  C CG     . GLU C 2 33  ? 32.418  20.581  42.082 1.00 71.35  ? 51  GLU C CG     1 
ATOM   6000  C CD     . GLU C 2 33  ? 33.791  20.130  42.534 1.00 84.36  ? 51  GLU C CD     1 
ATOM   6001  O OE1    . GLU C 2 33  ? 34.363  19.230  41.889 1.00 86.94  ? 51  GLU C OE1    1 
ATOM   6002  O OE2    . GLU C 2 33  ? 34.301  20.684  43.531 1.00 71.76  ? 51  GLU C OE2    1 
ATOM   6003  N N      . LYS C 2 34  ? 30.980  20.492  38.405 1.00 65.02  ? 52  LYS C N      1 
ATOM   6004  C CA     . LYS C 2 34  ? 31.251  21.373  37.280 1.00 63.79  ? 52  LYS C CA     1 
ATOM   6005  C C      . LYS C 2 34  ? 30.027  22.001  36.689 1.00 59.77  ? 52  LYS C C      1 
ATOM   6006  O O      . LYS C 2 34  ? 29.978  23.203  36.473 1.00 58.06  ? 52  LYS C O      1 
ATOM   6007  C CB     . LYS C 2 34  ? 31.997  20.628  36.189 1.00 56.39  ? 52  LYS C CB     1 
ATOM   6008  C CG     . LYS C 2 34  ? 33.348  21.236  35.867 1.00 63.00  ? 52  LYS C CG     1 
ATOM   6009  C CD     . LYS C 2 34  ? 33.973  20.589  34.647 1.00 66.72  ? 52  LYS C CD     1 
ATOM   6010  C CE     . LYS C 2 34  ? 35.295  21.247  34.300 1.00 73.64  ? 52  LYS C CE     1 
ATOM   6011  N NZ     . LYS C 2 34  ? 36.303  21.045  35.376 1.00 71.30  ? 52  LYS C NZ     1 
ATOM   6012  N N      . SER C 2 35  ? 29.046  21.186  36.379 1.00 59.20  ? 53  SER C N      1 
ATOM   6013  C CA     . SER C 2 35  ? 27.849  21.693  35.788 1.00 58.05  ? 53  SER C CA     1 
ATOM   6014  C C      . SER C 2 35  ? 27.249  22.729  36.667 1.00 60.26  ? 53  SER C C      1 
ATOM   6015  O O      . SER C 2 35  ? 27.059  23.858  36.243 1.00 72.63  ? 53  SER C O      1 
ATOM   6016  C CB     . SER C 2 35  ? 26.848  20.572  35.642 1.00 56.35  ? 53  SER C CB     1 
ATOM   6017  O OG     . SER C 2 35  ? 25.658  21.025  35.038 1.00 64.85  ? 53  SER C OG     1 
ATOM   6018  N N      . LEU C 2 36  ? 26.953  22.375  37.899 1.00 57.01  ? 54  LEU C N      1 
ATOM   6019  C CA     . LEU C 2 36  ? 26.243  23.277  38.773 1.00 60.25  ? 54  LEU C CA     1 
ATOM   6020  C C      . LEU C 2 36  ? 27.131  24.425  39.026 1.00 72.40  ? 54  LEU C C      1 
ATOM   6021  O O      . LEU C 2 36  ? 26.685  25.551  39.134 1.00 85.69  ? 54  LEU C O      1 
ATOM   6022  C CB     . LEU C 2 36  ? 25.771  22.607  40.037 1.00 62.31  ? 54  LEU C CB     1 
ATOM   6023  C CG     . LEU C 2 36  ? 24.612  21.685  39.698 1.00 68.20  ? 54  LEU C CG     1 
ATOM   6024  C CD1    . LEU C 2 36  ? 24.439  20.634  40.764 1.00 69.37  ? 54  LEU C CD1    1 
ATOM   6025  C CD2    . LEU C 2 36  ? 23.335  22.473  39.484 1.00 73.15  ? 54  LEU C CD2    1 
ATOM   6026  N N      . GLY C 2 37  ? 28.408  24.142  39.140 1.00 73.70  ? 55  GLY C N      1 
ATOM   6027  C CA     . GLY C 2 37  ? 29.364  25.203  39.342 1.00 77.32  ? 55  GLY C CA     1 
ATOM   6028  C C      . GLY C 2 37  ? 29.408  25.646  40.772 1.00 85.40  ? 55  GLY C C      1 
ATOM   6029  O O      . GLY C 2 37  ? 28.835  25.009  41.651 1.00 82.80  ? 55  GLY C O      1 
ATOM   6030  N N      . LYS C 2 38  ? 30.095  26.748  41.012 1.00 92.68  ? 56  LYS C N      1 
ATOM   6031  C CA     . LYS C 2 38  ? 30.215  27.255  42.383 1.00 101.17 ? 56  LYS C CA     1 
ATOM   6032  C C      . LYS C 2 38  ? 29.139  28.228  42.770 1.00 95.79  ? 56  LYS C C      1 
ATOM   6033  O O      . LYS C 2 38  ? 29.391  29.418  42.917 1.00 92.94  ? 56  LYS C O      1 
ATOM   6034  C CB     . LYS C 2 38  ? 31.558  27.953  42.596 1.00 94.50  ? 56  LYS C CB     1 
ATOM   6035  C CG     . LYS C 2 38  ? 32.744  27.026  42.790 1.00 98.23  ? 56  LYS C CG     1 
ATOM   6036  C CD     . LYS C 2 38  ? 33.933  27.791  43.349 1.00 81.76  ? 56  LYS C CD     1 
ATOM   6037  C CE     . LYS C 2 38  ? 35.178  26.923  43.438 1.00 84.68  ? 56  LYS C CE     1 
ATOM   6038  N NZ     . LYS C 2 38  ? 35.736  26.588  42.100 1.00 61.01  ? 56  LYS C NZ     1 
ATOM   6039  N N      . LYS C 2 39  ? 27.924  27.750  42.906 1.00 96.37  ? 57  LYS C N      1 
ATOM   6040  C CA     . LYS C 2 39  ? 26.859  28.630  43.310 1.00 93.71  ? 57  LYS C CA     1 
ATOM   6041  C C      . LYS C 2 39  ? 26.856  28.682  44.815 1.00 94.73  ? 57  LYS C C      1 
ATOM   6042  O O      . LYS C 2 39  ? 26.394  29.667  45.390 1.00 98.10  ? 57  LYS C O      1 
ATOM   6043  C CB     . LYS C 2 39  ? 25.524  28.163  42.747 1.00 89.05  ? 57  LYS C CB     1 
ATOM   6044  C CG     . LYS C 2 39  ? 25.531  28.005  41.237 1.00 87.95  ? 57  LYS C CG     1 
ATOM   6045  C CD     . LYS C 2 39  ? 25.892  29.307  40.541 1.00 85.82  ? 57  LYS C CD     1 
ATOM   6046  C CE     . LYS C 2 39  ? 26.206  29.085  39.070 1.00 78.00  ? 57  LYS C CE     1 
ATOM   6047  N NZ     . LYS C 2 39  ? 27.494  28.365  38.876 1.00 72.07  ? 57  LYS C NZ     1 
ATOM   6048  N N      . LYS C 2 40  ? 27.478  27.688  45.444 1.00 82.54  ? 58  LYS C N      1 
ATOM   6049  C CA     . LYS C 2 40  ? 27.587  27.644  46.902 1.00 82.88  ? 58  LYS C CA     1 
ATOM   6050  C C      . LYS C 2 40  ? 26.253  27.509  47.554 1.00 81.05  ? 58  LYS C C      1 
ATOM   6051  O O      . LYS C 2 40  ? 26.161  27.351  48.762 1.00 76.79  ? 58  LYS C O      1 
ATOM   6052  C CB     . LYS C 2 40  ? 28.418  28.793  47.475 1.00 85.21  ? 58  LYS C CB     1 
ATOM   6053  C CG     . LYS C 2 40  ? 29.876  28.748  47.061 1.00 81.68  ? 58  LYS C CG     1 
ATOM   6054  C CD     . LYS C 2 40  ? 30.629  29.965  47.559 1.00 84.31  ? 58  LYS C CD     1 
ATOM   6055  C CE     . LYS C 2 40  ? 32.098  29.883  47.185 1.00 85.88  ? 58  LYS C CE     1 
ATOM   6056  N NZ     . LYS C 2 40  ? 32.278  29.766  45.714 1.00 83.51  ? 58  LYS C NZ     1 
ATOM   6057  N N      . GLU C 2 41  ? 25.198  27.536  46.769 1.00 82.43  ? 59  GLU C N      1 
ATOM   6058  C CA     . GLU C 2 41  ? 23.906  27.267  47.344 1.00 84.09  ? 59  GLU C CA     1 
ATOM   6059  C C      . GLU C 2 41  ? 24.006  25.783  47.534 1.00 89.44  ? 59  GLU C C      1 
ATOM   6060  O O      . GLU C 2 41  ? 23.332  25.202  48.380 1.00 88.00  ? 59  GLU C O      1 
ATOM   6061  C CB     . GLU C 2 41  ? 22.817  27.549  46.328 1.00 80.20  ? 59  GLU C CB     1 
ATOM   6062  C CG     . GLU C 2 41  ? 23.058  28.791  45.494 1.00 88.00  ? 59  GLU C CG     1 
ATOM   6063  C CD     . GLU C 2 41  ? 22.130  28.874  44.302 1.00 93.83  ? 59  GLU C CD     1 
ATOM   6064  O OE1    . GLU C 2 41  ? 21.187  28.061  44.226 1.00 92.57  ? 59  GLU C OE1    1 
ATOM   6065  O OE2    . GLU C 2 41  ? 22.342  29.753  43.443 1.00 97.24  ? 59  GLU C OE2    1 
ATOM   6066  N N      . PHE C 2 42  ? 24.900  25.157  46.777 1.00 89.07  ? 60  PHE C N      1 
ATOM   6067  C CA     . PHE C 2 42  ? 25.017  23.710  46.816 1.00 80.05  ? 60  PHE C CA     1 
ATOM   6068  C C      . PHE C 2 42  ? 26.297  23.294  47.468 1.00 74.92  ? 60  PHE C C      1 
ATOM   6069  O O      . PHE C 2 42  ? 26.685  22.143  47.394 1.00 72.34  ? 60  PHE C O      1 
ATOM   6070  C CB     . PHE C 2 42  ? 25.067  23.178  45.399 1.00 81.30  ? 60  PHE C CB     1 
ATOM   6071  C CG     . PHE C 2 42  ? 24.115  23.843  44.448 1.00 82.61  ? 60  PHE C CG     1 
ATOM   6072  C CD1    . PHE C 2 42  ? 22.759  23.894  44.710 1.00 86.71  ? 60  PHE C CD1    1 
ATOM   6073  C CD2    . PHE C 2 42  ? 24.579  24.371  43.263 1.00 82.96  ? 60  PHE C CD2    1 
ATOM   6074  C CE1    . PHE C 2 42  ? 21.890  24.487  43.820 1.00 85.76  ? 60  PHE C CE1    1 
ATOM   6075  C CE2    . PHE C 2 42  ? 23.715  24.964  42.368 1.00 87.44  ? 60  PHE C CE2    1 
ATOM   6076  C CZ     . PHE C 2 42  ? 22.368  25.024  42.646 1.00 85.78  ? 60  PHE C CZ     1 
ATOM   6077  N N      . SER C 2 43  ? 26.970  24.230  48.102 1.00 73.58  ? 61  SER C N      1 
ATOM   6078  C CA     . SER C 2 43  ? 28.237  23.935  48.726 1.00 74.70  ? 61  SER C CA     1 
ATOM   6079  C C      . SER C 2 43  ? 28.115  22.823  49.714 1.00 70.90  ? 61  SER C C      1 
ATOM   6080  O O      . SER C 2 43  ? 28.930  21.921  49.735 1.00 72.41  ? 61  SER C O      1 
ATOM   6081  C CB     . SER C 2 43  ? 28.765  25.171  49.442 1.00 76.58  ? 61  SER C CB     1 
ATOM   6082  O OG     . SER C 2 43  ? 27.851  25.628  50.420 1.00 74.76  ? 61  SER C OG     1 
ATOM   6083  N N      . GLY C 2 44  ? 27.099  22.865  50.546 1.00 70.54  ? 62  GLY C N      1 
ATOM   6084  C CA     . GLY C 2 44  ? 26.991  21.868  51.586 1.00 72.99  ? 62  GLY C CA     1 
ATOM   6085  C C      . GLY C 2 44  ? 26.718  20.478  51.087 1.00 68.30  ? 62  GLY C C      1 
ATOM   6086  O O      . GLY C 2 44  ? 27.062  19.514  51.750 1.00 64.67  ? 62  GLY C O      1 
ATOM   6087  N N      . PHE C 2 45  ? 26.102  20.364  49.924 1.00 63.42  ? 63  PHE C N      1 
ATOM   6088  C CA     . PHE C 2 45  ? 25.759  19.073  49.387 1.00 54.88  ? 63  PHE C CA     1 
ATOM   6089  C C      . PHE C 2 45  ? 27.004  18.328  49.199 1.00 54.74  ? 63  PHE C C      1 
ATOM   6090  O O      . PHE C 2 45  ? 27.190  17.264  49.738 1.00 59.35  ? 63  PHE C O      1 
ATOM   6091  C CB     . PHE C 2 45  ? 25.138  19.260  48.023 1.00 60.43  ? 63  PHE C CB     1 
ATOM   6092  C CG     . PHE C 2 45  ? 24.846  17.986  47.307 1.00 60.69  ? 63  PHE C CG     1 
ATOM   6093  C CD1    . PHE C 2 45  ? 23.898  17.112  47.786 1.00 64.91  ? 63  PHE C CD1    1 
ATOM   6094  C CD2    . PHE C 2 45  ? 25.503  17.680  46.137 1.00 58.70  ? 63  PHE C CD2    1 
ATOM   6095  C CE1    . PHE C 2 45  ? 23.625  15.942  47.122 1.00 66.33  ? 63  PHE C CE1    1 
ATOM   6096  C CE2    . PHE C 2 45  ? 25.241  16.513  45.465 1.00 61.25  ? 63  PHE C CE2    1 
ATOM   6097  C CZ     . PHE C 2 45  ? 24.298  15.644  45.959 1.00 68.80  ? 63  PHE C CZ     1 
ATOM   6098  N N      . PHE C 2 46  ? 27.883  18.894  48.418 1.00 53.90  ? 64  PHE C N      1 
ATOM   6099  C CA     . PHE C 2 46  ? 29.084  18.199  48.097 1.00 54.84  ? 64  PHE C CA     1 
ATOM   6100  C C      . PHE C 2 46  ? 29.818  17.819  49.324 1.00 56.94  ? 64  PHE C C      1 
ATOM   6101  O O      . PHE C 2 46  ? 30.214  16.682  49.476 1.00 64.52  ? 64  PHE C O      1 
ATOM   6102  C CB     . PHE C 2 46  ? 29.937  19.082  47.214 1.00 64.89  ? 64  PHE C CB     1 
ATOM   6103  C CG     . PHE C 2 46  ? 29.270  19.451  45.921 1.00 66.32  ? 64  PHE C CG     1 
ATOM   6104  C CD1    . PHE C 2 46  ? 28.783  18.470  45.081 1.00 57.33  ? 64  PHE C CD1    1 
ATOM   6105  C CD2    . PHE C 2 46  ? 29.125  20.770  45.552 1.00 59.11  ? 64  PHE C CD2    1 
ATOM   6106  C CE1    . PHE C 2 46  ? 28.161  18.794  43.900 1.00 49.57  ? 64  PHE C CE1    1 
ATOM   6107  C CE2    . PHE C 2 46  ? 28.504  21.103  44.369 1.00 63.80  ? 64  PHE C CE2    1 
ATOM   6108  C CZ     . PHE C 2 46  ? 28.021  20.113  43.541 1.00 61.73  ? 64  PHE C CZ     1 
ATOM   6109  N N      . GLU C 2 47  ? 30.001  18.757  50.223 1.00 61.58  ? 65  GLU C N      1 
ATOM   6110  C CA     . GLU C 2 47  ? 30.794  18.474  51.400 1.00 59.73  ? 65  GLU C CA     1 
ATOM   6111  C C      . GLU C 2 47  ? 30.217  17.384  52.270 1.00 56.33  ? 65  GLU C C      1 
ATOM   6112  O O      . GLU C 2 47  ? 30.968  16.612  52.831 1.00 57.24  ? 65  GLU C O      1 
ATOM   6113  C CB     . GLU C 2 47  ? 31.047  19.743  52.185 1.00 64.41  ? 65  GLU C CB     1 
ATOM   6114  C CG     . GLU C 2 47  ? 31.895  20.747  51.426 1.00 77.56  ? 65  GLU C CG     1 
ATOM   6115  C CD     . GLU C 2 47  ? 31.538  22.182  51.749 1.00 81.99  ? 65  GLU C CD     1 
ATOM   6116  O OE1    . GLU C 2 47  ? 30.557  22.401  52.488 1.00 79.33  ? 65  GLU C OE1    1 
ATOM   6117  O OE2    . GLU C 2 47  ? 32.234  23.091  51.252 1.00 85.30  ? 65  GLU C OE2    1 
ATOM   6118  N N      . ASP C 2 48  ? 28.901  17.285  52.384 1.00 55.46  ? 66  ASP C N      1 
ATOM   6119  C CA     . ASP C 2 48  ? 28.339  16.196  53.153 1.00 50.10  ? 66  ASP C CA     1 
ATOM   6120  C C      . ASP C 2 48  ? 28.627  14.948  52.421 1.00 56.97  ? 66  ASP C C      1 
ATOM   6121  O O      . ASP C 2 48  ? 28.992  13.959  53.016 1.00 64.86  ? 66  ASP C O      1 
ATOM   6122  C CB     . ASP C 2 48  ? 26.845  16.300  53.335 1.00 50.83  ? 66  ASP C CB     1 
ATOM   6123  C CG     . ASP C 2 48  ? 26.330  15.378  54.412 1.00 58.31  ? 66  ASP C CG     1 
ATOM   6124  O OD1    . ASP C 2 48  ? 27.062  15.131  55.389 1.00 57.52  ? 66  ASP C OD1    1 
ATOM   6125  O OD2    . ASP C 2 48  ? 25.185  14.908  54.290 1.00 64.95  ? 66  ASP C OD2    1 
ATOM   6126  N N      . ILE C 2 49  ? 28.402  14.957  51.123 1.00 53.38  ? 67  ILE C N      1 
ATOM   6127  C CA     . ILE C 2 49  ? 28.567  13.741  50.364 1.00 52.50  ? 67  ILE C CA     1 
ATOM   6128  C C      . ILE C 2 49  ? 29.988  13.258  50.522 1.00 54.68  ? 67  ILE C C      1 
ATOM   6129  O O      . ILE C 2 49  ? 30.237  12.069  50.605 1.00 59.84  ? 67  ILE C O      1 
ATOM   6130  C CB     . ILE C 2 49  ? 28.200  13.937  48.895 1.00 51.29  ? 67  ILE C CB     1 
ATOM   6131  C CG1    . ILE C 2 49  ? 26.721  14.257  48.761 1.00 53.88  ? 67  ILE C CG1    1 
ATOM   6132  C CG2    . ILE C 2 49  ? 28.493  12.685  48.090 1.00 54.42  ? 67  ILE C CG2    1 
ATOM   6133  C CD1    . ILE C 2 49  ? 25.828  13.132  49.216 1.00 61.77  ? 67  ILE C CD1    1 
ATOM   6134  N N      . GLU C 2 50  ? 30.930  14.177  50.612 1.00 52.00  ? 68  GLU C N      1 
ATOM   6135  C CA     . GLU C 2 50  ? 32.310  13.781  50.756 1.00 58.53  ? 68  GLU C CA     1 
ATOM   6136  C C      . GLU C 2 50  ? 32.482  13.062  52.057 1.00 55.45  ? 68  GLU C C      1 
ATOM   6137  O O      . GLU C 2 50  ? 33.208  12.087  52.128 1.00 54.58  ? 68  GLU C O      1 
ATOM   6138  C CB     . GLU C 2 50  ? 33.240  14.974  50.667 1.00 59.29  ? 68  GLU C CB     1 
ATOM   6139  C CG     . GLU C 2 50  ? 33.445  15.499  49.260 1.00 51.88  ? 68  GLU C CG     1 
ATOM   6140  C CD     . GLU C 2 50  ? 34.484  16.599  49.196 1.00 62.69  ? 68  GLU C CD     1 
ATOM   6141  O OE1    . GLU C 2 50  ? 35.169  16.839  50.210 1.00 68.33  ? 68  GLU C OE1    1 
ATOM   6142  O OE2    . GLU C 2 50  ? 34.614  17.224  48.128 1.00 67.38  ? 68  GLU C OE2    1 
ATOM   6143  N N      . LYS C 2 51  ? 31.770  13.487  53.081 1.00 50.73  ? 69  LYS C N      1 
ATOM   6144  C CA     . LYS C 2 51  ? 31.851  12.826  54.364 1.00 52.70  ? 69  LYS C CA     1 
ATOM   6145  C C      . LYS C 2 51  ? 31.097  11.533  54.362 1.00 51.84  ? 69  LYS C C      1 
ATOM   6146  O O      . LYS C 2 51  ? 31.551  10.557  54.927 1.00 51.55  ? 69  LYS C O      1 
ATOM   6147  C CB     . LYS C 2 51  ? 31.317  13.730  55.453 1.00 57.19  ? 69  LYS C CB     1 
ATOM   6148  C CG     . LYS C 2 51  ? 32.197  14.946  55.703 1.00 62.25  ? 69  LYS C CG     1 
ATOM   6149  C CD     . LYS C 2 51  ? 31.696  15.802  56.852 1.00 57.38  ? 69  LYS C CD     1 
ATOM   6150  C CE     . LYS C 2 51  ? 30.353  16.432  56.529 1.00 62.40  ? 69  LYS C CE     1 
ATOM   6151  N NZ     . LYS C 2 51  ? 29.940  17.441  57.544 1.00 70.47  ? 69  LYS C NZ     1 
ATOM   6152  N N      . LEU C 2 52  ? 29.941  11.518  53.727 1.00 50.08  ? 70  LEU C N      1 
ATOM   6153  C CA     . LEU C 2 52  ? 29.163  10.308  53.642 1.00 49.82  ? 70  LEU C CA     1 
ATOM   6154  C C      . LEU C 2 52  ? 29.953  9.266   52.894 1.00 51.44  ? 70  LEU C C      1 
ATOM   6155  O O      . LEU C 2 52  ? 29.919  8.098   53.245 1.00 52.68  ? 70  LEU C O      1 
ATOM   6156  C CB     . LEU C 2 52  ? 27.824  10.563  52.972 1.00 41.31  ? 70  LEU C CB     1 
ATOM   6157  C CG     . LEU C 2 52  ? 26.777  11.307  53.792 1.00 43.80  ? 70  LEU C CG     1 
ATOM   6158  C CD1    . LEU C 2 52  ? 25.500  11.453  52.990 1.00 52.33  ? 70  LEU C CD1    1 
ATOM   6159  C CD2    . LEU C 2 52  ? 26.504  10.563  55.085 1.00 52.80  ? 70  LEU C CD2    1 
ATOM   6160  N N      . TYR C 2 53  ? 30.692  9.682   51.875 1.00 51.34  ? 71  TYR C N      1 
ATOM   6161  C CA     . TYR C 2 53  ? 31.510  8.756   51.104 1.00 49.51  ? 71  TYR C CA     1 
ATOM   6162  C C      . TYR C 2 53  ? 32.517  8.149   52.005 1.00 52.04  ? 71  TYR C C      1 
ATOM   6163  O O      . TYR C 2 53  ? 32.700  6.947   52.028 1.00 59.19  ? 71  TYR C O      1 
ATOM   6164  C CB     . TYR C 2 53  ? 32.260  9.483   50.005 1.00 39.38  ? 71  TYR C CB     1 
ATOM   6165  C CG     . TYR C 2 53  ? 33.156  8.612   49.157 1.00 42.57  ? 71  TYR C CG     1 
ATOM   6166  C CD1    . TYR C 2 53  ? 32.637  7.844   48.133 1.00 42.04  ? 71  TYR C CD1    1 
ATOM   6167  C CD2    . TYR C 2 53  ? 34.524  8.581   49.362 1.00 45.60  ? 71  TYR C CD2    1 
ATOM   6168  C CE1    . TYR C 2 53  ? 33.453  7.058   47.350 1.00 44.01  ? 71  TYR C CE1    1 
ATOM   6169  C CE2    . TYR C 2 53  ? 35.345  7.796   48.583 1.00 41.25  ? 71  TYR C CE2    1 
ATOM   6170  C CZ     . TYR C 2 53  ? 34.802  7.039   47.582 1.00 43.74  ? 71  TYR C CZ     1 
ATOM   6171  O OH     . TYR C 2 53  ? 35.616  6.259   46.814 1.00 49.47  ? 71  TYR C OH     1 
ATOM   6172  N N      . PHE C 2 54  ? 33.199  8.975   52.758 1.00 41.50  ? 72  PHE C N      1 
ATOM   6173  C CA     . PHE C 2 54  ? 34.261  8.475   53.575 1.00 40.83  ? 72  PHE C CA     1 
ATOM   6174  C C      . PHE C 2 54  ? 33.757  7.510   54.573 1.00 49.00  ? 72  PHE C C      1 
ATOM   6175  O O      . PHE C 2 54  ? 34.467  6.605   54.975 1.00 57.03  ? 72  PHE C O      1 
ATOM   6176  C CB     . PHE C 2 54  ? 34.902  9.628   54.301 1.00 48.41  ? 72  PHE C CB     1 
ATOM   6177  C CG     . PHE C 2 54  ? 35.829  9.218   55.397 1.00 47.73  ? 72  PHE C CG     1 
ATOM   6178  C CD1    . PHE C 2 54  ? 37.025  8.610   55.108 1.00 43.31  ? 72  PHE C CD1    1 
ATOM   6179  C CD2    . PHE C 2 54  ? 35.502  9.457   56.713 1.00 42.12  ? 72  PHE C CD2    1 
ATOM   6180  C CE1    . PHE C 2 54  ? 37.871  8.231   56.113 1.00 36.49  ? 72  PHE C CE1    1 
ATOM   6181  C CE2    . PHE C 2 54  ? 36.345  9.080   57.723 1.00 37.42  ? 72  PHE C CE2    1 
ATOM   6182  C CZ     . PHE C 2 54  ? 37.534  8.473   57.420 1.00 34.19  ? 72  PHE C CZ     1 
ATOM   6183  N N      . LYS C 2 55  ? 32.532  7.682   55.012 1.00 46.66  ? 73  LYS C N      1 
ATOM   6184  C CA     . LYS C 2 55  ? 32.066  6.827   56.075 1.00 50.67  ? 73  LYS C CA     1 
ATOM   6185  C C      . LYS C 2 55  ? 31.403  5.635   55.482 1.00 50.02  ? 73  LYS C C      1 
ATOM   6186  O O      . LYS C 2 55  ? 30.651  4.945   56.150 1.00 57.64  ? 73  LYS C O      1 
ATOM   6187  C CB     . LYS C 2 55  ? 31.148  7.588   57.008 1.00 47.80  ? 73  LYS C CB     1 
ATOM   6188  C CG     . LYS C 2 55  ? 31.811  8.759   57.709 1.00 42.66  ? 73  LYS C CG     1 
ATOM   6189  C CD     . LYS C 2 55  ? 30.765  9.712   58.256 1.00 46.16  ? 73  LYS C CD     1 
ATOM   6190  C CE     . LYS C 2 55  ? 31.345  11.096  58.485 1.00 48.65  ? 73  LYS C CE     1 
ATOM   6191  N NZ     . LYS C 2 55  ? 30.268  12.108  58.667 1.00 39.96  ? 73  LYS C NZ     1 
ATOM   6192  N N      . GLN C 2 56  ? 31.705  5.372   54.229 1.00 45.83  ? 74  GLN C N      1 
ATOM   6193  C CA     . GLN C 2 56  ? 31.179  4.204   53.563 1.00 47.09  ? 74  GLN C CA     1 
ATOM   6194  C C      . GLN C 2 56  ? 29.694  4.097   53.620 1.00 54.52  ? 74  GLN C C      1 
ATOM   6195  O O      . GLN C 2 56  ? 29.148  3.005   53.572 1.00 54.81  ? 74  GLN C O      1 
ATOM   6196  C CB     . GLN C 2 56  ? 31.883  2.936   54.022 1.00 45.13  ? 74  GLN C CB     1 
ATOM   6197  C CG     . GLN C 2 56  ? 33.329  2.877   53.579 1.00 43.85  ? 74  GLN C CG     1 
ATOM   6198  C CD     . GLN C 2 56  ? 34.051  1.670   54.117 1.00 47.07  ? 74  GLN C CD     1 
ATOM   6199  O OE1    . GLN C 2 56  ? 33.436  0.761   54.660 1.00 44.46  ? 74  GLN C OE1    1 
ATOM   6200  N NE2    . GLN C 2 56  ? 35.366  1.655   53.968 1.00 48.93  ? 74  GLN C NE2    1 
ATOM   6201  N N      . ASN C 2 57  ? 29.013  5.233   53.667 1.00 55.55  ? 75  ASN C N      1 
ATOM   6202  C CA     . ASN C 2 57  ? 27.556  5.224   53.616 1.00 57.96  ? 75  ASN C CA     1 
ATOM   6203  C C      . ASN C 2 57  ? 27.210  5.575   52.214 1.00 57.04  ? 75  ASN C C      1 
ATOM   6204  O O      . ASN C 2 57  ? 26.742  6.665   51.947 1.00 56.97  ? 75  ASN C O      1 
ATOM   6205  C CB     . ASN C 2 57  ? 26.954  6.265   54.539 1.00 58.42  ? 75  ASN C CB     1 
ATOM   6206  C CG     . ASN C 2 57  ? 25.482  6.045   54.778 1.00 67.24  ? 75  ASN C CG     1 
ATOM   6207  O OD1    . ASN C 2 57  ? 24.920  5.030   54.377 1.00 68.51  ? 75  ASN C OD1    1 
ATOM   6208  N ND2    . ASN C 2 57  ? 24.847  6.997   55.440 1.00 80.06  ? 75  ASN C ND2    1 
ATOM   6209  N N      . TYR C 2 58  ? 27.416  4.647   51.301 1.00 57.44  ? 76  TYR C N      1 
ATOM   6210  C CA     . TYR C 2 58  ? 27.186  4.930   49.902 1.00 50.60  ? 76  TYR C CA     1 
ATOM   6211  C C      . TYR C 2 58  ? 25.728  5.035   49.560 1.00 47.21  ? 76  TYR C C      1 
ATOM   6212  O O      . TYR C 2 58  ? 25.347  5.844   48.746 1.00 47.98  ? 76  TYR C O      1 
ATOM   6213  C CB     . TYR C 2 58  ? 27.820  3.850   49.053 1.00 45.05  ? 76  TYR C CB     1 
ATOM   6214  C CG     . TYR C 2 58  ? 29.317  3.736   49.137 1.00 44.02  ? 76  TYR C CG     1 
ATOM   6215  C CD1    . TYR C 2 58  ? 30.103  4.806   49.516 1.00 44.04  ? 76  TYR C CD1    1 
ATOM   6216  C CD2    . TYR C 2 58  ? 29.944  2.555   48.804 1.00 43.33  ? 76  TYR C CD2    1 
ATOM   6217  C CE1    . TYR C 2 58  ? 31.472  4.688   49.583 1.00 42.17  ? 76  TYR C CE1    1 
ATOM   6218  C CE2    . TYR C 2 58  ? 31.309  2.436   48.861 1.00 40.76  ? 76  TYR C CE2    1 
ATOM   6219  C CZ     . TYR C 2 58  ? 32.063  3.504   49.254 1.00 38.74  ? 76  TYR C CZ     1 
ATOM   6220  O OH     . TYR C 2 58  ? 33.420  3.372   49.309 1.00 39.78  ? 76  TYR C OH     1 
ATOM   6221  N N      . LYS C 2 59  ? 24.900  4.223   50.179 1.00 45.09  ? 77  LYS C N      1 
ATOM   6222  C CA     . LYS C 2 59  ? 23.492  4.222   49.843 1.00 47.47  ? 77  LYS C CA     1 
ATOM   6223  C C      . LYS C 2 59  ? 22.868  5.569   50.002 1.00 54.32  ? 77  LYS C C      1 
ATOM   6224  O O      . LYS C 2 59  ? 22.260  6.083   49.084 1.00 58.27  ? 77  LYS C O      1 
ATOM   6225  C CB     . LYS C 2 59  ? 22.734  3.238   50.711 1.00 43.63  ? 77  LYS C CB     1 
ATOM   6226  C CG     . LYS C 2 59  ? 21.403  2.809   50.125 1.00 57.84  ? 77  LYS C CG     1 
ATOM   6227  C CD     . LYS C 2 59  ? 20.720  1.782   51.007 1.00 61.88  ? 77  LYS C CD     1 
ATOM   6228  C CE     . LYS C 2 59  ? 19.555  1.128   50.285 1.00 65.89  ? 77  LYS C CE     1 
ATOM   6229  N NZ     . LYS C 2 59  ? 20.006  0.374   49.083 1.00 60.08  ? 77  LYS C NZ     1 
ATOM   6230  N N      . GLU C 2 60  ? 22.988  6.144   51.182 1.00 57.63  ? 78  GLU C N      1 
ATOM   6231  C CA     . GLU C 2 60  ? 22.371  7.424   51.443 1.00 62.60  ? 78  GLU C CA     1 
ATOM   6232  C C      . GLU C 2 60  ? 22.891  8.451   50.496 1.00 62.83  ? 78  GLU C C      1 
ATOM   6233  O O      . GLU C 2 60  ? 22.150  9.284   50.013 1.00 65.69  ? 78  GLU C O      1 
ATOM   6234  C CB     . GLU C 2 60  ? 22.647  7.880   52.864 1.00 68.43  ? 78  GLU C CB     1 
ATOM   6235  C CG     . GLU C 2 60  ? 21.645  8.906   53.370 1.00 82.32  ? 78  GLU C CG     1 
ATOM   6236  C CD     . GLU C 2 60  ? 21.978  9.447   54.747 1.00 88.15  ? 78  GLU C CD     1 
ATOM   6237  O OE1    . GLU C 2 60  ? 23.148  9.347   55.162 1.00 82.86  ? 78  GLU C OE1    1 
ATOM   6238  O OE2    . GLU C 2 60  ? 21.066  9.984   55.412 1.00 87.26  ? 78  GLU C OE2    1 
ATOM   6239  N N      . ALA C 2 61  ? 24.177  8.409   50.224 1.00 58.30  ? 79  ALA C N      1 
ATOM   6240  C CA     . ALA C 2 61  ? 24.754  9.408   49.371 1.00 54.26  ? 79  ALA C CA     1 
ATOM   6241  C C      . ALA C 2 61  ? 24.121  9.261   48.041 1.00 62.51  ? 79  ALA C C      1 
ATOM   6242  O O      . ALA C 2 61  ? 23.779  10.235  47.409 1.00 66.85  ? 79  ALA C O      1 
ATOM   6243  C CB     . ALA C 2 61  ? 26.232  9.206   49.257 1.00 52.34  ? 79  ALA C CB     1 
ATOM   6244  N N      . ILE C 2 62  ? 23.959  8.030   47.604 1.00 57.26  ? 80  ILE C N      1 
ATOM   6245  C CA     . ILE C 2 62  ? 23.391  7.802   46.306 1.00 53.40  ? 80  ILE C CA     1 
ATOM   6246  C C      . ILE C 2 62  ? 22.012  8.432   46.284 1.00 61.25  ? 80  ILE C C      1 
ATOM   6247  O O      . ILE C 2 62  ? 21.666  9.122   45.340 1.00 63.41  ? 80  ILE C O      1 
ATOM   6248  C CB     . ILE C 2 62  ? 23.376  6.315   45.956 1.00 53.84  ? 80  ILE C CB     1 
ATOM   6249  C CG1    . ILE C 2 62  ? 24.751  5.882   45.454 1.00 50.93  ? 80  ILE C CG1    1 
ATOM   6250  C CG2    . ILE C 2 62  ? 22.336  6.006   44.897 1.00 64.15  ? 80  ILE C CG2    1 
ATOM   6251  C CD1    . ILE C 2 62  ? 24.833  4.418   45.097 1.00 45.94  ? 80  ILE C CD1    1 
ATOM   6252  N N      . GLU C 2 63  ? 21.224  8.231   47.329 1.00 60.24  ? 81  GLU C N      1 
ATOM   6253  C CA     . GLU C 2 63  ? 19.904  8.828   47.381 1.00 59.39  ? 81  GLU C CA     1 
ATOM   6254  C C      . GLU C 2 63  ? 20.020  10.304  47.196 1.00 60.76  ? 81  GLU C C      1 
ATOM   6255  O O      . GLU C 2 63  ? 19.393  10.872  46.323 1.00 60.72  ? 81  GLU C O      1 
ATOM   6256  C CB     . GLU C 2 63  ? 19.241  8.575   48.718 1.00 54.37  ? 81  GLU C CB     1 
ATOM   6257  C CG     . GLU C 2 63  ? 18.862  7.135   48.987 1.00 68.92  ? 81  GLU C CG     1 
ATOM   6258  C CD     . GLU C 2 63  ? 18.246  6.963   50.359 1.00 82.60  ? 81  GLU C CD     1 
ATOM   6259  O OE1    . GLU C 2 63  ? 18.205  7.952   51.118 1.00 74.79  ? 81  GLU C OE1    1 
ATOM   6260  O OE2    . GLU C 2 63  ? 17.804  5.842   50.681 1.00 100.64 ? 81  GLU C OE2    1 
ATOM   6261  N N      . LYS C 2 64  ? 20.812  10.937  48.033 1.00 59.18  ? 82  LYS C N      1 
ATOM   6262  C CA     . LYS C 2 64  ? 20.938  12.380  47.989 1.00 62.77  ? 82  LYS C CA     1 
ATOM   6263  C C      . LYS C 2 64  ? 21.456  12.875  46.685 1.00 57.06  ? 82  LYS C C      1 
ATOM   6264  O O      . LYS C 2 64  ? 21.046  13.909  46.207 1.00 57.37  ? 82  LYS C O      1 
ATOM   6265  C CB     . LYS C 2 64  ? 21.881  12.832  49.090 1.00 60.58  ? 82  LYS C CB     1 
ATOM   6266  C CG     . LYS C 2 64  ? 21.323  12.684  50.494 1.00 57.05  ? 82  LYS C CG     1 
ATOM   6267  C CD     . LYS C 2 64  ? 22.354  13.070  51.540 1.00 59.83  ? 82  LYS C CD     1 
ATOM   6268  C CE     . LYS C 2 64  ? 22.940  14.446  51.273 1.00 63.21  ? 82  LYS C CE     1 
ATOM   6269  N NZ     . LYS C 2 64  ? 21.945  15.544  51.411 1.00 61.97  ? 82  LYS C NZ     1 
ATOM   6270  N N      . ILE C 2 65  ? 22.388  12.152  46.119 1.00 49.95  ? 83  ILE C N      1 
ATOM   6271  C CA     . ILE C 2 65  ? 22.929  12.542  44.856 1.00 54.71  ? 83  ILE C CA     1 
ATOM   6272  C C      . ILE C 2 65  ? 21.825  12.540  43.820 1.00 65.66  ? 83  ILE C C      1 
ATOM   6273  O O      . ILE C 2 65  ? 21.654  13.511  43.098 1.00 74.07  ? 83  ILE C O      1 
ATOM   6274  C CB     . ILE C 2 65  ? 24.071  11.614  44.461 1.00 54.04  ? 83  ILE C CB     1 
ATOM   6275  C CG1    . ILE C 2 65  ? 25.362  12.048  45.139 1.00 47.95  ? 83  ILE C CG1    1 
ATOM   6276  C CG2    . ILE C 2 65  ? 24.263  11.605  42.962 1.00 57.64  ? 83  ILE C CG2    1 
ATOM   6277  C CD1    . ILE C 2 65  ? 26.532  11.169  44.783 1.00 50.16  ? 83  ILE C CD1    1 
ATOM   6278  N N      . LEU C 2 66  ? 21.016  11.494  43.775 1.00 64.94  ? 84  LEU C N      1 
ATOM   6279  C CA     . LEU C 2 66  ? 19.939  11.406  42.791 1.00 58.48  ? 84  LEU C CA     1 
ATOM   6280  C C      . LEU C 2 66  ? 18.845  12.403  43.088 1.00 58.97  ? 84  LEU C C      1 
ATOM   6281  O O      . LEU C 2 66  ? 18.296  13.009  42.185 1.00 50.79  ? 84  LEU C O      1 
ATOM   6282  C CB     . LEU C 2 66  ? 19.361  9.998   42.778 1.00 56.46  ? 84  LEU C CB     1 
ATOM   6283  C CG     . LEU C 2 66  ? 20.253  8.883   42.255 1.00 53.81  ? 84  LEU C CG     1 
ATOM   6284  C CD1    . LEU C 2 66  ? 19.627  7.540   42.575 1.00 52.89  ? 84  LEU C CD1    1 
ATOM   6285  C CD2    . LEU C 2 66  ? 20.453  9.044   40.760 1.00 52.61  ? 84  LEU C CD2    1 
ATOM   6286  N N      . ASP C 2 67  ? 18.534  12.586  44.357 1.00 64.64  ? 85  ASP C N      1 
ATOM   6287  C CA     . ASP C 2 67  ? 17.476  13.498  44.745 1.00 64.53  ? 85  ASP C CA     1 
ATOM   6288  C C      . ASP C 2 67  ? 17.858  14.962  44.622 1.00 61.61  ? 85  ASP C C      1 
ATOM   6289  O O      . ASP C 2 67  ? 16.999  15.813  44.445 1.00 61.31  ? 85  ASP C O      1 
ATOM   6290  C CB     . ASP C 2 67  ? 17.023  13.183  46.167 1.00 66.38  ? 85  ASP C CB     1 
ATOM   6291  C CG     . ASP C 2 67  ? 16.373  11.825  46.288 1.00 61.43  ? 85  ASP C CG     1 
ATOM   6292  O OD1    . ASP C 2 67  ? 16.418  11.051  45.313 1.00 66.15  ? 85  ASP C OD1    1 
ATOM   6293  O OD2    . ASP C 2 67  ? 15.820  11.529  47.366 1.00 47.01  ? 85  ASP C OD2    1 
ATOM   6294  N N      . PHE C 2 68  ? 19.136  15.270  44.731 1.00 59.94  ? 86  PHE C N      1 
ATOM   6295  C CA     . PHE C 2 68  ? 19.598  16.632  44.552 1.00 62.95  ? 86  PHE C CA     1 
ATOM   6296  C C      . PHE C 2 68  ? 19.269  16.934  43.156 1.00 67.60  ? 86  PHE C C      1 
ATOM   6297  O O      . PHE C 2 68  ? 18.742  17.987  42.847 1.00 74.02  ? 86  PHE C O      1 
ATOM   6298  C CB     . PHE C 2 68  ? 21.101  16.639  44.613 1.00 61.31  ? 86  PHE C CB     1 
ATOM   6299  C CG     . PHE C 2 68  ? 21.713  17.994  44.611 1.00 65.86  ? 86  PHE C CG     1 
ATOM   6300  C CD1    . PHE C 2 68  ? 21.514  18.857  45.666 1.00 70.28  ? 86  PHE C CD1    1 
ATOM   6301  C CD2    . PHE C 2 68  ? 22.537  18.379  43.578 1.00 65.95  ? 86  PHE C CD2    1 
ATOM   6302  C CE1    . PHE C 2 68  ? 22.104  20.099  45.675 1.00 76.34  ? 86  PHE C CE1    1 
ATOM   6303  C CE2    . PHE C 2 68  ? 23.130  19.617  43.581 1.00 67.46  ? 86  PHE C CE2    1 
ATOM   6304  C CZ     . PHE C 2 68  ? 22.916  20.475  44.630 1.00 75.50  ? 86  PHE C CZ     1 
ATOM   6305  N N      . CYS C 2 69  ? 19.645  16.016  42.281 1.00 66.89  ? 87  CYS C N      1 
ATOM   6306  C CA     . CYS C 2 69  ? 19.416  16.208  40.871 1.00 65.26  ? 87  CYS C CA     1 
ATOM   6307  C C      . CYS C 2 69  ? 17.963  16.492  40.585 1.00 69.47  ? 87  CYS C C      1 
ATOM   6308  O O      . CYS C 2 69  ? 17.675  17.359  39.816 1.00 76.10  ? 87  CYS C O      1 
ATOM   6309  C CB     . CYS C 2 69  ? 19.898  14.999  40.093 1.00 62.49  ? 87  CYS C CB     1 
ATOM   6310  S SG     . CYS C 2 69  ? 21.680  14.765  40.099 1.00 64.43  ? 87  CYS C SG     1 
ATOM   6311  N N      . LYS C 2 70  ? 17.039  15.784  41.202 1.00 67.21  ? 88  LYS C N      1 
ATOM   6312  C CA     . LYS C 2 70  ? 15.643  15.992  40.890 1.00 64.47  ? 88  LYS C CA     1 
ATOM   6313  C C      . LYS C 2 70  ? 15.289  17.421  41.175 1.00 70.23  ? 88  LYS C C      1 
ATOM   6314  O O      . LYS C 2 70  ? 14.671  18.083  40.361 1.00 80.05  ? 88  LYS C O      1 
ATOM   6315  C CB     . LYS C 2 70  ? 14.761  15.095  41.738 1.00 67.86  ? 88  LYS C CB     1 
ATOM   6316  C CG     . LYS C 2 70  ? 15.010  13.611  41.551 1.00 69.22  ? 88  LYS C CG     1 
ATOM   6317  C CD     . LYS C 2 70  ? 14.406  12.814  42.694 1.00 64.91  ? 88  LYS C CD     1 
ATOM   6318  C CE     . LYS C 2 70  ? 12.916  13.069  42.829 1.00 67.20  ? 88  LYS C CE     1 
ATOM   6319  N NZ     . LYS C 2 70  ? 12.163  12.540  41.659 1.00 72.58  ? 88  LYS C NZ     1 
ATOM   6320  N N      . LYS C 2 71  ? 15.686  17.921  42.330 1.00 67.53  ? 89  LYS C N      1 
ATOM   6321  C CA     . LYS C 2 71  ? 15.342  19.284  42.713 1.00 70.30  ? 89  LYS C CA     1 
ATOM   6322  C C      . LYS C 2 71  ? 16.021  20.296  41.812 1.00 71.04  ? 89  LYS C C      1 
ATOM   6323  O O      . LYS C 2 71  ? 15.445  21.328  41.489 1.00 73.74  ? 89  LYS C O      1 
ATOM   6324  C CB     . LYS C 2 71  ? 15.723  19.522  44.172 1.00 68.62  ? 89  LYS C CB     1 
ATOM   6325  C CG     . LYS C 2 71  ? 15.722  20.974  44.621 1.00 74.46  ? 89  LYS C CG     1 
ATOM   6326  C CD     . LYS C 2 71  ? 14.335  21.465  45.000 1.00 75.76  ? 89  LYS C CD     1 
ATOM   6327  C CE     . LYS C 2 71  ? 13.921  20.949  46.369 1.00 71.28  ? 89  LYS C CE     1 
ATOM   6328  N NZ     . LYS C 2 71  ? 12.699  21.632  46.876 1.00 59.46  ? 89  LYS C NZ     1 
ATOM   6329  N N      . ASN C 2 72  ? 17.252  20.014  41.410 1.00 66.25  ? 90  ASN C N      1 
ATOM   6330  C CA     . ASN C 2 72  ? 17.989  20.933  40.558 1.00 64.45  ? 90  ASN C CA     1 
ATOM   6331  C C      . ASN C 2 72  ? 18.099  20.437  39.133 1.00 73.13  ? 90  ASN C C      1 
ATOM   6332  O O      . ASN C 2 72  ? 19.074  20.724  38.457 1.00 75.95  ? 90  ASN C O      1 
ATOM   6333  C CB     . ASN C 2 72  ? 19.357  21.196  41.148 1.00 60.32  ? 90  ASN C CB     1 
ATOM   6334  C CG     . ASN C 2 72  ? 19.278  21.900  42.475 1.00 73.37  ? 90  ASN C CG     1 
ATOM   6335  O OD1    . ASN C 2 72  ? 18.349  22.660  42.729 1.00 77.46  ? 90  ASN C OD1    1 
ATOM   6336  N ND2    . ASN C 2 72  ? 20.246  21.651  43.329 1.00 77.60  ? 90  ASN C ND2    1 
ATOM   6337  N N      . GLU C 2 73  ? 17.090  19.714  38.657 1.00 74.06  ? 91  GLU C N      1 
ATOM   6338  C CA     . GLU C 2 73  ? 17.127  19.124  37.319 1.00 71.74  ? 91  GLU C CA     1 
ATOM   6339  C C      . GLU C 2 73  ? 16.945  20.159  36.284 1.00 76.88  ? 91  GLU C C      1 
ATOM   6340  O O      . GLU C 2 73  ? 17.234  19.938  35.116 1.00 78.57  ? 91  GLU C O      1 
ATOM   6341  C CB     . GLU C 2 73  ? 15.980  18.148  37.161 1.00 71.46  ? 91  GLU C CB     1 
ATOM   6342  C CG     . GLU C 2 73  ? 16.374  16.706  36.883 1.00 87.46  ? 91  GLU C CG     1 
ATOM   6343  C CD     . GLU C 2 73  ? 15.179  15.765  36.903 1.00 91.39  ? 91  GLU C CD     1 
ATOM   6344  O OE1    . GLU C 2 73  ? 14.038  16.246  37.083 1.00 88.16  ? 91  GLU C OE1    1 
ATOM   6345  O OE2    . GLU C 2 73  ? 15.378  14.542  36.738 1.00 81.99  ? 91  GLU C OE2    1 
ATOM   6346  N N      . SER C 2 74  ? 16.400  21.287  36.691 1.00 72.87  ? 92  SER C N      1 
ATOM   6347  C CA     . SER C 2 74  ? 16.157  22.355  35.756 1.00 72.93  ? 92  SER C CA     1 
ATOM   6348  C C      . SER C 2 74  ? 17.485  22.793  35.235 1.00 73.52  ? 92  SER C C      1 
ATOM   6349  O O      . SER C 2 74  ? 17.589  23.382  34.169 1.00 75.21  ? 92  SER C O      1 
ATOM   6350  C CB     . SER C 2 74  ? 15.489  23.506  36.491 1.00 79.59  ? 92  SER C CB     1 
ATOM   6351  O OG     . SER C 2 74  ? 15.421  24.667  35.683 1.00 81.40  ? 92  SER C OG     1 
ATOM   6352  N N      . LEU C 2 75  ? 18.532  22.436  35.946 1.00 73.06  ? 93  LEU C N      1 
ATOM   6353  C CA     . LEU C 2 75  ? 19.841  22.898  35.562 1.00 74.08  ? 93  LEU C CA     1 
ATOM   6354  C C      . LEU C 2 75  ? 20.721  21.791  35.062 1.00 74.62  ? 93  LEU C C      1 
ATOM   6355  O O      . LEU C 2 75  ? 21.929  21.967  35.003 1.00 81.81  ? 93  LEU C O      1 
ATOM   6356  C CB     . LEU C 2 75  ? 20.525  23.511  36.776 1.00 77.70  ? 93  LEU C CB     1 
ATOM   6357  C CG     . LEU C 2 75  ? 19.930  24.712  37.519 1.00 82.71  ? 93  LEU C CG     1 
ATOM   6358  C CD1    . LEU C 2 75  ? 18.919  24.288  38.573 1.00 75.40  ? 93  LEU C CD1    1 
ATOM   6359  C CD2    . LEU C 2 75  ? 21.051  25.488  38.189 1.00 84.45  ? 93  LEU C CD2    1 
ATOM   6360  N N      . LEU C 2 76  ? 20.151  20.652  34.693 1.00 73.93  ? 94  LEU C N      1 
ATOM   6361  C CA     . LEU C 2 76  ? 20.991  19.514  34.323 1.00 75.77  ? 94  LEU C CA     1 
ATOM   6362  C C      . LEU C 2 76  ? 20.574  18.720  33.117 1.00 70.54  ? 94  LEU C C      1 
ATOM   6363  O O      . LEU C 2 76  ? 19.397  18.640  32.802 1.00 74.73  ? 94  LEU C O      1 
ATOM   6364  C CB     . LEU C 2 76  ? 21.109  18.547  35.499 1.00 80.46  ? 94  LEU C CB     1 
ATOM   6365  C CG     . LEU C 2 76  ? 21.727  19.034  36.812 1.00 78.28  ? 94  LEU C CG     1 
ATOM   6366  C CD1    . LEU C 2 76  ? 21.409  18.087  37.953 1.00 73.41  ? 94  LEU C CD1    1 
ATOM   6367  C CD2    . LEU C 2 76  ? 23.224  19.251  36.686 1.00 66.58  ? 94  LEU C CD2    1 
ATOM   6368  N N      . SER C 2 77  ? 21.545  18.095  32.470 1.00 70.69  ? 95  SER C N      1 
ATOM   6369  C CA     . SER C 2 77  ? 21.267  17.298  31.296 1.00 78.32  ? 95  SER C CA     1 
ATOM   6370  C C      . SER C 2 77  ? 20.488  16.065  31.648 1.00 71.19  ? 95  SER C C      1 
ATOM   6371  O O      . SER C 2 77  ? 20.878  15.309  32.517 1.00 70.84  ? 95  SER C O      1 
ATOM   6372  C CB     . SER C 2 77  ? 22.570  16.913  30.640 1.00 75.14  ? 95  SER C CB     1 
ATOM   6373  O OG     . SER C 2 77  ? 23.319  18.077  30.361 1.00 77.80  ? 95  SER C OG     1 
ATOM   6374  N N      . GLU C 2 78  ? 19.394  15.841  30.957 1.00 69.85  ? 96  GLU C N      1 
ATOM   6375  C CA     . GLU C 2 78  ? 18.539  14.727  31.291 1.00 74.57  ? 96  GLU C CA     1 
ATOM   6376  C C      . GLU C 2 78  ? 19.103  13.384  31.006 1.00 77.14  ? 96  GLU C C      1 
ATOM   6377  O O      . GLU C 2 78  ? 18.847  12.443  31.735 1.00 82.06  ? 96  GLU C O      1 
ATOM   6378  C CB     . GLU C 2 78  ? 17.229  14.872  30.534 1.00 81.64  ? 96  GLU C CB     1 
ATOM   6379  C CG     . GLU C 2 78  ? 16.270  13.692  30.640 1.00 85.69  ? 96  GLU C CG     1 
ATOM   6380  C CD     . GLU C 2 78  ? 15.769  13.447  32.049 1.00 81.10  ? 96  GLU C CD     1 
ATOM   6381  O OE1    . GLU C 2 78  ? 15.347  14.414  32.713 1.00 79.10  ? 96  GLU C OE1    1 
ATOM   6382  O OE2    . GLU C 2 78  ? 15.786  12.281  32.488 1.00 70.96  ? 96  GLU C OE2    1 
ATOM   6383  N N      . GLN C 2 79  ? 19.857  13.260  29.939 1.00 76.01  ? 97  GLN C N      1 
ATOM   6384  C CA     . GLN C 2 79  ? 20.342  11.947  29.593 1.00 78.57  ? 97  GLN C CA     1 
ATOM   6385  C C      . GLN C 2 79  ? 21.128  11.471  30.784 1.00 76.89  ? 97  GLN C C      1 
ATOM   6386  O O      . GLN C 2 79  ? 20.982  10.340  31.212 1.00 76.24  ? 97  GLN C O      1 
ATOM   6387  C CB     . GLN C 2 79  ? 21.242  11.997  28.370 1.00 82.65  ? 97  GLN C CB     1 
ATOM   6388  C CG     . GLN C 2 79  ? 20.746  12.896  27.252 1.00 82.48  ? 97  GLN C CG     1 
ATOM   6389  C CD     . GLN C 2 79  ? 21.792  13.093  26.173 1.00 87.66  ? 97  GLN C CD     1 
ATOM   6390  O OE1    . GLN C 2 79  ? 22.824  12.423  26.166 1.00 93.14  ? 97  GLN C OE1    1 
ATOM   6391  N NE2    . GLN C 2 79  ? 21.533  14.015  25.257 1.00 79.10  ? 97  GLN C NE2    1 
ATOM   6392  N N      . VAL C 2 80  ? 21.966  12.339  31.325 1.00 73.49  ? 98  VAL C N      1 
ATOM   6393  C CA     . VAL C 2 80  ? 22.822  11.950  32.427 1.00 68.15  ? 98  VAL C CA     1 
ATOM   6394  C C      . VAL C 2 80  ? 22.008  11.610  33.636 1.00 62.05  ? 98  VAL C C      1 
ATOM   6395  O O      . VAL C 2 80  ? 22.092  10.513  34.148 1.00 65.70  ? 98  VAL C O      1 
ATOM   6396  C CB     . VAL C 2 80  ? 23.797  13.069  32.783 1.00 67.79  ? 98  VAL C CB     1 
ATOM   6397  C CG1    . VAL C 2 80  ? 24.805  12.584  33.806 1.00 66.82  ? 98  VAL C CG1    1 
ATOM   6398  C CG2    . VAL C 2 80  ? 24.514  13.548  31.535 1.00 68.46  ? 98  VAL C CG2    1 
ATOM   6399  N N      . VAL C 2 81  ? 21.218  12.554  34.090 1.00 55.97  ? 99  VAL C N      1 
ATOM   6400  C CA     . VAL C 2 81  ? 20.449  12.323  35.275 1.00 56.79  ? 99  VAL C CA     1 
ATOM   6401  C C      . VAL C 2 81  ? 19.681  11.039  35.086 1.00 64.32  ? 99  VAL C C      1 
ATOM   6402  O O      . VAL C 2 81  ? 19.487  10.300  36.036 1.00 61.19  ? 99  VAL C O      1 
ATOM   6403  C CB     . VAL C 2 81  ? 19.527  13.499  35.578 1.00 60.73  ? 99  VAL C CB     1 
ATOM   6404  C CG1    . VAL C 2 81  ? 18.705  13.238  36.827 1.00 53.07  ? 99  VAL C CG1    1 
ATOM   6405  C CG2    . VAL C 2 81  ? 20.340  14.770  35.740 1.00 64.07  ? 99  VAL C CG2    1 
ATOM   6406  N N      . GLN C 2 82  ? 19.311  10.717  33.857 1.00 64.27  ? 100 GLN C N      1 
ATOM   6407  C CA     . GLN C 2 82  ? 18.618  9.463   33.608 1.00 65.36  ? 100 GLN C CA     1 
ATOM   6408  C C      . GLN C 2 82  ? 19.528  8.264   33.730 1.00 70.34  ? 100 GLN C C      1 
ATOM   6409  O O      . GLN C 2 82  ? 19.186  7.286   34.362 1.00 70.77  ? 100 GLN C O      1 
ATOM   6410  C CB     . GLN C 2 82  ? 17.938  9.435   32.248 1.00 67.01  ? 100 GLN C CB     1 
ATOM   6411  C CG     . GLN C 2 82  ? 17.334  8.082   31.905 1.00 72.23  ? 100 GLN C CG     1 
ATOM   6412  C CD     . GLN C 2 82  ? 16.285  8.152   30.817 1.00 75.01  ? 100 GLN C CD     1 
ATOM   6413  O OE1    . GLN C 2 82  ? 15.865  9.232   30.409 1.00 78.26  ? 100 GLN C OE1    1 
ATOM   6414  N NE2    . GLN C 2 82  ? 15.846  6.991   30.348 1.00 68.88  ? 100 GLN C NE2    1 
ATOM   6415  N N      . ARG C 2 83  ? 20.673  8.315   33.079 1.00 67.90  ? 101 ARG C N      1 
ATOM   6416  C CA     . ARG C 2 83  ? 21.562  7.184   33.092 1.00 65.95  ? 101 ARG C CA     1 
ATOM   6417  C C      . ARG C 2 83  ? 21.900  6.946   34.510 1.00 64.36  ? 101 ARG C C      1 
ATOM   6418  O O      . ARG C 2 83  ? 21.902  5.829   34.964 1.00 68.65  ? 101 ARG C O      1 
ATOM   6419  C CB     . ARG C 2 83  ? 22.822  7.512   32.330 1.00 68.17  ? 101 ARG C CB     1 
ATOM   6420  C CG     . ARG C 2 83  ? 23.732  6.334   32.049 1.00 77.01  ? 101 ARG C CG     1 
ATOM   6421  C CD     . ARG C 2 83  ? 23.400  5.692   30.716 1.00 69.39  ? 101 ARG C CD     1 
ATOM   6422  N NE     . ARG C 2 83  ? 24.281  4.569   30.430 1.00 69.91  ? 101 ARG C NE     1 
ATOM   6423  C CZ     . ARG C 2 83  ? 24.005  3.311   30.744 1.00 73.48  ? 101 ARG C CZ     1 
ATOM   6424  N NH1    . ARG C 2 83  ? 22.867  3.012   31.350 1.00 71.91  ? 101 ARG C NH1    1 
ATOM   6425  N NH2    . ARG C 2 83  ? 24.864  2.350   30.446 1.00 78.83  ? 101 ARG C NH2    1 
ATOM   6426  N N      . LEU C 2 84  ? 22.242  8.004   35.218 1.00 62.53  ? 102 LEU C N      1 
ATOM   6427  C CA     . LEU C 2 84  ? 22.554  7.871   36.625 1.00 64.10  ? 102 LEU C CA     1 
ATOM   6428  C C      . LEU C 2 84  ? 21.407  7.154   37.273 1.00 63.60  ? 102 LEU C C      1 
ATOM   6429  O O      . LEU C 2 84  ? 21.614  6.244   38.050 1.00 62.46  ? 102 LEU C O      1 
ATOM   6430  C CB     . LEU C 2 84  ? 22.738  9.230   37.289 1.00 53.76  ? 102 LEU C CB     1 
ATOM   6431  C CG     . LEU C 2 84  ? 23.848  10.186  36.857 1.00 55.56  ? 102 LEU C CG     1 
ATOM   6432  C CD1    . LEU C 2 84  ? 23.779  11.464  37.673 1.00 54.88  ? 102 LEU C CD1    1 
ATOM   6433  C CD2    . LEU C 2 84  ? 25.226  9.562   36.957 1.00 50.17  ? 102 LEU C CD2    1 
ATOM   6434  N N      . ALA C 2 85  ? 20.188  7.519   36.918 1.00 59.25  ? 103 ALA C N      1 
ATOM   6435  C CA     . ALA C 2 85  ? 19.032  6.935   37.562 1.00 55.97  ? 103 ALA C CA     1 
ATOM   6436  C C      . ALA C 2 85  ? 18.848  5.504   37.202 1.00 62.07  ? 103 ALA C C      1 
ATOM   6437  O O      . ALA C 2 85  ? 18.407  4.741   38.022 1.00 63.83  ? 103 ALA C O      1 
ATOM   6438  C CB     . ALA C 2 85  ? 17.804  7.701   37.191 1.00 56.26  ? 103 ALA C CB     1 
ATOM   6439  N N      . GLU C 2 86  ? 19.171  5.123   35.985 1.00 67.03  ? 104 GLU C N      1 
ATOM   6440  C CA     . GLU C 2 86  ? 19.086  3.722   35.609 1.00 67.34  ? 104 GLU C CA     1 
ATOM   6441  C C      . GLU C 2 86  ? 20.218  2.910   36.190 1.00 67.81  ? 104 GLU C C      1 
ATOM   6442  O O      . GLU C 2 86  ? 19.993  1.811   36.671 1.00 70.89  ? 104 GLU C O      1 
ATOM   6443  C CB     . GLU C 2 86  ? 19.098  3.573   34.092 1.00 70.20  ? 104 GLU C CB     1 
ATOM   6444  C CG     . GLU C 2 86  ? 17.848  4.076   33.400 1.00 81.67  ? 104 GLU C CG     1 
ATOM   6445  C CD     . GLU C 2 86  ? 17.883  3.820   31.911 1.00 88.66  ? 104 GLU C CD     1 
ATOM   6446  O OE1    . GLU C 2 86  ? 18.967  3.462   31.406 1.00 87.00  ? 104 GLU C OE1    1 
ATOM   6447  O OE2    . GLU C 2 86  ? 16.834  3.975   31.249 1.00 85.69  ? 104 GLU C OE2    1 
ATOM   6448  N N      . VAL C 2 87  ? 21.437  3.427   36.135 1.00 63.08  ? 105 VAL C N      1 
ATOM   6449  C CA     . VAL C 2 87  ? 22.589  2.671   36.585 1.00 59.78  ? 105 VAL C CA     1 
ATOM   6450  C C      . VAL C 2 87  ? 22.603  2.449   38.077 1.00 61.08  ? 105 VAL C C      1 
ATOM   6451  O O      . VAL C 2 87  ? 22.943  1.381   38.542 1.00 58.13  ? 105 VAL C O      1 
ATOM   6452  C CB     . VAL C 2 87  ? 23.867  3.366   36.123 1.00 60.76  ? 105 VAL C CB     1 
ATOM   6453  C CG1    . VAL C 2 87  ? 25.098  2.756   36.769 1.00 61.55  ? 105 VAL C CG1    1 
ATOM   6454  C CG2    . VAL C 2 87  ? 23.982  3.292   34.614 1.00 59.01  ? 105 VAL C CG2    1 
ATOM   6455  N N      . ALA C 2 88  ? 22.225  3.454   38.839 1.00 62.31  ? 106 ALA C N      1 
ATOM   6456  C CA     . ALA C 2 88  ? 22.282  3.368   40.303 1.00 66.90  ? 106 ALA C CA     1 
ATOM   6457  C C      . ALA C 2 88  ? 21.532  2.280   41.069 1.00 68.56  ? 106 ALA C C      1 
ATOM   6458  O O      . ALA C 2 88  ? 22.028  1.813   42.084 1.00 65.15  ? 106 ALA C O      1 
ATOM   6459  C CB     . ALA C 2 88  ? 21.954  4.713   40.905 1.00 63.77  ? 106 ALA C CB     1 
ATOM   6460  N N      . PRO C 2 89  ? 20.304  1.888   40.635 1.00 66.23  ? 107 PRO C N      1 
ATOM   6461  C CA     . PRO C 2 89  ? 19.688  0.818   41.418 1.00 64.75  ? 107 PRO C CA     1 
ATOM   6462  C C      . PRO C 2 89  ? 20.389  -0.513  41.288 1.00 64.90  ? 107 PRO C C      1 
ATOM   6463  O O      . PRO C 2 89  ? 20.170  -1.402  42.102 1.00 62.63  ? 107 PRO C O      1 
ATOM   6464  C CB     . PRO C 2 89  ? 18.312  0.710   40.804 1.00 62.61  ? 107 PRO C CB     1 
ATOM   6465  C CG     . PRO C 2 89  ? 18.006  2.088   40.383 1.00 72.14  ? 107 PRO C CG     1 
ATOM   6466  C CD     . PRO C 2 89  ? 19.292  2.483   39.742 1.00 64.47  ? 107 PRO C CD     1 
ATOM   6467  N N      . ARG C 2 90  ? 21.220  -0.662  40.277 1.00 61.15  ? 108 ARG C N      1 
ATOM   6468  C CA     . ARG C 2 90  ? 21.882  -1.923  40.074 1.00 61.99  ? 108 ARG C CA     1 
ATOM   6469  C C      . ARG C 2 90  ? 23.344  -1.762  40.305 1.00 60.77  ? 108 ARG C C      1 
ATOM   6470  O O      . ARG C 2 90  ? 24.152  -2.277  39.548 1.00 61.72  ? 108 ARG C O      1 
ATOM   6471  C CB     . ARG C 2 90  ? 21.621  -2.436  38.666 1.00 64.09  ? 108 ARG C CB     1 
ATOM   6472  C CG     . ARG C 2 90  ? 21.446  -1.359  37.619 1.00 68.07  ? 108 ARG C CG     1 
ATOM   6473  C CD     . ARG C 2 90  ? 21.076  -1.971  36.281 1.00 72.22  ? 108 ARG C CD     1 
ATOM   6474  N NE     . ARG C 2 90  ? 21.060  -0.979  35.214 1.00 81.05  ? 108 ARG C NE     1 
ATOM   6475  C CZ     . ARG C 2 90  ? 22.108  -0.694  34.451 1.00 92.31  ? 108 ARG C CZ     1 
ATOM   6476  N NH1    . ARG C 2 90  ? 23.258  -1.326  34.638 1.00 83.47  ? 108 ARG C NH1    1 
ATOM   6477  N NH2    . ARG C 2 90  ? 22.007  0.222   33.500 1.00 94.76  ? 108 ARG C NH2    1 
ATOM   6478  N N      . LEU C 2 91  ? 23.700  -1.056  41.361 1.00 55.42  ? 109 LEU C N      1 
ATOM   6479  C CA     . LEU C 2 91  ? 25.096  -0.791  41.587 1.00 54.10  ? 109 LEU C CA     1 
ATOM   6480  C C      . LEU C 2 91  ? 25.562  -1.631  42.715 1.00 54.20  ? 109 LEU C C      1 
ATOM   6481  O O      . LEU C 2 91  ? 24.897  -1.725  43.732 1.00 60.74  ? 109 LEU C O      1 
ATOM   6482  C CB     . LEU C 2 91  ? 25.345  0.675   41.856 1.00 51.54  ? 109 LEU C CB     1 
ATOM   6483  C CG     . LEU C 2 91  ? 25.705  1.528   40.655 1.00 54.51  ? 109 LEU C CG     1 
ATOM   6484  C CD1    . LEU C 2 91  ? 25.994  2.918   41.164 1.00 50.93  ? 109 LEU C CD1    1 
ATOM   6485  C CD2    . LEU C 2 91  ? 26.924  0.954   39.960 1.00 59.26  ? 109 LEU C CD2    1 
ATOM   6486  N N      . LYS C 2 92  ? 26.699  -2.270  42.535 1.00 50.72  ? 110 LYS C N      1 
ATOM   6487  C CA     . LYS C 2 92  ? 27.172  -3.174  43.530 1.00 48.77  ? 110 LYS C CA     1 
ATOM   6488  C C      . LYS C 2 92  ? 28.617  -2.914  43.778 1.00 53.57  ? 110 LYS C C      1 
ATOM   6489  O O      . LYS C 2 92  ? 29.286  -2.343  42.939 1.00 59.69  ? 110 LYS C O      1 
ATOM   6490  C CB     . LYS C 2 92  ? 27.006  -4.587  43.017 1.00 44.62  ? 110 LYS C CB     1 
ATOM   6491  C CG     . LYS C 2 92  ? 27.636  -4.831  41.659 1.00 48.57  ? 110 LYS C CG     1 
ATOM   6492  C CD     . LYS C 2 92  ? 27.781  -6.315  41.379 1.00 51.98  ? 110 LYS C CD     1 
ATOM   6493  C CE     . LYS C 2 92  ? 28.819  -6.947  42.288 1.00 47.92  ? 110 LYS C CE     1 
ATOM   6494  N NZ     . LYS C 2 92  ? 28.996  -8.391  41.987 1.00 43.79  ? 110 LYS C NZ     1 
ATOM   6495  N N      . SER C 2 93  ? 29.104  -3.308  44.943 1.00 46.64  ? 111 SER C N      1 
ATOM   6496  C CA     . SER C 2 93  ? 30.496  -3.155  45.245 1.00 44.44  ? 111 SER C CA     1 
ATOM   6497  C C      . SER C 2 93  ? 31.022  -4.519  45.513 1.00 40.01  ? 111 SER C C      1 
ATOM   6498  O O      . SER C 2 93  ? 30.367  -5.322  46.147 1.00 41.75  ? 111 SER C O      1 
ATOM   6499  C CB     . SER C 2 93  ? 30.697  -2.245  46.439 1.00 48.87  ? 111 SER C CB     1 
ATOM   6500  O OG     . SER C 2 93  ? 30.323  -0.915  46.144 1.00 49.60  ? 111 SER C OG     1 
ATOM   6501  N N      . ASN C 2 94  ? 32.191  -4.806  44.985 1.00 46.90  ? 112 ASN C N      1 
ATOM   6502  C CA     . ASN C 2 94  ? 32.811  -6.091  45.192 1.00 48.63  ? 112 ASN C CA     1 
ATOM   6503  C C      . ASN C 2 94  ? 34.075  -5.807  45.972 1.00 48.03  ? 112 ASN C C      1 
ATOM   6504  O O      . ASN C 2 94  ? 34.841  -4.955  45.567 1.00 52.98  ? 112 ASN C O      1 
ATOM   6505  C CB     . ASN C 2 94  ? 33.177  -6.716  43.856 1.00 51.35  ? 112 ASN C CB     1 
ATOM   6506  C CG     . ASN C 2 94  ? 33.591  -8.164  43.970 1.00 51.93  ? 112 ASN C CG     1 
ATOM   6507  O OD1    . ASN C 2 94  ? 33.141  -8.887  44.852 1.00 49.39  ? 112 ASN C OD1    1 
ATOM   6508  N ND2    . ASN C 2 94  ? 34.439  -8.602  43.053 1.00 57.49  ? 112 ASN C ND2    1 
ATOM   6509  N N      . PRO C 2 95  ? 34.318  -6.505  47.091 1.00 43.07  ? 113 PRO C N      1 
ATOM   6510  C CA     . PRO C 2 95  ? 35.513  -6.131  47.820 1.00 42.32  ? 113 PRO C CA     1 
ATOM   6511  C C      . PRO C 2 95  ? 36.810  -6.470  47.143 1.00 41.73  ? 113 PRO C C      1 
ATOM   6512  O O      . PRO C 2 95  ? 37.800  -5.820  47.407 1.00 46.67  ? 113 PRO C O      1 
ATOM   6513  C CB     . PRO C 2 95  ? 35.400  -6.965  49.078 1.00 42.31  ? 113 PRO C CB     1 
ATOM   6514  C CG     . PRO C 2 95  ? 34.567  -8.128  48.714 1.00 49.11  ? 113 PRO C CG     1 
ATOM   6515  C CD     . PRO C 2 95  ? 33.530  -7.486  47.875 1.00 43.72  ? 113 PRO C CD     1 
ATOM   6516  N N      . LYS C 2 96  ? 36.833  -7.452  46.270 1.00 43.32  ? 114 LYS C N      1 
ATOM   6517  C CA     . LYS C 2 96  ? 38.068  -7.867  45.656 1.00 44.53  ? 114 LYS C CA     1 
ATOM   6518  C C      . LYS C 2 96  ? 38.577  -6.752  44.831 1.00 40.19  ? 114 LYS C C      1 
ATOM   6519  O O      . LYS C 2 96  ? 39.771  -6.574  44.699 1.00 40.71  ? 114 LYS C O      1 
ATOM   6520  C CB     . LYS C 2 96  ? 37.841  -9.066  44.766 1.00 42.41  ? 114 LYS C CB     1 
ATOM   6521  C CG     . LYS C 2 96  ? 37.217  -10.255 45.467 1.00 44.87  ? 114 LYS C CG     1 
ATOM   6522  C CD     . LYS C 2 96  ? 37.223  -11.471 44.562 1.00 49.06  ? 114 LYS C CD     1 
ATOM   6523  C CE     . LYS C 2 96  ? 36.695  -12.690 45.290 1.00 42.33  ? 114 LYS C CE     1 
ATOM   6524  N NZ     . LYS C 2 96  ? 36.812  -13.912 44.453 1.00 29.30  ? 114 LYS C NZ     1 
ATOM   6525  N N      . ASP C 2 97  ? 37.667  -6.004  44.236 1.00 41.44  ? 115 ASP C N      1 
ATOM   6526  C CA     . ASP C 2 97  ? 38.072  -4.907  43.380 1.00 51.29  ? 115 ASP C CA     1 
ATOM   6527  C C      . ASP C 2 97  ? 37.357  -3.592  43.570 1.00 49.46  ? 115 ASP C C      1 
ATOM   6528  O O      . ASP C 2 97  ? 36.760  -3.076  42.644 1.00 52.23  ? 115 ASP C O      1 
ATOM   6529  C CB     . ASP C 2 97  ? 38.006  -5.328  41.913 1.00 57.76  ? 115 ASP C CB     1 
ATOM   6530  C CG     . ASP C 2 97  ? 36.685  -5.939  41.525 1.00 57.46  ? 115 ASP C CG     1 
ATOM   6531  O OD1    . ASP C 2 97  ? 35.779  -6.001  42.369 1.00 53.84  ? 115 ASP C OD1    1 
ATOM   6532  O OD2    . ASP C 2 97  ? 36.552  -6.354  40.357 1.00 54.06  ? 115 ASP C OD2    1 
ATOM   6533  N N      . ASN C 2 98  ? 37.421  -3.029  44.763 1.00 48.75  ? 116 ASN C N      1 
ATOM   6534  C CA     . ASN C 2 98  ? 36.844  -1.725  44.996 1.00 50.63  ? 116 ASN C CA     1 
ATOM   6535  C C      . ASN C 2 98  ? 37.985  -0.801  44.724 1.00 48.77  ? 116 ASN C C      1 
ATOM   6536  O O      . ASN C 2 98  ? 38.539  -0.229  45.637 1.00 51.02  ? 116 ASN C O      1 
ATOM   6537  C CB     . ASN C 2 98  ? 36.340  -1.615  46.421 1.00 44.26  ? 116 ASN C CB     1 
ATOM   6538  C CG     . ASN C 2 98  ? 34.840  -1.590  46.505 1.00 53.19  ? 116 ASN C CG     1 
ATOM   6539  O OD1    . ASN C 2 98  ? 34.176  -0.913  45.729 1.00 58.78  ? 116 ASN C OD1    1 
ATOM   6540  N ND2    . ASN C 2 98  ? 34.295  -2.318  47.463 1.00 48.59  ? 116 ASN C ND2    1 
ATOM   6541  N N      . GLU C 2 99  ? 38.333  -0.624  43.468 1.00 48.44  ? 117 GLU C N      1 
ATOM   6542  C CA     . GLU C 2 99  ? 39.503  0.157   43.125 1.00 44.53  ? 117 GLU C CA     1 
ATOM   6543  C C      . GLU C 2 99  ? 39.576  1.639   43.449 1.00 39.20  ? 117 GLU C C      1 
ATOM   6544  O O      . GLU C 2 99  ? 40.644  2.132   43.743 1.00 46.15  ? 117 GLU C O      1 
ATOM   6545  C CB     . GLU C 2 99  ? 39.847  -0.106  41.674 1.00 49.83  ? 117 GLU C CB     1 
ATOM   6546  C CG     . GLU C 2 99  ? 40.128  -1.571  41.407 1.00 56.93  ? 117 GLU C CG     1 
ATOM   6547  C CD     . GLU C 2 99  ? 40.454  -1.845  39.961 1.00 66.66  ? 117 GLU C CD     1 
ATOM   6548  O OE1    . GLU C 2 99  ? 40.434  -0.891  39.162 1.00 62.89  ? 117 GLU C OE1    1 
ATOM   6549  O OE2    . GLU C 2 99  ? 40.729  -3.013  39.627 1.00 70.16  ? 117 GLU C OE2    1 
ATOM   6550  N N      . SER C 2 100 ? 38.492  2.371   43.311 1.00 37.72  ? 118 SER C N      1 
ATOM   6551  C CA     . SER C 2 100 ? 38.514  3.792   43.570 1.00 34.32  ? 118 SER C CA     1 
ATOM   6552  C C      . SER C 2 100 ? 38.780  4.091   44.988 1.00 34.75  ? 118 SER C C      1 
ATOM   6553  O O      . SER C 2 100 ? 39.558  4.976   45.301 1.00 32.21  ? 118 SER C O      1 
ATOM   6554  C CB     . SER C 2 100 ? 37.155  4.344   43.277 1.00 36.86  ? 118 SER C CB     1 
ATOM   6555  O OG     . SER C 2 100 ? 36.155  3.460   43.730 1.00 48.34  ? 118 SER C OG     1 
ATOM   6556  N N      . ARG C 2 101 ? 38.133  3.347   45.869 1.00 36.99  ? 119 ARG C N      1 
ATOM   6557  C CA     . ARG C 2 101 ? 38.267  3.568   47.291 1.00 35.09  ? 119 ARG C CA     1 
ATOM   6558  C C      . ARG C 2 101 ? 39.673  3.303   47.708 1.00 33.92  ? 119 ARG C C      1 
ATOM   6559  O O      . ARG C 2 101 ? 40.178  3.941   48.598 1.00 37.77  ? 119 ARG C O      1 
ATOM   6560  C CB     . ARG C 2 101 ? 37.316  2.643   48.021 1.00 30.56  ? 119 ARG C CB     1 
ATOM   6561  C CG     . ARG C 2 101 ? 37.361  2.705   49.528 1.00 39.88  ? 119 ARG C CG     1 
ATOM   6562  C CD     . ARG C 2 101 ? 36.613  3.907   50.057 1.00 43.85  ? 119 ARG C CD     1 
ATOM   6563  N NE     . ARG C 2 101 ? 36.712  3.977   51.506 1.00 39.03  ? 119 ARG C NE     1 
ATOM   6564  C CZ     . ARG C 2 101 ? 36.089  4.877   52.247 1.00 44.22  ? 119 ARG C CZ     1 
ATOM   6565  N NH1    . ARG C 2 101 ? 35.311  5.773   51.672 1.00 48.62  ? 119 ARG C NH1    1 
ATOM   6566  N NH2    . ARG C 2 101 ? 36.240  4.871   53.558 1.00 44.97  ? 119 ARG C NH2    1 
ATOM   6567  N N      . ARG C 2 102 ? 40.327  2.374   47.055 1.00 30.94  ? 120 ARG C N      1 
ATOM   6568  C CA     . ARG C 2 102 ? 41.690  2.045   47.373 1.00 31.82  ? 120 ARG C CA     1 
ATOM   6569  C C      . ARG C 2 102 ? 42.603  3.207   47.160 1.00 32.48  ? 120 ARG C C      1 
ATOM   6570  O O      . ARG C 2 102 ? 43.490  3.446   47.954 1.00 36.65  ? 120 ARG C O      1 
ATOM   6571  C CB     . ARG C 2 102 ? 42.144  0.892   46.510 1.00 31.92  ? 120 ARG C CB     1 
ATOM   6572  C CG     . ARG C 2 102 ? 41.463  -0.420  46.841 1.00 34.31  ? 120 ARG C CG     1 
ATOM   6573  C CD     . ARG C 2 102 ? 41.997  -1.575  46.016 1.00 37.40  ? 120 ARG C CD     1 
ATOM   6574  N NE     . ARG C 2 102 ? 41.240  -2.793  46.271 1.00 34.77  ? 120 ARG C NE     1 
ATOM   6575  C CZ     . ARG C 2 102 ? 41.619  -3.755  47.100 1.00 36.43  ? 120 ARG C CZ     1 
ATOM   6576  N NH1    . ARG C 2 102 ? 42.762  -3.661  47.747 1.00 37.14  ? 120 ARG C NH1    1 
ATOM   6577  N NH2    . ARG C 2 102 ? 40.860  -4.821  47.271 1.00 41.17  ? 120 ARG C NH2    1 
ATOM   6578  N N      . LEU C 2 103 ? 42.431  3.939   46.082 1.00 27.33  ? 121 LEU C N      1 
ATOM   6579  C CA     . LEU C 2 103 ? 43.228  5.134   45.908 1.00 31.11  ? 121 LEU C CA     1 
ATOM   6580  C C      . LEU C 2 103 ? 42.886  6.179   46.954 1.00 34.49  ? 121 LEU C C      1 
ATOM   6581  O O      . LEU C 2 103 ? 43.768  6.801   47.515 1.00 35.25  ? 121 LEU C O      1 
ATOM   6582  C CB     . LEU C 2 103 ? 43.091  5.685   44.503 1.00 27.91  ? 121 LEU C CB     1 
ATOM   6583  C CG     . LEU C 2 103 ? 43.983  6.850   44.105 1.00 29.86  ? 121 LEU C CG     1 
ATOM   6584  C CD1    . LEU C 2 103 ? 45.410  6.387   43.895 1.00 33.11  ? 121 LEU C CD1    1 
ATOM   6585  C CD2    . LEU C 2 103 ? 43.453  7.476   42.835 1.00 37.92  ? 121 LEU C CD2    1 
ATOM   6586  N N      . TYR C 2 104 ? 41.609  6.358   47.245 1.00 33.40  ? 122 TYR C N      1 
ATOM   6587  C CA     . TYR C 2 104 ? 41.201  7.372   48.195 1.00 34.72  ? 122 TYR C CA     1 
ATOM   6588  C C      . TYR C 2 104 ? 41.755  7.058   49.540 1.00 41.00  ? 122 TYR C C      1 
ATOM   6589  O O      . TYR C 2 104 ? 42.318  7.910   50.191 1.00 44.83  ? 122 TYR C O      1 
ATOM   6590  C CB     . TYR C 2 104 ? 39.687  7.398   48.251 1.00 33.39  ? 122 TYR C CB     1 
ATOM   6591  C CG     . TYR C 2 104 ? 39.038  8.258   49.297 1.00 39.14  ? 122 TYR C CG     1 
ATOM   6592  C CD1    . TYR C 2 104 ? 38.781  9.590   49.057 1.00 44.70  ? 122 TYR C CD1    1 
ATOM   6593  C CD2    . TYR C 2 104 ? 38.615  7.720   50.500 1.00 41.60  ? 122 TYR C CD2    1 
ATOM   6594  C CE1    . TYR C 2 104 ? 38.165  10.378  50.003 1.00 52.97  ? 122 TYR C CE1    1 
ATOM   6595  C CE2    . TYR C 2 104 ? 38.001  8.499   51.453 1.00 42.86  ? 122 TYR C CE2    1 
ATOM   6596  C CZ     . TYR C 2 104 ? 37.779  9.827   51.197 1.00 53.13  ? 122 TYR C CZ     1 
ATOM   6597  O OH     . TYR C 2 104 ? 37.167  10.609  52.135 1.00 51.74  ? 122 TYR C OH     1 
ATOM   6598  N N      . GLU C 2 105 ? 41.645  5.815   49.950 1.00 36.23  ? 123 GLU C N      1 
ATOM   6599  C CA     . GLU C 2 105 ? 42.133  5.411   51.239 1.00 32.82  ? 123 GLU C CA     1 
ATOM   6600  C C      . GLU C 2 105 ? 43.623  5.500   51.373 1.00 37.20  ? 123 GLU C C      1 
ATOM   6601  O O      . GLU C 2 105 ? 44.117  5.908   52.398 1.00 44.18  ? 123 GLU C O      1 
ATOM   6602  C CB     . GLU C 2 105 ? 41.645  4.027   51.569 1.00 30.80  ? 123 GLU C CB     1 
ATOM   6603  C CG     . GLU C 2 105 ? 40.204  3.978   52.025 1.00 37.61  ? 123 GLU C CG     1 
ATOM   6604  C CD     . GLU C 2 105 ? 39.788  2.588   52.439 1.00 44.53  ? 123 GLU C CD     1 
ATOM   6605  O OE1    . GLU C 2 105 ? 40.615  1.671   52.304 1.00 45.33  ? 123 GLU C OE1    1 
ATOM   6606  O OE2    . GLU C 2 105 ? 38.643  2.412   52.900 1.00 42.97  ? 123 GLU C OE2    1 
ATOM   6607  N N      . THR C 2 106 ? 44.353  5.122   50.345 1.00 34.95  ? 124 THR C N      1 
ATOM   6608  C CA     . THR C 2 106 ? 45.799  5.185   50.385 1.00 36.62  ? 124 THR C CA     1 
ATOM   6609  C C      . THR C 2 106 ? 46.259  6.610   50.528 1.00 39.99  ? 124 THR C C      1 
ATOM   6610  O O      . THR C 2 106 ? 47.220  6.882   51.226 1.00 35.11  ? 124 THR C O      1 
ATOM   6611  C CB     . THR C 2 106 ? 46.406  4.561   49.146 1.00 38.19  ? 124 THR C CB     1 
ATOM   6612  O OG1    . THR C 2 106 ? 46.019  3.188   49.072 1.00 42.19  ? 124 THR C OG1    1 
ATOM   6613  C CG2    . THR C 2 106 ? 47.903  4.644   49.206 1.00 40.76  ? 124 THR C CG2    1 
ATOM   6614  N N      . LEU C 2 107 ? 45.573  7.534   49.870 1.00 43.55  ? 125 LEU C N      1 
ATOM   6615  C CA     . LEU C 2 107 ? 45.948  8.931   49.923 1.00 43.23  ? 125 LEU C CA     1 
ATOM   6616  C C      . LEU C 2 107 ? 45.451  9.554   51.185 1.00 45.78  ? 125 LEU C C      1 
ATOM   6617  O O      . LEU C 2 107 ? 46.025  10.511  51.680 1.00 49.34  ? 125 LEU C O      1 
ATOM   6618  C CB     . LEU C 2 107 ? 45.372  9.666   48.732 1.00 38.53  ? 125 LEU C CB     1 
ATOM   6619  C CG     . LEU C 2 107 ? 45.940  9.320   47.362 1.00 41.65  ? 125 LEU C CG     1 
ATOM   6620  C CD1    . LEU C 2 107 ? 45.129  10.004  46.280 1.00 47.94  ? 125 LEU C CD1    1 
ATOM   6621  C CD2    . LEU C 2 107 ? 47.399  9.728   47.277 1.00 49.27  ? 125 LEU C CD2    1 
ATOM   6622  N N      . TYR C 2 108 ? 44.378  9.017   51.717 1.00 40.35  ? 126 TYR C N      1 
ATOM   6623  C CA     . TYR C 2 108 ? 43.872  9.508   52.980 1.00 44.18  ? 126 TYR C CA     1 
ATOM   6624  C C      . TYR C 2 108 ? 44.810  9.120   54.110 1.00 43.79  ? 126 TYR C C      1 
ATOM   6625  O O      . TYR C 2 108 ? 44.739  9.669   55.196 1.00 43.19  ? 126 TYR C O      1 
ATOM   6626  C CB     . TYR C 2 108 ? 42.456  9.009   53.185 1.00 37.33  ? 126 TYR C CB     1 
ATOM   6627  C CG     . TYR C 2 108 ? 41.970  8.905   54.590 1.00 38.33  ? 126 TYR C CG     1 
ATOM   6628  C CD1    . TYR C 2 108 ? 41.500  10.013  55.263 1.00 39.16  ? 126 TYR C CD1    1 
ATOM   6629  C CD2    . TYR C 2 108 ? 41.948  7.685   55.232 1.00 42.98  ? 126 TYR C CD2    1 
ATOM   6630  C CE1    . TYR C 2 108 ? 41.043  9.910   56.554 1.00 42.14  ? 126 TYR C CE1    1 
ATOM   6631  C CE2    . TYR C 2 108 ? 41.496  7.573   56.519 1.00 41.61  ? 126 TYR C CE2    1 
ATOM   6632  C CZ     . TYR C 2 108 ? 41.047  8.689   57.169 1.00 42.73  ? 126 TYR C CZ     1 
ATOM   6633  O OH     . TYR C 2 108 ? 40.596  8.560   58.442 1.00 48.38  ? 126 TYR C OH     1 
ATOM   6634  N N      . ALA C 2 109 ? 45.731  8.210   53.857 1.00 37.11  ? 127 ALA C N      1 
ATOM   6635  C CA     . ALA C 2 109 ? 46.642  7.809   54.884 1.00 37.57  ? 127 ALA C CA     1 
ATOM   6636  C C      . ALA C 2 109 ? 47.689  8.836   54.967 1.00 41.97  ? 127 ALA C C      1 
ATOM   6637  O O      . ALA C 2 109 ? 48.186  9.142   56.024 1.00 45.85  ? 127 ALA C O      1 
ATOM   6638  C CB     . ALA C 2 109 ? 47.261  6.519   54.522 1.00 36.11  ? 127 ALA C CB     1 
ATOM   6639  N N      . ASP C 2 110 ? 48.037  9.396   53.841 1.00 44.61  ? 128 ASP C N      1 
ATOM   6640  C CA     . ASP C 2 110 ? 49.036  10.426  53.825 1.00 48.97  ? 128 ASP C CA     1 
ATOM   6641  C C      . ASP C 2 110 ? 48.481  11.679  54.446 1.00 46.64  ? 128 ASP C C      1 
ATOM   6642  O O      . ASP C 2 110 ? 49.186  12.386  55.131 1.00 44.08  ? 128 ASP C O      1 
ATOM   6643  C CB     . ASP C 2 110 ? 49.452  10.713  52.394 1.00 56.39  ? 128 ASP C CB     1 
ATOM   6644  C CG     . ASP C 2 110 ? 50.121  9.534   51.732 1.00 56.35  ? 128 ASP C CG     1 
ATOM   6645  O OD1    . ASP C 2 110 ? 50.727  8.718   52.452 1.00 63.51  ? 128 ASP C OD1    1 
ATOM   6646  O OD2    . ASP C 2 110 ? 50.054  9.432   50.491 1.00 46.08  ? 128 ASP C OD2    1 
ATOM   6647  N N      . HIS C 2 111 ? 47.215  11.966  54.218 1.00 43.36  ? 129 HIS C N      1 
ATOM   6648  C CA     . HIS C 2 111 ? 46.610  13.138  54.822 1.00 48.92  ? 129 HIS C CA     1 
ATOM   6649  C C      . HIS C 2 111 ? 46.631  12.996  56.320 1.00 45.99  ? 129 HIS C C      1 
ATOM   6650  O O      . HIS C 2 111 ? 47.042  13.896  57.028 1.00 45.31  ? 129 HIS C O      1 
ATOM   6651  C CB     . HIS C 2 111 ? 45.184  13.313  54.322 1.00 52.30  ? 129 HIS C CB     1 
ATOM   6652  C CG     . HIS C 2 111 ? 44.729  14.736  54.233 1.00 53.05  ? 129 HIS C CG     1 
ATOM   6653  N ND1    . HIS C 2 111 ? 45.416  15.696  53.524 1.00 46.72  ? 129 HIS C ND1    1 
ATOM   6654  C CD2    . HIS C 2 111 ? 43.629  15.350  54.726 1.00 52.75  ? 129 HIS C CD2    1 
ATOM   6655  C CE1    . HIS C 2 111 ? 44.773  16.846  53.608 1.00 50.17  ? 129 HIS C CE1    1 
ATOM   6656  N NE2    . HIS C 2 111 ? 43.685  16.662  54.332 1.00 56.28  ? 129 HIS C NE2    1 
ATOM   6657  N N      . LEU C 2 112 ? 46.212  11.848  56.809 1.00 45.34  ? 130 LEU C N      1 
ATOM   6658  C CA     . LEU C 2 112 ? 46.178  11.623  58.236 1.00 43.05  ? 130 LEU C CA     1 
ATOM   6659  C C      . LEU C 2 112 ? 47.580  11.572  58.792 1.00 42.87  ? 130 LEU C C      1 
ATOM   6660  O O      . LEU C 2 112 ? 47.826  12.101  59.838 1.00 46.05  ? 130 LEU C O      1 
ATOM   6661  C CB     . LEU C 2 112 ? 45.404  10.355  58.550 1.00 40.15  ? 130 LEU C CB     1 
ATOM   6662  C CG     . LEU C 2 112 ? 44.819  10.025  59.910 1.00 36.54  ? 130 LEU C CG     1 
ATOM   6663  C CD1    . LEU C 2 112 ? 43.944  11.150  60.415 1.00 34.10  ? 130 LEU C CD1    1 
ATOM   6664  C CD2    . LEU C 2 112 ? 44.003  8.758   59.755 1.00 37.99  ? 130 LEU C CD2    1 
ATOM   6665  N N      . GLU C 2 113 ? 48.508  10.918  58.126 1.00 40.59  ? 131 GLU C N      1 
ATOM   6666  C CA     . GLU C 2 113 ? 49.863  10.893  58.607 1.00 39.01  ? 131 GLU C CA     1 
ATOM   6667  C C      . GLU C 2 113 ? 50.332  12.292  58.778 1.00 45.91  ? 131 GLU C C      1 
ATOM   6668  O O      . GLU C 2 113 ? 50.910  12.628  59.793 1.00 55.89  ? 131 GLU C O      1 
ATOM   6669  C CB     . GLU C 2 113 ? 50.780  10.199  57.625 1.00 41.74  ? 131 GLU C CB     1 
ATOM   6670  C CG     . GLU C 2 113 ? 52.257  10.304  57.951 1.00 42.95  ? 131 GLU C CG     1 
ATOM   6671  C CD     . GLU C 2 113 ? 52.872  8.962   58.270 1.00 59.99  ? 131 GLU C CD     1 
ATOM   6672  O OE1    . GLU C 2 113 ? 52.202  7.936   58.053 1.00 62.33  ? 131 GLU C OE1    1 
ATOM   6673  O OE2    . GLU C 2 113 ? 54.025  8.930   58.734 1.00 64.75  ? 131 GLU C OE2    1 
ATOM   6674  N N      . SER C 2 114 ? 50.063  13.149  57.808 1.00 48.36  ? 132 SER C N      1 
ATOM   6675  C CA     . SER C 2 114 ? 50.565  14.517  57.883 1.00 45.48  ? 132 SER C CA     1 
ATOM   6676  C C      . SER C 2 114 ? 49.864  15.327  58.954 1.00 44.61  ? 132 SER C C      1 
ATOM   6677  O O      . SER C 2 114 ? 50.474  16.179  59.570 1.00 44.79  ? 132 SER C O      1 
ATOM   6678  C CB     . SER C 2 114 ? 50.453  15.213  56.545 1.00 38.95  ? 132 SER C CB     1 
ATOM   6679  O OG     . SER C 2 114 ? 51.116  14.471  55.542 1.00 44.30  ? 132 SER C OG     1 
ATOM   6680  N N      . VAL C 2 115 ? 48.594  15.052  59.209 1.00 40.31  ? 133 VAL C N      1 
ATOM   6681  C CA     . VAL C 2 115 ? 47.868  15.762  60.236 1.00 38.15  ? 133 VAL C CA     1 
ATOM   6682  C C      . VAL C 2 115 ? 48.452  15.416  61.556 1.00 45.25  ? 133 VAL C C      1 
ATOM   6683  O O      . VAL C 2 115 ? 48.791  16.288  62.333 1.00 50.25  ? 133 VAL C O      1 
ATOM   6684  C CB     . VAL C 2 115 ? 46.393  15.386  60.227 1.00 35.72  ? 133 VAL C CB     1 
ATOM   6685  C CG1    . VAL C 2 115 ? 45.708  15.842  61.504 1.00 41.23  ? 133 VAL C CG1    1 
ATOM   6686  C CG2    . VAL C 2 115 ? 45.709  16.010  59.027 1.00 56.43  ? 133 VAL C CG2    1 
ATOM   6687  N N      . ILE C 2 116 ? 48.586  14.130  61.819 1.00 49.89  ? 134 ILE C N      1 
ATOM   6688  C CA     . ILE C 2 116 ? 49.079  13.679  63.097 1.00 44.19  ? 134 ILE C CA     1 
ATOM   6689  C C      . ILE C 2 116 ? 50.436  14.255  63.263 1.00 47.58  ? 134 ILE C C      1 
ATOM   6690  O O      . ILE C 2 116 ? 50.834  14.596  64.352 1.00 56.50  ? 134 ILE C O      1 
ATOM   6691  C CB     . ILE C 2 116 ? 49.152  12.152  63.148 1.00 40.55  ? 134 ILE C CB     1 
ATOM   6692  C CG1    . ILE C 2 116 ? 47.783  11.532  62.874 1.00 38.53  ? 134 ILE C CG1    1 
ATOM   6693  C CG2    . ILE C 2 116 ? 49.661  11.674  64.492 1.00 49.29  ? 134 ILE C CG2    1 
ATOM   6694  C CD1    . ILE C 2 116 ? 46.669  12.106  63.714 1.00 43.86  ? 134 ILE C CD1    1 
ATOM   6695  N N      . LYS C 2 117 ? 51.150  14.426  62.175 1.00 47.30  ? 135 LYS C N      1 
ATOM   6696  C CA     . LYS C 2 117 ? 52.511  14.898  62.290 1.00 49.13  ? 135 LYS C CA     1 
ATOM   6697  C C      . LYS C 2 117 ? 52.515  16.258  62.911 1.00 55.49  ? 135 LYS C C      1 
ATOM   6698  O O      . LYS C 2 117 ? 53.221  16.483  63.880 1.00 62.38  ? 135 LYS C O      1 
ATOM   6699  C CB     . LYS C 2 117 ? 53.189  14.942  60.936 1.00 47.88  ? 135 LYS C CB     1 
ATOM   6700  C CG     . LYS C 2 117 ? 54.696  15.054  60.984 1.00 46.65  ? 135 LYS C CG     1 
ATOM   6701  C CD     . LYS C 2 117 ? 55.289  14.826  59.608 1.00 52.26  ? 135 LYS C CD     1 
ATOM   6702  C CE     . LYS C 2 117 ? 56.799  14.946  59.648 1.00 46.79  ? 135 LYS C CE     1 
ATOM   6703  N NZ     . LYS C 2 117 ? 57.408  14.774  58.302 1.00 56.98  ? 135 LYS C NZ     1 
ATOM   6704  N N      . GLN C 2 118 ? 51.705  17.171  62.392 1.00 53.24  ? 136 GLN C N      1 
ATOM   6705  C CA     . GLN C 2 118 ? 51.734  18.547  62.872 1.00 56.98  ? 136 GLN C CA     1 
ATOM   6706  C C      . GLN C 2 118 ? 51.134  18.720  64.229 1.00 60.88  ? 136 GLN C C      1 
ATOM   6707  O O      . GLN C 2 118 ? 51.502  19.637  64.947 1.00 70.07  ? 136 GLN C O      1 
ATOM   6708  C CB     . GLN C 2 118 ? 51.054  19.483  61.889 1.00 54.85  ? 136 GLN C CB     1 
ATOM   6709  C CG     . GLN C 2 118 ? 51.783  19.608  60.563 1.00 67.27  ? 136 GLN C CG     1 
ATOM   6710  C CD     . GLN C 2 118 ? 53.119  20.313  60.696 1.00 72.58  ? 136 GLN C CD     1 
ATOM   6711  O OE1    . GLN C 2 118 ? 54.177  19.696  60.571 1.00 67.39  ? 136 GLN C OE1    1 
ATOM   6712  N NE2    . GLN C 2 118 ? 53.077  21.614  60.952 1.00 73.89  ? 136 GLN C NE2    1 
ATOM   6713  N N      . GLU C 2 119 ? 50.224  17.844  64.611 1.00 53.57  ? 137 GLU C N      1 
ATOM   6714  C CA     . GLU C 2 119 ? 49.550  18.029  65.879 1.00 55.15  ? 137 GLU C CA     1 
ATOM   6715  C C      . GLU C 2 119 ? 50.194  17.254  67.008 1.00 62.12  ? 137 GLU C C      1 
ATOM   6716  O O      . GLU C 2 119 ? 49.739  17.314  68.142 1.00 65.26  ? 137 GLU C O      1 
ATOM   6717  C CB     . GLU C 2 119 ? 48.067  17.677  65.752 1.00 52.84  ? 137 GLU C CB     1 
ATOM   6718  C CG     . GLU C 2 119 ? 47.755  16.197  65.623 1.00 64.10  ? 137 GLU C CG     1 
ATOM   6719  C CD     . GLU C 2 119 ? 46.297  15.894  65.891 1.00 65.20  ? 137 GLU C CD     1 
ATOM   6720  O OE1    . GLU C 2 119 ? 45.551  16.840  66.205 1.00 65.92  ? 137 GLU C OE1    1 
ATOM   6721  O OE2    . GLU C 2 119 ? 45.895  14.718  65.795 1.00 56.34  ? 137 GLU C OE2    1 
ATOM   6722  N N      . SER C 2 120 ? 51.275  16.554  66.725 1.00 56.85  ? 138 SER C N      1 
ATOM   6723  C CA     . SER C 2 120 ? 51.865  15.707  67.741 1.00 60.58  ? 138 SER C CA     1 
ATOM   6724  C C      . SER C 2 120 ? 53.268  16.044  68.135 1.00 64.74  ? 138 SER C C      1 
ATOM   6725  O O      . SER C 2 120 ? 54.110  16.312  67.290 1.00 61.24  ? 138 SER C O      1 
ATOM   6726  C CB     . SER C 2 120 ? 51.841  14.251  67.296 1.00 60.45  ? 138 SER C CB     1 
ATOM   6727  O OG     . SER C 2 120 ? 50.536  13.826  66.977 1.00 59.63  ? 138 SER C OG     1 
ATOM   6728  N N      . ASP C 2 121 ? 53.514  16.070  69.442 1.00 72.15  ? 139 ASP C N      1 
ATOM   6729  C CA     . ASP C 2 121 ? 54.861  16.306  69.943 1.00 66.17  ? 139 ASP C CA     1 
ATOM   6730  C C      . ASP C 2 121 ? 55.484  14.945  70.148 1.00 70.55  ? 139 ASP C C      1 
ATOM   6731  O O      . ASP C 2 121 ? 56.577  14.856  70.713 1.00 70.81  ? 139 ASP C O      1 
ATOM   6732  C CB     . ASP C 2 121 ? 54.855  17.139  71.232 1.00 66.12  ? 139 ASP C CB     1 
ATOM   6733  C CG     . ASP C 2 121 ? 53.861  16.635  72.274 1.00 81.55  ? 139 ASP C CG     1 
ATOM   6734  O OD1    . ASP C 2 121 ? 52.994  15.791  71.961 1.00 80.66  ? 139 ASP C OD1    1 
ATOM   6735  O OD2    . ASP C 2 121 ? 53.945  17.104  73.428 1.00 83.55  ? 139 ASP C OD2    1 
ATOM   6736  N N      . LEU C 2 122 ? 54.781  13.888  69.730 1.00 69.91  ? 140 LEU C N      1 
ATOM   6737  C CA     . LEU C 2 122 ? 55.307  12.542  69.786 1.00 63.23  ? 140 LEU C CA     1 
ATOM   6738  C C      . LEU C 2 122 ? 55.490  12.174  71.221 1.00 65.11  ? 140 LEU C C      1 
ATOM   6739  O O      . LEU C 2 122 ? 56.188  11.228  71.527 1.00 64.96  ? 140 LEU C O      1 
ATOM   6740  C CB     . LEU C 2 122 ? 56.586  12.390  68.974 1.00 54.71  ? 140 LEU C CB     1 
ATOM   6741  C CG     . LEU C 2 122 ? 56.514  12.664  67.479 1.00 56.90  ? 140 LEU C CG     1 
ATOM   6742  C CD1    . LEU C 2 122 ? 57.905  12.862  66.910 1.00 62.49  ? 140 LEU C CD1    1 
ATOM   6743  C CD2    . LEU C 2 122 ? 55.828  11.492  66.817 1.00 64.69  ? 140 LEU C CD2    1 
ATOM   6744  N N      . SER C 2 123 ? 54.890  12.933  72.115 1.00 62.41  ? 141 SER C N      1 
ATOM   6745  C CA     . SER C 2 123 ? 54.936  12.598  73.515 1.00 59.24  ? 141 SER C CA     1 
ATOM   6746  C C      . SER C 2 123 ? 54.179  11.355  73.813 1.00 56.24  ? 141 SER C C      1 
ATOM   6747  O O      . SER C 2 123 ? 54.617  10.549  74.604 1.00 53.47  ? 141 SER C O      1 
ATOM   6748  C CB     . SER C 2 123 ? 54.316  13.712  74.324 1.00 62.41  ? 141 SER C CB     1 
ATOM   6749  O OG     . SER C 2 123 ? 52.941  13.856  74.033 1.00 68.84  ? 141 SER C OG     1 
ATOM   6750  N N      . VAL C 2 124 ? 53.027  11.189  73.195 1.00 54.33  ? 142 VAL C N      1 
ATOM   6751  C CA     . VAL C 2 124 ? 52.192  10.062  73.540 1.00 52.96  ? 142 VAL C CA     1 
ATOM   6752  C C      . VAL C 2 124 ? 52.887  8.790   73.213 1.00 52.65  ? 142 VAL C C      1 
ATOM   6753  O O      . VAL C 2 124 ? 52.752  7.812   73.917 1.00 53.02  ? 142 VAL C O      1 
ATOM   6754  C CB     . VAL C 2 124 ? 50.823  10.130  72.868 1.00 48.16  ? 142 VAL C CB     1 
ATOM   6755  C CG1    . VAL C 2 124 ? 50.936  10.288  71.364 1.00 51.95  ? 142 VAL C CG1    1 
ATOM   6756  C CG2    . VAL C 2 124 ? 49.960  8.958   73.264 1.00 40.60  ? 142 VAL C CG2    1 
ATOM   6757  N N      . PHE C 2 125 ? 53.672  8.799   72.166 1.00 48.84  ? 143 PHE C N      1 
ATOM   6758  C CA     . PHE C 2 125 ? 54.287  7.582   71.778 1.00 45.41  ? 143 PHE C CA     1 
ATOM   6759  C C      . PHE C 2 125 ? 55.408  7.307   72.726 1.00 51.34  ? 143 PHE C C      1 
ATOM   6760  O O      . PHE C 2 125 ? 55.850  6.180   72.841 1.00 53.29  ? 143 PHE C O      1 
ATOM   6761  C CB     . PHE C 2 125 ? 54.740  7.674   70.341 1.00 47.27  ? 143 PHE C CB     1 
ATOM   6762  C CG     . PHE C 2 125 ? 53.608  7.857   69.376 1.00 49.89  ? 143 PHE C CG     1 
ATOM   6763  C CD1    . PHE C 2 125 ? 52.679  6.857   69.190 1.00 47.72  ? 143 PHE C CD1    1 
ATOM   6764  C CD2    . PHE C 2 125 ? 53.464  9.031   68.670 1.00 51.80  ? 143 PHE C CD2    1 
ATOM   6765  C CE1    . PHE C 2 125 ? 51.632  7.017   68.313 1.00 38.93  ? 143 PHE C CE1    1 
ATOM   6766  C CE2    . PHE C 2 125 ? 52.418  9.198   67.790 1.00 48.97  ? 143 PHE C CE2    1 
ATOM   6767  C CZ     . PHE C 2 125 ? 51.500  8.190   67.612 1.00 37.42  ? 143 PHE C CZ     1 
ATOM   6768  N N      . ASN C 2 126 ? 55.854  8.329   73.439 1.00 54.34  ? 144 ASN C N      1 
ATOM   6769  C CA     . ASN C 2 126 ? 56.949  8.156   74.376 1.00 50.51  ? 144 ASN C CA     1 
ATOM   6770  C C      . ASN C 2 126 ? 56.375  7.777   75.719 1.00 50.62  ? 144 ASN C C      1 
ATOM   6771  O O      . ASN C 2 126 ? 57.105  7.460   76.647 1.00 50.44  ? 144 ASN C O      1 
ATOM   6772  C CB     . ASN C 2 126 ? 57.821  9.403   74.432 1.00 39.63  ? 144 ASN C CB     1 
ATOM   6773  C CG     . ASN C 2 126 ? 58.891  9.412   73.375 1.00 43.13  ? 144 ASN C CG     1 
ATOM   6774  O OD1    . ASN C 2 126 ? 59.708  8.505   73.302 1.00 48.84  ? 144 ASN C OD1    1 
ATOM   6775  N ND2    . ASN C 2 126 ? 58.905  10.451  72.563 1.00 43.05  ? 144 ASN C ND2    1 
ATOM   6776  N N      . GLU C 2 127 ? 55.061  7.785   75.838 1.00 52.61  ? 145 GLU C N      1 
ATOM   6777  C CA     . GLU C 2 127 ? 54.425  7.367   77.074 1.00 48.86  ? 145 GLU C CA     1 
ATOM   6778  C C      . GLU C 2 127 ? 53.828  6.032   76.801 1.00 52.96  ? 145 GLU C C      1 
ATOM   6779  O O      . GLU C 2 127 ? 53.690  5.225   77.705 1.00 54.87  ? 145 GLU C O      1 
ATOM   6780  C CB     . GLU C 2 127 ? 53.329  8.338   77.472 1.00 57.59  ? 145 GLU C CB     1 
ATOM   6781  C CG     . GLU C 2 127 ? 53.800  9.763   77.703 1.00 62.56  ? 145 GLU C CG     1 
ATOM   6782  C CD     . GLU C 2 127 ? 52.673  10.714  78.057 1.00 57.85  ? 145 GLU C CD     1 
ATOM   6783  O OE1    . GLU C 2 127 ? 51.521  10.267  78.183 1.00 59.02  ? 145 GLU C OE1    1 
ATOM   6784  O OE2    . GLU C 2 127 ? 52.944  11.917  78.213 1.00 53.93  ? 145 GLU C OE2    1 
ATOM   6785  N N      . LEU C 2 128 ? 53.427  5.798   75.556 1.00 51.08  ? 146 LEU C N      1 
ATOM   6786  C CA     . LEU C 2 128 ? 52.845  4.529   75.172 1.00 45.01  ? 146 LEU C CA     1 
ATOM   6787  C C      . LEU C 2 128 ? 53.999  3.612   75.057 1.00 50.34  ? 146 LEU C C      1 
ATOM   6788  O O      . LEU C 2 128 ? 53.835  2.408   75.028 1.00 60.13  ? 146 LEU C O      1 
ATOM   6789  C CB     . LEU C 2 128 ? 52.175  4.625   73.822 1.00 40.97  ? 146 LEU C CB     1 
ATOM   6790  C CG     . LEU C 2 128 ? 51.325  3.470   73.323 1.00 43.01  ? 146 LEU C CG     1 
ATOM   6791  C CD1    . LEU C 2 128 ? 50.016  3.456   74.083 1.00 44.02  ? 146 LEU C CD1    1 
ATOM   6792  C CD2    . LEU C 2 128 ? 51.071  3.645   71.839 1.00 51.65  ? 146 LEU C CD2    1 
ATOM   6793  N N      . ARG C 2 129 ? 55.194  4.171   75.000 1.00 44.99  ? 147 ARG C N      1 
ATOM   6794  C CA     . ARG C 2 129 ? 56.364  3.348   74.832 1.00 45.13  ? 147 ARG C CA     1 
ATOM   6795  C C      . ARG C 2 129 ? 56.402  2.399   75.982 1.00 49.46  ? 147 ARG C C      1 
ATOM   6796  O O      . ARG C 2 129 ? 56.653  1.223   75.817 1.00 54.56  ? 147 ARG C O      1 
ATOM   6797  C CB     . ARG C 2 129 ? 57.611  4.191   74.792 1.00 43.36  ? 147 ARG C CB     1 
ATOM   6798  C CG     . ARG C 2 129 ? 58.822  3.500   74.214 1.00 53.33  ? 147 ARG C CG     1 
ATOM   6799  C CD     . ARG C 2 129 ? 59.868  4.529   73.837 1.00 54.90  ? 147 ARG C CD     1 
ATOM   6800  N NE     . ARG C 2 129 ? 60.000  5.563   74.850 1.00 46.61  ? 147 ARG C NE     1 
ATOM   6801  C CZ     . ARG C 2 129 ? 60.815  5.483   75.893 1.00 48.89  ? 147 ARG C CZ     1 
ATOM   6802  N NH1    . ARG C 2 129 ? 61.575  4.413   76.061 1.00 56.59  ? 147 ARG C NH1    1 
ATOM   6803  N NH2    . ARG C 2 129 ? 60.870  6.473   76.767 1.00 52.10  ? 147 ARG C NH2    1 
ATOM   6804  N N      . ASP C 2 130 ? 56.072  2.877   77.159 1.00 49.16  ? 148 ASP C N      1 
ATOM   6805  C CA     . ASP C 2 130 ? 56.177  2.047   78.335 1.00 48.12  ? 148 ASP C CA     1 
ATOM   6806  C C      . ASP C 2 130 ? 55.083  1.039   78.459 1.00 49.22  ? 148 ASP C C      1 
ATOM   6807  O O      . ASP C 2 130 ? 55.323  -0.060  78.920 1.00 56.58  ? 148 ASP C O      1 
ATOM   6808  C CB     . ASP C 2 130 ? 56.189  2.904   79.583 1.00 48.96  ? 148 ASP C CB     1 
ATOM   6809  C CG     . ASP C 2 130 ? 56.656  2.150   80.798 1.00 59.52  ? 148 ASP C CG     1 
ATOM   6810  O OD1    . ASP C 2 130 ? 57.642  1.394   80.688 1.00 53.56  ? 148 ASP C OD1    1 
ATOM   6811  O OD2    . ASP C 2 130 ? 56.045  2.325   81.869 1.00 73.60  ? 148 ASP C OD2    1 
ATOM   6812  N N      . SER C 2 131 ? 53.870  1.376   78.074 1.00 44.65  ? 149 SER C N      1 
ATOM   6813  C CA     . SER C 2 131 ? 52.819  0.422   78.283 1.00 45.61  ? 149 SER C CA     1 
ATOM   6814  C C      . SER C 2 131 ? 53.200  -0.801  77.491 1.00 51.50  ? 149 SER C C      1 
ATOM   6815  O O      . SER C 2 131 ? 52.943  -1.905  77.921 1.00 54.19  ? 149 SER C O      1 
ATOM   6816  C CB     . SER C 2 131 ? 51.478  0.954   77.869 1.00 41.73  ? 149 SER C CB     1 
ATOM   6817  O OG     . SER C 2 131 ? 51.100  2.042   78.679 1.00 53.51  ? 149 SER C OG     1 
ATOM   6818  N N      . TYR C 2 132 ? 53.872  -0.623  76.363 1.00 46.99  ? 150 TYR C N      1 
ATOM   6819  C CA     . TYR C 2 132 ? 54.230  -1.753  75.530 1.00 40.92  ? 150 TYR C CA     1 
ATOM   6820  C C      . TYR C 2 132 ? 55.214  -2.523  76.276 1.00 46.16  ? 150 TYR C C      1 
ATOM   6821  O O      . TYR C 2 132 ? 55.079  -3.715  76.402 1.00 52.47  ? 150 TYR C O      1 
ATOM   6822  C CB     . TYR C 2 132 ? 54.881  -1.317  74.249 1.00 41.14  ? 150 TYR C CB     1 
ATOM   6823  C CG     . TYR C 2 132 ? 55.595  -2.382  73.462 1.00 43.14  ? 150 TYR C CG     1 
ATOM   6824  C CD1    . TYR C 2 132 ? 54.895  -3.345  72.772 1.00 45.83  ? 150 TYR C CD1    1 
ATOM   6825  C CD2    . TYR C 2 132 ? 56.977  -2.388  73.370 1.00 43.80  ? 150 TYR C CD2    1 
ATOM   6826  C CE1    . TYR C 2 132 ? 55.550  -4.304  72.033 1.00 51.77  ? 150 TYR C CE1    1 
ATOM   6827  C CE2    . TYR C 2 132 ? 57.639  -3.344  72.638 1.00 42.09  ? 150 TYR C CE2    1 
ATOM   6828  C CZ     . TYR C 2 132 ? 56.917  -4.299  71.972 1.00 50.03  ? 150 TYR C CZ     1 
ATOM   6829  O OH     . TYR C 2 132 ? 57.563  -5.251  71.233 1.00 60.21  ? 150 TYR C OH     1 
ATOM   6830  N N      . ASN C 2 133 ? 56.233  -1.846  76.779 1.00 44.54  ? 151 ASN C N      1 
ATOM   6831  C CA     . ASN C 2 133 ? 57.301  -2.543  77.464 1.00 45.59  ? 151 ASN C CA     1 
ATOM   6832  C C      . ASN C 2 133 ? 56.766  -3.285  78.658 1.00 46.10  ? 151 ASN C C      1 
ATOM   6833  O O      . ASN C 2 133 ? 57.446  -4.130  79.206 1.00 50.32  ? 151 ASN C O      1 
ATOM   6834  C CB     . ASN C 2 133 ? 58.395  -1.592  77.909 1.00 43.89  ? 151 ASN C CB     1 
ATOM   6835  C CG     . ASN C 2 133 ? 59.065  -0.886  76.761 1.00 52.81  ? 151 ASN C CG     1 
ATOM   6836  O OD1    . ASN C 2 133 ? 58.907  -1.260  75.607 1.00 55.78  ? 151 ASN C OD1    1 
ATOM   6837  N ND2    . ASN C 2 133 ? 59.832  0.144   77.081 1.00 53.41  ? 151 ASN C ND2    1 
ATOM   6838  N N      . ALA C 2 134 ? 55.555  -2.977  79.078 1.00 40.79  ? 152 ALA C N      1 
ATOM   6839  C CA     . ALA C 2 134 ? 54.973  -3.714  80.176 1.00 39.36  ? 152 ALA C CA     1 
ATOM   6840  C C      . ALA C 2 134 ? 54.068  -4.807  79.722 1.00 40.16  ? 152 ALA C C      1 
ATOM   6841  O O      . ALA C 2 134 ? 53.973  -5.828  80.380 1.00 47.28  ? 152 ALA C O      1 
ATOM   6842  C CB     . ALA C 2 134 ? 54.230  -2.785  81.092 1.00 44.33  ? 152 ALA C CB     1 
ATOM   6843  N N      . VAL C 2 135 ? 53.377  -4.597  78.612 1.00 40.77  ? 153 VAL C N      1 
ATOM   6844  C CA     . VAL C 2 135 ? 52.440  -5.591  78.102 1.00 43.74  ? 153 VAL C CA     1 
ATOM   6845  C C      . VAL C 2 135 ? 53.056  -6.511  77.070 1.00 41.94  ? 153 VAL C C      1 
ATOM   6846  O O      . VAL C 2 135 ? 52.393  -7.384  76.554 1.00 42.05  ? 153 VAL C O      1 
ATOM   6847  C CB     . VAL C 2 135 ? 51.166  -4.952  77.541 1.00 39.84  ? 153 VAL C CB     1 
ATOM   6848  C CG1    . VAL C 2 135 ? 50.478  -4.104  78.592 1.00 36.36  ? 153 VAL C CG1    1 
ATOM   6849  C CG2    . VAL C 2 135 ? 51.459  -4.155  76.289 1.00 42.75  ? 153 VAL C CG2    1 
ATOM   6850  N N      . LYS C 2 136 ? 54.335  -6.321  76.821 1.00 41.90  ? 154 LYS C N      1 
ATOM   6851  C CA     . LYS C 2 136 ? 55.013  -7.101  75.829 1.00 39.06  ? 154 LYS C CA     1 
ATOM   6852  C C      . LYS C 2 136 ? 55.150  -8.560  76.181 1.00 46.78  ? 154 LYS C C      1 
ATOM   6853  O O      . LYS C 2 136 ? 55.322  -8.904  77.345 1.00 51.48  ? 154 LYS C O      1 
ATOM   6854  C CB     . LYS C 2 136 ? 56.404  -6.534  75.579 1.00 37.84  ? 154 LYS C CB     1 
ATOM   6855  C CG     . LYS C 2 136 ? 57.339  -6.593  76.765 1.00 40.80  ? 154 LYS C CG     1 
ATOM   6856  C CD     . LYS C 2 136 ? 58.780  -6.688  76.315 1.00 40.23  ? 154 LYS C CD     1 
ATOM   6857  C CE     . LYS C 2 136 ? 59.632  -7.271  77.425 1.00 44.33  ? 154 LYS C CE     1 
ATOM   6858  N NZ     . LYS C 2 136 ? 61.026  -7.521  76.976 1.00 50.60  ? 154 LYS C NZ     1 
ATOM   6859  N N      . PRO C 2 137 ? 55.068  -9.448  75.172 1.00 49.50  ? 155 PRO C N      1 
ATOM   6860  C CA     . PRO C 2 137 ? 55.325  -10.797 75.596 1.00 47.18  ? 155 PRO C CA     1 
ATOM   6861  C C      . PRO C 2 137 ? 56.808  -10.822 75.709 1.00 49.59  ? 155 PRO C C      1 
ATOM   6862  O O      . PRO C 2 137 ? 57.477  -10.134 74.972 1.00 53.28  ? 155 PRO C O      1 
ATOM   6863  C CB     . PRO C 2 137 ? 54.905  -11.605 74.400 1.00 41.77  ? 155 PRO C CB     1 
ATOM   6864  C CG     . PRO C 2 137 ? 53.946  -10.766 73.671 1.00 43.30  ? 155 PRO C CG     1 
ATOM   6865  C CD     . PRO C 2 137 ? 54.597  -9.443  73.774 1.00 48.70  ? 155 PRO C CD     1 
ATOM   6866  N N      . GLU C 2 138 ? 57.342  -11.625 76.597 1.00 47.26  ? 156 GLU C N      1 
ATOM   6867  C CA     . GLU C 2 138 ? 58.765  -11.713 76.779 1.00 47.66  ? 156 GLU C CA     1 
ATOM   6868  C C      . GLU C 2 138 ? 59.521  -11.868 75.492 1.00 44.44  ? 156 GLU C C      1 
ATOM   6869  O O      . GLU C 2 138 ? 60.682  -11.506 75.416 1.00 42.99  ? 156 GLU C O      1 
ATOM   6870  C CB     . GLU C 2 138 ? 59.062  -12.910 77.655 1.00 50.11  ? 156 GLU C CB     1 
ATOM   6871  C CG     . GLU C 2 138 ? 59.148  -12.595 79.137 1.00 62.50  ? 156 GLU C CG     1 
ATOM   6872  C CD     . GLU C 2 138 ? 57.814  -12.690 79.837 1.00 73.02  ? 156 GLU C CD     1 
ATOM   6873  O OE1    . GLU C 2 138 ? 56.847  -13.170 79.214 1.00 84.59  ? 156 GLU C OE1    1 
ATOM   6874  O OE2    . GLU C 2 138 ? 57.738  -12.291 81.016 1.00 67.40  ? 156 GLU C OE2    1 
ATOM   6875  N N      . TYR C 2 139 ? 58.888  -12.426 74.484 1.00 43.28  ? 157 TYR C N      1 
ATOM   6876  C CA     . TYR C 2 139 ? 59.562  -12.672 73.237 1.00 39.31  ? 157 TYR C CA     1 
ATOM   6877  C C      . TYR C 2 139 ? 60.016  -11.378 72.702 1.00 42.13  ? 157 TYR C C      1 
ATOM   6878  O O      . TYR C 2 139 ? 61.048  -11.308 72.054 1.00 39.63  ? 157 TYR C O      1 
ATOM   6879  C CB     . TYR C 2 139 ? 58.597  -13.278 72.224 1.00 37.78  ? 157 TYR C CB     1 
ATOM   6880  C CG     . TYR C 2 139 ? 57.872  -14.496 72.678 1.00 45.14  ? 157 TYR C CG     1 
ATOM   6881  C CD1    . TYR C 2 139 ? 58.562  -15.612 73.112 1.00 56.23  ? 157 TYR C CD1    1 
ATOM   6882  C CD2    . TYR C 2 139 ? 56.497  -14.548 72.639 1.00 38.10  ? 157 TYR C CD2    1 
ATOM   6883  C CE1    . TYR C 2 139 ? 57.896  -16.743 73.525 1.00 59.42  ? 157 TYR C CE1    1 
ATOM   6884  C CE2    . TYR C 2 139 ? 55.822  -15.673 73.044 1.00 43.41  ? 157 TYR C CE2    1 
ATOM   6885  C CZ     . TYR C 2 139 ? 56.526  -16.766 73.486 1.00 62.60  ? 157 TYR C CZ     1 
ATOM   6886  O OH     . TYR C 2 139 ? 55.853  -17.888 73.892 1.00 70.22  ? 157 TYR C OH     1 
ATOM   6887  N N      . ALA C 2 140 ? 59.265  -10.335 72.979 1.00 42.14  ? 158 ALA C N      1 
ATOM   6888  C CA     . ALA C 2 140 ? 59.547  -9.068  72.359 1.00 37.10  ? 158 ALA C CA     1 
ATOM   6889  C C      . ALA C 2 140 ? 60.585  -8.204  72.970 1.00 44.46  ? 158 ALA C C      1 
ATOM   6890  O O      . ALA C 2 140 ? 60.831  -8.256  74.158 1.00 55.61  ? 158 ALA C O      1 
ATOM   6891  C CB     . ALA C 2 140 ? 58.265  -8.304  72.250 1.00 40.01  ? 158 ALA C CB     1 
ATOM   6892  N N      . VAL C 2 141 ? 61.203  -7.391  72.142 1.00 48.04  ? 159 VAL C N      1 
ATOM   6893  C CA     . VAL C 2 141 ? 62.210  -6.492  72.624 1.00 48.65  ? 159 VAL C CA     1 
ATOM   6894  C C      . VAL C 2 141 ? 61.600  -5.276  73.259 1.00 47.38  ? 159 VAL C C      1 
ATOM   6895  O O      . VAL C 2 141 ? 60.439  -4.973  73.037 1.00 45.68  ? 159 VAL C O      1 
ATOM   6896  C CB     . VAL C 2 141 ? 63.169  -6.084  71.503 1.00 50.99  ? 159 VAL C CB     1 
ATOM   6897  C CG1    . VAL C 2 141 ? 64.086  -7.236  71.142 1.00 52.12  ? 159 VAL C CG1    1 
ATOM   6898  C CG2    . VAL C 2 141 ? 62.391  -5.615  70.285 1.00 54.76  ? 159 VAL C CG2    1 
ATOM   6899  N N      . THR C 2 142 ? 62.383  -4.570  74.057 1.00 52.22  ? 160 THR C N      1 
ATOM   6900  C CA     . THR C 2 142 ? 61.889  -3.401  74.738 1.00 55.81  ? 160 THR C CA     1 
ATOM   6901  C C      . THR C 2 142 ? 62.323  -2.162  74.005 1.00 55.81  ? 160 THR C C      1 
ATOM   6902  O O      . THR C 2 142 ? 63.489  -2.019  73.675 1.00 60.78  ? 160 THR C O      1 
ATOM   6903  C CB     . THR C 2 142 ? 62.475  -3.333  76.135 1.00 52.82  ? 160 THR C CB     1 
ATOM   6904  O OG1    . THR C 2 142 ? 63.748  -3.986  76.139 1.00 60.74  ? 160 THR C OG1    1 
ATOM   6905  C CG2    . THR C 2 142 ? 61.570  -4.024  77.121 1.00 52.53  ? 160 THR C CG2    1 
ATOM   6906  N N      . HIS C 2 143 ? 61.390  -1.254  73.755 1.00 50.50  ? 161 HIS C N      1 
ATOM   6907  C CA     . HIS C 2 143 ? 61.740  -0.032  73.095 1.00 55.82  ? 161 HIS C CA     1 
ATOM   6908  C C      . HIS C 2 143 ? 62.143  0.841   74.218 1.00 58.34  ? 161 HIS C C      1 
ATOM   6909  O O      . HIS C 2 143 ? 61.328  1.212   75.039 1.00 52.11  ? 161 HIS C O      1 
ATOM   6910  C CB     . HIS C 2 143 ? 60.548  0.564   72.382 1.00 51.04  ? 161 HIS C CB     1 
ATOM   6911  C CG     . HIS C 2 143 ? 60.905  1.421   71.212 1.00 54.08  ? 161 HIS C CG     1 
ATOM   6912  N ND1    . HIS C 2 143 ? 60.994  2.792   71.293 1.00 57.26  ? 161 HIS C ND1    1 
ATOM   6913  C CD2    . HIS C 2 143 ? 61.189  1.102   69.928 1.00 60.83  ? 161 HIS C CD2    1 
ATOM   6914  C CE1    . HIS C 2 143 ? 61.318  3.282   70.112 1.00 63.54  ? 161 HIS C CE1    1 
ATOM   6915  N NE2    . HIS C 2 143 ? 61.446  2.276   69.265 1.00 65.99  ? 161 HIS C NE2    1 
ATOM   6916  N N      . GLU C 2 144 ? 63.418  1.169   74.269 1.00 63.03  ? 162 GLU C N      1 
ATOM   6917  C CA     . GLU C 2 144 ? 63.920  1.969   75.355 1.00 67.46  ? 162 GLU C CA     1 
ATOM   6918  C C      . GLU C 2 144 ? 64.547  3.185   74.766 1.00 70.47  ? 162 GLU C C      1 
ATOM   6919  O O      . GLU C 2 144 ? 65.052  4.034   75.485 1.00 76.30  ? 162 GLU C O      1 
ATOM   6920  C CB     . GLU C 2 144 ? 64.951  1.200   76.170 1.00 74.56  ? 162 GLU C CB     1 
ATOM   6921  C CG     . GLU C 2 144 ? 64.351  0.154   77.095 1.00 74.13  ? 162 GLU C CG     1 
ATOM   6922  C CD     . GLU C 2 144 ? 65.399  -0.686  77.792 1.00 72.99  ? 162 GLU C CD     1 
ATOM   6923  O OE1    . GLU C 2 144 ? 66.589  -0.570  77.444 1.00 76.19  ? 162 GLU C OE1    1 
ATOM   6924  O OE2    . GLU C 2 144 ? 65.031  -1.469  78.686 1.00 66.94  ? 162 GLU C OE2    1 
ATOM   6925  N N      . THR C 2 145 ? 64.536  3.277   73.451 1.00 64.56  ? 163 THR C N      1 
ATOM   6926  C CA     . THR C 2 145 ? 65.043  4.462   72.809 1.00 67.62  ? 163 THR C CA     1 
ATOM   6927  C C      . THR C 2 145 ? 64.029  5.568   72.928 1.00 62.77  ? 163 THR C C      1 
ATOM   6928  O O      . THR C 2 145 ? 63.012  5.416   73.574 1.00 61.29  ? 163 THR C O      1 
ATOM   6929  C CB     . THR C 2 145 ? 65.356  4.204   71.339 1.00 73.08  ? 163 THR C CB     1 
ATOM   6930  O OG1    . THR C 2 145 ? 64.180  4.414   70.551 1.00 75.83  ? 163 THR C OG1    1 
ATOM   6931  C CG2    . THR C 2 145 ? 65.846  2.780   71.149 1.00 62.32  ? 163 THR C CG2    1 
ATOM   6932  N N      . GLU C 2 146 ? 64.300  6.707   72.326 1.00 62.48  ? 164 GLU C N      1 
ATOM   6933  C CA     . GLU C 2 146 ? 63.328  7.772   72.350 1.00 56.39  ? 164 GLU C CA     1 
ATOM   6934  C C      . GLU C 2 146 ? 62.779  8.000   70.976 1.00 60.62  ? 164 GLU C C      1 
ATOM   6935  O O      . GLU C 2 146 ? 63.480  7.859   69.986 1.00 63.66  ? 164 GLU C O      1 
ATOM   6936  C CB     . GLU C 2 146 ? 63.929  9.046   72.907 1.00 60.55  ? 164 GLU C CB     1 
ATOM   6937  C CG     . GLU C 2 146 ? 64.216  8.991   74.398 1.00 72.84  ? 164 GLU C CG     1 
ATOM   6938  C CD     . GLU C 2 146 ? 65.698  9.008   74.717 1.00 77.08  ? 164 GLU C CD     1 
ATOM   6939  O OE1    . GLU C 2 146 ? 66.484  9.483   73.873 1.00 78.45  ? 164 GLU C OE1    1 
ATOM   6940  O OE2    . GLU C 2 146 ? 66.077  8.557   75.818 1.00 71.69  ? 164 GLU C OE2    1 
ATOM   6941  N N      . ILE C 2 147 ? 61.508  8.356   70.905 1.00 58.11  ? 165 ILE C N      1 
ATOM   6942  C CA     . ILE C 2 147 ? 60.852  8.549   69.628 1.00 54.37  ? 165 ILE C CA     1 
ATOM   6943  C C      . ILE C 2 147 ? 60.870  9.995   69.172 1.00 55.06  ? 165 ILE C C      1 
ATOM   6944  O O      . ILE C 2 147 ? 60.049  10.798  69.591 1.00 51.84  ? 165 ILE C O      1 
ATOM   6945  C CB     . ILE C 2 147 ? 59.420  8.030   69.722 1.00 47.85  ? 165 ILE C CB     1 
ATOM   6946  C CG1    . ILE C 2 147 ? 59.438  6.578   70.185 1.00 52.85  ? 165 ILE C CG1    1 
ATOM   6947  C CG2    . ILE C 2 147 ? 58.719  8.151   68.387 1.00 48.91  ? 165 ILE C CG2    1 
ATOM   6948  C CD1    . ILE C 2 147 ? 58.074  5.945   70.272 1.00 53.39  ? 165 ILE C CD1    1 
ATOM   6949  N N      . LYS C 2 148 ? 61.802  10.334  68.299 1.00 54.50  ? 166 LYS C N      1 
ATOM   6950  C CA     . LYS C 2 148 ? 61.913  11.697  67.825 1.00 54.23  ? 166 LYS C CA     1 
ATOM   6951  C C      . LYS C 2 148 ? 61.483  11.871  66.370 1.00 62.42  ? 166 LYS C C      1 
ATOM   6952  O O      . LYS C 2 148 ? 61.610  12.955  65.818 1.00 67.38  ? 166 LYS C O      1 
ATOM   6953  C CB     . LYS C 2 148 ? 63.350  12.157  67.979 1.00 49.47  ? 166 LYS C CB     1 
ATOM   6954  C CG     . LYS C 2 148 ? 63.919  12.043  69.378 1.00 53.44  ? 166 LYS C CG     1 
ATOM   6955  C CD     . LYS C 2 148 ? 65.435  12.052  69.326 1.00 50.63  ? 166 LYS C CD     1 
ATOM   6956  C CE     . LYS C 2 148 ? 66.034  12.253  70.704 1.00 55.76  ? 166 LYS C CE     1 
ATOM   6957  N NZ     . LYS C 2 148 ? 65.741  13.620  71.210 1.00 63.46  ? 166 LYS C NZ     1 
ATOM   6958  N N      . THR C 2 149 ? 61.000  10.819  65.734 1.00 65.21  ? 167 THR C N      1 
ATOM   6959  C CA     . THR C 2 149 ? 60.550  10.911  64.364 1.00 65.59  ? 167 THR C CA     1 
ATOM   6960  C C      . THR C 2 149 ? 59.204  10.224  64.281 1.00 72.25  ? 167 THR C C      1 
ATOM   6961  O O      . THR C 2 149 ? 58.964  9.263   64.993 1.00 71.43  ? 167 THR C O      1 
ATOM   6962  C CB     . THR C 2 149 ? 61.533  10.177  63.456 1.00 68.77  ? 167 THR C CB     1 
ATOM   6963  O OG1    . THR C 2 149 ? 62.869  10.417  63.910 1.00 66.02  ? 167 THR C OG1    1 
ATOM   6964  C CG2    . THR C 2 149 ? 61.395  10.642  62.018 1.00 72.87  ? 167 THR C CG2    1 
ATOM   6965  N N      . LEU C 2 150 ? 58.298  10.710  63.439 1.00 68.82  ? 168 LEU C N      1 
ATOM   6966  C CA     . LEU C 2 150 ? 57.008  10.054  63.288 1.00 64.47  ? 168 LEU C CA     1 
ATOM   6967  C C      . LEU C 2 150 ? 57.231  8.695   62.724 1.00 65.59  ? 168 LEU C C      1 
ATOM   6968  O O      . LEU C 2 150 ? 56.451  7.788   62.957 1.00 61.23  ? 168 LEU C O      1 
ATOM   6969  C CB     . LEU C 2 150 ? 56.071  10.827  62.386 1.00 56.06  ? 168 LEU C CB     1 
ATOM   6970  C CG     . LEU C 2 150 ? 54.599  10.439  62.464 1.00 56.64  ? 168 LEU C CG     1 
ATOM   6971  C CD1    . LEU C 2 150 ? 54.053  10.715  63.850 1.00 57.40  ? 168 LEU C CD1    1 
ATOM   6972  C CD2    . LEU C 2 150 ? 53.795  11.190  61.423 1.00 57.57  ? 168 LEU C CD2    1 
ATOM   6973  N N      . ASP C 2 151 ? 58.327  8.539   62.011 1.00 62.25  ? 169 ASP C N      1 
ATOM   6974  C CA     . ASP C 2 151 ? 58.619  7.266   61.406 1.00 64.35  ? 169 ASP C CA     1 
ATOM   6975  C C      . ASP C 2 151 ? 59.096  6.314   62.482 1.00 70.37  ? 169 ASP C C      1 
ATOM   6976  O O      . ASP C 2 151 ? 58.982  5.108   62.328 1.00 72.55  ? 169 ASP C O      1 
ATOM   6977  C CB     . ASP C 2 151 ? 59.671  7.425   60.322 1.00 66.01  ? 169 ASP C CB     1 
ATOM   6978  C CG     . ASP C 2 151 ? 59.393  6.583   59.102 1.00 70.98  ? 169 ASP C CG     1 
ATOM   6979  O OD1    . ASP C 2 151 ? 58.318  5.966   59.037 1.00 75.60  ? 169 ASP C OD1    1 
ATOM   6980  O OD2    . ASP C 2 151 ? 60.256  6.542   58.203 1.00 75.69  ? 169 ASP C OD2    1 
ATOM   6981  N N      . GLU C 2 152 ? 59.619  6.834   63.580 1.00 59.91  ? 170 GLU C N      1 
ATOM   6982  C CA     . GLU C 2 152 ? 60.015  5.948   64.637 1.00 54.90  ? 170 GLU C CA     1 
ATOM   6983  C C      . GLU C 2 152 ? 58.818  5.643   65.458 1.00 56.20  ? 170 GLU C C      1 
ATOM   6984  O O      . GLU C 2 152 ? 58.769  4.620   66.112 1.00 63.80  ? 170 GLU C O      1 
ATOM   6985  C CB     . GLU C 2 152 ? 61.151  6.504   65.459 1.00 55.63  ? 170 GLU C CB     1 
ATOM   6986  C CG     . GLU C 2 152 ? 62.486  6.432   64.748 1.00 57.08  ? 170 GLU C CG     1 
ATOM   6987  C CD     . GLU C 2 152 ? 63.624  6.966   65.589 1.00 71.59  ? 170 GLU C CD     1 
ATOM   6988  O OE1    . GLU C 2 152 ? 63.353  7.644   66.601 1.00 70.17  ? 170 GLU C OE1    1 
ATOM   6989  O OE2    . GLU C 2 152 ? 64.790  6.707   65.231 1.00 73.48  ? 170 GLU C OE2    1 
ATOM   6990  N N      . ALA C 2 153 ? 57.816  6.496   65.419 1.00 51.11  ? 171 ALA C N      1 
ATOM   6991  C CA     . ALA C 2 153 ? 56.600  6.171   66.129 1.00 52.20  ? 171 ALA C CA     1 
ATOM   6992  C C      . ALA C 2 153 ? 55.961  5.027   65.418 1.00 56.13  ? 171 ALA C C      1 
ATOM   6993  O O      . ALA C 2 153 ? 55.427  4.136   66.046 1.00 57.29  ? 171 ALA C O      1 
ATOM   6994  C CB     . ALA C 2 153 ? 55.669  7.340   66.173 1.00 42.07  ? 171 ALA C CB     1 
ATOM   6995  N N      . LYS C 2 154 ? 56.032  5.038   64.095 1.00 60.24  ? 172 LYS C N      1 
ATOM   6996  C CA     . LYS C 2 154 ? 55.419  3.994   63.299 1.00 55.26  ? 172 LYS C CA     1 
ATOM   6997  C C      . LYS C 2 154 ? 56.121  2.699   63.524 1.00 54.20  ? 172 LYS C C      1 
ATOM   6998  O O      . LYS C 2 154 ? 55.485  1.684   63.693 1.00 59.39  ? 172 LYS C O      1 
ATOM   6999  C CB     . LYS C 2 154 ? 55.473  4.345   61.826 1.00 53.19  ? 172 LYS C CB     1 
ATOM   7000  C CG     . LYS C 2 154 ? 54.495  5.409   61.384 1.00 58.06  ? 172 LYS C CG     1 
ATOM   7001  C CD     . LYS C 2 154 ? 54.835  5.875   59.984 1.00 52.37  ? 172 LYS C CD     1 
ATOM   7002  C CE     . LYS C 2 154 ? 55.252  4.710   59.105 1.00 60.59  ? 172 LYS C CE     1 
ATOM   7003  N NZ     . LYS C 2 154 ? 54.131  3.777   58.812 1.00 64.65  ? 172 LYS C NZ     1 
ATOM   7004  N N      . GLN C 2 155 ? 57.439  2.714   63.525 1.00 51.29  ? 173 GLN C N      1 
ATOM   7005  C CA     . GLN C 2 155 ? 58.165  1.480   63.687 1.00 48.27  ? 173 GLN C CA     1 
ATOM   7006  C C      . GLN C 2 155 ? 57.692  0.895   64.969 1.00 47.30  ? 173 GLN C C      1 
ATOM   7007  O O      . GLN C 2 155 ? 57.443  -0.291  65.063 1.00 50.50  ? 173 GLN C O      1 
ATOM   7008  C CB     . GLN C 2 155 ? 59.658  1.719   63.763 1.00 43.79  ? 173 GLN C CB     1 
ATOM   7009  C CG     . GLN C 2 155 ? 60.310  2.093   62.447 1.00 53.34  ? 173 GLN C CG     1 
ATOM   7010  C CD     . GLN C 2 155 ? 61.813  2.214   62.572 1.00 59.80  ? 173 GLN C CD     1 
ATOM   7011  O OE1    . GLN C 2 155 ? 62.413  1.667   63.495 1.00 55.86  ? 173 GLN C OE1    1 
ATOM   7012  N NE2    . GLN C 2 155 ? 62.430  2.931   61.643 1.00 53.20  ? 173 GLN C NE2    1 
ATOM   7013  N N      . PHE C 2 156 ? 57.512  1.742   65.958 1.00 46.83  ? 174 PHE C N      1 
ATOM   7014  C CA     . PHE C 2 156 ? 57.087  1.280   67.258 1.00 51.75  ? 174 PHE C CA     1 
ATOM   7015  C C      . PHE C 2 156 ? 55.699  0.718   67.246 1.00 48.68  ? 174 PHE C C      1 
ATOM   7016  O O      . PHE C 2 156 ? 55.485  -0.389  67.688 1.00 50.44  ? 174 PHE C O      1 
ATOM   7017  C CB     . PHE C 2 156 ? 57.181  2.424   68.264 1.00 48.28  ? 174 PHE C CB     1 
ATOM   7018  C CG     . PHE C 2 156 ? 56.603  2.113   69.601 1.00 48.24  ? 174 PHE C CG     1 
ATOM   7019  C CD1    . PHE C 2 156 ? 57.137  1.113   70.384 1.00 50.34  ? 174 PHE C CD1    1 
ATOM   7020  C CD2    . PHE C 2 156 ? 55.538  2.840   70.082 1.00 41.02  ? 174 PHE C CD2    1 
ATOM   7021  C CE1    . PHE C 2 156 ? 56.605  0.829   71.616 1.00 46.10  ? 174 PHE C CE1    1 
ATOM   7022  C CE2    . PHE C 2 156 ? 54.999  2.563   71.313 1.00 40.88  ? 174 PHE C CE2    1 
ATOM   7023  C CZ     . PHE C 2 156 ? 55.533  1.553   72.078 1.00 44.65  ? 174 PHE C CZ     1 
ATOM   7024  N N      . ILE C 2 157 ? 54.732  1.473   66.763 1.00 44.47  ? 175 ILE C N      1 
ATOM   7025  C CA     . ILE C 2 157 ? 53.368  1.009   66.868 1.00 43.33  ? 175 ILE C CA     1 
ATOM   7026  C C      . ILE C 2 157 ? 53.121  -0.244  66.094 1.00 48.81  ? 175 ILE C C      1 
ATOM   7027  O O      . ILE C 2 157 ? 52.381  -1.102  66.516 1.00 55.08  ? 175 ILE C O      1 
ATOM   7028  C CB     . ILE C 2 157 ? 52.336  2.084   66.514 1.00 42.25  ? 175 ILE C CB     1 
ATOM   7029  C CG1    . ILE C 2 157 ? 52.559  2.631   65.115 1.00 48.64  ? 175 ILE C CG1    1 
ATOM   7030  C CG2    . ILE C 2 157 ? 52.366  3.204   67.535 1.00 41.38  ? 175 ILE C CG2    1 
ATOM   7031  C CD1    . ILE C 2 157 ? 51.456  3.553   64.662 1.00 47.07  ? 175 ILE C CD1    1 
ATOM   7032  N N      . LEU C 2 158 ? 53.736  -0.370  64.945 1.00 47.73  ? 176 LEU C N      1 
ATOM   7033  C CA     . LEU C 2 158 ? 53.460  -1.508  64.106 1.00 48.13  ? 176 LEU C CA     1 
ATOM   7034  C C      . LEU C 2 158 ? 54.032  -2.737  64.718 1.00 53.04  ? 176 LEU C C      1 
ATOM   7035  O O      . LEU C 2 158 ? 53.755  -3.827  64.256 1.00 58.66  ? 176 LEU C O      1 
ATOM   7036  C CB     . LEU C 2 158 ? 54.084  -1.311  62.724 1.00 46.01  ? 176 LEU C CB     1 
ATOM   7037  C CG     . LEU C 2 158 ? 53.697  -0.143  61.823 1.00 45.46  ? 176 LEU C CG     1 
ATOM   7038  C CD1    . LEU C 2 158 ? 54.561  -0.122  60.578 1.00 45.46  ? 176 LEU C CD1    1 
ATOM   7039  C CD2    . LEU C 2 158 ? 52.240  -0.220  61.444 1.00 48.51  ? 176 LEU C CD2    1 
ATOM   7040  N N      . SER C 2 159 ? 54.842  -2.586  65.752 1.00 48.92  ? 177 SER C N      1 
ATOM   7041  C CA     . SER C 2 159 ? 55.526  -3.736  66.330 1.00 45.21  ? 177 SER C CA     1 
ATOM   7042  C C      . SER C 2 159 ? 54.747  -4.267  67.468 1.00 49.15  ? 177 SER C C      1 
ATOM   7043  O O      . SER C 2 159 ? 55.270  -4.988  68.295 1.00 48.63  ? 177 SER C O      1 
ATOM   7044  C CB     . SER C 2 159 ? 56.916  -3.372  66.797 1.00 43.94  ? 177 SER C CB     1 
ATOM   7045  O OG     . SER C 2 159 ? 56.878  -2.595  67.975 1.00 51.40  ? 177 SER C OG     1 
ATOM   7046  N N      . PHE C 2 160 ? 53.488  -3.866  67.554 1.00 49.57  ? 178 PHE C N      1 
ATOM   7047  C CA     . PHE C 2 160 ? 52.621  -4.393  68.582 1.00 50.42  ? 178 PHE C CA     1 
ATOM   7048  C C      . PHE C 2 160 ? 52.147  -5.648  67.944 1.00 57.93  ? 178 PHE C C      1 
ATOM   7049  O O      . PHE C 2 160 ? 51.305  -6.342  68.480 1.00 56.25  ? 178 PHE C O      1 
ATOM   7050  C CB     . PHE C 2 160 ? 51.425  -3.507  68.829 1.00 44.85  ? 178 PHE C CB     1 
ATOM   7051  C CG     . PHE C 2 160 ? 51.742  -2.193  69.461 1.00 49.78  ? 178 PHE C CG     1 
ATOM   7052  C CD1    . PHE C 2 160 ? 52.922  -1.994  70.132 1.00 49.18  ? 178 PHE C CD1    1 
ATOM   7053  C CD2    . PHE C 2 160 ? 50.831  -1.160  69.395 1.00 47.77  ? 178 PHE C CD2    1 
ATOM   7054  C CE1    . PHE C 2 160 ? 53.200  -0.782  70.713 1.00 46.19  ? 178 PHE C CE1    1 
ATOM   7055  C CE2    . PHE C 2 160 ? 51.101  0.056   69.974 1.00 45.14  ? 178 PHE C CE2    1 
ATOM   7056  C CZ     . PHE C 2 160 ? 52.289  0.245   70.636 1.00 48.41  ? 178 PHE C CZ     1 
ATOM   7057  N N      . VAL C 2 161 ? 52.683  -5.952  66.772 1.00 59.03  ? 179 VAL C N      1 
ATOM   7058  C CA     . VAL C 2 161 ? 52.315  -7.164  66.078 1.00 47.21  ? 179 VAL C CA     1 
ATOM   7059  C C      . VAL C 2 161 ? 52.911  -8.326  66.818 1.00 58.59  ? 179 VAL C C      1 
ATOM   7060  O O      . VAL C 2 161 ? 52.438  -9.440  66.699 1.00 67.09  ? 179 VAL C O      1 
ATOM   7061  C CB     . VAL C 2 161 ? 52.811  -7.144  64.644 1.00 48.82  ? 179 VAL C CB     1 
ATOM   7062  C CG1    . VAL C 2 161 ? 54.326  -7.216  64.577 1.00 57.78  ? 179 VAL C CG1    1 
ATOM   7063  C CG2    . VAL C 2 161 ? 52.171  -8.250  63.826 1.00 63.81  ? 179 VAL C CG2    1 
ATOM   7064  N N      . MET C 2 162 ? 53.917  -8.071  67.642 1.00 58.31  ? 180 MET C N      1 
ATOM   7065  C CA     . MET C 2 162 ? 54.577  -9.143  68.360 1.00 55.43  ? 180 MET C CA     1 
ATOM   7066  C C      . MET C 2 162 ? 53.728  -9.619  69.495 1.00 54.53  ? 180 MET C C      1 
ATOM   7067  O O      . MET C 2 162 ? 53.888  -10.736 69.962 1.00 54.14  ? 180 MET C O      1 
ATOM   7068  C CB     . MET C 2 162 ? 55.900  -8.674  68.908 1.00 50.44  ? 180 MET C CB     1 
ATOM   7069  C CG     . MET C 2 162 ? 56.895  -8.247  67.848 1.00 62.03  ? 180 MET C CG     1 
ATOM   7070  S SD     . MET C 2 162 ? 57.640  -9.649  67.000 1.00 92.55  ? 180 MET C SD     1 
ATOM   7071  C CE     . MET C 2 162 ? 58.520  -10.427 68.349 1.00 59.00  ? 180 MET C CE     1 
ATOM   7072  N N      . LEU C 2 163 ? 52.821  -8.775  69.959 1.00 53.55  ? 181 LEU C N      1 
ATOM   7073  C CA     . LEU C 2 163 ? 52.004  -9.112  71.105 1.00 51.51  ? 181 LEU C CA     1 
ATOM   7074  C C      . LEU C 2 163 ? 50.923  -10.006 70.678 1.00 53.17  ? 181 LEU C C      1 
ATOM   7075  O O      . LEU C 2 163 ? 50.081  -10.383 71.457 1.00 51.71  ? 181 LEU C O      1 
ATOM   7076  C CB     . LEU C 2 163 ? 51.328  -7.882  71.676 1.00 48.99  ? 181 LEU C CB     1 
ATOM   7077  C CG     . LEU C 2 163 ? 51.870  -6.487  71.919 1.00 44.69  ? 181 LEU C CG     1 
ATOM   7078  C CD1    . LEU C 2 163 ? 50.806  -5.724  72.679 1.00 38.90  ? 181 LEU C CD1    1 
ATOM   7079  C CD2    . LEU C 2 163 ? 53.105  -6.558  72.769 1.00 49.23  ? 181 LEU C CD2    1 
ATOM   7080  N N      . ASN C 2 164 ? 50.910  -10.351 69.421 1.00 55.11  ? 182 ASN C N      1 
ATOM   7081  C CA     . ASN C 2 164 ? 49.804  -11.116 68.934 1.00 53.12  ? 182 ASN C CA     1 
ATOM   7082  C C      . ASN C 2 164 ? 49.895  -12.527 69.381 1.00 55.10  ? 182 ASN C C      1 
ATOM   7083  O O      . ASN C 2 164 ? 50.974  -12.988 69.673 1.00 54.12  ? 182 ASN C O      1 
ATOM   7084  C CB     . ASN C 2 164 ? 49.709  -11.046 67.407 1.00 48.56  ? 182 ASN C CB     1 
ATOM   7085  C CG     . ASN C 2 164 ? 49.027  -9.805  66.918 1.00 55.23  ? 182 ASN C CG     1 
ATOM   7086  O OD1    . ASN C 2 164 ? 49.059  -8.774  67.569 1.00 65.40  ? 182 ASN C OD1    1 
ATOM   7087  N ND2    . ASN C 2 164 ? 48.410  -9.897  65.756 1.00 44.22  ? 182 ASN C ND2    1 
ATOM   7088  N N      . ASP C 2 165 ? 48.766  -13.195 69.479 1.00 51.40  ? 183 ASP C N      1 
ATOM   7089  C CA     . ASP C 2 165 ? 48.721  -14.600 69.796 1.00 49.76  ? 183 ASP C CA     1 
ATOM   7090  C C      . ASP C 2 165 ? 48.968  -15.016 71.213 1.00 54.84  ? 183 ASP C C      1 
ATOM   7091  O O      . ASP C 2 165 ? 49.034  -16.198 71.479 1.00 61.15  ? 183 ASP C O      1 
ATOM   7092  C CB     . ASP C 2 165 ? 49.485  -15.417 68.785 1.00 54.60  ? 183 ASP C CB     1 
ATOM   7093  C CG     . ASP C 2 165 ? 49.004  -15.181 67.371 1.00 63.96  ? 183 ASP C CG     1 
ATOM   7094  O OD1    . ASP C 2 165 ? 47.786  -15.010 67.183 1.00 65.15  ? 183 ASP C OD1    1 
ATOM   7095  O OD2    . ASP C 2 165 ? 49.839  -15.165 66.446 1.00 59.11  ? 183 ASP C OD2    1 
ATOM   7096  N N      . ASN C 2 166 ? 49.121  -14.079 72.126 1.00 50.59  ? 184 ASN C N      1 
ATOM   7097  C CA     . ASN C 2 166 ? 49.211  -14.414 73.534 1.00 45.83  ? 184 ASN C CA     1 
ATOM   7098  C C      . ASN C 2 166 ? 48.388  -13.395 74.260 1.00 46.65  ? 184 ASN C C      1 
ATOM   7099  O O      . ASN C 2 166 ? 47.369  -13.716 74.848 1.00 44.11  ? 184 ASN C O      1 
ATOM   7100  C CB     . ASN C 2 166 ? 50.637  -14.460 74.094 1.00 38.91  ? 184 ASN C CB     1 
ATOM   7101  C CG     . ASN C 2 166 ? 51.673  -13.871 73.176 1.00 49.41  ? 184 ASN C CG     1 
ATOM   7102  O OD1    . ASN C 2 166 ? 51.429  -12.891 72.492 1.00 45.98  ? 184 ASN C OD1    1 
ATOM   7103  N ND2    . ASN C 2 166 ? 52.862  -14.448 73.195 1.00 64.60  ? 184 ASN C ND2    1 
ATOM   7104  N N      . VAL C 2 167 ? 48.844  -12.158 74.247 1.00 49.03  ? 185 VAL C N      1 
ATOM   7105  C CA     . VAL C 2 167 ? 48.107  -11.084 74.878 1.00 50.78  ? 185 VAL C CA     1 
ATOM   7106  C C      . VAL C 2 167 ? 46.800  -10.777 74.174 1.00 46.36  ? 185 VAL C C      1 
ATOM   7107  O O      . VAL C 2 167 ? 45.813  -10.461 74.811 1.00 46.30  ? 185 VAL C O      1 
ATOM   7108  C CB     . VAL C 2 167 ? 49.003  -9.862  75.134 1.00 41.65  ? 185 VAL C CB     1 
ATOM   7109  C CG1    . VAL C 2 167 ? 50.444  -10.295 75.306 1.00 36.60  ? 185 VAL C CG1    1 
ATOM   7110  C CG2    . VAL C 2 167 ? 48.879  -8.843  74.028 1.00 35.21  ? 185 VAL C CG2    1 
ATOM   7111  N N      . GLU C 2 168 ? 46.779  -10.880 72.865 1.00 44.68  ? 186 GLU C N      1 
ATOM   7112  C CA     . GLU C 2 168 ? 45.600  -10.547 72.107 1.00 43.49  ? 186 GLU C CA     1 
ATOM   7113  C C      . GLU C 2 168 ? 44.365  -11.350 72.383 1.00 45.43  ? 186 GLU C C      1 
ATOM   7114  O O      . GLU C 2 168 ? 43.281  -10.809 72.415 1.00 41.39  ? 186 GLU C O      1 
ATOM   7115  C CB     . GLU C 2 168 ? 45.952  -10.612 70.626 1.00 44.95  ? 186 GLU C CB     1 
ATOM   7116  C CG     . GLU C 2 168 ? 45.763  -11.936 69.919 1.00 51.24  ? 186 GLU C CG     1 
ATOM   7117  C CD     . GLU C 2 168 ? 45.867  -11.802 68.415 1.00 65.76  ? 186 GLU C CD     1 
ATOM   7118  O OE1    . GLU C 2 168 ? 46.046  -10.671 67.933 1.00 68.67  ? 186 GLU C OE1    1 
ATOM   7119  O OE2    . GLU C 2 168 ? 45.770  -12.824 67.710 1.00 69.42  ? 186 GLU C OE2    1 
ATOM   7120  N N      . LEU C 2 169 ? 44.502  -12.631 72.632 1.00 50.80  ? 187 LEU C N      1 
ATOM   7121  C CA     . LEU C 2 169 ? 43.357  -13.507 72.767 1.00 49.84  ? 187 LEU C CA     1 
ATOM   7122  C C      . LEU C 2 169 ? 42.325  -13.260 73.851 1.00 48.61  ? 187 LEU C C      1 
ATOM   7123  O O      . LEU C 2 169 ? 41.153  -13.436 73.602 1.00 43.77  ? 187 LEU C O      1 
ATOM   7124  C CB     . LEU C 2 169 ? 43.867  -14.940 72.840 1.00 41.72  ? 187 LEU C CB     1 
ATOM   7125  C CG     . LEU C 2 169 ? 44.917  -15.396 71.840 1.00 45.14  ? 187 LEU C CG     1 
ATOM   7126  C CD1    . LEU C 2 169 ? 45.580  -16.655 72.363 1.00 46.25  ? 187 LEU C CD1    1 
ATOM   7127  C CD2    . LEU C 2 169 ? 44.278  -15.655 70.491 1.00 56.74  ? 187 LEU C CD2    1 
ATOM   7128  N N      . PRO C 2 170 ? 42.728  -12.890 75.053 1.00 49.77  ? 188 PRO C N      1 
ATOM   7129  C CA     . PRO C 2 170 ? 41.667  -12.649 76.014 1.00 45.41  ? 188 PRO C CA     1 
ATOM   7130  C C      . PRO C 2 170 ? 40.638  -11.643 75.578 1.00 53.19  ? 188 PRO C C      1 
ATOM   7131  O O      . PRO C 2 170 ? 39.542  -11.676 76.106 1.00 54.80  ? 188 PRO C O      1 
ATOM   7132  C CB     . PRO C 2 170 ? 42.423  -12.091 77.172 1.00 41.61  ? 188 PRO C CB     1 
ATOM   7133  C CG     . PRO C 2 170 ? 43.684  -12.868 77.171 1.00 46.40  ? 188 PRO C CG     1 
ATOM   7134  C CD     . PRO C 2 170 ? 44.029  -13.030 75.724 1.00 46.77  ? 188 PRO C CD     1 
ATOM   7135  N N      . LEU C 2 171 ? 40.973  -10.752 74.661 1.00 48.94  ? 189 LEU C N      1 
ATOM   7136  C CA     . LEU C 2 171 ? 40.025  -9.789  74.130 1.00 40.62  ? 189 LEU C CA     1 
ATOM   7137  C C      . LEU C 2 171 ? 39.314  -10.256 72.885 1.00 48.20  ? 189 LEU C C      1 
ATOM   7138  O O      . LEU C 2 171 ? 38.224  -9.800  72.606 1.00 52.91  ? 189 LEU C O      1 
ATOM   7139  C CB     . LEU C 2 171 ? 40.721  -8.479  73.803 1.00 41.29  ? 189 LEU C CB     1 
ATOM   7140  C CG     . LEU C 2 171 ? 40.856  -7.358  74.831 1.00 46.43  ? 189 LEU C CG     1 
ATOM   7141  C CD1    . LEU C 2 171 ? 41.834  -7.723  75.934 1.00 51.85  ? 189 LEU C CD1    1 
ATOM   7142  C CD2    . LEU C 2 171 ? 41.324  -6.102  74.119 1.00 38.37  ? 189 LEU C CD2    1 
ATOM   7143  N N      . LYS C 2 172 ? 39.908  -11.155 72.121 1.00 49.43  ? 190 LYS C N      1 
ATOM   7144  C CA     . LYS C 2 172 ? 39.320  -11.565 70.858 1.00 45.06  ? 190 LYS C CA     1 
ATOM   7145  C C      . LYS C 2 172 ? 38.132  -12.413 71.115 1.00 41.11  ? 190 LYS C C      1 
ATOM   7146  O O      . LYS C 2 172 ? 37.233  -12.501 70.304 1.00 48.96  ? 190 LYS C O      1 
ATOM   7147  C CB     . LYS C 2 172 ? 40.356  -12.332 70.052 1.00 39.06  ? 190 LYS C CB     1 
ATOM   7148  C CG     . LYS C 2 172 ? 39.976  -12.642 68.622 1.00 41.63  ? 190 LYS C CG     1 
ATOM   7149  C CD     . LYS C 2 172 ? 40.938  -13.651 68.025 1.00 44.68  ? 190 LYS C CD     1 
ATOM   7150  C CE     . LYS C 2 172 ? 42.345  -13.095 67.952 1.00 45.63  ? 190 LYS C CE     1 
ATOM   7151  N NZ     . LYS C 2 172 ? 43.249  -14.016 67.213 1.00 41.24  ? 190 LYS C NZ     1 
ATOM   7152  N N      . ALA C 2 173 ? 38.105  -13.042 72.262 1.00 31.94  ? 191 ALA C N      1 
ATOM   7153  C CA     . ALA C 2 173 ? 37.041  -13.968 72.546 1.00 36.10  ? 191 ALA C CA     1 
ATOM   7154  C C      . ALA C 2 173 ? 35.765  -13.277 72.786 1.00 40.03  ? 191 ALA C C      1 
ATOM   7155  O O      . ALA C 2 173 ? 34.705  -13.882 72.748 1.00 40.39  ? 191 ALA C O      1 
ATOM   7156  C CB     . ALA C 2 173 ? 37.391  -14.773 73.765 1.00 40.34  ? 191 ALA C CB     1 
ATOM   7157  N N      . GLN C 2 174 ? 35.834  -11.993 73.021 1.00 36.11  ? 192 GLN C N      1 
ATOM   7158  C CA     . GLN C 2 174 ? 34.633  -11.304 73.365 1.00 37.90  ? 192 GLN C CA     1 
ATOM   7159  C C      . GLN C 2 174 ? 34.020  -10.725 72.124 1.00 55.29  ? 192 GLN C C      1 
ATOM   7160  O O      . GLN C 2 174 ? 32.866  -10.330 72.141 1.00 67.76  ? 192 GLN C O      1 
ATOM   7161  C CB     . GLN C 2 174 ? 34.965  -10.240 74.381 1.00 44.61  ? 192 GLN C CB     1 
ATOM   7162  C CG     . GLN C 2 174 ? 35.974  -10.696 75.414 1.00 46.17  ? 192 GLN C CG     1 
ATOM   7163  C CD     . GLN C 2 174 ? 36.262  -9.637  76.448 1.00 45.13  ? 192 GLN C CD     1 
ATOM   7164  O OE1    . GLN C 2 174 ? 35.478  -8.713  76.640 1.00 48.11  ? 192 GLN C OE1    1 
ATOM   7165  N NE2    . GLN C 2 174 ? 37.389  -9.771  77.128 1.00 43.56  ? 192 GLN C NE2    1 
ATOM   7166  N N      . SER C 2 175 ? 34.775  -10.696 71.037 1.00 56.65  ? 193 SER C N      1 
ATOM   7167  C CA     . SER C 2 175 ? 34.306  -10.077 69.809 1.00 48.60  ? 193 SER C CA     1 
ATOM   7168  C C      . SER C 2 175 ? 33.406  -10.945 69.036 1.00 49.81  ? 193 SER C C      1 
ATOM   7169  O O      . SER C 2 175 ? 33.663  -12.123 68.894 1.00 50.12  ? 193 SER C O      1 
ATOM   7170  C CB     . SER C 2 175 ? 35.479  -9.772  68.928 1.00 46.24  ? 193 SER C CB     1 
ATOM   7171  O OG     . SER C 2 175 ? 35.052  -9.346  67.654 1.00 51.62  ? 193 SER C OG     1 
ATOM   7172  N N      . GLU C 2 176 ? 32.335  -10.370 68.533 1.00 49.26  ? 194 GLU C N      1 
ATOM   7173  C CA     . GLU C 2 176 ? 31.402  -11.122 67.727 1.00 56.16  ? 194 GLU C CA     1 
ATOM   7174  C C      . GLU C 2 176 ? 31.610  -10.927 66.232 1.00 53.53  ? 194 GLU C C      1 
ATOM   7175  O O      . GLU C 2 176 ? 30.910  -11.531 65.431 1.00 55.66  ? 194 GLU C O      1 
ATOM   7176  C CB     . GLU C 2 176 ? 29.982  -10.746 68.126 1.00 59.45  ? 194 GLU C CB     1 
ATOM   7177  C CG     . GLU C 2 176 ? 29.758  -10.741 69.628 1.00 56.99  ? 194 GLU C CG     1 
ATOM   7178  C CD     . GLU C 2 176 ? 28.422  -10.144 70.023 1.00 66.89  ? 194 GLU C CD     1 
ATOM   7179  O OE1    . GLU C 2 176 ? 27.544  -10.007 69.147 1.00 70.17  ? 194 GLU C OE1    1 
ATOM   7180  O OE2    . GLU C 2 176 ? 28.250  -9.815  71.214 1.00 60.28  ? 194 GLU C OE2    1 
ATOM   7181  N N      . ARG C 2 177 ? 32.554  -10.078 65.853 1.00 50.45  ? 195 ARG C N      1 
ATOM   7182  C CA     . ARG C 2 177 ? 32.817  -9.804  64.451 1.00 49.32  ? 195 ARG C CA     1 
ATOM   7183  C C      . ARG C 2 177 ? 33.998  -10.553 63.926 1.00 47.01  ? 195 ARG C C      1 
ATOM   7184  O O      . ARG C 2 177 ? 34.023  -10.930 62.776 1.00 45.58  ? 195 ARG C O      1 
ATOM   7185  C CB     . ARG C 2 177 ? 33.071  -8.321  64.286 1.00 47.53  ? 195 ARG C CB     1 
ATOM   7186  C CG     . ARG C 2 177 ? 31.914  -7.464  64.771 1.00 47.98  ? 195 ARG C CG     1 
ATOM   7187  C CD     . ARG C 2 177 ? 32.177  -5.978  64.601 1.00 47.51  ? 195 ARG C CD     1 
ATOM   7188  N NE     . ARG C 2 177 ? 31.049  -5.187  65.084 1.00 52.75  ? 195 ARG C NE     1 
ATOM   7189  C CZ     . ARG C 2 177 ? 30.981  -3.863  65.017 1.00 57.09  ? 195 ARG C CZ     1 
ATOM   7190  N NH1    . ARG C 2 177 ? 31.972  -3.172  64.484 1.00 52.37  ? 195 ARG C NH1    1 
ATOM   7191  N NH2    . ARG C 2 177 ? 29.915  -3.229  65.478 1.00 58.82  ? 195 ARG C NH2    1 
ATOM   7192  N N      . TYR C 2 178 ? 34.990  -10.761 64.760 1.00 41.51  ? 196 TYR C N      1 
ATOM   7193  C CA     . TYR C 2 178 ? 36.178  -11.470 64.353 1.00 35.77  ? 196 TYR C CA     1 
ATOM   7194  C C      . TYR C 2 178 ? 35.908  -12.901 63.998 1.00 38.42  ? 196 TYR C C      1 
ATOM   7195  O O      . TYR C 2 178 ? 36.596  -13.459 63.164 1.00 40.15  ? 196 TYR C O      1 
ATOM   7196  C CB     . TYR C 2 178 ? 37.286  -11.351 65.376 1.00 34.44  ? 196 TYR C CB     1 
ATOM   7197  C CG     . TYR C 2 178 ? 38.675  -11.497 64.812 1.00 36.45  ? 196 TYR C CG     1 
ATOM   7198  C CD1    . TYR C 2 178 ? 39.333  -10.419 64.257 1.00 40.97  ? 196 TYR C CD1    1 
ATOM   7199  C CD2    . TYR C 2 178 ? 39.331  -12.709 64.851 1.00 38.39  ? 196 TYR C CD2    1 
ATOM   7200  C CE1    . TYR C 2 178 ? 40.606  -10.552 63.748 1.00 43.17  ? 196 TYR C CE1    1 
ATOM   7201  C CE2    . TYR C 2 178 ? 40.603  -12.849 64.346 1.00 36.20  ? 196 TYR C CE2    1 
ATOM   7202  C CZ     . TYR C 2 178 ? 41.235  -11.768 63.798 1.00 36.48  ? 196 TYR C CZ     1 
ATOM   7203  O OH     . TYR C 2 178 ? 42.501  -11.924 63.300 1.00 33.56  ? 196 TYR C OH     1 
ATOM   7204  N N      . PRO C 2 179 ? 34.902  -13.522 64.606 1.00 39.99  ? 197 PRO C N      1 
ATOM   7205  C CA     . PRO C 2 179 ? 34.705  -14.893 64.169 1.00 37.07  ? 197 PRO C CA     1 
ATOM   7206  C C      . PRO C 2 179 ? 34.425  -15.015 62.701 1.00 40.34  ? 197 PRO C C      1 
ATOM   7207  O O      . PRO C 2 179 ? 34.644  -16.087 62.160 1.00 39.39  ? 197 PRO C O      1 
ATOM   7208  C CB     . PRO C 2 179 ? 33.470  -15.289 64.933 1.00 40.01  ? 197 PRO C CB     1 
ATOM   7209  C CG     . PRO C 2 179 ? 33.646  -14.632 66.245 1.00 47.86  ? 197 PRO C CG     1 
ATOM   7210  C CD     . PRO C 2 179 ? 34.363  -13.345 65.969 1.00 44.28  ? 197 PRO C CD     1 
ATOM   7211  N N      . LYS C 2 180 ? 34.060  -13.934 62.039 1.00 41.47  ? 198 LYS C N      1 
ATOM   7212  C CA     . LYS C 2 180 ? 33.674  -13.998 60.638 1.00 35.20  ? 198 LYS C CA     1 
ATOM   7213  C C      . LYS C 2 180 ? 34.713  -13.467 59.716 1.00 34.20  ? 198 LYS C C      1 
ATOM   7214  O O      . LYS C 2 180 ? 34.398  -12.878 58.715 1.00 34.69  ? 198 LYS C O      1 
ATOM   7215  C CB     . LYS C 2 180 ? 32.363  -13.287 60.460 1.00 32.25  ? 198 LYS C CB     1 
ATOM   7216  C CG     . LYS C 2 180 ? 31.206  -14.056 61.072 1.00 35.88  ? 198 LYS C CG     1 
ATOM   7217  C CD     . LYS C 2 180 ? 30.036  -13.162 61.422 1.00 40.73  ? 198 LYS C CD     1 
ATOM   7218  C CE     . LYS C 2 180 ? 28.797  -13.989 61.708 1.00 38.57  ? 198 LYS C CE     1 
ATOM   7219  N NZ     . LYS C 2 180 ? 29.068  -15.045 62.717 1.00 39.07  ? 198 LYS C NZ     1 
ATOM   7220  N N      . LYS C 2 181 ? 35.964  -13.691 60.057 1.00 33.98  ? 199 LYS C N      1 
ATOM   7221  C CA     . LYS C 2 181 ? 37.054  -13.257 59.225 1.00 38.36  ? 199 LYS C CA     1 
ATOM   7222  C C      . LYS C 2 181 ? 37.163  -14.059 57.980 1.00 37.30  ? 199 LYS C C      1 
ATOM   7223  O O      . LYS C 2 181 ? 36.985  -15.262 57.996 1.00 36.07  ? 199 LYS C O      1 
ATOM   7224  C CB     . LYS C 2 181 ? 38.364  -13.313 59.974 1.00 41.32  ? 199 LYS C CB     1 
ATOM   7225  C CG     . LYS C 2 181 ? 39.491  -12.502 59.372 1.00 41.50  ? 199 LYS C CG     1 
ATOM   7226  C CD     . LYS C 2 181 ? 40.702  -12.494 60.281 1.00 37.78  ? 199 LYS C CD     1 
ATOM   7227  C CE     . LYS C 2 181 ? 41.875  -11.804 59.615 1.00 40.01  ? 199 LYS C CE     1 
ATOM   7228  N NZ     . LYS C 2 181 ? 43.036  -11.605 60.521 1.00 37.27  ? 199 LYS C NZ     1 
ATOM   7229  N N      . ASP C 2 182 ? 37.497  -13.392 56.895 1.00 38.07  ? 200 ASP C N      1 
ATOM   7230  C CA     . ASP C 2 182 ? 37.560  -14.031 55.614 1.00 40.76  ? 200 ASP C CA     1 
ATOM   7231  C C      . ASP C 2 182 ? 38.932  -14.295 55.045 1.00 44.73  ? 200 ASP C C      1 
ATOM   7232  O O      . ASP C 2 182 ? 39.037  -14.589 53.876 1.00 46.89  ? 200 ASP C O      1 
ATOM   7233  C CB     . ASP C 2 182 ? 36.882  -13.122 54.622 1.00 50.40  ? 200 ASP C CB     1 
ATOM   7234  C CG     . ASP C 2 182 ? 35.442  -12.839 54.960 1.00 56.22  ? 200 ASP C CG     1 
ATOM   7235  O OD1    . ASP C 2 182 ? 34.963  -13.310 55.997 1.00 56.88  ? 200 ASP C OD1    1 
ATOM   7236  O OD2    . ASP C 2 182 ? 34.775  -12.139 54.179 1.00 53.40  ? 200 ASP C OD2    1 
ATOM   7237  N N      . ARG C 2 183 ? 39.996  -14.151 55.798 1.00 39.11  ? 201 ARG C N      1 
ATOM   7238  C CA     . ARG C 2 183 ? 41.266  -14.370 55.187 1.00 40.01  ? 201 ARG C CA     1 
ATOM   7239  C C      . ARG C 2 183 ? 41.318  -15.843 55.035 1.00 48.52  ? 201 ARG C C      1 
ATOM   7240  O O      . ARG C 2 183 ? 41.102  -16.565 55.990 1.00 50.67  ? 201 ARG C O      1 
ATOM   7241  C CB     . ARG C 2 183 ? 42.371  -13.861 56.075 1.00 33.07  ? 201 ARG C CB     1 
ATOM   7242  C CG     . ARG C 2 183 ? 43.777  -14.178 55.624 1.00 35.86  ? 201 ARG C CG     1 
ATOM   7243  C CD     . ARG C 2 183 ? 44.783  -13.387 56.434 1.00 33.69  ? 201 ARG C CD     1 
ATOM   7244  N NE     . ARG C 2 183 ? 46.107  -13.410 55.828 1.00 36.78  ? 201 ARG C NE     1 
ATOM   7245  C CZ     . ARG C 2 183 ? 47.123  -12.666 56.245 1.00 41.92  ? 201 ARG C CZ     1 
ATOM   7246  N NH1    . ARG C 2 183 ? 46.961  -11.842 57.264 1.00 49.13  ? 201 ARG C NH1    1 
ATOM   7247  N NH2    . ARG C 2 183 ? 48.297  -12.738 55.643 1.00 40.31  ? 201 ARG C NH2    1 
ATOM   7248  N N      . SER C 2 184 ? 41.607  -16.309 53.834 1.00 53.36  ? 202 SER C N      1 
ATOM   7249  C CA     . SER C 2 184 ? 41.659  -17.712 53.589 1.00 56.48  ? 202 SER C CA     1 
ATOM   7250  C C      . SER C 2 184 ? 42.961  -18.046 54.103 1.00 58.01  ? 202 SER C C      1 
ATOM   7251  O O      . SER C 2 184 ? 43.857  -17.229 54.100 1.00 56.76  ? 202 SER C O      1 
ATOM   7252  C CB     . SER C 2 184 ? 41.702  -18.029 52.137 1.00 56.38  ? 202 SER C CB     1 
ATOM   7253  O OG     . SER C 2 184 ? 42.930  -17.595 51.607 1.00 58.44  ? 202 SER C OG     1 
ATOM   7254  N N      . ARG C 2 185 ? 43.116  -19.282 54.488 1.00 57.00  ? 203 ARG C N      1 
ATOM   7255  C CA     . ARG C 2 185 ? 44.326  -19.686 55.117 1.00 60.13  ? 203 ARG C CA     1 
ATOM   7256  C C      . ARG C 2 185 ? 45.364  -20.126 54.129 1.00 65.97  ? 203 ARG C C      1 
ATOM   7257  O O      . ARG C 2 185 ? 46.422  -20.590 54.518 1.00 66.90  ? 203 ARG C O      1 
ATOM   7258  C CB     . ARG C 2 185 ? 43.950  -20.842 55.991 1.00 60.86  ? 203 ARG C CB     1 
ATOM   7259  C CG     . ARG C 2 185 ? 42.997  -21.792 55.285 1.00 68.24  ? 203 ARG C CG     1 
ATOM   7260  C CD     . ARG C 2 185 ? 42.100  -22.549 56.248 1.00 68.37  ? 203 ARG C CD     1 
ATOM   7261  N NE     . ARG C 2 185 ? 41.099  -21.691 56.873 1.00 66.86  ? 203 ARG C NE     1 
ATOM   7262  C CZ     . ARG C 2 185 ? 41.185  -21.223 58.112 1.00 64.59  ? 203 ARG C CZ     1 
ATOM   7263  N NH1    . ARG C 2 185 ? 42.227  -21.537 58.871 1.00 65.22  ? 203 ARG C NH1    1 
ATOM   7264  N NH2    . ARG C 2 185 ? 40.224  -20.448 58.594 1.00 61.58  ? 203 ARG C NH2    1 
ATOM   7265  N N      . GLU C 2 186 ? 45.076  -19.991 52.847 1.00 58.06  ? 204 GLU C N      1 
ATOM   7266  C CA     . GLU C 2 186 ? 45.998  -20.450 51.854 1.00 55.67  ? 204 GLU C CA     1 
ATOM   7267  C C      . GLU C 2 186 ? 47.179  -19.574 51.852 1.00 48.87  ? 204 GLU C C      1 
ATOM   7268  O O      . GLU C 2 186 ? 47.033  -18.371 51.869 1.00 54.40  ? 204 GLU C O      1 
ATOM   7269  C CB     . GLU C 2 186 ? 45.367  -20.327 50.496 1.00 62.79  ? 204 GLU C CB     1 
ATOM   7270  C CG     . GLU C 2 186 ? 44.074  -21.086 50.276 1.00 69.40  ? 204 GLU C CG     1 
ATOM   7271  C CD     . GLU C 2 186 ? 43.630  -21.033 48.825 1.00 67.04  ? 204 GLU C CD     1 
ATOM   7272  O OE1    . GLU C 2 186 ? 44.405  -21.471 47.953 1.00 65.47  ? 204 GLU C OE1    1 
ATOM   7273  O OE2    . GLU C 2 186 ? 42.512  -20.555 48.552 1.00 65.70  ? 204 GLU C OE2    1 
ATOM   7274  N N      . GLU C 2 187 ? 48.363  -20.149 51.808 1.00 48.84  ? 205 GLU C N      1 
ATOM   7275  C CA     . GLU C 2 187 ? 49.539  -19.331 51.690 1.00 53.67  ? 205 GLU C CA     1 
ATOM   7276  C C      . GLU C 2 187 ? 49.881  -19.152 50.255 1.00 64.11  ? 205 GLU C C      1 
ATOM   7277  O O      . GLU C 2 187 ? 50.743  -19.838 49.742 1.00 71.69  ? 205 GLU C O      1 
ATOM   7278  C CB     . GLU C 2 187 ? 50.711  -19.900 52.432 1.00 61.89  ? 205 GLU C CB     1 
ATOM   7279  C CG     . GLU C 2 187 ? 51.691  -18.844 52.899 1.00 71.23  ? 205 GLU C CG     1 
ATOM   7280  C CD     . GLU C 2 187 ? 51.138  -18.023 54.041 1.00 72.28  ? 205 GLU C CD     1 
ATOM   7281  O OE1    . GLU C 2 187 ? 50.425  -18.597 54.889 1.00 67.48  ? 205 GLU C OE1    1 
ATOM   7282  O OE2    . GLU C 2 187 ? 51.424  -16.808 54.093 1.00 76.74  ? 205 GLU C OE2    1 
ATOM   7283  N N      . LEU C 2 188 ? 49.194  -18.241 49.593 1.00 63.58  ? 206 LEU C N      1 
ATOM   7284  C CA     . LEU C 2 188 ? 49.445  -17.962 48.211 1.00 54.93  ? 206 LEU C CA     1 
ATOM   7285  C C      . LEU C 2 188 ? 50.789  -17.328 47.965 1.00 62.03  ? 206 LEU C C      1 
ATOM   7286  O O      . LEU C 2 188 ? 51.416  -17.618 46.963 1.00 67.94  ? 206 LEU C O      1 
ATOM   7287  C CB     . LEU C 2 188 ? 48.323  -17.127 47.641 1.00 56.40  ? 206 LEU C CB     1 
ATOM   7288  C CG     . LEU C 2 188 ? 46.948  -17.779 47.644 1.00 56.07  ? 206 LEU C CG     1 
ATOM   7289  C CD1    . LEU C 2 188 ? 45.966  -16.883 46.914 1.00 54.55  ? 206 LEU C CD1    1 
ATOM   7290  C CD2    . LEU C 2 188 ? 47.020  -19.144 46.982 1.00 58.50  ? 206 LEU C CD2    1 
ATOM   7291  N N      . GLY C 2 189 ? 51.242  -16.453 48.845 1.00 58.29  ? 207 GLY C N      1 
ATOM   7292  C CA     . GLY C 2 189 ? 52.563  -15.884 48.669 1.00 61.92  ? 207 GLY C CA     1 
ATOM   7293  C C      . GLY C 2 189 ? 52.771  -14.454 48.230 1.00 55.96  ? 207 GLY C C      1 
ATOM   7294  O O      . GLY C 2 189 ? 51.916  -13.614 48.427 1.00 53.60  ? 207 GLY C O      1 
ATOM   7295  N N      . ASN C 2 190 ? 53.930  -14.163 47.661 1.00 58.82  ? 208 ASN C N      1 
ATOM   7296  C CA     . ASN C 2 190 ? 54.269  -12.804 47.260 1.00 66.07  ? 208 ASN C CA     1 
ATOM   7297  C C      . ASN C 2 190 ? 54.291  -12.449 45.770 1.00 62.60  ? 208 ASN C C      1 
ATOM   7298  O O      . ASN C 2 190 ? 54.754  -13.250 44.969 1.00 56.26  ? 208 ASN C O      1 
ATOM   7299  C CB     . ASN C 2 190 ? 55.620  -12.450 47.856 1.00 74.09  ? 208 ASN C CB     1 
ATOM   7300  C CG     . ASN C 2 190 ? 55.597  -12.365 49.365 1.00 72.84  ? 208 ASN C CG     1 
ATOM   7301  O OD1    . ASN C 2 190 ? 54.859  -13.084 50.030 1.00 74.65  ? 208 ASN C OD1    1 
ATOM   7302  N ND2    . ASN C 2 190 ? 56.426  -11.488 49.915 1.00 63.50  ? 208 ASN C ND2    1 
ATOM   7303  N N      . THR C 2 191 ? 53.775  -11.265 45.400 1.00 60.68  ? 209 THR C N      1 
ATOM   7304  C CA     . THR C 2 191 ? 53.752  -10.780 44.012 1.00 57.21  ? 209 THR C CA     1 
ATOM   7305  C C      . THR C 2 191 ? 54.203  -9.346  44.115 1.00 51.98  ? 209 THR C C      1 
ATOM   7306  O O      . THR C 2 191 ? 53.815  -8.685  45.037 1.00 52.98  ? 209 THR C O      1 
ATOM   7307  C CB     . THR C 2 191 ? 52.343  -10.725 43.471 1.00 56.51  ? 209 THR C CB     1 
ATOM   7308  O OG1    . THR C 2 191 ? 51.481  -10.180 44.468 1.00 65.71  ? 209 THR C OG1    1 
ATOM   7309  C CG2    . THR C 2 191 ? 51.862  -12.103 43.119 1.00 58.79  ? 209 THR C CG2    1 
ATOM   7310  N N      . PRO C 2 192 ? 55.023  -8.837  43.177 1.00 49.57  ? 210 PRO C N      1 
ATOM   7311  C CA     . PRO C 2 192 ? 55.444  -7.467  43.444 1.00 45.54  ? 210 PRO C CA     1 
ATOM   7312  C C      . PRO C 2 192 ? 54.467  -6.394  43.056 1.00 47.04  ? 210 PRO C C      1 
ATOM   7313  O O      . PRO C 2 192 ? 53.544  -6.682  42.316 1.00 44.41  ? 210 PRO C O      1 
ATOM   7314  C CB     . PRO C 2 192 ? 56.704  -7.331  42.604 1.00 41.18  ? 210 PRO C CB     1 
ATOM   7315  C CG     . PRO C 2 192 ? 57.203  -8.712  42.423 1.00 51.40  ? 210 PRO C CG     1 
ATOM   7316  C CD     . PRO C 2 192 ? 55.939  -9.466  42.200 1.00 53.73  ? 210 PRO C CD     1 
ATOM   7317  N N      . SER C 2 193 ? 54.652  -5.180  43.571 1.00 46.45  ? 211 SER C N      1 
ATOM   7318  C CA     . SER C 2 193 ? 53.785  -4.065  43.253 1.00 38.05  ? 211 SER C CA     1 
ATOM   7319  C C      . SER C 2 193 ? 54.505  -2.756  43.289 1.00 38.10  ? 211 SER C C      1 
ATOM   7320  O O      . SER C 2 193 ? 55.469  -2.611  44.009 1.00 39.07  ? 211 SER C O      1 
ATOM   7321  C CB     . SER C 2 193 ? 52.623  -4.019  44.222 1.00 37.14  ? 211 SER C CB     1 
ATOM   7322  O OG     . SER C 2 193 ? 51.856  -2.851  44.071 1.00 40.66  ? 211 SER C OG     1 
ATOM   7323  N N      . ALA C 2 194 ? 54.065  -1.805  42.489 1.00 44.62  ? 212 ALA C N      1 
ATOM   7324  C CA     . ALA C 2 194 ? 54.620  -0.470  42.513 1.00 43.89  ? 212 ALA C CA     1 
ATOM   7325  C C      . ALA C 2 194 ? 53.515  0.429   42.893 1.00 39.88  ? 212 ALA C C      1 
ATOM   7326  O O      . ALA C 2 194 ? 53.567  1.612   42.649 1.00 39.84  ? 212 ALA C O      1 
ATOM   7327  C CB     . ALA C 2 194 ? 55.098  -0.078  41.164 1.00 41.18  ? 212 ALA C CB     1 
ATOM   7328  N N      . ASN C 2 195 ? 52.476  -0.142  43.448 1.00 41.93  ? 213 ASN C N      1 
ATOM   7329  C CA     . ASN C 2 195 ? 51.344  0.631   43.836 1.00 41.09  ? 213 ASN C CA     1 
ATOM   7330  C C      . ASN C 2 195 ? 51.274  0.786   45.366 1.00 41.95  ? 213 ASN C C      1 
ATOM   7331  O O      . ASN C 2 195 ? 51.442  -0.191  46.064 1.00 43.24  ? 213 ASN C O      1 
ATOM   7332  C CB     . ASN C 2 195 ? 50.078  -0.004  43.306 1.00 42.70  ? 213 ASN C CB     1 
ATOM   7333  C CG     . ASN C 2 195 ? 49.918  0.174   41.826 1.00 45.70  ? 213 ASN C CG     1 
ATOM   7334  O OD1    . ASN C 2 195 ? 50.657  0.922   41.200 1.00 49.14  ? 213 ASN C OD1    1 
ATOM   7335  N ND2    . ASN C 2 195 ? 48.942  -0.506  41.257 1.00 44.98  ? 213 ASN C ND2    1 
ATOM   7336  N N      . PRO C 2 196 ? 51.032  2.009   45.895 1.00 44.36  ? 214 PRO C N      1 
ATOM   7337  C CA     . PRO C 2 196 ? 51.022  2.209   47.336 1.00 38.34  ? 214 PRO C CA     1 
ATOM   7338  C C      . PRO C 2 196 ? 49.840  1.734   48.097 1.00 39.96  ? 214 PRO C C      1 
ATOM   7339  O O      . PRO C 2 196 ? 48.740  1.832   47.625 1.00 48.81  ? 214 PRO C O      1 
ATOM   7340  C CB     . PRO C 2 196 ? 51.019  3.715   47.459 1.00 42.48  ? 214 PRO C CB     1 
ATOM   7341  C CG     . PRO C 2 196 ? 51.424  4.254   46.137 1.00 43.97  ? 214 PRO C CG     1 
ATOM   7342  C CD     . PRO C 2 196 ? 50.891  3.269   45.165 1.00 50.69  ? 214 PRO C CD     1 
ATOM   7343  N N      . GLY C 2 197 ? 50.045  1.247   49.292 1.00 38.44  ? 215 GLY C N      1 
ATOM   7344  C CA     . GLY C 2 197 ? 48.938  0.893   50.140 1.00 34.28  ? 215 GLY C CA     1 
ATOM   7345  C C      . GLY C 2 197 ? 47.919  -0.100  49.730 1.00 34.69  ? 215 GLY C C      1 
ATOM   7346  O O      . GLY C 2 197 ? 48.262  -1.136  49.192 1.00 42.96  ? 215 GLY C O      1 
ATOM   7347  N N      . ILE C 2 198 ? 46.662  0.207   49.985 1.00 35.01  ? 216 ILE C N      1 
ATOM   7348  C CA     . ILE C 2 198 ? 45.593  -0.713  49.690 1.00 34.71  ? 216 ILE C CA     1 
ATOM   7349  C C      . ILE C 2 198 ? 45.544  -1.059  48.213 1.00 41.41  ? 216 ILE C C      1 
ATOM   7350  O O      . ILE C 2 198 ? 45.020  -2.088  47.840 1.00 47.04  ? 216 ILE C O      1 
ATOM   7351  C CB     . ILE C 2 198 ? 44.280  -0.096  50.167 1.00 25.94  ? 216 ILE C CB     1 
ATOM   7352  C CG1    . ILE C 2 198 ? 44.393  0.226   51.634 1.00 35.84  ? 216 ILE C CG1    1 
ATOM   7353  C CG2    . ILE C 2 198 ? 43.115  -1.044  50.019 1.00 27.66  ? 216 ILE C CG2    1 
ATOM   7354  C CD1    . ILE C 2 198 ? 44.885  -0.949  52.439 1.00 42.36  ? 216 ILE C CD1    1 
ATOM   7355  N N      . MET C 2 199 ? 46.148  -0.250  47.364 1.00 37.14  ? 217 MET C N      1 
ATOM   7356  C CA     . MET C 2 199 ? 46.051  -0.470  45.939 1.00 33.57  ? 217 MET C CA     1 
ATOM   7357  C C      . MET C 2 199 ? 46.566  -1.799  45.488 1.00 47.95  ? 217 MET C C      1 
ATOM   7358  O O      . MET C 2 199 ? 47.552  -2.291  46.006 1.00 52.81  ? 217 MET C O      1 
ATOM   7359  C CB     . MET C 2 199 ? 46.789  0.621   45.194 1.00 34.23  ? 217 MET C CB     1 
ATOM   7360  C CG     . MET C 2 199 ? 46.297  2.017   45.482 1.00 45.94  ? 217 MET C CG     1 
ATOM   7361  S SD     . MET C 2 199 ? 46.909  3.098   44.195 1.00 39.88  ? 217 MET C SD     1 
ATOM   7362  C CE     . MET C 2 199 ? 46.016  2.430   42.801 1.00 41.33  ? 217 MET C CE     1 
ATOM   7363  N N      . LYS C 2 200 ? 45.875  -2.405  44.533 1.00 52.38  ? 218 LYS C N      1 
ATOM   7364  C CA     . LYS C 2 200 ? 46.250  -3.710  44.033 1.00 44.67  ? 218 LYS C CA     1 
ATOM   7365  C C      . LYS C 2 200 ? 47.451  -3.634  43.161 1.00 45.33  ? 218 LYS C C      1 
ATOM   7366  O O      . LYS C 2 200 ? 47.700  -2.622  42.533 1.00 51.01  ? 218 LYS C O      1 
ATOM   7367  C CB     . LYS C 2 200 ? 45.083  -4.329  43.298 1.00 45.28  ? 218 LYS C CB     1 
ATOM   7368  C CG     . LYS C 2 200 ? 43.899  -4.635  44.193 1.00 48.45  ? 218 LYS C CG     1 
ATOM   7369  C CD     . LYS C 2 200 ? 42.992  -5.693  43.593 1.00 53.04  ? 218 LYS C CD     1 
ATOM   7370  C CE     . LYS C 2 200 ? 42.197  -5.154  42.421 1.00 55.18  ? 218 LYS C CE     1 
ATOM   7371  N NZ     . LYS C 2 200 ? 41.337  -6.214  41.834 1.00 45.87  ? 218 LYS C NZ     1 
ATOM   7372  N N      . PRO C 2 201 ? 48.214  -4.707  43.099 1.00 47.26  ? 219 PRO C N      1 
ATOM   7373  C CA     . PRO C 2 201 ? 49.457  -4.643  42.346 1.00 47.93  ? 219 PRO C CA     1 
ATOM   7374  C C      . PRO C 2 201 ? 49.337  -4.334  40.870 1.00 44.10  ? 219 PRO C C      1 
ATOM   7375  O O      . PRO C 2 201 ? 50.045  -3.461  40.403 1.00 46.23  ? 219 PRO C O      1 
ATOM   7376  C CB     . PRO C 2 201 ? 50.031  -6.044  42.533 1.00 51.81  ? 219 PRO C CB     1 
ATOM   7377  C CG     . PRO C 2 201 ? 48.917  -6.899  43.023 1.00 50.13  ? 219 PRO C CG     1 
ATOM   7378  C CD     . PRO C 2 201 ? 48.082  -5.971  43.835 1.00 54.30  ? 219 PRO C CD     1 
ATOM   7379  N N      . ASN C 2 202 ? 48.490  -5.038  40.142 1.00 42.79  ? 220 ASN C N      1 
ATOM   7380  C CA     . ASN C 2 202 ? 48.373  -4.871  38.709 1.00 42.45  ? 220 ASN C CA     1 
ATOM   7381  C C      . ASN C 2 202 ? 47.544  -3.687  38.277 1.00 45.46  ? 220 ASN C C      1 
ATOM   7382  O O      . ASN C 2 202 ? 47.669  -3.221  37.159 1.00 46.52  ? 220 ASN C O      1 
ATOM   7383  C CB     . ASN C 2 202 ? 47.852  -6.178  38.120 1.00 37.19  ? 220 ASN C CB     1 
ATOM   7384  C CG     . ASN C 2 202 ? 46.776  -6.820  38.967 1.00 44.70  ? 220 ASN C CG     1 
ATOM   7385  O OD1    . ASN C 2 202 ? 46.021  -6.147  39.661 1.00 49.23  ? 220 ASN C OD1    1 
ATOM   7386  N ND2    . ASN C 2 202 ? 46.691  -8.138  38.896 1.00 39.50  ? 220 ASN C ND2    1 
ATOM   7387  N N      . SER C 2 203 ? 46.734  -3.157  39.168 1.00 47.80  ? 221 SER C N      1 
ATOM   7388  C CA     . SER C 2 203 ? 45.827  -2.076  38.818 1.00 49.46  ? 221 SER C CA     1 
ATOM   7389  C C      . SER C 2 203 ? 46.468  -0.742  38.502 1.00 45.60  ? 221 SER C C      1 
ATOM   7390  O O      . SER C 2 203 ? 47.535  -0.445  38.997 1.00 44.00  ? 221 SER C O      1 
ATOM   7391  C CB     . SER C 2 203 ? 44.776  -1.950  39.911 1.00 48.39  ? 221 SER C CB     1 
ATOM   7392  O OG     . SER C 2 203 ? 43.972  -3.112  39.949 1.00 45.86  ? 221 SER C OG     1 
ATOM   7393  N N      . PRO C 2 204 ? 45.791  0.083   37.661 1.00 39.81  ? 222 PRO C N      1 
ATOM   7394  C CA     . PRO C 2 204 ? 46.442  1.304   37.226 1.00 36.36  ? 222 PRO C CA     1 
ATOM   7395  C C      . PRO C 2 204 ? 46.637  2.344   38.246 1.00 43.01  ? 222 PRO C C      1 
ATOM   7396  O O      . PRO C 2 204 ? 45.926  2.352   39.209 1.00 47.70  ? 222 PRO C O      1 
ATOM   7397  C CB     . PRO C 2 204 ? 45.458  1.841   36.230 1.00 41.07  ? 222 PRO C CB     1 
ATOM   7398  C CG     . PRO C 2 204 ? 44.771  0.660   35.683 1.00 41.28  ? 222 PRO C CG     1 
ATOM   7399  C CD     . PRO C 2 204 ? 44.497  -0.047  36.951 1.00 39.08  ? 222 PRO C CD     1 
ATOM   7400  N N      . ASN C 2 205 ? 47.596  3.230   38.032 1.00 41.07  ? 223 ASN C N      1 
ATOM   7401  C CA     . ASN C 2 205 ? 47.889  4.299   38.971 1.00 43.95  ? 223 ASN C CA     1 
ATOM   7402  C C      . ASN C 2 205 ? 48.345  5.493   38.215 1.00 51.38  ? 223 ASN C C      1 
ATOM   7403  O O      . ASN C 2 205 ? 48.399  5.459   37.000 1.00 48.52  ? 223 ASN C O      1 
ATOM   7404  C CB     . ASN C 2 205 ? 48.924  3.908   39.995 1.00 43.75  ? 223 ASN C CB     1 
ATOM   7405  C CG     . ASN C 2 205 ? 48.686  4.534   41.334 1.00 49.11  ? 223 ASN C CG     1 
ATOM   7406  O OD1    . ASN C 2 205 ? 47.996  5.533   41.453 1.00 54.09  ? 223 ASN C OD1    1 
ATOM   7407  N ND2    . ASN C 2 205 ? 49.266  3.948   42.354 1.00 51.78  ? 223 ASN C ND2    1 
ATOM   7408  N N      . PHE C 2 206 ? 48.745  6.551   38.909 1.00 55.12  ? 224 PHE C N      1 
ATOM   7409  C CA     . PHE C 2 206 ? 49.009  7.821   38.250 1.00 46.63  ? 224 PHE C CA     1 
ATOM   7410  C C      . PHE C 2 206 ? 50.387  8.313   37.865 1.00 51.05  ? 224 PHE C C      1 
ATOM   7411  O O      . PHE C 2 206 ? 50.503  9.462   37.513 1.00 61.71  ? 224 PHE C O      1 
ATOM   7412  C CB     . PHE C 2 206 ? 48.415  8.921   39.114 1.00 46.97  ? 224 PHE C CB     1 
ATOM   7413  C CG     . PHE C 2 206 ? 46.940  9.062   39.034 1.00 43.05  ? 224 PHE C CG     1 
ATOM   7414  C CD1    . PHE C 2 206 ? 46.266  8.855   37.855 1.00 39.81  ? 224 PHE C CD1    1 
ATOM   7415  C CD2    . PHE C 2 206 ? 46.237  9.478   40.141 1.00 42.67  ? 224 PHE C CD2    1 
ATOM   7416  C CE1    . PHE C 2 206 ? 44.902  9.016   37.796 1.00 37.01  ? 224 PHE C CE1    1 
ATOM   7417  C CE2    . PHE C 2 206 ? 44.881  9.648   40.090 1.00 39.00  ? 224 PHE C CE2    1 
ATOM   7418  C CZ     . PHE C 2 206 ? 44.211  9.418   38.916 1.00 38.12  ? 224 PHE C CZ     1 
ATOM   7419  N N      . THR C 2 207 ? 51.413  7.521   37.943 1.00 41.80  ? 225 THR C N      1 
ATOM   7420  C CA     . THR C 2 207 ? 52.749  7.894   37.501 1.00 56.62  ? 225 THR C CA     1 
ATOM   7421  C C      . THR C 2 207 ? 53.387  8.878   38.440 1.00 68.18  ? 225 THR C C      1 
ATOM   7422  O O      . THR C 2 207 ? 54.554  9.207   38.291 1.00 87.90  ? 225 THR C O      1 
ATOM   7423  C CB     . THR C 2 207 ? 52.850  8.325   36.044 1.00 59.57  ? 225 THR C CB     1 
ATOM   7424  O OG1    . THR C 2 207 ? 51.832  7.679   35.281 1.00 67.89  ? 225 THR C OG1    1 
ATOM   7425  C CG2    . THR C 2 207 ? 54.189  7.925   35.472 1.00 66.75  ? 225 THR C CG2    1 
ATOM   7426  N N      . ASP C 2 208 ? 52.649  9.343   39.435 1.00 63.24  ? 226 ASP C N      1 
ATOM   7427  C CA     . ASP C 2 208 ? 53.259  10.164  40.465 1.00 55.47  ? 226 ASP C CA     1 
ATOM   7428  C C      . ASP C 2 208 ? 53.080  9.394   41.740 1.00 58.77  ? 226 ASP C C      1 
ATOM   7429  O O      . ASP C 2 208 ? 53.933  9.442   42.611 1.00 62.49  ? 226 ASP C O      1 
ATOM   7430  C CB     . ASP C 2 208 ? 52.702  11.588  40.576 1.00 50.77  ? 226 ASP C CB     1 
ATOM   7431  C CG     . ASP C 2 208 ? 51.200  11.663  40.557 1.00 58.38  ? 226 ASP C CG     1 
ATOM   7432  O OD1    . ASP C 2 208 ? 50.527  10.640  40.710 1.00 72.55  ? 226 ASP C OD1    1 
ATOM   7433  O OD2    . ASP C 2 208 ? 50.677  12.782  40.403 1.00 52.75  ? 226 ASP C OD2    1 
ATOM   7434  N N      . ASN C 2 209 ? 51.969  8.676   41.860 1.00 56.12  ? 227 ASN C N      1 
ATOM   7435  C CA     . ASN C 2 209 ? 51.707  7.866   43.028 1.00 51.21  ? 227 ASN C CA     1 
ATOM   7436  C C      . ASN C 2 209 ? 52.183  6.475   42.779 1.00 48.92  ? 227 ASN C C      1 
ATOM   7437  O O      . ASN C 2 209 ? 51.394  5.567   42.719 1.00 46.95  ? 227 ASN C O      1 
ATOM   7438  C CB     . ASN C 2 209 ? 50.225  7.855   43.332 1.00 47.57  ? 227 ASN C CB     1 
ATOM   7439  C CG     . ASN C 2 209 ? 49.929  7.666   44.797 1.00 53.97  ? 227 ASN C CG     1 
ATOM   7440  O OD1    . ASN C 2 209 ? 50.723  8.040   45.654 1.00 68.28  ? 227 ASN C OD1    1 
ATOM   7441  N ND2    . ASN C 2 209 ? 48.772  7.094   45.096 1.00 46.71  ? 227 ASN C ND2    1 
ATOM   7442  N N      . LEU C 2 210 ? 53.479  6.295   42.655 1.00 48.12  ? 228 LEU C N      1 
ATOM   7443  C CA     . LEU C 2 210 ? 54.026  4.994   42.418 1.00 39.57  ? 228 LEU C CA     1 
ATOM   7444  C C      . LEU C 2 210 ? 55.171  4.795   43.365 1.00 41.23  ? 228 LEU C C      1 
ATOM   7445  O O      . LEU C 2 210 ? 56.106  5.565   43.359 1.00 48.31  ? 228 LEU C O      1 
ATOM   7446  C CB     . LEU C 2 210 ? 54.532  4.896   40.998 1.00 36.94  ? 228 LEU C CB     1 
ATOM   7447  C CG     . LEU C 2 210 ? 53.820  4.090   39.923 1.00 44.08  ? 228 LEU C CG     1 
ATOM   7448  C CD1    . LEU C 2 210 ? 52.431  4.619   39.671 1.00 47.33  ? 228 LEU C CD1    1 
ATOM   7449  C CD2    . LEU C 2 210 ? 54.628  4.163   38.644 1.00 49.20  ? 228 LEU C CD2    1 
ATOM   7450  N N      . VAL C 2 211 ? 55.115  3.755   44.175 1.00 40.83  ? 229 VAL C N      1 
ATOM   7451  C CA     . VAL C 2 211 ? 56.139  3.504   45.139 1.00 38.98  ? 229 VAL C CA     1 
ATOM   7452  C C      . VAL C 2 211 ? 57.266  2.669   44.543 1.00 44.48  ? 229 VAL C C      1 
ATOM   7453  O O      . VAL C 2 211 ? 57.138  2.167   43.441 1.00 45.51  ? 229 VAL C O      1 
ATOM   7454  C CB     . VAL C 2 211 ? 55.593  2.771   46.357 1.00 38.54  ? 229 VAL C CB     1 
ATOM   7455  C CG1    . VAL C 2 211 ? 54.866  3.721   47.281 1.00 36.47  ? 229 VAL C CG1    1 
ATOM   7456  C CG2    . VAL C 2 211 ? 54.737  1.596   45.950 1.00 47.44  ? 229 VAL C CG2    1 
ATOM   7457  N N      . PRO C 2 212 ? 58.392  2.522   45.253 1.00 42.64  ? 230 PRO C N      1 
ATOM   7458  C CA     . PRO C 2 212 ? 59.401  1.668   44.653 1.00 42.31  ? 230 PRO C CA     1 
ATOM   7459  C C      . PRO C 2 212 ? 58.988  0.232   44.627 1.00 47.34  ? 230 PRO C C      1 
ATOM   7460  O O      . PRO C 2 212 ? 58.227  -0.191  45.480 1.00 52.07  ? 230 PRO C O      1 
ATOM   7461  C CB     . PRO C 2 212 ? 60.571  1.819   45.601 1.00 44.83  ? 230 PRO C CB     1 
ATOM   7462  C CG     . PRO C 2 212 ? 60.004  2.329   46.876 1.00 49.12  ? 230 PRO C CG     1 
ATOM   7463  C CD     . PRO C 2 212 ? 58.929  3.246   46.414 1.00 47.47  ? 230 PRO C CD     1 
ATOM   7464  N N      . VAL C 2 213 ? 59.486  -0.533  43.671 1.00 43.86  ? 231 VAL C N      1 
ATOM   7465  C CA     . VAL C 2 213 ? 59.032  -1.903  43.551 1.00 39.94  ? 231 VAL C CA     1 
ATOM   7466  C C      . VAL C 2 213 ? 59.436  -2.686  44.764 1.00 38.56  ? 231 VAL C C      1 
ATOM   7467  O O      . VAL C 2 213 ? 60.580  -2.659  45.170 1.00 38.82  ? 231 VAL C O      1 
ATOM   7468  C CB     . VAL C 2 213 ? 59.518  -2.570  42.255 1.00 35.77  ? 231 VAL C CB     1 
ATOM   7469  C CG1    . VAL C 2 213 ? 58.619  -3.739  41.901 1.00 33.60  ? 231 VAL C CG1    1 
ATOM   7470  C CG2    . VAL C 2 213 ? 59.520  -1.565  41.118 1.00 39.26  ? 231 VAL C CG2    1 
ATOM   7471  N N      . ARG C 2 214 ? 58.494  -3.409  45.329 1.00 42.65  ? 232 ARG C N      1 
ATOM   7472  C CA     . ARG C 2 214 ? 58.736  -4.157  46.530 1.00 44.83  ? 232 ARG C CA     1 
ATOM   7473  C C      . ARG C 2 214 ? 57.853  -5.367  46.414 1.00 47.94  ? 232 ARG C C      1 
ATOM   7474  O O      . ARG C 2 214 ? 56.864  -5.331  45.712 1.00 55.58  ? 232 ARG C O      1 
ATOM   7475  C CB     . ARG C 2 214 ? 58.212  -3.324  47.670 1.00 50.28  ? 232 ARG C CB     1 
ATOM   7476  C CG     . ARG C 2 214 ? 56.797  -2.830  47.405 1.00 54.63  ? 232 ARG C CG     1 
ATOM   7477  C CD     . ARG C 2 214 ? 56.292  -1.791  48.381 1.00 55.63  ? 232 ARG C CD     1 
ATOM   7478  N NE     . ARG C 2 214 ? 54.936  -1.393  48.019 1.00 62.51  ? 232 ARG C NE     1 
ATOM   7479  C CZ     . ARG C 2 214 ? 53.839  -1.874  48.589 1.00 68.81  ? 232 ARG C CZ     1 
ATOM   7480  N NH1    . ARG C 2 214 ? 53.930  -2.760  49.566 1.00 68.88  ? 232 ARG C NH1    1 
ATOM   7481  N NH2    . ARG C 2 214 ? 52.650  -1.458  48.194 1.00 68.73  ? 232 ARG C NH2    1 
ATOM   7482  N N      . ASP C 2 215 ? 58.178  -6.455  47.076 1.00 47.99  ? 233 ASP C N      1 
ATOM   7483  C CA     . ASP C 2 215 ? 57.272  -7.579  47.031 1.00 54.04  ? 233 ASP C CA     1 
ATOM   7484  C C      . ASP C 2 215 ? 56.072  -7.301  47.886 1.00 50.42  ? 233 ASP C C      1 
ATOM   7485  O O      . ASP C 2 215 ? 56.198  -6.680  48.923 1.00 54.27  ? 233 ASP C O      1 
ATOM   7486  C CB     . ASP C 2 215 ? 57.961  -8.866  47.450 1.00 59.97  ? 233 ASP C CB     1 
ATOM   7487  C CG     . ASP C 2 215 ? 58.783  -9.479  46.332 1.00 70.37  ? 233 ASP C CG     1 
ATOM   7488  O OD1    . ASP C 2 215 ? 59.120  -8.758  45.374 1.00 76.95  ? 233 ASP C OD1    1 
ATOM   7489  O OD2    . ASP C 2 215 ? 59.098  -10.683 46.407 1.00 72.96  ? 233 ASP C OD2    1 
ATOM   7490  N N      . VAL C 2 216 ? 54.897  -7.743  47.463 1.00 49.17  ? 234 VAL C N      1 
ATOM   7491  C CA     . VAL C 2 216 ? 53.734  -7.575  48.300 1.00 47.22  ? 234 VAL C CA     1 
ATOM   7492  C C      . VAL C 2 216 ? 52.996  -8.889  48.536 1.00 46.63  ? 234 VAL C C      1 
ATOM   7493  O O      . VAL C 2 216 ? 53.203  -9.828  47.799 1.00 46.04  ? 234 VAL C O      1 
ATOM   7494  C CB     . VAL C 2 216 ? 52.757  -6.506  47.803 1.00 52.93  ? 234 VAL C CB     1 
ATOM   7495  C CG1    . VAL C 2 216 ? 53.494  -5.290  47.292 1.00 58.28  ? 234 VAL C CG1    1 
ATOM   7496  C CG2    . VAL C 2 216 ? 51.768  -7.042  46.786 1.00 50.69  ? 234 VAL C CG2    1 
ATOM   7497  N N      . PRO C 2 217 ? 52.153  -8.941  49.586 1.00 46.52  ? 235 PRO C N      1 
ATOM   7498  C CA     . PRO C 2 217 ? 51.554  -10.235 49.797 1.00 46.21  ? 235 PRO C CA     1 
ATOM   7499  C C      . PRO C 2 217 ? 50.259  -10.428 49.104 1.00 51.85  ? 235 PRO C C      1 
ATOM   7500  O O      . PRO C 2 217 ? 49.563  -9.464  48.828 1.00 54.53  ? 235 PRO C O      1 
ATOM   7501  C CB     . PRO C 2 217 ? 51.310  -10.234 51.280 1.00 45.13  ? 235 PRO C CB     1 
ATOM   7502  C CG     . PRO C 2 217 ? 50.939  -8.848  51.594 1.00 49.63  ? 235 PRO C CG     1 
ATOM   7503  C CD     . PRO C 2 217 ? 51.851  -8.042  50.731 1.00 54.69  ? 235 PRO C CD     1 
ATOM   7504  N N      . LYS C 2 218 ? 49.921  -11.676 48.820 1.00 49.91  ? 236 LYS C N      1 
ATOM   7505  C CA     . LYS C 2 218 ? 48.659  -11.985 48.197 1.00 48.21  ? 236 LYS C CA     1 
ATOM   7506  C C      . LYS C 2 218 ? 47.820  -12.733 49.176 1.00 43.55  ? 236 LYS C C      1 
ATOM   7507  O O      . LYS C 2 218 ? 48.280  -13.672 49.780 1.00 49.58  ? 236 LYS C O      1 
ATOM   7508  C CB     . LYS C 2 218 ? 48.874  -12.814 46.961 1.00 52.70  ? 236 LYS C CB     1 
ATOM   7509  C CG     . LYS C 2 218 ? 48.947  -12.018 45.670 1.00 55.20  ? 236 LYS C CG     1 
ATOM   7510  C CD     . LYS C 2 218 ? 47.761  -11.077 45.496 1.00 67.35  ? 236 LYS C CD     1 
ATOM   7511  C CE     . LYS C 2 218 ? 46.447  -11.810 45.260 1.00 63.57  ? 236 LYS C CE     1 
ATOM   7512  N NZ     . LYS C 2 218 ? 46.433  -12.617 44.013 1.00 52.22  ? 236 LYS C NZ     1 
ATOM   7513  N N      . ILE C 2 219 ? 46.583  -12.327 49.352 1.00 38.59  ? 237 ILE C N      1 
ATOM   7514  C CA     . ILE C 2 219 ? 45.740  -12.925 50.353 1.00 40.04  ? 237 ILE C CA     1 
ATOM   7515  C C      . ILE C 2 219 ? 44.433  -13.217 49.658 1.00 44.74  ? 237 ILE C C      1 
ATOM   7516  O O      . ILE C 2 219 ? 44.143  -12.581 48.655 1.00 49.20  ? 237 ILE C O      1 
ATOM   7517  C CB     . ILE C 2 219 ? 45.581  -11.988 51.568 1.00 39.30  ? 237 ILE C CB     1 
ATOM   7518  C CG1    . ILE C 2 219 ? 46.939  -11.669 52.180 1.00 37.95  ? 237 ILE C CG1    1 
ATOM   7519  C CG2    . ILE C 2 219 ? 44.696  -12.592 52.630 1.00 37.08  ? 237 ILE C CG2    1 
ATOM   7520  C CD1    . ILE C 2 219 ? 46.921  -10.508 53.138 1.00 43.26  ? 237 ILE C CD1    1 
ATOM   7521  N N      . ALA C 2 220 ? 43.644  -14.170 50.159 1.00 46.18  ? 238 ALA C N      1 
ATOM   7522  C CA     . ALA C 2 220 ? 42.433  -14.596 49.476 1.00 44.70  ? 238 ALA C CA     1 
ATOM   7523  C C      . ALA C 2 220 ? 41.235  -14.651 50.328 1.00 44.79  ? 238 ALA C C      1 
ATOM   7524  O O      . ALA C 2 220 ? 41.341  -14.810 51.511 1.00 51.11  ? 238 ALA C O      1 
ATOM   7525  C CB     . ALA C 2 220 ? 42.655  -15.961 48.929 1.00 47.00  ? 238 ALA C CB     1 
ATOM   7526  N N      . ILE C 2 221 ? 40.075  -14.561 49.721 1.00 37.02  ? 239 ILE C N      1 
ATOM   7527  C CA     . ILE C 2 221 ? 38.855  -14.530 50.478 1.00 47.35  ? 239 ILE C CA     1 
ATOM   7528  C C      . ILE C 2 221 ? 38.193  -15.869 50.599 1.00 46.94  ? 239 ILE C C      1 
ATOM   7529  O O      . ILE C 2 221 ? 38.050  -16.575 49.621 1.00 54.99  ? 239 ILE C O      1 
ATOM   7530  C CB     . ILE C 2 221 ? 37.848  -13.595 49.812 1.00 52.79  ? 239 ILE C CB     1 
ATOM   7531  C CG1    . ILE C 2 221 ? 38.491  -12.264 49.450 1.00 45.94  ? 239 ILE C CG1    1 
ATOM   7532  C CG2    . ILE C 2 221 ? 36.647  -13.341 50.700 1.00 55.07  ? 239 ILE C CG2    1 
ATOM   7533  C CD1    . ILE C 2 221 ? 37.476  -11.178 49.198 1.00 44.41  ? 239 ILE C CD1    1 
ATOM   7534  N N      . ASN C 2 222 ? 37.783  -16.243 51.793 1.00 50.37  ? 240 ASN C N      1 
ATOM   7535  C CA     . ASN C 2 222 ? 37.046  -17.473 51.932 1.00 60.20  ? 240 ASN C CA     1 
ATOM   7536  C C      . ASN C 2 222 ? 35.672  -16.994 51.626 1.00 63.69  ? 240 ASN C C      1 
ATOM   7537  O O      . ASN C 2 222 ? 35.223  -16.026 52.201 1.00 64.02  ? 240 ASN C O      1 
ATOM   7538  C CB     . ASN C 2 222 ? 37.105  -17.985 53.362 1.00 53.71  ? 240 ASN C CB     1 
ATOM   7539  C CG     . ASN C 2 222 ? 37.045  -19.492 53.448 1.00 58.24  ? 240 ASN C CG     1 
ATOM   7540  O OD1    . ASN C 2 222 ? 36.896  -20.176 52.443 1.00 70.53  ? 240 ASN C OD1    1 
ATOM   7541  N ND2    . ASN C 2 222 ? 37.168  -20.018 54.657 1.00 49.66  ? 240 ASN C ND2    1 
ATOM   7542  N N      . GLU C 2 223 ? 35.006  -17.617 50.674 1.00 61.36  ? 241 GLU C N      1 
ATOM   7543  C CA     . GLU C 2 223 ? 33.703  -17.136 50.285 1.00 61.15  ? 241 GLU C CA     1 
ATOM   7544  C C      . GLU C 2 223 ? 32.708  -18.106 50.812 1.00 64.28  ? 241 GLU C C      1 
ATOM   7545  O O      . GLU C 2 223 ? 31.527  -18.034 50.501 1.00 67.02  ? 241 GLU C O      1 
ATOM   7546  C CB     . GLU C 2 223 ? 33.576  -16.995 48.776 1.00 61.19  ? 241 GLU C CB     1 
ATOM   7547  C CG     . GLU C 2 223 ? 34.445  -15.916 48.158 1.00 73.08  ? 241 GLU C CG     1 
ATOM   7548  C CD     . GLU C 2 223 ? 35.567  -16.493 47.325 1.00 81.61  ? 241 GLU C CD     1 
ATOM   7549  O OE1    . GLU C 2 223 ? 35.756  -17.723 47.351 1.00 83.81  ? 241 GLU C OE1    1 
ATOM   7550  O OE2    . GLU C 2 223 ? 36.260  -15.721 46.641 1.00 77.75  ? 241 GLU C OE2    1 
ATOM   7551  N N      . LYS C 2 224 ? 33.191  -19.041 51.602 1.00 63.15  ? 242 LYS C N      1 
ATOM   7552  C CA     . LYS C 2 224 ? 32.303  -20.013 52.190 1.00 63.33  ? 242 LYS C CA     1 
ATOM   7553  C C      . LYS C 2 224 ? 32.051  -19.668 53.635 1.00 64.58  ? 242 LYS C C      1 
ATOM   7554  O O      . LYS C 2 224 ? 31.542  -20.482 54.392 1.00 69.51  ? 242 LYS C O      1 
ATOM   7555  C CB     . LYS C 2 224 ? 32.855  -21.422 52.051 1.00 57.39  ? 242 LYS C CB     1 
ATOM   7556  C CG     . LYS C 2 224 ? 33.314  -21.763 50.643 1.00 55.51  ? 242 LYS C CG     1 
ATOM   7557  C CD     . LYS C 2 224 ? 32.961  -23.191 50.262 1.00 58.36  ? 242 LYS C CD     1 
ATOM   7558  C CE     . LYS C 2 224 ? 31.459  -23.363 50.101 1.00 55.19  ? 242 LYS C CE     1 
ATOM   7559  N NZ     . LYS C 2 224 ? 31.085  -24.744 49.690 1.00 46.42  ? 242 LYS C NZ     1 
ATOM   7560  N N      . VAL C 2 225 ? 32.426  -18.463 54.028 1.00 57.19  ? 243 VAL C N      1 
ATOM   7561  C CA     . VAL C 2 225 ? 32.203  -18.044 55.386 1.00 48.22  ? 243 VAL C CA     1 
ATOM   7562  C C      . VAL C 2 225 ? 30.916  -17.271 55.469 1.00 51.41  ? 243 VAL C C      1 
ATOM   7563  O O      . VAL C 2 225 ? 30.714  -16.311 54.750 1.00 59.13  ? 243 VAL C O      1 
ATOM   7564  C CB     . VAL C 2 225 ? 33.376  -17.212 55.905 1.00 46.56  ? 243 VAL C CB     1 
ATOM   7565  C CG1    . VAL C 2 225 ? 33.769  -16.144 54.912 1.00 51.71  ? 243 VAL C CG1    1 
ATOM   7566  C CG2    . VAL C 2 225 ? 33.078  -16.624 57.270 1.00 45.86  ? 243 VAL C CG2    1 
ATOM   7567  N N      . ALA C 2 226 ? 30.008  -17.720 56.312 1.00 42.87  ? 244 ALA C N      1 
ATOM   7568  C CA     . ALA C 2 226 ? 28.770  -17.008 56.507 1.00 46.04  ? 244 ALA C CA     1 
ATOM   7569  C C      . ALA C 2 226 ? 29.025  -15.748 57.255 1.00 50.21  ? 244 ALA C C      1 
ATOM   7570  O O      . ALA C 2 226 ? 29.868  -15.716 58.131 1.00 54.16  ? 244 ALA C O      1 
ATOM   7571  C CB     . ALA C 2 226 ? 27.821  -17.854 57.296 1.00 44.72  ? 244 ALA C CB     1 
ATOM   7572  N N      . GLY C 2 227 ? 28.277  -14.707 56.944 1.00 53.29  ? 245 GLY C N      1 
ATOM   7573  C CA     . GLY C 2 227 ? 28.457  -13.429 57.601 1.00 52.16  ? 245 GLY C CA     1 
ATOM   7574  C C      . GLY C 2 227 ? 29.821  -12.900 57.331 1.00 47.88  ? 245 GLY C C      1 
ATOM   7575  O O      . GLY C 2 227 ? 30.385  -12.197 58.137 1.00 48.16  ? 245 GLY C O      1 
ATOM   7576  N N      . GLY C 2 228 ? 30.338  -13.194 56.164 1.00 45.72  ? 246 GLY C N      1 
ATOM   7577  C CA     . GLY C 2 228 ? 31.684  -12.808 55.861 1.00 48.59  ? 246 GLY C CA     1 
ATOM   7578  C C      . GLY C 2 228 ? 31.780  -11.337 55.854 1.00 52.45  ? 246 GLY C C      1 
ATOM   7579  O O      . GLY C 2 228 ? 30.832  -10.650 55.534 1.00 51.32  ? 246 GLY C O      1 
ATOM   7580  N N      . TYR C 2 229 ? 32.931  -10.834 56.229 1.00 50.63  ? 247 TYR C N      1 
ATOM   7581  C CA     . TYR C 2 229 ? 33.083  -9.415  56.313 1.00 51.44  ? 247 TYR C CA     1 
ATOM   7582  C C      . TYR C 2 229 ? 32.889  -8.913  54.919 1.00 56.31  ? 247 TYR C C      1 
ATOM   7583  O O      . TYR C 2 229 ? 32.297  -7.871  54.703 1.00 56.65  ? 247 TYR C O      1 
ATOM   7584  C CB     . TYR C 2 229 ? 34.441  -9.067  56.860 1.00 48.13  ? 247 TYR C CB     1 
ATOM   7585  C CG     . TYR C 2 229 ? 34.650  -7.609  57.134 1.00 49.80  ? 247 TYR C CG     1 
ATOM   7586  C CD1    . TYR C 2 229 ? 33.829  -6.925  58.008 1.00 44.71  ? 247 TYR C CD1    1 
ATOM   7587  C CD2    . TYR C 2 229 ? 35.683  -6.923  56.534 1.00 49.22  ? 247 TYR C CD2    1 
ATOM   7588  C CE1    . TYR C 2 229 ? 34.025  -5.589  58.263 1.00 44.63  ? 247 TYR C CE1    1 
ATOM   7589  C CE2    . TYR C 2 229 ? 35.890  -5.594  56.789 1.00 46.30  ? 247 TYR C CE2    1 
ATOM   7590  C CZ     . TYR C 2 229 ? 35.058  -4.935  57.649 1.00 49.76  ? 247 TYR C CZ     1 
ATOM   7591  O OH     . TYR C 2 229 ? 35.271  -3.608  57.885 1.00 54.58  ? 247 TYR C OH     1 
ATOM   7592  N N      . SER C 2 230 ? 33.361  -9.668  53.952 1.00 53.94  ? 248 SER C N      1 
ATOM   7593  C CA     . SER C 2 230 ? 33.273  -9.240  52.584 1.00 51.46  ? 248 SER C CA     1 
ATOM   7594  C C      . SER C 2 230 ? 31.854  -9.257  52.105 1.00 55.56  ? 248 SER C C      1 
ATOM   7595  O O      . SER C 2 230 ? 31.570  -8.794  51.015 1.00 64.33  ? 248 SER C O      1 
ATOM   7596  C CB     . SER C 2 230 ? 34.129  -10.122 51.723 1.00 53.44  ? 248 SER C CB     1 
ATOM   7597  O OG     . SER C 2 230 ? 35.479  -10.051 52.135 1.00 52.79  ? 248 SER C OG     1 
ATOM   7598  N N      . LYS C 2 231 ? 30.961  -9.855  52.865 1.00 51.73  ? 249 LYS C N      1 
ATOM   7599  C CA     . LYS C 2 231 ? 29.568  -9.827  52.503 1.00 44.89  ? 249 LYS C CA     1 
ATOM   7600  C C      . LYS C 2 231 ? 28.860  -8.778  53.308 1.00 50.12  ? 249 LYS C C      1 
ATOM   7601  O O      . LYS C 2 231 ? 28.047  -8.039  52.779 1.00 55.55  ? 249 LYS C O      1 
ATOM   7602  C CB     . LYS C 2 231 ? 28.958  -11.168 52.787 1.00 42.95  ? 249 LYS C CB     1 
ATOM   7603  C CG     . LYS C 2 231 ? 29.692  -12.307 52.097 1.00 52.25  ? 249 LYS C CG     1 
ATOM   7604  C CD     . LYS C 2 231 ? 29.224  -13.671 52.573 1.00 50.64  ? 249 LYS C CD     1 
ATOM   7605  C CE     . LYS C 2 231 ? 29.849  -14.774 51.739 1.00 37.54  ? 249 LYS C CE     1 
ATOM   7606  N NZ     . LYS C 2 231 ? 31.318  -14.583 51.633 1.00 51.18  ? 249 LYS C NZ     1 
ATOM   7607  N N      . THR C 2 232 ? 29.160  -8.705  54.593 1.00 53.98  ? 250 THR C N      1 
ATOM   7608  C CA     . THR C 2 232 ? 28.504  -7.750  55.453 1.00 53.86  ? 250 THR C CA     1 
ATOM   7609  C C      . THR C 2 232 ? 28.849  -6.326  55.074 1.00 56.33  ? 250 THR C C      1 
ATOM   7610  O O      . THR C 2 232 ? 27.997  -5.449  55.132 1.00 56.20  ? 250 THR C O      1 
ATOM   7611  C CB     . THR C 2 232 ? 28.854  -7.993  56.911 1.00 51.32  ? 250 THR C CB     1 
ATOM   7612  O OG1    . THR C 2 232 ? 30.268  -7.906  57.075 1.00 56.66  ? 250 THR C OG1    1 
ATOM   7613  C CG2    . THR C 2 232 ? 28.380  -9.361  57.342 1.00 45.27  ? 250 THR C CG2    1 
ATOM   7614  N N      . LYS C 2 233 ? 30.101  -6.081  54.711 1.00 58.61  ? 251 LYS C N      1 
ATOM   7615  C CA     . LYS C 2 233 ? 30.508  -4.762  54.242 1.00 55.74  ? 251 LYS C CA     1 
ATOM   7616  C C      . LYS C 2 233 ? 31.160  -4.933  52.912 1.00 56.39  ? 251 LYS C C      1 
ATOM   7617  O O      . LYS C 2 233 ? 32.366  -4.960  52.825 1.00 57.41  ? 251 LYS C O      1 
ATOM   7618  C CB     . LYS C 2 233 ? 31.531  -4.144  55.159 1.00 50.62  ? 251 LYS C CB     1 
ATOM   7619  C CG     . LYS C 2 233 ? 30.964  -3.162  56.166 1.00 61.01  ? 251 LYS C CG     1 
ATOM   7620  C CD     . LYS C 2 233 ? 30.456  -1.902  55.489 1.00 61.96  ? 251 LYS C CD     1 
ATOM   7621  C CE     . LYS C 2 233 ? 29.958  -0.896  56.512 1.00 64.96  ? 251 LYS C CE     1 
ATOM   7622  N NZ     . LYS C 2 233 ? 29.367  0.311   55.874 1.00 70.83  ? 251 LYS C NZ     1 
ATOM   7623  N N      . PRO C 2 234 ? 30.353  -5.053  51.828 1.00 54.58  ? 252 PRO C N      1 
ATOM   7624  C CA     . PRO C 2 234 ? 31.049  -5.300  50.578 1.00 51.36  ? 252 PRO C CA     1 
ATOM   7625  C C      . PRO C 2 234 ? 31.752  -4.073  50.112 1.00 51.21  ? 252 PRO C C      1 
ATOM   7626  O O      . PRO C 2 234 ? 32.609  -4.165  49.253 1.00 53.22  ? 252 PRO C O      1 
ATOM   7627  C CB     . PRO C 2 234 ? 29.922  -5.628  49.637 1.00 50.62  ? 252 PRO C CB     1 
ATOM   7628  C CG     . PRO C 2 234 ? 28.768  -4.852  50.127 1.00 60.09  ? 252 PRO C CG     1 
ATOM   7629  C CD     . PRO C 2 234 ? 28.886  -4.985  51.604 1.00 57.03  ? 252 PRO C CD     1 
ATOM   7630  N N      . THR C 2 235 ? 31.436  -2.933  50.693 1.00 49.11  ? 253 THR C N      1 
ATOM   7631  C CA     . THR C 2 235 ? 32.010  -1.673  50.268 1.00 46.20  ? 253 THR C CA     1 
ATOM   7632  C C      . THR C 2 235 ? 33.444  -1.534  50.669 1.00 45.21  ? 253 THR C C      1 
ATOM   7633  O O      . THR C 2 235 ? 34.099  -0.592  50.276 1.00 39.37  ? 253 THR C O      1 
ATOM   7634  C CB     . THR C 2 235 ? 31.245  -0.533  50.936 1.00 40.81  ? 253 THR C CB     1 
ATOM   7635  O OG1    . THR C 2 235 ? 31.661  -0.415  52.297 1.00 52.41  ? 253 THR C OG1    1 
ATOM   7636  C CG2    . THR C 2 235 ? 29.760  -0.794  50.897 1.00 40.81  ? 253 THR C CG2    1 
ATOM   7637  N N      . THR C 2 236 ? 33.941  -2.462  51.469 1.00 48.80  ? 254 THR C N      1 
ATOM   7638  C CA     . THR C 2 236 ? 35.290  -2.326  51.992 1.00 45.38  ? 254 THR C CA     1 
ATOM   7639  C C      . THR C 2 236 ? 36.260  -3.146  51.240 1.00 43.67  ? 254 THR C C      1 
ATOM   7640  O O      . THR C 2 236 ? 36.080  -4.335  51.045 1.00 43.11  ? 254 THR C O      1 
ATOM   7641  C CB     . THR C 2 236 ? 35.404  -2.566  53.516 1.00 47.11  ? 254 THR C CB     1 
ATOM   7642  O OG1    . THR C 2 236 ? 36.704  -2.176  53.967 1.00 42.19  ? 254 THR C OG1    1 
ATOM   7643  C CG2    . THR C 2 236 ? 35.173  -3.997  53.877 1.00 54.25  ? 254 THR C CG2    1 
ATOM   7644  N N      . PRO C 2 237 ? 37.339  -2.490  50.789 1.00 43.80  ? 255 PRO C N      1 
ATOM   7645  C CA     . PRO C 2 237 ? 38.210  -3.306  49.999 1.00 43.95  ? 255 PRO C CA     1 
ATOM   7646  C C      . PRO C 2 237 ? 38.870  -4.300  50.894 1.00 47.36  ? 255 PRO C C      1 
ATOM   7647  O O      . PRO C 2 237 ? 39.161  -3.947  52.016 1.00 56.61  ? 255 PRO C O      1 
ATOM   7648  C CB     . PRO C 2 237 ? 39.238  -2.311  49.571 1.00 44.79  ? 255 PRO C CB     1 
ATOM   7649  C CG     . PRO C 2 237 ? 38.579  -0.998  49.567 1.00 44.84  ? 255 PRO C CG     1 
ATOM   7650  C CD     . PRO C 2 237 ? 37.844  -1.097  50.836 1.00 44.17  ? 255 PRO C CD     1 
ATOM   7651  N N      . PHE C 2 238 ? 39.157  -5.501  50.428 1.00 43.76  ? 256 PHE C N      1 
ATOM   7652  C CA     . PHE C 2 238 ? 39.709  -6.519  51.282 1.00 42.74  ? 256 PHE C CA     1 
ATOM   7653  C C      . PHE C 2 238 ? 41.164  -6.572  51.078 1.00 47.45  ? 256 PHE C C      1 
ATOM   7654  O O      . PHE C 2 238 ? 41.605  -6.727  49.952 1.00 47.13  ? 256 PHE C O      1 
ATOM   7655  C CB     . PHE C 2 238 ? 39.149  -7.839  50.816 1.00 44.42  ? 256 PHE C CB     1 
ATOM   7656  C CG     . PHE C 2 238 ? 39.791  -9.070  51.403 1.00 46.62  ? 256 PHE C CG     1 
ATOM   7657  C CD1    . PHE C 2 238 ? 40.876  -9.673  50.794 1.00 43.07  ? 256 PHE C CD1    1 
ATOM   7658  C CD2    . PHE C 2 238 ? 39.237  -9.686  52.500 1.00 48.98  ? 256 PHE C CD2    1 
ATOM   7659  C CE1    . PHE C 2 238 ? 41.440  -10.812 51.315 1.00 41.98  ? 256 PHE C CE1    1 
ATOM   7660  C CE2    . PHE C 2 238 ? 39.791  -10.833 53.020 1.00 40.94  ? 256 PHE C CE2    1 
ATOM   7661  C CZ     . PHE C 2 238 ? 40.894  -11.396 52.428 1.00 39.57  ? 256 PHE C CZ     1 
ATOM   7662  N N      . VAL C 2 239 ? 41.948  -6.397  52.131 1.00 47.24  ? 257 VAL C N      1 
ATOM   7663  C CA     . VAL C 2 239 ? 43.359  -6.610  51.999 1.00 44.99  ? 257 VAL C CA     1 
ATOM   7664  C C      . VAL C 2 239 ? 43.640  -7.773  52.909 1.00 43.19  ? 257 VAL C C      1 
ATOM   7665  O O      . VAL C 2 239 ? 44.283  -8.709  52.482 1.00 38.51  ? 257 VAL C O      1 
ATOM   7666  C CB     . VAL C 2 239 ? 44.142  -5.390  52.346 1.00 43.27  ? 257 VAL C CB     1 
ATOM   7667  C CG1    . VAL C 2 239 ? 45.498  -5.459  51.680 1.00 46.27  ? 257 VAL C CG1    1 
ATOM   7668  C CG2    . VAL C 2 239 ? 43.414  -4.169  51.852 1.00 43.21  ? 257 VAL C CG2    1 
ATOM   7669  N N      . ALA C 2 240 ? 43.175  -7.740  54.156 1.00 50.80  ? 258 ALA C N      1 
ATOM   7670  C CA     . ALA C 2 240 ? 43.292  -8.900  55.061 1.00 45.11  ? 258 ALA C CA     1 
ATOM   7671  C C      . ALA C 2 240 ? 42.084  -9.185  55.924 1.00 45.69  ? 258 ALA C C      1 
ATOM   7672  O O      . ALA C 2 240 ? 42.209  -9.897  56.886 1.00 51.29  ? 258 ALA C O      1 
ATOM   7673  C CB     . ALA C 2 240 ? 44.491  -8.765  55.924 1.00 39.09  ? 258 ALA C CB     1 
ATOM   7674  N N      . SER C 2 241 ? 40.945  -8.627  55.614 1.00 36.12  ? 259 SER C N      1 
ATOM   7675  C CA     . SER C 2 241 ? 39.705  -8.775  56.352 1.00 38.70  ? 259 SER C CA     1 
ATOM   7676  C C      . SER C 2 241 ? 39.535  -8.096  57.638 1.00 43.30  ? 259 SER C C      1 
ATOM   7677  O O      . SER C 2 241 ? 38.692  -7.257  57.720 1.00 55.14  ? 259 SER C O      1 
ATOM   7678  C CB     . SER C 2 241 ? 39.201  -10.158 56.472 1.00 38.40  ? 259 SER C CB     1 
ATOM   7679  O OG     . SER C 2 241 ? 37.827  -10.128 56.782 1.00 35.41  ? 259 SER C OG     1 
ATOM   7680  N N      . LEU C 2 242 ? 40.287  -8.381  58.652 1.00 37.86  ? 260 LEU C N      1 
ATOM   7681  C CA     . LEU C 2 242 ? 40.023  -7.683  59.865 1.00 39.32  ? 260 LEU C CA     1 
ATOM   7682  C C      . LEU C 2 242 ? 41.292  -7.759  60.604 1.00 47.13  ? 260 LEU C C      1 
ATOM   7683  O O      . LEU C 2 242 ? 42.079  -8.618  60.313 1.00 52.39  ? 260 LEU C O      1 
ATOM   7684  C CB     . LEU C 2 242 ? 38.909  -8.348  60.653 1.00 39.74  ? 260 LEU C CB     1 
ATOM   7685  C CG     . LEU C 2 242 ? 37.419  -8.209  60.347 1.00 37.07  ? 260 LEU C CG     1 
ATOM   7686  C CD1    . LEU C 2 242 ? 36.619  -9.237  61.114 1.00 34.34  ? 260 LEU C CD1    1 
ATOM   7687  C CD2    . LEU C 2 242 ? 36.927  -6.814  60.655 1.00 43.92  ? 260 LEU C CD2    1 
ATOM   7688  N N      . SER C 2 243 ? 41.524  -6.881  61.561 1.00 47.27  ? 261 SER C N      1 
ATOM   7689  C CA     . SER C 2 243 ? 42.783  -6.864  62.243 1.00 42.19  ? 261 SER C CA     1 
ATOM   7690  C C      . SER C 2 243 ? 42.587  -7.367  63.578 1.00 44.17  ? 261 SER C C      1 
ATOM   7691  O O      . SER C 2 243 ? 41.606  -7.057  64.205 1.00 50.86  ? 261 SER C O      1 
ATOM   7692  C CB     . SER C 2 243 ? 43.289  -5.477  62.401 1.00 45.48  ? 261 SER C CB     1 
ATOM   7693  O OG     . SER C 2 243 ? 44.472  -5.459  63.162 1.00 49.53  ? 261 SER C OG     1 
ATOM   7694  N N      . GLY C 2 244 ? 43.519  -8.166  64.032 1.00 44.24  ? 262 GLY C N      1 
ATOM   7695  C CA     . GLY C 2 244 ? 43.449  -8.678  65.374 1.00 42.08  ? 262 GLY C CA     1 
ATOM   7696  C C      . GLY C 2 244 ? 44.603  -8.059  66.048 1.00 44.80  ? 262 GLY C C      1 
ATOM   7697  O O      . GLY C 2 244 ? 44.733  -8.135  67.250 1.00 47.32  ? 262 GLY C O      1 
ATOM   7698  N N      . THR C 2 245 ? 45.467  -7.436  65.271 1.00 44.91  ? 263 THR C N      1 
ATOM   7699  C CA     . THR C 2 245 ? 46.573  -6.740  65.857 1.00 43.83  ? 263 THR C CA     1 
ATOM   7700  C C      . THR C 2 245 ? 45.938  -5.542  66.486 1.00 46.59  ? 263 THR C C      1 
ATOM   7701  O O      . THR C 2 245 ? 46.547  -4.866  67.288 1.00 50.92  ? 263 THR C O      1 
ATOM   7702  C CB     . THR C 2 245 ? 47.577  -6.349  64.798 1.00 47.95  ? 263 THR C CB     1 
ATOM   7703  O OG1    . THR C 2 245 ? 47.744  -7.441  63.889 1.00 49.99  ? 263 THR C OG1    1 
ATOM   7704  C CG2    . THR C 2 245 ? 48.906  -6.033  65.428 1.00 49.69  ? 263 THR C CG2    1 
ATOM   7705  N N      . THR C 2 246 ? 44.679  -5.292  66.174 1.00 45.82  ? 264 THR C N      1 
ATOM   7706  C CA     . THR C 2 246 ? 43.959  -4.175  66.769 1.00 44.26  ? 264 THR C CA     1 
ATOM   7707  C C      . THR C 2 246 ? 43.702  -4.532  68.184 1.00 42.17  ? 264 THR C C      1 
ATOM   7708  O O      . THR C 2 246 ? 43.717  -3.696  69.058 1.00 45.55  ? 264 THR C O      1 
ATOM   7709  C CB     . THR C 2 246 ? 42.645  -3.919  66.050 1.00 39.84  ? 264 THR C CB     1 
ATOM   7710  O OG1    . THR C 2 246 ? 42.926  -3.439  64.735 1.00 39.33  ? 264 THR C OG1    1 
ATOM   7711  C CG2    . THR C 2 246 ? 41.856  -2.898  66.761 1.00 42.68  ? 264 THR C CG2    1 
ATOM   7712  N N      . TYR C 2 247 ? 43.524  -5.806  68.442 1.00 43.11  ? 265 TYR C N      1 
ATOM   7713  C CA     . TYR C 2 247 ? 43.318  -6.247  69.798 1.00 44.37  ? 265 TYR C CA     1 
ATOM   7714  C C      . TYR C 2 247 ? 44.604  -6.099  70.540 1.00 43.03  ? 265 TYR C C      1 
ATOM   7715  O O      . TYR C 2 247 ? 44.594  -5.796  71.708 1.00 43.72  ? 265 TYR C O      1 
ATOM   7716  C CB     . TYR C 2 247 ? 42.783  -7.665  69.828 1.00 38.88  ? 265 TYR C CB     1 
ATOM   7717  C CG     . TYR C 2 247 ? 41.411  -7.772  69.229 1.00 37.45  ? 265 TYR C CG     1 
ATOM   7718  C CD1    . TYR C 2 247 ? 40.331  -7.154  69.824 1.00 38.45  ? 265 TYR C CD1    1 
ATOM   7719  C CD2    . TYR C 2 247 ? 41.196  -8.477  68.066 1.00 37.61  ? 265 TYR C CD2    1 
ATOM   7720  C CE1    . TYR C 2 247 ? 39.074  -7.238  69.277 1.00 40.12  ? 265 TYR C CE1    1 
ATOM   7721  C CE2    . TYR C 2 247 ? 39.942  -8.564  67.512 1.00 41.20  ? 265 TYR C CE2    1 
ATOM   7722  C CZ     . TYR C 2 247 ? 38.886  -7.946  68.127 1.00 41.69  ? 265 TYR C CZ     1 
ATOM   7723  O OH     . TYR C 2 247 ? 37.634  -8.022  67.577 1.00 37.87  ? 265 TYR C OH     1 
ATOM   7724  N N      . SER C 2 248 ? 45.726  -6.237  69.868 1.00 39.06  ? 266 SER C N      1 
ATOM   7725  C CA     . SER C 2 248 ? 46.980  -6.010  70.530 1.00 38.44  ? 266 SER C CA     1 
ATOM   7726  C C      . SER C 2 248 ? 47.178  -4.539  70.787 1.00 43.58  ? 266 SER C C      1 
ATOM   7727  O O      . SER C 2 248 ? 47.785  -4.170  71.768 1.00 53.34  ? 266 SER C O      1 
ATOM   7728  C CB     . SER C 2 248 ? 48.113  -6.526  69.702 1.00 37.22  ? 266 SER C CB     1 
ATOM   7729  O OG     . SER C 2 248 ? 48.668  -5.493  68.925 1.00 50.33  ? 266 SER C OG     1 
ATOM   7730  N N      . LEU C 2 249 ? 46.679  -3.675  69.922 1.00 41.27  ? 267 LEU C N      1 
ATOM   7731  C CA     . LEU C 2 249 ? 46.779  -2.243  70.147 1.00 40.06  ? 267 LEU C CA     1 
ATOM   7732  C C      . LEU C 2 249 ? 45.983  -1.960  71.329 1.00 39.09  ? 267 LEU C C      1 
ATOM   7733  O O      . LEU C 2 249 ? 46.416  -1.283  72.226 1.00 46.31  ? 267 LEU C O      1 
ATOM   7734  C CB     . LEU C 2 249 ? 46.136  -1.462  69.026 1.00 50.22  ? 267 LEU C CB     1 
ATOM   7735  C CG     . LEU C 2 249 ? 45.968  0.049   69.164 1.00 46.28  ? 267 LEU C CG     1 
ATOM   7736  C CD1    . LEU C 2 249 ? 47.317  0.746   69.149 1.00 46.23  ? 267 LEU C CD1    1 
ATOM   7737  C CD2    . LEU C 2 249 ? 45.074  0.582   68.059 1.00 37.82  ? 267 LEU C CD2    1 
ATOM   7738  N N      . MET C 2 250 ? 44.793  -2.501  71.372 1.00 40.12  ? 268 MET C N      1 
ATOM   7739  C CA     . MET C 2 250 ? 43.927  -2.201  72.471 1.00 40.62  ? 268 MET C CA     1 
ATOM   7740  C C      . MET C 2 250 ? 44.484  -2.738  73.762 1.00 42.58  ? 268 MET C C      1 
ATOM   7741  O O      . MET C 2 250 ? 44.111  -2.273  74.808 1.00 41.60  ? 268 MET C O      1 
ATOM   7742  C CB     . MET C 2 250 ? 42.534  -2.711  72.216 1.00 37.98  ? 268 MET C CB     1 
ATOM   7743  C CG     . MET C 2 250 ? 41.802  -1.963  71.129 1.00 40.34  ? 268 MET C CG     1 
ATOM   7744  S SD     . MET C 2 250 ? 41.482  -0.289  71.669 1.00 48.71  ? 268 MET C SD     1 
ATOM   7745  C CE     . MET C 2 250 ? 40.598  -0.600  73.190 1.00 44.51  ? 268 MET C CE     1 
ATOM   7746  N N      . VAL C 2 251 ? 45.348  -3.738  73.720 1.00 43.80  ? 269 VAL C N      1 
ATOM   7747  C CA     . VAL C 2 251 ? 45.992  -4.197  74.948 1.00 38.81  ? 269 VAL C CA     1 
ATOM   7748  C C      . VAL C 2 251 ? 46.907  -3.123  75.482 1.00 40.67  ? 269 VAL C C      1 
ATOM   7749  O O      . VAL C 2 251 ? 46.933  -2.847  76.672 1.00 50.08  ? 269 VAL C O      1 
ATOM   7750  C CB     . VAL C 2 251 ? 46.752  -5.505  74.760 1.00 34.46  ? 269 VAL C CB     1 
ATOM   7751  C CG1    . VAL C 2 251 ? 47.596  -5.816  75.978 1.00 46.69  ? 269 VAL C CG1    1 
ATOM   7752  C CG2    . VAL C 2 251 ? 45.778  -6.639  74.525 1.00 34.89  ? 269 VAL C CG2    1 
ATOM   7753  N N      . VAL C 2 252 ? 47.636  -2.477  74.594 1.00 35.25  ? 270 VAL C N      1 
ATOM   7754  C CA     . VAL C 2 252 ? 48.531  -1.439  75.016 1.00 37.95  ? 270 VAL C CA     1 
ATOM   7755  C C      . VAL C 2 252 ? 47.688  -0.276  75.420 1.00 37.43  ? 270 VAL C C      1 
ATOM   7756  O O      . VAL C 2 252 ? 47.878  0.281   76.474 1.00 44.07  ? 270 VAL C O      1 
ATOM   7757  C CB     . VAL C 2 252 ? 49.474  -1.019  73.901 1.00 37.86  ? 270 VAL C CB     1 
ATOM   7758  C CG1    . VAL C 2 252 ? 50.591  -0.160  74.451 1.00 38.08  ? 270 VAL C CG1    1 
ATOM   7759  C CG2    . VAL C 2 252 ? 50.056  -2.238  73.222 1.00 37.01  ? 270 VAL C CG2    1 
ATOM   7760  N N      . LEU C 2 253 ? 46.733  0.092   74.595 1.00 35.32  ? 271 LEU C N      1 
ATOM   7761  C CA     . LEU C 2 253 ? 45.914  1.266   74.884 1.00 37.78  ? 271 LEU C CA     1 
ATOM   7762  C C      . LEU C 2 253 ? 45.061  1.178   76.114 1.00 43.21  ? 271 LEU C C      1 
ATOM   7763  O O      . LEU C 2 253 ? 44.861  2.166   76.787 1.00 45.29  ? 271 LEU C O      1 
ATOM   7764  C CB     . LEU C 2 253 ? 45.038  1.635   73.704 1.00 35.21  ? 271 LEU C CB     1 
ATOM   7765  C CG     . LEU C 2 253 ? 45.674  2.404   72.568 1.00 34.46  ? 271 LEU C CG     1 
ATOM   7766  C CD1    . LEU C 2 253 ? 44.589  2.694   71.560 1.00 33.10  ? 271 LEU C CD1    1 
ATOM   7767  C CD2    . LEU C 2 253 ? 46.213  3.698   73.130 1.00 44.12  ? 271 LEU C CD2    1 
ATOM   7768  N N      . THR C 2 254 ? 44.530  0.009   76.399 1.00 40.12  ? 272 THR C N      1 
ATOM   7769  C CA     . THR C 2 254 ? 43.680  -0.124  77.541 1.00 41.19  ? 272 THR C CA     1 
ATOM   7770  C C      . THR C 2 254 ? 44.563  0.233   78.685 1.00 44.94  ? 272 THR C C      1 
ATOM   7771  O O      . THR C 2 254 ? 44.146  0.896   79.614 1.00 49.68  ? 272 THR C O      1 
ATOM   7772  C CB     . THR C 2 254 ? 43.145  -1.538  77.707 1.00 41.59  ? 272 THR C CB     1 
ATOM   7773  O OG1    . THR C 2 254 ? 42.324  -1.872  76.587 1.00 39.27  ? 272 THR C OG1    1 
ATOM   7774  C CG2    . THR C 2 254 ? 42.306  -1.638  78.956 1.00 47.25  ? 272 THR C CG2    1 
ATOM   7775  N N      . ASP C 2 255 ? 45.829  -0.124  78.586 1.00 43.40  ? 273 ASP C N      1 
ATOM   7776  C CA     . ASP C 2 255 ? 46.759  0.167   79.666 1.00 48.67  ? 273 ASP C CA     1 
ATOM   7777  C C      . ASP C 2 255 ? 47.051  1.636   79.744 1.00 50.39  ? 273 ASP C C      1 
ATOM   7778  O O      . ASP C 2 255 ? 46.956  2.208   80.802 1.00 49.42  ? 273 ASP C O      1 
ATOM   7779  C CB     . ASP C 2 255 ? 48.063  -0.584  79.499 1.00 48.75  ? 273 ASP C CB     1 
ATOM   7780  C CG     . ASP C 2 255 ? 48.804  -0.763  80.798 1.00 57.76  ? 273 ASP C CG     1 
ATOM   7781  O OD1    . ASP C 2 255 ? 48.184  -0.600  81.865 1.00 61.91  ? 273 ASP C OD1    1 
ATOM   7782  O OD2    . ASP C 2 255 ? 50.008  -1.084  80.756 1.00 56.85  ? 273 ASP C OD2    1 
ATOM   7783  N N      . TYR C 2 256 ? 47.411  2.254   78.635 1.00 48.02  ? 274 TYR C N      1 
ATOM   7784  C CA     . TYR C 2 256 ? 47.782  3.650   78.659 1.00 44.10  ? 274 TYR C CA     1 
ATOM   7785  C C      . TYR C 2 256 ? 46.632  4.442   79.195 1.00 47.27  ? 274 TYR C C      1 
ATOM   7786  O O      . TYR C 2 256 ? 46.819  5.371   79.936 1.00 52.23  ? 274 TYR C O      1 
ATOM   7787  C CB     . TYR C 2 256 ? 48.215  4.106   77.282 1.00 36.14  ? 274 TYR C CB     1 
ATOM   7788  C CG     . TYR C 2 256 ? 48.483  5.565   77.122 1.00 50.36  ? 274 TYR C CG     1 
ATOM   7789  C CD1    . TYR C 2 256 ? 49.727  6.083   77.380 1.00 54.41  ? 274 TYR C CD1    1 
ATOM   7790  C CD2    . TYR C 2 256 ? 47.499  6.419   76.669 1.00 54.73  ? 274 TYR C CD2    1 
ATOM   7791  C CE1    . TYR C 2 256 ? 49.977  7.422   77.221 1.00 54.13  ? 274 TYR C CE1    1 
ATOM   7792  C CE2    . TYR C 2 256 ? 47.739  7.760   76.512 1.00 58.85  ? 274 TYR C CE2    1 
ATOM   7793  C CZ     . TYR C 2 256 ? 48.983  8.252   76.790 1.00 64.95  ? 274 TYR C CZ     1 
ATOM   7794  O OH     . TYR C 2 256 ? 49.233  9.588   76.635 1.00 82.73  ? 274 TYR C OH     1 
ATOM   7795  N N      . ILE C 2 257 ? 45.430  4.078   78.846 1.00 41.90  ? 275 ILE C N      1 
ATOM   7796  C CA     . ILE C 2 257 ? 44.323  4.775   79.412 1.00 46.29  ? 275 ILE C CA     1 
ATOM   7797  C C      . ILE C 2 257 ? 44.236  4.604   80.911 1.00 51.68  ? 275 ILE C C      1 
ATOM   7798  O O      . ILE C 2 257 ? 44.081  5.575   81.620 1.00 54.18  ? 275 ILE C O      1 
ATOM   7799  C CB     . ILE C 2 257 ? 43.017  4.329   78.769 1.00 43.12  ? 275 ILE C CB     1 
ATOM   7800  C CG1    . ILE C 2 257 ? 42.955  4.769   77.316 1.00 38.73  ? 275 ILE C CG1    1 
ATOM   7801  C CG2    . ILE C 2 257 ? 41.835  4.863   79.538 1.00 43.02  ? 275 ILE C CG2    1 
ATOM   7802  C CD1    . ILE C 2 257 ? 41.788  4.167   76.578 1.00 48.25  ? 275 ILE C CD1    1 
ATOM   7803  N N      . GLU C 2 258 ? 44.386  3.392   81.425 1.00 57.04  ? 276 GLU C N      1 
ATOM   7804  C CA     . GLU C 2 258 ? 44.354  3.158   82.868 1.00 54.59  ? 276 GLU C CA     1 
ATOM   7805  C C      . GLU C 2 258 ? 45.529  3.826   83.506 1.00 51.96  ? 276 GLU C C      1 
ATOM   7806  O O      . GLU C 2 258 ? 45.415  4.360   84.584 1.00 49.24  ? 276 GLU C O      1 
ATOM   7807  C CB     . GLU C 2 258 ? 44.325  1.680   83.171 1.00 47.26  ? 276 GLU C CB     1 
ATOM   7808  C CG     . GLU C 2 258 ? 43.126  0.940   82.606 1.00 57.46  ? 276 GLU C CG     1 
ATOM   7809  C CD     . GLU C 2 258 ? 41.854  1.167   83.396 1.00 77.00  ? 276 GLU C CD     1 
ATOM   7810  O OE1    . GLU C 2 258 ? 41.629  0.433   84.378 1.00 93.24  ? 276 GLU C OE1    1 
ATOM   7811  O OE2    . GLU C 2 258 ? 41.067  2.062   83.029 1.00 82.64  ? 276 GLU C OE2    1 
ATOM   7812  N N      . LYS C 2 259 ? 46.661  3.825   82.835 1.00 52.05  ? 277 LYS C N      1 
ATOM   7813  C CA     . LYS C 2 259 ? 47.862  4.445   83.342 1.00 47.44  ? 277 LYS C CA     1 
ATOM   7814  C C      . LYS C 2 259 ? 47.846  5.942   83.252 1.00 55.98  ? 277 LYS C C      1 
ATOM   7815  O O      . LYS C 2 259 ? 48.735  6.575   83.780 1.00 57.70  ? 277 LYS C O      1 
ATOM   7816  C CB     . LYS C 2 259 ? 49.053  3.968   82.536 1.00 46.55  ? 277 LYS C CB     1 
ATOM   7817  C CG     . LYS C 2 259 ? 49.842  2.814   83.122 1.00 54.68  ? 277 LYS C CG     1 
ATOM   7818  C CD     . LYS C 2 259 ? 51.126  2.613   82.333 1.00 57.79  ? 277 LYS C CD     1 
ATOM   7819  C CE     . LYS C 2 259 ? 52.177  1.863   83.132 1.00 54.33  ? 277 LYS C CE     1 
ATOM   7820  N NZ     . LYS C 2 259 ? 51.744  0.489   83.491 1.00 57.68  ? 277 LYS C NZ     1 
ATOM   7821  N N      . HIS C 2 260 ? 46.908  6.522   82.515 1.00 57.36  ? 278 HIS C N      1 
ATOM   7822  C CA     . HIS C 2 260 ? 46.788  7.960   82.427 1.00 50.08  ? 278 HIS C CA     1 
ATOM   7823  C C      . HIS C 2 260 ? 45.371  8.417   82.403 1.00 47.40  ? 278 HIS C C      1 
ATOM   7824  O O      . HIS C 2 260 ? 45.042  9.262   81.619 1.00 50.19  ? 278 HIS C O      1 
ATOM   7825  C CB     . HIS C 2 260 ? 47.454  8.481   81.186 1.00 48.64  ? 278 HIS C CB     1 
ATOM   7826  C CG     . HIS C 2 260 ? 48.931  8.257   81.139 1.00 57.15  ? 278 HIS C CG     1 
ATOM   7827  N ND1    . HIS C 2 260 ? 49.495  7.134   80.578 1.00 62.58  ? 278 HIS C ND1    1 
ATOM   7828  C CD2    . HIS C 2 260 ? 49.962  9.019   81.569 1.00 62.91  ? 278 HIS C CD2    1 
ATOM   7829  C CE1    . HIS C 2 260 ? 50.810  7.209   80.673 1.00 63.11  ? 278 HIS C CE1    1 
ATOM   7830  N NE2    . HIS C 2 260 ? 51.120  8.343   81.271 1.00 60.76  ? 278 HIS C NE2    1 
ATOM   7831  N N      . LYS C 2 261 ? 44.519  7.868   83.239 1.00 46.03  ? 279 LYS C N      1 
ATOM   7832  C CA     . LYS C 2 261 ? 43.113  8.221   83.239 1.00 46.45  ? 279 LYS C CA     1 
ATOM   7833  C C      . LYS C 2 261 ? 42.997  9.667   83.578 1.00 56.58  ? 279 LYS C C      1 
ATOM   7834  O O      . LYS C 2 261 ? 42.137  10.369  83.069 1.00 59.71  ? 279 LYS C O      1 
ATOM   7835  C CB     . LYS C 2 261 ? 42.375  7.414   84.280 1.00 46.68  ? 279 LYS C CB     1 
ATOM   7836  C CG     . LYS C 2 261 ? 40.889  7.235   84.012 1.00 70.48  ? 279 LYS C CG     1 
ATOM   7837  C CD     . LYS C 2 261 ? 40.046  8.377   84.565 1.00 78.46  ? 279 LYS C CD     1 
ATOM   7838  C CE     . LYS C 2 261 ? 38.575  8.206   84.220 1.00 76.13  ? 279 LYS C CE     1 
ATOM   7839  N NZ     . LYS C 2 261 ? 37.761  9.386   84.621 1.00 67.40  ? 279 LYS C NZ     1 
ATOM   7840  N N      . THR C 2 262 ? 43.837  10.119  84.480 1.00 56.98  ? 280 THR C N      1 
ATOM   7841  C CA     . THR C 2 262 ? 43.844  11.500  84.899 1.00 50.52  ? 280 THR C CA     1 
ATOM   7842  C C      . THR C 2 262 ? 44.200  12.540  83.852 1.00 51.73  ? 280 THR C C      1 
ATOM   7843  O O      . THR C 2 262 ? 43.686  13.638  83.885 1.00 58.87  ? 280 THR C O      1 
ATOM   7844  C CB     . THR C 2 262 ? 44.758  11.624  86.116 1.00 51.06  ? 280 THR C CB     1 
ATOM   7845  O OG1    . THR C 2 262 ? 44.249  10.810  87.177 1.00 54.93  ? 280 THR C OG1    1 
ATOM   7846  C CG2    . THR C 2 262 ? 44.788  13.053  86.586 1.00 49.41  ? 280 THR C CG2    1 
ATOM   7847  N N      . ASP C 2 263 ? 45.091  12.223  82.940 1.00 50.36  ? 281 ASP C N      1 
ATOM   7848  C CA     . ASP C 2 263 ? 45.551  13.209  81.996 1.00 54.60  ? 281 ASP C CA     1 
ATOM   7849  C C      . ASP C 2 263 ? 44.408  13.768  81.254 1.00 58.98  ? 281 ASP C C      1 
ATOM   7850  O O      . ASP C 2 263 ? 43.561  13.052  80.767 1.00 63.12  ? 281 ASP C O      1 
ATOM   7851  C CB     . ASP C 2 263 ? 46.508  12.557  81.022 1.00 53.05  ? 281 ASP C CB     1 
ATOM   7852  C CG     . ASP C 2 263 ? 47.481  13.523  80.420 1.00 68.81  ? 281 ASP C CG     1 
ATOM   7853  O OD1    . ASP C 2 263 ? 47.476  14.708  80.802 1.00 73.96  ? 281 ASP C OD1    1 
ATOM   7854  O OD2    . ASP C 2 263 ? 48.262  13.091  79.552 1.00 70.92  ? 281 ASP C OD2    1 
ATOM   7855  N N      . LYS C 2 264 ? 44.375  15.076  81.168 1.00 56.13  ? 282 LYS C N      1 
ATOM   7856  C CA     . LYS C 2 264 ? 43.284  15.730  80.519 1.00 58.21  ? 282 LYS C CA     1 
ATOM   7857  C C      . LYS C 2 264 ? 43.225  15.466  79.065 1.00 63.86  ? 282 LYS C C      1 
ATOM   7858  O O      . LYS C 2 264 ? 42.162  15.220  78.514 1.00 61.55  ? 282 LYS C O      1 
ATOM   7859  C CB     . LYS C 2 264 ? 43.494  17.211  80.702 1.00 63.43  ? 282 LYS C CB     1 
ATOM   7860  C CG     . LYS C 2 264 ? 43.714  17.640  82.143 1.00 66.89  ? 282 LYS C CG     1 
ATOM   7861  C CD     . LYS C 2 264 ? 42.411  17.665  82.929 1.00 70.85  ? 282 LYS C CD     1 
ATOM   7862  C CE     . LYS C 2 264 ? 41.454  18.717  82.388 1.00 57.99  ? 282 LYS C CE     1 
ATOM   7863  N NZ     . LYS C 2 264 ? 40.150  18.702  83.103 1.00 44.73  ? 282 LYS C NZ     1 
ATOM   7864  N N      . ASP C 2 265 ? 44.373  15.509  78.424 1.00 65.11  ? 283 ASP C N      1 
ATOM   7865  C CA     . ASP C 2 265 ? 44.399  15.389  76.993 1.00 63.09  ? 283 ASP C CA     1 
ATOM   7866  C C      . ASP C 2 265 ? 44.575  13.997  76.518 1.00 57.11  ? 283 ASP C C      1 
ATOM   7867  O O      . ASP C 2 265 ? 45.228  13.767  75.526 1.00 56.69  ? 283 ASP C O      1 
ATOM   7868  C CB     . ASP C 2 265 ? 45.497  16.266  76.433 1.00 62.27  ? 283 ASP C CB     1 
ATOM   7869  C CG     . ASP C 2 265 ? 46.852  16.003  77.041 1.00 69.47  ? 283 ASP C CG     1 
ATOM   7870  O OD1    . ASP C 2 265 ? 46.970  15.158  77.935 1.00 67.23  ? 283 ASP C OD1    1 
ATOM   7871  O OD2    . ASP C 2 265 ? 47.823  16.654  76.613 1.00 95.01  ? 283 ASP C OD2    1 
ATOM   7872  N N      . ILE C 2 266 ? 43.970  13.059  77.209 1.00 53.86  ? 284 ILE C N      1 
ATOM   7873  C CA     . ILE C 2 266 ? 44.048  11.689  76.759 1.00 55.48  ? 284 ILE C CA     1 
ATOM   7874  C C      . ILE C 2 266 ? 43.216  11.474  75.497 1.00 58.08  ? 284 ILE C C      1 
ATOM   7875  O O      . ILE C 2 266 ? 43.523  10.608  74.706 1.00 55.32  ? 284 ILE C O      1 
ATOM   7876  C CB     . ILE C 2 266 ? 43.695  10.700  77.888 1.00 47.56  ? 284 ILE C CB     1 
ATOM   7877  C CG1    . ILE C 2 266 ? 44.236  9.311   77.579 1.00 41.98  ? 284 ILE C CG1    1 
ATOM   7878  C CG2    . ILE C 2 266 ? 42.206  10.699  78.191 1.00 48.45  ? 284 ILE C CG2    1 
ATOM   7879  C CD1    . ILE C 2 266 ? 43.856  8.301   78.625 1.00 47.46  ? 284 ILE C CD1    1 
ATOM   7880  N N      . GLU C 2 267 ? 42.194  12.280  75.263 1.00 58.38  ? 285 GLU C N      1 
ATOM   7881  C CA     . GLU C 2 267 ? 41.440  12.143  74.035 1.00 48.59  ? 285 GLU C CA     1 
ATOM   7882  C C      . GLU C 2 267 ? 42.351  12.445  72.912 1.00 42.33  ? 285 GLU C C      1 
ATOM   7883  O O      . GLU C 2 267 ? 42.426  11.698  71.957 1.00 45.71  ? 285 GLU C O      1 
ATOM   7884  C CB     . GLU C 2 267 ? 40.289  13.132  73.974 1.00 42.06  ? 285 GLU C CB     1 
ATOM   7885  C CG     . GLU C 2 267 ? 38.975  12.612  74.504 1.00 47.61  ? 285 GLU C CG     1 
ATOM   7886  C CD     . GLU C 2 267 ? 37.808  13.403  73.967 1.00 53.30  ? 285 GLU C CD     1 
ATOM   7887  O OE1    . GLU C 2 267 ? 38.048  14.304  73.141 1.00 60.45  ? 285 GLU C OE1    1 
ATOM   7888  O OE2    . GLU C 2 267 ? 36.660  13.126  74.365 1.00 50.01  ? 285 GLU C OE2    1 
ATOM   7889  N N      . LYS C 2 268 ? 43.068  13.539  73.010 1.00 35.70  ? 286 LYS C N      1 
ATOM   7890  C CA     . LYS C 2 268 ? 43.892  13.939  71.908 1.00 42.08  ? 286 LYS C CA     1 
ATOM   7891  C C      . LYS C 2 268 ? 44.896  12.882  71.699 1.00 41.08  ? 286 LYS C C      1 
ATOM   7892  O O      . LYS C 2 268 ? 45.068  12.376  70.612 1.00 37.19  ? 286 LYS C O      1 
ATOM   7893  C CB     . LYS C 2 268 ? 44.579  15.255  72.227 1.00 40.44  ? 286 LYS C CB     1 
ATOM   7894  C CG     . LYS C 2 268 ? 45.410  15.827  71.094 1.00 38.09  ? 286 LYS C CG     1 
ATOM   7895  C CD     . LYS C 2 268 ? 46.047  17.145  71.492 1.00 34.01  ? 286 LYS C CD     1 
ATOM   7896  C CE     . LYS C 2 268 ? 46.986  16.979  72.674 1.00 42.13  ? 286 LYS C CE     1 
ATOM   7897  N NZ     . LYS C 2 268 ? 48.227  16.237  72.327 1.00 42.43  ? 286 LYS C NZ     1 
ATOM   7898  N N      . LYS C 2 269 ? 45.576  12.528  72.757 1.00 42.16  ? 287 LYS C N      1 
ATOM   7899  C CA     . LYS C 2 269 ? 46.654  11.603  72.608 1.00 45.04  ? 287 LYS C CA     1 
ATOM   7900  C C      . LYS C 2 269 ? 46.242  10.250  72.104 1.00 43.75  ? 287 LYS C C      1 
ATOM   7901  O O      . LYS C 2 269 ? 46.897  9.709   71.242 1.00 47.36  ? 287 LYS C O      1 
ATOM   7902  C CB     . LYS C 2 269 ? 47.431  11.524  73.903 1.00 49.27  ? 287 LYS C CB     1 
ATOM   7903  C CG     . LYS C 2 269 ? 48.186  12.793  74.242 1.00 48.63  ? 287 LYS C CG     1 
ATOM   7904  C CD     . LYS C 2 269 ? 48.836  12.679  75.607 1.00 61.43  ? 287 LYS C CD     1 
ATOM   7905  C CE     . LYS C 2 269 ? 49.798  13.822  75.868 1.00 70.11  ? 287 LYS C CE     1 
ATOM   7906  N NZ     . LYS C 2 269 ? 50.409  13.717  77.220 1.00 67.19  ? 287 LYS C NZ     1 
ATOM   7907  N N      . VAL C 2 270 ? 45.164  9.684   72.607 1.00 38.13  ? 288 VAL C N      1 
ATOM   7908  C CA     . VAL C 2 270 ? 44.809  8.340   72.201 1.00 37.12  ? 288 VAL C CA     1 
ATOM   7909  C C      . VAL C 2 270 ? 44.401  8.360   70.758 1.00 40.57  ? 288 VAL C C      1 
ATOM   7910  O O      . VAL C 2 270 ? 44.459  7.366   70.061 1.00 41.93  ? 288 VAL C O      1 
ATOM   7911  C CB     . VAL C 2 270 ? 43.746  7.762   73.121 1.00 38.99  ? 288 VAL C CB     1 
ATOM   7912  C CG1    . VAL C 2 270 ? 42.892  6.702   72.455 1.00 41.23  ? 288 VAL C CG1    1 
ATOM   7913  C CG2    . VAL C 2 270 ? 44.405  7.197   74.363 1.00 46.77  ? 288 VAL C CG2    1 
ATOM   7914  N N      . ASN C 2 271 ? 44.068  9.527   70.266 1.00 43.68  ? 289 ASN C N      1 
ATOM   7915  C CA     . ASN C 2 271 ? 43.616  9.634   68.899 1.00 41.82  ? 289 ASN C CA     1 
ATOM   7916  C C      . ASN C 2 271 ? 44.716  10.091  67.966 1.00 41.42  ? 289 ASN C C      1 
ATOM   7917  O O      . ASN C 2 271 ? 44.448  10.479  66.849 1.00 43.02  ? 289 ASN C O      1 
ATOM   7918  C CB     . ASN C 2 271 ? 42.420  10.564  68.829 1.00 41.02  ? 289 ASN C CB     1 
ATOM   7919  C CG     . ASN C 2 271 ? 41.130  9.873   69.149 1.00 46.50  ? 289 ASN C CG     1 
ATOM   7920  O OD1    . ASN C 2 271 ? 40.778  8.886   68.516 1.00 50.81  ? 289 ASN C OD1    1 
ATOM   7921  N ND2    . ASN C 2 271 ? 40.402  10.400  70.119 1.00 45.81  ? 289 ASN C ND2    1 
ATOM   7922  N N      . GLN C 2 272 ? 45.957  9.979   68.380 1.00 38.48  ? 290 GLN C N      1 
ATOM   7923  C CA     . GLN C 2 272 ? 47.043  10.279  67.492 1.00 35.61  ? 290 GLN C CA     1 
ATOM   7924  C C      . GLN C 2 272 ? 47.578  8.910   67.308 1.00 35.02  ? 290 GLN C C      1 
ATOM   7925  O O      . GLN C 2 272 ? 48.092  8.585   66.261 1.00 34.81  ? 290 GLN C O      1 
ATOM   7926  C CB     . GLN C 2 272 ? 48.031  11.173  68.186 1.00 37.42  ? 290 GLN C CB     1 
ATOM   7927  C CG     . GLN C 2 272 ? 47.508  12.570  68.439 1.00 40.15  ? 290 GLN C CG     1 
ATOM   7928  C CD     . GLN C 2 272 ? 48.501  13.432  69.174 1.00 47.24  ? 290 GLN C CD     1 
ATOM   7929  O OE1    . GLN C 2 272 ? 49.522  12.948  69.646 1.00 47.77  ? 290 GLN C OE1    1 
ATOM   7930  N NE2    . GLN C 2 272 ? 48.217  14.717  69.260 1.00 48.57  ? 290 GLN C NE2    1 
ATOM   7931  N N      . ILE C 2 273 ? 47.397  8.064   68.303 1.00 35.44  ? 291 ILE C N      1 
ATOM   7932  C CA     . ILE C 2 273 ? 47.824  6.681   68.205 1.00 37.32  ? 291 ILE C CA     1 
ATOM   7933  C C      . ILE C 2 273 ? 46.872  5.963   67.318 1.00 34.47  ? 291 ILE C C      1 
ATOM   7934  O O      . ILE C 2 273 ? 47.260  5.366   66.335 1.00 36.10  ? 291 ILE C O      1 
ATOM   7935  C CB     . ILE C 2 273 ? 47.749  5.990   69.561 1.00 34.80  ? 291 ILE C CB     1 
ATOM   7936  C CG1    . ILE C 2 273 ? 48.554  6.757   70.592 1.00 36.54  ? 291 ILE C CG1    1 
ATOM   7937  C CG2    . ILE C 2 273 ? 48.242  4.562   69.461 1.00 31.71  ? 291 ILE C CG2    1 
ATOM   7938  C CD1    . ILE C 2 273 ? 48.318  6.258   71.991 1.00 37.49  ? 291 ILE C CD1    1 
ATOM   7939  N N      . ILE C 2 274 ? 45.604  6.013   67.664 1.00 30.09  ? 292 ILE C N      1 
ATOM   7940  C CA     . ILE C 2 274 ? 44.613  5.292   66.911 1.00 31.12  ? 292 ILE C CA     1 
ATOM   7941  C C      . ILE C 2 274 ? 44.565  5.800   65.508 1.00 34.86  ? 292 ILE C C      1 
ATOM   7942  O O      . ILE C 2 274 ? 44.341  5.043   64.582 1.00 39.66  ? 292 ILE C O      1 
ATOM   7943  C CB     . ILE C 2 274 ? 43.259  5.381   67.596 1.00 33.17  ? 292 ILE C CB     1 
ATOM   7944  C CG1    . ILE C 2 274 ? 43.201  4.376   68.733 1.00 30.30  ? 292 ILE C CG1    1 
ATOM   7945  C CG2    . ILE C 2 274 ? 42.110  5.124   66.639 1.00 34.43  ? 292 ILE C CG2    1 
ATOM   7946  C CD1    . ILE C 2 274 ? 41.836  4.255   69.353 1.00 35.26  ? 292 ILE C CD1    1 
ATOM   7947  N N      . ASN C 2 275 ? 44.852  7.070   65.319 1.00 34.62  ? 293 ASN C N      1 
ATOM   7948  C CA     . ASN C 2 275 ? 44.774  7.644   63.996 1.00 34.32  ? 293 ASN C CA     1 
ATOM   7949  C C      . ASN C 2 275 ? 46.042  7.483   63.181 1.00 36.29  ? 293 ASN C C      1 
ATOM   7950  O O      . ASN C 2 275 ? 46.036  7.760   62.009 1.00 43.57  ? 293 ASN C O      1 
ATOM   7951  C CB     . ASN C 2 275 ? 44.367  9.088   64.074 1.00 30.98  ? 293 ASN C CB     1 
ATOM   7952  C CG     . ASN C 2 275 ? 42.912  9.267   64.375 1.00 33.39  ? 293 ASN C CG     1 
ATOM   7953  O OD1    . ASN C 2 275 ? 42.193  8.309   64.622 1.00 37.29  ? 293 ASN C OD1    1 
ATOM   7954  N ND2    . ASN C 2 275 ? 42.467  10.506  64.354 1.00 35.28  ? 293 ASN C ND2    1 
ATOM   7955  N N      . LEU C 2 276 ? 47.126  7.022   63.766 1.00 34.20  ? 294 LEU C N      1 
ATOM   7956  C CA     . LEU C 2 276 ? 48.314  6.757   62.981 1.00 33.80  ? 294 LEU C CA     1 
ATOM   7957  C C      . LEU C 2 276 ? 48.331  5.284   62.776 1.00 38.36  ? 294 LEU C C      1 
ATOM   7958  O O      . LEU C 2 276 ? 48.966  4.789   61.869 1.00 44.58  ? 294 LEU C O      1 
ATOM   7959  C CB     . LEU C 2 276 ? 49.590  7.160   63.693 1.00 31.66  ? 294 LEU C CB     1 
ATOM   7960  C CG     . LEU C 2 276 ? 50.927  7.090   62.963 1.00 32.26  ? 294 LEU C CG     1 
ATOM   7961  C CD1    . LEU C 2 276 ? 51.008  8.188   61.924 1.00 46.37  ? 294 LEU C CD1    1 
ATOM   7962  C CD2    . LEU C 2 276 ? 52.057  7.240   63.959 1.00 36.24  ? 294 LEU C CD2    1 
ATOM   7963  N N      . TRP C 2 277 ? 47.646  4.557   63.627 1.00 37.88  ? 295 TRP C N      1 
ATOM   7964  C CA     . TRP C 2 277 ? 47.562  3.138   63.441 1.00 41.67  ? 295 TRP C CA     1 
ATOM   7965  C C      . TRP C 2 277 ? 46.867  3.009   62.145 1.00 42.52  ? 295 TRP C C      1 
ATOM   7966  O O      . TRP C 2 277 ? 47.339  2.342   61.243 1.00 44.71  ? 295 TRP C O      1 
ATOM   7967  C CB     . TRP C 2 277 ? 46.729  2.530   64.546 1.00 41.56  ? 295 TRP C CB     1 
ATOM   7968  C CG     . TRP C 2 277 ? 46.558  1.063   64.532 1.00 45.31  ? 295 TRP C CG     1 
ATOM   7969  C CD1    . TRP C 2 277 ? 45.509  0.372   64.024 1.00 49.82  ? 295 TRP C CD1    1 
ATOM   7970  C CD2    . TRP C 2 277 ? 47.436  0.096   65.102 1.00 45.66  ? 295 TRP C CD2    1 
ATOM   7971  N NE1    . TRP C 2 277 ? 45.685  -0.970  64.218 1.00 48.62  ? 295 TRP C NE1    1 
ATOM   7972  C CE2    . TRP C 2 277 ? 46.863  -1.165  64.882 1.00 49.25  ? 295 TRP C CE2    1 
ATOM   7973  C CE3    . TRP C 2 277 ? 48.658  0.171   65.766 1.00 45.18  ? 295 TRP C CE3    1 
ATOM   7974  C CZ2    . TRP C 2 277 ? 47.468  -2.336  65.301 1.00 46.23  ? 295 TRP C CZ2    1 
ATOM   7975  C CZ3    . TRP C 2 277 ? 49.251  -0.990  66.180 1.00 47.61  ? 295 TRP C CZ3    1 
ATOM   7976  C CH2    . TRP C 2 277 ? 48.661  -2.227  65.948 1.00 44.42  ? 295 TRP C CH2    1 
ATOM   7977  N N      . ILE C 2 278 ? 45.733  3.665   62.036 1.00 34.08  ? 296 ILE C N      1 
ATOM   7978  C CA     . ILE C 2 278 ? 44.956  3.602   60.817 1.00 39.66  ? 296 ILE C CA     1 
ATOM   7979  C C      . ILE C 2 278 ? 45.784  4.025   59.620 1.00 36.72  ? 296 ILE C C      1 
ATOM   7980  O O      . ILE C 2 278 ? 45.785  3.357   58.608 1.00 34.35  ? 296 ILE C O      1 
ATOM   7981  C CB     . ILE C 2 278 ? 43.687  4.453   60.948 1.00 36.85  ? 296 ILE C CB     1 
ATOM   7982  C CG1    . ILE C 2 278 ? 42.719  3.801   61.921 1.00 33.19  ? 296 ILE C CG1    1 
ATOM   7983  C CG2    . ILE C 2 278 ? 43.014  4.645   59.606 1.00 37.14  ? 296 ILE C CG2    1 
ATOM   7984  C CD1    . ILE C 2 278 ? 41.553  4.690   62.273 1.00 37.65  ? 296 ILE C CD1    1 
ATOM   7985  N N      . SER C 2 279 ? 46.533  5.108   59.733 1.00 34.22  ? 297 SER C N      1 
ATOM   7986  C CA     . SER C 2 279 ? 47.281  5.606   58.601 1.00 34.13  ? 297 SER C CA     1 
ATOM   7987  C C      . SER C 2 279 ? 48.288  4.619   58.195 1.00 37.40  ? 297 SER C C      1 
ATOM   7988  O O      . SER C 2 279 ? 48.378  4.282   57.042 1.00 41.67  ? 297 SER C O      1 
ATOM   7989  C CB     . SER C 2 279 ? 47.996  6.899   58.932 1.00 30.76  ? 297 SER C CB     1 
ATOM   7990  O OG     . SER C 2 279 ? 49.237  6.686   59.563 1.00 27.59  ? 297 SER C OG     1 
ATOM   7991  N N      . SER C 2 280 ? 49.025  4.086   59.136 1.00 38.30  ? 298 SER C N      1 
ATOM   7992  C CA     . SER C 2 280 ? 50.095  3.189   58.791 1.00 43.37  ? 298 SER C CA     1 
ATOM   7993  C C      . SER C 2 280 ? 49.615  1.878   58.197 1.00 41.14  ? 298 SER C C      1 
ATOM   7994  O O      . SER C 2 280 ? 50.194  1.368   57.258 1.00 39.94  ? 298 SER C O      1 
ATOM   7995  C CB     . SER C 2 280 ? 50.947  2.948   60.009 1.00 42.39  ? 298 SER C CB     1 
ATOM   7996  O OG     . SER C 2 280 ? 51.453  4.164   60.511 1.00 47.19  ? 298 SER C OG     1 
ATOM   7997  N N      . TYR C 2 281 ? 48.548  1.328   58.727 1.00 37.50  ? 299 TYR C N      1 
ATOM   7998  C CA     . TYR C 2 281 ? 48.037  0.101   58.165 1.00 40.89  ? 299 TYR C CA     1 
ATOM   7999  C C      . TYR C 2 281 ? 47.616  0.250   56.703 1.00 41.79  ? 299 TYR C C      1 
ATOM   8000  O O      . TYR C 2 281 ? 48.100  -0.473  55.851 1.00 43.15  ? 299 TYR C O      1 
ATOM   8001  C CB     . TYR C 2 281 ? 46.955  -0.483  59.062 1.00 37.75  ? 299 TYR C CB     1 
ATOM   8002  C CG     . TYR C 2 281 ? 47.523  -1.422  60.090 1.00 40.11  ? 299 TYR C CG     1 
ATOM   8003  C CD1    . TYR C 2 281 ? 48.654  -1.085  60.803 1.00 40.48  ? 299 TYR C CD1    1 
ATOM   8004  C CD2    . TYR C 2 281 ? 46.942  -2.648  60.334 1.00 41.90  ? 299 TYR C CD2    1 
ATOM   8005  C CE1    . TYR C 2 281 ? 49.190  -1.942  61.732 1.00 43.75  ? 299 TYR C CE1    1 
ATOM   8006  C CE2    . TYR C 2 281 ? 47.474  -3.513  61.264 1.00 45.02  ? 299 TYR C CE2    1 
ATOM   8007  C CZ     . TYR C 2 281 ? 48.600  -3.149  61.955 1.00 47.08  ? 299 TYR C CZ     1 
ATOM   8008  O OH     . TYR C 2 281 ? 49.143  -3.994  62.880 1.00 44.92  ? 299 TYR C OH     1 
ATOM   8009  N N      . ILE C 2 282 ? 46.766  1.211   56.391 1.00 41.23  ? 300 ILE C N      1 
ATOM   8010  C CA     . ILE C 2 282 ? 46.322  1.441   55.026 1.00 32.04  ? 300 ILE C CA     1 
ATOM   8011  C C      . ILE C 2 282 ? 47.490  1.786   54.145 1.00 36.40  ? 300 ILE C C      1 
ATOM   8012  O O      . ILE C 2 282 ? 47.594  1.305   53.039 1.00 44.98  ? 300 ILE C O      1 
ATOM   8013  C CB     . ILE C 2 282 ? 45.382  2.644   54.998 1.00 30.75  ? 300 ILE C CB     1 
ATOM   8014  C CG1    . ILE C 2 282 ? 44.157  2.411   55.861 1.00 33.65  ? 300 ILE C CG1    1 
ATOM   8015  C CG2    . ILE C 2 282 ? 44.948  2.981   53.595 1.00 38.13  ? 300 ILE C CG2    1 
ATOM   8016  C CD1    . ILE C 2 282 ? 43.275  3.632   55.902 1.00 40.31  ? 300 ILE C CD1    1 
ATOM   8017  N N      . LYS C 2 283 ? 48.382  2.620   54.631 1.00 35.92  ? 301 LYS C N      1 
ATOM   8018  C CA     . LYS C 2 283 ? 49.533  3.033   53.853 1.00 42.40  ? 301 LYS C CA     1 
ATOM   8019  C C      . LYS C 2 283 ? 50.489  1.922   53.549 1.00 43.66  ? 301 LYS C C      1 
ATOM   8020  O O      . LYS C 2 283 ? 51.069  1.879   52.479 1.00 39.08  ? 301 LYS C O      1 
ATOM   8021  C CB     . LYS C 2 283 ? 50.277  4.150   54.573 1.00 38.57  ? 301 LYS C CB     1 
ATOM   8022  C CG     . LYS C 2 283 ? 50.963  5.141   53.662 1.00 44.17  ? 301 LYS C CG     1 
ATOM   8023  C CD     . LYS C 2 283 ? 51.686  6.183   54.490 1.00 53.07  ? 301 LYS C CD     1 
ATOM   8024  C CE     . LYS C 2 283 ? 52.595  5.516   55.503 1.00 56.62  ? 301 LYS C CE     1 
ATOM   8025  N NZ     . LYS C 2 283 ? 53.576  6.485   56.054 1.00 57.83  ? 301 LYS C NZ     1 
ATOM   8026  N N      . GLU C 2 284 ? 50.711  1.043   54.505 1.00 41.99  ? 302 GLU C N      1 
ATOM   8027  C CA     . GLU C 2 284 ? 51.705  0.009   54.312 1.00 43.82  ? 302 GLU C CA     1 
ATOM   8028  C C      . GLU C 2 284 ? 51.128  -1.259  53.708 1.00 45.16  ? 302 GLU C C      1 
ATOM   8029  O O      . GLU C 2 284 ? 51.858  -2.158  53.324 1.00 45.86  ? 302 GLU C O      1 
ATOM   8030  C CB     . GLU C 2 284 ? 52.440  -0.232  55.630 1.00 39.28  ? 302 GLU C CB     1 
ATOM   8031  C CG     . GLU C 2 284 ? 53.222  0.960   56.143 1.00 44.22  ? 302 GLU C CG     1 
ATOM   8032  C CD     . GLU C 2 284 ? 54.645  0.979   55.638 1.00 54.20  ? 302 GLU C CD     1 
ATOM   8033  O OE1    . GLU C 2 284 ? 55.185  -0.104  55.343 1.00 46.78  ? 302 GLU C OE1    1 
ATOM   8034  O OE2    . GLU C 2 284 ? 55.228  2.076   55.546 1.00 62.96  ? 302 GLU C OE2    1 
ATOM   8035  N N      . GLY C 2 285 ? 49.829  -1.374  53.641 1.00 40.08  ? 303 GLY C N      1 
ATOM   8036  C CA     . GLY C 2 285 ? 49.265  -2.503  52.961 1.00 32.28  ? 303 GLY C CA     1 
ATOM   8037  C C      . GLY C 2 285 ? 48.710  -3.567  53.815 1.00 36.13  ? 303 GLY C C      1 
ATOM   8038  O O      . GLY C 2 285 ? 48.170  -4.532  53.322 1.00 45.80  ? 303 GLY C O      1 
ATOM   8039  N N      . TYR C 2 286 ? 48.852  -3.438  55.105 1.00 35.62  ? 304 TYR C N      1 
ATOM   8040  C CA     . TYR C 2 286 ? 48.421  -4.521  55.931 1.00 36.90  ? 304 TYR C CA     1 
ATOM   8041  C C      . TYR C 2 286 ? 46.936  -4.794  55.908 1.00 41.02  ? 304 TYR C C      1 
ATOM   8042  O O      . TYR C 2 286 ? 46.558  -5.931  55.752 1.00 47.75  ? 304 TYR C O      1 
ATOM   8043  C CB     . TYR C 2 286 ? 48.947  -4.326  57.336 1.00 34.88  ? 304 TYR C CB     1 
ATOM   8044  C CG     . TYR C 2 286 ? 50.426  -4.090  57.409 1.00 35.52  ? 304 TYR C CG     1 
ATOM   8045  C CD1    . TYR C 2 286 ? 51.310  -4.935  56.774 1.00 34.27  ? 304 TYR C CD1    1 
ATOM   8046  C CD2    . TYR C 2 286 ? 50.939  -3.032  58.125 1.00 40.69  ? 304 TYR C CD2    1 
ATOM   8047  C CE1    . TYR C 2 286 ? 52.665  -4.726  56.841 1.00 36.43  ? 304 TYR C CE1    1 
ATOM   8048  C CE2    . TYR C 2 286 ? 52.293  -2.817  58.203 1.00 46.14  ? 304 TYR C CE2    1 
ATOM   8049  C CZ     . TYR C 2 286 ? 53.151  -3.669  57.558 1.00 43.68  ? 304 TYR C CZ     1 
ATOM   8050  O OH     . TYR C 2 286 ? 54.509  -3.468  57.624 1.00 44.43  ? 304 TYR C OH     1 
ATOM   8051  N N      . HIS C 2 287 ? 46.089  -3.781  56.006 1.00 39.83  ? 305 HIS C N      1 
ATOM   8052  C CA     . HIS C 2 287 ? 44.645  -3.951  56.045 1.00 39.46  ? 305 HIS C CA     1 
ATOM   8053  C C      . HIS C 2 287 ? 44.068  -2.633  55.577 1.00 39.82  ? 305 HIS C C      1 
ATOM   8054  O O      . HIS C 2 287 ? 44.788  -1.671  55.495 1.00 36.41  ? 305 HIS C O      1 
ATOM   8055  C CB     . HIS C 2 287 ? 44.115  -4.194  57.450 1.00 40.05  ? 305 HIS C CB     1 
ATOM   8056  C CG     . HIS C 2 287 ? 44.685  -5.369  58.170 1.00 45.16  ? 305 HIS C CG     1 
ATOM   8057  N ND1    . HIS C 2 287 ? 44.002  -6.552  58.310 1.00 52.82  ? 305 HIS C ND1    1 
ATOM   8058  C CD2    . HIS C 2 287 ? 45.830  -5.513  58.874 1.00 52.19  ? 305 HIS C CD2    1 
ATOM   8059  C CE1    . HIS C 2 287 ? 44.724  -7.395  59.024 1.00 57.74  ? 305 HIS C CE1    1 
ATOM   8060  N NE2    . HIS C 2 287 ? 45.841  -6.789  59.377 1.00 53.57  ? 305 HIS C NE2    1 
ATOM   8061  N N      . SER C 2 288 ? 42.783  -2.571  55.265 1.00 39.66  ? 306 SER C N      1 
ATOM   8062  C CA     . SER C 2 288 ? 42.104  -1.342  54.862 1.00 37.55  ? 306 SER C CA     1 
ATOM   8063  C C      . SER C 2 288 ? 41.661  -0.529  56.038 1.00 40.19  ? 306 SER C C      1 
ATOM   8064  O O      . SER C 2 288 ? 41.918  -0.886  57.159 1.00 40.24  ? 306 SER C O      1 
ATOM   8065  C CB     . SER C 2 288 ? 40.838  -1.677  54.119 1.00 35.80  ? 306 SER C CB     1 
ATOM   8066  O OG     . SER C 2 288 ? 41.104  -2.044  52.791 1.00 39.37  ? 306 SER C OG     1 
ATOM   8067  N N      . TYR C 2 289 ? 40.968  0.567   55.792 1.00 37.29  ? 307 TYR C N      1 
ATOM   8068  C CA     . TYR C 2 289 ? 40.453  1.390   56.879 1.00 38.89  ? 307 TYR C CA     1 
ATOM   8069  C C      . TYR C 2 289 ? 39.455  0.712   57.734 1.00 36.59  ? 307 TYR C C      1 
ATOM   8070  O O      . TYR C 2 289 ? 39.684  0.499   58.905 1.00 38.73  ? 307 TYR C O      1 
ATOM   8071  C CB     . TYR C 2 289 ? 39.809  2.646   56.296 1.00 41.21  ? 307 TYR C CB     1 
ATOM   8072  C CG     . TYR C 2 289 ? 39.087  3.575   57.244 1.00 35.25  ? 307 TYR C CG     1 
ATOM   8073  C CD1    . TYR C 2 289 ? 39.780  4.452   58.051 1.00 29.31  ? 307 TYR C CD1    1 
ATOM   8074  C CD2    . TYR C 2 289 ? 37.706  3.617   57.276 1.00 37.85  ? 307 TYR C CD2    1 
ATOM   8075  C CE1    . TYR C 2 289 ? 39.119  5.313   58.899 1.00 31.58  ? 307 TYR C CE1    1 
ATOM   8076  C CE2    . TYR C 2 289 ? 37.036  4.469   58.122 1.00 32.10  ? 307 TYR C CE2    1 
ATOM   8077  C CZ     . TYR C 2 289 ? 37.749  5.315   58.930 1.00 32.27  ? 307 TYR C CZ     1 
ATOM   8078  O OH     . TYR C 2 289 ? 37.070  6.162   59.767 1.00 29.97  ? 307 TYR C OH     1 
ATOM   8079  N N      . SER C 2 290 ? 38.343  0.358   57.160 1.00 34.53  ? 308 SER C N      1 
ATOM   8080  C CA     . SER C 2 290 ? 37.321  -0.175  57.976 1.00 37.90  ? 308 SER C CA     1 
ATOM   8081  C C      . SER C 2 290 ? 37.634  -1.528  58.469 1.00 39.96  ? 308 SER C C      1 
ATOM   8082  O O      . SER C 2 290 ? 36.897  -2.066  59.252 1.00 40.36  ? 308 SER C O      1 
ATOM   8083  C CB     . SER C 2 290 ? 36.030  -0.191  57.222 1.00 42.88  ? 308 SER C CB     1 
ATOM   8084  O OG     . SER C 2 290 ? 35.613  1.120   56.909 1.00 50.28  ? 308 SER C OG     1 
ATOM   8085  N N      . GLU C 2 291 ? 38.680  -2.131  57.977 1.00 39.37  ? 309 GLU C N      1 
ATOM   8086  C CA     . GLU C 2 291 ? 39.063  -3.398  58.513 1.00 39.80  ? 309 GLU C CA     1 
ATOM   8087  C C      . GLU C 2 291 ? 39.543  -3.227  59.923 1.00 40.70  ? 309 GLU C C      1 
ATOM   8088  O O      . GLU C 2 291 ? 39.274  -4.051  60.765 1.00 45.34  ? 309 GLU C O      1 
ATOM   8089  C CB     . GLU C 2 291 ? 40.057  -4.070  57.604 1.00 43.78  ? 309 GLU C CB     1 
ATOM   8090  C CG     . GLU C 2 291 ? 39.491  -4.345  56.225 1.00 45.55  ? 309 GLU C CG     1 
ATOM   8091  C CD     . GLU C 2 291 ? 40.320  -5.324  55.438 1.00 46.74  ? 309 GLU C CD     1 
ATOM   8092  O OE1    . GLU C 2 291 ? 41.449  -5.609  55.854 1.00 45.60  ? 309 GLU C OE1    1 
ATOM   8093  O OE2    . GLU C 2 291 ? 39.840  -5.820  54.411 1.00 44.97  ? 309 GLU C OE2    1 
ATOM   8094  N N      . VAL C 2 292 ? 40.253  -2.155  60.200 1.00 35.83  ? 310 VAL C N      1 
ATOM   8095  C CA     . VAL C 2 292 ? 40.696  -1.858  61.547 1.00 31.98  ? 310 VAL C CA     1 
ATOM   8096  C C      . VAL C 2 292 ? 39.602  -1.188  62.329 1.00 32.22  ? 310 VAL C C      1 
ATOM   8097  O O      . VAL C 2 292 ? 39.228  -1.632  63.388 1.00 34.90  ? 310 VAL C O      1 
ATOM   8098  C CB     . VAL C 2 292 ? 41.840  -0.875  61.517 1.00 31.82  ? 310 VAL C CB     1 
ATOM   8099  C CG1    . VAL C 2 292 ? 42.368  -0.646  62.911 1.00 44.15  ? 310 VAL C CG1    1 
ATOM   8100  C CG2    . VAL C 2 292 ? 42.941  -1.368  60.599 1.00 32.26  ? 310 VAL C CG2    1 
ATOM   8101  N N      . VAL C 2 293 ? 39.065  -0.117  61.801 1.00 35.14  ? 311 VAL C N      1 
ATOM   8102  C CA     . VAL C 2 293 ? 38.052  0.621   62.532 1.00 34.96  ? 311 VAL C CA     1 
ATOM   8103  C C      . VAL C 2 293 ? 36.940  -0.237  63.028 1.00 34.17  ? 311 VAL C C      1 
ATOM   8104  O O      . VAL C 2 293 ? 36.580  -0.156  64.182 1.00 37.50  ? 311 VAL C O      1 
ATOM   8105  C CB     . VAL C 2 293 ? 37.486  1.755   61.676 1.00 32.50  ? 311 VAL C CB     1 
ATOM   8106  C CG1    . VAL C 2 293 ? 36.197  2.308   62.246 1.00 32.03  ? 311 VAL C CG1    1 
ATOM   8107  C CG2    . VAL C 2 293 ? 38.511  2.854   61.546 1.00 32.07  ? 311 VAL C CG2    1 
ATOM   8108  N N      . ASP C 2 294 ? 36.403  -1.090  62.187 1.00 37.38  ? 312 ASP C N      1 
ATOM   8109  C CA     . ASP C 2 294 ? 35.252  -1.861  62.591 1.00 38.94  ? 312 ASP C CA     1 
ATOM   8110  C C      . ASP C 2 294 ? 35.593  -2.741  63.756 1.00 42.40  ? 312 ASP C C      1 
ATOM   8111  O O      . ASP C 2 294 ? 34.714  -3.150  64.489 1.00 45.14  ? 312 ASP C O      1 
ATOM   8112  C CB     . ASP C 2 294 ? 34.657  -2.612  61.423 1.00 41.44  ? 312 ASP C CB     1 
ATOM   8113  C CG     . ASP C 2 294 ? 33.901  -1.707  60.485 1.00 47.63  ? 312 ASP C CG     1 
ATOM   8114  O OD1    . ASP C 2 294 ? 33.540  -0.592  60.901 1.00 55.78  ? 312 ASP C OD1    1 
ATOM   8115  O OD2    . ASP C 2 294 ? 33.658  -2.103  59.335 1.00 41.47  ? 312 ASP C OD2    1 
ATOM   8116  N N      . VAL C 2 295 ? 36.864  -3.010  63.985 1.00 38.59  ? 313 VAL C N      1 
ATOM   8117  C CA     . VAL C 2 295 ? 37.236  -3.791  65.152 1.00 38.04  ? 313 VAL C CA     1 
ATOM   8118  C C      . VAL C 2 295 ? 37.193  -2.941  66.400 1.00 39.86  ? 313 VAL C C      1 
ATOM   8119  O O      . VAL C 2 295 ? 36.617  -3.340  67.394 1.00 39.69  ? 313 VAL C O      1 
ATOM   8120  C CB     . VAL C 2 295 ? 38.614  -4.424  64.972 1.00 38.09  ? 313 VAL C CB     1 
ATOM   8121  C CG1    . VAL C 2 295 ? 39.057  -5.100  66.246 1.00 41.38  ? 313 VAL C CG1    1 
ATOM   8122  C CG2    . VAL C 2 295 ? 38.582  -5.422  63.834 1.00 38.62  ? 313 VAL C CG2    1 
ATOM   8123  N N      . LEU C 2 296 ? 37.771  -1.748  66.334 1.00 36.99  ? 314 LEU C N      1 
ATOM   8124  C CA     . LEU C 2 296 ? 37.824  -0.844  67.478 1.00 33.01  ? 314 LEU C CA     1 
ATOM   8125  C C      . LEU C 2 296 ? 36.490  -0.290  67.838 1.00 36.23  ? 314 LEU C C      1 
ATOM   8126  O O      . LEU C 2 296 ? 36.325  0.269   68.899 1.00 43.42  ? 314 LEU C O      1 
ATOM   8127  C CB     . LEU C 2 296 ? 38.700  0.345   67.140 1.00 30.37  ? 314 LEU C CB     1 
ATOM   8128  C CG     . LEU C 2 296 ? 40.184  0.230   66.846 1.00 30.96  ? 314 LEU C CG     1 
ATOM   8129  C CD1    . LEU C 2 296 ? 40.594  1.327   65.885 1.00 27.82  ? 314 LEU C CD1    1 
ATOM   8130  C CD2    . LEU C 2 296 ? 40.955  0.348   68.143 1.00 29.42  ? 314 LEU C CD2    1 
ATOM   8131  N N      . THR C 2 297 ? 35.522  -0.424  66.954 1.00 37.50  ? 315 THR C N      1 
ATOM   8132  C CA     . THR C 2 297 ? 34.219  0.158   67.190 1.00 43.37  ? 315 THR C CA     1 
ATOM   8133  C C      . THR C 2 297 ? 33.247  -0.789  67.787 1.00 42.65  ? 315 THR C C      1 
ATOM   8134  O O      . THR C 2 297 ? 32.089  -0.458  67.944 1.00 44.98  ? 315 THR C O      1 
ATOM   8135  C CB     . THR C 2 297 ? 33.552  0.641   65.906 1.00 45.33  ? 315 THR C CB     1 
ATOM   8136  O OG1    . THR C 2 297 ? 33.473  -0.437  64.973 1.00 43.02  ? 315 THR C OG1    1 
ATOM   8137  C CG2    . THR C 2 297 ? 34.311  1.787   65.304 1.00 38.92  ? 315 THR C CG2    1 
ATOM   8138  N N      . GLU C 2 298 ? 33.690  -1.983  68.083 1.00 40.97  ? 316 GLU C N      1 
ATOM   8139  C CA     . GLU C 2 298 ? 32.771  -2.955  68.574 1.00 43.15  ? 316 GLU C CA     1 
ATOM   8140  C C      . GLU C 2 298 ? 32.331  -2.460  69.901 1.00 44.42  ? 316 GLU C C      1 
ATOM   8141  O O      . GLU C 2 298 ? 33.093  -1.823  70.605 1.00 44.72  ? 316 GLU C O      1 
ATOM   8142  C CB     . GLU C 2 298 ? 33.461  -4.292  68.711 1.00 44.85  ? 316 GLU C CB     1 
ATOM   8143  C CG     . GLU C 2 298 ? 32.511  -5.431  69.009 1.00 47.83  ? 316 GLU C CG     1 
ATOM   8144  C CD     . GLU C 2 298 ? 32.922  -6.712  68.344 1.00 59.74  ? 316 GLU C CD     1 
ATOM   8145  O OE1    . GLU C 2 298 ? 34.106  -6.830  67.975 1.00 59.64  ? 316 GLU C OE1    1 
ATOM   8146  O OE2    . GLU C 2 298 ? 32.051  -7.590  68.195 1.00 65.22  ? 316 GLU C OE2    1 
ATOM   8147  N N      . PRO C 2 299 ? 31.030  -2.657  70.233 1.00 43.20  ? 317 PRO C N      1 
ATOM   8148  C CA     . PRO C 2 299 ? 30.622  -2.264  71.571 1.00 44.84  ? 317 PRO C CA     1 
ATOM   8149  C C      . PRO C 2 299 ? 31.572  -2.560  72.721 1.00 50.23  ? 317 PRO C C      1 
ATOM   8150  O O      . PRO C 2 299 ? 31.779  -1.683  73.551 1.00 52.09  ? 317 PRO C O      1 
ATOM   8151  C CB     . PRO C 2 299 ? 29.380  -3.079  71.754 1.00 45.57  ? 317 PRO C CB     1 
ATOM   8152  C CG     . PRO C 2 299 ? 28.854  -3.240  70.383 1.00 41.72  ? 317 PRO C CG     1 
ATOM   8153  C CD     . PRO C 2 299 ? 30.055  -3.409  69.505 1.00 46.32  ? 317 PRO C CD     1 
ATOM   8154  N N      . PHE C 2 300 ? 32.118  -3.759  72.804 1.00 48.12  ? 318 PHE C N      1 
ATOM   8155  C CA     . PHE C 2 300 ? 32.958  -4.101  73.941 1.00 44.36  ? 318 PHE C CA     1 
ATOM   8156  C C      . PHE C 2 300 ? 34.209  -3.275  74.005 1.00 42.72  ? 318 PHE C C      1 
ATOM   8157  O O      . PHE C 2 300 ? 34.615  -2.855  75.070 1.00 47.82  ? 318 PHE C O      1 
ATOM   8158  C CB     . PHE C 2 300 ? 33.232  -5.608  74.019 1.00 40.40  ? 318 PHE C CB     1 
ATOM   8159  C CG     . PHE C 2 300 ? 34.446  -6.081  73.277 1.00 38.24  ? 318 PHE C CG     1 
ATOM   8160  C CD1    . PHE C 2 300 ? 34.390  -6.339  71.927 1.00 44.21  ? 318 PHE C CD1    1 
ATOM   8161  C CD2    . PHE C 2 300 ? 35.620  -6.343  73.952 1.00 35.39  ? 318 PHE C CD2    1 
ATOM   8162  C CE1    . PHE C 2 300 ? 35.497  -6.799  71.252 1.00 46.23  ? 318 PHE C CE1    1 
ATOM   8163  C CE2    . PHE C 2 300 ? 36.729  -6.806  73.285 1.00 34.67  ? 318 PHE C CE2    1 
ATOM   8164  C CZ     . PHE C 2 300 ? 36.666  -7.037  71.932 1.00 40.23  ? 318 PHE C CZ     1 
ATOM   8165  N N      . LEU C 2 301 ? 34.797  -2.983  72.860 1.00 40.63  ? 319 LEU C N      1 
ATOM   8166  C CA     . LEU C 2 301 ? 36.053  -2.274  72.865 1.00 44.37  ? 319 LEU C CA     1 
ATOM   8167  C C      . LEU C 2 301 ? 35.794  -0.826  73.100 1.00 50.57  ? 319 LEU C C      1 
ATOM   8168  O O      . LEU C 2 301 ? 36.641  -0.113  73.606 1.00 48.95  ? 319 LEU C O      1 
ATOM   8169  C CB     . LEU C 2 301 ? 36.810  -2.473  71.567 1.00 42.25  ? 319 LEU C CB     1 
ATOM   8170  C CG     . LEU C 2 301 ? 37.723  -3.678  71.423 1.00 41.95  ? 319 LEU C CG     1 
ATOM   8171  C CD1    . LEU C 2 301 ? 38.464  -3.626  70.104 1.00 40.14  ? 319 LEU C CD1    1 
ATOM   8172  C CD2    . LEU C 2 301 ? 38.710  -3.705  72.570 1.00 46.97  ? 319 LEU C CD2    1 
ATOM   8173  N N      . GLN C 2 302 ? 34.585  -0.389  72.824 1.00 48.64  ? 320 GLN C N      1 
ATOM   8174  C CA     . GLN C 2 302 ? 34.319  1.008   72.981 1.00 49.86  ? 320 GLN C CA     1 
ATOM   8175  C C      . GLN C 2 302 ? 34.168  1.295   74.438 1.00 57.50  ? 320 GLN C C      1 
ATOM   8176  O O      . GLN C 2 302 ? 34.307  2.423   74.860 1.00 69.04  ? 320 GLN C O      1 
ATOM   8177  C CB     . GLN C 2 302 ? 33.092  1.455   72.216 1.00 48.40  ? 320 GLN C CB     1 
ATOM   8178  C CG     . GLN C 2 302 ? 33.366  1.789   70.769 1.00 50.36  ? 320 GLN C CG     1 
ATOM   8179  C CD     . GLN C 2 302 ? 34.348  2.925   70.631 1.00 55.96  ? 320 GLN C CD     1 
ATOM   8180  O OE1    . GLN C 2 302 ? 34.084  4.043   71.064 1.00 66.08  ? 320 GLN C OE1    1 
ATOM   8181  N NE2    . GLN C 2 302 ? 35.486  2.649   70.018 1.00 51.89  ? 320 GLN C NE2    1 
ATOM   8182  N N      . SER C 2 303 ? 33.887  0.281   75.227 1.00 51.54  ? 321 SER C N      1 
ATOM   8183  C CA     . SER C 2 303 ? 33.637  0.522   76.640 1.00 65.53  ? 321 SER C CA     1 
ATOM   8184  C C      . SER C 2 303 ? 34.830  1.132   77.319 1.00 64.98  ? 321 SER C C      1 
ATOM   8185  O O      . SER C 2 303 ? 34.679  1.980   78.178 1.00 62.84  ? 321 SER C O      1 
ATOM   8186  C CB     . SER C 2 303 ? 33.249  -0.769  77.359 1.00 65.99  ? 321 SER C CB     1 
ATOM   8187  O OG     . SER C 2 303 ? 33.235  -0.599  78.762 1.00 61.25  ? 321 SER C OG     1 
ATOM   8188  N N      . ILE C 2 304 ? 36.026  0.721   76.938 1.00 58.31  ? 322 ILE C N      1 
ATOM   8189  C CA     . ILE C 2 304 ? 37.207  1.214   77.617 1.00 62.59  ? 322 ILE C CA     1 
ATOM   8190  C C      . ILE C 2 304 ? 37.247  2.701   77.407 1.00 64.39  ? 322 ILE C C      1 
ATOM   8191  O O      . ILE C 2 304 ? 37.460  3.466   78.337 1.00 66.27  ? 322 ILE C O      1 
ATOM   8192  C CB     . ILE C 2 304 ? 38.483  0.570   77.063 1.00 57.86  ? 322 ILE C CB     1 
ATOM   8193  C CG1    . ILE C 2 304 ? 38.516  -0.921  77.395 1.00 53.20  ? 322 ILE C CG1    1 
ATOM   8194  C CG2    . ILE C 2 304 ? 39.712  1.224   77.663 1.00 53.13  ? 322 ILE C CG2    1 
ATOM   8195  C CD1    . ILE C 2 304 ? 38.010  -1.830  76.300 1.00 48.23  ? 322 ILE C CD1    1 
ATOM   8196  N N      . PHE C 2 305 ? 36.974  3.123   76.187 1.00 62.67  ? 323 PHE C N      1 
ATOM   8197  C CA     . PHE C 2 305 ? 37.008  4.528   75.863 1.00 57.23  ? 323 PHE C CA     1 
ATOM   8198  C C      . PHE C 2 305 ? 35.905  5.257   76.594 1.00 62.07  ? 323 PHE C C      1 
ATOM   8199  O O      . PHE C 2 305 ? 36.130  6.321   77.137 1.00 64.41  ? 323 PHE C O      1 
ATOM   8200  C CB     . PHE C 2 305 ? 36.883  4.708   74.358 1.00 49.37  ? 323 PHE C CB     1 
ATOM   8201  C CG     . PHE C 2 305 ? 37.950  4.026   73.584 1.00 46.38  ? 323 PHE C CG     1 
ATOM   8202  C CD1    . PHE C 2 305 ? 39.254  4.447   73.676 1.00 46.10  ? 323 PHE C CD1    1 
ATOM   8203  C CD2    . PHE C 2 305 ? 37.646  2.971   72.761 1.00 50.72  ? 323 PHE C CD2    1 
ATOM   8204  C CE1    . PHE C 2 305 ? 40.246  3.822   72.963 1.00 38.45  ? 323 PHE C CE1    1 
ATOM   8205  C CE2    . PHE C 2 305 ? 38.629  2.337   72.043 1.00 53.96  ? 323 PHE C CE2    1 
ATOM   8206  C CZ     . PHE C 2 305 ? 39.931  2.769   72.142 1.00 50.14  ? 323 PHE C CZ     1 
ATOM   8207  N N      . ASP C 2 306 ? 34.702  4.710   76.629 1.00 64.14  ? 324 ASP C N      1 
ATOM   8208  C CA     . ASP C 2 306 ? 33.592  5.400   77.250 1.00 70.88  ? 324 ASP C CA     1 
ATOM   8209  C C      . ASP C 2 306 ? 33.916  5.680   78.680 1.00 71.52  ? 324 ASP C C      1 
ATOM   8210  O O      . ASP C 2 306 ? 33.769  6.792   79.142 1.00 70.98  ? 324 ASP C O      1 
ATOM   8211  C CB     . ASP C 2 306 ? 32.349  4.527   77.167 1.00 72.69  ? 324 ASP C CB     1 
ATOM   8212  C CG     . ASP C 2 306 ? 31.179  5.070   77.982 1.00 85.29  ? 324 ASP C CG     1 
ATOM   8213  O OD1    . ASP C 2 306 ? 31.001  6.304   78.056 1.00 91.85  ? 324 ASP C OD1    1 
ATOM   8214  O OD2    . ASP C 2 306 ? 30.414  4.254   78.538 1.00 78.51  ? 324 ASP C OD2    1 
ATOM   8215  N N      . LYS C 2 307 ? 34.393  4.681   79.387 1.00 67.44  ? 325 LYS C N      1 
ATOM   8216  C CA     . LYS C 2 307 ? 34.672  4.824   80.802 1.00 67.36  ? 325 LYS C CA     1 
ATOM   8217  C C      . LYS C 2 307 ? 35.750  5.819   81.074 1.00 60.04  ? 325 LYS C C      1 
ATOM   8218  O O      . LYS C 2 307 ? 35.868  6.319   82.186 1.00 55.55  ? 325 LYS C O      1 
ATOM   8219  C CB     . LYS C 2 307 ? 35.073  3.485   81.386 1.00 69.54  ? 325 LYS C CB     1 
ATOM   8220  C CG     . LYS C 2 307 ? 34.009  2.407   81.279 1.00 66.10  ? 325 LYS C CG     1 
ATOM   8221  C CD     . LYS C 2 307 ? 32.699  2.840   81.908 1.00 78.33  ? 325 LYS C CD     1 
ATOM   8222  C CE     . LYS C 2 307 ? 31.672  1.727   81.845 1.00 78.51  ? 325 LYS C CE     1 
ATOM   8223  N NZ     . LYS C 2 307 ? 30.363  2.169   82.399 1.00 82.93  ? 325 LYS C NZ     1 
ATOM   8224  N N      . ALA C 2 308 ? 36.599  6.043   80.093 1.00 56.47  ? 326 ALA C N      1 
ATOM   8225  C CA     . ALA C 2 308 ? 37.648  7.014   80.238 1.00 60.65  ? 326 ALA C CA     1 
ATOM   8226  C C      . ALA C 2 308 ? 37.298  8.310   79.577 1.00 57.00  ? 326 ALA C C      1 
ATOM   8227  O O      . ALA C 2 308 ? 38.110  9.209   79.534 1.00 51.09  ? 326 ALA C O      1 
ATOM   8228  C CB     . ALA C 2 308 ? 38.873  6.460   79.623 1.00 52.89  ? 326 ALA C CB     1 
ATOM   8229  N N      . ASN C 2 309 ? 36.098  8.405   79.054 1.00 55.44  ? 327 ASN C N      1 
ATOM   8230  C CA     . ASN C 2 309 ? 35.674  9.586   78.344 1.00 55.82  ? 327 ASN C CA     1 
ATOM   8231  C C      . ASN C 2 309 ? 36.571  9.894   77.173 1.00 53.76  ? 327 ASN C C      1 
ATOM   8232  O O      . ASN C 2 309 ? 37.025  11.010  77.031 1.00 54.05  ? 327 ASN C O      1 
ATOM   8233  C CB     . ASN C 2 309 ? 35.506  10.760  79.285 1.00 57.10  ? 327 ASN C CB     1 
ATOM   8234  C CG     . ASN C 2 309 ? 34.599  10.433  80.452 1.00 69.62  ? 327 ASN C CG     1 
ATOM   8235  O OD1    . ASN C 2 309 ? 34.852  10.842  81.580 1.00 83.66  ? 327 ASN C OD1    1 
ATOM   8236  N ND2    . ASN C 2 309 ? 33.548  9.672   80.188 1.00 65.86  ? 327 ASN C ND2    1 
ATOM   8237  N N      . ILE C 2 310 ? 36.814  8.907   76.320 1.00 49.45  ? 328 ILE C N      1 
ATOM   8238  C CA     . ILE C 2 310 ? 37.606  9.134   75.130 1.00 51.10  ? 328 ILE C CA     1 
ATOM   8239  C C      . ILE C 2 310 ? 36.705  8.981   73.938 1.00 48.07  ? 328 ILE C C      1 
ATOM   8240  O O      . ILE C 2 310 ? 36.121  7.934   73.733 1.00 49.74  ? 328 ILE C O      1 
ATOM   8241  C CB     . ILE C 2 310 ? 38.788  8.179   75.018 1.00 47.40  ? 328 ILE C CB     1 
ATOM   8242  C CG1    . ILE C 2 310 ? 39.611  8.227   76.290 1.00 47.72  ? 328 ILE C CG1    1 
ATOM   8243  C CG2    . ILE C 2 310 ? 39.673  8.559   73.850 1.00 42.56  ? 328 ILE C CG2    1 
ATOM   8244  C CD1    . ILE C 2 310 ? 41.009  7.719   76.091 1.00 53.30  ? 328 ILE C CD1    1 
ATOM   8245  N N      . LYS C 2 311 ? 36.564  10.043  73.161 1.00 47.11  ? 329 LYS C N      1 
ATOM   8246  C CA     . LYS C 2 311 ? 35.707  10.020  72.000 1.00 47.49  ? 329 LYS C CA     1 
ATOM   8247  C C      . LYS C 2 311 ? 36.602  9.939   70.826 1.00 53.47  ? 329 LYS C C      1 
ATOM   8248  O O      . LYS C 2 311 ? 37.410  10.825  70.597 1.00 56.27  ? 329 LYS C O      1 
ATOM   8249  C CB     . LYS C 2 311 ? 34.888  11.291  71.940 1.00 56.23  ? 329 LYS C CB     1 
ATOM   8250  C CG     . LYS C 2 311 ? 34.163  11.554  70.632 1.00 64.28  ? 329 LYS C CG     1 
ATOM   8251  C CD     . LYS C 2 311 ? 33.033  10.573  70.389 1.00 62.33  ? 329 LYS C CD     1 
ATOM   8252  C CE     . LYS C 2 311 ? 32.181  11.036  69.220 1.00 68.64  ? 329 LYS C CE     1 
ATOM   8253  N NZ     . LYS C 2 311 ? 33.015  11.476  68.067 1.00 59.54  ? 329 LYS C NZ     1 
ATOM   8254  N N      . LEU C 2 312 ? 36.468  8.872   70.064 1.00 49.06  ? 330 LEU C N      1 
ATOM   8255  C CA     . LEU C 2 312 ? 37.372  8.664   68.974 1.00 43.31  ? 330 LEU C CA     1 
ATOM   8256  C C      . LEU C 2 312 ? 36.875  9.180   67.646 1.00 48.14  ? 330 LEU C C      1 
ATOM   8257  O O      . LEU C 2 312 ? 35.739  8.938   67.277 1.00 49.54  ? 330 LEU C O      1 
ATOM   8258  C CB     . LEU C 2 312 ? 37.669  7.187   68.892 1.00 47.77  ? 330 LEU C CB     1 
ATOM   8259  C CG     . LEU C 2 312 ? 38.057  6.390   70.122 1.00 51.10  ? 330 LEU C CG     1 
ATOM   8260  C CD1    . LEU C 2 312 ? 38.182  4.948   69.686 1.00 47.10  ? 330 LEU C CD1    1 
ATOM   8261  C CD2    . LEU C 2 312 ? 39.382  6.882   70.659 1.00 54.63  ? 330 LEU C CD2    1 
ATOM   8262  N N      . ASN C 2 313 ? 37.726  9.882   66.912 1.00 48.05  ? 331 ASN C N      1 
ATOM   8263  C CA     . ASN C 2 313 ? 37.335  10.455  65.643 1.00 45.04  ? 331 ASN C CA     1 
ATOM   8264  C C      . ASN C 2 313 ? 37.480  9.450   64.567 1.00 42.28  ? 331 ASN C C      1 
ATOM   8265  O O      . ASN C 2 313 ? 36.918  9.615   63.502 1.00 48.31  ? 331 ASN C O      1 
ATOM   8266  C CB     . ASN C 2 313 ? 38.192  11.666  65.333 1.00 47.08  ? 331 ASN C CB     1 
ATOM   8267  C CG     . ASN C 2 313 ? 39.660  11.434  65.583 1.00 51.60  ? 331 ASN C CG     1 
ATOM   8268  O OD1    . ASN C 2 313 ? 40.105  10.309  65.776 1.00 50.75  ? 331 ASN C OD1    1 
ATOM   8269  N ND2    . ASN C 2 313 ? 40.429  12.512  65.573 1.00 47.76  ? 331 ASN C ND2    1 
ATOM   8270  N N      . TYR C 2 314 ? 38.217  8.391   64.844 1.00 36.01  ? 332 TYR C N      1 
ATOM   8271  C CA     . TYR C 2 314 ? 38.389  7.321   63.891 1.00 38.17  ? 332 TYR C CA     1 
ATOM   8272  C C      . TYR C 2 314 ? 38.951  7.850   62.616 1.00 39.20  ? 332 TYR C C      1 
ATOM   8273  O O      . TYR C 2 314 ? 38.716  7.312   61.559 1.00 42.96  ? 332 TYR C O      1 
ATOM   8274  C CB     . TYR C 2 314 ? 37.082  6.607   63.614 1.00 35.98  ? 332 TYR C CB     1 
ATOM   8275  C CG     . TYR C 2 314 ? 36.433  5.976   64.795 1.00 31.31  ? 332 TYR C CG     1 
ATOM   8276  C CD1    . TYR C 2 314 ? 37.088  5.015   65.536 1.00 40.92  ? 332 TYR C CD1    1 
ATOM   8277  C CD2    . TYR C 2 314 ? 35.145  6.314   65.148 1.00 33.60  ? 332 TYR C CD2    1 
ATOM   8278  C CE1    . TYR C 2 314 ? 36.481  4.422   66.615 1.00 46.24  ? 332 TYR C CE1    1 
ATOM   8279  C CE2    . TYR C 2 314 ? 34.529  5.729   66.223 1.00 41.83  ? 332 TYR C CE2    1 
ATOM   8280  C CZ     . TYR C 2 314 ? 35.204  4.787   66.950 1.00 49.15  ? 332 TYR C CZ     1 
ATOM   8281  O OH     . TYR C 2 314 ? 34.580  4.214   68.013 1.00 45.98  ? 332 TYR C OH     1 
ATOM   8282  N N      . GLY C 2 315 ? 39.729  8.894   62.709 1.00 31.26  ? 333 GLY C N      1 
ATOM   8283  C CA     . GLY C 2 315 ? 40.380  9.374   61.526 1.00 30.28  ? 333 GLY C CA     1 
ATOM   8284  C C      . GLY C 2 315 ? 39.578  10.312  60.698 1.00 34.00  ? 333 GLY C C      1 
ATOM   8285  O O      . GLY C 2 315 ? 40.066  10.809  59.709 1.00 39.14  ? 333 GLY C O      1 
ATOM   8286  N N      . VAL C 2 316 ? 38.348  10.580  61.078 1.00 36.08  ? 334 VAL C N      1 
ATOM   8287  C CA     . VAL C 2 316 ? 37.535  11.433  60.257 1.00 33.41  ? 334 VAL C CA     1 
ATOM   8288  C C      . VAL C 2 316 ? 38.253  12.735  60.237 1.00 42.57  ? 334 VAL C C      1 
ATOM   8289  O O      . VAL C 2 316 ? 38.750  13.208  61.251 1.00 49.10  ? 334 VAL C O      1 
ATOM   8290  C CB     . VAL C 2 316 ? 36.071  11.553  60.707 1.00 28.48  ? 334 VAL C CB     1 
ATOM   8291  C CG1    . VAL C 2 316 ? 35.926  12.352  61.987 1.00 46.47  ? 334 VAL C CG1    1 
ATOM   8292  C CG2    . VAL C 2 316 ? 35.225  12.165  59.607 1.00 32.05  ? 334 VAL C CG2    1 
ATOM   8293  N N      . LEU C 2 317 ? 38.393  13.294  59.056 1.00 47.94  ? 335 LEU C N      1 
ATOM   8294  C CA     . LEU C 2 317 ? 39.118  14.530  58.919 1.00 45.84  ? 335 LEU C CA     1 
ATOM   8295  C C      . LEU C 2 317 ? 38.171  15.476  58.254 1.00 53.52  ? 335 LEU C C      1 
ATOM   8296  O O      . LEU C 2 317 ? 37.347  15.063  57.457 1.00 59.11  ? 335 LEU C O      1 
ATOM   8297  C CB     . LEU C 2 317 ? 40.366  14.320  58.072 1.00 44.42  ? 335 LEU C CB     1 
ATOM   8298  C CG     . LEU C 2 317 ? 41.572  13.603  58.654 1.00 36.24  ? 335 LEU C CG     1 
ATOM   8299  C CD1    . LEU C 2 317 ? 42.586  13.360  57.555 1.00 38.05  ? 335 LEU C CD1    1 
ATOM   8300  C CD2    . LEU C 2 317 ? 42.170  14.443  59.765 1.00 32.23  ? 335 LEU C CD2    1 
ATOM   8301  N N      . ASP C 2 318 ? 38.284  16.753  58.558 1.00 51.37  ? 336 ASP C N      1 
ATOM   8302  C CA     . ASP C 2 318 ? 37.341  17.707  58.025 1.00 58.06  ? 336 ASP C CA     1 
ATOM   8303  C C      . ASP C 2 318 ? 37.489  17.974  56.535 1.00 55.97  ? 336 ASP C C      1 
ATOM   8304  O O      . ASP C 2 318 ? 36.507  18.263  55.864 1.00 53.67  ? 336 ASP C O      1 
ATOM   8305  C CB     . ASP C 2 318 ? 37.418  18.990  58.830 1.00 48.74  ? 336 ASP C CB     1 
ATOM   8306  C CG     . ASP C 2 318 ? 36.902  18.821  60.239 1.00 51.54  ? 336 ASP C CG     1 
ATOM   8307  O OD1    . ASP C 2 318 ? 36.303  17.768  60.531 1.00 62.66  ? 336 ASP C OD1    1 
ATOM   8308  O OD2    . ASP C 2 318 ? 37.086  19.744  61.053 1.00 45.84  ? 336 ASP C OD2    1 
ATOM   8309  N N      . ASP C 2 319 ? 38.695  17.844  56.003 1.00 53.23  ? 337 ASP C N      1 
ATOM   8310  C CA     . ASP C 2 319 ? 38.919  18.092  54.585 1.00 49.54  ? 337 ASP C CA     1 
ATOM   8311  C C      . ASP C 2 319 ? 39.426  16.878  53.876 1.00 55.40  ? 337 ASP C C      1 
ATOM   8312  O O      . ASP C 2 319 ? 40.604  16.563  53.963 1.00 50.49  ? 337 ASP C O      1 
ATOM   8313  C CB     . ASP C 2 319 ? 39.911  19.220  54.374 1.00 50.19  ? 337 ASP C CB     1 
ATOM   8314  C CG     . ASP C 2 319 ? 39.934  19.718  52.956 1.00 63.26  ? 337 ASP C CG     1 
ATOM   8315  O OD1    . ASP C 2 319 ? 38.896  19.616  52.278 1.00 74.04  ? 337 ASP C OD1    1 
ATOM   8316  O OD2    . ASP C 2 319 ? 40.985  20.231  52.526 1.00 63.88  ? 337 ASP C OD2    1 
ATOM   8317  N N      . THR C 2 320 ? 38.553  16.218  53.126 1.00 59.62  ? 338 THR C N      1 
ATOM   8318  C CA     . THR C 2 320 ? 38.940  15.053  52.367 1.00 55.91  ? 338 THR C CA     1 
ATOM   8319  C C      . THR C 2 320 ? 38.913  15.385  50.916 1.00 54.45  ? 338 THR C C      1 
ATOM   8320  O O      . THR C 2 320 ? 38.976  14.501  50.089 1.00 58.46  ? 338 THR C O      1 
ATOM   8321  C CB     . THR C 2 320 ? 37.936  13.931  52.555 1.00 47.98  ? 338 THR C CB     1 
ATOM   8322  O OG1    . THR C 2 320 ? 36.665  14.348  52.056 1.00 55.64  ? 338 THR C OG1    1 
ATOM   8323  C CG2    . THR C 2 320 ? 37.803  13.575  54.024 1.00 55.05  ? 338 THR C CG2    1 
ATOM   8324  N N      . HIS C 2 321 ? 38.855  16.658  50.590 1.00 47.60  ? 339 HIS C N      1 
ATOM   8325  C CA     . HIS C 2 321 ? 38.718  17.057  49.214 1.00 51.38  ? 339 HIS C CA     1 
ATOM   8326  C C      . HIS C 2 321 ? 39.824  16.615  48.357 1.00 54.62  ? 339 HIS C C      1 
ATOM   8327  O O      . HIS C 2 321 ? 39.616  16.196  47.233 1.00 59.31  ? 339 HIS C O      1 
ATOM   8328  C CB     . HIS C 2 321 ? 38.676  18.564  49.133 1.00 58.05  ? 339 HIS C CB     1 
ATOM   8329  C CG     . HIS C 2 321 ? 38.310  19.091  47.784 1.00 68.62  ? 339 HIS C CG     1 
ATOM   8330  N ND1    . HIS C 2 321 ? 38.827  20.264  47.281 1.00 62.30  ? 339 HIS C ND1    1 
ATOM   8331  C CD2    . HIS C 2 321 ? 37.481  18.605  46.831 1.00 69.21  ? 339 HIS C CD2    1 
ATOM   8332  C CE1    . HIS C 2 321 ? 38.329  20.481  46.078 1.00 66.11  ? 339 HIS C CE1    1 
ATOM   8333  N NE2    . HIS C 2 321 ? 37.511  19.487  45.780 1.00 72.66  ? 339 HIS C NE2    1 
ATOM   8334  N N      . ALA C 2 322 ? 41.023  16.715  48.861 1.00 49.25  ? 340 ALA C N      1 
ATOM   8335  C CA     . ALA C 2 322 ? 42.145  16.408  48.029 1.00 49.11  ? 340 ALA C CA     1 
ATOM   8336  C C      . ALA C 2 322 ? 41.958  15.054  47.498 1.00 49.23  ? 340 ALA C C      1 
ATOM   8337  O O      . ALA C 2 322 ? 42.037  14.826  46.308 1.00 53.80  ? 340 ALA C O      1 
ATOM   8338  C CB     . ALA C 2 322 ? 43.393  16.447  48.856 1.00 52.84  ? 340 ALA C CB     1 
ATOM   8339  N N      . GLU C 2 323 ? 41.725  14.128  48.398 1.00 48.09  ? 341 GLU C N      1 
ATOM   8340  C CA     . GLU C 2 323 ? 41.636  12.753  48.003 1.00 49.64  ? 341 GLU C CA     1 
ATOM   8341  C C      . GLU C 2 323 ? 40.506  12.509  47.067 1.00 53.21  ? 341 GLU C C      1 
ATOM   8342  O O      . GLU C 2 323 ? 40.649  11.750  46.133 1.00 58.55  ? 341 GLU C O      1 
ATOM   8343  C CB     . GLU C 2 323 ? 41.488  11.903  49.240 1.00 52.83  ? 341 GLU C CB     1 
ATOM   8344  C CG     . GLU C 2 323 ? 42.681  11.985  50.173 1.00 63.29  ? 341 GLU C CG     1 
ATOM   8345  C CD     . GLU C 2 323 ? 42.542  13.064  51.225 1.00 64.97  ? 341 GLU C CD     1 
ATOM   8346  O OE1    . GLU C 2 323 ? 41.503  13.097  51.903 1.00 62.55  ? 341 GLU C OE1    1 
ATOM   8347  O OE2    . GLU C 2 323 ? 43.481  13.866  51.383 1.00 63.86  ? 341 GLU C OE2    1 
ATOM   8348  N N      . PHE C 2 324 ? 39.383  13.165  47.276 1.00 49.84  ? 342 PHE C N      1 
ATOM   8349  C CA     . PHE C 2 324 ? 38.221  12.888  46.459 1.00 47.35  ? 342 PHE C CA     1 
ATOM   8350  C C      . PHE C 2 324 ? 38.586  13.265  45.085 1.00 47.62  ? 342 PHE C C      1 
ATOM   8351  O O      . PHE C 2 324 ? 38.215  12.608  44.153 1.00 49.46  ? 342 PHE C O      1 
ATOM   8352  C CB     . PHE C 2 324 ? 37.049  13.743  46.888 1.00 48.04  ? 342 PHE C CB     1 
ATOM   8353  C CG     . PHE C 2 324 ? 35.715  13.092  46.741 1.00 40.25  ? 342 PHE C CG     1 
ATOM   8354  C CD1    . PHE C 2 324 ? 35.344  12.063  47.567 1.00 50.35  ? 342 PHE C CD1    1 
ATOM   8355  C CD2    . PHE C 2 324 ? 34.813  13.554  45.814 1.00 37.03  ? 342 PHE C CD2    1 
ATOM   8356  C CE1    . PHE C 2 324 ? 34.105  11.478  47.446 1.00 52.32  ? 342 PHE C CE1    1 
ATOM   8357  C CE2    . PHE C 2 324 ? 33.572  12.975  45.687 1.00 40.62  ? 342 PHE C CE2    1 
ATOM   8358  C CZ     . PHE C 2 324 ? 33.216  11.934  46.505 1.00 44.78  ? 342 PHE C CZ     1 
ATOM   8359  N N      . ARG C 2 325 ? 39.321  14.340  44.943 1.00 49.98  ? 343 ARG C N      1 
ATOM   8360  C CA     . ARG C 2 325 ? 39.595  14.825  43.610 1.00 57.42  ? 343 ARG C CA     1 
ATOM   8361  C C      . ARG C 2 325 ? 40.408  13.847  42.847 1.00 59.11  ? 343 ARG C C      1 
ATOM   8362  O O      . ARG C 2 325 ? 40.098  13.521  41.718 1.00 65.02  ? 343 ARG C O      1 
ATOM   8363  C CB     . ARG C 2 325 ? 40.301  16.170  43.646 1.00 69.05  ? 343 ARG C CB     1 
ATOM   8364  C CG     . ARG C 2 325 ? 40.376  16.866  42.303 1.00 70.48  ? 343 ARG C CG     1 
ATOM   8365  C CD     . ARG C 2 325 ? 41.259  18.098  42.384 1.00 78.20  ? 343 ARG C CD     1 
ATOM   8366  N NE     . ARG C 2 325 ? 42.618  17.768  42.806 1.00 85.55  ? 343 ARG C NE     1 
ATOM   8367  C CZ     . ARG C 2 325 ? 43.618  17.501  41.973 1.00 91.25  ? 343 ARG C CZ     1 
ATOM   8368  N NH1    . ARG C 2 325 ? 43.423  17.524  40.663 1.00 99.49  ? 343 ARG C NH1    1 
ATOM   8369  N NH2    . ARG C 2 325 ? 44.819  17.214  42.451 1.00 88.95  ? 343 ARG C NH2    1 
ATOM   8370  N N      . LYS C 2 326 ? 41.447  13.342  43.462 1.00 54.95  ? 344 LYS C N      1 
ATOM   8371  C CA     . LYS C 2 326 ? 42.322  12.467  42.740 1.00 56.11  ? 344 LYS C CA     1 
ATOM   8372  C C      . LYS C 2 326 ? 41.578  11.199  42.502 1.00 49.48  ? 344 LYS C C      1 
ATOM   8373  O O      . LYS C 2 326 ? 41.813  10.518  41.530 1.00 51.14  ? 344 LYS C O      1 
ATOM   8374  C CB     . LYS C 2 326 ? 43.593  12.265  43.533 1.00 58.72  ? 344 LYS C CB     1 
ATOM   8375  C CG     . LYS C 2 326 ? 44.195  13.572  44.023 1.00 61.51  ? 344 LYS C CG     1 
ATOM   8376  C CD     . LYS C 2 326 ? 45.635  13.416  44.477 1.00 61.36  ? 344 LYS C CD     1 
ATOM   8377  C CE     . LYS C 2 326 ? 46.567  13.226  43.290 1.00 70.49  ? 344 LYS C CE     1 
ATOM   8378  N NZ     . LYS C 2 326 ? 47.999  13.143  43.691 1.00 68.35  ? 344 LYS C NZ     1 
ATOM   8379  N N      . ALA C 2 327 ? 40.647  10.887  43.365 1.00 45.30  ? 345 ALA C N      1 
ATOM   8380  C CA     . ALA C 2 327 ? 39.810  9.727   43.153 1.00 44.37  ? 345 ALA C CA     1 
ATOM   8381  C C      . ALA C 2 327 ? 38.817  9.939   42.040 1.00 51.22  ? 345 ALA C C      1 
ATOM   8382  O O      . ALA C 2 327 ? 38.485  9.010   41.331 1.00 53.33  ? 345 ALA C O      1 
ATOM   8383  C CB     . ALA C 2 327 ? 39.081  9.403   44.415 1.00 43.76  ? 345 ALA C CB     1 
ATOM   8384  N N      . GLN C 2 328 ? 38.320  11.152  41.875 1.00 53.68  ? 346 GLN C N      1 
ATOM   8385  C CA     . GLN C 2 328 ? 37.396  11.457  40.796 1.00 50.71  ? 346 GLN C CA     1 
ATOM   8386  C C      . GLN C 2 328 ? 38.095  11.331  39.481 1.00 52.63  ? 346 GLN C C      1 
ATOM   8387  O O      . GLN C 2 328 ? 37.506  10.922  38.501 1.00 60.11  ? 346 GLN C O      1 
ATOM   8388  C CB     . GLN C 2 328 ? 36.879  12.878  40.924 1.00 49.35  ? 346 GLN C CB     1 
ATOM   8389  C CG     . GLN C 2 328 ? 35.812  13.075  41.978 1.00 49.04  ? 346 GLN C CG     1 
ATOM   8390  C CD     . GLN C 2 328 ? 35.357  14.513  42.070 1.00 52.64  ? 346 GLN C CD     1 
ATOM   8391  O OE1    . GLN C 2 328 ? 36.016  15.416  41.561 1.00 54.21  ? 346 GLN C OE1    1 
ATOM   8392  N NE2    . GLN C 2 328 ? 34.229  14.733  42.720 1.00 50.13  ? 346 GLN C NE2    1 
ATOM   8393  N N      . ASP C 2 329 ? 39.373  11.643  39.444 1.00 51.18  ? 347 ASP C N      1 
ATOM   8394  C CA     . ASP C 2 329 ? 40.067  11.625  38.184 1.00 54.28  ? 347 ASP C CA     1 
ATOM   8395  C C      . ASP C 2 329 ? 40.392  10.212  37.800 1.00 52.71  ? 347 ASP C C      1 
ATOM   8396  O O      . ASP C 2 329 ? 40.414  9.878   36.634 1.00 62.01  ? 347 ASP C O      1 
ATOM   8397  C CB     . ASP C 2 329 ? 41.315  12.474  38.261 1.00 58.27  ? 347 ASP C CB     1 
ATOM   8398  C CG     . ASP C 2 329 ? 41.015  13.930  38.537 1.00 67.41  ? 347 ASP C CG     1 
ATOM   8399  O OD1    . ASP C 2 329 ? 39.829  14.311  38.516 1.00 65.14  ? 347 ASP C OD1    1 
ATOM   8400  O OD2    . ASP C 2 329 ? 41.968  14.697  38.772 1.00 66.09  ? 347 ASP C OD2    1 
ATOM   8401  N N      . TYR C 2 330 ? 40.653  9.377   38.777 1.00 43.66  ? 348 TYR C N      1 
ATOM   8402  C CA     . TYR C 2 330 ? 40.963  8.000   38.509 1.00 44.18  ? 348 TYR C CA     1 
ATOM   8403  C C      . TYR C 2 330 ? 39.800  7.381   37.845 1.00 47.12  ? 348 TYR C C      1 
ATOM   8404  O O      . TYR C 2 330 ? 39.930  6.787   36.795 1.00 46.18  ? 348 TYR C O      1 
ATOM   8405  C CB     . TYR C 2 330 ? 41.146  7.323   39.847 1.00 45.44  ? 348 TYR C CB     1 
ATOM   8406  C CG     . TYR C 2 330 ? 41.794  5.967   39.877 1.00 46.60  ? 348 TYR C CG     1 
ATOM   8407  C CD1    . TYR C 2 330 ? 43.127  5.796   39.544 1.00 40.59  ? 348 TYR C CD1    1 
ATOM   8408  C CD2    . TYR C 2 330 ? 41.087  4.867   40.322 1.00 42.62  ? 348 TYR C CD2    1 
ATOM   8409  C CE1    . TYR C 2 330 ? 43.719  4.556   39.610 1.00 33.55  ? 348 TYR C CE1    1 
ATOM   8410  C CE2    . TYR C 2 330 ? 41.672  3.627   40.392 1.00 40.83  ? 348 TYR C CE2    1 
ATOM   8411  C CZ     . TYR C 2 330 ? 42.984  3.480   40.033 1.00 38.23  ? 348 TYR C CZ     1 
ATOM   8412  O OH     . TYR C 2 330 ? 43.540  2.237   40.111 1.00 45.50  ? 348 TYR C OH     1 
ATOM   8413  N N      . VAL C 2 331 ? 38.641  7.503   38.463 1.00 45.22  ? 349 VAL C N      1 
ATOM   8414  C CA     . VAL C 2 331 ? 37.465  6.856   37.941 1.00 48.29  ? 349 VAL C CA     1 
ATOM   8415  C C      . VAL C 2 331 ? 37.154  7.360   36.580 1.00 50.97  ? 349 VAL C C      1 
ATOM   8416  O O      . VAL C 2 331 ? 36.727  6.612   35.751 1.00 49.55  ? 349 VAL C O      1 
ATOM   8417  C CB     . VAL C 2 331 ? 36.264  6.971   38.876 1.00 43.59  ? 349 VAL C CB     1 
ATOM   8418  C CG1    . VAL C 2 331 ? 36.608  6.345   40.206 1.00 45.96  ? 349 VAL C CG1    1 
ATOM   8419  C CG2    . VAL C 2 331 ? 35.844  8.401   39.087 1.00 47.24  ? 349 VAL C CG2    1 
ATOM   8420  N N      . PHE C 2 332 ? 37.412  8.621   36.313 1.00 52.13  ? 350 PHE C N      1 
ATOM   8421  C CA     . PHE C 2 332 ? 37.096  9.183   35.029 1.00 51.40  ? 350 PHE C CA     1 
ATOM   8422  C C      . PHE C 2 332 ? 37.863  8.416   34.012 1.00 54.63  ? 350 PHE C C      1 
ATOM   8423  O O      . PHE C 2 332 ? 37.290  7.823   33.120 1.00 59.42  ? 350 PHE C O      1 
ATOM   8424  C CB     . PHE C 2 332 ? 37.546  10.616  34.971 1.00 53.51  ? 350 PHE C CB     1 
ATOM   8425  C CG     . PHE C 2 332 ? 36.671  11.488  34.147 1.00 67.54  ? 350 PHE C CG     1 
ATOM   8426  C CD1    . PHE C 2 332 ? 35.365  11.711  34.522 1.00 71.80  ? 350 PHE C CD1    1 
ATOM   8427  C CD2    . PHE C 2 332 ? 37.154  12.099  33.011 1.00 69.74  ? 350 PHE C CD2    1 
ATOM   8428  C CE1    . PHE C 2 332 ? 34.545  12.517  33.773 1.00 74.47  ? 350 PHE C CE1    1 
ATOM   8429  C CE2    . PHE C 2 332 ? 36.342  12.910  32.256 1.00 83.54  ? 350 PHE C CE2    1 
ATOM   8430  C CZ     . PHE C 2 332 ? 35.035  13.122  32.642 1.00 83.68  ? 350 PHE C CZ     1 
ATOM   8431  N N      . GLY C 2 333 ? 39.174  8.423   34.130 1.00 48.21  ? 351 GLY C N      1 
ATOM   8432  C CA     . GLY C 2 333 ? 40.005  7.782   33.136 1.00 47.84  ? 351 GLY C CA     1 
ATOM   8433  C C      . GLY C 2 333 ? 39.904  6.296   33.022 1.00 45.04  ? 351 GLY C C      1 
ATOM   8434  O O      . GLY C 2 333 ? 39.950  5.750   31.943 1.00 44.53  ? 351 GLY C O      1 
ATOM   8435  N N      . LEU C 2 334 ? 39.779  5.628   34.146 1.00 44.98  ? 352 LEU C N      1 
ATOM   8436  C CA     . LEU C 2 334 ? 39.709  4.197   34.122 1.00 43.88  ? 352 LEU C CA     1 
ATOM   8437  C C      . LEU C 2 334 ? 38.426  3.801   33.443 1.00 44.53  ? 352 LEU C C      1 
ATOM   8438  O O      . LEU C 2 334 ? 38.405  2.841   32.697 1.00 48.03  ? 352 LEU C O      1 
ATOM   8439  C CB     . LEU C 2 334 ? 39.791  3.628   35.524 1.00 43.05  ? 352 LEU C CB     1 
ATOM   8440  C CG     . LEU C 2 334 ? 41.131  3.611   36.239 1.00 41.03  ? 352 LEU C CG     1 
ATOM   8441  C CD1    . LEU C 2 334 ? 41.202  2.320   37.030 1.00 38.78  ? 352 LEU C CD1    1 
ATOM   8442  C CD2    . LEU C 2 334 ? 42.268  3.668   35.239 1.00 52.20  ? 352 LEU C CD2    1 
ATOM   8443  N N      . THR C 2 335 ? 37.350  4.530   33.689 1.00 43.34  ? 353 THR C N      1 
ATOM   8444  C CA     . THR C 2 335 ? 36.094  4.264   33.012 1.00 46.11  ? 353 THR C CA     1 
ATOM   8445  C C      . THR C 2 335 ? 36.069  4.654   31.551 1.00 49.28  ? 353 THR C C      1 
ATOM   8446  O O      . THR C 2 335 ? 35.451  3.970   30.754 1.00 51.56  ? 353 THR C O      1 
ATOM   8447  C CB     . THR C 2 335 ? 34.929  4.911   33.716 1.00 49.21  ? 353 THR C CB     1 
ATOM   8448  O OG1    . THR C 2 335 ? 35.165  6.313   33.827 1.00 56.72  ? 353 THR C OG1    1 
ATOM   8449  C CG2    . THR C 2 335 ? 34.746  4.304   35.093 1.00 49.23  ? 353 THR C CG2    1 
ATOM   8450  N N      . ILE C 2 336 ? 36.698  5.759   31.172 1.00 47.54  ? 354 ILE C N      1 
ATOM   8451  C CA     . ILE C 2 336 ? 36.784  6.163   29.767 1.00 47.50  ? 354 ILE C CA     1 
ATOM   8452  C C      . ILE C 2 336 ? 37.674  5.245   28.992 1.00 49.96  ? 354 ILE C C      1 
ATOM   8453  O O      . ILE C 2 336 ? 37.374  4.924   27.862 1.00 55.37  ? 354 ILE C O      1 
ATOM   8454  C CB     . ILE C 2 336 ? 37.274  7.594   29.602 1.00 42.53  ? 354 ILE C CB     1 
ATOM   8455  C CG1    . ILE C 2 336 ? 36.157  8.567   29.942 1.00 53.47  ? 354 ILE C CG1    1 
ATOM   8456  C CG2    . ILE C 2 336 ? 37.718  7.885   28.184 1.00 45.37  ? 354 ILE C CG2    1 
ATOM   8457  C CD1    . ILE C 2 336 ? 36.516  10.005  29.665 1.00 63.39  ? 354 ILE C CD1    1 
ATOM   8458  N N      . GLN C 2 337 ? 38.760  4.776   29.579 1.00 46.80  ? 355 GLN C N      1 
ATOM   8459  C CA     . GLN C 2 337 ? 39.592  3.803   28.895 1.00 42.86  ? 355 GLN C CA     1 
ATOM   8460  C C      . GLN C 2 337 ? 38.901  2.485   28.710 1.00 48.07  ? 355 GLN C C      1 
ATOM   8461  O O      . GLN C 2 337 ? 39.256  1.743   27.831 1.00 47.93  ? 355 GLN C O      1 
ATOM   8462  C CB     . GLN C 2 337 ? 41.006  3.675   29.450 1.00 44.17  ? 355 GLN C CB     1 
ATOM   8463  C CG     . GLN C 2 337 ? 41.194  2.767   30.650 1.00 61.87  ? 355 GLN C CG     1 
ATOM   8464  C CD     . GLN C 2 337 ? 42.662  2.582   30.997 1.00 61.89  ? 355 GLN C CD     1 
ATOM   8465  O OE1    . GLN C 2 337 ? 43.543  3.050   30.278 1.00 49.33  ? 355 GLN C OE1    1 
ATOM   8466  N NE2    . GLN C 2 337 ? 42.930  1.888   32.096 1.00 46.37  ? 355 GLN C NE2    1 
ATOM   8467  N N      . SER C 2 338 ? 37.925  2.156   29.528 1.00 43.34  ? 356 SER C N      1 
ATOM   8468  C CA     . SER C 2 338 ? 37.177  0.950   29.280 1.00 46.38  ? 356 SER C CA     1 
ATOM   8469  C C      . SER C 2 338 ? 36.484  1.109   27.978 1.00 46.56  ? 356 SER C C      1 
ATOM   8470  O O      . SER C 2 338 ? 36.425  0.195   27.188 1.00 48.07  ? 356 SER C O      1 
ATOM   8471  C CB     . SER C 2 338 ? 36.130  0.756   30.339 1.00 48.44  ? 356 SER C CB     1 
ATOM   8472  O OG     . SER C 2 338 ? 36.702  0.293   31.546 1.00 49.75  ? 356 SER C OG     1 
ATOM   8473  N N      . ALA C 2 339 ? 35.930  2.271   27.746 1.00 41.54  ? 357 ALA C N      1 
ATOM   8474  C CA     . ALA C 2 339 ? 35.276  2.548   26.487 1.00 42.08  ? 357 ALA C CA     1 
ATOM   8475  C C      . ALA C 2 339 ? 36.127  2.604   25.262 1.00 40.40  ? 357 ALA C C      1 
ATOM   8476  O O      . ALA C 2 339 ? 35.705  2.144   24.235 1.00 50.50  ? 357 ALA C O      1 
ATOM   8477  C CB     . ALA C 2 339 ? 34.479  3.810   26.583 1.00 43.65  ? 357 ALA C CB     1 
ATOM   8478  N N      . MET C 2 340 ? 37.304  3.183   25.325 1.00 35.75  ? 358 MET C N      1 
ATOM   8479  C CA     . MET C 2 340 ? 38.131  3.168   24.163 1.00 39.10  ? 358 MET C CA     1 
ATOM   8480  C C      . MET C 2 340 ? 38.400  1.751   23.894 1.00 46.90  ? 358 MET C C      1 
ATOM   8481  O O      . MET C 2 340 ? 38.276  1.287   22.785 1.00 51.45  ? 358 MET C O      1 
ATOM   8482  C CB     . MET C 2 340 ? 39.467  3.783   24.463 1.00 37.58  ? 358 MET C CB     1 
ATOM   8483  C CG     . MET C 2 340 ? 40.384  3.882   23.265 1.00 41.38  ? 358 MET C CG     1 
ATOM   8484  S SD     . MET C 2 340 ? 41.952  3.079   23.590 1.00 46.96  ? 358 MET C SD     1 
ATOM   8485  C CE     . MET C 2 340 ? 42.362  3.815   25.160 1.00 46.87  ? 358 MET C CE     1 
ATOM   8486  N N      . HIS C 2 341 ? 38.727  1.027   24.934 1.00 42.40  ? 359 HIS C N      1 
ATOM   8487  C CA     . HIS C 2 341 ? 39.081  -0.339  24.756 1.00 40.49  ? 359 HIS C CA     1 
ATOM   8488  C C      . HIS C 2 341 ? 37.912  -1.086  24.209 1.00 45.53  ? 359 HIS C C      1 
ATOM   8489  O O      . HIS C 2 341 ? 38.101  -1.916  23.374 1.00 55.09  ? 359 HIS C O      1 
ATOM   8490  C CB     . HIS C 2 341 ? 39.556  -0.942  26.052 1.00 42.98  ? 359 HIS C CB     1 
ATOM   8491  C CG     . HIS C 2 341 ? 40.904  -0.479  26.503 1.00 41.69  ? 359 HIS C CG     1 
ATOM   8492  N ND1    . HIS C 2 341 ? 41.904  -0.119  25.631 1.00 31.29  ? 359 HIS C ND1    1 
ATOM   8493  C CD2    . HIS C 2 341 ? 41.430  -0.363  27.743 1.00 43.58  ? 359 HIS C CD2    1 
ATOM   8494  C CE1    . HIS C 2 341 ? 42.982  0.219   26.313 1.00 33.44  ? 359 HIS C CE1    1 
ATOM   8495  N NE2    . HIS C 2 341 ? 42.719  0.082   27.597 1.00 39.08  ? 359 HIS C NE2    1 
ATOM   8496  N N      . HIS C 2 342 ? 36.694  -0.821  24.642 1.00 42.05  ? 360 HIS C N      1 
ATOM   8497  C CA     . HIS C 2 342 ? 35.551  -1.479  24.025 1.00 43.96  ? 360 HIS C CA     1 
ATOM   8498  C C      . HIS C 2 342 ? 35.380  -1.134  22.564 1.00 52.91  ? 360 HIS C C      1 
ATOM   8499  O O      . HIS C 2 342 ? 35.077  -1.998  21.769 1.00 58.46  ? 360 HIS C O      1 
ATOM   8500  C CB     . HIS C 2 342 ? 34.278  -1.159  24.749 1.00 42.11  ? 360 HIS C CB     1 
ATOM   8501  C CG     . HIS C 2 342 ? 33.053  -1.676  24.070 1.00 59.21  ? 360 HIS C CG     1 
ATOM   8502  N ND1    . HIS C 2 342 ? 32.217  -0.870  23.331 1.00 71.56  ? 360 HIS C ND1    1 
ATOM   8503  C CD2    . HIS C 2 342 ? 32.524  -2.920  24.013 1.00 61.37  ? 360 HIS C CD2    1 
ATOM   8504  C CE1    . HIS C 2 342 ? 31.223  -1.594  22.850 1.00 62.96  ? 360 HIS C CE1    1 
ATOM   8505  N NE2    . HIS C 2 342 ? 31.387  -2.841  23.249 1.00 61.87  ? 360 HIS C NE2    1 
ATOM   8506  N N      . GLU C 2 343 ? 35.561  0.115   22.183 1.00 50.03  ? 361 GLU C N      1 
ATOM   8507  C CA     . GLU C 2 343 ? 35.496  0.475   20.784 1.00 45.99  ? 361 GLU C CA     1 
ATOM   8508  C C      . GLU C 2 343 ? 36.601  -0.182  20.022 1.00 54.10  ? 361 GLU C C      1 
ATOM   8509  O O      . GLU C 2 343 ? 36.391  -0.659  18.930 1.00 60.04  ? 361 GLU C O      1 
ATOM   8510  C CB     . GLU C 2 343 ? 35.595  1.968   20.615 1.00 47.32  ? 361 GLU C CB     1 
ATOM   8511  C CG     . GLU C 2 343 ? 35.477  2.468   19.192 1.00 64.06  ? 361 GLU C CG     1 
ATOM   8512  C CD     . GLU C 2 343 ? 35.498  3.979   19.115 1.00 62.63  ? 361 GLU C CD     1 
ATOM   8513  O OE1    . GLU C 2 343 ? 35.569  4.626   20.176 1.00 48.04  ? 361 GLU C OE1    1 
ATOM   8514  O OE2    . GLU C 2 343 ? 35.440  4.519   17.995 1.00 64.20  ? 361 GLU C OE2    1 
ATOM   8515  N N      . LEU C 2 344 ? 37.787  -0.230  20.592 1.00 51.24  ? 362 LEU C N      1 
ATOM   8516  C CA     . LEU C 2 344 ? 38.917  -0.833  19.917 1.00 51.03  ? 362 LEU C CA     1 
ATOM   8517  C C      . LEU C 2 344 ? 38.596  -2.263  19.717 1.00 49.47  ? 362 LEU C C      1 
ATOM   8518  O O      . LEU C 2 344 ? 38.899  -2.837  18.698 1.00 53.27  ? 362 LEU C O      1 
ATOM   8519  C CB     . LEU C 2 344 ? 40.170  -0.721  20.776 1.00 42.98  ? 362 LEU C CB     1 
ATOM   8520  C CG     . LEU C 2 344 ? 41.552  -1.061  20.254 1.00 40.21  ? 362 LEU C CG     1 
ATOM   8521  C CD1    . LEU C 2 344 ? 41.948  -0.048  19.198 1.00 43.94  ? 362 LEU C CD1    1 
ATOM   8522  C CD2    . LEU C 2 344 ? 42.512  -1.007  21.426 1.00 33.91  ? 362 LEU C CD2    1 
ATOM   8523  N N      . GLN C 2 345 ? 37.983  -2.857  20.708 1.00 50.76  ? 363 GLN C N      1 
ATOM   8524  C CA     . GLN C 2 345 ? 37.650  -4.237  20.620 1.00 56.42  ? 363 GLN C CA     1 
ATOM   8525  C C      . GLN C 2 345 ? 36.702  -4.365  19.491 1.00 61.92  ? 363 GLN C C      1 
ATOM   8526  O O      . GLN C 2 345 ? 36.822  -5.269  18.700 1.00 65.85  ? 363 GLN C O      1 
ATOM   8527  C CB     . GLN C 2 345 ? 36.950  -4.705  21.883 1.00 56.85  ? 363 GLN C CB     1 
ATOM   8528  C CG     . GLN C 2 345 ? 37.867  -5.051  23.047 1.00 56.69  ? 363 GLN C CG     1 
ATOM   8529  C CD     . GLN C 2 345 ? 37.099  -5.494  24.279 1.00 58.77  ? 363 GLN C CD     1 
ATOM   8530  O OE1    . GLN C 2 345 ? 35.991  -6.016  24.178 1.00 63.37  ? 363 GLN C OE1    1 
ATOM   8531  N NE2    . GLN C 2 345 ? 37.688  -5.298  25.447 1.00 57.15  ? 363 GLN C NE2    1 
ATOM   8532  N N      . GLU C 2 346 ? 35.759  -3.454  19.389 1.00 57.15  ? 364 GLU C N      1 
ATOM   8533  C CA     . GLU C 2 346 ? 34.772  -3.573  18.356 1.00 60.00  ? 364 GLU C CA     1 
ATOM   8534  C C      . GLU C 2 346 ? 35.255  -2.991  17.072 1.00 57.16  ? 364 GLU C C      1 
ATOM   8535  O O      . GLU C 2 346 ? 34.459  -2.703  16.198 1.00 55.54  ? 364 GLU C O      1 
ATOM   8536  C CB     . GLU C 2 346 ? 33.474  -2.926  18.762 1.00 62.55  ? 364 GLU C CB     1 
ATOM   8537  C CG     . GLU C 2 346 ? 32.678  -3.724  19.773 1.00 64.84  ? 364 GLU C CG     1 
ATOM   8538  C CD     . GLU C 2 346 ? 31.193  -3.453  19.667 1.00 77.37  ? 364 GLU C CD     1 
ATOM   8539  O OE1    . GLU C 2 346 ? 30.795  -2.629  18.821 1.00 82.26  ? 364 GLU C OE1    1 
ATOM   8540  O OE2    . GLU C 2 346 ? 30.422  -4.069  20.426 1.00 77.10  ? 364 GLU C OE2    1 
ATOM   8541  N N      . ARG C 2 347 ? 36.552  -2.785  16.947 1.00 57.28  ? 365 ARG C N      1 
ATOM   8542  C CA     . ARG C 2 347 ? 37.059  -2.352  15.661 1.00 57.80  ? 365 ARG C CA     1 
ATOM   8543  C C      . ARG C 2 347 ? 37.899  -3.490  15.213 1.00 65.88  ? 365 ARG C C      1 
ATOM   8544  O O      . ARG C 2 347 ? 38.037  -3.763  14.028 1.00 63.37  ? 365 ARG C O      1 
ATOM   8545  C CB     . ARG C 2 347 ? 37.910  -1.106  15.796 1.00 55.72  ? 365 ARG C CB     1 
ATOM   8546  C CG     . ARG C 2 347 ? 37.105  0.177   15.830 1.00 62.24  ? 365 ARG C CG     1 
ATOM   8547  C CD     . ARG C 2 347 ? 37.983  1.390   15.589 1.00 65.94  ? 365 ARG C CD     1 
ATOM   8548  N NE     . ARG C 2 347 ? 37.189  2.609   15.482 1.00 63.38  ? 365 ARG C NE     1 
ATOM   8549  C CZ     . ARG C 2 347 ? 37.693  3.804   15.197 1.00 60.51  ? 365 ARG C CZ     1 
ATOM   8550  N NH1    . ARG C 2 347 ? 38.994  3.942   14.987 1.00 53.93  ? 365 ARG C NH1    1 
ATOM   8551  N NH2    . ARG C 2 347 ? 36.896  4.858   15.119 1.00 56.92  ? 365 ARG C NH2    1 
ATOM   8552  N N      . PHE C 2 348 ? 38.470  -4.180  16.174 1.00 67.57  ? 366 PHE C N      1 
ATOM   8553  C CA     . PHE C 2 348 ? 39.249  -5.329  15.832 1.00 66.86  ? 366 PHE C CA     1 
ATOM   8554  C C      . PHE C 2 348 ? 38.293  -6.477  15.772 1.00 69.50  ? 366 PHE C C      1 
ATOM   8555  O O      . PHE C 2 348 ? 38.612  -7.513  15.218 1.00 76.06  ? 366 PHE C O      1 
ATOM   8556  C CB     . PHE C 2 348 ? 40.354  -5.547  16.832 1.00 59.63  ? 366 PHE C CB     1 
ATOM   8557  C CG     . PHE C 2 348 ? 41.599  -4.798  16.513 1.00 61.87  ? 366 PHE C CG     1 
ATOM   8558  C CD1    . PHE C 2 348 ? 42.430  -5.229  15.505 1.00 69.15  ? 366 PHE C CD1    1 
ATOM   8559  C CD2    . PHE C 2 348 ? 41.940  -3.670  17.219 1.00 50.57  ? 366 PHE C CD2    1 
ATOM   8560  C CE1    . PHE C 2 348 ? 43.583  -4.547  15.198 1.00 69.13  ? 366 PHE C CE1    1 
ATOM   8561  C CE2    . PHE C 2 348 ? 43.094  -2.984  16.925 1.00 54.83  ? 366 PHE C CE2    1 
ATOM   8562  C CZ     . PHE C 2 348 ? 43.918  -3.422  15.912 1.00 62.40  ? 366 PHE C CZ     1 
ATOM   8563  N N      . LYS C 2 349 ? 37.092  -6.295  16.292 1.00 69.75  ? 367 LYS C N      1 
ATOM   8564  C CA     . LYS C 2 349 ? 36.084  -7.340  16.175 1.00 70.68  ? 367 LYS C CA     1 
ATOM   8565  C C      . LYS C 2 349 ? 35.630  -7.406  14.739 1.00 71.98  ? 367 LYS C C      1 
ATOM   8566  O O      . LYS C 2 349 ? 35.284  -8.465  14.241 1.00 75.91  ? 367 LYS C O      1 
ATOM   8567  C CB     . LYS C 2 349 ? 34.886  -7.056  17.068 1.00 65.43  ? 367 LYS C CB     1 
ATOM   8568  C CG     . LYS C 2 349 ? 34.248  -8.289  17.683 1.00 69.59  ? 367 LYS C CG     1 
ATOM   8569  C CD     . LYS C 2 349 ? 35.167  -8.940  18.704 1.00 69.73  ? 367 LYS C CD     1 
ATOM   8570  C CE     . LYS C 2 349 ? 35.358  -8.058  19.927 1.00 69.02  ? 367 LYS C CE     1 
ATOM   8571  N NZ     . LYS C 2 349 ? 36.322  -8.640  20.901 1.00 59.45  ? 367 LYS C NZ     1 
ATOM   8572  N N      . ASN C 2 350 ? 35.672  -6.294  14.036 1.00 71.94  ? 368 ASN C N      1 
ATOM   8573  C CA     . ASN C 2 350 ? 35.316  -6.323  12.637 1.00 73.03  ? 368 ASN C CA     1 
ATOM   8574  C C      . ASN C 2 350 ? 36.499  -6.768  11.803 1.00 76.99  ? 368 ASN C C      1 
ATOM   8575  O O      . ASN C 2 350 ? 36.322  -7.297  10.714 1.00 71.88  ? 368 ASN C O      1 
ATOM   8576  C CB     . ASN C 2 350 ? 34.809  -4.964  12.189 1.00 65.82  ? 368 ASN C CB     1 
ATOM   8577  C CG     . ASN C 2 350 ? 33.601  -4.508  12.980 1.00 69.09  ? 368 ASN C CG     1 
ATOM   8578  O OD1    . ASN C 2 350 ? 33.447  -3.324  13.265 1.00 76.01  ? 368 ASN C OD1    1 
ATOM   8579  N ND2    . ASN C 2 350 ? 32.742  -5.451  13.349 1.00 57.74  ? 368 ASN C ND2    1 
ATOM   8580  N N      . LYS C 2 351 ? 37.708  -6.606  12.328 1.00 80.52  ? 369 LYS C N      1 
ATOM   8581  C CA     . LYS C 2 351 ? 38.904  -7.027  11.597 1.00 90.34  ? 369 LYS C CA     1 
ATOM   8582  C C      . LYS C 2 351 ? 38.965  -8.515  11.417 1.00 93.59  ? 369 LYS C C      1 
ATOM   8583  O O      . LYS C 2 351 ? 38.834  -9.021  10.303 1.00 103.58 ? 369 LYS C O      1 
ATOM   8584  C CB     . LYS C 2 351 ? 40.179  -6.604  12.311 1.00 84.25  ? 369 LYS C CB     1 
ATOM   8585  C CG     . LYS C 2 351 ? 41.433  -6.849  11.485 1.00 83.46  ? 369 LYS C CG     1 
ATOM   8586  C CD     . LYS C 2 351 ? 42.692  -6.568  12.281 1.00 83.82  ? 369 LYS C CD     1 
ATOM   8587  C CE     . LYS C 2 351 ? 43.945  -6.815  11.460 1.00 83.76  ? 369 LYS C CE     1 
ATOM   8588  N NZ     . LYS C 2 351 ? 45.179  -6.600  12.268 1.00 83.03  ? 369 LYS C NZ     1 
ATOM   8589  N N      . GLU C 2 352 ? 39.176  -9.225  12.512 1.00 93.46  ? 370 GLU C N      1 
ATOM   8590  C CA     . GLU C 2 352 ? 39.282  -10.671 12.456 1.00 95.53  ? 370 GLU C CA     1 
ATOM   8591  C C      . GLU C 2 352 ? 37.927  -11.331 12.252 1.00 88.13  ? 370 GLU C C      1 
ATOM   8592  O O      . GLU C 2 352 ? 36.884  -10.692 12.377 1.00 89.19  ? 370 GLU C O      1 
ATOM   8593  C CB     . GLU C 2 352 ? 39.917  -11.175 13.747 1.00 97.52  ? 370 GLU C CB     1 
ATOM   8594  C CG     . GLU C 2 352 ? 41.061  -10.302 14.239 1.00 100.88 ? 370 GLU C CG     1 
ATOM   8595  C CD     . GLU C 2 352 ? 41.524  -10.659 15.638 1.00 97.80  ? 370 GLU C CD     1 
ATOM   8596  O OE1    . GLU C 2 352 ? 41.491  -11.853 15.995 1.00 102.68 ? 370 GLU C OE1    1 
ATOM   8597  O OE2    . GLU C 2 352 ? 41.933  -9.741  16.378 1.00 83.77  ? 370 GLU C OE2    1 
ATOM   8598  N N      . LYS D 2 5   ? 49.185  36.375  27.822 1.00 62.04  ? 23  LYS D N      1 
ATOM   8599  C CA     . LYS D 2 5   ? 49.090  37.743  27.342 1.00 73.40  ? 23  LYS D CA     1 
ATOM   8600  C C      . LYS D 2 5   ? 49.447  38.695  28.445 1.00 70.11  ? 23  LYS D C      1 
ATOM   8601  O O      . LYS D 2 5   ? 49.494  39.895  28.248 1.00 66.58  ? 23  LYS D O      1 
ATOM   8602  C CB     . LYS D 2 5   ? 47.695  38.027  26.794 1.00 68.70  ? 23  LYS D CB     1 
ATOM   8603  C CG     . LYS D 2 5   ? 46.546  37.648  27.705 1.00 65.28  ? 23  LYS D CG     1 
ATOM   8604  C CD     . LYS D 2 5   ? 45.239  37.844  26.964 1.00 54.54  ? 23  LYS D CD     1 
ATOM   8605  C CE     . LYS D 2 5   ? 45.335  37.246  25.572 1.00 52.44  ? 23  LYS D CE     1 
ATOM   8606  N NZ     . LYS D 2 5   ? 44.134  37.546  24.748 1.00 73.53  ? 23  LYS D NZ     1 
ATOM   8607  N N      . ILE D 2 6   ? 49.801  38.149  29.588 1.00 70.51  ? 24  ILE D N      1 
ATOM   8608  C CA     . ILE D 2 6   ? 50.169  38.960  30.725 1.00 69.06  ? 24  ILE D CA     1 
ATOM   8609  C C      . ILE D 2 6   ? 51.438  39.730  30.483 1.00 68.21  ? 24  ILE D C      1 
ATOM   8610  O O      . ILE D 2 6   ? 51.570  40.861  30.906 1.00 68.68  ? 24  ILE D O      1 
ATOM   8611  C CB     . ILE D 2 6   ? 50.338  38.059  31.965 1.00 68.16  ? 24  ILE D CB     1 
ATOM   8612  C CG1    . ILE D 2 6   ? 49.036  37.323  32.259 1.00 73.64  ? 24  ILE D CG1    1 
ATOM   8613  C CG2    . ILE D 2 6   ? 50.685  38.864  33.198 1.00 68.18  ? 24  ILE D CG2    1 
ATOM   8614  C CD1    . ILE D 2 6   ? 47.942  38.227  32.783 1.00 71.41  ? 24  ILE D CD1    1 
ATOM   8615  N N      . GLU D 2 7   ? 52.373  39.146  29.766 1.00 68.29  ? 25  GLU D N      1 
ATOM   8616  C CA     . GLU D 2 7   ? 53.655  39.808  29.589 1.00 76.69  ? 25  GLU D CA     1 
ATOM   8617  C C      . GLU D 2 7   ? 53.499  41.184  28.992 1.00 76.81  ? 25  GLU D C      1 
ATOM   8618  O O      . GLU D 2 7   ? 54.272  42.083  29.287 1.00 74.03  ? 25  GLU D O      1 
ATOM   8619  C CB     . GLU D 2 7   ? 54.576  38.969  28.717 1.00 84.29  ? 25  GLU D CB     1 
ATOM   8620  C CG     . GLU D 2 7   ? 56.028  39.418  28.726 1.00 87.42  ? 25  GLU D CG     1 
ATOM   8621  C CD     . GLU D 2 7   ? 56.752  39.089  27.437 1.00 96.46  ? 25  GLU D CD     1 
ATOM   8622  O OE1    . GLU D 2 7   ? 56.072  38.855  26.417 1.00 99.45  ? 25  GLU D OE1    1 
ATOM   8623  O OE2    . GLU D 2 7   ? 58.000  39.078  27.438 1.00 91.68  ? 25  GLU D OE2    1 
ATOM   8624  N N      . LEU D 2 8   ? 52.498  41.357  28.146 1.00 78.14  ? 26  LEU D N      1 
ATOM   8625  C CA     . LEU D 2 8   ? 52.326  42.638  27.476 1.00 77.57  ? 26  LEU D CA     1 
ATOM   8626  C C      . LEU D 2 8   ? 51.221  43.438  28.054 1.00 70.78  ? 26  LEU D C      1 
ATOM   8627  O O      . LEU D 2 8   ? 51.254  44.649  28.042 1.00 71.85  ? 26  LEU D O      1 
ATOM   8628  C CB     . LEU D 2 8   ? 52.015  42.420  26.007 1.00 83.21  ? 26  LEU D CB     1 
ATOM   8629  C CG     . LEU D 2 8   ? 52.980  41.531  25.215 1.00 89.82  ? 26  LEU D CG     1 
ATOM   8630  C CD1    . LEU D 2 8   ? 52.418  40.126  25.040 1.00 76.45  ? 26  LEU D CD1    1 
ATOM   8631  C CD2    . LEU D 2 8   ? 53.279  42.153  23.859 1.00 86.17  ? 26  LEU D CD2    1 
ATOM   8632  N N      . SER D 2 9   ? 50.206  42.756  28.527 1.00 69.47  ? 27  SER D N      1 
ATOM   8633  C CA     . SER D 2 9   ? 49.122  43.464  29.112 1.00 65.73  ? 27  SER D CA     1 
ATOM   8634  C C      . SER D 2 9   ? 49.711  44.253  30.257 1.00 69.72  ? 27  SER D C      1 
ATOM   8635  O O      . SER D 2 9   ? 49.368  45.409  30.451 1.00 75.51  ? 27  SER D O      1 
ATOM   8636  C CB     . SER D 2 9   ? 48.033  42.521  29.567 1.00 60.33  ? 27  SER D CB     1 
ATOM   8637  O OG     . SER D 2 9   ? 48.440  41.770  30.687 1.00 75.55  ? 27  SER D OG     1 
ATOM   8638  N N      . ILE D 2 10  ? 50.674  43.679  30.963 1.00 66.03  ? 28  ILE D N      1 
ATOM   8639  C CA     . ILE D 2 10  ? 51.242  44.372  32.107 1.00 66.78  ? 28  ILE D CA     1 
ATOM   8640  C C      . ILE D 2 10  ? 52.106  45.524  31.658 1.00 65.85  ? 28  ILE D C      1 
ATOM   8641  O O      . ILE D 2 10  ? 52.008  46.612  32.197 1.00 69.73  ? 28  ILE D O      1 
ATOM   8642  C CB     . ILE D 2 10  ? 52.024  43.446  33.044 1.00 67.95  ? 28  ILE D CB     1 
ATOM   8643  C CG1    . ILE D 2 10  ? 51.084  42.423  33.674 1.00 69.94  ? 28  ILE D CG1    1 
ATOM   8644  C CG2    . ILE D 2 10  ? 52.688  44.231  34.160 1.00 56.05  ? 28  ILE D CG2    1 
ATOM   8645  C CD1    . ILE D 2 10  ? 49.952  43.024  34.475 1.00 68.07  ? 28  ILE D CD1    1 
ATOM   8646  N N      . SER D 2 11  ? 52.928  45.316  30.647 1.00 57.10  ? 29  SER D N      1 
ATOM   8647  C CA     . SER D 2 11  ? 53.831  46.358  30.246 1.00 59.13  ? 29  SER D CA     1 
ATOM   8648  C C      . SER D 2 11  ? 53.030  47.515  29.739 1.00 65.34  ? 29  SER D C      1 
ATOM   8649  O O      . SER D 2 11  ? 53.409  48.666  29.909 1.00 59.95  ? 29  SER D O      1 
ATOM   8650  C CB     . SER D 2 11  ? 54.763  45.838  29.190 1.00 51.62  ? 29  SER D CB     1 
ATOM   8651  O OG     . SER D 2 11  ? 54.043  45.370  28.076 1.00 68.66  ? 29  SER D OG     1 
ATOM   8652  N N      . LEU D 2 12  ? 51.901  47.223  29.125 1.00 66.39  ? 30  LEU D N      1 
ATOM   8653  C CA     . LEU D 2 12  ? 51.033  48.279  28.635 1.00 58.46  ? 30  LEU D CA     1 
ATOM   8654  C C      . LEU D 2 12  ? 50.513  49.076  29.789 1.00 63.18  ? 30  LEU D C      1 
ATOM   8655  O O      . LEU D 2 12  ? 50.423  50.293  29.723 1.00 71.18  ? 30  LEU D O      1 
ATOM   8656  C CB     . LEU D 2 12  ? 49.877  47.711  27.827 1.00 46.77  ? 30  LEU D CB     1 
ATOM   8657  C CG     . LEU D 2 12  ? 50.192  47.249  26.410 1.00 48.50  ? 30  LEU D CG     1 
ATOM   8658  C CD1    . LEU D 2 12  ? 49.012  46.504  25.816 1.00 59.40  ? 30  LEU D CD1    1 
ATOM   8659  C CD2    . LEU D 2 12  ? 50.579  48.432  25.543 1.00 49.14  ? 30  LEU D CD2    1 
ATOM   8660  N N      . SER D 2 13  ? 50.157  48.397  30.860 1.00 58.45  ? 31  SER D N      1 
ATOM   8661  C CA     . SER D 2 13  ? 49.694  49.087  32.046 1.00 56.60  ? 31  SER D CA     1 
ATOM   8662  C C      . SER D 2 13  ? 50.775  49.944  32.665 1.00 61.72  ? 31  SER D C      1 
ATOM   8663  O O      . SER D 2 13  ? 50.512  51.032  33.137 1.00 59.90  ? 31  SER D O      1 
ATOM   8664  C CB     . SER D 2 13  ? 49.174  48.079  33.041 1.00 49.84  ? 31  SER D CB     1 
ATOM   8665  O OG     . SER D 2 13  ? 48.154  47.292  32.462 1.00 53.50  ? 31  SER D OG     1 
ATOM   8666  N N      . LEU D 2 14  ? 51.999  49.459  32.662 1.00 59.75  ? 32  LEU D N      1 
ATOM   8667  C CA     . LEU D 2 14  ? 53.096  50.181  33.259 1.00 58.88  ? 32  LEU D CA     1 
ATOM   8668  C C      . LEU D 2 14  ? 53.299  51.451  32.529 1.00 59.03  ? 32  LEU D C      1 
ATOM   8669  O O      . LEU D 2 14  ? 53.749  52.432  33.093 1.00 64.81  ? 32  LEU D O      1 
ATOM   8670  C CB     . LEU D 2 14  ? 54.366  49.359  33.201 1.00 64.49  ? 32  LEU D CB     1 
ATOM   8671  C CG     . LEU D 2 14  ? 54.407  48.107  34.068 1.00 63.55  ? 32  LEU D CG     1 
ATOM   8672  C CD1    . LEU D 2 14  ? 55.669  47.321  33.780 1.00 59.48  ? 32  LEU D CD1    1 
ATOM   8673  C CD2    . LEU D 2 14  ? 54.324  48.480  35.535 1.00 68.23  ? 32  LEU D CD2    1 
ATOM   8674  N N      . ASP D 2 15  ? 52.966  51.446  31.260 1.00 57.29  ? 33  ASP D N      1 
ATOM   8675  C CA     . ASP D 2 15  ? 53.137  52.632  30.461 1.00 57.55  ? 33  ASP D CA     1 
ATOM   8676  C C      . ASP D 2 15  ? 52.323  53.778  31.005 1.00 51.14  ? 33  ASP D C      1 
ATOM   8677  O O      . ASP D 2 15  ? 52.712  54.921  30.835 1.00 50.44  ? 33  ASP D O      1 
ATOM   8678  C CB     . ASP D 2 15  ? 52.749  52.365  29.010 1.00 61.70  ? 33  ASP D CB     1 
ATOM   8679  C CG     . ASP D 2 15  ? 53.941  52.346  28.084 1.00 64.17  ? 33  ASP D CG     1 
ATOM   8680  O OD1    . ASP D 2 15  ? 55.034  52.773  28.505 1.00 67.35  ? 33  ASP D OD1    1 
ATOM   8681  O OD2    . ASP D 2 15  ? 53.788  51.900  26.931 1.00 58.96  ? 33  ASP D OD2    1 
ATOM   8682  N N      . SER D 2 16  ? 51.221  53.507  31.689 1.00 46.19  ? 34  SER D N      1 
ATOM   8683  C CA     . SER D 2 16  ? 50.351  54.591  32.107 1.00 43.69  ? 34  SER D CA     1 
ATOM   8684  C C      . SER D 2 16  ? 51.098  55.636  32.855 1.00 45.82  ? 34  SER D C      1 
ATOM   8685  O O      . SER D 2 16  ? 51.897  55.335  33.725 1.00 52.30  ? 34  SER D O      1 
ATOM   8686  C CB     . SER D 2 16  ? 49.262  54.080  33.015 1.00 44.68  ? 34  SER D CB     1 
ATOM   8687  O OG     . SER D 2 16  ? 48.449  55.139  33.474 1.00 45.28  ? 34  SER D OG     1 
ATOM   8688  N N      . PRO D 2 17  ? 50.850  56.889  32.513 1.00 41.41  ? 35  PRO D N      1 
ATOM   8689  C CA     . PRO D 2 17  ? 51.560  57.985  33.147 1.00 41.58  ? 35  PRO D CA     1 
ATOM   8690  C C      . PRO D 2 17  ? 51.208  58.162  34.592 1.00 42.86  ? 35  PRO D C      1 
ATOM   8691  O O      . PRO D 2 17  ? 52.088  58.406  35.400 1.00 37.52  ? 35  PRO D O      1 
ATOM   8692  C CB     . PRO D 2 17  ? 51.063  59.195  32.368 1.00 42.75  ? 35  PRO D CB     1 
ATOM   8693  C CG     . PRO D 2 17  ? 49.812  58.775  31.685 1.00 44.36  ? 35  PRO D CG     1 
ATOM   8694  C CD     . PRO D 2 17  ? 50.035  57.336  31.374 1.00 48.05  ? 35  PRO D CD     1 
ATOM   8695  N N      . LYS D 2 18  ? 49.940  58.050  34.920 1.00 45.17  ? 36  LYS D N      1 
ATOM   8696  C CA     . LYS D 2 18  ? 49.492  58.285  36.275 1.00 46.70  ? 36  LYS D CA     1 
ATOM   8697  C C      . LYS D 2 18  ? 49.521  57.064  37.166 1.00 53.94  ? 36  LYS D C      1 
ATOM   8698  O O      . LYS D 2 18  ? 48.622  56.845  37.962 1.00 60.14  ? 36  LYS D O      1 
ATOM   8699  C CB     . LYS D 2 18  ? 48.098  58.889  36.236 1.00 53.80  ? 36  LYS D CB     1 
ATOM   8700  C CG     . LYS D 2 18  ? 47.223  58.374  35.111 1.00 53.32  ? 36  LYS D CG     1 
ATOM   8701  C CD     . LYS D 2 18  ? 46.194  59.418  34.710 1.00 72.26  ? 36  LYS D CD     1 
ATOM   8702  C CE     . LYS D 2 18  ? 45.401  59.907  35.910 1.00 76.44  ? 36  LYS D CE     1 
ATOM   8703  N NZ     . LYS D 2 18  ? 44.395  60.938  35.535 1.00 61.67  ? 36  LYS D NZ     1 
ATOM   8704  N N      . LEU D 2 19  ? 50.598  56.309  37.110 1.00 48.19  ? 37  LEU D N      1 
ATOM   8705  C CA     . LEU D 2 19  ? 50.710  55.135  37.932 1.00 47.72  ? 37  LEU D CA     1 
ATOM   8706  C C      . LEU D 2 19  ? 51.071  55.491  39.354 1.00 50.33  ? 37  LEU D C      1 
ATOM   8707  O O      . LEU D 2 19  ? 52.091  56.112  39.585 1.00 51.59  ? 37  LEU D O      1 
ATOM   8708  C CB     . LEU D 2 19  ? 51.744  54.196  37.330 1.00 45.06  ? 37  LEU D CB     1 
ATOM   8709  C CG     . LEU D 2 19  ? 51.594  52.695  37.566 1.00 55.03  ? 37  LEU D CG     1 
ATOM   8710  C CD1    . LEU D 2 19  ? 50.376  52.177  36.827 1.00 53.47  ? 37  LEU D CD1    1 
ATOM   8711  C CD2    . LEU D 2 19  ? 52.836  51.968  37.084 1.00 51.16  ? 37  LEU D CD2    1 
ATOM   8712  N N      . ASP D 2 20  ? 50.256  55.097  40.322 1.00 52.47  ? 38  ASP D N      1 
ATOM   8713  C CA     . ASP D 2 20  ? 50.541  55.351  41.725 1.00 53.72  ? 38  ASP D CA     1 
ATOM   8714  C C      . ASP D 2 20  ? 51.365  54.233  42.237 1.00 53.14  ? 38  ASP D C      1 
ATOM   8715  O O      . ASP D 2 20  ? 51.579  53.264  41.543 1.00 53.26  ? 38  ASP D O      1 
ATOM   8716  C CB     . ASP D 2 20  ? 49.263  55.340  42.557 1.00 54.07  ? 38  ASP D CB     1 
ATOM   8717  C CG     . ASP D 2 20  ? 48.293  56.420  42.171 1.00 71.82  ? 38  ASP D CG     1 
ATOM   8718  O OD1    . ASP D 2 20  ? 48.723  57.461  41.639 1.00 79.31  ? 38  ASP D OD1    1 
ATOM   8719  O OD2    . ASP D 2 20  ? 47.087  56.228  42.422 1.00 70.08  ? 38  ASP D OD2    1 
ATOM   8720  N N      . GLU D 2 21  ? 51.808  54.334  43.475 1.00 53.72  ? 39  GLU D N      1 
ATOM   8721  C CA     . GLU D 2 21  ? 52.609  53.290  44.069 1.00 51.16  ? 39  GLU D CA     1 
ATOM   8722  C C      . GLU D 2 21  ? 51.718  52.157  44.393 1.00 42.30  ? 39  GLU D C      1 
ATOM   8723  O O      . GLU D 2 21  ? 52.127  51.016  44.370 1.00 42.56  ? 39  GLU D O      1 
ATOM   8724  C CB     . GLU D 2 21  ? 53.263  53.784  45.343 1.00 55.11  ? 39  GLU D CB     1 
ATOM   8725  C CG     . GLU D 2 21  ? 54.476  54.661  45.118 1.00 60.26  ? 39  GLU D CG     1 
ATOM   8726  C CD     . GLU D 2 21  ? 55.210  54.971  46.400 1.00 63.59  ? 39  GLU D CD     1 
ATOM   8727  O OE1    . GLU D 2 21  ? 54.552  55.038  47.453 1.00 72.98  ? 39  GLU D OE1    1 
ATOM   8728  O OE2    . GLU D 2 21  ? 56.443  55.153  46.353 1.00 59.95  ? 39  GLU D OE2    1 
ATOM   8729  N N      . SER D 2 22  ? 50.472  52.458  44.670 1.00 43.96  ? 40  SER D N      1 
ATOM   8730  C CA     . SER D 2 22  ? 49.551  51.423  45.035 1.00 44.03  ? 40  SER D CA     1 
ATOM   8731  C C      . SER D 2 22  ? 49.401  50.508  43.867 1.00 46.51  ? 40  SER D C      1 
ATOM   8732  O O      . SER D 2 22  ? 49.311  49.312  44.025 1.00 53.63  ? 40  SER D O      1 
ATOM   8733  C CB     . SER D 2 22  ? 48.216  52.020  45.410 1.00 40.47  ? 40  SER D CB     1 
ATOM   8734  O OG     . SER D 2 22  ? 48.367  52.990  46.426 1.00 41.98  ? 40  SER D OG     1 
ATOM   8735  N N      . ASP D 2 23  ? 49.447  51.047  42.673 1.00 50.85  ? 41  ASP D N      1 
ATOM   8736  C CA     . ASP D 2 23  ? 49.209  50.256  41.482 1.00 46.28  ? 41  ASP D CA     1 
ATOM   8737  C C      . ASP D 2 23  ? 50.298  49.278  41.116 1.00 45.65  ? 41  ASP D C      1 
ATOM   8738  O O      . ASP D 2 23  ? 50.015  48.145  40.786 1.00 44.53  ? 41  ASP D O      1 
ATOM   8739  C CB     . ASP D 2 23  ? 48.993  51.215  40.322 1.00 46.39  ? 41  ASP D CB     1 
ATOM   8740  C CG     . ASP D 2 23  ? 47.855  52.179  40.561 1.00 56.10  ? 41  ASP D CG     1 
ATOM   8741  O OD1    . ASP D 2 23  ? 47.094  51.989  41.526 1.00 58.69  ? 41  ASP D OD1    1 
ATOM   8742  O OD2    . ASP D 2 23  ? 47.709  53.128  39.771 1.00 64.93  ? 41  ASP D OD2    1 
ATOM   8743  N N      . PHE D 2 24  ? 51.537  49.728  41.092 1.00 42.06  ? 42  PHE D N      1 
ATOM   8744  C CA     . PHE D 2 24  ? 52.653  48.880  40.752 1.00 38.41  ? 42  PHE D CA     1 
ATOM   8745  C C      . PHE D 2 24  ? 52.537  47.687  41.620 1.00 47.72  ? 42  PHE D C      1 
ATOM   8746  O O      . PHE D 2 24  ? 52.648  46.573  41.157 1.00 53.99  ? 42  PHE D O      1 
ATOM   8747  C CB     . PHE D 2 24  ? 53.906  49.649  41.085 1.00 38.25  ? 42  PHE D CB     1 
ATOM   8748  C CG     . PHE D 2 24  ? 55.188  48.893  40.946 1.00 41.96  ? 42  PHE D CG     1 
ATOM   8749  C CD1    . PHE D 2 24  ? 55.664  48.108  41.977 1.00 49.65  ? 42  PHE D CD1    1 
ATOM   8750  C CD2    . PHE D 2 24  ? 55.967  49.056  39.827 1.00 47.98  ? 42  PHE D CD2    1 
ATOM   8751  C CE1    . PHE D 2 24  ? 56.860  47.441  41.863 1.00 55.61  ? 42  PHE D CE1    1 
ATOM   8752  C CE2    . PHE D 2 24  ? 57.168  48.401  39.711 1.00 53.64  ? 42  PHE D CE2    1 
ATOM   8753  C CZ     . PHE D 2 24  ? 57.613  47.589  40.726 1.00 57.44  ? 42  PHE D CZ     1 
ATOM   8754  N N      . ILE D 2 25  ? 52.345  47.903  42.903 1.00 45.53  ? 43  ILE D N      1 
ATOM   8755  C CA     . ILE D 2 25  ? 52.228  46.802  43.835 1.00 44.32  ? 43  ILE D CA     1 
ATOM   8756  C C      . ILE D 2 25  ? 51.151  45.868  43.381 1.00 43.37  ? 43  ILE D C      1 
ATOM   8757  O O      . ILE D 2 25  ? 51.397  44.700  43.220 1.00 46.87  ? 43  ILE D O      1 
ATOM   8758  C CB     . ILE D 2 25  ? 51.920  47.300  45.238 1.00 38.82  ? 43  ILE D CB     1 
ATOM   8759  C CG1    . ILE D 2 25  ? 53.083  48.141  45.743 1.00 35.08  ? 43  ILE D CG1    1 
ATOM   8760  C CG2    . ILE D 2 25  ? 51.668  46.138  46.178 1.00 45.38  ? 43  ILE D CG2    1 
ATOM   8761  C CD1    . ILE D 2 25  ? 52.899  48.610  47.160 1.00 35.16  ? 43  ILE D CD1    1 
ATOM   8762  N N      . LEU D 2 26  ? 49.963  46.383  43.126 1.00 40.46  ? 44  LEU D N      1 
ATOM   8763  C CA     . LEU D 2 26  ? 48.851  45.549  42.703 1.00 42.60  ? 44  LEU D CA     1 
ATOM   8764  C C      . LEU D 2 26  ? 49.090  44.859  41.373 1.00 47.30  ? 44  LEU D C      1 
ATOM   8765  O O      . LEU D 2 26  ? 48.874  43.666  41.235 1.00 46.35  ? 44  LEU D O      1 
ATOM   8766  C CB     . LEU D 2 26  ? 47.588  46.377  42.630 1.00 35.99  ? 44  LEU D CB     1 
ATOM   8767  C CG     . LEU D 2 26  ? 46.808  46.665  43.896 1.00 36.27  ? 44  LEU D CG     1 
ATOM   8768  C CD1    . LEU D 2 26  ? 45.823  47.767  43.586 1.00 47.99  ? 44  LEU D CD1    1 
ATOM   8769  C CD2    . LEU D 2 26  ? 46.073  45.416  44.324 1.00 40.65  ? 44  LEU D CD2    1 
ATOM   8770  N N      . LEU D 2 27  ? 49.546  45.596  40.390 1.00 44.97  ? 45  LEU D N      1 
ATOM   8771  C CA     . LEU D 2 27  ? 49.832  45.008  39.102 1.00 52.70  ? 45  LEU D CA     1 
ATOM   8772  C C      . LEU D 2 27  ? 50.973  44.013  39.142 1.00 51.16  ? 45  LEU D C      1 
ATOM   8773  O O      . LEU D 2 27  ? 50.905  42.981  38.504 1.00 51.97  ? 45  LEU D O      1 
ATOM   8774  C CB     . LEU D 2 27  ? 50.178  46.102  38.100 1.00 48.20  ? 45  LEU D CB     1 
ATOM   8775  C CG     . LEU D 2 27  ? 49.097  46.938  37.436 1.00 38.10  ? 45  LEU D CG     1 
ATOM   8776  C CD1    . LEU D 2 27  ? 49.759  48.097  36.714 1.00 41.32  ? 45  LEU D CD1    1 
ATOM   8777  C CD2    . LEU D 2 27  ? 48.311  46.081  36.461 1.00 55.37  ? 45  LEU D CD2    1 
ATOM   8778  N N      . SER D 2 28  ? 52.055  44.342  39.828 1.00 42.97  ? 46  SER D N      1 
ATOM   8779  C CA     . SER D 2 28  ? 53.211  43.476  39.821 1.00 45.40  ? 46  SER D CA     1 
ATOM   8780  C C      . SER D 2 28  ? 52.899  42.155  40.369 1.00 48.47  ? 46  SER D C      1 
ATOM   8781  O O      . SER D 2 28  ? 53.220  41.145  39.779 1.00 47.70  ? 46  SER D O      1 
ATOM   8782  C CB     . SER D 2 28  ? 54.278  44.012  40.707 1.00 47.91  ? 46  SER D CB     1 
ATOM   8783  O OG     . SER D 2 28  ? 55.330  43.078  40.779 1.00 62.05  ? 46  SER D OG     1 
ATOM   8784  N N      . VAL D 2 29  ? 52.309  42.145  41.545 1.00 45.94  ? 47  VAL D N      1 
ATOM   8785  C CA     . VAL D 2 29  ? 52.051  40.896  42.172 1.00 43.38  ? 47  VAL D CA     1 
ATOM   8786  C C      . VAL D 2 29  ? 51.179  40.097  41.263 1.00 48.85  ? 47  VAL D C      1 
ATOM   8787  O O      . VAL D 2 29  ? 51.251  38.898  41.276 1.00 55.08  ? 47  VAL D O      1 
ATOM   8788  C CB     . VAL D 2 29  ? 51.462  41.041  43.558 1.00 41.26  ? 47  VAL D CB     1 
ATOM   8789  C CG1    . VAL D 2 29  ? 52.470  41.670  44.496 1.00 47.10  ? 47  VAL D CG1    1 
ATOM   8790  C CG2    . VAL D 2 29  ? 50.183  41.829  43.523 1.00 43.86  ? 47  VAL D CG2    1 
ATOM   8791  N N      . LYS D 2 30  ? 50.396  40.746  40.421 1.00 49.70  ? 48  LYS D N      1 
ATOM   8792  C CA     . LYS D 2 30  ? 49.568  40.013  39.457 1.00 57.96  ? 48  LYS D CA     1 
ATOM   8793  C C      . LYS D 2 30  ? 50.402  39.321  38.413 1.00 54.57  ? 48  LYS D C      1 
ATOM   8794  O O      . LYS D 2 30  ? 50.169  38.175  38.084 1.00 57.27  ? 48  LYS D O      1 
ATOM   8795  C CB     . LYS D 2 30  ? 48.535  40.903  38.775 1.00 54.80  ? 48  LYS D CB     1 
ATOM   8796  C CG     . LYS D 2 30  ? 47.544  40.148  37.909 1.00 51.92  ? 48  LYS D CG     1 
ATOM   8797  C CD     . LYS D 2 30  ? 46.529  41.079  37.269 1.00 56.89  ? 48  LYS D CD     1 
ATOM   8798  C CE     . LYS D 2 30  ? 45.549  40.297  36.412 1.00 56.20  ? 48  LYS D CE     1 
ATOM   8799  N NZ     . LYS D 2 30  ? 44.530  41.170  35.774 1.00 54.00  ? 48  LYS D NZ     1 
ATOM   8800  N N      . TYR D 2 31  ? 51.382  40.020  37.887 1.00 50.88  ? 49  TYR D N      1 
ATOM   8801  C CA     . TYR D 2 31  ? 52.215  39.405  36.909 1.00 55.09  ? 49  TYR D CA     1 
ATOM   8802  C C      . TYR D 2 31  ? 52.872  38.292  37.621 1.00 58.74  ? 49  TYR D C      1 
ATOM   8803  O O      . TYR D 2 31  ? 52.908  37.181  37.135 1.00 63.82  ? 49  TYR D O      1 
ATOM   8804  C CB     . TYR D 2 31  ? 53.262  40.383  36.415 1.00 54.07  ? 49  TYR D CB     1 
ATOM   8805  C CG     . TYR D 2 31  ? 54.366  39.786  35.605 1.00 51.89  ? 49  TYR D CG     1 
ATOM   8806  C CD1    . TYR D 2 31  ? 54.118  39.246  34.362 1.00 54.04  ? 49  TYR D CD1    1 
ATOM   8807  C CD2    . TYR D 2 31  ? 55.666  39.786  36.073 1.00 51.49  ? 49  TYR D CD2    1 
ATOM   8808  C CE1    . TYR D 2 31  ? 55.130  38.699  33.614 1.00 63.95  ? 49  TYR D CE1    1 
ATOM   8809  C CE2    . TYR D 2 31  ? 56.685  39.242  35.332 1.00 54.97  ? 49  TYR D CE2    1 
ATOM   8810  C CZ     . TYR D 2 31  ? 56.404  38.703  34.105 1.00 63.60  ? 49  TYR D CZ     1 
ATOM   8811  O OH     . TYR D 2 31  ? 57.406  38.159  33.365 1.00 71.91  ? 49  TYR D OH     1 
ATOM   8812  N N      . LEU D 2 32  ? 53.337  38.552  38.819 1.00 52.05  ? 50  LEU D N      1 
ATOM   8813  C CA     . LEU D 2 32  ? 54.083  37.534  39.493 1.00 53.07  ? 50  LEU D CA     1 
ATOM   8814  C C      . LEU D 2 32  ? 53.186  36.383  39.872 1.00 59.29  ? 50  LEU D C      1 
ATOM   8815  O O      . LEU D 2 32  ? 53.576  35.244  39.761 1.00 65.75  ? 50  LEU D O      1 
ATOM   8816  C CB     . LEU D 2 32  ? 54.794  38.117  40.691 1.00 55.32  ? 50  LEU D CB     1 
ATOM   8817  C CG     . LEU D 2 32  ? 55.939  39.060  40.388 1.00 48.12  ? 50  LEU D CG     1 
ATOM   8818  C CD1    . LEU D 2 32  ? 56.406  39.691  41.686 1.00 51.69  ? 50  LEU D CD1    1 
ATOM   8819  C CD2    . LEU D 2 32  ? 57.033  38.238  39.743 1.00 53.67  ? 50  LEU D CD2    1 
ATOM   8820  N N      . GLU D 2 33  ? 51.977  36.663  40.301 1.00 57.50  ? 51  GLU D N      1 
ATOM   8821  C CA     . GLU D 2 33  ? 51.056  35.595  40.615 1.00 63.42  ? 51  GLU D CA     1 
ATOM   8822  C C      . GLU D 2 33  ? 50.781  34.753  39.395 1.00 73.47  ? 51  GLU D C      1 
ATOM   8823  O O      . GLU D 2 33  ? 51.008  33.558  39.417 1.00 84.31  ? 51  GLU D O      1 
ATOM   8824  C CB     . GLU D 2 33  ? 49.742  36.129  41.176 1.00 58.83  ? 51  GLU D CB     1 
ATOM   8825  C CG     . GLU D 2 33  ? 49.761  36.445  42.657 1.00 66.27  ? 51  GLU D CG     1 
ATOM   8826  C CD     . GLU D 2 33  ? 48.488  37.121  43.109 1.00 82.48  ? 51  GLU D CD     1 
ATOM   8827  O OE1    . GLU D 2 33  ? 47.552  37.218  42.290 1.00 78.79  ? 51  GLU D OE1    1 
ATOM   8828  O OE2    . GLU D 2 33  ? 48.423  37.554  44.280 1.00 83.96  ? 51  GLU D OE2    1 
ATOM   8829  N N      . LYS D 2 34  ? 50.344  35.367  38.309 1.00 60.79  ? 52  LYS D N      1 
ATOM   8830  C CA     . LYS D 2 34  ? 50.006  34.609  37.123 1.00 62.77  ? 52  LYS D CA     1 
ATOM   8831  C C      . LYS D 2 34  ? 51.201  33.877  36.563 1.00 66.30  ? 52  LYS D C      1 
ATOM   8832  O O      . LYS D 2 34  ? 51.176  32.661  36.446 1.00 64.76  ? 52  LYS D O      1 
ATOM   8833  C CB     . LYS D 2 34  ? 49.402  35.514  36.061 1.00 67.11  ? 52  LYS D CB     1 
ATOM   8834  C CG     . LYS D 2 34  ? 48.099  36.176  36.467 1.00 72.83  ? 52  LYS D CG     1 
ATOM   8835  C CD     . LYS D 2 34  ? 46.975  35.164  36.585 1.00 73.99  ? 52  LYS D CD     1 
ATOM   8836  C CE     . LYS D 2 34  ? 46.644  34.546  35.239 1.00 65.97  ? 52  LYS D CE     1 
ATOM   8837  N NZ     . LYS D 2 34  ? 45.593  33.502  35.374 1.00 77.14  ? 52  LYS D NZ     1 
ATOM   8838  N N      . SER D 2 35  ? 52.254  34.599  36.212 1.00 63.55  ? 53  SER D N      1 
ATOM   8839  C CA     . SER D 2 35  ? 53.382  33.946  35.574 1.00 68.05  ? 53  SER D CA     1 
ATOM   8840  C C      . SER D 2 35  ? 54.089  32.912  36.422 1.00 71.00  ? 53  SER D C      1 
ATOM   8841  O O      . SER D 2 35  ? 54.392  31.829  35.937 1.00 70.93  ? 53  SER D O      1 
ATOM   8842  C CB     . SER D 2 35  ? 54.396  34.973  35.101 1.00 58.63  ? 53  SER D CB     1 
ATOM   8843  O OG     . SER D 2 35  ? 54.875  35.741  36.180 1.00 72.01  ? 53  SER D OG     1 
ATOM   8844  N N      . LEU D 2 36  ? 54.358  33.217  37.680 1.00 67.40  ? 54  LEU D N      1 
ATOM   8845  C CA     . LEU D 2 36  ? 55.094  32.281  38.499 1.00 70.13  ? 54  LEU D CA     1 
ATOM   8846  C C      . LEU D 2 36  ? 54.252  31.085  38.674 1.00 78.56  ? 54  LEU D C      1 
ATOM   8847  O O      . LEU D 2 36  ? 54.720  29.959  38.677 1.00 84.43  ? 54  LEU D O      1 
ATOM   8848  C CB     . LEU D 2 36  ? 55.473  32.864  39.833 1.00 65.49  ? 54  LEU D CB     1 
ATOM   8849  C CG     . LEU D 2 36  ? 56.761  33.642  39.669 1.00 68.06  ? 54  LEU D CG     1 
ATOM   8850  C CD1    . LEU D 2 36  ? 57.035  34.422  40.922 1.00 62.57  ? 54  LEU D CD1    1 
ATOM   8851  C CD2    . LEU D 2 36  ? 57.903  32.696  39.361 1.00 66.69  ? 54  LEU D CD2    1 
ATOM   8852  N N      . GLY D 2 37  ? 52.979  31.330  38.832 1.00 78.72  ? 55  GLY D N      1 
ATOM   8853  C CA     . GLY D 2 37  ? 52.080  30.237  39.014 1.00 78.23  ? 55  GLY D CA     1 
ATOM   8854  C C      . GLY D 2 37  ? 51.937  30.050  40.485 1.00 82.86  ? 55  GLY D C      1 
ATOM   8855  O O      . GLY D 2 37  ? 52.677  30.620  41.277 1.00 82.23  ? 55  GLY D O      1 
ATOM   8856  N N      . LYS D 2 38  ? 50.964  29.251  40.858 1.00 84.36  ? 56  LYS D N      1 
ATOM   8857  C CA     . LYS D 2 38  ? 50.773  28.982  42.261 1.00 86.77  ? 56  LYS D CA     1 
ATOM   8858  C C      . LYS D 2 38  ? 51.643  27.832  42.684 1.00 90.04  ? 56  LYS D C      1 
ATOM   8859  O O      . LYS D 2 38  ? 51.225  26.680  42.631 1.00 93.84  ? 56  LYS D O      1 
ATOM   8860  C CB     . LYS D 2 38  ? 49.313  28.677  42.572 1.00 87.78  ? 56  LYS D CB     1 
ATOM   8861  C CG     . LYS D 2 38  ? 48.964  28.737  44.049 1.00 86.25  ? 56  LYS D CG     1 
ATOM   8862  C CD     . LYS D 2 38  ? 47.568  28.194  44.294 1.00 85.01  ? 56  LYS D CD     1 
ATOM   8863  C CE     . LYS D 2 38  ? 46.534  28.921  43.451 1.00 79.20  ? 56  LYS D CE     1 
ATOM   8864  N NZ     . LYS D 2 38  ? 45.181  28.316  43.594 1.00 66.68  ? 56  LYS D NZ     1 
ATOM   8865  N N      . LYS D 2 39  ? 52.870  28.130  43.061 1.00 87.08  ? 57  LYS D N      1 
ATOM   8866  C CA     . LYS D 2 39  ? 53.709  27.098  43.601 1.00 75.35  ? 57  LYS D CA     1 
ATOM   8867  C C      . LYS D 2 39  ? 53.899  27.676  44.964 1.00 73.75  ? 57  LYS D C      1 
ATOM   8868  O O      . LYS D 2 39  ? 54.054  28.880  45.100 1.00 80.26  ? 57  LYS D O      1 
ATOM   8869  C CB     . LYS D 2 39  ? 55.009  26.989  42.830 1.00 72.18  ? 57  LYS D CB     1 
ATOM   8870  C CG     . LYS D 2 39  ? 55.506  28.278  42.213 1.00 82.84  ? 57  LYS D CG     1 
ATOM   8871  C CD     . LYS D 2 39  ? 56.676  27.983  41.294 1.00 86.36  ? 57  LYS D CD     1 
ATOM   8872  C CE     . LYS D 2 39  ? 56.313  26.906  40.286 1.00 71.81  ? 57  LYS D CE     1 
ATOM   8873  N NZ     . LYS D 2 39  ? 57.418  26.659  39.320 1.00 65.57  ? 57  LYS D NZ     1 
ATOM   8874  N N      . LYS D 2 40  ? 53.758  26.859  45.995 1.00 64.10  ? 58  LYS D N      1 
ATOM   8875  C CA     . LYS D 2 40  ? 53.812  27.394  47.340 1.00 63.15  ? 58  LYS D CA     1 
ATOM   8876  C C      . LYS D 2 40  ? 55.223  27.677  47.673 1.00 62.97  ? 58  LYS D C      1 
ATOM   8877  O O      . LYS D 2 40  ? 55.558  27.939  48.816 1.00 68.09  ? 58  LYS D O      1 
ATOM   8878  C CB     . LYS D 2 40  ? 53.195  26.446  48.345 1.00 59.17  ? 58  LYS D CB     1 
ATOM   8879  C CG     . LYS D 2 40  ? 51.709  26.211  48.147 1.00 61.24  ? 58  LYS D CG     1 
ATOM   8880  C CD     . LYS D 2 40  ? 50.907  27.432  48.551 1.00 65.13  ? 58  LYS D CD     1 
ATOM   8881  C CE     . LYS D 2 40  ? 49.415  27.151  48.542 1.00 70.49  ? 58  LYS D CE     1 
ATOM   8882  N NZ     . LYS D 2 40  ? 48.644  28.267  49.153 1.00 58.60  ? 58  LYS D NZ     1 
ATOM   8883  N N      . GLU D 2 41  ? 56.077  27.655  46.673 1.00 63.79  ? 59  GLU D N      1 
ATOM   8884  C CA     . GLU D 2 41  ? 57.447  28.021  46.918 1.00 67.47  ? 59  GLU D CA     1 
ATOM   8885  C C      . GLU D 2 41  ? 57.479  29.493  47.222 1.00 68.99  ? 59  GLU D C      1 
ATOM   8886  O O      . GLU D 2 41  ? 58.322  29.956  47.979 1.00 67.16  ? 59  GLU D O      1 
ATOM   8887  C CB     . GLU D 2 41  ? 58.286  27.742  45.688 1.00 70.17  ? 59  GLU D CB     1 
ATOM   8888  C CG     . GLU D 2 41  ? 58.130  26.344  45.126 1.00 80.07  ? 59  GLU D CG     1 
ATOM   8889  C CD     . GLU D 2 41  ? 59.006  26.108  43.914 1.00 87.99  ? 59  GLU D CD     1 
ATOM   8890  O OE1    . GLU D 2 41  ? 59.742  27.036  43.520 1.00 86.22  ? 59  GLU D OE1    1 
ATOM   8891  O OE2    . GLU D 2 41  ? 58.961  24.995  43.353 1.00 91.64  ? 59  GLU D OE2    1 
ATOM   8892  N N      . PHE D 2 42  ? 56.523  30.242  46.693 1.00 70.62  ? 60  PHE D N      1 
ATOM   8893  C CA     . PHE D 2 42  ? 56.562  31.688  46.842 1.00 60.98  ? 60  PHE D CA     1 
ATOM   8894  C C      . PHE D 2 42  ? 55.355  32.288  47.488 1.00 58.53  ? 60  PHE D C      1 
ATOM   8895  O O      . PHE D 2 42  ? 55.150  33.479  47.406 1.00 56.53  ? 60  PHE D O      1 
ATOM   8896  C CB     . PHE D 2 42  ? 56.646  32.311  45.474 1.00 66.79  ? 60  PHE D CB     1 
ATOM   8897  C CG     . PHE D 2 42  ? 57.784  31.821  44.632 1.00 69.16  ? 60  PHE D CG     1 
ATOM   8898  C CD1    . PHE D 2 42  ? 59.073  31.800  45.121 1.00 70.41  ? 60  PHE D CD1    1 
ATOM   8899  C CD2    . PHE D 2 42  ? 57.563  31.429  43.328 1.00 69.13  ? 60  PHE D CD2    1 
ATOM   8900  C CE1    . PHE D 2 42  ? 60.116  31.362  44.334 1.00 75.05  ? 60  PHE D CE1    1 
ATOM   8901  C CE2    . PHE D 2 42  ? 58.600  30.998  42.535 1.00 74.68  ? 60  PHE D CE2    1 
ATOM   8902  C CZ     . PHE D 2 42  ? 59.880  30.964  43.038 1.00 76.90  ? 60  PHE D CZ     1 
ATOM   8903  N N      . SER D 2 43  ? 54.529  31.473  48.109 1.00 63.04  ? 61  SER D N      1 
ATOM   8904  C CA     . SER D 2 43  ? 53.293  31.977  48.677 1.00 68.57  ? 61  SER D CA     1 
ATOM   8905  C C      . SER D 2 43  ? 53.536  32.820  49.887 1.00 72.65  ? 61  SER D C      1 
ATOM   8906  O O      . SER D 2 43  ? 52.680  33.580  50.291 1.00 77.22  ? 61  SER D O      1 
ATOM   8907  C CB     . SER D 2 43  ? 52.379  30.833  49.058 1.00 68.71  ? 61  SER D CB     1 
ATOM   8908  O OG     . SER D 2 43  ? 51.128  31.317  49.503 1.00 75.99  ? 61  SER D OG     1 
ATOM   8909  N N      . GLY D 2 44  ? 54.700  32.704  50.492 1.00 67.47  ? 62  GLY D N      1 
ATOM   8910  C CA     . GLY D 2 44  ? 54.994  33.582  51.601 1.00 71.54  ? 62  GLY D CA     1 
ATOM   8911  C C      . GLY D 2 44  ? 55.005  35.011  51.119 1.00 73.07  ? 62  GLY D C      1 
ATOM   8912  O O      . GLY D 2 44  ? 54.541  35.907  51.813 1.00 62.84  ? 62  GLY D O      1 
ATOM   8913  N N      . PHE D 2 45  ? 55.496  35.227  49.908 1.00 78.57  ? 63  PHE D N      1 
ATOM   8914  C CA     . PHE D 2 45  ? 55.633  36.564  49.358 1.00 66.36  ? 63  PHE D CA     1 
ATOM   8915  C C      . PHE D 2 45  ? 54.346  37.284  49.226 1.00 62.61  ? 63  PHE D C      1 
ATOM   8916  O O      . PHE D 2 45  ? 54.159  38.332  49.807 1.00 69.43  ? 63  PHE D O      1 
ATOM   8917  C CB     . PHE D 2 45  ? 56.240  36.428  47.974 1.00 60.57  ? 63  PHE D CB     1 
ATOM   8918  C CG     . PHE D 2 45  ? 56.579  37.718  47.316 1.00 61.10  ? 63  PHE D CG     1 
ATOM   8919  C CD1    . PHE D 2 45  ? 57.575  38.522  47.821 1.00 69.85  ? 63  PHE D CD1    1 
ATOM   8920  C CD2    . PHE D 2 45  ? 55.933  38.100  46.160 1.00 67.04  ? 63  PHE D CD2    1 
ATOM   8921  C CE1    . PHE D 2 45  ? 57.897  39.706  47.203 1.00 70.20  ? 63  PHE D CE1    1 
ATOM   8922  C CE2    . PHE D 2 45  ? 56.247  39.281  45.533 1.00 71.26  ? 63  PHE D CE2    1 
ATOM   8923  C CZ     . PHE D 2 45  ? 57.231  40.083  46.056 1.00 72.46  ? 63  PHE D CZ     1 
ATOM   8924  N N      . PHE D 2 46  ? 53.448  36.742  48.441 1.00 59.32  ? 64  PHE D N      1 
ATOM   8925  C CA     . PHE D 2 46  ? 52.220  37.447  48.177 1.00 64.98  ? 64  PHE D CA     1 
ATOM   8926  C C      . PHE D 2 46  ? 51.472  37.745  49.438 1.00 61.04  ? 64  PHE D C      1 
ATOM   8927  O O      . PHE D 2 46  ? 50.801  38.747  49.531 1.00 61.43  ? 64  PHE D O      1 
ATOM   8928  C CB     . PHE D 2 46  ? 51.379  36.655  47.189 1.00 72.77  ? 64  PHE D CB     1 
ATOM   8929  C CG     . PHE D 2 46  ? 52.130  36.269  45.946 1.00 67.66  ? 64  PHE D CG     1 
ATOM   8930  C CD1    . PHE D 2 46  ? 52.632  37.240  45.098 1.00 59.10  ? 64  PHE D CD1    1 
ATOM   8931  C CD2    . PHE D 2 46  ? 52.352  34.942  45.635 1.00 66.12  ? 64  PHE D CD2    1 
ATOM   8932  C CE1    . PHE D 2 46  ? 53.336  36.897  43.965 1.00 54.42  ? 64  PHE D CE1    1 
ATOM   8933  C CE2    . PHE D 2 46  ? 53.054  34.593  44.500 1.00 65.44  ? 64  PHE D CE2    1 
ATOM   8934  C CZ     . PHE D 2 46  ? 53.547  35.571  43.665 1.00 63.06  ? 64  PHE D CZ     1 
ATOM   8935  N N      . GLU D 2 47  ? 51.662  36.950  50.459 1.00 63.77  ? 65  GLU D N      1 
ATOM   8936  C CA     . GLU D 2 47  ? 50.925  37.182  51.670 1.00 67.40  ? 65  GLU D CA     1 
ATOM   8937  C C      . GLU D 2 47  ? 51.454  38.368  52.446 1.00 66.53  ? 65  GLU D C      1 
ATOM   8938  O O      . GLU D 2 47  ? 50.682  39.095  53.034 1.00 61.86  ? 65  GLU D O      1 
ATOM   8939  C CB     . GLU D 2 47  ? 50.893  35.934  52.529 1.00 75.13  ? 65  GLU D CB     1 
ATOM   8940  C CG     . GLU D 2 47  ? 49.890  34.910  52.021 1.00 90.47  ? 65  GLU D CG     1 
ATOM   8941  C CD     . GLU D 2 47  ? 49.945  33.602  52.775 1.00 100.64 ? 65  GLU D CD     1 
ATOM   8942  O OE1    . GLU D 2 47  ? 51.061  33.153  53.107 1.00 108.10 ? 65  GLU D OE1    1 
ATOM   8943  O OE2    . GLU D 2 47  ? 48.871  33.027  53.041 1.00 96.22  ? 65  GLU D OE2    1 
ATOM   8944  N N      . ASP D 2 48  ? 52.756  38.585  52.450 1.00 66.89  ? 66  ASP D N      1 
ATOM   8945  C CA     . ASP D 2 48  ? 53.289  39.752  53.111 1.00 59.03  ? 66  ASP D CA     1 
ATOM   8946  C C      . ASP D 2 48  ? 52.948  40.956  52.291 1.00 61.21  ? 66  ASP D C      1 
ATOM   8947  O O      . ASP D 2 48  ? 52.571  41.971  52.831 1.00 63.97  ? 66  ASP D O      1 
ATOM   8948  C CB     . ASP D 2 48  ? 54.789  39.653  53.280 1.00 62.64  ? 66  ASP D CB     1 
ATOM   8949  C CG     . ASP D 2 48  ? 55.246  40.101  54.647 1.00 68.67  ? 66  ASP D CG     1 
ATOM   8950  O OD1    . ASP D 2 48  ? 54.384  40.299  55.526 1.00 67.98  ? 66  ASP D OD1    1 
ATOM   8951  O OD2    . ASP D 2 48  ? 56.468  40.247  54.847 1.00 77.41  ? 66  ASP D OD2    1 
ATOM   8952  N N      . ILE D 2 49  ? 53.055  40.859  50.976 1.00 56.81  ? 67  ILE D N      1 
ATOM   8953  C CA     . ILE D 2 49  ? 52.819  42.016  50.137 1.00 49.57  ? 67  ILE D CA     1 
ATOM   8954  C C      . ILE D 2 49  ? 51.379  42.466  50.225 1.00 49.23  ? 67  ILE D C      1 
ATOM   8955  O O      . ILE D 2 49  ? 51.086  43.642  50.138 1.00 55.77  ? 67  ILE D O      1 
ATOM   8956  C CB     . ILE D 2 49  ? 53.206  41.755  48.685 1.00 49.00  ? 67  ILE D CB     1 
ATOM   8957  C CG1    . ILE D 2 49  ? 54.618  41.198  48.601 1.00 52.97  ? 67  ILE D CG1    1 
ATOM   8958  C CG2    . ILE D 2 49  ? 53.148  43.034  47.873 1.00 53.29  ? 67  ILE D CG2    1 
ATOM   8959  C CD1    . ILE D 2 49  ? 55.679  42.172  49.043 1.00 61.43  ? 67  ILE D CD1    1 
ATOM   8960  N N      . GLU D 2 50  ? 50.468  41.544  50.449 1.00 49.76  ? 68  GLU D N      1 
ATOM   8961  C CA     . GLU D 2 50  ? 49.078  41.914  50.583 1.00 52.29  ? 68  GLU D CA     1 
ATOM   8962  C C      . GLU D 2 50  ? 48.753  42.327  51.982 1.00 50.66  ? 68  GLU D C      1 
ATOM   8963  O O      . GLU D 2 50  ? 47.652  42.766  52.260 1.00 46.57  ? 68  GLU D O      1 
ATOM   8964  C CB     . GLU D 2 50  ? 48.164  40.786  50.118 1.00 55.89  ? 68  GLU D CB     1 
ATOM   8965  C CG     . GLU D 2 50  ? 47.901  39.662  51.104 1.00 75.06  ? 68  GLU D CG     1 
ATOM   8966  C CD     . GLU D 2 50  ? 47.081  38.541  50.489 1.00 78.44  ? 68  GLU D CD     1 
ATOM   8967  O OE1    . GLU D 2 50  ? 46.970  38.501  49.248 1.00 69.47  ? 68  GLU D OE1    1 
ATOM   8968  O OE2    . GLU D 2 50  ? 46.554  37.695  51.243 1.00 79.23  ? 68  GLU D OE2    1 
ATOM   8969  N N      . LYS D 2 51  ? 49.729  42.239  52.867 1.00 53.18  ? 69  LYS D N      1 
ATOM   8970  C CA     . LYS D 2 51  ? 49.526  42.651  54.240 1.00 51.57  ? 69  LYS D CA     1 
ATOM   8971  C C      . LYS D 2 51  ? 50.211  43.953  54.472 1.00 45.72  ? 69  LYS D C      1 
ATOM   8972  O O      . LYS D 2 51  ? 49.702  44.796  55.174 1.00 50.98  ? 69  LYS D O      1 
ATOM   8973  C CB     . LYS D 2 51  ? 50.045  41.590  55.178 1.00 52.91  ? 69  LYS D CB     1 
ATOM   8974  C CG     . LYS D 2 51  ? 49.104  40.403  55.320 1.00 58.89  ? 69  LYS D CG     1 
ATOM   8975  C CD     . LYS D 2 51  ? 49.660  39.345  56.256 1.00 59.32  ? 69  LYS D CD     1 
ATOM   8976  C CE     . LYS D 2 51  ? 49.793  39.873  57.672 1.00 60.69  ? 69  LYS D CE     1 
ATOM   8977  N NZ     . LYS D 2 51  ? 48.484  40.298  58.236 1.00 64.58  ? 69  LYS D NZ     1 
ATOM   8978  N N      . LEU D 2 52  ? 51.357  44.144  53.863 1.00 41.75  ? 70  LEU D N      1 
ATOM   8979  C CA     . LEU D 2 52  ? 52.042  45.402  53.966 1.00 41.94  ? 70  LEU D CA     1 
ATOM   8980  C C      . LEU D 2 52  ? 51.233  46.426  53.223 1.00 47.71  ? 70  LEU D C      1 
ATOM   8981  O O      . LEU D 2 52  ? 51.199  47.580  53.608 1.00 48.45  ? 70  LEU D O      1 
ATOM   8982  C CB     . LEU D 2 52  ? 53.417  45.298  53.336 1.00 40.44  ? 70  LEU D CB     1 
ATOM   8983  C CG     . LEU D 2 52  ? 54.461  44.369  53.932 1.00 42.50  ? 70  LEU D CG     1 
ATOM   8984  C CD1    . LEU D 2 52  ? 55.668  44.351  53.020 1.00 50.37  ? 70  LEU D CD1    1 
ATOM   8985  C CD2    . LEU D 2 52  ? 54.850  44.818  55.326 1.00 56.50  ? 70  LEU D CD2    1 
ATOM   8986  N N      . TYR D 2 53  ? 50.590  46.017  52.140 1.00 47.57  ? 71  TYR D N      1 
ATOM   8987  C CA     . TYR D 2 53  ? 49.777  46.926  51.351 1.00 43.26  ? 71  TYR D CA     1 
ATOM   8988  C C      . TYR D 2 53  ? 48.727  47.513  52.226 1.00 46.60  ? 71  TYR D C      1 
ATOM   8989  O O      . TYR D 2 53  ? 48.496  48.699  52.197 1.00 53.76  ? 71  TYR D O      1 
ATOM   8990  C CB     . TYR D 2 53  ? 49.099  46.199  50.209 1.00 34.60  ? 71  TYR D CB     1 
ATOM   8991  C CG     . TYR D 2 53  ? 48.321  47.061  49.254 1.00 36.44  ? 71  TYR D CG     1 
ATOM   8992  C CD1    . TYR D 2 53  ? 48.956  47.736  48.230 1.00 36.41  ? 71  TYR D CD1    1 
ATOM   8993  C CD2    . TYR D 2 53  ? 46.948  47.168  49.352 1.00 36.45  ? 71  TYR D CD2    1 
ATOM   8994  C CE1    . TYR D 2 53  ? 48.245  48.514  47.345 1.00 35.78  ? 71  TYR D CE1    1 
ATOM   8995  C CE2    . TYR D 2 53  ? 46.230  47.945  48.471 1.00 34.42  ? 71  TYR D CE2    1 
ATOM   8996  C CZ     . TYR D 2 53  ? 46.885  48.612  47.473 1.00 35.48  ? 71  TYR D CZ     1 
ATOM   8997  O OH     . TYR D 2 53  ? 46.165  49.382  46.605 1.00 40.14  ? 71  TYR D OH     1 
ATOM   8998  N N      . PHE D 2 54  ? 48.083  46.697  53.027 1.00 44.02  ? 72  PHE D N      1 
ATOM   8999  C CA     . PHE D 2 54  ? 47.005  47.188  53.837 1.00 42.67  ? 72  PHE D CA     1 
ATOM   9000  C C      . PHE D 2 54  ? 47.538  48.164  54.792 1.00 47.38  ? 72  PHE D C      1 
ATOM   9001  O O      . PHE D 2 54  ? 46.872  49.118  55.153 1.00 54.45  ? 72  PHE D O      1 
ATOM   9002  C CB     . PHE D 2 54  ? 46.395  46.076  54.649 1.00 45.16  ? 72  PHE D CB     1 
ATOM   9003  C CG     . PHE D 2 54  ? 45.285  46.519  55.537 1.00 39.82  ? 72  PHE D CG     1 
ATOM   9004  C CD1    . PHE D 2 54  ? 44.137  47.050  55.002 1.00 41.93  ? 72  PHE D CD1    1 
ATOM   9005  C CD2    . PHE D 2 54  ? 45.392  46.402  56.900 1.00 41.08  ? 72  PHE D CD2    1 
ATOM   9006  C CE1    . PHE D 2 54  ? 43.114  47.464  55.811 1.00 41.07  ? 72  PHE D CE1    1 
ATOM   9007  C CE2    . PHE D 2 54  ? 44.373  46.815  57.718 1.00 43.15  ? 72  PHE D CE2    1 
ATOM   9008  C CZ     . PHE D 2 54  ? 43.233  47.344  57.172 1.00 41.81  ? 72  PHE D CZ     1 
ATOM   9009  N N      . LYS D 2 55  ? 48.770  47.970  55.194 1.00 46.36  ? 73  LYS D N      1 
ATOM   9010  C CA     . LYS D 2 55  ? 49.293  48.834  56.220 1.00 52.24  ? 73  LYS D CA     1 
ATOM   9011  C C      . LYS D 2 55  ? 50.088  49.941  55.614 1.00 50.18  ? 73  LYS D C      1 
ATOM   9012  O O      . LYS D 2 55  ? 50.810  50.637  56.307 1.00 58.60  ? 73  LYS D O      1 
ATOM   9013  C CB     . LYS D 2 55  ? 50.063  48.032  57.256 1.00 54.00  ? 73  LYS D CB     1 
ATOM   9014  C CG     . LYS D 2 55  ? 49.248  46.898  57.850 1.00 52.12  ? 73  LYS D CG     1 
ATOM   9015  C CD     . LYS D 2 55  ? 49.898  46.314  59.089 1.00 55.31  ? 73  LYS D CD     1 
ATOM   9016  C CE     . LYS D 2 55  ? 49.786  47.265  60.268 1.00 62.60  ? 73  LYS D CE     1 
ATOM   9017  N NZ     . LYS D 2 55  ? 50.264  46.639  61.531 1.00 60.67  ? 73  LYS D NZ     1 
ATOM   9018  N N      . GLN D 2 56  ? 49.939  50.122  54.325 1.00 47.84  ? 74  GLN D N      1 
ATOM   9019  C CA     . GLN D 2 56  ? 50.568  51.243  53.670 1.00 49.99  ? 74  GLN D CA     1 
ATOM   9020  C C      . GLN D 2 56  ? 52.054  51.361  53.762 1.00 52.26  ? 74  GLN D C      1 
ATOM   9021  O O      . GLN D 2 56  ? 52.585  52.462  53.725 1.00 50.07  ? 74  GLN D O      1 
ATOM   9022  C CB     . GLN D 2 56  ? 49.853  52.533  54.047 1.00 49.55  ? 74  GLN D CB     1 
ATOM   9023  C CG     . GLN D 2 56  ? 48.360  52.448  53.790 1.00 50.92  ? 74  GLN D CG     1 
ATOM   9024  C CD     . GLN D 2 56  ? 47.649  53.762  53.969 1.00 51.81  ? 74  GLN D CD     1 
ATOM   9025  O OE1    . GLN D 2 56  ? 48.274  54.807  54.067 1.00 46.14  ? 74  GLN D OE1    1 
ATOM   9026  N NE2    . GLN D 2 56  ? 46.329  53.715  54.002 1.00 47.06  ? 74  GLN D NE2    1 
ATOM   9027  N N      . ASN D 2 57  ? 52.751  50.235  53.843 1.00 53.57  ? 75  ASN D N      1 
ATOM   9028  C CA     . ASN D 2 57  ? 54.210  50.263  53.818 1.00 58.57  ? 75  ASN D CA     1 
ATOM   9029  C C      . ASN D 2 57  ? 54.578  49.988  52.404 1.00 59.65  ? 75  ASN D C      1 
ATOM   9030  O O      . ASN D 2 57  ? 55.185  48.975  52.117 1.00 58.31  ? 75  ASN D O      1 
ATOM   9031  C CB     . ASN D 2 57  ? 54.815  49.193  54.701 1.00 53.43  ? 75  ASN D CB     1 
ATOM   9032  C CG     . ASN D 2 57  ? 56.131  49.620  55.299 1.00 67.53  ? 75  ASN D CG     1 
ATOM   9033  O OD1    . ASN D 2 57  ? 56.899  50.349  54.679 1.00 72.71  ? 75  ASN D OD1    1 
ATOM   9034  N ND2    . ASN D 2 57  ? 56.397  49.168  56.515 1.00 78.88  ? 75  ASN D ND2    1 
ATOM   9035  N N      . TYR D 2 58  ? 54.225  50.891  51.503 1.00 59.19  ? 76  TYR D N      1 
ATOM   9036  C CA     . TYR D 2 58  ? 54.442  50.652  50.084 1.00 51.08  ? 76  TYR D CA     1 
ATOM   9037  C C      . TYR D 2 58  ? 55.880  50.507  49.654 1.00 53.27  ? 76  TYR D C      1 
ATOM   9038  O O      . TYR D 2 58  ? 56.186  49.684  48.815 1.00 52.28  ? 76  TYR D O      1 
ATOM   9039  C CB     . TYR D 2 58  ? 53.752  51.723  49.251 1.00 44.47  ? 76  TYR D CB     1 
ATOM   9040  C CG     . TYR D 2 58  ? 52.262  51.774  49.409 1.00 41.91  ? 76  TYR D CG     1 
ATOM   9041  C CD1    . TYR D 2 58  ? 51.550  50.669  49.832 1.00 43.94  ? 76  TYR D CD1    1 
ATOM   9042  C CD2    . TYR D 2 58  ? 51.565  52.927  49.125 1.00 46.10  ? 76  TYR D CD2    1 
ATOM   9043  C CE1    . TYR D 2 58  ? 50.188  50.718  49.983 1.00 42.72  ? 76  TYR D CE1    1 
ATOM   9044  C CE2    . TYR D 2 58  ? 50.202  52.980  49.268 1.00 46.79  ? 76  TYR D CE2    1 
ATOM   9045  C CZ     . TYR D 2 58  ? 49.527  51.873  49.699 1.00 43.60  ? 76  TYR D CZ     1 
ATOM   9046  O OH     . TYR D 2 58  ? 48.177  51.927  49.848 1.00 41.46  ? 76  TYR D OH     1 
ATOM   9047  N N      . LYS D 2 59  ? 56.778  51.289  50.209 1.00 50.40  ? 77  LYS D N      1 
ATOM   9048  C CA     . LYS D 2 59  ? 58.135  51.226  49.730 1.00 48.06  ? 77  LYS D CA     1 
ATOM   9049  C C      . LYS D 2 59  ? 58.718  49.897  50.023 1.00 54.42  ? 77  LYS D C      1 
ATOM   9050  O O      . LYS D 2 59  ? 59.463  49.361  49.229 1.00 59.10  ? 77  LYS D O      1 
ATOM   9051  C CB     . LYS D 2 59  ? 58.987  52.299  50.360 1.00 44.43  ? 77  LYS D CB     1 
ATOM   9052  C CG     . LYS D 2 59  ? 59.504  53.321  49.366 1.00 55.32  ? 77  LYS D CG     1 
ATOM   9053  C CD     . LYS D 2 59  ? 60.202  54.466  50.073 1.00 44.29  ? 77  LYS D CD     1 
ATOM   9054  C CE     . LYS D 2 59  ? 60.721  55.485  49.077 1.00 48.02  ? 77  LYS D CE     1 
ATOM   9055  N NZ     . LYS D 2 59  ? 61.757  54.899  48.184 1.00 63.63  ? 77  LYS D NZ     1 
ATOM   9056  N N      . GLU D 2 60  ? 58.380  49.347  51.171 1.00 57.56  ? 78  GLU D N      1 
ATOM   9057  C CA     . GLU D 2 60  ? 58.965  48.089  51.573 1.00 60.00  ? 78  GLU D CA     1 
ATOM   9058  C C      . GLU D 2 60  ? 58.553  47.070  50.580 1.00 61.44  ? 78  GLU D C      1 
ATOM   9059  O O      . GLU D 2 60  ? 59.367  46.330  50.075 1.00 63.80  ? 78  GLU D O      1 
ATOM   9060  C CB     . GLU D 2 60  ? 58.471  47.685  52.954 1.00 58.78  ? 78  GLU D CB     1 
ATOM   9061  C CG     . GLU D 2 60  ? 59.204  46.513  53.573 1.00 66.69  ? 78  GLU D CG     1 
ATOM   9062  C CD     . GLU D 2 60  ? 58.658  46.150  54.935 1.00 72.94  ? 78  GLU D CD     1 
ATOM   9063  O OE1    . GLU D 2 60  ? 57.717  46.822  55.387 1.00 73.17  ? 78  GLU D OE1    1 
ATOM   9064  O OE2    . GLU D 2 60  ? 59.164  45.197  55.556 1.00 81.82  ? 78  GLU D OE2    1 
ATOM   9065  N N      . ALA D 2 61  ? 57.274  47.017  50.287 1.00 59.24  ? 79  ALA D N      1 
ATOM   9066  C CA     . ALA D 2 61  ? 56.791  46.001  49.398 1.00 55.29  ? 79  ALA D CA     1 
ATOM   9067  C C      . ALA D 2 61  ? 57.443  46.184  48.075 1.00 61.38  ? 79  ALA D C      1 
ATOM   9068  O O      . ALA D 2 61  ? 57.761  45.228  47.408 1.00 60.29  ? 79  ALA D O      1 
ATOM   9069  C CB     . ALA D 2 61  ? 55.299  46.096  49.264 1.00 51.36  ? 79  ALA D CB     1 
ATOM   9070  N N      . ILE D 2 62  ? 57.646  47.425  47.684 1.00 62.94  ? 80  ILE D N      1 
ATOM   9071  C CA     . ILE D 2 62  ? 58.231  47.685  46.393 1.00 63.18  ? 80  ILE D CA     1 
ATOM   9072  C C      . ILE D 2 62  ? 59.593  47.033  46.383 1.00 68.22  ? 80  ILE D C      1 
ATOM   9073  O O      . ILE D 2 62  ? 59.931  46.317  45.455 1.00 69.08  ? 80  ILE D O      1 
ATOM   9074  C CB     . ILE D 2 62  ? 58.315  49.185  46.078 1.00 58.58  ? 80  ILE D CB     1 
ATOM   9075  C CG1    . ILE D 2 62  ? 56.949  49.721  45.657 1.00 51.98  ? 80  ILE D CG1    1 
ATOM   9076  C CG2    . ILE D 2 62  ? 59.312  49.460  44.968 1.00 61.72  ? 80  ILE D CG2    1 
ATOM   9077  C CD1    . ILE D 2 62  ? 56.957  51.196  45.330 1.00 48.12  ? 80  ILE D CD1    1 
ATOM   9078  N N      . GLU D 2 63  ? 60.366  47.227  47.440 1.00 68.91  ? 81  GLU D N      1 
ATOM   9079  C CA     . GLU D 2 63  ? 61.705  46.672  47.475 1.00 66.62  ? 81  GLU D CA     1 
ATOM   9080  C C      . GLU D 2 63  ? 61.606  45.197  47.363 1.00 68.34  ? 81  GLU D C      1 
ATOM   9081  O O      . GLU D 2 63  ? 62.295  44.576  46.577 1.00 70.24  ? 81  GLU D O      1 
ATOM   9082  C CB     . GLU D 2 63  ? 62.412  47.029  48.768 1.00 61.58  ? 81  GLU D CB     1 
ATOM   9083  C CG     . GLU D 2 63  ? 62.592  48.523  48.986 1.00 71.80  ? 81  GLU D CG     1 
ATOM   9084  C CD     . GLU D 2 63  ? 63.495  49.181  47.957 1.00 85.37  ? 81  GLU D CD     1 
ATOM   9085  O OE1    . GLU D 2 63  ? 64.372  48.499  47.390 1.00 91.40  ? 81  GLU D OE1    1 
ATOM   9086  O OE2    . GLU D 2 63  ? 63.337  50.397  47.725 1.00 84.57  ? 81  GLU D OE2    1 
ATOM   9087  N N      . LYS D 2 64  ? 60.729  44.622  48.151 1.00 63.79  ? 82  LYS D N      1 
ATOM   9088  C CA     . LYS D 2 64  ? 60.610  43.190  48.155 1.00 63.61  ? 82  LYS D CA     1 
ATOM   9089  C C      . LYS D 2 64  ? 60.162  42.708  46.808 1.00 63.26  ? 82  LYS D C      1 
ATOM   9090  O O      . LYS D 2 64  ? 60.587  41.665  46.346 1.00 70.09  ? 82  LYS D O      1 
ATOM   9091  C CB     . LYS D 2 64  ? 59.641  42.751  49.240 1.00 62.66  ? 82  LYS D CB     1 
ATOM   9092  C CG     . LYS D 2 64  ? 60.177  42.928  50.651 1.00 63.09  ? 82  LYS D CG     1 
ATOM   9093  C CD     . LYS D 2 64  ? 59.078  42.807  51.693 1.00 59.09  ? 82  LYS D CD     1 
ATOM   9094  C CE     . LYS D 2 64  ? 58.310  41.506  51.553 1.00 69.08  ? 82  LYS D CE     1 
ATOM   9095  N NZ     . LYS D 2 64  ? 59.161  40.303  51.762 1.00 77.75  ? 82  LYS D NZ     1 
ATOM   9096  N N      . ILE D 2 65  ? 59.331  43.480  46.145 1.00 56.92  ? 83  ILE D N      1 
ATOM   9097  C CA     . ILE D 2 65  ? 58.811  43.041  44.876 1.00 60.48  ? 83  ILE D CA     1 
ATOM   9098  C C      . ILE D 2 65  ? 59.939  43.007  43.893 1.00 65.15  ? 83  ILE D C      1 
ATOM   9099  O O      . ILE D 2 65  ? 60.110  42.037  43.173 1.00 70.33  ? 83  ILE D O      1 
ATOM   9100  C CB     . ILE D 2 65  ? 57.690  43.960  44.388 1.00 57.60  ? 83  ILE D CB     1 
ATOM   9101  C CG1    . ILE D 2 65  ? 56.358  43.559  45.012 1.00 56.74  ? 83  ILE D CG1    1 
ATOM   9102  C CG2    . ILE D 2 65  ? 57.572  43.918  42.880 1.00 57.70  ? 83  ILE D CG2    1 
ATOM   9103  C CD1    . ILE D 2 65  ? 55.234  44.494  44.651 1.00 51.09  ? 83  ILE D CD1    1 
ATOM   9104  N N      . LEU D 2 66  ? 60.750  44.045  43.869 1.00 63.79  ? 84  LEU D N      1 
ATOM   9105  C CA     . LEU D 2 66  ? 61.818  44.112  42.889 1.00 63.36  ? 84  LEU D CA     1 
ATOM   9106  C C      . LEU D 2 66  ? 62.824  43.017  43.106 1.00 67.08  ? 84  LEU D C      1 
ATOM   9107  O O      . LEU D 2 66  ? 63.302  42.436  42.151 1.00 56.09  ? 84  LEU D O      1 
ATOM   9108  C CB     . LEU D 2 66  ? 62.482  45.472  42.936 1.00 63.82  ? 84  LEU D CB     1 
ATOM   9109  C CG     . LEU D 2 66  ? 61.560  46.632  42.567 1.00 56.05  ? 84  LEU D CG     1 
ATOM   9110  C CD1    . LEU D 2 66  ? 62.214  47.966  42.864 1.00 61.72  ? 84  LEU D CD1    1 
ATOM   9111  C CD2    . LEU D 2 66  ? 61.164  46.545  41.106 1.00 62.60  ? 84  LEU D CD2    1 
ATOM   9112  N N      . ASP D 2 67  ? 63.145  42.722  44.359 1.00 70.13  ? 85  ASP D N      1 
ATOM   9113  C CA     . ASP D 2 67  ? 64.150  41.706  44.645 1.00 66.79  ? 85  ASP D CA     1 
ATOM   9114  C C      . ASP D 2 67  ? 63.608  40.302  44.553 1.00 67.85  ? 85  ASP D C      1 
ATOM   9115  O O      . ASP D 2 67  ? 64.357  39.369  44.313 1.00 72.55  ? 85  ASP D O      1 
ATOM   9116  C CB     . ASP D 2 67  ? 64.924  41.966  45.949 1.00 62.21  ? 85  ASP D CB     1 
ATOM   9117  C CG     . ASP D 2 67  ? 64.060  41.944  47.188 1.00 73.11  ? 85  ASP D CG     1 
ATOM   9118  O OD1    . ASP D 2 67  ? 63.257  41.010  47.378 1.00 78.66  ? 85  ASP D OD1    1 
ATOM   9119  O OD2    . ASP D 2 67  ? 64.229  42.862  48.015 1.00 77.60  ? 85  ASP D OD2    1 
ATOM   9120  N N      . PHE D 2 68  ? 62.310  40.133  44.742 1.00 60.24  ? 86  PHE D N      1 
ATOM   9121  C CA     . PHE D 2 68  ? 61.722  38.825  44.574 1.00 62.40  ? 86  PHE D CA     1 
ATOM   9122  C C      . PHE D 2 68  ? 61.991  38.518  43.164 1.00 63.30  ? 86  PHE D C      1 
ATOM   9123  O O      . PHE D 2 68  ? 62.396  37.425  42.814 1.00 61.29  ? 86  PHE D O      1 
ATOM   9124  C CB     . PHE D 2 68  ? 60.238  38.908  44.711 1.00 57.71  ? 86  PHE D CB     1 
ATOM   9125  C CG     . PHE D 2 68  ? 59.555  37.602  44.588 1.00 60.33  ? 86  PHE D CG     1 
ATOM   9126  C CD1    . PHE D 2 68  ? 59.751  36.621  45.531 1.00 66.73  ? 86  PHE D CD1    1 
ATOM   9127  C CD2    . PHE D 2 68  ? 58.708  37.360  43.539 1.00 62.93  ? 86  PHE D CD2    1 
ATOM   9128  C CE1    . PHE D 2 68  ? 59.112  35.412  45.425 1.00 66.35  ? 86  PHE D CE1    1 
ATOM   9129  C CE2    . PHE D 2 68  ? 58.062  36.161  43.427 1.00 68.24  ? 86  PHE D CE2    1 
ATOM   9130  C CZ     . PHE D 2 68  ? 58.267  35.184  44.367 1.00 72.17  ? 86  PHE D CZ     1 
ATOM   9131  N N      . CYS D 2 69  ? 61.763  39.504  42.321 1.00 64.02  ? 87  CYS D N      1 
ATOM   9132  C CA     . CYS D 2 69  ? 61.971  39.324  40.902 1.00 67.42  ? 87  CYS D CA     1 
ATOM   9133  C C      . CYS D 2 69  ? 63.439  39.237  40.543 1.00 69.08  ? 87  CYS D C      1 
ATOM   9134  O O      . CYS D 2 69  ? 63.792  38.601  39.576 1.00 76.42  ? 87  CYS D O      1 
ATOM   9135  C CB     . CYS D 2 69  ? 61.333  40.462  40.120 1.00 68.84  ? 87  CYS D CB     1 
ATOM   9136  S SG     . CYS D 2 69  ? 59.543  40.529  40.154 1.00 62.90  ? 87  CYS D SG     1 
ATOM   9137  N N      . LYS D 2 70  ? 64.314  39.864  41.298 1.00 59.25  ? 88  LYS D N      1 
ATOM   9138  C CA     . LYS D 2 70  ? 65.689  39.799  40.905 1.00 58.24  ? 88  LYS D CA     1 
ATOM   9139  C C      . LYS D 2 70  ? 66.098  38.383  41.087 1.00 64.28  ? 88  LYS D C      1 
ATOM   9140  O O      . LYS D 2 70  ? 66.840  37.836  40.297 1.00 68.87  ? 88  LYS D O      1 
ATOM   9141  C CB     . LYS D 2 70  ? 66.561  40.669  41.776 1.00 63.11  ? 88  LYS D CB     1 
ATOM   9142  C CG     . LYS D 2 70  ? 66.714  42.102  41.299 1.00 64.29  ? 88  LYS D CG     1 
ATOM   9143  C CD     . LYS D 2 70  ? 67.957  42.763  41.884 1.00 65.81  ? 88  LYS D CD     1 
ATOM   9144  C CE     . LYS D 2 70  ? 67.852  43.013  43.383 1.00 69.19  ? 88  LYS D CE     1 
ATOM   9145  N NZ     . LYS D 2 70  ? 68.280  41.869  44.237 1.00 53.17  ? 88  LYS D NZ     1 
ATOM   9146  N N      . LYS D 2 71  ? 65.602  37.748  42.128 1.00 66.48  ? 89  LYS D N      1 
ATOM   9147  C CA     . LYS D 2 71  ? 66.062  36.397  42.404 1.00 68.92  ? 89  LYS D CA     1 
ATOM   9148  C C      . LYS D 2 71  ? 65.434  35.455  41.429 1.00 63.42  ? 89  LYS D C      1 
ATOM   9149  O O      . LYS D 2 71  ? 66.063  34.511  40.973 1.00 70.62  ? 89  LYS D O      1 
ATOM   9150  C CB     . LYS D 2 71  ? 65.739  35.993  43.840 1.00 65.01  ? 89  LYS D CB     1 
ATOM   9151  C CG     . LYS D 2 71  ? 66.127  34.567  44.187 1.00 69.20  ? 89  LYS D CG     1 
ATOM   9152  C CD     . LYS D 2 71  ? 65.779  34.231  45.624 1.00 69.80  ? 89  LYS D CD     1 
ATOM   9153  C CE     . LYS D 2 71  ? 65.877  32.736  45.879 1.00 74.07  ? 89  LYS D CE     1 
ATOM   9154  N NZ     . LYS D 2 71  ? 64.802  31.980  45.181 1.00 62.36  ? 89  LYS D NZ     1 
ATOM   9155  N N      . ASN D 2 72  ? 64.213  35.743  41.041 1.00 59.45  ? 90  ASN D N      1 
ATOM   9156  C CA     . ASN D 2 72  ? 63.497  34.842  40.170 1.00 67.38  ? 90  ASN D CA     1 
ATOM   9157  C C      . ASN D 2 72  ? 63.451  35.344  38.746 1.00 71.67  ? 90  ASN D C      1 
ATOM   9158  O O      . ASN D 2 72  ? 62.534  35.032  38.013 1.00 75.21  ? 90  ASN D O      1 
ATOM   9159  C CB     . ASN D 2 72  ? 62.110  34.580  40.715 1.00 63.85  ? 90  ASN D CB     1 
ATOM   9160  C CG     . ASN D 2 72  ? 62.139  33.871  42.045 1.00 63.00  ? 90  ASN D CG     1 
ATOM   9161  O OD1    . ASN D 2 72  ? 63.001  33.036  42.297 1.00 65.06  ? 90  ASN D OD1    1 
ATOM   9162  N ND2    . ASN D 2 72  ? 61.193  34.197  42.903 1.00 68.35  ? 90  ASN D ND2    1 
ATOM   9163  N N      . GLU D 2 73  ? 64.428  36.144  38.358 1.00 70.98  ? 91  GLU D N      1 
ATOM   9164  C CA     . GLU D 2 73  ? 64.486  36.672  37.007 1.00 71.44  ? 91  GLU D CA     1 
ATOM   9165  C C      . GLU D 2 73  ? 64.642  35.588  35.978 1.00 84.45  ? 91  GLU D C      1 
ATOM   9166  O O      . GLU D 2 73  ? 64.300  35.772  34.826 1.00 79.98  ? 91  GLU D O      1 
ATOM   9167  C CB     . GLU D 2 73  ? 65.612  37.682  36.858 1.00 70.02  ? 91  GLU D CB     1 
ATOM   9168  C CG     . GLU D 2 73  ? 67.000  37.179  37.182 1.00 66.27  ? 91  GLU D CG     1 
ATOM   9169  C CD     . GLU D 2 73  ? 67.985  38.319  37.315 1.00 80.73  ? 91  GLU D CD     1 
ATOM   9170  O OE1    . GLU D 2 73  ? 67.697  39.413  36.788 1.00 80.13  ? 91  GLU D OE1    1 
ATOM   9171  O OE2    . GLU D 2 73  ? 69.040  38.123  37.951 1.00 88.88  ? 91  GLU D OE2    1 
ATOM   9172  N N      . SER D 2 74  ? 65.239  34.478  36.351 1.00 86.04  ? 92  SER D N      1 
ATOM   9173  C CA     . SER D 2 74  ? 65.321  33.411  35.405 1.00 83.36  ? 92  SER D CA     1 
ATOM   9174  C C      . SER D 2 74  ? 63.932  32.979  35.067 1.00 81.30  ? 92  SER D C      1 
ATOM   9175  O O      . SER D 2 74  ? 63.582  32.853  33.906 1.00 80.41  ? 92  SER D O      1 
ATOM   9176  C CB     . SER D 2 74  ? 66.021  32.247  36.080 1.00 78.27  ? 92  SER D CB     1 
ATOM   9177  O OG     . SER D 2 74  ? 65.942  31.078  35.285 1.00 100.26 ? 92  SER D OG     1 
ATOM   9178  N N      . LEU D 2 75  ? 63.117  32.799  36.085 1.00 80.34  ? 93  LEU D N      1 
ATOM   9179  C CA     . LEU D 2 75  ? 61.760  32.336  35.881 1.00 79.81  ? 93  LEU D CA     1 
ATOM   9180  C C      . LEU D 2 75  ? 60.889  33.322  35.141 1.00 80.27  ? 93  LEU D C      1 
ATOM   9181  O O      . LEU D 2 75  ? 60.085  32.934  34.304 1.00 87.87  ? 93  LEU D O      1 
ATOM   9182  C CB     . LEU D 2 75  ? 61.131  32.012  37.233 1.00 74.31  ? 93  LEU D CB     1 
ATOM   9183  C CG     . LEU D 2 75  ? 61.694  30.838  38.042 1.00 79.65  ? 93  LEU D CG     1 
ATOM   9184  C CD1    . LEU D 2 75  ? 62.907  31.229  38.869 1.00 78.88  ? 93  LEU D CD1    1 
ATOM   9185  C CD2    . LEU D 2 75  ? 60.630  30.252  38.953 1.00 74.80  ? 93  LEU D CD2    1 
ATOM   9186  N N      . LEU D 2 76  ? 61.055  34.601  35.424 1.00 30.00  ? 94  LEU D N      1 
ATOM   9187  C CA     . LEU D 2 76  ? 60.200  35.617  34.838 1.00 30.00  ? 94  LEU D CA     1 
ATOM   9188  C C      . LEU D 2 76  ? 60.787  36.265  33.633 1.00 30.00  ? 94  LEU D C      1 
ATOM   9189  O O      . LEU D 2 76  ? 61.747  35.774  33.061 1.00 30.00  ? 94  LEU D O      1 
ATOM   9190  C CB     . LEU D 2 76  ? 59.940  36.720  35.853 1.00 30.00  ? 94  LEU D CB     1 
ATOM   9191  C CG     . LEU D 2 76  ? 58.930  36.490  36.967 1.00 30.00  ? 94  LEU D CG     1 
ATOM   9192  C CD1    . LEU D 2 76  ? 57.962  35.397  36.567 1.00 30.00  ? 94  LEU D CD1    1 
ATOM   9193  C CD2    . LEU D 2 76  ? 59.600  36.182  38.291 1.00 30.00  ? 94  LEU D CD2    1 
ATOM   9194  N N      . SER D 2 77  ? 60.222  37.398  33.254 1.00 82.36  ? 95  SER D N      1 
ATOM   9195  C CA     . SER D 2 77  ? 60.674  38.054  32.059 1.00 86.40  ? 95  SER D CA     1 
ATOM   9196  C C      . SER D 2 77  ? 61.345  39.334  32.379 1.00 88.12  ? 95  SER D C      1 
ATOM   9197  O O      . SER D 2 77  ? 60.799  40.176  33.060 1.00 86.09  ? 95  SER D O      1 
ATOM   9198  C CB     . SER D 2 77  ? 59.501  38.341  31.156 1.00 84.07  ? 95  SER D CB     1 
ATOM   9199  O OG     . SER D 2 77  ? 58.745  37.165  30.943 1.00 75.71  ? 95  SER D OG     1 
ATOM   9200  N N      . GLU D 2 78  ? 62.529  39.504  31.845 1.00 86.93  ? 96  GLU D N      1 
ATOM   9201  C CA     . GLU D 2 78  ? 63.276  40.692  32.119 1.00 91.49  ? 96  GLU D CA     1 
ATOM   9202  C C      . GLU D 2 78  ? 62.551  41.873  31.585 1.00 86.12  ? 96  GLU D C      1 
ATOM   9203  O O      . GLU D 2 78  ? 62.678  42.956  32.106 1.00 91.34  ? 96  GLU D O      1 
ATOM   9204  C CB     . GLU D 2 78  ? 64.678  40.628  31.525 1.00 102.46 ? 96  GLU D CB     1 
ATOM   9205  C CG     . GLU D 2 78  ? 65.619  41.695  32.067 1.00 99.90  ? 96  GLU D CG     1 
ATOM   9206  C CD     . GLU D 2 78  ? 66.989  41.659  31.426 1.00 96.40  ? 96  GLU D CD     1 
ATOM   9207  O OE1    . GLU D 2 78  ? 67.209  40.819  30.530 1.00 90.93  ? 96  GLU D OE1    1 
ATOM   9208  O OE2    . GLU D 2 78  ? 67.846  42.474  31.822 1.00 89.48  ? 96  GLU D OE2    1 
ATOM   9209  N N      . GLN D 2 79  ? 61.811  41.706  30.516 1.00 74.37  ? 97  GLN D N      1 
ATOM   9210  C CA     . GLN D 2 79  ? 61.217  42.895  29.979 1.00 84.31  ? 97  GLN D CA     1 
ATOM   9211  C C      . GLN D 2 79  ? 60.309  43.550  30.995 1.00 86.95  ? 97  GLN D C      1 
ATOM   9212  O O      . GLN D 2 79  ? 60.437  44.739  31.262 1.00 83.39  ? 97  GLN D O      1 
ATOM   9213  C CB     . GLN D 2 79  ? 60.377  42.549  28.759 1.00 91.41  ? 97  GLN D CB     1 
ATOM   9214  C CG     . GLN D 2 79  ? 61.087  42.738  27.435 1.00 87.52  ? 97  GLN D CG     1 
ATOM   9215  C CD     . GLN D 2 79  ? 60.130  42.675  26.267 1.00 82.91  ? 97  GLN D CD     1 
ATOM   9216  O OE1    . GLN D 2 79  ? 58.933  42.457  26.444 1.00 89.25  ? 97  GLN D OE1    1 
ATOM   9217  N NE2    . GLN D 2 79  ? 60.652  42.871  25.063 1.00 79.20  ? 97  GLN D NE2    1 
ATOM   9218  N N      . VAL D 2 80  ? 59.436  42.776  31.620 1.00 86.79  ? 98  VAL D N      1 
ATOM   9219  C CA     . VAL D 2 80  ? 58.596  43.352  32.638 1.00 81.48  ? 98  VAL D CA     1 
ATOM   9220  C C      . VAL D 2 80  ? 59.452  43.775  33.800 1.00 79.21  ? 98  VAL D C      1 
ATOM   9221  O O      . VAL D 2 80  ? 59.291  44.864  34.314 1.00 76.70  ? 98  VAL D O      1 
ATOM   9222  C CB     . VAL D 2 80  ? 57.516  42.385  33.083 1.00 73.88  ? 98  VAL D CB     1 
ATOM   9223  C CG1    . VAL D 2 80  ? 56.476  43.101  33.924 1.00 72.74  ? 98  VAL D CG1    1 
ATOM   9224  C CG2    . VAL D 2 80  ? 56.871  41.742  31.871 1.00 71.42  ? 98  VAL D CG2    1 
ATOM   9225  N N      . VAL D 2 81  ? 60.415  42.949  34.177 1.00 78.19  ? 99  VAL D N      1 
ATOM   9226  C CA     . VAL D 2 81  ? 61.227  43.251  35.343 1.00 79.18  ? 99  VAL D CA     1 
ATOM   9227  C C      . VAL D 2 81  ? 62.036  44.519  35.171 1.00 75.22  ? 99  VAL D C      1 
ATOM   9228  O O      . VAL D 2 81  ? 62.155  45.321  36.087 1.00 73.71  ? 99  VAL D O      1 
ATOM   9229  C CB     . VAL D 2 81  ? 62.111  42.060  35.739 1.00 78.25  ? 99  VAL D CB     1 
ATOM   9230  C CG1    . VAL D 2 81  ? 63.090  42.438  36.838 1.00 69.00  ? 99  VAL D CG1    1 
ATOM   9231  C CG2    . VAL D 2 81  ? 61.250  40.892  36.183 1.00 71.94  ? 99  VAL D CG2    1 
ATOM   9232  N N      . GLN D 2 82  ? 62.591  44.716  33.998 1.00 69.18  ? 100 GLN D N      1 
ATOM   9233  C CA     . GLN D 2 82  ? 63.345  45.909  33.786 1.00 72.92  ? 100 GLN D CA     1 
ATOM   9234  C C      . GLN D 2 82  ? 62.447  47.100  33.854 1.00 75.93  ? 100 GLN D C      1 
ATOM   9235  O O      . GLN D 2 82  ? 62.807  48.120  34.416 1.00 73.25  ? 100 GLN D O      1 
ATOM   9236  C CB     . GLN D 2 82  ? 64.052  45.869  32.453 1.00 77.89  ? 100 GLN D CB     1 
ATOM   9237  C CG     . GLN D 2 82  ? 65.162  46.893  32.324 1.00 78.62  ? 100 GLN D CG     1 
ATOM   9238  C CD     . GLN D 2 82  ? 66.304  46.402  31.462 1.00 85.51  ? 100 GLN D CD     1 
ATOM   9239  O OE1    . GLN D 2 82  ? 66.331  45.244  31.052 1.00 88.33  ? 100 GLN D OE1    1 
ATOM   9240  N NE2    . GLN D 2 82  ? 67.258  47.279  31.187 1.00 81.01  ? 100 GLN D NE2    1 
ATOM   9241  N N      . ARG D 2 83  ? 61.273  46.988  33.256 1.00 75.57  ? 101 ARG D N      1 
ATOM   9242  C CA     . ARG D 2 83  ? 60.373  48.119  33.238 1.00 71.16  ? 101 ARG D CA     1 
ATOM   9243  C C      . ARG D 2 83  ? 59.950  48.437  34.628 1.00 70.58  ? 101 ARG D C      1 
ATOM   9244  O O      . ARG D 2 83  ? 59.913  49.590  35.018 1.00 70.10  ? 101 ARG D O      1 
ATOM   9245  C CB     . ARG D 2 83  ? 59.150  47.833  32.403 1.00 71.62  ? 101 ARG D CB     1 
ATOM   9246  C CG     . ARG D 2 83  ? 59.417  47.788  30.913 1.00 78.25  ? 101 ARG D CG     1 
ATOM   9247  C CD     . ARG D 2 83  ? 58.200  48.277  30.161 1.00 72.91  ? 101 ARG D CD     1 
ATOM   9248  N NE     . ARG D 2 83  ? 57.753  49.541  30.726 1.00 73.67  ? 101 ARG D NE     1 
ATOM   9249  C CZ     . ARG D 2 83  ? 56.695  50.215  30.305 1.00 70.20  ? 101 ARG D CZ     1 
ATOM   9250  N NH1    . ARG D 2 83  ? 55.968  49.748  29.303 1.00 65.96  ? 101 ARG D NH1    1 
ATOM   9251  N NH2    . ARG D 2 83  ? 56.369  51.356  30.887 1.00 72.41  ? 101 ARG D NH2    1 
ATOM   9252  N N      . LEU D 2 84  ? 59.645  47.407  35.393 1.00 71.39  ? 102 LEU D N      1 
ATOM   9253  C CA     . LEU D 2 84  ? 59.192  47.617  36.746 1.00 72.33  ? 102 LEU D CA     1 
ATOM   9254  C C      . LEU D 2 84  ? 60.243  48.406  37.454 1.00 65.98  ? 102 LEU D C      1 
ATOM   9255  O O      . LEU D 2 84  ? 59.952  49.123  38.392 1.00 61.09  ? 102 LEU D O      1 
ATOM   9256  C CB     . LEU D 2 84  ? 58.986  46.287  37.467 1.00 64.40  ? 102 LEU D CB     1 
ATOM   9257  C CG     . LEU D 2 84  ? 57.854  45.321  37.102 1.00 63.26  ? 102 LEU D CG     1 
ATOM   9258  C CD1    . LEU D 2 84  ? 57.967  44.046  37.918 1.00 64.89  ? 102 LEU D CD1    1 
ATOM   9259  C CD2    . LEU D 2 84  ? 56.476  45.925  37.278 1.00 56.80  ? 102 LEU D CD2    1 
ATOM   9260  N N      . ALA D 2 85  ? 61.473  48.303  36.992 1.00 62.51  ? 103 ALA D N      1 
ATOM   9261  C CA     . ALA D 2 85  ? 62.537  48.956  37.696 1.00 57.85  ? 103 ALA D CA     1 
ATOM   9262  C C      . ALA D 2 85  ? 62.744  50.331  37.193 1.00 65.45  ? 103 ALA D C      1 
ATOM   9263  O O      . ALA D 2 85  ? 63.207  51.173  37.924 1.00 70.08  ? 103 ALA D O      1 
ATOM   9264  C CB     . ALA D 2 85  ? 63.802  48.168  37.552 1.00 57.97  ? 103 ALA D CB     1 
ATOM   9265  N N      . GLU D 2 86  ? 62.397  50.609  35.955 1.00 68.68  ? 104 GLU D N      1 
ATOM   9266  C CA     . GLU D 2 86  ? 62.534  51.983  35.499 1.00 69.11  ? 104 GLU D CA     1 
ATOM   9267  C C      . GLU D 2 86  ? 61.453  52.882  36.053 1.00 69.81  ? 104 GLU D C      1 
ATOM   9268  O O      . GLU D 2 86  ? 61.726  54.008  36.434 1.00 71.54  ? 104 GLU D O      1 
ATOM   9269  C CB     . GLU D 2 86  ? 62.564  52.051  33.978 1.00 70.06  ? 104 GLU D CB     1 
ATOM   9270  C CG     . GLU D 2 86  ? 63.676  51.235  33.340 1.00 79.16  ? 104 GLU D CG     1 
ATOM   9271  C CD     . GLU D 2 86  ? 65.010  51.956  33.325 1.00 85.38  ? 104 GLU D CD     1 
ATOM   9272  O OE1    . GLU D 2 86  ? 65.021  53.204  33.370 1.00 74.91  ? 104 GLU D OE1    1 
ATOM   9273  O OE2    . GLU D 2 86  ? 66.053  51.273  33.250 1.00 86.56  ? 104 GLU D OE2    1 
ATOM   9274  N N      . VAL D 2 87  ? 60.234  52.380  36.150 1.00 66.63  ? 105 VAL D N      1 
ATOM   9275  C CA     . VAL D 2 87  ? 59.121  53.192  36.608 1.00 63.55  ? 105 VAL D CA     1 
ATOM   9276  C C      . VAL D 2 87  ? 59.145  53.404  38.094 1.00 65.89  ? 105 VAL D C      1 
ATOM   9277  O O      . VAL D 2 87  ? 58.705  54.431  38.579 1.00 63.75  ? 105 VAL D O      1 
ATOM   9278  C CB     . VAL D 2 87  ? 57.813  52.514  36.227 1.00 67.67  ? 105 VAL D CB     1 
ATOM   9279  C CG1    . VAL D 2 87  ? 56.636  53.442  36.458 1.00 72.29  ? 105 VAL D CG1    1 
ATOM   9280  C CG2    . VAL D 2 87  ? 57.845  52.103  34.767 1.00 67.63  ? 105 VAL D CG2    1 
ATOM   9281  N N      . ALA D 2 88  ? 59.674  52.434  38.825 1.00 69.82  ? 106 ALA D N      1 
ATOM   9282  C CA     . ALA D 2 88  ? 59.696  52.487  40.293 1.00 65.37  ? 106 ALA D CA     1 
ATOM   9283  C C      . ALA D 2 88  ? 60.331  53.660  40.992 1.00 67.20  ? 106 ALA D C      1 
ATOM   9284  O O      . ALA D 2 88  ? 59.763  54.174  41.943 1.00 68.35  ? 106 ALA D O      1 
ATOM   9285  C CB     . ALA D 2 88  ? 60.268  51.210  40.857 1.00 59.18  ? 106 ALA D CB     1 
ATOM   9286  N N      . PRO D 2 89  ? 61.557  54.065  40.587 1.00 68.81  ? 107 PRO D N      1 
ATOM   9287  C CA     . PRO D 2 89  ? 62.089  55.184  41.357 1.00 71.43  ? 107 PRO D CA     1 
ATOM   9288  C C      . PRO D 2 89  ? 61.230  56.407  41.344 1.00 62.90  ? 107 PRO D C      1 
ATOM   9289  O O      . PRO D 2 89  ? 61.321  57.215  42.255 1.00 67.37  ? 107 PRO D O      1 
ATOM   9290  C CB     . PRO D 2 89  ? 63.398  55.501  40.643 1.00 74.94  ? 107 PRO D CB     1 
ATOM   9291  C CG     . PRO D 2 89  ? 63.309  54.858  39.314 1.00 73.60  ? 107 PRO D CG     1 
ATOM   9292  C CD     . PRO D 2 89  ? 62.578  53.605  39.626 1.00 66.59  ? 107 PRO D CD     1 
ATOM   9293  N N      . ARG D 2 90  ? 60.369  56.547  40.365 1.00 57.27  ? 108 ARG D N      1 
ATOM   9294  C CA     . ARG D 2 90  ? 59.628  57.778  40.252 1.00 60.57  ? 108 ARG D CA     1 
ATOM   9295  C C      . ARG D 2 90  ? 58.208  57.697  40.729 1.00 63.94  ? 108 ARG D C      1 
ATOM   9296  O O      . ARG D 2 90  ? 57.479  58.672  40.657 1.00 71.24  ? 108 ARG D O      1 
ATOM   9297  C CB     . ARG D 2 90  ? 59.622  58.216  38.796 1.00 62.64  ? 108 ARG D CB     1 
ATOM   9298  C CG     . ARG D 2 90  ? 60.958  58.131  38.088 1.00 66.21  ? 108 ARG D CG     1 
ATOM   9299  C CD     . ARG D 2 90  ? 60.743  58.343  36.602 1.00 68.82  ? 108 ARG D CD     1 
ATOM   9300  N NE     . ARG D 2 90  ? 59.645  57.513  36.121 1.00 74.99  ? 108 ARG D NE     1 
ATOM   9301  C CZ     . ARG D 2 90  ? 59.083  57.630  34.925 1.00 78.94  ? 108 ARG D CZ     1 
ATOM   9302  N NH1    . ARG D 2 90  ? 59.505  58.559  34.078 1.00 80.52  ? 108 ARG D NH1    1 
ATOM   9303  N NH2    . ARG D 2 90  ? 58.087  56.827  34.580 1.00 73.07  ? 108 ARG D NH2    1 
ATOM   9304  N N      . LEU D 2 91  ? 57.798  56.537  41.200 1.00 60.63  ? 109 LEU D N      1 
ATOM   9305  C CA     . LEU D 2 91  ? 56.411  56.359  41.576 1.00 64.09  ? 109 LEU D CA     1 
ATOM   9306  C C      . LEU D 2 91  ? 56.016  57.252  42.717 1.00 67.53  ? 109 LEU D C      1 
ATOM   9307  O O      . LEU D 2 91  ? 56.750  57.380  43.682 1.00 74.33  ? 109 LEU D O      1 
ATOM   9308  C CB     . LEU D 2 91  ? 56.161  54.906  41.938 1.00 59.38  ? 109 LEU D CB     1 
ATOM   9309  C CG     . LEU D 2 91  ? 56.167  53.828  40.869 1.00 60.83  ? 109 LEU D CG     1 
ATOM   9310  C CD1    . LEU D 2 91  ? 56.136  52.483  41.563 1.00 53.93  ? 109 LEU D CD1    1 
ATOM   9311  C CD2    . LEU D 2 91  ? 54.960  53.997  39.969 1.00 65.23  ? 109 LEU D CD2    1 
ATOM   9312  N N      . LYS D 2 92  ? 54.848  57.867  42.627 1.00 65.00  ? 110 LYS D N      1 
ATOM   9313  C CA     . LYS D 2 92  ? 54.367  58.683  43.720 1.00 66.01  ? 110 LYS D CA     1 
ATOM   9314  C C      . LYS D 2 92  ? 52.873  58.588  43.792 1.00 63.64  ? 110 LYS D C      1 
ATOM   9315  O O      . LYS D 2 92  ? 52.238  58.278  42.806 1.00 62.78  ? 110 LYS D O      1 
ATOM   9316  C CB     . LYS D 2 92  ? 54.810  60.125  43.547 1.00 62.17  ? 110 LYS D CB     1 
ATOM   9317  C CG     . LYS D 2 92  ? 54.861  60.934  44.839 1.00 76.98  ? 110 LYS D CG     1 
ATOM   9318  C CD     . LYS D 2 92  ? 53.792  62.021  44.869 1.00 90.81  ? 110 LYS D CD     1 
ATOM   9319  C CE     . LYS D 2 92  ? 53.726  62.717  46.222 1.00 74.91  ? 110 LYS D CE     1 
ATOM   9320  N NZ     . LYS D 2 92  ? 52.613  63.706  46.301 1.00 46.86  ? 110 LYS D NZ     1 
ATOM   9321  N N      . SER D 2 93  ? 52.313  58.826  44.966 1.00 61.74  ? 111 SER D N      1 
ATOM   9322  C CA     . SER D 2 93  ? 50.889  58.731  45.148 1.00 58.26  ? 111 SER D CA     1 
ATOM   9323  C C      . SER D 2 93  ? 50.345  60.082  45.497 1.00 58.16  ? 111 SER D C      1 
ATOM   9324  O O      . SER D 2 93  ? 50.868  60.751  46.361 1.00 62.36  ? 111 SER D O      1 
ATOM   9325  C CB     . SER D 2 93  ? 50.581  57.730  46.247 1.00 53.61  ? 111 SER D CB     1 
ATOM   9326  O OG     . SER D 2 93  ? 51.427  57.928  47.357 1.00 66.61  ? 111 SER D OG     1 
ATOM   9327  N N      . ASN D 2 94  ? 49.308  60.505  44.802 1.00 57.17  ? 112 ASN D N      1 
ATOM   9328  C CA     . ASN D 2 94  ? 48.679  61.778  45.081 1.00 56.15  ? 112 ASN D CA     1 
ATOM   9329  C C      . ASN D 2 94  ? 47.488  61.432  45.899 1.00 55.67  ? 112 ASN D C      1 
ATOM   9330  O O      . ASN D 2 94  ? 46.749  60.530  45.563 1.00 60.63  ? 112 ASN D O      1 
ATOM   9331  C CB     . ASN D 2 94  ? 48.227  62.413  43.775 1.00 57.46  ? 112 ASN D CB     1 
ATOM   9332  C CG     . ASN D 2 94  ? 47.583  63.766  43.960 1.00 59.07  ? 112 ASN D CG     1 
ATOM   9333  O OD1    . ASN D 2 94  ? 47.931  64.518  44.863 1.00 68.67  ? 112 ASN D OD1    1 
ATOM   9334  N ND2    . ASN D 2 94  ? 46.654  64.094  43.075 1.00 59.84  ? 112 ASN D ND2    1 
ATOM   9335  N N      . PRO D 2 95  ? 47.303  62.114  47.043 1.00 53.40  ? 113 PRO D N      1 
ATOM   9336  C CA     . PRO D 2 95  ? 46.171  61.656  47.831 1.00 52.33  ? 113 PRO D CA     1 
ATOM   9337  C C      . PRO D 2 95  ? 44.862  61.728  47.144 1.00 53.03  ? 113 PRO D C      1 
ATOM   9338  O O      . PRO D 2 95  ? 44.070  60.816  47.260 1.00 61.79  ? 113 PRO D O      1 
ATOM   9339  C CB     . PRO D 2 95  ? 46.127  62.659  48.957 1.00 56.99  ? 113 PRO D CB     1 
ATOM   9340  C CG     . PRO D 2 95  ? 47.539  63.002  49.188 1.00 66.40  ? 113 PRO D CG     1 
ATOM   9341  C CD     . PRO D 2 95  ? 48.079  63.127  47.803 1.00 60.21  ? 113 PRO D CD     1 
ATOM   9342  N N      . LYS D 2 96  ? 44.594  62.826  46.475 1.00 50.30  ? 114 LYS D N      1 
ATOM   9343  C CA     . LYS D 2 96  ? 43.297  63.019  45.875 1.00 52.01  ? 114 LYS D CA     1 
ATOM   9344  C C      . LYS D 2 96  ? 43.053  62.060  44.752 1.00 54.16  ? 114 LYS D C      1 
ATOM   9345  O O      . LYS D 2 96  ? 41.948  61.954  44.257 1.00 56.49  ? 114 LYS D O      1 
ATOM   9346  C CB     . LYS D 2 96  ? 43.161  64.451  45.378 1.00 51.09  ? 114 LYS D CB     1 
ATOM   9347  C CG     . LYS D 2 96  ? 42.154  65.284  46.145 1.00 46.86  ? 114 LYS D CG     1 
ATOM   9348  C CD     . LYS D 2 96  ? 40.763  64.676  46.059 1.00 53.78  ? 114 LYS D CD     1 
ATOM   9349  C CE     . LYS D 2 96  ? 39.730  65.538  46.760 1.00 46.02  ? 114 LYS D CE     1 
ATOM   9350  N NZ     . LYS D 2 96  ? 38.395  64.884  46.763 1.00 51.40  ? 114 LYS D NZ     1 
ATOM   9351  N N      . ASP D 2 97  ? 44.077  61.335  44.358 1.00 54.49  ? 115 ASP D N      1 
ATOM   9352  C CA     . ASP D 2 97  ? 43.936  60.433  43.248 1.00 56.43  ? 115 ASP D CA     1 
ATOM   9353  C C      . ASP D 2 97  ? 44.619  59.155  43.590 1.00 60.85  ? 115 ASP D C      1 
ATOM   9354  O O      . ASP D 2 97  ? 45.659  58.847  43.034 1.00 64.41  ? 115 ASP D O      1 
ATOM   9355  C CB     . ASP D 2 97  ? 44.596  61.040  42.033 1.00 63.64  ? 115 ASP D CB     1 
ATOM   9356  C CG     . ASP D 2 97  ? 44.157  60.394  40.741 1.00 85.88  ? 115 ASP D CG     1 
ATOM   9357  O OD1    . ASP D 2 97  ? 42.943  60.396  40.460 1.00 86.32  ? 115 ASP D OD1    1 
ATOM   9358  O OD2    . ASP D 2 97  ? 45.029  59.899  39.995 1.00 90.63  ? 115 ASP D OD2    1 
ATOM   9359  N N      . ASN D 2 98  ? 44.074  58.421  44.546 1.00 59.16  ? 116 ASN D N      1 
ATOM   9360  C CA     . ASN D 2 98  ? 44.622  57.136  44.918 1.00 61.74  ? 116 ASN D CA     1 
ATOM   9361  C C      . ASN D 2 98  ? 43.435  56.284  44.708 1.00 57.37  ? 116 ASN D C      1 
ATOM   9362  O O      . ASN D 2 98  ? 42.915  55.716  45.642 1.00 56.06  ? 116 ASN D O      1 
ATOM   9363  C CB     . ASN D 2 98  ? 45.049  57.111  46.370 1.00 51.48  ? 116 ASN D CB     1 
ATOM   9364  C CG     . ASN D 2 98  ? 46.503  57.453  46.552 1.00 52.51  ? 116 ASN D CG     1 
ATOM   9365  O OD1    . ASN D 2 98  ? 47.328  57.169  45.691 1.00 59.47  ? 116 ASN D OD1    1 
ATOM   9366  N ND2    . ASN D 2 98  ? 46.829  58.055  47.680 1.00 51.32  ? 116 ASN D ND2    1 
ATOM   9367  N N      . GLU D 2 99  ? 42.985  56.199  43.472 1.00 55.42  ? 117 GLU D N      1 
ATOM   9368  C CA     . GLU D 2 99  ? 41.763  55.485  43.159 1.00 52.25  ? 117 GLU D CA     1 
ATOM   9369  C C      . GLU D 2 99  ? 41.716  53.997  43.425 1.00 51.07  ? 117 GLU D C      1 
ATOM   9370  O O      . GLU D 2 99  ? 40.690  53.474  43.822 1.00 51.40  ? 117 GLU D O      1 
ATOM   9371  C CB     . GLU D 2 99  ? 41.444  55.760  41.700 1.00 55.00  ? 117 GLU D CB     1 
ATOM   9372  C CG     . GLU D 2 99  ? 41.017  57.190  41.438 1.00 60.47  ? 117 GLU D CG     1 
ATOM   9373  C CD     . GLU D 2 99  ? 41.182  57.577  39.991 1.00 68.10  ? 117 GLU D CD     1 
ATOM   9374  O OE1    . GLU D 2 99  ? 41.923  56.877  39.279 1.00 74.45  ? 117 GLU D OE1    1 
ATOM   9375  O OE2    . GLU D 2 99  ? 40.584  58.585  39.572 1.00 72.51  ? 117 GLU D OE2    1 
ATOM   9376  N N      . SER D 2 100 ? 42.815  53.302  43.218 1.00 50.48  ? 118 SER D N      1 
ATOM   9377  C CA     . SER D 2 100 ? 42.820  51.878  43.411 1.00 39.83  ? 118 SER D CA     1 
ATOM   9378  C C      . SER D 2 100 ? 42.622  51.623  44.857 1.00 41.47  ? 118 SER D C      1 
ATOM   9379  O O      . SER D 2 100 ? 41.929  50.697  45.234 1.00 36.87  ? 118 SER D O      1 
ATOM   9380  C CB     . SER D 2 100 ? 44.155  51.323  42.978 1.00 34.59  ? 118 SER D CB     1 
ATOM   9381  O OG     . SER D 2 100 ? 45.212  52.011  43.608 1.00 50.74  ? 118 SER D OG     1 
ATOM   9382  N N      . ARG D 2 101 ? 43.236  52.450  45.692 1.00 47.49  ? 119 ARG D N      1 
ATOM   9383  C CA     . ARG D 2 101 ? 43.177  52.259  47.130 1.00 41.83  ? 119 ARG D CA     1 
ATOM   9384  C C      . ARG D 2 101 ? 41.793  52.453  47.644 1.00 36.91  ? 119 ARG D C      1 
ATOM   9385  O O      . ARG D 2 101 ? 41.350  51.738  48.511 1.00 37.29  ? 119 ARG D O      1 
ATOM   9386  C CB     . ARG D 2 101 ? 44.136  53.231  47.778 1.00 39.76  ? 119 ARG D CB     1 
ATOM   9387  C CG     . ARG D 2 101 ? 44.222  53.146  49.284 1.00 44.64  ? 119 ARG D CG     1 
ATOM   9388  C CD     . ARG D 2 101 ? 44.981  51.925  49.744 1.00 41.36  ? 119 ARG D CD     1 
ATOM   9389  N NE     . ARG D 2 101 ? 44.885  51.784  51.184 1.00 31.21  ? 119 ARG D NE     1 
ATOM   9390  C CZ     . ARG D 2 101 ? 45.475  50.825  51.871 1.00 33.72  ? 119 ARG D CZ     1 
ATOM   9391  N NH1    . ARG D 2 101 ? 46.215  49.936  51.244 1.00 41.03  ? 119 ARG D NH1    1 
ATOM   9392  N NH2    . ARG D 2 101 ? 45.328  50.764  53.181 1.00 39.30  ? 119 ARG D NH2    1 
ATOM   9393  N N      . ARG D 2 102 ? 41.079  53.402  47.093 1.00 32.91  ? 120 ARG D N      1 
ATOM   9394  C CA     . ARG D 2 102 ? 39.721  53.636  47.488 1.00 33.09  ? 120 ARG D CA     1 
ATOM   9395  C C      . ARG D 2 102 ? 38.824  52.474  47.181 1.00 35.54  ? 120 ARG D C      1 
ATOM   9396  O O      . ARG D 2 102 ? 37.777  52.345  47.783 1.00 36.11  ? 120 ARG D O      1 
ATOM   9397  C CB     . ARG D 2 102 ? 39.227  54.867  46.780 1.00 43.42  ? 120 ARG D CB     1 
ATOM   9398  C CG     . ARG D 2 102 ? 40.004  56.121  47.132 1.00 40.17  ? 120 ARG D CG     1 
ATOM   9399  C CD     . ARG D 2 102 ? 39.692  57.256  46.177 1.00 37.07  ? 120 ARG D CD     1 
ATOM   9400  N NE     . ARG D 2 102 ? 40.518  58.422  46.450 1.00 36.07  ? 120 ARG D NE     1 
ATOM   9401  C CZ     . ARG D 2 102 ? 40.124  59.460  47.172 1.00 38.96  ? 120 ARG D CZ     1 
ATOM   9402  N NH1    . ARG D 2 102 ? 38.909  59.491  47.684 1.00 35.20  ? 120 ARG D NH1    1 
ATOM   9403  N NH2    . ARG D 2 102 ? 40.941  60.478  47.371 1.00 42.70  ? 120 ARG D NH2    1 
ATOM   9404  N N      . LEU D 2 103 ? 39.187  51.640  46.220 1.00 37.12  ? 121 LEU D N      1 
ATOM   9405  C CA     . LEU D 2 103 ? 38.428  50.433  45.949 1.00 31.13  ? 121 LEU D CA     1 
ATOM   9406  C C      . LEU D 2 103 ? 38.785  49.361  46.946 1.00 32.66  ? 121 LEU D C      1 
ATOM   9407  O O      . LEU D 2 103 ? 37.916  48.700  47.474 1.00 36.34  ? 121 LEU D O      1 
ATOM   9408  C CB     . LEU D 2 103 ? 38.643  49.965  44.528 1.00 25.68  ? 121 LEU D CB     1 
ATOM   9409  C CG     . LEU D 2 103 ? 37.783  48.806  44.064 1.00 28.36  ? 121 LEU D CG     1 
ATOM   9410  C CD1    . LEU D 2 103 ? 36.317  49.185  44.052 1.00 31.21  ? 121 LEU D CD1    1 
ATOM   9411  C CD2    . LEU D 2 103 ? 38.232  48.418  42.680 1.00 40.50  ? 121 LEU D CD2    1 
ATOM   9412  N N      . TYR D 2 104 ? 40.061  49.196  47.233 1.00 29.42  ? 122 TYR D N      1 
ATOM   9413  C CA     . TYR D 2 104 ? 40.491  48.201  48.182 1.00 31.44  ? 122 TYR D CA     1 
ATOM   9414  C C      . TYR D 2 104 ? 39.790  48.500  49.449 1.00 36.11  ? 122 TYR D C      1 
ATOM   9415  O O      . TYR D 2 104 ? 39.155  47.637  50.025 1.00 39.29  ? 122 TYR D O      1 
ATOM   9416  C CB     . TYR D 2 104 ? 41.989  48.321  48.372 1.00 31.66  ? 122 TYR D CB     1 
ATOM   9417  C CG     . TYR D 2 104 ? 42.632  47.387  49.361 1.00 37.20  ? 122 TYR D CG     1 
ATOM   9418  C CD1    . TYR D 2 104 ? 43.062  46.135  48.977 1.00 40.19  ? 122 TYR D CD1    1 
ATOM   9419  C CD2    . TYR D 2 104 ? 42.862  47.779  50.666 1.00 42.16  ? 122 TYR D CD2    1 
ATOM   9420  C CE1    . TYR D 2 104 ? 43.665  45.280  49.873 1.00 52.03  ? 122 TYR D CE1    1 
ATOM   9421  C CE2    . TYR D 2 104 ? 43.464  46.934  51.569 1.00 43.67  ? 122 TYR D CE2    1 
ATOM   9422  C CZ     . TYR D 2 104 ? 43.864  45.686  51.165 1.00 52.87  ? 122 TYR D CZ     1 
ATOM   9423  O OH     . TYR D 2 104 ? 44.466  44.844  52.060 1.00 46.67  ? 122 TYR D OH     1 
ATOM   9424  N N      . GLU D 2 105 ? 39.842  49.745  49.881 1.00 35.61  ? 123 GLU D N      1 
ATOM   9425  C CA     . GLU D 2 105 ? 39.268  50.117  51.164 1.00 36.17  ? 123 GLU D CA     1 
ATOM   9426  C C      . GLU D 2 105 ? 37.768  50.139  51.259 1.00 37.67  ? 123 GLU D C      1 
ATOM   9427  O O      . GLU D 2 105 ? 37.233  49.867  52.309 1.00 46.17  ? 123 GLU D O      1 
ATOM   9428  C CB     . GLU D 2 105 ? 39.805  51.464  51.618 1.00 30.86  ? 123 GLU D CB     1 
ATOM   9429  C CG     . GLU D 2 105 ? 41.298  51.527  51.856 1.00 33.72  ? 123 GLU D CG     1 
ATOM   9430  C CD     . GLU D 2 105 ? 41.669  52.730  52.690 1.00 40.40  ? 123 GLU D CD     1 
ATOM   9431  O OE1    . GLU D 2 105 ? 40.759  53.317  53.299 1.00 41.29  ? 123 GLU D OE1    1 
ATOM   9432  O OE2    . GLU D 2 105 ? 42.857  53.087  52.749 1.00 45.63  ? 123 GLU D OE2    1 
ATOM   9433  N N      . THR D 2 106 ? 37.070  50.472  50.198 1.00 32.19  ? 124 THR D N      1 
ATOM   9434  C CA     . THR D 2 106 ? 35.640  50.420  50.285 1.00 33.27  ? 124 THR D CA     1 
ATOM   9435  C C      . THR D 2 106 ? 35.210  49.005  50.464 1.00 39.21  ? 124 THR D C      1 
ATOM   9436  O O      . THR D 2 106 ? 34.287  48.735  51.211 1.00 42.62  ? 124 THR D O      1 
ATOM   9437  C CB     . THR D 2 106 ? 34.983  50.955  49.034 1.00 39.21  ? 124 THR D CB     1 
ATOM   9438  O OG1    . THR D 2 106 ? 35.209  52.362  48.955 1.00 48.56  ? 124 THR D OG1    1 
ATOM   9439  C CG2    . THR D 2 106 ? 33.491  50.713  49.079 1.00 40.16  ? 124 THR D CG2    1 
ATOM   9440  N N      . LEU D 2 107 ? 35.891  48.085  49.801 1.00 40.97  ? 125 LEU D N      1 
ATOM   9441  C CA     . LEU D 2 107 ? 35.506  46.686  49.863 1.00 38.81  ? 125 LEU D CA     1 
ATOM   9442  C C      . LEU D 2 107 ? 35.952  46.017  51.122 1.00 38.77  ? 125 LEU D C      1 
ATOM   9443  O O      . LEU D 2 107 ? 35.325  45.094  51.603 1.00 40.63  ? 125 LEU D O      1 
ATOM   9444  C CB     . LEU D 2 107 ? 36.081  45.965  48.659 1.00 35.33  ? 125 LEU D CB     1 
ATOM   9445  C CG     . LEU D 2 107 ? 35.489  46.220  47.281 1.00 29.87  ? 125 LEU D CG     1 
ATOM   9446  C CD1    . LEU D 2 107 ? 36.382  45.585  46.230 1.00 28.96  ? 125 LEU D CD1    1 
ATOM   9447  C CD2    . LEU D 2 107 ? 34.092  45.634  47.218 1.00 33.66  ? 125 LEU D CD2    1 
ATOM   9448  N N      . TYR D 2 108 ? 37.054  46.471  51.661 1.00 40.40  ? 126 TYR D N      1 
ATOM   9449  C CA     . TYR D 2 108 ? 37.530  45.913  52.895 1.00 44.60  ? 126 TYR D CA     1 
ATOM   9450  C C      . TYR D 2 108 ? 36.543  46.212  53.992 1.00 44.25  ? 126 TYR D C      1 
ATOM   9451  O O      . TYR D 2 108 ? 36.388  45.438  54.915 1.00 53.65  ? 126 TYR D O      1 
ATOM   9452  C CB     . TYR D 2 108 ? 38.930  46.438  53.193 1.00 39.26  ? 126 TYR D CB     1 
ATOM   9453  C CG     . TYR D 2 108 ? 39.279  46.597  54.641 1.00 46.60  ? 126 TYR D CG     1 
ATOM   9454  C CD1    . TYR D 2 108 ? 39.684  45.513  55.402 1.00 51.55  ? 126 TYR D CD1    1 
ATOM   9455  C CD2    . TYR D 2 108 ? 39.234  47.842  55.242 1.00 51.52  ? 126 TYR D CD2    1 
ATOM   9456  C CE1    . TYR D 2 108 ? 40.009  45.664  56.732 1.00 52.59  ? 126 TYR D CE1    1 
ATOM   9457  C CE2    . TYR D 2 108 ? 39.557  48.003  56.568 1.00 49.96  ? 126 TYR D CE2    1 
ATOM   9458  C CZ     . TYR D 2 108 ? 39.942  46.911  57.304 1.00 51.94  ? 126 TYR D CZ     1 
ATOM   9459  O OH     . TYR D 2 108 ? 40.270  47.083  58.618 1.00 54.35  ? 126 TYR D OH     1 
ATOM   9460  N N      . ALA D 2 109 ? 35.846  47.319  53.885 1.00 34.65  ? 127 ALA D N      1 
ATOM   9461  C CA     . ALA D 2 109 ? 34.908  47.684  54.905 1.00 39.29  ? 127 ALA D CA     1 
ATOM   9462  C C      . ALA D 2 109 ? 33.860  46.635  55.009 1.00 45.56  ? 127 ALA D C      1 
ATOM   9463  O O      . ALA D 2 109 ? 33.462  46.251  56.086 1.00 50.72  ? 127 ALA D O      1 
ATOM   9464  C CB     . ALA D 2 109 ? 34.263  48.978  54.556 1.00 40.84  ? 127 ALA D CB     1 
ATOM   9465  N N      . ASP D 2 110 ? 33.403  46.156  53.875 1.00 46.40  ? 128 ASP D N      1 
ATOM   9466  C CA     . ASP D 2 110 ? 32.388  45.129  53.868 1.00 49.35  ? 128 ASP D CA     1 
ATOM   9467  C C      . ASP D 2 110 ? 32.889  43.840  54.495 1.00 51.01  ? 128 ASP D C      1 
ATOM   9468  O O      . ASP D 2 110 ? 32.172  43.212  55.245 1.00 53.83  ? 128 ASP D O      1 
ATOM   9469  C CB     . ASP D 2 110 ? 31.921  44.872  52.447 1.00 51.94  ? 128 ASP D CB     1 
ATOM   9470  C CG     . ASP D 2 110 ? 31.339  46.098  51.796 1.00 55.55  ? 128 ASP D CG     1 
ATOM   9471  O OD1    . ASP D 2 110 ? 30.858  46.981  52.528 1.00 66.96  ? 128 ASP D OD1    1 
ATOM   9472  O OD2    . ASP D 2 110 ? 31.349  46.174  50.552 1.00 44.07  ? 128 ASP D OD2    1 
ATOM   9473  N N      . HIS D 2 111 ? 34.109  43.425  54.172 1.00 48.72  ? 129 HIS D N      1 
ATOM   9474  C CA     . HIS D 2 111 ? 34.678  42.210  54.746 1.00 45.77  ? 129 HIS D CA     1 
ATOM   9475  C C      . HIS D 2 111 ? 34.723  42.414  56.215 1.00 52.49  ? 129 HIS D C      1 
ATOM   9476  O O      . HIS D 2 111 ? 34.292  41.562  56.972 1.00 56.62  ? 129 HIS D O      1 
ATOM   9477  C CB     . HIS D 2 111 ? 36.085  41.964  54.236 1.00 39.80  ? 129 HIS D CB     1 
ATOM   9478  C CG     . HIS D 2 111 ? 36.622  40.610  54.561 1.00 50.18  ? 129 HIS D CG     1 
ATOM   9479  N ND1    . HIS D 2 111 ? 37.962  40.305  54.479 1.00 53.45  ? 129 HIS D ND1    1 
ATOM   9480  C CD2    . HIS D 2 111 ? 36.001  39.477  54.961 1.00 61.86  ? 129 HIS D CD2    1 
ATOM   9481  C CE1    . HIS D 2 111 ? 38.145  39.043  54.822 1.00 59.71  ? 129 HIS D CE1    1 
ATOM   9482  N NE2    . HIS D 2 111 ? 36.971  38.518  55.118 1.00 67.47  ? 129 HIS D NE2    1 
ATOM   9483  N N      . LEU D 2 112 ? 35.251  43.555  56.635 1.00 48.85  ? 130 LEU D N      1 
ATOM   9484  C CA     . LEU D 2 112 ? 35.373  43.837  58.050 1.00 48.18  ? 130 LEU D CA     1 
ATOM   9485  C C      . LEU D 2 112 ? 34.008  43.906  58.677 1.00 51.22  ? 130 LEU D C      1 
ATOM   9486  O O      . LEU D 2 112 ? 33.816  43.454  59.786 1.00 58.99  ? 130 LEU D O      1 
ATOM   9487  C CB     . LEU D 2 112 ? 36.128  45.130  58.288 1.00 44.35  ? 130 LEU D CB     1 
ATOM   9488  C CG     . LEU D 2 112 ? 36.434  45.560  59.714 1.00 44.87  ? 130 LEU D CG     1 
ATOM   9489  C CD1    . LEU D 2 112 ? 37.328  44.536  60.391 1.00 47.82  ? 130 LEU D CD1    1 
ATOM   9490  C CD2    . LEU D 2 112 ? 37.107  46.917  59.680 1.00 44.85  ? 130 LEU D CD2    1 
ATOM   9491  N N      . GLU D 2 113 ? 33.037  44.421  57.951 1.00 43.17  ? 131 GLU D N      1 
ATOM   9492  C CA     . GLU D 2 113 ? 31.737  44.565  58.536 1.00 47.28  ? 131 GLU D CA     1 
ATOM   9493  C C      . GLU D 2 113 ? 31.097  43.212  58.579 1.00 54.56  ? 131 GLU D C      1 
ATOM   9494  O O      . GLU D 2 113 ? 30.260  42.950  59.426 1.00 60.68  ? 131 GLU D O      1 
ATOM   9495  C CB     . GLU D 2 113 ? 30.883  45.524  57.740 1.00 47.92  ? 131 GLU D CB     1 
ATOM   9496  C CG     . GLU D 2 113 ? 29.653  46.009  58.485 1.00 53.43  ? 131 GLU D CG     1 
ATOM   9497  C CD     . GLU D 2 113 ? 28.782  46.906  57.641 1.00 73.19  ? 131 GLU D CD     1 
ATOM   9498  O OE1    . GLU D 2 113 ? 29.162  47.193  56.489 1.00 82.85  ? 131 GLU D OE1    1 
ATOM   9499  O OE2    . GLU D 2 113 ? 27.714  47.321  58.131 1.00 66.98  ? 131 GLU D OE2    1 
ATOM   9500  N N      . SER D 2 114 ? 31.488  42.334  57.671 1.00 51.20  ? 132 SER D N      1 
ATOM   9501  C CA     . SER D 2 114 ? 30.942  40.989  57.660 1.00 46.62  ? 132 SER D CA     1 
ATOM   9502  C C      . SER D 2 114 ? 31.584  40.173  58.738 1.00 52.49  ? 132 SER D C      1 
ATOM   9503  O O      . SER D 2 114 ? 30.984  39.245  59.248 1.00 58.08  ? 132 SER D O      1 
ATOM   9504  C CB     . SER D 2 114 ? 31.135  40.326  56.318 1.00 45.30  ? 132 SER D CB     1 
ATOM   9505  O OG     . SER D 2 114 ? 30.355  40.972  55.333 1.00 46.94  ? 132 SER D OG     1 
ATOM   9506  N N      . VAL D 2 115 ? 32.819  40.491  59.081 1.00 49.13  ? 133 VAL D N      1 
ATOM   9507  C CA     . VAL D 2 115 ? 33.493  39.788  60.151 1.00 51.63  ? 133 VAL D CA     1 
ATOM   9508  C C      . VAL D 2 115 ? 32.769  40.047  61.444 1.00 54.61  ? 133 VAL D C      1 
ATOM   9509  O O      . VAL D 2 115 ? 32.428  39.123  62.165 1.00 57.83  ? 133 VAL D O      1 
ATOM   9510  C CB     . VAL D 2 115 ? 34.959  40.218  60.258 1.00 43.61  ? 133 VAL D CB     1 
ATOM   9511  C CG1    . VAL D 2 115 ? 35.562  39.788  61.583 1.00 55.97  ? 133 VAL D CG1    1 
ATOM   9512  C CG2    . VAL D 2 115 ? 35.759  39.644  59.105 1.00 42.29  ? 133 VAL D CG2    1 
ATOM   9513  N N      . ILE D 2 116 ? 32.488  41.300  61.719 1.00 46.35  ? 134 ILE D N      1 
ATOM   9514  C CA     . ILE D 2 116 ? 31.851  41.666  62.965 1.00 48.39  ? 134 ILE D CA     1 
ATOM   9515  C C      . ILE D 2 116 ? 30.478  41.065  63.028 1.00 52.12  ? 134 ILE D C      1 
ATOM   9516  O O      . ILE D 2 116 ? 29.974  40.807  64.103 1.00 59.35  ? 134 ILE D O      1 
ATOM   9517  C CB     . ILE D 2 116 ? 31.883  43.184  63.197 1.00 42.96  ? 134 ILE D CB     1 
ATOM   9518  C CG1    . ILE D 2 116 ? 33.331  43.654  63.147 1.00 40.58  ? 134 ILE D CG1    1 
ATOM   9519  C CG2    . ILE D 2 116 ? 31.283  43.561  64.537 1.00 40.89  ? 134 ILE D CG2    1 
ATOM   9520  C CD1    . ILE D 2 116 ? 33.492  45.078  62.695 1.00 32.64  ? 134 ILE D CD1    1 
ATOM   9521  N N      . LYS D 2 117 ? 29.870  40.794  61.896 1.00 50.90  ? 135 LYS D N      1 
ATOM   9522  C CA     . LYS D 2 117 ? 28.531  40.270  61.949 1.00 54.46  ? 135 LYS D CA     1 
ATOM   9523  C C      . LYS D 2 117 ? 28.582  38.957  62.685 1.00 61.34  ? 135 LYS D C      1 
ATOM   9524  O O      . LYS D 2 117 ? 27.809  38.739  63.607 1.00 68.16  ? 135 LYS D O      1 
ATOM   9525  C CB     . LYS D 2 117 ? 27.968  40.066  60.553 1.00 53.36  ? 135 LYS D CB     1 
ATOM   9526  C CG     . LYS D 2 117 ? 27.400  41.310  59.906 1.00 52.64  ? 135 LYS D CG     1 
ATOM   9527  C CD     . LYS D 2 117 ? 26.303  40.951  58.922 1.00 60.38  ? 135 LYS D CD     1 
ATOM   9528  C CE     . LYS D 2 117 ? 25.170  40.209  59.610 1.00 49.87  ? 135 LYS D CE     1 
ATOM   9529  N NZ     . LYS D 2 117 ? 24.528  41.018  60.683 1.00 51.99  ? 135 LYS D NZ     1 
ATOM   9530  N N      . GLN D 2 118 ? 29.482  38.077  62.289 1.00 60.03  ? 136 GLN D N      1 
ATOM   9531  C CA     . GLN D 2 118 ? 29.650  36.783  62.925 1.00 61.88  ? 136 GLN D CA     1 
ATOM   9532  C C      . GLN D 2 118 ? 30.259  36.870  64.300 1.00 65.79  ? 136 GLN D C      1 
ATOM   9533  O O      . GLN D 2 118 ? 29.793  36.216  65.223 1.00 67.73  ? 136 GLN D O      1 
ATOM   9534  C CB     . GLN D 2 118 ? 30.535  35.918  62.042 1.00 57.56  ? 136 GLN D CB     1 
ATOM   9535  C CG     . GLN D 2 118 ? 30.087  35.861  60.594 1.00 61.59  ? 136 GLN D CG     1 
ATOM   9536  C CD     . GLN D 2 118 ? 31.247  35.696  59.633 1.00 71.79  ? 136 GLN D CD     1 
ATOM   9537  O OE1    . GLN D 2 118 ? 32.403  35.650  60.044 1.00 71.17  ? 136 GLN D OE1    1 
ATOM   9538  N NE2    . GLN D 2 118 ? 30.942  35.613  58.346 1.00 66.23  ? 136 GLN D NE2    1 
ATOM   9539  N N      . GLU D 2 119 ? 31.289  37.687  64.451 1.00 62.14  ? 137 GLU D N      1 
ATOM   9540  C CA     . GLU D 2 119 ? 32.008  37.809  65.720 1.00 59.08  ? 137 GLU D CA     1 
ATOM   9541  C C      . GLU D 2 119 ? 31.221  38.367  66.884 1.00 59.36  ? 137 GLU D C      1 
ATOM   9542  O O      . GLU D 2 119 ? 31.401  37.946  68.014 1.00 60.15  ? 137 GLU D O      1 
ATOM   9543  C CB     . GLU D 2 119 ? 33.283  38.619  65.498 1.00 58.24  ? 137 GLU D CB     1 
ATOM   9544  C CG     . GLU D 2 119 ? 34.202  38.762  66.694 1.00 67.06  ? 137 GLU D CG     1 
ATOM   9545  C CD     . GLU D 2 119 ? 35.330  39.745  66.444 1.00 71.49  ? 137 GLU D CD     1 
ATOM   9546  O OE1    . GLU D 2 119 ? 35.384  40.325  65.342 1.00 67.94  ? 137 GLU D OE1    1 
ATOM   9547  O OE2    . GLU D 2 119 ? 36.165  39.942  67.351 1.00 70.85  ? 137 GLU D OE2    1 
ATOM   9548  N N      . SER D 2 120 ? 30.353  39.323  66.635 1.00 58.35  ? 138 SER D N      1 
ATOM   9549  C CA     . SER D 2 120 ? 29.664  39.979  67.731 1.00 57.93  ? 138 SER D CA     1 
ATOM   9550  C C      . SER D 2 120 ? 28.279  39.541  68.145 1.00 56.57  ? 138 SER D C      1 
ATOM   9551  O O      . SER D 2 120 ? 27.418  39.331  67.308 1.00 60.70  ? 138 SER D O      1 
ATOM   9552  C CB     . SER D 2 120 ? 29.612  41.477  67.436 1.00 58.31  ? 138 SER D CB     1 
ATOM   9553  O OG     . SER D 2 120 ? 29.212  42.216  68.572 1.00 53.85  ? 138 SER D OG     1 
ATOM   9554  N N      . ASP D 2 121 ? 28.060  39.393  69.436 1.00 56.45  ? 139 ASP D N      1 
ATOM   9555  C CA     . ASP D 2 121 ? 26.741  39.121  69.963 1.00 51.57  ? 139 ASP D CA     1 
ATOM   9556  C C      . ASP D 2 121 ? 26.065  40.427  70.147 1.00 55.04  ? 139 ASP D C      1 
ATOM   9557  O O      . ASP D 2 121 ? 25.032  40.502  70.806 1.00 50.51  ? 139 ASP D O      1 
ATOM   9558  C CB     . ASP D 2 121 ? 26.797  38.360  71.295 1.00 62.66  ? 139 ASP D CB     1 
ATOM   9559  C CG     . ASP D 2 121 ? 27.881  38.862  72.256 1.00 61.01  ? 139 ASP D CG     1 
ATOM   9560  O OD1    . ASP D 2 121 ? 28.790  39.616  71.861 1.00 63.16  ? 139 ASP D OD1    1 
ATOM   9561  O OD2    . ASP D 2 121 ? 27.828  38.471  73.440 1.00 48.28  ? 139 ASP D OD2    1 
ATOM   9562  N N      . LEU D 2 122 ? 26.657  41.469  69.585 1.00 59.63  ? 140 LEU D N      1 
ATOM   9563  C CA     . LEU D 2 122 ? 26.111  42.805  69.713 1.00 56.54  ? 140 LEU D CA     1 
ATOM   9564  C C      . LEU D 2 122 ? 25.879  43.104  71.160 1.00 55.51  ? 140 LEU D C      1 
ATOM   9565  O O      . LEU D 2 122 ? 24.951  43.812  71.508 1.00 57.59  ? 140 LEU D O      1 
ATOM   9566  C CB     . LEU D 2 122 ? 24.862  42.971  68.862 1.00 54.73  ? 140 LEU D CB     1 
ATOM   9567  C CG     . LEU D 2 122 ? 25.113  42.642  67.396 1.00 51.62  ? 140 LEU D CG     1 
ATOM   9568  C CD1    . LEU D 2 122 ? 23.838  42.762  66.594 1.00 51.48  ? 140 LEU D CD1    1 
ATOM   9569  C CD2    . LEU D 2 122 ? 26.184  43.557  66.838 1.00 49.98  ? 140 LEU D CD2    1 
ATOM   9570  N N      . SER D 2 123 ? 26.727  42.556  72.010 1.00 52.21  ? 141 SER D N      1 
ATOM   9571  C CA     . SER D 2 123 ? 26.644  42.833  73.424 1.00 54.25  ? 141 SER D CA     1 
ATOM   9572  C C      . SER D 2 123 ? 27.255  44.136  73.753 1.00 50.72  ? 141 SER D C      1 
ATOM   9573  O O      . SER D 2 123 ? 26.682  44.919  74.481 1.00 46.41  ? 141 SER D O      1 
ATOM   9574  C CB     . SER D 2 123 ? 27.410  41.774  74.184 1.00 51.42  ? 141 SER D CB     1 
ATOM   9575  O OG     . SER D 2 123 ? 28.750  41.702  73.748 1.00 54.23  ? 141 SER D OG     1 
ATOM   9576  N N      . VAL D 2 124 ? 28.439  44.384  73.235 1.00 47.87  ? 142 VAL D N      1 
ATOM   9577  C CA     . VAL D 2 124 ? 29.148  45.578  73.612 1.00 42.69  ? 142 VAL D CA     1 
ATOM   9578  C C      . VAL D 2 124 ? 28.390  46.817  73.282 1.00 45.87  ? 142 VAL D C      1 
ATOM   9579  O O      . VAL D 2 124 ? 28.378  47.757  74.037 1.00 42.86  ? 142 VAL D O      1 
ATOM   9580  C CB     . VAL D 2 124 ? 30.524  45.601  72.973 1.00 41.54  ? 142 VAL D CB     1 
ATOM   9581  C CG1    . VAL D 2 124 ? 30.467  45.411  71.472 1.00 50.60  ? 142 VAL D CG1    1 
ATOM   9582  C CG2    . VAL D 2 124 ? 31.270  46.839  73.368 1.00 37.74  ? 142 VAL D CG2    1 
ATOM   9583  N N      . PHE D 2 125 ? 27.676  46.809  72.181 1.00 50.18  ? 143 PHE D N      1 
ATOM   9584  C CA     . PHE D 2 125 ? 27.008  48.010  71.753 1.00 48.21  ? 143 PHE D CA     1 
ATOM   9585  C C      . PHE D 2 125 ? 25.811  48.254  72.626 1.00 53.93  ? 143 PHE D C      1 
ATOM   9586  O O      . PHE D 2 125 ? 25.449  49.393  72.862 1.00 50.17  ? 143 PHE D O      1 
ATOM   9587  C CB     . PHE D 2 125 ? 26.641  47.905  70.286 1.00 42.48  ? 143 PHE D CB     1 
ATOM   9588  C CG     . PHE D 2 125 ? 27.797  47.585  69.399 1.00 40.60  ? 143 PHE D CG     1 
ATOM   9589  C CD1    . PHE D 2 125 ? 28.812  48.492  69.222 1.00 36.25  ? 143 PHE D CD1    1 
ATOM   9590  C CD2    . PHE D 2 125 ? 27.861  46.380  68.739 1.00 49.93  ? 143 PHE D CD2    1 
ATOM   9591  C CE1    . PHE D 2 125 ? 29.877  48.202  68.406 1.00 39.30  ? 143 PHE D CE1    1 
ATOM   9592  C CE2    . PHE D 2 125 ? 28.924  46.081  67.921 1.00 46.83  ? 143 PHE D CE2    1 
ATOM   9593  C CZ     . PHE D 2 125 ? 29.936  46.995  67.755 1.00 36.75  ? 143 PHE D CZ     1 
ATOM   9594  N N      . ASN D 2 126 ? 25.217  47.200  73.169 1.00 58.09  ? 144 ASN D N      1 
ATOM   9595  C CA     . ASN D 2 126 ? 24.084  47.360  74.081 1.00 54.22  ? 144 ASN D CA     1 
ATOM   9596  C C      . ASN D 2 126 ? 24.592  47.775  75.439 1.00 54.33  ? 144 ASN D C      1 
ATOM   9597  O O      . ASN D 2 126 ? 23.814  48.142  76.308 1.00 50.92  ? 144 ASN D O      1 
ATOM   9598  C CB     . ASN D 2 126 ? 23.290  46.078  74.174 1.00 49.48  ? 144 ASN D CB     1 
ATOM   9599  C CG     . ASN D 2 126 ? 22.237  45.969  73.109 1.00 54.73  ? 144 ASN D CG     1 
ATOM   9600  O OD1    . ASN D 2 126 ? 21.273  46.724  73.103 1.00 60.54  ? 144 ASN D OD1    1 
ATOM   9601  N ND2    . ASN D 2 126 ? 22.401  45.012  72.213 1.00 55.39  ? 144 ASN D ND2    1 
ATOM   9602  N N      . GLU D 2 127 ? 25.902  47.702  75.633 1.00 56.43  ? 145 GLU D N      1 
ATOM   9603  C CA     . GLU D 2 127 ? 26.510  48.129  76.885 1.00 51.23  ? 145 GLU D CA     1 
ATOM   9604  C C      . GLU D 2 127 ? 27.248  49.443  76.725 1.00 50.28  ? 145 GLU D C      1 
ATOM   9605  O O      . GLU D 2 127 ? 27.575  50.080  77.712 1.00 47.11  ? 145 GLU D O      1 
ATOM   9606  C CB     . GLU D 2 127 ? 27.485  47.064  77.373 1.00 53.41  ? 145 GLU D CB     1 
ATOM   9607  C CG     . GLU D 2 127 ? 26.858  45.715  77.674 1.00 55.55  ? 145 GLU D CG     1 
ATOM   9608  C CD     . GLU D 2 127 ? 27.893  44.655  77.975 1.00 56.28  ? 145 GLU D CD     1 
ATOM   9609  O OE1    . GLU D 2 127 ? 29.097  44.943  77.834 1.00 52.53  ? 145 GLU D OE1    1 
ATOM   9610  O OE2    . GLU D 2 127 ? 27.502  43.533  78.351 1.00 55.81  ? 145 GLU D OE2    1 
ATOM   9611  N N      . LEU D 2 128 ? 27.526  49.845  75.488 1.00 45.06  ? 146 LEU D N      1 
ATOM   9612  C CA     . LEU D 2 128 ? 28.191  51.110  75.234 1.00 40.71  ? 146 LEU D CA     1 
ATOM   9613  C C      . LEU D 2 128 ? 27.122  52.152  75.201 1.00 43.43  ? 146 LEU D C      1 
ATOM   9614  O O      . LEU D 2 128 ? 27.394  53.340  75.195 1.00 44.00  ? 146 LEU D O      1 
ATOM   9615  C CB     . LEU D 2 128 ? 28.931  51.078  73.916 1.00 31.64  ? 146 LEU D CB     1 
ATOM   9616  C CG     . LEU D 2 128 ? 29.851  52.231  73.571 1.00 29.02  ? 146 LEU D CG     1 
ATOM   9617  C CD1    . LEU D 2 128 ? 30.916  52.324  74.634 1.00 38.44  ? 146 LEU D CD1    1 
ATOM   9618  C CD2    . LEU D 2 128 ? 30.477  51.986  72.219 1.00 31.03  ? 146 LEU D CD2    1 
ATOM   9619  N N      . ARG D 2 129 ? 25.884  51.712  75.195 1.00 46.91  ? 147 ARG D N      1 
ATOM   9620  C CA     . ARG D 2 129 ? 24.781  52.629  75.151 1.00 45.00  ? 147 ARG D CA     1 
ATOM   9621  C C      . ARG D 2 129 ? 24.787  53.459  76.392 1.00 46.35  ? 147 ARG D C      1 
ATOM   9622  O O      . ARG D 2 129 ? 24.606  54.657  76.346 1.00 51.58  ? 147 ARG D O      1 
ATOM   9623  C CB     . ARG D 2 129 ? 23.502  51.822  75.042 1.00 50.78  ? 147 ARG D CB     1 
ATOM   9624  C CG     . ARG D 2 129 ? 22.299  52.560  74.518 1.00 58.86  ? 147 ARG D CG     1 
ATOM   9625  C CD     . ARG D 2 129 ? 21.167  51.586  74.241 1.00 57.13  ? 147 ARG D CD     1 
ATOM   9626  N NE     . ARG D 2 129 ? 20.987  50.634  75.330 1.00 49.84  ? 147 ARG D NE     1 
ATOM   9627  C CZ     . ARG D 2 129 ? 20.240  50.854  76.406 1.00 62.40  ? 147 ARG D CZ     1 
ATOM   9628  N NH1    . ARG D 2 129 ? 19.601  52.002  76.556 1.00 61.01  ? 147 ARG D NH1    1 
ATOM   9629  N NH2    . ARG D 2 129 ? 20.142  49.923  77.339 1.00 64.16  ? 147 ARG D NH2    1 
ATOM   9630  N N      . ASP D 2 130 ? 25.019  52.823  77.514 1.00 45.09  ? 148 ASP D N      1 
ATOM   9631  C CA     . ASP D 2 130 ? 25.030  53.539  78.761 1.00 47.90  ? 148 ASP D CA     1 
ATOM   9632  C C      . ASP D 2 130 ? 26.146  54.549  78.858 1.00 48.99  ? 148 ASP D C      1 
ATOM   9633  O O      . ASP D 2 130 ? 25.950  55.628  79.388 1.00 51.12  ? 148 ASP D O      1 
ATOM   9634  C CB     . ASP D 2 130 ? 25.079  52.583  79.932 1.00 48.63  ? 148 ASP D CB     1 
ATOM   9635  C CG     . ASP D 2 130 ? 23.724  52.009  80.269 1.00 65.07  ? 148 ASP D CG     1 
ATOM   9636  O OD1    . ASP D 2 130 ? 23.273  51.082  79.566 1.00 60.40  ? 148 ASP D OD1    1 
ATOM   9637  O OD2    . ASP D 2 130 ? 23.112  52.482  81.247 1.00 69.44  ? 148 ASP D OD2    1 
ATOM   9638  N N      . SER D 2 131 ? 27.326  54.214  78.378 1.00 46.32  ? 149 SER D N      1 
ATOM   9639  C CA     . SER D 2 131 ? 28.394  55.169  78.385 1.00 41.88  ? 149 SER D CA     1 
ATOM   9640  C C      . SER D 2 131 ? 28.055  56.362  77.497 1.00 54.44  ? 149 SER D C      1 
ATOM   9641  O O      . SER D 2 131 ? 28.340  57.484  77.868 1.00 54.62  ? 149 SER D O      1 
ATOM   9642  C CB     . SER D 2 131 ? 29.680  54.509  77.959 1.00 34.68  ? 149 SER D CB     1 
ATOM   9643  O OG     . SER D 2 131 ? 29.912  53.339  78.712 1.00 43.80  ? 149 SER D OG     1 
ATOM   9644  N N      . TYR D 2 132 ? 27.459  56.154  76.328 1.00 46.22  ? 150 TYR D N      1 
ATOM   9645  C CA     . TYR D 2 132 ? 27.046  57.282  75.501 1.00 38.09  ? 150 TYR D CA     1 
ATOM   9646  C C      . TYR D 2 132 ? 25.988  58.084  76.138 1.00 44.70  ? 150 TYR D C      1 
ATOM   9647  O O      . TYR D 2 132 ? 26.040  59.283  76.107 1.00 58.88  ? 150 TYR D O      1 
ATOM   9648  C CB     . TYR D 2 132 ? 26.529  56.847  74.157 1.00 46.32  ? 150 TYR D CB     1 
ATOM   9649  C CG     . TYR D 2 132 ? 25.727  57.879  73.391 1.00 48.41  ? 150 TYR D CG     1 
ATOM   9650  C CD1    . TYR D 2 132 ? 26.345  58.937  72.752 1.00 49.28  ? 150 TYR D CD1    1 
ATOM   9651  C CD2    . TYR D 2 132 ? 24.353  57.776  73.286 1.00 42.10  ? 150 TYR D CD2    1 
ATOM   9652  C CE1    . TYR D 2 132 ? 25.613  59.869  72.050 1.00 43.96  ? 150 TYR D CE1    1 
ATOM   9653  C CE2    . TYR D 2 132 ? 23.616  58.704  72.592 1.00 39.50  ? 150 TYR D CE2    1 
ATOM   9654  C CZ     . TYR D 2 132 ? 24.253  59.747  71.977 1.00 44.16  ? 150 TYR D CZ     1 
ATOM   9655  O OH     . TYR D 2 132 ? 23.524  60.672  71.281 1.00 67.97  ? 150 TYR D OH     1 
ATOM   9656  N N      . ASN D 2 133 ? 25.034  57.440  76.766 1.00 40.32  ? 151 ASN D N      1 
ATOM   9657  C CA     . ASN D 2 133 ? 23.928  58.161  77.340 1.00 46.92  ? 151 ASN D CA     1 
ATOM   9658  C C      . ASN D 2 133 ? 24.400  58.997  78.501 1.00 47.24  ? 151 ASN D C      1 
ATOM   9659  O O      . ASN D 2 133 ? 23.651  59.790  79.040 1.00 45.92  ? 151 ASN D O      1 
ATOM   9660  C CB     . ASN D 2 133 ? 22.844  57.222  77.804 1.00 51.18  ? 151 ASN D CB     1 
ATOM   9661  C CG     . ASN D 2 133 ? 22.078  56.608  76.665 1.00 59.32  ? 151 ASN D CG     1 
ATOM   9662  O OD1    . ASN D 2 133 ? 22.378  56.848  75.505 1.00 57.53  ? 151 ASN D OD1    1 
ATOM   9663  N ND2    . ASN D 2 133 ? 21.080  55.805  76.993 1.00 70.94  ? 151 ASN D ND2    1 
ATOM   9664  N N      . ALA D 2 134 ? 25.617  58.774  78.942 1.00 42.05  ? 152 ALA D N      1 
ATOM   9665  C CA     . ALA D 2 134 ? 26.158  59.538  80.033 1.00 42.60  ? 152 ALA D CA     1 
ATOM   9666  C C      . ALA D 2 134 ? 26.992  60.675  79.578 1.00 47.62  ? 152 ALA D C      1 
ATOM   9667  O O      . ALA D 2 134 ? 26.864  61.777  80.081 1.00 59.12  ? 152 ALA D O      1 
ATOM   9668  C CB     . ALA D 2 134 ? 27.009  58.649  80.881 1.00 49.05  ? 152 ALA D CB     1 
ATOM   9669  N N      . VAL D 2 135 ? 27.889  60.405  78.651 1.00 48.54  ? 153 VAL D N      1 
ATOM   9670  C CA     . VAL D 2 135 ? 28.776  61.444  78.151 1.00 54.60  ? 153 VAL D CA     1 
ATOM   9671  C C      . VAL D 2 135 ? 28.088  62.266  77.077 1.00 53.72  ? 153 VAL D C      1 
ATOM   9672  O O      . VAL D 2 135 ? 28.677  63.176  76.526 1.00 53.22  ? 153 VAL D O      1 
ATOM   9673  C CB     . VAL D 2 135 ? 30.080  60.834  77.624 1.00 50.32  ? 153 VAL D CB     1 
ATOM   9674  C CG1    . VAL D 2 135 ? 30.785  60.068  78.726 1.00 39.39  ? 153 VAL D CG1    1 
ATOM   9675  C CG2    . VAL D 2 135 ? 29.806  59.925  76.443 1.00 59.07  ? 153 VAL D CG2    1 
ATOM   9676  N N      . LYS D 2 136 ? 26.832  61.937  76.815 1.00 54.13  ? 154 LYS D N      1 
ATOM   9677  C CA     . LYS D 2 136 ? 26.087  62.631  75.805 1.00 47.53  ? 154 LYS D CA     1 
ATOM   9678  C C      . LYS D 2 136 ? 25.974  64.048  76.234 1.00 57.40  ? 154 LYS D C      1 
ATOM   9679  O O      . LYS D 2 136 ? 25.824  64.331  77.420 1.00 65.09  ? 154 LYS D O      1 
ATOM   9680  C CB     . LYS D 2 136 ? 24.694  62.048  75.610 1.00 47.24  ? 154 LYS D CB     1 
ATOM   9681  C CG     . LYS D 2 136 ? 23.727  62.233  76.757 1.00 55.91  ? 154 LYS D CG     1 
ATOM   9682  C CD     . LYS D 2 136 ? 22.307  62.274  76.239 1.00 55.12  ? 154 LYS D CD     1 
ATOM   9683  C CE     . LYS D 2 136 ? 21.423  63.030  77.205 1.00 44.36  ? 154 LYS D CE     1 
ATOM   9684  N NZ     . LYS D 2 136 ? 20.075  63.262  76.626 1.00 51.40  ? 154 LYS D NZ     1 
ATOM   9685  N N      . PRO D 2 137 ? 26.074  64.984  75.281 1.00 59.13  ? 155 PRO D N      1 
ATOM   9686  C CA     . PRO D 2 137 ? 25.883  66.305  75.807 1.00 55.58  ? 155 PRO D CA     1 
ATOM   9687  C C      . PRO D 2 137 ? 24.402  66.401  75.944 1.00 59.41  ? 155 PRO D C      1 
ATOM   9688  O O      . PRO D 2 137 ? 23.667  65.649  75.335 1.00 62.74  ? 155 PRO D O      1 
ATOM   9689  C CB     . PRO D 2 137 ? 26.417  67.189  74.706 1.00 52.06  ? 155 PRO D CB     1 
ATOM   9690  C CG     . PRO D 2 137 ? 27.149  66.295  73.770 1.00 62.21  ? 155 PRO D CG     1 
ATOM   9691  C CD     . PRO D 2 137 ? 26.375  65.034  73.850 1.00 65.29  ? 155 PRO D CD     1 
ATOM   9692  N N      . GLU D 2 138 ? 23.932  67.322  76.739 1.00 61.16  ? 156 GLU D N      1 
ATOM   9693  C CA     . GLU D 2 138 ? 22.527  67.380  76.990 1.00 69.20  ? 156 GLU D CA     1 
ATOM   9694  C C      . GLU D 2 138 ? 21.733  67.560  75.729 1.00 62.23  ? 156 GLU D C      1 
ATOM   9695  O O      . GLU D 2 138 ? 20.569  67.200  75.676 1.00 62.25  ? 156 GLU D O      1 
ATOM   9696  C CB     . GLU D 2 138 ? 22.262  68.507  77.979 1.00 84.50  ? 156 GLU D CB     1 
ATOM   9697  C CG     . GLU D 2 138 ? 21.089  68.243  78.909 1.00 102.28 ? 156 GLU D CG     1 
ATOM   9698  C CD     . GLU D 2 138 ? 21.249  66.960  79.701 1.00 104.65 ? 156 GLU D CD     1 
ATOM   9699  O OE1    . GLU D 2 138 ? 22.327  66.751  80.296 1.00 101.00 ? 156 GLU D OE1    1 
ATOM   9700  O OE2    . GLU D 2 138 ? 20.287  66.164  79.738 1.00 98.67  ? 156 GLU D OE2    1 
ATOM   9701  N N      . TYR D 2 139 ? 22.315  68.181  74.716 1.00 58.71  ? 157 TYR D N      1 
ATOM   9702  C CA     . TYR D 2 139 ? 21.554  68.468  73.508 1.00 58.59  ? 157 TYR D CA     1 
ATOM   9703  C C      . TYR D 2 139 ? 21.259  67.220  72.737 1.00 54.77  ? 157 TYR D C      1 
ATOM   9704  O O      . TYR D 2 139 ? 20.402  67.212  71.861 1.00 51.12  ? 157 TYR D O      1 
ATOM   9705  C CB     . TYR D 2 139 ? 22.236  69.519  72.627 1.00 53.14  ? 157 TYR D CB     1 
ATOM   9706  C CG     . TYR D 2 139 ? 23.697  69.352  72.335 1.00 52.40  ? 157 TYR D CG     1 
ATOM   9707  C CD1    . TYR D 2 139 ? 24.128  68.497  71.346 1.00 56.49  ? 157 TYR D CD1    1 
ATOM   9708  C CD2    . TYR D 2 139 ? 24.643  70.106  73.004 1.00 53.83  ? 157 TYR D CD2    1 
ATOM   9709  C CE1    . TYR D 2 139 ? 25.463  68.362  71.059 1.00 59.31  ? 157 TYR D CE1    1 
ATOM   9710  C CE2    . TYR D 2 139 ? 25.985  69.978  72.722 1.00 55.43  ? 157 TYR D CE2    1 
ATOM   9711  C CZ     . TYR D 2 139 ? 26.387  69.100  71.747 1.00 59.26  ? 157 TYR D CZ     1 
ATOM   9712  O OH     . TYR D 2 139 ? 27.719  68.961  71.458 1.00 53.98  ? 157 TYR D OH     1 
ATOM   9713  N N      . ALA D 2 140 ? 21.968  66.157  73.064 1.00 51.30  ? 158 ALA D N      1 
ATOM   9714  C CA     . ALA D 2 140 ? 21.799  64.905  72.368 1.00 52.91  ? 158 ALA D CA     1 
ATOM   9715  C C      . ALA D 2 140 ? 20.677  64.052  72.889 1.00 53.21  ? 158 ALA D C      1 
ATOM   9716  O O      . ALA D 2 140 ? 20.080  64.359  73.907 1.00 56.55  ? 158 ALA D O      1 
ATOM   9717  C CB     . ALA D 2 140 ? 23.094  64.139  72.363 1.00 49.09  ? 158 ALA D CB     1 
ATOM   9718  N N      . VAL D 2 141 ? 20.382  62.977  72.181 1.00 51.52  ? 159 VAL D N      1 
ATOM   9719  C CA     . VAL D 2 141 ? 19.284  62.131  72.567 1.00 50.54  ? 159 VAL D CA     1 
ATOM   9720  C C      . VAL D 2 141 ? 19.779  60.793  73.065 1.00 51.86  ? 159 VAL D C      1 
ATOM   9721  O O      . VAL D 2 141 ? 20.702  60.218  72.506 1.00 48.47  ? 159 VAL D O      1 
ATOM   9722  C CB     . VAL D 2 141 ? 18.309  61.985  71.396 1.00 55.35  ? 159 VAL D CB     1 
ATOM   9723  C CG1    . VAL D 2 141 ? 19.009  61.475  70.148 1.00 57.93  ? 159 VAL D CG1    1 
ATOM   9724  C CG2    . VAL D 2 141 ? 17.109  61.133  71.766 1.00 49.80  ? 159 VAL D CG2    1 
ATOM   9725  N N      . THR D 2 142 ? 19.210  60.317  74.158 1.00 53.01  ? 160 THR D N      1 
ATOM   9726  C CA     . THR D 2 142 ? 19.626  59.065  74.733 1.00 59.79  ? 160 THR D CA     1 
ATOM   9727  C C      . THR D 2 142 ? 19.231  57.941  73.836 1.00 63.55  ? 160 THR D C      1 
ATOM   9728  O O      . THR D 2 142 ? 18.241  58.045  73.131 1.00 72.18  ? 160 THR D O      1 
ATOM   9729  C CB     . THR D 2 142 ? 18.885  58.836  76.034 1.00 59.37  ? 160 THR D CB     1 
ATOM   9730  O OG1    . THR D 2 142 ? 17.478  58.931  75.793 1.00 70.53  ? 160 THR D OG1    1 
ATOM   9731  C CG2    . THR D 2 142 ? 19.272  59.870  77.059 1.00 64.18  ? 160 THR D CG2    1 
ATOM   9732  N N      . HIS D 2 143 ? 19.976  56.849  73.848 1.00 53.58  ? 161 HIS D N      1 
ATOM   9733  C CA     . HIS D 2 143 ? 19.556  55.712  73.074 1.00 58.50  ? 161 HIS D CA     1 
ATOM   9734  C C      . HIS D 2 143 ? 18.945  54.820  74.092 1.00 66.53  ? 161 HIS D C      1 
ATOM   9735  O O      . HIS D 2 143 ? 19.589  54.457  75.054 1.00 71.04  ? 161 HIS D O      1 
ATOM   9736  C CB     . HIS D 2 143 ? 20.738  55.032  72.431 1.00 54.27  ? 161 HIS D CB     1 
ATOM   9737  C CG     . HIS D 2 143 ? 20.388  54.242  71.210 1.00 63.79  ? 161 HIS D CG     1 
ATOM   9738  N ND1    . HIS D 2 143 ? 19.939  52.942  71.267 1.00 66.91  ? 161 HIS D ND1    1 
ATOM   9739  C CD2    . HIS D 2 143 ? 20.419  54.574  69.899 1.00 64.31  ? 161 HIS D CD2    1 
ATOM   9740  C CE1    . HIS D 2 143 ? 19.708  52.506  70.043 1.00 70.27  ? 161 HIS D CE1    1 
ATOM   9741  N NE2    . HIS D 2 143 ? 19.990  53.477  69.193 1.00 67.98  ? 161 HIS D NE2    1 
ATOM   9742  N N      . GLU D 2 144 ? 17.688  54.470  73.915 1.00 71.03  ? 162 GLU D N      1 
ATOM   9743  C CA     . GLU D 2 144 ? 17.018  53.677  74.923 1.00 77.49  ? 162 GLU D CA     1 
ATOM   9744  C C      . GLU D 2 144 ? 16.447  52.414  74.320 1.00 80.92  ? 162 GLU D C      1 
ATOM   9745  O O      . GLU D 2 144 ? 15.990  51.538  75.046 1.00 80.37  ? 162 GLU D O      1 
ATOM   9746  C CB     . GLU D 2 144 ? 15.931  54.489  75.599 1.00 77.65  ? 162 GLU D CB     1 
ATOM   9747  C CG     . GLU D 2 144 ? 15.982  54.449  77.115 1.00 84.47  ? 162 GLU D CG     1 
ATOM   9748  C CD     . GLU D 2 144 ? 17.046  55.363  77.682 1.00 95.31  ? 162 GLU D CD     1 
ATOM   9749  O OE1    . GLU D 2 144 ? 16.746  56.557  77.887 1.00 90.98  ? 162 GLU D OE1    1 
ATOM   9750  O OE2    . GLU D 2 144 ? 18.177  54.891  77.927 1.00 97.23  ? 162 GLU D OE2    1 
ATOM   9751  N N      . THR D 2 145 ? 16.457  52.312  72.998 1.00 74.50  ? 163 THR D N      1 
ATOM   9752  C CA     . THR D 2 145 ? 16.014  51.095  72.340 1.00 70.29  ? 163 THR D CA     1 
ATOM   9753  C C      . THR D 2 145 ? 17.127  50.065  72.225 1.00 73.43  ? 163 THR D C      1 
ATOM   9754  O O      . THR D 2 145 ? 18.293  50.417  72.155 1.00 73.68  ? 163 THR D O      1 
ATOM   9755  C CB     . THR D 2 145 ? 15.466  51.408  70.954 1.00 73.69  ? 163 THR D CB     1 
ATOM   9756  O OG1    . THR D 2 145 ? 16.499  51.994  70.157 1.00 78.33  ? 163 THR D OG1    1 
ATOM   9757  C CG2    . THR D 2 145 ? 14.311  52.384  71.057 1.00 74.15  ? 163 THR D CG2    1 
ATOM   9758  N N      . GLU D 2 146 ? 16.782  48.790  72.200 1.00 68.69  ? 164 GLU D N      1 
ATOM   9759  C CA     . GLU D 2 146 ? 17.779  47.731  72.142 1.00 62.95  ? 164 GLU D CA     1 
ATOM   9760  C C      . GLU D 2 146 ? 18.477  47.668  70.822 1.00 65.50  ? 164 GLU D C      1 
ATOM   9761  O O      . GLU D 2 146 ? 17.846  47.684  69.779 1.00 69.45  ? 164 GLU D O      1 
ATOM   9762  C CB     . GLU D 2 146 ? 17.097  46.391  72.385 1.00 69.49  ? 164 GLU D CB     1 
ATOM   9763  C CG     . GLU D 2 146 ? 17.906  45.157  72.019 1.00 69.74  ? 164 GLU D CG     1 
ATOM   9764  C CD     . GLU D 2 146 ? 18.581  44.516  73.209 1.00 68.06  ? 164 GLU D CD     1 
ATOM   9765  O OE1    . GLU D 2 146 ? 18.506  45.083  74.316 1.00 69.51  ? 164 GLU D OE1    1 
ATOM   9766  O OE2    . GLU D 2 146 ? 19.186  43.441  73.037 1.00 60.73  ? 164 GLU D OE2    1 
ATOM   9767  N N      . ILE D 2 147 ? 19.789  47.537  70.860 1.00 58.51  ? 165 ILE D N      1 
ATOM   9768  C CA     . ILE D 2 147 ? 20.567  47.455  69.650 1.00 57.89  ? 165 ILE D CA     1 
ATOM   9769  C C      . ILE D 2 147 ? 20.685  46.011  69.229 1.00 57.02  ? 165 ILE D C      1 
ATOM   9770  O O      . ILE D 2 147 ? 21.657  45.347  69.542 1.00 54.83  ? 165 ILE D O      1 
ATOM   9771  C CB     . ILE D 2 147 ? 21.943  48.044  69.911 1.00 52.05  ? 165 ILE D CB     1 
ATOM   9772  C CG1    . ILE D 2 147 ? 21.800  49.427  70.533 1.00 56.86  ? 165 ILE D CG1    1 
ATOM   9773  C CG2    . ILE D 2 147 ? 22.729  48.132  68.636 1.00 45.36  ? 165 ILE D CG2    1 
ATOM   9774  C CD1    . ILE D 2 147 ? 23.104  50.172  70.646 1.00 58.78  ? 165 ILE D CD1    1 
ATOM   9775  N N      . LYS D 2 148 ? 19.722  45.514  68.473 1.00 54.13  ? 166 LYS D N      1 
ATOM   9776  C CA     . LYS D 2 148 ? 19.736  44.103  68.130 1.00 53.27  ? 166 LYS D CA     1 
ATOM   9777  C C      . LYS D 2 148 ? 20.195  43.680  66.748 1.00 54.59  ? 166 LYS D C      1 
ATOM   9778  O O      . LYS D 2 148 ? 20.631  42.556  66.584 1.00 60.43  ? 166 LYS D O      1 
ATOM   9779  C CB     . LYS D 2 148 ? 18.346  43.538  68.361 1.00 51.25  ? 166 LYS D CB     1 
ATOM   9780  C CG     . LYS D 2 148 ? 17.228  44.454  67.908 1.00 60.03  ? 166 LYS D CG     1 
ATOM   9781  C CD     . LYS D 2 148 ? 15.890  43.743  67.978 1.00 77.96  ? 166 LYS D CD     1 
ATOM   9782  C CE     . LYS D 2 148 ? 15.488  43.436  69.410 1.00 86.09  ? 166 LYS D CE     1 
ATOM   9783  N NZ     . LYS D 2 148 ? 14.952  44.636  70.112 1.00 88.09  ? 166 LYS D NZ     1 
ATOM   9784  N N      . THR D 2 149 ? 20.095  44.531  65.740 1.00 56.25  ? 167 THR D N      1 
ATOM   9785  C CA     . THR D 2 149 ? 20.391  44.094  64.383 1.00 50.20  ? 167 THR D CA     1 
ATOM   9786  C C      . THR D 2 149 ? 21.699  44.415  63.698 1.00 54.35  ? 167 THR D C      1 
ATOM   9787  O O      . THR D 2 149 ? 21.926  43.889  62.619 1.00 63.88  ? 167 THR D O      1 
ATOM   9788  C CB     . THR D 2 149 ? 19.302  44.624  63.457 1.00 57.83  ? 167 THR D CB     1 
ATOM   9789  O OG1    . THR D 2 149 ? 19.258  46.052  63.551 1.00 62.19  ? 167 THR D OG1    1 
ATOM   9790  C CG2    . THR D 2 149 ? 17.954  44.061  63.850 1.00 46.42  ? 167 THR D CG2    1 
ATOM   9791  N N      . LEU D 2 150 ? 22.517  45.289  64.255 1.00 51.50  ? 168 LEU D N      1 
ATOM   9792  C CA     . LEU D 2 150 ? 23.809  45.706  63.666 1.00 57.21  ? 168 LEU D CA     1 
ATOM   9793  C C      . LEU D 2 150 ? 23.674  46.798  62.637 1.00 63.21  ? 168 LEU D C      1 
ATOM   9794  O O      . LEU D 2 150 ? 24.657  47.353  62.172 1.00 62.27  ? 168 LEU D O      1 
ATOM   9795  C CB     . LEU D 2 150 ? 24.688  44.560  63.145 1.00 47.06  ? 168 LEU D CB     1 
ATOM   9796  C CG     . LEU D 2 150 ? 26.168  44.813  62.831 1.00 48.08  ? 168 LEU D CG     1 
ATOM   9797  C CD1    . LEU D 2 150 ? 26.855  45.655  63.890 1.00 50.63  ? 168 LEU D CD1    1 
ATOM   9798  C CD2    . LEU D 2 150 ? 26.910  43.512  62.646 1.00 62.28  ? 168 LEU D CD2    1 
ATOM   9799  N N      . ASP D 2 151 ? 22.460  47.155  62.290 1.00 60.59  ? 169 ASP D N      1 
ATOM   9800  C CA     . ASP D 2 151 ? 22.317  48.280  61.407 1.00 58.59  ? 169 ASP D CA     1 
ATOM   9801  C C      . ASP D 2 151 ? 21.814  49.290  62.370 1.00 62.75  ? 169 ASP D C      1 
ATOM   9802  O O      . ASP D 2 151 ? 21.901  50.480  62.134 1.00 62.70  ? 169 ASP D O      1 
ATOM   9803  C CB     . ASP D 2 151 ? 21.316  47.992  60.318 1.00 61.80  ? 169 ASP D CB     1 
ATOM   9804  C CG     . ASP D 2 151 ? 21.738  48.550  58.975 1.00 77.45  ? 169 ASP D CG     1 
ATOM   9805  O OD1    . ASP D 2 151 ? 22.530  49.513  58.949 1.00 80.10  ? 169 ASP D OD1    1 
ATOM   9806  O OD2    . ASP D 2 151 ? 21.273  48.025  57.941 1.00 70.71  ? 169 ASP D OD2    1 
ATOM   9807  N N      . GLU D 2 152 ? 21.235  48.822  63.454 1.00 57.66  ? 170 GLU D N      1 
ATOM   9808  C CA     . GLU D 2 152 ? 20.834  49.724  64.493 1.00 53.83  ? 170 GLU D CA     1 
ATOM   9809  C C      . GLU D 2 152 ? 22.097  50.226  65.108 1.00 57.01  ? 170 GLU D C      1 
ATOM   9810  O O      . GLU D 2 152 ? 22.195  51.380  65.478 1.00 56.99  ? 170 GLU D O      1 
ATOM   9811  C CB     . GLU D 2 152 ? 19.990  48.992  65.513 1.00 57.33  ? 170 GLU D CB     1 
ATOM   9812  C CG     . GLU D 2 152 ? 19.435  49.869  66.618 1.00 66.66  ? 170 GLU D CG     1 
ATOM   9813  C CD     . GLU D 2 152 ? 18.110  50.497  66.250 1.00 73.68  ? 170 GLU D CD     1 
ATOM   9814  O OE1    . GLU D 2 152 ? 17.500  50.058  65.254 1.00 71.52  ? 170 GLU D OE1    1 
ATOM   9815  O OE2    . GLU D 2 152 ? 17.675  51.422  66.964 1.00 75.38  ? 170 GLU D OE2    1 
ATOM   9816  N N      . ALA D 2 153 ? 23.075  49.345  65.249 1.00 53.91  ? 171 ALA D N      1 
ATOM   9817  C CA     . ALA D 2 153 ? 24.339  49.719  65.882 1.00 54.78  ? 171 ALA D CA     1 
ATOM   9818  C C      . ALA D 2 153 ? 25.154  50.740  65.166 1.00 52.09  ? 171 ALA D C      1 
ATOM   9819  O O      . ALA D 2 153 ? 25.723  51.603  65.791 1.00 49.78  ? 171 ALA D O      1 
ATOM   9820  C CB     . ALA D 2 153 ? 25.182  48.507  66.139 1.00 48.56  ? 171 ALA D CB     1 
ATOM   9821  N N      . LYS D 2 154 ? 25.236  50.640  63.856 1.00 55.64  ? 172 LYS D N      1 
ATOM   9822  C CA     . LYS D 2 154 ? 25.937  51.644  63.105 1.00 53.60  ? 172 LYS D CA     1 
ATOM   9823  C C      . LYS D 2 154 ? 25.327  52.977  63.437 1.00 53.07  ? 172 LYS D C      1 
ATOM   9824  O O      . LYS D 2 154 ? 26.043  53.901  63.748 1.00 55.92  ? 172 LYS D O      1 
ATOM   9825  C CB     . LYS D 2 154 ? 25.821  51.389  61.619 1.00 45.81  ? 172 LYS D CB     1 
ATOM   9826  C CG     . LYS D 2 154 ? 26.487  50.117  61.145 1.00 52.90  ? 172 LYS D CG     1 
ATOM   9827  C CD     . LYS D 2 154 ? 26.398  50.003  59.636 1.00 57.32  ? 172 LYS D CD     1 
ATOM   9828  C CE     . LYS D 2 154 ? 26.893  51.268  58.956 1.00 56.08  ? 172 LYS D CE     1 
ATOM   9829  N NZ     . LYS D 2 154 ? 26.987  51.115  57.478 1.00 51.62  ? 172 LYS D NZ     1 
ATOM   9830  N N      . GLN D 2 155 ? 24.009  53.087  63.401 1.00 56.31  ? 173 GLN D N      1 
ATOM   9831  C CA     . GLN D 2 155 ? 23.356  54.370  63.626 1.00 56.61  ? 173 GLN D CA     1 
ATOM   9832  C C      . GLN D 2 155 ? 23.808  54.938  64.934 1.00 52.92  ? 173 GLN D C      1 
ATOM   9833  O O      . GLN D 2 155 ? 24.034  56.129  65.045 1.00 53.06  ? 173 GLN D O      1 
ATOM   9834  C CB     . GLN D 2 155 ? 21.844  54.222  63.637 1.00 57.08  ? 173 GLN D CB     1 
ATOM   9835  C CG     . GLN D 2 155 ? 21.258  53.704  62.340 1.00 57.15  ? 173 GLN D CG     1 
ATOM   9836  C CD     . GLN D 2 155 ? 19.756  53.540  62.419 1.00 65.14  ? 173 GLN D CD     1 
ATOM   9837  O OE1    . GLN D 2 155 ? 19.096  54.160  63.250 1.00 67.65  ? 173 GLN D OE1    1 
ATOM   9838  N NE2    . GLN D 2 155 ? 19.208  52.702  61.549 1.00 73.44  ? 173 GLN D NE2    1 
ATOM   9839  N N      . PHE D 2 156 ? 23.969  54.086  65.926 1.00 55.33  ? 174 PHE D N      1 
ATOM   9840  C CA     . PHE D 2 156 ? 24.379  54.523  67.251 1.00 55.82  ? 174 PHE D CA     1 
ATOM   9841  C C      . PHE D 2 156 ? 25.789  55.035  67.247 1.00 51.83  ? 174 PHE D C      1 
ATOM   9842  O O      . PHE D 2 156 ? 26.064  56.095  67.771 1.00 50.96  ? 174 PHE D O      1 
ATOM   9843  C CB     . PHE D 2 156 ? 24.255  53.339  68.198 1.00 51.67  ? 174 PHE D CB     1 
ATOM   9844  C CG     . PHE D 2 156 ? 24.758  53.594  69.571 1.00 50.66  ? 174 PHE D CG     1 
ATOM   9845  C CD1    . PHE D 2 156 ? 24.122  54.492  70.394 1.00 54.11  ? 174 PHE D CD1    1 
ATOM   9846  C CD2    . PHE D 2 156 ? 25.847  52.901  70.048 1.00 48.76  ? 174 PHE D CD2    1 
ATOM   9847  C CE1    . PHE D 2 156 ? 24.578  54.716  71.666 1.00 48.86  ? 174 PHE D CE1    1 
ATOM   9848  C CE2    . PHE D 2 156 ? 26.311  53.118  71.319 1.00 51.78  ? 174 PHE D CE2    1 
ATOM   9849  C CZ     . PHE D 2 156 ? 25.677  54.032  72.127 1.00 51.78  ? 174 PHE D CZ     1 
ATOM   9850  N N      . ILE D 2 157 ? 26.697  54.287  66.644 1.00 51.40  ? 175 ILE D N      1 
ATOM   9851  C CA     . ILE D 2 157 ? 28.097  54.653  66.669 1.00 44.98  ? 175 ILE D CA     1 
ATOM   9852  C C      . ILE D 2 157 ? 28.264  55.883  65.843 1.00 46.10  ? 175 ILE D C      1 
ATOM   9853  O O      . ILE D 2 157 ? 29.223  56.609  65.970 1.00 47.67  ? 175 ILE D O      1 
ATOM   9854  C CB     . ILE D 2 157 ? 28.985  53.507  66.158 1.00 39.82  ? 175 ILE D CB     1 
ATOM   9855  C CG1    . ILE D 2 157 ? 28.616  52.201  66.826 1.00 49.72  ? 175 ILE D CG1    1 
ATOM   9856  C CG2    . ILE D 2 157 ? 30.412  53.690  66.580 1.00 44.25  ? 175 ILE D CG2    1 
ATOM   9857  C CD1    . ILE D 2 157 ? 29.103  52.112  68.252 1.00 45.07  ? 175 ILE D CD1    1 
ATOM   9858  N N      . LEU D 2 158 ? 27.302  56.165  65.005 1.00 50.65  ? 176 LEU D N      1 
ATOM   9859  C CA     . LEU D 2 158 ? 27.470  57.291  64.122 1.00 56.23  ? 176 LEU D CA     1 
ATOM   9860  C C      . LEU D 2 158 ? 26.743  58.466  64.687 1.00 57.68  ? 176 LEU D C      1 
ATOM   9861  O O      . LEU D 2 158 ? 26.574  59.466  64.010 1.00 63.92  ? 176 LEU D O      1 
ATOM   9862  C CB     . LEU D 2 158 ? 26.949  56.983  62.720 1.00 50.71  ? 176 LEU D CB     1 
ATOM   9863  C CG     . LEU D 2 158 ? 27.586  55.863  61.894 1.00 44.83  ? 176 LEU D CG     1 
ATOM   9864  C CD1    . LEU D 2 158 ? 26.980  55.792  60.506 1.00 51.44  ? 176 LEU D CD1    1 
ATOM   9865  C CD2    . LEU D 2 158 ? 29.089  55.988  61.810 1.00 42.95  ? 176 LEU D CD2    1 
ATOM   9866  N N      . SER D 2 159 ? 26.305  58.360  65.929 1.00 52.32  ? 177 SER D N      1 
ATOM   9867  C CA     . SER D 2 159 ? 25.557  59.429  66.548 1.00 50.37  ? 177 SER D CA     1 
ATOM   9868  C C      . SER D 2 159 ? 26.486  59.964  67.559 1.00 51.83  ? 177 SER D C      1 
ATOM   9869  O O      . SER D 2 159 ? 26.142  60.850  68.322 1.00 50.44  ? 177 SER D O      1 
ATOM   9870  C CB     . SER D 2 159 ? 24.298  58.913  67.211 1.00 47.25  ? 177 SER D CB     1 
ATOM   9871  O OG     . SER D 2 159 ? 24.562  58.409  68.500 1.00 50.83  ? 177 SER D OG     1 
ATOM   9872  N N      . PHE D 2 160 ? 27.702  59.454  67.551 1.00 52.42  ? 178 PHE D N      1 
ATOM   9873  C CA     . PHE D 2 160 ? 28.699  59.960  68.460 1.00 53.11  ? 178 PHE D CA     1 
ATOM   9874  C C      . PHE D 2 160 ? 29.171  61.236  67.834 1.00 57.44  ? 178 PHE D C      1 
ATOM   9875  O O      . PHE D 2 160 ? 29.906  61.989  68.443 1.00 58.76  ? 178 PHE D O      1 
ATOM   9876  C CB     . PHE D 2 160 ? 29.872  59.004  68.610 1.00 50.07  ? 178 PHE D CB     1 
ATOM   9877  C CG     . PHE D 2 160 ? 29.541  57.706  69.284 1.00 47.39  ? 178 PHE D CG     1 
ATOM   9878  C CD1    . PHE D 2 160 ? 28.415  57.574  70.064 1.00 47.81  ? 178 PHE D CD1    1 
ATOM   9879  C CD2    . PHE D 2 160 ? 30.384  56.622  69.150 1.00 38.96  ? 178 PHE D CD2    1 
ATOM   9880  C CE1    . PHE D 2 160 ? 28.123  56.378  70.683 1.00 43.29  ? 178 PHE D CE1    1 
ATOM   9881  C CE2    . PHE D 2 160 ? 30.100  55.426  69.765 1.00 36.98  ? 178 PHE D CE2    1 
ATOM   9882  C CZ     . PHE D 2 160 ? 28.968  55.304  70.533 1.00 42.91  ? 178 PHE D CZ     1 
ATOM   9883  N N      . VAL D 2 161 ? 28.742  61.508  66.614 1.00 56.69  ? 179 VAL D N      1 
ATOM   9884  C CA     . VAL D 2 161 ? 29.103  62.751  65.977 1.00 51.73  ? 179 VAL D CA     1 
ATOM   9885  C C      . VAL D 2 161 ? 28.417  63.879  66.681 1.00 54.63  ? 179 VAL D C      1 
ATOM   9886  O O      . VAL D 2 161 ? 28.849  65.015  66.599 1.00 55.63  ? 179 VAL D O      1 
ATOM   9887  C CB     . VAL D 2 161 ? 28.641  62.771  64.539 1.00 56.10  ? 179 VAL D CB     1 
ATOM   9888  C CG1    . VAL D 2 161 ? 27.127  62.694  64.462 1.00 57.38  ? 179 VAL D CG1    1 
ATOM   9889  C CG2    . VAL D 2 161 ? 29.160  64.006  63.823 1.00 58.81  ? 179 VAL D CG2    1 
ATOM   9890  N N      . MET D 2 162 ? 27.368  63.579  67.425 1.00 59.89  ? 180 MET D N      1 
ATOM   9891  C CA     . MET D 2 162 ? 26.607  64.617  68.108 1.00 59.81  ? 180 MET D CA     1 
ATOM   9892  C C      . MET D 2 162 ? 27.358  65.180  69.279 1.00 59.20  ? 180 MET D C      1 
ATOM   9893  O O      . MET D 2 162 ? 27.154  66.321  69.655 1.00 55.61  ? 180 MET D O      1 
ATOM   9894  C CB     . MET D 2 162 ? 25.260  64.092  68.568 1.00 53.81  ? 180 MET D CB     1 
ATOM   9895  C CG     . MET D 2 162 ? 24.199  64.091  67.486 1.00 58.71  ? 180 MET D CG     1 
ATOM   9896  S SD     . MET D 2 162 ? 23.627  65.748  67.076 1.00 82.48  ? 180 MET D SD     1 
ATOM   9897  C CE     . MET D 2 162 ? 22.583  66.106  68.483 1.00 54.88  ? 180 MET D CE     1 
ATOM   9898  N N      . LEU D 2 163 ? 28.253  64.396  69.847 1.00 59.31  ? 181 LEU D N      1 
ATOM   9899  C CA     . LEU D 2 163 ? 29.039  64.854  70.975 1.00 57.05  ? 181 LEU D CA     1 
ATOM   9900  C C      . LEU D 2 163 ? 30.140  65.760  70.522 1.00 57.32  ? 181 LEU D C      1 
ATOM   9901  O O      . LEU D 2 163 ? 30.857  66.291  71.342 1.00 59.11  ? 181 LEU D O      1 
ATOM   9902  C CB     . LEU D 2 163 ? 29.688  63.662  71.664 1.00 55.87  ? 181 LEU D CB     1 
ATOM   9903  C CG     . LEU D 2 163 ? 28.879  62.392  71.898 1.00 61.34  ? 181 LEU D CG     1 
ATOM   9904  C CD1    . LEU D 2 163 ? 29.778  61.172  71.828 1.00 58.21  ? 181 LEU D CD1    1 
ATOM   9905  C CD2    . LEU D 2 163 ? 28.193  62.459  73.245 1.00 59.34  ? 181 LEU D CD2    1 
ATOM   9906  N N      . ASN D 2 164 ? 30.300  65.940  69.226 1.00 59.27  ? 182 ASN D N      1 
ATOM   9907  C CA     . ASN D 2 164 ? 31.432  66.699  68.726 1.00 56.64  ? 182 ASN D CA     1 
ATOM   9908  C C      . ASN D 2 164 ? 31.475  68.133  69.117 1.00 58.23  ? 182 ASN D C      1 
ATOM   9909  O O      . ASN D 2 164 ? 30.457  68.720  69.429 1.00 58.50  ? 182 ASN D O      1 
ATOM   9910  C CB     . ASN D 2 164 ? 31.509  66.615  67.205 1.00 57.17  ? 182 ASN D CB     1 
ATOM   9911  C CG     . ASN D 2 164 ? 32.503  65.592  66.722 1.00 58.67  ? 182 ASN D CG     1 
ATOM   9912  O OD1    . ASN D 2 164 ? 32.923  64.717  67.472 1.00 60.34  ? 182 ASN D OD1    1 
ATOM   9913  N ND2    . ASN D 2 164 ? 32.889  65.699  65.459 1.00 55.34  ? 182 ASN D ND2    1 
ATOM   9914  N N      . ASP D 2 165 ? 32.674  68.683  69.148 1.00 59.95  ? 183 ASP D N      1 
ATOM   9915  C CA     . ASP D 2 165 ? 32.857  70.087  69.449 1.00 53.81  ? 183 ASP D CA     1 
ATOM   9916  C C      . ASP D 2 165 ? 32.478  70.552  70.840 1.00 49.26  ? 183 ASP D C      1 
ATOM   9917  O O      . ASP D 2 165 ? 32.471  71.734  71.107 1.00 55.58  ? 183 ASP D O      1 
ATOM   9918  C CB     . ASP D 2 165 ? 32.226  70.927  68.350 1.00 54.91  ? 183 ASP D CB     1 
ATOM   9919  C CG     . ASP D 2 165 ? 32.949  70.793  67.030 1.00 59.53  ? 183 ASP D CG     1 
ATOM   9920  O OD1    . ASP D 2 165 ? 34.147  70.450  67.038 1.00 59.66  ? 183 ASP D OD1    1 
ATOM   9921  O OD2    . ASP D 2 165 ? 32.326  71.042  65.982 1.00 51.94  ? 183 ASP D OD2    1 
ATOM   9922  N N      . ASN D 2 166 ? 32.251  69.626  71.743 1.00 46.44  ? 184 ASN D N      1 
ATOM   9923  C CA     . ASN D 2 166 ? 31.949  69.978  73.108 1.00 47.99  ? 184 ASN D CA     1 
ATOM   9924  C C      . ASN D 2 166 ? 32.809  69.084  73.932 1.00 51.26  ? 184 ASN D C      1 
ATOM   9925  O O      . ASN D 2 166 ? 33.750  69.538  74.560 1.00 54.81  ? 184 ASN D O      1 
ATOM   9926  C CB     . ASN D 2 166 ? 30.489  69.673  73.409 1.00 47.40  ? 184 ASN D CB     1 
ATOM   9927  C CG     . ASN D 2 166 ? 30.051  70.122  74.790 1.00 61.01  ? 184 ASN D CG     1 
ATOM   9928  O OD1    . ASN D 2 166 ? 28.921  69.862  75.194 1.00 71.38  ? 184 ASN D OD1    1 
ATOM   9929  N ND2    . ASN D 2 166 ? 30.930  70.798  75.516 1.00 63.70  ? 184 ASN D ND2    1 
ATOM   9930  N N      . VAL D 2 167 ? 32.491  67.802  73.940 1.00 44.67  ? 185 VAL D N      1 
ATOM   9931  C CA     . VAL D 2 167 ? 33.243  66.857  74.726 1.00 47.29  ? 185 VAL D CA     1 
ATOM   9932  C C      . VAL D 2 167 ? 34.518  66.437  74.041 1.00 47.91  ? 185 VAL D C      1 
ATOM   9933  O O      . VAL D 2 167 ? 35.454  66.002  74.688 1.00 45.74  ? 185 VAL D O      1 
ATOM   9934  C CB     . VAL D 2 167 ? 32.369  65.646  75.038 1.00 44.66  ? 185 VAL D CB     1 
ATOM   9935  C CG1    . VAL D 2 167 ? 30.976  66.101  75.428 1.00 41.80  ? 185 VAL D CG1    1 
ATOM   9936  C CG2    . VAL D 2 167 ? 32.290  64.698  73.862 1.00 56.19  ? 185 VAL D CG2    1 
ATOM   9937  N N      . GLU D 2 168 ? 34.576  66.589  72.737 1.00 50.16  ? 186 GLU D N      1 
ATOM   9938  C CA     . GLU D 2 168 ? 35.722  66.172  71.969 1.00 51.26  ? 186 GLU D CA     1 
ATOM   9939  C C      . GLU D 2 168 ? 36.926  67.004  72.252 1.00 54.95  ? 186 GLU D C      1 
ATOM   9940  O O      . GLU D 2 168 ? 38.041  66.510  72.237 1.00 53.42  ? 186 GLU D O      1 
ATOM   9941  C CB     . GLU D 2 168 ? 35.339  66.369  70.513 1.00 54.55  ? 186 GLU D CB     1 
ATOM   9942  C CG     . GLU D 2 168 ? 36.484  66.365  69.516 1.00 68.11  ? 186 GLU D CG     1 
ATOM   9943  C CD     . GLU D 2 168 ? 36.089  66.942  68.174 1.00 65.64  ? 186 GLU D CD     1 
ATOM   9944  O OE1    . GLU D 2 168 ? 34.959  67.448  68.064 1.00 67.35  ? 186 GLU D OE1    1 
ATOM   9945  O OE2    . GLU D 2 168 ? 36.902  66.900  67.231 1.00 52.30  ? 186 GLU D OE2    1 
ATOM   9946  N N      . LEU D 2 169 ? 36.716  68.280  72.512 1.00 54.67  ? 187 LEU D N      1 
ATOM   9947  C CA     . LEU D 2 169 ? 37.814  69.220  72.693 1.00 52.45  ? 187 LEU D CA     1 
ATOM   9948  C C      . LEU D 2 169 ? 38.907  68.947  73.726 1.00 51.97  ? 187 LEU D C      1 
ATOM   9949  O O      . LEU D 2 169 ? 40.079  69.155  73.438 1.00 48.17  ? 187 LEU D O      1 
ATOM   9950  C CB     . LEU D 2 169 ? 37.237  70.622  72.876 1.00 45.10  ? 187 LEU D CB     1 
ATOM   9951  C CG     . LEU D 2 169 ? 36.332  71.179  71.785 1.00 43.69  ? 187 LEU D CG     1 
ATOM   9952  C CD1    . LEU D 2 169 ? 35.744  72.494  72.258 1.00 51.78  ? 187 LEU D CD1    1 
ATOM   9953  C CD2    . LEU D 2 169 ? 37.111  71.378  70.500 1.00 46.33  ? 187 LEU D CD2    1 
ATOM   9954  N N      . PRO D 2 170 ? 38.552  68.516  74.956 1.00 51.30  ? 188 PRO D N      1 
ATOM   9955  C CA     . PRO D 2 170 ? 39.689  68.252  75.842 1.00 48.19  ? 188 PRO D CA     1 
ATOM   9956  C C      . PRO D 2 170 ? 40.608  67.174  75.319 1.00 56.11  ? 188 PRO D C      1 
ATOM   9957  O O      . PRO D 2 170 ? 41.814  67.297  75.457 1.00 57.58  ? 188 PRO D O      1 
ATOM   9958  C CB     . PRO D 2 170 ? 39.024  67.774  77.104 1.00 41.61  ? 188 PRO D CB     1 
ATOM   9959  C CG     . PRO D 2 170 ? 37.755  68.532  77.146 1.00 46.84  ? 188 PRO D CG     1 
ATOM   9960  C CD     . PRO D 2 170 ? 37.288  68.483  75.729 1.00 53.41  ? 188 PRO D CD     1 
ATOM   9961  N N      . LEU D 2 171 ? 40.066  66.147  74.685 1.00 53.33  ? 189 LEU D N      1 
ATOM   9962  C CA     . LEU D 2 171 ? 40.880  65.041  74.212 1.00 44.67  ? 189 LEU D CA     1 
ATOM   9963  C C      . LEU D 2 171 ? 41.625  65.437  72.985 1.00 43.83  ? 189 LEU D C      1 
ATOM   9964  O O      . LEU D 2 171 ? 42.730  64.991  72.764 1.00 42.57  ? 189 LEU D O      1 
ATOM   9965  C CB     . LEU D 2 171 ? 39.994  63.852  73.918 1.00 43.01  ? 189 LEU D CB     1 
ATOM   9966  C CG     . LEU D 2 171 ? 40.587  62.454  74.008 1.00 45.31  ? 189 LEU D CG     1 
ATOM   9967  C CD1    . LEU D 2 171 ? 41.307  62.270  75.332 1.00 51.33  ? 189 LEU D CD1    1 
ATOM   9968  C CD2    . LEU D 2 171 ? 39.465  61.445  73.877 1.00 39.16  ? 189 LEU D CD2    1 
ATOM   9969  N N      . LYS D 2 172 ? 41.060  66.353  72.214 1.00 52.80  ? 190 LYS D N      1 
ATOM   9970  C CA     . LYS D 2 172 ? 41.670  66.780  70.958 1.00 56.21  ? 190 LYS D CA     1 
ATOM   9971  C C      . LYS D 2 172 ? 42.845  67.689  71.177 1.00 51.82  ? 190 LYS D C      1 
ATOM   9972  O O      . LYS D 2 172 ? 43.727  67.790  70.335 1.00 49.09  ? 190 LYS D O      1 
ATOM   9973  C CB     . LYS D 2 172 ? 40.627  67.485  70.085 1.00 44.54  ? 190 LYS D CB     1 
ATOM   9974  C CG     . LYS D 2 172 ? 41.081  67.804  68.674 1.00 46.26  ? 190 LYS D CG     1 
ATOM   9975  C CD     . LYS D 2 172 ? 40.638  69.185  68.232 1.00 56.11  ? 190 LYS D CD     1 
ATOM   9976  C CE     . LYS D 2 172 ? 39.162  69.214  67.898 1.00 63.15  ? 190 LYS D CE     1 
ATOM   9977  N NZ     . LYS D 2 172 ? 38.761  70.507  67.281 1.00 53.41  ? 190 LYS D NZ     1 
ATOM   9978  N N      . ALA D 2 173 ? 42.858  68.371  72.302 1.00 45.05  ? 191 ALA D N      1 
ATOM   9979  C CA     . ALA D 2 173 ? 43.903  69.338  72.562 1.00 42.71  ? 191 ALA D CA     1 
ATOM   9980  C C      . ALA D 2 173 ? 45.252  68.743  72.580 1.00 46.61  ? 191 ALA D C      1 
ATOM   9981  O O      . ALA D 2 173 ? 46.237  69.436  72.386 1.00 41.18  ? 191 ALA D O      1 
ATOM   9982  C CB     . ALA D 2 173 ? 43.650  69.968  73.901 1.00 47.99  ? 191 ALA D CB     1 
ATOM   9983  N N      . GLN D 2 174 ? 45.323  67.454  72.814 1.00 51.47  ? 192 GLN D N      1 
ATOM   9984  C CA     . GLN D 2 174 ? 46.619  66.837  72.976 1.00 53.70  ? 192 GLN D CA     1 
ATOM   9985  C C      . GLN D 2 174 ? 47.191  66.229  71.722 1.00 61.50  ? 192 GLN D C      1 
ATOM   9986  O O      . GLN D 2 174 ? 48.292  65.705  71.757 1.00 70.60  ? 192 GLN D O      1 
ATOM   9987  C CB     . GLN D 2 174 ? 46.529  65.790  74.071 1.00 53.22  ? 192 GLN D CB     1 
ATOM   9988  C CG     . GLN D 2 174 ? 45.463  66.105  75.102 1.00 57.61  ? 192 GLN D CG     1 
ATOM   9989  C CD     . GLN D 2 174 ? 45.332  65.025  76.141 1.00 54.24  ? 192 GLN D CD     1 
ATOM   9990  O OE1    . GLN D 2 174 ? 44.378  65.001  76.911 1.00 54.26  ? 192 GLN D OE1    1 
ATOM   9991  N NE2    . GLN D 2 174 ? 46.297  64.119  76.170 1.00 53.20  ? 192 GLN D NE2    1 
ATOM   9992  N N      . SER D 2 175 ? 46.472  66.322  70.613 1.00 51.83  ? 193 SER D N      1 
ATOM   9993  C CA     . SER D 2 175 ? 46.951  65.754  69.376 1.00 43.79  ? 193 SER D CA     1 
ATOM   9994  C C      . SER D 2 175 ? 48.016  66.582  68.761 1.00 43.71  ? 193 SER D C      1 
ATOM   9995  O O      . SER D 2 175 ? 47.934  67.794  68.753 1.00 47.42  ? 193 SER D O      1 
ATOM   9996  C CB     . SER D 2 175 ? 45.823  65.590  68.400 1.00 48.02  ? 193 SER D CB     1 
ATOM   9997  O OG     . SER D 2 175 ? 46.199  64.743  67.335 1.00 51.07  ? 193 SER D OG     1 
ATOM   9998  N N      . GLU D 2 176 ? 49.025  65.940  68.234 1.00 43.21  ? 194 GLU D N      1 
ATOM   9999  C CA     . GLU D 2 176 ? 50.089  66.648  67.571 1.00 56.36  ? 194 GLU D CA     1 
ATOM   10000 C C      . GLU D 2 176 ? 49.927  66.354  66.103 1.00 56.96  ? 194 GLU D C      1 
ATOM   10001 O O      . GLU D 2 176 ? 50.673  66.840  65.262 1.00 57.91  ? 194 GLU D O      1 
ATOM   10002 C CB     . GLU D 2 176 ? 51.429  66.152  68.102 1.00 56.06  ? 194 GLU D CB     1 
ATOM   10003 C CG     . GLU D 2 176 ? 52.670  66.650  67.369 1.00 67.20  ? 194 GLU D CG     1 
ATOM   10004 C CD     . GLU D 2 176 ? 52.862  68.157  67.433 1.00 76.09  ? 194 GLU D CD     1 
ATOM   10005 O OE1    . GLU D 2 176 ? 52.200  68.826  68.251 1.00 77.05  ? 194 GLU D OE1    1 
ATOM   10006 O OE2    . GLU D 2 176 ? 53.696  68.673  66.661 1.00 64.90  ? 194 GLU D OE2    1 
ATOM   10007 N N      . ARG D 2 177 ? 48.885  65.616  65.777 1.00 53.88  ? 195 ARG D N      1 
ATOM   10008 C CA     . ARG D 2 177 ? 48.656  65.245  64.408 1.00 52.02  ? 195 ARG D CA     1 
ATOM   10009 C C      . ARG D 2 177 ? 47.443  65.956  63.860 1.00 51.69  ? 195 ARG D C      1 
ATOM   10010 O O      . ARG D 2 177 ? 47.420  66.333  62.707 1.00 51.01  ? 195 ARG D O      1 
ATOM   10011 C CB     . ARG D 2 177 ? 48.462  63.740  64.355 1.00 44.91  ? 195 ARG D CB     1 
ATOM   10012 C CG     . ARG D 2 177 ? 49.673  62.948  64.805 1.00 42.57  ? 195 ARG D CG     1 
ATOM   10013 C CD     . ARG D 2 177 ? 49.358  61.465  64.867 1.00 43.63  ? 195 ARG D CD     1 
ATOM   10014 N NE     . ARG D 2 177 ? 50.561  60.665  65.048 1.00 48.91  ? 195 ARG D NE     1 
ATOM   10015 C CZ     . ARG D 2 177 ? 50.557  59.349  65.202 1.00 47.42  ? 195 ARG D CZ     1 
ATOM   10016 N NH1    . ARG D 2 177 ? 49.413  58.690  65.208 1.00 44.72  ? 195 ARG D NH1    1 
ATOM   10017 N NH2    . ARG D 2 177 ? 51.696  58.693  65.358 1.00 48.58  ? 195 ARG D NH2    1 
ATOM   10018 N N      . TYR D 2 178 ? 46.423  66.135  64.677 1.00 47.52  ? 196 TYR D N      1 
ATOM   10019 C CA     . TYR D 2 178 ? 45.211  66.799  64.242 1.00 48.47  ? 196 TYR D CA     1 
ATOM   10020 C C      . TYR D 2 178 ? 45.462  68.223  63.886 1.00 52.49  ? 196 TYR D C      1 
ATOM   10021 O O      . TYR D 2 178 ? 44.748  68.786  63.071 1.00 45.62  ? 196 TYR D O      1 
ATOM   10022 C CB     . TYR D 2 178 ? 44.151  66.757  65.322 1.00 49.44  ? 196 TYR D CB     1 
ATOM   10023 C CG     . TYR D 2 178 ? 42.762  67.136  64.874 1.00 49.48  ? 196 TYR D CG     1 
ATOM   10024 C CD1    . TYR D 2 178 ? 42.336  68.450  64.909 1.00 51.46  ? 196 TYR D CD1    1 
ATOM   10025 C CD2    . TYR D 2 178 ? 41.870  66.175  64.438 1.00 53.28  ? 196 TYR D CD2    1 
ATOM   10026 C CE1    . TYR D 2 178 ? 41.068  68.801  64.505 1.00 57.13  ? 196 TYR D CE1    1 
ATOM   10027 C CE2    . TYR D 2 178 ? 40.597  66.517  64.036 1.00 57.29  ? 196 TYR D CE2    1 
ATOM   10028 C CZ     . TYR D 2 178 ? 40.205  67.832  64.073 1.00 57.71  ? 196 TYR D CZ     1 
ATOM   10029 O OH     . TYR D 2 178 ? 38.940  68.187  63.673 1.00 64.20  ? 196 TYR D OH     1 
ATOM   10030 N N      . PRO D 2 179 ? 46.457  68.854  64.516 1.00 54.11  ? 197 PRO D N      1 
ATOM   10031 C CA     . PRO D 2 179 ? 46.605  70.241  64.104 1.00 47.30  ? 197 PRO D CA     1 
ATOM   10032 C C      . PRO D 2 179 ? 47.055  70.348  62.674 1.00 44.69  ? 197 PRO D C      1 
ATOM   10033 O O      . PRO D 2 179 ? 47.156  71.457  62.171 1.00 41.40  ? 197 PRO D O      1 
ATOM   10034 C CB     . PRO D 2 179 ? 47.658  70.756  65.060 1.00 42.57  ? 197 PRO D CB     1 
ATOM   10035 C CG     . PRO D 2 179 ? 47.414  69.998  66.304 1.00 44.92  ? 197 PRO D CG     1 
ATOM   10036 C CD     . PRO D 2 179 ? 47.132  68.616  65.807 1.00 49.64  ? 197 PRO D CD     1 
ATOM   10037 N N      . LYS D 2 180 ? 47.284  69.225  62.009 1.00 43.39  ? 198 LYS D N      1 
ATOM   10038 C CA     . LYS D 2 180 ? 47.776  69.239  60.639 1.00 44.12  ? 198 LYS D CA     1 
ATOM   10039 C C      . LYS D 2 180 ? 46.717  68.791  59.660 1.00 41.87  ? 198 LYS D C      1 
ATOM   10040 O O      . LYS D 2 180 ? 47.035  68.333  58.581 1.00 37.22  ? 198 LYS D O      1 
ATOM   10041 C CB     . LYS D 2 180 ? 48.985  68.340  60.525 1.00 42.30  ? 198 LYS D CB     1 
ATOM   10042 C CG     . LYS D 2 180 ? 49.944  68.414  61.695 1.00 41.30  ? 198 LYS D CG     1 
ATOM   10043 C CD     . LYS D 2 180 ? 50.951  69.532  61.526 1.00 40.25  ? 198 LYS D CD     1 
ATOM   10044 C CE     . LYS D 2 180 ? 51.945  69.520  62.671 1.00 36.93  ? 198 LYS D CE     1 
ATOM   10045 N NZ     . LYS D 2 180 ? 53.031  70.515  62.469 1.00 51.26  ? 198 LYS D NZ     1 
ATOM   10046 N N      . LYS D 2 181 ? 45.454  68.944  60.007 1.00 41.29  ? 199 LYS D N      1 
ATOM   10047 C CA     . LYS D 2 181 ? 44.363  68.552  59.145 1.00 34.13  ? 199 LYS D CA     1 
ATOM   10048 C C      . LYS D 2 181 ? 44.188  69.503  58.012 1.00 44.44  ? 199 LYS D C      1 
ATOM   10049 O O      . LYS D 2 181 ? 44.362  70.703  58.171 1.00 44.45  ? 199 LYS D O      1 
ATOM   10050 C CB     . LYS D 2 181 ? 43.086  68.510  59.945 1.00 34.83  ? 199 LYS D CB     1 
ATOM   10051 C CG     . LYS D 2 181 ? 41.922  67.824  59.276 1.00 37.60  ? 199 LYS D CG     1 
ATOM   10052 C CD     . LYS D 2 181 ? 40.720  67.804  60.198 1.00 38.96  ? 199 LYS D CD     1 
ATOM   10053 C CE     . LYS D 2 181 ? 39.529  67.172  59.511 1.00 49.09  ? 199 LYS D CE     1 
ATOM   10054 N NZ     . LYS D 2 181 ? 38.335  67.195  60.389 1.00 43.64  ? 199 LYS D NZ     1 
ATOM   10055 N N      . ASP D 2 182 ? 43.774  68.985  56.867 1.00 48.21  ? 200 ASP D N      1 
ATOM   10056 C CA     . ASP D 2 182 ? 43.648  69.805  55.686 1.00 44.49  ? 200 ASP D CA     1 
ATOM   10057 C C      . ASP D 2 182 ? 42.285  69.929  55.083 1.00 42.15  ? 200 ASP D C      1 
ATOM   10058 O O      . ASP D 2 182 ? 42.194  70.206  53.913 1.00 53.24  ? 200 ASP D O      1 
ATOM   10059 C CB     . ASP D 2 182 ? 44.519  69.242  54.582 1.00 47.31  ? 200 ASP D CB     1 
ATOM   10060 C CG     . ASP D 2 182 ? 45.993  69.474  54.798 1.00 58.53  ? 200 ASP D CG     1 
ATOM   10061 O OD1    . ASP D 2 182 ? 46.405  69.769  55.930 1.00 69.19  ? 200 ASP D OD1    1 
ATOM   10062 O OD2    . ASP D 2 182 ? 46.757  69.343  53.821 1.00 55.10  ? 200 ASP D OD2    1 
ATOM   10063 N N      . ARG D 2 183 ? 41.212  69.726  55.811 1.00 31.02  ? 201 ARG D N      1 
ATOM   10064 C CA     . ARG D 2 183 ? 39.957  69.940  55.181 1.00 33.88  ? 201 ARG D CA     1 
ATOM   10065 C C      . ARG D 2 183 ? 40.000  71.415  55.068 1.00 50.95  ? 201 ARG D C      1 
ATOM   10066 O O      . ARG D 2 183 ? 40.263  72.074  56.053 1.00 59.51  ? 201 ARG D O      1 
ATOM   10067 C CB     . ARG D 2 183 ? 38.837  69.543  56.087 1.00 26.52  ? 201 ARG D CB     1 
ATOM   10068 C CG     . ARG D 2 183 ? 37.452  69.695  55.500 1.00 31.72  ? 201 ARG D CG     1 
ATOM   10069 C CD     . ARG D 2 183 ? 36.445  68.939  56.342 1.00 34.34  ? 201 ARG D CD     1 
ATOM   10070 N NE     . ARG D 2 183 ? 35.124  68.919  55.735 1.00 43.63  ? 201 ARG D NE     1 
ATOM   10071 C CZ     . ARG D 2 183 ? 34.099  68.231  56.218 1.00 48.18  ? 201 ARG D CZ     1 
ATOM   10072 N NH1    . ARG D 2 183 ? 34.250  67.503  57.308 1.00 51.29  ? 201 ARG D NH1    1 
ATOM   10073 N NH2    . ARG D 2 183 ? 32.927  68.262  55.610 1.00 44.90  ? 201 ARG D NH2    1 
ATOM   10074 N N      . SER D 2 184 ? 39.735  71.964  53.893 1.00 48.20  ? 202 SER D N      1 
ATOM   10075 C CA     . SER D 2 184 ? 39.678  73.387  53.747 1.00 52.77  ? 202 SER D CA     1 
ATOM   10076 C C      . SER D 2 184 ? 38.290  73.698  54.062 1.00 58.40  ? 202 SER D C      1 
ATOM   10077 O O      . SER D 2 184 ? 37.435  72.848  53.918 1.00 57.93  ? 202 SER D O      1 
ATOM   10078 C CB     . SER D 2 184 ? 39.933  73.791  52.340 1.00 54.61  ? 202 SER D CB     1 
ATOM   10079 O OG     . SER D 2 184 ? 39.872  75.193  52.193 1.00 63.71  ? 202 SER D OG     1 
ATOM   10080 N N      . ARG D 2 185 ? 38.020  74.915  54.476 1.00 55.08  ? 203 ARG D N      1 
ATOM   10081 C CA     . ARG D 2 185 ? 36.688  75.232  54.926 1.00 58.75  ? 203 ARG D CA     1 
ATOM   10082 C C      . ARG D 2 185 ? 35.752  75.673  53.833 1.00 58.27  ? 203 ARG D C      1 
ATOM   10083 O O      . ARG D 2 185 ? 34.617  76.020  54.103 1.00 54.22  ? 203 ARG D O      1 
ATOM   10084 C CB     . ARG D 2 185 ? 36.750  76.333  55.955 1.00 63.65  ? 203 ARG D CB     1 
ATOM   10085 C CG     . ARG D 2 185 ? 37.882  76.237  56.964 1.00 72.84  ? 203 ARG D CG     1 
ATOM   10086 C CD     . ARG D 2 185 ? 37.687  77.308  58.024 1.00 69.38  ? 203 ARG D CD     1 
ATOM   10087 N NE     . ARG D 2 185 ? 38.846  77.504  58.882 1.00 72.84  ? 203 ARG D NE     1 
ATOM   10088 C CZ     . ARG D 2 185 ? 38.887  78.404  59.856 1.00 74.74  ? 203 ARG D CZ     1 
ATOM   10089 N NH1    . ARG D 2 185 ? 37.837  79.173  60.083 1.00 80.57  ? 203 ARG D NH1    1 
ATOM   10090 N NH2    . ARG D 2 185 ? 39.970  78.540  60.603 1.00 66.98  ? 203 ARG D NH2    1 
ATOM   10091 N N      . GLU D 2 186 ? 36.228  75.660  52.600 1.00 55.75  ? 204 GLU D N      1 
ATOM   10092 C CA     . GLU D 2 186 ? 35.386  76.056  51.521 1.00 50.30  ? 204 GLU D CA     1 
ATOM   10093 C C      . GLU D 2 186 ? 34.271  75.097  51.540 1.00 49.41  ? 204 GLU D C      1 
ATOM   10094 O O      . GLU D 2 186 ? 34.486  73.902  51.524 1.00 59.96  ? 204 GLU D O      1 
ATOM   10095 C CB     . GLU D 2 186 ? 36.144  75.928  50.217 1.00 50.39  ? 204 GLU D CB     1 
ATOM   10096 C CG     . GLU D 2 186 ? 35.408  76.542  49.038 1.00 73.86  ? 204 GLU D CG     1 
ATOM   10097 C CD     . GLU D 2 186 ? 36.247  76.623  47.779 1.00 83.04  ? 204 GLU D CD     1 
ATOM   10098 O OE1    . GLU D 2 186 ? 37.471  76.412  47.858 1.00 88.45  ? 204 GLU D OE1    1 
ATOM   10099 O OE2    . GLU D 2 186 ? 35.679  76.905  46.706 1.00 78.97  ? 204 GLU D OE2    1 
ATOM   10100 N N      . GLU D 2 187 ? 33.064  75.605  51.542 1.00 46.96  ? 205 GLU D N      1 
ATOM   10101 C CA     . GLU D 2 187 ? 31.953  74.727  51.650 1.00 50.26  ? 205 GLU D CA     1 
ATOM   10102 C C      . GLU D 2 187 ? 31.555  74.496  50.265 1.00 55.22  ? 205 GLU D C      1 
ATOM   10103 O O      . GLU D 2 187 ? 30.449  74.818  49.881 1.00 63.71  ? 205 GLU D O      1 
ATOM   10104 C CB     . GLU D 2 187 ? 30.797  75.331  52.414 1.00 48.43  ? 205 GLU D CB     1 
ATOM   10105 C CG     . GLU D 2 187 ? 31.071  75.568  53.885 1.00 57.30  ? 205 GLU D CG     1 
ATOM   10106 C CD     . GLU D 2 187 ? 30.840  74.330  54.717 1.00 63.67  ? 205 GLU D CD     1 
ATOM   10107 O OE1    . GLU D 2 187 ? 30.090  73.451  54.255 1.00 67.84  ? 205 GLU D OE1    1 
ATOM   10108 O OE2    . GLU D 2 187 ? 31.399  74.240  55.828 1.00 63.18  ? 205 GLU D OE2    1 
ATOM   10109 N N      . LEU D 2 188 ? 32.453  73.930  49.491 1.00 54.82  ? 206 LEU D N      1 
ATOM   10110 C CA     . LEU D 2 188 ? 32.085  73.584  48.146 1.00 52.51  ? 206 LEU D CA     1 
ATOM   10111 C C      . LEU D 2 188 ? 30.932  72.620  48.404 1.00 56.04  ? 206 LEU D C      1 
ATOM   10112 O O      . LEU D 2 188 ? 31.013  71.823  49.328 1.00 65.47  ? 206 LEU D O      1 
ATOM   10113 C CB     . LEU D 2 188 ? 33.293  72.894  47.538 1.00 53.42  ? 206 LEU D CB     1 
ATOM   10114 C CG     . LEU D 2 188 ? 33.556  72.729  46.048 1.00 57.28  ? 206 LEU D CG     1 
ATOM   10115 C CD1    . LEU D 2 188 ? 35.013  72.322  45.887 1.00 54.14  ? 206 LEU D CD1    1 
ATOM   10116 C CD2    . LEU D 2 188 ? 32.650  71.669  45.439 1.00 61.40  ? 206 LEU D CD2    1 
ATOM   10117 N N      . GLY D 2 189 ? 29.857  72.656  47.625 1.00 51.16  ? 207 GLY D N      1 
ATOM   10118 C CA     . GLY D 2 189 ? 28.702  71.830  47.931 1.00 55.38  ? 207 GLY D CA     1 
ATOM   10119 C C      . GLY D 2 189 ? 28.661  70.353  47.650 1.00 63.82  ? 207 GLY D C      1 
ATOM   10120 O O      . GLY D 2 189 ? 29.590  69.806  47.085 1.00 70.14  ? 207 GLY D O      1 
ATOM   10121 N N      . ASN D 2 190 ? 27.563  69.705  48.026 1.00 60.48  ? 208 ASN D N      1 
ATOM   10122 C CA     . ASN D 2 190 ? 27.398  68.281  47.797 1.00 59.81  ? 208 ASN D CA     1 
ATOM   10123 C C      . ASN D 2 190 ? 27.325  67.935  46.312 1.00 65.68  ? 208 ASN D C      1 
ATOM   10124 O O      . ASN D 2 190 ? 26.932  68.774  45.510 1.00 69.20  ? 208 ASN D O      1 
ATOM   10125 C CB     . ASN D 2 190 ? 26.135  67.807  48.499 1.00 53.38  ? 208 ASN D CB     1 
ATOM   10126 C CG     . ASN D 2 190 ? 26.276  67.746  50.004 1.00 68.00  ? 208 ASN D CG     1 
ATOM   10127 O OD1    . ASN D 2 190 ? 25.405  67.218  50.690 1.00 69.69  ? 208 ASN D OD1    1 
ATOM   10128 N ND2    . ASN D 2 190 ? 27.371  68.280  50.525 1.00 72.77  ? 208 ASN D ND2    1 
ATOM   10129 N N      . THR D 2 191 ? 27.691  66.708  45.933 1.00 58.70  ? 209 THR D N      1 
ATOM   10130 C CA     . THR D 2 191 ? 27.683  66.281  44.537 1.00 52.14  ? 209 THR D CA     1 
ATOM   10131 C C      . THR D 2 191 ? 27.105  64.923  44.458 1.00 47.94  ? 209 THR D C      1 
ATOM   10132 O O      . THR D 2 191 ? 27.221  64.163  45.384 1.00 52.57  ? 209 THR D O      1 
ATOM   10133 C CB     . THR D 2 191 ? 29.094  66.113  43.992 1.00 57.69  ? 209 THR D CB     1 
ATOM   10134 O OG1    . THR D 2 191 ? 29.891  65.423  44.957 1.00 62.97  ? 209 THR D OG1    1 
ATOM   10135 C CG2    . THR D 2 191 ? 29.723  67.458  43.694 1.00 70.13  ? 209 THR D CG2    1 
ATOM   10136 N N      . PRO D 2 192 ? 26.521  64.562  43.298 1.00 47.22  ? 210 PRO D N      1 
ATOM   10137 C CA     . PRO D 2 192 ? 26.026  63.197  43.309 1.00 44.55  ? 210 PRO D CA     1 
ATOM   10138 C C      . PRO D 2 192 ? 27.058  62.170  42.965 1.00 45.82  ? 210 PRO D C      1 
ATOM   10139 O O      . PRO D 2 192 ? 28.011  62.498  42.283 1.00 45.67  ? 210 PRO D O      1 
ATOM   10140 C CB     . PRO D 2 192 ? 24.962  63.201  42.219 1.00 39.70  ? 210 PRO D CB     1 
ATOM   10141 C CG     . PRO D 2 192 ? 24.729  64.620  41.851 1.00 56.03  ? 210 PRO D CG     1 
ATOM   10142 C CD     . PRO D 2 192 ? 26.051  65.262  42.083 1.00 58.51  ? 210 PRO D CD     1 
ATOM   10143 N N      . SER D 2 193 ? 26.866  60.940  43.424 1.00 44.44  ? 211 SER D N      1 
ATOM   10144 C CA     . SER D 2 193 ? 27.764  59.857  43.098 1.00 39.10  ? 211 SER D CA     1 
ATOM   10145 C C      . SER D 2 193 ? 27.045  58.576  43.222 1.00 38.53  ? 211 SER D C      1 
ATOM   10146 O O      . SER D 2 193 ? 26.211  58.416  44.085 1.00 38.60  ? 211 SER D O      1 
ATOM   10147 C CB     . SER D 2 193 ? 28.922  59.811  44.045 1.00 40.86  ? 211 SER D CB     1 
ATOM   10148 O OG     . SER D 2 193 ? 29.629  58.599  43.925 1.00 42.15  ? 211 SER D OG     1 
ATOM   10149 N N      . ALA D 2 194 ? 27.398  57.623  42.391 1.00 38.57  ? 212 ALA D N      1 
ATOM   10150 C CA     . ALA D 2 194 ? 26.806  56.312  42.480 1.00 40.77  ? 212 ALA D CA     1 
ATOM   10151 C C      . ALA D 2 194 ? 27.880  55.331  42.798 1.00 48.56  ? 212 ALA D C      1 
ATOM   10152 O O      . ALA D 2 194 ? 27.696  54.140  42.631 1.00 44.91  ? 212 ALA D O      1 
ATOM   10153 C CB     . ALA D 2 194 ? 26.171  55.948  41.176 1.00 34.79  ? 212 ALA D CB     1 
ATOM   10154 N N      . ASN D 2 195 ? 29.019  55.829  43.243 1.00 49.31  ? 213 ASN D N      1 
ATOM   10155 C CA     . ASN D 2 195 ? 30.131  54.974  43.554 1.00 44.10  ? 213 ASN D CA     1 
ATOM   10156 C C      . ASN D 2 195 ? 30.176  54.775  45.037 1.00 47.13  ? 213 ASN D C      1 
ATOM   10157 O O      . ASN D 2 195 ? 29.949  55.705  45.783 1.00 46.16  ? 213 ASN D O      1 
ATOM   10158 C CB     . ASN D 2 195 ? 31.415  55.591  43.040 1.00 38.40  ? 213 ASN D CB     1 
ATOM   10159 C CG     . ASN D 2 195 ? 31.472  55.648  41.538 1.00 44.77  ? 213 ASN D CG     1 
ATOM   10160 O OD1    . ASN D 2 195 ? 30.626  55.089  40.852 1.00 45.87  ? 213 ASN D OD1    1 
ATOM   10161 N ND2    . ASN D 2 195 ? 32.473  56.326  41.018 1.00 48.31  ? 213 ASN D ND2    1 
ATOM   10162 N N      . PRO D 2 196 ? 30.534  53.569  45.481 1.00 48.49  ? 214 PRO D N      1 
ATOM   10163 C CA     . PRO D 2 196 ? 30.498  53.272  46.903 1.00 40.73  ? 214 PRO D CA     1 
ATOM   10164 C C      . PRO D 2 196 ? 31.641  53.772  47.723 1.00 45.14  ? 214 PRO D C      1 
ATOM   10165 O O      . PRO D 2 196 ? 32.701  53.997  47.186 1.00 47.11  ? 214 PRO D O      1 
ATOM   10166 C CB     . PRO D 2 196 ? 30.597  51.760  46.917 1.00 41.68  ? 214 PRO D CB     1 
ATOM   10167 C CG     . PRO D 2 196 ? 30.338  51.293  45.533 1.00 42.80  ? 214 PRO D CG     1 
ATOM   10168 C CD     . PRO D 2 196 ? 30.902  52.380  44.703 1.00 45.48  ? 214 PRO D CD     1 
ATOM   10169 N N      . GLY D 2 197 ? 31.440  53.954  49.012 1.00 46.93  ? 215 GLY D N      1 
ATOM   10170 C CA     . GLY D 2 197 ? 32.521  54.315  49.908 1.00 44.23  ? 215 GLY D CA     1 
ATOM   10171 C C      . GLY D 2 197 ? 33.365  55.537  49.754 1.00 45.67  ? 215 GLY D C      1 
ATOM   10172 O O      . GLY D 2 197 ? 32.850  56.623  49.544 1.00 55.40  ? 215 GLY D O      1 
ATOM   10173 N N      . ILE D 2 198 ? 34.671  55.359  49.840 1.00 36.44  ? 216 ILE D N      1 
ATOM   10174 C CA     . ILE D 2 198 ? 35.582  56.465  49.715 1.00 37.77  ? 216 ILE D CA     1 
ATOM   10175 C C      . ILE D 2 198 ? 35.902  56.699  48.251 1.00 43.95  ? 216 ILE D C      1 
ATOM   10176 O O      . ILE D 2 198 ? 36.735  57.518  47.923 1.00 38.94  ? 216 ILE D O      1 
ATOM   10177 C CB     . ILE D 2 198 ? 36.842  56.236  50.527 1.00 32.30  ? 216 ILE D CB     1 
ATOM   10178 C CG1    . ILE D 2 198 ? 37.519  54.940  50.123 1.00 39.72  ? 216 ILE D CG1    1 
ATOM   10179 C CG2    . ILE D 2 198 ? 36.505  56.188  52.003 1.00 38.26  ? 216 ILE D CG2    1 
ATOM   10180 C CD1    . ILE D 2 198 ? 38.780  54.683  50.912 1.00 38.85  ? 216 ILE D CD1    1 
ATOM   10181 N N      . MET D 2 199 ? 35.243  55.970  47.366 1.00 44.22  ? 217 MET D N      1 
ATOM   10182 C CA     . MET D 2 199 ? 35.459  56.118  45.936 1.00 40.82  ? 217 MET D CA     1 
ATOM   10183 C C      . MET D 2 199 ? 35.021  57.481  45.478 1.00 47.36  ? 217 MET D C      1 
ATOM   10184 O O      . MET D 2 199 ? 34.121  58.066  46.058 1.00 47.38  ? 217 MET D O      1 
ATOM   10185 C CB     . MET D 2 199 ? 34.692  55.052  45.147 1.00 38.12  ? 217 MET D CB     1 
ATOM   10186 C CG     . MET D 2 199 ? 35.203  53.635  45.291 1.00 48.61  ? 217 MET D CG     1 
ATOM   10187 S SD     . MET D 2 199 ? 34.599  52.601  43.949 1.00 29.45  ? 217 MET D SD     1 
ATOM   10188 C CE     . MET D 2 199 ? 35.777  53.010  42.671 1.00 35.19  ? 217 MET D CE     1 
ATOM   10189 N N      . LYS D 2 200 ? 35.661  58.008  44.447 1.00 44.69  ? 218 LYS D N      1 
ATOM   10190 C CA     . LYS D 2 200 ? 35.345  59.340  43.997 1.00 34.02  ? 218 LYS D CA     1 
ATOM   10191 C C      . LYS D 2 200 ? 34.201  59.242  43.071 1.00 35.98  ? 218 LYS D C      1 
ATOM   10192 O O      . LYS D 2 200 ? 34.086  58.270  42.360 1.00 42.55  ? 218 LYS D O      1 
ATOM   10193 C CB     . LYS D 2 200 ? 36.531  59.980  43.315 1.00 34.32  ? 218 LYS D CB     1 
ATOM   10194 C CG     . LYS D 2 200 ? 37.523  60.606  44.273 1.00 39.11  ? 218 LYS D CG     1 
ATOM   10195 C CD     . LYS D 2 200 ? 38.596  61.370  43.527 1.00 41.15  ? 218 LYS D CD     1 
ATOM   10196 C CE     . LYS D 2 200 ? 39.377  60.453  42.605 1.00 51.36  ? 218 LYS D CE     1 
ATOM   10197 N NZ     . LYS D 2 200 ? 40.352  61.229  41.795 1.00 64.80  ? 218 LYS D NZ     1 
ATOM   10198 N N      . PRO D 2 201 ? 33.346  60.251  43.050 1.00 38.87  ? 219 PRO D N      1 
ATOM   10199 C CA     . PRO D 2 201 ? 32.151  60.095  42.244 1.00 41.17  ? 219 PRO D CA     1 
ATOM   10200 C C      . PRO D 2 201 ? 32.364  59.902  40.778 1.00 40.62  ? 219 PRO D C      1 
ATOM   10201 O O      . PRO D 2 201 ? 31.570  59.224  40.151 1.00 37.08  ? 219 PRO D O      1 
ATOM   10202 C CB     . PRO D 2 201 ? 31.451  61.431  42.447 1.00 44.67  ? 219 PRO D CB     1 
ATOM   10203 C CG     . PRO D 2 201 ? 32.500  62.396  42.830 1.00 47.40  ? 219 PRO D CG     1 
ATOM   10204 C CD     . PRO D 2 201 ? 33.317  61.563  43.744 1.00 52.44  ? 219 PRO D CD     1 
ATOM   10205 N N      . ASN D 2 202 ? 33.393  60.507  40.215 1.00 42.30  ? 220 ASN D N      1 
ATOM   10206 C CA     . ASN D 2 202 ? 33.591  60.466  38.778 1.00 41.82  ? 220 ASN D CA     1 
ATOM   10207 C C      . ASN D 2 202 ? 34.639  59.443  38.398 1.00 40.04  ? 220 ASN D C      1 
ATOM   10208 O O      . ASN D 2 202 ? 35.305  59.583  37.384 1.00 40.46  ? 220 ASN D O      1 
ATOM   10209 C CB     . ASN D 2 202 ? 34.015  61.856  38.284 1.00 35.11  ? 220 ASN D CB     1 
ATOM   10210 C CG     . ASN D 2 202 ? 32.939  62.899  38.447 1.00 30.38  ? 220 ASN D CG     1 
ATOM   10211 O OD1    . ASN D 2 202 ? 33.221  64.037  38.800 1.00 31.76  ? 220 ASN D OD1    1 
ATOM   10212 N ND2    . ASN D 2 202 ? 31.707  62.524  38.183 1.00 29.40  ? 220 ASN D ND2    1 
ATOM   10213 N N      . SER D 2 203 ? 34.809  58.421  39.213 1.00 36.44  ? 221 SER D N      1 
ATOM   10214 C CA     . SER D 2 203 ? 35.831  57.436  38.941 1.00 37.37  ? 221 SER D CA     1 
ATOM   10215 C C      . SER D 2 203 ? 35.270  56.087  38.630 1.00 38.95  ? 221 SER D C      1 
ATOM   10216 O O      . SER D 2 203 ? 34.272  55.681  39.186 1.00 38.27  ? 221 SER D O      1 
ATOM   10217 C CB     . SER D 2 203 ? 36.814  57.361  40.077 1.00 41.97  ? 221 SER D CB     1 
ATOM   10218 O OG     . SER D 2 203 ? 37.685  58.472  40.041 1.00 47.18  ? 221 SER D OG     1 
ATOM   10219 N N      . PRO D 2 204 ? 35.947  55.340  37.731 1.00 37.77  ? 222 PRO D N      1 
ATOM   10220 C CA     . PRO D 2 204 ? 35.311  54.099  37.340 1.00 38.66  ? 222 PRO D CA     1 
ATOM   10221 C C      . PRO D 2 204 ? 35.167  53.059  38.390 1.00 44.37  ? 222 PRO D C      1 
ATOM   10222 O O      . PRO D 2 204 ? 35.974  53.010  39.285 1.00 45.63  ? 222 PRO D O      1 
ATOM   10223 C CB     . PRO D 2 204 ? 36.263  53.575  36.294 1.00 39.07  ? 222 PRO D CB     1 
ATOM   10224 C CG     . PRO D 2 204 ? 36.863  54.778  35.693 1.00 35.03  ? 222 PRO D CG     1 
ATOM   10225 C CD     . PRO D 2 204 ? 37.176  55.538  36.927 1.00 37.09  ? 222 PRO D CD     1 
ATOM   10226 N N      . ASN D 2 205 ? 34.156  52.216  38.281 1.00 44.91  ? 223 ASN D N      1 
ATOM   10227 C CA     . ASN D 2 205 ? 33.999  51.113  39.204 1.00 43.27  ? 223 ASN D CA     1 
ATOM   10228 C C      . ASN D 2 205 ? 33.306  49.979  38.526 1.00 51.51  ? 223 ASN D C      1 
ATOM   10229 O O      . ASN D 2 205 ? 32.659  50.168  37.507 1.00 48.83  ? 223 ASN D O      1 
ATOM   10230 C CB     . ASN D 2 205 ? 33.297  51.479  40.506 1.00 39.48  ? 223 ASN D CB     1 
ATOM   10231 C CG     . ASN D 2 205 ? 31.992  52.182  40.300 1.00 52.47  ? 223 ASN D CG     1 
ATOM   10232 O OD1    . ASN D 2 205 ? 31.750  52.791  39.270 1.00 71.34  ? 223 ASN D OD1    1 
ATOM   10233 N ND2    . ASN D 2 205 ? 31.146  52.130  41.308 1.00 51.34  ? 223 ASN D ND2    1 
ATOM   10234 N N      . PHE D 2 206 ? 33.454  48.785  39.077 1.00 57.77  ? 224 PHE D N      1 
ATOM   10235 C CA     . PHE D 2 206 ? 32.880  47.635  38.450 1.00 51.85  ? 224 PHE D CA     1 
ATOM   10236 C C      . PHE D 2 206 ? 31.418  47.847  38.513 1.00 51.62  ? 224 PHE D C      1 
ATOM   10237 O O      . PHE D 2 206 ? 30.905  48.372  39.477 1.00 60.65  ? 224 PHE D O      1 
ATOM   10238 C CB     . PHE D 2 206 ? 33.248  46.377  39.192 1.00 53.96  ? 224 PHE D CB     1 
ATOM   10239 C CG     . PHE D 2 206 ? 34.708  46.199  39.425 1.00 50.02  ? 224 PHE D CG     1 
ATOM   10240 C CD1    . PHE D 2 206 ? 35.570  46.010  38.373 1.00 49.32  ? 224 PHE D CD1    1 
ATOM   10241 C CD2    . PHE D 2 206 ? 35.207  46.172  40.703 1.00 51.30  ? 224 PHE D CD2    1 
ATOM   10242 C CE1    . PHE D 2 206 ? 36.916  45.825  38.586 1.00 48.80  ? 224 PHE D CE1    1 
ATOM   10243 C CE2    . PHE D 2 206 ? 36.549  45.985  40.924 1.00 52.58  ? 224 PHE D CE2    1 
ATOM   10244 C CZ     . PHE D 2 206 ? 37.407  45.814  39.863 1.00 48.12  ? 224 PHE D CZ     1 
ATOM   10245 N N      . THR D 2 207 ? 30.724  47.435  37.486 1.00 40.60  ? 225 THR D N      1 
ATOM   10246 C CA     . THR D 2 207 ? 29.320  47.676  37.451 1.00 43.53  ? 225 THR D CA     1 
ATOM   10247 C C      . THR D 2 207 ? 28.572  46.946  38.557 1.00 55.28  ? 225 THR D C      1 
ATOM   10248 O O      . THR D 2 207 ? 27.443  47.298  38.865 1.00 57.20  ? 225 THR D O      1 
ATOM   10249 C CB     . THR D 2 207 ? 28.771  47.365  36.070 1.00 50.32  ? 225 THR D CB     1 
ATOM   10250 O OG1    . THR D 2 207 ? 29.252  46.091  35.655 1.00 65.93  ? 225 THR D OG1    1 
ATOM   10251 C CG2    . THR D 2 207 ? 29.256  48.396  35.080 1.00 49.19  ? 225 THR D CG2    1 
ATOM   10252 N N      . ASP D 2 208 ? 29.189  45.971  39.206 1.00 57.60  ? 226 ASP D N      1 
ATOM   10253 C CA     . ASP D 2 208 ? 28.513  45.302  40.310 1.00 52.57  ? 226 ASP D CA     1 
ATOM   10254 C C      . ASP D 2 208 ? 28.547  46.117  41.576 1.00 54.39  ? 226 ASP D C      1 
ATOM   10255 O O      . ASP D 2 208 ? 27.583  46.129  42.331 1.00 52.88  ? 226 ASP D O      1 
ATOM   10256 C CB     . ASP D 2 208 ? 28.990  43.857  40.535 1.00 50.81  ? 226 ASP D CB     1 
ATOM   10257 C CG     . ASP D 2 208 ? 30.489  43.719  40.628 1.00 60.22  ? 226 ASP D CG     1 
ATOM   10258 O OD1    . ASP D 2 208 ? 31.174  44.702  40.941 1.00 68.40  ? 226 ASP D OD1    1 
ATOM   10259 O OD2    . ASP D 2 208 ? 30.989  42.599  40.406 1.00 54.06  ? 226 ASP D OD2    1 
ATOM   10260 N N      . ASN D 2 209 ? 29.642  46.829  41.789 1.00 56.07  ? 227 ASN D N      1 
ATOM   10261 C CA     . ASN D 2 209 ? 29.791  47.638  42.984 1.00 58.24  ? 227 ASN D CA     1 
ATOM   10262 C C      . ASN D 2 209 ? 29.383  49.066  42.724 1.00 58.58  ? 227 ASN D C      1 
ATOM   10263 O O      . ASN D 2 209 ? 30.229  49.937  42.699 1.00 60.22  ? 227 ASN D O      1 
ATOM   10264 C CB     . ASN D 2 209 ? 31.231  47.593  43.477 1.00 55.27  ? 227 ASN D CB     1 
ATOM   10265 C CG     . ASN D 2 209 ? 31.694  46.192  43.793 1.00 62.74  ? 227 ASN D CG     1 
ATOM   10266 O OD1    . ASN D 2 209 ? 32.821  45.819  43.485 1.00 62.95  ? 227 ASN D OD1    1 
ATOM   10267 N ND2    . ASN D 2 209 ? 30.821  45.403  44.401 1.00 65.89  ? 227 ASN D ND2    1 
ATOM   10268 N N      . LEU D 2 210 ? 28.082  49.322  42.573 1.00 55.59  ? 228 LEU D N      1 
ATOM   10269 C CA     . LEU D 2 210 ? 27.558  50.671  42.356 1.00 47.95  ? 228 LEU D CA     1 
ATOM   10270 C C      . LEU D 2 210 ? 26.395  50.919  43.291 1.00 45.43  ? 228 LEU D C      1 
ATOM   10271 O O      . LEU D 2 210 ? 25.320  50.390  43.086 1.00 52.53  ? 228 LEU D O      1 
ATOM   10272 C CB     . LEU D 2 210 ? 27.072  50.828  40.924 1.00 46.96  ? 228 LEU D CB     1 
ATOM   10273 C CG     . LEU D 2 210 ? 28.021  51.137  39.772 1.00 53.74  ? 228 LEU D CG     1 
ATOM   10274 C CD1    . LEU D 2 210 ? 27.381  50.725  38.462 1.00 49.54  ? 228 LEU D CD1    1 
ATOM   10275 C CD2    . LEU D 2 210 ? 28.308  52.623  39.747 1.00 53.78  ? 228 LEU D CD2    1 
ATOM   10276 N N      . VAL D 2 211 ? 26.590  51.740  44.301 1.00 37.47  ? 229 VAL D N      1 
ATOM   10277 C CA     . VAL D 2 211 ? 25.555  52.032  45.260 1.00 34.94  ? 229 VAL D CA     1 
ATOM   10278 C C      . VAL D 2 211 ? 24.543  52.914  44.567 1.00 39.84  ? 229 VAL D C      1 
ATOM   10279 O O      . VAL D 2 211 ? 24.852  53.571  43.586 1.00 41.75  ? 229 VAL D O      1 
ATOM   10280 C CB     . VAL D 2 211 ? 26.177  52.728  46.475 1.00 40.43  ? 229 VAL D CB     1 
ATOM   10281 C CG1    . VAL D 2 211 ? 26.395  54.207  46.228 1.00 47.48  ? 229 VAL D CG1    1 
ATOM   10282 C CG2    . VAL D 2 211 ? 25.395  52.485  47.753 1.00 43.22  ? 229 VAL D CG2    1 
ATOM   10283 N N      . PRO D 2 212 ? 23.276  52.924  45.047 1.00 40.10  ? 230 PRO D N      1 
ATOM   10284 C CA     . PRO D 2 212 ? 22.367  53.857  44.391 1.00 38.55  ? 230 PRO D CA     1 
ATOM   10285 C C      . PRO D 2 212 ? 22.798  55.301  44.459 1.00 42.22  ? 230 PRO D C      1 
ATOM   10286 O O      . PRO D 2 212 ? 23.481  55.685  45.385 1.00 59.79  ? 230 PRO D O      1 
ATOM   10287 C CB     . PRO D 2 212 ? 21.107  53.688  45.203 1.00 37.70  ? 230 PRO D CB     1 
ATOM   10288 C CG     . PRO D 2 212 ? 21.086  52.250  45.517 1.00 46.22  ? 230 PRO D CG     1 
ATOM   10289 C CD     . PRO D 2 212 ? 22.504  51.975  45.890 1.00 46.34  ? 230 PRO D CD     1 
ATOM   10290 N N      . VAL D 2 213 ? 22.369  56.117  43.514 1.00 36.38  ? 231 VAL D N      1 
ATOM   10291 C CA     . VAL D 2 213 ? 22.814  57.495  43.476 1.00 35.32  ? 231 VAL D CA     1 
ATOM   10292 C C      . VAL D 2 213 ? 22.450  58.236  44.715 1.00 35.14  ? 231 VAL D C      1 
ATOM   10293 O O      . VAL D 2 213 ? 21.340  58.125  45.202 1.00 40.82  ? 231 VAL D O      1 
ATOM   10294 C CB     . VAL D 2 213 ? 22.339  58.212  42.209 1.00 47.54  ? 231 VAL D CB     1 
ATOM   10295 C CG1    . VAL D 2 213 ? 20.860  57.970  41.967 1.00 53.07  ? 231 VAL D CG1    1 
ATOM   10296 C CG2    . VAL D 2 213 ? 22.678  59.691  42.229 1.00 40.84  ? 231 VAL D CG2    1 
ATOM   10297 N N      . ARG D 2 214 ? 23.383  58.993  45.254 1.00 43.73  ? 232 ARG D N      1 
ATOM   10298 C CA     . ARG D 2 214 ? 23.142  59.730  46.474 1.00 48.15  ? 232 ARG D CA     1 
ATOM   10299 C C      . ARG D 2 214 ? 23.787  61.050  46.288 1.00 52.92  ? 232 ARG D C      1 
ATOM   10300 O O      . ARG D 2 214 ? 24.309  61.325  45.226 1.00 53.28  ? 232 ARG D O      1 
ATOM   10301 C CB     . ARG D 2 214 ? 23.846  59.016  47.603 1.00 39.72  ? 232 ARG D CB     1 
ATOM   10302 C CG     . ARG D 2 214 ? 25.224  58.528  47.212 1.00 41.37  ? 232 ARG D CG     1 
ATOM   10303 C CD     . ARG D 2 214 ? 25.863  57.685  48.289 1.00 41.51  ? 232 ARG D CD     1 
ATOM   10304 N NE     . ARG D 2 214 ? 27.247  57.396  47.949 1.00 41.29  ? 232 ARG D NE     1 
ATOM   10305 C CZ     . ARG D 2 214 ? 28.111  56.816  48.769 1.00 57.17  ? 232 ARG D CZ     1 
ATOM   10306 N NH1    . ARG D 2 214 ? 27.734  56.455  49.987 1.00 59.13  ? 232 ARG D NH1    1 
ATOM   10307 N NH2    . ARG D 2 214 ? 29.353  56.603  48.373 1.00 56.55  ? 232 ARG D NH2    1 
ATOM   10308 N N      . ASP D 2 215 ? 23.794  61.882  47.313 1.00 53.10  ? 233 ASP D N      1 
ATOM   10309 C CA     . ASP D 2 215 ? 24.501  63.146  47.218 1.00 52.65  ? 233 ASP D CA     1 
ATOM   10310 C C      . ASP D 2 215 ? 25.674  63.129  48.160 1.00 52.87  ? 233 ASP D C      1 
ATOM   10311 O O      . ASP D 2 215 ? 25.538  63.469  49.325 1.00 53.45  ? 233 ASP D O      1 
ATOM   10312 C CB     . ASP D 2 215 ? 23.579  64.318  47.510 1.00 52.05  ? 233 ASP D CB     1 
ATOM   10313 C CG     . ASP D 2 215 ? 23.234  65.110  46.269 1.00 56.75  ? 233 ASP D CG     1 
ATOM   10314 O OD1    . ASP D 2 215 ? 23.826  64.842  45.211 1.00 53.13  ? 233 ASP D OD1    1 
ATOM   10315 O OD2    . ASP D 2 215 ? 22.374  66.008  46.348 1.00 57.80  ? 233 ASP D OD2    1 
ATOM   10316 N N      . VAL D 2 216 ? 26.840  62.749  47.659 1.00 48.78  ? 234 VAL D N      1 
ATOM   10317 C CA     . VAL D 2 216 ? 28.023  62.719  48.476 1.00 43.38  ? 234 VAL D CA     1 
ATOM   10318 C C      . VAL D 2 216 ? 28.554  64.112  48.637 1.00 49.62  ? 234 VAL D C      1 
ATOM   10319 O O      . VAL D 2 216 ? 28.413  64.936  47.767 1.00 60.01  ? 234 VAL D O      1 
ATOM   10320 C CB     . VAL D 2 216 ? 29.105  61.835  47.868 1.00 42.77  ? 234 VAL D CB     1 
ATOM   10321 C CG1    . VAL D 2 216 ? 28.552  60.455  47.608 1.00 53.17  ? 234 VAL D CG1    1 
ATOM   10322 C CG2    . VAL D 2 216 ? 29.697  62.426  46.604 1.00 41.81  ? 234 VAL D CG2    1 
ATOM   10323 N N      . PRO D 2 217 ? 29.195  64.408  49.783 1.00 50.59  ? 235 PRO D N      1 
ATOM   10324 C CA     . PRO D 2 217 ? 29.690  65.769  49.819 1.00 46.11  ? 235 PRO D CA     1 
ATOM   10325 C C      . PRO D 2 217 ? 31.020  65.921  49.187 1.00 47.08  ? 235 PRO D C      1 
ATOM   10326 O O      . PRO D 2 217 ? 31.717  64.943  49.001 1.00 50.23  ? 235 PRO D O      1 
ATOM   10327 C CB     . PRO D 2 217 ? 29.849  66.031  51.297 1.00 54.63  ? 235 PRO D CB     1 
ATOM   10328 C CG     . PRO D 2 217 ? 28.992  65.029  51.984 1.00 60.62  ? 235 PRO D CG     1 
ATOM   10329 C CD     . PRO D 2 217 ? 29.213  63.827  51.142 1.00 64.00  ? 235 PRO D CD     1 
ATOM   10330 N N      . LYS D 2 218 ? 31.387  67.154  48.879 1.00 51.86  ? 236 LYS D N      1 
ATOM   10331 C CA     . LYS D 2 218 ? 32.674  67.426  48.282 1.00 56.05  ? 236 LYS D CA     1 
ATOM   10332 C C      . LYS D 2 218 ? 33.529  68.214  49.251 1.00 55.46  ? 236 LYS D C      1 
ATOM   10333 O O      . LYS D 2 218 ? 33.052  69.173  49.841 1.00 49.61  ? 236 LYS D O      1 
ATOM   10334 C CB     . LYS D 2 218 ? 32.494  68.171  46.979 1.00 59.78  ? 236 LYS D CB     1 
ATOM   10335 C CG     . LYS D 2 218 ? 33.373  67.645  45.859 1.00 67.09  ? 236 LYS D CG     1 
ATOM   10336 C CD     . LYS D 2 218 ? 33.270  66.132  45.766 1.00 71.89  ? 236 LYS D CD     1 
ATOM   10337 C CE     . LYS D 2 218 ? 34.176  65.575  44.681 1.00 76.27  ? 236 LYS D CE     1 
ATOM   10338 N NZ     . LYS D 2 218 ? 35.609  65.878  44.936 1.00 85.04  ? 236 LYS D NZ     1 
ATOM   10339 N N      . ILE D 2 219 ? 34.776  67.795  49.465 1.00 52.78  ? 237 ILE D N      1 
ATOM   10340 C CA     . ILE D 2 219 ? 35.654  68.441  50.426 1.00 45.78  ? 237 ILE D CA     1 
ATOM   10341 C C      . ILE D 2 219 ? 36.933  68.806  49.700 1.00 44.05  ? 237 ILE D C      1 
ATOM   10342 O O      . ILE D 2 219 ? 37.182  68.280  48.623 1.00 42.99  ? 237 ILE D O      1 
ATOM   10343 C CB     . ILE D 2 219 ? 35.915  67.532  51.642 1.00 36.68  ? 237 ILE D CB     1 
ATOM   10344 C CG1    . ILE D 2 219 ? 34.609  67.160  52.331 1.00 35.93  ? 237 ILE D CG1    1 
ATOM   10345 C CG2    . ILE D 2 219 ? 36.834  68.190  52.645 1.00 36.31  ? 237 ILE D CG2    1 
ATOM   10346 C CD1    . ILE D 2 219 ? 34.109  65.778  51.981 1.00 44.01  ? 237 ILE D CD1    1 
ATOM   10347 N N      . ALA D 2 220 ? 37.759  69.705  50.244 1.00 42.35  ? 238 ALA D N      1 
ATOM   10348 C CA     . ALA D 2 220 ? 38.962  70.170  49.567 1.00 39.72  ? 238 ALA D CA     1 
ATOM   10349 C C      . ALA D 2 220 ? 40.177  70.232  50.427 1.00 43.30  ? 238 ALA D C      1 
ATOM   10350 O O      . ALA D 2 220 ? 40.056  70.258  51.622 1.00 49.23  ? 238 ALA D O      1 
ATOM   10351 C CB     . ALA D 2 220 ? 38.696  71.537  49.056 1.00 50.29  ? 238 ALA D CB     1 
ATOM   10352 N N      . ILE D 2 221 ? 41.353  70.334  49.839 1.00 40.25  ? 239 ILE D N      1 
ATOM   10353 C CA     . ILE D 2 221 ? 42.577  70.287  50.614 1.00 47.77  ? 239 ILE D CA     1 
ATOM   10354 C C      . ILE D 2 221 ? 43.240  71.628  50.729 1.00 56.43  ? 239 ILE D C      1 
ATOM   10355 O O      . ILE D 2 221 ? 43.434  72.296  49.736 1.00 66.98  ? 239 ILE D O      1 
ATOM   10356 C CB     . ILE D 2 221 ? 43.608  69.355  49.969 1.00 54.37  ? 239 ILE D CB     1 
ATOM   10357 C CG1    . ILE D 2 221 ? 43.029  67.993  49.644 1.00 60.26  ? 239 ILE D CG1    1 
ATOM   10358 C CG2    . ILE D 2 221 ? 44.813  69.148  50.862 1.00 56.78  ? 239 ILE D CG2    1 
ATOM   10359 C CD1    . ILE D 2 221 ? 44.098  66.966  49.353 1.00 53.38  ? 239 ILE D CD1    1 
ATOM   10360 N N      . ASN D 2 222 ? 43.602  72.044  51.929 1.00 56.11  ? 240 ASN D N      1 
ATOM   10361 C CA     . ASN D 2 222 ? 44.144  73.363  52.063 1.00 59.28  ? 240 ASN D CA     1 
ATOM   10362 C C      . ASN D 2 222 ? 45.407  73.460  51.319 1.00 62.53  ? 240 ASN D C      1 
ATOM   10363 O O      . ASN D 2 222 ? 45.603  74.420  50.601 1.00 57.29  ? 240 ASN D O      1 
ATOM   10364 C CB     . ASN D 2 222 ? 44.424  73.696  53.505 1.00 56.30  ? 240 ASN D CB     1 
ATOM   10365 C CG     . ASN D 2 222 ? 44.407  75.186  53.769 1.00 62.88  ? 240 ASN D CG     1 
ATOM   10366 O OD1    . ASN D 2 222 ? 45.142  75.688  54.612 1.00 60.87  ? 240 ASN D OD1    1 
ATOM   10367 N ND2    . ASN D 2 222 ? 43.566  75.902  53.042 1.00 74.74  ? 240 ASN D ND2    1 
ATOM   10368 N N      . GLU D 2 223 ? 46.294  72.511  51.497 1.00 67.14  ? 241 GLU D N      1 
ATOM   10369 C CA     . GLU D 2 223 ? 47.528  72.476  50.718 1.00 69.39  ? 241 GLU D CA     1 
ATOM   10370 C C      . GLU D 2 223 ? 48.460  73.607  51.056 1.00 66.66  ? 241 GLU D C      1 
ATOM   10371 O O      . GLU D 2 223 ? 49.468  73.811  50.405 1.00 70.65  ? 241 GLU D O      1 
ATOM   10372 C CB     . GLU D 2 223 ? 47.259  72.398  49.206 1.00 67.26  ? 241 GLU D CB     1 
ATOM   10373 C CG     . GLU D 2 223 ? 48.315  71.649  48.409 1.00 68.46  ? 241 GLU D CG     1 
ATOM   10374 C CD     . GLU D 2 223 ? 48.060  71.702  46.920 1.00 79.02  ? 241 GLU D CD     1 
ATOM   10375 O OE1    . GLU D 2 223 ? 46.919  72.024  46.530 1.00 80.47  ? 241 GLU D OE1    1 
ATOM   10376 O OE2    . GLU D 2 223 ? 48.997  71.419  46.143 1.00 74.38  ? 241 GLU D OE2    1 
ATOM   10377 N N      . LYS D 2 224 ? 48.134  74.352  52.077 1.00 56.93  ? 242 LYS D N      1 
ATOM   10378 C CA     . LYS D 2 224 ? 49.027  75.373  52.500 1.00 58.26  ? 242 LYS D CA     1 
ATOM   10379 C C      . LYS D 2 224 ? 49.357  75.007  53.912 1.00 69.42  ? 242 LYS D C      1 
ATOM   10380 O O      . LYS D 2 224 ? 50.036  75.743  54.603 1.00 76.89  ? 242 LYS D O      1 
ATOM   10381 C CB     . LYS D 2 224 ? 48.353  76.724  52.429 1.00 59.58  ? 242 LYS D CB     1 
ATOM   10382 C CG     . LYS D 2 224 ? 48.043  77.211  51.027 1.00 63.85  ? 242 LYS D CG     1 
ATOM   10383 C CD     . LYS D 2 224 ? 47.292  78.530  51.066 1.00 57.81  ? 242 LYS D CD     1 
ATOM   10384 C CE     . LYS D 2 224 ? 45.874  78.352  51.580 1.00 57.99  ? 242 LYS D CE     1 
ATOM   10385 N NZ     . LYS D 2 224 ? 44.994  77.698  50.574 1.00 53.58  ? 242 LYS D NZ     1 
ATOM   10386 N N      . VAL D 2 225 ? 48.847  73.876  54.365 1.00 66.37  ? 243 VAL D N      1 
ATOM   10387 C CA     . VAL D 2 225 ? 49.120  73.421  55.697 1.00 54.29  ? 243 VAL D CA     1 
ATOM   10388 C C      . VAL D 2 225 ? 50.434  72.758  55.554 1.00 58.64  ? 243 VAL D C      1 
ATOM   10389 O O      . VAL D 2 225 ? 50.681  72.078  54.582 1.00 63.86  ? 243 VAL D O      1 
ATOM   10390 C CB     . VAL D 2 225 ? 48.105  72.396  56.145 1.00 44.79  ? 243 VAL D CB     1 
ATOM   10391 C CG1    . VAL D 2 225 ? 48.464  71.847  57.509 1.00 48.20  ? 243 VAL D CG1    1 
ATOM   10392 C CG2    . VAL D 2 225 ? 46.735  73.029  56.202 1.00 51.11  ? 243 VAL D CG2    1 
ATOM   10393 N N      . ALA D 2 226 ? 51.307  72.978  56.502 1.00 54.58  ? 244 ALA D N      1 
ATOM   10394 C CA     . ALA D 2 226 ? 52.590  72.356  56.464 1.00 57.67  ? 244 ALA D CA     1 
ATOM   10395 C C      . ALA D 2 226 ? 52.561  71.137  57.337 1.00 65.29  ? 244 ALA D C      1 
ATOM   10396 O O      . ALA D 2 226 ? 52.213  71.228  58.502 1.00 63.63  ? 244 ALA D O      1 
ATOM   10397 C CB     . ALA D 2 226 ? 53.617  73.319  56.964 1.00 45.68  ? 244 ALA D CB     1 
ATOM   10398 N N      . GLY D 2 227 ? 52.940  69.991  56.786 1.00 63.11  ? 245 GLY D N      1 
ATOM   10399 C CA     . GLY D 2 227 ? 52.951  68.764  57.549 1.00 59.13  ? 245 GLY D CA     1 
ATOM   10400 C C      . GLY D 2 227 ? 51.580  68.202  57.545 1.00 59.56  ? 245 GLY D C      1 
ATOM   10401 O O      . GLY D 2 227 ? 51.237  67.382  58.376 1.00 60.05  ? 245 GLY D O      1 
ATOM   10402 N N      . GLY D 2 228 ? 50.787  68.658  56.604 1.00 55.12  ? 246 GLY D N      1 
ATOM   10403 C CA     . GLY D 2 228 ? 49.426  68.209  56.544 1.00 57.07  ? 246 GLY D CA     1 
ATOM   10404 C C      . GLY D 2 228 ? 49.424  66.731  56.408 1.00 56.14  ? 246 GLY D C      1 
ATOM   10405 O O      . GLY D 2 228 ? 50.358  66.151  55.877 1.00 57.60  ? 246 GLY D O      1 
ATOM   10406 N N      . TYR D 2 229 ? 48.366  66.103  56.888 1.00 51.81  ? 247 TYR D N      1 
ATOM   10407 C CA     . TYR D 2 229 ? 48.305  64.672  56.832 1.00 53.45  ? 247 TYR D CA     1 
ATOM   10408 C C      . TYR D 2 229 ? 48.487  64.321  55.409 1.00 57.36  ? 247 TYR D C      1 
ATOM   10409 O O      . TYR D 2 229 ? 49.154  63.355  55.085 1.00 63.07  ? 247 TYR D O      1 
ATOM   10410 C CB     . TYR D 2 229 ? 46.970  64.154  57.301 1.00 46.71  ? 247 TYR D CB     1 
ATOM   10411 C CG     . TYR D 2 229 ? 46.977  62.673  57.488 1.00 45.66  ? 247 TYR D CG     1 
ATOM   10412 C CD1    . TYR D 2 229 ? 47.954  62.076  58.250 1.00 50.56  ? 247 TYR D CD1    1 
ATOM   10413 C CD2    . TYR D 2 229 ? 46.023  61.871  56.895 1.00 48.95  ? 247 TYR D CD2    1 
ATOM   10414 C CE1    . TYR D 2 229 ? 47.983  60.718  58.425 1.00 61.52  ? 247 TYR D CE1    1 
ATOM   10415 C CE2    . TYR D 2 229 ? 46.041  60.508  57.068 1.00 48.20  ? 247 TYR D CE2    1 
ATOM   10416 C CZ     . TYR D 2 229 ? 47.028  59.944  57.836 1.00 57.72  ? 247 TYR D CZ     1 
ATOM   10417 O OH     . TYR D 2 229 ? 47.076  58.593  58.021 1.00 59.37  ? 247 TYR D OH     1 
ATOM   10418 N N      . SER D 2 230 ? 47.973  65.141  54.524 1.00 57.79  ? 248 SER D N      1 
ATOM   10419 C CA     . SER D 2 230 ? 48.018  64.772  53.130 1.00 58.00  ? 248 SER D CA     1 
ATOM   10420 C C      . SER D 2 230 ? 49.392  64.811  52.544 1.00 58.94  ? 248 SER D C      1 
ATOM   10421 O O      . SER D 2 230 ? 49.638  64.210  51.516 1.00 62.62  ? 248 SER D O      1 
ATOM   10422 C CB     . SER D 2 230 ? 47.107  65.675  52.347 1.00 66.33  ? 248 SER D CB     1 
ATOM   10423 O OG     . SER D 2 230 ? 45.948  65.967  53.104 1.00 65.00  ? 248 SER D OG     1 
ATOM   10424 N N      . LYS D 2 231 ? 50.304  65.501  53.188 1.00 55.26  ? 249 LYS D N      1 
ATOM   10425 C CA     . LYS D 2 231 ? 51.612  65.646  52.607 1.00 52.77  ? 249 LYS D CA     1 
ATOM   10426 C C      . LYS D 2 231 ? 52.542  64.732  53.306 1.00 60.00  ? 249 LYS D C      1 
ATOM   10427 O O      . LYS D 2 231 ? 53.610  64.422  52.807 1.00 61.84  ? 249 LYS D O      1 
ATOM   10428 C CB     . LYS D 2 231 ? 52.085  67.059  52.774 1.00 54.75  ? 249 LYS D CB     1 
ATOM   10429 C CG     . LYS D 2 231 ? 51.217  68.085  52.076 1.00 62.61  ? 249 LYS D CG     1 
ATOM   10430 C CD     . LYS D 2 231 ? 51.793  69.480  52.212 1.00 56.72  ? 249 LYS D CD     1 
ATOM   10431 C CE     . LYS D 2 231 ? 50.802  70.494  51.691 1.00 49.85  ? 249 LYS D CE     1 
ATOM   10432 N NZ     . LYS D 2 231 ? 49.482  70.239  52.324 1.00 59.74  ? 249 LYS D NZ     1 
ATOM   10433 N N      . THR D 2 232 ? 52.134  64.284  54.475 1.00 62.63  ? 250 THR D N      1 
ATOM   10434 C CA     . THR D 2 232 ? 52.952  63.366  55.214 1.00 60.55  ? 250 THR D CA     1 
ATOM   10435 C C      . THR D 2 232 ? 52.611  61.997  54.730 1.00 61.46  ? 250 THR D C      1 
ATOM   10436 O O      . THR D 2 232 ? 53.490  61.168  54.521 1.00 63.43  ? 250 THR D O      1 
ATOM   10437 C CB     . THR D 2 232 ? 52.692  63.433  56.721 1.00 54.28  ? 250 THR D CB     1 
ATOM   10438 O OG1    . THR D 2 232 ? 51.355  63.026  57.014 1.00 56.91  ? 250 THR D OG1    1 
ATOM   10439 C CG2    . THR D 2 232 ? 52.917  64.833  57.233 1.00 53.12  ? 250 THR D CG2    1 
ATOM   10440 N N      . LYS D 2 233 ? 51.330  61.753  54.533 1.00 58.82  ? 251 LYS D N      1 
ATOM   10441 C CA     . LYS D 2 233 ? 50.893  60.451  54.091 1.00 56.79  ? 251 LYS D CA     1 
ATOM   10442 C C      . LYS D 2 233 ? 50.358  60.652  52.723 1.00 55.90  ? 251 LYS D C      1 
ATOM   10443 O O      . LYS D 2 233 ? 49.165  60.740  52.549 1.00 53.07  ? 251 LYS D O      1 
ATOM   10444 C CB     . LYS D 2 233 ? 49.760  59.961  54.967 1.00 48.68  ? 251 LYS D CB     1 
ATOM   10445 C CG     . LYS D 2 233 ? 49.567  58.459  55.010 1.00 56.11  ? 251 LYS D CG     1 
ATOM   10446 C CD     . LYS D 2 233 ? 50.612  57.799  55.888 1.00 59.54  ? 251 LYS D CD     1 
ATOM   10447 C CE     . LYS D 2 233 ? 50.168  56.411  56.310 1.00 59.92  ? 251 LYS D CE     1 
ATOM   10448 N NZ     . LYS D 2 233 ? 51.250  55.674  57.017 1.00 77.10  ? 251 LYS D NZ     1 
ATOM   10449 N N      . PRO D 2 234 ? 51.248  60.718  51.713 1.00 53.30  ? 252 PRO D N      1 
ATOM   10450 C CA     . PRO D 2 234 ? 50.624  60.882  50.422 1.00 53.84  ? 252 PRO D CA     1 
ATOM   10451 C C      . PRO D 2 234 ? 49.997  59.609  50.001 1.00 54.75  ? 252 PRO D C      1 
ATOM   10452 O O      . PRO D 2 234 ? 49.411  59.574  48.943 1.00 58.21  ? 252 PRO D O      1 
ATOM   10453 C CB     . PRO D 2 234 ? 51.803  61.162  49.527 1.00 55.25  ? 252 PRO D CB     1 
ATOM   10454 C CG     . PRO D 2 234 ? 52.928  60.425  50.129 1.00 50.71  ? 252 PRO D CG     1 
ATOM   10455 C CD     . PRO D 2 234 ? 52.725  60.695  51.578 1.00 56.73  ? 252 PRO D CD     1 
ATOM   10456 N N      . THR D 2 235 ? 50.083  58.573  50.813 1.00 48.07  ? 253 THR D N      1 
ATOM   10457 C CA     . THR D 2 235 ? 49.585  57.272  50.422 1.00 46.85  ? 253 THR D CA     1 
ATOM   10458 C C      . THR D 2 235 ? 48.165  57.085  50.848 1.00 46.96  ? 253 THR D C      1 
ATOM   10459 O O      . THR D 2 235 ? 47.663  55.980  50.826 1.00 42.48  ? 253 THR D O      1 
ATOM   10460 C CB     . THR D 2 235 ? 50.421  56.168  51.070 1.00 40.92  ? 253 THR D CB     1 
ATOM   10461 O OG1    . THR D 2 235 ? 50.238  56.199  52.485 1.00 49.76  ? 253 THR D OG1    1 
ATOM   10462 C CG2    . THR D 2 235 ? 51.881  56.357  50.758 1.00 43.01  ? 253 THR D CG2    1 
ATOM   10463 N N      . THR D 2 236 ? 47.506  58.155  51.253 1.00 46.28  ? 254 THR D N      1 
ATOM   10464 C CA     . THR D 2 236 ? 46.171  57.999  51.792 1.00 46.76  ? 254 THR D CA     1 
ATOM   10465 C C      . THR D 2 236 ? 45.122  58.606  50.932 1.00 44.03  ? 254 THR D C      1 
ATOM   10466 O O      . THR D 2 236 ? 45.285  59.682  50.387 1.00 49.07  ? 254 THR D O      1 
ATOM   10467 C CB     . THR D 2 236 ? 46.046  58.516  53.244 1.00 46.10  ? 254 THR D CB     1 
ATOM   10468 O OG1    . THR D 2 236 ? 44.841  58.020  53.835 1.00 40.82  ? 254 THR D OG1    1 
ATOM   10469 C CG2    . THR D 2 236 ? 46.054  60.029  53.312 1.00 46.62  ? 254 THR D CG2    1 
ATOM   10470 N N      . PRO D 2 237 ? 44.038  57.881  50.771 1.00 42.56  ? 255 PRO D N      1 
ATOM   10471 C CA     . PRO D 2 237 ? 42.968  58.473  50.038 1.00 44.68  ? 255 PRO D CA     1 
ATOM   10472 C C      . PRO D 2 237 ? 42.445  59.569  50.895 1.00 42.69  ? 255 PRO D C      1 
ATOM   10473 O O      . PRO D 2 237 ? 42.358  59.346  52.077 1.00 48.66  ? 255 PRO D O      1 
ATOM   10474 C CB     . PRO D 2 237 ? 41.976  57.353  50.029 1.00 48.92  ? 255 PRO D CB     1 
ATOM   10475 C CG     . PRO D 2 237 ? 42.779  56.120  49.999 1.00 46.25  ? 255 PRO D CG     1 
ATOM   10476 C CD     . PRO D 2 237 ? 43.812  56.445  51.009 1.00 43.27  ? 255 PRO D CD     1 
ATOM   10477 N N      . PHE D 2 238 ? 42.097  60.721  50.352 1.00 42.63  ? 256 PHE D N      1 
ATOM   10478 C CA     . PHE D 2 238 ? 41.665  61.822  51.172 1.00 42.63  ? 256 PHE D CA     1 
ATOM   10479 C C      . PHE D 2 238 ? 40.192  61.951  51.020 1.00 45.33  ? 256 PHE D C      1 
ATOM   10480 O O      . PHE D 2 238 ? 39.728  62.119  49.911 1.00 55.44  ? 256 PHE D O      1 
ATOM   10481 C CB     . PHE D 2 238 ? 42.311  63.089  50.647 1.00 41.86  ? 256 PHE D CB     1 
ATOM   10482 C CG     . PHE D 2 238 ? 41.729  64.368  51.180 1.00 42.83  ? 256 PHE D CG     1 
ATOM   10483 C CD1    . PHE D 2 238 ? 42.236  64.949  52.319 1.00 51.23  ? 256 PHE D CD1    1 
ATOM   10484 C CD2    . PHE D 2 238 ? 40.721  65.021  50.506 1.00 41.44  ? 256 PHE D CD2    1 
ATOM   10485 C CE1    . PHE D 2 238 ? 41.721  66.134  52.799 1.00 41.40  ? 256 PHE D CE1    1 
ATOM   10486 C CE2    . PHE D 2 238 ? 40.200  66.201  50.984 1.00 40.57  ? 256 PHE D CE2    1 
ATOM   10487 C CZ     . PHE D 2 238 ? 40.701  66.760  52.130 1.00 36.41  ? 256 PHE D CZ     1 
ATOM   10488 N N      . VAL D 2 239 ? 39.421  61.848  52.089 1.00 38.49  ? 257 VAL D N      1 
ATOM   10489 C CA     . VAL D 2 239 ? 38.017  62.158  52.055 1.00 40.17  ? 257 VAL D CA     1 
ATOM   10490 C C      . VAL D 2 239 ? 38.508  63.015  53.156 1.00 42.96  ? 257 VAL D C      1 
ATOM   10491 O O      . VAL D 2 239 ? 39.700  63.067  53.267 1.00 42.98  ? 257 VAL D O      1 
ATOM   10492 C CB     . VAL D 2 239 ? 37.215  60.967  52.433 1.00 38.17  ? 257 VAL D CB     1 
ATOM   10493 C CG1    . VAL D 2 239 ? 35.769  61.196  52.061 1.00 45.63  ? 257 VAL D CG1    1 
ATOM   10494 C CG2    . VAL D 2 239 ? 37.747  59.741  51.720 1.00 46.55  ? 257 VAL D CG2    1 
ATOM   10495 N N      . ALA D 2 240 ? 37.712  63.659  53.990 1.00 49.58  ? 258 ALA D N      1 
ATOM   10496 C CA     . ALA D 2 240 ? 38.240  64.631  54.990 1.00 49.51  ? 258 ALA D CA     1 
ATOM   10497 C C      . ALA D 2 240 ? 39.522  64.202  55.670 1.00 51.17  ? 258 ALA D C      1 
ATOM   10498 O O      . ALA D 2 240 ? 39.691  63.073  56.073 1.00 53.17  ? 258 ALA D O      1 
ATOM   10499 C CB     . ALA D 2 240 ? 37.190  64.892  56.022 1.00 44.80  ? 258 ALA D CB     1 
ATOM   10500 N N      . SER D 2 241 ? 40.421  65.123  55.909 1.00 37.58  ? 259 SER D N      1 
ATOM   10501 C CA     . SER D 2 241 ? 41.720  64.688  56.374 1.00 41.85  ? 259 SER D CA     1 
ATOM   10502 C C      . SER D 2 241 ? 41.824  63.889  57.641 1.00 50.74  ? 259 SER D C      1 
ATOM   10503 O O      . SER D 2 241 ? 42.623  62.991  57.678 1.00 59.92  ? 259 SER D O      1 
ATOM   10504 C CB     . SER D 2 241 ? 42.746  65.794  56.346 1.00 39.01  ? 259 SER D CB     1 
ATOM   10505 O OG     . SER D 2 241 ? 44.026  65.288  56.039 1.00 41.26  ? 259 SER D OG     1 
ATOM   10506 N N      . LEU D 2 242 ? 41.073  64.153  58.683 1.00 48.14  ? 260 LEU D N      1 
ATOM   10507 C CA     . LEU D 2 242 ? 41.254  63.332  59.855 1.00 44.30  ? 260 LEU D CA     1 
ATOM   10508 C C      . LEU D 2 242 ? 40.072  63.394  60.735 1.00 47.39  ? 260 LEU D C      1 
ATOM   10509 O O      . LEU D 2 242 ? 39.452  64.426  60.823 1.00 55.87  ? 260 LEU D O      1 
ATOM   10510 C CB     . LEU D 2 242 ? 42.471  63.768  60.649 1.00 40.08  ? 260 LEU D CB     1 
ATOM   10511 C CG     . LEU D 2 242 ? 43.934  63.651  60.224 1.00 44.91  ? 260 LEU D CG     1 
ATOM   10512 C CD1    . LEU D 2 242 ? 44.807  64.375  61.229 1.00 49.07  ? 260 LEU D CD1    1 
ATOM   10513 C CD2    . LEU D 2 242 ? 44.363  62.204  60.110 1.00 37.56  ? 260 LEU D CD2    1 
ATOM   10514 N N      . SER D 2 243 ? 39.786  62.318  61.446 1.00 43.42  ? 261 SER D N      1 
ATOM   10515 C CA     . SER D 2 243 ? 38.588  62.242  62.255 1.00 47.87  ? 261 SER D CA     1 
ATOM   10516 C C      . SER D 2 243 ? 38.814  62.767  63.610 1.00 56.13  ? 261 SER D C      1 
ATOM   10517 O O      . SER D 2 243 ? 39.656  62.274  64.327 1.00 62.28  ? 261 SER D O      1 
ATOM   10518 C CB     . SER D 2 243 ? 38.087  60.816  62.398 1.00 44.78  ? 261 SER D CB     1 
ATOM   10519 O OG     . SER D 2 243 ? 37.233  60.463  61.336 1.00 54.78  ? 261 SER D OG     1 
ATOM   10520 N N      . GLY D 2 244 ? 38.060  63.773  63.978 1.00 55.56  ? 262 GLY D N      1 
ATOM   10521 C CA     . GLY D 2 244 ? 38.151  64.303  65.315 1.00 51.83  ? 262 GLY D CA     1 
ATOM   10522 C C      . GLY D 2 244 ? 37.003  63.693  66.020 1.00 52.15  ? 262 GLY D C      1 
ATOM   10523 O O      . GLY D 2 244 ? 36.904  63.776  67.226 1.00 48.96  ? 262 GLY D O      1 
ATOM   10524 N N      . THR D 2 245 ? 36.115  63.081  65.259 1.00 55.93  ? 263 THR D N      1 
ATOM   10525 C CA     . THR D 2 245 ? 34.969  62.427  65.842 1.00 53.42  ? 263 THR D CA     1 
ATOM   10526 C C      . THR D 2 245 ? 35.502  61.165  66.438 1.00 49.39  ? 263 THR D C      1 
ATOM   10527 O O      . THR D 2 245 ? 34.823  60.480  67.176 1.00 48.70  ? 263 THR D O      1 
ATOM   10528 C CB     . THR D 2 245 ? 33.903  62.154  64.792 1.00 50.89  ? 263 THR D CB     1 
ATOM   10529 O OG1    . THR D 2 245 ? 32.827  61.414  65.374 1.00 55.42  ? 263 THR D OG1    1 
ATOM   10530 C CG2    . THR D 2 245 ? 34.488  61.372  63.652 1.00 55.15  ? 263 THR D CG2    1 
ATOM   10531 N N      . THR D 2 246 ? 36.747  60.848  66.166 1.00 47.34  ? 264 THR D N      1 
ATOM   10532 C CA     . THR D 2 246 ? 37.318  59.696  66.809 1.00 49.96  ? 264 THR D CA     1 
ATOM   10533 C C      . THR D 2 246 ? 37.430  60.081  68.233 1.00 50.40  ? 264 THR D C      1 
ATOM   10534 O O      . THR D 2 246 ? 37.164  59.293  69.122 1.00 49.94  ? 264 THR D O      1 
ATOM   10535 C CB     . THR D 2 246 ? 38.698  59.406  66.288 1.00 45.76  ? 264 THR D CB     1 
ATOM   10536 O OG1    . THR D 2 246 ? 38.601  58.460  65.222 1.00 50.18  ? 264 THR D OG1    1 
ATOM   10537 C CG2    . THR D 2 246 ? 39.552  58.841  67.382 1.00 42.31  ? 264 THR D CG2    1 
ATOM   10538 N N      . TYR D 2 247 ? 37.788  61.329  68.476 1.00 47.23  ? 265 TYR D N      1 
ATOM   10539 C CA     . TYR D 2 247 ? 38.010  61.757  69.825 1.00 41.13  ? 265 TYR D CA     1 
ATOM   10540 C C      . TYR D 2 247 ? 36.720  61.639  70.545 1.00 44.66  ? 265 TYR D C      1 
ATOM   10541 O O      . TYR D 2 247 ? 36.702  61.301  71.706 1.00 50.50  ? 265 TYR D O      1 
ATOM   10542 C CB     . TYR D 2 247 ? 38.583  63.153  69.854 1.00 37.55  ? 265 TYR D CB     1 
ATOM   10543 C CG     . TYR D 2 247 ? 39.944  63.226  69.213 1.00 40.61  ? 265 TYR D CG     1 
ATOM   10544 C CD1    . TYR D 2 247 ? 40.919  62.309  69.533 1.00 43.79  ? 265 TYR D CD1    1 
ATOM   10545 C CD2    . TYR D 2 247 ? 40.251  64.200  68.289 1.00 47.30  ? 265 TYR D CD2    1 
ATOM   10546 C CE1    . TYR D 2 247 ? 42.161  62.360  68.951 1.00 44.55  ? 265 TYR D CE1    1 
ATOM   10547 C CE2    . TYR D 2 247 ? 41.497  64.256  67.705 1.00 45.58  ? 265 TYR D CE2    1 
ATOM   10548 C CZ     . TYR D 2 247 ? 42.447  63.330  68.044 1.00 41.78  ? 265 TYR D CZ     1 
ATOM   10549 O OH     . TYR D 2 247 ? 43.690  63.366  67.472 1.00 41.52  ? 265 TYR D OH     1 
ATOM   10550 N N      . SER D 2 248 ? 35.617  61.833  69.860 1.00 44.38  ? 266 SER D N      1 
ATOM   10551 C CA     . SER D 2 248 ? 34.343  61.651  70.513 1.00 46.95  ? 266 SER D CA     1 
ATOM   10552 C C      . SER D 2 248 ? 34.083  60.190  70.796 1.00 49.15  ? 266 SER D C      1 
ATOM   10553 O O      . SER D 2 248 ? 33.467  59.874  71.798 1.00 47.68  ? 266 SER D O      1 
ATOM   10554 C CB     . SER D 2 248 ? 33.216  62.295  69.734 1.00 47.45  ? 266 SER D CB     1 
ATOM   10555 O OG     . SER D 2 248 ? 32.832  61.502  68.634 1.00 56.04  ? 266 SER D OG     1 
ATOM   10556 N N      . LEU D 2 249 ? 34.526  59.280  69.936 1.00 44.48  ? 267 LEU D N      1 
ATOM   10557 C CA     . LEU D 2 249 ? 34.385  57.849  70.220 1.00 43.84  ? 267 LEU D CA     1 
ATOM   10558 C C      . LEU D 2 249 ? 35.183  57.541  71.434 1.00 45.67  ? 267 LEU D C      1 
ATOM   10559 O O      . LEU D 2 249 ? 34.732  56.844  72.313 1.00 43.12  ? 267 LEU D O      1 
ATOM   10560 C CB     . LEU D 2 249 ? 34.946  56.995  69.103 1.00 37.97  ? 267 LEU D CB     1 
ATOM   10561 C CG     . LEU D 2 249 ? 35.066  55.483  69.244 1.00 34.29  ? 267 LEU D CG     1 
ATOM   10562 C CD1    . LEU D 2 249 ? 33.706  54.823  69.140 1.00 32.93  ? 267 LEU D CD1    1 
ATOM   10563 C CD2    . LEU D 2 249 ? 35.997  54.952  68.170 1.00 33.65  ? 267 LEU D CD2    1 
ATOM   10564 N N      . MET D 2 250 ? 36.392  58.059  71.491 1.00 44.80  ? 268 MET D N      1 
ATOM   10565 C CA     . MET D 2 250 ? 37.252  57.776  72.603 1.00 39.28  ? 268 MET D CA     1 
ATOM   10566 C C      . MET D 2 250 ? 36.712  58.319  73.902 1.00 39.68  ? 268 MET D C      1 
ATOM   10567 O O      . MET D 2 250 ? 37.049  57.809  74.944 1.00 40.38  ? 268 MET D O      1 
ATOM   10568 C CB     . MET D 2 250 ? 38.640  58.301  72.336 1.00 37.73  ? 268 MET D CB     1 
ATOM   10569 C CG     . MET D 2 250 ? 39.383  57.591  71.240 1.00 39.20  ? 268 MET D CG     1 
ATOM   10570 S SD     . MET D 2 250 ? 39.863  55.983  71.852 1.00 64.25  ? 268 MET D SD     1 
ATOM   10571 C CE     . MET D 2 250 ? 40.771  56.438  73.320 1.00 46.98  ? 268 MET D CE     1 
ATOM   10572 N N      . VAL D 2 251 ? 35.859  59.328  73.875 1.00 35.56  ? 269 VAL D N      1 
ATOM   10573 C CA     . VAL D 2 251 ? 35.257  59.802  75.114 1.00 36.11  ? 269 VAL D CA     1 
ATOM   10574 C C      . VAL D 2 251 ? 34.357  58.719  75.599 1.00 37.85  ? 269 VAL D C      1 
ATOM   10575 O O      . VAL D 2 251 ? 34.341  58.377  76.767 1.00 39.88  ? 269 VAL D O      1 
ATOM   10576 C CB     . VAL D 2 251 ? 34.430  61.064  74.906 1.00 37.13  ? 269 VAL D CB     1 
ATOM   10577 C CG1    . VAL D 2 251 ? 33.707  61.449  76.180 1.00 37.55  ? 269 VAL D CG1    1 
ATOM   10578 C CG2    . VAL D 2 251 ? 35.321  62.208  74.469 1.00 40.99  ? 269 VAL D CG2    1 
ATOM   10579 N N      . VAL D 2 252 ? 33.636  58.125  74.680 1.00 38.41  ? 270 VAL D N      1 
ATOM   10580 C CA     . VAL D 2 252 ? 32.715  57.092  75.046 1.00 40.26  ? 270 VAL D CA     1 
ATOM   10581 C C      . VAL D 2 252 ? 33.494  55.882  75.415 1.00 41.22  ? 270 VAL D C      1 
ATOM   10582 O O      . VAL D 2 252 ? 33.239  55.265  76.428 1.00 43.58  ? 270 VAL D O      1 
ATOM   10583 C CB     . VAL D 2 252 ? 31.808  56.752  73.874 1.00 43.17  ? 270 VAL D CB     1 
ATOM   10584 C CG1    . VAL D 2 252 ? 30.663  55.877  74.332 1.00 42.66  ? 270 VAL D CG1    1 
ATOM   10585 C CG2    . VAL D 2 252 ? 31.256  58.019  73.256 1.00 42.08  ? 270 VAL D CG2    1 
ATOM   10586 N N      . LEU D 2 253 ? 34.464  55.527  74.595 1.00 38.18  ? 271 LEU D N      1 
ATOM   10587 C CA     . LEU D 2 253 ? 35.210  54.310  74.831 1.00 36.40  ? 271 LEU D CA     1 
ATOM   10588 C C      . LEU D 2 253 ? 36.011  54.351  76.089 1.00 39.65  ? 271 LEU D C      1 
ATOM   10589 O O      . LEU D 2 253 ? 36.096  53.365  76.780 1.00 46.19  ? 271 LEU D O      1 
ATOM   10590 C CB     . LEU D 2 253 ? 36.113  53.975  73.668 1.00 31.62  ? 271 LEU D CB     1 
ATOM   10591 C CG     . LEU D 2 253 ? 35.430  53.333  72.482 1.00 33.88  ? 271 LEU D CG     1 
ATOM   10592 C CD1    . LEU D 2 253 ? 36.455  52.466  71.797 1.00 32.62  ? 271 LEU D CD1    1 
ATOM   10593 C CD2    . LEU D 2 253 ? 34.311  52.463  72.993 1.00 32.55  ? 271 LEU D CD2    1 
ATOM   10594 N N      . THR D 2 254 ? 36.608  55.486  76.404 1.00 38.04  ? 272 THR D N      1 
ATOM   10595 C CA     . THR D 2 254 ? 37.320  55.599  77.664 1.00 38.71  ? 272 THR D CA     1 
ATOM   10596 C C      . THR D 2 254 ? 36.382  55.222  78.773 1.00 40.33  ? 272 THR D C      1 
ATOM   10597 O O      . THR D 2 254 ? 36.740  54.468  79.655 1.00 45.22  ? 272 THR D O      1 
ATOM   10598 C CB     . THR D 2 254 ? 37.890  56.994  77.920 1.00 35.52  ? 272 THR D CB     1 
ATOM   10599 O OG1    . THR D 2 254 ? 38.822  57.321  76.886 1.00 38.29  ? 272 THR D OG1    1 
ATOM   10600 C CG2    . THR D 2 254 ? 38.608  57.041  79.243 1.00 30.04  ? 272 THR D CG2    1 
ATOM   10601 N N      . ASP D 2 255 ? 35.149  55.677  78.697 1.00 39.13  ? 273 ASP D N      1 
ATOM   10602 C CA     . ASP D 2 255 ? 34.187  55.356  79.731 1.00 42.33  ? 273 ASP D CA     1 
ATOM   10603 C C      . ASP D 2 255 ? 33.869  53.880  79.746 1.00 49.43  ? 273 ASP D C      1 
ATOM   10604 O O      . ASP D 2 255 ? 33.830  53.285  80.800 1.00 48.87  ? 273 ASP D O      1 
ATOM   10605 C CB     . ASP D 2 255 ? 32.917  56.158  79.577 1.00 42.15  ? 273 ASP D CB     1 
ATOM   10606 C CG     . ASP D 2 255 ? 32.182  56.333  80.874 1.00 47.83  ? 273 ASP D CG     1 
ATOM   10607 O OD1    . ASP D 2 255 ? 32.802  56.138  81.932 1.00 58.48  ? 273 ASP D OD1    1 
ATOM   10608 O OD2    . ASP D 2 255 ? 30.986  56.676  80.842 1.00 48.79  ? 273 ASP D OD2    1 
ATOM   10609 N N      . TYR D 2 256 ? 33.648  53.263  78.593 1.00 45.92  ? 274 TYR D N      1 
ATOM   10610 C CA     . TYR D 2 256 ? 33.282  51.862  78.570 1.00 41.41  ? 274 TYR D CA     1 
ATOM   10611 C C      . TYR D 2 256 ? 34.390  51.141  79.202 1.00 42.63  ? 274 TYR D C      1 
ATOM   10612 O O      . TYR D 2 256 ? 34.186  50.234  79.956 1.00 51.85  ? 274 TYR D O      1 
ATOM   10613 C CB     . TYR D 2 256 ? 33.114  51.337  77.167 1.00 37.23  ? 274 TYR D CB     1 
ATOM   10614 C CG     . TYR D 2 256 ? 32.714  49.894  77.081 1.00 43.05  ? 274 TYR D CG     1 
ATOM   10615 C CD1    . TYR D 2 256 ? 31.483  49.475  77.528 1.00 43.99  ? 274 TYR D CD1    1 
ATOM   10616 C CD2    . TYR D 2 256 ? 33.563  48.954  76.537 1.00 43.73  ? 274 TYR D CD2    1 
ATOM   10617 C CE1    . TYR D 2 256 ? 31.112  48.156  77.451 1.00 42.92  ? 274 TYR D CE1    1 
ATOM   10618 C CE2    . TYR D 2 256 ? 33.201  47.632  76.457 1.00 49.79  ? 274 TYR D CE2    1 
ATOM   10619 C CZ     . TYR D 2 256 ? 31.971  47.243  76.918 1.00 51.95  ? 274 TYR D CZ     1 
ATOM   10620 O OH     . TYR D 2 256 ? 31.592  45.930  76.847 1.00 66.50  ? 274 TYR D OH     1 
ATOM   10621 N N      . ILE D 2 257 ? 35.592  51.533  78.882 1.00 35.38  ? 275 ILE D N      1 
ATOM   10622 C CA     . ILE D 2 257 ? 36.692  50.807  79.407 1.00 40.02  ? 275 ILE D CA     1 
ATOM   10623 C C      . ILE D 2 257 ? 36.666  50.946  80.908 1.00 53.93  ? 275 ILE D C      1 
ATOM   10624 O O      . ILE D 2 257 ? 36.749  49.962  81.602 1.00 63.13  ? 275 ILE D O      1 
ATOM   10625 C CB     . ILE D 2 257 ? 38.017  51.273  78.816 1.00 32.85  ? 275 ILE D CB     1 
ATOM   10626 C CG1    . ILE D 2 257 ? 38.098  50.907  77.345 1.00 32.06  ? 275 ILE D CG1    1 
ATOM   10627 C CG2    . ILE D 2 257 ? 39.181  50.645  79.545 1.00 33.74  ? 275 ILE D CG2    1 
ATOM   10628 C CD1    . ILE D 2 257 ? 39.297  51.507  76.660 1.00 27.96  ? 275 ILE D CD1    1 
ATOM   10629 N N      . GLU D 2 258 ? 36.473  52.136  81.443 1.00 50.39  ? 276 GLU D N      1 
ATOM   10630 C CA     . GLU D 2 258 ? 36.525  52.290  82.883 1.00 47.26  ? 276 GLU D CA     1 
ATOM   10631 C C      . GLU D 2 258 ? 35.408  51.529  83.501 1.00 52.15  ? 276 GLU D C      1 
ATOM   10632 O O      . GLU D 2 258 ? 35.607  50.823  84.457 1.00 56.18  ? 276 GLU D O      1 
ATOM   10633 C CB     . GLU D 2 258 ? 36.358  53.744  83.262 1.00 41.93  ? 276 GLU D CB     1 
ATOM   10634 C CG     . GLU D 2 258 ? 37.517  54.664  82.934 1.00 45.13  ? 276 GLU D CG     1 
ATOM   10635 C CD     . GLU D 2 258 ? 37.167  56.125  83.163 1.00 55.41  ? 276 GLU D CD     1 
ATOM   10636 O OE1    . GLU D 2 258 ? 35.980  56.434  83.385 1.00 51.90  ? 276 GLU D OE1    1 
ATOM   10637 O OE2    . GLU D 2 258 ? 38.077  56.973  83.114 1.00 51.49  ? 276 GLU D OE2    1 
ATOM   10638 N N      . LYS D 2 259 ? 34.221  51.662  82.947 1.00 51.91  ? 277 LYS D N      1 
ATOM   10639 C CA     . LYS D 2 259 ? 33.048  51.016  83.492 1.00 53.96  ? 277 LYS D CA     1 
ATOM   10640 C C      . LYS D 2 259 ? 33.060  49.535  83.386 1.00 58.96  ? 277 LYS D C      1 
ATOM   10641 O O      . LYS D 2 259 ? 32.273  48.870  84.021 1.00 59.85  ? 277 LYS D O      1 
ATOM   10642 C CB     . LYS D 2 259 ? 31.815  51.521  82.777 1.00 50.23  ? 277 LYS D CB     1 
ATOM   10643 C CG     . LYS D 2 259 ? 31.459  52.957  83.101 1.00 56.75  ? 277 LYS D CG     1 
ATOM   10644 C CD     . LYS D 2 259 ? 29.998  53.237  82.806 1.00 53.60  ? 277 LYS D CD     1 
ATOM   10645 C CE     . LYS D 2 259 ? 29.561  54.549  83.429 1.00 53.09  ? 277 LYS D CE     1 
ATOM   10646 N NZ     . LYS D 2 259 ? 28.080  54.644  83.516 1.00 51.77  ? 277 LYS D NZ     1 
ATOM   10647 N N      . HIS D 2 260 ? 33.906  49.003  82.536 1.00 59.75  ? 278 HIS D N      1 
ATOM   10648 C CA     . HIS D 2 260 ? 33.966  47.581  82.346 1.00 54.91  ? 278 HIS D CA     1 
ATOM   10649 C C      . HIS D 2 260 ? 35.392  47.193  82.341 1.00 52.63  ? 278 HIS D C      1 
ATOM   10650 O O      . HIS D 2 260 ? 35.817  46.385  81.555 1.00 55.53  ? 278 HIS D O      1 
ATOM   10651 C CB     . HIS D 2 260 ? 33.292  47.187  81.058 1.00 54.30  ? 278 HIS D CB     1 
ATOM   10652 C CG     . HIS D 2 260 ? 31.804  47.323  81.091 1.00 61.16  ? 278 HIS D CG     1 
ATOM   10653 N ND1    . HIS D 2 260 ? 31.153  48.469  80.696 1.00 60.88  ? 278 HIS D ND1    1 
ATOM   10654 C CD2    . HIS D 2 260 ? 30.839  46.461  81.486 1.00 67.41  ? 278 HIS D CD2    1 
ATOM   10655 C CE1    . HIS D 2 260 ? 29.850  48.307  80.838 1.00 61.14  ? 278 HIS D CE1    1 
ATOM   10656 N NE2    . HIS D 2 260 ? 29.633  47.097  81.317 1.00 69.26  ? 278 HIS D NE2    1 
ATOM   10657 N N      . LYS D 2 261 ? 36.152  47.797  83.214 1.00 50.42  ? 279 LYS D N      1 
ATOM   10658 C CA     . LYS D 2 261 ? 37.541  47.506  83.272 1.00 52.41  ? 279 LYS D CA     1 
ATOM   10659 C C      . LYS D 2 261 ? 37.729  46.085  83.633 1.00 64.19  ? 279 LYS D C      1 
ATOM   10660 O O      . LYS D 2 261 ? 38.583  45.406  83.092 1.00 68.58  ? 279 LYS D O      1 
ATOM   10661 C CB     . LYS D 2 261 ? 38.153  48.348  84.357 1.00 54.72  ? 279 LYS D CB     1 
ATOM   10662 C CG     . LYS D 2 261 ? 39.238  49.296  83.880 1.00 69.86  ? 279 LYS D CG     1 
ATOM   10663 C CD     . LYS D 2 261 ? 40.444  48.550  83.336 1.00 78.89  ? 279 LYS D CD     1 
ATOM   10664 C CE     . LYS D 2 261 ? 41.269  47.928  84.450 1.00 72.48  ? 279 LYS D CE     1 
ATOM   10665 N NZ     . LYS D 2 261 ? 41.814  48.962  85.373 1.00 68.13  ? 279 LYS D NZ     1 
ATOM   10666 N N      . THR D 2 262 ? 36.937  45.611  84.563 1.00 61.01  ? 280 THR D N      1 
ATOM   10667 C CA     . THR D 2 262 ? 37.091  44.264  85.035 1.00 53.33  ? 280 THR D CA     1 
ATOM   10668 C C      . THR D 2 262 ? 36.853  43.194  84.028 1.00 50.59  ? 280 THR D C      1 
ATOM   10669 O O      . THR D 2 262 ? 37.484  42.160  84.058 1.00 54.55  ? 280 THR D O      1 
ATOM   10670 C CB     . THR D 2 262 ? 36.167  44.015  86.209 1.00 54.42  ? 280 THR D CB     1 
ATOM   10671 O OG1    . THR D 2 262 ? 34.918  44.665  85.970 1.00 50.79  ? 280 THR D OG1    1 
ATOM   10672 C CG2    . THR D 2 262 ? 36.776  44.584  87.458 1.00 56.54  ? 280 THR D CG2    1 
ATOM   10673 N N      . ASP D 2 263 ? 35.946  43.417  83.118 1.00 52.38  ? 281 ASP D N      1 
ATOM   10674 C CA     . ASP D 2 263 ? 35.591  42.327  82.267 1.00 61.04  ? 281 ASP D CA     1 
ATOM   10675 C C      . ASP D 2 263 ? 36.680  41.704  81.465 1.00 60.73  ? 281 ASP D C      1 
ATOM   10676 O O      . ASP D 2 263 ? 37.549  42.368  80.949 1.00 64.01  ? 281 ASP D O      1 
ATOM   10677 C CB     . ASP D 2 263 ? 34.249  42.554  81.537 1.00 59.80  ? 281 ASP D CB     1 
ATOM   10678 C CG     . ASP D 2 263 ? 34.353  43.408  80.324 1.00 67.84  ? 281 ASP D CG     1 
ATOM   10679 O OD1    . ASP D 2 263 ? 33.381  43.425  79.543 1.00 74.14  ? 281 ASP D OD1    1 
ATOM   10680 O OD2    . ASP D 2 263 ? 35.380  44.063  80.144 1.00 65.99  ? 281 ASP D OD2    1 
ATOM   10681 N N      . LYS D 2 264 ? 36.667  40.394  81.427 1.00 55.35  ? 282 LYS D N      1 
ATOM   10682 C CA     . LYS D 2 264 ? 37.673  39.645  80.734 1.00 52.64  ? 282 LYS D CA     1 
ATOM   10683 C C      . LYS D 2 264 ? 37.679  39.852  79.264 1.00 54.02  ? 282 LYS D C      1 
ATOM   10684 O O      . LYS D 2 264 ? 38.725  39.836  78.635 1.00 53.39  ? 282 LYS D O      1 
ATOM   10685 C CB     . LYS D 2 264 ? 37.381  38.187  81.017 1.00 57.72  ? 282 LYS D CB     1 
ATOM   10686 C CG     . LYS D 2 264 ? 37.216  37.840  82.487 1.00 53.46  ? 282 LYS D CG     1 
ATOM   10687 C CD     . LYS D 2 264 ? 38.550  37.847  83.216 1.00 54.84  ? 282 LYS D CD     1 
ATOM   10688 C CE     . LYS D 2 264 ? 39.500  36.808  82.648 1.00 43.75  ? 282 LYS D CE     1 
ATOM   10689 N NZ     . LYS D 2 264 ? 40.859  36.914  83.241 1.00 27.88  ? 282 LYS D NZ     1 
ATOM   10690 N N      . ASP D 2 265 ? 36.510  40.029  78.693 1.00 55.66  ? 283 ASP D N      1 
ATOM   10691 C CA     . ASP D 2 265 ? 36.392  40.114  77.261 1.00 56.98  ? 283 ASP D CA     1 
ATOM   10692 C C      . ASP D 2 265 ? 36.455  41.512  76.712 1.00 57.04  ? 283 ASP D C      1 
ATOM   10693 O O      . ASP D 2 265 ? 36.016  41.755  75.609 1.00 53.59  ? 283 ASP D O      1 
ATOM   10694 C CB     . ASP D 2 265 ? 35.122  39.421  76.798 1.00 57.59  ? 283 ASP D CB     1 
ATOM   10695 C CG     . ASP D 2 265 ? 33.922  39.699  77.690 1.00 63.38  ? 283 ASP D CG     1 
ATOM   10696 O OD1    . ASP D 2 265 ? 33.959  40.631  78.512 1.00 62.83  ? 283 ASP D OD1    1 
ATOM   10697 O OD2    . ASP D 2 265 ? 32.914  38.980  77.556 1.00 60.16  ? 283 ASP D OD2    1 
ATOM   10698 N N      . ILE D 2 266 ? 36.998  42.443  77.475 1.00 56.00  ? 284 ILE D N      1 
ATOM   10699 C CA     . ILE D 2 266 ? 37.109  43.810  77.021 1.00 53.36  ? 284 ILE D CA     1 
ATOM   10700 C C      . ILE D 2 266 ? 37.948  43.978  75.768 1.00 50.20  ? 284 ILE D C      1 
ATOM   10701 O O      . ILE D 2 266 ? 37.602  44.755  74.907 1.00 52.85  ? 284 ILE D O      1 
ATOM   10702 C CB     . ILE D 2 266 ? 37.621  44.732  78.146 1.00 48.04  ? 284 ILE D CB     1 
ATOM   10703 C CG1    . ILE D 2 266 ? 37.351  46.193  77.828 1.00 45.06  ? 284 ILE D CG1    1 
ATOM   10704 C CG2    . ILE D 2 266 ? 39.081  44.482  78.487 1.00 45.72  ? 284 ILE D CG2    1 
ATOM   10705 C CD1    . ILE D 2 266 ? 37.787  47.102  78.944 1.00 50.81  ? 284 ILE D CD1    1 
ATOM   10706 N N      . GLU D 2 267 ? 39.041  43.275  75.624 1.00 46.01  ? 285 GLU D N      1 
ATOM   10707 C CA     . GLU D 2 267 ? 39.843  43.515  74.469 1.00 43.63  ? 285 GLU D CA     1 
ATOM   10708 C C      . GLU D 2 267 ? 39.102  43.175  73.261 1.00 42.11  ? 285 GLU D C      1 
ATOM   10709 O O      . GLU D 2 267 ? 39.103  43.913  72.307 1.00 39.07  ? 285 GLU D O      1 
ATOM   10710 C CB     . GLU D 2 267 ? 41.079  42.661  74.505 1.00 39.29  ? 285 GLU D CB     1 
ATOM   10711 C CG     . GLU D 2 267 ? 42.042  42.888  73.360 1.00 41.60  ? 285 GLU D CG     1 
ATOM   10712 C CD     . GLU D 2 267 ? 43.453  42.519  73.733 1.00 46.04  ? 285 GLU D CD     1 
ATOM   10713 O OE1    . GLU D 2 267 ? 43.824  42.727  74.899 1.00 45.60  ? 285 GLU D OE1    1 
ATOM   10714 O OE2    . GLU D 2 267 ? 44.192  42.029  72.866 1.00 53.06  ? 285 GLU D OE2    1 
ATOM   10715 N N      . LYS D 2 268 ? 38.440  42.056  73.278 1.00 44.33  ? 286 LYS D N      1 
ATOM   10716 C CA     . LYS D 2 268 ? 37.803  41.655  72.081 1.00 43.44  ? 286 LYS D CA     1 
ATOM   10717 C C      . LYS D 2 268 ? 36.792  42.660  71.779 1.00 42.61  ? 286 LYS D C      1 
ATOM   10718 O O      . LYS D 2 268 ? 36.663  43.096  70.663 1.00 46.22  ? 286 LYS D O      1 
ATOM   10719 C CB     . LYS D 2 268 ? 37.083  40.362  72.310 1.00 44.78  ? 286 LYS D CB     1 
ATOM   10720 C CG     . LYS D 2 268 ? 37.930  39.288  72.970 1.00 57.62  ? 286 LYS D CG     1 
ATOM   10721 C CD     . LYS D 2 268 ? 37.266  37.926  72.846 1.00 59.42  ? 286 LYS D CD     1 
ATOM   10722 C CE     . LYS D 2 268 ? 38.049  36.851  73.577 1.00 52.47  ? 286 LYS D CE     1 
ATOM   10723 N NZ     . LYS D 2 268 ? 37.985  37.038  75.051 1.00 61.17  ? 286 LYS D NZ     1 
ATOM   10724 N N      . LYS D 2 269 ? 36.063  43.064  72.781 1.00 40.01  ? 287 LYS D N      1 
ATOM   10725 C CA     . LYS D 2 269 ? 34.978  43.952  72.527 1.00 38.94  ? 287 LYS D CA     1 
ATOM   10726 C C      . LYS D 2 269 ? 35.345  45.308  72.016 1.00 39.47  ? 287 LYS D C      1 
ATOM   10727 O O      . LYS D 2 269 ? 34.689  45.825  71.148 1.00 38.89  ? 287 LYS D O      1 
ATOM   10728 C CB     . LYS D 2 269 ? 34.122  44.052  73.765 1.00 45.12  ? 287 LYS D CB     1 
ATOM   10729 C CG     . LYS D 2 269 ? 33.270  42.835  74.059 1.00 45.68  ? 287 LYS D CG     1 
ATOM   10730 C CD     . LYS D 2 269 ? 32.560  43.034  75.384 1.00 49.76  ? 287 LYS D CD     1 
ATOM   10731 C CE     . LYS D 2 269 ? 31.622  41.892  75.712 1.00 55.39  ? 287 LYS D CE     1 
ATOM   10732 N NZ     . LYS D 2 269 ? 31.138  42.001  77.113 1.00 51.43  ? 287 LYS D NZ     1 
ATOM   10733 N N      . VAL D 2 270 ? 36.385  45.906  72.545 1.00 43.24  ? 288 VAL D N      1 
ATOM   10734 C CA     . VAL D 2 270 ? 36.703  47.263  72.165 1.00 39.25  ? 288 VAL D CA     1 
ATOM   10735 C C      . VAL D 2 270 ? 37.085  47.231  70.729 1.00 39.66  ? 288 VAL D C      1 
ATOM   10736 O O      . VAL D 2 270 ? 36.950  48.197  70.016 1.00 38.34  ? 288 VAL D O      1 
ATOM   10737 C CB     . VAL D 2 270 ? 37.760  47.890  73.082 1.00 32.25  ? 288 VAL D CB     1 
ATOM   10738 C CG1    . VAL D 2 270 ? 38.395  49.123  72.475 1.00 36.10  ? 288 VAL D CG1    1 
ATOM   10739 C CG2    . VAL D 2 270 ? 37.130  48.230  74.418 1.00 30.65  ? 288 VAL D CG2    1 
ATOM   10740 N N      . ASN D 2 271 ? 37.498  46.077  70.275 1.00 38.97  ? 289 ASN D N      1 
ATOM   10741 C CA     . ASN D 2 271 ? 37.921  45.984  68.910 1.00 38.90  ? 289 ASN D CA     1 
ATOM   10742 C C      . ASN D 2 271 ? 36.756  45.640  68.000 1.00 43.08  ? 289 ASN D C      1 
ATOM   10743 O O      . ASN D 2 271 ? 36.957  45.416  66.826 1.00 42.70  ? 289 ASN D O      1 
ATOM   10744 C CB     . ASN D 2 271 ? 39.052  44.989  68.778 1.00 40.45  ? 289 ASN D CB     1 
ATOM   10745 C CG     . ASN D 2 271 ? 40.341  45.499  69.351 1.00 51.43  ? 289 ASN D CG     1 
ATOM   10746 O OD1    . ASN D 2 271 ? 40.712  46.641  69.123 1.00 51.07  ? 289 ASN D OD1    1 
ATOM   10747 N ND2    . ASN D 2 271 ? 41.043  44.648  70.084 1.00 52.02  ? 289 ASN D ND2    1 
ATOM   10748 N N      . GLN D 2 272 ? 35.527  45.618  68.502 1.00 40.30  ? 290 GLN D N      1 
ATOM   10749 C CA     . GLN D 2 272 ? 34.365  45.407  67.643 1.00 32.65  ? 290 GLN D CA     1 
ATOM   10750 C C      . GLN D 2 272 ? 33.800  46.778  67.410 1.00 34.82  ? 290 GLN D C      1 
ATOM   10751 O O      . GLN D 2 272 ? 33.230  47.031  66.373 1.00 34.91  ? 290 GLN D O      1 
ATOM   10752 C CB     . GLN D 2 272 ? 33.348  44.504  68.308 1.00 33.70  ? 290 GLN D CB     1 
ATOM   10753 C CG     . GLN D 2 272 ? 33.765  43.054  68.418 1.00 35.98  ? 290 GLN D CG     1 
ATOM   10754 C CD     . GLN D 2 272 ? 32.727  42.226  69.134 1.00 39.95  ? 290 GLN D CD     1 
ATOM   10755 O OE1    . GLN D 2 272 ? 32.817  41.006  69.193 1.00 49.83  ? 290 GLN D OE1    1 
ATOM   10756 N NE2    . GLN D 2 272 ? 31.727  42.890  69.679 1.00 38.49  ? 290 GLN D NE2    1 
ATOM   10757 N N      . ILE D 2 273 ? 33.939  47.672  68.376 1.00 39.19  ? 291 ILE D N      1 
ATOM   10758 C CA     . ILE D 2 273 ? 33.539  49.063  68.212 1.00 35.34  ? 291 ILE D CA     1 
ATOM   10759 C C      . ILE D 2 273 ? 34.554  49.860  67.452 1.00 32.44  ? 291 ILE D C      1 
ATOM   10760 O O      . ILE D 2 273 ? 34.196  50.611  66.586 1.00 37.56  ? 291 ILE D O      1 
ATOM   10761 C CB     . ILE D 2 273 ? 33.417  49.765  69.548 1.00 34.02  ? 291 ILE D CB     1 
ATOM   10762 C CG1    . ILE D 2 273 ? 32.920  48.801  70.613 1.00 37.27  ? 291 ILE D CG1    1 
ATOM   10763 C CG2    . ILE D 2 273 ? 32.512  50.971  69.423 1.00 33.44  ? 291 ILE D CG2    1 
ATOM   10764 C CD1    . ILE D 2 273 ? 33.290  49.235  72.005 1.00 39.52  ? 291 ILE D CD1    1 
ATOM   10765 N N      . ILE D 2 274 ? 35.826  49.730  67.783 1.00 30.84  ? 292 ILE D N      1 
ATOM   10766 C CA     . ILE D 2 274 ? 36.871  50.422  67.047 1.00 32.02  ? 292 ILE D CA     1 
ATOM   10767 C C      . ILE D 2 274 ? 36.846  49.974  65.621 1.00 33.79  ? 292 ILE D C      1 
ATOM   10768 O O      . ILE D 2 274 ? 36.905  50.783  64.717 1.00 37.77  ? 292 ILE D O      1 
ATOM   10769 C CB     . ILE D 2 274 ? 38.244  50.138  67.632 1.00 32.16  ? 292 ILE D CB     1 
ATOM   10770 C CG1    . ILE D 2 274 ? 38.396  50.806  68.994 1.00 33.17  ? 292 ILE D CG1    1 
ATOM   10771 C CG2    . ILE D 2 274 ? 39.347  50.628  66.712 1.00 31.22  ? 292 ILE D CG2    1 
ATOM   10772 C CD1    . ILE D 2 274 ? 38.701  52.279  68.921 1.00 34.53  ? 292 ILE D CD1    1 
ATOM   10773 N N      . ASN D 2 275 ? 36.673  48.687  65.399 1.00 33.81  ? 293 ASN D N      1 
ATOM   10774 C CA     . ASN D 2 275 ? 36.680  48.160  64.054 1.00 32.19  ? 293 ASN D CA     1 
ATOM   10775 C C      . ASN D 2 275 ? 35.425  48.411  63.244 1.00 31.05  ? 293 ASN D C      1 
ATOM   10776 O O      . ASN D 2 275 ? 35.520  48.642  62.065 1.00 37.45  ? 293 ASN D O      1 
ATOM   10777 C CB     . ASN D 2 275 ? 37.026  46.698  64.080 1.00 32.68  ? 293 ASN D CB     1 
ATOM   10778 C CG     . ASN D 2 275 ? 38.488  46.455  64.325 1.00 38.42  ? 293 ASN D CG     1 
ATOM   10779 O OD1    . ASN D 2 275 ? 39.264  47.384  64.519 1.00 41.60  ? 293 ASN D OD1    1 
ATOM   10780 N ND2    . ASN D 2 275 ? 38.875  45.198  64.315 1.00 45.71  ? 293 ASN D ND2    1 
ATOM   10781 N N      . LEU D 2 276 ? 34.245  48.368  63.827 1.00 26.26  ? 294 LEU D N      1 
ATOM   10782 C CA     . LEU D 2 276 ? 33.058  48.703  63.072 1.00 23.34  ? 294 LEU D CA     1 
ATOM   10783 C C      . LEU D 2 276 ? 33.156  50.140  62.693 1.00 31.36  ? 294 LEU D C      1 
ATOM   10784 O O      . LEU D 2 276 ? 32.757  50.516  61.612 1.00 41.35  ? 294 LEU D O      1 
ATOM   10785 C CB     . LEU D 2 276 ? 31.802  48.514  63.890 1.00 19.93  ? 294 LEU D CB     1 
ATOM   10786 C CG     . LEU D 2 276 ? 30.457  48.900  63.301 1.00 22.21  ? 294 LEU D CG     1 
ATOM   10787 C CD1    . LEU D 2 276 ? 30.104  47.930  62.191 1.00 36.84  ? 294 LEU D CD1    1 
ATOM   10788 C CD2    . LEU D 2 276 ? 29.407  48.858  64.393 1.00 28.88  ? 294 LEU D CD2    1 
ATOM   10789 N N      . TRP D 2 277 ? 33.686  50.962  63.571 1.00 32.67  ? 295 TRP D N      1 
ATOM   10790 C CA     . TRP D 2 277 ? 33.761  52.379  63.321 1.00 27.77  ? 295 TRP D CA     1 
ATOM   10791 C C      . TRP D 2 277 ? 34.578  52.565  62.090 1.00 35.30  ? 295 TRP D C      1 
ATOM   10792 O O      . TRP D 2 277 ? 34.245  53.366  61.246 1.00 47.50  ? 295 TRP D O      1 
ATOM   10793 C CB     . TRP D 2 277 ? 34.387  53.038  64.527 1.00 28.33  ? 295 TRP D CB     1 
ATOM   10794 C CG     . TRP D 2 277 ? 34.779  54.462  64.464 1.00 37.93  ? 295 TRP D CG     1 
ATOM   10795 C CD1    . TRP D 2 277 ? 35.981  54.952  64.089 1.00 43.95  ? 295 TRP D CD1    1 
ATOM   10796 C CD2    . TRP D 2 277 ? 34.004  55.586  64.888 1.00 39.99  ? 295 TRP D CD2    1 
ATOM   10797 N NE1    . TRP D 2 277 ? 35.995  56.315  64.206 1.00 40.58  ? 295 TRP D NE1    1 
ATOM   10798 C CE2    . TRP D 2 277 ? 34.789  56.727  64.694 1.00 39.30  ? 295 TRP D CE2    1 
ATOM   10799 C CE3    . TRP D 2 277 ? 32.716  55.739  65.385 1.00 39.59  ? 295 TRP D CE3    1 
ATOM   10800 C CZ2    . TRP D 2 277 ? 34.332  57.996  64.983 1.00 39.46  ? 295 TRP D CZ2    1 
ATOM   10801 C CZ3    . TRP D 2 277 ? 32.266  56.996  65.670 1.00 36.50  ? 295 TRP D CZ3    1 
ATOM   10802 C CH2    . TRP D 2 277 ? 33.066  58.108  65.471 1.00 39.01  ? 295 TRP D CH2    1 
ATOM   10803 N N      . ILE D 2 278 ? 35.618  51.777  61.932 1.00 29.57  ? 296 ILE D N      1 
ATOM   10804 C CA     . ILE D 2 278 ? 36.464  51.897  60.767 1.00 34.01  ? 296 ILE D CA     1 
ATOM   10805 C C      . ILE D 2 278 ? 35.703  51.492  59.524 1.00 35.54  ? 296 ILE D C      1 
ATOM   10806 O O      . ILE D 2 278 ? 35.780  52.147  58.509 1.00 37.42  ? 296 ILE D O      1 
ATOM   10807 C CB     . ILE D 2 278 ? 37.737  51.072  60.929 1.00 35.65  ? 296 ILE D CB     1 
ATOM   10808 C CG1    . ILE D 2 278 ? 38.635  51.703  61.981 1.00 38.44  ? 296 ILE D CG1    1 
ATOM   10809 C CG2    . ILE D 2 278 ? 38.491  50.964  59.622 1.00 41.26  ? 296 ILE D CG2    1 
ATOM   10810 C CD1    . ILE D 2 278 ? 39.830  50.854  62.324 1.00 41.88  ? 296 ILE D CD1    1 
ATOM   10811 N N      . SER D 2 279 ? 34.960  50.408  59.599 1.00 33.34  ? 297 SER D N      1 
ATOM   10812 C CA     . SER D 2 279 ? 34.226  49.920  58.458 1.00 32.00  ? 297 SER D CA     1 
ATOM   10813 C C      . SER D 2 279 ? 33.282  50.938  58.009 1.00 35.80  ? 297 SER D C      1 
ATOM   10814 O O      . SER D 2 279 ? 33.275  51.309  56.862 1.00 45.10  ? 297 SER D O      1 
ATOM   10815 C CB     . SER D 2 279 ? 33.359  48.768  58.875 1.00 30.80  ? 297 SER D CB     1 
ATOM   10816 O OG     . SER D 2 279 ? 34.085  47.843  59.646 1.00 41.14  ? 297 SER D OG     1 
ATOM   10817 N N      . SER D 2 280 ? 32.417  51.353  58.902 1.00 34.29  ? 298 SER D N      1 
ATOM   10818 C CA     . SER D 2 280 ? 31.390  52.295  58.563 1.00 38.32  ? 298 SER D CA     1 
ATOM   10819 C C      . SER D 2 280 ? 31.891  53.638  58.104 1.00 43.92  ? 298 SER D C      1 
ATOM   10820 O O      . SER D 2 280 ? 31.283  54.260  57.254 1.00 52.90  ? 298 SER D O      1 
ATOM   10821 C CB     . SER D 2 280 ? 30.495  52.455  59.757 1.00 40.49  ? 298 SER D CB     1 
ATOM   10822 O OG     . SER D 2 280 ? 29.984  51.201  60.153 1.00 52.38  ? 298 SER D OG     1 
ATOM   10823 N N      . TYR D 2 281 ? 32.992  54.117  58.644 1.00 37.26  ? 299 TYR D N      1 
ATOM   10824 C CA     . TYR D 2 281 ? 33.547  55.370  58.158 1.00 38.77  ? 299 TYR D CA     1 
ATOM   10825 C C      . TYR D 2 281 ? 34.071  55.288  56.730 1.00 41.90  ? 299 TYR D C      1 
ATOM   10826 O O      . TYR D 2 281 ? 33.854  56.194  55.951 1.00 48.48  ? 299 TYR D O      1 
ATOM   10827 C CB     . TYR D 2 281 ? 34.555  55.944  59.149 1.00 37.86  ? 299 TYR D CB     1 
ATOM   10828 C CG     . TYR D 2 281 ? 33.924  56.937  60.084 1.00 43.96  ? 299 TYR D CG     1 
ATOM   10829 C CD1    . TYR D 2 281 ? 32.839  56.582  60.859 1.00 41.32  ? 299 TYR D CD1    1 
ATOM   10830 C CD2    . TYR D 2 281 ? 34.392  58.235  60.172 1.00 41.71  ? 299 TYR D CD2    1 
ATOM   10831 C CE1    . TYR D 2 281 ? 32.241  57.489  61.703 1.00 40.28  ? 299 TYR D CE1    1 
ATOM   10832 C CE2    . TYR D 2 281 ? 33.800  59.149  61.014 1.00 35.74  ? 299 TYR D CE2    1 
ATOM   10833 C CZ     . TYR D 2 281 ? 32.725  58.766  61.776 1.00 38.34  ? 299 TYR D CZ     1 
ATOM   10834 O OH     . TYR D 2 281 ? 32.122  59.661  62.622 1.00 38.67  ? 299 TYR D OH     1 
ATOM   10835 N N      . ILE D 2 282 ? 34.684  54.185  56.348 1.00 42.13  ? 300 ILE D N      1 
ATOM   10836 C CA     . ILE D 2 282 ? 35.142  53.997  54.982 1.00 36.84  ? 300 ILE D CA     1 
ATOM   10837 C C      . ILE D 2 282 ? 33.975  53.632  54.089 1.00 43.65  ? 300 ILE D C      1 
ATOM   10838 O O      . ILE D 2 282 ? 34.015  53.902  52.907 1.00 51.78  ? 300 ILE D O      1 
ATOM   10839 C CB     . ILE D 2 282 ? 36.195  52.891  54.925 1.00 34.34  ? 300 ILE D CB     1 
ATOM   10840 C CG1    . ILE D 2 282 ? 37.274  53.134  55.969 1.00 32.43  ? 300 ILE D CG1    1 
ATOM   10841 C CG2    . ILE D 2 282 ? 36.828  52.821  53.551 1.00 40.79  ? 300 ILE D CG2    1 
ATOM   10842 C CD1    . ILE D 2 282 ? 38.320  52.050  56.000 1.00 36.65  ? 300 ILE D CD1    1 
ATOM   10843 N N      . LYS D 2 283 ? 32.925  53.037  54.644 1.00 44.78  ? 301 LYS D N      1 
ATOM   10844 C CA     . LYS D 2 283 ? 31.730  52.657  53.875 1.00 47.65  ? 301 LYS D CA     1 
ATOM   10845 C C      . LYS D 2 283 ? 30.785  53.784  53.566 1.00 49.57  ? 301 LYS D C      1 
ATOM   10846 O O      . LYS D 2 283 ? 30.414  53.996  52.425 1.00 47.87  ? 301 LYS D O      1 
ATOM   10847 C CB     . LYS D 2 283 ? 30.943  51.557  54.591 1.00 41.01  ? 301 LYS D CB     1 
ATOM   10848 C CG     . LYS D 2 283 ? 29.756  51.016  53.812 1.00 53.15  ? 301 LYS D CG     1 
ATOM   10849 C CD     . LYS D 2 283 ? 30.179  50.490  52.450 1.00 52.41  ? 301 LYS D CD     1 
ATOM   10850 C CE     . LYS D 2 283 ? 28.977  50.161  51.582 1.00 50.08  ? 301 LYS D CE     1 
ATOM   10851 N NZ     . LYS D 2 283 ? 29.383  49.785  50.202 1.00 46.56  ? 301 LYS D NZ     1 
ATOM   10852 N N      . GLU D 2 284 ? 30.403  54.534  54.579 1.00 44.21  ? 302 GLU D N      1 
ATOM   10853 C CA     . GLU D 2 284 ? 29.448  55.597  54.365 1.00 48.82  ? 302 GLU D CA     1 
ATOM   10854 C C      . GLU D 2 284 ? 30.105  56.850  53.825 1.00 52.20  ? 302 GLU D C      1 
ATOM   10855 O O      . GLU D 2 284 ? 29.459  57.877  53.682 1.00 54.63  ? 302 GLU D O      1 
ATOM   10856 C CB     . GLU D 2 284 ? 28.631  55.853  55.621 1.00 37.61  ? 302 GLU D CB     1 
ATOM   10857 C CG     . GLU D 2 284 ? 27.736  54.695  56.013 1.00 46.63  ? 302 GLU D CG     1 
ATOM   10858 C CD     . GLU D 2 284 ? 26.551  54.546  55.087 1.00 53.40  ? 302 GLU D CD     1 
ATOM   10859 O OE1    . GLU D 2 284 ? 25.969  55.577  54.709 1.00 44.56  ? 302 GLU D OE1    1 
ATOM   10860 O OE2    . GLU D 2 284 ? 26.196  53.398  54.749 1.00 60.54  ? 302 GLU D OE2    1 
ATOM   10861 N N      . GLY D 2 285 ? 31.393  56.806  53.559 1.00 44.16  ? 303 GLY D N      1 
ATOM   10862 C CA     . GLY D 2 285 ? 32.054  57.923  52.930 1.00 39.14  ? 303 GLY D CA     1 
ATOM   10863 C C      . GLY D 2 285 ? 32.699  58.958  53.776 1.00 40.40  ? 303 GLY D C      1 
ATOM   10864 O O      . GLY D 2 285 ? 33.273  59.891  53.265 1.00 44.23  ? 303 GLY D O      1 
ATOM   10865 N N      . TYR D 2 286 ? 32.589  58.845  55.071 1.00 38.87  ? 304 TYR D N      1 
ATOM   10866 C CA     . TYR D 2 286 ? 33.117  59.886  55.886 1.00 33.51  ? 304 TYR D CA     1 
ATOM   10867 C C      . TYR D 2 286 ? 34.611  60.079  55.836 1.00 37.51  ? 304 TYR D C      1 
ATOM   10868 O O      . TYR D 2 286 ? 35.057  61.185  55.661 1.00 41.71  ? 304 TYR D O      1 
ATOM   10869 C CB     . TYR D 2 286 ? 32.683  59.642  57.301 1.00 32.10  ? 304 TYR D CB     1 
ATOM   10870 C CG     . TYR D 2 286 ? 31.209  59.403  57.476 1.00 40.73  ? 304 TYR D CG     1 
ATOM   10871 C CD1    . TYR D 2 286 ? 30.289  60.381  57.168 1.00 40.28  ? 304 TYR D CD1    1 
ATOM   10872 C CD2    . TYR D 2 286 ? 30.742  58.207  57.979 1.00 46.04  ? 304 TYR D CD2    1 
ATOM   10873 C CE1    . TYR D 2 286 ? 28.944  60.169  57.341 1.00 36.84  ? 304 TYR D CE1    1 
ATOM   10874 C CE2    . TYR D 2 286 ? 29.399  57.987  58.159 1.00 47.20  ? 304 TYR D CE2    1 
ATOM   10875 C CZ     . TYR D 2 286 ? 28.507  58.974  57.837 1.00 44.91  ? 304 TYR D CZ     1 
ATOM   10876 O OH     . TYR D 2 286 ? 27.163  58.766  58.011 1.00 47.21  ? 304 TYR D OH     1 
ATOM   10877 N N      . HIS D 2 287 ? 35.397  59.023  55.925 1.00 39.52  ? 305 HIS D N      1 
ATOM   10878 C CA     . HIS D 2 287 ? 36.840  59.151  55.981 1.00 41.10  ? 305 HIS D CA     1 
ATOM   10879 C C      . HIS D 2 287 ? 37.479  57.869  55.538 1.00 40.56  ? 305 HIS D C      1 
ATOM   10880 O O      . HIS D 2 287 ? 36.816  56.863  55.448 1.00 40.13  ? 305 HIS D O      1 
ATOM   10881 C CB     . HIS D 2 287 ? 37.299  59.386  57.390 1.00 40.60  ? 305 HIS D CB     1 
ATOM   10882 C CG     . HIS D 2 287 ? 37.186  60.789  57.864 1.00 43.73  ? 305 HIS D CG     1 
ATOM   10883 N ND1    . HIS D 2 287 ? 36.046  61.283  58.452 1.00 54.23  ? 305 HIS D ND1    1 
ATOM   10884 C CD2    . HIS D 2 287 ? 38.095  61.786  57.906 1.00 45.49  ? 305 HIS D CD2    1 
ATOM   10885 C CE1    . HIS D 2 287 ? 36.243  62.539  58.797 1.00 50.62  ? 305 HIS D CE1    1 
ATOM   10886 N NE2    . HIS D 2 287 ? 37.480  62.867  58.482 1.00 54.08  ? 305 HIS D NE2    1 
ATOM   10887 N N      . SER D 2 288 ? 38.770  57.896  55.261 1.00 38.21  ? 306 SER D N      1 
ATOM   10888 C CA     . SER D 2 288 ? 39.510  56.722  54.869 1.00 39.55  ? 306 SER D CA     1 
ATOM   10889 C C      . SER D 2 288 ? 39.915  55.927  56.068 1.00 46.69  ? 306 SER D C      1 
ATOM   10890 O O      . SER D 2 288 ? 39.459  56.190  57.161 1.00 51.91  ? 306 SER D O      1 
ATOM   10891 C CB     . SER D 2 288 ? 40.757  57.150  54.173 1.00 36.34  ? 306 SER D CB     1 
ATOM   10892 O OG     . SER D 2 288 ? 40.440  57.547  52.864 1.00 50.45  ? 306 SER D OG     1 
ATOM   10893 N N      . TYR D 2 289 ? 40.769  54.935  55.883 1.00 43.91  ? 307 TYR D N      1 
ATOM   10894 C CA     . TYR D 2 289 ? 41.243  54.127  57.000 1.00 44.59  ? 307 TYR D CA     1 
ATOM   10895 C C      . TYR D 2 289 ? 42.250  54.843  57.788 1.00 45.89  ? 307 TYR D C      1 
ATOM   10896 O O      . TYR D 2 289 ? 42.166  54.915  58.995 1.00 45.68  ? 307 TYR D O      1 
ATOM   10897 C CB     . TYR D 2 289 ? 41.892  52.864  56.448 1.00 47.32  ? 307 TYR D CB     1 
ATOM   10898 C CG     . TYR D 2 289 ? 42.546  51.941  57.449 1.00 48.38  ? 307 TYR D CG     1 
ATOM   10899 C CD1    . TYR D 2 289 ? 41.789  51.110  58.252 1.00 43.48  ? 307 TYR D CD1    1 
ATOM   10900 C CD2    . TYR D 2 289 ? 43.926  51.866  57.552 1.00 47.35  ? 307 TYR D CD2    1 
ATOM   10901 C CE1    . TYR D 2 289 ? 42.383  50.256  59.154 1.00 44.24  ? 307 TYR D CE1    1 
ATOM   10902 C CE2    . TYR D 2 289 ? 44.530  51.015  58.453 1.00 39.99  ? 307 TYR D CE2    1 
ATOM   10903 C CZ     . TYR D 2 289 ? 43.752  50.214  59.250 1.00 41.90  ? 307 TYR D CZ     1 
ATOM   10904 O OH     . TYR D 2 289 ? 44.352  49.367  60.145 1.00 41.06  ? 307 TYR D OH     1 
ATOM   10905 N N      . SER D 2 290 ? 43.213  55.390  57.107 1.00 46.09  ? 308 SER D N      1 
ATOM   10906 C CA     . SER D 2 290 ? 44.275  56.035  57.788 1.00 46.67  ? 308 SER D CA     1 
ATOM   10907 C C      . SER D 2 290 ? 43.867  57.362  58.338 1.00 46.19  ? 308 SER D C      1 
ATOM   10908 O O      . SER D 2 290 ? 44.675  58.087  58.854 1.00 46.35  ? 308 SER D O      1 
ATOM   10909 C CB     . SER D 2 290 ? 45.407  56.195  56.812 1.00 52.58  ? 308 SER D CB     1 
ATOM   10910 O OG     . SER D 2 290 ? 45.925  54.931  56.474 1.00 51.60  ? 308 SER D OG     1 
ATOM   10911 N N      . GLU D 2 291 ? 42.613  57.710  58.226 1.00 45.18  ? 309 GLU D N      1 
ATOM   10912 C CA     . GLU D 2 291 ? 42.242  59.007  58.673 1.00 43.05  ? 309 GLU D CA     1 
ATOM   10913 C C      . GLU D 2 291 ? 41.547  58.835  59.942 1.00 41.01  ? 309 GLU D C      1 
ATOM   10914 O O      . GLU D 2 291 ? 41.313  59.785  60.647 1.00 49.50  ? 309 GLU D O      1 
ATOM   10915 C CB     . GLU D 2 291 ? 41.419  59.707  57.622 1.00 51.84  ? 309 GLU D CB     1 
ATOM   10916 C CG     . GLU D 2 291 ? 42.224  59.957  56.360 1.00 53.13  ? 309 GLU D CG     1 
ATOM   10917 C CD     . GLU D 2 291 ? 41.442  60.662  55.290 1.00 46.21  ? 309 GLU D CD     1 
ATOM   10918 O OE1    . GLU D 2 291 ? 40.236  60.410  55.187 1.00 44.57  ? 309 GLU D OE1    1 
ATOM   10919 O OE2    . GLU D 2 291 ? 42.030  61.470  54.551 1.00 41.04  ? 309 GLU D OE2    1 
ATOM   10920 N N      . VAL D 2 292 ? 41.253  57.602  60.278 1.00 36.00  ? 310 VAL D N      1 
ATOM   10921 C CA     . VAL D 2 292 ? 40.655  57.310  61.559 1.00 41.26  ? 310 VAL D CA     1 
ATOM   10922 C C      . VAL D 2 292 ? 41.733  56.645  62.351 1.00 42.74  ? 310 VAL D C      1 
ATOM   10923 O O      . VAL D 2 292 ? 41.987  56.977  63.489 1.00 39.40  ? 310 VAL D O      1 
ATOM   10924 C CB     . VAL D 2 292 ? 39.518  56.317  61.447 1.00 39.68  ? 310 VAL D CB     1 
ATOM   10925 C CG1    . VAL D 2 292 ? 38.984  55.988  62.822 1.00 43.81  ? 310 VAL D CG1    1 
ATOM   10926 C CG2    . VAL D 2 292 ? 38.419  56.878  60.565 1.00 44.28  ? 310 VAL D CG2    1 
ATOM   10927 N N      . VAL D 2 293 ? 42.399  55.701  61.725 1.00 45.01  ? 311 VAL D N      1 
ATOM   10928 C CA     . VAL D 2 293 ? 43.417  54.972  62.447 1.00 40.16  ? 311 VAL D CA     1 
ATOM   10929 C C      . VAL D 2 293 ? 44.493  55.875  62.930 1.00 37.52  ? 311 VAL D C      1 
ATOM   10930 O O      . VAL D 2 293 ? 44.875  55.794  64.073 1.00 44.91  ? 311 VAL D O      1 
ATOM   10931 C CB     . VAL D 2 293 ? 43.986  53.825  61.605 1.00 38.50  ? 311 VAL D CB     1 
ATOM   10932 C CG1    . VAL D 2 293 ? 45.464  53.606  61.843 1.00 37.50  ? 311 VAL D CG1    1 
ATOM   10933 C CG2    . VAL D 2 293 ? 43.208  52.558  61.876 1.00 40.27  ? 311 VAL D CG2    1 
ATOM   10934 N N      . ASP D 2 294 ? 44.954  56.787  62.098 1.00 37.20  ? 312 ASP D N      1 
ATOM   10935 C CA     . ASP D 2 294 ? 46.080  57.608  62.487 1.00 41.88  ? 312 ASP D CA     1 
ATOM   10936 C C      . ASP D 2 294 ? 45.757  58.659  63.504 1.00 41.97  ? 312 ASP D C      1 
ATOM   10937 O O      . ASP D 2 294 ? 46.562  59.542  63.752 1.00 35.28  ? 312 ASP D O      1 
ATOM   10938 C CB     . ASP D 2 294 ? 46.828  58.148  61.291 1.00 43.71  ? 312 ASP D CB     1 
ATOM   10939 C CG     . ASP D 2 294 ? 47.912  57.208  60.816 1.00 45.55  ? 312 ASP D CG     1 
ATOM   10940 O OD1    . ASP D 2 294 ? 47.796  55.992  61.047 1.00 42.76  ? 312 ASP D OD1    1 
ATOM   10941 O OD2    . ASP D 2 294 ? 48.887  57.687  60.211 1.00 49.60  ? 312 ASP D OD2    1 
ATOM   10942 N N      . VAL D 2 295 ? 44.582  58.599  64.106 1.00 43.14  ? 313 VAL D N      1 
ATOM   10943 C CA     . VAL D 2 295 ? 44.301  59.509  65.208 1.00 47.50  ? 313 VAL D CA     1 
ATOM   10944 C C      . VAL D 2 295 ? 44.234  58.646  66.442 1.00 45.05  ? 313 VAL D C      1 
ATOM   10945 O O      . VAL D 2 295 ? 44.724  59.035  67.476 1.00 43.45  ? 313 VAL D O      1 
ATOM   10946 C CB     . VAL D 2 295 ? 43.042  60.370  65.031 1.00 44.97  ? 313 VAL D CB     1 
ATOM   10947 C CG1    . VAL D 2 295 ? 43.208  61.300  63.849 1.00 42.03  ? 313 VAL D CG1    1 
ATOM   10948 C CG2    . VAL D 2 295 ? 41.804  59.542  64.840 1.00 46.07  ? 313 VAL D CG2    1 
ATOM   10949 N N      . LEU D 2 296 ? 43.678  57.445  66.327 1.00 40.01  ? 314 LEU D N      1 
ATOM   10950 C CA     . LEU D 2 296 ? 43.590  56.517  67.450 1.00 37.74  ? 314 LEU D CA     1 
ATOM   10951 C C      . LEU D 2 296 ? 44.945  55.948  67.769 1.00 46.04  ? 314 LEU D C      1 
ATOM   10952 O O      . LEU D 2 296 ? 45.207  55.576  68.898 1.00 51.59  ? 314 LEU D O      1 
ATOM   10953 C CB     . LEU D 2 296 ? 42.666  55.365  67.111 1.00 35.79  ? 314 LEU D CB     1 
ATOM   10954 C CG     . LEU D 2 296 ? 41.171  55.534  66.940 1.00 37.50  ? 314 LEU D CG     1 
ATOM   10955 C CD1    . LEU D 2 296 ? 40.647  54.419  66.057 1.00 33.53  ? 314 LEU D CD1    1 
ATOM   10956 C CD2    . LEU D 2 296 ? 40.527  55.476  68.306 1.00 37.00  ? 314 LEU D CD2    1 
ATOM   10957 N N      . THR D 2 297 ? 45.819  55.873  66.780 1.00 43.72  ? 315 THR D N      1 
ATOM   10958 C CA     . THR D 2 297 ? 47.150  55.345  66.993 1.00 43.00  ? 315 THR D CA     1 
ATOM   10959 C C      . THR D 2 297 ? 48.035  56.293  67.740 1.00 49.36  ? 315 THR D C      1 
ATOM   10960 O O      . THR D 2 297 ? 49.100  55.901  68.180 1.00 52.22  ? 315 THR D O      1 
ATOM   10961 C CB     . THR D 2 297 ? 47.881  55.074  65.680 1.00 38.76  ? 315 THR D CB     1 
ATOM   10962 O OG1    . THR D 2 297 ? 47.806  56.228  64.845 1.00 40.51  ? 315 THR D OG1    1 
ATOM   10963 C CG2    . THR D 2 297 ? 47.291  53.888  64.973 1.00 39.81  ? 315 THR D CG2    1 
ATOM   10964 N N      . GLU D 2 298 ? 47.642  57.544  67.885 1.00 45.16  ? 316 GLU D N      1 
ATOM   10965 C CA     . GLU D 2 298 ? 48.507  58.509  68.508 1.00 38.21  ? 316 GLU D CA     1 
ATOM   10966 C C      . GLU D 2 298 ? 48.777  58.062  69.879 1.00 41.59  ? 316 GLU D C      1 
ATOM   10967 O O      . GLU D 2 298 ? 47.900  57.548  70.542 1.00 42.53  ? 316 GLU D O      1 
ATOM   10968 C CB     . GLU D 2 298 ? 47.857  59.869  68.551 1.00 43.59  ? 316 GLU D CB     1 
ATOM   10969 C CG     . GLU D 2 298 ? 48.834  60.992  68.813 1.00 49.62  ? 316 GLU D CG     1 
ATOM   10970 C CD     . GLU D 2 298 ? 48.350  62.307  68.283 1.00 56.58  ? 316 GLU D CD     1 
ATOM   10971 O OE1    . GLU D 2 298 ? 47.166  62.386  67.908 1.00 55.12  ? 316 GLU D OE1    1 
ATOM   10972 O OE2    . GLU D 2 298 ? 49.159  63.250  68.241 1.00 59.94  ? 316 GLU D OE2    1 
ATOM   10973 N N      . PRO D 2 299 ? 50.067  58.170  70.309 1.00 43.16  ? 317 PRO D N      1 
ATOM   10974 C CA     . PRO D 2 299 ? 50.408  57.821  71.677 1.00 45.82  ? 317 PRO D CA     1 
ATOM   10975 C C      . PRO D 2 299 ? 49.454  58.179  72.774 1.00 49.32  ? 317 PRO D C      1 
ATOM   10976 O O      . PRO D 2 299 ? 49.151  57.319  73.584 1.00 50.85  ? 317 PRO D O      1 
ATOM   10977 C CB     . PRO D 2 299 ? 51.660  58.634  71.883 1.00 43.51  ? 317 PRO D CB     1 
ATOM   10978 C CG     . PRO D 2 299 ? 52.243  58.736  70.533 1.00 39.94  ? 317 PRO D CG     1 
ATOM   10979 C CD     . PRO D 2 299 ? 51.084  58.884  69.600 1.00 41.03  ? 317 PRO D CD     1 
ATOM   10980 N N      . PHE D 2 300 ? 49.005  59.417  72.846 1.00 45.55  ? 318 PHE D N      1 
ATOM   10981 C CA     . PHE D 2 300 ? 48.178  59.823  73.971 1.00 41.84  ? 318 PHE D CA     1 
ATOM   10982 C C      . PHE D 2 300 ? 46.922  59.022  74.083 1.00 45.29  ? 318 PHE D C      1 
ATOM   10983 O O      . PHE D 2 300 ? 46.441  58.788  75.177 1.00 41.74  ? 318 PHE D O      1 
ATOM   10984 C CB     . PHE D 2 300 ? 47.910  61.324  73.971 1.00 40.53  ? 318 PHE D CB     1 
ATOM   10985 C CG     . PHE D 2 300 ? 46.784  61.765  73.095 1.00 46.93  ? 318 PHE D CG     1 
ATOM   10986 C CD1    . PHE D 2 300 ? 46.974  61.959  71.746 1.00 49.04  ? 318 PHE D CD1    1 
ATOM   10987 C CD2    . PHE D 2 300 ? 45.549  62.043  73.637 1.00 47.54  ? 318 PHE D CD2    1 
ATOM   10988 C CE1    . PHE D 2 300 ? 45.940  62.383  70.946 1.00 49.89  ? 318 PHE D CE1    1 
ATOM   10989 C CE2    . PHE D 2 300 ? 44.512  62.470  72.845 1.00 47.63  ? 318 PHE D CE2    1 
ATOM   10990 C CZ     . PHE D 2 300 ? 44.709  62.642  71.497 1.00 51.38  ? 318 PHE D CZ     1 
ATOM   10991 N N      . LEU D 2 301 ? 46.429  58.523  72.967 1.00 48.27  ? 319 LEU D N      1 
ATOM   10992 C CA     . LEU D 2 301 ? 45.193  57.781  72.990 1.00 49.70  ? 319 LEU D CA     1 
ATOM   10993 C C      . LEU D 2 301 ? 45.448  56.355  73.385 1.00 56.42  ? 319 LEU D C      1 
ATOM   10994 O O      . LEU D 2 301 ? 44.652  55.746  74.072 1.00 55.22  ? 319 LEU D O      1 
ATOM   10995 C CB     . LEU D 2 301 ? 44.505  57.850  71.651 1.00 48.40  ? 319 LEU D CB     1 
ATOM   10996 C CG     . LEU D 2 301 ? 43.713  59.129  71.427 1.00 52.73  ? 319 LEU D CG     1 
ATOM   10997 C CD1    . LEU D 2 301 ? 42.906  59.032  70.152 1.00 55.44  ? 319 LEU D CD1    1 
ATOM   10998 C CD2    . LEU D 2 301 ? 42.787  59.360  72.605 1.00 49.90  ? 319 LEU D CD2    1 
ATOM   10999 N N      . GLN D 2 302 ? 46.581  55.818  72.969 1.00 56.12  ? 320 GLN D N      1 
ATOM   11000 C CA     . GLN D 2 302 ? 46.882  54.437  73.256 1.00 51.92  ? 320 GLN D CA     1 
ATOM   11001 C C      . GLN D 2 302 ? 47.013  54.215  74.731 1.00 53.23  ? 320 GLN D C      1 
ATOM   11002 O O      . GLN D 2 302 ? 46.862  53.110  75.189 1.00 58.04  ? 320 GLN D O      1 
ATOM   11003 C CB     . GLN D 2 302 ? 48.136  53.987  72.536 1.00 49.16  ? 320 GLN D CB     1 
ATOM   11004 C CG     . GLN D 2 302 ? 47.952  53.773  71.050 1.00 50.75  ? 320 GLN D CG     1 
ATOM   11005 C CD     . GLN D 2 302 ? 46.964  52.672  70.749 1.00 66.38  ? 320 GLN D CD     1 
ATOM   11006 O OE1    . GLN D 2 302 ? 47.144  51.528  71.162 1.00 62.68  ? 320 GLN D OE1    1 
ATOM   11007 N NE2    . GLN D 2 302 ? 45.916  53.009  70.015 1.00 67.07  ? 320 GLN D NE2    1 
ATOM   11008 N N      . SER D 2 303 ? 47.325  55.240  75.491 1.00 48.20  ? 321 SER D N      1 
ATOM   11009 C CA     . SER D 2 303 ? 47.554  55.023  76.906 1.00 55.72  ? 321 SER D CA     1 
ATOM   11010 C C      . SER D 2 303 ? 46.289  54.534  77.525 1.00 55.59  ? 321 SER D C      1 
ATOM   11011 O O      . SER D 2 303 ? 46.311  53.778  78.476 1.00 56.61  ? 321 SER D O      1 
ATOM   11012 C CB     . SER D 2 303 ? 47.974  56.305  77.605 1.00 58.69  ? 321 SER D CB     1 
ATOM   11013 O OG     . SER D 2 303 ? 49.197  56.786  77.087 1.00 63.75  ? 321 SER D OG     1 
ATOM   11014 N N      . ILE D 2 304 ? 45.165  54.913  76.964 1.00 52.92  ? 322 ILE D N      1 
ATOM   11015 C CA     . ILE D 2 304 ? 43.925  54.537  77.582 1.00 54.35  ? 322 ILE D CA     1 
ATOM   11016 C C      . ILE D 2 304 ? 43.873  53.046  77.455 1.00 57.98  ? 322 ILE D C      1 
ATOM   11017 O O      . ILE D 2 304 ? 43.658  52.337  78.426 1.00 65.07  ? 322 ILE D O      1 
ATOM   11018 C CB     . ILE D 2 304 ? 42.727  55.207  76.902 1.00 49.94  ? 322 ILE D CB     1 
ATOM   11019 C CG1    . ILE D 2 304 ? 42.579  56.653  77.376 1.00 47.67  ? 322 ILE D CG1    1 
ATOM   11020 C CG2    . ILE D 2 304 ? 41.444  54.477  77.240 1.00 46.95  ? 322 ILE D CG2    1 
ATOM   11021 C CD1    . ILE D 2 304 ? 43.377  57.671  76.596 1.00 48.89  ? 322 ILE D CD1    1 
ATOM   11022 N N      . PHE D 2 305 ? 44.160  52.552  76.270 1.00 52.58  ? 323 PHE D N      1 
ATOM   11023 C CA     . PHE D 2 305 ? 44.075  51.134  76.028 1.00 49.80  ? 323 PHE D CA     1 
ATOM   11024 C C      . PHE D 2 305 ? 45.173  50.395  76.724 1.00 54.35  ? 323 PHE D C      1 
ATOM   11025 O O      . PHE D 2 305 ? 44.927  49.390  77.361 1.00 55.93  ? 323 PHE D O      1 
ATOM   11026 C CB     . PHE D 2 305 ? 44.194  50.872  74.539 1.00 47.05  ? 323 PHE D CB     1 
ATOM   11027 C CG     . PHE D 2 305 ? 43.179  51.582  73.709 1.00 48.76  ? 323 PHE D CG     1 
ATOM   11028 C CD1    . PHE D 2 305 ? 41.835  51.369  73.911 1.00 48.34  ? 323 PHE D CD1    1 
ATOM   11029 C CD2    . PHE D 2 305 ? 43.575  52.435  72.707 1.00 52.22  ? 323 PHE D CD2    1 
ATOM   11030 C CE1    . PHE D 2 305 ? 40.899  52.013  73.139 1.00 44.40  ? 323 PHE D CE1    1 
ATOM   11031 C CE2    . PHE D 2 305 ? 42.647  53.084  71.929 1.00 50.19  ? 323 PHE D CE2    1 
ATOM   11032 C CZ     . PHE D 2 305 ? 41.306  52.870  72.145 1.00 46.09  ? 323 PHE D CZ     1 
ATOM   11033 N N      . ASP D 2 306 ? 46.400  50.855  76.566 1.00 52.76  ? 324 ASP D N      1 
ATOM   11034 C CA     . ASP D 2 306 ? 47.531  50.138  77.111 1.00 54.02  ? 324 ASP D CA     1 
ATOM   11035 C C      . ASP D 2 306 ? 47.397  49.895  78.583 1.00 54.22  ? 324 ASP D C      1 
ATOM   11036 O O      . ASP D 2 306 ? 47.676  48.809  79.059 1.00 57.30  ? 324 ASP D O      1 
ATOM   11037 C CB     . ASP D 2 306 ? 48.804  50.909  76.812 1.00 56.00  ? 324 ASP D CB     1 
ATOM   11038 C CG     . ASP D 2 306 ? 49.199  50.844  75.354 1.00 58.81  ? 324 ASP D CG     1 
ATOM   11039 O OD1    . ASP D 2 306 ? 48.528  50.134  74.584 1.00 63.75  ? 324 ASP D OD1    1 
ATOM   11040 O OD2    . ASP D 2 306 ? 50.190  51.502  74.975 1.00 54.70  ? 324 ASP D OD2    1 
ATOM   11041 N N      . LYS D 2 307 ? 46.947  50.890  79.320 1.00 54.44  ? 325 LYS D N      1 
ATOM   11042 C CA     . LYS D 2 307 ? 46.848  50.757  80.764 1.00 56.27  ? 325 LYS D CA     1 
ATOM   11043 C C      . LYS D 2 307 ? 45.681  49.905  81.171 1.00 54.81  ? 325 LYS D C      1 
ATOM   11044 O O      . LYS D 2 307 ? 45.500  49.620  82.348 1.00 52.24  ? 325 LYS D O      1 
ATOM   11045 C CB     . LYS D 2 307 ? 46.765  52.121  81.427 1.00 59.64  ? 325 LYS D CB     1 
ATOM   11046 C CG     . LYS D 2 307 ? 48.003  52.980  81.226 1.00 61.30  ? 325 LYS D CG     1 
ATOM   11047 C CD     . LYS D 2 307 ? 48.051  54.137  82.213 1.00 54.56  ? 325 LYS D CD     1 
ATOM   11048 C CE     . LYS D 2 307 ? 46.773  54.954  82.189 1.00 51.45  ? 325 LYS D CE     1 
ATOM   11049 N NZ     . LYS D 2 307 ? 46.035  54.875  83.479 1.00 47.71  ? 325 LYS D NZ     1 
ATOM   11050 N N      . ALA D 2 308 ? 44.920  49.444  80.195 1.00 51.87  ? 326 ALA D N      1 
ATOM   11051 C CA     . ALA D 2 308 ? 43.822  48.544  80.488 1.00 54.31  ? 326 ALA D CA     1 
ATOM   11052 C C      . ALA D 2 308 ? 43.990  47.311  79.643 1.00 52.27  ? 326 ALA D C      1 
ATOM   11053 O O      . ALA D 2 308 ? 43.042  46.577  79.421 1.00 46.95  ? 326 ALA D O      1 
ATOM   11054 C CB     . ALA D 2 308 ? 42.514  49.212  80.199 1.00 50.03  ? 326 ALA D CB     1 
ATOM   11055 N N      . ASN D 2 309 ? 45.200  47.105  79.153 1.00 50.03  ? 327 ASN D N      1 
ATOM   11056 C CA     . ASN D 2 309 ? 45.504  45.947  78.336 1.00 49.66  ? 327 ASN D CA     1 
ATOM   11057 C C      . ASN D 2 309 ? 44.587  45.736  77.186 1.00 51.70  ? 327 ASN D C      1 
ATOM   11058 O O      . ASN D 2 309 ? 43.857  44.757  77.156 1.00 51.44  ? 327 ASN D O      1 
ATOM   11059 C CB     . ASN D 2 309 ? 45.581  44.679  79.164 1.00 56.56  ? 327 ASN D CB     1 
ATOM   11060 C CG     . ASN D 2 309 ? 46.573  43.683  78.604 1.00 65.11  ? 327 ASN D CG     1 
ATOM   11061 O OD1    . ASN D 2 309 ? 47.362  44.010  77.720 1.00 70.25  ? 327 ASN D OD1    1 
ATOM   11062 N ND2    . ASN D 2 309 ? 46.540  42.463  79.119 1.00 68.35  ? 327 ASN D ND2    1 
ATOM   11063 N N      . ILE D 2 310 ? 44.607  46.643  76.225 1.00 47.90  ? 328 ILE D N      1 
ATOM   11064 C CA     . ILE D 2 310 ? 43.830  46.454  75.024 1.00 43.99  ? 328 ILE D CA     1 
ATOM   11065 C C      . ILE D 2 310 ? 44.800  46.670  73.886 1.00 44.05  ? 328 ILE D C      1 
ATOM   11066 O O      . ILE D 2 310 ? 45.341  47.744  73.738 1.00 48.60  ? 328 ILE D O      1 
ATOM   11067 C CB     . ILE D 2 310 ? 42.626  47.394  74.947 1.00 39.44  ? 328 ILE D CB     1 
ATOM   11068 C CG1    . ILE D 2 310 ? 41.844  47.375  76.251 1.00 41.52  ? 328 ILE D CG1    1 
ATOM   11069 C CG2    . ILE D 2 310 ? 41.695  46.976  73.832 1.00 43.22  ? 328 ILE D CG2    1 
ATOM   11070 C CD1    . ILE D 2 310 ? 40.502  48.046  76.151 1.00 44.26  ? 328 ILE D CD1    1 
ATOM   11071 N N      . LYS D 2 311 ? 45.077  45.626  73.119 1.00 45.96  ? 329 LYS D N      1 
ATOM   11072 C CA     . LYS D 2 311 ? 45.977  45.720  71.995 1.00 41.82  ? 329 LYS D CA     1 
ATOM   11073 C C      . LYS D 2 311 ? 45.004  45.722  70.894 1.00 45.01  ? 329 LYS D C      1 
ATOM   11074 O O      . LYS D 2 311 ? 44.096  44.905  70.879 1.00 46.52  ? 329 LYS D O      1 
ATOM   11075 C CB     . LYS D 2 311 ? 46.827  44.480  71.906 1.00 47.50  ? 329 LYS D CB     1 
ATOM   11076 C CG     . LYS D 2 311 ? 47.266  43.946  73.254 1.00 54.29  ? 329 LYS D CG     1 
ATOM   11077 C CD     . LYS D 2 311 ? 47.680  42.491  73.152 1.00 51.44  ? 329 LYS D CD     1 
ATOM   11078 C CE     . LYS D 2 311 ? 47.926  41.912  74.531 1.00 59.26  ? 329 LYS D CE     1 
ATOM   11079 N NZ     . LYS D 2 311 ? 46.718  42.061  75.382 1.00 54.95  ? 329 LYS D NZ     1 
ATOM   11080 N N      . LEU D 2 312 ? 45.170  46.629  69.953 1.00 47.25  ? 330 LEU D N      1 
ATOM   11081 C CA     . LEU D 2 312 ? 44.164  46.771  68.935 1.00 45.32  ? 330 LEU D CA     1 
ATOM   11082 C C      . LEU D 2 312 ? 44.561  46.291  67.569 1.00 49.46  ? 330 LEU D C      1 
ATOM   11083 O O      . LEU D 2 312 ? 45.615  46.652  67.074 1.00 51.08  ? 330 LEU D O      1 
ATOM   11084 C CB     . LEU D 2 312 ? 43.723  48.228  68.871 1.00 47.09  ? 330 LEU D CB     1 
ATOM   11085 C CG     . LEU D 2 312 ? 43.471  49.109  70.091 1.00 47.09  ? 330 LEU D CG     1 
ATOM   11086 C CD1    . LEU D 2 312 ? 43.421  50.544  69.620 1.00 44.64  ? 330 LEU D CD1    1 
ATOM   11087 C CD2    . LEU D 2 312 ? 42.174  48.778  70.794 1.00 48.33  ? 330 LEU D CD2    1 
ATOM   11088 N N      . ASN D 2 313 ? 43.716  45.492  66.936 1.00 51.69  ? 331 ASN D N      1 
ATOM   11089 C CA     . ASN D 2 313 ? 44.021  44.952  65.629 1.00 46.56  ? 331 ASN D CA     1 
ATOM   11090 C C      . ASN D 2 313 ? 43.925  46.012  64.588 1.00 46.38  ? 331 ASN D C      1 
ATOM   11091 O O      . ASN D 2 313 ? 44.608  45.925  63.581 1.00 48.34  ? 331 ASN D O      1 
ATOM   11092 C CB     . ASN D 2 313 ? 43.080  43.802  65.303 1.00 41.07  ? 331 ASN D CB     1 
ATOM   11093 C CG     . ASN D 2 313 ? 41.638  44.076  65.678 1.00 49.38  ? 331 ASN D CG     1 
ATOM   11094 O OD1    . ASN D 2 313 ? 41.260  45.196  66.009 1.00 51.30  ? 331 ASN D OD1    1 
ATOM   11095 N ND2    . ASN D 2 313 ? 40.816  43.038  65.617 1.00 44.86  ? 331 ASN D ND2    1 
ATOM   11096 N N      . TYR D 2 314 ? 43.103  47.020  64.835 1.00 42.99  ? 332 TYR D N      1 
ATOM   11097 C CA     . TYR D 2 314 ? 42.904  48.117  63.902 1.00 44.76  ? 332 TYR D CA     1 
ATOM   11098 C C      . TYR D 2 314 ? 42.243  47.619  62.656 1.00 45.86  ? 332 TYR D C      1 
ATOM   11099 O O      . TYR D 2 314 ? 42.212  48.292  61.645 1.00 48.26  ? 332 TYR D O      1 
ATOM   11100 C CB     . TYR D 2 314 ? 44.205  48.830  63.569 1.00 47.30  ? 332 TYR D CB     1 
ATOM   11101 C CG     . TYR D 2 314 ? 44.827  49.577  64.706 1.00 45.18  ? 332 TYR D CG     1 
ATOM   11102 C CD1    . TYR D 2 314 ? 44.121  50.550  65.386 1.00 46.14  ? 332 TYR D CD1    1 
ATOM   11103 C CD2    . TYR D 2 314 ? 46.133  49.332  65.077 1.00 47.06  ? 332 TYR D CD2    1 
ATOM   11104 C CE1    . TYR D 2 314 ? 44.697  51.246  66.422 1.00 50.73  ? 332 TYR D CE1    1 
ATOM   11105 C CE2    . TYR D 2 314 ? 46.717  50.020  66.112 1.00 49.90  ? 332 TYR D CE2    1 
ATOM   11106 C CZ     . TYR D 2 314 ? 45.991  50.973  66.779 1.00 52.17  ? 332 TYR D CZ     1 
ATOM   11107 O OH     . TYR D 2 314 ? 46.577  51.656  67.805 1.00 56.66  ? 332 TYR D OH     1 
ATOM   11108 N N      . GLY D 2 315 ? 41.695  46.435  62.726 1.00 39.08  ? 333 GLY D N      1 
ATOM   11109 C CA     . GLY D 2 315 ? 41.009  45.905  61.583 1.00 43.37  ? 333 GLY D CA     1 
ATOM   11110 C C      . GLY D 2 315 ? 41.871  45.131  60.630 1.00 47.79  ? 333 GLY D C      1 
ATOM   11111 O O      . GLY D 2 315 ? 41.413  44.739  59.575 1.00 55.13  ? 333 GLY D O      1 
ATOM   11112 N N      . VAL D 2 316 ? 43.115  44.881  60.994 1.00 41.71  ? 334 VAL D N      1 
ATOM   11113 C CA     . VAL D 2 316 ? 43.945  44.092  60.138 1.00 40.29  ? 334 VAL D CA     1 
ATOM   11114 C C      . VAL D 2 316 ? 43.235  42.789  60.123 1.00 42.80  ? 334 VAL D C      1 
ATOM   11115 O O      . VAL D 2 316 ? 42.705  42.345  61.131 1.00 44.24  ? 334 VAL D O      1 
ATOM   11116 C CB     . VAL D 2 316 ? 45.408  44.019  60.585 1.00 36.99  ? 334 VAL D CB     1 
ATOM   11117 C CG1    . VAL D 2 316 ? 45.599  43.081  61.764 1.00 57.95  ? 334 VAL D CG1    1 
ATOM   11118 C CG2    . VAL D 2 316 ? 46.305  43.614  59.431 1.00 36.54  ? 334 VAL D CG2    1 
ATOM   11119 N N      . LEU D 2 317 ? 43.181  42.167  58.970 1.00 48.20  ? 335 LEU D N      1 
ATOM   11120 C CA     . LEU D 2 317 ? 42.391  40.979  58.861 1.00 48.51  ? 335 LEU D CA     1 
ATOM   11121 C C      . LEU D 2 317 ? 43.222  39.883  58.299 1.00 50.90  ? 335 LEU D C      1 
ATOM   11122 O O      . LEU D 2 317 ? 44.258  40.117  57.698 1.00 49.74  ? 335 LEU D O      1 
ATOM   11123 C CB     . LEU D 2 317 ? 41.184  41.264  57.981 1.00 51.18  ? 335 LEU D CB     1 
ATOM   11124 C CG     . LEU D 2 317 ? 39.779  40.900  58.449 1.00 53.73  ? 335 LEU D CG     1 
ATOM   11125 C CD1    . LEU D 2 317 ? 39.622  41.110  59.943 1.00 49.46  ? 335 LEU D CD1    1 
ATOM   11126 C CD2    . LEU D 2 317 ? 38.771  41.735  57.683 1.00 44.09  ? 335 LEU D CD2    1 
ATOM   11127 N N      . ASP D 2 318 ? 42.792  38.647  58.536 1.00 51.36  ? 336 ASP D N      1 
ATOM   11128 C CA     . ASP D 2 318 ? 43.560  37.489  58.089 1.00 53.43  ? 336 ASP D CA     1 
ATOM   11129 C C      . ASP D 2 318 ? 43.711  37.399  56.575 1.00 54.99  ? 336 ASP D C      1 
ATOM   11130 O O      . ASP D 2 318 ? 44.795  37.093  56.079 1.00 50.61  ? 336 ASP D O      1 
ATOM   11131 C CB     . ASP D 2 318 ? 42.976  36.185  58.657 1.00 56.67  ? 336 ASP D CB     1 
ATOM   11132 C CG     . ASP D 2 318 ? 41.529  35.945  58.240 1.00 77.96  ? 336 ASP D CG     1 
ATOM   11133 O OD1    . ASP D 2 318 ? 40.766  36.922  58.073 1.00 70.48  ? 336 ASP D OD1    1 
ATOM   11134 O OD2    . ASP D 2 318 ? 41.150  34.766  58.092 1.00 96.88  ? 336 ASP D OD2    1 
ATOM   11135 N N      . ASP D 2 319 ? 42.636  37.664  55.839 1.00 53.34  ? 337 ASP D N      1 
ATOM   11136 C CA     . ASP D 2 319 ? 42.708  37.547  54.400 1.00 45.22  ? 337 ASP D CA     1 
ATOM   11137 C C      . ASP D 2 319 ? 42.230  38.792  53.752 1.00 54.66  ? 337 ASP D C      1 
ATOM   11138 O O      . ASP D 2 319 ? 41.115  39.217  53.992 1.00 58.03  ? 337 ASP D O      1 
ATOM   11139 C CB     . ASP D 2 319 ? 41.829  36.413  53.924 1.00 50.48  ? 337 ASP D CB     1 
ATOM   11140 C CG     . ASP D 2 319 ? 42.065  36.067  52.477 1.00 67.68  ? 337 ASP D CG     1 
ATOM   11141 O OD1    . ASP D 2 319 ? 43.224  36.156  52.027 1.00 71.89  ? 337 ASP D OD1    1 
ATOM   11142 O OD2    . ASP D 2 319 ? 41.094  35.691  51.793 1.00 71.20  ? 337 ASP D OD2    1 
ATOM   11143 N N      . THR D 2 320 ? 43.064  39.395  52.924 1.00 60.77  ? 338 THR D N      1 
ATOM   11144 C CA     . THR D 2 320 ? 42.661  40.566  52.187 1.00 61.05  ? 338 THR D CA     1 
ATOM   11145 C C      . THR D 2 320 ? 42.704  40.272  50.729 1.00 60.17  ? 338 THR D C      1 
ATOM   11146 O O      . THR D 2 320 ? 42.557  41.172  49.930 1.00 64.24  ? 338 THR D O      1 
ATOM   11147 C CB     . THR D 2 320 ? 43.630  41.723  52.406 1.00 55.94  ? 338 THR D CB     1 
ATOM   11148 O OG1    . THR D 2 320 ? 44.924  41.359  51.919 1.00 61.75  ? 338 THR D OG1    1 
ATOM   11149 C CG2    . THR D 2 320 ? 43.727  42.069  53.883 1.00 55.21  ? 338 THR D CG2    1 
ATOM   11150 N N      . HIS D 2 321 ? 42.904  39.024  50.353 1.00 56.00  ? 339 HIS D N      1 
ATOM   11151 C CA     . HIS D 2 321 ? 43.094  38.739  48.945 1.00 58.60  ? 339 HIS D CA     1 
ATOM   11152 C C      . HIS D 2 321 ? 41.931  39.072  48.084 1.00 56.41  ? 339 HIS D C      1 
ATOM   11153 O O      . HIS D 2 321 ? 42.101  39.520  46.968 1.00 56.84  ? 339 HIS D O      1 
ATOM   11154 C CB     . HIS D 2 321 ? 43.480  37.298  48.695 1.00 62.91  ? 339 HIS D CB     1 
ATOM   11155 C CG     . HIS D 2 321 ? 43.993  37.054  47.312 1.00 64.80  ? 339 HIS D CG     1 
ATOM   11156 N ND1    . HIS D 2 321 ? 45.240  37.470  46.902 1.00 66.23  ? 339 HIS D ND1    1 
ATOM   11157 C CD2    . HIS D 2 321 ? 43.424  36.456  46.241 1.00 64.62  ? 339 HIS D CD2    1 
ATOM   11158 C CE1    . HIS D 2 321 ? 45.420  37.133  45.638 1.00 69.70  ? 339 HIS D CE1    1 
ATOM   11159 N NE2    . HIS D 2 321 ? 44.332  36.515  45.213 1.00 73.45  ? 339 HIS D NE2    1 
ATOM   11160 N N      . ALA D 2 322 ? 40.746  38.854  48.575 1.00 53.17  ? 340 ALA D N      1 
ATOM   11161 C CA     . ALA D 2 322 ? 39.606  39.055  47.738 1.00 49.03  ? 340 ALA D CA     1 
ATOM   11162 C C      . ALA D 2 322 ? 39.685  40.435  47.237 1.00 48.18  ? 340 ALA D C      1 
ATOM   11163 O O      . ALA D 2 322 ? 39.422  40.687  46.088 1.00 57.92  ? 340 ALA D O      1 
ATOM   11164 C CB     . ALA D 2 322 ? 38.358  38.892  48.562 1.00 42.21  ? 340 ALA D CB     1 
ATOM   11165 N N      . GLU D 2 323 ? 40.067  41.354  48.088 1.00 40.87  ? 341 GLU D N      1 
ATOM   11166 C CA     . GLU D 2 323 ? 40.042  42.728  47.694 1.00 37.65  ? 341 GLU D CA     1 
ATOM   11167 C C      . GLU D 2 323 ? 41.282  43.069  46.970 1.00 43.62  ? 341 GLU D C      1 
ATOM   11168 O O      . GLU D 2 323 ? 41.307  44.024  46.223 1.00 50.54  ? 341 GLU D O      1 
ATOM   11169 C CB     . GLU D 2 323 ? 39.888  43.597  48.913 1.00 42.31  ? 341 GLU D CB     1 
ATOM   11170 C CG     . GLU D 2 323 ? 38.709  43.199  49.787 1.00 52.42  ? 341 GLU D CG     1 
ATOM   11171 C CD     . GLU D 2 323 ? 39.124  42.521  51.079 1.00 60.41  ? 341 GLU D CD     1 
ATOM   11172 O OE1    . GLU D 2 323 ? 40.220  42.822  51.584 1.00 56.42  ? 341 GLU D OE1    1 
ATOM   11173 O OE2    . GLU D 2 323 ? 38.346  41.701  51.603 1.00 54.11  ? 341 GLU D OE2    1 
ATOM   11174 N N      . PHE D 2 324 ? 42.307  42.261  47.113 1.00 41.83  ? 342 PHE D N      1 
ATOM   11175 C CA     . PHE D 2 324 ? 43.521  42.510  46.372 1.00 42.98  ? 342 PHE D CA     1 
ATOM   11176 C C      . PHE D 2 324 ? 43.248  42.158  44.947 1.00 51.94  ? 342 PHE D C      1 
ATOM   11177 O O      . PHE D 2 324 ? 43.580  42.905  44.053 1.00 52.40  ? 342 PHE D O      1 
ATOM   11178 C CB     . PHE D 2 324 ? 44.667  41.685  46.897 1.00 45.79  ? 342 PHE D CB     1 
ATOM   11179 C CG     . PHE D 2 324 ? 45.980  42.386  46.892 1.00 40.12  ? 342 PHE D CG     1 
ATOM   11180 C CD1    . PHE D 2 324 ? 46.128  43.598  47.518 1.00 41.12  ? 342 PHE D CD1    1 
ATOM   11181 C CD2    . PHE D 2 324 ? 47.076  41.811  46.292 1.00 40.13  ? 342 PHE D CD2    1 
ATOM   11182 C CE1    . PHE D 2 324 ? 47.342  44.239  47.521 1.00 44.49  ? 342 PHE D CE1    1 
ATOM   11183 C CE2    . PHE D 2 324 ? 48.294  42.445  46.297 1.00 38.00  ? 342 PHE D CE2    1 
ATOM   11184 C CZ     . PHE D 2 324 ? 48.429  43.665  46.909 1.00 41.25  ? 342 PHE D CZ     1 
ATOM   11185 N N      . ARG D 2 325 ? 42.618  41.020  44.724 1.00 54.27  ? 343 ARG D N      1 
ATOM   11186 C CA     . ARG D 2 325 ? 42.370  40.574  43.365 1.00 50.37  ? 343 ARG D CA     1 
ATOM   11187 C C      . ARG D 2 325 ? 41.486  41.548  42.678 1.00 51.30  ? 343 ARG D C      1 
ATOM   11188 O O      . ARG D 2 325 ? 41.743  41.950  41.561 1.00 59.51  ? 343 ARG D O      1 
ATOM   11189 C CB     . ARG D 2 325 ? 41.694  39.215  43.340 1.00 53.83  ? 343 ARG D CB     1 
ATOM   11190 C CG     . ARG D 2 325 ? 41.363  38.713  41.949 1.00 58.67  ? 343 ARG D CG     1 
ATOM   11191 C CD     . ARG D 2 325 ? 40.155  37.799  41.969 1.00 58.41  ? 343 ARG D CD     1 
ATOM   11192 N NE     . ARG D 2 325 ? 39.141  38.267  42.908 1.00 60.28  ? 343 ARG D NE     1 
ATOM   11193 C CZ     . ARG D 2 325 ? 37.882  37.848  42.916 1.00 63.30  ? 343 ARG D CZ     1 
ATOM   11194 N NH1    . ARG D 2 325 ? 37.472  36.965  42.020 1.00 71.08  ? 343 ARG D NH1    1 
ATOM   11195 N NH2    . ARG D 2 325 ? 37.028  38.320  43.808 1.00 55.53  ? 343 ARG D NH2    1 
ATOM   11196 N N      . LYS D 2 326 ? 40.431  41.954  43.340 1.00 47.37  ? 344 LYS D N      1 
ATOM   11197 C CA     . LYS D 2 326 ? 39.498  42.816  42.682 1.00 52.23  ? 344 LYS D CA     1 
ATOM   11198 C C      . LYS D 2 326 ? 40.158  44.103  42.351 1.00 53.59  ? 344 LYS D C      1 
ATOM   11199 O O      . LYS D 2 326 ? 39.914  44.658  41.301 1.00 60.28  ? 344 LYS D O      1 
ATOM   11200 C CB     . LYS D 2 326 ? 38.250  43.022  43.511 1.00 50.46  ? 344 LYS D CB     1 
ATOM   11201 C CG     . LYS D 2 326 ? 37.423  41.760  43.650 1.00 58.09  ? 344 LYS D CG     1 
ATOM   11202 C CD     . LYS D 2 326 ? 35.984  42.058  44.017 1.00 51.98  ? 344 LYS D CD     1 
ATOM   11203 C CE     . LYS D 2 326 ? 35.246  42.684  42.849 1.00 53.98  ? 344 LYS D CE     1 
ATOM   11204 N NZ     . LYS D 2 326 ? 33.810  42.903  43.169 1.00 60.07  ? 344 LYS D NZ     1 
ATOM   11205 N N      . ALA D 2 327 ? 41.007  44.596  43.220 1.00 51.83  ? 345 ALA D N      1 
ATOM   11206 C CA     . ALA D 2 327 ? 41.706  45.830  42.929 1.00 52.15  ? 345 ALA D CA     1 
ATOM   11207 C C      . ALA D 2 327 ? 42.736  45.666  41.845 1.00 56.49  ? 345 ALA D C      1 
ATOM   11208 O O      . ALA D 2 327 ? 43.041  46.613  41.146 1.00 54.55  ? 345 ALA D O      1 
ATOM   11209 C CB     . ALA D 2 327 ? 42.348  46.370  44.166 1.00 38.91  ? 345 ALA D CB     1 
ATOM   11210 N N      . GLN D 2 328 ? 43.271  44.466  41.685 1.00 55.52  ? 346 GLN D N      1 
ATOM   11211 C CA     . GLN D 2 328 ? 44.282  44.208  40.672 1.00 53.34  ? 346 GLN D CA     1 
ATOM   11212 C C      . GLN D 2 328 ? 43.680  44.358  39.327 1.00 47.43  ? 346 GLN D C      1 
ATOM   11213 O O      . GLN D 2 328 ? 44.302  44.848  38.409 1.00 41.39  ? 346 GLN D O      1 
ATOM   11214 C CB     . GLN D 2 328 ? 44.777  42.781  40.805 1.00 57.02  ? 346 GLN D CB     1 
ATOM   11215 C CG     . GLN D 2 328 ? 45.823  42.560  41.875 1.00 50.69  ? 346 GLN D CG     1 
ATOM   11216 C CD     . GLN D 2 328 ? 46.113  41.095  42.093 1.00 52.65  ? 346 GLN D CD     1 
ATOM   11217 O OE1    . GLN D 2 328 ? 45.446  40.232  41.531 1.00 55.41  ? 346 GLN D OE1    1 
ATOM   11218 N NE2    . GLN D 2 328 ? 47.106  40.808  42.911 1.00 49.79  ? 346 GLN D NE2    1 
ATOM   11219 N N      . ASP D 2 329 ? 42.440  43.957  39.200 1.00 50.60  ? 347 ASP D N      1 
ATOM   11220 C CA     . ASP D 2 329 ? 41.797  44.006  37.922 1.00 53.73  ? 347 ASP D CA     1 
ATOM   11221 C C      . ASP D 2 329 ? 41.334  45.405  37.643 1.00 53.89  ? 347 ASP D C      1 
ATOM   11222 O O      . ASP D 2 329 ? 41.252  45.812  36.502 1.00 58.34  ? 347 ASP D O      1 
ATOM   11223 C CB     . ASP D 2 329 ? 40.639  43.033  37.910 1.00 60.31  ? 347 ASP D CB     1 
ATOM   11224 C CG     . ASP D 2 329 ? 41.079  41.598  38.140 1.00 61.17  ? 347 ASP D CG     1 
ATOM   11225 O OD1    . ASP D 2 329 ? 42.296  41.329  38.160 1.00 56.53  ? 347 ASP D OD1    1 
ATOM   11226 O OD2    . ASP D 2 329 ? 40.203  40.728  38.295 1.00 52.60  ? 347 ASP D OD2    1 
ATOM   11227 N N      . TYR D 2 330 ? 41.040  46.159  38.677 1.00 51.64  ? 348 TYR D N      1 
ATOM   11228 C CA     . TYR D 2 330 ? 40.655  47.536  38.490 1.00 46.94  ? 348 TYR D CA     1 
ATOM   11229 C C      . TYR D 2 330 ? 41.762  48.238  37.823 1.00 48.01  ? 348 TYR D C      1 
ATOM   11230 O O      . TYR D 2 330 ? 41.577  48.833  36.786 1.00 53.78  ? 348 TYR D O      1 
ATOM   11231 C CB     . TYR D 2 330 ? 40.460  48.174  39.838 1.00 48.63  ? 348 TYR D CB     1 
ATOM   11232 C CG     . TYR D 2 330 ? 39.980  49.588  39.824 1.00 53.60  ? 348 TYR D CG     1 
ATOM   11233 C CD1    . TYR D 2 330 ? 38.668  49.884  39.528 1.00 49.48  ? 348 TYR D CD1    1 
ATOM   11234 C CD2    . TYR D 2 330 ? 40.829  50.630  40.153 1.00 54.20  ? 348 TYR D CD2    1 
ATOM   11235 C CE1    . TYR D 2 330 ? 38.219  51.177  39.538 1.00 47.28  ? 348 TYR D CE1    1 
ATOM   11236 C CE2    . TYR D 2 330 ? 40.386  51.932  40.161 1.00 45.96  ? 348 TYR D CE2    1 
ATOM   11237 C CZ     . TYR D 2 330 ? 39.079  52.195  39.853 1.00 46.54  ? 348 TYR D CZ     1 
ATOM   11238 O OH     . TYR D 2 330 ? 38.633  53.487  39.861 1.00 52.62  ? 348 TYR D OH     1 
ATOM   11239 N N      . VAL D 2 331 ? 42.931  48.197  38.433 1.00 43.82  ? 349 VAL D N      1 
ATOM   11240 C CA     . VAL D 2 331 ? 44.043  48.927  37.897 1.00 43.34  ? 349 VAL D CA     1 
ATOM   11241 C C      . VAL D 2 331 ? 44.339  48.360  36.558 1.00 49.23  ? 349 VAL D C      1 
ATOM   11242 O O      . VAL D 2 331 ? 44.587  49.103  35.651 1.00 51.00  ? 349 VAL D O      1 
ATOM   11243 C CB     . VAL D 2 331 ? 45.270  48.920  38.810 1.00 39.15  ? 349 VAL D CB     1 
ATOM   11244 C CG1    . VAL D 2 331 ? 45.607  47.539  39.308 1.00 49.99  ? 349 VAL D CG1    1 
ATOM   11245 C CG2    . VAL D 2 331 ? 46.462  49.547  38.123 1.00 37.83  ? 349 VAL D CG2    1 
ATOM   11246 N N      . PHE D 2 332 ? 44.216  47.057  36.376 1.00 50.45  ? 350 PHE D N      1 
ATOM   11247 C CA     . PHE D 2 332 ? 44.576  46.457  35.104 1.00 48.23  ? 350 PHE D CA     1 
ATOM   11248 C C      . PHE D 2 332 ? 43.819  47.160  34.039 1.00 46.06  ? 350 PHE D C      1 
ATOM   11249 O O      . PHE D 2 332 ? 44.397  47.717  33.130 1.00 48.97  ? 350 PHE D O      1 
ATOM   11250 C CB     . PHE D 2 332 ? 44.217  44.998  35.097 1.00 48.22  ? 350 PHE D CB     1 
ATOM   11251 C CG     . PHE D 2 332 ? 44.512  44.300  33.813 1.00 56.51  ? 350 PHE D CG     1 
ATOM   11252 C CD1    . PHE D 2 332 ? 45.808  44.165  33.373 1.00 60.41  ? 350 PHE D CD1    1 
ATOM   11253 C CD2    . PHE D 2 332 ? 43.491  43.746  33.065 1.00 62.19  ? 350 PHE D CD2    1 
ATOM   11254 C CE1    . PHE D 2 332 ? 46.080  43.511  32.194 1.00 66.76  ? 350 PHE D CE1    1 
ATOM   11255 C CE2    . PHE D 2 332 ? 43.756  43.087  31.884 1.00 60.50  ? 350 PHE D CE2    1 
ATOM   11256 C CZ     . PHE D 2 332 ? 45.054  42.970  31.448 1.00 64.64  ? 350 PHE D CZ     1 
ATOM   11257 N N      . GLY D 2 333 ? 42.512  47.153  34.155 1.00 41.87  ? 351 GLY D N      1 
ATOM   11258 C CA     . GLY D 2 333 ? 41.681  47.746  33.134 1.00 46.97  ? 351 GLY D CA     1 
ATOM   11259 C C      . GLY D 2 333 ? 41.670  49.240  33.059 1.00 50.25  ? 351 GLY D C      1 
ATOM   11260 O O      . GLY D 2 333 ? 41.581  49.803  31.990 1.00 52.56  ? 351 GLY D O      1 
ATOM   11261 N N      . LEU D 2 334 ? 41.742  49.895  34.194 1.00 43.97  ? 352 LEU D N      1 
ATOM   11262 C CA     . LEU D 2 334 ? 41.757  51.323  34.205 1.00 41.53  ? 352 LEU D CA     1 
ATOM   11263 C C      . LEU D 2 334 ? 43.011  51.723  33.497 1.00 44.56  ? 352 LEU D C      1 
ATOM   11264 O O      . LEU D 2 334 ? 43.079  52.785  32.906 1.00 50.00  ? 352 LEU D O      1 
ATOM   11265 C CB     . LEU D 2 334 ? 41.770  51.798  35.639 1.00 47.67  ? 352 LEU D CB     1 
ATOM   11266 C CG     . LEU D 2 334 ? 41.936  53.263  36.019 1.00 63.10  ? 352 LEU D CG     1 
ATOM   11267 C CD1    . LEU D 2 334 ? 40.587  53.952  35.970 1.00 57.94  ? 352 LEU D CD1    1 
ATOM   11268 C CD2    . LEU D 2 334 ? 42.526  53.360  37.418 1.00 49.62  ? 352 LEU D CD2    1 
ATOM   11269 N N      . THR D 2 335 ? 44.016  50.865  33.532 1.00 40.40  ? 353 THR D N      1 
ATOM   11270 C CA     . THR D 2 335 ? 45.281  51.209  32.916 1.00 43.84  ? 353 THR D CA     1 
ATOM   11271 C C      . THR D 2 335 ? 45.455  50.751  31.477 1.00 49.43  ? 353 THR D C      1 
ATOM   11272 O O      . THR D 2 335 ? 46.145  51.413  30.719 1.00 52.75  ? 353 THR D O      1 
ATOM   11273 C CB     . THR D 2 335 ? 46.472  50.788  33.755 1.00 41.59  ? 353 THR D CB     1 
ATOM   11274 O OG1    . THR D 2 335 ? 46.422  49.383  33.992 1.00 45.31  ? 353 THR D OG1    1 
ATOM   11275 C CG2    . THR D 2 335 ? 46.486  51.546  35.063 1.00 44.14  ? 353 THR D CG2    1 
ATOM   11276 N N      . ILE D 2 336 ? 44.851  49.646  31.058 1.00 45.33  ? 354 ILE D N      1 
ATOM   11277 C CA     . ILE D 2 336 ? 44.960  49.281  29.660 1.00 42.56  ? 354 ILE D CA     1 
ATOM   11278 C C      . ILE D 2 336 ? 44.079  50.205  28.887 1.00 48.01  ? 354 ILE D C      1 
ATOM   11279 O O      . ILE D 2 336 ? 44.344  50.493  27.738 1.00 54.13  ? 354 ILE D O      1 
ATOM   11280 C CB     . ILE D 2 336 ? 44.601  47.832  29.354 1.00 40.25  ? 354 ILE D CB     1 
ATOM   11281 C CG1    . ILE D 2 336 ? 43.263  47.458  29.969 1.00 48.42  ? 354 ILE D CG1    1 
ATOM   11282 C CG2    . ILE D 2 336 ? 45.688  46.894  29.844 1.00 40.05  ? 354 ILE D CG2    1 
ATOM   11283 C CD1    . ILE D 2 336 ? 42.952  45.987  29.863 1.00 57.84  ? 354 ILE D CD1    1 
ATOM   11284 N N      . GLN D 2 337 ? 43.044  50.723  29.524 1.00 47.95  ? 355 GLN D N      1 
ATOM   11285 C CA     . GLN D 2 337 ? 42.166  51.654  28.861 1.00 44.81  ? 355 GLN D CA     1 
ATOM   11286 C C      . GLN D 2 337 ? 42.935  52.890  28.582 1.00 49.46  ? 355 GLN D C      1 
ATOM   11287 O O      . GLN D 2 337 ? 42.813  53.457  27.529 1.00 54.78  ? 355 GLN D O      1 
ATOM   11288 C CB     . GLN D 2 337 ? 40.958  52.009  29.703 1.00 44.02  ? 355 GLN D CB     1 
ATOM   11289 C CG     . GLN D 2 337 ? 39.652  52.019  28.936 1.00 52.52  ? 355 GLN D CG     1 
ATOM   11290 C CD     . GLN D 2 337 ? 38.507  52.629  29.718 1.00 60.64  ? 355 GLN D CD     1 
ATOM   11291 O OE1    . GLN D 2 337 ? 37.396  52.762  29.207 1.00 64.48  ? 355 GLN D OE1    1 
ATOM   11292 N NE2    . GLN D 2 337 ? 38.773  53.013  30.959 1.00 60.22  ? 355 GLN D NE2    1 
ATOM   11293 N N      . SER D 2 338 ? 43.728  53.341  29.533 1.00 41.07  ? 356 SER D N      1 
ATOM   11294 C CA     . SER D 2 338 ? 44.430  54.584  29.348 1.00 40.91  ? 356 SER D CA     1 
ATOM   11295 C C      . SER D 2 338 ? 45.218  54.459  28.101 1.00 45.81  ? 356 SER D C      1 
ATOM   11296 O O      . SER D 2 338 ? 45.294  55.376  27.309 1.00 49.57  ? 356 SER D O      1 
ATOM   11297 C CB     . SER D 2 338 ? 45.364  54.844  30.492 1.00 42.68  ? 356 SER D CB     1 
ATOM   11298 O OG     . SER D 2 338 ? 45.887  56.155  30.417 1.00 54.33  ? 356 SER D OG     1 
ATOM   11299 N N      . ALA D 2 339 ? 45.768  53.289  27.880 1.00 45.63  ? 357 ALA D N      1 
ATOM   11300 C CA     . ALA D 2 339 ? 46.597  53.098  26.723 1.00 47.43  ? 357 ALA D CA     1 
ATOM   11301 C C      . ALA D 2 339 ? 45.763  53.109  25.499 1.00 51.34  ? 357 ALA D C      1 
ATOM   11302 O O      . ALA D 2 339 ? 46.180  53.653  24.493 1.00 61.50  ? 357 ALA D O      1 
ATOM   11303 C CB     . ALA D 2 339 ? 47.351  51.804  26.812 1.00 40.72  ? 357 ALA D CB     1 
ATOM   11304 N N      . MET D 2 340 ? 44.595  52.511  25.542 1.00 45.87  ? 358 MET D N      1 
ATOM   11305 C CA     . MET D 2 340 ? 43.726  52.558  24.389 1.00 49.89  ? 358 MET D CA     1 
ATOM   11306 C C      . MET D 2 340 ? 43.404  53.991  24.116 1.00 51.81  ? 358 MET D C      1 
ATOM   11307 O O      . MET D 2 340 ? 43.438  54.424  22.982 1.00 51.52  ? 358 MET D O      1 
ATOM   11308 C CB     . MET D 2 340 ? 42.456  51.778  24.686 1.00 46.09  ? 358 MET D CB     1 
ATOM   11309 C CG     . MET D 2 340 ? 41.397  51.815  23.614 1.00 50.76  ? 358 MET D CG     1 
ATOM   11310 S SD     . MET D 2 340 ? 39.950  52.731  24.147 1.00 46.54  ? 358 MET D SD     1 
ATOM   11311 C CE     . MET D 2 340 ? 39.200  51.582  25.287 1.00 46.62  ? 358 MET D CE     1 
ATOM   11312 N N      . HIS D 2 341 ? 43.170  54.753  25.154 1.00 46.65  ? 359 HIS D N      1 
ATOM   11313 C CA     . HIS D 2 341 ? 42.724  56.111  25.031 1.00 43.04  ? 359 HIS D CA     1 
ATOM   11314 C C      . HIS D 2 341 ? 43.848  56.946  24.542 1.00 48.52  ? 359 HIS D C      1 
ATOM   11315 O O      . HIS D 2 341 ? 43.659  58.103  24.237 1.00 59.22  ? 359 HIS D O      1 
ATOM   11316 C CB     . HIS D 2 341 ? 42.271  56.625  26.376 1.00 40.49  ? 359 HIS D CB     1 
ATOM   11317 C CG     . HIS D 2 341 ? 40.898  56.197  26.764 1.00 39.41  ? 359 HIS D CG     1 
ATOM   11318 N ND1    . HIS D 2 341 ? 40.105  56.941  27.607 1.00 47.15  ? 359 HIS D ND1    1 
ATOM   11319 C CD2    . HIS D 2 341 ? 40.172  55.110  26.429 1.00 40.82  ? 359 HIS D CD2    1 
ATOM   11320 C CE1    . HIS D 2 341 ? 38.949  56.328  27.775 1.00 46.88  ? 359 HIS D CE1    1 
ATOM   11321 N NE2    . HIS D 2 341 ? 38.966  55.212  27.073 1.00 44.29  ? 359 HIS D NE2    1 
ATOM   11322 N N      . HIS D 2 342 ? 45.016  56.359  24.383 1.00 43.85  ? 360 HIS D N      1 
ATOM   11323 C CA     . HIS D 2 342 ? 46.108  57.117  23.787 1.00 51.63  ? 360 HIS D CA     1 
ATOM   11324 C C      . HIS D 2 342 ? 46.397  56.666  22.385 1.00 55.94  ? 360 HIS D C      1 
ATOM   11325 O O      . HIS D 2 342 ? 46.881  57.448  21.585 1.00 57.66  ? 360 HIS D O      1 
ATOM   11326 C CB     . HIS D 2 342 ? 47.341  57.130  24.654 1.00 53.77  ? 360 HIS D CB     1 
ATOM   11327 C CG     . HIS D 2 342 ? 47.285  58.161  25.735 1.00 69.31  ? 360 HIS D CG     1 
ATOM   11328 N ND1    . HIS D 2 342 ? 46.487  58.025  26.849 1.00 75.67  ? 360 HIS D ND1    1 
ATOM   11329 C CD2    . HIS D 2 342 ? 47.902  59.358  25.858 1.00 72.27  ? 360 HIS D CD2    1 
ATOM   11330 C CE1    . HIS D 2 342 ? 46.627  59.087  27.621 1.00 74.15  ? 360 HIS D CE1    1 
ATOM   11331 N NE2    . HIS D 2 342 ? 47.480  59.911  27.042 1.00 79.77  ? 360 HIS D NE2    1 
ATOM   11332 N N      . GLU D 2 343 ? 46.096  55.424  22.054 1.00 51.85  ? 361 GLU D N      1 
ATOM   11333 C CA     . GLU D 2 343 ? 46.269  54.981  20.689 1.00 51.89  ? 361 GLU D CA     1 
ATOM   11334 C C      . GLU D 2 343 ? 45.103  55.523  19.923 1.00 58.05  ? 361 GLU D C      1 
ATOM   11335 O O      . GLU D 2 343 ? 45.229  55.868  18.763 1.00 65.99  ? 361 GLU D O      1 
ATOM   11336 C CB     . GLU D 2 343 ? 46.272  53.466  20.618 1.00 52.07  ? 361 GLU D CB     1 
ATOM   11337 C CG     . GLU D 2 343 ? 46.512  52.891  19.237 1.00 62.66  ? 361 GLU D CG     1 
ATOM   11338 C CD     . GLU D 2 343 ? 46.344  51.390  19.210 1.00 57.38  ? 361 GLU D CD     1 
ATOM   11339 O OE1    . GLU D 2 343 ? 45.783  50.844  20.175 1.00 51.23  ? 361 GLU D OE1    1 
ATOM   11340 O OE2    . GLU D 2 343 ? 46.769  50.758  18.227 1.00 53.19  ? 361 GLU D OE2    1 
ATOM   11341 N N      . LEU D 2 344 ? 43.951  55.604  20.568 1.00 53.40  ? 362 LEU D N      1 
ATOM   11342 C CA     . LEU D 2 344 ? 42.759  56.095  19.909 1.00 47.04  ? 362 LEU D CA     1 
ATOM   11343 C C      . LEU D 2 344 ? 43.055  57.464  19.486 1.00 52.69  ? 362 LEU D C      1 
ATOM   11344 O O      . LEU D 2 344 ? 42.658  57.888  18.424 1.00 66.46  ? 362 LEU D O      1 
ATOM   11345 C CB     . LEU D 2 344 ? 41.593  56.141  20.890 1.00 44.22  ? 362 LEU D CB     1 
ATOM   11346 C CG     . LEU D 2 344 ? 40.257  56.807  20.596 1.00 35.87  ? 362 LEU D CG     1 
ATOM   11347 C CD1    . LEU D 2 344 ? 39.359  55.834  19.860 1.00 33.44  ? 362 LEU D CD1    1 
ATOM   11348 C CD2    . LEU D 2 344 ? 39.631  57.181  21.923 1.00 51.34  ? 362 LEU D CD2    1 
ATOM   11349 N N      . GLN D 2 345 ? 43.758  58.188  20.315 1.00 51.42  ? 363 GLN D N      1 
ATOM   11350 C CA     . GLN D 2 345 ? 43.994  59.565  20.009 1.00 60.45  ? 363 GLN D CA     1 
ATOM   11351 C C      . GLN D 2 345 ? 45.232  59.817  19.206 1.00 67.11  ? 363 GLN D C      1 
ATOM   11352 O O      . GLN D 2 345 ? 45.466  60.932  18.799 1.00 78.77  ? 363 GLN D O      1 
ATOM   11353 C CB     . GLN D 2 345 ? 43.987  60.388  21.280 1.00 63.01  ? 363 GLN D CB     1 
ATOM   11354 C CG     . GLN D 2 345 ? 42.604  60.518  21.900 1.00 63.38  ? 363 GLN D CG     1 
ATOM   11355 C CD     . GLN D 2 345 ? 42.560  61.468  23.082 1.00 71.02  ? 363 GLN D CD     1 
ATOM   11356 O OE1    . GLN D 2 345 ? 43.132  61.196  24.135 1.00 68.21  ? 363 GLN D OE1    1 
ATOM   11357 N NE2    . GLN D 2 345 ? 41.865  62.585  22.915 1.00 62.81  ? 363 GLN D NE2    1 
ATOM   11358 N N      . GLU D 2 346 ? 46.032  58.804  18.937 1.00 59.39  ? 364 GLU D N      1 
ATOM   11359 C CA     . GLU D 2 346 ? 47.164  59.012  18.060 1.00 61.45  ? 364 GLU D CA     1 
ATOM   11360 C C      . GLU D 2 346 ? 46.678  58.593  16.715 1.00 64.10  ? 364 GLU D C      1 
ATOM   11361 O O      . GLU D 2 346 ? 47.419  58.604  15.756 1.00 68.55  ? 364 GLU D O      1 
ATOM   11362 C CB     . GLU D 2 346 ? 48.352  58.177  18.466 1.00 67.82  ? 364 GLU D CB     1 
ATOM   11363 C CG     . GLU D 2 346 ? 49.684  58.710  17.955 1.00 77.08  ? 364 GLU D CG     1 
ATOM   11364 C CD     . GLU D 2 346 ? 50.879  57.910  18.440 1.00 84.73  ? 364 GLU D CD     1 
ATOM   11365 O OE1    . GLU D 2 346 ? 50.736  57.138  19.409 1.00 83.73  ? 364 GLU D OE1    1 
ATOM   11366 O OE2    . GLU D 2 346 ? 51.971  58.062  17.855 1.00 78.79  ? 364 GLU D OE2    1 
ATOM   11367 N N      . ARG D 2 347 ? 45.428  58.169  16.636 1.00 59.67  ? 365 ARG D N      1 
ATOM   11368 C CA     . ARG D 2 347 ? 44.856  57.839  15.354 1.00 55.22  ? 365 ARG D CA     1 
ATOM   11369 C C      . ARG D 2 347 ? 43.862  58.878  14.941 1.00 59.88  ? 365 ARG D C      1 
ATOM   11370 O O      . ARG D 2 347 ? 43.322  58.816  13.854 1.00 64.65  ? 365 ARG D O      1 
ATOM   11371 C CB     . ARG D 2 347 ? 44.215  56.468  15.391 1.00 55.65  ? 365 ARG D CB     1 
ATOM   11372 C CG     . ARG D 2 347 ? 45.223  55.343  15.548 1.00 66.01  ? 365 ARG D CG     1 
ATOM   11373 C CD     . ARG D 2 347 ? 44.607  53.977  15.307 1.00 68.36  ? 365 ARG D CD     1 
ATOM   11374 N NE     . ARG D 2 347 ? 45.603  52.916  15.421 1.00 71.80  ? 365 ARG D NE     1 
ATOM   11375 C CZ     . ARG D 2 347 ? 45.367  51.636  15.152 1.00 75.89  ? 365 ARG D CZ     1 
ATOM   11376 N NH1    . ARG D 2 347 ? 44.166  51.250  14.746 1.00 72.13  ? 365 ARG D NH1    1 
ATOM   11377 N NH2    . ARG D 2 347 ? 46.334  50.740  15.283 1.00 73.20  ? 365 ARG D NH2    1 
ATOM   11378 N N      . PHE D 2 348 ? 43.620  59.852  15.791 1.00 59.56  ? 366 PHE D N      1 
ATOM   11379 C CA     . PHE D 2 348 ? 42.747  60.931  15.396 1.00 64.50  ? 366 PHE D CA     1 
ATOM   11380 C C      . PHE D 2 348 ? 43.556  62.174  15.266 1.00 64.50  ? 366 PHE D C      1 
ATOM   11381 O O      . PHE D 2 348 ? 43.061  63.191  14.810 1.00 61.64  ? 366 PHE D O      1 
ATOM   11382 C CB     . PHE D 2 348 ? 41.607  61.107  16.364 1.00 61.32  ? 366 PHE D CB     1 
ATOM   11383 C CG     . PHE D 2 348 ? 40.413  60.315  15.985 1.00 69.41  ? 366 PHE D CG     1 
ATOM   11384 C CD1    . PHE D 2 348 ? 39.653  60.694  14.896 1.00 72.38  ? 366 PHE D CD1    1 
ATOM   11385 C CD2    . PHE D 2 348 ? 40.088  59.165  16.665 1.00 69.46  ? 366 PHE D CD2    1 
ATOM   11386 C CE1    . PHE D 2 348 ? 38.568  59.955  14.507 1.00 72.31  ? 366 PHE D CE1    1 
ATOM   11387 C CE2    . PHE D 2 348 ? 39.001  58.420  16.288 1.00 62.42  ? 366 PHE D CE2    1 
ATOM   11388 C CZ     . PHE D 2 348 ? 38.244  58.813  15.203 1.00 63.20  ? 366 PHE D CZ     1 
ATOM   11389 N N      . LYS D 2 349 ? 44.807  62.103  15.684 1.00 70.65  ? 367 LYS D N      1 
ATOM   11390 C CA     . LYS D 2 349 ? 45.695  63.228  15.482 1.00 69.63  ? 367 LYS D CA     1 
ATOM   11391 C C      . LYS D 2 349 ? 46.535  62.866  14.284 1.00 71.77  ? 367 LYS D C      1 
ATOM   11392 O O      . LYS D 2 349 ? 47.342  63.664  13.825 1.00 73.97  ? 367 LYS D O      1 
ATOM   11393 C CB     . LYS D 2 349 ? 46.587  63.445  16.696 1.00 61.23  ? 367 LYS D CB     1 
ATOM   11394 C CG     . LYS D 2 349 ? 45.836  63.862  17.947 1.00 76.85  ? 367 LYS D CG     1 
ATOM   11395 C CD     . LYS D 2 349 ? 44.753  64.882  17.647 1.00 91.63  ? 367 LYS D CD     1 
ATOM   11396 C CE     . LYS D 2 349 ? 43.669  64.847  18.710 1.00 102.73 ? 367 LYS D CE     1 
ATOM   11397 N NZ     . LYS D 2 349 ? 43.028  63.507  18.802 1.00 100.23 ? 367 LYS D NZ     1 
ATOM   11398 N N      . ASN D 2 350 ? 46.354  61.659  13.773 1.00 75.25  ? 368 ASN D N      1 
ATOM   11399 C CA     . ASN D 2 350 ? 47.096  61.206  12.609 1.00 75.46  ? 368 ASN D CA     1 
ATOM   11400 C C      . ASN D 2 350 ? 46.210  61.312  11.394 1.00 83.39  ? 368 ASN D C      1 
ATOM   11401 O O      . ASN D 2 350 ? 46.527  60.776  10.340 1.00 78.49  ? 368 ASN D O      1 
ATOM   11402 C CB     . ASN D 2 350 ? 47.577  59.782  12.796 1.00 66.31  ? 368 ASN D CB     1 
ATOM   11403 C CG     . ASN D 2 350 ? 48.989  59.716  13.330 1.00 74.57  ? 368 ASN D CG     1 
ATOM   11404 O OD1    . ASN D 2 350 ? 49.532  58.637  13.547 1.00 71.77  ? 368 ASN D OD1    1 
ATOM   11405 N ND2    . ASN D 2 350 ? 49.595  60.876  13.545 1.00 79.43  ? 368 ASN D ND2    1 
ATOM   11406 N N      . LYS D 2 351 ? 45.072  61.972  11.549 1.00 88.21  ? 369 LYS D N      1 
ATOM   11407 C CA     . LYS D 2 351 ? 44.145  62.157  10.442 1.00 83.43  ? 369 LYS D CA     1 
ATOM   11408 C C      . LYS D 2 351 ? 44.070  63.640  10.090 1.00 93.88  ? 369 LYS D C      1 
ATOM   11409 O O      . LYS D 2 351 ? 44.288  64.477  10.968 1.00 88.47  ? 369 LYS D O      1 
ATOM   11410 C CB     . LYS D 2 351 ? 42.768  61.615  10.828 1.00 78.15  ? 369 LYS D CB     1 
ATOM   11411 C CG     . LYS D 2 351 ? 41.750  61.594  9.701  1.00 84.02  ? 369 LYS D CG     1 
ATOM   11412 C CD     . LYS D 2 351 ? 42.296  60.886  8.470  1.00 83.00  ? 369 LYS D CD     1 
ATOM   11413 C CE     . LYS D 2 351 ? 41.420  61.151  7.257  1.00 80.12  ? 369 LYS D CE     1 
ATOM   11414 N NZ     . LYS D 2 351 ? 42.050  60.680  5.995  1.00 49.34  ? 369 LYS D NZ     1 
ATOM   11415 N N      . GLU D 2 352 ? 43.802  63.970  8.823  1.00 97.57  ? 370 GLU D N      1 
ATOM   11416 C CA     . GLU D 2 352 ? 43.702  65.345  8.355  1.00 88.75  ? 370 GLU D CA     1 
ATOM   11417 C C      . GLU D 2 352 ? 45.026  66.046  8.593  1.00 84.23  ? 370 GLU D C      1 
ATOM   11418 O O      . GLU D 2 352 ? 46.082  65.418  8.546  1.00 75.58  ? 370 GLU D O      1 
ATOM   11419 C CB     . GLU D 2 352 ? 42.569  66.084  9.054  1.00 97.99  ? 370 GLU D CB     1 
ATOM   11420 C CG     . GLU D 2 352 ? 42.527  67.578  8.761  1.00 94.64  ? 370 GLU D CG     1 
ATOM   11421 C CD     . GLU D 2 352 ? 41.408  68.297  9.491  1.00 85.76  ? 370 GLU D CD     1 
ATOM   11422 O OE1    . GLU D 2 352 ? 40.676  67.643  10.261 1.00 88.20  ? 370 GLU D OE1    1 
ATOM   11423 O OE2    . GLU D 2 352 ? 41.257  69.520  9.294  1.00 80.34  ? 370 GLU D OE2    1 
ATOM   11424 N N      . MET E 3 1   ? 7.192   85.195  67.221 1.00 66.60  ? 1   MET E N      1 
ATOM   11425 C CA     . MET E 3 1   ? 7.645   83.877  67.664 1.00 79.85  ? 1   MET E CA     1 
ATOM   11426 C C      . MET E 3 1   ? 9.055   83.916  68.198 1.00 83.39  ? 1   MET E C      1 
ATOM   11427 O O      . MET E 3 1   ? 9.997   83.871  67.420 1.00 80.43  ? 1   MET E O      1 
ATOM   11428 C CB     . MET E 3 1   ? 7.598   82.878  66.509 1.00 81.52  ? 1   MET E CB     1 
ATOM   11429 C CG     . MET E 3 1   ? 7.988   81.457  66.868 1.00 82.85  ? 1   MET E CG     1 
ATOM   11430 S SD     . MET E 3 1   ? 7.630   80.344  65.504 1.00 88.38  ? 1   MET E SD     1 
ATOM   11431 C CE     . MET E 3 1   ? 5.843   80.407  65.509 1.00 79.94  ? 1   MET E CE     1 
ATOM   11432 N N      . GLN E 3 2   ? 9.225   83.997  69.512 1.00 79.79  ? 2   GLN E N      1 
ATOM   11433 C CA     . GLN E 3 2   ? 10.582  84.117  69.991 1.00 76.32  ? 2   GLN E CA     1 
ATOM   11434 C C      . GLN E 3 2   ? 11.224  82.822  70.437 1.00 87.13  ? 2   GLN E C      1 
ATOM   11435 O O      . GLN E 3 2   ? 10.952  82.325  71.527 1.00 83.61  ? 2   GLN E O      1 
ATOM   11436 C CB     . GLN E 3 2   ? 10.764  85.255  71.012 1.00 63.84  ? 2   GLN E CB     1 
ATOM   11437 C CG     . GLN E 3 2   ? 9.953   85.216  72.293 1.00 69.41  ? 2   GLN E CG     1 
ATOM   11438 C CD     . GLN E 3 2   ? 10.399  86.292  73.266 1.00 56.12  ? 2   GLN E CD     1 
ATOM   11439 O OE1    . GLN E 3 2   ? 11.173  87.170  72.912 1.00 48.02  ? 2   GLN E OE1    1 
ATOM   11440 N NE2    . GLN E 3 2   ? 9.913   86.225  74.494 1.00 56.69  ? 2   GLN E NE2    1 
ATOM   11441 N N      . ILE E 3 3   ? 12.096  82.271  69.596 1.00 88.36  ? 3   ILE E N      1 
ATOM   11442 C CA     . ILE E 3 3   ? 12.834  81.078  69.956 1.00 77.59  ? 3   ILE E CA     1 
ATOM   11443 C C      . ILE E 3 3   ? 14.002  81.517  70.816 1.00 77.00  ? 3   ILE E C      1 
ATOM   11444 O O      . ILE E 3 3   ? 14.395  82.669  70.754 1.00 84.59  ? 3   ILE E O      1 
ATOM   11445 C CB     . ILE E 3 3   ? 13.299  80.340  68.704 1.00 63.71  ? 3   ILE E CB     1 
ATOM   11446 C CG1    . ILE E 3 3   ? 14.295  81.180  67.920 1.00 72.17  ? 3   ILE E CG1    1 
ATOM   11447 C CG2    . ILE E 3 3   ? 12.107  79.994  67.835 1.00 63.87  ? 3   ILE E CG2    1 
ATOM   11448 C CD1    . ILE E 3 3   ? 14.835  80.475  66.700 1.00 76.63  ? 3   ILE E CD1    1 
ATOM   11449 N N      . PHE E 3 4   ? 14.535  80.644  71.652 1.00 66.90  ? 4   PHE E N      1 
ATOM   11450 C CA     . PHE E 3 4   ? 15.697  80.988  72.429 1.00 62.88  ? 4   PHE E CA     1 
ATOM   11451 C C      . PHE E 3 4   ? 16.751  80.025  71.959 1.00 63.69  ? 4   PHE E C      1 
ATOM   11452 O O      . PHE E 3 4   ? 16.477  78.858  71.866 1.00 69.31  ? 4   PHE E O      1 
ATOM   11453 C CB     . PHE E 3 4   ? 15.441  80.740  73.885 1.00 67.96  ? 4   PHE E CB     1 
ATOM   11454 C CG     . PHE E 3 4   ? 14.357  81.577  74.481 1.00 71.69  ? 4   PHE E CG     1 
ATOM   11455 C CD1    . PHE E 3 4   ? 13.027  81.274  74.270 1.00 74.10  ? 4   PHE E CD1    1 
ATOM   11456 C CD2    . PHE E 3 4   ? 14.672  82.631  75.312 1.00 78.55  ? 4   PHE E CD2    1 
ATOM   11457 C CE1    . PHE E 3 4   ? 12.032  82.035  74.842 1.00 79.02  ? 4   PHE E CE1    1 
ATOM   11458 C CE2    . PHE E 3 4   ? 13.682  83.396  75.892 1.00 82.44  ? 4   PHE E CE2    1 
ATOM   11459 C CZ     . PHE E 3 4   ? 12.357  83.097  75.657 1.00 81.93  ? 4   PHE E CZ     1 
ATOM   11460 N N      . VAL E 3 5   ? 17.947  80.490  71.632 1.00 62.94  ? 5   VAL E N      1 
ATOM   11461 C CA     . VAL E 3 5   ? 19.036  79.611  71.218 1.00 62.45  ? 5   VAL E CA     1 
ATOM   11462 C C      . VAL E 3 5   ? 20.096  79.563  72.292 1.00 66.03  ? 5   VAL E C      1 
ATOM   11463 O O      . VAL E 3 5   ? 20.598  80.596  72.689 1.00 65.94  ? 5   VAL E O      1 
ATOM   11464 C CB     . VAL E 3 5   ? 19.658  80.089  69.923 1.00 58.52  ? 5   VAL E CB     1 
ATOM   11465 C CG1    . VAL E 3 5   ? 20.800  79.187  69.513 1.00 52.24  ? 5   VAL E CG1    1 
ATOM   11466 C CG2    . VAL E 3 5   ? 18.605  80.159  68.834 1.00 55.72  ? 5   VAL E CG2    1 
ATOM   11467 N N      . LYS E 3 6   ? 20.451  78.381  72.775 1.00 63.02  ? 6   LYS E N      1 
ATOM   11468 C CA     . LYS E 3 6   ? 21.371  78.292  73.890 1.00 58.23  ? 6   LYS E CA     1 
ATOM   11469 C C      . LYS E 3 6   ? 22.772  77.863  73.539 1.00 53.94  ? 6   LYS E C      1 
ATOM   11470 O O      . LYS E 3 6   ? 22.976  76.832  72.924 1.00 57.09  ? 6   LYS E O      1 
ATOM   11471 C CB     . LYS E 3 6   ? 20.797  77.331  74.911 1.00 60.64  ? 6   LYS E CB     1 
ATOM   11472 C CG     . LYS E 3 6   ? 19.316  77.505  75.176 1.00 64.42  ? 6   LYS E CG     1 
ATOM   11473 C CD     . LYS E 3 6   ? 19.073  78.474  76.316 1.00 72.60  ? 6   LYS E CD     1 
ATOM   11474 C CE     . LYS E 3 6   ? 19.612  77.921  77.623 1.00 67.22  ? 6   LYS E CE     1 
ATOM   11475 N NZ     . LYS E 3 6   ? 19.468  78.904  78.733 1.00 62.02  ? 6   LYS E NZ     1 
ATOM   11476 N N      . THR E 3 7   ? 23.749  78.652  73.943 1.00 54.49  ? 7   THR E N      1 
ATOM   11477 C CA     . THR E 3 7   ? 25.124  78.317  73.683 1.00 58.47  ? 7   THR E CA     1 
ATOM   11478 C C      . THR E 3 7   ? 25.574  77.329  74.699 1.00 58.42  ? 7   THR E C      1 
ATOM   11479 O O      . THR E 3 7   ? 24.823  76.943  75.581 1.00 62.36  ? 7   THR E O      1 
ATOM   11480 C CB     . THR E 3 7   ? 26.029  79.531  73.824 1.00 64.64  ? 7   THR E CB     1 
ATOM   11481 O OG1    . THR E 3 7   ? 25.869  80.095  75.129 1.00 61.57  ? 7   THR E OG1    1 
ATOM   11482 C CG2    . THR E 3 7   ? 25.680  80.571  72.788 1.00 66.31  ? 7   THR E CG2    1 
ATOM   11483 N N      . LEU E 3 8   ? 26.831  76.938  74.610 1.00 54.30  ? 8   LEU E N      1 
ATOM   11484 C CA     . LEU E 3 8   ? 27.340  75.952  75.530 1.00 59.20  ? 8   LEU E CA     1 
ATOM   11485 C C      . LEU E 3 8   ? 27.512  76.575  76.915 1.00 65.27  ? 8   LEU E C      1 
ATOM   11486 O O      . LEU E 3 8   ? 27.327  75.902  77.919 1.00 62.44  ? 8   LEU E O      1 
ATOM   11487 C CB     . LEU E 3 8   ? 28.635  75.341  74.994 1.00 50.13  ? 8   LEU E CB     1 
ATOM   11488 C CG     . LEU E 3 8   ? 28.600  74.718  73.603 1.00 41.95  ? 8   LEU E CG     1 
ATOM   11489 C CD1    . LEU E 3 8   ? 29.976  74.184  73.247 1.00 34.30  ? 8   LEU E CD1    1 
ATOM   11490 C CD2    . LEU E 3 8   ? 27.570  73.605  73.555 1.00 53.39  ? 8   LEU E CD2    1 
ATOM   11491 N N      . THR E 3 9   ? 27.806  77.869  76.977 1.00 59.51  ? 9   THR E N      1 
ATOM   11492 C CA     . THR E 3 9   ? 28.012  78.547  78.242 1.00 50.71  ? 9   THR E CA     1 
ATOM   11493 C C      . THR E 3 9   ? 26.690  78.774  78.857 1.00 56.51  ? 9   THR E C      1 
ATOM   11494 O O      . THR E 3 9   ? 26.581  79.410  79.892 1.00 59.94  ? 9   THR E O      1 
ATOM   11495 C CB     . THR E 3 9   ? 28.622  79.920  78.024 1.00 59.80  ? 9   THR E CB     1 
ATOM   11496 O OG1    . THR E 3 9   ? 27.683  80.752  77.340 1.00 60.96  ? 9   THR E OG1    1 
ATOM   11497 C CG2    . THR E 3 9   ? 29.883  79.801  77.194 1.00 60.96  ? 9   THR E CG2    1 
ATOM   11498 N N      . GLY E 3 10  ? 25.654  78.287  78.210 1.00 60.87  ? 10  GLY E N      1 
ATOM   11499 C CA     . GLY E 3 10  ? 24.321  78.401  78.764 1.00 60.22  ? 10  GLY E CA     1 
ATOM   11500 C C      . GLY E 3 10  ? 23.540  79.626  78.376 1.00 63.39  ? 10  GLY E C      1 
ATOM   11501 O O      . GLY E 3 10  ? 22.347  79.694  78.628 1.00 66.24  ? 10  GLY E O      1 
ATOM   11502 N N      . LYS E 3 11  ? 24.190  80.603  77.780 1.00 61.47  ? 11  LYS E N      1 
ATOM   11503 C CA     . LYS E 3 11  ? 23.493  81.830  77.480 1.00 68.10  ? 11  LYS E CA     1 
ATOM   11504 C C      . LYS E 3 11  ? 22.514  81.691  76.346 1.00 75.50  ? 11  LYS E C      1 
ATOM   11505 O O      . LYS E 3 11  ? 22.690  80.850  75.485 1.00 75.79  ? 11  LYS E O      1 
ATOM   11506 C CB     . LYS E 3 11  ? 24.479  82.946  77.197 1.00 74.28  ? 11  LYS E CB     1 
ATOM   11507 C CG     . LYS E 3 11  ? 25.254  83.385  78.425 1.00 71.50  ? 11  LYS E CG     1 
ATOM   11508 C CD     . LYS E 3 11  ? 26.173  84.551  78.112 1.00 68.03  ? 11  LYS E CD     1 
ATOM   11509 C CE     . LYS E 3 11  ? 27.065  84.870  79.299 1.00 74.90  ? 11  LYS E CE     1 
ATOM   11510 N NZ     . LYS E 3 11  ? 28.037  85.946  78.971 1.00 78.92  ? 11  LYS E NZ     1 
ATOM   11511 N N      . THR E 3 12  ? 21.464  82.507  76.362 1.00 76.74  ? 12  THR E N      1 
ATOM   11512 C CA     . THR E 3 12  ? 20.431  82.413  75.337 1.00 71.14  ? 12  THR E CA     1 
ATOM   11513 C C      . THR E 3 12  ? 20.328  83.639  74.451 1.00 65.17  ? 12  THR E C      1 
ATOM   11514 O O      . THR E 3 12  ? 20.264  84.765  74.945 1.00 69.86  ? 12  THR E O      1 
ATOM   11515 C CB     . THR E 3 12  ? 19.045  82.137  75.950 1.00 74.49  ? 12  THR E CB     1 
ATOM   11516 O OG1    . THR E 3 12  ? 18.115  81.847  74.901 1.00 74.89  ? 12  THR E OG1    1 
ATOM   11517 C CG2    . THR E 3 12  ? 18.552  83.344  76.732 1.00 76.62  ? 12  THR E CG2    1 
ATOM   11518 N N      . ILE E 3 13  ? 20.318  83.431  73.139 1.00 58.68  ? 13  ILE E N      1 
ATOM   11519 C CA     . ILE E 3 13  ? 20.154  84.530  72.231 1.00 60.00  ? 13  ILE E CA     1 
ATOM   11520 C C      . ILE E 3 13  ? 18.725  84.417  71.800 1.00 63.59  ? 13  ILE E C      1 
ATOM   11521 O O      . ILE E 3 13  ? 18.397  83.557  71.005 1.00 66.39  ? 13  ILE E O      1 
ATOM   11522 C CB     . ILE E 3 13  ? 21.048  84.310  71.020 1.00 57.46  ? 13  ILE E CB     1 
ATOM   11523 C CG1    . ILE E 3 13  ? 22.435  83.855  71.463 1.00 60.21  ? 13  ILE E CG1    1 
ATOM   11524 C CG2    . ILE E 3 13  ? 21.148  85.562  70.182 1.00 66.65  ? 13  ILE E CG2    1 
ATOM   11525 C CD1    . ILE E 3 13  ? 23.291  83.355  70.326 1.00 66.01  ? 13  ILE E CD1    1 
ATOM   11526 N N      . THR E 3 14  ? 17.865  85.296  72.283 1.00 64.73  ? 14  THR E N      1 
ATOM   11527 C CA     . THR E 3 14  ? 16.452  85.186  71.981 1.00 60.43  ? 14  THR E CA     1 
ATOM   11528 C C      . THR E 3 14  ? 16.209  85.761  70.625 1.00 62.50  ? 14  THR E C      1 
ATOM   11529 O O      . THR E 3 14  ? 16.471  86.932  70.395 1.00 66.94  ? 14  THR E O      1 
ATOM   11530 C CB     . THR E 3 14  ? 15.608  85.934  73.002 1.00 61.49  ? 14  THR E CB     1 
ATOM   11531 O OG1    . THR E 3 14  ? 15.997  85.549  74.324 1.00 64.61  ? 14  THR E OG1    1 
ATOM   11532 C CG2    . THR E 3 14  ? 14.145  85.632  72.798 1.00 61.36  ? 14  THR E CG2    1 
ATOM   11533 N N      . LEU E 3 15  ? 15.716  84.948  69.710 1.00 57.98  ? 15  LEU E N      1 
ATOM   11534 C CA     . LEU E 3 15  ? 15.549  85.410  68.354 1.00 67.20  ? 15  LEU E CA     1 
ATOM   11535 C C      . LEU E 3 15  ? 14.091  85.398  68.030 1.00 75.66  ? 15  LEU E C      1 
ATOM   11536 O O      . LEU E 3 15  ? 13.337  84.671  68.648 1.00 73.66  ? 15  LEU E O      1 
ATOM   11537 C CB     . LEU E 3 15  ? 16.272  84.503  67.376 1.00 60.98  ? 15  LEU E CB     1 
ATOM   11538 C CG     . LEU E 3 15  ? 17.757  84.639  67.108 1.00 62.88  ? 15  LEU E CG     1 
ATOM   11539 C CD1    . LEU E 3 15  ? 17.943  84.008  65.745 1.00 56.42  ? 15  LEU E CD1    1 
ATOM   11540 C CD2    . LEU E 3 15  ? 18.142  86.106  67.056 1.00 71.48  ? 15  LEU E CD2    1 
ATOM   11541 N N      . GLU E 3 16  ? 13.686  86.203  67.056 1.00 76.68  ? 16  GLU E N      1 
ATOM   11542 C CA     . GLU E 3 16  ? 12.290  86.282  66.666 1.00 71.41  ? 16  GLU E CA     1 
ATOM   11543 C C      . GLU E 3 16  ? 12.176  85.841  65.241 1.00 66.07  ? 16  GLU E C      1 
ATOM   11544 O O      . GLU E 3 16  ? 12.670  86.501  64.339 1.00 60.27  ? 16  GLU E O      1 
ATOM   11545 C CB     . GLU E 3 16  ? 11.750  87.692  66.857 1.00 68.75  ? 16  GLU E CB     1 
ATOM   11546 C CG     . GLU E 3 16  ? 11.455  88.041  68.300 1.00 66.24  ? 16  GLU E CG     1 
ATOM   11547 C CD     . GLU E 3 16  ? 10.983  89.464  68.454 1.00 74.41  ? 16  GLU E CD     1 
ATOM   11548 O OE1    . GLU E 3 16  ? 11.169  90.254  67.507 1.00 71.62  ? 16  GLU E OE1    1 
ATOM   11549 O OE2    . GLU E 3 16  ? 10.433  89.794  69.522 1.00 85.25  ? 16  GLU E OE2    1 
ATOM   11550 N N      . VAL E 3 17  ? 11.518  84.715  65.027 1.00 71.17  ? 17  VAL E N      1 
ATOM   11551 C CA     . VAL E 3 17  ? 11.410  84.180  63.698 1.00 77.20  ? 17  VAL E CA     1 
ATOM   11552 C C      . VAL E 3 17  ? 9.982   84.001  63.339 1.00 80.29  ? 17  VAL E C      1 
ATOM   11553 O O      . VAL E 3 17  ? 9.110   84.143  64.178 1.00 78.77  ? 17  VAL E O      1 
ATOM   11554 C CB     . VAL E 3 17  ? 12.010  82.777  63.621 1.00 82.79  ? 17  VAL E CB     1 
ATOM   11555 C CG1    . VAL E 3 17  ? 13.500  82.805  63.907 1.00 84.20  ? 17  VAL E CG1    1 
ATOM   11556 C CG2    . VAL E 3 17  ? 11.312  81.846  64.593 1.00 84.63  ? 17  VAL E CG2    1 
ATOM   11557 N N      . GLU E 3 18  ? 9.728   83.617  62.099 1.00 89.66  ? 18  GLU E N      1 
ATOM   11558 C CA     . GLU E 3 18  ? 8.374   83.281  61.693 1.00 92.30  ? 18  GLU E CA     1 
ATOM   11559 C C      . GLU E 3 18  ? 8.576   81.852  61.224 1.00 89.87  ? 18  GLU E C      1 
ATOM   11560 O O      . GLU E 3 18  ? 9.680   81.491  60.845 1.00 86.30  ? 18  GLU E O      1 
ATOM   11561 C CB     . GLU E 3 18  ? 7.877   84.221  60.607 1.00 90.33  ? 18  GLU E CB     1 
ATOM   11562 C CG     . GLU E 3 18  ? 7.725   85.659  61.076 1.00 77.38  ? 18  GLU E CG     1 
ATOM   11563 C CD     . GLU E 3 18  ? 6.817   85.785  62.285 1.00 89.58  ? 18  GLU E CD     1 
ATOM   11564 O OE1    . GLU E 3 18  ? 5.754   85.132  62.312 1.00 93.57  ? 18  GLU E OE1    1 
ATOM   11565 O OE2    . GLU E 3 18  ? 7.158   86.553  63.210 1.00 93.55  ? 18  GLU E OE2    1 
ATOM   11566 N N      . PRO E 3 19  ? 7.515   80.998  61.250 1.00 86.22  ? 19  PRO E N      1 
ATOM   11567 C CA     . PRO E 3 19  ? 7.783   79.585  60.939 1.00 77.77  ? 19  PRO E CA     1 
ATOM   11568 C C      . PRO E 3 19  ? 8.324   79.283  59.582 1.00 79.33  ? 19  PRO E C      1 
ATOM   11569 O O      . PRO E 3 19  ? 8.965   78.264  59.389 1.00 77.52  ? 19  PRO E O      1 
ATOM   11570 C CB     . PRO E 3 19  ? 6.414   78.939  61.044 1.00 73.14  ? 19  PRO E CB     1 
ATOM   11571 C CG     . PRO E 3 19  ? 5.621   79.836  61.912 1.00 83.63  ? 19  PRO E CG     1 
ATOM   11572 C CD     . PRO E 3 19  ? 6.067   81.195  61.494 1.00 91.65  ? 19  PRO E CD     1 
ATOM   11573 N N      . SER E 3 20  ? 8.019   80.127  58.627 1.00 83.83  ? 20  SER E N      1 
ATOM   11574 C CA     . SER E 3 20  ? 8.411   79.836  57.272 1.00 82.49  ? 20  SER E CA     1 
ATOM   11575 C C      . SER E 3 20  ? 9.873   79.976  57.139 1.00 84.06  ? 20  SER E C      1 
ATOM   11576 O O      . SER E 3 20  ? 10.433  79.654  56.103 1.00 84.02  ? 20  SER E O      1 
ATOM   11577 C CB     . SER E 3 20  ? 7.762   80.840  56.335 1.00 77.15  ? 20  SER E CB     1 
ATOM   11578 O OG     . SER E 3 20  ? 8.279   82.138  56.560 1.00 73.93  ? 20  SER E OG     1 
ATOM   11579 N N      . ASP E 3 21  ? 10.520  80.435  58.194 1.00 83.98  ? 21  ASP E N      1 
ATOM   11580 C CA     . ASP E 3 21  ? 11.941  80.710  58.082 1.00 84.29  ? 21  ASP E CA     1 
ATOM   11581 C C      . ASP E 3 21  ? 12.810  79.507  57.873 1.00 77.66  ? 21  ASP E C      1 
ATOM   11582 O O      . ASP E 3 21  ? 12.893  78.628  58.715 1.00 73.81  ? 21  ASP E O      1 
ATOM   11583 C CB     . ASP E 3 21  ? 12.433  81.588  59.234 1.00 84.80  ? 21  ASP E CB     1 
ATOM   11584 C CG     . ASP E 3 21  ? 12.180  83.052  58.992 1.00 80.95  ? 21  ASP E CG     1 
ATOM   11585 O OD1    . ASP E 3 21  ? 12.508  83.537  57.891 1.00 77.79  ? 21  ASP E OD1    1 
ATOM   11586 O OD2    . ASP E 3 21  ? 11.664  83.723  59.904 1.00 87.12  ? 21  ASP E OD2    1 
ATOM   11587 N N      . THR E 3 22  ? 13.468  79.474  56.734 1.00 76.35  ? 22  THR E N      1 
ATOM   11588 C CA     . THR E 3 22  ? 14.376  78.402  56.449 1.00 73.88  ? 22  THR E CA     1 
ATOM   11589 C C      . THR E 3 22  ? 15.440  78.477  57.509 1.00 72.74  ? 22  THR E C      1 
ATOM   11590 O O      . THR E 3 22  ? 15.744  79.542  58.011 1.00 76.19  ? 22  THR E O      1 
ATOM   11591 C CB     . THR E 3 22  ? 14.993  78.645  55.068 1.00 73.36  ? 22  THR E CB     1 
ATOM   11592 O OG1    . THR E 3 22  ? 13.946  78.807  54.106 1.00 85.73  ? 22  THR E OG1    1 
ATOM   11593 C CG2    . THR E 3 22  ? 15.878  77.511  54.637 1.00 70.39  ? 22  THR E CG2    1 
ATOM   11594 N N      . ILE E 3 23  ? 16.019  77.346  57.867 1.00 73.24  ? 23  ILE E N      1 
ATOM   11595 C CA     . ILE E 3 23  ? 17.054  77.315  58.878 1.00 69.83  ? 23  ILE E CA     1 
ATOM   11596 C C      . ILE E 3 23  ? 18.217  78.155  58.417 1.00 67.86  ? 23  ILE E C      1 
ATOM   11597 O O      . ILE E 3 23  ? 18.899  78.765  59.216 1.00 70.02  ? 23  ILE E O      1 
ATOM   11598 C CB     . ILE E 3 23  ? 17.469  75.868  59.173 1.00 65.61  ? 23  ILE E CB     1 
ATOM   11599 C CG1    . ILE E 3 23  ? 16.464  75.220  60.115 1.00 64.64  ? 23  ILE E CG1    1 
ATOM   11600 C CG2    . ILE E 3 23  ? 18.840  75.793  59.825 1.00 70.54  ? 23  ILE E CG2    1 
ATOM   11601 C CD1    . ILE E 3 23  ? 16.412  75.877  61.474 1.00 51.28  ? 23  ILE E CD1    1 
ATOM   11602 N N      . GLU E 3 24  ? 18.429  78.233  57.118 1.00 71.91  ? 24  GLU E N      1 
ATOM   11603 C CA     . GLU E 3 24  ? 19.543  78.997  56.596 1.00 73.65  ? 24  GLU E CA     1 
ATOM   11604 C C      . GLU E 3 24  ? 19.375  80.439  56.975 1.00 69.23  ? 24  GLU E C      1 
ATOM   11605 O O      . GLU E 3 24  ? 20.346  81.117  57.272 1.00 69.15  ? 24  GLU E O      1 
ATOM   11606 C CB     . GLU E 3 24  ? 19.617  78.842  55.093 1.00 79.58  ? 24  GLU E CB     1 
ATOM   11607 C CG     . GLU E 3 24  ? 20.961  79.203  54.488 1.00 86.83  ? 24  GLU E CG     1 
ATOM   11608 C CD     . GLU E 3 24  ? 21.156  78.604  53.106 1.00 101.55 ? 24  GLU E CD     1 
ATOM   11609 O OE1    . GLU E 3 24  ? 20.850  77.407  52.928 1.00 100.40 ? 24  GLU E OE1    1 
ATOM   11610 O OE2    . GLU E 3 24  ? 21.625  79.325  52.202 1.00 106.96 ? 24  GLU E OE2    1 
ATOM   11611 N N      . ASN E 3 25  ? 18.142  80.909  57.041 1.00 70.88  ? 25  ASN E N      1 
ATOM   11612 C CA     . ASN E 3 25  ? 17.893  82.274  57.466 1.00 64.53  ? 25  ASN E CA     1 
ATOM   11613 C C      . ASN E 3 25  ? 18.183  82.377  58.927 1.00 64.50  ? 25  ASN E C      1 
ATOM   11614 O O      . ASN E 3 25  ? 18.804  83.326  59.359 1.00 62.42  ? 25  ASN E O      1 
ATOM   11615 C CB     . ASN E 3 25  ? 16.450  82.675  57.224 1.00 67.85  ? 25  ASN E CB     1 
ATOM   11616 C CG     . ASN E 3 25  ? 16.046  82.559  55.768 1.00 76.15  ? 25  ASN E CG     1 
ATOM   11617 O OD1    . ASN E 3 25  ? 16.890  82.445  54.881 1.00 73.44  ? 25  ASN E OD1    1 
ATOM   11618 N ND2    . ASN E 3 25  ? 14.744  82.594  55.515 1.00 70.96  ? 25  ASN E ND2    1 
ATOM   11619 N N      . VAL E 3 26  ? 17.731  81.398  59.701 1.00 72.86  ? 26  VAL E N      1 
ATOM   11620 C CA     . VAL E 3 26  ? 17.914  81.448  61.146 1.00 66.34  ? 26  VAL E CA     1 
ATOM   11621 C C      . VAL E 3 26  ? 19.376  81.445  61.510 1.00 62.07  ? 26  VAL E C      1 
ATOM   11622 O O      . VAL E 3 26  ? 19.782  82.162  62.395 1.00 63.37  ? 26  VAL E O      1 
ATOM   11623 C CB     . VAL E 3 26  ? 17.190  80.308  61.854 1.00 66.75  ? 26  VAL E CB     1 
ATOM   11624 C CG1    . VAL E 3 26  ? 17.282  80.466  63.363 1.00 57.45  ? 26  VAL E CG1    1 
ATOM   11625 C CG2    . VAL E 3 26  ? 15.735  80.289  61.430 1.00 74.01  ? 26  VAL E CG2    1 
ATOM   11626 N N      . LYS E 3 27  ? 20.191  80.699  60.790 1.00 64.16  ? 27  LYS E N      1 
ATOM   11627 C CA     . LYS E 3 27  ? 21.622  80.719  61.042 1.00 64.90  ? 27  LYS E CA     1 
ATOM   11628 C C      . LYS E 3 27  ? 22.210  82.089  60.842 1.00 65.22  ? 27  LYS E C      1 
ATOM   11629 O O      . LYS E 3 27  ? 23.083  82.500  61.593 1.00 65.58  ? 27  LYS E O      1 
ATOM   11630 C CB     . LYS E 3 27  ? 22.355  79.760  60.125 1.00 64.46  ? 27  LYS E CB     1 
ATOM   11631 C CG     . LYS E 3 27  ? 22.302  78.303  60.531 1.00 68.71  ? 27  LYS E CG     1 
ATOM   11632 C CD     . LYS E 3 27  ? 23.262  77.493  59.681 1.00 68.22  ? 27  LYS E CD     1 
ATOM   11633 C CE     . LYS E 3 27  ? 23.390  76.072  60.192 1.00 65.31  ? 27  LYS E CE     1 
ATOM   11634 N NZ     . LYS E 3 27  ? 24.379  75.309  59.382 1.00 56.43  ? 27  LYS E NZ     1 
ATOM   11635 N N      . ALA E 3 28  ? 21.770  82.791  59.805 1.00 60.59  ? 28  ALA E N      1 
ATOM   11636 C CA     . ALA E 3 28  ? 22.344  84.092  59.498 1.00 55.71  ? 28  ALA E CA     1 
ATOM   11637 C C      . ALA E 3 28  ? 21.673  85.167  60.274 1.00 52.96  ? 28  ALA E C      1 
ATOM   11638 O O      . ALA E 3 28  ? 22.157  86.279  60.333 1.00 53.44  ? 28  ALA E O      1 
ATOM   11639 C CB     . ALA E 3 28  ? 22.261  84.382  58.027 1.00 53.55  ? 28  ALA E CB     1 
ATOM   11640 N N      . LYS E 3 29  ? 20.566  84.852  60.909 1.00 47.12  ? 29  LYS E N      1 
ATOM   11641 C CA     . LYS E 3 29  ? 19.968  85.842  61.755 1.00 46.80  ? 29  LYS E CA     1 
ATOM   11642 C C      . LYS E 3 29  ? 20.793  85.813  63.001 1.00 53.64  ? 29  LYS E C      1 
ATOM   11643 O O      . LYS E 3 29  ? 20.768  86.751  63.782 1.00 54.56  ? 29  LYS E O      1 
ATOM   11644 C CB     . LYS E 3 29  ? 18.516  85.525  62.051 1.00 42.87  ? 29  LYS E CB     1 
ATOM   11645 C CG     . LYS E 3 29  ? 17.538  85.975  60.982 1.00 51.37  ? 29  LYS E CG     1 
ATOM   11646 C CD     . LYS E 3 29  ? 16.183  85.321  61.174 1.00 48.77  ? 29  LYS E CD     1 
ATOM   11647 C CE     . LYS E 3 29  ? 15.616  85.619  62.546 1.00 50.44  ? 29  LYS E CE     1 
ATOM   11648 N NZ     . LYS E 3 29  ? 15.192  87.035  62.683 1.00 49.82  ? 29  LYS E NZ     1 
ATOM   11649 N N      . ILE E 3 30  ? 21.537  84.738  63.198 1.00 53.89  ? 30  ILE E N      1 
ATOM   11650 C CA     . ILE E 3 30  ? 22.399  84.648  64.364 1.00 56.52  ? 30  ILE E CA     1 
ATOM   11651 C C      . ILE E 3 30  ? 23.687  85.374  64.054 1.00 59.26  ? 30  ILE E C      1 
ATOM   11652 O O      . ILE E 3 30  ? 24.365  85.837  64.954 1.00 65.12  ? 30  ILE E O      1 
ATOM   11653 C CB     . ILE E 3 30  ? 22.602  83.205  64.860 1.00 49.22  ? 30  ILE E CB     1 
ATOM   11654 C CG1    . ILE E 3 30  ? 21.264  82.572  65.190 1.00 48.17  ? 30  ILE E CG1    1 
ATOM   11655 C CG2    . ILE E 3 30  ? 23.433  83.163  66.126 1.00 50.09  ? 30  ILE E CG2    1 
ATOM   11656 C CD1    . ILE E 3 30  ? 21.375  81.413  66.144 1.00 45.26  ? 30  ILE E CD1    1 
ATOM   11657 N N      . GLN E 3 31  ? 24.030  85.517  62.782 1.00 53.13  ? 31  GLN E N      1 
ATOM   11658 C CA     . GLN E 3 31  ? 25.213  86.288  62.440 1.00 50.91  ? 31  GLN E CA     1 
ATOM   11659 C C      . GLN E 3 31  ? 24.939  87.739  62.701 1.00 59.19  ? 31  GLN E C      1 
ATOM   11660 O O      . GLN E 3 31  ? 25.843  88.554  62.823 1.00 63.28  ? 31  GLN E O      1 
ATOM   11661 C CB     . GLN E 3 31  ? 25.595  86.124  60.980 1.00 50.63  ? 31  GLN E CB     1 
ATOM   11662 C CG     . GLN E 3 31  ? 27.032  86.520  60.690 1.00 46.16  ? 31  GLN E CG     1 
ATOM   11663 C CD     . GLN E 3 31  ? 27.372  86.485  59.223 1.00 51.43  ? 31  GLN E CD     1 
ATOM   11664 O OE1    . GLN E 3 31  ? 26.490  86.449  58.372 1.00 53.36  ? 31  GLN E OE1    1 
ATOM   11665 N NE2    . GLN E 3 31  ? 28.660  86.503  58.916 1.00 49.38  ? 31  GLN E NE2    1 
ATOM   11666 N N      . ASP E 3 32  ? 23.680  88.074  62.867 1.00 58.02  ? 32  ASP E N      1 
ATOM   11667 C CA     . ASP E 3 32  ? 23.357  89.438  63.180 1.00 59.60  ? 32  ASP E CA     1 
ATOM   11668 C C      . ASP E 3 32  ? 23.695  89.729  64.588 1.00 58.49  ? 32  ASP E C      1 
ATOM   11669 O O      . ASP E 3 32  ? 24.609  90.480  64.848 1.00 73.95  ? 32  ASP E O      1 
ATOM   11670 C CB     . ASP E 3 32  ? 21.891  89.698  62.970 1.00 71.99  ? 32  ASP E CB     1 
ATOM   11671 C CG     . ASP E 3 32  ? 21.518  89.753  61.495 1.00 81.50  ? 32  ASP E CG     1 
ATOM   11672 O OD1    . ASP E 3 32  ? 22.417  89.585  60.644 1.00 84.95  ? 32  ASP E OD1    1 
ATOM   11673 O OD2    . ASP E 3 32  ? 20.327  89.969  61.184 1.00 82.41  ? 32  ASP E OD2    1 
ATOM   11674 N N      . LYS E 3 33  ? 22.986  89.123  65.516 1.00 50.94  ? 33  LYS E N      1 
ATOM   11675 C CA     . LYS E 3 33  ? 23.215  89.431  66.907 1.00 53.03  ? 33  LYS E CA     1 
ATOM   11676 C C      . LYS E 3 33  ? 24.648  89.212  67.334 1.00 54.39  ? 33  LYS E C      1 
ATOM   11677 O O      . LYS E 3 33  ? 25.283  90.150  67.799 1.00 54.50  ? 33  LYS E O      1 
ATOM   11678 C CB     . LYS E 3 33  ? 22.250  88.665  67.794 1.00 56.12  ? 33  LYS E CB     1 
ATOM   11679 C CG     . LYS E 3 33  ? 22.055  89.291  69.161 1.00 53.91  ? 33  LYS E CG     1 
ATOM   11680 C CD     . LYS E 3 33  ? 20.678  88.976  69.711 1.00 59.42  ? 33  LYS E CD     1 
ATOM   11681 C CE     . LYS E 3 33  ? 20.516  89.525  71.116 1.00 64.04  ? 33  LYS E CE     1 
ATOM   11682 N NZ     . LYS E 3 33  ? 21.566  88.998  72.027 1.00 63.04  ? 33  LYS E NZ     1 
ATOM   11683 N N      . GLU E 3 34  ? 25.177  88.000  67.218 1.00 57.41  ? 34  GLU E N      1 
ATOM   11684 C CA     . GLU E 3 34  ? 26.513  87.733  67.763 1.00 53.61  ? 34  GLU E CA     1 
ATOM   11685 C C      . GLU E 3 34  ? 27.672  87.642  66.810 1.00 52.45  ? 34  GLU E C      1 
ATOM   11686 O O      . GLU E 3 34  ? 28.804  87.525  67.238 1.00 49.51  ? 34  GLU E O      1 
ATOM   11687 C CB     . GLU E 3 34  ? 26.479  86.508  68.656 1.00 53.70  ? 34  GLU E CB     1 
ATOM   11688 C CG     . GLU E 3 34  ? 25.494  86.606  69.806 1.00 56.53  ? 34  GLU E CG     1 
ATOM   11689 C CD     . GLU E 3 34  ? 26.018  87.438  70.955 1.00 60.86  ? 34  GLU E CD     1 
ATOM   11690 O OE1    . GLU E 3 34  ? 27.248  87.465  71.152 1.00 60.73  ? 34  GLU E OE1    1 
ATOM   11691 O OE2    . GLU E 3 34  ? 25.200  88.052  71.670 1.00 62.83  ? 34  GLU E OE2    1 
ATOM   11692 N N      . GLY E 3 35  ? 27.418  87.684  65.522 1.00 53.24  ? 35  GLY E N      1 
ATOM   11693 C CA     . GLY E 3 35  ? 28.507  87.713  64.567 1.00 53.90  ? 35  GLY E CA     1 
ATOM   11694 C C      . GLY E 3 35  ? 29.007  86.387  64.111 1.00 57.82  ? 35  GLY E C      1 
ATOM   11695 O O      . GLY E 3 35  ? 29.798  86.322  63.187 1.00 61.24  ? 35  GLY E O      1 
ATOM   11696 N N      . ILE E 3 36  ? 28.555  85.331  64.754 1.00 55.36  ? 36  ILE E N      1 
ATOM   11697 C CA     . ILE E 3 36  ? 28.998  84.006  64.426 1.00 49.38  ? 36  ILE E CA     1 
ATOM   11698 C C      . ILE E 3 36  ? 28.732  83.684  62.983 1.00 55.93  ? 36  ILE E C      1 
ATOM   11699 O O      . ILE E 3 36  ? 27.604  83.757  62.536 1.00 61.54  ? 36  ILE E O      1 
ATOM   11700 C CB     . ILE E 3 36  ? 28.257  83.000  65.283 1.00 49.03  ? 36  ILE E CB     1 
ATOM   11701 C CG1    . ILE E 3 36  ? 28.254  83.448  66.737 1.00 44.80  ? 36  ILE E CG1    1 
ATOM   11702 C CG2    . ILE E 3 36  ? 28.912  81.653  65.129 1.00 55.87  ? 36  ILE E CG2    1 
ATOM   11703 C CD1    . ILE E 3 36  ? 27.181  82.788  67.564 1.00 47.45  ? 36  ILE E CD1    1 
ATOM   11704 N N      . PRO E 3 37  ? 29.795  83.309  62.220 1.00 52.61  ? 37  PRO E N      1 
ATOM   11705 C CA     . PRO E 3 37  ? 29.468  83.027  60.832 1.00 54.96  ? 37  PRO E CA     1 
ATOM   11706 C C      . PRO E 3 37  ? 28.506  81.896  60.701 1.00 55.33  ? 37  PRO E C      1 
ATOM   11707 O O      . PRO E 3 37  ? 28.496  81.003  61.523 1.00 62.94  ? 37  PRO E O      1 
ATOM   11708 C CB     . PRO E 3 37  ? 30.798  82.591  60.252 1.00 50.25  ? 37  PRO E CB     1 
ATOM   11709 C CG     . PRO E 3 37  ? 31.807  83.311  61.050 1.00 55.38  ? 37  PRO E CG     1 
ATOM   11710 C CD     . PRO E 3 37  ? 31.262  83.240  62.432 1.00 46.33  ? 37  PRO E CD     1 
ATOM   11711 N N      . PRO E 3 38  ? 27.682  81.898  59.635 1.00 51.29  ? 38  PRO E N      1 
ATOM   11712 C CA     . PRO E 3 38  ? 26.716  80.814  59.633 1.00 55.75  ? 38  PRO E CA     1 
ATOM   11713 C C      . PRO E 3 38  ? 27.335  79.463  59.442 1.00 55.07  ? 38  PRO E C      1 
ATOM   11714 O O      . PRO E 3 38  ? 26.800  78.468  59.887 1.00 53.79  ? 38  PRO E O      1 
ATOM   11715 C CB     . PRO E 3 38  ? 25.851  81.141  58.427 1.00 53.66  ? 38  PRO E CB     1 
ATOM   11716 C CG     . PRO E 3 38  ? 25.993  82.597  58.224 1.00 51.82  ? 38  PRO E CG     1 
ATOM   11717 C CD     . PRO E 3 38  ? 27.447  82.789  58.476 1.00 54.81  ? 38  PRO E CD     1 
ATOM   11718 N N      . ASP E 3 39  ? 28.447  79.408  58.766 1.00 58.18  ? 39  ASP E N      1 
ATOM   11719 C CA     . ASP E 3 39  ? 29.055  78.136  58.474 1.00 59.23  ? 39  ASP E CA     1 
ATOM   11720 C C      . ASP E 3 39  ? 29.534  77.478  59.721 1.00 50.82  ? 39  ASP E C      1 
ATOM   11721 O O      . ASP E 3 39  ? 29.474  76.278  59.831 1.00 51.52  ? 39  ASP E O      1 
ATOM   11722 C CB     . ASP E 3 39  ? 30.239  78.347  57.535 1.00 59.91  ? 39  ASP E CB     1 
ATOM   11723 C CG     . ASP E 3 39  ? 29.848  78.987  56.228 1.00 65.39  ? 39  ASP E CG     1 
ATOM   11724 O OD1    . ASP E 3 39  ? 28.649  78.997  55.888 1.00 59.66  ? 39  ASP E OD1    1 
ATOM   11725 O OD2    . ASP E 3 39  ? 30.756  79.472  55.532 1.00 77.02  ? 39  ASP E OD2    1 
ATOM   11726 N N      . GLN E 3 40  ? 30.020  78.253  60.661 1.00 51.33  ? 40  GLN E N      1 
ATOM   11727 C CA     . GLN E 3 40  ? 30.561  77.713  61.871 1.00 48.11  ? 40  GLN E CA     1 
ATOM   11728 C C      . GLN E 3 40  ? 29.434  77.126  62.602 1.00 55.02  ? 40  GLN E C      1 
ATOM   11729 O O      . GLN E 3 40  ? 29.611  76.246  63.417 1.00 55.04  ? 40  GLN E O      1 
ATOM   11730 C CB     . GLN E 3 40  ? 31.118  78.834  62.711 1.00 46.04  ? 40  GLN E CB     1 
ATOM   11731 C CG     . GLN E 3 40  ? 31.815  78.405  63.982 1.00 53.60  ? 40  GLN E CG     1 
ATOM   11732 C CD     . GLN E 3 40  ? 32.569  79.539  64.632 1.00 51.94  ? 40  GLN E CD     1 
ATOM   11733 O OE1    . GLN E 3 40  ? 32.535  80.663  64.155 1.00 50.45  ? 40  GLN E OE1    1 
ATOM   11734 N NE2    . GLN E 3 40  ? 33.264  79.247  65.719 1.00 47.25  ? 40  GLN E NE2    1 
ATOM   11735 N N      . GLN E 3 41  ? 28.241  77.589  62.317 1.00 56.76  ? 41  GLN E N      1 
ATOM   11736 C CA     . GLN E 3 41  ? 27.104  77.126  63.085 1.00 53.04  ? 41  GLN E CA     1 
ATOM   11737 C C      . GLN E 3 41  ? 26.528  75.796  62.772 1.00 51.93  ? 41  GLN E C      1 
ATOM   11738 O O      . GLN E 3 41  ? 26.347  75.452  61.621 1.00 54.15  ? 41  GLN E O      1 
ATOM   11739 C CB     . GLN E 3 41  ? 25.974  78.150  63.029 1.00 53.70  ? 41  GLN E CB     1 
ATOM   11740 C CG     . GLN E 3 41  ? 26.327  79.547  63.483 1.00 56.58  ? 41  GLN E CG     1 
ATOM   11741 C CD     . GLN E 3 41  ? 25.121  80.454  63.456 1.00 62.43  ? 41  GLN E CD     1 
ATOM   11742 O OE1    . GLN E 3 41  ? 23.989  79.986  63.393 1.00 56.24  ? 41  GLN E OE1    1 
ATOM   11743 N NE2    . GLN E 3 41  ? 25.354  81.755  63.503 1.00 61.78  ? 41  GLN E NE2    1 
ATOM   11744 N N      . ARG E 3 42  ? 26.198  75.058  63.811 1.00 56.88  ? 42  ARG E N      1 
ATOM   11745 C CA     . ARG E 3 42  ? 25.546  73.786  63.661 1.00 63.59  ? 42  ARG E CA     1 
ATOM   11746 C C      . ARG E 3 42  ? 24.436  73.956  64.662 1.00 65.64  ? 42  ARG E C      1 
ATOM   11747 O O      . ARG E 3 42  ? 24.712  74.222  65.819 1.00 63.95  ? 42  ARG E O      1 
ATOM   11748 C CB     . ARG E 3 42  ? 26.445  72.652  64.134 1.00 57.43  ? 42  ARG E CB     1 
ATOM   11749 C CG     . ARG E 3 42  ? 27.697  72.430  63.316 1.00 60.50  ? 42  ARG E CG     1 
ATOM   11750 C CD     . ARG E 3 42  ? 28.023  70.948  63.254 1.00 68.55  ? 42  ARG E CD     1 
ATOM   11751 N NE     . ARG E 3 42  ? 28.010  70.327  64.573 1.00 77.33  ? 42  ARG E NE     1 
ATOM   11752 C CZ     . ARG E 3 42  ? 28.112  69.019  64.782 1.00 77.92  ? 42  ARG E CZ     1 
ATOM   11753 N NH1    . ARG E 3 42  ? 28.231  68.191  63.753 1.00 67.64  ? 42  ARG E NH1    1 
ATOM   11754 N NH2    . ARG E 3 42  ? 28.086  68.536  66.016 1.00 67.93  ? 42  ARG E NH2    1 
ATOM   11755 N N      . LEU E 3 43  ? 23.185  73.859  64.244 1.00 60.19  ? 43  LEU E N      1 
ATOM   11756 C CA     . LEU E 3 43  ? 22.096  74.125  65.167 1.00 58.45  ? 43  LEU E CA     1 
ATOM   11757 C C      . LEU E 3 43  ? 21.394  72.851  65.488 1.00 57.93  ? 43  LEU E C      1 
ATOM   11758 O O      . LEU E 3 43  ? 21.206  72.034  64.610 1.00 59.27  ? 43  LEU E O      1 
ATOM   11759 C CB     . LEU E 3 43  ? 21.145  75.161  64.586 1.00 60.32  ? 43  LEU E CB     1 
ATOM   11760 C CG     . LEU E 3 43  ? 21.366  76.627  64.959 1.00 56.63  ? 43  LEU E CG     1 
ATOM   11761 C CD1    . LEU E 3 43  ? 20.694  77.541  63.955 1.00 58.42  ? 43  LEU E CD1    1 
ATOM   11762 C CD2    . LEU E 3 43  ? 20.830  76.899  66.351 1.00 51.70  ? 43  LEU E CD2    1 
ATOM   11763 N N      . ILE E 3 44  ? 20.978  72.665  66.733 1.00 58.40  ? 44  ILE E N      1 
ATOM   11764 C CA     . ILE E 3 44  ? 20.420  71.389  67.139 1.00 59.46  ? 44  ILE E CA     1 
ATOM   11765 C C      . ILE E 3 44  ? 19.157  71.462  67.953 1.00 63.00  ? 44  ILE E C      1 
ATOM   11766 O O      . ILE E 3 44  ? 19.112  72.189  68.926 1.00 62.47  ? 44  ILE E O      1 
ATOM   11767 C CB     . ILE E 3 44  ? 21.461  70.651  67.984 1.00 53.74  ? 44  ILE E CB     1 
ATOM   11768 C CG1    . ILE E 3 44  ? 22.660  70.247  67.125 1.00 64.36  ? 44  ILE E CG1    1 
ATOM   11769 C CG2    . ILE E 3 44  ? 20.870  69.417  68.637 1.00 65.01  ? 44  ILE E CG2    1 
ATOM   11770 C CD1    . ILE E 3 44  ? 23.969  70.188  67.873 1.00 60.11  ? 44  ILE E CD1    1 
ATOM   11771 N N      . PHE E 3 45  ? 18.129  70.716  67.565 1.00 63.16  ? 45  PHE E N      1 
ATOM   11772 C CA     . PHE E 3 45  ? 16.882  70.666  68.318 1.00 61.09  ? 45  PHE E CA     1 
ATOM   11773 C C      . PHE E 3 45  ? 16.362  69.267  68.219 1.00 63.40  ? 45  PHE E C      1 
ATOM   11774 O O      . PHE E 3 45  ? 16.500  68.643  67.178 1.00 63.39  ? 45  PHE E O      1 
ATOM   11775 C CB     . PHE E 3 45  ? 15.867  71.617  67.730 1.00 58.23  ? 45  PHE E CB     1 
ATOM   11776 C CG     . PHE E 3 45  ? 14.535  71.601  68.410 1.00 56.01  ? 45  PHE E CG     1 
ATOM   11777 C CD1    . PHE E 3 45  ? 14.420  71.932  69.743 1.00 70.83  ? 45  PHE E CD1    1 
ATOM   11778 C CD2    . PHE E 3 45  ? 13.395  71.293  67.702 1.00 49.79  ? 45  PHE E CD2    1 
ATOM   11779 C CE1    . PHE E 3 45  ? 13.191  71.925  70.367 1.00 74.66  ? 45  PHE E CE1    1 
ATOM   11780 C CE2    . PHE E 3 45  ? 12.163  71.288  68.314 1.00 54.58  ? 45  PHE E CE2    1 
ATOM   11781 C CZ     . PHE E 3 45  ? 12.059  71.604  69.650 1.00 67.18  ? 45  PHE E CZ     1 
ATOM   11782 N N      . ALA E 3 46  ? 15.809  68.754  69.308 1.00 67.14  ? 46  ALA E N      1 
ATOM   11783 C CA     . ALA E 3 46  ? 15.262  67.405  69.330 1.00 69.12  ? 46  ALA E CA     1 
ATOM   11784 C C      . ALA E 3 46  ? 16.278  66.381  68.924 1.00 71.22  ? 46  ALA E C      1 
ATOM   11785 O O      . ALA E 3 46  ? 15.968  65.438  68.213 1.00 73.74  ? 46  ALA E O      1 
ATOM   11786 C CB     . ALA E 3 46  ? 14.040  67.304  68.448 1.00 66.42  ? 46  ALA E CB     1 
ATOM   11787 N N      . GLY E 3 47  ? 17.506  66.565  69.360 1.00 65.79  ? 47  GLY E N      1 
ATOM   11788 C CA     . GLY E 3 47  ? 18.526  65.596  69.077 1.00 61.30  ? 47  GLY E CA     1 
ATOM   11789 C C      . GLY E 3 47  ? 18.700  65.413  67.615 1.00 65.87  ? 47  GLY E C      1 
ATOM   11790 O O      . GLY E 3 47  ? 18.962  64.317  67.154 1.00 81.16  ? 47  GLY E O      1 
ATOM   11791 N N      . LYS E 3 48  ? 18.559  66.484  66.868 1.00 62.49  ? 48  LYS E N      1 
ATOM   11792 C CA     . LYS E 3 48  ? 18.798  66.395  65.454 1.00 67.05  ? 48  LYS E CA     1 
ATOM   11793 C C      . LYS E 3 48  ? 19.563  67.612  65.053 1.00 69.68  ? 48  LYS E C      1 
ATOM   11794 O O      . LYS E 3 48  ? 19.365  68.672  65.625 1.00 72.04  ? 48  LYS E O      1 
ATOM   11795 C CB     . LYS E 3 48  ? 17.482  66.366  64.682 1.00 74.15  ? 48  LYS E CB     1 
ATOM   11796 C CG     . LYS E 3 48  ? 16.708  65.061  64.754 1.00 74.21  ? 48  LYS E CG     1 
ATOM   11797 C CD     . LYS E 3 48  ? 15.325  65.201  64.138 1.00 72.97  ? 48  LYS E CD     1 
ATOM   11798 C CE     . LYS E 3 48  ? 15.404  65.565  62.666 1.00 72.23  ? 48  LYS E CE     1 
ATOM   11799 N NZ     . LYS E 3 48  ? 14.057  65.587  62.030 1.00 49.75  ? 48  LYS E NZ     1 
ATOM   11800 N N      . GLN E 3 49  ? 20.445  67.482  64.079 1.00 66.82  ? 49  GLN E N      1 
ATOM   11801 C CA     . GLN E 3 49  ? 21.129  68.648  63.586 1.00 67.31  ? 49  GLN E CA     1 
ATOM   11802 C C      . GLN E 3 49  ? 20.204  69.223  62.549 1.00 67.09  ? 49  GLN E C      1 
ATOM   11803 O O      . GLN E 3 49  ? 19.934  68.596  61.539 1.00 69.35  ? 49  GLN E O      1 
ATOM   11804 C CB     . GLN E 3 49  ? 22.486  68.301  62.998 1.00 64.95  ? 49  GLN E CB     1 
ATOM   11805 C CG     . GLN E 3 49  ? 23.283  69.493  62.508 1.00 67.71  ? 49  GLN E CG     1 
ATOM   11806 C CD     . GLN E 3 49  ? 24.665  69.097  62.041 1.00 69.55  ? 49  GLN E CD     1 
ATOM   11807 O OE1    . GLN E 3 49  ? 25.090  67.960  62.225 1.00 71.25  ? 49  GLN E OE1    1 
ATOM   11808 N NE2    . GLN E 3 49  ? 25.378  70.036  61.433 1.00 72.04  ? 49  GLN E NE2    1 
ATOM   11809 N N      . LEU E 3 50  ? 19.699  70.413  62.812 1.00 65.80  ? 50  LEU E N      1 
ATOM   11810 C CA     . LEU E 3 50  ? 18.767  71.023  61.910 1.00 60.75  ? 50  LEU E CA     1 
ATOM   11811 C C      . LEU E 3 50  ? 19.482  71.241  60.618 1.00 63.82  ? 50  LEU E C      1 
ATOM   11812 O O      . LEU E 3 50  ? 20.663  71.569  60.601 1.00 62.85  ? 50  LEU E O      1 
ATOM   11813 C CB     . LEU E 3 50  ? 18.230  72.301  62.517 1.00 59.89  ? 50  LEU E CB     1 
ATOM   11814 C CG     . LEU E 3 50  ? 17.624  72.084  63.898 1.00 59.68  ? 50  LEU E CG     1 
ATOM   11815 C CD1    . LEU E 3 50  ? 16.992  73.371  64.365 1.00 55.09  ? 50  LEU E CD1    1 
ATOM   11816 C CD2    . LEU E 3 50  ? 16.588  70.974  63.883 1.00 62.24  ? 50  LEU E CD2    1 
ATOM   11817 N N      . GLU E 3 51  ? 18.788  71.036  59.512 1.00 65.92  ? 51  GLU E N      1 
ATOM   11818 C CA     . GLU E 3 51  ? 19.447  71.128  58.233 1.00 65.57  ? 51  GLU E CA     1 
ATOM   11819 C C      . GLU E 3 51  ? 19.113  72.423  57.614 1.00 67.33  ? 51  GLU E C      1 
ATOM   11820 O O      . GLU E 3 51  ? 18.051  72.971  57.850 1.00 66.09  ? 51  GLU E O      1 
ATOM   11821 C CB     . GLU E 3 51  ? 19.010  69.997  57.326 1.00 75.13  ? 51  GLU E CB     1 
ATOM   11822 C CG     . GLU E 3 51  ? 20.052  69.610  56.291 1.00 80.55  ? 51  GLU E CG     1 
ATOM   11823 C CD     . GLU E 3 51  ? 19.644  68.404  55.473 1.00 85.89  ? 51  GLU E CD     1 
ATOM   11824 O OE1    . GLU E 3 51  ? 18.726  67.675  55.903 1.00 92.79  ? 51  GLU E OE1    1 
ATOM   11825 O OE2    . GLU E 3 51  ? 20.247  68.187  54.401 1.00 79.60  ? 51  GLU E OE2    1 
ATOM   11826 N N      . ASP E 3 52  ? 20.033  72.929  56.822 1.00 70.92  ? 52  ASP E N      1 
ATOM   11827 C CA     . ASP E 3 52  ? 19.844  74.224  56.225 1.00 81.06  ? 52  ASP E CA     1 
ATOM   11828 C C      . ASP E 3 52  ? 18.591  74.323  55.389 1.00 79.71  ? 52  ASP E C      1 
ATOM   11829 O O      . ASP E 3 52  ? 17.833  75.259  55.545 1.00 82.54  ? 52  ASP E O      1 
ATOM   11830 C CB     . ASP E 3 52  ? 21.076  74.580  55.402 1.00 85.79  ? 52  ASP E CB     1 
ATOM   11831 C CG     . ASP E 3 52  ? 22.229  75.039  56.256 1.00 93.31  ? 52  ASP E CG     1 
ATOM   11832 O OD1    . ASP E 3 52  ? 22.393  74.498  57.365 1.00 88.99  ? 52  ASP E OD1    1 
ATOM   11833 O OD2    . ASP E 3 52  ? 22.973  75.940  55.821 1.00 96.30  ? 52  ASP E OD2    1 
ATOM   11834 N N      . GLY E 3 53  ? 18.348  73.367  54.512 1.00 68.04  ? 53  GLY E N      1 
ATOM   11835 C CA     . GLY E 3 53  ? 17.211  73.463  53.620 1.00 61.89  ? 53  GLY E CA     1 
ATOM   11836 C C      . GLY E 3 53  ? 15.835  73.536  54.219 1.00 61.49  ? 53  GLY E C      1 
ATOM   11837 O O      . GLY E 3 53  ? 15.020  74.351  53.824 1.00 66.45  ? 53  GLY E O      1 
ATOM   11838 N N      . ARG E 3 54  ? 15.558  72.710  55.196 1.00 61.64  ? 54  ARG E N      1 
ATOM   11839 C CA     . ARG E 3 54  ? 14.223  72.666  55.727 1.00 65.14  ? 54  ARG E CA     1 
ATOM   11840 C C      . ARG E 3 54  ? 13.892  73.781  56.653 1.00 65.22  ? 54  ARG E C      1 
ATOM   11841 O O      . ARG E 3 54  ? 14.759  74.329  57.299 1.00 66.47  ? 54  ARG E O      1 
ATOM   11842 C CB     . ARG E 3 54  ? 13.974  71.335  56.414 1.00 72.29  ? 54  ARG E CB     1 
ATOM   11843 C CG     . ARG E 3 54  ? 14.108  70.125  55.509 1.00 73.76  ? 54  ARG E CG     1 
ATOM   11844 C CD     . ARG E 3 54  ? 15.366  69.333  55.825 1.00 76.97  ? 54  ARG E CD     1 
ATOM   11845 N NE     . ARG E 3 54  ? 15.636  68.319  54.812 1.00 85.55  ? 54  ARG E NE     1 
ATOM   11846 C CZ     . ARG E 3 54  ? 16.409  68.513  53.748 1.00 93.51  ? 54  ARG E CZ     1 
ATOM   11847 N NH1    . ARG E 3 54  ? 17.001  69.683  53.560 1.00 88.37  ? 54  ARG E NH1    1 
ATOM   11848 N NH2    . ARG E 3 54  ? 16.596  67.534  52.875 1.00 91.59  ? 54  ARG E NH2    1 
ATOM   11849 N N      . THR E 3 55  ? 12.630  74.131  56.677 1.00 68.41  ? 55  THR E N      1 
ATOM   11850 C CA     . THR E 3 55  ? 12.212  75.240  57.466 1.00 72.58  ? 55  THR E CA     1 
ATOM   11851 C C      . THR E 3 55  ? 12.022  74.842  58.872 1.00 73.73  ? 55  THR E C      1 
ATOM   11852 O O      . THR E 3 55  ? 11.961  73.674  59.192 1.00 72.92  ? 55  THR E O      1 
ATOM   11853 C CB     . THR E 3 55  ? 10.864  75.728  56.971 1.00 77.04  ? 55  THR E CB     1 
ATOM   11854 O OG1    . THR E 3 55  ? 9.884   74.724  57.231 1.00 82.86  ? 55  THR E OG1    1 
ATOM   11855 C CG2    . THR E 3 55  ? 10.918  75.998  55.479 1.00 73.06  ? 55  THR E CG2    1 
ATOM   11856 N N      . LEU E 3 56  ? 11.876  75.830  59.732 1.00 71.85  ? 56  LEU E N      1 
ATOM   11857 C CA     . LEU E 3 56  ? 11.753  75.531  61.120 1.00 75.00  ? 56  LEU E CA     1 
ATOM   11858 C C      . LEU E 3 56  ? 10.398  74.943  61.318 1.00 85.78  ? 56  LEU E C      1 
ATOM   11859 O O      . LEU E 3 56  ? 10.135  74.301  62.326 1.00 87.31  ? 56  LEU E O      1 
ATOM   11860 C CB     . LEU E 3 56  ? 11.994  76.764  61.966 1.00 68.60  ? 56  LEU E CB     1 
ATOM   11861 C CG     . LEU E 3 56  ? 11.085  77.980  61.982 1.00 82.03  ? 56  LEU E CG     1 
ATOM   11862 C CD1    . LEU E 3 56  ? 10.162  77.920  63.186 1.00 86.66  ? 56  LEU E CD1    1 
ATOM   11863 C CD2    . LEU E 3 56  ? 11.982  79.194  62.098 1.00 90.23  ? 56  LEU E CD2    1 
ATOM   11864 N N      . SER E 3 57  ? 9.529   75.137  60.338 1.00 85.70  ? 57  SER E N      1 
ATOM   11865 C CA     . SER E 3 57  ? 8.179   74.612  60.442 1.00 85.41  ? 57  SER E CA     1 
ATOM   11866 C C      . SER E 3 57  ? 8.275   73.127  60.381 1.00 77.43  ? 57  SER E C      1 
ATOM   11867 O O      . SER E 3 57  ? 7.539   72.418  61.053 1.00 71.68  ? 57  SER E O      1 
ATOM   11868 C CB     . SER E 3 57  ? 7.313   75.100  59.290 1.00 78.45  ? 57  SER E CB     1 
ATOM   11869 O OG     . SER E 3 57  ? 7.423   74.250  58.167 1.00 78.32  ? 57  SER E OG     1 
ATOM   11870 N N      . ASP E 3 58  ? 9.212   72.640  59.586 1.00 71.43  ? 58  ASP E N      1 
ATOM   11871 C CA     . ASP E 3 58  ? 9.324   71.209  59.385 1.00 79.17  ? 58  ASP E CA     1 
ATOM   11872 C C      . ASP E 3 58  ? 9.760   70.425  60.612 1.00 80.33  ? 58  ASP E C      1 
ATOM   11873 O O      . ASP E 3 58  ? 9.607   69.209  60.655 1.00 80.14  ? 58  ASP E O      1 
ATOM   11874 C CB     . ASP E 3 58  ? 10.244  70.911  58.196 1.00 73.48  ? 58  ASP E CB     1 
ATOM   11875 C CG     . ASP E 3 58  ? 9.732   71.496  56.898 1.00 73.29  ? 58  ASP E CG     1 
ATOM   11876 O OD1    . ASP E 3 58  ? 8.610   72.037  56.882 1.00 72.29  ? 58  ASP E OD1    1 
ATOM   11877 O OD2    . ASP E 3 58  ? 10.453  71.412  55.885 1.00 72.38  ? 58  ASP E OD2    1 
ATOM   11878 N N      . TYR E 3 59  ? 10.302  71.093  61.614 1.00 69.41  ? 59  TYR E N      1 
ATOM   11879 C CA     . TYR E 3 59  ? 10.808  70.356  62.760 1.00 71.89  ? 59  TYR E CA     1 
ATOM   11880 C C      . TYR E 3 59  ? 9.919   70.614  63.939 1.00 70.98  ? 59  TYR E C      1 
ATOM   11881 O O      . TYR E 3 59  ? 10.320  70.403  65.077 1.00 62.19  ? 59  TYR E O      1 
ATOM   11882 C CB     . TYR E 3 59  ? 12.228  70.775  63.110 1.00 70.16  ? 59  TYR E CB     1 
ATOM   11883 C CG     . TYR E 3 59  ? 13.264  70.596  62.033 1.00 63.92  ? 59  TYR E CG     1 
ATOM   11884 C CD1    . TYR E 3 59  ? 13.791  69.351  61.753 1.00 60.39  ? 59  TYR E CD1    1 
ATOM   11885 C CD2    . TYR E 3 59  ? 13.752  71.683  61.335 1.00 66.27  ? 59  TYR E CD2    1 
ATOM   11886 C CE1    . TYR E 3 59  ? 14.757  69.191  60.783 1.00 61.35  ? 59  TYR E CE1    1 
ATOM   11887 C CE2    . TYR E 3 59  ? 14.717  71.532  60.365 1.00 60.10  ? 59  TYR E CE2    1 
ATOM   11888 C CZ     . TYR E 3 59  ? 15.213  70.284  60.097 1.00 57.06  ? 59  TYR E CZ     1 
ATOM   11889 O OH     . TYR E 3 59  ? 16.169  70.127  59.134 1.00 55.20  ? 59  TYR E OH     1 
ATOM   11890 N N      . ASN E 3 60  ? 8.721   71.093  63.662 1.00 70.51  ? 60  ASN E N      1 
ATOM   11891 C CA     . ASN E 3 60  ? 7.790   71.410  64.722 1.00 75.67  ? 60  ASN E CA     1 
ATOM   11892 C C      . ASN E 3 60  ? 8.468   72.314  65.684 1.00 74.07  ? 60  ASN E C      1 
ATOM   11893 O O      . ASN E 3 60  ? 8.559   72.019  66.861 1.00 75.19  ? 60  ASN E O      1 
ATOM   11894 C CB     . ASN E 3 60  ? 7.282   70.163  65.426 1.00 76.42  ? 60  ASN E CB     1 
ATOM   11895 C CG     . ASN E 3 60  ? 5.799   70.226  65.717 1.00 80.65  ? 60  ASN E CG     1 
ATOM   11896 O OD1    . ASN E 3 60  ? 5.171   71.273  65.574 1.00 81.81  ? 60  ASN E OD1    1 
ATOM   11897 N ND2    . ASN E 3 60  ? 5.231   69.102  66.132 1.00 82.23  ? 60  ASN E ND2    1 
ATOM   11898 N N      . ILE E 3 61  ? 8.896   73.467  65.199 1.00 80.72  ? 61  ILE E N      1 
ATOM   11899 C CA     . ILE E 3 61  ? 9.491   74.457  66.083 1.00 87.04  ? 61  ILE E CA     1 
ATOM   11900 C C      . ILE E 3 61  ? 8.447   75.485  66.394 1.00 82.68  ? 61  ILE E C      1 
ATOM   11901 O O      . ILE E 3 61  ? 7.850   76.056  65.499 1.00 79.61  ? 61  ILE E O      1 
ATOM   11902 C CB     . ILE E 3 61  ? 10.772  75.038  65.496 1.00 84.29  ? 61  ILE E CB     1 
ATOM   11903 C CG1    . ILE E 3 61  ? 11.845  73.947  65.441 1.00 76.54  ? 61  ILE E CG1    1 
ATOM   11904 C CG2    . ILE E 3 61  ? 11.269  76.207  66.323 1.00 78.17  ? 61  ILE E CG2    1 
ATOM   11905 C CD1    . ILE E 3 61  ? 13.134  74.357  64.771 1.00 62.12  ? 61  ILE E CD1    1 
ATOM   11906 N N      . GLN E 3 62  ? 8.184   75.689  67.668 1.00 80.18  ? 62  GLN E N      1 
ATOM   11907 C CA     . GLN E 3 62  ? 7.109   76.560  68.052 1.00 77.89  ? 62  GLN E CA     1 
ATOM   11908 C C      . GLN E 3 62  ? 7.537   77.633  68.974 1.00 81.64  ? 62  GLN E C      1 
ATOM   11909 O O      . GLN E 3 62  ? 8.713   77.899  69.109 1.00 87.94  ? 62  GLN E O      1 
ATOM   11910 C CB     . GLN E 3 62  ? 6.097   75.790  68.873 1.00 84.25  ? 62  GLN E CB     1 
ATOM   11911 C CG     . GLN E 3 62  ? 5.585   74.513  68.229 1.00 91.79  ? 62  GLN E CG     1 
ATOM   11912 C CD     . GLN E 3 62  ? 6.187   73.269  68.852 1.00 101.21 ? 62  GLN E CD     1 
ATOM   11913 O OE1    . GLN E 3 62  ? 7.085   73.353  69.691 1.00 102.20 ? 62  GLN E OE1    1 
ATOM   11914 N NE2    . GLN E 3 62  ? 5.693   72.106  68.446 1.00 94.03  ? 62  GLN E NE2    1 
ATOM   11915 N N      . LYS E 3 63  ? 6.579   78.240  69.647 1.00 81.86  ? 63  LYS E N      1 
ATOM   11916 C CA     . LYS E 3 63  ? 6.890   79.397  70.449 1.00 82.81  ? 63  LYS E CA     1 
ATOM   11917 C C      . LYS E 3 63  ? 8.117   79.443  71.271 1.00 83.52  ? 63  LYS E C      1 
ATOM   11918 O O      . LYS E 3 63  ? 8.867   80.393  71.195 1.00 84.16  ? 63  LYS E O      1 
ATOM   11919 C CB     . LYS E 3 63  ? 5.708   79.689  71.366 1.00 82.01  ? 63  LYS E CB     1 
ATOM   11920 C CG     . LYS E 3 63  ? 5.849   80.956  72.198 1.00 89.73  ? 63  LYS E CG     1 
ATOM   11921 C CD     . LYS E 3 63  ? 4.993   80.898  73.452 1.00 89.34  ? 63  LYS E CD     1 
ATOM   11922 C CE     . LYS E 3 63  ? 3.526   81.133  73.147 1.00 83.35  ? 63  LYS E CE     1 
ATOM   11923 N NZ     . LYS E 3 63  ? 3.247   82.570  72.880 1.00 92.81  ? 63  LYS E NZ     1 
ATOM   11924 N N      . GLU E 3 64  ? 8.370   78.435  72.057 1.00 84.98  ? 64  GLU E N      1 
ATOM   11925 C CA     . GLU E 3 64  ? 9.601   78.507  72.766 1.00 90.99  ? 64  GLU E CA     1 
ATOM   11926 C C      . GLU E 3 64  ? 10.220  77.274  72.339 1.00 85.53  ? 64  GLU E C      1 
ATOM   11927 O O      . GLU E 3 64  ? 9.714   76.197  72.594 1.00 87.21  ? 64  GLU E O      1 
ATOM   11928 C CB     . GLU E 3 64  ? 9.414   78.470  74.273 1.00 98.45  ? 64  GLU E CB     1 
ATOM   11929 C CG     . GLU E 3 64  ? 8.222   79.242  74.828 1.00 91.99  ? 64  GLU E CG     1 
ATOM   11930 C CD     . GLU E 3 64  ? 8.427   80.748  74.907 1.00 88.99  ? 64  GLU E CD     1 
ATOM   11931 O OE1    . GLU E 3 64  ? 7.898   81.364  75.853 1.00 93.17  ? 64  GLU E OE1    1 
ATOM   11932 O OE2    . GLU E 3 64  ? 9.101   81.325  74.033 1.00 84.37  ? 64  GLU E OE2    1 
ATOM   11933 N N      . SER E 3 65  ? 11.316  77.401  71.652 1.00 80.40  ? 65  SER E N      1 
ATOM   11934 C CA     . SER E 3 65  ? 12.006  76.232  71.304 1.00 85.76  ? 65  SER E CA     1 
ATOM   11935 C C      . SER E 3 65  ? 13.369  76.631  71.706 1.00 83.35  ? 65  SER E C      1 
ATOM   11936 O O      . SER E 3 65  ? 13.850  77.667  71.286 1.00 76.19  ? 65  SER E O      1 
ATOM   11937 C CB     . SER E 3 65  ? 11.882  75.989  69.821 1.00 78.40  ? 65  SER E CB     1 
ATOM   11938 O OG     . SER E 3 65  ? 10.546  75.693  69.478 1.00 84.97  ? 65  SER E OG     1 
ATOM   11939 N N      . THR E 3 66  ? 14.002  75.837  72.549 1.00 80.17  ? 66  THR E N      1 
ATOM   11940 C CA     . THR E 3 66  ? 15.354  76.143  72.880 1.00 71.00  ? 66  THR E CA     1 
ATOM   11941 C C      . THR E 3 66  ? 16.145  75.337  71.920 1.00 64.69  ? 66  THR E C      1 
ATOM   11942 O O      . THR E 3 66  ? 16.354  74.157  72.109 1.00 64.67  ? 66  THR E O      1 
ATOM   11943 C CB     . THR E 3 66  ? 15.670  75.820  74.329 1.00 62.94  ? 66  THR E CB     1 
ATOM   11944 O OG1    . THR E 3 66  ? 14.791  74.783  74.773 1.00 77.67  ? 66  THR E OG1    1 
ATOM   11945 C CG2    . THR E 3 66  ? 15.438  77.032  75.190 1.00 57.58  ? 66  THR E CG2    1 
ATOM   11946 N N      . LEU E 3 67  ? 16.566  75.977  70.853 1.00 63.82  ? 67  LEU E N      1 
ATOM   11947 C CA     . LEU E 3 67  ? 17.394  75.308  69.908 1.00 61.58  ? 67  LEU E CA     1 
ATOM   11948 C C      . LEU E 3 67  ? 18.763  75.532  70.510 1.00 63.80  ? 67  LEU E C      1 
ATOM   11949 O O      . LEU E 3 67  ? 18.965  76.518  71.178 1.00 58.40  ? 67  LEU E O      1 
ATOM   11950 C CB     . LEU E 3 67  ? 17.231  75.906  68.523 1.00 48.01  ? 67  LEU E CB     1 
ATOM   11951 C CG     . LEU E 3 67  ? 15.942  75.807  67.734 1.00 52.17  ? 67  LEU E CG     1 
ATOM   11952 C CD1    . LEU E 3 67  ? 14.963  76.831  68.255 1.00 69.98  ? 67  LEU E CD1    1 
ATOM   11953 C CD2    . LEU E 3 67  ? 16.278  76.157  66.303 1.00 59.59  ? 67  LEU E CD2    1 
ATOM   11954 N N      . HIS E 3 68  ? 19.701  74.630  70.305 1.00 62.93  ? 68  HIS E N      1 
ATOM   11955 C CA     . HIS E 3 68  ? 21.005  74.707  70.966 1.00 54.52  ? 68  HIS E CA     1 
ATOM   11956 C C      . HIS E 3 68  ? 22.051  74.974  69.943 1.00 50.68  ? 68  HIS E C      1 
ATOM   11957 O O      . HIS E 3 68  ? 21.890  74.583  68.805 1.00 54.89  ? 68  HIS E O      1 
ATOM   11958 C CB     . HIS E 3 68  ? 21.330  73.394  71.660 1.00 54.47  ? 68  HIS E CB     1 
ATOM   11959 C CG     . HIS E 3 68  ? 20.744  73.261  73.026 1.00 53.75  ? 68  HIS E CG     1 
ATOM   11960 N ND1    . HIS E 3 68  ? 19.446  72.858  73.243 1.00 53.93  ? 68  HIS E ND1    1 
ATOM   11961 C CD2    . HIS E 3 68  ? 21.289  73.454  74.249 1.00 54.59  ? 68  HIS E CD2    1 
ATOM   11962 C CE1    . HIS E 3 68  ? 19.210  72.825  74.542 1.00 51.82  ? 68  HIS E CE1    1 
ATOM   11963 N NE2    . HIS E 3 68  ? 20.313  73.182  75.175 1.00 53.72  ? 68  HIS E NE2    1 
ATOM   11964 N N      . LEU E 3 69  ? 23.156  75.599  70.321 1.00 47.11  ? 69  LEU E N      1 
ATOM   11965 C CA     . LEU E 3 69  ? 24.141  75.997  69.322 1.00 53.64  ? 69  LEU E CA     1 
ATOM   11966 C C      . LEU E 3 69  ? 25.532  75.484  69.534 1.00 51.88  ? 69  LEU E C      1 
ATOM   11967 O O      . LEU E 3 69  ? 26.181  75.807  70.520 1.00 52.33  ? 69  LEU E O      1 
ATOM   11968 C CB     . LEU E 3 69  ? 24.196  77.519  69.218 1.00 50.54  ? 69  LEU E CB     1 
ATOM   11969 C CG     . LEU E 3 69  ? 25.054  78.188  68.156 1.00 42.23  ? 69  LEU E CG     1 
ATOM   11970 C CD1    . LEU E 3 69  ? 24.551  77.829  66.773 1.00 44.90  ? 69  LEU E CD1    1 
ATOM   11971 C CD2    . LEU E 3 69  ? 25.009  79.688  68.361 1.00 44.88  ? 69  LEU E CD2    1 
ATOM   11972 N N      . VAL E 3 70  ? 25.992  74.661  68.614 1.00 49.75  ? 70  VAL E N      1 
ATOM   11973 C CA     . VAL E 3 70  ? 27.346  74.202  68.695 1.00 53.16  ? 70  VAL E CA     1 
ATOM   11974 C C      . VAL E 3 70  ? 27.958  74.901  67.551 1.00 49.90  ? 70  VAL E C      1 
ATOM   11975 O O      . VAL E 3 70  ? 27.320  75.099  66.541 1.00 54.08  ? 70  VAL E O      1 
ATOM   11976 C CB     . VAL E 3 70  ? 27.467  72.713  68.503 1.00 55.80  ? 70  VAL E CB     1 
ATOM   11977 C CG1    . VAL E 3 70  ? 28.927  72.299  68.486 1.00 54.72  ? 70  VAL E CG1    1 
ATOM   11978 C CG2    . VAL E 3 70  ? 26.725  71.990  69.611 1.00 53.19  ? 70  VAL E CG2    1 
ATOM   11979 N N      . LEU E 3 71  ? 29.184  75.323  67.710 1.00 44.23  ? 71  LEU E N      1 
ATOM   11980 C CA     . LEU E 3 71  ? 29.798  76.074  66.691 1.00 42.13  ? 71  LEU E CA     1 
ATOM   11981 C C      . LEU E 3 71  ? 30.958  75.228  66.420 1.00 40.68  ? 71  LEU E C      1 
ATOM   11982 O O      . LEU E 3 71  ? 31.304  74.390  67.226 1.00 41.25  ? 71  LEU E O      1 
ATOM   11983 C CB     . LEU E 3 71  ? 30.209  77.415  67.244 1.00 45.42  ? 71  LEU E CB     1 
ATOM   11984 C CG     . LEU E 3 71  ? 29.083  78.369  67.611 1.00 48.66  ? 71  LEU E CG     1 
ATOM   11985 C CD1    . LEU E 3 71  ? 29.657  79.676  68.122 1.00 41.45  ? 71  LEU E CD1    1 
ATOM   11986 C CD2    . LEU E 3 71  ? 28.211  78.609  66.395 1.00 54.76  ? 71  LEU E CD2    1 
ATOM   11987 N N      . ARG E 3 72  ? 31.626  75.448  65.327 1.00 43.98  ? 72  ARG E N      1 
ATOM   11988 C CA     . ARG E 3 72  ? 32.666  74.561  64.975 1.00 44.17  ? 72  ARG E CA     1 
ATOM   11989 C C      . ARG E 3 72  ? 34.023  75.120  65.015 1.00 41.26  ? 72  ARG E C      1 
ATOM   11990 O O      . ARG E 3 72  ? 34.330  76.055  64.319 1.00 46.34  ? 72  ARG E O      1 
ATOM   11991 C CB     . ARG E 3 72  ? 32.392  74.060  63.569 1.00 54.18  ? 72  ARG E CB     1 
ATOM   11992 C CG     . ARG E 3 72  ? 31.029  73.435  63.390 1.00 51.40  ? 72  ARG E CG     1 
ATOM   11993 C CD     . ARG E 3 72  ? 31.085  72.378  62.315 1.00 51.24  ? 72  ARG E CD     1 
ATOM   11994 N NE     . ARG E 3 72  ? 31.375  72.937  61.008 1.00 51.46  ? 72  ARG E NE     1 
ATOM   11995 C CZ     . ARG E 3 72  ? 30.446  73.229  60.110 1.00 60.03  ? 72  ARG E CZ     1 
ATOM   11996 N NH1    . ARG E 3 72  ? 29.171  73.018  60.386 1.00 59.65  ? 72  ARG E NH1    1 
ATOM   11997 N NH2    . ARG E 3 72  ? 30.788  73.729  58.935 1.00 63.60  ? 72  ARG E NH2    1 
ATOM   11998 N N      . LEU E 3 73  ? 34.870  74.528  65.815 1.00 47.24  ? 73  LEU E N      1 
ATOM   11999 C CA     . LEU E 3 73  ? 36.236  74.945  65.804 1.00 62.65  ? 73  LEU E CA     1 
ATOM   12000 C C      . LEU E 3 73  ? 36.843  73.995  64.820 1.00 61.15  ? 73  LEU E C      1 
ATOM   12001 O O      . LEU E 3 73  ? 37.136  72.858  65.150 1.00 62.45  ? 73  LEU E O      1 
ATOM   12002 C CB     . LEU E 3 73  ? 36.879  74.770  67.173 1.00 49.77  ? 73  LEU E CB     1 
ATOM   12003 C CG     . LEU E 3 73  ? 36.356  75.553  68.370 1.00 51.41  ? 73  LEU E CG     1 
ATOM   12004 C CD1    . LEU E 3 73  ? 35.052  74.968  68.885 1.00 47.20  ? 73  LEU E CD1    1 
ATOM   12005 C CD2    . LEU E 3 73  ? 37.408  75.524  69.462 1.00 60.74  ? 73  LEU E CD2    1 
ATOM   12006 N N      . ARG E 3 74  ? 37.022  74.448  63.599 1.00 54.30  ? 74  ARG E N      1 
ATOM   12007 C CA     . ARG E 3 74  ? 37.573  73.608  62.584 1.00 58.51  ? 74  ARG E CA     1 
ATOM   12008 C C      . ARG E 3 74  ? 38.844  74.208  62.160 1.00 65.40  ? 74  ARG E C      1 
ATOM   12009 O O      . ARG E 3 74  ? 39.416  73.797  61.164 1.00 77.02  ? 74  ARG E O      1 
ATOM   12010 C CB     . ARG E 3 74  ? 36.645  73.644  61.391 1.00 65.64  ? 74  ARG E CB     1 
ATOM   12011 C CG     . ARG E 3 74  ? 36.928  72.609  60.307 1.00 73.18  ? 74  ARG E CG     1 
ATOM   12012 C CD     . ARG E 3 74  ? 36.059  72.801  59.071 1.00 79.94  ? 74  ARG E CD     1 
ATOM   12013 N NE     . ARG E 3 74  ? 34.790  72.084  59.161 1.00 81.17  ? 74  ARG E NE     1 
ATOM   12014 C CZ     . ARG E 3 74  ? 33.880  72.048  58.193 1.00 78.85  ? 74  ARG E CZ     1 
ATOM   12015 N NH1    . ARG E 3 74  ? 34.094  72.685  57.051 1.00 72.36  ? 74  ARG E NH1    1 
ATOM   12016 N NH2    . ARG E 3 74  ? 32.757  71.369  58.364 1.00 70.90  ? 74  ARG E NH2    1 
ATOM   12017 N N      . GLY E 3 75  ? 39.347  75.168  62.905 1.00 69.91  ? 75  GLY E N      1 
ATOM   12018 C CA     . GLY E 3 75  ? 40.508  75.894  62.420 1.00 79.63  ? 75  GLY E CA     1 
ATOM   12019 C C      . GLY E 3 75  ? 41.767  75.129  62.127 1.00 95.75  ? 75  GLY E C      1 
ATOM   12020 O O      . GLY E 3 75  ? 42.410  75.373  61.113 1.00 89.59  ? 75  GLY E O      1 
ATOM   12021 N N      . GLY E 3 76  ? 42.121  74.200  62.992 1.00 105.79 ? 76  GLY E N      1 
ATOM   12022 C CA     . GLY E 3 76  ? 43.297  73.376  62.798 1.00 95.88  ? 76  GLY E CA     1 
ATOM   12023 C C      . GLY E 3 76  ? 43.139  72.297  63.848 1.00 100.73 ? 76  GLY E C      1 
ATOM   12024 O O      . GLY E 3 76  ? 43.433  72.499  65.029 1.00 87.79  ? 76  GLY E O      1 
ATOM   12025 O OXT    . GLY E 3 76  ? 42.664  71.210  63.559 1.00 106.65 ? 76  GLY E OXT    1 
ATOM   12026 N N      . MET F 3 1   ? -19.512 77.706  13.096 1.00 69.36  ? 1   MET F N      1 
ATOM   12027 C CA     . MET F 3 1   ? -19.199 78.687  12.066 1.00 85.90  ? 1   MET F CA     1 
ATOM   12028 C C      . MET F 3 1   ? -18.001 78.246  11.250 1.00 88.53  ? 1   MET F C      1 
ATOM   12029 O O      . MET F 3 1   ? -17.420 77.217  11.545 1.00 84.96  ? 1   MET F O      1 
ATOM   12030 C CB     . MET F 3 1   ? -18.938 80.059  12.692 1.00 79.05  ? 1   MET F CB     1 
ATOM   12031 C CG     . MET F 3 1   ? -20.181 80.745  13.216 1.00 79.00  ? 1   MET F CG     1 
ATOM   12032 S SD     . MET F 3 1   ? -19.760 82.121  14.288 1.00 83.17  ? 1   MET F SD     1 
ATOM   12033 C CE     . MET F 3 1   ? -18.448 82.877  13.343 1.00 76.19  ? 1   MET F CE     1 
ATOM   12034 N N      . GLN F 3 2   ? -17.649 78.993  10.207 1.00 87.44  ? 2   GLN F N      1 
ATOM   12035 C CA     . GLN F 3 2   ? -16.449 78.679  9.436  1.00 83.97  ? 2   GLN F CA     1 
ATOM   12036 C C      . GLN F 3 2   ? -15.656 79.908  9.071  1.00 82.88  ? 2   GLN F C      1 
ATOM   12037 O O      . GLN F 3 2   ? -15.582 80.272  7.903  1.00 72.87  ? 2   GLN F O      1 
ATOM   12038 C CB     . GLN F 3 2   ? -16.775 77.904  8.169  1.00 75.37  ? 2   GLN F CB     1 
ATOM   12039 C CG     . GLN F 3 2   ? -15.948 76.638  8.015  1.00 82.02  ? 2   GLN F CG     1 
ATOM   12040 C CD     . GLN F 3 2   ? -16.090 75.992  6.653  1.00 73.55  ? 2   GLN F CD     1 
ATOM   12041 O OE1    . GLN F 3 2   ? -16.675 76.565  5.739  1.00 84.19  ? 2   GLN F OE1    1 
ATOM   12042 N NE2    . GLN F 3 2   ? -15.542 74.794  6.509  1.00 59.39  ? 2   GLN F NE2    1 
ATOM   12043 N N      . ILE F 3 3   ? -15.049 80.550  10.068 1.00 81.89  ? 3   ILE F N      1 
ATOM   12044 C CA     . ILE F 3 3   ? -14.189 81.698  9.795  1.00 76.95  ? 3   ILE F CA     1 
ATOM   12045 C C      . ILE F 3 3   ? -12.992 81.293  8.942  1.00 80.31  ? 3   ILE F C      1 
ATOM   12046 O O      . ILE F 3 3   ? -12.591 80.135  8.936  1.00 83.06  ? 3   ILE F O      1 
ATOM   12047 C CB     . ILE F 3 3   ? -13.733 82.391  11.086 1.00 61.35  ? 3   ILE F CB     1 
ATOM   12048 C CG1    . ILE F 3 3   ? -12.607 81.618  11.759 1.00 74.97  ? 3   ILE F CG1    1 
ATOM   12049 C CG2    . ILE F 3 3   ? -14.911 82.575  12.023 1.00 62.75  ? 3   ILE F CG2    1 
ATOM   12050 C CD1    . ILE F 3 3   ? -11.952 82.381  12.882 1.00 76.67  ? 3   ILE F CD1    1 
ATOM   12051 N N      . PHE F 3 4   ? -12.445 82.230  8.188  1.00 70.36  ? 4   PHE F N      1 
ATOM   12052 C CA     . PHE F 3 4   ? -11.291 81.945  7.367  1.00 65.42  ? 4   PHE F CA     1 
ATOM   12053 C C      . PHE F 3 4   ? -10.179 82.840  7.874  1.00 63.69  ? 4   PHE F C      1 
ATOM   12054 O O      . PHE F 3 4   ? -10.434 83.970  8.237  1.00 67.15  ? 4   PHE F O      1 
ATOM   12055 C CB     . PHE F 3 4   ? -11.578 82.310  5.923  1.00 66.03  ? 4   PHE F CB     1 
ATOM   12056 C CG     . PHE F 3 4   ? -12.394 81.305  5.158  1.00 74.54  ? 4   PHE F CG     1 
ATOM   12057 C CD1    . PHE F 3 4   ? -13.249 80.429  5.784  1.00 74.74  ? 4   PHE F CD1    1 
ATOM   12058 C CD2    . PHE F 3 4   ? -12.316 81.274  3.779  1.00 78.19  ? 4   PHE F CD2    1 
ATOM   12059 C CE1    . PHE F 3 4   ? -13.998 79.526  5.059  1.00 78.94  ? 4   PHE F CE1    1 
ATOM   12060 C CE2    . PHE F 3 4   ? -13.059 80.374  3.045  1.00 82.24  ? 4   PHE F CE2    1 
ATOM   12061 C CZ     . PHE F 3 4   ? -13.901 79.494  3.686  1.00 78.03  ? 4   PHE F CZ     1 
ATOM   12062 N N      . VAL F 3 5   ? -8.949  82.357  7.919  1.00 61.36  ? 5   VAL F N      1 
ATOM   12063 C CA     . VAL F 3 5   ? -7.834  83.196  8.325  1.00 59.83  ? 5   VAL F CA     1 
ATOM   12064 C C      . VAL F 3 5   ? -6.745  83.160  7.267  1.00 60.32  ? 5   VAL F C      1 
ATOM   12065 O O      . VAL F 3 5   ? -6.234  82.099  6.951  1.00 57.30  ? 5   VAL F O      1 
ATOM   12066 C CB     . VAL F 3 5   ? -7.284  82.789  9.694  1.00 61.67  ? 5   VAL F CB     1 
ATOM   12067 C CG1    . VAL F 3 5   ? -6.023  83.565  10.014 1.00 59.74  ? 5   VAL F CG1    1 
ATOM   12068 C CG2    . VAL F 3 5   ? -8.322  82.986  10.783 1.00 61.01  ? 5   VAL F CG2    1 
ATOM   12069 N N      . LYS F 3 6   ? -6.382  84.314  6.710  1.00 61.85  ? 6   LYS F N      1 
ATOM   12070 C CA     . LYS F 3 6   ? -5.415  84.365  5.610  1.00 59.38  ? 6   LYS F CA     1 
ATOM   12071 C C      . LYS F 3 6   ? -4.001  84.747  5.920  1.00 61.67  ? 6   LYS F C      1 
ATOM   12072 O O      . LYS F 3 6   ? -3.739  85.845  6.380  1.00 64.41  ? 6   LYS F O      1 
ATOM   12073 C CB     . LYS F 3 6   ? -5.897  85.331  4.544  1.00 59.26  ? 6   LYS F CB     1 
ATOM   12074 C CG     . LYS F 3 6   ? -7.035  84.814  3.692  1.00 70.76  ? 6   LYS F CG     1 
ATOM   12075 C CD     . LYS F 3 6   ? -6.859  85.241  2.244  1.00 76.47  ? 6   LYS F CD     1 
ATOM   12076 C CE     . LYS F 3 6   ? -6.549  86.724  2.137  1.00 71.81  ? 6   LYS F CE     1 
ATOM   12077 N NZ     . LYS F 3 6   ? -6.439  87.167  0.722  1.00 59.84  ? 6   LYS F NZ     1 
ATOM   12078 N N      . THR F 3 7   ? -3.067  83.865  5.626  1.00 62.15  ? 7   THR F N      1 
ATOM   12079 C CA     . THR F 3 7   ? -1.684  84.172  5.828  1.00 57.52  ? 7   THR F CA     1 
ATOM   12080 C C      . THR F 3 7   ? -1.303  85.027  4.687  1.00 60.58  ? 7   THR F C      1 
ATOM   12081 O O      . THR F 3 7   ? -2.025  85.124  3.713  1.00 63.62  ? 7   THR F O      1 
ATOM   12082 C CB     . THR F 3 7   ? -0.836  82.927  5.761  1.00 58.95  ? 7   THR F CB     1 
ATOM   12083 O OG1    . THR F 3 7   ? -0.960  82.344  4.462  1.00 65.29  ? 7   THR F OG1    1 
ATOM   12084 C CG2    . THR F 3 7   ? -1.294  81.928  6.799  1.00 62.53  ? 7   THR F CG2    1 
ATOM   12085 N N      . LEU F 3 8   ? -0.145  85.646  4.771  1.00 58.75  ? 8   LEU F N      1 
ATOM   12086 C CA     . LEU F 3 8   ? 0.265   86.582  3.745  1.00 62.28  ? 8   LEU F CA     1 
ATOM   12087 C C      . LEU F 3 8   ? 0.577   85.916  2.411  1.00 62.76  ? 8   LEU F C      1 
ATOM   12088 O O      . LEU F 3 8   ? 0.519   86.565  1.377  1.00 63.45  ? 8   LEU F O      1 
ATOM   12089 C CB     . LEU F 3 8   ? 1.447   87.418  4.239  1.00 55.78  ? 8   LEU F CB     1 
ATOM   12090 C CG     . LEU F 3 8   ? 1.368   88.177  5.567  1.00 49.09  ? 8   LEU F CG     1 
ATOM   12091 C CD1    . LEU F 3 8   ? 1.794   87.307  6.740  1.00 56.77  ? 8   LEU F CD1    1 
ATOM   12092 C CD2    . LEU F 3 8   ? 2.280   89.387  5.491  1.00 52.25  ? 8   LEU F CD2    1 
ATOM   12093 N N      . THR F 3 9   ? 0.872   84.623  2.407  1.00 59.08  ? 9   THR F N      1 
ATOM   12094 C CA     . THR F 3 9   ? 1.090   83.914  1.157  1.00 53.95  ? 9   THR F CA     1 
ATOM   12095 C C      . THR F 3 9   ? -0.234  83.733  0.511  1.00 59.24  ? 9   THR F C      1 
ATOM   12096 O O      . THR F 3 9   ? -0.330  83.163  -0.566 1.00 59.75  ? 9   THR F O      1 
ATOM   12097 C CB     . THR F 3 9   ? 1.628   82.523  1.398  1.00 59.05  ? 9   THR F CB     1 
ATOM   12098 O OG1    . THR F 3 9   ? 1.027   81.983  2.575  1.00 59.81  ? 9   THR F OG1    1 
ATOM   12099 C CG2    . THR F 3 9   ? 3.103   82.569  1.591  1.00 60.26  ? 9   THR F CG2    1 
ATOM   12100 N N      . GLY F 3 10  ? -1.289  84.152  1.187  1.00 60.08  ? 10  GLY F N      1 
ATOM   12101 C CA     . GLY F 3 10  ? -2.613  84.081  0.607  1.00 57.94  ? 10  GLY F CA     1 
ATOM   12102 C C      . GLY F 3 10  ? -3.403  82.858  0.950  1.00 59.46  ? 10  GLY F C      1 
ATOM   12103 O O      . GLY F 3 10  ? -4.607  82.819  0.761  1.00 59.65  ? 10  GLY F O      1 
ATOM   12104 N N      . LYS F 3 11  ? -2.734  81.852  1.466  1.00 62.28  ? 11  LYS F N      1 
ATOM   12105 C CA     . LYS F 3 11  ? -3.414  80.626  1.808  1.00 63.37  ? 11  LYS F CA     1 
ATOM   12106 C C      . LYS F 3 11  ? -4.361  80.869  2.950  1.00 64.00  ? 11  LYS F C      1 
ATOM   12107 O O      . LYS F 3 11  ? -4.120  81.724  3.783  1.00 65.90  ? 11  LYS F O      1 
ATOM   12108 C CB     . LYS F 3 11  ? -2.404  79.551  2.167  1.00 62.53  ? 11  LYS F CB     1 
ATOM   12109 C CG     . LYS F 3 11  ? -1.379  79.302  1.074  1.00 56.49  ? 11  LYS F CG     1 
ATOM   12110 C CD     . LYS F 3 11  ? -0.097  78.712  1.636  1.00 62.52  ? 11  LYS F CD     1 
ATOM   12111 C CE     . LYS F 3 11  ? 1.003   78.699  0.588  1.00 55.67  ? 11  LYS F CE     1 
ATOM   12112 N NZ     . LYS F 3 11  ? 2.342   78.468  1.194  1.00 57.11  ? 11  LYS F NZ     1 
ATOM   12113 N N      . THR F 3 12  ? -5.458  80.138  2.986  1.00 63.14  ? 12  THR F N      1 
ATOM   12114 C CA     . THR F 3 12  ? -6.433  80.351  4.026  1.00 63.24  ? 12  THR F CA     1 
ATOM   12115 C C      . THR F 3 12  ? -6.453  79.174  4.935  1.00 68.91  ? 12  THR F C      1 
ATOM   12116 O O      . THR F 3 12  ? -6.288  78.045  4.487  1.00 68.33  ? 12  THR F O      1 
ATOM   12117 C CB     . THR F 3 12  ? -7.843  80.471  3.461  1.00 63.88  ? 12  THR F CB     1 
ATOM   12118 O OG1    . THR F 3 12  ? -8.331  79.173  3.108  1.00 77.50  ? 12  THR F OG1    1 
ATOM   12119 C CG2    . THR F 3 12  ? -7.858  81.361  2.234  1.00 68.97  ? 12  THR F CG2    1 
ATOM   12120 N N      . ILE F 3 13  ? -6.610  79.407  6.226  1.00 67.14  ? 13  ILE F N      1 
ATOM   12121 C CA     . ILE F 3 13  ? -6.753  78.294  7.123  1.00 59.50  ? 13  ILE F CA     1 
ATOM   12122 C C      . ILE F 3 13  ? -8.182  78.402  7.515  1.00 62.30  ? 13  ILE F C      1 
ATOM   12123 O O      . ILE F 3 13  ? -8.664  79.478  7.819  1.00 70.72  ? 13  ILE F O      1 
ATOM   12124 C CB     . ILE F 3 13  ? -5.763  78.330  8.287  1.00 59.40  ? 13  ILE F CB     1 
ATOM   12125 C CG1    . ILE F 3 13  ? -5.954  79.544  9.184  1.00 64.05  ? 13  ILE F CG1    1 
ATOM   12126 C CG2    . ILE F 3 13  ? -4.338  78.322  7.757  1.00 60.93  ? 13  ILE F CG2    1 
ATOM   12127 C CD1    . ILE F 3 13  ? -4.896  79.662  10.255 1.00 63.33  ? 13  ILE F CD1    1 
ATOM   12128 N N      . THR F 3 14  ? -8.905  77.305  7.417  1.00 60.56  ? 14  THR F N      1 
ATOM   12129 C CA     . THR F 3 14  ? -10.326 77.351  7.686  1.00 63.53  ? 14  THR F CA     1 
ATOM   12130 C C      . THR F 3 14  ? -10.568 76.820  9.056  1.00 59.91  ? 14  THR F C      1 
ATOM   12131 O O      . THR F 3 14  ? -10.305 75.664  9.338  1.00 64.88  ? 14  THR F O      1 
ATOM   12132 C CB     . THR F 3 14  ? -11.110 76.553  6.649  1.00 69.88  ? 14  THR F CB     1 
ATOM   12133 O OG1    . THR F 3 14  ? -10.857 77.087  5.343  1.00 71.14  ? 14  THR F OG1    1 
ATOM   12134 C CG2    . THR F 3 14  ? -12.574 76.641  6.928  1.00 69.37  ? 14  THR F CG2    1 
ATOM   12135 N N      . LEU F 3 15  ? -11.009 77.687  9.936  1.00 57.75  ? 15  LEU F N      1 
ATOM   12136 C CA     . LEU F 3 15  ? -11.206 77.284  11.289 1.00 59.34  ? 15  LEU F CA     1 
ATOM   12137 C C      . LEU F 3 15  ? -12.683 77.325  11.532 1.00 70.89  ? 15  LEU F C      1 
ATOM   12138 O O      . LEU F 3 15  ? -13.396 78.035  10.850 1.00 72.10  ? 15  LEU F O      1 
ATOM   12139 C CB     . LEU F 3 15  ? -10.485 78.230  12.222 1.00 49.73  ? 15  LEU F CB     1 
ATOM   12140 C CG     . LEU F 3 15  ? -9.316  77.669  13.008 1.00 57.96  ? 15  LEU F CG     1 
ATOM   12141 C CD1    . LEU F 3 15  ? -8.107  77.535  12.101 1.00 55.14  ? 15  LEU F CD1    1 
ATOM   12142 C CD2    . LEU F 3 15  ? -9.034  78.632  14.144 1.00 63.49  ? 15  LEU F CD2    1 
ATOM   12143 N N      . GLU F 3 16  ? -13.153 76.537  12.483 1.00 77.99  ? 16  GLU F N      1 
ATOM   12144 C CA     . GLU F 3 16  ? -14.558 76.502  12.812 1.00 74.86  ? 16  GLU F CA     1 
ATOM   12145 C C      . GLU F 3 16  ? -14.692 76.772  14.273 1.00 67.20  ? 16  GLU F C      1 
ATOM   12146 O O      . GLU F 3 16  ? -14.105 76.065  15.081 1.00 66.21  ? 16  GLU F O      1 
ATOM   12147 C CB     . GLU F 3 16  ? -15.130 75.131  12.515 1.00 83.39  ? 16  GLU F CB     1 
ATOM   12148 C CG     . GLU F 3 16  ? -14.920 74.629  11.097 1.00 80.99  ? 16  GLU F CG     1 
ATOM   12149 C CD     . GLU F 3 16  ? -15.760 73.402  10.798 1.00 91.43  ? 16  GLU F CD     1 
ATOM   12150 O OE1    . GLU F 3 16  ? -16.878 73.302  11.343 1.00 84.35  ? 16  GLU F OE1    1 
ATOM   12151 O OE2    . GLU F 3 16  ? -15.300 72.532  10.030 1.00 90.63  ? 16  GLU F OE2    1 
ATOM   12152 N N      . VAL F 3 17  ? -15.512 77.740  14.617 1.00 66.81  ? 17  VAL F N      1 
ATOM   12153 C CA     . VAL F 3 17  ? -15.556 78.172  15.978 1.00 67.78  ? 17  VAL F CA     1 
ATOM   12154 C C      . VAL F 3 17  ? -16.961 78.615  16.231 1.00 69.28  ? 17  VAL F C      1 
ATOM   12155 O O      . VAL F 3 17  ? -17.800 78.490  15.357 1.00 74.53  ? 17  VAL F O      1 
ATOM   12156 C CB     . VAL F 3 17  ? -14.578 79.345  16.028 1.00 72.07  ? 17  VAL F CB     1 
ATOM   12157 C CG1    . VAL F 3 17  ? -15.090 80.546  15.272 1.00 85.25  ? 17  VAL F CG1    1 
ATOM   12158 C CG2    . VAL F 3 17  ? -13.987 79.629  17.385 1.00 77.80  ? 17  VAL F CG2    1 
ATOM   12159 N N      . GLU F 3 18  ? -17.243 79.109  17.425 1.00 70.02  ? 18  GLU F N      1 
ATOM   12160 C CA     . GLU F 3 18  ? -18.560 79.567  17.761 1.00 78.71  ? 18  GLU F CA     1 
ATOM   12161 C C      . GLU F 3 18  ? -18.360 81.005  18.194 1.00 82.15  ? 18  GLU F C      1 
ATOM   12162 O O      . GLU F 3 18  ? -17.260 81.394  18.552 1.00 82.29  ? 18  GLU F O      1 
ATOM   12163 C CB     . GLU F 3 18  ? -19.137 78.706  18.879 1.00 76.48  ? 18  GLU F CB     1 
ATOM   12164 C CG     . GLU F 3 18  ? -19.473 77.288  18.460 1.00 74.60  ? 18  GLU F CG     1 
ATOM   12165 C CD     . GLU F 3 18  ? -20.626 77.236  17.482 1.00 79.72  ? 18  GLU F CD     1 
ATOM   12166 O OE1    . GLU F 3 18  ? -21.693 77.800  17.794 1.00 81.91  ? 18  GLU F OE1    1 
ATOM   12167 O OE2    . GLU F 3 18  ? -20.469 76.622  16.409 1.00 84.79  ? 18  GLU F OE2    1 
ATOM   12168 N N      . PRO F 3 19  ? -19.429 81.843  18.144 1.00 79.18  ? 19  PRO F N      1 
ATOM   12169 C CA     . PRO F 3 19  ? -19.124 83.227  18.498 1.00 76.14  ? 19  PRO F CA     1 
ATOM   12170 C C      . PRO F 3 19  ? -19.003 83.376  19.977 1.00 80.27  ? 19  PRO F C      1 
ATOM   12171 O O      . PRO F 3 19  ? -18.882 84.485  20.486 1.00 82.87  ? 19  PRO F O      1 
ATOM   12172 C CB     . PRO F 3 19  ? -20.340 83.977  18.001 1.00 75.72  ? 19  PRO F CB     1 
ATOM   12173 C CG     . PRO F 3 19  ? -21.453 83.020  18.196 1.00 77.37  ? 19  PRO F CG     1 
ATOM   12174 C CD     . PRO F 3 19  ? -20.873 81.687  17.836 1.00 78.47  ? 19  PRO F CD     1 
ATOM   12175 N N      . SER F 3 20  ? -19.049 82.254  20.672 1.00 76.93  ? 20  SER F N      1 
ATOM   12176 C CA     . SER F 3 20  ? -18.946 82.275  22.109 1.00 77.10  ? 20  SER F CA     1 
ATOM   12177 C C      . SER F 3 20  ? -17.505 82.020  22.447 1.00 81.02  ? 20  SER F C      1 
ATOM   12178 O O      . SER F 3 20  ? -17.188 81.640  23.567 1.00 80.11  ? 20  SER F O      1 
ATOM   12179 C CB     . SER F 3 20  ? -19.822 81.177  22.685 1.00 68.96  ? 20  SER F CB     1 
ATOM   12180 O OG     . SER F 3 20  ? -21.129 81.235  22.147 1.00 66.21  ? 20  SER F OG     1 
ATOM   12181 N N      . ASP F 3 21  ? -16.616 82.230  21.481 1.00 83.06  ? 21  ASP F N      1 
ATOM   12182 C CA     . ASP F 3 21  ? -15.200 81.931  21.687 1.00 83.22  ? 21  ASP F CA     1 
ATOM   12183 C C      . ASP F 3 21  ? -14.258 83.115  21.702 1.00 87.82  ? 21  ASP F C      1 
ATOM   12184 O O      . ASP F 3 21  ? -14.255 83.923  20.786 1.00 87.41  ? 21  ASP F O      1 
ATOM   12185 C CB     . ASP F 3 21  ? -14.724 80.936  20.641 1.00 83.43  ? 21  ASP F CB     1 
ATOM   12186 C CG     . ASP F 3 21  ? -15.299 79.551  20.847 1.00 86.93  ? 21  ASP F CG     1 
ATOM   12187 O OD1    . ASP F 3 21  ? -15.557 79.180  22.008 1.00 86.44  ? 21  ASP F OD1    1 
ATOM   12188 O OD2    . ASP F 3 21  ? -15.480 78.824  19.853 1.00 88.95  ? 21  ASP F OD2    1 
ATOM   12189 N N      . THR F 3 22  ? -13.445 83.209  22.745 1.00 95.79  ? 22  THR F N      1 
ATOM   12190 C CA     . THR F 3 22  ? -12.483 84.286  22.848 1.00 90.25  ? 22  THR F CA     1 
ATOM   12191 C C      . THR F 3 22  ? -11.485 84.155  21.745 1.00 89.09  ? 22  THR F C      1 
ATOM   12192 O O      . THR F 3 22  ? -11.258 83.072  21.229 1.00 89.75  ? 22  THR F O      1 
ATOM   12193 C CB     . THR F 3 22  ? -11.713 84.230  24.176 1.00 81.80  ? 22  THR F CB     1 
ATOM   12194 O OG1    . THR F 3 22  ? -11.065 82.961  24.302 1.00 83.69  ? 22  THR F OG1    1 
ATOM   12195 C CG2    . THR F 3 22  ? -12.655 84.422  25.337 1.00 80.26  ? 22  THR F CG2    1 
ATOM   12196 N N      . ILE F 3 23  ? -10.901 85.270  21.352 1.00 87.72  ? 23  ILE F N      1 
ATOM   12197 C CA     . ILE F 3 23  ? -9.884  85.229  20.336 1.00 87.37  ? 23  ILE F CA     1 
ATOM   12198 C C      . ILE F 3 23  ? -8.769  84.385  20.895 1.00 85.73  ? 23  ILE F C      1 
ATOM   12199 O O      . ILE F 3 23  ? -8.054  83.780  20.163 1.00 84.91  ? 23  ILE F O      1 
ATOM   12200 C CB     . ILE F 3 23  ? -9.372  86.635  19.987 1.00 83.41  ? 23  ILE F CB     1 
ATOM   12201 C CG1    . ILE F 3 23  ? -10.530 87.547  19.607 1.00 77.99  ? 23  ILE F CG1    1 
ATOM   12202 C CG2    . ILE F 3 23  ? -8.369  86.595  18.845 1.00 77.92  ? 23  ILE F CG2    1 
ATOM   12203 C CD1    . ILE F 3 23  ? -11.153 87.210  18.277 1.00 72.35  ? 23  ILE F CD1    1 
ATOM   12204 N N      . GLU F 3 24  ? -8.635  84.327  22.209 1.00 86.24  ? 24  GLU F N      1 
ATOM   12205 C CA     . GLU F 3 24  ? -7.573  83.553  22.817 1.00 84.09  ? 24  GLU F CA     1 
ATOM   12206 C C      . GLU F 3 24  ? -7.741  82.141  22.350 1.00 81.09  ? 24  GLU F C      1 
ATOM   12207 O O      . GLU F 3 24  ? -6.783  81.499  21.950 1.00 79.32  ? 24  GLU F O      1 
ATOM   12208 C CB     . GLU F 3 24  ? -7.675  83.635  24.324 1.00 88.00  ? 24  GLU F CB     1 
ATOM   12209 C CG     . GLU F 3 24  ? -6.510  83.017  25.078 1.00 104.52 ? 24  GLU F CG     1 
ATOM   12210 C CD     . GLU F 3 24  ? -6.592  83.247  26.578 1.00 108.72 ? 24  GLU F CD     1 
ATOM   12211 O OE1    . GLU F 3 24  ? -6.505  84.417  27.014 1.00 112.29 ? 24  GLU F OE1    1 
ATOM   12212 O OE2    . GLU F 3 24  ? -6.736  82.255  27.327 1.00 92.03  ? 24  GLU F OE2    1 
ATOM   12213 N N      . ASN F 3 25  ? -8.972  81.664  22.338 1.00 81.46  ? 25  ASN F N      1 
ATOM   12214 C CA     . ASN F 3 25  ? -9.247  80.321  21.867 1.00 77.92  ? 25  ASN F CA     1 
ATOM   12215 C C      . ASN F 3 25  ? -8.941  80.250  20.403 1.00 80.17  ? 25  ASN F C      1 
ATOM   12216 O O      . ASN F 3 25  ? -8.242  79.354  19.961 1.00 77.73  ? 25  ASN F O      1 
ATOM   12217 C CB     . ASN F 3 25  ? -10.717 79.981  22.077 1.00 81.92  ? 25  ASN F CB     1 
ATOM   12218 C CG     . ASN F 3 25  ? -11.016 78.515  21.852 1.00 97.47  ? 25  ASN F CG     1 
ATOM   12219 O OD1    . ASN F 3 25  ? -10.144 77.660  22.001 1.00 95.95  ? 25  ASN F OD1    1 
ATOM   12220 N ND2    . ASN F 3 25  ? -12.261 78.213  21.505 1.00 95.34  ? 25  ASN F ND2    1 
ATOM   12221 N N      . VAL F 3 26  ? -9.467  81.194  19.635 1.00 82.84  ? 26  VAL F N      1 
ATOM   12222 C CA     . VAL F 3 26  ? -9.285  81.165  18.191 1.00 80.05  ? 26  VAL F CA     1 
ATOM   12223 C C      . VAL F 3 26  ? -7.827  81.171  17.788 1.00 75.05  ? 26  VAL F C      1 
ATOM   12224 O O      . VAL F 3 26  ? -7.432  80.478  16.870 1.00 67.15  ? 26  VAL F O      1 
ATOM   12225 C CB     . VAL F 3 26  ? -10.013 82.338  17.545 1.00 78.53  ? 26  VAL F CB     1 
ATOM   12226 C CG1    . VAL F 3 26  ? -9.971  82.228  16.033 1.00 76.24  ? 26  VAL F CG1    1 
ATOM   12227 C CG2    . VAL F 3 26  ? -11.450 82.370  18.021 1.00 87.67  ? 26  VAL F CG2    1 
ATOM   12228 N N      . LYS F 3 27  ? -7.012  81.938  18.480 1.00 77.74  ? 27  LYS F N      1 
ATOM   12229 C CA     . LYS F 3 27  ? -5.606  81.956  18.179 1.00 73.61  ? 27  LYS F CA     1 
ATOM   12230 C C      . LYS F 3 27  ? -5.007  80.605  18.483 1.00 73.42  ? 27  LYS F C      1 
ATOM   12231 O O      . LYS F 3 27  ? -4.106  80.153  17.794 1.00 73.54  ? 27  LYS F O      1 
ATOM   12232 C CB     . LYS F 3 27  ? -4.913  83.032  18.994 1.00 74.43  ? 27  LYS F CB     1 
ATOM   12233 C CG     . LYS F 3 27  ? -5.284  84.440  18.579 1.00 67.55  ? 27  LYS F CG     1 
ATOM   12234 C CD     . LYS F 3 27  ? -4.828  85.464  19.597 1.00 65.85  ? 27  LYS F CD     1 
ATOM   12235 C CE     . LYS F 3 27  ? -3.326  85.637  19.565 1.00 71.76  ? 27  LYS F CE     1 
ATOM   12236 N NZ     . LYS F 3 27  ? -2.846  86.607  20.586 1.00 73.48  ? 27  LYS F NZ     1 
ATOM   12237 N N      . ALA F 3 28  ? -5.536  79.927  19.484 1.00 71.57  ? 28  ALA F N      1 
ATOM   12238 C CA     . ALA F 3 28  ? -4.948  78.661  19.881 1.00 66.36  ? 28  ALA F CA     1 
ATOM   12239 C C      . ALA F 3 28  ? -5.352  77.568  18.965 1.00 62.68  ? 28  ALA F C      1 
ATOM   12240 O O      . ALA F 3 28  ? -4.591  76.661  18.702 1.00 64.57  ? 28  ALA F O      1 
ATOM   12241 C CB     . ALA F 3 28  ? -5.374  78.320  21.278 1.00 59.94  ? 28  ALA F CB     1 
ATOM   12242 N N      . LYS F 3 29  ? -6.552  77.646  18.444 1.00 63.25  ? 29  LYS F N      1 
ATOM   12243 C CA     . LYS F 3 29  ? -7.014  76.571  17.618 1.00 63.24  ? 29  LYS F CA     1 
ATOM   12244 C C      . LYS F 3 29  ? -6.179  76.646  16.389 1.00 62.71  ? 29  LYS F C      1 
ATOM   12245 O O      . LYS F 3 29  ? -5.972  75.652  15.715 1.00 64.46  ? 29  LYS F O      1 
ATOM   12246 C CB     . LYS F 3 29  ? -8.488  76.722  17.303 1.00 59.19  ? 29  LYS F CB     1 
ATOM   12247 C CG     . LYS F 3 29  ? -9.410  76.233  18.401 1.00 65.26  ? 29  LYS F CG     1 
ATOM   12248 C CD     . LYS F 3 29  ? -9.197  74.750  18.648 1.00 70.37  ? 29  LYS F CD     1 
ATOM   12249 C CE     . LYS F 3 29  ? -10.284 74.171  19.537 1.00 71.83  ? 29  LYS F CE     1 
ATOM   12250 N NZ     . LYS F 3 29  ? -10.174 72.691  19.649 1.00 61.81  ? 29  LYS F NZ     1 
ATOM   12251 N N      . ILE F 3 30  ? -5.639  77.816  16.121 1.00 62.55  ? 30  ILE F N      1 
ATOM   12252 C CA     . ILE F 3 30  ? -4.823  77.984  14.942 1.00 64.82  ? 30  ILE F CA     1 
ATOM   12253 C C      . ILE F 3 30  ? -3.551  77.238  15.206 1.00 66.26  ? 30  ILE F C      1 
ATOM   12254 O O      . ILE F 3 30  ? -3.017  76.579  14.332 1.00 67.85  ? 30  ILE F O      1 
ATOM   12255 C CB     . ILE F 3 30  ? -4.537  79.465  14.634 1.00 63.53  ? 30  ILE F CB     1 
ATOM   12256 C CG1    . ILE F 3 30  ? -5.784  80.149  14.097 1.00 57.01  ? 30  ILE F CG1    1 
ATOM   12257 C CG2    . ILE F 3 30  ? -3.411  79.615  13.628 1.00 63.03  ? 30  ILE F CG2    1 
ATOM   12258 C CD1    . ILE F 3 30  ? -5.574  81.606  13.780 1.00 60.31  ? 30  ILE F CD1    1 
ATOM   12259 N N      . GLN F 3 31  ? -3.082  77.317  16.441 1.00 65.66  ? 31  GLN F N      1 
ATOM   12260 C CA     . GLN F 3 31  ? -1.843  76.649  16.808 1.00 68.19  ? 31  GLN F CA     1 
ATOM   12261 C C      . GLN F 3 31  ? -1.995  75.170  16.649 1.00 67.66  ? 31  GLN F C      1 
ATOM   12262 O O      . GLN F 3 31  ? -1.122  74.494  16.143 1.00 70.38  ? 31  GLN F O      1 
ATOM   12263 C CB     . GLN F 3 31  ? -1.485  76.951  18.260 1.00 66.98  ? 31  GLN F CB     1 
ATOM   12264 C CG     . GLN F 3 31  ? -0.200  76.319  18.760 1.00 57.88  ? 31  GLN F CG     1 
ATOM   12265 C CD     . GLN F 3 31  ? 0.037   76.593  20.226 1.00 52.09  ? 31  GLN F CD     1 
ATOM   12266 O OE1    . GLN F 3 31  ? -0.903  76.798  20.987 1.00 48.98  ? 31  GLN F OE1    1 
ATOM   12267 N NE2    . GLN F 3 31  ? 1.296   76.590  20.634 1.00 46.07  ? 31  GLN F NE2    1 
ATOM   12268 N N      . ASP F 3 32  ? -3.112  74.639  17.089 1.00 71.08  ? 32  ASP F N      1 
ATOM   12269 C CA     . ASP F 3 32  ? -3.294  73.209  17.014 1.00 78.37  ? 32  ASP F CA     1 
ATOM   12270 C C      . ASP F 3 32  ? -3.168  72.795  15.575 1.00 75.00  ? 32  ASP F C      1 
ATOM   12271 O O      . ASP F 3 32  ? -2.452  71.862  15.261 1.00 79.26  ? 32  ASP F O      1 
ATOM   12272 C CB     . ASP F 3 32  ? -4.650  72.805  17.580 1.00 82.15  ? 32  ASP F CB     1 
ATOM   12273 C CG     . ASP F 3 32  ? -4.788  73.133  19.057 1.00 88.91  ? 32  ASP F CG     1 
ATOM   12274 O OD1    . ASP F 3 32  ? -3.764  73.445  19.698 1.00 91.26  ? 32  ASP F OD1    1 
ATOM   12275 O OD2    . ASP F 3 32  ? -5.920  73.070  19.580 1.00 85.38  ? 32  ASP F OD2    1 
ATOM   12276 N N      . LYS F 3 33  ? -3.798  73.528  14.685 1.00 59.39  ? 33  LYS F N      1 
ATOM   12277 C CA     . LYS F 3 33  ? -3.742  73.184  13.290 1.00 61.75  ? 33  LYS F CA     1 
ATOM   12278 C C      . LYS F 3 33  ? -2.375  73.435  12.674 1.00 63.62  ? 33  LYS F C      1 
ATOM   12279 O O      . LYS F 3 33  ? -1.801  72.538  12.065 1.00 65.73  ? 33  LYS F O      1 
ATOM   12280 C CB     . LYS F 3 33  ? -4.810  73.956  12.528 1.00 65.84  ? 33  LYS F CB     1 
ATOM   12281 C CG     . LYS F 3 33  ? -5.113  73.401  11.149 1.00 62.30  ? 33  LYS F CG     1 
ATOM   12282 C CD     . LYS F 3 33  ? -6.104  74.279  10.409 1.00 60.27  ? 33  LYS F CD     1 
ATOM   12283 C CE     . LYS F 3 33  ? -6.432  73.694  9.047  1.00 66.67  ? 33  LYS F CE     1 
ATOM   12284 N NZ     . LYS F 3 33  ? -5.207  73.393  8.258  1.00 63.78  ? 33  LYS F NZ     1 
ATOM   12285 N N      . GLU F 3 34  ? -1.829  74.638  12.814 1.00 66.77  ? 34  GLU F N      1 
ATOM   12286 C CA     . GLU F 3 34  ? -0.573  74.972  12.119 1.00 64.89  ? 34  GLU F CA     1 
ATOM   12287 C C      . GLU F 3 34  ? 0.705   75.110  12.931 1.00 59.87  ? 34  GLU F C      1 
ATOM   12288 O O      . GLU F 3 34  ? 1.763   75.290  12.361 1.00 56.97  ? 34  GLU F O      1 
ATOM   12289 C CB     . GLU F 3 34  ? -0.776  76.231  11.279 1.00 62.23  ? 34  GLU F CB     1 
ATOM   12290 C CG     . GLU F 3 34  ? -2.053  76.248  10.468 1.00 58.53  ? 34  GLU F CG     1 
ATOM   12291 C CD     . GLU F 3 34  ? -1.851  75.711  9.075  1.00 60.98  ? 34  GLU F CD     1 
ATOM   12292 O OE1    . GLU F 3 34  ? -0.700  75.713  8.602  1.00 58.51  ? 34  GLU F OE1    1 
ATOM   12293 O OE2    . GLU F 3 34  ? -2.844  75.300  8.446  1.00 72.23  ? 34  GLU F OE2    1 
ATOM   12294 N N      . GLY F 3 35  ? 0.627   75.045  14.243 1.00 59.88  ? 35  GLY F N      1 
ATOM   12295 C CA     . GLY F 3 35  ? 1.831   75.066  15.048 1.00 58.50  ? 35  GLY F CA     1 
ATOM   12296 C C      . GLY F 3 35  ? 2.260   76.427  15.483 1.00 62.39  ? 35  GLY F C      1 
ATOM   12297 O O      . GLY F 3 35  ? 3.119   76.559  16.338 1.00 63.58  ? 35  GLY F O      1 
ATOM   12298 N N      . ILE F 3 36  ? 1.668   77.443  14.884 1.00 61.93  ? 36  ILE F N      1 
ATOM   12299 C CA     . ILE F 3 36  ? 2.018   78.808  15.200 1.00 58.96  ? 36  ILE F CA     1 
ATOM   12300 C C      . ILE F 3 36  ? 1.787   79.159  16.651 1.00 58.57  ? 36  ILE F C      1 
ATOM   12301 O O      . ILE F 3 36  ? 0.677   79.072  17.135 1.00 58.33  ? 36  ILE F O      1 
ATOM   12302 C CB     . ILE F 3 36  ? 1.184   79.760  14.348 1.00 55.53  ? 36  ILE F CB     1 
ATOM   12303 C CG1    . ILE F 3 36  ? 1.193   79.316  12.894 1.00 54.20  ? 36  ILE F CG1    1 
ATOM   12304 C CG2    . ILE F 3 36  ? 1.713   81.166  14.481 1.00 57.44  ? 36  ILE F CG2    1 
ATOM   12305 C CD1    . ILE F 3 36  ? 0.242   80.092  12.023 1.00 56.85  ? 36  ILE F CD1    1 
ATOM   12306 N N      . PRO F 3 37  ? 2.866   79.568  17.369 1.00 56.91  ? 37  PRO F N      1 
ATOM   12307 C CA     . PRO F 3 37  ? 2.602   79.996  18.736 1.00 57.46  ? 37  PRO F CA     1 
ATOM   12308 C C      . PRO F 3 37  ? 1.632   81.123  18.821 1.00 53.30  ? 37  PRO F C      1 
ATOM   12309 O O      . PRO F 3 37  ? 1.636   81.997  17.982 1.00 56.43  ? 37  PRO F O      1 
ATOM   12310 C CB     . PRO F 3 37  ? 3.957   80.472  19.205 1.00 55.93  ? 37  PRO F CB     1 
ATOM   12311 C CG     . PRO F 3 37  ? 4.919   79.632  18.462 1.00 61.18  ? 37  PRO F CG     1 
ATOM   12312 C CD     . PRO F 3 37  ? 4.326   79.602  17.097 1.00 54.26  ? 37  PRO F CD     1 
ATOM   12313 N N      . PRO F 3 38  ? 0.813   81.142  19.895 1.00 51.49  ? 38  PRO F N      1 
ATOM   12314 C CA     . PRO F 3 38  ? -0.191  82.184  19.899 1.00 58.72  ? 38  PRO F CA     1 
ATOM   12315 C C      . PRO F 3 38  ? 0.348   83.553  20.276 1.00 62.16  ? 38  PRO F C      1 
ATOM   12316 O O      . PRO F 3 38  ? -0.379  84.531  20.234 1.00 62.11  ? 38  PRO F O      1 
ATOM   12317 C CB     . PRO F 3 38  ? -1.180  81.683  20.954 1.00 52.95  ? 38  PRO F CB     1 
ATOM   12318 C CG     . PRO F 3 38  ? -0.891  80.246  21.146 1.00 48.43  ? 38  PRO F CG     1 
ATOM   12319 C CD     . PRO F 3 38  ? 0.588   80.249  21.054 1.00 56.41  ? 38  PRO F CD     1 
ATOM   12320 N N      . ASP F 3 39  ? 1.613   83.645  20.634 1.00 59.55  ? 39  ASP F N      1 
ATOM   12321 C CA     . ASP F 3 39  ? 2.176   84.915  21.050 1.00 54.42  ? 39  ASP F CA     1 
ATOM   12322 C C      . ASP F 3 39  ? 2.869   85.473  19.870 1.00 53.62  ? 39  ASP F C      1 
ATOM   12323 O O      . ASP F 3 39  ? 3.370   86.581  19.910 1.00 58.18  ? 39  ASP F O      1 
ATOM   12324 C CB     . ASP F 3 39  ? 3.167   84.731  22.185 1.00 65.80  ? 39  ASP F CB     1 
ATOM   12325 C CG     . ASP F 3 39  ? 2.510   84.268  23.475 1.00 71.03  ? 39  ASP F CG     1 
ATOM   12326 O OD1    . ASP F 3 39  ? 1.266   84.170  23.521 1.00 75.16  ? 39  ASP F OD1    1 
ATOM   12327 O OD2    . ASP F 3 39  ? 3.245   84.009  24.450 1.00 54.03  ? 39  ASP F OD2    1 
ATOM   12328 N N      . GLN F 3 40  ? 2.894   84.715  18.795 1.00 55.95  ? 40  GLN F N      1 
ATOM   12329 C CA     . GLN F 3 40  ? 3.479   85.197  17.582 1.00 53.84  ? 40  GLN F CA     1 
ATOM   12330 C C      . GLN F 3 40  ? 2.304   85.793  16.914 1.00 56.73  ? 40  GLN F C      1 
ATOM   12331 O O      . GLN F 3 40  ? 2.419   86.715  16.137 1.00 57.35  ? 40  GLN F O      1 
ATOM   12332 C CB     . GLN F 3 40  ? 3.971   84.029  16.755 1.00 49.11  ? 40  GLN F CB     1 
ATOM   12333 C CG     . GLN F 3 40  ? 4.929   84.404  15.654 1.00 55.55  ? 40  GLN F CG     1 
ATOM   12334 C CD     . GLN F 3 40  ? 5.342   83.217  14.830 1.00 56.24  ? 40  GLN F CD     1 
ATOM   12335 O OE1    . GLN F 3 40  ? 5.118   82.077  15.211 1.00 55.25  ? 40  GLN F OE1    1 
ATOM   12336 N NE2    . GLN F 3 40  ? 5.955   83.479  13.692 1.00 58.25  ? 40  GLN F NE2    1 
ATOM   12337 N N      . GLN F 3 41  ? 1.135   85.300  17.253 1.00 58.03  ? 41  GLN F N      1 
ATOM   12338 C CA     . GLN F 3 41  ? -0.059  85.720  16.549 1.00 56.21  ? 41  GLN F CA     1 
ATOM   12339 C C      . GLN F 3 41  ? -0.680  87.043  16.811 1.00 60.95  ? 41  GLN F C      1 
ATOM   12340 O O      . GLN F 3 41  ? -0.886  87.424  17.949 1.00 63.88  ? 41  GLN F O      1 
ATOM   12341 C CB     . GLN F 3 41  ? -1.144  84.655  16.686 1.00 57.26  ? 41  GLN F CB     1 
ATOM   12342 C CG     . GLN F 3 41  ? -0.757  83.296  16.144 1.00 60.86  ? 41  GLN F CG     1 
ATOM   12343 C CD     . GLN F 3 41  ? -1.919  82.337  16.124 1.00 61.44  ? 41  GLN F CD     1 
ATOM   12344 O OE1    . GLN F 3 41  ? -3.042  82.723  15.835 1.00 65.40  ? 41  GLN F OE1    1 
ATOM   12345 N NE2    . GLN F 3 41  ? -1.653  81.077  16.424 1.00 61.60  ? 41  GLN F NE2    1 
ATOM   12346 N N      . ARG F 3 42  ? -1.044  87.723  15.740 1.00 65.89  ? 42  ARG F N      1 
ATOM   12347 C CA     . ARG F 3 42  ? -1.728  88.989  15.840 1.00 64.76  ? 42  ARG F CA     1 
ATOM   12348 C C      . ARG F 3 42  ? -2.786  88.803  14.807 1.00 68.61  ? 42  ARG F C      1 
ATOM   12349 O O      . ARG F 3 42  ? -2.470  88.498  13.669 1.00 67.13  ? 42  ARG F O      1 
ATOM   12350 C CB     . ARG F 3 42  ? -0.817  90.117  15.398 1.00 63.97  ? 42  ARG F CB     1 
ATOM   12351 C CG     . ARG F 3 42  ? 0.061   90.664  16.503 1.00 67.76  ? 42  ARG F CG     1 
ATOM   12352 C CD     . ARG F 3 42  ? 1.064   91.680  15.996 1.00 69.69  ? 42  ARG F CD     1 
ATOM   12353 N NE     . ARG F 3 42  ? 0.422   92.863  15.446 1.00 94.19  ? 42  ARG F NE     1 
ATOM   12354 C CZ     . ARG F 3 42  ? 1.077   93.957  15.078 1.00 92.32  ? 42  ARG F CZ     1 
ATOM   12355 N NH1    . ARG F 3 42  ? 2.394   94.013  15.216 1.00 85.28  ? 42  ARG F NH1    1 
ATOM   12356 N NH2    . ARG F 3 42  ? 0.418   94.993  14.581 1.00 81.69  ? 42  ARG F NH2    1 
ATOM   12357 N N      . LEU F 3 43  ? -4.044  88.933  15.180 1.00 71.24  ? 43  LEU F N      1 
ATOM   12358 C CA     . LEU F 3 43  ? -5.098  88.661  14.220 1.00 68.63  ? 43  LEU F CA     1 
ATOM   12359 C C      . LEU F 3 43  ? -5.768  89.950  13.930 1.00 66.51  ? 43  LEU F C      1 
ATOM   12360 O O      . LEU F 3 43  ? -6.216  90.623  14.834 1.00 65.21  ? 43  LEU F O      1 
ATOM   12361 C CB     . LEU F 3 43  ? -6.089  87.635  14.748 1.00 67.50  ? 43  LEU F CB     1 
ATOM   12362 C CG     . LEU F 3 43  ? -5.872  86.142  14.511 1.00 58.24  ? 43  LEU F CG     1 
ATOM   12363 C CD1    . LEU F 3 43  ? -6.816  85.347  15.389 1.00 59.80  ? 43  LEU F CD1    1 
ATOM   12364 C CD2    . LEU F 3 43  ? -6.135  85.808  13.060 1.00 63.14  ? 43  LEU F CD2    1 
ATOM   12365 N N      . ILE F 3 44  ? -5.857  90.315  12.665 1.00 66.62  ? 44  ILE F N      1 
ATOM   12366 C CA     . ILE F 3 44  ? -6.389  91.606  12.316 1.00 60.26  ? 44  ILE F CA     1 
ATOM   12367 C C      . ILE F 3 44  ? -7.656  91.487  11.525 1.00 63.71  ? 44  ILE F C      1 
ATOM   12368 O O      . ILE F 3 44  ? -7.665  90.850  10.485 1.00 63.77  ? 44  ILE F O      1 
ATOM   12369 C CB     . ILE F 3 44  ? -5.368  92.343  11.464 1.00 52.33  ? 44  ILE F CB     1 
ATOM   12370 C CG1    . ILE F 3 44  ? -3.966  92.139  12.036 1.00 59.95  ? 44  ILE F CG1    1 
ATOM   12371 C CG2    . ILE F 3 44  ? -5.711  93.818  11.372 1.00 63.10  ? 44  ILE F CG2    1 
ATOM   12372 C CD1    . ILE F 3 44  ? -2.878  92.849  11.270 1.00 61.90  ? 44  ILE F CD1    1 
ATOM   12373 N N      . PHE F 3 45  ? -8.743  92.070  12.011 1.00 65.20  ? 45  PHE F N      1 
ATOM   12374 C CA     . PHE F 3 45  ? -9.996  92.060  11.272 1.00 65.84  ? 45  PHE F CA     1 
ATOM   12375 C C      . PHE F 3 45  ? -10.585 93.432  11.346 1.00 68.49  ? 45  PHE F C      1 
ATOM   12376 O O      . PHE F 3 45  ? -10.569 94.038  12.408 1.00 66.93  ? 45  PHE F O      1 
ATOM   12377 C CB     . PHE F 3 45  ? -10.974 91.066  11.857 1.00 62.19  ? 45  PHE F CB     1 
ATOM   12378 C CG     . PHE F 3 45  ? -12.298 91.021  11.157 1.00 65.35  ? 45  PHE F CG     1 
ATOM   12379 C CD1    . PHE F 3 45  ? -12.382 90.643  9.832  1.00 72.89  ? 45  PHE F CD1    1 
ATOM   12380 C CD2    . PHE F 3 45  ? -13.460 91.330  11.833 1.00 60.51  ? 45  PHE F CD2    1 
ATOM   12381 C CE1    . PHE F 3 45  ? -13.600 90.592  9.186  1.00 71.12  ? 45  PHE F CE1    1 
ATOM   12382 C CE2    . PHE F 3 45  ? -14.681 91.279  11.199 1.00 67.89  ? 45  PHE F CE2    1 
ATOM   12383 C CZ     . PHE F 3 45  ? -14.751 90.910  9.873  1.00 75.21  ? 45  PHE F CZ     1 
ATOM   12384 N N      . ALA F 3 46  ? -11.081 93.934  10.222 1.00 69.26  ? 46  ALA F N      1 
ATOM   12385 C CA     . ALA F 3 46  ? -11.693 95.249  10.171 1.00 68.96  ? 46  ALA F CA     1 
ATOM   12386 C C      . ALA F 3 46  ? -10.764 96.331  10.646 1.00 76.80  ? 46  ALA F C      1 
ATOM   12387 O O      . ALA F 3 46  ? -11.190 97.282  11.285 1.00 81.13  ? 46  ALA F O      1 
ATOM   12388 C CB     . ALA F 3 46  ? -12.982 95.263  10.958 1.00 68.62  ? 46  ALA F CB     1 
ATOM   12389 N N      . GLY F 3 47  ? -9.477  96.181  10.387 1.00 75.41  ? 47  GLY F N      1 
ATOM   12390 C CA     . GLY F 3 47  ? -8.527  97.225  10.732 1.00 63.70  ? 47  GLY F CA     1 
ATOM   12391 C C      . GLY F 3 47  ? -7.896  97.168  12.086 1.00 66.86  ? 47  GLY F C      1 
ATOM   12392 O O      . GLY F 3 47  ? -6.954  97.898  12.339 1.00 75.43  ? 47  GLY F O      1 
ATOM   12393 N N      . LYS F 3 48  ? -8.391  96.313  12.963 1.00 74.52  ? 48  LYS F N      1 
ATOM   12394 C CA     . LYS F 3 48  ? -7.870  96.304  14.319 1.00 77.80  ? 48  LYS F CA     1 
ATOM   12395 C C      . LYS F 3 48  ? -7.271  94.995  14.752 1.00 75.92  ? 48  LYS F C      1 
ATOM   12396 O O      . LYS F 3 48  ? -7.776  93.944  14.392 1.00 75.37  ? 48  LYS F O      1 
ATOM   12397 C CB     . LYS F 3 48  ? -8.977  96.675  15.299 1.00 83.65  ? 48  LYS F CB     1 
ATOM   12398 C CG     . LYS F 3 48  ? -9.639  98.015  15.043 1.00 82.44  ? 48  LYS F CG     1 
ATOM   12399 C CD     . LYS F 3 48  ? -10.804 98.225  15.994 1.00 91.29  ? 48  LYS F CD     1 
ATOM   12400 C CE     . LYS F 3 48  ? -10.352 98.150  17.441 1.00 85.46  ? 48  LYS F CE     1 
ATOM   12401 N NZ     . LYS F 3 48  ? -11.489 98.361  18.380 1.00 71.15  ? 48  LYS F NZ     1 
ATOM   12402 N N      . GLN F 3 49  ? -6.184  95.050  15.516 1.00 71.66  ? 49  GLN F N      1 
ATOM   12403 C CA     . GLN F 3 49  ? -5.597  93.840  16.049 1.00 75.42  ? 49  GLN F CA     1 
ATOM   12404 C C      . GLN F 3 49  ? -6.602  93.411  17.054 1.00 74.41  ? 49  GLN F C      1 
ATOM   12405 O O      . GLN F 3 49  ? -6.877  94.127  18.000 1.00 81.34  ? 49  GLN F O      1 
ATOM   12406 C CB     . GLN F 3 49  ? -4.308  94.108  16.802 1.00 76.80  ? 49  GLN F CB     1 
ATOM   12407 C CG     . GLN F 3 49  ? -3.270  94.943  16.087 1.00 90.74  ? 49  GLN F CG     1 
ATOM   12408 C CD     . GLN F 3 49  ? -2.023  95.104  16.935 1.00 100.49 ? 49  GLN F CD     1 
ATOM   12409 O OE1    . GLN F 3 49  ? -1.624  94.182  17.646 1.00 83.17  ? 49  GLN F OE1    1 
ATOM   12410 N NE2    . GLN F 3 49  ? -1.403  96.276  16.869 1.00 99.66  ? 49  GLN F NE2    1 
ATOM   12411 N N      . LEU F 3 50  ? -7.157  92.234  16.880 1.00 70.33  ? 50  LEU F N      1 
ATOM   12412 C CA     . LEU F 3 50  ? -8.189  91.791  17.764 1.00 67.59  ? 50  LEU F CA     1 
ATOM   12413 C C      . LEU F 3 50  ? -7.609  91.448  19.112 1.00 73.45  ? 50  LEU F C      1 
ATOM   12414 O O      . LEU F 3 50  ? -6.683  90.664  19.210 1.00 70.02  ? 50  LEU F O      1 
ATOM   12415 C CB     . LEU F 3 50  ? -8.866  90.593  17.143 1.00 69.18  ? 50  LEU F CB     1 
ATOM   12416 C CG     . LEU F 3 50  ? -9.338  90.766  15.708 1.00 67.73  ? 50  LEU F CG     1 
ATOM   12417 C CD1    . LEU F 3 50  ? -9.869  89.444  15.210 1.00 63.69  ? 50  LEU F CD1    1 
ATOM   12418 C CD2    . LEU F 3 50  ? -10.396 91.845  15.605 1.00 74.09  ? 50  LEU F CD2    1 
ATOM   12419 N N      . GLU F 3 51  ? -8.160  92.023  20.168 1.00 80.75  ? 51  GLU F N      1 
ATOM   12420 C CA     . GLU F 3 51  ? -7.690  91.726  21.501 1.00 75.63  ? 51  GLU F CA     1 
ATOM   12421 C C      . GLU F 3 51  ? -8.175  90.363  21.823 1.00 79.32  ? 51  GLU F C      1 
ATOM   12422 O O      . GLU F 3 51  ? -9.310  90.026  21.527 1.00 82.83  ? 51  GLU F O      1 
ATOM   12423 C CB     . GLU F 3 51  ? -8.214  92.729  22.514 1.00 83.97  ? 51  GLU F CB     1 
ATOM   12424 C CG     . GLU F 3 51  ? -7.973  92.333  23.964 1.00 100.91 ? 51  GLU F CG     1 
ATOM   12425 C CD     . GLU F 3 51  ? -7.966  93.511  24.917 1.00 109.73 ? 51  GLU F CD     1 
ATOM   12426 O OE1    . GLU F 3 51  ? -7.416  94.569  24.551 1.00 113.75 ? 51  GLU F OE1    1 
ATOM   12427 O OE2    . GLU F 3 51  ? -8.493  93.373  26.040 1.00 109.04 ? 51  GLU F OE2    1 
ATOM   12428 N N      . ASP F 3 52  ? -7.324  89.570  22.443 1.00 81.80  ? 52  ASP F N      1 
ATOM   12429 C CA     . ASP F 3 52  ? -7.653  88.194  22.724 1.00 84.12  ? 52  ASP F CA     1 
ATOM   12430 C C      . ASP F 3 52  ? -8.866  87.971  23.595 1.00 82.97  ? 52  ASP F C      1 
ATOM   12431 O O      . ASP F 3 52  ? -9.700  87.138  23.284 1.00 85.19  ? 52  ASP F O      1 
ATOM   12432 C CB     . ASP F 3 52  ? -6.448  87.544  23.380 1.00 87.90  ? 52  ASP F CB     1 
ATOM   12433 C CG     . ASP F 3 52  ? -5.152  87.817  22.639 1.00 86.28  ? 52  ASP F CG     1 
ATOM   12434 O OD1    . ASP F 3 52  ? -5.186  88.364  21.520 1.00 86.40  ? 52  ASP F OD1    1 
ATOM   12435 O OD2    . ASP F 3 52  ? -4.083  87.472  23.180 1.00 82.36  ? 52  ASP F OD2    1 
ATOM   12436 N N      . GLY F 3 53  ? -8.964  88.680  24.704 1.00 75.83  ? 53  GLY F N      1 
ATOM   12437 C CA     . GLY F 3 53  ? -10.051 88.444  25.633 1.00 73.55  ? 53  GLY F CA     1 
ATOM   12438 C C      . GLY F 3 53  ? -11.443 88.572  25.083 1.00 75.20  ? 53  GLY F C      1 
ATOM   12439 O O      . GLY F 3 53  ? -12.308 87.767  25.388 1.00 77.50  ? 53  GLY F O      1 
ATOM   12440 N N      . ARG F 3 54  ? -11.675 89.582  24.277 1.00 75.69  ? 54  ARG F N      1 
ATOM   12441 C CA     . ARG F 3 54  ? -13.008 89.821  23.795 1.00 76.72  ? 54  ARG F CA     1 
ATOM   12442 C C      . ARG F 3 54  ? -13.432 88.778  22.797 1.00 83.53  ? 54  ARG F C      1 
ATOM   12443 O O      . ARG F 3 54  ? -12.629 88.350  21.989 1.00 87.51  ? 54  ARG F O      1 
ATOM   12444 C CB     . ARG F 3 54  ? -13.053 91.196  23.172 1.00 83.07  ? 54  ARG F CB     1 
ATOM   12445 C CG     . ARG F 3 54  ? -12.218 92.238  23.899 1.00 83.46  ? 54  ARG F CG     1 
ATOM   12446 C CD     . ARG F 3 54  ? -12.678 93.642  23.543 1.00 90.66  ? 54  ARG F CD     1 
ATOM   12447 N NE     . ARG F 3 54  ? -11.820 94.676  24.113 1.00 89.32  ? 54  ARG F NE     1 
ATOM   12448 C CZ     . ARG F 3 54  ? -10.952 95.394  23.410 1.00 92.51  ? 54  ARG F CZ     1 
ATOM   12449 N NH1    . ARG F 3 54  ? -10.835 95.202  22.105 1.00 90.78  ? 54  ARG F NH1    1 
ATOM   12450 N NH2    . ARG F 3 54  ? -10.211 96.314  24.007 1.00 92.58  ? 54  ARG F NH2    1 
ATOM   12451 N N      . THR F 3 55  ? -14.691 88.365  22.833 1.00 86.15  ? 55  THR F N      1 
ATOM   12452 C CA     . THR F 3 55  ? -15.161 87.310  21.940 1.00 91.25  ? 55  THR F CA     1 
ATOM   12453 C C      . THR F 3 55  ? -15.288 87.742  20.511 1.00 86.42  ? 55  THR F C      1 
ATOM   12454 O O      . THR F 3 55  ? -15.138 88.909  20.189 1.00 84.07  ? 55  THR F O      1 
ATOM   12455 C CB     . THR F 3 55  ? -16.530 86.778  22.364 1.00 94.69  ? 55  THR F CB     1 
ATOM   12456 O OG1    . THR F 3 55  ? -17.422 87.876  22.569 1.00 106.31 ? 55  THR F OG1    1 
ATOM   12457 C CG2    . THR F 3 55  ? -16.415 85.987  23.655 1.00 88.99  ? 55  THR F CG2    1 
ATOM   12458 N N      . LEU F 3 56  ? -15.573 86.791  19.638 1.00 82.52  ? 56  LEU F N      1 
ATOM   12459 C CA     . LEU F 3 56  ? -15.673 87.100  18.234 1.00 80.36  ? 56  LEU F CA     1 
ATOM   12460 C C      . LEU F 3 56  ? -16.788 88.069  18.100 1.00 90.26  ? 56  LEU F C      1 
ATOM   12461 O O      . LEU F 3 56  ? -16.800 88.912  17.216 1.00 86.96  ? 56  LEU F O      1 
ATOM   12462 C CB     . LEU F 3 56  ? -16.012 85.861  17.433 1.00 76.28  ? 56  LEU F CB     1 
ATOM   12463 C CG     . LEU F 3 56  ? -14.999 84.738  17.252 1.00 80.57  ? 56  LEU F CG     1 
ATOM   12464 C CD1    . LEU F 3 56  ? -15.645 83.617  16.460 1.00 80.08  ? 56  LEU F CD1    1 
ATOM   12465 C CD2    . LEU F 3 56  ? -13.774 85.248  16.520 1.00 79.66  ? 56  LEU F CD2    1 
ATOM   12466 N N      . SER F 3 57  ? -17.777 87.919  18.957 1.00 95.68  ? 57  SER F N      1 
ATOM   12467 C CA     . SER F 3 57  ? -18.962 88.748  18.822 1.00 97.86  ? 57  SER F CA     1 
ATOM   12468 C C      . SER F 3 57  ? -18.711 90.218  19.023 1.00 93.86  ? 57  SER F C      1 
ATOM   12469 O O      . SER F 3 57  ? -19.419 91.048  18.465 1.00 89.91  ? 57  SER F O      1 
ATOM   12470 C CB     . SER F 3 57  ? -20.053 88.287  19.784 1.00 96.60  ? 57  SER F CB     1 
ATOM   12471 O OG     . SER F 3 57  ? -19.709 88.594  21.123 1.00 96.94  ? 57  SER F OG     1 
ATOM   12472 N N      . ASP F 3 58  ? -17.714 90.570  19.816 1.00 90.36  ? 58  ASP F N      1 
ATOM   12473 C CA     . ASP F 3 58  ? -17.514 91.981  20.114 1.00 97.94  ? 58  ASP F CA     1 
ATOM   12474 C C      . ASP F 3 58  ? -17.139 92.782  18.875 1.00 94.52  ? 58  ASP F C      1 
ATOM   12475 O O      . ASP F 3 58  ? -17.395 93.979  18.807 1.00 87.71  ? 58  ASP F O      1 
ATOM   12476 C CB     . ASP F 3 58  ? -16.491 92.175  21.234 1.00 91.41  ? 58  ASP F CB     1 
ATOM   12477 C CG     . ASP F 3 58  ? -16.972 91.628  22.563 1.00 92.52  ? 58  ASP F CG     1 
ATOM   12478 O OD1    . ASP F 3 58  ? -17.919 90.816  22.575 1.00 91.73  ? 58  ASP F OD1    1 
ATOM   12479 O OD2    . ASP F 3 58  ? -16.399 92.012  23.601 1.00 92.65  ? 58  ASP F OD2    1 
ATOM   12480 N N      . TYR F 3 59  ? -16.551 92.129  17.884 1.00 90.05  ? 59  TYR F N      1 
ATOM   12481 C CA     . TYR F 3 59  ? -16.108 92.839  16.699 1.00 82.56  ? 59  TYR F CA     1 
ATOM   12482 C C      . TYR F 3 59  ? -17.067 92.512  15.611 1.00 85.55  ? 59  TYR F C      1 
ATOM   12483 O O      . TYR F 3 59  ? -16.773 92.733  14.441 1.00 82.92  ? 59  TYR F O      1 
ATOM   12484 C CB     . TYR F 3 59  ? -14.726 92.373  16.273 1.00 78.64  ? 59  TYR F CB     1 
ATOM   12485 C CG     . TYR F 3 59  ? -13.710 92.285  17.381 1.00 76.38  ? 59  TYR F CG     1 
ATOM   12486 C CD1    . TYR F 3 59  ? -13.004 93.401  17.788 1.00 82.15  ? 59  TYR F CD1    1 
ATOM   12487 C CD2    . TYR F 3 59  ? -13.439 91.079  18.002 1.00 74.39  ? 59  TYR F CD2    1 
ATOM   12488 C CE1    . TYR F 3 59  ? -12.066 93.323  18.792 1.00 79.46  ? 59  TYR F CE1    1 
ATOM   12489 C CE2    . TYR F 3 59  ? -12.507 90.994  19.008 1.00 76.30  ? 59  TYR F CE2    1 
ATOM   12490 C CZ     . TYR F 3 59  ? -11.823 92.120  19.394 1.00 78.81  ? 59  TYR F CZ     1 
ATOM   12491 O OH     . TYR F 3 59  ? -10.896 92.043  20.395 1.00 83.68  ? 59  TYR F OH     1 
ATOM   12492 N N      . ASN F 3 60  ? -18.214 91.976  15.998 1.00 85.36  ? 60  ASN F N      1 
ATOM   12493 C CA     . ASN F 3 60  ? -19.226 91.588  15.032 1.00 86.31  ? 60  ASN F CA     1 
ATOM   12494 C C      . ASN F 3 60  ? -18.607 90.641  14.050 1.00 84.44  ? 60  ASN F C      1 
ATOM   12495 O O      . ASN F 3 60  ? -18.911 90.674  12.865 1.00 83.47  ? 60  ASN F O      1 
ATOM   12496 C CB     . ASN F 3 60  ? -19.861 92.787  14.331 1.00 81.09  ? 60  ASN F CB     1 
ATOM   12497 C CG     . ASN F 3 60  ? -21.322 92.562  14.024 1.00 83.09  ? 60  ASN F CG     1 
ATOM   12498 O OD1    . ASN F 3 60  ? -21.934 91.624  14.531 1.00 72.71  ? 60  ASN F OD1    1 
ATOM   12499 N ND2    . ASN F 3 60  ? -21.892 93.425  13.194 1.00 90.36  ? 60  ASN F ND2    1 
ATOM   12500 N N      . ILE F 3 61  ? -17.721 89.792  14.537 1.00 86.79  ? 61  ILE F N      1 
ATOM   12501 C CA     . ILE F 3 61  ? -17.168 88.787  13.658 1.00 87.23  ? 61  ILE F CA     1 
ATOM   12502 C C      . ILE F 3 61  ? -18.305 87.845  13.354 1.00 79.62  ? 61  ILE F C      1 
ATOM   12503 O O      . ILE F 3 61  ? -19.051 87.468  14.251 1.00 78.88  ? 61  ILE F O      1 
ATOM   12504 C CB     . ILE F 3 61  ? -15.928 88.124  14.268 1.00 86.14  ? 61  ILE F CB     1 
ATOM   12505 C CG1    . ILE F 3 61  ? -14.836 89.168  14.462 1.00 80.05  ? 61  ILE F CG1    1 
ATOM   12506 C CG2    . ILE F 3 61  ? -15.410 87.014  13.377 1.00 80.47  ? 61  ILE F CG2    1 
ATOM   12507 C CD1    . ILE F 3 61  ? -13.523 88.601  14.934 1.00 72.37  ? 61  ILE F CD1    1 
ATOM   12508 N N      . GLN F 3 62  ? -18.439 87.439  12.106 1.00 78.73  ? 62  GLN F N      1 
ATOM   12509 C CA     . GLN F 3 62  ? -19.598 86.656  11.714 1.00 83.01  ? 62  GLN F CA     1 
ATOM   12510 C C      . GLN F 3 62  ? -19.264 85.541  10.772 1.00 79.86  ? 62  GLN F C      1 
ATOM   12511 O O      . GLN F 3 62  ? -18.106 85.297  10.493 1.00 85.63  ? 62  GLN F O      1 
ATOM   12512 C CB     . GLN F 3 62  ? -20.618 87.577  11.058 1.00 90.21  ? 62  GLN F CB     1 
ATOM   12513 C CG     . GLN F 3 62  ? -21.486 88.347  12.042 1.00 88.43  ? 62  GLN F CG     1 
ATOM   12514 C CD     . GLN F 3 62  ? -21.899 89.706  11.520 1.00 90.12  ? 62  GLN F CD     1 
ATOM   12515 O OE1    . GLN F 3 62  ? -22.847 90.310  12.016 1.00 86.72  ? 62  GLN F OE1    1 
ATOM   12516 N NE2    . GLN F 3 62  ? -21.188 90.191  10.512 1.00 92.96  ? 62  GLN F NE2    1 
ATOM   12517 N N      . LYS F 3 63  ? -20.272 84.847  10.276 1.00 68.91  ? 63  LYS F N      1 
ATOM   12518 C CA     . LYS F 3 63  ? -20.000 83.688  9.455  1.00 71.98  ? 63  LYS F CA     1 
ATOM   12519 C C      . LYS F 3 63  ? -19.154 83.999  8.260  1.00 75.71  ? 63  LYS F C      1 
ATOM   12520 O O      . LYS F 3 63  ? -19.348 85.013  7.610  1.00 82.72  ? 63  LYS F O      1 
ATOM   12521 C CB     . LYS F 3 63  ? -21.310 83.079  8.980  1.00 72.04  ? 63  LYS F CB     1 
ATOM   12522 C CG     . LYS F 3 63  ? -21.176 81.885  8.046  1.00 73.25  ? 63  LYS F CG     1 
ATOM   12523 C CD     . LYS F 3 63  ? -20.722 80.633  8.780  1.00 87.16  ? 63  LYS F CD     1 
ATOM   12524 C CE     . LYS F 3 63  ? -20.619 79.451  7.828  1.00 87.77  ? 63  LYS F CE     1 
ATOM   12525 N NZ     . LYS F 3 63  ? -20.295 78.173  8.518  1.00 70.55  ? 63  LYS F NZ     1 
ATOM   12526 N N      . GLU F 3 64  ? -18.207 83.126  7.957  1.00 77.75  ? 64  GLU F N      1 
ATOM   12527 C CA     . GLU F 3 64  ? -17.335 83.285  6.798  1.00 77.81  ? 64  GLU F CA     1 
ATOM   12528 C C      . GLU F 3 64  ? -16.546 84.554  6.822  1.00 75.85  ? 64  GLU F C      1 
ATOM   12529 O O      . GLU F 3 64  ? -15.964 84.942  5.820  1.00 78.04  ? 64  GLU F O      1 
ATOM   12530 C CB     . GLU F 3 64  ? -18.089 83.124  5.481  1.00 81.32  ? 64  GLU F CB     1 
ATOM   12531 C CG     . GLU F 3 64  ? -17.287 82.474  4.366  1.00 83.91  ? 64  GLU F CG     1 
ATOM   12532 C CD     . GLU F 3 64  ? -17.646 81.019  4.167  1.00 87.20  ? 64  GLU F CD     1 
ATOM   12533 O OE1    . GLU F 3 64  ? -18.463 80.497  4.950  1.00 90.06  ? 64  GLU F OE1    1 
ATOM   12534 O OE2    . GLU F 3 64  ? -17.120 80.399  3.221  1.00 80.93  ? 64  GLU F OE2    1 
ATOM   12535 N N      . SER F 3 65  ? -16.493 85.200  7.966  1.00 67.32  ? 65  SER F N      1 
ATOM   12536 C CA     . SER F 3 65  ? -15.654 86.363  8.063  1.00 69.45  ? 65  SER F CA     1 
ATOM   12537 C C      . SER F 3 65  ? -14.268 85.928  7.697  1.00 72.97  ? 65  SER F C      1 
ATOM   12538 O O      . SER F 3 65  ? -13.835 84.855  8.087  1.00 82.20  ? 65  SER F O      1 
ATOM   12539 C CB     . SER F 3 65  ? -15.625 86.865  9.483  1.00 75.56  ? 65  SER F CB     1 
ATOM   12540 O OG     . SER F 3 65  ? -15.318 85.809  10.367 1.00 82.32  ? 65  SER F OG     1 
ATOM   12541 N N      . THR F 3 66  ? -13.548 86.756  6.960  1.00 66.87  ? 66  THR F N      1 
ATOM   12542 C CA     . THR F 3 66  ? -12.167 86.434  6.622  1.00 64.76  ? 66  THR F CA     1 
ATOM   12543 C C      . THR F 3 66  ? -11.178 87.249  7.449  1.00 63.71  ? 66  THR F C      1 
ATOM   12544 O O      . THR F 3 66  ? -10.889 88.389  7.120  1.00 68.80  ? 66  THR F O      1 
ATOM   12545 C CB     . THR F 3 66  ? -11.894 86.589  5.118  1.00 56.75  ? 66  THR F CB     1 
ATOM   12546 O OG1    . THR F 3 66  ? -12.876 85.859  4.376  1.00 48.90  ? 66  THR F OG1    1 
ATOM   12547 C CG2    . THR F 3 66  ? -10.518 86.065  4.767  1.00 53.84  ? 66  THR F CG2    1 
ATOM   12548 N N      . LEU F 3 67  ? -10.661 86.669  8.523  1.00 63.52  ? 67  LEU F N      1 
ATOM   12549 C CA     . LEU F 3 67  ? -9.700  87.361  9.364  1.00 61.08  ? 67  LEU F CA     1 
ATOM   12550 C C      . LEU F 3 67  ? -8.308  87.262  8.765  1.00 65.03  ? 67  LEU F C      1 
ATOM   12551 O O      . LEU F 3 67  ? -8.108  86.514  7.819  1.00 63.98  ? 67  LEU F O      1 
ATOM   12552 C CB     . LEU F 3 67  ? -9.732  86.791  10.771 1.00 53.48  ? 67  LEU F CB     1 
ATOM   12553 C CG     . LEU F 3 67  ? -10.845 87.136  11.754 1.00 57.55  ? 67  LEU F CG     1 
ATOM   12554 C CD1    . LEU F 3 67  ? -12.172 86.558  11.309 1.00 67.82  ? 67  LEU F CD1    1 
ATOM   12555 C CD2    . LEU F 3 67  ? -10.470 86.572  13.110 1.00 55.59  ? 67  LEU F CD2    1 
ATOM   12556 N N      . HIS F 3 68  ? -7.356  88.030  9.274  1.00 62.13  ? 68  HIS F N      1 
ATOM   12557 C CA     . HIS F 3 68  ? -6.022  88.061  8.684  1.00 60.32  ? 68  HIS F CA     1 
ATOM   12558 C C      . HIS F 3 68  ? -4.968  87.756  9.711  1.00 59.07  ? 68  HIS F C      1 
ATOM   12559 O O      . HIS F 3 68  ? -5.133  88.086  10.869 1.00 57.50  ? 68  HIS F O      1 
ATOM   12560 C CB     . HIS F 3 68  ? -5.748  89.440  8.095  1.00 57.19  ? 68  HIS F CB     1 
ATOM   12561 C CG     . HIS F 3 68  ? -6.241  89.624  6.698  1.00 58.09  ? 68  HIS F CG     1 
ATOM   12562 N ND1    . HIS F 3 68  ? -7.499  90.102  6.411  1.00 50.29  ? 68  HIS F ND1    1 
ATOM   12563 C CD2    . HIS F 3 68  ? -5.633  89.422  5.506  1.00 64.08  ? 68  HIS F CD2    1 
ATOM   12564 C CE1    . HIS F 3 68  ? -7.653  90.169  5.100  1.00 56.74  ? 68  HIS F CE1    1 
ATOM   12565 N NE2    . HIS F 3 68  ? -6.533  89.764  4.529  1.00 57.51  ? 68  HIS F NE2    1 
ATOM   12566 N N      . LEU F 3 69  ? -3.854  87.175  9.295  1.00 57.52  ? 69  LEU F N      1 
ATOM   12567 C CA     . LEU F 3 69  ? -2.849  86.757  10.262 1.00 61.03  ? 69  LEU F CA     1 
ATOM   12568 C C      . LEU F 3 69  ? -1.449  87.252  10.008 1.00 60.40  ? 69  LEU F C      1 
ATOM   12569 O O      . LEU F 3 69  ? -0.823  86.879  9.025  1.00 54.60  ? 69  LEU F O      1 
ATOM   12570 C CB     . LEU F 3 69  ? -2.816  85.236  10.336 1.00 59.81  ? 69  LEU F CB     1 
ATOM   12571 C CG     . LEU F 3 69  ? -1.978  84.543  11.403 1.00 58.93  ? 69  LEU F CG     1 
ATOM   12572 C CD1    . LEU F 3 69  ? -2.408  84.972  12.793 1.00 58.29  ? 69  LEU F CD1    1 
ATOM   12573 C CD2    . LEU F 3 69  ? -2.109  83.039  11.244 1.00 58.12  ? 69  LEU F CD2    1 
ATOM   12574 N N      . VAL F 3 70  ? -0.950  88.107  10.888 1.00 58.55  ? 70  VAL F N      1 
ATOM   12575 C CA     . VAL F 3 70  ? 0.415   88.545  10.762 1.00 53.08  ? 70  VAL F CA     1 
ATOM   12576 C C      . VAL F 3 70  ? 1.067   87.867  11.910 1.00 54.85  ? 70  VAL F C      1 
ATOM   12577 O O      . VAL F 3 70  ? 0.522   87.831  12.996 1.00 54.77  ? 70  VAL F O      1 
ATOM   12578 C CB     . VAL F 3 70  ? 0.571   90.051  10.862 1.00 54.08  ? 70  VAL F CB     1 
ATOM   12579 C CG1    . VAL F 3 70  ? 2.032   90.442  10.739 1.00 64.13  ? 70  VAL F CG1    1 
ATOM   12580 C CG2    . VAL F 3 70  ? -0.231  90.728  9.770  1.00 59.38  ? 70  VAL F CG2    1 
ATOM   12581 N N      . LEU F 3 71  ? 2.196   87.245  11.658 1.00 51.21  ? 71  LEU F N      1 
ATOM   12582 C CA     . LEU F 3 71  ? 2.856   86.503  12.669 1.00 46.15  ? 71  LEU F CA     1 
ATOM   12583 C C      . LEU F 3 71  ? 3.967   87.383  13.062 1.00 47.26  ? 71  LEU F C      1 
ATOM   12584 O O      . LEU F 3 71  ? 4.788   87.750  12.240 1.00 42.80  ? 71  LEU F O      1 
ATOM   12585 C CB     . LEU F 3 71  ? 3.399   85.235  12.061 1.00 48.04  ? 71  LEU F CB     1 
ATOM   12586 C CG     . LEU F 3 71  ? 2.364   84.269  11.523 1.00 47.85  ? 71  LEU F CG     1 
ATOM   12587 C CD1    . LEU F 3 71  ? 3.020   82.957  11.143 1.00 40.41  ? 71  LEU F CD1    1 
ATOM   12588 C CD2    . LEU F 3 71  ? 1.362   84.055  12.633 1.00 53.02  ? 71  LEU F CD2    1 
ATOM   12589 N N      . ARG F 3 72  ? 3.985   87.747  14.326 1.00 52.02  ? 72  ARG F N      1 
ATOM   12590 C CA     . ARG F 3 72  ? 4.995   88.633  14.828 1.00 50.94  ? 72  ARG F CA     1 
ATOM   12591 C C      . ARG F 3 72  ? 6.348   88.022  14.688 1.00 53.23  ? 72  ARG F C      1 
ATOM   12592 O O      . ARG F 3 72  ? 6.681   87.067  15.364 1.00 53.50  ? 72  ARG F O      1 
ATOM   12593 C CB     . ARG F 3 72  ? 4.703   88.938  16.290 1.00 48.20  ? 72  ARG F CB     1 
ATOM   12594 C CG     . ARG F 3 72  ? 5.221   90.261  16.799 1.00 58.80  ? 72  ARG F CG     1 
ATOM   12595 C CD     . ARG F 3 72  ? 4.725   90.439  18.215 1.00 60.09  ? 72  ARG F CD     1 
ATOM   12596 N NE     . ARG F 3 72  ? 3.363   89.937  18.339 1.00 59.90  ? 72  ARG F NE     1 
ATOM   12597 C CZ     . ARG F 3 72  ? 2.681   89.906  19.476 1.00 64.80  ? 72  ARG F CZ     1 
ATOM   12598 N NH1    . ARG F 3 72  ? 3.240   90.346  20.594 1.00 64.95  ? 72  ARG F NH1    1 
ATOM   12599 N NH2    . ARG F 3 72  ? 1.445   89.430  19.499 1.00 64.22  ? 72  ARG F NH2    1 
ATOM   12600 N N      . LEU F 3 73  ? 7.182   88.586  13.841 1.00 52.88  ? 73  LEU F N      1 
ATOM   12601 C CA     . LEU F 3 73  ? 8.539   88.105  13.757 1.00 55.74  ? 73  LEU F CA     1 
ATOM   12602 C C      . LEU F 3 73  ? 9.278   88.807  14.861 1.00 62.21  ? 73  LEU F C      1 
ATOM   12603 O O      . LEU F 3 73  ? 9.337   90.033  14.893 1.00 60.06  ? 73  LEU F O      1 
ATOM   12604 C CB     . LEU F 3 73  ? 9.153   88.404  12.399 1.00 49.67  ? 73  LEU F CB     1 
ATOM   12605 C CG     . LEU F 3 73  ? 10.420  87.642  12.029 1.00 47.11  ? 73  LEU F CG     1 
ATOM   12606 C CD1    . LEU F 3 73  ? 10.387  87.237  10.567 1.00 59.98  ? 73  LEU F CD1    1 
ATOM   12607 C CD2    . LEU F 3 73  ? 11.661  88.462  12.331 1.00 67.21  ? 73  LEU F CD2    1 
ATOM   12608 N N      . ARG F 3 74  ? 9.832   88.034  15.785 1.00 64.00  ? 74  ARG F N      1 
ATOM   12609 C CA     . ARG F 3 74  ? 10.601  88.595  16.870 1.00 57.40  ? 74  ARG F CA     1 
ATOM   12610 C C      . ARG F 3 74  ? 11.685  87.616  17.168 1.00 67.40  ? 74  ARG F C      1 
ATOM   12611 O O      . ARG F 3 74  ? 11.641  86.479  16.719 1.00 67.51  ? 74  ARG F O      1 
ATOM   12612 C CB     . ARG F 3 74  ? 9.728   88.757  18.093 1.00 53.72  ? 74  ARG F CB     1 
ATOM   12613 C CG     . ARG F 3 74  ? 8.986   87.497  18.484 1.00 50.92  ? 74  ARG F CG     1 
ATOM   12614 C CD     . ARG F 3 74  ? 7.638   87.823  19.089 1.00 48.28  ? 74  ARG F CD     1 
ATOM   12615 N NE     . ARG F 3 74  ? 6.963   86.609  19.514 1.00 51.61  ? 74  ARG F NE     1 
ATOM   12616 C CZ     . ARG F 3 74  ? 6.998   86.140  20.751 1.00 64.91  ? 74  ARG F CZ     1 
ATOM   12617 N NH1    . ARG F 3 74  ? 7.663   86.791  21.691 1.00 61.04  ? 74  ARG F NH1    1 
ATOM   12618 N NH2    . ARG F 3 74  ? 6.362   85.021  21.050 1.00 76.46  ? 74  ARG F NH2    1 
ATOM   12619 N N      . GLY F 3 75  ? 12.632  88.026  17.990 1.00 67.88  ? 75  GLY F N      1 
ATOM   12620 C CA     . GLY F 3 75  ? 13.739  87.163  18.333 1.00 69.41  ? 75  GLY F CA     1 
ATOM   12621 C C      . GLY F 3 75  ? 14.658  87.181  17.160 1.00 80.12  ? 75  GLY F C      1 
ATOM   12622 O O      . GLY F 3 75  ? 15.846  86.921  17.281 1.00 87.86  ? 75  GLY F O      1 
ATOM   12623 N N      . GLY F 3 76  ? 14.105  87.502  16.007 1.00 91.08  ? 76  GLY F N      1 
ATOM   12624 C CA     . GLY F 3 76  ? 14.915  87.585  14.809 1.00 98.62  ? 76  GLY F CA     1 
ATOM   12625 C C      . GLY F 3 76  ? 14.586  88.750  13.889 1.00 102.08 ? 76  GLY F C      1 
ATOM   12626 O O      . GLY F 3 76  ? 15.191  88.893  12.832 1.00 106.82 ? 76  GLY F O      1 
ATOM   12627 O OXT    . GLY F 3 76  ? 13.712  89.570  14.159 1.00 93.26  ? 76  GLY F OXT    1 
HETATM 12628 P PG     . ATP G 4 .   ? 5.578   1.505   18.728 1.00 79.02  ? 401 ATP A PG     1 
HETATM 12629 O O1G    . ATP G 4 .   ? 5.407   2.953   19.041 1.00 51.70  ? 401 ATP A O1G    1 
HETATM 12630 O O2G    . ATP G 4 .   ? 6.210   0.689   19.814 1.00 69.54  ? 401 ATP A O2G    1 
HETATM 12631 O O3G    . ATP G 4 .   ? 4.376   0.848   18.114 1.00 60.46  ? 401 ATP A O3G    1 
HETATM 12632 P PB     . ATP G 4 .   ? 8.097   2.102   17.438 1.00 58.62  ? 401 ATP A PB     1 
HETATM 12633 O O1B    . ATP G 4 .   ? 8.044   3.430   16.777 1.00 51.92  ? 401 ATP A O1B    1 
HETATM 12634 O O2B    . ATP G 4 .   ? 8.814   1.949   18.740 1.00 49.61  ? 401 ATP A O2B    1 
HETATM 12635 O O3B    . ATP G 4 .   ? 6.606   1.528   17.503 1.00 75.14  ? 401 ATP A O3B    1 
HETATM 12636 P PA     . ATP G 4 .   ? 7.928   0.580   15.145 1.00 44.81  ? 401 ATP A PA     1 
HETATM 12637 O O1A    . ATP G 4 .   ? 7.559   1.728   14.276 1.00 50.16  ? 401 ATP A O1A    1 
HETATM 12638 O O2A    . ATP G 4 .   ? 6.854   -0.366  15.557 1.00 46.36  ? 401 ATP A O2A    1 
HETATM 12639 O O3A    . ATP G 4 .   ? 8.767   1.129   16.379 1.00 53.22  ? 401 ATP A O3A    1 
HETATM 12640 O "O5'"  . ATP G 4 .   ? 9.020   -0.299  14.398 1.00 48.23  ? 401 ATP A "O5'"  1 
HETATM 12641 C "C5'"  . ATP G 4 .   ? 9.880   0.287   13.449 1.00 49.92  ? 401 ATP A "C5'"  1 
HETATM 12642 C "C4'"  . ATP G 4 .   ? 11.063  -0.634  13.281 1.00 49.45  ? 401 ATP A "C4'"  1 
HETATM 12643 O "O4'"  . ATP G 4 .   ? 10.660  -1.972  13.054 1.00 51.66  ? 401 ATP A "O4'"  1 
HETATM 12644 C "C3'"  . ATP G 4 .   ? 11.922  -0.325  12.075 1.00 54.34  ? 401 ATP A "C3'"  1 
HETATM 12645 O "O3'"  . ATP G 4 .   ? 12.926  0.655   12.328 1.00 67.94  ? 401 ATP A "O3'"  1 
HETATM 12646 C "C2'"  . ATP G 4 .   ? 12.607  -1.627  11.809 1.00 51.12  ? 401 ATP A "C2'"  1 
HETATM 12647 O "O2'"  . ATP G 4 .   ? 13.945  -1.455  12.258 1.00 52.28  ? 401 ATP A "O2'"  1 
HETATM 12648 C "C1'"  . ATP G 4 .   ? 11.823  -2.656  12.604 1.00 58.10  ? 401 ATP A "C1'"  1 
HETATM 12649 N N9     . ATP G 4 .   ? 11.479  -3.867  11.815 1.00 65.83  ? 401 ATP A N9     1 
HETATM 12650 C C8     . ATP G 4 .   ? 11.979  -5.090  12.065 1.00 60.13  ? 401 ATP A C8     1 
HETATM 12651 N N7     . ATP G 4 .   ? 11.493  -6.005  11.204 1.00 56.73  ? 401 ATP A N7     1 
HETATM 12652 C C5     . ATP G 4 .   ? 10.666  -5.372  10.374 1.00 58.38  ? 401 ATP A C5     1 
HETATM 12653 C C6     . ATP G 4 .   ? 9.819   -5.778  9.249  1.00 57.72  ? 401 ATP A C6     1 
HETATM 12654 N N6     . ATP G 4 .   ? 9.804   -7.062  8.839  1.00 54.07  ? 401 ATP A N6     1 
HETATM 12655 N N1     . ATP G 4 .   ? 9.091   -4.822  8.647  1.00 58.93  ? 401 ATP A N1     1 
HETATM 12656 C C2     . ATP G 4 .   ? 9.118   -3.543  9.058  1.00 56.79  ? 401 ATP A C2     1 
HETATM 12657 N N3     . ATP G 4 .   ? 9.862   -3.112  10.092 1.00 52.39  ? 401 ATP A N3     1 
HETATM 12658 C C4     . ATP G 4 .   ? 10.656  -3.960  10.771 1.00 57.76  ? 401 ATP A C4     1 
HETATM 12659 H "H5'1" . ATP G 4 .   ? 10.234  1.255   13.811 1.00 59.68  ? 401 ATP A "H5'1" 1 
HETATM 12660 H "H5'2" . ATP G 4 .   ? 9.356   0.429   12.502 1.00 59.68  ? 401 ATP A "H5'2" 1 
HETATM 12661 H "H4'"  . ATP G 4 .   ? 11.675  -0.584  14.195 1.00 59.11  ? 401 ATP A "H4'"  1 
HETATM 12662 H "H3'"  . ATP G 4 .   ? 11.310  -0.060  11.203 1.00 64.97  ? 401 ATP A "H3'"  1 
HETATM 12663 H "HO3'" . ATP G 4 .   ? 12.598  1.342   12.923 1.00 81.30  ? 401 ATP A "HO3'" 1 
HETATM 12664 H "H2'"  . ATP G 4 .   ? 12.590  -1.862  10.741 1.00 61.11  ? 401 ATP A "H2'"  1 
HETATM 12665 H "HO2'" . ATP G 4 .   ? 13.971  -1.044  13.133 1.00 62.50  ? 401 ATP A "HO2'" 1 
HETATM 12666 H "H1'"  . ATP G 4 .   ? 12.415  -2.950  13.482 1.00 69.49  ? 401 ATP A "H1'"  1 
HETATM 12667 H H8     . ATP G 4 .   ? 12.679  -5.320  12.853 1.00 71.92  ? 401 ATP A H8     1 
HETATM 12668 H HN61   . ATP G 4 .   ? 9.228   -7.337  8.058  1.00 64.65  ? 401 ATP A HN61   1 
HETATM 12669 H HN62   . ATP G 4 .   ? 10.370  -7.748  9.320  1.00 64.65  ? 401 ATP A HN62   1 
HETATM 12670 H H2     . ATP G 4 .   ? 8.510   -2.821  8.529  1.00 67.91  ? 401 ATP A H2     1 
HETATM 12671 P PG     . ATP H 4 .   ? 21.318  53.420  18.803 1.00 81.10  ? 401 ATP B PG     1 
HETATM 12672 O O1G    . ATP H 4 .   ? 20.473  53.988  19.906 1.00 75.70  ? 401 ATP B O1G    1 
HETATM 12673 O O2G    . ATP H 4 .   ? 22.087  54.450  18.020 1.00 48.68  ? 401 ATP B O2G    1 
HETATM 12674 O O3G    . ATP H 4 .   ? 22.151  52.261  19.254 1.00 59.54  ? 401 ATP B O3G    1 
HETATM 12675 P PB     . ATP H 4 .   ? 19.024  53.457  17.104 1.00 65.83  ? 401 ATP B PB     1 
HETATM 12676 O O1B    . ATP H 4 .   ? 18.981  54.850  17.602 1.00 68.46  ? 401 ATP B O1B    1 
HETATM 12677 O O2B    . ATP H 4 .   ? 17.806  52.610  17.275 1.00 56.43  ? 401 ATP B O2B    1 
HETATM 12678 O O3B    . ATP H 4 .   ? 20.299  52.725  17.760 1.00 69.82  ? 401 ATP B O3B    1 
HETATM 12679 P PA     . ATP H 4 .   ? 19.825  54.865  14.834 1.00 64.12  ? 401 ATP B PA     1 
HETATM 12680 O O1A    . ATP H 4 .   ? 20.310  54.491  13.465 1.00 59.80  ? 401 ATP B O1A    1 
HETATM 12681 O O2A    . ATP H 4 .   ? 20.763  55.654  15.692 1.00 53.37  ? 401 ATP B O2A    1 
HETATM 12682 O O3A    . ATP H 4 .   ? 19.368  53.509  15.550 1.00 59.20  ? 401 ATP B O3A    1 
HETATM 12683 O "O5'"  . ATP H 4 .   ? 18.445  55.657  14.695 1.00 55.71  ? 401 ATP B "O5'"  1 
HETATM 12684 C "C5'"  . ATP H 4 .   ? 17.514  55.328  13.668 1.00 59.45  ? 401 ATP B "C5'"  1 
HETATM 12685 C "C4'"  . ATP H 4 .   ? 16.441  56.396  13.602 1.00 55.05  ? 401 ATP B "C4'"  1 
HETATM 12686 O "O4'"  . ATP H 4 .   ? 16.958  57.636  13.133 1.00 53.09  ? 401 ATP B "O4'"  1 
HETATM 12687 C "C3'"  . ATP H 4 .   ? 15.342  56.050  12.622 1.00 59.62  ? 401 ATP B "C3'"  1 
HETATM 12688 O "O3'"  . ATP H 4 .   ? 14.127  55.834  13.326 1.00 59.60  ? 401 ATP B "O3'"  1 
HETATM 12689 C "C2'"  . ATP H 4 .   ? 15.162  57.271  11.771 1.00 53.50  ? 401 ATP B "C2'"  1 
HETATM 12690 O "O2'"  . ATP H 4 .   ? 13.789  57.580  11.613 1.00 64.74  ? 401 ATP B "O2'"  1 
HETATM 12691 C "C1'"  . ATP H 4 .   ? 15.842  58.328  12.591 1.00 50.39  ? 401 ATP B "C1'"  1 
HETATM 12692 N N9     . ATP H 4 .   ? 16.176  59.553  11.823 1.00 56.34  ? 401 ATP B N9     1 
HETATM 12693 C C8     . ATP H 4 .   ? 15.698  60.762  12.167 1.00 56.17  ? 401 ATP B C8     1 
HETATM 12694 N N7     . ATP H 4 .   ? 16.137  61.718  11.325 1.00 53.38  ? 401 ATP B N7     1 
HETATM 12695 C C5     . ATP H 4 .   ? 16.916  61.121  10.424 1.00 56.68  ? 401 ATP B C5     1 
HETATM 12696 C C6     . ATP H 4 .   ? 17.687  61.581  9.267  1.00 60.93  ? 401 ATP B C6     1 
HETATM 12697 N N6     . ATP H 4 .   ? 17.696  62.888  8.922  1.00 62.96  ? 401 ATP B N6     1 
HETATM 12698 N N1     . ATP H 4 .   ? 18.370  60.655  8.575  1.00 60.62  ? 401 ATP B N1     1 
HETATM 12699 C C2     . ATP H 4 .   ? 18.359  59.360  8.918  1.00 57.90  ? 401 ATP B C2     1 
HETATM 12700 N N3     . ATP H 4 .   ? 17.676  58.877  9.968  1.00 49.17  ? 401 ATP B N3     1 
HETATM 12701 C C4     . ATP H 4 .   ? 16.945  59.694  10.747 1.00 52.01  ? 401 ATP B C4     1 
HETATM 12702 H "H5'1" . ATP H 4 .   ? 17.060  54.358  13.881 1.00 71.11  ? 401 ATP B "H5'1" 1 
HETATM 12703 H "H5'2" . ATP H 4 .   ? 18.009  55.272  12.697 1.00 71.11  ? 401 ATP B "H5'2" 1 
HETATM 12704 H "H4'"  . ATP H 4 .   ? 16.002  56.522  14.602 1.00 65.83  ? 401 ATP B "H4'"  1 
HETATM 12705 H "H3'"  . ATP H 4 .   ? 15.617  55.185  12.002 1.00 71.30  ? 401 ATP B "H3'"  1 
HETATM 12706 H "HO3'" . ATP H 4 .   ? 13.400  55.749  12.694 1.00 71.29  ? 401 ATP B "HO3'" 1 
HETATM 12707 H "H2'"  . ATP H 4 .   ? 15.663  57.131  10.804 1.00 63.97  ? 401 ATP B "H2'"  1 
HETATM 12708 H "HO2'" . ATP H 4 .   ? 13.634  57.814  10.690 1.00 77.45  ? 401 ATP B "HO2'" 1 
HETATM 12709 H "H1'"  . ATP H 4 .   ? 15.163  58.595  13.412 1.00 60.23  ? 401 ATP B "H1'"  1 
HETATM 12710 H H8     . ATP H 4 .   ? 15.043  60.950  13.009 1.00 67.17  ? 401 ATP B H8     1 
HETATM 12711 H HN61   . ATP H 4 .   ? 18.229  63.197  8.121  1.00 75.32  ? 401 ATP B HN61   1 
HETATM 12712 H HN62   . ATP H 4 .   ? 17.169  63.556  9.466  1.00 75.32  ? 401 ATP B HN62   1 
HETATM 12713 H H2     . ATP H 4 .   ? 18.933  58.674  8.311  1.00 69.25  ? 401 ATP B H2     1 
HETATM 12714 P PB     . AR6 I 5 .   ? 35.421  65.283  61.065 1.00 63.27  ? 401 AR6 D PB     1 
HETATM 12715 O O1B    . AR6 I 5 .   ? 36.469  65.542  62.097 1.00 49.03  ? 401 AR6 D O1B    1 
HETATM 12716 C C1D    . AR6 I 5 .   ? 31.902  68.748  62.383 1.00 64.46  ? 401 AR6 D C1D    1 
HETATM 12717 O O1D    . AR6 I 5 .   ? 30.827  69.258  63.165 1.00 57.19  ? 401 AR6 D O1D    1 
HETATM 12718 O O2B    . AR6 I 5 .   ? 35.685  65.599  59.627 1.00 62.99  ? 401 AR6 D O2B    1 
HETATM 12719 C C2D    . AR6 I 5 .   ? 31.735  69.136  60.930 1.00 64.84  ? 401 AR6 D C2D    1 
HETATM 12720 O O2D    . AR6 I 5 .   ? 30.374  69.437  60.641 1.00 71.84  ? 401 AR6 D O2D    1 
HETATM 12721 O O3A    . AR6 I 5 .   ? 34.965  63.761  61.197 1.00 61.80  ? 401 AR6 D O3A    1 
HETATM 12722 C C3D    . AR6 I 5 .   ? 32.109  67.914  60.144 1.00 66.27  ? 401 AR6 D C3D    1 
HETATM 12723 O O3D    . AR6 I 5 .   ? 31.302  67.807  58.975 1.00 61.92  ? 401 AR6 D O3D    1 
HETATM 12724 C C4D    . AR6 I 5 .   ? 31.841  66.778  61.108 1.00 68.12  ? 401 AR6 D C4D    1 
HETATM 12725 O O4D    . AR6 I 5 .   ? 31.919  67.323  62.425 1.00 72.40  ? 401 AR6 D O4D    1 
HETATM 12726 C C5D    . AR6 I 5 .   ? 32.834  65.642  60.950 1.00 64.98  ? 401 AR6 D C5D    1 
HETATM 12727 O O5D    . AR6 I 5 .   ? 34.086  66.043  61.491 1.00 71.87  ? 401 AR6 D O5D    1 
HETATM 12728 H H1D    . AR6 I 5 .   ? 32.857  69.147  62.750 1.00 77.12  ? 401 AR6 D H1D    1 
HETATM 12729 H H2D    . AR6 I 5 .   ? 32.402  69.972  60.683 1.00 77.58  ? 401 AR6 D H2D    1 
HETATM 12730 H HO2D   . AR6 I 5 .   ? 29.970  69.885  61.393 1.00 85.97  ? 401 AR6 D HO2D   1 
HETATM 12731 H H3D    . AR6 I 5 .   ? 33.176  67.960  59.885 1.00 79.29  ? 401 AR6 D H3D    1 
HETATM 12732 H HO3D   . AR6 I 5 .   ? 31.418  68.601  58.435 1.00 74.07  ? 401 AR6 D HO3D   1 
HETATM 12733 H H4D    . AR6 I 5 .   ? 30.829  66.392  60.925 1.00 81.51  ? 401 AR6 D H4D    1 
HETATM 12734 H H5D    . AR6 I 5 .   ? 32.939  65.388  59.893 1.00 77.74  ? 401 AR6 D H5D    1 
HETATM 12735 H H5DA   . AR6 I 5 .   ? 32.462  64.763  61.480 1.00 77.74  ? 401 AR6 D H5DA   1 
HETATM 12736 H HD1    . AR6 I 5 .   ? 31.099  69.308  64.091 1.00 68.39  ? 401 AR6 D HD1    1 
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