data_8K6I
# 
_entry.id   8K6I 
# 
_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   8K6I         pdb_00008k6i 10.2210/pdb8k6i/pdb 
WWPDB D_1300039653 ?            ?                   
# 
_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                        8K6I 
_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 8720.961  2  ? ? ? ? 
4 non-polymer syn 'PHOSPHATE ION' 94.971    1  ? ? ? ? 
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  ? ? ? ? 
6 water       nat water 18.015    35 ? ? ? ? 
# 
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 GSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 
GSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG E,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'PHOSPHATE ION' PO4 
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 
6 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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   GLY n 
3 2   SER n 
3 3   MET n 
3 4   GLN n 
3 5   ILE n 
3 6   PHE n 
3 7   VAL n 
3 8   LYS n 
3 9   THR n 
3 10  LEU n 
3 11  THR n 
3 12  GLY n 
3 13  LYS n 
3 14  THR n 
3 15  ILE n 
3 16  THR n 
3 17  LEU n 
3 18  GLU n 
3 19  VAL n 
3 20  GLU n 
3 21  PRO n 
3 22  SER n 
3 23  ASP n 
3 24  THR n 
3 25  ILE n 
3 26  GLU n 
3 27  ASN n 
3 28  VAL n 
3 29  LYS n 
3 30  ALA n 
3 31  LYS n 
3 32  ILE n 
3 33  GLN n 
3 34  ASP n 
3 35  LYS n 
3 36  GLU n 
3 37  GLY n 
3 38  ILE n 
3 39  PRO n 
3 40  PRO n 
3 41  ASP n 
3 42  GLN n 
3 43  GLN n 
3 44  ARG n 
3 45  LEU n 
3 46  ILE n 
3 47  PHE n 
3 48  ALA n 
3 49  GLY n 
3 50  LYS n 
3 51  GLN n 
3 52  LEU n 
3 53  GLU n 
3 54  ASP n 
3 55  GLY n 
3 56  ARG n 
3 57  THR n 
3 58  LEU n 
3 59  SER n 
3 60  ASP n 
3 61  TYR n 
3 62  ASN n 
3 63  ILE n 
3 64  GLN n 
3 65  LYS n 
3 66  GLU n 
3 67  SER n 
3 68  THR n 
3 69  LEU n 
3 70  HIS n 
3 71  LEU n 
3 72  VAL n 
3 73  LEU n 
3 74  ARG n 
3 75  LEU n 
3 76  ARG n 
3 77  GLY n 
3 78  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 78  human ? UBC ? ? ? ? ? ? '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 
CYS 'L-peptide linking' y CYSTEINE ?                           'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                           'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                           'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ?                           'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE ?                           'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER ?                           'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                           'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ?                           'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ?                           'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ?                           'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                           'C9 H11 N O2'       165.189 
PO4 non-polymer         . 'PHOSPHATE ION' ?                           'O4 P -3'           94.971  
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   5   ILE ILE 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 ALA 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  ?   ?   ?   A . n 
A 1 47  MET 47  47  ?   ?   ?   A . n 
A 1 48  GLY 48  48  ?   ?   ?   A . n 
A 1 49  GLN 49  49  ?   ?   ?   A . n 
A 1 50  LYS 50  50  ?   ?   ?   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 ALA 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  ?   ?   ?   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  ?   ?   ?   C . n 
C 2 36  LEU 36  54  ?   ?   ?   C . n 
C 2 37  GLY 37  55  ?   ?   ?   C . n 
C 2 38  LYS 38  56  ?   ?   ?   C . n 
C 2 39  LYS 39  57  ?   ?   ?   C . n 
C 2 40  LYS 40  58  ?   ?   ?   C . n 
C 2 41  GLU 41  59  ?   ?   ?   C . n 
C 2 42  PHE 42  60  ?   ?   ?   C . n 
C 2 43  SER 43  61  ?   ?   ?   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 ?   ?   ?   C . n 
C 2 90  ARG 90  108 ?   ?   ?   C . n 
C 2 91  LEU 91  109 ?   ?   ?   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 ?   ?   ?   C . n 
C 2 146 GLU 146 164 ?   ?   ?   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 ?   ?   ?   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  22  GLN GLN 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  ?   ?   ?   D . n 
D 2 39  LYS 39  57  ?   ?   ?   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 ?   ?   ?   D . n 
D 2 352 GLU 352 370 ?   ?   ?   D . n 
E 3 1   GLY 1   -1  -1  GLY GLY E . n 
E 3 2   SER 2   0   0   SER SER E . n 
E 3 3   MET 3   1   1   MET MET E . n 
E 3 4   GLN 4   2   2   GLN GLN E . n 
E 3 5   ILE 5   3   3   ILE ILE E . n 
E 3 6   PHE 6   4   4   PHE PHE E . n 
E 3 7   VAL 7   5   5   VAL VAL E . n 
E 3 8   LYS 8   6   6   LYS LYS E . n 
E 3 9   THR 9   7   7   THR THR E . n 
E 3 10  LEU 10  8   8   LEU LEU E . n 
E 3 11  THR 11  9   9   THR THR E . n 
E 3 12  GLY 12  10  10  GLY GLY E . n 
E 3 13  LYS 13  11  11  LYS LYS E . n 
E 3 14  THR 14  12  12  THR THR E . n 
E 3 15  ILE 15  13  13  ILE ILE E . n 
E 3 16  THR 16  14  14  THR THR E . n 
E 3 17  LEU 17  15  15  LEU LEU E . n 
E 3 18  GLU 18  16  16  GLU GLU E . n 
E 3 19  VAL 19  17  17  VAL VAL E . n 
E 3 20  GLU 20  18  18  GLU GLU E . n 
E 3 21  PRO 21  19  19  PRO PRO E . n 
E 3 22  SER 22  20  20  SER SER E . n 
E 3 23  ASP 23  21  21  ASP ASP E . n 
E 3 24  THR 24  22  22  THR THR E . n 
E 3 25  ILE 25  23  23  ILE ILE E . n 
E 3 26  GLU 26  24  24  GLU GLU E . n 
E 3 27  ASN 27  25  25  ASN ASN E . n 
E 3 28  VAL 28  26  26  VAL VAL E . n 
E 3 29  LYS 29  27  27  LYS LYS E . n 
E 3 30  ALA 30  28  28  ALA ALA E . n 
E 3 31  LYS 31  29  29  LYS LYS E . n 
E 3 32  ILE 32  30  30  ILE ILE E . n 
E 3 33  GLN 33  31  31  GLN GLN E . n 
E 3 34  ASP 34  32  32  ASP ASP E . n 
E 3 35  LYS 35  33  33  LYS LYS E . n 
E 3 36  GLU 36  34  34  GLU GLU E . n 
E 3 37  GLY 37  35  35  GLY GLY E . n 
E 3 38  ILE 38  36  36  ILE ILE E . n 
E 3 39  PRO 39  37  37  PRO PRO E . n 
E 3 40  PRO 40  38  38  PRO PRO E . n 
E 3 41  ASP 41  39  39  ASP ASP E . n 
E 3 42  GLN 42  40  40  GLN GLN E . n 
E 3 43  GLN 43  41  41  GLN GLN E . n 
E 3 44  ARG 44  42  42  ARG ARG E . n 
E 3 45  LEU 45  43  43  LEU LEU E . n 
E 3 46  ILE 46  44  44  ILE ILE E . n 
E 3 47  PHE 47  45  45  PHE PHE E . n 
E 3 48  ALA 48  46  46  ALA ALA E . n 
E 3 49  GLY 49  47  47  GLY GLY E . n 
E 3 50  LYS 50  48  48  LYS LYS E . n 
E 3 51  GLN 51  49  49  GLN GLN E . n 
E 3 52  LEU 52  50  50  LEU LEU E . n 
E 3 53  GLU 53  51  51  GLU GLU E . n 
E 3 54  ASP 54  52  52  ASP ASP E . n 
E 3 55  GLY 55  53  53  GLY GLY E . n 
E 3 56  ARG 56  54  54  ARG ARG E . n 
E 3 57  THR 57  55  55  THR THR E . n 
E 3 58  LEU 58  56  56  LEU LEU E . n 
E 3 59  SER 59  57  57  SER SER E . n 
E 3 60  ASP 60  58  58  ASP ASP E . n 
E 3 61  TYR 61  59  59  TYR TYR E . n 
E 3 62  ASN 62  60  60  ASN ASN E . n 
E 3 63  ILE 63  61  61  ILE ILE E . n 
E 3 64  GLN 64  62  62  GLN GLN E . n 
E 3 65  LYS 65  63  63  LYS LYS E . n 
E 3 66  GLU 66  64  64  GLU GLU E . n 
E 3 67  SER 67  65  65  SER SER E . n 
E 3 68  THR 68  66  66  THR THR E . n 
E 3 69  LEU 69  67  67  LEU LEU E . n 
E 3 70  HIS 70  68  68  HIS HIS E . n 
E 3 71  LEU 71  69  69  LEU LEU E . n 
E 3 72  VAL 72  70  70  VAL VAL E . n 
E 3 73  LEU 73  71  71  LEU LEU E . n 
E 3 74  ARG 74  72  72  ARG ARG E . n 
E 3 75  LEU 75  73  73  LEU LEU E . n 
E 3 76  ARG 76  74  74  ARG ARG E . n 
E 3 77  GLY 77  75  75  GLY GLY E . n 
E 3 78  GLY 78  76  76  GLY GLY E . n 
F 3 1   GLY 1   -1  ?   ?   ?   F . n 
F 3 2   SER 2   0   0   SER SER F . n 
F 3 3   MET 3   1   1   MET MET F . n 
F 3 4   GLN 4   2   2   GLN GLN F . n 
F 3 5   ILE 5   3   3   ILE ILE F . n 
F 3 6   PHE 6   4   4   PHE PHE F . n 
F 3 7   VAL 7   5   5   VAL VAL F . n 
F 3 8   LYS 8   6   6   LYS LYS F . n 
F 3 9   THR 9   7   7   THR THR F . n 
F 3 10  LEU 10  8   8   LEU LEU F . n 
F 3 11  THR 11  9   9   THR THR F . n 
F 3 12  GLY 12  10  10  GLY GLY F . n 
F 3 13  LYS 13  11  11  LYS LYS F . n 
F 3 14  THR 14  12  12  THR THR F . n 
F 3 15  ILE 15  13  13  ILE ILE F . n 
F 3 16  THR 16  14  14  THR THR F . n 
F 3 17  LEU 17  15  15  LEU LEU F . n 
F 3 18  GLU 18  16  16  GLU GLU F . n 
F 3 19  VAL 19  17  17  VAL VAL F . n 
F 3 20  GLU 20  18  18  GLU GLU F . n 
F 3 21  PRO 21  19  19  PRO PRO F . n 
F 3 22  SER 22  20  20  SER SER F . n 
F 3 23  ASP 23  21  21  ASP ASP F . n 
F 3 24  THR 24  22  22  THR THR F . n 
F 3 25  ILE 25  23  23  ILE ILE F . n 
F 3 26  GLU 26  24  24  GLU GLU F . n 
F 3 27  ASN 27  25  25  ASN ASN F . n 
F 3 28  VAL 28  26  26  VAL VAL F . n 
F 3 29  LYS 29  27  27  LYS LYS F . n 
F 3 30  ALA 30  28  28  ALA ALA F . n 
F 3 31  LYS 31  29  29  LYS LYS F . n 
F 3 32  ILE 32  30  30  ILE ILE F . n 
F 3 33  GLN 33  31  31  GLN GLN F . n 
F 3 34  ASP 34  32  32  ASP ASP F . n 
F 3 35  LYS 35  33  33  LYS LYS F . n 
F 3 36  GLU 36  34  34  GLU GLU F . n 
F 3 37  GLY 37  35  35  GLY GLY F . n 
F 3 38  ILE 38  36  36  ILE ILE F . n 
F 3 39  PRO 39  37  37  PRO PRO F . n 
F 3 40  PRO 40  38  38  PRO PRO F . n 
F 3 41  ASP 41  39  39  ASP ASP F . n 
F 3 42  GLN 42  40  40  GLN GLN F . n 
F 3 43  GLN 43  41  41  GLN GLN F . n 
F 3 44  ARG 44  42  42  ARG ARG F . n 
F 3 45  LEU 45  43  43  LEU LEU F . n 
F 3 46  ILE 46  44  44  ILE ILE F . n 
F 3 47  PHE 47  45  45  PHE PHE F . n 
F 3 48  ALA 48  46  46  ALA ALA F . n 
F 3 49  GLY 49  47  47  GLY GLY F . n 
F 3 50  LYS 50  48  48  LYS LYS F . n 
F 3 51  GLN 51  49  49  GLN GLN F . n 
F 3 52  LEU 52  50  50  LEU LEU F . n 
F 3 53  GLU 53  51  51  GLU GLU F . n 
F 3 54  ASP 54  52  52  ASP ASP F . n 
F 3 55  GLY 55  53  53  GLY GLY F . n 
F 3 56  ARG 56  54  54  ARG ARG F . n 
F 3 57  THR 57  55  55  THR THR F . n 
F 3 58  LEU 58  56  56  LEU LEU F . n 
F 3 59  SER 59  57  57  SER SER F . n 
F 3 60  ASP 60  58  58  ASP ASP F . n 
F 3 61  TYR 61  59  59  TYR TYR F . n 
F 3 62  ASN 62  60  60  ASN ASN F . n 
F 3 63  ILE 63  61  61  ILE ILE F . n 
F 3 64  GLN 64  62  62  GLN GLN F . n 
F 3 65  LYS 65  63  63  LYS LYS F . n 
F 3 66  GLU 66  64  64  GLU GLU F . n 
F 3 67  SER 67  65  65  SER SER F . n 
F 3 68  THR 68  66  66  THR THR F . n 
F 3 69  LEU 69  67  67  LEU LEU F . n 
F 3 70  HIS 70  68  68  HIS HIS F . n 
F 3 71  LEU 71  69  69  LEU LEU F . n 
F 3 72  VAL 72  70  70  VAL VAL F . n 
F 3 73  LEU 73  71  71  LEU LEU F . n 
F 3 74  ARG 74  72  72  ARG ARG F . n 
F 3 75  LEU 75  73  73  LEU LEU F . n 
F 3 76  ARG 76  74  74  ARG ARG F . n 
F 3 77  GLY 77  75  75  GLY GLY F . n 
F 3 78  GLY 78  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 PO4 ? ? PO4 ? ? '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 PO4 1  401 3   PO4 PO4 C . 
H 5 AR6 1  401 401 AR6 AR6 D . 
I 6 HOH 1  401 30  HOH HOH A . 
I 6 HOH 2  402 21  HOH HOH A . 
I 6 HOH 3  403 11  HOH HOH A . 
I 6 HOH 4  404 16  HOH HOH A . 
I 6 HOH 5  405 32  HOH HOH A . 
I 6 HOH 6  406 31  HOH HOH A . 
I 6 HOH 7  407 7   HOH HOH A . 
I 6 HOH 8  408 35  HOH HOH A . 
I 6 HOH 9  409 33  HOH HOH A . 
J 6 HOH 1  401 25  HOH HOH B . 
J 6 HOH 2  402 9   HOH HOH B . 
J 6 HOH 3  403 22  HOH HOH B . 
J 6 HOH 4  404 19  HOH HOH B . 
J 6 HOH 5  405 8   HOH HOH B . 
J 6 HOH 6  406 23  HOH HOH B . 
J 6 HOH 7  407 10  HOH HOH B . 
J 6 HOH 8  408 1   HOH HOH B . 
J 6 HOH 9  409 17  HOH HOH B . 
J 6 HOH 10 410 18  HOH HOH B . 
K 6 HOH 1  501 26  HOH HOH C . 
K 6 HOH 2  502 28  HOH HOH C . 
K 6 HOH 3  503 4   HOH HOH C . 
K 6 HOH 4  504 3   HOH HOH C . 
K 6 HOH 5  505 12  HOH HOH C . 
L 6 HOH 1  501 13  HOH HOH D . 
L 6 HOH 2  502 20  HOH HOH D . 
L 6 HOH 3  503 14  HOH HOH D . 
L 6 HOH 4  504 36  HOH HOH D . 
L 6 HOH 5  505 34  HOH HOH D . 
L 6 HOH 6  506 29  HOH HOH D . 
L 6 HOH 7  507 27  HOH HOH D . 
L 6 HOH 8  508 5   HOH HOH D . 
L 6 HOH 9  509 24  HOH HOH D . 
M 6 HOH 1  101 2   HOH HOH F . 
M 6 HOH 2  102 15  HOH HOH F . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 41  ? CG    ? A GLN 41 CG    
2  1 Y 1 A GLN 41  ? CD    ? A GLN 41 CD    
3  1 Y 1 A GLN 41  ? OE1   ? A GLN 41 OE1   
4  1 Y 1 A GLN 41  ? NE2   ? A GLN 41 NE2   
5  1 Y 1 B GLN 41  ? CG    ? B GLN 41 CG    
6  1 Y 1 B GLN 41  ? CD    ? B GLN 41 CD    
7  1 Y 1 B GLN 41  ? OE1   ? B GLN 41 OE1   
8  1 Y 1 B GLN 41  ? NE2   ? B GLN 41 NE2   
9  1 N 1 D AR6 401 ? N1    ? H AR6 1  N1    
10 1 N 1 D AR6 401 ? C2    ? H AR6 1  C2    
11 1 N 1 D AR6 401 ? N3    ? H AR6 1  N3    
12 1 N 1 D AR6 401 ? C4    ? H AR6 1  C4    
13 1 N 1 D AR6 401 ? C5    ? H AR6 1  C5    
14 1 N 1 D AR6 401 ? C6    ? H AR6 1  C6    
15 1 N 1 D AR6 401 ? N6    ? H AR6 1  N6    
16 1 N 1 D AR6 401 ? N7    ? H AR6 1  N7    
17 1 N 1 D AR6 401 ? C8    ? H AR6 1  C8    
18 1 N 1 D AR6 401 ? N9    ? H AR6 1  N9    
19 1 N 1 D AR6 401 ? PA    ? H AR6 1  PA    
20 1 N 1 D AR6 401 ? "C1'" ? H AR6 1  "C1'" 
21 1 N 1 D AR6 401 ? O1A   ? H AR6 1  O1A   
22 1 N 1 D AR6 401 ? "C2'" ? H AR6 1  "C2'" 
23 1 N 1 D AR6 401 ? "O2'" ? H AR6 1  "O2'" 
24 1 N 1 D AR6 401 ? O2A   ? H AR6 1  O2A   
25 1 N 1 D AR6 401 ? "C3'" ? H AR6 1  "C3'" 
26 1 N 1 D AR6 401 ? "O3'" ? H AR6 1  "O3'" 
27 1 N 1 D AR6 401 ? "C4'" ? H AR6 1  "C4'" 
28 1 N 1 D AR6 401 ? "O4'" ? H AR6 1  "O4'" 
29 1 N 1 D AR6 401 ? "C5'" ? H AR6 1  "C5'" 
30 1 N 1 D AR6 401 ? "O5'" ? H 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   ? ? ? '(1.19.2_4158: ???)' 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                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8K6I 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.377 
_cell.length_a_esd                 ? 
_cell.length_b                     165.308 
_cell.length_b_esd                 ? 
_cell.length_c                     224.652 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8K6I 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 2 21 21' 
_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                   8K6I 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.01 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          59.07 
_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    'Sodium Chloride, PEG8000, 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         2023-06-04 
_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   0.979183 
_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 BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979183 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8K6I 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.19 
_reflns.d_resolution_low                               41.33 
_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                                     36304 
_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                           91 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.56 
_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                                   0.75 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    3.19 
_reflns_shell.d_res_low                                     3.3 
_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                             1662 
_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                                  0.69 
_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                                 8K6I 
_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                            3.19 
_refine.ls_d_res_low                             41.33 
_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                     33338 
_refine.ls_number_reflns_R_free                  1662 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.15 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2933 
_refine.ls_R_factor_R_free                       0.3148 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2922 
_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                          0.00 
_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       MLHL 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 33.47 
_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                            0.45 
_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.details                          ? 
_refine_hist.d_res_high                       3.19 
_refine_hist.d_res_low                        41.33 
_refine_hist.number_atoms_solvent             35 
_refine_hist.number_atoms_total               12503 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        12449 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         19 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.023  ? 12708 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 2.443  ? 17175 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.989 ? 4810  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.168  ? 1934  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 2203  ? 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' 3.19 3.28  . . 122 2522 90.00 . . . . 0.3397 . . . . . . . . . . . 0.3480 
'X-RAY DIFFRACTION' 3.28 3.39  . . 123 2591 90.00 . . . . 0.3301 . . . . . . . . . . . 0.3474 
'X-RAY DIFFRACTION' 3.39 3.51  . . 141 2705 95.00 . . . . 0.2892 . . . . . . . . . . . 0.2988 
'X-RAY DIFFRACTION' 3.51 3.65  . . 147 2654 93.00 . . . . 0.3007 . . . . . . . . . . . 0.3753 
'X-RAY DIFFRACTION' 3.65 3.82  . . 147 2663 93.00 . . . . 0.2905 . . . . . . . . . . . 0.3277 
'X-RAY DIFFRACTION' 3.82 4.02  . . 146 2585 91.00 . . . . 0.2856 . . . . . . . . . . . 0.3305 
'X-RAY DIFFRACTION' 4.02 4.27  . . 117 2583 90.00 . . . . 0.2923 . . . . . . . . . . . 0.3170 
'X-RAY DIFFRACTION' 4.27 4.60  . . 163 2606 90.00 . . . . 0.2697 . . . . . . . . . . . 0.2896 
'X-RAY DIFFRACTION' 4.60 5.06  . . 135 2616 90.00 . . . . 0.2740 . . . . . . . . . . . 0.2736 
'X-RAY DIFFRACTION' 5.06 5.79  . . 144 2650 90.00 . . . . 0.3123 . . . . . . . . . . . 0.3190 
'X-RAY DIFFRACTION' 5.79 7.29  . . 128 2651 89.00 . . . . 0.3055 . . . . . . . . . . . 0.3146 
'X-RAY DIFFRACTION' 7.29 41.33 . . 149 2850 92.00 . . . . 0.2590 . . . . . . . . . . . 0.2781 
# 
_struct.entry_id                     8K6I 
_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        8K6I 
_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 5 ? 
I N N 6 ? 
J N N 6 ? 
K N N 6 ? 
L N N 6 ? 
M N N 6 ? 
# 
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 8K6I             8K6I       ? 2 ? 1 
3 UNP UBC_HUMAN        P0CG48     ? 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 8K6I A 1 ? 375 ? A0A8C6VAB1 1  ? 375 ? 1  375 
2 1 8K6I B 1 ? 375 ? A0A8C6VAB1 1  ? 375 ? 1  375 
3 2 8K6I C 1 ? 352 ? 8K6I       19 ? 370 ? 19 370 
4 2 8K6I D 1 ? 352 ? 8K6I       19 ? 370 ? 19 370 
5 3 8K6I E 3 ? 78  ? P0CG48     1  ? 76  ? 1  76  
6 3 8K6I F 3 ? 78  ? P0CG48     1  ? 76  ? 1  76  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
5 8K6I GLY E 1 ? UNP P0CG48 ? ? 'expression tag' -1 1 
5 8K6I SER E 2 ? UNP P0CG48 ? ? 'expression tag' 0  2 
6 8K6I GLY F 1 ? UNP P0CG48 ? ? 'expression tag' -1 3 
6 8K6I SER F 2 ? UNP P0CG48 ? ? 'expression tag' 0  4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 LYS A 84  ? ASN A 92  ? LYS A 84  ASN A 92  1 ? 9  
HELX_P HELX_P3  AA3 PRO A 112 ? ARG A 116 ? PRO A 112 ARG A 116 5 ? 5  
HELX_P HELX_P4  AA4 GLU A 117 ? THR A 126 ? GLU A 117 THR A 126 1 ? 10 
HELX_P HELX_P5  AA5 GLN A 137 ? ALA A 144 ? GLN A 137 ALA A 144 1 ? 8  
HELX_P HELX_P6  AA6 ALA A 181 ? GLU A 195 ? ALA A 181 GLU A 195 1 ? 15 
HELX_P HELX_P7  AA7 GLU A 205 ? CYS A 217 ? GLU A 205 CYS A 217 1 ? 13 
HELX_P HELX_P8  AA8 PHE A 223 ? SER A 233 ? PHE A 223 SER A 233 1 ? 11 
HELX_P HELX_P9  AA9 GLY A 251 ? CYS A 257 ? GLY A 251 CYS A 257 1 ? 7  
HELX_P HELX_P10 AB1 GLU A 276 ? MET A 283 ? GLU A 276 MET A 283 1 ? 8  
HELX_P HELX_P11 AB2 ARG A 290 ? ALA A 295 ? ARG A 290 ALA A 295 1 ? 6  
HELX_P HELX_P12 AB3 GLY A 308 ? THR A 318 ? GLY A 308 THR A 318 1 ? 11 
HELX_P HELX_P13 AB4 VAL A 339 ? ALA A 347 ? VAL A 339 ALA A 347 1 ? 9  
HELX_P HELX_P14 AB5 THR A 351 ? TRP A 356 ? THR A 351 TRP A 356 5 ? 6  
HELX_P HELX_P15 AB6 LYS A 359 ? GLY A 366 ? LYS A 359 GLY A 366 1 ? 8  
HELX_P HELX_P16 AB7 PRO A 367 ? LYS A 373 ? PRO A 367 LYS A 373 5 ? 7  
HELX_P HELX_P17 AB8 GLY B 55  ? LYS B 61  ? GLY B 55  LYS B 61  1 ? 7  
HELX_P HELX_P18 AB9 ASP B 81  ? TRP B 86  ? ASP B 81  TRP B 86  1 ? 6  
HELX_P HELX_P19 AC1 TRP B 86  ? TYR B 91  ? TRP B 86  TYR B 91  1 ? 6  
HELX_P HELX_P20 AC2 PRO B 112 ? THR B 126 ? PRO B 112 THR B 126 1 ? 15 
HELX_P HELX_P21 AC3 GLN B 137 ? SER B 141 ? GLN B 137 SER B 141 1 ? 5  
HELX_P HELX_P22 AC4 ALA B 181 ? GLU B 195 ? ALA B 181 GLU B 195 1 ? 15 
HELX_P HELX_P23 AC5 ILE B 208 ? LEU B 216 ? ILE B 208 LEU B 216 1 ? 9  
HELX_P HELX_P24 AC6 ASP B 222 ? THR B 229 ? ASP B 222 THR B 229 1 ? 8  
HELX_P HELX_P25 AC7 GLY B 251 ? CYS B 257 ? GLY B 251 CYS B 257 1 ? 7  
HELX_P HELX_P26 AC8 PRO B 258 ? ALA B 260 ? PRO B 258 ALA B 260 5 ? 3  
HELX_P HELX_P27 AC9 GLN B 263 ? GLY B 268 ? GLN B 263 GLY B 268 5 ? 6  
HELX_P HELX_P28 AD1 GLY B 273 ? MET B 283 ? GLY B 273 MET B 283 1 ? 11 
HELX_P HELX_P29 AD2 ARG B 290 ? ALA B 295 ? ARG B 290 ALA B 295 1 ? 6  
HELX_P HELX_P30 AD3 GLY B 308 ? ALA B 319 ? GLY B 308 ALA B 319 1 ? 12 
HELX_P HELX_P31 AD4 TYR B 337 ? SER B 348 ? TYR B 337 SER B 348 1 ? 12 
HELX_P HELX_P32 AD5 LYS B 359 ? GLY B 366 ? LYS B 359 GLY B 366 1 ? 8  
HELX_P HELX_P33 AD6 LEU C 8   ? SER C 16  ? LEU C 26  SER C 34  1 ? 9  
HELX_P HELX_P34 AD7 ASP C 20  ? LYS C 34  ? ASP C 38  LYS C 52  1 ? 15 
HELX_P HELX_P35 AD8 PHE C 45  ? PHE C 54  ? PHE C 63  PHE C 72  1 ? 10 
HELX_P HELX_P36 AD9 ASN C 57  ? ASN C 72  ? ASN C 75  ASN C 90  1 ? 16 
HELX_P HELX_P37 AE1 SER C 77  ? ALA C 88  ? SER C 95  ALA C 106 1 ? 12 
HELX_P HELX_P38 AE2 GLU C 99  ? LYS C 117 ? GLU C 117 LYS C 135 1 ? 19 
HELX_P HELX_P39 AE3 LEU C 128 ? LYS C 136 ? LEU C 146 LYS C 154 1 ? 9  
HELX_P HELX_P40 AE4 ASP C 151 ? LEU C 158 ? ASP C 169 LEU C 176 1 ? 8  
HELX_P HELX_P41 AE5 GLU C 168 ? LYS C 172 ? GLU C 186 LYS C 190 5 ? 5  
HELX_P HELX_P42 AE6 GLY C 228 ? LYS C 233 ? GLY C 246 LYS C 251 1 ? 6  
HELX_P HELX_P43 AE7 THR C 245 ? LYS C 261 ? THR C 263 LYS C 279 1 ? 17 
HELX_P HELX_P44 AE8 ASP C 265 ? TYR C 281 ? ASP C 283 TYR C 299 1 ? 17 
HELX_P HELX_P45 AE9 SER C 288 ? ASP C 294 ? SER C 306 ASP C 312 1 ? 7  
HELX_P HELX_P46 AF1 GLU C 298 ? LYS C 307 ? GLU C 316 LYS C 325 1 ? 10 
HELX_P HELX_P47 AF2 THR C 320 ? GLU C 343 ? THR C 338 GLU C 361 1 ? 24 
HELX_P HELX_P48 AF3 ASP D 20  ? GLY D 37  ? ASP D 38  GLY D 55  1 ? 18 
HELX_P HELX_P49 AF4 PHE D 45  ? LYS D 55  ? PHE D 63  LYS D 73  1 ? 11 
HELX_P HELX_P50 AF5 ASN D 57  ? ASN D 72  ? ASN D 75  ASN D 90  1 ? 16 
HELX_P HELX_P51 AF6 GLN D 79  ? ALA D 85  ? GLN D 97  ALA D 103 1 ? 7  
HELX_P HELX_P52 AF7 VAL D 87  ? LEU D 91  ? VAL D 105 LEU D 109 5 ? 5  
HELX_P HELX_P53 AF8 GLU D 99  ? TYR D 108 ? GLU D 117 TYR D 126 1 ? 10 
HELX_P HELX_P54 AF9 ALA D 109 ? GLU D 119 ? ALA D 127 GLU D 137 1 ? 11 
HELX_P HELX_P55 AG1 SER D 123 ? GLU D 127 ? SER D 141 GLU D 145 5 ? 5  
HELX_P HELX_P56 AG2 ASP D 130 ? LYS D 136 ? ASP D 148 LYS D 154 1 ? 7  
HELX_P HELX_P57 AG3 GLU D 152 ? LEU D 158 ? GLU D 170 LEU D 176 1 ? 7  
HELX_P HELX_P58 AG4 GLU D 168 ? ALA D 173 ? GLU D 186 ALA D 191 1 ? 6  
HELX_P HELX_P59 AG5 SER D 248 ? HIS D 260 ? SER D 266 HIS D 278 1 ? 13 
HELX_P HELX_P60 AG6 ASP D 265 ? LYS D 283 ? ASP D 283 LYS D 301 1 ? 19 
HELX_P HELX_P61 AG7 SER D 288 ? THR D 297 ? SER D 306 THR D 315 1 ? 10 
HELX_P HELX_P62 AG8 GLU D 298 ? LYS D 307 ? GLU D 316 LYS D 325 1 ? 10 
HELX_P HELX_P63 AG9 THR D 320 ? ARG D 325 ? THR D 338 ARG D 343 1 ? 6  
HELX_P HELX_P64 AH1 ALA D 327 ? GLU D 346 ? ALA D 345 GLU D 364 1 ? 20 
HELX_P HELX_P65 AH2 THR E 24  ? LYS E 35  ? THR E 22  LYS E 33  1 ? 12 
HELX_P HELX_P66 AH3 THR E 57  ? TYR E 61  ? THR E 55  TYR E 59  5 ? 5  
HELX_P HELX_P67 AH4 THR F 24  ? LYS F 35  ? THR F 22  LYS F 33  1 ? 12 
# 
_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 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 5 ? 
AA7 ? 2 ? 
AA8 ? 6 ? 
AA9 ? 3 ? 
AB1 ? 5 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 2 ? 
AB5 ? 5 ? 
AB6 ? 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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? parallel      
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? parallel      
AB6 3 4 ? anti-parallel 
AB6 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 LEU A 8   ? ASP A 11  ? LEU A 8   ASP A 11  
AA1 2 LYS A 18  ? PHE A 21  ? LYS A 18  PHE A 21  
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 LEU A 105 ? GLU A 107 ? LEU A 105 GLU A 107 
AA3 2 VAL A 134 ? ILE A 136 ? VAL A 134 ILE A 136 
AA4 1 ALA A 131 ? MET A 132 ? ALA A 131 MET A 132 
AA4 2 ILE A 357 ? SER A 358 ? ILE A 357 SER A 358 
AA5 1 TYR A 169 ? ALA A 170 ? TYR A 169 ALA A 170 
AA5 2 THR A 160 ? TYR A 166 ? THR A 160 TYR A 166 
AA5 3 LEU A 176 ? LEU A 178 ? LEU A 176 LEU A 178 
AA6 1 TYR A 169 ? ALA A 170 ? TYR A 169 ALA A 170 
AA6 2 THR A 160 ? TYR A 166 ? THR A 160 TYR A 166 
AA6 3 GLY A 150 ? SER A 155 ? GLY A 150 SER A 155 
AA6 4 THR A 297 ? SER A 300 ? THR A 297 SER A 300 
AA6 5 ILE A 329 ? ILE A 330 ? ILE A 329 ILE A 330 
AA7 1 LYS A 238 ? LEU A 242 ? LYS A 238 LEU A 242 
AA7 2 GLN A 246 ? ILE A 250 ? GLN A 246 ILE A 250 
AA8 1 ALA B 29  ? PRO B 32  ? ALA B 29  PRO B 32  
AA8 2 MET B 16  ? PHE B 21  ? MET B 16  PHE B 21  
AA8 3 LEU B 8   ? GLY B 13  ? LEU B 8   GLY B 13  
AA8 4 VAL B 103 ? GLU B 107 ? VAL B 103 GLU B 107 
AA8 5 ALA B 131 ? ILE B 136 ? ALA B 131 ILE B 136 
AA8 6 ILE B 357 ? SER B 358 ? ILE B 357 SER B 358 
AA9 1 TYR B 53  ? VAL B 54  ? TYR B 53  VAL B 54  
AA9 2 VAL B 35  ? GLY B 36  ? VAL B 35  GLY B 36  
AA9 3 LEU B 67  ? LYS B 68  ? LEU B 67  LYS B 68  
AB1 1 LEU B 176 ? ARG B 177 ? LEU B 176 ARG B 177 
AB1 2 THR B 160 ? TYR B 166 ? THR B 160 TYR B 166 
AB1 3 THR B 149 ? SER B 155 ? THR B 149 SER B 155 
AB1 4 THR B 297 ? GLY B 301 ? THR B 297 GLY B 301 
AB1 5 ILE B 329 ? ILE B 330 ? ILE B 329 ILE B 330 
AB2 1 SER B 239 ? GLU B 241 ? SER B 239 GLU B 241 
AB2 2 VAL B 247 ? THR B 249 ? VAL B 247 THR B 249 
AB3 1 ASN C 190 ? SER C 193 ? ASN C 208 SER C 211 
AB3 2 ARG C 214 ? PRO C 217 ? ARG C 232 PRO C 235 
AB4 1 THR D 191 ? SER D 193 ? THR D 209 SER D 211 
AB4 2 ARG D 214 ? VAL D 216 ? ARG D 232 VAL D 234 
AB5 1 THR E 14  ? LEU E 17  ? THR E 12  LEU E 15  
AB5 2 ILE E 5   ? LYS E 8   ? ILE E 3   LYS E 6   
AB5 3 THR E 68  ? LEU E 71  ? THR E 66  LEU E 69  
AB5 4 LEU E 45  ? PHE E 47  ? LEU E 43  PHE E 45  
AB5 5 LYS E 50  ? GLN E 51  ? LYS E 48  GLN E 49  
AB6 1 THR F 14  ? VAL F 19  ? THR F 12  VAL F 17  
AB6 2 MET F 3   ? LYS F 8   ? MET F 1   LYS F 6   
AB6 3 THR F 68  ? LEU F 73  ? THR F 66  LEU F 71  
AB6 4 GLN F 43  ? PHE F 47  ? GLN F 41  PHE F 45  
AB6 5 LYS F 50  ? GLN F 51  ? 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 N ASP A 11  ? N ASP A 11  O LYS A 18  ? O LYS A 18  
AA2 1 2 O TYR A 53  ? O TYR A 53  N GLY A 36  ? N GLY A 36  
AA2 2 3 N ARG A 37  ? N ARG A 37  O THR A 66  ? O THR A 66  
AA3 1 2 N GLU A 107 ? N GLU A 107 O ALA A 135 ? O ALA A 135 
AA4 1 2 N MET A 132 ? N MET A 132 O ILE A 357 ? O ILE A 357 
AA5 1 2 O TYR A 169 ? O TYR A 169 N TYR A 166 ? N TYR A 166 
AA5 2 3 N THR A 160 ? N THR A 160 O LEU A 178 ? O LEU A 178 
AA6 1 2 O TYR A 169 ? O TYR A 169 N TYR A 166 ? N TYR A 166 
AA6 2 3 O ILE A 165 ? O ILE A 165 N GLY A 150 ? N GLY A 150 
AA6 3 4 N MET A 153 ? N MET A 153 O VAL A 298 ? O VAL A 298 
AA6 4 5 N THR A 297 ? N THR A 297 O ILE A 330 ? O ILE A 330 
AA7 1 2 N TYR A 240 ? N TYR A 240 O ILE A 248 ? O ILE A 248 
AA8 1 2 O PHE B 31  ? O PHE B 31  N CYS B 17  ? N CYS B 17  
AA8 2 3 O LYS B 18  ? O LYS B 18  N ASP B 11  ? N ASP B 11  
AA8 3 4 N LEU B 8   ? N LEU B 8   O LEU B 104 ? O LEU B 104 
AA8 4 5 N GLU B 107 ? N GLU B 107 O ALA B 135 ? O ALA B 135 
AA8 5 6 N MET B 132 ? N MET B 132 O ILE B 357 ? O ILE B 357 
AA9 1 2 O TYR B 53  ? O TYR B 53  N GLY B 36  ? N GLY B 36  
AA9 2 3 N VAL B 35  ? N VAL B 35  O LYS B 68  ? O LYS B 68  
AB1 1 2 O LEU B 176 ? O LEU B 176 N THR B 162 ? N THR B 162 
AB1 2 3 O ILE B 165 ? O ILE B 165 N GLY B 150 ? N GLY B 150 
AB1 3 4 N MET B 153 ? N MET B 153 O VAL B 298 ? O VAL B 298 
AB1 4 5 N THR B 297 ? N THR B 297 O ILE B 330 ? O ILE B 330 
AB2 1 2 N TYR B 240 ? N TYR B 240 O ILE B 248 ? O ILE B 248 
AB3 1 2 N THR C 191 ? N THR C 209 O VAL C 216 ? O VAL C 234 
AB4 1 2 N THR D 191 ? N THR D 209 O VAL D 216 ? O VAL D 234 
AB5 1 2 O ILE E 15  ? O ILE E 13  N VAL E 7   ? N VAL E 5   
AB5 2 3 N PHE E 6   ? N PHE E 4   O LEU E 69  ? O LEU E 67  
AB5 3 4 O HIS E 70  ? O HIS E 68  N ILE E 46  ? N ILE E 44  
AB5 4 5 N PHE E 47  ? N PHE E 45  O LYS E 50  ? O LYS E 48  
AB6 1 2 O LEU F 17  ? O LEU F 15  N ILE F 5   ? N ILE F 3   
AB6 2 3 N LYS F 8   ? N LYS F 6   O LEU F 69  ? O LEU F 67  
AB6 3 4 O HIS F 70  ? O HIS F 68  N ILE F 46  ? N ILE F 44  
AB6 4 5 N PHE F 47  ? N PHE F 45  O LYS F 50  ? O LYS F 48  
# 
_pdbx_entry_details.entry_id                   8K6I 
_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 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            D 
_pdbx_validate_rmsd_bond.auth_comp_id_1            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_1             230 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            D 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_2             230 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.377 
_pdbx_validate_rmsd_bond.bond_target_value         1.474 
_pdbx_validate_rmsd_bond.bond_deviation            -0.097 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.014 
_pdbx_validate_rmsd_bond.linker_flag               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 N  A SER 14  ? ? CA A SER 14  ? ? C  A SER 14  ? ? 94.06  111.00 -16.94 2.70 N 
2  1 N  A ASP 24  ? ? CA A ASP 24  ? ? C  A ASP 24  ? ? 129.25 111.00 18.25  2.70 N 
3  1 N  A GLY 42  ? ? CA A GLY 42  ? ? C  A GLY 42  ? ? 95.18  113.10 -17.92 2.50 N 
4  1 N  A VAL 45  ? ? CA A VAL 45  ? ? CB A VAL 45  ? ? 128.76 111.50 17.26  2.20 N 
5  1 C  A ASN 111 ? ? N  A PRO 112 ? ? CA A PRO 112 ? ? 109.71 119.30 -9.59  1.50 Y 
6  1 N  A LYS 284 ? ? CA A LYS 284 ? ? C  A LYS 284 ? ? 91.82  111.00 -19.18 2.70 N 
7  1 N  B ARG 95  ? ? CA B ARG 95  ? ? C  B ARG 95  ? ? 130.98 111.00 19.98  2.70 N 
8  1 C  B ALA 108 ? ? N  B PRO 109 ? ? CA B PRO 109 ? ? 109.54 119.30 -9.76  1.50 Y 
9  1 CA C LEU 37  ? ? CB C LEU 37  ? ? CG C LEU 37  ? ? 132.60 115.30 17.30  2.30 N 
10 1 N  C GLU 137 ? ? CA C GLU 137 ? ? C  C GLU 137 ? ? 88.19  111.00 -22.81 2.70 N 
11 1 N  C LEU 181 ? ? CA C LEU 181 ? ? C  C LEU 181 ? ? 87.16  111.00 -23.84 2.70 N 
12 1 CB C ASN 182 ? ? CA C ASN 182 ? ? C  C ASN 182 ? ? 98.35  110.40 -12.05 2.00 N 
13 1 N  C ILE 216 ? ? CA C ILE 216 ? ? C  C ILE 216 ? ? 93.25  111.00 -17.75 2.70 N 
14 1 CA C LEU 228 ? ? CB C LEU 228 ? ? CG C LEU 228 ? ? 134.61 115.30 19.31  2.30 N 
15 1 N  C ALA 258 ? ? CA C ALA 258 ? ? C  C ALA 258 ? ? 89.21  111.00 -21.79 2.70 N 
16 1 N  C LEU 260 ? ? CA C LEU 260 ? ? C  C LEU 260 ? ? 91.09  111.00 -19.91 2.70 N 
17 1 N  D ALA 191 ? ? CA D ALA 191 ? ? C  D ALA 191 ? ? 91.01  111.00 -19.99 2.70 N 
18 1 N  D MET 217 ? ? CA D MET 217 ? ? C  D MET 217 ? ? 92.54  111.00 -18.46 2.70 N 
19 1 N  D SER 259 ? ? CA D SER 259 ? ? C  D SER 259 ? ? 127.85 111.00 16.85  2.70 N 
20 1 CB D ASP 337 ? ? CA D ASP 337 ? ? C  D ASP 337 ? ? 98.18  110.40 -12.22 2.00 N 
21 1 N  E PHE 45  ? ? CA E PHE 45  ? ? C  E PHE 45  ? ? 93.26  111.00 -17.74 2.70 N 
22 1 N  E ASP 58  ? ? CA E ASP 58  ? ? C  E ASP 58  ? ? 94.71  111.00 -16.29 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 HIS A 73  ? ? -146.99 20.85   
2  1 THR A 77  ? ? 56.59   -122.25 
3  1 ALA A 181 ? ? -156.87 -158.36 
4  1 GLU A 195 ? ? -90.22  37.41   
5  1 THR A 201 ? ? -141.63 -38.14  
6  1 GLU A 226 ? ? -139.63 -33.45  
7  1 SER A 234 ? ? -85.51  49.49   
8  1 PRO A 243 ? ? -66.04  6.38    
9  1 LYS A 284 ? ? -147.36 15.40   
10 1 ASN A 296 ? ? -156.97 52.76   
11 1 THR A 304 ? ? -94.47  41.81   
12 1 GLU A 334 ? ? -94.94  45.52   
13 1 LYS A 373 ? ? -132.37 -57.91  
14 1 SER B 14  ? ? 52.19   -136.45 
15 1 THR B 77  ? ? 74.54   -56.88  
16 1 THR B 89  ? ? -121.10 -55.64  
17 1 TYR B 91  ? ? -129.73 -72.44  
18 1 ASN B 128 ? ? 37.44   52.80   
19 1 SER B 145 ? ? -69.07  4.52    
20 1 ALA B 181 ? ? -165.96 -141.62 
21 1 SER B 234 ? ? -98.65  34.76   
22 1 ILE B 250 ? ? -109.74 -61.09  
23 1 PRO B 258 ? ? -79.19  31.09   
24 1 SER B 271 ? ? -103.86 -167.07 
25 1 ASN B 296 ? ? -145.61 57.14   
26 1 THR B 304 ? ? -92.06  43.90   
27 1 PRO B 322 ? ? -46.66  155.29  
28 1 GLU B 334 ? ? -108.71 50.75   
29 1 SER B 368 ? ? -101.42 42.43   
30 1 LYS B 373 ? ? -143.01 -34.09  
31 1 ASP C 38  ? ? -125.19 -167.69 
32 1 GLN C 74  ? ? 38.34   44.93   
33 1 ASN C 75  ? ? -109.25 65.45   
34 1 ASN C 90  ? ? -119.01 69.99   
35 1 SER C 141 ? ? -150.98 63.55   
36 1 TYR C 157 ? ? -143.55 -30.02  
37 1 ASN C 184 ? ? -134.11 -81.02  
38 1 ALA C 212 ? ? -118.33 55.97   
39 1 ASN C 220 ? ? -103.52 64.36   
40 1 GLU C 241 ? ? 57.39   18.12   
41 1 VAL C 257 ? ? -132.59 -31.10  
42 1 THR C 315 ? ? -93.56  49.21   
43 1 GLU C 364 ? ? -148.75 15.25   
44 1 ASP D 38  ? ? -118.20 -166.87 
45 1 ASN D 75  ? ? -102.00 70.63   
46 1 GLU D 104 ? ? 57.35   10.84   
47 1 VAL D 105 ? ? -130.31 -30.63  
48 1 PRO D 113 ? ? -75.07  25.03   
49 1 LYS D 114 ? ? -106.39 -64.10  
50 1 THR D 160 ? ? 55.72   -143.94 
51 1 GLU D 162 ? ? 73.70   -12.25  
52 1 ASP D 183 ? ? 76.91   -0.18   
53 1 ASN D 184 ? ? -126.42 -81.18  
54 1 GLN D 192 ? ? 82.23   -4.61   
55 1 LYS D 198 ? ? -105.27 66.37   
56 1 ASN D 220 ? ? -115.46 50.20   
57 1 GLU D 241 ? ? -100.86 55.29   
58 1 LYS D 242 ? ? -154.41 36.07   
59 1 TYR D 247 ? ? 84.15   -7.61   
60 1 SER D 261 ? ? 50.39   -138.32 
61 1 HIS D 278 ? ? -106.82 53.61   
62 1 ASP D 337 ? ? -100.66 79.12   
63 1 LYS D 344 ? ? 82.46   8.67    
64 1 ARG D 365 ? ? -143.72 -12.40  
65 1 MET E 1   ? ? -155.98 62.93   
66 1 THR E 7   ? ? -109.72 -155.61 
67 1 GLN E 62  ? ? -106.27 -154.80 
68 1 PRO F 19  ? ? -66.79  1.11    
69 1 LYS F 63  ? ? 55.92   -128.58 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 409 ? 5.81  . 
2 1 O ? B HOH 410 ? 6.14  . 
3 1 O ? C HOH 504 ? 6.15  . 
4 1 O ? C HOH 505 ? 7.65  . 
5 1 O ? D HOH 506 ? 10.63 . 
6 1 O ? D HOH 507 ? 11.08 . 
7 1 O ? D HOH 508 ? 11.31 . 
8 1 O ? D HOH 509 ? 11.58 . 
# 
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 GLY 46  ? A GLY 46  
6  1 Y 1 A MET 47  ? A MET 47  
7  1 Y 1 A GLY 48  ? A GLY 48  
8  1 Y 1 A GLN 49  ? A GLN 49  
9  1 Y 1 A LYS 50  ? A LYS 50  
10 1 Y 1 B MET 1   ? B MET 1   
11 1 Y 1 B GLU 2   ? B GLU 2   
12 1 Y 1 B GLU 3   ? B GLU 3   
13 1 Y 1 B GLU 4   ? B GLU 4   
14 1 Y 1 C MET 19  ? C MET 1   
15 1 Y 1 C SER 20  ? C SER 2   
16 1 Y 1 C TYR 21  ? C TYR 3   
17 1 Y 1 C GLN 22  ? C GLN 4   
18 1 Y 1 C LYS 23  ? C LYS 5   
19 1 Y 1 C ILE 24  ? C ILE 6   
20 1 Y 1 C SER 53  ? C SER 35  
21 1 Y 1 C LEU 54  ? C LEU 36  
22 1 Y 1 C GLY 55  ? C GLY 37  
23 1 Y 1 C LYS 56  ? C LYS 38  
24 1 Y 1 C LYS 57  ? C LYS 39  
25 1 Y 1 C LYS 58  ? C LYS 40  
26 1 Y 1 C GLU 59  ? C GLU 41  
27 1 Y 1 C PHE 60  ? C PHE 42  
28 1 Y 1 C SER 61  ? C SER 43  
29 1 Y 1 C PRO 107 ? C PRO 89  
30 1 Y 1 C ARG 108 ? C ARG 90  
31 1 Y 1 C LEU 109 ? C LEU 91  
32 1 Y 1 C THR 163 ? C THR 145 
33 1 Y 1 C GLU 164 ? C GLU 146 
34 1 Y 1 C GLU 370 ? C GLU 352 
35 1 Y 1 D MET 19  ? D MET 1   
36 1 Y 1 D SER 20  ? D SER 2   
37 1 Y 1 D TYR 21  ? D TYR 3   
38 1 Y 1 D LYS 56  ? D LYS 38  
39 1 Y 1 D LYS 57  ? D LYS 39  
40 1 Y 1 D LYS 369 ? D LYS 351 
41 1 Y 1 D GLU 370 ? D GLU 352 
42 1 Y 1 F GLY -1  ? F GLY 1   
# 
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 
CYS N      N N N 133 
CYS CA     C N R 134 
CYS C      C N N 135 
CYS O      O N N 136 
CYS CB     C N N 137 
CYS SG     S N N 138 
CYS OXT    O N N 139 
CYS H      H N N 140 
CYS H2     H N N 141 
CYS HA     H N N 142 
CYS HB2    H N N 143 
CYS HB3    H N N 144 
CYS HG     H N N 145 
CYS HXT    H N N 146 
GLN N      N N N 147 
GLN CA     C N S 148 
GLN C      C N N 149 
GLN O      O N N 150 
GLN CB     C N N 151 
GLN CG     C N N 152 
GLN CD     C N N 153 
GLN OE1    O N N 154 
GLN NE2    N N N 155 
GLN OXT    O N N 156 
GLN H      H N N 157 
GLN H2     H N N 158 
GLN HA     H N N 159 
GLN HB2    H N N 160 
GLN HB3    H N N 161 
GLN HG2    H N N 162 
GLN HG3    H N N 163 
GLN HE21   H N N 164 
GLN HE22   H N N 165 
GLN HXT    H N N 166 
GLU N      N N N 167 
GLU CA     C N S 168 
GLU C      C N N 169 
GLU O      O N N 170 
GLU CB     C N N 171 
GLU CG     C N N 172 
GLU CD     C N N 173 
GLU OE1    O N N 174 
GLU OE2    O N N 175 
GLU OXT    O N N 176 
GLU H      H N N 177 
GLU H2     H N N 178 
GLU HA     H N N 179 
GLU HB2    H N N 180 
GLU HB3    H N N 181 
GLU HG2    H N N 182 
GLU HG3    H N N 183 
GLU HE2    H N N 184 
GLU HXT    H N N 185 
GLY N      N N N 186 
GLY CA     C N N 187 
GLY C      C N N 188 
GLY O      O N N 189 
GLY OXT    O N N 190 
GLY H      H N N 191 
GLY H2     H N N 192 
GLY HA2    H N N 193 
GLY HA3    H N N 194 
GLY HXT    H N N 195 
HIS N      N N N 196 
HIS CA     C N S 197 
HIS C      C N N 198 
HIS O      O N N 199 
HIS CB     C N N 200 
HIS CG     C Y N 201 
HIS ND1    N Y N 202 
HIS CD2    C Y N 203 
HIS CE1    C Y N 204 
HIS NE2    N Y N 205 
HIS OXT    O N N 206 
HIS H      H N N 207 
HIS H2     H N N 208 
HIS HA     H N N 209 
HIS HB2    H N N 210 
HIS HB3    H N N 211 
HIS HD1    H N N 212 
HIS HD2    H N N 213 
HIS HE1    H N N 214 
HIS HE2    H N N 215 
HIS HXT    H N N 216 
HOH O      O N N 217 
HOH H1     H N N 218 
HOH H2     H N N 219 
ILE N      N N N 220 
ILE CA     C N S 221 
ILE C      C N N 222 
ILE O      O N N 223 
ILE CB     C N S 224 
ILE CG1    C N N 225 
ILE CG2    C N N 226 
ILE CD1    C N N 227 
ILE OXT    O N N 228 
ILE H      H N N 229 
ILE H2     H N N 230 
ILE HA     H N N 231 
ILE HB     H N N 232 
ILE HG12   H N N 233 
ILE HG13   H N N 234 
ILE HG21   H N N 235 
ILE HG22   H N N 236 
ILE HG23   H N N 237 
ILE HD11   H N N 238 
ILE HD12   H N N 239 
ILE HD13   H N N 240 
ILE HXT    H N N 241 
LEU N      N N N 242 
LEU CA     C N S 243 
LEU C      C N N 244 
LEU O      O N N 245 
LEU CB     C N N 246 
LEU CG     C N N 247 
LEU CD1    C N N 248 
LEU CD2    C N N 249 
LEU OXT    O N N 250 
LEU H      H N N 251 
LEU H2     H N N 252 
LEU HA     H N N 253 
LEU HB2    H N N 254 
LEU HB3    H N N 255 
LEU HG     H N N 256 
LEU HD11   H N N 257 
LEU HD12   H N N 258 
LEU HD13   H N N 259 
LEU HD21   H N N 260 
LEU HD22   H N N 261 
LEU HD23   H N N 262 
LEU HXT    H N N 263 
LYS N      N N N 264 
LYS CA     C N S 265 
LYS C      C N N 266 
LYS O      O N N 267 
LYS CB     C N N 268 
LYS CG     C N N 269 
LYS CD     C N N 270 
LYS CE     C N N 271 
LYS NZ     N N N 272 
LYS OXT    O N N 273 
LYS H      H N N 274 
LYS H2     H N N 275 
LYS HA     H N N 276 
LYS HB2    H N N 277 
LYS HB3    H N N 278 
LYS HG2    H N N 279 
LYS HG3    H N N 280 
LYS HD2    H N N 281 
LYS HD3    H N N 282 
LYS HE2    H N N 283 
LYS HE3    H N N 284 
LYS HZ1    H N N 285 
LYS HZ2    H N N 286 
LYS HZ3    H N N 287 
LYS HXT    H N N 288 
MET N      N N N 289 
MET CA     C N S 290 
MET C      C N N 291 
MET O      O N N 292 
MET CB     C N N 293 
MET CG     C N N 294 
MET SD     S N N 295 
MET CE     C N N 296 
MET OXT    O N N 297 
MET H      H N N 298 
MET H2     H N N 299 
MET HA     H N N 300 
MET HB2    H N N 301 
MET HB3    H N N 302 
MET HG2    H N N 303 
MET HG3    H N N 304 
MET HE1    H N N 305 
MET HE2    H N N 306 
MET HE3    H N N 307 
MET HXT    H N N 308 
PHE N      N N N 309 
PHE CA     C N S 310 
PHE C      C N N 311 
PHE O      O N N 312 
PHE CB     C N N 313 
PHE CG     C Y N 314 
PHE CD1    C Y N 315 
PHE CD2    C Y N 316 
PHE CE1    C Y N 317 
PHE CE2    C Y N 318 
PHE CZ     C Y N 319 
PHE OXT    O N N 320 
PHE H      H N N 321 
PHE H2     H N N 322 
PHE HA     H N N 323 
PHE HB2    H N N 324 
PHE HB3    H N N 325 
PHE HD1    H N N 326 
PHE HD2    H N N 327 
PHE HE1    H N N 328 
PHE HE2    H N N 329 
PHE HZ     H N N 330 
PHE HXT    H N N 331 
PO4 P      P N N 332 
PO4 O1     O N N 333 
PO4 O2     O N N 334 
PO4 O3     O N N 335 
PO4 O4     O N N 336 
PRO N      N N N 337 
PRO CA     C N S 338 
PRO C      C N N 339 
PRO O      O N N 340 
PRO CB     C N N 341 
PRO CG     C N N 342 
PRO CD     C N N 343 
PRO OXT    O N N 344 
PRO H      H N N 345 
PRO HA     H N N 346 
PRO HB2    H N N 347 
PRO HB3    H N N 348 
PRO HG2    H N N 349 
PRO HG3    H N N 350 
PRO HD2    H N N 351 
PRO HD3    H N N 352 
PRO HXT    H N N 353 
SER N      N N N 354 
SER CA     C N S 355 
SER C      C N N 356 
SER O      O N N 357 
SER CB     C N N 358 
SER OG     O N N 359 
SER OXT    O N N 360 
SER H      H N N 361 
SER H2     H N N 362 
SER HA     H N N 363 
SER HB2    H N N 364 
SER HB3    H N N 365 
SER HG     H N N 366 
SER HXT    H N N 367 
THR N      N N N 368 
THR CA     C N S 369 
THR C      C N N 370 
THR O      O N N 371 
THR CB     C N R 372 
THR OG1    O N N 373 
THR CG2    C N N 374 
THR OXT    O N N 375 
THR H      H N N 376 
THR H2     H N N 377 
THR HA     H N N 378 
THR HB     H N N 379 
THR HG1    H N N 380 
THR HG21   H N N 381 
THR HG22   H N N 382 
THR HG23   H N N 383 
THR HXT    H N N 384 
TRP N      N N N 385 
TRP CA     C N S 386 
TRP C      C N N 387 
TRP O      O N N 388 
TRP CB     C N N 389 
TRP CG     C Y N 390 
TRP CD1    C Y N 391 
TRP CD2    C Y N 392 
TRP NE1    N Y N 393 
TRP CE2    C Y N 394 
TRP CE3    C Y N 395 
TRP CZ2    C Y N 396 
TRP CZ3    C Y N 397 
TRP CH2    C Y N 398 
TRP OXT    O N N 399 
TRP H      H N N 400 
TRP H2     H N N 401 
TRP HA     H N N 402 
TRP HB2    H N N 403 
TRP HB3    H N N 404 
TRP HD1    H N N 405 
TRP HE1    H N N 406 
TRP HE3    H N N 407 
TRP HZ2    H N N 408 
TRP HZ3    H N N 409 
TRP HH2    H N N 410 
TRP HXT    H N N 411 
TYR N      N N N 412 
TYR CA     C N S 413 
TYR C      C N N 414 
TYR O      O N N 415 
TYR CB     C N N 416 
TYR CG     C Y N 417 
TYR CD1    C Y N 418 
TYR CD2    C Y N 419 
TYR CE1    C Y N 420 
TYR CE2    C Y N 421 
TYR CZ     C Y N 422 
TYR OH     O N N 423 
TYR OXT    O N N 424 
TYR H      H N N 425 
TYR H2     H N N 426 
TYR HA     H N N 427 
TYR HB2    H N N 428 
TYR HB3    H N N 429 
TYR HD1    H N N 430 
TYR HD2    H N N 431 
TYR HE1    H N N 432 
TYR HE2    H N N 433 
TYR HH     H N N 434 
TYR HXT    H N N 435 
VAL N      N N N 436 
VAL CA     C N S 437 
VAL C      C N N 438 
VAL O      O N N 439 
VAL CB     C N N 440 
VAL CG1    C N N 441 
VAL CG2    C N N 442 
VAL OXT    O N N 443 
VAL H      H N N 444 
VAL H2     H N N 445 
VAL HA     H N N 446 
VAL HB     H N N 447 
VAL HG11   H N N 448 
VAL HG12   H N N 449 
VAL HG13   H N N 450 
VAL HG21   H N N 451 
VAL HG22   H N N 452 
VAL HG23   H N N 453 
VAL HXT    H N N 454 
# 
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 
CYS N     CA     sing N N 132 
CYS N     H      sing N N 133 
CYS N     H2     sing N N 134 
CYS CA    C      sing N N 135 
CYS CA    CB     sing N N 136 
CYS CA    HA     sing N N 137 
CYS C     O      doub N N 138 
CYS C     OXT    sing N N 139 
CYS CB    SG     sing N N 140 
CYS CB    HB2    sing N N 141 
CYS CB    HB3    sing N N 142 
CYS SG    HG     sing N N 143 
CYS OXT   HXT    sing N N 144 
GLN N     CA     sing N N 145 
GLN N     H      sing N N 146 
GLN N     H2     sing N N 147 
GLN CA    C      sing N N 148 
GLN CA    CB     sing N N 149 
GLN CA    HA     sing N N 150 
GLN C     O      doub N N 151 
GLN C     OXT    sing N N 152 
GLN CB    CG     sing N N 153 
GLN CB    HB2    sing N N 154 
GLN CB    HB3    sing N N 155 
GLN CG    CD     sing N N 156 
GLN CG    HG2    sing N N 157 
GLN CG    HG3    sing N N 158 
GLN CD    OE1    doub N N 159 
GLN CD    NE2    sing N N 160 
GLN NE2   HE21   sing N N 161 
GLN NE2   HE22   sing N N 162 
GLN OXT   HXT    sing N N 163 
GLU N     CA     sing N N 164 
GLU N     H      sing N N 165 
GLU N     H2     sing N N 166 
GLU CA    C      sing N N 167 
GLU CA    CB     sing N N 168 
GLU CA    HA     sing N N 169 
GLU C     O      doub N N 170 
GLU C     OXT    sing N N 171 
GLU CB    CG     sing N N 172 
GLU CB    HB2    sing N N 173 
GLU CB    HB3    sing N N 174 
GLU CG    CD     sing N N 175 
GLU CG    HG2    sing N N 176 
GLU CG    HG3    sing N N 177 
GLU CD    OE1    doub N N 178 
GLU CD    OE2    sing N N 179 
GLU OE2   HE2    sing N N 180 
GLU OXT   HXT    sing N N 181 
GLY N     CA     sing N N 182 
GLY N     H      sing N N 183 
GLY N     H2     sing N N 184 
GLY CA    C      sing N N 185 
GLY CA    HA2    sing N N 186 
GLY CA    HA3    sing N N 187 
GLY C     O      doub N N 188 
GLY C     OXT    sing N N 189 
GLY OXT   HXT    sing N N 190 
HIS N     CA     sing N N 191 
HIS N     H      sing N N 192 
HIS N     H2     sing N N 193 
HIS CA    C      sing N N 194 
HIS CA    CB     sing N N 195 
HIS CA    HA     sing N N 196 
HIS C     O      doub N N 197 
HIS C     OXT    sing N N 198 
HIS CB    CG     sing N N 199 
HIS CB    HB2    sing N N 200 
HIS CB    HB3    sing N N 201 
HIS CG    ND1    sing Y N 202 
HIS CG    CD2    doub Y N 203 
HIS ND1   CE1    doub Y N 204 
HIS ND1   HD1    sing N N 205 
HIS CD2   NE2    sing Y N 206 
HIS CD2   HD2    sing N N 207 
HIS CE1   NE2    sing Y N 208 
HIS CE1   HE1    sing N N 209 
HIS NE2   HE2    sing N N 210 
HIS OXT   HXT    sing N N 211 
HOH O     H1     sing N N 212 
HOH O     H2     sing N N 213 
ILE N     CA     sing N N 214 
ILE N     H      sing N N 215 
ILE N     H2     sing N N 216 
ILE CA    C      sing N N 217 
ILE CA    CB     sing N N 218 
ILE CA    HA     sing N N 219 
ILE C     O      doub N N 220 
ILE C     OXT    sing N N 221 
ILE CB    CG1    sing N N 222 
ILE CB    CG2    sing N N 223 
ILE CB    HB     sing N N 224 
ILE CG1   CD1    sing N N 225 
ILE CG1   HG12   sing N N 226 
ILE CG1   HG13   sing N N 227 
ILE CG2   HG21   sing N N 228 
ILE CG2   HG22   sing N N 229 
ILE CG2   HG23   sing N N 230 
ILE CD1   HD11   sing N N 231 
ILE CD1   HD12   sing N N 232 
ILE CD1   HD13   sing N N 233 
ILE OXT   HXT    sing N N 234 
LEU N     CA     sing N N 235 
LEU N     H      sing N N 236 
LEU N     H2     sing N N 237 
LEU CA    C      sing N N 238 
LEU CA    CB     sing N N 239 
LEU CA    HA     sing N N 240 
LEU C     O      doub N N 241 
LEU C     OXT    sing N N 242 
LEU CB    CG     sing N N 243 
LEU CB    HB2    sing N N 244 
LEU CB    HB3    sing N N 245 
LEU CG    CD1    sing N N 246 
LEU CG    CD2    sing N N 247 
LEU CG    HG     sing N N 248 
LEU CD1   HD11   sing N N 249 
LEU CD1   HD12   sing N N 250 
LEU CD1   HD13   sing N N 251 
LEU CD2   HD21   sing N N 252 
LEU CD2   HD22   sing N N 253 
LEU CD2   HD23   sing N N 254 
LEU OXT   HXT    sing N N 255 
LYS N     CA     sing N N 256 
LYS N     H      sing N N 257 
LYS N     H2     sing N N 258 
LYS CA    C      sing N N 259 
LYS CA    CB     sing N N 260 
LYS CA    HA     sing N N 261 
LYS C     O      doub N N 262 
LYS C     OXT    sing N N 263 
LYS CB    CG     sing N N 264 
LYS CB    HB2    sing N N 265 
LYS CB    HB3    sing N N 266 
LYS CG    CD     sing N N 267 
LYS CG    HG2    sing N N 268 
LYS CG    HG3    sing N N 269 
LYS CD    CE     sing N N 270 
LYS CD    HD2    sing N N 271 
LYS CD    HD3    sing N N 272 
LYS CE    NZ     sing N N 273 
LYS CE    HE2    sing N N 274 
LYS CE    HE3    sing N N 275 
LYS NZ    HZ1    sing N N 276 
LYS NZ    HZ2    sing N N 277 
LYS NZ    HZ3    sing N N 278 
LYS OXT   HXT    sing N N 279 
MET N     CA     sing N N 280 
MET N     H      sing N N 281 
MET N     H2     sing N N 282 
MET CA    C      sing N N 283 
MET CA    CB     sing N N 284 
MET CA    HA     sing N N 285 
MET C     O      doub N N 286 
MET C     OXT    sing N N 287 
MET CB    CG     sing N N 288 
MET CB    HB2    sing N N 289 
MET CB    HB3    sing N N 290 
MET CG    SD     sing N N 291 
MET CG    HG2    sing N N 292 
MET CG    HG3    sing N N 293 
MET SD    CE     sing N N 294 
MET CE    HE1    sing N N 295 
MET CE    HE2    sing N N 296 
MET CE    HE3    sing N N 297 
MET OXT   HXT    sing N N 298 
PHE N     CA     sing N N 299 
PHE N     H      sing N N 300 
PHE N     H2     sing N N 301 
PHE CA    C      sing N N 302 
PHE CA    CB     sing N N 303 
PHE CA    HA     sing N N 304 
PHE C     O      doub N N 305 
PHE C     OXT    sing N N 306 
PHE CB    CG     sing N N 307 
PHE CB    HB2    sing N N 308 
PHE CB    HB3    sing N N 309 
PHE CG    CD1    doub Y N 310 
PHE CG    CD2    sing Y N 311 
PHE CD1   CE1    sing Y N 312 
PHE CD1   HD1    sing N N 313 
PHE CD2   CE2    doub Y N 314 
PHE CD2   HD2    sing N N 315 
PHE CE1   CZ     doub Y N 316 
PHE CE1   HE1    sing N N 317 
PHE CE2   CZ     sing Y N 318 
PHE CE2   HE2    sing N N 319 
PHE CZ    HZ     sing N N 320 
PHE OXT   HXT    sing N N 321 
PO4 P     O1     doub N N 322 
PO4 P     O2     sing N N 323 
PO4 P     O3     sing N N 324 
PO4 P     O4     sing N N 325 
PRO N     CA     sing N N 326 
PRO N     CD     sing N N 327 
PRO N     H      sing N N 328 
PRO CA    C      sing N N 329 
PRO CA    CB     sing N N 330 
PRO CA    HA     sing N N 331 
PRO C     O      doub N N 332 
PRO C     OXT    sing N N 333 
PRO CB    CG     sing N N 334 
PRO CB    HB2    sing N N 335 
PRO CB    HB3    sing N N 336 
PRO CG    CD     sing N N 337 
PRO CG    HG2    sing N N 338 
PRO CG    HG3    sing N N 339 
PRO CD    HD2    sing N N 340 
PRO CD    HD3    sing N N 341 
PRO OXT   HXT    sing N N 342 
SER N     CA     sing N N 343 
SER N     H      sing N N 344 
SER N     H2     sing N N 345 
SER CA    C      sing N N 346 
SER CA    CB     sing N N 347 
SER CA    HA     sing N N 348 
SER C     O      doub N N 349 
SER C     OXT    sing N N 350 
SER CB    OG     sing N N 351 
SER CB    HB2    sing N N 352 
SER CB    HB3    sing N N 353 
SER OG    HG     sing N N 354 
SER OXT   HXT    sing N N 355 
THR N     CA     sing N N 356 
THR N     H      sing N N 357 
THR N     H2     sing N N 358 
THR CA    C      sing N N 359 
THR CA    CB     sing N N 360 
THR CA    HA     sing N N 361 
THR C     O      doub N N 362 
THR C     OXT    sing N N 363 
THR CB    OG1    sing N N 364 
THR CB    CG2    sing N N 365 
THR CB    HB     sing N N 366 
THR OG1   HG1    sing N N 367 
THR CG2   HG21   sing N N 368 
THR CG2   HG22   sing N N 369 
THR CG2   HG23   sing N N 370 
THR OXT   HXT    sing N N 371 
TRP N     CA     sing N N 372 
TRP N     H      sing N N 373 
TRP N     H2     sing N N 374 
TRP CA    C      sing N N 375 
TRP CA    CB     sing N N 376 
TRP CA    HA     sing N N 377 
TRP C     O      doub N N 378 
TRP C     OXT    sing N N 379 
TRP CB    CG     sing N N 380 
TRP CB    HB2    sing N N 381 
TRP CB    HB3    sing N N 382 
TRP CG    CD1    doub Y N 383 
TRP CG    CD2    sing Y N 384 
TRP CD1   NE1    sing Y N 385 
TRP CD1   HD1    sing N N 386 
TRP CD2   CE2    doub Y N 387 
TRP CD2   CE3    sing Y N 388 
TRP NE1   CE2    sing Y N 389 
TRP NE1   HE1    sing N N 390 
TRP CE2   CZ2    sing Y N 391 
TRP CE3   CZ3    doub Y N 392 
TRP CE3   HE3    sing N N 393 
TRP CZ2   CH2    doub Y N 394 
TRP CZ2   HZ2    sing N N 395 
TRP CZ3   CH2    sing Y N 396 
TRP CZ3   HZ3    sing N N 397 
TRP CH2   HH2    sing N N 398 
TRP OXT   HXT    sing N N 399 
TYR N     CA     sing N N 400 
TYR N     H      sing N N 401 
TYR N     H2     sing N N 402 
TYR CA    C      sing N N 403 
TYR CA    CB     sing N N 404 
TYR CA    HA     sing N N 405 
TYR C     O      doub N N 406 
TYR C     OXT    sing N N 407 
TYR CB    CG     sing N N 408 
TYR CB    HB2    sing N N 409 
TYR CB    HB3    sing N N 410 
TYR CG    CD1    doub Y N 411 
TYR CG    CD2    sing Y N 412 
TYR CD1   CE1    sing Y N 413 
TYR CD1   HD1    sing N N 414 
TYR CD2   CE2    doub Y N 415 
TYR CD2   HD2    sing N N 416 
TYR CE1   CZ     doub Y N 417 
TYR CE1   HE1    sing N N 418 
TYR CE2   CZ     sing Y N 419 
TYR CE2   HE2    sing N N 420 
TYR CZ    OH     sing N N 421 
TYR OH    HH     sing N N 422 
TYR OXT   HXT    sing N N 423 
VAL N     CA     sing N N 424 
VAL N     H      sing N N 425 
VAL N     H2     sing N N 426 
VAL CA    C      sing N N 427 
VAL CA    CB     sing N N 428 
VAL CA    HA     sing N N 429 
VAL C     O      doub N N 430 
VAL C     OXT    sing N N 431 
VAL CB    CG1    sing N N 432 
VAL CB    CG2    sing N N 433 
VAL CB    HB     sing N N 434 
VAL CG1   HG11   sing N N 435 
VAL CG1   HG12   sing N N 436 
VAL CG1   HG13   sing N N 437 
VAL CG2   HG21   sing N N 438 
VAL CG2   HG22   sing N N 439 
VAL CG2   HG23   sing N N 440 
VAL OXT   HXT    sing N N 441 
# 
_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                    8K6I 
_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]   0.017429 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006049 
_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]   0.004451 
_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    . ILE A 1 5   ? 40.868  65.683  20.372  1.00 27.47  ? 5   ILE A N    1 
ATOM   2     C CA   . ILE A 1 5   ? 40.934  64.596  21.318  1.00 35.18  ? 5   ILE A CA   1 
ATOM   3     C C    . ILE A 1 5   ? 40.350  64.973  22.656  1.00 36.36  ? 5   ILE A C    1 
ATOM   4     O O    . ILE A 1 5   ? 40.999  64.940  23.691  1.00 45.78  ? 5   ILE A O    1 
ATOM   5     C CB   . ILE A 1 5   ? 42.340  63.973  21.374  1.00 52.47  ? 5   ILE A CB   1 
ATOM   6     C CG1  . ILE A 1 5   ? 42.322  62.605  22.077  1.00 49.07  ? 5   ILE A CG1  1 
ATOM   7     C CG2  . ILE A 1 5   ? 43.397  64.947  21.906  1.00 46.75  ? 5   ILE A CG2  1 
ATOM   8     C CD1  . ILE A 1 5   ? 41.632  61.513  21.280  1.00 48.24  ? 5   ILE A CD1  1 
ATOM   9     N N    . ALA A 1 6   ? 39.074  65.303  22.641  1.00 33.10  ? 6   ALA A N    1 
ATOM   10    C CA   . ALA A 1 6   ? 38.387  65.617  23.851  1.00 23.59  ? 6   ALA A CA   1 
ATOM   11    C C    . ALA A 1 6   ? 37.394  64.540  24.055  1.00 22.45  ? 6   ALA A C    1 
ATOM   12    O O    . ALA A 1 6   ? 36.661  64.218  23.151  1.00 19.70  ? 6   ALA A O    1 
ATOM   13    C CB   . ALA A 1 6   ? 37.664  66.910  23.683  1.00 17.10  ? 6   ALA A CB   1 
ATOM   14    N N    . ALA A 1 7   ? 37.382  63.950  25.237  1.00 24.20  ? 7   ALA A N    1 
ATOM   15    C CA   . ALA A 1 7   ? 36.401  62.943  25.577  1.00 18.52  ? 7   ALA A CA   1 
ATOM   16    C C    . ALA A 1 7   ? 35.120  63.549  26.025  1.00 16.69  ? 7   ALA A C    1 
ATOM   17    O O    . ALA A 1 7   ? 35.070  64.701  26.406  1.00 12.96  ? 7   ALA A O    1 
ATOM   18    C CB   . ALA A 1 7   ? 36.933  61.981  26.610  1.00 12.24  ? 7   ALA A CB   1 
ATOM   19    N N    . LEU A 1 8   ? 34.069  62.767  25.974  1.00 16.89  ? 8   LEU A N    1 
ATOM   20    C CA   . LEU A 1 8   ? 32.778  63.278  26.290  1.00 13.48  ? 8   LEU A CA   1 
ATOM   21    C C    . LEU A 1 8   ? 32.278  62.482  27.446  1.00 11.26  ? 8   LEU A C    1 
ATOM   22    O O    . LEU A 1 8   ? 32.627  61.341  27.584  1.00 10.09  ? 8   LEU A O    1 
ATOM   23    C CB   . LEU A 1 8   ? 31.859  63.143  25.071  1.00 9.48   ? 8   LEU A CB   1 
ATOM   24    C CG   . LEU A 1 8   ? 32.326  63.637  23.723  1.00 9.00   ? 8   LEU A CG   1 
ATOM   25    C CD1  . LEU A 1 8   ? 31.530  62.961  22.629  1.00 15.67  ? 8   LEU A CD1  1 
ATOM   26    C CD2  . LEU A 1 8   ? 32.115  65.120  23.688  1.00 7.46   ? 8   LEU A CD2  1 
ATOM   27    N N    . VAL A 1 9   ? 31.538  63.110  28.335  1.00 7.54   ? 9   VAL A N    1 
ATOM   28    C CA   . VAL A 1 9   ? 30.983  62.446  29.482  1.00 7.13   ? 9   VAL A CA   1 
ATOM   29    C C    . VAL A 1 9   ? 29.480  62.659  29.531  1.00 6.78   ? 9   VAL A C    1 
ATOM   30    O O    . VAL A 1 9   ? 29.038  63.768  29.595  1.00 6.69   ? 9   VAL A O    1 
ATOM   31    C CB   . VAL A 1 9   ? 31.726  62.866  30.764  1.00 8.71   ? 9   VAL A CB   1 
ATOM   32    C CG1  . VAL A 1 9   ? 33.023  62.104  30.884  1.00 8.79   ? 9   VAL A CG1  1 
ATOM   33    C CG2  . VAL A 1 9   ? 32.042  64.329  30.763  1.00 11.55  ? 9   VAL A CG2  1 
ATOM   34    N N    . ILE A 1 10  ? 28.698  61.585  29.495  1.00 7.40   ? 10  ILE A N    1 
ATOM   35    C CA   . ILE A 1 10  ? 27.229  61.690  29.485  1.00 10.43  ? 10  ILE A CA   1 
ATOM   36    C C    . ILE A 1 10  ? 26.479  60.942  30.602  1.00 9.60   ? 10  ILE A C    1 
ATOM   37    O O    . ILE A 1 10  ? 26.643  59.749  30.743  1.00 10.25  ? 10  ILE A O    1 
ATOM   38    C CB   . ILE A 1 10  ? 26.640  61.366  28.082  1.00 6.80   ? 10  ILE A CB   1 
ATOM   39    C CG1  . ILE A 1 10  ? 25.139  61.252  28.090  1.00 7.34   ? 10  ILE A CG1  1 
ATOM   40    C CG2  . ILE A 1 10  ? 27.261  60.126  27.490  1.00 11.64  ? 10  ILE A CG2  1 
ATOM   41    C CD1  . ILE A 1 10  ? 24.614  60.961  26.713  1.00 8.34   ? 10  ILE A CD1  1 
ATOM   42    N N    . ASP A 1 11  ? 25.658  61.636  31.398  1.00 6.79   ? 11  ASP A N    1 
ATOM   43    C CA   . ASP A 1 11  ? 24.928  60.941  32.415  1.00 7.59   ? 11  ASP A CA   1 
ATOM   44    C C    . ASP A 1 11  ? 23.509  60.785  32.005  1.00 8.92   ? 11  ASP A C    1 
ATOM   45    O O    . ASP A 1 11  ? 22.718  61.683  32.110  1.00 8.82   ? 11  ASP A O    1 
ATOM   46    C CB   . ASP A 1 11  ? 25.121  61.565  33.801  1.00 10.47  ? 11  ASP A CB   1 
ATOM   47    C CG   . ASP A 1 11  ? 24.597  60.718  34.919  1.00 11.85  ? 11  ASP A CG   1 
ATOM   48    O OD1  . ASP A 1 11  ? 24.712  59.492  34.842  1.00 12.41  ? 11  ASP A OD1  1 
ATOM   49    O OD2  . ASP A 1 11  ? 24.086  61.284  35.900  1.00 10.60  ? 11  ASP A OD2  1 
ATOM   50    N N    . ASN A 1 12  ? 23.162  59.636  31.487  1.00 9.44   ? 12  ASN A N    1 
ATOM   51    C CA   . ASN A 1 12  ? 21.811  59.388  31.157  1.00 7.67   ? 12  ASN A CA   1 
ATOM   52    C C    . ASN A 1 12  ? 21.319  59.033  32.477  1.00 11.13  ? 12  ASN A C    1 
ATOM   53    O O    . ASN A 1 12  ? 21.774  58.104  33.089  1.00 19.77  ? 12  ASN A O    1 
ATOM   54    C CB   . ASN A 1 12  ? 21.655  58.189  30.270  1.00 6.37   ? 12  ASN A CB   1 
ATOM   55    C CG   . ASN A 1 12  ? 22.901  57.811  29.566  1.00 12.58  ? 12  ASN A CG   1 
ATOM   56    O OD1  . ASN A 1 12  ? 23.457  56.753  29.809  1.00 21.51  ? 12  ASN A OD1  1 
ATOM   57    N ND2  . ASN A 1 12  ? 23.330  58.648  28.662  1.00 16.46  ? 12  ASN A ND2  1 
ATOM   58    N N    . GLY A 1 13  ? 20.358  59.753  32.939  1.00 9.71   ? 13  GLY A N    1 
ATOM   59    C CA   . GLY A 1 13  ? 19.841  59.495  34.228  1.00 11.04  ? 13  GLY A CA   1 
ATOM   60    C C    . GLY A 1 13  ? 18.368  59.510  34.103  1.00 11.65  ? 13  GLY A C    1 
ATOM   61    O O    . GLY A 1 13  ? 17.855  60.009  33.131  1.00 9.65   ? 13  GLY A O    1 
ATOM   62    N N    . SER A 1 14  ? 17.683  58.946  35.075  1.00 11.44  ? 14  SER A N    1 
ATOM   63    C CA   . SER A 1 14  ? 16.287  59.000  35.104  1.00 9.93   ? 14  SER A CA   1 
ATOM   64    C C    . SER A 1 14  ? 16.241  60.437  35.116  1.00 14.11  ? 14  SER A C    1 
ATOM   65    O O    . SER A 1 14  ? 16.973  61.087  35.851  1.00 23.73  ? 14  SER A O    1 
ATOM   66    C CB   . SER A 1 14  ? 15.890  58.521  36.456  1.00 11.89  ? 14  SER A CB   1 
ATOM   67    O OG   . SER A 1 14  ? 16.897  58.773  37.409  1.00 12.37  ? 14  SER A OG   1 
ATOM   68    N N    . GLY A 1 15  ? 15.349  61.005  34.372  1.00 12.61  ? 15  GLY A N    1 
ATOM   69    C CA   . GLY A 1 15  ? 15.390  62.438  34.246  1.00 10.68  ? 15  GLY A CA   1 
ATOM   70    C C    . GLY A 1 15  ? 16.487  63.095  33.491  1.00 7.62   ? 15  GLY A C    1 
ATOM   71    O O    . GLY A 1 15  ? 16.790  62.730  32.412  1.00 13.39  ? 15  GLY A O    1 
ATOM   72    N N    . MET A 1 16  ? 17.117  64.069  34.061  1.00 7.17   ? 16  MET A N    1 
ATOM   73    C CA   . MET A 1 16  ? 18.044  64.859  33.315  1.00 8.22   ? 16  MET A CA   1 
ATOM   74    C C    . MET A 1 16  ? 19.252  64.204  32.773  1.00 9.42   ? 16  MET A C    1 
ATOM   75    O O    . MET A 1 16  ? 19.909  63.452  33.446  1.00 9.95   ? 16  MET A O    1 
ATOM   76    C CB   . MET A 1 16  ? 18.442  66.063  34.152  1.00 8.59   ? 16  MET A CB   1 
ATOM   77    C CG   . MET A 1 16  ? 17.368  66.598  35.068  1.00 9.69   ? 16  MET A CG   1 
ATOM   78    S SD   . MET A 1 16  ? 16.055  67.385  34.144  1.00 13.71  ? 16  MET A SD   1 
ATOM   79    C CE   . MET A 1 16  ? 14.754  67.421  35.365  1.00 6.95   ? 16  MET A CE   1 
ATOM   80    N N    . CYS A 1 17  ? 19.583  64.552  31.547  1.00 10.21  ? 17  CYS A N    1 
ATOM   81    C CA   . CYS A 1 17  ? 20.756  64.010  30.950  1.00 10.16  ? 17  CYS A CA   1 
ATOM   82    C C    . CYS A 1 17  ? 21.739  65.107  31.059  1.00 11.08  ? 17  CYS A C    1 
ATOM   83    O O    . CYS A 1 17  ? 21.546  66.170  30.525  1.00 10.35  ? 17  CYS A O    1 
ATOM   84    C CB   . CYS A 1 17  ? 20.506  63.577  29.513  1.00 11.62  ? 17  CYS A CB   1 
ATOM   85    S SG   . CYS A 1 17  ? 21.861  62.736  28.686  1.00 13.22  ? 17  CYS A SG   1 
ATOM   86    N N    . LYS A 1 18  ? 22.805  64.850  31.778  1.00 8.77   ? 18  LYS A N    1 
ATOM   87    C CA   . LYS A 1 18  ? 23.764  65.838  32.024  1.00 10.29  ? 18  LYS A CA   1 
ATOM   88    C C    . LYS A 1 18  ? 24.901  65.348  31.244  1.00 16.33  ? 18  LYS A C    1 
ATOM   89    O O    . LYS A 1 18  ? 25.346  64.242  31.478  1.00 14.52  ? 18  LYS A O    1 
ATOM   90    C CB   . LYS A 1 18  ? 24.108  65.801  33.491  1.00 10.80  ? 18  LYS A CB   1 
ATOM   91    C CG   . LYS A 1 18  ? 22.960  65.433  34.398  1.00 10.72  ? 18  LYS A CG   1 
ATOM   92    C CD   . LYS A 1 18  ? 23.453  64.919  35.729  1.00 9.72   ? 18  LYS A CD   1 
ATOM   93    C CE   . LYS A 1 18  ? 22.293  64.374  36.528  1.00 9.42   ? 18  LYS A CE   1 
ATOM   94    N NZ   . LYS A 1 18  ? 21.543  63.349  35.761  1.00 7.38   ? 18  LYS A NZ   1 
ATOM   95    N N    . ALA A 1 19  ? 25.404  66.156  30.313  1.00 16.56  ? 19  ALA A N    1 
ATOM   96    C CA   . ALA A 1 19  ? 26.459  65.705  29.452  1.00 9.22   ? 19  ALA A CA   1 
ATOM   97    C C    . ALA A 1 19  ? 27.450  66.743  29.189  1.00 7.22   ? 19  ALA A C    1 
ATOM   98    O O    . ALA A 1 19  ? 27.151  67.905  29.246  1.00 9.31   ? 19  ALA A O    1 
ATOM   99    C CB   . ALA A 1 19  ? 25.872  65.275  28.152  1.00 9.54   ? 19  ALA A CB   1 
ATOM   100   N N    . GLY A 1 20  ? 28.645  66.318  28.870  1.00 6.33   ? 20  GLY A N    1 
ATOM   101   C CA   . GLY A 1 20  ? 29.657  67.267  28.515  1.00 6.65   ? 20  GLY A CA   1 
ATOM   102   C C    . GLY A 1 20  ? 30.964  66.800  28.011  1.00 7.18   ? 20  GLY A C    1 
ATOM   103   O O    . GLY A 1 20  ? 31.026  65.941  27.192  1.00 12.16  ? 20  GLY A O    1 
ATOM   104   N N    . PHE A 1 21  ? 32.006  67.437  28.462  1.00 6.31   ? 21  PHE A N    1 
ATOM   105   C CA   . PHE A 1 21  ? 33.303  67.146  27.979  1.00 9.73   ? 21  PHE A CA   1 
ATOM   106   C C    . PHE A 1 21  ? 34.142  66.747  29.125  1.00 10.23  ? 21  PHE A C    1 
ATOM   107   O O    . PHE A 1 21  ? 33.967  67.246  30.204  1.00 11.06  ? 21  PHE A O    1 
ATOM   108   C CB   . PHE A 1 21  ? 33.857  68.405  27.338  1.00 12.93  ? 21  PHE A CB   1 
ATOM   109   C CG   . PHE A 1 21  ? 33.251  68.723  26.006  1.00 10.62  ? 21  PHE A CG   1 
ATOM   110   C CD1  . PHE A 1 21  ? 33.753  68.155  24.860  1.00 8.83   ? 21  PHE A CD1  1 
ATOM   111   C CD2  . PHE A 1 21  ? 32.179  69.584  25.907  1.00 10.17  ? 21  PHE A CD2  1 
ATOM   112   C CE1  . PHE A 1 21  ? 33.203  68.438  23.638  1.00 11.31  ? 21  PHE A CE1  1 
ATOM   113   C CE2  . PHE A 1 21  ? 31.622  69.871  24.692  1.00 8.78   ? 21  PHE A CE2  1 
ATOM   114   C CZ   . PHE A 1 21  ? 32.134  69.297  23.555  1.00 15.66  ? 21  PHE A CZ   1 
ATOM   115   N N    . ALA A 1 22  ? 35.123  65.906  28.887  1.00 10.16  ? 22  ALA A N    1 
ATOM   116   C CA   . ALA A 1 22  ? 35.843  65.378  29.998  1.00 7.94   ? 22  ALA A CA   1 
ATOM   117   C C    . ALA A 1 22  ? 36.584  66.258  30.900  1.00 13.93  ? 22  ALA A C    1 
ATOM   118   O O    . ALA A 1 22  ? 36.423  66.168  32.032  1.00 40.50  ? 22  ALA A O    1 
ATOM   119   C CB   . ALA A 1 22  ? 36.722  64.234  29.616  1.00 8.47   ? 22  ALA A CB   1 
ATOM   120   N N    . GLY A 1 23  ? 37.356  67.185  30.488  1.00 9.86   ? 23  GLY A N    1 
ATOM   121   C CA   . GLY A 1 23  ? 38.071  67.917  31.504  1.00 21.17  ? 23  GLY A CA   1 
ATOM   122   C C    . GLY A 1 23  ? 37.439  68.791  32.550  1.00 21.04  ? 23  GLY A C    1 
ATOM   123   O O    . GLY A 1 23  ? 37.845  68.747  33.687  1.00 17.81  ? 23  GLY A O    1 
ATOM   124   N N    . ASP A 1 24  ? 36.423  69.545  32.210  1.00 25.46  ? 24  ASP A N    1 
ATOM   125   C CA   . ASP A 1 24  ? 35.865  70.586  33.082  1.00 31.29  ? 24  ASP A CA   1 
ATOM   126   C C    . ASP A 1 24  ? 34.966  70.445  34.265  1.00 34.21  ? 24  ASP A C    1 
ATOM   127   O O    . ASP A 1 24  ? 34.545  69.361  34.626  1.00 38.77  ? 24  ASP A O    1 
ATOM   128   C CB   . ASP A 1 24  ? 35.163  71.604  32.181  1.00 49.75  ? 24  ASP A CB   1 
ATOM   129   C CG   . ASP A 1 24  ? 34.634  70.987  30.895  1.00 48.93  ? 24  ASP A CG   1 
ATOM   130   O OD1  . ASP A 1 24  ? 35.390  70.943  29.902  1.00 43.03  ? 24  ASP A OD1  1 
ATOM   131   O OD2  . ASP A 1 24  ? 33.459  70.563  30.871  1.00 36.52  ? 24  ASP A OD2  1 
ATOM   132   N N    . ASP A 1 25  ? 34.673  71.577  34.883  1.00 34.47  ? 25  ASP A N    1 
ATOM   133   C CA   . ASP A 1 25  ? 33.857  71.585  36.078  1.00 32.91  ? 25  ASP A CA   1 
ATOM   134   C C    . ASP A 1 25  ? 32.474  71.153  36.018  1.00 20.39  ? 25  ASP A C    1 
ATOM   135   O O    . ASP A 1 25  ? 32.060  70.394  36.850  1.00 26.33  ? 25  ASP A O    1 
ATOM   136   C CB   . ASP A 1 25  ? 33.776  73.008  36.587  1.00 42.77  ? 25  ASP A CB   1 
ATOM   137   C CG   . ASP A 1 25  ? 35.066  73.468  37.272  1.00 63.47  ? 25  ASP A CG   1 
ATOM   138   O OD1  . ASP A 1 25  ? 36.125  72.834  37.060  1.00 60.12  ? 25  ASP A OD1  1 
ATOM   139   O OD2  . ASP A 1 25  ? 35.021  74.467  38.024  1.00 52.78  ? 25  ASP A OD2  1 
ATOM   140   N N    . ALA A 1 26  ? 31.732  71.608  35.043  1.00 17.41  ? 26  ALA A N    1 
ATOM   141   C CA   . ALA A 1 26  ? 30.340  71.288  35.050  1.00 14.37  ? 26  ALA A CA   1 
ATOM   142   C C    . ALA A 1 26  ? 29.754  70.926  33.712  1.00 18.85  ? 26  ALA A C    1 
ATOM   143   O O    . ALA A 1 26  ? 30.238  71.363  32.684  1.00 21.47  ? 26  ALA A O    1 
ATOM   144   C CB   . ALA A 1 26  ? 29.584  72.413  35.681  1.00 11.84  ? 26  ALA A CB   1 
ATOM   145   N N    . PRO A 1 27  ? 28.711  70.112  33.714  1.00 17.68  ? 27  PRO A N    1 
ATOM   146   C CA   . PRO A 1 27  ? 28.049  69.719  32.494  1.00 12.02  ? 27  PRO A CA   1 
ATOM   147   C C    . PRO A 1 27  ? 27.764  70.842  31.543  1.00 12.03  ? 27  PRO A C    1 
ATOM   148   O O    . PRO A 1 27  ? 27.327  71.873  31.997  1.00 15.87  ? 27  PRO A O    1 
ATOM   149   C CB   . PRO A 1 27  ? 26.748  69.193  33.032  1.00 10.96  ? 27  PRO A CB   1 
ATOM   150   C CG   . PRO A 1 27  ? 27.106  68.535  34.296  1.00 13.59  ? 27  PRO A CG   1 
ATOM   151   C CD   . PRO A 1 27  ? 28.188  69.381  34.879  1.00 16.65  ? 27  PRO A CD   1 
ATOM   152   N N    . ARG A 1 28  ? 27.922  70.647  30.244  1.00 10.65  ? 28  ARG A N    1 
ATOM   153   C CA   . ARG A 1 28  ? 27.543  71.680  29.292  1.00 10.82  ? 28  ARG A CA   1 
ATOM   154   C C    . ARG A 1 28  ? 26.078  71.860  29.292  1.00 11.44  ? 28  ARG A C    1 
ATOM   155   O O    . ARG A 1 28  ? 25.570  72.929  29.579  1.00 14.44  ? 28  ARG A O    1 
ATOM   156   C CB   . ARG A 1 28  ? 27.985  71.335  27.891  1.00 8.51   ? 28  ARG A CB   1 
ATOM   157   C CG   . ARG A 1 28  ? 28.042  72.486  26.909  1.00 14.18  ? 28  ARG A CG   1 
ATOM   158   C CD   . ARG A 1 28  ? 29.286  73.319  27.136  1.00 18.46  ? 28  ARG A CD   1 
ATOM   159   N NE   . ARG A 1 28  ? 30.320  72.536  27.795  1.00 20.60  ? 28  ARG A NE   1 
ATOM   160   C CZ   . ARG A 1 28  ? 31.494  73.016  28.178  1.00 23.62  ? 28  ARG A CZ   1 
ATOM   161   N NH1  . ARG A 1 28  ? 31.808  74.280  27.963  1.00 27.81  ? 28  ARG A NH1  1 
ATOM   162   N NH2  . ARG A 1 28  ? 32.353  72.222  28.778  1.00 16.78  ? 28  ARG A NH2  1 
ATOM   163   N N    . ALA A 1 29  ? 25.376  70.798  28.982  1.00 11.41  ? 29  ALA A N    1 
ATOM   164   C CA   . ALA A 1 29  ? 23.945  70.845  29.001  1.00 10.84  ? 29  ALA A CA   1 
ATOM   165   C C    . ALA A 1 29  ? 23.351  69.817  29.915  1.00 10.01  ? 29  ALA A C    1 
ATOM   166   O O    . ALA A 1 29  ? 23.896  68.750  30.071  1.00 11.34  ? 29  ALA A O    1 
ATOM   167   C CB   . ALA A 1 29  ? 23.445  70.659  27.619  1.00 11.68  ? 29  ALA A CB   1 
ATOM   168   N N    . VAL A 1 30  ? 22.247  70.161  30.549  1.00 7.80   ? 30  VAL A N    1 
ATOM   169   C CA   . VAL A 1 30  ? 21.592  69.280  31.478  1.00 9.29   ? 30  VAL A CA   1 
ATOM   170   C C    . VAL A 1 30  ? 20.128  69.118  31.100  1.00 11.28  ? 30  VAL A C    1 
ATOM   171   O O    . VAL A 1 30  ? 19.279  69.083  31.956  1.00 23.59  ? 30  VAL A O    1 
ATOM   172   C CB   . VAL A 1 30  ? 21.728  69.783  32.913  1.00 7.12   ? 30  VAL A CB   1 
ATOM   173   C CG1  . VAL A 1 30  ? 21.493  68.666  33.909  1.00 11.72  ? 30  VAL A CG1  1 
ATOM   174   C CG2  . VAL A 1 30  ? 23.100  70.382  33.151  1.00 7.31   ? 30  VAL A CG2  1 
ATOM   175   N N    . PHE A 1 31  ? 19.819  68.986  29.831  1.00 9.37   ? 31  PHE A N    1 
ATOM   176   C CA   . PHE A 1 31  ? 18.449  68.876  29.350  1.00 10.39  ? 31  PHE A CA   1 
ATOM   177   C C    . PHE A 1 31  ? 17.688  67.657  29.774  1.00 10.98  ? 31  PHE A C    1 
ATOM   178   O O    . PHE A 1 31  ? 18.256  66.672  30.184  1.00 15.77  ? 31  PHE A O    1 
ATOM   179   C CB   . PHE A 1 31  ? 18.480  68.839  27.838  1.00 12.58  ? 31  PHE A CB   1 
ATOM   180   C CG   . PHE A 1 31  ? 19.351  67.751  27.261  1.00 15.56  ? 31  PHE A CG   1 
ATOM   181   C CD1  . PHE A 1 31  ? 20.734  67.831  27.310  1.00 12.67  ? 31  PHE A CD1  1 
ATOM   182   C CD2  . PHE A 1 31  ? 18.788  66.670  26.630  1.00 15.29  ? 31  PHE A CD2  1 
ATOM   183   C CE1  . PHE A 1 31  ? 21.527  66.846  26.789  1.00 9.28   ? 31  PHE A CE1  1 
ATOM   184   C CE2  . PHE A 1 31  ? 19.577  65.682  26.101  1.00 17.19  ? 31  PHE A CE2  1 
ATOM   185   C CZ   . PHE A 1 31  ? 20.944  65.774  26.178  1.00 11.47  ? 31  PHE A CZ   1 
ATOM   186   N N    . PRO A 1 32  ? 16.395  67.701  29.688  1.00 9.25   ? 32  PRO A N    1 
ATOM   187   C CA   . PRO A 1 32  ? 15.721  66.484  30.068  1.00 10.01  ? 32  PRO A CA   1 
ATOM   188   C C    . PRO A 1 32  ? 15.889  65.251  29.226  1.00 15.81  ? 32  PRO A C    1 
ATOM   189   O O    . PRO A 1 32  ? 16.329  65.376  28.109  1.00 29.74  ? 32  PRO A O    1 
ATOM   190   C CB   . PRO A 1 32  ? 14.280  66.877  29.950  1.00 9.48   ? 32  PRO A CB   1 
ATOM   191   C CG   . PRO A 1 32  ? 14.240  68.308  30.312  1.00 13.51  ? 32  PRO A CG   1 
ATOM   192   C CD   . PRO A 1 32  ? 15.537  68.879  29.840  1.00 15.71  ? 32  PRO A CD   1 
ATOM   193   N N    . SER A 1 33  ? 15.605  64.063  29.760  1.00 11.58  ? 33  SER A N    1 
ATOM   194   C CA   . SER A 1 33  ? 15.609  62.832  28.987  1.00 11.02  ? 33  SER A CA   1 
ATOM   195   C C    . SER A 1 33  ? 14.208  62.573  28.493  1.00 14.82  ? 33  SER A C    1 
ATOM   196   O O    . SER A 1 33  ? 13.502  61.774  29.071  1.00 14.64  ? 33  SER A O    1 
ATOM   197   C CB   . SER A 1 33  ? 16.048  61.680  29.839  1.00 8.19   ? 33  SER A CB   1 
ATOM   198   O OG   . SER A 1 33  ? 17.450  61.630  29.991  1.00 11.28  ? 33  SER A OG   1 
ATOM   199   N N    . ILE A 1 34  ? 13.836  63.252  27.422  1.00 15.60  ? 34  ILE A N    1 
ATOM   200   C CA   . ILE A 1 34  ? 12.519  63.147  26.919  1.00 16.35  ? 34  ILE A CA   1 
ATOM   201   C C    . ILE A 1 34  ? 12.536  63.149  25.410  1.00 18.63  ? 34  ILE A C    1 
ATOM   202   O O    . ILE A 1 34  ? 13.433  63.700  24.818  1.00 16.27  ? 34  ILE A O    1 
ATOM   203   C CB   . ILE A 1 34  ? 11.717  64.321  27.510  1.00 15.41  ? 34  ILE A CB   1 
ATOM   204   C CG1  . ILE A 1 34  ? 10.218  64.088  27.486  1.00 21.66  ? 34  ILE A CG1  1 
ATOM   205   C CG2  . ILE A 1 34  ? 12.063  65.622  26.836  1.00 15.41  ? 34  ILE A CG2  1 
ATOM   206   C CD1  . ILE A 1 34  ? 9.501   65.164  28.259  1.00 17.93  ? 34  ILE A CD1  1 
ATOM   207   N N    . VAL A 1 35  ? 11.582  62.459  24.791  1.00 16.52  ? 35  VAL A N    1 
ATOM   208   C CA   . VAL A 1 35  ? 11.439  62.410  23.346  1.00 19.20  ? 35  VAL A CA   1 
ATOM   209   C C    . VAL A 1 35  ? 10.021  62.713  23.003  1.00 20.02  ? 35  VAL A C    1 
ATOM   210   O O    . VAL A 1 35  ? 9.140   62.120  23.554  1.00 26.57  ? 35  VAL A O    1 
ATOM   211   C CB   . VAL A 1 35  ? 11.679  60.995  22.827  1.00 20.40  ? 35  VAL A CB   1 
ATOM   212   C CG1  . VAL A 1 35  ? 11.378  60.878  21.348  1.00 22.00  ? 35  VAL A CG1  1 
ATOM   213   C CG2  . VAL A 1 35  ? 13.105  60.583  23.094  1.00 23.39  ? 35  VAL A CG2  1 
ATOM   214   N N    . GLY A 1 36  ? 9.787   63.608  22.078  1.00 17.12  ? 36  GLY A N    1 
ATOM   215   C CA   . GLY A 1 36  ? 8.446   63.886  21.658  1.00 18.39  ? 36  GLY A CA   1 
ATOM   216   C C    . GLY A 1 36  ? 8.206   63.715  20.197  1.00 26.67  ? 36  GLY A C    1 
ATOM   217   O O    . GLY A 1 36  ? 8.965   64.219  19.402  1.00 33.05  ? 36  GLY A O    1 
ATOM   218   N N    . ARG A 1 37  ? 7.144   63.023  19.829  1.00 28.34  ? 37  ARG A N    1 
ATOM   219   C CA   . ARG A 1 37  ? 6.826   62.761  18.455  1.00 23.78  ? 37  ARG A CA   1 
ATOM   220   C C    . ARG A 1 37  ? 5.341   63.020  18.448  1.00 27.07  ? 37  ARG A C    1 
ATOM   221   O O    . ARG A 1 37  ? 4.685   62.667  19.398  1.00 30.43  ? 37  ARG A O    1 
ATOM   222   C CB   . ARG A 1 37  ? 7.148   61.317  18.193  1.00 23.06  ? 37  ARG A CB   1 
ATOM   223   C CG   . ARG A 1 37  ? 8.600   60.915  18.332  1.00 20.44  ? 37  ARG A CG   1 
ATOM   224   C CD   . ARG A 1 37  ? 8.659   59.484  18.821  1.00 28.05  ? 37  ARG A CD   1 
ATOM   225   N NE   . ARG A 1 37  ? 7.454   58.757  18.440  1.00 33.24  ? 37  ARG A NE   1 
ATOM   226   C CZ   . ARG A 1 37  ? 7.172   57.516  18.820  1.00 42.78  ? 37  ARG A CZ   1 
ATOM   227   N NH1  . ARG A 1 37  ? 8.009   56.851  19.600  1.00 43.36  ? 37  ARG A NH1  1 
ATOM   228   N NH2  . ARG A 1 37  ? 6.048   56.940  18.422  1.00 38.69  ? 37  ARG A NH2  1 
ATOM   229   N N    . PRO A 1 38  ? 4.763   63.646  17.378  1.00 23.61  ? 38  PRO A N    1 
ATOM   230   C CA   . PRO A 1 38  ? 3.352   64.066  17.472  1.00 20.16  ? 38  PRO A CA   1 
ATOM   231   C C    . PRO A 1 38  ? 2.211   63.066  17.498  1.00 24.30  ? 38  PRO A C    1 
ATOM   232   O O    . PRO A 1 38  ? 2.442   61.872  17.456  1.00 34.05  ? 38  PRO A O    1 
ATOM   233   C CB   . PRO A 1 38  ? 3.183   64.992  16.282  1.00 19.05  ? 38  PRO A CB   1 
ATOM   234   C CG   . PRO A 1 38  ? 4.490   65.053  15.580  1.00 21.96  ? 38  PRO A CG   1 
ATOM   235   C CD   . PRO A 1 38  ? 5.235   63.837  15.992  1.00 20.16  ? 38  PRO A CD   1 
ATOM   236   N N    . ARG A 1 39  ? 0.983   63.561  17.619  1.00 19.79  ? 39  ARG A N    1 
ATOM   237   C CA   . ARG A 1 39  ? -0.175  62.682  17.643  1.00 28.21  ? 39  ARG A CA   1 
ATOM   238   C C    . ARG A 1 39  ? -1.170  62.794  16.494  1.00 33.76  ? 39  ARG A C    1 
ATOM   239   O O    . ARG A 1 39  ? -1.912  61.865  16.210  1.00 34.23  ? 39  ARG A O    1 
ATOM   240   C CB   . ARG A 1 39  ? -0.925  62.904  18.929  1.00 34.91  ? 39  ARG A CB   1 
ATOM   241   C CG   . ARG A 1 39  ? -1.916  61.809  19.311  1.00 38.84  ? 39  ARG A CG   1 
ATOM   242   C CD   . ARG A 1 39  ? -1.202  60.556  19.799  1.00 40.08  ? 39  ARG A CD   1 
ATOM   243   N NE   . ARG A 1 39  ? -2.046  59.370  19.752  1.00 43.65  ? 39  ARG A NE   1 
ATOM   244   C CZ   . ARG A 1 39  ? -2.047  58.500  18.748  1.00 42.81  ? 39  ARG A CZ   1 
ATOM   245   N NH1  . ARG A 1 39  ? -1.244  58.678  17.709  1.00 36.02  ? 39  ARG A NH1  1 
ATOM   246   N NH2  . ARG A 1 39  ? -2.851  57.447  18.783  1.00 37.50  ? 39  ARG A NH2  1 
ATOM   247   N N    . HIS A 1 40  ? -1.195  63.930  15.828  1.00 38.99  ? 40  HIS A N    1 
ATOM   248   C CA   . HIS A 1 40  ? -2.112  64.132  14.737  1.00 35.21  ? 40  HIS A CA   1 
ATOM   249   C C    . HIS A 1 40  ? -1.248  64.613  13.625  1.00 35.24  ? 40  HIS A C    1 
ATOM   250   O O    . HIS A 1 40  ? -0.035  64.550  13.703  1.00 36.62  ? 40  HIS A O    1 
ATOM   251   C CB   . HIS A 1 40  ? -3.042  65.299  15.026  1.00 32.89  ? 40  HIS A CB   1 
ATOM   252   C CG   . HIS A 1 40  ? -4.488  64.935  14.953  1.00 42.26  ? 40  HIS A CG   1 
ATOM   253   N ND1  . HIS A 1 40  ? -5.089  64.521  13.785  1.00 43.30  ? 40  HIS A ND1  1 
ATOM   254   C CD2  . HIS A 1 40  ? -5.451  64.904  15.903  1.00 50.14  ? 40  HIS A CD2  1 
ATOM   255   C CE1  . HIS A 1 40  ? -6.361  64.256  14.017  1.00 44.64  ? 40  HIS A CE1  1 
ATOM   256   N NE2  . HIS A 1 40  ? -6.607  64.480  15.294  1.00 41.38  ? 40  HIS A NE2  1 
ATOM   257   N N    . GLN A 1 41  ? -1.868  65.065  12.554  1.00 34.99  ? 41  GLN A N    1 
ATOM   258   C CA   . GLN A 1 41  ? -1.124  65.615  11.469  1.00 26.63  ? 41  GLN A CA   1 
ATOM   259   C C    . GLN A 1 41  ? -1.040  67.079  11.406  1.00 24.38  ? 41  GLN A C    1 
ATOM   260   O O    . GLN A 1 41  ? -1.608  67.659  10.522  1.00 34.98  ? 41  GLN A O    1 
ATOM   261   C CB   . GLN A 1 41  ? -1.914  65.168  10.310  1.00 27.02  ? 41  GLN A CB   1 
ATOM   262   N N    . GLY A 1 42  ? -0.343  67.700  12.330  1.00 25.82  ? 42  GLY A N    1 
ATOM   263   C CA   . GLY A 1 42  ? -0.116  69.123  12.294  1.00 23.84  ? 42  GLY A CA   1 
ATOM   264   C C    . GLY A 1 42  ? 1.329   69.020  11.953  1.00 27.43  ? 42  GLY A C    1 
ATOM   265   O O    . GLY A 1 42  ? 2.066   69.995  12.015  1.00 26.33  ? 42  GLY A O    1 
ATOM   266   N N    . VAL A 1 43  ? 1.735   67.832  11.560  1.00 29.68  ? 43  VAL A N    1 
ATOM   267   C CA   . VAL A 1 43  ? 3.110   67.558  11.237  1.00 29.26  ? 43  VAL A CA   1 
ATOM   268   C C    . VAL A 1 43  ? 3.490   68.224  9.929   1.00 39.14  ? 43  VAL A C    1 
ATOM   269   O O    . VAL A 1 43  ? 4.662   68.219  9.560   1.00 39.65  ? 43  VAL A O    1 
ATOM   270   C CB   . VAL A 1 43  ? 3.306   66.026  11.153  1.00 30.48  ? 43  VAL A CB   1 
ATOM   271   C CG1  . VAL A 1 43  ? 2.624   65.457  9.923   1.00 23.69  ? 43  VAL A CG1  1 
ATOM   272   C CG2  . VAL A 1 43  ? 4.766   65.618  11.221  1.00 28.00  ? 43  VAL A CG2  1 
ATOM   273   N N    . MET A 1 44  ? 2.534   68.870  9.267   1.00 43.88  ? 44  MET A N    1 
ATOM   274   C CA   . MET A 1 44  ? 2.760   69.464  7.951   1.00 29.47  ? 44  MET A CA   1 
ATOM   275   C C    . MET A 1 44  ? 3.512   70.702  8.379   1.00 37.33  ? 44  MET A C    1 
ATOM   276   O O    . MET A 1 44  ? 2.904   71.651  8.830   1.00 61.87  ? 44  MET A O    1 
ATOM   277   C CB   . MET A 1 44  ? 1.417   69.722  7.327   1.00 24.06  ? 44  MET A CB   1 
ATOM   278   C CG   . MET A 1 44  ? 0.350   68.744  7.780   1.00 27.65  ? 44  MET A CG   1 
ATOM   279   S SD   . MET A 1 44  ? -1.308  69.452  7.843   1.00 48.33  ? 44  MET A SD   1 
ATOM   280   C CE   . MET A 1 44  ? -1.031  70.907  8.845   1.00 23.77  ? 44  MET A CE   1 
ATOM   281   N N    . VAL A 1 45  ? 4.826   70.716  8.224   1.00 26.25  ? 45  VAL A N    1 
ATOM   282   C CA   . VAL A 1 45  ? 5.613   71.892  8.528   1.00 30.65  ? 45  VAL A CA   1 
ATOM   283   C C    . VAL A 1 45  ? 6.989   71.320  8.391   1.00 30.74  ? 45  VAL A C    1 
ATOM   284   O O    . VAL A 1 45  ? 7.189   70.135  8.619   1.00 34.75  ? 45  VAL A O    1 
ATOM   285   C CB   . VAL A 1 45  ? 5.629   72.732  9.813   1.00 32.14  ? 45  VAL A CB   1 
ATOM   286   C CG1  . VAL A 1 45  ? 6.691   73.810  9.732   1.00 35.28  ? 45  VAL A CG1  1 
ATOM   287   C CG2  . VAL A 1 45  ? 4.266   73.332  10.115  1.00 37.54  ? 45  VAL A CG2  1 
ATOM   288   N N    . ASP A 1 51  ? 9.981   64.407  11.735  1.00 17.02  ? 51  ASP A N    1 
ATOM   289   C CA   . ASP A 1 51  ? 11.237  64.168  12.396  1.00 17.52  ? 51  ASP A CA   1 
ATOM   290   C C    . ASP A 1 51  ? 11.049  63.748  13.850  1.00 23.30  ? 51  ASP A C    1 
ATOM   291   O O    . ASP A 1 51  ? 10.512  62.674  14.109  1.00 20.44  ? 51  ASP A O    1 
ATOM   292   C CB   . ASP A 1 51  ? 12.055  65.419  12.275  1.00 15.63  ? 51  ASP A CB   1 
ATOM   293   C CG   . ASP A 1 51  ? 11.906  66.074  10.942  1.00 18.58  ? 51  ASP A CG   1 
ATOM   294   O OD1  . ASP A 1 51  ? 12.062  65.385  9.918   1.00 15.34  ? 51  ASP A OD1  1 
ATOM   295   O OD2  . ASP A 1 51  ? 11.633  67.285  10.917  1.00 25.73  ? 51  ASP A OD2  1 
ATOM   296   N N    . SER A 1 52  ? 11.483  64.579  14.797  1.00 30.06  ? 52  SER A N    1 
ATOM   297   C CA   . SER A 1 52  ? 11.340  64.326  16.228  1.00 18.33  ? 52  SER A CA   1 
ATOM   298   C C    . SER A 1 52  ? 11.642  65.620  16.907  1.00 19.76  ? 52  SER A C    1 
ATOM   299   O O    . SER A 1 52  ? 12.253  66.490  16.309  1.00 19.33  ? 52  SER A O    1 
ATOM   300   C CB   . SER A 1 52  ? 12.369  63.331  16.695  1.00 14.61  ? 52  SER A CB   1 
ATOM   301   O OG   . SER A 1 52  ? 13.681  63.819  16.525  1.00 18.85  ? 52  SER A OG   1 
ATOM   302   N N    . TYR A 1 53  ? 11.214  65.778  18.151  1.00 19.89  ? 53  TYR A N    1 
ATOM   303   C CA   . TYR A 1 53  ? 11.560  66.941  18.933  1.00 19.42  ? 53  TYR A CA   1 
ATOM   304   C C    . TYR A 1 53  ? 12.004  66.318  20.205  1.00 17.49  ? 53  TYR A C    1 
ATOM   305   O O    . TYR A 1 53  ? 11.266  65.594  20.782  1.00 18.05  ? 53  TYR A O    1 
ATOM   306   C CB   . TYR A 1 53  ? 10.333  67.776  19.205  1.00 20.16  ? 53  TYR A CB   1 
ATOM   307   C CG   . TYR A 1 53  ? 9.993   68.810  18.177  1.00 21.41  ? 53  TYR A CG   1 
ATOM   308   C CD1  . TYR A 1 53  ? 10.979  69.495  17.502  1.00 22.38  ? 53  TYR A CD1  1 
ATOM   309   C CD2  . TYR A 1 53  ? 8.681   69.106  17.886  1.00 20.11  ? 53  TYR A CD2  1 
ATOM   310   C CE1  . TYR A 1 53  ? 10.666  70.446  16.556  1.00 24.05  ? 53  TYR A CE1  1 
ATOM   311   C CE2  . TYR A 1 53  ? 8.356   70.049  16.945  1.00 22.51  ? 53  TYR A CE2  1 
ATOM   312   C CZ   . TYR A 1 53  ? 9.353   70.720  16.286  1.00 26.61  ? 53  TYR A CZ   1 
ATOM   313   O OH   . TYR A 1 53  ? 9.038   71.668  15.348  1.00 27.20  ? 53  TYR A OH   1 
ATOM   314   N N    . VAL A 1 54  ? 13.229  66.558  20.626  1.00 15.88  ? 54  VAL A N    1 
ATOM   315   C CA   . VAL A 1 54  ? 13.748  65.995  21.866  1.00 18.86  ? 54  VAL A CA   1 
ATOM   316   C C    . VAL A 1 54  ? 14.360  67.035  22.800  1.00 19.35  ? 54  VAL A C    1 
ATOM   317   O O    . VAL A 1 54  ? 15.177  67.832  22.392  1.00 22.64  ? 54  VAL A O    1 
ATOM   318   C CB   . VAL A 1 54  ? 14.754  64.869  21.572  1.00 19.01  ? 54  VAL A CB   1 
ATOM   319   C CG1  . VAL A 1 54  ? 15.662  64.572  22.750  1.00 16.81  ? 54  VAL A CG1  1 
ATOM   320   C CG2  . VAL A 1 54  ? 14.076  63.628  21.042  1.00 17.58  ? 54  VAL A CG2  1 
ATOM   321   N N    . GLY A 1 55  ? 13.936  67.058  24.051  1.00 16.60  ? 55  GLY A N    1 
ATOM   322   C CA   . GLY A 1 55  ? 14.521  67.947  25.023  1.00 16.50  ? 55  GLY A CA   1 
ATOM   323   C C    . GLY A 1 55  ? 13.619  68.936  25.661  1.00 19.72  ? 55  GLY A C    1 
ATOM   324   O O    . GLY A 1 55  ? 12.500  68.631  25.983  1.00 18.52  ? 55  GLY A O    1 
ATOM   325   N N    . ASP A 1 56  ? 14.124  70.134  25.889  1.00 25.39  ? 56  ASP A N    1 
ATOM   326   C CA   . ASP A 1 56  ? 13.301  71.198  26.414  1.00 19.98  ? 56  ASP A CA   1 
ATOM   327   C C    . ASP A 1 56  ? 12.278  71.565  25.367  1.00 26.12  ? 56  ASP A C    1 
ATOM   328   O O    . ASP A 1 56  ? 11.227  72.073  25.710  1.00 24.28  ? 56  ASP A O    1 
ATOM   329   C CB   . ASP A 1 56  ? 14.147  72.371  26.860  1.00 17.30  ? 56  ASP A CB   1 
ATOM   330   C CG   . ASP A 1 56  ? 15.309  71.966  27.706  1.00 20.86  ? 56  ASP A CG   1 
ATOM   331   O OD1  . ASP A 1 56  ? 16.294  71.456  27.150  1.00 28.96  ? 56  ASP A OD1  1 
ATOM   332   O OD2  . ASP A 1 56  ? 15.246  72.180  28.927  1.00 33.44  ? 56  ASP A OD2  1 
ATOM   333   N N    . GLU A 1 57  ? 12.595  71.362  24.096  1.00 28.31  ? 57  GLU A N    1 
ATOM   334   C CA   . GLU A 1 57  ? 11.666  71.577  23.001  1.00 20.26  ? 57  GLU A CA   1 
ATOM   335   C C    . GLU A 1 57  ? 10.499  70.674  23.063  1.00 20.09  ? 57  GLU A C    1 
ATOM   336   O O    . GLU A 1 57  ? 9.395   71.078  22.842  1.00 18.15  ? 57  GLU A O    1 
ATOM   337   C CB   . GLU A 1 57  ? 12.379  71.316  21.700  1.00 32.50  ? 57  GLU A CB   1 
ATOM   338   C CG   . GLU A 1 57  ? 11.622  71.715  20.445  1.00 37.08  ? 57  GLU A CG   1 
ATOM   339   C CD   . GLU A 1 57  ? 12.478  72.432  19.418  1.00 33.46  ? 57  GLU A CD   1 
ATOM   340   O OE1  . GLU A 1 57  ? 12.632  73.661  19.522  1.00 38.49  ? 57  GLU A OE1  1 
ATOM   341   O OE2  . GLU A 1 57  ? 12.988  71.775  18.495  1.00 31.48  ? 57  GLU A OE2  1 
ATOM   342   N N    . ALA A 1 58  ? 10.727  69.444  23.418  1.00 20.82  ? 58  ALA A N    1 
ATOM   343   C CA   . ALA A 1 58  ? 9.665   68.494  23.515  1.00 20.72  ? 58  ALA A CA   1 
ATOM   344   C C    . ALA A 1 58  ? 8.660   68.901  24.536  1.00 27.13  ? 58  ALA A C    1 
ATOM   345   O O    . ALA A 1 58  ? 7.475   68.747  24.322  1.00 24.86  ? 58  ALA A O    1 
ATOM   346   C CB   . ALA A 1 58  ? 10.255  67.189  23.909  1.00 19.79  ? 58  ALA A CB   1 
ATOM   347   N N    . GLN A 1 59  ? 9.109   69.359  25.681  1.00 31.67  ? 59  GLN A N    1 
ATOM   348   C CA   . GLN A 1 59  ? 8.213   69.861  26.683  1.00 24.63  ? 59  GLN A CA   1 
ATOM   349   C C    . GLN A 1 59  ? 7.583   71.165  26.295  1.00 29.32  ? 59  GLN A C    1 
ATOM   350   O O    . GLN A 1 59  ? 6.443   71.401  26.638  1.00 38.87  ? 59  GLN A O    1 
ATOM   351   C CB   . GLN A 1 59  ? 8.904   69.943  28.023  1.00 27.10  ? 59  GLN A CB   1 
ATOM   352   C CG   . GLN A 1 59  ? 7.954   70.082  29.199  1.00 26.57  ? 59  GLN A CG   1 
ATOM   353   C CD   . GLN A 1 59  ? 6.953   68.953  29.270  1.00 24.79  ? 59  GLN A CD   1 
ATOM   354   O OE1  . GLN A 1 59  ? 7.304   67.792  29.108  1.00 25.04  ? 59  GLN A OE1  1 
ATOM   355   N NE2  . GLN A 1 59  ? 5.699   69.292  29.529  1.00 28.48  ? 59  GLN A NE2  1 
ATOM   356   N N    . SER A 1 60  ? 8.316   72.054  25.644  1.00 27.16  ? 60  SER A N    1 
ATOM   357   C CA   . SER A 1 60  ? 7.724   73.301  25.157  1.00 25.14  ? 60  SER A CA   1 
ATOM   358   C C    . SER A 1 60  ? 6.692   73.117  24.073  1.00 34.81  ? 60  SER A C    1 
ATOM   359   O O    . SER A 1 60  ? 5.652   73.764  24.094  1.00 34.83  ? 60  SER A O    1 
ATOM   360   C CB   . SER A 1 60  ? 8.782   74.275  24.674  1.00 21.78  ? 60  SER A CB   1 
ATOM   361   O OG   . SER A 1 60  ? 8.218   75.539  24.395  1.00 50.11  ? 60  SER A OG   1 
ATOM   362   N N    . LYS A 1 61  ? 6.965   72.229  23.127  1.00 31.41  ? 61  LYS A N    1 
ATOM   363   C CA   . LYS A 1 61  ? 6.051   71.998  22.034  1.00 26.49  ? 61  LYS A CA   1 
ATOM   364   C C    . LYS A 1 61  ? 5.025   70.980  22.408  1.00 28.38  ? 61  LYS A C    1 
ATOM   365   O O    . LYS A 1 61  ? 4.207   70.634  21.596  1.00 37.88  ? 61  LYS A O    1 
ATOM   366   C CB   . LYS A 1 61  ? 6.802   71.529  20.802  1.00 29.88  ? 61  LYS A CB   1 
ATOM   367   C CG   . LYS A 1 61  ? 8.037   72.324  20.436  1.00 27.64  ? 61  LYS A CG   1 
ATOM   368   C CD   . LYS A 1 61  ? 7.716   73.685  19.869  1.00 36.72  ? 61  LYS A CD   1 
ATOM   369   C CE   . LYS A 1 61  ? 8.993   74.430  19.531  1.00 37.68  ? 61  LYS A CE   1 
ATOM   370   N NZ   . LYS A 1 61  ? 9.773   74.750  20.754  1.00 27.60  ? 61  LYS A NZ   1 
ATOM   371   N N    . ARG A 1 62  ? 5.038   70.528  23.638  1.00 20.81  ? 62  ARG A N    1 
ATOM   372   C CA   . ARG A 1 62  ? 4.062   69.589  24.055  1.00 19.80  ? 62  ARG A CA   1 
ATOM   373   C C    . ARG A 1 62  ? 2.771   70.298  23.913  1.00 24.38  ? 62  ARG A C    1 
ATOM   374   O O    . ARG A 1 62  ? 2.661   71.466  24.238  1.00 29.44  ? 62  ARG A O    1 
ATOM   375   C CB   . ARG A 1 62  ? 4.274   69.126  25.468  1.00 24.07  ? 62  ARG A CB   1 
ATOM   376   C CG   . ARG A 1 62  ? 3.737   67.738  25.725  1.00 32.86  ? 62  ARG A CG   1 
ATOM   377   C CD   . ARG A 1 62  ? 2.357   67.755  26.353  1.00 35.20  ? 62  ARG A CD   1 
ATOM   378   N NE   . ARG A 1 62  ? 1.871   66.402  26.587  1.00 47.66  ? 62  ARG A NE   1 
ATOM   379   C CZ   . ARG A 1 62  ? 1.101   65.729  25.743  1.00 52.82  ? 62  ARG A CZ   1 
ATOM   380   N NH1  . ARG A 1 62  ? 0.713   66.287  24.606  1.00 66.49  ? 62  ARG A NH1  1 
ATOM   381   N NH2  . ARG A 1 62  ? 0.717   64.498  26.037  1.00 44.12  ? 62  ARG A NH2  1 
ATOM   382   N N    . GLY A 1 63  ? 1.777   69.590  23.430  1.00 25.29  ? 63  GLY A N    1 
ATOM   383   C CA   . GLY A 1 63  ? 0.496   70.181  23.208  1.00 28.61  ? 63  GLY A CA   1 
ATOM   384   C C    . GLY A 1 63  ? 0.152   69.575  21.893  1.00 42.22  ? 63  GLY A C    1 
ATOM   385   O O    . GLY A 1 63  ? -0.998  69.577  21.477  1.00 43.91  ? 63  GLY A O    1 
ATOM   386   N N    . ILE A 1 64  ? 1.165   69.049  21.227  1.00 42.63  ? 64  ILE A N    1 
ATOM   387   C CA   . ILE A 1 64  ? 0.966   68.393  19.954  1.00 32.41  ? 64  ILE A CA   1 
ATOM   388   C C    . ILE A 1 64  ? 1.796   67.148  19.999  1.00 32.60  ? 64  ILE A C    1 
ATOM   389   O O    . ILE A 1 64  ? 1.419   66.139  19.424  1.00 35.85  ? 64  ILE A O    1 
ATOM   390   C CB   . ILE A 1 64  ? 1.334   69.317  18.792  1.00 41.99  ? 64  ILE A CB   1 
ATOM   391   C CG1  . ILE A 1 64  ? 0.962   68.685  17.441  1.00 70.77  ? 64  ILE A CG1  1 
ATOM   392   C CG2  . ILE A 1 64  ? 2.800   69.716  18.795  1.00 33.66  ? 64  ILE A CG2  1 
ATOM   393   C CD1  . ILE A 1 64  ? -0.525  68.588  17.168  1.00 61.11  ? 64  ILE A CD1  1 
ATOM   394   N N    . LEU A 1 65  ? 2.887   67.187  20.746  1.00 27.19  ? 65  LEU A N    1 
ATOM   395   C CA   . LEU A 1 65  ? 3.758   66.062  20.864  1.00 24.95  ? 65  LEU A CA   1 
ATOM   396   C C    . LEU A 1 65  ? 3.348   65.044  21.859  1.00 26.36  ? 65  LEU A C    1 
ATOM   397   O O    . LEU A 1 65  ? 2.837   65.376  22.887  1.00 27.53  ? 65  LEU A O    1 
ATOM   398   C CB   . LEU A 1 65  ? 5.136   66.534  21.190  1.00 21.87  ? 65  LEU A CB   1 
ATOM   399   C CG   . LEU A 1 65  ? 5.837   67.466  20.241  1.00 24.38  ? 65  LEU A CG   1 
ATOM   400   C CD1  . LEU A 1 65  ? 7.110   67.835  20.956  1.00 23.43  ? 65  LEU A CD1  1 
ATOM   401   C CD2  . LEU A 1 65  ? 6.136   66.739  18.951  1.00 30.70  ? 65  LEU A CD2  1 
ATOM   402   N N    . THR A 1 66  ? 3.594   63.781  21.551  1.00 25.59  ? 66  THR A N    1 
ATOM   403   C CA   . THR A 1 66  ? 3.287   62.696  22.446  1.00 28.66  ? 66  THR A CA   1 
ATOM   404   C C    . THR A 1 66  ? 4.532   62.144  23.068  1.00 31.54  ? 66  THR A C    1 
ATOM   405   O O    . THR A 1 66  ? 5.193   61.325  22.472  1.00 29.29  ? 66  THR A O    1 
ATOM   406   C CB   . THR A 1 66  ? 2.580   61.542  21.739  1.00 25.89  ? 66  THR A CB   1 
ATOM   407   O OG1  . THR A 1 66  ? 1.356   61.997  21.173  1.00 32.49  ? 66  THR A OG1  1 
ATOM   408   C CG2  . THR A 1 66  ? 2.297   60.447  22.726  1.00 20.96  ? 66  THR A CG2  1 
ATOM   409   N N    . LEU A 1 67  ? 4.805   62.518  24.312  1.00 21.67  ? 67  LEU A N    1 
ATOM   410   C CA   . LEU A 1 67  ? 6.038   62.146  24.963  1.00 16.30  ? 67  LEU A CA   1 
ATOM   411   C C    . LEU A 1 67  ? 6.263   60.775  25.508  1.00 10.93  ? 67  LEU A C    1 
ATOM   412   O O    . LEU A 1 67  ? 5.399   60.194  26.127  1.00 9.87   ? 67  LEU A O    1 
ATOM   413   C CB   . LEU A 1 67  ? 6.462   63.193  25.976  1.00 18.49  ? 67  LEU A CB   1 
ATOM   414   C CG   . LEU A 1 67  ? 6.218   64.650  25.673  1.00 20.79  ? 67  LEU A CG   1 
ATOM   415   C CD1  . LEU A 1 67  ? 6.086   65.386  26.984  1.00 20.37  ? 67  LEU A CD1  1 
ATOM   416   C CD2  . LEU A 1 67  ? 7.438   65.134  24.954  1.00 20.38  ? 67  LEU A CD2  1 
ATOM   417   N N    . LYS A 1 68  ? 7.460   60.257  25.277  1.00 11.51  ? 68  LYS A N    1 
ATOM   418   C CA   . LYS A 1 68  ? 7.829   58.942  25.717  1.00 11.66  ? 68  LYS A CA   1 
ATOM   419   C C    . LYS A 1 68  ? 9.015   59.226  26.570  1.00 14.95  ? 68  LYS A C    1 
ATOM   420   O O    . LYS A 1 68  ? 9.776   60.118  26.242  1.00 15.38  ? 68  LYS A O    1 
ATOM   421   C CB   . LYS A 1 68  ? 8.211   58.088  24.546  1.00 12.57  ? 68  LYS A CB   1 
ATOM   422   C CG   . LYS A 1 68  ? 7.141   57.127  24.073  1.00 12.42  ? 68  LYS A CG   1 
ATOM   423   C CD   . LYS A 1 68  ? 6.242   57.761  23.037  1.00 19.45  ? 68  LYS A CD   1 
ATOM   424   C CE   . LYS A 1 68  ? 5.057   56.865  22.767  1.00 20.97  ? 68  LYS A CE   1 
ATOM   425   N NZ   . LYS A 1 68  ? 4.388   56.515  24.044  1.00 17.59  ? 68  LYS A NZ   1 
ATOM   426   N N    . TYR A 1 69  ? 9.178   58.507  27.683  1.00 13.06  ? 69  TYR A N    1 
ATOM   427   C CA   . TYR A 1 69  ? 10.214  58.798  28.646  1.00 10.02  ? 69  TYR A CA   1 
ATOM   428   C C    . TYR A 1 69  ? 11.081  57.633  28.753  1.00 10.29  ? 69  TYR A C    1 
ATOM   429   O O    . TYR A 1 69  ? 10.867  56.767  29.568  1.00 10.40  ? 69  TYR A O    1 
ATOM   430   C CB   . TYR A 1 69  ? 9.530   59.021  29.951  1.00 10.63  ? 69  TYR A CB   1 
ATOM   431   C CG   . TYR A 1 69  ? 8.456   60.072  29.927  1.00 12.16  ? 69  TYR A CG   1 
ATOM   432   C CD1  . TYR A 1 69  ? 8.774   61.407  29.818  1.00 12.58  ? 69  TYR A CD1  1 
ATOM   433   C CD2  . TYR A 1 69  ? 7.125   59.724  30.032  1.00 13.94  ? 69  TYR A CD2  1 
ATOM   434   C CE1  . TYR A 1 69  ? 7.791   62.369  29.799  1.00 15.35  ? 69  TYR A CE1  1 
ATOM   435   C CE2  . TYR A 1 69  ? 6.136   60.678  30.013  1.00 13.56  ? 69  TYR A CE2  1 
ATOM   436   C CZ   . TYR A 1 69  ? 6.476   61.998  29.895  1.00 17.28  ? 69  TYR A CZ   1 
ATOM   437   O OH   . TYR A 1 69  ? 5.491   62.952  29.879  1.00 16.69  ? 69  TYR A OH   1 
ATOM   438   N N    . PRO A 1 70  ? 12.117  57.621  27.952  1.00 9.94   ? 70  PRO A N    1 
ATOM   439   C CA   . PRO A 1 70  ? 12.892  56.403  27.893  1.00 11.37  ? 70  PRO A CA   1 
ATOM   440   C C    . PRO A 1 70  ? 13.613  55.971  29.126  1.00 12.31  ? 70  PRO A C    1 
ATOM   441   O O    . PRO A 1 70  ? 13.503  54.841  29.501  1.00 9.11   ? 70  PRO A O    1 
ATOM   442   C CB   . PRO A 1 70  ? 13.889  56.725  26.815  1.00 11.69  ? 70  PRO A CB   1 
ATOM   443   C CG   . PRO A 1 70  ? 13.366  57.900  26.081  1.00 11.38  ? 70  PRO A CG   1 
ATOM   444   C CD   . PRO A 1 70  ? 12.694  58.684  27.134  1.00 10.94  ? 70  PRO A CD   1 
ATOM   445   N N    . ILE A 1 71  ? 14.317  56.880  29.781  1.00 16.63  ? 71  ILE A N    1 
ATOM   446   C CA   . ILE A 1 71  ? 15.011  56.573  31.007  1.00 13.81  ? 71  ILE A CA   1 
ATOM   447   C C    . ILE A 1 71  ? 14.250  57.321  32.069  1.00 16.52  ? 71  ILE A C    1 
ATOM   448   O O    . ILE A 1 71  ? 14.191  58.534  32.063  1.00 19.37  ? 71  ILE A O    1 
ATOM   449   C CB   . ILE A 1 71  ? 16.510  56.858  30.865  1.00 7.68   ? 71  ILE A CB   1 
ATOM   450   C CG1  . ILE A 1 71  ? 17.264  56.479  32.126  1.00 11.89  ? 71  ILE A CG1  1 
ATOM   451   C CG2  . ILE A 1 71  ? 16.760  58.274  30.395  1.00 7.25   ? 71  ILE A CG2  1 
ATOM   452   C CD1  . ILE A 1 71  ? 18.681  56.055  31.841  1.00 13.08  ? 71  ILE A CD1  1 
ATOM   453   N N    . GLU A 1 72  ? 13.601  56.570  32.946  1.00 10.66  ? 72  GLU A N    1 
ATOM   454   C CA   . GLU A 1 72  ? 12.827  57.164  33.994  1.00 10.68  ? 72  GLU A CA   1 
ATOM   455   C C    . GLU A 1 72  ? 13.052  56.363  35.193  1.00 10.13  ? 72  GLU A C    1 
ATOM   456   O O    . GLU A 1 72  ? 12.415  56.585  36.191  1.00 11.85  ? 72  GLU A O    1 
ATOM   457   C CB   . GLU A 1 72  ? 11.350  57.137  33.693  1.00 10.22  ? 72  GLU A CB   1 
ATOM   458   C CG   . GLU A 1 72  ? 10.705  58.508  33.650  1.00 15.26  ? 72  GLU A CG   1 
ATOM   459   C CD   . GLU A 1 72  ? 9.203   58.435  33.587  1.00 21.92  ? 72  GLU A CD   1 
ATOM   460   O OE1  . GLU A 1 72  ? 8.667   57.313  33.627  1.00 25.97  ? 72  GLU A OE1  1 
ATOM   461   O OE2  . GLU A 1 72  ? 8.559   59.494  33.502  1.00 22.82  ? 72  GLU A OE2  1 
ATOM   462   N N    . HIS A 1 73  ? 13.888  55.360  35.102  1.00 9.71   ? 73  HIS A N    1 
ATOM   463   C CA   . HIS A 1 73  ? 14.234  54.625  36.285  1.00 8.96   ? 73  HIS A CA   1 
ATOM   464   C C    . HIS A 1 73  ? 15.615  54.113  36.275  1.00 9.13   ? 73  HIS A C    1 
ATOM   465   O O    . HIS A 1 73  ? 15.925  53.186  36.975  1.00 11.93  ? 73  HIS A O    1 
ATOM   466   C CB   . HIS A 1 73  ? 13.252  53.532  36.555  1.00 10.87  ? 73  HIS A CB   1 
ATOM   467   C CG   . HIS A 1 73  ? 11.982  54.007  37.184  1.00 12.33  ? 73  HIS A CG   1 
ATOM   468   N ND1  . HIS A 1 73  ? 11.911  54.418  38.497  1.00 15.10  ? 73  HIS A ND1  1 
ATOM   469   C CD2  . HIS A 1 73  ? 10.730  54.122  36.688  1.00 11.21  ? 73  HIS A CD2  1 
ATOM   470   C CE1  . HIS A 1 73  ? 10.673  54.776  38.777  1.00 14.62  ? 73  HIS A CE1  1 
ATOM   471   N NE2  . HIS A 1 73  ? 9.935   54.603  37.698  1.00 10.86  ? 73  HIS A NE2  1 
ATOM   472   N N    . GLY A 1 74  ? 16.454  54.701  35.470  1.00 7.64   ? 74  GLY A N    1 
ATOM   473   C CA   . GLY A 1 74  ? 17.825  54.298  35.369  1.00 8.29   ? 74  GLY A CA   1 
ATOM   474   C C    . GLY A 1 74  ? 17.980  53.271  34.319  1.00 8.76   ? 74  GLY A C    1 
ATOM   475   O O    . GLY A 1 74  ? 19.083  52.924  33.954  1.00 9.44   ? 74  GLY A O    1 
ATOM   476   N N    . ILE A 1 75  ? 16.869  52.816  33.780  1.00 8.70   ? 75  ILE A N    1 
ATOM   477   C CA   . ILE A 1 75  ? 16.907  51.804  32.789  1.00 8.14   ? 75  ILE A CA   1 
ATOM   478   C C    . ILE A 1 75  ? 16.414  52.431  31.534  1.00 12.21  ? 75  ILE A C    1 
ATOM   479   O O    . ILE A 1 75  ? 15.527  53.253  31.579  1.00 13.30  ? 75  ILE A O    1 
ATOM   480   C CB   . ILE A 1 75  ? 16.104  50.584  33.221  1.00 7.81   ? 75  ILE A CB   1 
ATOM   481   C CG1  . ILE A 1 75  ? 14.731  51.003  33.739  1.00 11.29  ? 75  ILE A CG1  1 
ATOM   482   C CG2  . ILE A 1 75  ? 16.861  49.803  34.280  1.00 7.24   ? 75  ILE A CG2  1 
ATOM   483   C CD1  . ILE A 1 75  ? 13.886  49.848  34.224  1.00 16.38  ? 75  ILE A CD1  1 
ATOM   484   N N    . VAL A 1 76  ? 17.011  52.085  30.418  1.00 11.47  ? 76  VAL A N    1 
ATOM   485   C CA   . VAL A 1 76  ? 16.683  52.639  29.136  1.00 13.63  ? 76  VAL A CA   1 
ATOM   486   C C    . VAL A 1 76  ? 15.412  52.272  28.412  1.00 14.75  ? 76  VAL A C    1 
ATOM   487   O O    . VAL A 1 76  ? 15.012  53.021  27.552  1.00 18.34  ? 76  VAL A O    1 
ATOM   488   C CB   . VAL A 1 76  ? 17.849  52.403  28.234  1.00 20.56  ? 76  VAL A CB   1 
ATOM   489   C CG1  . VAL A 1 76  ? 18.915  53.454  28.485  1.00 17.09  ? 76  VAL A CG1  1 
ATOM   490   C CG2  . VAL A 1 76  ? 18.423  51.055  28.589  1.00 28.60  ? 76  VAL A CG2  1 
ATOM   491   N N    . THR A 1 77  ? 14.812  51.116  28.659  1.00 12.12  ? 77  THR A N    1 
ATOM   492   C CA   . THR A 1 77  ? 13.517  50.777  28.067  1.00 11.01  ? 77  THR A CA   1 
ATOM   493   C C    . THR A 1 77  ? 13.497  50.833  26.567  1.00 15.17  ? 77  THR A C    1 
ATOM   494   O O    . THR A 1 77  ? 14.214  50.094  25.941  1.00 24.60  ? 77  THR A O    1 
ATOM   495   C CB   . THR A 1 77  ? 12.330  51.494  28.695  1.00 11.28  ? 77  THR A CB   1 
ATOM   496   O OG1  . THR A 1 77  ? 12.367  52.883  28.395  1.00 22.69  ? 77  THR A OG1  1 
ATOM   497   C CG2  . THR A 1 77  ? 12.335  51.298  30.188  1.00 15.17  ? 77  THR A CG2  1 
ATOM   498   N N    . ASN A 1 78  ? 12.635  51.627  25.963  1.00 14.22  ? 78  ASN A N    1 
ATOM   499   C CA   . ASN A 1 78  ? 12.662  51.786  24.515  1.00 18.60  ? 78  ASN A CA   1 
ATOM   500   C C    . ASN A 1 78  ? 13.928  52.395  24.058  1.00 19.73  ? 78  ASN A C    1 
ATOM   501   O O    . ASN A 1 78  ? 14.385  53.364  24.621  1.00 22.80  ? 78  ASN A O    1 
ATOM   502   C CB   . ASN A 1 78  ? 11.470  52.618  24.042  1.00 21.65  ? 78  ASN A CB   1 
ATOM   503   C CG   . ASN A 1 78  ? 11.372  52.691  22.531  1.00 44.67  ? 78  ASN A CG   1 
ATOM   504   O OD1  . ASN A 1 78  ? 12.348  52.452  21.822  1.00 50.73  ? 78  ASN A OD1  1 
ATOM   505   N ND2  . ASN A 1 78  ? 10.188  53.023  22.030  1.00 60.42  ? 78  ASN A ND2  1 
ATOM   506   N N    . TRP A 1 79  ? 14.529  51.851  23.017  1.00 15.81  ? 79  TRP A N    1 
ATOM   507   C CA   . TRP A 1 79  ? 15.813  52.331  22.599  1.00 16.72  ? 79  TRP A CA   1 
ATOM   508   C C    . TRP A 1 79  ? 15.786  53.153  21.370  1.00 21.86  ? 79  TRP A C    1 
ATOM   509   O O    . TRP A 1 79  ? 16.781  53.748  21.031  1.00 27.33  ? 79  TRP A O    1 
ATOM   510   C CB   . TRP A 1 79  ? 16.729  51.178  22.302  1.00 14.45  ? 79  TRP A CB   1 
ATOM   511   C CG   . TRP A 1 79  ? 17.260  50.451  23.418  1.00 22.18  ? 79  TRP A CG   1 
ATOM   512   C CD1  . TRP A 1 79  ? 16.725  49.355  24.011  1.00 39.69  ? 79  TRP A CD1  1 
ATOM   513   C CD2  . TRP A 1 79  ? 18.492  50.703  24.063  1.00 24.40  ? 79  TRP A CD2  1 
ATOM   514   N NE1  . TRP A 1 79  ? 17.543  48.920  25.020  1.00 35.01  ? 79  TRP A NE1  1 
ATOM   515   C CE2  . TRP A 1 79  ? 18.638  49.739  25.069  1.00 29.03  ? 79  TRP A CE2  1 
ATOM   516   C CE3  . TRP A 1 79  ? 19.484  51.663  23.901  1.00 21.96  ? 79  TRP A CE3  1 
ATOM   517   C CZ2  . TRP A 1 79  ? 19.732  49.704  25.894  1.00 18.58  ? 79  TRP A CZ2  1 
ATOM   518   C CZ3  . TRP A 1 79  ? 20.555  51.627  24.724  1.00 20.84  ? 79  TRP A CZ3  1 
ATOM   519   C CH2  . TRP A 1 79  ? 20.672  50.661  25.714  1.00 17.48  ? 79  TRP A CH2  1 
ATOM   520   N N    . ASP A 1 80  ? 14.681  53.205  20.684  1.00 21.00  ? 80  ASP A N    1 
ATOM   521   C CA   . ASP A 1 80  ? 14.659  53.884  19.423  1.00 18.34  ? 80  ASP A CA   1 
ATOM   522   C C    . ASP A 1 80  ? 14.469  55.283  19.807  1.00 17.12  ? 80  ASP A C    1 
ATOM   523   O O    . ASP A 1 80  ? 14.496  56.146  18.967  1.00 16.53  ? 80  ASP A O    1 
ATOM   524   C CB   . ASP A 1 80  ? 13.524  53.384  18.532  1.00 20.76  ? 80  ASP A CB   1 
ATOM   525   C CG   . ASP A 1 80  ? 13.809  52.048  17.905  1.00 24.46  ? 80  ASP A CG   1 
ATOM   526   O OD1  . ASP A 1 80  ? 14.975  51.618  17.873  1.00 29.58  ? 80  ASP A OD1  1 
ATOM   527   O OD2  . ASP A 1 80  ? 12.850  51.427  17.426  1.00 28.61  ? 80  ASP A OD2  1 
ATOM   528   N N    . ASP A 1 81  ? 14.286  55.517  21.090  1.00 19.44  ? 81  ASP A N    1 
ATOM   529   C CA   . ASP A 1 81  ? 14.080  56.842  21.607  1.00 18.04  ? 81  ASP A CA   1 
ATOM   530   C C    . ASP A 1 81  ? 15.235  57.288  22.453  1.00 14.43  ? 81  ASP A C    1 
ATOM   531   O O    . ASP A 1 81  ? 15.286  58.431  22.802  1.00 13.11  ? 81  ASP A O    1 
ATOM   532   C CB   . ASP A 1 81  ? 12.820  56.861  22.448  1.00 19.03  ? 81  ASP A CB   1 
ATOM   533   C CG   . ASP A 1 81  ? 11.585  56.514  21.679  1.00 27.92  ? 81  ASP A CG   1 
ATOM   534   O OD1  . ASP A 1 81  ? 11.305  57.158  20.651  1.00 35.79  ? 81  ASP A OD1  1 
ATOM   535   O OD2  . ASP A 1 81  ? 10.870  55.609  22.138  1.00 22.94  ? 81  ASP A OD2  1 
ATOM   536   N N    . MET A 1 82  ? 16.157  56.402  22.787  1.00 13.09  ? 82  MET A N    1 
ATOM   537   C CA   . MET A 1 82  ? 17.349  56.750  23.531  1.00 12.56  ? 82  MET A CA   1 
ATOM   538   C C    . MET A 1 82  ? 18.378  57.054  22.514  1.00 12.29  ? 82  MET A C    1 
ATOM   539   O O    . MET A 1 82  ? 19.342  57.718  22.778  1.00 13.32  ? 82  MET A O    1 
ATOM   540   C CB   . MET A 1 82  ? 17.780  55.578  24.353  1.00 11.86  ? 82  MET A CB   1 
ATOM   541   C CG   . MET A 1 82  ? 18.780  55.882  25.442  1.00 15.72  ? 82  MET A CG   1 
ATOM   542   S SD   . MET A 1 82  ? 18.069  56.796  26.801  1.00 12.21  ? 82  MET A SD   1 
ATOM   543   C CE   . MET A 1 82  ? 19.376  57.944  27.164  1.00 9.53   ? 82  MET A CE   1 
ATOM   544   N N    . GLU A 1 83  ? 18.168  56.583  21.311  1.00 13.18  ? 83  GLU A N    1 
ATOM   545   C CA   . GLU A 1 83  ? 19.058  56.847  20.214  1.00 16.95  ? 83  GLU A CA   1 
ATOM   546   C C    . GLU A 1 83  ? 18.895  58.246  19.855  1.00 16.15  ? 83  GLU A C    1 
ATOM   547   O O    . GLU A 1 83  ? 19.690  58.788  19.127  1.00 17.33  ? 83  GLU A O    1 
ATOM   548   C CB   . GLU A 1 83  ? 18.589  56.079  18.998  1.00 16.61  ? 83  GLU A CB   1 
ATOM   549   C CG   . GLU A 1 83  ? 19.170  54.693  18.818  1.00 24.41  ? 83  GLU A CG   1 
ATOM   550   C CD   . GLU A 1 83  ? 18.643  54.015  17.571  1.00 20.89  ? 83  GLU A CD   1 
ATOM   551   O OE1  . GLU A 1 83  ? 18.357  54.738  16.605  1.00 16.84  ? 83  GLU A OE1  1 
ATOM   552   O OE2  . GLU A 1 83  ? 18.509  52.774  17.550  1.00 16.31  ? 83  GLU A OE2  1 
ATOM   553   N N    . LYS A 1 84  ? 17.849  58.860  20.351  1.00 12.91  ? 84  LYS A N    1 
ATOM   554   C CA   . LYS A 1 84  ? 17.554  60.227  20.001  1.00 15.22  ? 84  LYS A CA   1 
ATOM   555   C C    . LYS A 1 84  ? 17.901  61.219  21.077  1.00 16.51  ? 84  LYS A C    1 
ATOM   556   O O    . LYS A 1 84  ? 17.929  62.391  20.829  1.00 19.13  ? 84  LYS A O    1 
ATOM   557   C CB   . LYS A 1 84  ? 16.103  60.322  19.600  1.00 18.33  ? 84  LYS A CB   1 
ATOM   558   C CG   . LYS A 1 84  ? 15.634  59.261  18.631  1.00 14.02  ? 84  LYS A CG   1 
ATOM   559   C CD   . LYS A 1 84  ? 14.633  59.828  17.648  1.00 11.39  ? 84  LYS A CD   1 
ATOM   560   C CE   . LYS A 1 84  ? 13.223  59.377  17.965  1.00 16.91  ? 84  LYS A CE   1 
ATOM   561   N NZ   . LYS A 1 84  ? 12.396  59.263  16.734  1.00 19.14  ? 84  LYS A NZ   1 
ATOM   562   N N    . ILE A 1 85  ? 18.176  60.768  22.287  1.00 13.85  ? 85  ILE A N    1 
ATOM   563   C CA   . ILE A 1 85  ? 18.586  61.639  23.354  1.00 13.53  ? 85  ILE A CA   1 
ATOM   564   C C    . ILE A 1 85  ? 20.068  61.581  23.350  1.00 15.81  ? 85  ILE A C    1 
ATOM   565   O O    . ILE A 1 85  ? 20.703  62.280  24.082  1.00 20.20  ? 85  ILE A O    1 
ATOM   566   C CB   . ILE A 1 85  ? 18.081  61.181  24.725  1.00 13.94  ? 85  ILE A CB   1 
ATOM   567   C CG1  . ILE A 1 85  ? 16.728  60.532  24.616  1.00 19.21  ? 85  ILE A CG1  1 
ATOM   568   C CG2  . ILE A 1 85  ? 17.887  62.364  25.654  1.00 15.29  ? 85  ILE A CG2  1 
ATOM   569   C CD1  . ILE A 1 85  ? 16.124  60.239  25.957  1.00 12.01  ? 85  ILE A CD1  1 
ATOM   570   N N    . TRP A 1 86  ? 20.645  60.739  22.526  1.00 13.11  ? 86  TRP A N    1 
ATOM   571   C CA   . TRP A 1 86  ? 22.093  60.628  22.403  1.00 14.38  ? 86  TRP A CA   1 
ATOM   572   C C    . TRP A 1 86  ? 22.450  61.322  21.164  1.00 15.87  ? 86  TRP A C    1 
ATOM   573   O O    . TRP A 1 86  ? 23.557  61.682  20.926  1.00 12.63  ? 86  TRP A O    1 
ATOM   574   C CB   . TRP A 1 86  ? 22.515  59.186  22.291  1.00 12.16  ? 86  TRP A CB   1 
ATOM   575   C CG   . TRP A 1 86  ? 22.514  58.450  23.551  1.00 12.28  ? 86  TRP A CG   1 
ATOM   576   C CD1  . TRP A 1 86  ? 22.532  58.973  24.790  1.00 12.02  ? 86  TRP A CD1  1 
ATOM   577   C CD2  . TRP A 1 86  ? 22.493  57.035  23.710  1.00 14.62  ? 86  TRP A CD2  1 
ATOM   578   N NE1  . TRP A 1 86  ? 22.530  57.983  25.721  1.00 10.98  ? 86  TRP A NE1  1 
ATOM   579   C CE2  . TRP A 1 86  ? 22.507  56.776  25.083  1.00 13.72  ? 86  TRP A CE2  1 
ATOM   580   C CE3  . TRP A 1 86  ? 22.465  55.959  22.823  1.00 16.25  ? 86  TRP A CE3  1 
ATOM   581   C CZ2  . TRP A 1 86  ? 22.496  55.492  25.598  1.00 14.77  ? 86  TRP A CZ2  1 
ATOM   582   C CZ3  . TRP A 1 86  ? 22.458  54.690  23.333  1.00 17.45  ? 86  TRP A CZ3  1 
ATOM   583   C CH2  . TRP A 1 86  ? 22.472  54.465  24.706  1.00 21.69  ? 86  TRP A CH2  1 
ATOM   584   N N    . HIS A 1 87  ? 21.460  61.563  20.366  1.00 17.67  ? 87  HIS A N    1 
ATOM   585   C CA   . HIS A 1 87  ? 21.666  62.263  19.151  1.00 21.01  ? 87  HIS A CA   1 
ATOM   586   C C    . HIS A 1 87  ? 21.708  63.685  19.647  1.00 22.06  ? 87  HIS A C    1 
ATOM   587   O O    . HIS A 1 87  ? 22.716  64.322  19.511  1.00 20.96  ? 87  HIS A O    1 
ATOM   588   C CB   . HIS A 1 87  ? 20.489  61.904  18.255  1.00 19.77  ? 87  HIS A CB   1 
ATOM   589   C CG   . HIS A 1 87  ? 20.418  62.621  16.948  1.00 27.27  ? 87  HIS A CG   1 
ATOM   590   N ND1  . HIS A 1 87  ? 20.566  61.966  15.746  1.00 19.56  ? 87  HIS A ND1  1 
ATOM   591   C CD2  . HIS A 1 87  ? 20.116  63.903  16.643  1.00 29.35  ? 87  HIS A CD2  1 
ATOM   592   C CE1  . HIS A 1 87  ? 20.414  62.826  14.757  1.00 26.35  ? 87  HIS A CE1  1 
ATOM   593   N NE2  . HIS A 1 87  ? 20.143  64.010  15.274  1.00 31.04  ? 87  HIS A NE2  1 
ATOM   594   N N    . HIS A 1 88  ? 20.650  64.171  20.270  1.00 17.05  ? 88  HIS A N    1 
ATOM   595   C CA   . HIS A 1 88  ? 20.597  65.514  20.793  1.00 16.55  ? 88  HIS A CA   1 
ATOM   596   C C    . HIS A 1 88  ? 21.786  65.855  21.583  1.00 17.28  ? 88  HIS A C    1 
ATOM   597   O O    . HIS A 1 88  ? 22.319  66.904  21.416  1.00 20.84  ? 88  HIS A O    1 
ATOM   598   C CB   . HIS A 1 88  ? 19.423  65.629  21.707  1.00 20.10  ? 88  HIS A CB   1 
ATOM   599   C CG   . HIS A 1 88  ? 18.850  67.004  21.815  1.00 23.36  ? 88  HIS A CG   1 
ATOM   600   N ND1  . HIS A 1 88  ? 18.660  67.821  20.725  1.00 22.75  ? 88  HIS A ND1  1 
ATOM   601   C CD2  . HIS A 1 88  ? 18.393  67.692  22.884  1.00 17.10  ? 88  HIS A CD2  1 
ATOM   602   C CE1  . HIS A 1 88  ? 18.132  68.963  21.121  1.00 22.20  ? 88  HIS A CE1  1 
ATOM   603   N NE2  . HIS A 1 88  ? 17.962  68.910  22.428  1.00 25.71  ? 88  HIS A NE2  1 
ATOM   604   N N    . THR A 1 89  ? 22.243  64.972  22.434  1.00 18.24  ? 89  THR A N    1 
ATOM   605   C CA   . THR A 1 89  ? 23.398  65.215  23.293  1.00 16.28  ? 89  THR A CA   1 
ATOM   606   C C    . THR A 1 89  ? 24.554  65.669  22.505  1.00 12.80  ? 89  THR A C    1 
ATOM   607   O O    . THR A 1 89  ? 25.094  66.682  22.780  1.00 11.67  ? 89  THR A O    1 
ATOM   608   C CB   . THR A 1 89  ? 23.793  63.960  24.081  1.00 11.51  ? 89  THR A CB   1 
ATOM   609   O OG1  . THR A 1 89  ? 22.745  63.580  24.965  1.00 6.33   ? 89  THR A OG1  1 
ATOM   610   C CG2  . THR A 1 89  ? 25.025  64.195  24.862  1.00 10.85  ? 89  THR A CG2  1 
ATOM   611   N N    . PHE A 1 90  ? 24.906  64.972  21.457  1.00 12.95  ? 90  PHE A N    1 
ATOM   612   C CA   . PHE A 1 90  ? 26.103  65.301  20.732  1.00 15.43  ? 90  PHE A CA   1 
ATOM   613   C C    . PHE A 1 90  ? 25.884  66.216  19.592  1.00 17.89  ? 90  PHE A C    1 
ATOM   614   O O    . PHE A 1 90  ? 26.622  67.134  19.404  1.00 19.44  ? 90  PHE A O    1 
ATOM   615   C CB   . PHE A 1 90  ? 26.726  64.062  20.143  1.00 12.69  ? 90  PHE A CB   1 
ATOM   616   C CG   . PHE A 1 90  ? 26.997  62.964  21.116  1.00 10.79  ? 90  PHE A CG   1 
ATOM   617   C CD1  . PHE A 1 90  ? 27.745  63.183  22.237  1.00 12.28  ? 90  PHE A CD1  1 
ATOM   618   C CD2  . PHE A 1 90  ? 26.547  61.692  20.863  1.00 9.86   ? 90  PHE A CD2  1 
ATOM   619   C CE1  . PHE A 1 90  ? 27.992  62.158  23.113  1.00 14.26  ? 90  PHE A CE1  1 
ATOM   620   C CE2  . PHE A 1 90  ? 26.790  60.661  21.729  1.00 10.35  ? 90  PHE A CE2  1 
ATOM   621   C CZ   . PHE A 1 90  ? 27.513  60.896  22.858  1.00 12.69  ? 90  PHE A CZ   1 
ATOM   622   N N    . TYR A 1 91  ? 24.878  65.979  18.794  1.00 14.81  ? 91  TYR A N    1 
ATOM   623   C CA   . TYR A 1 91  ? 24.722  66.757  17.614  1.00 16.54  ? 91  TYR A CA   1 
ATOM   624   C C    . TYR A 1 91  ? 24.215  68.131  17.894  1.00 17.96  ? 91  TYR A C    1 
ATOM   625   O O    . TYR A 1 91  ? 24.675  69.082  17.294  1.00 22.15  ? 91  TYR A O    1 
ATOM   626   C CB   . TYR A 1 91  ? 23.831  66.013  16.647  1.00 17.81  ? 91  TYR A CB   1 
ATOM   627   C CG   . TYR A 1 91  ? 24.401  64.737  16.105  1.00 18.08  ? 91  TYR A CG   1 
ATOM   628   C CD1  . TYR A 1 91  ? 25.527  64.734  15.312  1.00 17.72  ? 91  TYR A CD1  1 
ATOM   629   C CD2  . TYR A 1 91  ? 23.797  63.536  16.367  1.00 17.97  ? 91  TYR A CD2  1 
ATOM   630   C CE1  . TYR A 1 91  ? 26.033  63.560  14.803  1.00 15.49  ? 91  TYR A CE1  1 
ATOM   631   C CE2  . TYR A 1 91  ? 24.295  62.358  15.874  1.00 17.82  ? 91  TYR A CE2  1 
ATOM   632   C CZ   . TYR A 1 91  ? 25.414  62.375  15.098  1.00 12.82  ? 91  TYR A CZ   1 
ATOM   633   O OH   . TYR A 1 91  ? 25.894  61.188  14.617  1.00 11.06  ? 91  TYR A OH   1 
ATOM   634   N N    . ASN A 1 92  ? 23.248  68.261  18.779  1.00 15.64  ? 92  ASN A N    1 
ATOM   635   C CA   . ASN A 1 92  ? 22.629  69.557  18.996  1.00 24.09  ? 92  ASN A CA   1 
ATOM   636   C C    . ASN A 1 92  ? 22.689  70.163  20.379  1.00 20.38  ? 92  ASN A C    1 
ATOM   637   O O    . ASN A 1 92  ? 22.019  71.150  20.625  1.00 18.47  ? 92  ASN A O    1 
ATOM   638   C CB   . ASN A 1 92  ? 21.177  69.491  18.554  1.00 31.87  ? 92  ASN A CB   1 
ATOM   639   C CG   . ASN A 1 92  ? 20.520  70.849  18.466  1.00 43.84  ? 92  ASN A CG   1 
ATOM   640   O OD1  . ASN A 1 92  ? 21.165  71.852  18.174  1.00 51.14  ? 92  ASN A OD1  1 
ATOM   641   N ND2  . ASN A 1 92  ? 19.217  70.882  18.692  1.00 46.28  ? 92  ASN A ND2  1 
ATOM   642   N N    . GLU A 1 93  ? 23.484  69.611  21.278  1.00 17.99  ? 93  GLU A N    1 
ATOM   643   C CA   . GLU A 1 93  ? 23.636  70.160  22.601  1.00 12.43  ? 93  GLU A CA   1 
ATOM   644   C C    . GLU A 1 93  ? 25.085  70.392  22.918  1.00 11.70  ? 93  GLU A C    1 
ATOM   645   O O    . GLU A 1 93  ? 25.458  71.442  23.408  1.00 11.78  ? 93  GLU A O    1 
ATOM   646   C CB   . GLU A 1 93  ? 22.971  69.275  23.649  1.00 9.36   ? 93  GLU A CB   1 
ATOM   647   C CG   . GLU A 1 93  ? 21.464  69.254  23.617  1.00 12.78  ? 93  GLU A CG   1 
ATOM   648   C CD   . GLU A 1 93  ? 20.852  70.312  24.488  1.00 12.02  ? 93  GLU A CD   1 
ATOM   649   O OE1  . GLU A 1 93  ? 21.590  70.927  25.254  1.00 8.48   ? 93  GLU A OE1  1 
ATOM   650   O OE2  . GLU A 1 93  ? 19.633  70.531  24.410  1.00 15.19  ? 93  GLU A OE2  1 
ATOM   651   N N    . LEU A 1 94  ? 25.916  69.414  22.655  1.00 11.12  ? 94  LEU A N    1 
ATOM   652   C CA   . LEU A 1 94  ? 27.333  69.568  22.904  1.00 11.23  ? 94  LEU A CA   1 
ATOM   653   C C    . LEU A 1 94  ? 27.887  70.119  21.649  1.00 17.57  ? 94  LEU A C    1 
ATOM   654   O O    . LEU A 1 94  ? 28.958  70.700  21.669  1.00 16.93  ? 94  LEU A O    1 
ATOM   655   C CB   . LEU A 1 94  ? 28.007  68.237  23.228  1.00 8.35   ? 94  LEU A CB   1 
ATOM   656   C CG   . LEU A 1 94  ? 27.753  67.516  24.522  1.00 8.88   ? 94  LEU A CG   1 
ATOM   657   C CD1  . LEU A 1 94  ? 28.791  66.429  24.650  1.00 9.16   ? 94  LEU A CD1  1 
ATOM   658   C CD2  . LEU A 1 94  ? 27.863  68.521  25.631  1.00 13.22  ? 94  LEU A CD2  1 
ATOM   659   N N    . ARG A 1 95  ? 27.146  69.974  20.558  1.00 17.07  ? 95  ARG A N    1 
ATOM   660   C CA   . ARG A 1 95  ? 27.560  70.429  19.234  1.00 12.34  ? 95  ARG A CA   1 
ATOM   661   C C    . ARG A 1 95  ? 28.819  69.799  18.789  1.00 12.74  ? 95  ARG A C    1 
ATOM   662   O O    . ARG A 1 95  ? 29.772  70.471  18.459  1.00 12.93  ? 95  ARG A O    1 
ATOM   663   C CB   . ARG A 1 95  ? 27.548  71.926  19.109  1.00 13.96  ? 95  ARG A CB   1 
ATOM   664   C CG   . ARG A 1 95  ? 26.218  72.534  19.502  1.00 20.48  ? 95  ARG A CG   1 
ATOM   665   C CD   . ARG A 1 95  ? 25.670  73.442  18.426  1.00 31.01  ? 95  ARG A CD   1 
ATOM   666   N NE   . ARG A 1 95  ? 24.309  73.850  18.736  1.00 30.47  ? 95  ARG A NE   1 
ATOM   667   C CZ   . ARG A 1 95  ? 23.439  74.256  17.828  1.00 34.19  ? 95  ARG A CZ   1 
ATOM   668   N NH1  . ARG A 1 95  ? 23.798  74.313  16.561  1.00 33.49  ? 95  ARG A NH1  1 
ATOM   669   N NH2  . ARG A 1 95  ? 22.216  74.605  18.188  1.00 36.65  ? 95  ARG A NH2  1 
ATOM   670   N N    . VAL A 1 96  ? 28.795  68.484  18.707  1.00 13.76  ? 96  VAL A N    1 
ATOM   671   C CA   . VAL A 1 96  ? 29.957  67.727  18.359  1.00 16.24  ? 96  VAL A CA   1 
ATOM   672   C C    . VAL A 1 96  ? 29.613  66.531  17.527  1.00 13.29  ? 96  VAL A C    1 
ATOM   673   O O    . VAL A 1 96  ? 28.471  66.189  17.396  1.00 14.54  ? 96  VAL A O    1 
ATOM   674   C CB   . VAL A 1 96  ? 30.767  67.376  19.630  1.00 19.28  ? 96  VAL A CB   1 
ATOM   675   C CG1  . VAL A 1 96  ? 30.023  66.486  20.608  1.00 17.69  ? 96  VAL A CG1  1 
ATOM   676   C CG2  . VAL A 1 96  ? 32.127  66.842  19.273  1.00 18.61  ? 96  VAL A CG2  1 
ATOM   677   N N    . ALA A 1 97  ? 30.605  65.936  16.903  1.00 15.77  ? 97  ALA A N    1 
ATOM   678   C CA   . ALA A 1 97  ? 30.414  64.760  16.123  1.00 16.08  ? 97  ALA A CA   1 
ATOM   679   C C    . ALA A 1 97  ? 30.889  63.640  16.919  1.00 15.64  ? 97  ALA A C    1 
ATOM   680   O O    . ALA A 1 97  ? 32.059  63.573  17.216  1.00 17.55  ? 97  ALA A O    1 
ATOM   681   C CB   . ALA A 1 97  ? 31.290  64.873  14.925  1.00 22.82  ? 97  ALA A CB   1 
ATOM   682   N N    . PRO A 1 98  ? 29.990  62.648  17.196  1.00 13.78  ? 98  PRO A N    1 
ATOM   683   C CA   . PRO A 1 98  ? 30.421  61.617  18.098  1.00 13.08  ? 98  PRO A CA   1 
ATOM   684   C C    . PRO A 1 98  ? 31.390  60.717  17.493  1.00 14.95  ? 98  PRO A C    1 
ATOM   685   O O    . PRO A 1 98  ? 31.803  59.795  18.132  1.00 16.25  ? 98  PRO A O    1 
ATOM   686   C CB   . PRO A 1 98  ? 29.172  60.822  18.273  1.00 12.68  ? 98  PRO A CB   1 
ATOM   687   C CG   . PRO A 1 98  ? 28.054  61.611  17.744  1.00 13.05  ? 98  PRO A CG   1 
ATOM   688   C CD   . PRO A 1 98  ? 28.704  62.216  16.600  1.00 15.71  ? 98  PRO A CD   1 
ATOM   689   N N    . GLU A 1 99  ? 31.719  60.937  16.223  1.00 20.64  ? 99  GLU A N    1 
ATOM   690   C CA   . GLU A 1 99  ? 32.611  60.046  15.498  1.00 21.21  ? 99  GLU A CA   1 
ATOM   691   C C    . GLU A 1 99  ? 34.063  60.359  15.785  1.00 19.35  ? 99  GLU A C    1 
ATOM   692   O O    . GLU A 1 99  ? 34.929  59.495  15.643  1.00 21.16  ? 99  GLU A O    1 
ATOM   693   C CB   . GLU A 1 99  ? 32.324  60.161  13.994  1.00 25.41  ? 99  GLU A CB   1 
ATOM   694   C CG   . GLU A 1 99  ? 32.964  59.096  13.118  1.00 47.42  ? 99  GLU A CG   1 
ATOM   695   C CD   . GLU A 1 99  ? 34.245  59.562  12.454  1.00 66.37  ? 99  GLU A CD   1 
ATOM   696   O OE1  . GLU A 1 99  ? 34.496  60.784  12.433  1.00 58.55  ? 99  GLU A OE1  1 
ATOM   697   O OE2  . GLU A 1 99  ? 35.003  58.701  11.959  1.00 64.04  ? 99  GLU A OE2  1 
ATOM   698   N N    . GLU A 1 100 ? 34.342  61.589  16.196  1.00 18.70  ? 100 GLU A N    1 
ATOM   699   C CA   . GLU A 1 100 ? 35.708  61.980  16.428  1.00 23.97  ? 100 GLU A CA   1 
ATOM   700   C C    . GLU A 1 100 ? 36.091  62.066  17.854  1.00 23.82  ? 100 GLU A C    1 
ATOM   701   O O    . GLU A 1 100 ? 37.256  62.012  18.178  1.00 30.79  ? 100 GLU A O    1 
ATOM   702   C CB   . GLU A 1 100 ? 35.904  63.373  15.853  1.00 29.79  ? 100 GLU A CB   1 
ATOM   703   C CG   . GLU A 1 100 ? 35.819  63.458  14.346  1.00 42.47  ? 100 GLU A CG   1 
ATOM   704   C CD   . GLU A 1 100 ? 35.949  64.872  13.846  1.00 40.96  ? 100 GLU A CD   1 
ATOM   705   O OE1  . GLU A 1 100 ? 35.915  65.788  14.687  1.00 45.94  ? 100 GLU A OE1  1 
ATOM   706   O OE2  . GLU A 1 100 ? 36.085  65.063  12.622  1.00 33.18  ? 100 GLU A OE2  1 
ATOM   707   N N    . HIS A 1 101 ? 35.119  62.205  18.729  1.00 22.41  ? 101 HIS A N    1 
ATOM   708   C CA   . HIS A 1 101 ? 35.399  62.383  20.110  1.00 14.81  ? 101 HIS A CA   1 
ATOM   709   C C    . HIS A 1 101 ? 35.045  61.146  20.898  1.00 13.03  ? 101 HIS A C    1 
ATOM   710   O O    . HIS A 1 101 ? 33.963  60.643  20.773  1.00 13.83  ? 101 HIS A O    1 
ATOM   711   C CB   . HIS A 1 101 ? 34.659  63.606  20.569  1.00 13.77  ? 101 HIS A CB   1 
ATOM   712   C CG   . HIS A 1 101 ? 35.332  64.887  20.203  1.00 22.87  ? 101 HIS A CG   1 
ATOM   713   N ND1  . HIS A 1 101 ? 34.934  66.104  20.701  1.00 27.99  ? 101 HIS A ND1  1 
ATOM   714   C CD2  . HIS A 1 101 ? 36.390  65.142  19.397  1.00 26.15  ? 101 HIS A CD2  1 
ATOM   715   C CE1  . HIS A 1 101 ? 35.707  67.056  20.210  1.00 29.96  ? 101 HIS A CE1  1 
ATOM   716   N NE2  . HIS A 1 101 ? 36.600  66.497  19.417  1.00 33.27  ? 101 HIS A NE2  1 
ATOM   717   N N    . PRO A 1 102 ? 35.998  60.587  21.729  1.00 13.03  ? 102 PRO A N    1 
ATOM   718   C CA   . PRO A 1 102 ? 35.599  59.452  22.570  1.00 11.27  ? 102 PRO A CA   1 
ATOM   719   C C    . PRO A 1 102 ? 34.541  59.736  23.600  1.00 13.13  ? 102 PRO A C    1 
ATOM   720   O O    . PRO A 1 102 ? 34.327  60.873  23.901  1.00 13.58  ? 102 PRO A O    1 
ATOM   721   C CB   . PRO A 1 102 ? 36.897  59.030  23.210  1.00 8.96   ? 102 PRO A CB   1 
ATOM   722   C CG   . PRO A 1 102 ? 37.789  60.188  23.146  1.00 13.50  ? 102 PRO A CG   1 
ATOM   723   C CD   . PRO A 1 102 ? 37.476  60.751  21.819  1.00 17.02  ? 102 PRO A CD   1 
ATOM   724   N N    . VAL A 1 103 ? 33.885  58.734  24.161  1.00 12.66  ? 103 VAL A N    1 
ATOM   725   C CA   . VAL A 1 103 ? 32.764  58.969  25.070  1.00 11.21  ? 103 VAL A CA   1 
ATOM   726   C C    . VAL A 1 103 ? 32.846  58.313  26.419  1.00 11.95  ? 103 VAL A C    1 
ATOM   727   O O    . VAL A 1 103 ? 33.687  57.463  26.614  1.00 15.91  ? 103 VAL A O    1 
ATOM   728   C CB   . VAL A 1 103 ? 31.439  58.539  24.359  1.00 10.13  ? 103 VAL A CB   1 
ATOM   729   C CG1  . VAL A 1 103 ? 30.230  58.633  25.260  1.00 10.41  ? 103 VAL A CG1  1 
ATOM   730   C CG2  . VAL A 1 103 ? 31.193  59.317  23.089  1.00 16.16  ? 103 VAL A CG2  1 
ATOM   731   N N    . LEU A 1 104 ? 32.059  58.748  27.391  1.00 10.46  ? 104 LEU A N    1 
ATOM   732   C CA   . LEU A 1 104 ? 31.945  58.064  28.657  1.00 10.17  ? 104 LEU A CA   1 
ATOM   733   C C    . LEU A 1 104 ? 30.499  58.087  28.975  1.00 10.97  ? 104 LEU A C    1 
ATOM   734   O O    . LEU A 1 104 ? 29.924  59.117  29.196  1.00 9.10   ? 104 LEU A O    1 
ATOM   735   C CB   . LEU A 1 104 ? 32.684  58.654  29.811  1.00 8.97   ? 104 LEU A CB   1 
ATOM   736   C CG   . LEU A 1 104 ? 32.792  57.625  30.919  1.00 9.74   ? 104 LEU A CG   1 
ATOM   737   C CD1  . LEU A 1 104 ? 34.148  56.969  30.882  1.00 12.52  ? 104 LEU A CD1  1 
ATOM   738   C CD2  . LEU A 1 104 ? 32.509  58.252  32.259  1.00 9.03   ? 104 LEU A CD2  1 
ATOM   739   N N    . LEU A 1 105 ? 29.895  56.922  29.000  1.00 10.13  ? 105 LEU A N    1 
ATOM   740   C CA   . LEU A 1 105 ? 28.519  56.833  29.268  1.00 11.92  ? 105 LEU A CA   1 
ATOM   741   C C    . LEU A 1 105 ? 28.402  56.335  30.653  1.00 14.64  ? 105 LEU A C    1 
ATOM   742   O O    . LEU A 1 105 ? 29.377  55.912  31.222  1.00 18.09  ? 105 LEU A O    1 
ATOM   743   C CB   . LEU A 1 105 ? 27.911  55.840  28.308  1.00 14.83  ? 105 LEU A CB   1 
ATOM   744   C CG   . LEU A 1 105 ? 27.005  56.167  27.143  1.00 13.56  ? 105 LEU A CG   1 
ATOM   745   C CD1  . LEU A 1 105 ? 26.594  54.842  26.545  1.00 12.14  ? 105 LEU A CD1  1 
ATOM   746   C CD2  . LEU A 1 105 ? 25.787  56.872  27.665  1.00 13.95  ? 105 LEU A CD2  1 
ATOM   747   N N    . THR A 1 106 ? 27.206  56.409  31.225  1.00 18.33  ? 106 THR A N    1 
ATOM   748   C CA   . THR A 1 106 ? 26.942  55.958  32.580  1.00 12.11  ? 106 THR A CA   1 
ATOM   749   C C    . THR A 1 106 ? 25.837  54.952  32.552  1.00 12.83  ? 106 THR A C    1 
ATOM   750   O O    . THR A 1 106 ? 25.007  54.956  31.665  1.00 15.70  ? 106 THR A O    1 
ATOM   751   C CB   . THR A 1 106 ? 26.465  57.096  33.454  1.00 8.46   ? 106 THR A CB   1 
ATOM   752   O OG1  . THR A 1 106 ? 25.336  57.707  32.843  1.00 7.75   ? 106 THR A OG1  1 
ATOM   753   C CG2  . THR A 1 106 ? 27.568  58.090  33.662  1.00 7.28   ? 106 THR A CG2  1 
ATOM   754   N N    . GLU A 1 107 ? 25.818  54.080  33.542  1.00 9.54   ? 107 GLU A N    1 
ATOM   755   C CA   . GLU A 1 107 ? 24.769  53.098  33.634  1.00 9.32   ? 107 GLU A CA   1 
ATOM   756   C C    . GLU A 1 107 ? 24.156  53.008  34.978  1.00 11.28  ? 107 GLU A C    1 
ATOM   757   O O    . GLU A 1 107 ? 24.633  53.580  35.914  1.00 11.36  ? 107 GLU A O    1 
ATOM   758   C CB   . GLU A 1 107 ? 25.303  51.725  33.254  1.00 9.78   ? 107 GLU A CB   1 
ATOM   759   C CG   . GLU A 1 107 ? 26.178  51.003  34.252  1.00 11.40  ? 107 GLU A CG   1 
ATOM   760   C CD   . GLU A 1 107 ? 26.948  49.927  33.561  1.00 13.60  ? 107 GLU A CD   1 
ATOM   761   O OE1  . GLU A 1 107 ? 26.560  49.640  32.425  1.00 14.38  ? 107 GLU A OE1  1 
ATOM   762   O OE2  . GLU A 1 107 ? 27.921  49.394  34.117  1.00 13.66  ? 107 GLU A OE2  1 
ATOM   763   N N    . ALA A 1 108 ? 23.087  52.258  35.083  1.00 15.31  ? 108 ALA A N    1 
ATOM   764   C CA   . ALA A 1 108 ? 22.420  52.069  36.338  1.00 7.37   ? 108 ALA A CA   1 
ATOM   765   C C    . ALA A 1 108 ? 22.980  50.951  37.075  1.00 6.56   ? 108 ALA A C    1 
ATOM   766   O O    . ALA A 1 108 ? 23.565  50.047  36.527  1.00 6.10   ? 108 ALA A O    1 
ATOM   767   C CB   . ALA A 1 108 ? 20.962  51.799  36.133  1.00 6.41   ? 108 ALA A CB   1 
ATOM   768   N N    . PRO A 1 109 ? 22.863  51.045  38.428  1.00 8.84   ? 109 PRO A N    1 
ATOM   769   C CA   . PRO A 1 109 ? 23.285  49.857  39.118  1.00 9.70   ? 109 PRO A CA   1 
ATOM   770   C C    . PRO A 1 109 ? 22.432  48.663  38.811  1.00 11.62  ? 109 PRO A C    1 
ATOM   771   O O    . PRO A 1 109 ? 21.240  48.807  38.601  1.00 12.57  ? 109 PRO A O    1 
ATOM   772   C CB   . PRO A 1 109 ? 23.150  50.257  40.552  1.00 6.77   ? 109 PRO A CB   1 
ATOM   773   C CG   . PRO A 1 109 ? 23.499  51.669  40.575  1.00 8.51   ? 109 PRO A CG   1 
ATOM   774   C CD   . PRO A 1 109 ? 22.777  52.176  39.408  1.00 9.28   ? 109 PRO A CD   1 
ATOM   775   N N    . LEU A 1 110 ? 23.040  47.490  38.718  1.00 10.16  ? 110 LEU A N    1 
ATOM   776   C CA   . LEU A 1 110 ? 22.339  46.262  38.416  1.00 7.36   ? 110 LEU A CA   1 
ATOM   777   C C    . LEU A 1 110 ? 21.612  46.392  37.083  1.00 7.12   ? 110 LEU A C    1 
ATOM   778   O O    . LEU A 1 110 ? 20.430  46.128  36.985  1.00 8.43   ? 110 LEU A O    1 
ATOM   779   C CB   . LEU A 1 110 ? 21.488  45.839  39.613  1.00 4.91   ? 110 LEU A CB   1 
ATOM   780   C CG   . LEU A 1 110 ? 22.059  45.105  40.800  1.00 5.09   ? 110 LEU A CG   1 
ATOM   781   C CD1  . LEU A 1 110 ? 20.916  44.991  41.780  1.00 7.23   ? 110 LEU A CD1  1 
ATOM   782   C CD2  . LEU A 1 110 ? 22.462  43.729  40.332  1.00 9.16   ? 110 LEU A CD2  1 
ATOM   783   N N    . ASN A 1 111 ? 22.341  46.774  36.047  1.00 6.85   ? 111 ASN A N    1 
ATOM   784   C CA   . ASN A 1 111 ? 21.729  47.057  34.759  1.00 11.35  ? 111 ASN A CA   1 
ATOM   785   C C    . ASN A 1 111 ? 21.707  45.814  34.001  1.00 11.95  ? 111 ASN A C    1 
ATOM   786   O O    . ASN A 1 111 ? 22.672  45.067  34.030  1.00 15.34  ? 111 ASN A O    1 
ATOM   787   C CB   . ASN A 1 111 ? 22.559  48.083  33.970  1.00 11.32  ? 111 ASN A CB   1 
ATOM   788   C CG   . ASN A 1 111 ? 21.761  48.863  32.945  1.00 9.39   ? 111 ASN A CG   1 
ATOM   789   O OD1  . ASN A 1 111 ? 20.545  48.889  32.968  1.00 13.15  ? 111 ASN A OD1  1 
ATOM   790   N ND2  . ASN A 1 111 ? 22.464  49.529  32.053  1.00 7.85   ? 111 ASN A ND2  1 
ATOM   791   N N    . PRO A 1 112 ? 20.606  45.583  33.276  1.00 10.10  ? 112 PRO A N    1 
ATOM   792   C CA   . PRO A 1 112 ? 20.736  44.337  32.585  1.00 11.30  ? 112 PRO A CA   1 
ATOM   793   C C    . PRO A 1 112 ? 21.839  44.294  31.598  1.00 11.82  ? 112 PRO A C    1 
ATOM   794   O O    . PRO A 1 112 ? 22.110  45.233  30.923  1.00 12.61  ? 112 PRO A O    1 
ATOM   795   C CB   . PRO A 1 112 ? 19.408  44.196  31.941  1.00 15.41  ? 112 PRO A CB   1 
ATOM   796   C CG   . PRO A 1 112 ? 18.463  44.801  32.887  1.00 13.17  ? 112 PRO A CG   1 
ATOM   797   C CD   . PRO A 1 112 ? 19.191  46.047  33.188  1.00 10.01  ? 112 PRO A CD   1 
ATOM   798   N N    . LYS A 1 113 ? 22.478  43.163  31.504  1.00 12.01  ? 113 LYS A N    1 
ATOM   799   C CA   . LYS A 1 113 ? 23.568  42.999  30.591  1.00 16.03  ? 113 LYS A CA   1 
ATOM   800   C C    . LYS A 1 113 ? 23.256  43.365  29.165  1.00 14.79  ? 113 LYS A C    1 
ATOM   801   O O    . LYS A 1 113 ? 24.031  44.029  28.519  1.00 11.87  ? 113 LYS A O    1 
ATOM   802   C CB   . LYS A 1 113 ? 24.031  41.553  30.687  1.00 16.11  ? 113 LYS A CB   1 
ATOM   803   C CG   . LYS A 1 113 ? 23.044  40.555  31.256  1.00 33.72  ? 113 LYS A CG   1 
ATOM   804   C CD   . LYS A 1 113 ? 23.606  39.160  31.033  1.00 44.58  ? 113 LYS A CD   1 
ATOM   805   C CE   . LYS A 1 113 ? 22.835  38.075  31.767  1.00 22.54  ? 113 LYS A CE   1 
ATOM   806   N NZ   . LYS A 1 113 ? 23.449  36.732  31.572  1.00 11.78  ? 113 LYS A NZ   1 
ATOM   807   N N    . ALA A 1 114 ? 22.133  42.918  28.665  1.00 13.80  ? 114 ALA A N    1 
ATOM   808   C CA   . ALA A 1 114 ? 21.732  43.180  27.306  1.00 12.47  ? 114 ALA A CA   1 
ATOM   809   C C    . ALA A 1 114 ? 21.485  44.610  27.066  1.00 14.45  ? 114 ALA A C    1 
ATOM   810   O O    . ALA A 1 114 ? 21.494  45.052  25.943  1.00 16.24  ? 114 ALA A O    1 
ATOM   811   C CB   . ALA A 1 114 ? 20.449  42.464  27.074  1.00 9.21   ? 114 ALA A CB   1 
ATOM   812   N N    . ASN A 1 115 ? 21.218  45.345  28.129  1.00 12.17  ? 115 ASN A N    1 
ATOM   813   C CA   . ASN A 1 115 ? 20.919  46.731  28.023  1.00 10.40  ? 115 ASN A CA   1 
ATOM   814   C C    . ASN A 1 115 ? 22.194  47.502  28.096  1.00 13.96  ? 115 ASN A C    1 
ATOM   815   O O    . ASN A 1 115 ? 22.174  48.694  28.219  1.00 18.01  ? 115 ASN A O    1 
ATOM   816   C CB   . ASN A 1 115 ? 20.034  47.128  29.162  1.00 10.09  ? 115 ASN A CB   1 
ATOM   817   C CG   . ASN A 1 115 ? 18.638  46.589  29.051  1.00 15.15  ? 115 ASN A CG   1 
ATOM   818   O OD1  . ASN A 1 115 ? 18.430  45.423  28.751  1.00 18.56  ? 115 ASN A OD1  1 
ATOM   819   N ND2  . ASN A 1 115 ? 17.665  47.440  29.327  1.00 21.50  ? 115 ASN A ND2  1 
ATOM   820   N N    . ARG A 1 116 ? 23.322  46.827  28.051  1.00 10.74  ? 116 ARG A N    1 
ATOM   821   C CA   . ARG A 1 116 ? 24.603  47.482  28.063  1.00 11.27  ? 116 ARG A CA   1 
ATOM   822   C C    . ARG A 1 116 ? 25.364  46.958  26.929  1.00 14.74  ? 116 ARG A C    1 
ATOM   823   O O    . ARG A 1 116 ? 26.546  47.161  26.856  1.00 15.20  ? 116 ARG A O    1 
ATOM   824   C CB   . ARG A 1 116 ? 25.412  47.170  29.286  1.00 12.22  ? 116 ARG A CB   1 
ATOM   825   C CG   . ARG A 1 116 ? 24.713  47.199  30.617  1.00 14.78  ? 116 ARG A CG   1 
ATOM   826   C CD   . ARG A 1 116 ? 25.491  46.340  31.591  1.00 14.68  ? 116 ARG A CD   1 
ATOM   827   N NE   . ARG A 1 116 ? 26.830  46.863  31.783  1.00 9.33   ? 116 ARG A NE   1 
ATOM   828   C CZ   . ARG A 1 116 ? 27.944  46.204  31.514  1.00 9.20   ? 116 ARG A CZ   1 
ATOM   829   N NH1  . ARG A 1 116 ? 27.893  44.988  31.027  1.00 12.44  ? 116 ARG A NH1  1 
ATOM   830   N NH2  . ARG A 1 116 ? 29.102  46.773  31.727  1.00 8.86   ? 116 ARG A NH2  1 
ATOM   831   N N    . GLU A 1 117 ? 24.687  46.290  26.021  1.00 15.57  ? 117 GLU A N    1 
ATOM   832   C CA   . GLU A 1 117 ? 25.314  45.749  24.844  1.00 14.29  ? 117 GLU A CA   1 
ATOM   833   C C    . GLU A 1 117 ? 24.737  46.514  23.726  1.00 14.75  ? 117 GLU A C    1 
ATOM   834   O O    . GLU A 1 117 ? 25.285  46.546  22.658  1.00 15.41  ? 117 GLU A O    1 
ATOM   835   C CB   . GLU A 1 117 ? 24.909  44.314  24.675  1.00 11.28  ? 117 GLU A CB   1 
ATOM   836   C CG   . GLU A 1 117 ? 25.680  43.311  25.491  1.00 14.99  ? 117 GLU A CG   1 
ATOM   837   C CD   . GLU A 1 117 ? 25.472  41.914  24.972  1.00 19.23  ? 117 GLU A CD   1 
ATOM   838   O OE1  . GLU A 1 117 ? 25.172  41.778  23.776  1.00 28.36  ? 117 GLU A OE1  1 
ATOM   839   O OE2  . GLU A 1 117 ? 25.596  40.951  25.746  1.00 15.64  ? 117 GLU A OE2  1 
ATOM   840   N N    . LYS A 1 118 ? 23.626  47.168  23.974  1.00 12.96  ? 118 LYS A N    1 
ATOM   841   C CA   . LYS A 1 118 ? 22.963  47.943  22.965  1.00 14.98  ? 118 LYS A CA   1 
ATOM   842   C C    . LYS A 1 118 ? 23.408  49.336  23.090  1.00 17.04  ? 118 LYS A C    1 
ATOM   843   O O    . LYS A 1 118 ? 23.019  50.154  22.319  1.00 18.41  ? 118 LYS A O    1 
ATOM   844   C CB   . LYS A 1 118 ? 21.469  47.884  23.142  1.00 13.83  ? 118 LYS A CB   1 
ATOM   845   C CG   . LYS A 1 118 ? 20.772  46.840  22.310  1.00 19.32  ? 118 LYS A CG   1 
ATOM   846   C CD   . LYS A 1 118 ? 20.643  47.304  20.876  1.00 22.09  ? 118 LYS A CD   1 
ATOM   847   C CE   . LYS A 1 118 ? 19.295  47.944  20.627  1.00 15.35  ? 118 LYS A CE   1 
ATOM   848   N NZ   . LYS A 1 118 ? 19.196  48.373  19.210  1.00 13.39  ? 118 LYS A NZ   1 
ATOM   849   N N    . MET A 1 119 ? 24.210  49.643  24.083  1.00 14.62  ? 119 MET A N    1 
ATOM   850   C CA   . MET A 1 119 ? 24.778  50.961  24.215  1.00 11.57  ? 119 MET A CA   1 
ATOM   851   C C    . MET A 1 119 ? 26.084  50.884  23.539  1.00 10.17  ? 119 MET A C    1 
ATOM   852   O O    . MET A 1 119 ? 26.508  51.812  22.963  1.00 7.95   ? 119 MET A O    1 
ATOM   853   C CB   . MET A 1 119 ? 24.985  51.277  25.673  1.00 14.78  ? 119 MET A CB   1 
ATOM   854   C CG   . MET A 1 119 ? 23.759  51.115  26.530  1.00 16.64  ? 119 MET A CG   1 
ATOM   855   S SD   . MET A 1 119 ? 23.911  51.885  28.138  1.00 13.34  ? 119 MET A SD   1 
ATOM   856   C CE   . MET A 1 119 ? 25.508  51.295  28.631  1.00 9.36   ? 119 MET A CE   1 
ATOM   857   N N    . THR A 1 120 ? 26.720  49.738  23.581  1.00 13.51  ? 120 THR A N    1 
ATOM   858   C CA   . THR A 1 120 ? 27.951  49.512  22.868  1.00 12.13  ? 120 THR A CA   1 
ATOM   859   C C    . THR A 1 120 ? 27.686  49.503  21.412  1.00 11.07  ? 120 THR A C    1 
ATOM   860   O O    . THR A 1 120 ? 28.394  50.125  20.675  1.00 14.14  ? 120 THR A O    1 
ATOM   861   C CB   . THR A 1 120 ? 28.502  48.177  23.273  1.00 12.97  ? 120 THR A CB   1 
ATOM   862   O OG1  . THR A 1 120 ? 28.147  47.961  24.633  1.00 10.41  ? 120 THR A OG1  1 
ATOM   863   C CG2  . THR A 1 120 ? 29.991  48.150  23.103  1.00 13.00  ? 120 THR A CG2  1 
ATOM   864   N N    . GLN A 1 121 ? 26.669  48.801  20.975  1.00 10.49  ? 121 GLN A N    1 
ATOM   865   C CA   . GLN A 1 121 ? 26.274  48.794  19.589  1.00 12.04  ? 121 GLN A CA   1 
ATOM   866   C C    . GLN A 1 121 ? 25.977  50.150  19.109  1.00 10.46  ? 121 GLN A C    1 
ATOM   867   O O    . GLN A 1 121 ? 26.650  50.662  18.305  1.00 9.29   ? 121 GLN A O    1 
ATOM   868   C CB   . GLN A 1 121 ? 24.966  48.065  19.460  1.00 12.80  ? 121 GLN A CB   1 
ATOM   869   C CG   . GLN A 1 121 ? 24.993  46.572  19.330  1.00 13.69  ? 121 GLN A CG   1 
ATOM   870   C CD   . GLN A 1 121 ? 24.037  46.100  18.277  1.00 14.50  ? 121 GLN A CD   1 
ATOM   871   O OE1  . GLN A 1 121 ? 22.936  46.613  18.160  1.00 13.36  ? 121 GLN A OE1  1 
ATOM   872   N NE2  . GLN A 1 121 ? 24.456  45.130  17.492  1.00 23.79  ? 121 GLN A NE2  1 
ATOM   873   N N    . ILE A 1 122 ? 24.911  50.737  19.586  1.00 8.32   ? 122 ILE A N    1 
ATOM   874   C CA   . ILE A 1 122 ? 24.515  52.055  19.205  1.00 6.93   ? 122 ILE A CA   1 
ATOM   875   C C    . ILE A 1 122 ? 25.572  53.137  19.250  1.00 7.60   ? 122 ILE A C    1 
ATOM   876   O O    . ILE A 1 122 ? 25.554  54.036  18.478  1.00 9.22   ? 122 ILE A O    1 
ATOM   877   C CB   . ILE A 1 122 ? 23.219  52.358  19.933  1.00 7.80   ? 122 ILE A CB   1 
ATOM   878   C CG1  . ILE A 1 122 ? 22.180  51.367  19.456  1.00 12.59  ? 122 ILE A CG1  1 
ATOM   879   C CG2  . ILE A 1 122 ? 22.695  53.753  19.666  1.00 8.27   ? 122 ILE A CG2  1 
ATOM   880   C CD1  . ILE A 1 122 ? 20.837  51.590  20.077  1.00 24.81  ? 122 ILE A CD1  1 
ATOM   881   N N    . MET A 1 123 ? 26.571  53.034  20.075  1.00 8.95   ? 123 MET A N    1 
ATOM   882   C CA   . MET A 1 123 ? 27.622  54.022  20.056  1.00 8.97   ? 123 MET A CA   1 
ATOM   883   C C    . MET A 1 123 ? 28.641  53.706  19.013  1.00 9.57   ? 123 MET A C    1 
ATOM   884   O O    . MET A 1 123 ? 29.188  54.579  18.401  1.00 10.49  ? 123 MET A O    1 
ATOM   885   C CB   . MET A 1 123 ? 28.234  54.204  21.429  1.00 6.14   ? 123 MET A CB   1 
ATOM   886   C CG   . MET A 1 123 ? 27.265  54.771  22.438  1.00 6.80   ? 123 MET A CG   1 
ATOM   887   S SD   . MET A 1 123 ? 27.550  56.496  22.725  1.00 12.42  ? 123 MET A SD   1 
ATOM   888   C CE   . MET A 1 123 ? 25.897  57.116  22.609  1.00 9.34   ? 123 MET A CE   1 
ATOM   889   N N    . PHE A 1 124 ? 28.856  52.444  18.743  1.00 8.85   ? 124 PHE A N    1 
ATOM   890   C CA   . PHE A 1 124 ? 29.825  52.037  17.752  1.00 11.00  ? 124 PHE A CA   1 
ATOM   891   C C    . PHE A 1 124 ? 29.252  51.757  16.374  1.00 12.94  ? 124 PHE A C    1 
ATOM   892   O O    . PHE A 1 124 ? 29.987  51.607  15.425  1.00 13.30  ? 124 PHE A O    1 
ATOM   893   C CB   . PHE A 1 124 ? 30.513  50.823  18.265  1.00 10.64  ? 124 PHE A CB   1 
ATOM   894   C CG   . PHE A 1 124 ? 31.578  51.091  19.243  1.00 11.65  ? 124 PHE A CG   1 
ATOM   895   C CD1  . PHE A 1 124 ? 32.481  52.088  19.038  1.00 14.10  ? 124 PHE A CD1  1 
ATOM   896   C CD2  . PHE A 1 124 ? 31.692  50.313  20.349  1.00 14.00  ? 124 PHE A CD2  1 
ATOM   897   C CE1  . PHE A 1 124 ? 33.477  52.322  19.945  1.00 14.86  ? 124 PHE A CE1  1 
ATOM   898   C CE2  . PHE A 1 124 ? 32.687  50.527  21.248  1.00 22.32  ? 124 PHE A CE2  1 
ATOM   899   C CZ   . PHE A 1 124 ? 33.583  51.538  21.048  1.00 21.08  ? 124 PHE A CZ   1 
ATOM   900   N N    . GLU A 1 125 ? 27.942  51.724  16.244  1.00 11.24  ? 125 GLU A N    1 
ATOM   901   C CA   . GLU A 1 125 ? 27.287  51.451  14.996  1.00 7.32   ? 125 GLU A CA   1 
ATOM   902   C C    . GLU A 1 125 ? 26.275  52.486  14.572  1.00 6.32   ? 125 GLU A C    1 
ATOM   903   O O    . GLU A 1 125 ? 25.809  52.436  13.462  1.00 10.52  ? 125 GLU A O    1 
ATOM   904   C CB   . GLU A 1 125 ? 26.523  50.172  15.154  1.00 8.24   ? 125 GLU A CB   1 
ATOM   905   C CG   . GLU A 1 125 ? 27.298  48.888  14.928  1.00 14.41  ? 125 GLU A CG   1 
ATOM   906   C CD   . GLU A 1 125 ? 26.418  47.658  15.055  1.00 17.07  ? 125 GLU A CD   1 
ATOM   907   O OE1  . GLU A 1 125 ? 25.192  47.801  14.921  1.00 16.93  ? 125 GLU A OE1  1 
ATOM   908   O OE2  . GLU A 1 125 ? 26.943  46.553  15.288  1.00 12.96  ? 125 GLU A OE2  1 
ATOM   909   N N    . THR A 1 126 ? 25.907  53.414  15.425  1.00 8.55   ? 126 THR A N    1 
ATOM   910   C CA   . THR A 1 126 ? 24.990  54.441  15.053  1.00 4.57   ? 126 THR A CA   1 
ATOM   911   C C    . THR A 1 126 ? 25.687  55.762  15.139  1.00 5.50   ? 126 THR A C    1 
ATOM   912   O O    . THR A 1 126 ? 25.386  56.679  14.387  1.00 5.37   ? 126 THR A O    1 
ATOM   913   C CB   . THR A 1 126 ? 23.709  54.343  15.888  1.00 6.60   ? 126 THR A CB   1 
ATOM   914   O OG1  . THR A 1 126 ? 23.181  53.018  15.804  1.00 13.18  ? 126 THR A OG1  1 
ATOM   915   C CG2  . THR A 1 126 ? 22.639  55.314  15.436  1.00 7.73   ? 126 THR A CG2  1 
ATOM   916   N N    . PHE A 1 127 ? 26.667  55.869  16.019  1.00 8.06   ? 127 PHE A N    1 
ATOM   917   C CA   . PHE A 1 127 ? 27.436  57.122  16.194  1.00 9.38   ? 127 PHE A CA   1 
ATOM   918   C C    . PHE A 1 127 ? 28.927  57.029  15.887  1.00 10.61  ? 127 PHE A C    1 
ATOM   919   O O    . PHE A 1 127 ? 29.585  58.025  15.841  1.00 15.08  ? 127 PHE A O    1 
ATOM   920   C CB   . PHE A 1 127 ? 27.244  57.672  17.610  1.00 6.10   ? 127 PHE A CB   1 
ATOM   921   C CG   . PHE A 1 127 ? 25.829  57.966  17.972  1.00 5.10   ? 127 PHE A CG   1 
ATOM   922   C CD1  . PHE A 1 127 ? 25.201  59.080  17.482  1.00 7.50   ? 127 PHE A CD1  1 
ATOM   923   C CD2  . PHE A 1 127 ? 25.139  57.139  18.817  1.00 5.03   ? 127 PHE A CD2  1 
ATOM   924   C CE1  . PHE A 1 127 ? 23.900  59.351  17.811  1.00 10.00  ? 127 PHE A CE1  1 
ATOM   925   C CE2  . PHE A 1 127 ? 23.838  57.397  19.152  1.00 6.12   ? 127 PHE A CE2  1 
ATOM   926   C CZ   . PHE A 1 127 ? 23.214  58.506  18.645  1.00 9.31   ? 127 PHE A CZ   1 
ATOM   927   N N    . ASN A 1 128 ? 29.470  55.850  15.697  1.00 9.81   ? 128 ASN A N    1 
ATOM   928   C CA   . ASN A 1 128 ? 30.905  55.628  15.455  1.00 13.38  ? 128 ASN A CA   1 
ATOM   929   C C    . ASN A 1 128 ? 31.813  56.228  16.439  1.00 15.70  ? 128 ASN A C    1 
ATOM   930   O O    . ASN A 1 128 ? 32.767  56.873  16.079  1.00 19.80  ? 128 ASN A O    1 
ATOM   931   C CB   . ASN A 1 128 ? 31.398  55.936  14.045  1.00 12.68  ? 128 ASN A CB   1 
ATOM   932   C CG   . ASN A 1 128 ? 32.388  54.916  13.531  1.00 14.76  ? 128 ASN A CG   1 
ATOM   933   O OD1  . ASN A 1 128 ? 32.389  53.768  13.957  1.00 17.76  ? 128 ASN A OD1  1 
ATOM   934   N ND2  . ASN A 1 128 ? 33.231  55.333  12.608  1.00 9.81   ? 128 ASN A ND2  1 
ATOM   935   N N    . THR A 1 129 ? 31.545  55.970  17.697  1.00 13.01  ? 129 THR A N    1 
ATOM   936   C CA   . THR A 1 129 ? 32.362  56.502  18.721  1.00 14.09  ? 129 THR A CA   1 
ATOM   937   C C    . THR A 1 129 ? 33.718  55.913  18.486  1.00 18.66  ? 129 THR A C    1 
ATOM   938   O O    . THR A 1 129 ? 33.838  54.767  18.105  1.00 15.59  ? 129 THR A O    1 
ATOM   939   C CB   . THR A 1 129 ? 31.786  56.203  20.093  1.00 11.80  ? 129 THR A CB   1 
ATOM   940   O OG1  . THR A 1 129 ? 31.309  54.867  20.134  1.00 12.55  ? 129 THR A OG1  1 
ATOM   941   C CG2  . THR A 1 129 ? 30.657  57.144  20.371  1.00 11.44  ? 129 THR A CG2  1 
ATOM   942   N N    . PRO A 1 130 ? 34.799  56.749  18.685  1.00 15.32  ? 130 PRO A N    1 
ATOM   943   C CA   . PRO A 1 130 ? 36.082  56.122  18.483  1.00 14.53  ? 130 PRO A CA   1 
ATOM   944   C C    . PRO A 1 130 ? 36.339  55.156  19.535  1.00 16.21  ? 130 PRO A C    1 
ATOM   945   O O    . PRO A 1 130 ? 37.037  54.189  19.315  1.00 15.30  ? 130 PRO A O    1 
ATOM   946   C CB   . PRO A 1 130 ? 37.046  57.254  18.714  1.00 15.91  ? 130 PRO A CB   1 
ATOM   947   C CG   . PRO A 1 130 ? 36.325  58.467  18.393  1.00 20.31  ? 130 PRO A CG   1 
ATOM   948   C CD   . PRO A 1 130 ? 35.001  58.188  18.983  1.00 16.64  ? 130 PRO A CD   1 
ATOM   949   N N    . ALA A 1 131 ? 35.815  55.442  20.705  1.00 20.01  ? 131 ALA A N    1 
ATOM   950   C CA   . ALA A 1 131 ? 35.966  54.574  21.832  1.00 13.86  ? 131 ALA A CA   1 
ATOM   951   C C    . ALA A 1 131 ? 34.965  54.955  22.857  1.00 11.35  ? 131 ALA A C    1 
ATOM   952   O O    . ALA A 1 131 ? 34.514  56.075  22.890  1.00 10.59  ? 131 ALA A O    1 
ATOM   953   C CB   . ALA A 1 131 ? 37.343  54.679  22.380  1.00 11.69  ? 131 ALA A CB   1 
ATOM   954   N N    . MET A 1 132 ? 34.600  54.004  23.700  1.00 12.46  ? 132 MET A N    1 
ATOM   955   C CA   . MET A 1 132 ? 33.643  54.253  24.745  1.00 11.30  ? 132 MET A CA   1 
ATOM   956   C C    . MET A 1 132 ? 33.879  53.470  25.996  1.00 14.24  ? 132 MET A C    1 
ATOM   957   O O    . MET A 1 132 ? 34.634  52.519  26.005  1.00 15.89  ? 132 MET A O    1 
ATOM   958   C CB   . MET A 1 132 ? 32.256  53.898  24.268  1.00 10.14  ? 132 MET A CB   1 
ATOM   959   C CG   . MET A 1 132 ? 31.986  52.417  24.237  1.00 11.23  ? 132 MET A CG   1 
ATOM   960   S SD   . MET A 1 132 ? 30.283  52.125  23.855  1.00 21.56  ? 132 MET A SD   1 
ATOM   961   C CE   . MET A 1 132 ? 29.519  52.495  25.422  1.00 14.90  ? 132 MET A CE   1 
ATOM   962   N N    . TYR A 1 133 ? 33.213  53.873  27.069  1.00 13.26  ? 133 TYR A N    1 
ATOM   963   C CA   . TYR A 1 133 ? 33.260  53.150  28.309  1.00 12.08  ? 133 TYR A CA   1 
ATOM   964   C C    . TYR A 1 133 ? 32.007  53.456  29.078  1.00 12.93  ? 133 TYR A C    1 
ATOM   965   O O    . TYR A 1 133 ? 31.468  54.512  28.920  1.00 11.17  ? 133 TYR A O    1 
ATOM   966   C CB   . TYR A 1 133 ? 34.480  53.543  29.121  1.00 13.54  ? 133 TYR A CB   1 
ATOM   967   C CG   . TYR A 1 133 ? 34.857  52.590  30.232  1.00 16.69  ? 133 TYR A CG   1 
ATOM   968   C CD1  . TYR A 1 133 ? 35.292  51.322  29.952  1.00 16.29  ? 133 TYR A CD1  1 
ATOM   969   C CD2  . TYR A 1 133 ? 34.771  52.962  31.559  1.00 15.05  ? 133 TYR A CD2  1 
ATOM   970   C CE1  . TYR A 1 133 ? 35.648  50.449  30.953  1.00 17.30  ? 133 TYR A CE1  1 
ATOM   971   C CE2  . TYR A 1 133 ? 35.121  52.090  32.567  1.00 14.06  ? 133 TYR A CE2  1 
ATOM   972   C CZ   . TYR A 1 133 ? 35.558  50.831  32.252  1.00 17.63  ? 133 TYR A CZ   1 
ATOM   973   O OH   . TYR A 1 133 ? 35.910  49.940  33.233  1.00 13.10  ? 133 TYR A OH   1 
ATOM   974   N N    . VAL A 1 134 ? 31.509  52.520  29.879  1.00 14.10  ? 134 VAL A N    1 
ATOM   975   C CA   . VAL A 1 134 ? 30.382  52.760  30.755  1.00 10.99  ? 134 VAL A CA   1 
ATOM   976   C C    . VAL A 1 134 ? 30.816  52.463  32.146  1.00 13.38  ? 134 VAL A C    1 
ATOM   977   O O    . VAL A 1 134 ? 31.576  51.547  32.368  1.00 13.70  ? 134 VAL A O    1 
ATOM   978   C CB   . VAL A 1 134 ? 29.183  51.873  30.485  1.00 11.08  ? 134 VAL A CB   1 
ATOM   979   C CG1  . VAL A 1 134 ? 28.124  52.119  31.513  1.00 12.05  ? 134 VAL A CG1  1 
ATOM   980   C CG2  . VAL A 1 134 ? 28.627  52.111  29.103  1.00 16.31  ? 134 VAL A CG2  1 
ATOM   981   N N    . ALA A 1 135 ? 30.355  53.251  33.098  1.00 12.62  ? 135 ALA A N    1 
ATOM   982   C CA   . ALA A 1 135 ? 30.651  53.015  34.484  1.00 10.30  ? 135 ALA A CA   1 
ATOM   983   C C    . ALA A 1 135 ? 29.362  53.182  35.186  1.00 11.21  ? 135 ALA A C    1 
ATOM   984   O O    . ALA A 1 135 ? 28.411  53.649  34.609  1.00 10.27  ? 135 ALA A O    1 
ATOM   985   C CB   . ALA A 1 135 ? 31.643  54.000  34.984  1.00 9.86   ? 135 ALA A CB   1 
ATOM   986   N N    . ILE A 1 136 ? 29.293  52.767  36.426  1.00 10.26  ? 136 ILE A N    1 
ATOM   987   C CA   . ILE A 1 136 ? 28.027  52.802  37.110  1.00 8.26   ? 136 ILE A CA   1 
ATOM   988   C C    . ILE A 1 136 ? 27.953  54.166  37.652  1.00 6.68   ? 136 ILE A C    1 
ATOM   989   O O    . ILE A 1 136 ? 28.952  54.719  38.045  1.00 9.81   ? 136 ILE A O    1 
ATOM   990   C CB   . ILE A 1 136 ? 27.921  51.699  38.175  1.00 6.53   ? 136 ILE A CB   1 
ATOM   991   C CG1  . ILE A 1 136 ? 27.944  50.321  37.541  1.00 8.16   ? 136 ILE A CG1  1 
ATOM   992   C CG2  . ILE A 1 136 ? 26.668  51.820  38.991  1.00 5.59   ? 136 ILE A CG2  1 
ATOM   993   C CD1  . ILE A 1 136 ? 29.126  49.481  37.949  1.00 8.34   ? 136 ILE A CD1  1 
ATOM   994   N N    . GLN A 1 137 ? 26.776  54.739  37.635  1.00 5.20   ? 137 GLN A N    1 
ATOM   995   C CA   . GLN A 1 137 ? 26.570  56.059  38.115  1.00 5.94   ? 137 GLN A CA   1 
ATOM   996   C C    . GLN A 1 137 ? 27.030  56.204  39.515  1.00 6.73   ? 137 GLN A C    1 
ATOM   997   O O    . GLN A 1 137 ? 27.340  57.258  39.947  1.00 8.73   ? 137 GLN A O    1 
ATOM   998   C CB   . GLN A 1 137 ? 25.094  56.349  38.041  1.00 6.00   ? 137 GLN A CB   1 
ATOM   999   C CG   . GLN A 1 137 ? 24.615  56.763  36.683  1.00 7.89   ? 137 GLN A CG   1 
ATOM   1000  C CD   . GLN A 1 137 ? 23.123  56.745  36.583  1.00 10.94  ? 137 GLN A CD   1 
ATOM   1001  O OE1  . GLN A 1 137 ? 22.484  55.769  36.935  1.00 9.88   ? 137 GLN A OE1  1 
ATOM   1002  N NE2  . GLN A 1 137 ? 22.557  57.832  36.104  1.00 16.35  ? 137 GLN A NE2  1 
ATOM   1003  N N    . ALA A 1 138 ? 27.122  55.140  40.251  1.00 5.42   ? 138 ALA A N    1 
ATOM   1004  C CA   . ALA A 1 138 ? 27.466  55.240  41.629  1.00 5.01   ? 138 ALA A CA   1 
ATOM   1005  C C    . ALA A 1 138 ? 28.927  55.096  41.880  1.00 7.76   ? 138 ALA A C    1 
ATOM   1006  O O    . ALA A 1 138 ? 29.436  55.510  42.879  1.00 12.26  ? 138 ALA A O    1 
ATOM   1007  C CB   . ALA A 1 138 ? 26.761  54.160  42.333  1.00 5.72   ? 138 ALA A CB   1 
ATOM   1008  N N    . VAL A 1 139 ? 29.636  54.470  40.984  1.00 5.17   ? 139 VAL A N    1 
ATOM   1009  C CA   . VAL A 1 139 ? 31.016  54.196  41.221  1.00 6.28   ? 139 VAL A CA   1 
ATOM   1010  C C    . VAL A 1 139 ? 31.652  55.472  40.902  1.00 7.49   ? 139 VAL A C    1 
ATOM   1011  O O    . VAL A 1 139 ? 32.692  55.800  41.415  1.00 11.34  ? 139 VAL A O    1 
ATOM   1012  C CB   . VAL A 1 139 ? 31.452  53.037  40.332  1.00 5.60   ? 139 VAL A CB   1 
ATOM   1013  C CG1  . VAL A 1 139 ? 32.927  52.788  40.433  1.00 6.04   ? 139 VAL A CG1  1 
ATOM   1014  C CG2  . VAL A 1 139 ? 30.718  51.782  40.735  1.00 5.40   ? 139 VAL A CG2  1 
ATOM   1015  N N    . LEU A 1 140 ? 30.961  56.275  40.128  1.00 7.11   ? 140 LEU A N    1 
ATOM   1016  C CA   . LEU A 1 140 ? 31.515  57.534  39.676  1.00 9.03   ? 140 LEU A CA   1 
ATOM   1017  C C    . LEU A 1 140 ? 31.283  58.614  40.665  1.00 9.34   ? 140 LEU A C    1 
ATOM   1018  O O    . LEU A 1 140 ? 32.093  59.481  40.801  1.00 11.85  ? 140 LEU A O    1 
ATOM   1019  C CB   . LEU A 1 140 ? 30.951  57.897  38.311  1.00 7.65   ? 140 LEU A CB   1 
ATOM   1020  C CG   . LEU A 1 140 ? 31.360  57.125  37.078  1.00 6.55   ? 140 LEU A CG   1 
ATOM   1021  C CD1  . LEU A 1 140 ? 30.705  57.755  35.874  1.00 5.39   ? 140 LEU A CD1  1 
ATOM   1022  C CD2  . LEU A 1 140 ? 32.861  57.164  36.949  1.00 9.66   ? 140 LEU A CD2  1 
ATOM   1023  N N    . SER A 1 141 ? 30.200  58.561  41.409  1.00 7.38   ? 141 SER A N    1 
ATOM   1024  C CA   . SER A 1 141 ? 29.970  59.537  42.452  1.00 7.53   ? 141 SER A CA   1 
ATOM   1025  C C    . SER A 1 141 ? 30.905  59.326  43.586  1.00 10.43  ? 141 SER A C    1 
ATOM   1026  O O    . SER A 1 141 ? 31.075  60.194  44.413  1.00 15.80  ? 141 SER A O    1 
ATOM   1027  C CB   . SER A 1 141 ? 28.573  59.451  42.969  1.00 5.70   ? 141 SER A CB   1 
ATOM   1028  O OG   . SER A 1 141 ? 27.727  58.847  42.052  1.00 12.98  ? 141 SER A OG   1 
ATOM   1029  N N    . LEU A 1 142 ? 31.548  58.194  43.631  1.00 10.70  ? 142 LEU A N    1 
ATOM   1030  C CA   . LEU A 1 142 ? 32.406  57.880  44.741  1.00 15.81  ? 142 LEU A CA   1 
ATOM   1031  C C    . LEU A 1 142 ? 33.783  58.305  44.398  1.00 14.70  ? 142 LEU A C    1 
ATOM   1032  O O    . LEU A 1 142 ? 34.528  58.659  45.271  1.00 15.07  ? 142 LEU A O    1 
ATOM   1033  C CB   . LEU A 1 142 ? 32.356  56.363  45.025  1.00 13.17  ? 142 LEU A CB   1 
ATOM   1034  C CG   . LEU A 1 142 ? 32.859  55.760  46.329  1.00 15.01  ? 142 LEU A CG   1 
ATOM   1035  C CD1  . LEU A 1 142 ? 31.994  56.143  47.507  1.00 6.83   ? 142 LEU A CD1  1 
ATOM   1036  C CD2  . LEU A 1 142 ? 32.883  54.263  46.183  1.00 15.87  ? 142 LEU A CD2  1 
ATOM   1037  N N    . TYR A 1 143 ? 34.133  58.255  43.124  1.00 11.45  ? 143 TYR A N    1 
ATOM   1038  C CA   . TYR A 1 143 ? 35.465  58.629  42.683  1.00 11.36  ? 143 TYR A CA   1 
ATOM   1039  C C    . TYR A 1 143 ? 35.641  60.104  42.757  1.00 11.04  ? 143 TYR A C    1 
ATOM   1040  O O    . TYR A 1 143 ? 36.716  60.580  43.034  1.00 11.83  ? 143 TYR A O    1 
ATOM   1041  C CB   . TYR A 1 143 ? 35.641  58.167  41.254  1.00 11.20  ? 143 TYR A CB   1 
ATOM   1042  C CG   . TYR A 1 143 ? 35.938  56.721  41.018  1.00 11.59  ? 143 TYR A CG   1 
ATOM   1043  C CD1  . TYR A 1 143 ? 36.529  55.934  41.984  1.00 12.61  ? 143 TYR A CD1  1 
ATOM   1044  C CD2  . TYR A 1 143 ? 35.649  56.147  39.799  1.00 9.06   ? 143 TYR A CD2  1 
ATOM   1045  C CE1  . TYR A 1 143 ? 36.804  54.606  41.743  1.00 9.61   ? 143 TYR A CE1  1 
ATOM   1046  C CE2  . TYR A 1 143 ? 35.923  54.825  39.552  1.00 7.99   ? 143 TYR A CE2  1 
ATOM   1047  C CZ   . TYR A 1 143 ? 36.503  54.065  40.529  1.00 6.72   ? 143 TYR A CZ   1 
ATOM   1048  O OH   . TYR A 1 143 ? 36.769  52.757  40.272  1.00 7.43   ? 143 TYR A OH   1 
ATOM   1049  N N    . ALA A 1 144 ? 34.581  60.847  42.543  1.00 8.67   ? 144 ALA A N    1 
ATOM   1050  C CA   . ALA A 1 144 ? 34.627  62.275  42.698  1.00 9.77   ? 144 ALA A CA   1 
ATOM   1051  C C    . ALA A 1 144 ? 34.898  62.657  44.117  1.00 16.70  ? 144 ALA A C    1 
ATOM   1052  O O    . ALA A 1 144 ? 35.356  63.753  44.375  1.00 24.83  ? 144 ALA A O    1 
ATOM   1053  C CB   . ALA A 1 144 ? 33.313  62.844  42.302  1.00 7.28   ? 144 ALA A CB   1 
ATOM   1054  N N    . SER A 1 145 ? 34.665  61.758  45.061  1.00 18.27  ? 145 SER A N    1 
ATOM   1055  C CA   . SER A 1 145 ? 34.842  62.025  46.467  1.00 13.40  ? 145 SER A CA   1 
ATOM   1056  C C    . SER A 1 145 ? 36.190  61.546  46.927  1.00 12.60  ? 145 SER A C    1 
ATOM   1057  O O    . SER A 1 145 ? 36.546  61.714  48.062  1.00 14.58  ? 145 SER A O    1 
ATOM   1058  C CB   . SER A 1 145 ? 33.715  61.358  47.216  1.00 12.02  ? 145 SER A CB   1 
ATOM   1059  O OG   . SER A 1 145 ? 32.526  61.450  46.474  1.00 8.51   ? 145 SER A OG   1 
ATOM   1060  N N    . GLY A 1 146 ? 36.956  60.940  46.053  1.00 12.55  ? 146 GLY A N    1 
ATOM   1061  C CA   . GLY A 1 146 ? 38.302  60.519  46.391  1.00 15.48  ? 146 GLY A CA   1 
ATOM   1062  C C    . GLY A 1 146 ? 38.283  59.152  46.888  1.00 12.87  ? 146 GLY A C    1 
ATOM   1063  O O    . GLY A 1 146 ? 39.265  58.655  47.397  1.00 16.20  ? 146 GLY A O    1 
ATOM   1064  N N    . ARG A 1 147 ? 37.172  58.491  46.673  1.00 14.41  ? 147 ARG A N    1 
ATOM   1065  C CA   . ARG A 1 147 ? 36.984  57.181  47.212  1.00 14.39  ? 147 ARG A CA   1 
ATOM   1066  C C    . ARG A 1 147 ? 36.857  56.097  46.212  1.00 12.84  ? 147 ARG A C    1 
ATOM   1067  O O    . ARG A 1 147 ? 36.313  56.304  45.170  1.00 13.35  ? 147 ARG A O    1 
ATOM   1068  C CB   . ARG A 1 147 ? 35.727  57.232  48.038  1.00 12.26  ? 147 ARG A CB   1 
ATOM   1069  C CG   . ARG A 1 147 ? 35.938  57.374  49.521  1.00 11.82  ? 147 ARG A CG   1 
ATOM   1070  C CD   . ARG A 1 147 ? 34.972  58.380  50.093  1.00 8.45   ? 147 ARG A CD   1 
ATOM   1071  N NE   . ARG A 1 147 ? 35.515  58.945  51.310  1.00 10.29  ? 147 ARG A NE   1 
ATOM   1072  C CZ   . ARG A 1 147 ? 35.603  60.243  51.547  1.00 12.38  ? 147 ARG A CZ   1 
ATOM   1073  N NH1  . ARG A 1 147 ? 35.166  61.104  50.652  1.00 13.76  ? 147 ARG A NH1  1 
ATOM   1074  N NH2  . ARG A 1 147 ? 36.119  60.673  52.679  1.00 11.35  ? 147 ARG A NH2  1 
ATOM   1075  N N    . THR A 1 148 ? 37.371  54.925  46.536  1.00 11.09  ? 148 THR A N    1 
ATOM   1076  C CA   . THR A 1 148 ? 37.315  53.799  45.669  1.00 11.05  ? 148 THR A CA   1 
ATOM   1077  C C    . THR A 1 148 ? 36.496  52.796  46.410  1.00 9.19   ? 148 THR A C    1 
ATOM   1078  O O    . THR A 1 148 ? 35.857  51.976  45.806  1.00 12.18  ? 148 THR A O    1 
ATOM   1079  C CB   . THR A 1 148 ? 38.713  53.246  45.471  1.00 15.23  ? 148 THR A CB   1 
ATOM   1080  O OG1  . THR A 1 148 ? 39.340  53.066  46.741  1.00 20.48  ? 148 THR A OG1  1 
ATOM   1081  C CG2  . THR A 1 148 ? 39.549  54.183  44.630  1.00 13.52  ? 148 THR A CG2  1 
ATOM   1082  N N    . THR A 1 149 ? 36.475  52.871  47.727  1.00 8.29   ? 149 THR A N    1 
ATOM   1083  C CA   . THR A 1 149 ? 35.692  51.957  48.564  1.00 9.79   ? 149 THR A CA   1 
ATOM   1084  C C    . THR A 1 149 ? 34.699  52.721  49.417  1.00 7.93   ? 149 THR A C    1 
ATOM   1085  O O    . THR A 1 149 ? 35.064  53.673  50.066  1.00 6.90   ? 149 THR A O    1 
ATOM   1086  C CB   . THR A 1 149 ? 36.569  51.049  49.460  1.00 8.11   ? 149 THR A CB   1 
ATOM   1087  O OG1  . THR A 1 149 ? 37.384  50.197  48.657  1.00 9.58   ? 149 THR A OG1  1 
ATOM   1088  C CG2  . THR A 1 149 ? 35.734  50.211  50.388  1.00 6.95   ? 149 THR A CG2  1 
ATOM   1089  N N    . GLY A 1 150 ? 33.431  52.324  49.386  1.00 6.75   ? 150 GLY A N    1 
ATOM   1090  C CA   . GLY A 1 150 ? 32.396  52.968  50.150  1.00 6.16   ? 150 GLY A CA   1 
ATOM   1091  C C    . GLY A 1 150 ? 30.991  52.611  49.795  1.00 6.41   ? 150 GLY A C    1 
ATOM   1092  O O    . GLY A 1 150 ? 30.778  51.594  49.207  1.00 6.12   ? 150 GLY A O    1 
ATOM   1093  N N    . ILE A 1 151 ? 30.029  53.444  50.177  1.00 4.24   ? 151 ILE A N    1 
ATOM   1094  C CA   . ILE A 1 151 ? 28.640  53.248  49.841  1.00 6.37   ? 151 ILE A CA   1 
ATOM   1095  C C    . ILE A 1 151 ? 28.053  54.545  49.301  1.00 5.49   ? 151 ILE A C    1 
ATOM   1096  O O    . ILE A 1 151 ? 27.992  55.524  49.977  1.00 4.96   ? 151 ILE A O    1 
ATOM   1097  C CB   . ILE A 1 151 ? 27.806  52.588  50.969  1.00 6.44   ? 151 ILE A CB   1 
ATOM   1098  C CG1  . ILE A 1 151 ? 26.329  52.584  50.646  1.00 5.97   ? 151 ILE A CG1  1 
ATOM   1099  C CG2  . ILE A 1 151 ? 28.032  53.244  52.300  1.00 3.78   ? 151 ILE A CG2  1 
ATOM   1100  C CD1  . ILE A 1 151 ? 25.664  51.335  51.125  1.00 6.13   ? 151 ILE A CD1  1 
ATOM   1101  N N    . VAL A 1 152 ? 27.644  54.561  48.042  1.00 6.92   ? 152 VAL A N    1 
ATOM   1102  C CA   . VAL A 1 152 ? 26.980  55.714  47.447  1.00 5.87   ? 152 VAL A CA   1 
ATOM   1103  C C    . VAL A 1 152 ? 25.457  55.586  47.455  1.00 5.76   ? 152 VAL A C    1 
ATOM   1104  O O    . VAL A 1 152 ? 24.913  54.549  47.190  1.00 4.93   ? 152 VAL A O    1 
ATOM   1105  C CB   . VAL A 1 152 ? 27.483  55.942  46.003  1.00 5.45   ? 152 VAL A CB   1 
ATOM   1106  C CG1  . VAL A 1 152 ? 26.510  56.729  45.154  1.00 6.34   ? 152 VAL A CG1  1 
ATOM   1107  C CG2  . VAL A 1 152 ? 28.797  56.657  46.011  1.00 7.32   ? 152 VAL A CG2  1 
ATOM   1108  N N    . MET A 1 153 ? 24.802  56.675  47.836  1.00 4.41   ? 153 MET A N    1 
ATOM   1109  C CA   . MET A 1 153 ? 23.387  56.741  47.707  1.00 7.92   ? 153 MET A CA   1 
ATOM   1110  C C    . MET A 1 153 ? 23.237  57.759  46.617  1.00 10.77  ? 153 MET A C    1 
ATOM   1111  O O    . MET A 1 153 ? 23.800  58.823  46.720  1.00 7.14   ? 153 MET A O    1 
ATOM   1112  C CB   . MET A 1 153 ? 22.667  57.300  48.911  1.00 6.08   ? 153 MET A CB   1 
ATOM   1113  C CG   . MET A 1 153 ? 21.212  57.496  48.605  1.00 3.99   ? 153 MET A CG   1 
ATOM   1114  S SD   . MET A 1 153 ? 20.447  57.802  50.150  1.00 14.89  ? 153 MET A SD   1 
ATOM   1115  C CE   . MET A 1 153 ? 20.758  59.536  50.343  1.00 15.53  ? 153 MET A CE   1 
ATOM   1116  N N    . ASP A 1 154 ? 22.488  57.427  45.569  1.00 9.87   ? 154 ASP A N    1 
ATOM   1117  C CA   . ASP A 1 154 ? 22.315  58.302  44.465  1.00 6.31   ? 154 ASP A CA   1 
ATOM   1118  C C    . ASP A 1 154 ? 20.861  58.427  44.346  1.00 12.28  ? 154 ASP A C    1 
ATOM   1119  O O    . ASP A 1 154 ? 20.204  57.492  43.988  1.00 8.97   ? 154 ASP A O    1 
ATOM   1120  C CB   . ASP A 1 154 ? 22.902  57.638  43.207  1.00 12.24  ? 154 ASP A CB   1 
ATOM   1121  C CG   . ASP A 1 154 ? 23.464  58.609  42.197  1.00 7.92   ? 154 ASP A CG   1 
ATOM   1122  O OD1  . ASP A 1 154 ? 24.295  59.437  42.558  1.00 7.39   ? 154 ASP A OD1  1 
ATOM   1123  O OD2  . ASP A 1 154 ? 23.122  58.499  41.011  1.00 5.31   ? 154 ASP A OD2  1 
ATOM   1124  N N    . SER A 1 155 ? 20.354  59.610  44.607  1.00 6.80   ? 155 SER A N    1 
ATOM   1125  C CA   . SER A 1 155 ? 18.970  59.863  44.421  1.00 6.39   ? 155 SER A CA   1 
ATOM   1126  C C    . SER A 1 155 ? 18.815  60.983  43.469  1.00 7.82   ? 155 SER A C    1 
ATOM   1127  O O    . SER A 1 155 ? 19.010  62.113  43.816  1.00 9.55   ? 155 SER A O    1 
ATOM   1128  C CB   . SER A 1 155 ? 18.236  60.160  45.725  1.00 5.57   ? 155 SER A CB   1 
ATOM   1129  O OG   . SER A 1 155 ? 16.839  60.197  45.578  1.00 5.93   ? 155 SER A OG   1 
ATOM   1130  N N    . GLY A 1 156 ? 18.453  60.675  42.251  1.00 6.08   ? 156 GLY A N    1 
ATOM   1131  C CA   . GLY A 1 156 ? 18.169  61.687  41.303  1.00 7.29   ? 156 GLY A CA   1 
ATOM   1132  C C    . GLY A 1 156 ? 16.702  61.736  41.098  1.00 9.25   ? 156 GLY A C    1 
ATOM   1133  O O    . GLY A 1 156 ? 15.953  61.581  42.012  1.00 8.43   ? 156 GLY A O    1 
ATOM   1134  N N    . ASP A 1 157 ? 16.285  62.010  39.891  1.00 9.42   ? 157 ASP A N    1 
ATOM   1135  C CA   . ASP A 1 157 ? 14.889  62.169  39.595  1.00 10.19  ? 157 ASP A CA   1 
ATOM   1136  C C    . ASP A 1 157 ? 13.950  61.039  39.617  1.00 11.46  ? 157 ASP A C    1 
ATOM   1137  O O    . ASP A 1 157 ? 12.847  61.206  40.016  1.00 13.09  ? 157 ASP A O    1 
ATOM   1138  C CB   . ASP A 1 157 ? 14.695  63.047  38.369  1.00 13.28  ? 157 ASP A CB   1 
ATOM   1139  C CG   . ASP A 1 157 ? 15.384  64.374  38.501  1.00 21.73  ? 157 ASP A CG   1 
ATOM   1140  O OD1  . ASP A 1 157 ? 14.991  65.169  39.378  1.00 31.05  ? 157 ASP A OD1  1 
ATOM   1141  O OD2  . ASP A 1 157 ? 16.332  64.621  37.735  1.00 14.62  ? 157 ASP A OD2  1 
ATOM   1142  N N    . GLY A 1 158 ? 14.327  59.876  39.183  1.00 8.68   ? 158 GLY A N    1 
ATOM   1143  C CA   . GLY A 1 158 ? 13.334  58.825  39.132  1.00 7.73   ? 158 GLY A CA   1 
ATOM   1144  C C    . GLY A 1 158 ? 13.639  57.593  39.907  1.00 9.24   ? 158 GLY A C    1 
ATOM   1145  O O    . GLY A 1 158 ? 12.759  56.807  40.183  1.00 8.61   ? 158 GLY A O    1 
ATOM   1146  N N    . VAL A 1 159 ? 14.890  57.422  40.282  1.00 8.16   ? 159 VAL A N    1 
ATOM   1147  C CA   . VAL A 1 159 ? 15.195  56.297  41.078  1.00 8.05   ? 159 VAL A CA   1 
ATOM   1148  C C    . VAL A 1 159 ? 16.134  56.653  42.177  1.00 7.60   ? 159 VAL A C    1 
ATOM   1149  O O    . VAL A 1 159 ? 16.794  57.659  42.094  1.00 8.33   ? 159 VAL A O    1 
ATOM   1150  C CB   . VAL A 1 159 ? 15.792  55.192  40.223  1.00 7.32   ? 159 VAL A CB   1 
ATOM   1151  C CG1  . VAL A 1 159 ? 17.049  55.655  39.527  1.00 8.45   ? 159 VAL A CG1  1 
ATOM   1152  C CG2  . VAL A 1 159 ? 16.043  53.961  41.049  1.00 13.31  ? 159 VAL A CG2  1 
ATOM   1153  N N    . THR A 1 160 ? 16.156  55.863  43.241  1.00 7.15   ? 160 THR A N    1 
ATOM   1154  C CA   . THR A 1 160 ? 17.127  56.048  44.304  1.00 6.96   ? 160 THR A CA   1 
ATOM   1155  C C    . THR A 1 160 ? 17.798  54.720  44.441  1.00 8.57   ? 160 THR A C    1 
ATOM   1156  O O    . THR A 1 160 ? 17.173  53.720  44.361  1.00 10.91  ? 160 THR A O    1 
ATOM   1157  C CB   . THR A 1 160 ? 16.536  56.425  45.654  1.00 5.45   ? 160 THR A CB   1 
ATOM   1158  O OG1  . THR A 1 160 ? 15.976  57.735  45.583  1.00 6.28   ? 160 THR A OG1  1 
ATOM   1159  C CG2  . THR A 1 160 ? 17.590  56.398  46.720  1.00 5.30   ? 160 THR A CG2  1 
ATOM   1160  N N    . HIS A 1 161 ? 19.089  54.694  44.587  1.00 8.16   ? 161 HIS A N    1 
ATOM   1161  C CA   . HIS A 1 161 ? 19.776  53.466  44.667  1.00 7.49   ? 161 HIS A CA   1 
ATOM   1162  C C    . HIS A 1 161 ? 20.706  53.644  45.811  1.00 6.18   ? 161 HIS A C    1 
ATOM   1163  O O    . HIS A 1 161 ? 21.164  54.726  46.042  1.00 4.91   ? 161 HIS A O    1 
ATOM   1164  C CB   . HIS A 1 161 ? 20.595  53.291  43.409  1.00 8.92   ? 161 HIS A CB   1 
ATOM   1165  C CG   . HIS A 1 161 ? 20.026  52.363  42.381  1.00 11.88  ? 161 HIS A CG   1 
ATOM   1166  N ND1  . HIS A 1 161 ? 19.560  52.805  41.165  1.00 19.80  ? 161 HIS A ND1  1 
ATOM   1167  C CD2  . HIS A 1 161 ? 19.943  51.015  42.344  1.00 15.28  ? 161 HIS A CD2  1 
ATOM   1168  C CE1  . HIS A 1 161 ? 19.166  51.775  40.445  1.00 25.23  ? 161 HIS A CE1  1 
ATOM   1169  N NE2  . HIS A 1 161 ? 19.385  50.675  41.138  1.00 19.32  ? 161 HIS A NE2  1 
ATOM   1170  N N    . THR A 1 162 ? 20.969  52.591  46.554  1.00 7.27   ? 162 THR A N    1 
ATOM   1171  C CA   . THR A 1 162 ? 21.917  52.607  47.646  1.00 7.09   ? 162 THR A CA   1 
ATOM   1172  C C    . THR A 1 162 ? 22.881  51.518  47.220  1.00 7.32   ? 162 THR A C    1 
ATOM   1173  O O    . THR A 1 162 ? 22.582  50.364  47.379  1.00 7.34   ? 162 THR A O    1 
ATOM   1174  C CB   . THR A 1 162 ? 21.262  52.380  49.013  1.00 6.54   ? 162 THR A CB   1 
ATOM   1175  O OG1  . THR A 1 162 ? 20.355  53.441  49.298  1.00 5.83   ? 162 THR A OG1  1 
ATOM   1176  C CG2  . THR A 1 162 ? 22.307  52.380  50.048  1.00 8.54   ? 162 THR A CG2  1 
ATOM   1177  N N    . VAL A 1 163 ? 24.030  51.884  46.670  1.00 6.45   ? 163 VAL A N    1 
ATOM   1178  C CA   . VAL A 1 163 ? 24.968  50.962  46.101  1.00 7.46   ? 163 VAL A CA   1 
ATOM   1179  C C    . VAL A 1 163 ? 26.246  50.793  46.835  1.00 8.77   ? 163 VAL A C    1 
ATOM   1180  O O    . VAL A 1 163 ? 26.987  51.745  46.991  1.00 0.82   ? 163 VAL A O    1 
ATOM   1181  C CB   . VAL A 1 163 ? 25.390  51.589  44.783  1.00 7.85   ? 163 VAL A CB   1 
ATOM   1182  C CG1  . VAL A 1 163 ? 26.351  50.730  43.993  1.00 8.41   ? 163 VAL A CG1  1 
ATOM   1183  C CG2  . VAL A 1 163 ? 24.167  51.918  43.975  1.00 6.78   ? 163 VAL A CG2  1 
ATOM   1184  N N    . PRO A 1 164 ? 26.528  49.538  47.341  1.00 7.44   ? 164 PRO A N    1 
ATOM   1185  C CA   . PRO A 1 164 ? 27.850  49.366  47.919  1.00 6.50   ? 164 PRO A CA   1 
ATOM   1186  C C    . PRO A 1 164 ? 28.974  49.149  46.940  1.00 4.95   ? 164 PRO A C    1 
ATOM   1187  O O    . PRO A 1 164 ? 28.745  48.503  45.964  1.00 6.56   ? 164 PRO A O    1 
ATOM   1188  C CB   . PRO A 1 164 ? 27.644  48.176  48.776  1.00 5.99   ? 164 PRO A CB   1 
ATOM   1189  C CG   . PRO A 1 164 ? 26.279  48.323  49.257  1.00 6.61   ? 164 PRO A CG   1 
ATOM   1190  C CD   . PRO A 1 164 ? 25.642  48.517  47.948  1.00 6.76   ? 164 PRO A CD   1 
ATOM   1191  N N    . ILE A 1 165 ? 30.159  49.711  47.175  1.00 5.99   ? 165 ILE A N    1 
ATOM   1192  C CA   . ILE A 1 165 ? 31.322  49.624  46.267  1.00 7.10   ? 165 ILE A CA   1 
ATOM   1193  C C    . ILE A 1 165 ? 32.561  49.291  47.059  1.00 6.98   ? 165 ILE A C    1 
ATOM   1194  O O    . ILE A 1 165 ? 32.869  49.978  47.985  1.00 6.10   ? 165 ILE A O    1 
ATOM   1195  C CB   . ILE A 1 165 ? 31.585  50.922  45.462  1.00 6.32   ? 165 ILE A CB   1 
ATOM   1196  C CG1  . ILE A 1 165 ? 30.394  51.322  44.604  1.00 6.94   ? 165 ILE A CG1  1 
ATOM   1197  C CG2  . ILE A 1 165 ? 32.791  50.804  44.567  1.00 5.29   ? 165 ILE A CG2  1 
ATOM   1198  C CD1  . ILE A 1 165 ? 29.799  52.656  44.970  1.00 7.61   ? 165 ILE A CD1  1 
ATOM   1199  N N    . TYR A 1 166 ? 33.242  48.202  46.724  1.00 7.15   ? 166 TYR A N    1 
ATOM   1200  C CA   . TYR A 1 166 ? 34.444  47.810  47.379  1.00 7.91   ? 166 TYR A CA   1 
ATOM   1201  C C    . TYR A 1 166 ? 35.492  47.779  46.349  1.00 11.23  ? 166 TYR A C    1 
ATOM   1202  O O    . TYR A 1 166 ? 35.452  46.928  45.499  1.00 16.88  ? 166 TYR A O    1 
ATOM   1203  C CB   . TYR A 1 166 ? 34.335  46.420  47.874  1.00 11.61  ? 166 TYR A CB   1 
ATOM   1204  C CG   . TYR A 1 166 ? 35.577  45.972  48.615  1.00 19.47  ? 166 TYR A CG   1 
ATOM   1205  C CD1  . TYR A 1 166 ? 36.076  46.710  49.671  1.00 14.36  ? 166 TYR A CD1  1 
ATOM   1206  C CD2  . TYR A 1 166 ? 36.254  44.829  48.248  1.00 20.47  ? 166 TYR A CD2  1 
ATOM   1207  C CE1  . TYR A 1 166 ? 37.210  46.325  50.337  1.00 13.00  ? 166 TYR A CE1  1 
ATOM   1208  C CE2  . TYR A 1 166 ? 37.386  44.435  48.916  1.00 19.87  ? 166 TYR A CE2  1 
ATOM   1209  C CZ   . TYR A 1 166 ? 37.855  45.186  49.958  1.00 17.10  ? 166 TYR A CZ   1 
ATOM   1210  O OH   . TYR A 1 166 ? 38.984  44.790  50.624  1.00 23.48  ? 166 TYR A OH   1 
ATOM   1211  N N    . GLU A 1 167 ? 36.440  48.699  46.401  1.00 9.52   ? 167 GLU A N    1 
ATOM   1212  C CA   . GLU A 1 167 ? 37.501  48.817  45.420  1.00 11.48  ? 167 GLU A CA   1 
ATOM   1213  C C    . GLU A 1 167 ? 37.013  48.903  44.018  1.00 9.26   ? 167 GLU A C    1 
ATOM   1214  O O    . GLU A 1 167 ? 37.263  48.029  43.221  1.00 10.68  ? 167 GLU A O    1 
ATOM   1215  C CB   . GLU A 1 167 ? 38.517  47.704  45.580  1.00 16.37  ? 167 GLU A CB   1 
ATOM   1216  C CG   . GLU A 1 167 ? 39.382  47.781  46.822  1.00 16.92  ? 167 GLU A CG   1 
ATOM   1217  C CD   . GLU A 1 167 ? 40.317  46.599  46.927  1.00 22.33  ? 167 GLU A CD   1 
ATOM   1218  O OE1  . GLU A 1 167 ? 40.163  45.660  46.129  1.00 27.21  ? 167 GLU A OE1  1 
ATOM   1219  O OE2  . GLU A 1 167 ? 41.206  46.601  47.798  1.00 25.49  ? 167 GLU A OE2  1 
ATOM   1220  N N    . GLY A 1 168 ? 36.298  49.948  43.706  1.00 6.32   ? 168 GLY A N    1 
ATOM   1221  C CA   . GLY A 1 168 ? 35.763  50.119  42.383  1.00 6.45   ? 168 GLY A CA   1 
ATOM   1222  C C    . GLY A 1 168 ? 34.651  49.250  41.900  1.00 7.69   ? 168 GLY A C    1 
ATOM   1223  O O    . GLY A 1 168 ? 34.001  49.557  40.926  1.00 8.48   ? 168 GLY A O    1 
ATOM   1224  N N    . TYR A 1 169 ? 34.427  48.144  42.557  1.00 6.92   ? 169 TYR A N    1 
ATOM   1225  C CA   . TYR A 1 169 ? 33.446  47.208  42.117  1.00 6.81   ? 169 TYR A CA   1 
ATOM   1226  C C    . TYR A 1 169 ? 32.271  47.389  42.915  1.00 7.41   ? 169 TYR A C    1 
ATOM   1227  O O    . TYR A 1 169 ? 32.315  47.369  44.101  1.00 6.84   ? 169 TYR A O    1 
ATOM   1228  C CB   . TYR A 1 169 ? 33.938  45.775  42.306  1.00 6.90   ? 169 TYR A CB   1 
ATOM   1229  C CG   . TYR A 1 169 ? 32.967  44.724  41.875  1.00 7.35   ? 169 TYR A CG   1 
ATOM   1230  C CD1  . TYR A 1 169 ? 32.510  44.668  40.579  1.00 7.25   ? 169 TYR A CD1  1 
ATOM   1231  C CD2  . TYR A 1 169 ? 32.504  43.789  42.770  1.00 7.96   ? 169 TYR A CD2  1 
ATOM   1232  C CE1  . TYR A 1 169 ? 31.605  43.715  40.193  1.00 7.45   ? 169 TYR A CE1  1 
ATOM   1233  C CE2  . TYR A 1 169 ? 31.606  42.831  42.388  1.00 8.26   ? 169 TYR A CE2  1 
ATOM   1234  C CZ   . TYR A 1 169 ? 31.162  42.800  41.099  1.00 7.90   ? 169 TYR A CZ   1 
ATOM   1235  O OH   . TYR A 1 169 ? 30.270  41.832  40.718  1.00 8.98   ? 169 TYR A OH   1 
ATOM   1236  N N    . ALA A 1 170 ? 31.167  47.491  42.234  1.00 6.22   ? 170 ALA A N    1 
ATOM   1237  C CA   . ALA A 1 170 ? 29.941  47.627  42.892  1.00 6.66   ? 170 ALA A CA   1 
ATOM   1238  C C    . ALA A 1 170 ? 29.396  46.302  43.131  1.00 6.92   ? 170 ALA A C    1 
ATOM   1239  O O    . ALA A 1 170 ? 29.164  45.569  42.203  1.00 6.12   ? 170 ALA A O    1 
ATOM   1240  C CB   . ALA A 1 170 ? 29.018  48.447  42.060  1.00 6.35   ? 170 ALA A CB   1 
ATOM   1241  N N    . LEU A 1 171 ? 29.155  46.013  44.389  1.00 5.85   ? 171 LEU A N    1 
ATOM   1242  C CA   . LEU A 1 171 ? 28.687  44.758  44.821  1.00 3.66   ? 171 LEU A CA   1 
ATOM   1243  C C    . LEU A 1 171 ? 27.296  44.544  44.498  1.00 6.33   ? 171 LEU A C    1 
ATOM   1244  O O    . LEU A 1 171 ? 26.439  45.086  45.120  1.00 5.20   ? 171 LEU A O    1 
ATOM   1245  C CB   . LEU A 1 171 ? 28.910  44.723  46.316  1.00 5.70   ? 171 LEU A CB   1 
ATOM   1246  C CG   . LEU A 1 171 ? 30.321  45.087  46.733  1.00 7.44   ? 171 LEU A CG   1 
ATOM   1247  C CD1  . LEU A 1 171 ? 30.341  45.497  48.186  1.00 8.32   ? 171 LEU A CD1  1 
ATOM   1248  C CD2  . LEU A 1 171 ? 31.257  43.925  46.485  1.00 12.20  ? 171 LEU A CD2  1 
ATOM   1249  N N    . PRO A 1 172 ? 27.038  43.583  43.564  1.00 5.98   ? 172 PRO A N    1 
ATOM   1250  C CA   . PRO A 1 172 ? 25.665  43.460  43.133  1.00 6.23   ? 172 PRO A CA   1 
ATOM   1251  C C    . PRO A 1 172 ? 24.719  42.757  44.077  1.00 7.70   ? 172 PRO A C    1 
ATOM   1252  O O    . PRO A 1 172 ? 23.510  42.813  43.897  1.00 8.56   ? 172 PRO A O    1 
ATOM   1253  C CB   . PRO A 1 172 ? 25.824  42.670  41.853  1.00 5.34   ? 172 PRO A CB   1 
ATOM   1254  C CG   . PRO A 1 172 ? 26.859  41.696  42.139  1.00 6.98   ? 172 PRO A CG   1 
ATOM   1255  C CD   . PRO A 1 172 ? 27.835  42.482  42.924  1.00 9.15   ? 172 PRO A CD   1 
ATOM   1256  N N    . HIS A 1 173 ? 25.247  42.138  45.104  1.00 6.25   ? 173 HIS A N    1 
ATOM   1257  C CA   . HIS A 1 173 ? 24.448  41.403  46.048  1.00 7.33   ? 173 HIS A CA   1 
ATOM   1258  C C    . HIS A 1 173 ? 23.856  42.301  47.075  1.00 9.46   ? 173 HIS A C    1 
ATOM   1259  O O    . HIS A 1 173 ? 22.912  41.928  47.744  1.00 9.64   ? 173 HIS A O    1 
ATOM   1260  C CB   . HIS A 1 173 ? 25.322  40.365  46.706  1.00 8.94   ? 173 HIS A CB   1 
ATOM   1261  C CG   . HIS A 1 173 ? 26.690  40.833  47.075  1.00 7.27   ? 173 HIS A CG   1 
ATOM   1262  N ND1  . HIS A 1 173 ? 26.976  41.379  48.303  1.00 6.27   ? 173 HIS A ND1  1 
ATOM   1263  C CD2  . HIS A 1 173 ? 27.862  40.767  46.409  1.00 6.32   ? 173 HIS A CD2  1 
ATOM   1264  C CE1  . HIS A 1 173 ? 28.259  41.672  48.362  1.00 7.50   ? 173 HIS A CE1  1 
ATOM   1265  N NE2  . HIS A 1 173 ? 28.819  41.313  47.224  1.00 10.63  ? 173 HIS A NE2  1 
ATOM   1266  N N    . ALA A 1 174 ? 24.340  43.525  47.141  1.00 7.94   ? 174 ALA A N    1 
ATOM   1267  C CA   . ALA A 1 174 ? 23.911  44.457  48.125  1.00 7.57   ? 174 ALA A CA   1 
ATOM   1268  C C    . ALA A 1 174 ? 23.142  45.609  47.569  1.00 7.12   ? 174 ALA A C    1 
ATOM   1269  O O    . ALA A 1 174 ? 22.369  46.200  48.273  1.00 8.49   ? 174 ALA A O    1 
ATOM   1270  C CB   . ALA A 1 174 ? 25.147  44.955  48.728  1.00 5.70   ? 174 ALA A CB   1 
ATOM   1271  N N    . ILE A 1 175 ? 23.326  45.941  46.309  1.00 5.44   ? 175 ILE A N    1 
ATOM   1272  C CA   . ILE A 1 175 ? 22.711  47.092  45.716  1.00 5.86   ? 175 ILE A CA   1 
ATOM   1273  C C    . ILE A 1 175 ? 21.283  47.025  45.923  1.00 6.69   ? 175 ILE A C    1 
ATOM   1274  O O    . ILE A 1 175 ? 20.654  46.054  45.575  1.00 5.70   ? 175 ILE A O    1 
ATOM   1275  C CB   . ILE A 1 175 ? 23.078  47.261  44.236  1.00 5.30   ? 175 ILE A CB   1 
ATOM   1276  C CG1  . ILE A 1 175 ? 24.573  47.465  44.085  1.00 5.39   ? 175 ILE A CG1  1 
ATOM   1277  C CG2  . ILE A 1 175 ? 22.341  48.420  43.607  1.00 5.39   ? 175 ILE A CG2  1 
ATOM   1278  C CD1  . ILE A 1 175 ? 25.062  47.330  42.668  1.00 5.65   ? 175 ILE A CD1  1 
ATOM   1279  N N    . LEU A 1 176 ? 20.736  48.063  46.528  1.00 0.82   ? 176 LEU A N    1 
ATOM   1280  C CA   . LEU A 1 176 ? 19.314  48.138  46.720  1.00 7.11   ? 176 LEU A CA   1 
ATOM   1281  C C    . LEU A 1 176 ? 18.813  49.357  46.033  1.00 7.79   ? 176 LEU A C    1 
ATOM   1282  O O    . LEU A 1 176 ? 19.544  50.287  45.866  1.00 6.67   ? 176 LEU A O    1 
ATOM   1283  C CB   . LEU A 1 176 ? 18.928  48.112  48.195  1.00 9.27   ? 176 LEU A CB   1 
ATOM   1284  C CG   . LEU A 1 176 ? 18.910  46.791  48.966  1.00 6.46   ? 176 LEU A CG   1 
ATOM   1285  C CD1  . LEU A 1 176 ? 18.416  47.003  50.378  1.00 3.04   ? 176 LEU A CD1  1 
ATOM   1286  C CD2  . LEU A 1 176 ? 18.021  45.793  48.259  1.00 11.99  ? 176 LEU A CD2  1 
ATOM   1287  N N    . ARG A 1 177 ? 17.567  49.336  45.594  1.00 9.49   ? 177 ARG A N    1 
ATOM   1288  C CA   . ARG A 1 177 ? 17.002  50.429  44.841  1.00 9.37   ? 177 ARG A CA   1 
ATOM   1289  C C    . ARG A 1 177 ? 15.688  50.900  45.367  1.00 11.94  ? 177 ARG A C    1 
ATOM   1290  O O    . ARG A 1 177 ? 14.830  50.091  45.675  1.00 15.61  ? 177 ARG A O    1 
ATOM   1291  C CB   . ARG A 1 177 ? 16.839  49.982  43.400  1.00 10.10  ? 177 ARG A CB   1 
ATOM   1292  C CG   . ARG A 1 177 ? 15.886  50.746  42.522  1.00 10.56  ? 177 ARG A CG   1 
ATOM   1293  C CD   . ARG A 1 177 ? 15.975  50.147  41.139  1.00 13.26  ? 177 ARG A CD   1 
ATOM   1294  N NE   . ARG A 1 177 ? 14.938  50.609  40.241  1.00 11.59  ? 177 ARG A NE   1 
ATOM   1295  C CZ   . ARG A 1 177 ? 14.955  50.406  38.934  1.00 12.34  ? 177 ARG A CZ   1 
ATOM   1296  N NH1  . ARG A 1 177 ? 15.963  49.766  38.376  1.00 14.53  ? 177 ARG A NH1  1 
ATOM   1297  N NH2  . ARG A 1 177 ? 13.969  50.851  38.187  1.00 15.78  ? 177 ARG A NH2  1 
ATOM   1298  N N    . LEU A 1 178 ? 15.523  52.210  45.484  1.00 12.05  ? 178 LEU A N    1 
ATOM   1299  C CA   . LEU A 1 178 ? 14.268  52.791  45.898  1.00 10.02  ? 178 LEU A CA   1 
ATOM   1300  C C    . LEU A 1 178 ? 13.857  53.576  44.687  1.00 10.03  ? 178 LEU A C    1 
ATOM   1301  O O    . LEU A 1 178 ? 14.629  54.296  44.110  1.00 9.61   ? 178 LEU A O    1 
ATOM   1302  C CB   . LEU A 1 178 ? 14.437  53.635  47.158  1.00 7.71   ? 178 LEU A CB   1 
ATOM   1303  C CG   . LEU A 1 178 ? 13.262  53.749  48.117  1.00 10.20  ? 178 LEU A CG   1 
ATOM   1304  C CD1  . LEU A 1 178 ? 12.930  52.385  48.687  1.00 16.23  ? 178 LEU A CD1  1 
ATOM   1305  C CD2  . LEU A 1 178 ? 13.576  54.724  49.231  1.00 6.81   ? 178 LEU A CD2  1 
ATOM   1306  N N    . ASP A 1 179 ? 12.638  53.419  44.261  1.00 11.31  ? 179 ASP A N    1 
ATOM   1307  C CA   . ASP A 1 179 ? 12.182  54.044  43.061  1.00 12.49  ? 179 ASP A CA   1 
ATOM   1308  C C    . ASP A 1 179 ? 11.510  55.293  43.523  1.00 17.55  ? 179 ASP A C    1 
ATOM   1309  O O    . ASP A 1 179 ? 10.676  55.850  42.827  1.00 21.96  ? 179 ASP A O    1 
ATOM   1310  C CB   . ASP A 1 179 ? 11.192  53.139  42.347  1.00 10.82  ? 179 ASP A CB   1 
ATOM   1311  C CG   . ASP A 1 179 ? 11.781  51.823  41.935  1.00 13.52  ? 179 ASP A CG   1 
ATOM   1312  O OD1  . ASP A 1 179 ? 12.323  51.753  40.822  1.00 12.99  ? 179 ASP A OD1  1 
ATOM   1313  O OD2  . ASP A 1 179 ? 11.667  50.848  42.699  1.00 15.78  ? 179 ASP A OD2  1 
ATOM   1314  N N    . LEU A 1 180 ? 11.883  55.758  44.700  1.00 9.10   ? 180 LEU A N    1 
ATOM   1315  C CA   . LEU A 1 180 ? 11.328  56.967  45.217  1.00 8.22   ? 180 LEU A CA   1 
ATOM   1316  C C    . LEU A 1 180 ? 12.354  57.982  45.072  1.00 8.09   ? 180 LEU A C    1 
ATOM   1317  O O    . LEU A 1 180 ? 13.434  57.831  45.585  1.00 7.62   ? 180 LEU A O    1 
ATOM   1318  C CB   . LEU A 1 180 ? 10.995  56.831  46.675  1.00 9.18   ? 180 LEU A CB   1 
ATOM   1319  C CG   . LEU A 1 180 ? 10.868  57.973  47.662  1.00 8.02   ? 180 LEU A CG   1 
ATOM   1320  C CD1  . LEU A 1 180 ? 9.903   59.024  47.176  1.00 9.24   ? 180 LEU A CD1  1 
ATOM   1321  C CD2  . LEU A 1 180 ? 10.389  57.375  48.963  1.00 8.95   ? 180 LEU A CD2  1 
ATOM   1322  N N    . ALA A 1 181 ? 12.005  59.047  44.379  1.00 8.08   ? 181 ALA A N    1 
ATOM   1323  C CA   . ALA A 1 181 ? 12.899  60.132  44.227  1.00 7.65   ? 181 ALA A CA   1 
ATOM   1324  C C    . ALA A 1 181 ? 12.221  61.401  43.925  1.00 8.55   ? 181 ALA A C    1 
ATOM   1325  O O    . ALA A 1 181 ? 11.054  61.540  44.191  1.00 7.00   ? 181 ALA A O    1 
ATOM   1326  C CB   . ALA A 1 181 ? 13.906  59.837  43.208  1.00 6.57   ? 181 ALA A CB   1 
ATOM   1327  N N    . GLY A 1 182 ? 12.950  62.331  43.348  1.00 7.54   ? 182 GLY A N    1 
ATOM   1328  C CA   . GLY A 1 182 ? 12.440  63.648  43.073  1.00 7.95   ? 182 GLY A CA   1 
ATOM   1329  C C    . GLY A 1 182 ? 11.285  63.805  42.190  1.00 10.71  ? 182 GLY A C    1 
ATOM   1330  O O    . GLY A 1 182 ? 10.667  64.830  42.239  1.00 13.04  ? 182 GLY A O    1 
ATOM   1331  N N    . ARG A 1 183 ? 11.030  62.863  41.313  1.00 12.78  ? 183 ARG A N    1 
ATOM   1332  C CA   . ARG A 1 183 ? 9.832   62.922  40.528  1.00 16.25  ? 183 ARG A CA   1 
ATOM   1333  C C    . ARG A 1 183 ? 8.707   62.823  41.509  1.00 14.12  ? 183 ARG A C    1 
ATOM   1334  O O    . ARG A 1 183 ? 7.739   63.544  41.415  1.00 13.72  ? 183 ARG A O    1 
ATOM   1335  C CB   . ARG A 1 183 ? 9.785   61.737  39.600  1.00 12.84  ? 183 ARG A CB   1 
ATOM   1336  C CG   . ARG A 1 183 ? 10.583  61.831  38.314  1.00 14.65  ? 183 ARG A CG   1 
ATOM   1337  C CD   . ARG A 1 183 ? 9.928   62.642  37.226  1.00 21.30  ? 183 ARG A CD   1 
ATOM   1338  N NE   . ARG A 1 183 ? 10.449  62.240  35.931  1.00 15.91  ? 183 ARG A NE   1 
ATOM   1339  C CZ   . ARG A 1 183 ? 11.536  62.750  35.374  1.00 22.49  ? 183 ARG A CZ   1 
ATOM   1340  N NH1  . ARG A 1 183 ? 12.219  63.697  35.994  1.00 25.16  ? 183 ARG A NH1  1 
ATOM   1341  N NH2  . ARG A 1 183 ? 11.933  62.323  34.189  1.00 36.77  ? 183 ARG A NH2  1 
ATOM   1342  N N    . ASP A 1 184 ? 8.824   61.908  42.456  1.00 11.13  ? 184 ASP A N    1 
ATOM   1343  C CA   . ASP A 1 184 ? 7.825   61.730  43.497  1.00 14.14  ? 184 ASP A CA   1 
ATOM   1344  C C    . ASP A 1 184 ? 7.765   62.830  44.526  1.00 14.37  ? 184 ASP A C    1 
ATOM   1345  O O    . ASP A 1 184 ? 6.719   63.102  45.071  1.00 14.48  ? 184 ASP A O    1 
ATOM   1346  C CB   . ASP A 1 184 ? 7.985   60.340  44.102  1.00 11.58  ? 184 ASP A CB   1 
ATOM   1347  C CG   . ASP A 1 184 ? 7.303   59.270  43.297  1.00 10.49  ? 184 ASP A CG   1 
ATOM   1348  O OD1  . ASP A 1 184 ? 6.601   59.595  42.326  1.00 11.25  ? 184 ASP A OD1  1 
ATOM   1349  O OD2  . ASP A 1 184 ? 7.461   58.091  43.650  1.00 14.15  ? 184 ASP A OD2  1 
ATOM   1350  N N    . LEU A 1 185 ? 8.908   63.383  44.881  1.00 15.89  ? 185 LEU A N    1 
ATOM   1351  C CA   . LEU A 1 185 ? 8.983   64.492  45.822  1.00 11.48  ? 185 LEU A CA   1 
ATOM   1352  C C    . LEU A 1 185 ? 8.351   65.791  45.341  1.00 13.02  ? 185 LEU A C    1 
ATOM   1353  O O    . LEU A 1 185 ? 7.646   66.413  46.077  1.00 12.44  ? 185 LEU A O    1 
ATOM   1354  C CB   . LEU A 1 185 ? 10.427  64.679  46.287  1.00 7.15   ? 185 LEU A CB   1 
ATOM   1355  C CG   . LEU A 1 185 ? 11.074  63.633  47.176  1.00 6.93   ? 185 LEU A CG   1 
ATOM   1356  C CD1  . LEU A 1 185 ? 12.032  64.385  48.062  1.00 10.04  ? 185 LEU A CD1  1 
ATOM   1357  C CD2  . LEU A 1 185 ? 10.050  62.926  48.041  1.00 12.91  ? 185 LEU A CD2  1 
ATOM   1358  N N    . THR A 1 186 ? 8.530   66.179  44.090  1.00 11.00  ? 186 THR A N    1 
ATOM   1359  C CA   . THR A 1 186 ? 7.871   67.362  43.571  1.00 10.37  ? 186 THR A CA   1 
ATOM   1360  C C    . THR A 1 186 ? 6.391   67.176  43.633  1.00 15.13  ? 186 THR A C    1 
ATOM   1361  O O    . THR A 1 186 ? 5.684   68.061  44.061  1.00 22.31  ? 186 THR A O    1 
ATOM   1362  C CB   . THR A 1 186 ? 8.274   67.617  42.142  1.00 13.37  ? 186 THR A CB   1 
ATOM   1363  O OG1  . THR A 1 186 ? 9.643   67.998  42.120  1.00 18.93  ? 186 THR A OG1  1 
ATOM   1364  C CG2  . THR A 1 186 ? 7.463   68.719  41.536  1.00 15.19  ? 186 THR A CG2  1 
ATOM   1365  N N    . ASP A 1 187 ? 5.897   66.014  43.282  1.00 11.76  ? 187 ASP A N    1 
ATOM   1366  C CA   . ASP A 1 187 ? 4.507   65.709  43.345  1.00 10.32  ? 187 ASP A CA   1 
ATOM   1367  C C    . ASP A 1 187 ? 3.871   65.589  44.730  1.00 13.57  ? 187 ASP A C    1 
ATOM   1368  O O    . ASP A 1 187 ? 2.665   65.488  44.801  1.00 15.80  ? 187 ASP A O    1 
ATOM   1369  C CB   . ASP A 1 187 ? 4.379   64.400  42.645  1.00 18.44  ? 187 ASP A CB   1 
ATOM   1370  C CG   . ASP A 1 187 ? 4.492   64.510  41.156  1.00 30.73  ? 187 ASP A CG   1 
ATOM   1371  O OD1  . ASP A 1 187 ? 4.176   65.577  40.607  1.00 35.00  ? 187 ASP A OD1  1 
ATOM   1372  O OD2  . ASP A 1 187 ? 4.864   63.503  40.524  1.00 25.13  ? 187 ASP A OD2  1 
ATOM   1373  N N    . TYR A 1 188 ? 4.639   65.572  45.817  1.00 15.79  ? 188 TYR A N    1 
ATOM   1374  C CA   . TYR A 1 188 ? 4.139   65.537  47.205  1.00 15.36  ? 188 TYR A CA   1 
ATOM   1375  C C    . TYR A 1 188 ? 3.996   66.913  47.701  1.00 15.57  ? 188 TYR A C    1 
ATOM   1376  O O    . TYR A 1 188 ? 3.070   67.193  48.404  1.00 16.75  ? 188 TYR A O    1 
ATOM   1377  C CB   . TYR A 1 188 ? 5.144   64.859  48.124  1.00 15.52  ? 188 TYR A CB   1 
ATOM   1378  C CG   . TYR A 1 188 ? 4.664   64.471  49.487  1.00 13.14  ? 188 TYR A CG   1 
ATOM   1379  C CD1  . TYR A 1 188 ? 3.929   63.325  49.678  1.00 10.41  ? 188 TYR A CD1  1 
ATOM   1380  C CD2  . TYR A 1 188 ? 4.980   65.233  50.591  1.00 17.60  ? 188 TYR A CD2  1 
ATOM   1381  C CE1  . TYR A 1 188 ? 3.495   62.964  50.930  1.00 14.20  ? 188 TYR A CE1  1 
ATOM   1382  C CE2  . TYR A 1 188 ? 4.549   64.882  51.846  1.00 17.75  ? 188 TYR A CE2  1 
ATOM   1383  C CZ   . TYR A 1 188 ? 3.806   63.747  52.005  1.00 13.60  ? 188 TYR A CZ   1 
ATOM   1384  O OH   . TYR A 1 188 ? 3.373   63.406  53.251  1.00 12.09  ? 188 TYR A OH   1 
ATOM   1385  N N    . LEU A 1 189 ? 4.927   67.788  47.370  1.00 15.46  ? 189 LEU A N    1 
ATOM   1386  C CA   . LEU A 1 189 ? 4.841   69.177  47.746  1.00 16.29  ? 189 LEU A CA   1 
ATOM   1387  C C    . LEU A 1 189 ? 3.618   69.693  47.124  1.00 17.50  ? 189 LEU A C    1 
ATOM   1388  O O    . LEU A 1 189 ? 2.805   70.269  47.783  1.00 17.13  ? 189 LEU A O    1 
ATOM   1389  C CB   . LEU A 1 189 ? 6.001   69.918  47.193  1.00 12.46  ? 189 LEU A CB   1 
ATOM   1390  C CG   . LEU A 1 189 ? 6.182   71.297  47.793  1.00 18.75  ? 189 LEU A CG   1 
ATOM   1391  C CD1  . LEU A 1 189 ? 6.362   71.233  49.289  1.00 21.80  ? 189 LEU A CD1  1 
ATOM   1392  C CD2  . LEU A 1 189 ? 7.320   72.034  47.141  1.00 19.02  ? 189 LEU A CD2  1 
ATOM   1393  N N    . MET A 1 190 ? 3.474   69.514  45.835  1.00 14.60  ? 190 MET A N    1 
ATOM   1394  C CA   . MET A 1 190 ? 2.254   69.866  45.166  1.00 19.21  ? 190 MET A CA   1 
ATOM   1395  C C    . MET A 1 190 ? 1.082   69.396  45.943  1.00 20.21  ? 190 MET A C    1 
ATOM   1396  O O    . MET A 1 190 ? 0.231   70.166  46.228  1.00 22.04  ? 190 MET A O    1 
ATOM   1397  C CB   . MET A 1 190 ? 2.178   69.104  43.869  1.00 22.55  ? 190 MET A CB   1 
ATOM   1398  C CG   . MET A 1 190 ? 2.397   69.881  42.594  1.00 25.52  ? 190 MET A CG   1 
ATOM   1399  S SD   . MET A 1 190 ? 2.701   68.806  41.193  1.00 37.38  ? 190 MET A SD   1 
ATOM   1400  C CE   . MET A 1 190 ? 1.110   68.780  40.399  1.00 22.53  ? 190 MET A CE   1 
ATOM   1401  N N    . LYS A 1 191 ? 1.013   68.118  46.260  1.00 17.59  ? 191 LYS A N    1 
ATOM   1402  C CA   . LYS A 1 191 ? -0.148  67.545  46.939  1.00 18.40  ? 191 LYS A CA   1 
ATOM   1403  C C    . LYS A 1 191 ? -0.521  68.086  48.251  1.00 19.34  ? 191 LYS A C    1 
ATOM   1404  O O    . LYS A 1 191 ? -1.662  68.317  48.502  1.00 22.76  ? 191 LYS A O    1 
ATOM   1405  C CB   . LYS A 1 191 ? 0.041   66.070  47.121  1.00 22.36  ? 191 LYS A CB   1 
ATOM   1406  C CG   . LYS A 1 191 ? -1.122  65.331  47.737  1.00 28.86  ? 191 LYS A CG   1 
ATOM   1407  C CD   . LYS A 1 191 ? -0.770  63.858  47.853  1.00 29.11  ? 191 LYS A CD   1 
ATOM   1408  C CE   . LYS A 1 191 ? 0.331   63.619  48.875  1.00 13.68  ? 191 LYS A CE   1 
ATOM   1409  N NZ   . LYS A 1 191 ? -0.100  63.967  50.255  1.00 21.18  ? 191 LYS A NZ   1 
ATOM   1410  N N    . ILE A 1 192 ? 0.441   68.265  49.121  1.00 18.13  ? 192 ILE A N    1 
ATOM   1411  C CA   . ILE A 1 192 ? 0.192   68.781  50.448  1.00 19.66  ? 192 ILE A CA   1 
ATOM   1412  C C    . ILE A 1 192 ? -0.006  70.245  50.454  1.00 21.45  ? 192 ILE A C    1 
ATOM   1413  O O    . ILE A 1 192 ? -0.298  70.828  51.475  1.00 26.79  ? 192 ILE A O    1 
ATOM   1414  C CB   . ILE A 1 192 ? 1.366   68.426  51.361  1.00 19.79  ? 192 ILE A CB   1 
ATOM   1415  C CG1  . ILE A 1 192 ? 2.638   69.176  50.992  1.00 15.27  ? 192 ILE A CG1  1 
ATOM   1416  C CG2  . ILE A 1 192 ? 1.589   66.929  51.351  1.00 20.45  ? 192 ILE A CG2  1 
ATOM   1417  C CD1  . ILE A 1 192 ? 3.849   68.714  51.761  1.00 13.26  ? 192 ILE A CD1  1 
ATOM   1418  N N    . LEU A 1 193 ? 0.142   70.856  49.300  1.00 18.33  ? 193 LEU A N    1 
ATOM   1419  C CA   . LEU A 1 193 ? -0.047  72.264  49.197  1.00 18.71  ? 193 LEU A CA   1 
ATOM   1420  C C    . LEU A 1 193 ? -1.365  72.425  48.555  1.00 24.64  ? 193 LEU A C    1 
ATOM   1421  O O    . LEU A 1 193 ? -1.991  73.436  48.722  1.00 30.45  ? 193 LEU A O    1 
ATOM   1422  C CB   . LEU A 1 193 ? 1.062   72.928  48.401  1.00 16.75  ? 193 LEU A CB   1 
ATOM   1423  C CG   . LEU A 1 193 ? 2.279   73.531  49.089  1.00 18.16  ? 193 LEU A CG   1 
ATOM   1424  C CD1  . LEU A 1 193 ? 3.301   73.916  48.037  1.00 14.02  ? 193 LEU A CD1  1 
ATOM   1425  C CD2  . LEU A 1 193 ? 1.880   74.745  49.894  1.00 16.60  ? 193 LEU A CD2  1 
ATOM   1426  N N    . THR A 1 194 ? -1.807  71.457  47.766  1.00 26.35  ? 194 THR A N    1 
ATOM   1427  C CA   . THR A 1 194 ? -3.154  71.538  47.214  1.00 26.72  ? 194 THR A CA   1 
ATOM   1428  C C    . THR A 1 194 ? -4.133  71.464  48.356  1.00 31.01  ? 194 THR A C    1 
ATOM   1429  O O    . THR A 1 194 ? -5.184  72.086  48.300  1.00 38.55  ? 194 THR A O    1 
ATOM   1430  C CB   . THR A 1 194 ? -3.497  70.503  46.143  1.00 21.56  ? 194 THR A CB   1 
ATOM   1431  O OG1  . THR A 1 194 ? -3.438  69.184  46.686  1.00 23.55  ? 194 THR A OG1  1 
ATOM   1432  C CG2  . THR A 1 194 ? -2.607  70.633  44.971  1.00 24.49  ? 194 THR A CG2  1 
ATOM   1433  N N    . GLU A 1 195 ? -3.800  70.734  49.407  1.00 24.20  ? 195 GLU A N    1 
ATOM   1434  C CA   . GLU A 1 195 ? -4.619  70.666  50.583  1.00 24.08  ? 195 GLU A CA   1 
ATOM   1435  C C    . GLU A 1 195 ? -4.171  71.758  51.508  1.00 26.82  ? 195 GLU A C    1 
ATOM   1436  O O    . GLU A 1 195 ? -4.108  71.541  52.707  1.00 24.52  ? 195 GLU A O    1 
ATOM   1437  C CB   . GLU A 1 195 ? -4.387  69.350  51.247  1.00 22.76  ? 195 GLU A CB   1 
ATOM   1438  C CG   . GLU A 1 195 ? -4.473  68.168  50.309  1.00 26.32  ? 195 GLU A CG   1 
ATOM   1439  C CD   . GLU A 1 195 ? -3.695  66.972  50.807  1.00 28.48  ? 195 GLU A CD   1 
ATOM   1440  O OE1  . GLU A 1 195 ? -3.205  67.020  51.950  1.00 28.13  ? 195 GLU A OE1  1 
ATOM   1441  O OE2  . GLU A 1 195 ? -3.575  65.987  50.055  1.00 23.52  ? 195 GLU A OE2  1 
ATOM   1442  N N    . ARG A 1 196 ? -3.804  72.925  50.983  1.00 27.12  ? 196 ARG A N    1 
ATOM   1443  C CA   . ARG A 1 196 ? -3.446  74.078  51.821  1.00 25.69  ? 196 ARG A CA   1 
ATOM   1444  C C    . ARG A 1 196 ? -4.232  75.252  51.321  1.00 28.16  ? 196 ARG A C    1 
ATOM   1445  O O    . ARG A 1 196 ? -4.511  76.203  52.039  1.00 33.81  ? 196 ARG A O    1 
ATOM   1446  C CB   . ARG A 1 196 ? -1.940  74.303  51.835  1.00 21.08  ? 196 ARG A CB   1 
ATOM   1447  C CG   . ARG A 1 196 ? -1.383  75.404  52.712  1.00 17.23  ? 196 ARG A CG   1 
ATOM   1448  C CD   . ARG A 1 196 ? -1.615  75.119  54.181  1.00 25.70  ? 196 ARG A CD   1 
ATOM   1449  N NE   . ARG A 1 196 ? -0.887  73.942  54.628  1.00 44.18  ? 196 ARG A NE   1 
ATOM   1450  C CZ   . ARG A 1 196 ? -0.986  73.415  55.842  1.00 45.53  ? 196 ARG A CZ   1 
ATOM   1451  N NH1  . ARG A 1 196 ? -1.795  73.955  56.733  1.00 32.50  ? 196 ARG A NH1  1 
ATOM   1452  N NH2  . ARG A 1 196 ? -0.277  72.348  56.160  1.00 44.61  ? 196 ARG A NH2  1 
ATOM   1453  N N    . GLY A 1 197 ? -4.693  75.161  50.099  1.00 27.62  ? 197 GLY A N    1 
ATOM   1454  C CA   . GLY A 1 197 ? -5.510  76.213  49.563  1.00 27.81  ? 197 GLY A CA   1 
ATOM   1455  C C    . GLY A 1 197 ? -4.820  76.668  48.330  1.00 40.97  ? 197 GLY A C    1 
ATOM   1456  O O    . GLY A 1 197 ? -5.318  77.552  47.653  1.00 51.34  ? 197 GLY A O    1 
ATOM   1457  N N    . TYR A 1 198 ? -3.708  76.025  47.973  1.00 40.72  ? 198 TYR A N    1 
ATOM   1458  C CA   . TYR A 1 198 ? -2.931  76.430  46.808  1.00 34.69  ? 198 TYR A CA   1 
ATOM   1459  C C    . TYR A 1 198 ? -3.214  75.481  45.669  1.00 35.48  ? 198 TYR A C    1 
ATOM   1460  O O    . TYR A 1 198 ? -3.716  74.417  45.907  1.00 37.87  ? 198 TYR A O    1 
ATOM   1461  C CB   . TYR A 1 198 ? -1.473  76.548  47.183  1.00 27.39  ? 198 TYR A CB   1 
ATOM   1462  C CG   . TYR A 1 198 ? -1.232  77.646  48.177  1.00 28.02  ? 198 TYR A CG   1 
ATOM   1463  C CD1  . TYR A 1 198 ? -2.051  78.760  48.215  1.00 34.67  ? 198 TYR A CD1  1 
ATOM   1464  C CD2  . TYR A 1 198 ? -0.196  77.577  49.075  1.00 28.80  ? 198 TYR A CD2  1 
ATOM   1465  C CE1  . TYR A 1 198 ? -1.856  79.761  49.132  1.00 34.86  ? 198 TYR A CE1  1 
ATOM   1466  C CE2  . TYR A 1 198 ? 0.016   78.581  49.991  1.00 36.70  ? 198 TYR A CE2  1 
ATOM   1467  C CZ   . TYR A 1 198 ? -0.821  79.669  50.010  1.00 38.07  ? 198 TYR A CZ   1 
ATOM   1468  O OH   . TYR A 1 198 ? -0.628  80.681  50.907  1.00 37.32  ? 198 TYR A OH   1 
ATOM   1469  N N    . SER A 1 199 ? -2.961  75.865  44.425  1.00 34.69  ? 199 SER A N    1 
ATOM   1470  C CA   . SER A 1 199 ? -3.343  75.028  43.281  1.00 33.21  ? 199 SER A CA   1 
ATOM   1471  C C    . SER A 1 199 ? -2.219  74.588  42.501  1.00 30.49  ? 199 SER A C    1 
ATOM   1472  O O    . SER A 1 199 ? -1.585  75.404  41.872  1.00 32.57  ? 199 SER A O    1 
ATOM   1473  C CB   . SER A 1 199 ? -4.146  75.817  42.282  1.00 38.29  ? 199 SER A CB   1 
ATOM   1474  O OG   . SER A 1 199 ? -4.254  75.109  41.060  1.00 46.04  ? 199 SER A OG   1 
ATOM   1475  N N    . PHE A 1 200 ? -1.991  73.287  42.469  1.00 28.84  ? 200 PHE A N    1 
ATOM   1476  C CA   . PHE A 1 200 ? -0.849  72.747  41.786  1.00 26.13  ? 200 PHE A CA   1 
ATOM   1477  C C    . PHE A 1 200 ? -1.317  71.522  41.092  1.00 22.71  ? 200 PHE A C    1 
ATOM   1478  O O    . PHE A 1 200 ? -1.561  70.517  41.712  1.00 26.08  ? 200 PHE A O    1 
ATOM   1479  C CB   . PHE A 1 200 ? 0.256   72.544  42.778  1.00 21.27  ? 200 PHE A CB   1 
ATOM   1480  C CG   . PHE A 1 200 ? 0.803   73.819  43.326  1.00 21.51  ? 200 PHE A CG   1 
ATOM   1481  C CD1  . PHE A 1 200 ? 1.318   74.783  42.477  1.00 21.00  ? 200 PHE A CD1  1 
ATOM   1482  C CD2  . PHE A 1 200 ? 0.775   74.069  44.674  1.00 26.72  ? 200 PHE A CD2  1 
ATOM   1483  C CE1  . PHE A 1 200 ? 1.812   75.969  42.969  1.00 27.18  ? 200 PHE A CE1  1 
ATOM   1484  C CE2  . PHE A 1 200 ? 1.268   75.254  45.172  1.00 34.47  ? 200 PHE A CE2  1 
ATOM   1485  C CZ   . PHE A 1 200 ? 1.785   76.204  44.322  1.00 31.35  ? 200 PHE A CZ   1 
ATOM   1486  N N    . THR A 1 201 ? -1.494  71.626  39.788  1.00 24.90  ? 201 THR A N    1 
ATOM   1487  C CA   . THR A 1 201 ? -2.029  70.533  39.000  1.00 27.60  ? 201 THR A CA   1 
ATOM   1488  C C    . THR A 1 201 ? -1.384  70.396  37.662  1.00 26.03  ? 201 THR A C    1 
ATOM   1489  O O    . THR A 1 201 ? -1.181  69.295  37.189  1.00 32.01  ? 201 THR A O    1 
ATOM   1490  C CB   . THR A 1 201 ? -3.503  70.798  38.664  1.00 25.77  ? 201 THR A CB   1 
ATOM   1491  O OG1  . THR A 1 201 ? -3.717  72.207  38.538  1.00 30.87  ? 201 THR A OG1  1 
ATOM   1492  C CG2  . THR A 1 201 ? -4.419  70.254  39.733  1.00 28.66  ? 201 THR A CG2  1 
ATOM   1493  N N    . THR A 1 202 ? -1.083  71.509  37.044  1.00 18.51  ? 202 THR A N    1 
ATOM   1494  C CA   . THR A 1 202 ? -0.590  71.450  35.716  1.00 18.81  ? 202 THR A CA   1 
ATOM   1495  C C    . THR A 1 202 ? 0.833   71.133  35.650  1.00 22.75  ? 202 THR A C    1 
ATOM   1496  O O    . THR A 1 202 ? 1.534   71.265  36.621  1.00 24.95  ? 202 THR A O    1 
ATOM   1497  C CB   . THR A 1 202 ? -0.816  72.771  35.008  1.00 24.08  ? 202 THR A CB   1 
ATOM   1498  O OG1  . THR A 1 202 ? 0.116   73.740  35.479  1.00 27.10  ? 202 THR A OG1  1 
ATOM   1499  C CG2  . THR A 1 202 ? -2.217  73.261  35.251  1.00 23.62  ? 202 THR A CG2  1 
ATOM   1500  N N    . THR A 1 203 ? 1.294   70.790  34.467  1.00 21.28  ? 203 THR A N    1 
ATOM   1501  C CA   . THR A 1 203 ? 2.660   70.414  34.264  1.00 18.76  ? 203 THR A CA   1 
ATOM   1502  C C    . THR A 1 203 ? 3.473   71.642  34.174  1.00 18.25  ? 203 THR A C    1 
ATOM   1503  O O    . THR A 1 203 ? 4.648   71.580  33.850  1.00 22.40  ? 203 THR A O    1 
ATOM   1504  C CB   . THR A 1 203 ? 2.808   69.615  32.992  1.00 19.24  ? 203 THR A CB   1 
ATOM   1505  O OG1  . THR A 1 203 ? 2.214   70.330  31.905  1.00 27.53  ? 203 THR A OG1  1 
ATOM   1506  C CG2  . THR A 1 203 ? 2.124   68.278  33.147  1.00 21.81  ? 203 THR A CG2  1 
ATOM   1507  N N    . ALA A 1 204 ? 2.831   72.777  34.340  1.00 15.98  ? 204 ALA A N    1 
ATOM   1508  C CA   . ALA A 1 204 ? 3.543   74.008  34.389  1.00 24.11  ? 204 ALA A CA   1 
ATOM   1509  C C    . ALA A 1 204 ? 3.514   74.578  35.771  1.00 25.62  ? 204 ALA A C    1 
ATOM   1510  O O    . ALA A 1 204 ? 4.286   75.447  36.090  1.00 23.98  ? 204 ALA A O    1 
ATOM   1511  C CB   . ALA A 1 204 ? 2.930   74.961  33.438  1.00 28.64  ? 204 ALA A CB   1 
ATOM   1512  N N    . GLU A 1 205 ? 2.594   74.120  36.591  1.00 21.74  ? 205 GLU A N    1 
ATOM   1513  C CA   . GLU A 1 205 ? 2.572   74.545  37.971  1.00 21.10  ? 205 GLU A CA   1 
ATOM   1514  C C    . GLU A 1 205 ? 3.365   73.521  38.718  1.00 23.07  ? 205 GLU A C    1 
ATOM   1515  O O    . GLU A 1 205 ? 3.799   73.777  39.827  1.00 25.03  ? 205 GLU A O    1 
ATOM   1516  C CB   . GLU A 1 205 ? 1.149   74.654  38.490  1.00 21.37  ? 205 GLU A CB   1 
ATOM   1517  C CG   . GLU A 1 205 ? 0.426   75.936  38.167  1.00 18.91  ? 205 GLU A CG   1 
ATOM   1518  C CD   . GLU A 1 205 ? -1.028  75.860  38.552  1.00 26.59  ? 205 GLU A CD   1 
ATOM   1519  O OE1  . GLU A 1 205 ? -1.551  74.738  38.657  1.00 23.08  ? 205 GLU A OE1  1 
ATOM   1520  O OE2  . GLU A 1 205 ? -1.651  76.919  38.739  1.00 34.83  ? 205 GLU A OE2  1 
ATOM   1521  N N    . ARG A 1 206 ? 3.552   72.350  38.134  1.00 22.10  ? 206 ARG A N    1 
ATOM   1522  C CA   . ARG A 1 206 ? 4.428   71.338  38.704  1.00 23.00  ? 206 ARG A CA   1 
ATOM   1523  C C    . ARG A 1 206 ? 5.876   71.772  38.701  1.00 23.98  ? 206 ARG A C    1 
ATOM   1524  O O    . ARG A 1 206 ? 6.609   71.495  39.626  1.00 28.52  ? 206 ARG A O    1 
ATOM   1525  C CB   . ARG A 1 206 ? 4.284   70.030  37.959  1.00 19.41  ? 206 ARG A CB   1 
ATOM   1526  C CG   . ARG A 1 206 ? 5.272   68.957  38.366  1.00 19.78  ? 206 ARG A CG   1 
ATOM   1527  C CD   . ARG A 1 206 ? 4.820   67.565  37.972  1.00 22.20  ? 206 ARG A CD   1 
ATOM   1528  N NE   . ARG A 1 206 ? 5.935   66.627  38.031  1.00 22.75  ? 206 ARG A NE   1 
ATOM   1529  C CZ   . ARG A 1 206 ? 5.820   65.316  37.876  1.00 22.77  ? 206 ARG A CZ   1 
ATOM   1530  N NH1  . ARG A 1 206 ? 4.632   64.778  37.674  1.00 24.24  ? 206 ARG A NH1  1 
ATOM   1531  N NH2  . ARG A 1 206 ? 6.891   64.545  37.935  1.00 17.99  ? 206 ARG A NH2  1 
ATOM   1532  N N    . GLU A 1 207 ? 6.309   72.447  37.667  1.00 18.43  ? 207 GLU A N    1 
ATOM   1533  C CA   . GLU A 1 207 ? 7.651   72.949  37.641  1.00 20.00  ? 207 GLU A CA   1 
ATOM   1534  C C    . GLU A 1 207 ? 7.937   73.954  38.687  1.00 24.59  ? 207 GLU A C    1 
ATOM   1535  O O    . GLU A 1 207 ? 9.054   74.063  39.129  1.00 30.31  ? 207 GLU A O    1 
ATOM   1536  C CB   . GLU A 1 207 ? 8.001   73.515  36.289  1.00 31.39  ? 207 GLU A CB   1 
ATOM   1537  C CG   . GLU A 1 207 ? 7.269   74.774  35.866  1.00 35.06  ? 207 GLU A CG   1 
ATOM   1538  C CD   . GLU A 1 207 ? 7.369   75.064  34.379  1.00 46.71  ? 207 GLU A CD   1 
ATOM   1539  O OE1  . GLU A 1 207 ? 7.850   74.202  33.618  1.00 45.00  ? 207 GLU A OE1  1 
ATOM   1540  O OE2  . GLU A 1 207 ? 6.952   76.161  33.966  1.00 49.94  ? 207 GLU A OE2  1 
ATOM   1541  N N    . ILE A 1 208 ? 6.971   74.786  39.008  1.00 26.39  ? 208 ILE A N    1 
ATOM   1542  C CA   . ILE A 1 208 ? 7.136   75.763  40.056  1.00 24.49  ? 208 ILE A CA   1 
ATOM   1543  C C    . ILE A 1 208 ? 7.286   75.084  41.371  1.00 19.77  ? 208 ILE A C    1 
ATOM   1544  O O    . ILE A 1 208 ? 8.072   75.519  42.188  1.00 14.83  ? 208 ILE A O    1 
ATOM   1545  C CB   . ILE A 1 208 ? 5.970   76.724  40.098  1.00 28.66  ? 208 ILE A CB   1 
ATOM   1546  C CG1  . ILE A 1 208 ? 5.501   77.059  38.691  1.00 30.81  ? 208 ILE A CG1  1 
ATOM   1547  C CG2  . ILE A 1 208 ? 6.411   78.017  40.743  1.00 30.23  ? 208 ILE A CG2  1 
ATOM   1548  C CD1  . ILE A 1 208 ? 6.425   78.003  37.951  1.00 38.72  ? 208 ILE A CD1  1 
ATOM   1549  N N    . VAL A 1 209 ? 6.541   74.013  41.583  1.00 16.86  ? 209 VAL A N    1 
ATOM   1550  C CA   . VAL A 1 209 ? 6.625   73.245  42.799  1.00 14.48  ? 209 VAL A CA   1 
ATOM   1551  C C    . VAL A 1 209 ? 7.966   72.615  42.866  1.00 15.09  ? 209 VAL A C    1 
ATOM   1552  O O    . VAL A 1 209 ? 8.479   72.399  43.940  1.00 14.35  ? 209 VAL A O    1 
ATOM   1553  C CB   . VAL A 1 209 ? 5.508   72.255  42.817  1.00 17.47  ? 209 VAL A CB   1 
ATOM   1554  C CG1  . VAL A 1 209 ? 5.646   71.287  43.953  1.00 27.10  ? 209 VAL A CG1  1 
ATOM   1555  C CG2  . VAL A 1 209 ? 4.210   72.999  42.943  1.00 20.57  ? 209 VAL A CG2  1 
ATOM   1556  N N    . ARG A 1 210 ? 8.556   72.312  41.733  1.00 11.24  ? 210 ARG A N    1 
ATOM   1557  C CA   . ARG A 1 210 ? 9.920   71.843  41.712  1.00 12.72  ? 210 ARG A CA   1 
ATOM   1558  C C    . ARG A 1 210 ? 10.849  72.949  42.166  1.00 16.31  ? 210 ARG A C    1 
ATOM   1559  O O    . ARG A 1 210 ? 11.830  72.681  42.824  1.00 20.32  ? 210 ARG A O    1 
ATOM   1560  C CB   . ARG A 1 210 ? 10.262  71.322  40.336  1.00 19.45  ? 210 ARG A CB   1 
ATOM   1561  C CG   . ARG A 1 210 ? 11.669  70.782  40.106  1.00 26.93  ? 210 ARG A CG   1 
ATOM   1562  C CD   . ARG A 1 210 ? 11.726  69.259  39.992  1.00 33.71  ? 210 ARG A CD   1 
ATOM   1563  N NE   . ARG A 1 210 ? 10.539  68.656  39.373  1.00 44.25  ? 210 ARG A NE   1 
ATOM   1564  C CZ   . ARG A 1 210 ? 10.371  67.349  39.165  1.00 29.61  ? 210 ARG A CZ   1 
ATOM   1565  N NH1  . ARG A 1 210 ? 11.309  66.482  39.516  1.00 17.30  ? 210 ARG A NH1  1 
ATOM   1566  N NH2  . ARG A 1 210 ? 9.256   66.909  38.605  1.00 18.25  ? 210 ARG A NH2  1 
ATOM   1567  N N    . ASP A 1 211 ? 10.607  74.194  41.771  1.00 16.11  ? 211 ASP A N    1 
ATOM   1568  C CA   . ASP A 1 211 ? 11.399  75.331  42.291  1.00 18.59  ? 211 ASP A CA   1 
ATOM   1569  C C    . ASP A 1 211 ? 11.137  75.663  43.731  1.00 19.19  ? 211 ASP A C    1 
ATOM   1570  O O    . ASP A 1 211 ? 12.047  76.003  44.444  1.00 20.33  ? 211 ASP A O    1 
ATOM   1571  C CB   . ASP A 1 211 ? 11.362  76.556  41.411  1.00 17.94  ? 211 ASP A CB   1 
ATOM   1572  C CG   . ASP A 1 211 ? 12.743  77.046  41.066  1.00 27.34  ? 211 ASP A CG   1 
ATOM   1573  O OD1  . ASP A 1 211 ? 13.710  76.294  41.284  1.00 21.98  ? 211 ASP A OD1  1 
ATOM   1574  O OD2  . ASP A 1 211 ? 12.867  78.181  40.573  1.00 41.52  ? 211 ASP A OD2  1 
ATOM   1575  N N    . ILE A 1 212 ? 9.896   75.580  44.168  1.00 13.36  ? 212 ILE A N    1 
ATOM   1576  C CA   . ILE A 1 212 ? 9.633   75.773  45.563  1.00 12.28  ? 212 ILE A CA   1 
ATOM   1577  C C    . ILE A 1 212 ? 10.337  74.690  46.315  1.00 16.58  ? 212 ILE A C    1 
ATOM   1578  O O    . ILE A 1 212 ? 10.839  74.919  47.384  1.00 17.99  ? 212 ILE A O    1 
ATOM   1579  C CB   . ILE A 1 212 ? 8.162   75.720  45.891  1.00 12.92  ? 212 ILE A CB   1 
ATOM   1580  C CG1  . ILE A 1 212 ? 7.377   76.687  45.023  1.00 16.47  ? 212 ILE A CG1  1 
ATOM   1581  C CG2  . ILE A 1 212 ? 7.934   76.052  47.347  1.00 16.91  ? 212 ILE A CG2  1 
ATOM   1582  C CD1  . ILE A 1 212 ? 5.885   76.612  45.231  1.00 21.01  ? 212 ILE A CD1  1 
ATOM   1583  N N    . LYS A 1 213 ? 10.335  73.481  45.791  1.00 13.90  ? 213 LYS A N    1 
ATOM   1584  C CA   . LYS A 1 213 ? 10.995  72.372  46.453  1.00 16.12  ? 213 LYS A CA   1 
ATOM   1585  C C    . LYS A 1 213 ? 12.485  72.365  46.545  1.00 14.42  ? 213 LYS A C    1 
ATOM   1586  O O    . LYS A 1 213 ? 13.057  72.197  47.589  1.00 15.59  ? 213 LYS A O    1 
ATOM   1587  C CB   . LYS A 1 213 ? 10.573  71.072  45.756  1.00 14.03  ? 213 LYS A CB   1 
ATOM   1588  C CG   . LYS A 1 213 ? 11.030  69.805  46.440  1.00 14.84  ? 213 LYS A CG   1 
ATOM   1589  C CD   . LYS A 1 213 ? 11.017  68.657  45.463  1.00 15.55  ? 213 LYS A CD   1 
ATOM   1590  C CE   . LYS A 1 213 ? 11.941  68.933  44.302  1.00 15.04  ? 213 LYS A CE   1 
ATOM   1591  N NZ   . LYS A 1 213 ? 12.133  67.741  43.448  1.00 13.13  ? 213 LYS A NZ   1 
ATOM   1592  N N    . GLU A 1 214 ? 13.125  72.624  45.452  1.00 11.75  ? 214 GLU A N    1 
ATOM   1593  C CA   . GLU A 1 214 ? 14.544  72.531  45.450  1.00 16.62  ? 214 GLU A CA   1 
ATOM   1594  C C    . GLU A 1 214 ? 15.188  73.847  45.815  1.00 21.96  ? 214 GLU A C    1 
ATOM   1595  O O    . GLU A 1 214 ? 16.387  74.018  45.672  1.00 20.74  ? 214 GLU A O    1 
ATOM   1596  C CB   . GLU A 1 214 ? 15.008  71.991  44.110  1.00 23.85  ? 214 GLU A CB   1 
ATOM   1597  C CG   . GLU A 1 214 ? 15.202  70.486  44.062  1.00 22.95  ? 214 GLU A CG   1 
ATOM   1598  C CD   . GLU A 1 214 ? 16.274  69.978  45.012  1.00 27.22  ? 214 GLU A CD   1 
ATOM   1599  O OE1  . GLU A 1 214 ? 17.218  70.723  45.352  1.00 22.18  ? 214 GLU A OE1  1 
ATOM   1600  O OE2  . GLU A 1 214 ? 16.177  68.806  45.409  1.00 30.57  ? 214 GLU A OE2  1 
ATOM   1601  N N    . LYS A 1 215 ? 14.394  74.784  46.282  1.00 19.70  ? 215 LYS A N    1 
ATOM   1602  C CA   . LYS A 1 215 ? 14.939  76.016  46.775  1.00 18.12  ? 215 LYS A CA   1 
ATOM   1603  C C    . LYS A 1 215 ? 14.509  76.292  48.219  1.00 18.30  ? 215 LYS A C    1 
ATOM   1604  O O    . LYS A 1 215 ? 15.272  76.870  48.976  1.00 17.36  ? 215 LYS A O    1 
ATOM   1605  C CB   . LYS A 1 215 ? 14.488  77.133  45.867  1.00 19.51  ? 215 LYS A CB   1 
ATOM   1606  C CG   . LYS A 1 215 ? 15.336  78.391  45.922  1.00 25.87  ? 215 LYS A CG   1 
ATOM   1607  C CD   . LYS A 1 215 ? 14.598  79.559  45.294  1.00 30.76  ? 215 LYS A CD   1 
ATOM   1608  C CE   . LYS A 1 215 ? 14.191  79.240  43.869  1.00 38.26  ? 215 LYS A CE   1 
ATOM   1609  N NZ   . LYS A 1 215 ? 13.319  80.289  43.276  1.00 36.29  ? 215 LYS A NZ   1 
ATOM   1610  N N    . LEU A 1 216 ? 13.310  75.875  48.612  1.00 16.05  ? 216 LEU A N    1 
ATOM   1611  C CA   . LEU A 1 216 ? 12.831  76.081  49.975  1.00 13.75  ? 216 LEU A CA   1 
ATOM   1612  C C    . LEU A 1 216 ? 12.746  74.888  50.912  1.00 16.96  ? 216 LEU A C    1 
ATOM   1613  O O    . LEU A 1 216 ? 12.645  75.054  52.096  1.00 18.20  ? 216 LEU A O    1 
ATOM   1614  C CB   . LEU A 1 216 ? 11.480  76.755  49.945  1.00 12.58  ? 216 LEU A CB   1 
ATOM   1615  C CG   . LEU A 1 216 ? 11.387  78.266  49.793  1.00 14.77  ? 216 LEU A CG   1 
ATOM   1616  C CD1  . LEU A 1 216 ? 9.966   78.697  50.111  1.00 17.59  ? 216 LEU A CD1  1 
ATOM   1617  C CD2  . LEU A 1 216 ? 12.363  78.930  50.746  1.00 17.73  ? 216 LEU A CD2  1 
ATOM   1618  N N    . CYS A 1 217 ? 12.843  73.682  50.416  1.00 18.04  ? 217 CYS A N    1 
ATOM   1619  C CA   . CYS A 1 217 ? 12.664  72.524  51.237  1.00 13.35  ? 217 CYS A CA   1 
ATOM   1620  C C    . CYS A 1 217 ? 13.976  72.028  51.766  1.00 15.92  ? 217 CYS A C    1 
ATOM   1621  O O    . CYS A 1 217 ? 14.976  72.086  51.059  1.00 15.09  ? 217 CYS A O    1 
ATOM   1622  C CB   . CYS A 1 217 ? 11.930  71.440  50.443  1.00 11.42  ? 217 CYS A CB   1 
ATOM   1623  S SG   . CYS A 1 217 ? 10.208  71.669  49.989  1.00 10.23  ? 217 CYS A SG   1 
ATOM   1624  N N    . TYR A 1 218 ? 13.983  71.516  52.995  1.00 16.15  ? 218 TYR A N    1 
ATOM   1625  C CA   . TYR A 1 218 ? 15.184  71.027  53.654  1.00 14.70  ? 218 TYR A CA   1 
ATOM   1626  C C    . TYR A 1 218 ? 14.832  69.826  54.469  1.00 13.12  ? 218 TYR A C    1 
ATOM   1627  O O    . TYR A 1 218 ? 13.694  69.607  54.770  1.00 10.46  ? 218 TYR A O    1 
ATOM   1628  C CB   . TYR A 1 218 ? 15.730  72.091  54.596  1.00 13.98  ? 218 TYR A CB   1 
ATOM   1629  C CG   . TYR A 1 218 ? 14.904  72.426  55.822  1.00 11.04  ? 218 TYR A CG   1 
ATOM   1630  C CD1  . TYR A 1 218 ? 13.630  72.966  55.716  1.00 9.92   ? 218 TYR A CD1  1 
ATOM   1631  C CD2  . TYR A 1 218 ? 15.423  72.240  57.085  1.00 9.18   ? 218 TYR A CD2  1 
ATOM   1632  C CE1  . TYR A 1 218 ? 12.892  73.263  56.829  1.00 9.72   ? 218 TYR A CE1  1 
ATOM   1633  C CE2  . TYR A 1 218 ? 14.686  72.539  58.201  1.00 12.22  ? 218 TYR A CE2  1 
ATOM   1634  C CZ   . TYR A 1 218 ? 13.426  73.052  58.058  1.00 10.10  ? 218 TYR A CZ   1 
ATOM   1635  O OH   . TYR A 1 218 ? 12.703  73.359  59.166  1.00 8.22   ? 218 TYR A OH   1 
ATOM   1636  N N    . VAL A 1 219 ? 15.803  69.058  54.910  1.00 13.77  ? 219 VAL A N    1 
ATOM   1637  C CA   . VAL A 1 219 ? 15.483  67.961  55.778  1.00 14.44  ? 219 VAL A CA   1 
ATOM   1638  C C    . VAL A 1 219 ? 15.800  68.326  57.189  1.00 11.85  ? 219 VAL A C    1 
ATOM   1639  O O    . VAL A 1 219 ? 16.784  68.958  57.461  1.00 10.41  ? 219 VAL A O    1 
ATOM   1640  C CB   . VAL A 1 219 ? 16.121  66.633  55.368  1.00 15.30  ? 219 VAL A CB   1 
ATOM   1641  C CG1  . VAL A 1 219 ? 15.450  65.457  56.044  1.00 12.29  ? 219 VAL A CG1  1 
ATOM   1642  C CG2  . VAL A 1 219 ? 16.034  66.430  53.884  1.00 14.76  ? 219 VAL A CG2  1 
ATOM   1643  N N    . ALA A 1 220 ? 14.952  67.918  58.099  1.00 12.73  ? 220 ALA A N    1 
ATOM   1644  C CA   . ALA A 1 220 ? 15.089  68.193  59.483  1.00 12.02  ? 220 ALA A CA   1 
ATOM   1645  C C    . ALA A 1 220 ? 15.821  67.110  60.151  1.00 12.62  ? 220 ALA A C    1 
ATOM   1646  O O    . ALA A 1 220 ? 15.940  66.061  59.620  1.00 14.43  ? 220 ALA A O    1 
ATOM   1647  C CB   . ALA A 1 220 ? 13.694  68.194  60.000  1.00 12.00  ? 220 ALA A CB   1 
ATOM   1648  N N    . LEU A 1 221 ? 16.300  67.347  61.345  1.00 10.94  ? 221 LEU A N    1 
ATOM   1649  C CA   . LEU A 1 221 ? 17.047  66.358  62.057  1.00 9.95   ? 221 LEU A CA   1 
ATOM   1650  C C    . LEU A 1 221 ? 16.029  65.636  62.846  1.00 11.46  ? 221 LEU A C    1 
ATOM   1651  O O    . LEU A 1 221 ? 16.240  64.490  63.190  1.00 10.72  ? 221 LEU A O    1 
ATOM   1652  C CB   . LEU A 1 221 ? 18.127  66.990  62.916  1.00 7.16   ? 221 LEU A CB   1 
ATOM   1653  C CG   . LEU A 1 221 ? 19.319  66.205  63.416  1.00 8.63   ? 221 LEU A CG   1 
ATOM   1654  C CD1  . LEU A 1 221 ? 20.075  65.641  62.247  1.00 11.77  ? 221 LEU A CD1  1 
ATOM   1655  C CD2  . LEU A 1 221 ? 20.212  67.124  64.215  1.00 8.41   ? 221 LEU A CD2  1 
ATOM   1656  N N    . ASP A 1 222 ? 14.899  66.277  63.119  1.00 11.01  ? 222 ASP A N    1 
ATOM   1657  C CA   . ASP A 1 222 ? 13.806  65.586  63.787  1.00 13.08  ? 222 ASP A CA   1 
ATOM   1658  C C    . ASP A 1 222 ? 12.487  66.078  63.306  1.00 15.85  ? 222 ASP A C    1 
ATOM   1659  O O    . ASP A 1 222 ? 12.183  67.237  63.495  1.00 17.25  ? 222 ASP A O    1 
ATOM   1660  C CB   . ASP A 1 222 ? 13.908  65.686  65.278  1.00 19.26  ? 222 ASP A CB   1 
ATOM   1661  C CG   . ASP A 1 222 ? 13.530  64.392  66.001  1.00 24.70  ? 222 ASP A CG   1 
ATOM   1662  O OD1  . ASP A 1 222 ? 12.349  64.222  66.356  1.00 25.63  ? 222 ASP A OD1  1 
ATOM   1663  O OD2  . ASP A 1 222 ? 14.418  63.559  66.253  1.00 18.74  ? 222 ASP A OD2  1 
ATOM   1664  N N    . PHE A 1 223 ? 11.694  65.197  62.690  1.00 12.08  ? 223 PHE A N    1 
ATOM   1665  C CA   . PHE A 1 223 ? 10.448  65.596  62.078  1.00 11.64  ? 223 PHE A CA   1 
ATOM   1666  C C    . PHE A 1 223 ? 9.501   66.158  63.015  1.00 17.78  ? 223 PHE A C    1 
ATOM   1667  O O    . PHE A 1 223 ? 9.008   67.239  62.802  1.00 20.52  ? 223 PHE A O    1 
ATOM   1668  C CB   . PHE A 1 223 ? 9.785   64.414  61.452  1.00 8.19   ? 223 PHE A CB   1 
ATOM   1669  C CG   . PHE A 1 223 ? 8.631   64.748  60.570  1.00 8.33   ? 223 PHE A CG   1 
ATOM   1670  C CD1  . PHE A 1 223 ? 8.767   65.643  59.542  1.00 11.61  ? 223 PHE A CD1  1 
ATOM   1671  C CD2  . PHE A 1 223 ? 7.414   64.147  60.760  1.00 8.18   ? 223 PHE A CD2  1 
ATOM   1672  C CE1  . PHE A 1 223 ? 7.713   65.937  58.715  1.00 11.08  ? 223 PHE A CE1  1 
ATOM   1673  C CE2  . PHE A 1 223 ? 6.350   64.444  59.947  1.00 9.16   ? 223 PHE A CE2  1 
ATOM   1674  C CZ   . PHE A 1 223 ? 6.502   65.340  58.919  1.00 9.62   ? 223 PHE A CZ   1 
ATOM   1675  N N    . GLU A 1 224 ? 9.224   65.435  64.079  1.00 18.15  ? 224 GLU A N    1 
ATOM   1676  C CA   . GLU A 1 224 ? 8.200   65.855  65.000  1.00 21.11  ? 224 GLU A CA   1 
ATOM   1677  C C    . GLU A 1 224 ? 8.544   67.072  65.795  1.00 20.52  ? 224 GLU A C    1 
ATOM   1678  O O    . GLU A 1 224 ? 7.675   67.790  66.248  1.00 19.34  ? 224 GLU A O    1 
ATOM   1679  C CB   . GLU A 1 224 ? 7.892   64.715  65.942  1.00 21.11  ? 224 GLU A CB   1 
ATOM   1680  C CG   . GLU A 1 224 ? 6.785   64.990  66.934  1.00 23.17  ? 224 GLU A CG   1 
ATOM   1681  C CD   . GLU A 1 224 ? 6.507   63.790  67.801  1.00 22.69  ? 224 GLU A CD   1 
ATOM   1682  O OE1  . GLU A 1 224 ? 7.201   62.776  67.647  1.00 28.80  ? 224 GLU A OE1  1 
ATOM   1683  O OE2  . GLU A 1 224 ? 5.594   63.853  68.634  1.00 30.48  ? 224 GLU A OE2  1 
ATOM   1684  N N    . GLN A 1 225 ? 9.828   67.317  65.953  1.00 19.02  ? 225 GLN A N    1 
ATOM   1685  C CA   . GLN A 1 225 ? 10.284  68.435  66.739  1.00 19.84  ? 225 GLN A CA   1 
ATOM   1686  C C    . GLN A 1 225 ? 10.453  69.643  65.962  1.00 21.05  ? 225 GLN A C    1 
ATOM   1687  O O    . GLN A 1 225 ? 11.265  70.454  66.320  1.00 28.36  ? 225 GLN A O    1 
ATOM   1688  C CB   . GLN A 1 225 ? 11.654  68.238  67.328  1.00 19.39  ? 225 GLN A CB   1 
ATOM   1689  C CG   . GLN A 1 225 ? 11.848  67.153  68.351  1.00 21.22  ? 225 GLN A CG   1 
ATOM   1690  C CD   . GLN A 1 225 ? 13.298  67.093  68.763  1.00 16.03  ? 225 GLN A CD   1 
ATOM   1691  O OE1  . GLN A 1 225 ? 14.121  67.849  68.256  1.00 5.54   ? 225 GLN A OE1  1 
ATOM   1692  N NE2  . GLN A 1 225 ? 13.620  66.206  69.681  1.00 29.68  ? 225 GLN A NE2  1 
ATOM   1693  N N    . GLU A 1 226 ? 9.752   69.766  64.858  1.00 21.70  ? 226 GLU A N    1 
ATOM   1694  C CA   . GLU A 1 226 ? 9.714   70.943  64.058  1.00 28.63  ? 226 GLU A CA   1 
ATOM   1695  C C    . GLU A 1 226 ? 8.319   71.168  63.589  1.00 28.58  ? 226 GLU A C    1 
ATOM   1696  O O    . GLU A 1 226 ? 7.817   72.256  63.451  1.00 42.23  ? 226 GLU A O    1 
ATOM   1697  C CB   . GLU A 1 226 ? 10.723  70.968  62.946  1.00 24.34  ? 226 GLU A CB   1 
ATOM   1698  C CG   . GLU A 1 226 ? 12.165  71.017  63.407  1.00 34.83  ? 226 GLU A CG   1 
ATOM   1699  C CD   . GLU A 1 226 ? 13.136  70.967  62.261  1.00 27.70  ? 226 GLU A CD   1 
ATOM   1700  O OE1  . GLU A 1 226 ? 12.692  70.708  61.134  1.00 41.46  ? 226 GLU A OE1  1 
ATOM   1701  O OE2  . GLU A 1 226 ? 14.339  71.193  62.484  1.00 27.12  ? 226 GLU A OE2  1 
ATOM   1702  N N    . MET A 1 227 ? 7.661   70.050  63.373  1.00 24.95  ? 227 MET A N    1 
ATOM   1703  C CA   . MET A 1 227 ? 6.249   70.088  63.064  1.00 26.42  ? 227 MET A CA   1 
ATOM   1704  C C    . MET A 1 227 ? 5.698   70.835  64.221  1.00 25.93  ? 227 MET A C    1 
ATOM   1705  O O    . MET A 1 227 ? 4.738   71.557  64.088  1.00 22.07  ? 227 MET A O    1 
ATOM   1706  C CB   . MET A 1 227 ? 5.565   68.760  62.845  1.00 19.95  ? 227 MET A CB   1 
ATOM   1707  C CG   . MET A 1 227 ? 6.080   67.979  61.674  1.00 14.79  ? 227 MET A CG   1 
ATOM   1708  S SD   . MET A 1 227 ? 5.304   68.633  60.215  1.00 17.25  ? 227 MET A SD   1 
ATOM   1709  C CE   . MET A 1 227 ? 3.754   67.755  60.291  1.00 14.60  ? 227 MET A CE   1 
ATOM   1710  N N    . ALA A 1 228 ? 6.353   70.716  65.355  1.00 27.21  ? 228 ALA A N    1 
ATOM   1711  C CA   . ALA A 1 228 ? 5.954   71.443  66.562  1.00 27.43  ? 228 ALA A CA   1 
ATOM   1712  C C    . ALA A 1 228 ? 6.490   72.839  66.502  1.00 31.41  ? 228 ALA A C    1 
ATOM   1713  O O    . ALA A 1 228 ? 5.806   73.774  66.866  1.00 31.94  ? 228 ALA A O    1 
ATOM   1714  C CB   . ALA A 1 228 ? 6.536   70.771  67.785  1.00 26.02  ? 228 ALA A CB   1 
ATOM   1715  N N    . THR A 1 229 ? 7.712   72.987  66.018  1.00 23.84  ? 229 THR A N    1 
ATOM   1716  C CA   . THR A 1 229 ? 8.280   74.288  65.900  1.00 22.32  ? 229 THR A CA   1 
ATOM   1717  C C    . THR A 1 229 ? 7.388   75.041  64.970  1.00 21.34  ? 229 THR A C    1 
ATOM   1718  O O    . THR A 1 229 ? 7.198   76.210  65.120  1.00 28.59  ? 229 THR A O    1 
ATOM   1719  C CB   . THR A 1 229 ? 9.733   74.227  65.431  1.00 19.77  ? 229 THR A CB   1 
ATOM   1720  O OG1  . THR A 1 229 ? 10.520  73.550  66.412  1.00 22.91  ? 229 THR A OG1  1 
ATOM   1721  C CG2  . THR A 1 229 ? 10.303  75.610  65.230  1.00 22.01  ? 229 THR A CG2  1 
ATOM   1722  N N    . ALA A 1 230 ? 6.880   74.397  63.969  1.00 23.04  ? 230 ALA A N    1 
ATOM   1723  C CA   . ALA A 1 230 ? 5.957   75.007  63.053  1.00 29.28  ? 230 ALA A CA   1 
ATOM   1724  C C    . ALA A 1 230 ? 4.557   75.370  63.526  1.00 31.41  ? 230 ALA A C    1 
ATOM   1725  O O    . ALA A 1 230 ? 3.995   76.356  63.076  1.00 37.12  ? 230 ALA A O    1 
ATOM   1726  C CB   . ALA A 1 230 ? 5.892   74.173  61.794  1.00 22.86  ? 230 ALA A CB   1 
ATOM   1727  N N    . ALA A 1 231 ? 3.946   74.566  64.372  1.00 28.96  ? 231 ALA A N    1 
ATOM   1728  C CA   . ALA A 1 231 ? 2.553   74.807  64.754  1.00 31.51  ? 231 ALA A CA   1 
ATOM   1729  C C    . ALA A 1 231 ? 2.380   75.633  65.965  1.00 37.16  ? 231 ALA A C    1 
ATOM   1730  O O    . ALA A 1 231 ? 1.268   75.816  66.418  1.00 34.24  ? 231 ALA A O    1 
ATOM   1731  C CB   . ALA A 1 231 ? 1.818   73.507  64.913  1.00 23.38  ? 231 ALA A CB   1 
ATOM   1732  N N    . SER A 1 232 ? 3.474   76.064  66.548  1.00 38.40  ? 232 SER A N    1 
ATOM   1733  C CA   . SER A 1 232 ? 3.423   76.948  67.663  1.00 27.39  ? 232 SER A CA   1 
ATOM   1734  C C    . SER A 1 232 ? 4.106   78.220  67.263  1.00 30.30  ? 232 SER A C    1 
ATOM   1735  O O    . SER A 1 232 ? 3.837   79.256  67.844  1.00 36.81  ? 232 SER A O    1 
ATOM   1736  C CB   . SER A 1 232 ? 4.222   76.329  68.777  1.00 34.13  ? 232 SER A CB   1 
ATOM   1737  O OG   . SER A 1 232 ? 4.268   74.919  68.677  1.00 31.83  ? 232 SER A OG   1 
ATOM   1738  N N    . SER A 1 233 ? 5.024   78.150  66.304  1.00 33.98  ? 233 SER A N    1 
ATOM   1739  C CA   . SER A 1 233 ? 5.799   79.312  65.879  1.00 34.56  ? 233 SER A CA   1 
ATOM   1740  C C    . SER A 1 233 ? 6.027   79.409  64.399  1.00 35.98  ? 233 SER A C    1 
ATOM   1741  O O    . SER A 1 233 ? 6.464   78.468  63.784  1.00 42.70  ? 233 SER A O    1 
ATOM   1742  C CB   . SER A 1 233 ? 7.136   79.335  66.563  1.00 37.10  ? 233 SER A CB   1 
ATOM   1743  O OG   . SER A 1 233 ? 7.700   80.623  66.471  1.00 52.29  ? 233 SER A OG   1 
ATOM   1744  N N    . SER A 1 234 ? 5.795   80.574  63.822  1.00 44.38  ? 234 SER A N    1 
ATOM   1745  C CA   . SER A 1 234 ? 5.929   80.767  62.388  1.00 44.28  ? 234 SER A CA   1 
ATOM   1746  C C    . SER A 1 234 ? 7.350   81.081  62.063  1.00 40.98  ? 234 SER A C    1 
ATOM   1747  O O    . SER A 1 234 ? 7.648   82.069  61.416  1.00 47.64  ? 234 SER A O    1 
ATOM   1748  C CB   . SER A 1 234 ? 5.066   81.962  62.001  1.00 41.95  ? 234 SER A CB   1 
ATOM   1749  O OG   . SER A 1 234 ? 5.250   83.028  62.910  1.00 37.47  ? 234 SER A OG   1 
ATOM   1750  N N    . SER A 1 235 ? 8.241   80.279  62.577  1.00 33.97  ? 235 SER A N    1 
ATOM   1751  C CA   . SER A 1 235 ? 9.611   80.562  62.378  1.00 34.29  ? 235 SER A CA   1 
ATOM   1752  C C    . SER A 1 235 ? 10.068  79.773  61.191  1.00 35.97  ? 235 SER A C    1 
ATOM   1753  O O    . SER A 1 235 ? 11.254  79.543  61.018  1.00 42.81  ? 235 SER A O    1 
ATOM   1754  C CB   . SER A 1 235 ? 10.344  80.180  63.644  1.00 37.00  ? 235 SER A CB   1 
ATOM   1755  O OG   . SER A 1 235 ? 9.861   80.944  64.730  1.00 29.35  ? 235 SER A OG   1 
ATOM   1756  N N    . LEU A 1 236 ? 9.160   79.389  60.317  1.00 31.16  ? 236 LEU A N    1 
ATOM   1757  C CA   . LEU A 1 236 ? 9.572   78.575  59.198  1.00 27.38  ? 236 LEU A CA   1 
ATOM   1758  C C    . LEU A 1 236 ? 8.860   79.020  57.979  1.00 21.30  ? 236 LEU A C    1 
ATOM   1759  O O    . LEU A 1 236 ? 9.248   78.721  56.878  1.00 21.52  ? 236 LEU A O    1 
ATOM   1760  C CB   . LEU A 1 236 ? 9.276   77.107  59.453  1.00 28.43  ? 236 LEU A CB   1 
ATOM   1761  C CG   . LEU A 1 236 ? 9.888   76.294  60.590  1.00 27.47  ? 236 LEU A CG   1 
ATOM   1762  C CD1  . LEU A 1 236 ? 9.141   76.506  61.885  1.00 23.22  ? 236 LEU A CD1  1 
ATOM   1763  C CD2  . LEU A 1 236 ? 9.830   74.832  60.224  1.00 25.27  ? 236 LEU A CD2  1 
ATOM   1764  N N    . GLU A 1 237 ? 7.817   79.772  58.169  1.00 21.12  ? 237 GLU A N    1 
ATOM   1765  C CA   . GLU A 1 237 ? 7.054   80.112  57.030  1.00 21.36  ? 237 GLU A CA   1 
ATOM   1766  C C    . GLU A 1 237 ? 7.592   81.218  56.222  1.00 25.90  ? 237 GLU A C    1 
ATOM   1767  O O    . GLU A 1 237 ? 7.340   82.366  56.516  1.00 35.05  ? 237 GLU A O    1 
ATOM   1768  C CB   . GLU A 1 237 ? 5.639   80.442  57.463  1.00 20.61  ? 237 GLU A CB   1 
ATOM   1769  C CG   . GLU A 1 237 ? 4.866   79.303  58.079  1.00 21.65  ? 237 GLU A CG   1 
ATOM   1770  C CD   . GLU A 1 237 ? 3.378   79.545  58.035  1.00 27.10  ? 237 GLU A CD   1 
ATOM   1771  O OE1  . GLU A 1 237 ? 2.732   79.101  57.071  1.00 33.90  ? 237 GLU A OE1  1 
ATOM   1772  O OE2  . GLU A 1 237 ? 2.855   80.191  58.959  1.00 46.09  ? 237 GLU A OE2  1 
ATOM   1773  N N    . LYS A 1 238 ? 8.307   80.876  55.169  1.00 27.04  ? 238 LYS A N    1 
ATOM   1774  C CA   . LYS A 1 238 ? 8.833   81.853  54.255  1.00 26.42  ? 238 LYS A CA   1 
ATOM   1775  C C    . LYS A 1 238 ? 7.808   82.006  53.184  1.00 25.39  ? 238 LYS A C    1 
ATOM   1776  O O    . LYS A 1 238 ? 6.708   81.522  53.322  1.00 26.55  ? 238 LYS A O    1 
ATOM   1777  C CB   . LYS A 1 238 ? 10.168  81.390  53.691  1.00 19.56  ? 238 LYS A CB   1 
ATOM   1778  C CG   . LYS A 1 238 ? 11.167  81.051  54.775  1.00 18.51  ? 238 LYS A CG   1 
ATOM   1779  C CD   . LYS A 1 238 ? 12.563  80.890  54.222  1.00 21.39  ? 238 LYS A CD   1 
ATOM   1780  C CE   . LYS A 1 238 ? 13.570  80.805  55.349  1.00 13.87  ? 238 LYS A CE   1 
ATOM   1781  N NZ   . LYS A 1 238 ? 14.948  80.634  54.822  1.00 23.60  ? 238 LYS A NZ   1 
ATOM   1782  N N    . SER A 1 239 ? 8.149   82.703  52.118  1.00 25.82  ? 239 SER A N    1 
ATOM   1783  C CA   . SER A 1 239 ? 7.225   82.910  51.033  1.00 22.97  ? 239 SER A CA   1 
ATOM   1784  C C    . SER A 1 239 ? 7.816   82.663  49.682  1.00 22.53  ? 239 SER A C    1 
ATOM   1785  O O    . SER A 1 239 ? 9.024   82.570  49.533  1.00 23.92  ? 239 SER A O    1 
ATOM   1786  C CB   . SER A 1 239 ? 6.744   84.332  51.073  1.00 29.59  ? 239 SER A CB   1 
ATOM   1787  O OG   . SER A 1 239 ? 6.142   84.643  52.316  1.00 37.67  ? 239 SER A OG   1 
ATOM   1788  N N    . TYR A 1 240 ? 6.964   82.580  48.684  1.00 22.06  ? 240 TYR A N    1 
ATOM   1789  C CA   . TYR A 1 240 ? 7.414   82.335  47.331  1.00 29.60  ? 240 TYR A CA   1 
ATOM   1790  C C    . TYR A 1 240 ? 6.615   83.057  46.279  1.00 34.12  ? 240 TYR A C    1 
ATOM   1791  O O    . TYR A 1 240 ? 5.429   82.851  46.157  1.00 35.94  ? 240 TYR A O    1 
ATOM   1792  C CB   . TYR A 1 240 ? 7.449   80.830  47.010  1.00 27.23  ? 240 TYR A CB   1 
ATOM   1793  C CG   . TYR A 1 240 ? 8.098   80.472  45.700  1.00 21.52  ? 240 TYR A CG   1 
ATOM   1794  C CD1  . TYR A 1 240 ? 9.467   80.341  45.598  1.00 19.40  ? 240 TYR A CD1  1 
ATOM   1795  C CD2  . TYR A 1 240 ? 7.338   80.257  44.570  1.00 19.69  ? 240 TYR A CD2  1 
ATOM   1796  C CE1  . TYR A 1 240 ? 10.062  80.025  44.399  1.00 19.38  ? 240 TYR A CE1  1 
ATOM   1797  C CE2  . TYR A 1 240 ? 7.924   79.943  43.371  1.00 20.60  ? 240 TYR A CE2  1 
ATOM   1798  C CZ   . TYR A 1 240 ? 9.285   79.828  43.290  1.00 23.75  ? 240 TYR A CZ   1 
ATOM   1799  O OH   . TYR A 1 240 ? 9.862   79.510  42.088  1.00 20.17  ? 240 TYR A OH   1 
ATOM   1800  N N    . GLU A 1 241 ? 7.297   83.850  45.470  1.00 31.52  ? 241 GLU A N    1 
ATOM   1801  C CA   . GLU A 1 241 ? 6.649   84.603  44.426  1.00 35.99  ? 241 GLU A CA   1 
ATOM   1802  C C    . GLU A 1 241 ? 6.385   83.778  43.243  1.00 36.48  ? 241 GLU A C    1 
ATOM   1803  O O    . GLU A 1 241 ? 7.287   83.456  42.491  1.00 33.32  ? 241 GLU A O    1 
ATOM   1804  C CB   . GLU A 1 241 ? 7.560   85.739  43.978  1.00 46.21  ? 241 GLU A CB   1 
ATOM   1805  C CG   . GLU A 1 241 ? 6.931   87.118  43.922  1.00 42.55  ? 241 GLU A CG   1 
ATOM   1806  C CD   . GLU A 1 241 ? 6.031   87.320  42.721  1.00 57.22  ? 241 GLU A CD   1 
ATOM   1807  O OE1  . GLU A 1 241 ? 6.517   87.169  41.588  1.00 64.40  ? 241 GLU A OE1  1 
ATOM   1808  O OE2  . GLU A 1 241 ? 4.840   87.639  42.906  1.00 51.92  ? 241 GLU A OE2  1 
ATOM   1809  N N    . LEU A 1 242 ? 5.144   83.422  43.069  1.00 36.56  ? 242 LEU A N    1 
ATOM   1810  C CA   . LEU A 1 242 ? 4.803   82.697  41.901  1.00 42.90  ? 242 LEU A CA   1 
ATOM   1811  C C    . LEU A 1 242 ? 4.944   83.774  40.905  1.00 49.75  ? 242 LEU A C    1 
ATOM   1812  O O    . LEU A 1 242 ? 4.544   84.888  41.167  1.00 52.15  ? 242 LEU A O    1 
ATOM   1813  C CB   . LEU A 1 242 ? 3.359   82.226  41.950  1.00 46.63  ? 242 LEU A CB   1 
ATOM   1814  C CG   . LEU A 1 242 ? 3.066   80.935  42.709  1.00 52.71  ? 242 LEU A CG   1 
ATOM   1815  C CD1  . LEU A 1 242 ? 1.727   80.342  42.315  1.00 56.70  ? 242 LEU A CD1  1 
ATOM   1816  C CD2  . LEU A 1 242 ? 4.167   79.929  42.486  1.00 46.63  ? 242 LEU A CD2  1 
ATOM   1817  N N    . PRO A 1 243 ? 5.519   83.481  39.690  1.00 51.48  ? 243 PRO A N    1 
ATOM   1818  C CA   . PRO A 1 243 ? 5.620   84.631  38.781  1.00 45.37  ? 243 PRO A CA   1 
ATOM   1819  C C    . PRO A 1 243 ? 4.419   85.342  38.180  1.00 42.05  ? 243 PRO A C    1 
ATOM   1820  O O    . PRO A 1 243 ? 4.590   86.279  37.417  1.00 44.63  ? 243 PRO A O    1 
ATOM   1821  C CB   . PRO A 1 243 ? 6.361   84.044  37.605  1.00 41.78  ? 243 PRO A CB   1 
ATOM   1822  C CG   . PRO A 1 243 ? 5.975   82.618  37.586  1.00 35.32  ? 243 PRO A CG   1 
ATOM   1823  C CD   . PRO A 1 243 ? 6.091   82.279  39.026  1.00 42.86  ? 243 PRO A CD   1 
ATOM   1824  N N    . ASP A 1 244 ? 3.236   84.923  38.649  1.00 39.47  ? 244 ASP A N    1 
ATOM   1825  C CA   . ASP A 1 244 ? 1.953   85.441  38.202  1.00 47.19  ? 244 ASP A CA   1 
ATOM   1826  C C    . ASP A 1 244 ? 1.311   86.158  39.380  1.00 44.23  ? 244 ASP A C    1 
ATOM   1827  O O    . ASP A 1 244 ? 0.119   86.033  39.614  1.00 44.54  ? 244 ASP A O    1 
ATOM   1828  C CB   . ASP A 1 244 ? 1.130   84.204  37.887  1.00 51.76  ? 244 ASP A CB   1 
ATOM   1829  C CG   . ASP A 1 244 ? -0.059  84.496  36.990  1.00 54.12  ? 244 ASP A CG   1 
ATOM   1830  O OD1  . ASP A 1 244 ? 0.041   85.399  36.128  1.00 61.41  ? 244 ASP A OD1  1 
ATOM   1831  O OD2  . ASP A 1 244 ? -1.094  83.812  37.144  1.00 56.06  ? 244 ASP A OD2  1 
ATOM   1832  N N    . GLY A 1 245 ? 2.080   86.905  40.124  1.00 38.45  ? 245 GLY A N    1 
ATOM   1833  C CA   . GLY A 1 245 ? 1.669   87.619  41.304  1.00 44.88  ? 245 GLY A CA   1 
ATOM   1834  C C    . GLY A 1 245 ? 1.119   86.962  42.532  1.00 47.81  ? 245 GLY A C    1 
ATOM   1835  O O    . GLY A 1 245 ? 0.095   87.375  43.053  1.00 47.66  ? 245 GLY A O    1 
ATOM   1836  N N    . GLN A 1 246 ? 1.784   85.925  42.997  1.00 50.32  ? 246 GLN A N    1 
ATOM   1837  C CA   . GLN A 1 246 ? 1.304   85.211  44.145  1.00 48.03  ? 246 GLN A CA   1 
ATOM   1838  C C    . GLN A 1 246 ? 2.374   84.782  45.077  1.00 51.83  ? 246 GLN A C    1 
ATOM   1839  O O    . GLN A 1 246 ? 2.816   83.654  44.994  1.00 51.80  ? 246 GLN A O    1 
ATOM   1840  C CB   . GLN A 1 246 ? 0.564   83.978  43.723  1.00 49.14  ? 246 GLN A CB   1 
ATOM   1841  C CG   . GLN A 1 246 ? -0.928  84.015  43.991  1.00 49.78  ? 246 GLN A CG   1 
ATOM   1842  C CD   . GLN A 1 246 ? -1.708  83.069  43.103  1.00 48.74  ? 246 GLN A CD   1 
ATOM   1843  O OE1  . GLN A 1 246 ? -2.221  83.462  42.057  1.00 37.60  ? 246 GLN A OE1  1 
ATOM   1844  N NE2  . GLN A 1 246 ? -1.809  81.814  43.522  1.00 42.90  ? 246 GLN A NE2  1 
ATOM   1845  N N    . VAL A 1 247 ? 2.825   85.680  45.957  1.00 53.47  ? 247 VAL A N    1 
ATOM   1846  C CA   . VAL A 1 247 ? 3.770   85.306  46.992  1.00 48.94  ? 247 VAL A CA   1 
ATOM   1847  C C    . VAL A 1 247 ? 3.036   84.413  47.997  1.00 46.10  ? 247 VAL A C    1 
ATOM   1848  O O    . VAL A 1 247 ? 2.295   84.905  48.847  1.00 44.14  ? 247 VAL A O    1 
ATOM   1849  C CB   . VAL A 1 247 ? 4.354   86.538  47.629  1.00 48.46  ? 247 VAL A CB   1 
ATOM   1850  C CG1  . VAL A 1 247 ? 5.788   86.307  48.065  1.00 44.28  ? 247 VAL A CG1  1 
ATOM   1851  C CG2  . VAL A 1 247 ? 4.287   87.679  46.641  1.00 63.45  ? 247 VAL A CG2  1 
ATOM   1852  N N    . ILE A 1 248 ? 3.241   83.096  47.912  1.00 38.58  ? 248 ILE A N    1 
ATOM   1853  C CA   . ILE A 1 248 ? 2.500   82.168  48.742  1.00 32.81  ? 248 ILE A CA   1 
ATOM   1854  C C    . ILE A 1 248 ? 3.245   81.650  49.938  1.00 32.24  ? 248 ILE A C    1 
ATOM   1855  O O    . ILE A 1 248 ? 4.439   81.803  50.030  1.00 28.93  ? 248 ILE A O    1 
ATOM   1856  C CB   . ILE A 1 248 ? 2.001   81.039  47.866  1.00 35.50  ? 248 ILE A CB   1 
ATOM   1857  C CG1  . ILE A 1 248 ? 3.116   80.539  46.956  1.00 41.27  ? 248 ILE A CG1  1 
ATOM   1858  C CG2  . ILE A 1 248 ? 0.850   81.518  47.005  1.00 39.49  ? 248 ILE A CG2  1 
ATOM   1859  C CD1  . ILE A 1 248 ? 2.899   79.131  46.456  1.00 40.45  ? 248 ILE A CD1  1 
ATOM   1860  N N    . THR A 1 249 ? 2.542   81.005  50.857  1.00 31.52  ? 249 THR A N    1 
ATOM   1861  C CA   . THR A 1 249 ? 3.163   80.582  52.109  1.00 33.92  ? 249 THR A CA   1 
ATOM   1862  C C    . THR A 1 249 ? 3.517   79.121  52.217  1.00 33.16  ? 249 THR A C    1 
ATOM   1863  O O    . THR A 1 249 ? 2.674   78.257  52.013  1.00 28.00  ? 249 THR A O    1 
ATOM   1864  C CB   . THR A 1 249 ? 2.283   80.945  53.321  1.00 33.12  ? 249 THR A CB   1 
ATOM   1865  O OG1  . THR A 1 249 ? 1.257   79.962  53.496  1.00 38.69  ? 249 THR A OG1  1 
ATOM   1866  C CG2  . THR A 1 249 ? 1.642   82.303  53.142  1.00 33.74  ? 249 THR A CG2  1 
ATOM   1867  N N    . ILE A 1 250 ? 4.778   78.841  52.562  1.00 26.73  ? 250 ILE A N    1 
ATOM   1868  C CA   . ILE A 1 250 ? 5.257   77.476  52.680  1.00 24.84  ? 250 ILE A CA   1 
ATOM   1869  C C    . ILE A 1 250 ? 5.975   77.344  53.985  1.00 17.76  ? 250 ILE A C    1 
ATOM   1870  O O    . ILE A 1 250 ? 6.966   77.992  54.188  1.00 16.28  ? 250 ILE A O    1 
ATOM   1871  C CB   . ILE A 1 250 ? 6.205   77.080  51.542  1.00 18.78  ? 250 ILE A CB   1 
ATOM   1872  C CG1  . ILE A 1 250 ? 5.494   77.064  50.193  1.00 20.78  ? 250 ILE A CG1  1 
ATOM   1873  C CG2  . ILE A 1 250 ? 6.798   75.704  51.781  1.00 22.83  ? 250 ILE A CG2  1 
ATOM   1874  C CD1  . ILE A 1 250 ? 5.744   78.306  49.370  1.00 29.24  ? 250 ILE A CD1  1 
ATOM   1875  N N    . GLY A 1 251 ? 5.467   76.508  54.875  1.00 16.05  ? 251 GLY A N    1 
ATOM   1876  C CA   . GLY A 1 251 ? 6.065   76.349  56.163  1.00 16.65  ? 251 GLY A CA   1 
ATOM   1877  C C    . GLY A 1 251 ? 6.438   74.961  56.520  1.00 18.91  ? 251 GLY A C    1 
ATOM   1878  O O    . GLY A 1 251 ? 7.577   74.598  56.480  1.00 23.23  ? 251 GLY A O    1 
ATOM   1879  N N    . ASN A 1 252 ? 5.462   74.173  56.908  1.00 15.23  ? 252 ASN A N    1 
ATOM   1880  C CA   . ASN A 1 252 ? 5.698   72.824  57.310  1.00 11.34  ? 252 ASN A CA   1 
ATOM   1881  C C    . ASN A 1 252 ? 5.832   72.104  56.077  1.00 16.39  ? 252 ASN A C    1 
ATOM   1882  O O    . ASN A 1 252 ? 6.421   71.074  56.054  1.00 18.48  ? 252 ASN A O    1 
ATOM   1883  C CB   . ASN A 1 252 ? 4.529   72.262  58.088  1.00 12.11  ? 252 ASN A CB   1 
ATOM   1884  C CG   . ASN A 1 252 ? 3.249   72.158  57.290  1.00 22.55  ? 252 ASN A CG   1 
ATOM   1885  O OD1  . ASN A 1 252 ? 3.280   71.901  56.095  1.00 30.00  ? 252 ASN A OD1  1 
ATOM   1886  N ND2  . ASN A 1 252 ? 2.113   72.282  57.963  1.00 18.98  ? 252 ASN A ND2  1 
ATOM   1887  N N    . GLU A 1 253 ? 5.387   72.693  54.996  1.00 12.53  ? 253 GLU A N    1 
ATOM   1888  C CA   . GLU A 1 253 ? 5.353   72.011  53.745  1.00 11.72  ? 253 GLU A CA   1 
ATOM   1889  C C    . GLU A 1 253 ? 6.694   71.929  53.258  1.00 12.80  ? 253 GLU A C    1 
ATOM   1890  O O    . GLU A 1 253 ? 6.981   71.157  52.390  1.00 13.86  ? 253 GLU A O    1 
ATOM   1891  C CB   . GLU A 1 253 ? 4.487   72.756  52.786  1.00 12.71  ? 253 GLU A CB   1 
ATOM   1892  C CG   . GLU A 1 253 ? 3.062   72.286  52.818  1.00 16.05  ? 253 GLU A CG   1 
ATOM   1893  C CD   . GLU A 1 253 ? 2.138   73.287  53.433  1.00 16.66  ? 253 GLU A CD   1 
ATOM   1894  O OE1  . GLU A 1 253 ? 2.522   74.460  53.565  1.00 14.76  ? 253 GLU A OE1  1 
ATOM   1895  O OE2  . GLU A 1 253 ? 1.019   72.890  53.776  1.00 22.75  ? 253 GLU A OE2  1 
ATOM   1896  N N    . ARG A 1 254 ? 7.560   72.691  53.863  1.00 14.02  ? 254 ARG A N    1 
ATOM   1897  C CA   . ARG A 1 254 ? 8.929   72.723  53.453  1.00 12.29  ? 254 ARG A CA   1 
ATOM   1898  C C    . ARG A 1 254 ? 9.523   71.394  53.739  1.00 11.66  ? 254 ARG A C    1 
ATOM   1899  O O    . ARG A 1 254 ? 9.756   70.652  52.840  1.00 16.40  ? 254 ARG A O    1 
ATOM   1900  C CB   . ARG A 1 254 ? 9.669   73.847  54.137  1.00 12.22  ? 254 ARG A CB   1 
ATOM   1901  C CG   . ARG A 1 254 ? 9.405   75.220  53.559  1.00 13.05  ? 254 ARG A CG   1 
ATOM   1902  C CD   . ARG A 1 254 ? 10.058  76.302  54.404  1.00 13.47  ? 254 ARG A CD   1 
ATOM   1903  N NE   . ARG A 1 254 ? 11.497  76.341  54.191  1.00 14.82  ? 254 ARG A NE   1 
ATOM   1904  C CZ   . ARG A 1 254 ? 12.375  76.909  55.003  1.00 11.94  ? 254 ARG A CZ   1 
ATOM   1905  N NH1  . ARG A 1 254 ? 11.970  77.504  56.106  1.00 25.08  ? 254 ARG A NH1  1 
ATOM   1906  N NH2  . ARG A 1 254 ? 13.661  76.876  54.707  1.00 8.27   ? 254 ARG A NH2  1 
ATOM   1907  N N    . PHE A 1 255 ? 9.684   71.020  54.984  1.00 10.29  ? 255 PHE A N    1 
ATOM   1908  C CA   . PHE A 1 255 ? 10.343  69.769  55.345  1.00 12.30  ? 255 PHE A CA   1 
ATOM   1909  C C    . PHE A 1 255 ? 9.547   68.502  55.265  1.00 12.21  ? 255 PHE A C    1 
ATOM   1910  O O    . PHE A 1 255 ? 10.078  67.437  55.449  1.00 13.03  ? 255 PHE A O    1 
ATOM   1911  C CB   . PHE A 1 255 ? 10.944  69.866  56.731  1.00 16.28  ? 255 PHE A CB   1 
ATOM   1912  C CG   . PHE A 1 255 ? 9.970   70.216  57.796  1.00 12.36  ? 255 PHE A CG   1 
ATOM   1913  C CD1  . PHE A 1 255 ? 9.638   71.523  58.043  1.00 11.05  ? 255 PHE A CD1  1 
ATOM   1914  C CD2  . PHE A 1 255 ? 9.423   69.236  58.571  1.00 12.39  ? 255 PHE A CD2  1 
ATOM   1915  C CE1  . PHE A 1 255 ? 8.744   71.840  59.015  1.00 16.87  ? 255 PHE A CE1  1 
ATOM   1916  C CE2  . PHE A 1 255 ? 8.531   69.545  59.546  1.00 18.12  ? 255 PHE A CE2  1 
ATOM   1917  C CZ   . PHE A 1 255 ? 8.182   70.848  59.761  1.00 20.93  ? 255 PHE A CZ   1 
ATOM   1918  N N    . ARG A 1 256 ? 8.276   68.603  54.998  1.00 11.36  ? 256 ARG A N    1 
ATOM   1919  C CA   . ARG A 1 256 ? 7.452   67.446  54.857  1.00 12.04  ? 256 ARG A CA   1 
ATOM   1920  C C    . ARG A 1 256 ? 7.753   66.771  53.532  1.00 17.30  ? 256 ARG A C    1 
ATOM   1921  O O    . ARG A 1 256 ? 7.556   65.577  53.422  1.00 18.77  ? 256 ARG A O    1 
ATOM   1922  C CB   . ARG A 1 256 ? 6.013   67.893  54.945  1.00 12.21  ? 256 ARG A CB   1 
ATOM   1923  C CG   . ARG A 1 256 ? 5.403   67.897  56.317  1.00 12.11  ? 256 ARG A CG   1 
ATOM   1924  C CD   . ARG A 1 256 ? 4.091   68.642  56.275  1.00 9.15   ? 256 ARG A CD   1 
ATOM   1925  N NE   . ARG A 1 256 ? 3.026   67.843  55.697  1.00 12.84  ? 256 ARG A NE   1 
ATOM   1926  C CZ   . ARG A 1 256 ? 1.828   68.322  55.401  1.00 17.23  ? 256 ARG A CZ   1 
ATOM   1927  N NH1  . ARG A 1 256 ? 1.559   69.591  55.633  1.00 17.89  ? 256 ARG A NH1  1 
ATOM   1928  N NH2  . ARG A 1 256 ? 0.902   67.536  54.881  1.00 14.85  ? 256 ARG A NH2  1 
ATOM   1929  N N    . CYS A 1 257 ? 8.231   67.514  52.520  1.00 20.71  ? 257 CYS A N    1 
ATOM   1930  C CA   . CYS A 1 257 ? 8.639   66.941  51.195  1.00 15.34  ? 257 CYS A CA   1 
ATOM   1931  C C    . CYS A 1 257 ? 9.926   66.189  51.195  1.00 15.37  ? 257 CYS A C    1 
ATOM   1932  O O    . CYS A 1 257 ? 9.971   65.053  50.801  1.00 17.82  ? 257 CYS A O    1 
ATOM   1933  C CB   . CYS A 1 257 ? 8.573   67.936  50.057  1.00 15.02  ? 257 CYS A CB   1 
ATOM   1934  S SG   . CYS A 1 257 ? 8.919   67.331  48.420  1.00 20.51  ? 257 CYS A SG   1 
ATOM   1935  N N    . PRO A 1 258 ? 11.019  66.796  51.708  1.00 14.06  ? 258 PRO A N    1 
ATOM   1936  C CA   . PRO A 1 258 ? 12.185  65.945  51.705  1.00 15.96  ? 258 PRO A CA   1 
ATOM   1937  C C    . PRO A 1 258 ? 12.222  64.773  52.610  1.00 11.88  ? 258 PRO A C    1 
ATOM   1938  O O    . PRO A 1 258 ? 13.131  64.001  52.576  1.00 12.91  ? 258 PRO A O    1 
ATOM   1939  C CB   . PRO A 1 258 ? 13.169  66.944  52.212  1.00 14.69  ? 258 PRO A CB   1 
ATOM   1940  C CG   . PRO A 1 258 ? 12.718  68.205  51.701  1.00 17.75  ? 258 PRO A CG   1 
ATOM   1941  C CD   . PRO A 1 258 ? 11.330  68.099  52.146  1.00 15.15  ? 258 PRO A CD   1 
ATOM   1942  N N    . GLU A 1 259 ? 11.250  64.635  53.447  1.00 9.32   ? 259 GLU A N    1 
ATOM   1943  C CA   . GLU A 1 259 ? 11.298  63.632  54.457  1.00 11.49  ? 259 GLU A CA   1 
ATOM   1944  C C    . GLU A 1 259 ? 10.458  62.461  54.071  1.00 13.82  ? 259 GLU A C    1 
ATOM   1945  O O    . GLU A 1 259 ? 10.390  61.474  54.756  1.00 17.27  ? 259 GLU A O    1 
ATOM   1946  C CB   . GLU A 1 259 ? 10.875  64.355  55.738  1.00 11.15  ? 259 GLU A CB   1 
ATOM   1947  C CG   . GLU A 1 259 ? 10.407  63.559  56.911  1.00 8.61   ? 259 GLU A CG   1 
ATOM   1948  C CD   . GLU A 1 259 ? 11.387  63.666  58.018  1.00 7.49   ? 259 GLU A CD   1 
ATOM   1949  O OE1  . GLU A 1 259 ? 12.163  64.631  58.024  1.00 7.16   ? 259 GLU A OE1  1 
ATOM   1950  O OE2  . GLU A 1 259 ? 11.370  62.785  58.868  1.00 8.83   ? 259 GLU A OE2  1 
ATOM   1951  N N    . ALA A 1 260 ? 9.885   62.512  52.889  1.00 11.22  ? 260 ALA A N    1 
ATOM   1952  C CA   . ALA A 1 260 ? 9.093   61.417  52.392  1.00 9.60   ? 260 ALA A CA   1 
ATOM   1953  C C    . ALA A 1 260 ? 10.083  60.482  51.827  1.00 11.75  ? 260 ALA A C    1 
ATOM   1954  O O    . ALA A 1 260 ? 9.737   59.580  51.119  1.00 17.71  ? 260 ALA A O    1 
ATOM   1955  C CB   . ALA A 1 260 ? 8.147   61.898  51.337  1.00 7.90   ? 260 ALA A CB   1 
ATOM   1956  N N    . LEU A 1 261 ? 11.336  60.684  52.158  1.00 7.68   ? 261 LEU A N    1 
ATOM   1957  C CA   . LEU A 1 261 ? 12.378  59.868  51.656  1.00 8.68   ? 261 LEU A CA   1 
ATOM   1958  C C    . LEU A 1 261 ? 12.800  59.117  52.825  1.00 8.52   ? 261 LEU A C    1 
ATOM   1959  O O    . LEU A 1 261 ? 13.459  58.125  52.709  1.00 9.01   ? 261 LEU A O    1 
ATOM   1960  C CB   . LEU A 1 261 ? 13.535  60.752  51.240  1.00 8.98   ? 261 LEU A CB   1 
ATOM   1961  C CG   . LEU A 1 261 ? 13.566  61.574  49.976  1.00 9.28   ? 261 LEU A CG   1 
ATOM   1962  C CD1  . LEU A 1 261 ? 14.841  62.383  50.071  1.00 5.08   ? 261 LEU A CD1  1 
ATOM   1963  C CD2  . LEU A 1 261 ? 13.576  60.679  48.752  1.00 11.27  ? 261 LEU A CD2  1 
ATOM   1964  N N    . PHE A 1 262 ? 12.426  59.594  53.990  1.00 8.16   ? 262 PHE A N    1 
ATOM   1965  C CA   . PHE A 1 262 ? 12.880  59.001  55.212  1.00 7.85   ? 262 PHE A CA   1 
ATOM   1966  C C    . PHE A 1 262 ? 11.761  58.283  55.755  1.00 6.54   ? 262 PHE A C    1 
ATOM   1967  O O    . PHE A 1 262 ? 11.910  57.416  56.563  1.00 7.34   ? 262 PHE A O    1 
ATOM   1968  C CB   . PHE A 1 262 ? 13.310  60.084  56.151  1.00 8.68   ? 262 PHE A CB   1 
ATOM   1969  C CG   . PHE A 1 262 ? 14.702  60.551  55.895  1.00 5.74   ? 262 PHE A CG   1 
ATOM   1970  C CD1  . PHE A 1 262 ? 15.763  59.867  56.405  1.00 5.77   ? 262 PHE A CD1  1 
ATOM   1971  C CD2  . PHE A 1 262 ? 14.939  61.645  55.106  1.00 5.67   ? 262 PHE A CD2  1 
ATOM   1972  C CE1  . PHE A 1 262 ? 17.040  60.261  56.150  1.00 5.22   ? 262 PHE A CE1  1 
ATOM   1973  C CE2  . PHE A 1 262 ? 16.215  62.050  54.843  1.00 5.01   ? 262 PHE A CE2  1 
ATOM   1974  C CZ   . PHE A 1 262 ? 17.271  61.355  55.365  1.00 5.45   ? 262 PHE A CZ   1 
ATOM   1975  N N    . GLN A 1 263 ? 10.599  58.650  55.308  1.00 9.52   ? 263 GLN A N    1 
ATOM   1976  C CA   . GLN A 1 263 ? 9.422   57.961  55.699  1.00 7.64   ? 263 GLN A CA   1 
ATOM   1977  C C    . GLN A 1 263 ? 8.738   57.717  54.443  1.00 7.13   ? 263 GLN A C    1 
ATOM   1978  O O    . GLN A 1 263 ? 7.872   58.461  54.090  1.00 7.65   ? 263 GLN A O    1 
ATOM   1979  C CB   . GLN A 1 263 ? 8.585   58.855  56.547  1.00 7.89   ? 263 GLN A CB   1 
ATOM   1980  C CG   . GLN A 1 263 ? 8.733   58.633  58.031  1.00 7.77   ? 263 GLN A CG   1 
ATOM   1981  C CD   . GLN A 1 263 ? 8.795   59.931  58.788  1.00 8.17   ? 263 GLN A CD   1 
ATOM   1982  O OE1  . GLN A 1 263 ? 7.789   60.592  58.973  1.00 7.08   ? 263 GLN A OE1  1 
ATOM   1983  N NE2  . GLN A 1 263 ? 9.980   60.298  59.231  1.00 11.94  ? 263 GLN A NE2  1 
ATOM   1984  N N    . PRO A 1 264 ? 9.100   56.588  53.747  1.00 6.54   ? 264 PRO A N    1 
ATOM   1985  C CA   . PRO A 1 264 ? 8.498   56.388  52.443  1.00 7.11   ? 264 PRO A CA   1 
ATOM   1986  C C    . PRO A 1 264 ? 7.037   56.021  52.544  1.00 9.29   ? 264 PRO A C    1 
ATOM   1987  O O    . PRO A 1 264 ? 6.381   55.843  51.555  1.00 7.95   ? 264 PRO A O    1 
ATOM   1988  C CB   . PRO A 1 264 ? 9.317   55.239  51.908  1.00 6.61   ? 264 PRO A CB   1 
ATOM   1989  C CG   . PRO A 1 264 ? 9.526   54.420  53.047  1.00 6.88   ? 264 PRO A CG   1 
ATOM   1990  C CD   . PRO A 1 264 ? 9.960   55.407  54.039  1.00 8.28   ? 264 PRO A CD   1 
ATOM   1991  N N    . SER A 1 265 ? 6.508   56.006  53.746  1.00 9.66   ? 265 SER A N    1 
ATOM   1992  C CA   . SER A 1 265 ? 5.155   55.633  53.995  1.00 7.40   ? 265 SER A CA   1 
ATOM   1993  C C    . SER A 1 265 ? 4.244   56.779  53.792  1.00 11.66  ? 265 SER A C    1 
ATOM   1994  O O    . SER A 1 265 ? 3.033   56.633  53.870  1.00 17.26  ? 265 SER A O    1 
ATOM   1995  C CB   . SER A 1 265 ? 5.074   55.222  55.435  1.00 4.75   ? 265 SER A CB   1 
ATOM   1996  O OG   . SER A 1 265 ? 5.680   56.169  56.281  1.00 5.18   ? 265 SER A OG   1 
ATOM   1997  N N    . PHE A 1 266 ? 4.805   57.949  53.604  1.00 8.66   ? 266 PHE A N    1 
ATOM   1998  C CA   . PHE A 1 266 ? 4.001   59.118  53.437  1.00 9.21   ? 266 PHE A CA   1 
ATOM   1999  C C    . PHE A 1 266 ? 3.326   59.038  52.089  1.00 10.48  ? 266 PHE A C    1 
ATOM   2000  O O    . PHE A 1 266 ? 2.171   59.379  51.963  1.00 10.31  ? 266 PHE A O    1 
ATOM   2001  C CB   . PHE A 1 266 ? 4.897   60.332  53.547  1.00 8.98   ? 266 PHE A CB   1 
ATOM   2002  C CG   . PHE A 1 266 ? 5.037   60.869  54.927  1.00 7.71   ? 266 PHE A CG   1 
ATOM   2003  C CD1  . PHE A 1 266 ? 4.398   60.280  55.985  1.00 6.36   ? 266 PHE A CD1  1 
ATOM   2004  C CD2  . PHE A 1 266 ? 5.799   61.987  55.152  1.00 11.35  ? 266 PHE A CD2  1 
ATOM   2005  C CE1  . PHE A 1 266 ? 4.524   60.796  57.250  1.00 6.03   ? 266 PHE A CE1  1 
ATOM   2006  C CE2  . PHE A 1 266 ? 5.934   62.509  56.411  1.00 6.05   ? 266 PHE A CE2  1 
ATOM   2007  C CZ   . PHE A 1 266 ? 5.292   61.913  57.461  1.00 5.01   ? 266 PHE A CZ   1 
ATOM   2008  N N    . LEU A 1 267 ? 4.033   58.560  51.083  1.00 11.36  ? 267 LEU A N    1 
ATOM   2009  C CA   . LEU A 1 267 ? 3.519   58.462  49.731  1.00 9.83   ? 267 LEU A CA   1 
ATOM   2010  C C    . LEU A 1 267 ? 2.825   57.162  49.405  1.00 14.72  ? 267 LEU A C    1 
ATOM   2011  O O    . LEU A 1 267 ? 2.376   56.923  48.303  1.00 23.79  ? 267 LEU A O    1 
ATOM   2012  C CB   . LEU A 1 267 ? 4.666   58.654  48.762  1.00 10.79  ? 267 LEU A CB   1 
ATOM   2013  C CG   . LEU A 1 267 ? 5.462   59.944  48.654  1.00 17.04  ? 267 LEU A CG   1 
ATOM   2014  C CD1  . LEU A 1 267 ? 6.622   59.749  47.701  1.00 18.05  ? 267 LEU A CD1  1 
ATOM   2015  C CD2  . LEU A 1 267 ? 4.531   60.985  48.077  1.00 24.46  ? 267 LEU A CD2  1 
ATOM   2016  N N    . GLY A 1 268 ? 2.757   56.300  50.384  1.00 10.87  ? 268 GLY A N    1 
ATOM   2017  C CA   . GLY A 1 268 ? 2.125   55.030  50.230  1.00 9.80   ? 268 GLY A CA   1 
ATOM   2018  C C    . GLY A 1 268 ? 3.159   53.976  50.076  1.00 11.26  ? 268 GLY A C    1 
ATOM   2019  O O    . GLY A 1 268 ? 2.850   52.807  49.996  1.00 13.23  ? 268 GLY A O    1 
ATOM   2020  N N    . MET A 1 269 ? 4.400   54.347  50.064  1.00 12.67  ? 269 MET A N    1 
ATOM   2021  C CA   . MET A 1 269 ? 5.344   53.307  49.832  1.00 18.32  ? 269 MET A CA   1 
ATOM   2022  C C    . MET A 1 269 ? 5.707   52.488  51.035  1.00 20.13  ? 269 MET A C    1 
ATOM   2023  O O    . MET A 1 269 ? 6.136   53.005  52.043  1.00 18.60  ? 269 MET A O    1 
ATOM   2024  C CB   . MET A 1 269 ? 6.596   53.828  49.115  1.00 11.72  ? 269 MET A CB   1 
ATOM   2025  C CG   . MET A 1 269 ? 6.386   54.302  47.707  1.00 9.19   ? 269 MET A CG   1 
ATOM   2026  S SD   . MET A 1 269 ? 7.977   54.917  47.188  1.00 26.20  ? 269 MET A SD   1 
ATOM   2027  C CE   . MET A 1 269 ? 8.869   53.391  47.010  1.00 21.55  ? 269 MET A CE   1 
ATOM   2028  N N    . GLU A 1 270 ? 5.496   51.195  50.945  1.00 23.85  ? 270 GLU A N    1 
ATOM   2029  C CA   . GLU A 1 270 ? 5.818   50.298  52.026  1.00 26.97  ? 270 GLU A CA   1 
ATOM   2030  C C    . GLU A 1 270 ? 7.218   49.819  51.912  1.00 23.39  ? 270 GLU A C    1 
ATOM   2031  O O    . GLU A 1 270 ? 7.455   48.636  51.763  1.00 26.13  ? 270 GLU A O    1 
ATOM   2032  C CB   . GLU A 1 270 ? 4.904   49.097  52.045  1.00 37.15  ? 270 GLU A CB   1 
ATOM   2033  C CG   . GLU A 1 270 ? 3.435   49.458  52.199  1.00 35.20  ? 270 GLU A CG   1 
ATOM   2034  C CD   . GLU A 1 270 ? 2.563   48.262  52.514  1.00 50.36  ? 270 GLU A CD   1 
ATOM   2035  O OE1  . GLU A 1 270 ? 3.071   47.125  52.504  1.00 53.95  ? 270 GLU A OE1  1 
ATOM   2036  O OE2  . GLU A 1 270 ? 1.364   48.463  52.777  1.00 58.53  ? 270 GLU A OE2  1 
ATOM   2037  N N    . SER A 1 271 ? 8.155   50.728  52.043  1.00 16.57  ? 271 SER A N    1 
ATOM   2038  C CA   . SER A 1 271 ? 9.510   50.378  51.873  1.00 10.21  ? 271 SER A CA   1 
ATOM   2039  C C    . SER A 1 271 ? 10.325  50.922  52.990  1.00 8.57   ? 271 SER A C    1 
ATOM   2040  O O    . SER A 1 271 ? 9.796   51.271  54.032  1.00 7.69   ? 271 SER A O    1 
ATOM   2041  C CB   . SER A 1 271 ? 9.970   50.901  50.532  1.00 10.86  ? 271 SER A CB   1 
ATOM   2042  O OG   . SER A 1 271 ? 9.576   52.231  50.330  1.00 17.86  ? 271 SER A OG   1 
ATOM   2043  N N    . CYS A 1 272 ? 11.619  51.023  52.778  1.00 12.21  ? 272 CYS A N    1 
ATOM   2044  C CA   . CYS A 1 272 ? 12.488  51.433  53.821  1.00 9.55   ? 272 CYS A CA   1 
ATOM   2045  C C    . CYS A 1 272 ? 13.123  52.689  53.369  1.00 7.90   ? 272 CYS A C    1 
ATOM   2046  O O    . CYS A 1 272 ? 13.548  52.766  52.254  1.00 9.46   ? 272 CYS A O    1 
ATOM   2047  C CB   . CYS A 1 272 ? 13.511  50.333  53.993  1.00 8.14   ? 272 CYS A CB   1 
ATOM   2048  S SG   . CYS A 1 272 ? 13.394  49.324  55.480  1.00 34.33  ? 272 CYS A SG   1 
ATOM   2049  N N    . GLY A 1 273 ? 13.193  53.676  54.231  1.00 5.20   ? 273 GLY A N    1 
ATOM   2050  C CA   . GLY A 1 273 ? 13.726  54.948  53.861  1.00 5.55   ? 273 GLY A CA   1 
ATOM   2051  C C    . GLY A 1 273 ? 15.155  54.886  53.517  1.00 7.22   ? 273 GLY A C    1 
ATOM   2052  O O    . GLY A 1 273 ? 15.783  53.894  53.697  1.00 8.51   ? 273 GLY A O    1 
ATOM   2053  N N    . ILE A 1 274 ? 15.738  55.982  53.101  1.00 6.46   ? 274 ILE A N    1 
ATOM   2054  C CA   . ILE A 1 274 ? 17.064  55.928  52.603  1.00 6.05   ? 274 ILE A CA   1 
ATOM   2055  C C    . ILE A 1 274 ? 18.023  55.724  53.697  1.00 6.16   ? 274 ILE A C    1 
ATOM   2056  O O    . ILE A 1 274 ? 19.162  55.408  53.461  1.00 8.02   ? 274 ILE A O    1 
ATOM   2057  C CB   . ILE A 1 274 ? 17.352  57.172  51.821  1.00 6.23   ? 274 ILE A CB   1 
ATOM   2058  C CG1  . ILE A 1 274 ? 16.895  58.396  52.589  1.00 7.89   ? 274 ILE A CG1  1 
ATOM   2059  C CG2  . ILE A 1 274 ? 16.642  57.120  50.485  1.00 5.55   ? 274 ILE A CG2  1 
ATOM   2060  C CD1  . ILE A 1 274 ? 17.202  59.672  51.861  1.00 9.40   ? 274 ILE A CD1  1 
ATOM   2061  N N    . HIS A 1 275 ? 17.565  55.810  54.925  1.00 6.05   ? 275 HIS A N    1 
ATOM   2062  C CA   . HIS A 1 275 ? 18.441  55.593  56.085  1.00 5.94   ? 275 HIS A CA   1 
ATOM   2063  C C    . HIS A 1 275 ? 18.462  54.188  56.499  1.00 7.31   ? 275 HIS A C    1 
ATOM   2064  O O    . HIS A 1 275 ? 19.348  53.777  57.220  1.00 7.05   ? 275 HIS A O    1 
ATOM   2065  C CB   . HIS A 1 275 ? 18.056  56.480  57.241  1.00 3.51   ? 275 HIS A CB   1 
ATOM   2066  C CG   . HIS A 1 275 ? 16.687  56.255  57.786  1.00 6.71   ? 275 HIS A CG   1 
ATOM   2067  N ND1  . HIS A 1 275 ? 15.552  56.694  57.149  1.00 3.60   ? 275 HIS A ND1  1 
ATOM   2068  C CD2  . HIS A 1 275 ? 16.278  55.714  58.952  1.00 4.09   ? 275 HIS A CD2  1 
ATOM   2069  C CE1  . HIS A 1 275 ? 14.500  56.392  57.880  1.00 3.51   ? 275 HIS A CE1  1 
ATOM   2070  N NE2  . HIS A 1 275 ? 14.913  55.799  58.981  1.00 4.69   ? 275 HIS A NE2  1 
ATOM   2071  N N    . GLU A 1 276 ? 17.487  53.438  56.014  1.00 6.27   ? 276 GLU A N    1 
ATOM   2072  C CA   . GLU A 1 276 ? 17.348  52.076  56.336  1.00 5.77   ? 276 GLU A CA   1 
ATOM   2073  C C    . GLU A 1 276 ? 17.736  51.283  55.173  1.00 8.55   ? 276 GLU A C    1 
ATOM   2074  O O    . GLU A 1 276 ? 18.354  50.281  55.347  1.00 13.18  ? 276 GLU A O    1 
ATOM   2075  C CB   . GLU A 1 276 ? 15.916  51.831  56.594  1.00 7.75   ? 276 GLU A CB   1 
ATOM   2076  C CG   . GLU A 1 276 ? 15.359  52.507  57.826  1.00 8.60   ? 276 GLU A CG   1 
ATOM   2077  C CD   . GLU A 1 276 ? 13.847  52.558  57.857  1.00 7.06   ? 276 GLU A CD   1 
ATOM   2078  O OE1  . GLU A 1 276 ? 13.246  53.346  57.110  1.00 5.67   ? 276 GLU A OE1  1 
ATOM   2079  O OE2  . GLU A 1 276 ? 13.257  51.816  58.652  1.00 7.34   ? 276 GLU A OE2  1 
ATOM   2080  N N    . THR A 1 277 ? 17.456  51.714  53.962  1.00 7.38   ? 277 THR A N    1 
ATOM   2081  C CA   . THR A 1 277 ? 17.887  51.028  52.768  1.00 0.82   ? 277 THR A CA   1 
ATOM   2082  C C    . THR A 1 277 ? 19.373  50.972  52.721  1.00 8.84   ? 277 THR A C    1 
ATOM   2083  O O    . THR A 1 277 ? 19.940  50.244  51.960  1.00 8.96   ? 277 THR A O    1 
ATOM   2084  C CB   . THR A 1 277 ? 17.433  51.809  51.552  1.00 8.17   ? 277 THR A CB   1 
ATOM   2085  O OG1  . THR A 1 277 ? 16.106  52.261  51.751  1.00 10.70  ? 277 THR A OG1  1 
ATOM   2086  C CG2  . THR A 1 277 ? 17.417  50.985  50.290  1.00 10.22  ? 277 THR A CG2  1 
ATOM   2087  N N    . THR A 1 278 ? 20.039  51.726  53.568  1.00 10.54  ? 278 THR A N    1 
ATOM   2088  C CA   . THR A 1 278 ? 21.486  51.833  53.536  1.00 9.02   ? 278 THR A CA   1 
ATOM   2089  C C    . THR A 1 278 ? 22.069  50.967  54.584  1.00 7.88   ? 278 THR A C    1 
ATOM   2090  O O    . THR A 1 278 ? 23.214  50.633  54.523  1.00 7.29   ? 278 THR A O    1 
ATOM   2091  C CB   . THR A 1 278 ? 21.882  53.308  53.652  1.00 10.06  ? 278 THR A CB   1 
ATOM   2092  O OG1  . THR A 1 278 ? 21.190  54.058  52.651  1.00 6.69   ? 278 THR A OG1  1 
ATOM   2093  C CG2  . THR A 1 278 ? 23.369  53.535  53.465  1.00 10.46  ? 278 THR A CG2  1 
ATOM   2094  N N    . PHE A 1 279 ? 21.260  50.527  55.524  1.00 6.79   ? 279 PHE A N    1 
ATOM   2095  C CA   . PHE A 1 279 ? 21.710  49.597  56.543  1.00 7.30   ? 279 PHE A CA   1 
ATOM   2096  C C    . PHE A 1 279 ? 21.717  48.221  56.020  1.00 7.61   ? 279 PHE A C    1 
ATOM   2097  O O    . PHE A 1 279 ? 22.589  47.455  56.290  1.00 8.95   ? 279 PHE A O    1 
ATOM   2098  C CB   . PHE A 1 279 ? 20.736  49.616  57.693  1.00 7.19   ? 279 PHE A CB   1 
ATOM   2099  C CG   . PHE A 1 279 ? 21.082  48.684  58.807  1.00 8.21   ? 279 PHE A CG   1 
ATOM   2100  C CD1  . PHE A 1 279 ? 22.213  48.877  59.555  1.00 8.24   ? 279 PHE A CD1  1 
ATOM   2101  C CD2  . PHE A 1 279 ? 20.264  47.624  59.113  1.00 9.77   ? 279 PHE A CD2  1 
ATOM   2102  C CE1  . PHE A 1 279 ? 22.529  48.023  60.577  1.00 8.04   ? 279 PHE A CE1  1 
ATOM   2103  C CE2  . PHE A 1 279 ? 20.580  46.760  60.132  1.00 10.30  ? 279 PHE A CE2  1 
ATOM   2104  C CZ   . PHE A 1 279 ? 21.712  46.965  60.871  1.00 6.89   ? 279 PHE A CZ   1 
ATOM   2105  N N    . ASN A 1 280 ? 20.711  47.889  55.258  1.00 6.24   ? 280 ASN A N    1 
ATOM   2106  C CA   . ASN A 1 280 ? 20.581  46.579  54.736  1.00 6.38   ? 280 ASN A CA   1 
ATOM   2107  C C    . ASN A 1 280 ? 21.589  46.344  53.697  1.00 6.91   ? 280 ASN A C    1 
ATOM   2108  O O    . ASN A 1 280 ? 22.103  45.281  53.631  1.00 6.33   ? 280 ASN A O    1 
ATOM   2109  C CB   . ASN A 1 280 ? 19.180  46.448  54.182  1.00 5.61   ? 280 ASN A CB   1 
ATOM   2110  C CG   . ASN A 1 280 ? 18.117  46.948  55.126  1.00 5.47   ? 280 ASN A CG   1 
ATOM   2111  O OD1  . ASN A 1 280 ? 17.272  47.729  54.734  1.00 5.57   ? 280 ASN A OD1  1 
ATOM   2112  N ND2  . ASN A 1 280 ? 18.122  46.463  56.354  1.00 4.72   ? 280 ASN A ND2  1 
ATOM   2113  N N    . SER A 1 281 ? 21.922  47.334  52.899  1.00 7.13   ? 281 SER A N    1 
ATOM   2114  C CA   . SER A 1 281 ? 22.958  47.224  51.903  1.00 6.06   ? 281 SER A CA   1 
ATOM   2115  C C    . SER A 1 281 ? 24.361  47.158  52.494  1.00 10.57  ? 281 SER A C    1 
ATOM   2116  O O    . SER A 1 281 ? 25.206  46.485  51.977  1.00 9.40   ? 281 SER A O    1 
ATOM   2117  C CB   . SER A 1 281 ? 22.845  48.395  50.990  1.00 5.47   ? 281 SER A CB   1 
ATOM   2118  O OG   . SER A 1 281 ? 21.510  48.617  50.651  1.00 7.70   ? 281 SER A OG   1 
ATOM   2119  N N    . ILE A 1 282 ? 24.612  47.813  53.602  1.00 7.65   ? 282 ILE A N    1 
ATOM   2120  C CA   . ILE A 1 282 ? 25.908  47.777  54.265  1.00 8.47   ? 282 ILE A CA   1 
ATOM   2121  C C    . ILE A 1 282 ? 26.149  46.458  54.963  1.00 7.40   ? 282 ILE A C    1 
ATOM   2122  O O    . ILE A 1 282 ? 27.248  46.012  55.186  1.00 11.43  ? 282 ILE A O    1 
ATOM   2123  C CB   . ILE A 1 282 ? 26.007  48.992  55.234  1.00 9.04   ? 282 ILE A CB   1 
ATOM   2124  C CG1  . ILE A 1 282 ? 26.597  50.204  54.554  1.00 7.48   ? 282 ILE A CG1  1 
ATOM   2125  C CG2  . ILE A 1 282 ? 26.833  48.711  56.464  1.00 10.68  ? 282 ILE A CG2  1 
ATOM   2126  C CD1  . ILE A 1 282 ? 26.538  51.431  55.425  1.00 5.94   ? 282 ILE A CD1  1 
ATOM   2127  N N    . MET A 1 283 ? 25.101  45.757  55.211  1.00 7.14   ? 283 MET A N    1 
ATOM   2128  C CA   . MET A 1 283 ? 25.194  44.512  55.881  1.00 10.87  ? 283 MET A CA   1 
ATOM   2129  C C    . MET A 1 283 ? 24.616  43.446  55.010  1.00 13.58  ? 283 MET A C    1 
ATOM   2130  O O    . MET A 1 283 ? 23.666  42.805  55.401  1.00 23.29  ? 283 MET A O    1 
ATOM   2131  C CB   . MET A 1 283 ? 24.307  44.599  57.122  1.00 17.97  ? 283 MET A CB   1 
ATOM   2132  C CG   . MET A 1 283 ? 24.751  45.611  58.154  1.00 24.96  ? 283 MET A CG   1 
ATOM   2133  S SD   . MET A 1 283 ? 24.661  44.923  59.800  1.00 20.13  ? 283 MET A SD   1 
ATOM   2134  C CE   . MET A 1 283 ? 25.760  46.021  60.674  1.00 8.34   ? 283 MET A CE   1 
ATOM   2135  N N    . LYS A 1 284 ? 25.109  43.276  53.805  1.00 9.19   ? 284 LYS A N    1 
ATOM   2136  C CA   . LYS A 1 284 ? 24.612  42.279  52.886  1.00 9.07   ? 284 LYS A CA   1 
ATOM   2137  C C    . LYS A 1 284 ? 25.918  42.090  52.313  1.00 8.48   ? 284 LYS A C    1 
ATOM   2138  O O    . LYS A 1 284 ? 26.056  41.500  51.271  1.00 11.73  ? 284 LYS A O    1 
ATOM   2139  C CB   . LYS A 1 284 ? 23.675  42.847  51.866  1.00 6.45   ? 284 LYS A CB   1 
ATOM   2140  C CG   . LYS A 1 284 ? 22.223  42.469  52.019  1.00 4.99   ? 284 LYS A CG   1 
ATOM   2141  C CD   . LYS A 1 284 ? 21.428  43.017  50.854  1.00 5.64   ? 284 LYS A CD   1 
ATOM   2142  C CE   . LYS A 1 284 ? 19.944  42.833  51.068  1.00 10.44  ? 284 LYS A CE   1 
ATOM   2143  N NZ   . LYS A 1 284 ? 19.200  43.001  49.795  1.00 8.84   ? 284 LYS A NZ   1 
ATOM   2144  N N    . CYS A 1 285 ? 26.910  42.583  53.028  1.00 9.44   ? 285 CYS A N    1 
ATOM   2145  C CA   . CYS A 1 285 ? 28.276  42.510  52.584  1.00 11.06  ? 285 CYS A CA   1 
ATOM   2146  C C    . CYS A 1 285 ? 29.114  41.996  53.723  1.00 13.29  ? 285 CYS A C    1 
ATOM   2147  O O    . CYS A 1 285 ? 28.667  41.935  54.832  1.00 13.26  ? 285 CYS A O    1 
ATOM   2148  C CB   . CYS A 1 285 ? 28.793  43.891  52.141  1.00 10.83  ? 285 CYS A CB   1 
ATOM   2149  S SG   . CYS A 1 285 ? 27.821  44.905  51.030  1.00 11.76  ? 285 CYS A SG   1 
ATOM   2150  N N    . ASP A 1 286 ? 30.342  41.635  53.445  1.00 14.23  ? 286 ASP A N    1 
ATOM   2151  C CA   . ASP A 1 286 ? 31.175  41.036  54.444  1.00 15.44  ? 286 ASP A CA   1 
ATOM   2152  C C    . ASP A 1 286 ? 31.464  41.862  55.582  1.00 19.02  ? 286 ASP A C    1 
ATOM   2153  O O    . ASP A 1 286 ? 31.727  43.025  55.447  1.00 26.72  ? 286 ASP A O    1 
ATOM   2154  C CB   . ASP A 1 286 ? 32.508  40.589  53.869  1.00 23.79  ? 286 ASP A CB   1 
ATOM   2155  C CG   . ASP A 1 286 ? 32.892  39.193  54.282  1.00 23.92  ? 286 ASP A CG   1 
ATOM   2156  O OD1  . ASP A 1 286 ? 32.427  38.721  55.332  1.00 18.36  ? 286 ASP A OD1  1 
ATOM   2157  O OD2  . ASP A 1 286 ? 33.675  38.565  53.548  1.00 27.05  ? 286 ASP A OD2  1 
ATOM   2158  N N    . VAL A 1 287 ? 31.494  41.220  56.737  1.00 23.79  ? 287 VAL A N    1 
ATOM   2159  C CA   . VAL A 1 287 ? 31.721  41.883  57.976  1.00 14.77  ? 287 VAL A CA   1 
ATOM   2160  C C    . VAL A 1 287 ? 33.015  42.532  57.951  1.00 13.50  ? 287 VAL A C    1 
ATOM   2161  O O    . VAL A 1 287 ? 33.294  43.443  58.696  1.00 15.84  ? 287 VAL A O    1 
ATOM   2162  C CB   . VAL A 1 287 ? 31.655  40.843  59.079  1.00 11.50  ? 287 VAL A CB   1 
ATOM   2163  C CG1  . VAL A 1 287 ? 31.993  41.447  60.424  1.00 20.58  ? 287 VAL A CG1  1 
ATOM   2164  C CG2  . VAL A 1 287 ? 30.271  40.230  59.131  1.00 9.54   ? 287 VAL A CG2  1 
ATOM   2165  N N    . ASP A 1 288 ? 33.821  42.158  57.010  1.00 13.89  ? 288 ASP A N    1 
ATOM   2166  C CA   . ASP A 1 288 ? 35.156  42.660  57.035  1.00 20.97  ? 288 ASP A CA   1 
ATOM   2167  C C    . ASP A 1 288 ? 35.277  44.032  56.422  1.00 25.59  ? 288 ASP A C    1 
ATOM   2168  O O    . ASP A 1 288 ? 36.215  44.755  56.711  1.00 25.15  ? 288 ASP A O    1 
ATOM   2169  C CB   . ASP A 1 288 ? 36.077  41.648  56.343  1.00 24.44  ? 288 ASP A CB   1 
ATOM   2170  C CG   . ASP A 1 288 ? 36.191  40.335  57.091  1.00 30.01  ? 288 ASP A CG   1 
ATOM   2171  O OD1  . ASP A 1 288 ? 35.296  39.980  57.878  1.00 34.96  ? 288 ASP A OD1  1 
ATOM   2172  O OD2  . ASP A 1 288 ? 37.203  39.643  56.886  1.00 37.22  ? 288 ASP A OD2  1 
ATOM   2173  N N    . ILE A 1 289 ? 34.327  44.404  55.586  1.00 24.08  ? 289 ILE A N    1 
ATOM   2174  C CA   . ILE A 1 289 ? 34.394  45.662  54.874  1.00 16.46  ? 289 ILE A CA   1 
ATOM   2175  C C    . ILE A 1 289 ? 33.374  46.653  55.364  1.00 17.54  ? 289 ILE A C    1 
ATOM   2176  O O    . ILE A 1 289 ? 33.394  47.776  54.952  1.00 18.95  ? 289 ILE A O    1 
ATOM   2177  C CB   . ILE A 1 289 ? 34.231  45.444  53.369  1.00 15.00  ? 289 ILE A CB   1 
ATOM   2178  C CG1  . ILE A 1 289 ? 32.789  45.131  52.985  1.00 19.38  ? 289 ILE A CG1  1 
ATOM   2179  C CG2  . ILE A 1 289 ? 35.130  44.319  52.897  1.00 19.27  ? 289 ILE A CG2  1 
ATOM   2180  C CD1  . ILE A 1 289 ? 32.494  45.388  51.527  1.00 14.81  ? 289 ILE A CD1  1 
ATOM   2181  N N    . ARG A 1 290 ? 32.514  46.260  56.288  1.00 16.07  ? 290 ARG A N    1 
ATOM   2182  C CA   . ARG A 1 290 ? 31.471  47.130  56.817  1.00 12.89  ? 290 ARG A CA   1 
ATOM   2183  C C    . ARG A 1 290 ? 31.960  48.384  57.461  1.00 14.47  ? 290 ARG A C    1 
ATOM   2184  O O    . ARG A 1 290 ? 31.221  49.323  57.594  1.00 10.74  ? 290 ARG A O    1 
ATOM   2185  C CB   . ARG A 1 290 ? 30.616  46.362  57.795  1.00 8.18   ? 290 ARG A CB   1 
ATOM   2186  C CG   . ARG A 1 290 ? 29.742  45.322  57.147  1.00 9.94   ? 290 ARG A CG   1 
ATOM   2187  C CD   . ARG A 1 290 ? 28.951  44.569  58.188  1.00 9.72   ? 290 ARG A CD   1 
ATOM   2188  N NE   . ARG A 1 290 ? 28.298  43.391  57.642  1.00 11.76  ? 290 ARG A NE   1 
ATOM   2189  C CZ   . ARG A 1 290 ? 27.461  42.634  58.329  1.00 12.52  ? 290 ARG A CZ   1 
ATOM   2190  N NH1  . ARG A 1 290 ? 27.187  42.933  59.581  1.00 9.22   ? 290 ARG A NH1  1 
ATOM   2191  N NH2  . ARG A 1 290 ? 26.895  41.580  57.770  1.00 15.76  ? 290 ARG A NH2  1 
ATOM   2192  N N    . LYS A 1 291 ? 33.235  48.438  57.795  1.00 20.03  ? 291 LYS A N    1 
ATOM   2193  C CA   . LYS A 1 291 ? 33.823  49.569  58.483  1.00 17.64  ? 291 LYS A CA   1 
ATOM   2194  C C    . LYS A 1 291 ? 34.215  50.594  57.522  1.00 14.24  ? 291 LYS A C    1 
ATOM   2195  O O    . LYS A 1 291 ? 34.328  51.759  57.849  1.00 14.98  ? 291 LYS A O    1 
ATOM   2196  C CB   . LYS A 1 291 ? 35.088  49.082  59.148  1.00 15.81  ? 291 LYS A CB   1 
ATOM   2197  C CG   . LYS A 1 291 ? 36.137  48.611  58.174  1.00 20.93  ? 291 LYS A CG   1 
ATOM   2198  C CD   . LYS A 1 291 ? 37.378  48.164  58.910  1.00 19.71  ? 291 LYS A CD   1 
ATOM   2199  C CE   . LYS A 1 291 ? 38.443  47.686  57.950  1.00 34.19  ? 291 LYS A CE   1 
ATOM   2200  N NZ   . LYS A 1 291 ? 39.652  47.254  58.700  1.00 52.40  ? 291 LYS A NZ   1 
ATOM   2201  N N    . ASP A 1 292 ? 34.378  50.178  56.298  1.00 9.77   ? 292 ASP A N    1 
ATOM   2202  C CA   . ASP A 1 292 ? 34.835  51.068  55.283  1.00 12.71  ? 292 ASP A CA   1 
ATOM   2203  C C    . ASP A 1 292 ? 33.674  51.611  54.514  1.00 12.98  ? 292 ASP A C    1 
ATOM   2204  O O    . ASP A 1 292 ? 33.865  52.382  53.621  1.00 13.37  ? 292 ASP A O    1 
ATOM   2205  C CB   . ASP A 1 292 ? 35.731  50.284  54.346  1.00 16.39  ? 292 ASP A CB   1 
ATOM   2206  C CG   . ASP A 1 292 ? 37.058  49.933  54.946  1.00 21.05  ? 292 ASP A CG   1 
ATOM   2207  O OD1  . ASP A 1 292 ? 37.586  50.733  55.738  1.00 22.09  ? 292 ASP A OD1  1 
ATOM   2208  O OD2  . ASP A 1 292 ? 37.583  48.858  54.597  1.00 15.79  ? 292 ASP A OD2  1 
ATOM   2209  N N    . LEU A 1 293 ? 32.462  51.210  54.861  1.00 13.84  ? 293 LEU A N    1 
ATOM   2210  C CA   . LEU A 1 293 ? 31.261  51.606  54.187  1.00 7.35   ? 293 LEU A CA   1 
ATOM   2211  C C    . LEU A 1 293 ? 30.574  52.556  55.068  1.00 5.55   ? 293 LEU A C    1 
ATOM   2212  O O    . LEU A 1 293 ? 30.051  53.519  54.629  1.00 5.56   ? 293 LEU A O    1 
ATOM   2213  C CB   . LEU A 1 293 ? 30.402  50.370  54.032  1.00 7.27   ? 293 LEU A CB   1 
ATOM   2214  C CG   . LEU A 1 293 ? 30.838  49.124  53.276  1.00 7.92   ? 293 LEU A CG   1 
ATOM   2215  C CD1  . LEU A 1 293 ? 29.697  48.133  53.230  1.00 7.18   ? 293 LEU A CD1  1 
ATOM   2216  C CD2  . LEU A 1 293 ? 31.319  49.433  51.880  1.00 7.40   ? 293 LEU A CD2  1 
ATOM   2217  N N    . TYR A 1 294 ? 30.606  52.295  56.348  1.00 6.38   ? 294 TYR A N    1 
ATOM   2218  C CA   . TYR A 1 294 ? 29.987  53.145  57.327  1.00 7.45   ? 294 TYR A CA   1 
ATOM   2219  C C    . TYR A 1 294 ? 30.679  54.444  57.473  1.00 7.75   ? 294 TYR A C    1 
ATOM   2220  O O    . TYR A 1 294 ? 30.079  55.440  57.767  1.00 7.64   ? 294 TYR A O    1 
ATOM   2221  C CB   . TYR A 1 294 ? 30.008  52.426  58.645  1.00 8.66   ? 294 TYR A CB   1 
ATOM   2222  C CG   . TYR A 1 294 ? 28.759  51.688  58.988  1.00 8.82   ? 294 TYR A CG   1 
ATOM   2223  C CD1  . TYR A 1 294 ? 27.528  52.267  58.819  1.00 7.24   ? 294 TYR A CD1  1 
ATOM   2224  C CD2  . TYR A 1 294 ? 28.817  50.414  59.502  1.00 8.87   ? 294 TYR A CD2  1 
ATOM   2225  C CE1  . TYR A 1 294 ? 26.381  51.592  59.149  1.00 7.39   ? 294 TYR A CE1  1 
ATOM   2226  C CE2  . TYR A 1 294 ? 27.676  49.730  59.834  1.00 9.49   ? 294 TYR A CE2  1 
ATOM   2227  C CZ   . TYR A 1 294 ? 26.462  50.330  59.652  1.00 9.18   ? 294 TYR A CZ   1 
ATOM   2228  O OH   . TYR A 1 294 ? 25.322  49.663  59.969  1.00 10.72  ? 294 TYR A OH   1 
ATOM   2229  N N    . ALA A 1 295 ? 31.960  54.459  57.237  1.00 9.53   ? 295 ALA A N    1 
ATOM   2230  C CA   . ALA A 1 295 ? 32.712  55.676  57.281  1.00 10.82  ? 295 ALA A CA   1 
ATOM   2231  C C    . ALA A 1 295 ? 32.915  56.221  55.934  1.00 12.59  ? 295 ALA A C    1 
ATOM   2232  O O    . ALA A 1 295 ? 33.847  56.968  55.749  1.00 12.51  ? 295 ALA A O    1 
ATOM   2233  C CB   . ALA A 1 295 ? 34.055  55.393  57.849  1.00 9.66   ? 295 ALA A CB   1 
ATOM   2234  N N    . ASN A 1 296 ? 32.063  55.867  54.982  1.00 9.50   ? 296 ASN A N    1 
ATOM   2235  C CA   . ASN A 1 296 ? 32.218  56.277  53.603  1.00 8.43   ? 296 ASN A CA   1 
ATOM   2236  C C    . ASN A 1 296 ? 30.946  56.241  52.884  1.00 5.64   ? 296 ASN A C    1 
ATOM   2237  O O    . ASN A 1 296 ? 30.882  55.684  51.825  1.00 6.21   ? 296 ASN A O    1 
ATOM   2238  C CB   . ASN A 1 296 ? 33.192  55.413  52.859  1.00 10.82  ? 296 ASN A CB   1 
ATOM   2239  C CG   . ASN A 1 296 ? 34.644  55.723  53.191  1.00 10.73  ? 296 ASN A CG   1 
ATOM   2240  O OD1  . ASN A 1 296 ? 35.080  56.862  53.105  1.00 9.30   ? 296 ASN A OD1  1 
ATOM   2241  N ND2  . ASN A 1 296 ? 35.382  54.714  53.609  1.00 10.53  ? 296 ASN A ND2  1 
ATOM   2242  N N    . THR A 1 297 ? 29.937  56.894  53.433  1.00 4.84   ? 297 THR A N    1 
ATOM   2243  C CA   . THR A 1 297 ? 28.650  57.009  52.785  1.00 4.57   ? 297 THR A CA   1 
ATOM   2244  C C    . THR A 1 297 ? 28.549  58.305  51.999  1.00 4.85   ? 297 THR A C    1 
ATOM   2245  O O    . THR A 1 297 ? 28.611  59.353  52.573  1.00 5.04   ? 297 THR A O    1 
ATOM   2246  C CB   . THR A 1 297 ? 27.503  56.872  53.799  1.00 4.45   ? 297 THR A CB   1 
ATOM   2247  O OG1  . THR A 1 297 ? 27.808  55.847  54.743  1.00 5.53   ? 297 THR A OG1  1 
ATOM   2248  C CG2  . THR A 1 297 ? 26.192  56.549  53.118  1.00 3.32   ? 297 THR A CG2  1 
ATOM   2249  N N    . VAL A 1 298 ? 28.361  58.235  50.684  1.00 4.60   ? 298 VAL A N    1 
ATOM   2250  C CA   . VAL A 1 298 ? 28.308  59.407  49.830  1.00 4.39   ? 298 VAL A CA   1 
ATOM   2251  C C    . VAL A 1 298 ? 26.921  59.696  49.406  1.00 5.23   ? 298 VAL A C    1 
ATOM   2252  O O    . VAL A 1 298 ? 26.199  58.832  49.008  1.00 5.10   ? 298 VAL A O    1 
ATOM   2253  C CB   . VAL A 1 298 ? 29.253  59.313  48.616  1.00 4.22   ? 298 VAL A CB   1 
ATOM   2254  C CG1  . VAL A 1 298 ? 29.127  60.502  47.686  1.00 5.42   ? 298 VAL A CG1  1 
ATOM   2255  C CG2  . VAL A 1 298 ? 30.687  59.149  49.071  1.00 4.37   ? 298 VAL A CG2  1 
ATOM   2256  N N    . LEU A 1 299 ? 26.521  60.945  49.551  1.00 5.99   ? 299 LEU A N    1 
ATOM   2257  C CA   . LEU A 1 299 ? 25.220  61.372  49.173  1.00 6.32   ? 299 LEU A CA   1 
ATOM   2258  C C    . LEU A 1 299 ? 25.386  62.126  47.895  1.00 7.09   ? 299 LEU A C    1 
ATOM   2259  O O    . LEU A 1 299 ? 25.966  63.165  47.890  1.00 7.97   ? 299 LEU A O    1 
ATOM   2260  C CB   . LEU A 1 299 ? 24.651  62.205  50.271  1.00 6.68   ? 299 LEU A CB   1 
ATOM   2261  C CG   . LEU A 1 299 ? 23.679  61.497  51.218  1.00 7.28   ? 299 LEU A CG   1 
ATOM   2262  C CD1  . LEU A 1 299 ? 24.228  60.251  51.888  1.00 4.62   ? 299 LEU A CD1  1 
ATOM   2263  C CD2  . LEU A 1 299 ? 23.143  62.457  52.249  1.00 5.33   ? 299 LEU A CD2  1 
ATOM   2264  N N    . SER A 1 300 ? 24.953  61.544  46.782  1.00 8.44   ? 300 SER A N    1 
ATOM   2265  C CA   . SER A 1 300 ? 25.089  62.129  45.496  1.00 5.60   ? 300 SER A CA   1 
ATOM   2266  C C    . SER A 1 300 ? 23.760  62.116  44.946  1.00 6.13   ? 300 SER A C    1 
ATOM   2267  O O    . SER A 1 300 ? 22.954  61.336  45.339  1.00 7.26   ? 300 SER A O    1 
ATOM   2268  C CB   . SER A 1 300 ? 25.890  61.260  44.636  1.00 8.61   ? 300 SER A CB   1 
ATOM   2269  O OG   . SER A 1 300 ? 25.729  61.642  43.288  1.00 12.59  ? 300 SER A OG   1 
ATOM   2270  N N    . GLY A 1 301 ? 23.500  63.018  44.046  1.00 7.17   ? 301 GLY A N    1 
ATOM   2271  C CA   . GLY A 1 301 ? 22.200  63.145  43.497  1.00 7.56   ? 301 GLY A CA   1 
ATOM   2272  C C    . GLY A 1 301 ? 21.560  64.466  43.684  1.00 7.12   ? 301 GLY A C    1 
ATOM   2273  O O    . GLY A 1 301 ? 22.057  65.308  44.377  1.00 6.68   ? 301 GLY A O    1 
ATOM   2274  N N    . GLY A 1 302 ? 20.445  64.632  43.020  1.00 7.26   ? 302 GLY A N    1 
ATOM   2275  C CA   . GLY A 1 302 ? 19.695  65.840  43.135  1.00 8.43   ? 302 GLY A CA   1 
ATOM   2276  C C    . GLY A 1 302 ? 18.645  65.842  44.200  1.00 10.34  ? 302 GLY A C    1 
ATOM   2277  O O    . GLY A 1 302 ? 18.165  66.900  44.575  1.00 11.55  ? 302 GLY A O    1 
ATOM   2278  N N    . THR A 1 303 ? 18.276  64.668  44.685  1.00 8.04   ? 303 THR A N    1 
ATOM   2279  C CA   . THR A 1 303 ? 17.337  64.606  45.758  1.00 8.35   ? 303 THR A CA   1 
ATOM   2280  C C    . THR A 1 303 ? 18.093  64.432  47.055  1.00 9.45   ? 303 THR A C    1 
ATOM   2281  O O    . THR A 1 303 ? 17.546  64.561  48.125  1.00 11.47  ? 303 THR A O    1 
ATOM   2282  C CB   . THR A 1 303 ? 16.198  63.635  45.418  1.00 7.40   ? 303 THR A CB   1 
ATOM   2283  O OG1  . THR A 1 303 ? 15.460  64.165  44.315  1.00 9.29   ? 303 THR A OG1  1 
ATOM   2284  C CG2  . THR A 1 303 ? 15.241  63.436  46.543  1.00 9.86   ? 303 THR A CG2  1 
ATOM   2285  N N    . THR A 1 304 ? 19.375  64.186  46.985  1.00 7.48   ? 304 THR A N    1 
ATOM   2286  C CA   . THR A 1 304 ? 20.163  64.149  48.176  1.00 8.70   ? 304 THR A CA   1 
ATOM   2287  C C    . THR A 1 304 ? 20.729  65.517  48.308  1.00 10.47  ? 304 THR A C    1 
ATOM   2288  O O    . THR A 1 304 ? 21.877  65.614  48.644  1.00 8.45   ? 304 THR A O    1 
ATOM   2289  C CB   . THR A 1 304 ? 21.335  63.252  48.009  1.00 8.41   ? 304 THR A CB   1 
ATOM   2290  O OG1  . THR A 1 304 ? 22.108  63.733  46.919  1.00 14.49  ? 304 THR A OG1  1 
ATOM   2291  C CG2  . THR A 1 304 ? 20.881  61.867  47.704  1.00 7.88   ? 304 THR A CG2  1 
ATOM   2292  N N    . MET A 1 305 ? 19.944  66.575  48.051  1.00 12.64  ? 305 MET A N    1 
ATOM   2293  C CA   . MET A 1 305 ? 20.423  67.955  48.046  1.00 13.04  ? 305 MET A CA   1 
ATOM   2294  C C    . MET A 1 305 ? 19.482  68.864  48.738  1.00 12.40  ? 305 MET A C    1 
ATOM   2295  O O    . MET A 1 305 ? 19.085  69.887  48.208  1.00 17.31  ? 305 MET A O    1 
ATOM   2296  C CB   . MET A 1 305 ? 20.621  68.481  46.617  1.00 8.68   ? 305 MET A CB   1 
ATOM   2297  C CG   . MET A 1 305 ? 21.968  68.246  45.987  1.00 7.63   ? 305 MET A CG   1 
ATOM   2298  S SD   . MET A 1 305 ? 23.030  69.644  46.302  1.00 14.18  ? 305 MET A SD   1 
ATOM   2299  C CE   . MET A 1 305 ? 22.043  70.956  45.618  1.00 25.71  ? 305 MET A CE   1 
ATOM   2300  N N    . TYR A 1 306 ? 19.111  68.496  49.931  1.00 9.57   ? 306 TYR A N    1 
ATOM   2301  C CA   . TYR A 1 306 ? 18.244  69.300  50.688  1.00 10.34  ? 306 TYR A CA   1 
ATOM   2302  C C    . TYR A 1 306 ? 19.060  69.589  51.895  1.00 13.00  ? 306 TYR A C    1 
ATOM   2303  O O    . TYR A 1 306 ? 19.612  68.700  52.486  1.00 13.13  ? 306 TYR A O    1 
ATOM   2304  C CB   . TYR A 1 306 ? 17.036  68.511  51.059  1.00 10.23  ? 306 TYR A CB   1 
ATOM   2305  C CG   . TYR A 1 306 ? 16.122  68.137  49.935  1.00 11.73  ? 306 TYR A CG   1 
ATOM   2306  C CD1  . TYR A 1 306 ? 15.340  69.088  49.311  1.00 11.96  ? 306 TYR A CD1  1 
ATOM   2307  C CD2  . TYR A 1 306 ? 16.011  66.827  49.519  1.00 11.25  ? 306 TYR A CD2  1 
ATOM   2308  C CE1  . TYR A 1 306 ? 14.489  68.745  48.289  1.00 13.11  ? 306 TYR A CE1  1 
ATOM   2309  C CE2  . TYR A 1 306 ? 15.167  66.480  48.496  1.00 10.93  ? 306 TYR A CE2  1 
ATOM   2310  C CZ   . TYR A 1 306 ? 14.411  67.445  47.887  1.00 12.96  ? 306 TYR A CZ   1 
ATOM   2311  O OH   . TYR A 1 306 ? 13.573  67.101  46.866  1.00 11.71  ? 306 TYR A OH   1 
ATOM   2312  N N    . PRO A 1 307 ? 19.137  70.846  52.285  1.00 15.80  ? 307 PRO A N    1 
ATOM   2313  C CA   . PRO A 1 307 ? 20.012  71.111  53.394  1.00 12.03  ? 307 PRO A CA   1 
ATOM   2314  C C    . PRO A 1 307 ? 19.563  70.306  54.577  1.00 21.17  ? 307 PRO A C    1 
ATOM   2315  O O    . PRO A 1 307 ? 18.402  70.372  54.907  1.00 34.81  ? 307 PRO A O    1 
ATOM   2316  C CB   . PRO A 1 307 ? 19.776  72.584  53.652  1.00 7.76   ? 307 PRO A CB   1 
ATOM   2317  C CG   . PRO A 1 307 ? 18.759  73.070  52.686  1.00 7.09   ? 307 PRO A CG   1 
ATOM   2318  C CD   . PRO A 1 307 ? 18.703  72.068  51.602  1.00 15.51  ? 307 PRO A CD   1 
ATOM   2319  N N    . GLY A 1 308 ? 20.454  69.593  55.252  1.00 23.89  ? 308 GLY A N    1 
ATOM   2320  C CA   . GLY A 1 308 ? 20.087  68.731  56.372  1.00 17.11  ? 308 GLY A CA   1 
ATOM   2321  C C    . GLY A 1 308 ? 19.853  67.275  56.146  1.00 15.02  ? 308 GLY A C    1 
ATOM   2322  O O    . GLY A 1 308 ? 19.575  66.568  57.088  1.00 15.40  ? 308 GLY A O    1 
ATOM   2323  N N    . ILE A 1 309 ? 19.929  66.832  54.910  1.00 13.15  ? 309 ILE A N    1 
ATOM   2324  C CA   . ILE A 1 309 ? 19.812  65.422  54.590  1.00 12.89  ? 309 ILE A CA   1 
ATOM   2325  C C    . ILE A 1 309 ? 21.036  64.707  55.105  1.00 17.46  ? 309 ILE A C    1 
ATOM   2326  O O    . ILE A 1 309 ? 20.983  63.534  55.407  1.00 18.49  ? 309 ILE A O    1 
ATOM   2327  C CB   . ILE A 1 309 ? 19.562  65.177  53.079  1.00 7.98   ? 309 ILE A CB   1 
ATOM   2328  C CG1  . ILE A 1 309 ? 19.067  63.764  52.829  1.00 7.05   ? 309 ILE A CG1  1 
ATOM   2329  C CG2  . ILE A 1 309 ? 20.799  65.481  52.257  1.00 10.72  ? 309 ILE A CG2  1 
ATOM   2330  C CD1  . ILE A 1 309 ? 18.334  63.625  51.524  1.00 11.33  ? 309 ILE A CD1  1 
ATOM   2331  N N    . ALA A 1 310 ? 22.150  65.405  55.206  1.00 15.21  ? 310 ALA A N    1 
ATOM   2332  C CA   . ALA A 1 310 ? 23.383  64.782  55.604  1.00 11.53  ? 310 ALA A CA   1 
ATOM   2333  C C    . ALA A 1 310 ? 23.506  64.438  57.036  1.00 12.81  ? 310 ALA A C    1 
ATOM   2334  O O    . ALA A 1 310 ? 24.002  63.391  57.369  1.00 17.77  ? 310 ALA A O    1 
ATOM   2335  C CB   . ALA A 1 310 ? 24.506  65.692  55.234  1.00 10.29  ? 310 ALA A CB   1 
ATOM   2336  N N    . ASP A 1 311 ? 23.107  65.330  57.896  1.00 13.39  ? 311 ASP A N    1 
ATOM   2337  C CA   . ASP A 1 311 ? 23.258  65.128  59.303  1.00 12.34  ? 311 ASP A CA   1 
ATOM   2338  C C    . ASP A 1 311 ? 22.178  64.243  59.809  1.00 11.97  ? 311 ASP A C    1 
ATOM   2339  O O    . ASP A 1 311 ? 22.290  63.690  60.876  1.00 11.83  ? 311 ASP A O    1 
ATOM   2340  C CB   . ASP A 1 311 ? 23.223  66.495  59.967  1.00 12.87  ? 311 ASP A CB   1 
ATOM   2341  C CG   . ASP A 1 311 ? 23.981  67.531  59.205  1.00 20.95  ? 311 ASP A CG   1 
ATOM   2342  O OD1  . ASP A 1 311 ? 25.217  67.422  59.134  1.00 25.99  ? 311 ASP A OD1  1 
ATOM   2343  O OD2  . ASP A 1 311 ? 23.345  68.461  58.683  1.00 30.99  ? 311 ASP A OD2  1 
ATOM   2344  N N    . ARG A 1 312 ? 21.121  64.102  59.048  1.00 12.81  ? 312 ARG A N    1 
ATOM   2345  C CA   . ARG A 1 312 ? 20.009  63.255  59.408  1.00 10.18  ? 312 ARG A CA   1 
ATOM   2346  C C    . ARG A 1 312 ? 20.367  61.849  59.135  1.00 11.56  ? 312 ARG A C    1 
ATOM   2347  O O    . ARG A 1 312 ? 19.969  60.999  59.837  1.00 7.60   ? 312 ARG A O    1 
ATOM   2348  C CB   . ARG A 1 312 ? 18.858  63.635  58.548  1.00 8.97   ? 312 ARG A CB   1 
ATOM   2349  C CG   . ARG A 1 312 ? 17.640  62.805  58.715  1.00 8.82   ? 312 ARG A CG   1 
ATOM   2350  C CD   . ARG A 1 312 ? 17.016  63.108  60.038  1.00 12.14  ? 312 ARG A CD   1 
ATOM   2351  N NE   . ARG A 1 312 ? 15.836  62.311  60.182  1.00 9.57   ? 312 ARG A NE   1 
ATOM   2352  C CZ   . ARG A 1 312 ? 14.665  62.626  59.676  1.00 10.00  ? 312 ARG A CZ   1 
ATOM   2353  N NH1  . ARG A 1 312 ? 14.514  63.749  59.009  1.00 8.97   ? 312 ARG A NH1  1 
ATOM   2354  N NH2  . ARG A 1 312 ? 13.651  61.809  59.855  1.00 12.97  ? 312 ARG A NH2  1 
ATOM   2355  N N    . MET A 1 313 ? 21.234  61.607  58.175  1.00 15.10  ? 313 MET A N    1 
ATOM   2356  C CA   . MET A 1 313 ? 21.685  60.269  57.881  1.00 11.55  ? 313 MET A CA   1 
ATOM   2357  C C    . MET A 1 313 ? 22.531  59.802  58.994  1.00 8.35   ? 313 MET A C    1 
ATOM   2358  O O    . MET A 1 313 ? 22.431  58.726  59.391  1.00 6.75   ? 313 MET A O    1 
ATOM   2359  C CB   . MET A 1 313 ? 22.437  60.213  56.574  1.00 7.27   ? 313 MET A CB   1 
ATOM   2360  C CG   . MET A 1 313 ? 21.576  60.327  55.337  1.00 13.57  ? 313 MET A CG   1 
ATOM   2361  S SD   . MET A 1 313 ? 20.433  58.975  55.086  1.00 19.02  ? 313 MET A SD   1 
ATOM   2362  C CE   . MET A 1 313 ? 21.447  57.894  54.108  1.00 20.39  ? 313 MET A CE   1 
ATOM   2363  N N    . GLN A 1 314 ? 23.306  60.650  59.588  1.00 7.80   ? 314 GLN A N    1 
ATOM   2364  C CA   . GLN A 1 314 ? 24.090  60.278  60.728  1.00 8.84   ? 314 GLN A CA   1 
ATOM   2365  C C    . GLN A 1 314 ? 23.222  59.910  61.884  1.00 10.19  ? 314 GLN A C    1 
ATOM   2366  O O    . GLN A 1 314 ? 23.383  58.874  62.440  1.00 9.99   ? 314 GLN A O    1 
ATOM   2367  C CB   . GLN A 1 314 ? 24.993  61.422  61.111  1.00 7.01   ? 314 GLN A CB   1 
ATOM   2368  C CG   . GLN A 1 314 ? 25.989  61.113  62.199  1.00 8.43   ? 314 GLN A CG   1 
ATOM   2369  C CD   . GLN A 1 314 ? 27.372  60.915  61.657  1.00 8.24   ? 314 GLN A CD   1 
ATOM   2370  O OE1  . GLN A 1 314 ? 27.622  61.123  60.477  1.00 8.86   ? 314 GLN A OE1  1 
ATOM   2371  N NE2  . GLN A 1 314 ? 28.282  60.508  62.518  1.00 9.20   ? 314 GLN A NE2  1 
ATOM   2372  N N    . LYS A 1 315 ? 22.263  60.729  62.257  1.00 9.46   ? 315 LYS A N    1 
ATOM   2373  C CA   . LYS A 1 315 ? 21.337  60.383  63.317  1.00 7.57   ? 315 LYS A CA   1 
ATOM   2374  C C    . LYS A 1 315 ? 20.760  59.073  63.067  1.00 8.91   ? 315 LYS A C    1 
ATOM   2375  O O    . LYS A 1 315 ? 20.865  58.211  63.896  1.00 10.82  ? 315 LYS A O    1 
ATOM   2376  C CB   . LYS A 1 315 ? 20.179  61.351  63.335  1.00 7.69   ? 315 LYS A CB   1 
ATOM   2377  C CG   . LYS A 1 315 ? 19.418  61.382  64.642  1.00 8.14   ? 315 LYS A CG   1 
ATOM   2378  C CD   . LYS A 1 315 ? 18.588  62.639  64.775  1.00 9.05   ? 315 LYS A CD   1 
ATOM   2379  C CE   . LYS A 1 315 ? 18.201  62.856  66.226  1.00 25.39  ? 315 LYS A CE   1 
ATOM   2380  N NZ   . LYS A 1 315 ? 17.425  64.106  66.454  1.00 20.58  ? 315 LYS A NZ   1 
ATOM   2381  N N    . GLU A 1 316 ? 20.102  58.917  61.935  1.00 8.49   ? 316 GLU A N    1 
ATOM   2382  C CA   . GLU A 1 316 ? 19.418  57.683  61.588  1.00 5.22   ? 316 GLU A CA   1 
ATOM   2383  C C    . GLU A 1 316 ? 20.219  56.454  61.383  1.00 4.55   ? 316 GLU A C    1 
ATOM   2384  O O    . GLU A 1 316 ? 19.778  55.400  61.730  1.00 6.25   ? 316 GLU A O    1 
ATOM   2385  C CB   . GLU A 1 316 ? 18.568  57.966  60.398  1.00 4.96   ? 316 GLU A CB   1 
ATOM   2386  C CG   . GLU A 1 316 ? 17.630  59.154  60.557  1.00 6.20   ? 316 GLU A CG   1 
ATOM   2387  C CD   . GLU A 1 316 ? 16.403  58.903  61.415  1.00 6.60   ? 316 GLU A CD   1 
ATOM   2388  O OE1  . GLU A 1 316 ? 16.351  57.931  62.184  1.00 8.11   ? 316 GLU A OE1  1 
ATOM   2389  O OE2  . GLU A 1 316 ? 15.466  59.701  61.313  1.00 5.19   ? 316 GLU A OE2  1 
ATOM   2390  N N    . ILE A 1 317 ? 21.346  56.555  60.730  1.00 5.53   ? 317 ILE A N    1 
ATOM   2391  C CA   . ILE A 1 317 ? 22.258  55.442  60.571  1.00 5.64   ? 317 ILE A CA   1 
ATOM   2392  C C    . ILE A 1 317 ? 22.974  55.075  61.847  1.00 8.46   ? 317 ILE A C    1 
ATOM   2393  O O    . ILE A 1 317 ? 23.217  53.925  62.082  1.00 12.13  ? 317 ILE A O    1 
ATOM   2394  C CB   . ILE A 1 317 ? 23.206  55.682  59.387  1.00 0.82   ? 317 ILE A CB   1 
ATOM   2395  C CG1  . ILE A 1 317 ? 22.396  55.864  58.113  1.00 6.05   ? 317 ILE A CG1  1 
ATOM   2396  C CG2  . ILE A 1 317 ? 24.150  54.522  59.195  1.00 4.73   ? 317 ILE A CG2  1 
ATOM   2397  C CD1  . ILE A 1 317 ? 23.235  55.954  56.869  1.00 6.04   ? 317 ILE A CD1  1 
ATOM   2398  N N    . THR A 1 318 ? 23.267  56.030  62.717  1.00 7.37   ? 318 THR A N    1 
ATOM   2399  C CA   . THR A 1 318 ? 24.064  55.773  63.892  1.00 6.55   ? 318 THR A CA   1 
ATOM   2400  C C    . THR A 1 318 ? 23.241  55.239  64.980  1.00 10.06  ? 318 THR A C    1 
ATOM   2401  O O    . THR A 1 318 ? 23.717  54.954  66.050  1.00 26.28  ? 318 THR A O    1 
ATOM   2402  C CB   . THR A 1 318 ? 24.809  57.022  64.324  1.00 7.45   ? 318 THR A CB   1 
ATOM   2403  O OG1  . THR A 1 318 ? 25.384  57.646  63.182  1.00 13.20  ? 318 THR A OG1  1 
ATOM   2404  C CG2  . THR A 1 318 ? 25.958  56.706  65.253  1.00 10.21  ? 318 THR A CG2  1 
ATOM   2405  N N    . ALA A 1 319 ? 22.005  54.969  64.695  1.00 8.87   ? 319 ALA A N    1 
ATOM   2406  C CA   . ALA A 1 319 ? 21.125  54.460  65.680  1.00 6.96   ? 319 ALA A CA   1 
ATOM   2407  C C    . ALA A 1 319 ? 20.655  53.133  65.207  1.00 8.84   ? 319 ALA A C    1 
ATOM   2408  O O    . ALA A 1 319 ? 20.090  52.373  65.961  1.00 14.79  ? 319 ALA A O    1 
ATOM   2409  C CB   . ALA A 1 319 ? 19.987  55.411  65.833  1.00 5.37   ? 319 ALA A CB   1 
ATOM   2410  N N    . LEU A 1 320 ? 20.859  52.837  63.945  1.00 7.41   ? 320 LEU A N    1 
ATOM   2411  C CA   . LEU A 1 320 ? 20.519  51.527  63.424  1.00 11.20  ? 320 LEU A CA   1 
ATOM   2412  C C    . LEU A 1 320 ? 21.772  50.732  63.331  1.00 11.52  ? 320 LEU A C    1 
ATOM   2413  O O    . LEU A 1 320 ? 21.718  49.578  63.000  1.00 10.72  ? 320 LEU A O    1 
ATOM   2414  C CB   . LEU A 1 320 ? 19.863  51.627  62.060  1.00 9.12   ? 320 LEU A CB   1 
ATOM   2415  C CG   . LEU A 1 320 ? 18.502  52.290  61.901  1.00 9.02   ? 320 LEU A CG   1 
ATOM   2416  C CD1  . LEU A 1 320 ? 18.232  52.594  60.444  1.00 6.35   ? 320 LEU A CD1  1 
ATOM   2417  C CD2  . LEU A 1 320 ? 17.417  51.396  62.463  1.00 14.08  ? 320 LEU A CD2  1 
ATOM   2418  N N    . ALA A 1 321 ? 22.881  51.300  63.750  1.00 9.92   ? 321 ALA A N    1 
ATOM   2419  C CA   . ALA A 1 321 ? 24.168  50.674  63.593  1.00 9.60   ? 321 ALA A CA   1 
ATOM   2420  C C    . ALA A 1 321 ? 24.886  50.331  64.825  1.00 14.12  ? 321 ALA A C    1 
ATOM   2421  O O    . ALA A 1 321 ? 24.616  50.905  65.872  1.00 16.35  ? 321 ALA A O    1 
ATOM   2422  C CB   . ALA A 1 321 ? 25.051  51.628  62.871  1.00 9.02   ? 321 ALA A CB   1 
ATOM   2423  N N    . PRO A 1 322 ? 25.848  49.407  64.704  1.00 11.72  ? 322 PRO A N    1 
ATOM   2424  C CA   . PRO A 1 322 ? 26.685  49.107  65.852  1.00 17.27  ? 322 PRO A CA   1 
ATOM   2425  C C    . PRO A 1 322 ? 27.373  50.383  66.360  1.00 25.60  ? 322 PRO A C    1 
ATOM   2426  O O    . PRO A 1 322 ? 27.847  51.121  65.523  1.00 28.99  ? 322 PRO A O    1 
ATOM   2427  C CB   . PRO A 1 322 ? 27.655  48.145  65.248  1.00 14.15  ? 322 PRO A CB   1 
ATOM   2428  C CG   . PRO A 1 322 ? 26.811  47.333  64.341  1.00 12.92  ? 322 PRO A CG   1 
ATOM   2429  C CD   . PRO A 1 322 ? 25.883  48.322  63.716  1.00 11.53  ? 322 PRO A CD   1 
ATOM   2430  N N    . SER A 1 323 ? 27.466  50.637  67.665  1.00 18.84  ? 323 SER A N    1 
ATOM   2431  C CA   . SER A 1 323 ? 27.954  51.921  68.199  1.00 17.23  ? 323 SER A CA   1 
ATOM   2432  C C    . SER A 1 323 ? 29.399  52.145  68.098  1.00 20.33  ? 323 SER A C    1 
ATOM   2433  O O    . SER A 1 323 ? 29.903  53.191  68.452  1.00 23.53  ? 323 SER A O    1 
ATOM   2434  C CB   . SER A 1 323 ? 27.554  52.084  69.653  1.00 18.46  ? 323 SER A CB   1 
ATOM   2435  O OG   . SER A 1 323 ? 27.776  53.405  70.100  1.00 23.52  ? 323 SER A OG   1 
ATOM   2436  N N    . THR A 1 324 ? 30.099  51.133  67.681  1.00 23.95  ? 324 THR A N    1 
ATOM   2437  C CA   . THR A 1 324 ? 31.519  51.217  67.550  1.00 25.44  ? 324 THR A CA   1 
ATOM   2438  C C    . THR A 1 324 ? 31.841  51.612  66.127  1.00 28.61  ? 324 THR A C    1 
ATOM   2439  O O    . THR A 1 324 ? 32.997  51.611  65.724  1.00 32.03  ? 324 THR A O    1 
ATOM   2440  C CB   . THR A 1 324 ? 32.102  49.842  67.840  1.00 25.25  ? 324 THR A CB   1 
ATOM   2441  O OG1  . THR A 1 324 ? 31.493  48.874  66.977  1.00 24.05  ? 324 THR A OG1  1 
ATOM   2442  C CG2  . THR A 1 324 ? 31.835  49.458  69.276  1.00 19.84  ? 324 THR A CG2  1 
ATOM   2443  N N    . MET A 1 325 ? 30.819  51.942  65.354  1.00 22.16  ? 325 MET A N    1 
ATOM   2444  C CA   . MET A 1 325 ? 31.027  52.222  63.969  1.00 21.75  ? 325 MET A CA   1 
ATOM   2445  C C    . MET A 1 325 ? 30.964  53.676  63.766  1.00 19.39  ? 325 MET A C    1 
ATOM   2446  O O    . MET A 1 325 ? 30.046  54.334  64.204  1.00 14.77  ? 325 MET A O    1 
ATOM   2447  C CB   . MET A 1 325 ? 30.001  51.517  63.115  1.00 18.95  ? 325 MET A CB   1 
ATOM   2448  C CG   . MET A 1 325 ? 30.221  50.032  62.959  1.00 22.74  ? 325 MET A CG   1 
ATOM   2449  S SD   . MET A 1 325 ? 31.626  49.669  61.913  1.00 28.09  ? 325 MET A SD   1 
ATOM   2450  C CE   . MET A 1 325 ? 31.675  47.893  62.051  1.00 19.13  ? 325 MET A CE   1 
ATOM   2451  N N    . LYS A 1 326 ? 31.958  54.150  63.044  1.00 17.32  ? 326 LYS A N    1 
ATOM   2452  C CA   . LYS A 1 326 ? 32.068  55.524  62.768  1.00 14.45  ? 326 LYS A CA   1 
ATOM   2453  C C    . LYS A 1 326 ? 31.200  55.644  61.591  1.00 12.77  ? 326 LYS A C    1 
ATOM   2454  O O    . LYS A 1 326 ? 31.215  54.808  60.715  1.00 13.79  ? 326 LYS A O    1 
ATOM   2455  C CB   . LYS A 1 326 ? 33.496  55.780  62.353  1.00 13.44  ? 326 LYS A CB   1 
ATOM   2456  C CG   . LYS A 1 326 ? 34.512  54.948  63.111  1.00 18.04  ? 326 LYS A CG   1 
ATOM   2457  C CD   . LYS A 1 326 ? 35.623  54.474  62.194  1.00 21.27  ? 326 LYS A CD   1 
ATOM   2458  C CE   . LYS A 1 326 ? 35.183  53.303  61.332  1.00 25.26  ? 326 LYS A CE   1 
ATOM   2459  N NZ   . LYS A 1 326 ? 35.052  52.047  62.116  1.00 27.90  ? 326 LYS A NZ   1 
ATOM   2460  N N    . ILE A 1 327 ? 30.410  56.689  61.579  1.00 11.88  ? 327 ILE A N    1 
ATOM   2461  C CA   . ILE A 1 327 ? 29.581  56.880  60.461  1.00 11.79  ? 327 ILE A CA   1 
ATOM   2462  C C    . ILE A 1 327 ? 30.101  58.180  59.936  1.00 13.22  ? 327 ILE A C    1 
ATOM   2463  O O    . ILE A 1 327 ? 30.274  59.114  60.698  1.00 10.04  ? 327 ILE A O    1 
ATOM   2464  C CB   . ILE A 1 327 ? 28.105  56.950  60.941  1.00 7.47   ? 327 ILE A CB   1 
ATOM   2465  C CG1  . ILE A 1 327 ? 27.820  55.871  61.972  1.00 9.07   ? 327 ILE A CG1  1 
ATOM   2466  C CG2  . ILE A 1 327 ? 27.142  56.854  59.775  1.00 7.68   ? 327 ILE A CG2  1 
ATOM   2467  C CD1  . ILE A 1 327 ? 27.298  54.590  61.389  1.00 12.01  ? 327 ILE A CD1  1 
ATOM   2468  N N    . LYS A 1 328 ? 30.381  58.239  58.642  1.00 13.77  ? 328 LYS A N    1 
ATOM   2469  C CA   . LYS A 1 328 ? 30.796  59.454  58.022  1.00 9.81   ? 328 LYS A CA   1 
ATOM   2470  C C    . LYS A 1 328 ? 29.994  59.626  56.827  1.00 7.89   ? 328 LYS A C    1 
ATOM   2471  O O    . LYS A 1 328 ? 30.210  58.954  55.864  1.00 10.98  ? 328 LYS A O    1 
ATOM   2472  C CB   . LYS A 1 328 ? 32.257  59.443  57.633  1.00 6.82   ? 328 LYS A CB   1 
ATOM   2473  C CG   . LYS A 1 328 ? 32.860  60.809  57.389  1.00 7.94   ? 328 LYS A CG   1 
ATOM   2474  C CD   . LYS A 1 328 ? 34.248  60.693  56.793  1.00 7.95   ? 328 LYS A CD   1 
ATOM   2475  C CE   . LYS A 1 328 ? 34.651  61.994  56.127  1.00 12.93  ? 328 LYS A CE   1 
ATOM   2476  N NZ   . LYS A 1 328 ? 36.043  61.970  55.610  1.00 11.98  ? 328 LYS A NZ   1 
ATOM   2477  N N    . ILE A 1 329 ? 29.043  60.530  56.876  1.00 6.47   ? 329 ILE A N    1 
ATOM   2478  C CA   . ILE A 1 329 ? 28.281  60.873  55.710  1.00 6.95   ? 329 ILE A CA   1 
ATOM   2479  C C    . ILE A 1 329 ? 29.016  61.968  54.923  1.00 7.96   ? 329 ILE A C    1 
ATOM   2480  O O    . ILE A 1 329 ? 29.452  62.959  55.489  1.00 8.19   ? 329 ILE A O    1 
ATOM   2481  C CB   . ILE A 1 329 ? 26.864  61.277  56.120  1.00 7.20   ? 329 ILE A CB   1 
ATOM   2482  C CG1  . ILE A 1 329 ? 26.296  60.267  57.116  1.00 8.86   ? 329 ILE A CG1  1 
ATOM   2483  C CG2  . ILE A 1 329 ? 25.968  61.442  54.913  1.00 7.31   ? 329 ILE A CG2  1 
ATOM   2484  C CD1  . ILE A 1 329 ? 25.946  58.929  56.520  1.00 8.10   ? 329 ILE A CD1  1 
ATOM   2485  N N    . ILE A 1 330 ? 29.211  61.782  53.622  1.00 6.75   ? 330 ILE A N    1 
ATOM   2486  C CA   . ILE A 1 330 ? 29.988  62.718  52.800  1.00 6.46   ? 330 ILE A CA   1 
ATOM   2487  C C    . ILE A 1 330 ? 29.125  63.304  51.742  1.00 6.71   ? 330 ILE A C    1 
ATOM   2488  O O    . ILE A 1 330 ? 28.755  62.662  50.805  1.00 6.09   ? 330 ILE A O    1 
ATOM   2489  C CB   . ILE A 1 330 ? 31.207  62.032  52.172  1.00 5.80   ? 330 ILE A CB   1 
ATOM   2490  C CG1  . ILE A 1 330 ? 32.036  61.334  53.230  1.00 6.25   ? 330 ILE A CG1  1 
ATOM   2491  C CG2  . ILE A 1 330 ? 32.072  63.037  51.436  1.00 7.75   ? 330 ILE A CG2  1 
ATOM   2492  C CD1  . ILE A 1 330 ? 32.257  59.888  52.927  1.00 6.44   ? 330 ILE A CD1  1 
ATOM   2493  N N    . ALA A 1 331 ? 28.790  64.556  51.901  1.00 6.55   ? 331 ALA A N    1 
ATOM   2494  C CA   . ALA A 1 331 ? 27.911  65.199  51.005  1.00 8.55   ? 331 ALA A CA   1 
ATOM   2495  C C    . ALA A 1 331 ? 28.672  66.295  50.411  1.00 10.01  ? 331 ALA A C    1 
ATOM   2496  O O    . ALA A 1 331 ? 28.802  67.334  51.012  1.00 11.66  ? 331 ALA A O    1 
ATOM   2497  C CB   . ALA A 1 331 ? 26.785  65.750  51.779  1.00 7.11   ? 331 ALA A CB   1 
ATOM   2498  N N    . PRO A 1 332 ? 29.207  66.042  49.168  1.00 10.46  ? 332 PRO A N    1 
ATOM   2499  C CA   . PRO A 1 332 ? 29.997  67.082  48.608  1.00 12.68  ? 332 PRO A CA   1 
ATOM   2500  C C    . PRO A 1 332 ? 29.082  68.172  48.280  1.00 15.47  ? 332 PRO A C    1 
ATOM   2501  O O    . PRO A 1 332 ? 28.020  67.932  47.814  1.00 18.76  ? 332 PRO A O    1 
ATOM   2502  C CB   . PRO A 1 332 ? 30.435  66.458  47.326  1.00 14.78  ? 332 PRO A CB   1 
ATOM   2503  C CG   . PRO A 1 332 ? 30.586  65.037  47.611  1.00 15.45  ? 332 PRO A CG   1 
ATOM   2504  C CD   . PRO A 1 332 ? 29.267  64.874  48.236  1.00 12.19  ? 332 PRO A CD   1 
ATOM   2505  N N    . PRO A 1 333 ? 29.498  69.447  48.485  1.00 18.22  ? 333 PRO A N    1 
ATOM   2506  C CA   . PRO A 1 333 ? 28.556  70.446  48.033  1.00 15.70  ? 333 PRO A CA   1 
ATOM   2507  C C    . PRO A 1 333 ? 28.279  70.278  46.569  1.00 23.56  ? 333 PRO A C    1 
ATOM   2508  O O    . PRO A 1 333 ? 27.285  70.814  46.103  1.00 29.43  ? 333 PRO A O    1 
ATOM   2509  C CB   . PRO A 1 333 ? 29.339  71.704  48.219  1.00 12.95  ? 333 PRO A CB   1 
ATOM   2510  C CG   . PRO A 1 333 ? 30.096  71.478  49.451  1.00 19.64  ? 333 PRO A CG   1 
ATOM   2511  C CD   . PRO A 1 333 ? 30.626  70.120  49.192  1.00 21.41  ? 333 PRO A CD   1 
ATOM   2512  N N    . GLU A 1 334 ? 29.108  69.527  45.845  1.00 23.72  ? 334 GLU A N    1 
ATOM   2513  C CA   . GLU A 1 334 ? 28.947  69.304  44.394  1.00 18.83  ? 334 GLU A CA   1 
ATOM   2514  C C    . GLU A 1 334 ? 28.191  68.018  44.179  1.00 21.32  ? 334 GLU A C    1 
ATOM   2515  O O    . GLU A 1 334 ? 28.548  67.243  43.317  1.00 15.42  ? 334 GLU A O    1 
ATOM   2516  C CB   . GLU A 1 334 ? 30.299  69.411  43.710  1.00 14.02  ? 334 GLU A CB   1 
ATOM   2517  C CG   . GLU A 1 334 ? 31.411  68.522  44.256  1.00 28.23  ? 334 GLU A CG   1 
ATOM   2518  C CD   . GLU A 1 334 ? 32.297  69.210  45.265  1.00 35.57  ? 334 GLU A CD   1 
ATOM   2519  O OE1  . GLU A 1 334 ? 32.098  70.413  45.497  1.00 43.84  ? 334 GLU A OE1  1 
ATOM   2520  O OE2  . GLU A 1 334 ? 33.184  68.540  45.831  1.00 27.45  ? 334 GLU A OE2  1 
ATOM   2521  N N    . ARG A 1 335 ? 27.104  67.815  44.933  1.00 22.18  ? 335 ARG A N    1 
ATOM   2522  C CA   . ARG A 1 335 ? 26.318  66.593  44.858  1.00 10.75  ? 335 ARG A CA   1 
ATOM   2523  C C    . ARG A 1 335 ? 25.492  66.351  43.666  1.00 8.61   ? 335 ARG A C    1 
ATOM   2524  O O    . ARG A 1 335 ? 25.497  65.292  43.102  1.00 10.66  ? 335 ARG A O    1 
ATOM   2525  C CB   . ARG A 1 335 ? 25.512  66.383  46.137  1.00 9.24   ? 335 ARG A CB   1 
ATOM   2526  C CG   . ARG A 1 335 ? 26.229  66.135  47.419  1.00 14.11  ? 335 ARG A CG   1 
ATOM   2527  C CD   . ARG A 1 335 ? 25.225  66.135  48.549  1.00 9.67   ? 335 ARG A CD   1 
ATOM   2528  N NE   . ARG A 1 335 ? 24.579  67.422  48.720  1.00 8.57   ? 335 ARG A NE   1 
ATOM   2529  C CZ   . ARG A 1 335 ? 23.665  67.683  49.636  1.00 10.93  ? 335 ARG A CZ   1 
ATOM   2530  N NH1  . ARG A 1 335 ? 23.278  66.740  50.474  1.00 16.48  ? 335 ARG A NH1  1 
ATOM   2531  N NH2  . ARG A 1 335 ? 23.131  68.890  49.712  1.00 15.65  ? 335 ARG A NH2  1 
ATOM   2532  N N    . LYS A 1 336 ? 24.862  67.386  43.185  1.00 7.57   ? 336 LYS A N    1 
ATOM   2533  C CA   . LYS A 1 336 ? 23.970  67.213  42.059  1.00 9.44   ? 336 LYS A CA   1 
ATOM   2534  C C    . LYS A 1 336 ? 24.538  66.616  40.837  1.00 9.72   ? 336 LYS A C    1 
ATOM   2535  O O    . LYS A 1 336 ? 23.848  65.915  40.139  1.00 17.30  ? 336 LYS A O    1 
ATOM   2536  C CB   . LYS A 1 336 ? 23.289  68.541  41.775  1.00 10.79  ? 336 LYS A CB   1 
ATOM   2537  C CG   . LYS A 1 336 ? 21.876  68.446  41.258  1.00 11.44  ? 336 LYS A CG   1 
ATOM   2538  C CD   . LYS A 1 336 ? 21.206  69.800  41.317  1.00 11.14  ? 336 LYS A CD   1 
ATOM   2539  C CE   . LYS A 1 336 ? 20.333  69.922  42.551  1.00 18.00  ? 336 LYS A CE   1 
ATOM   2540  N NZ   . LYS A 1 336 ? 18.891  69.717  42.260  1.00 19.07  ? 336 LYS A NZ   1 
ATOM   2541  N N    . TYR A 1 337 ? 25.798  66.876  40.562  1.00 7.50   ? 337 TYR A N    1 
ATOM   2542  C CA   . TYR A 1 337 ? 26.438  66.385  39.375  1.00 9.06   ? 337 TYR A CA   1 
ATOM   2543  C C    . TYR A 1 337 ? 27.771  65.831  39.779  1.00 13.76  ? 337 TYR A C    1 
ATOM   2544  O O    . TYR A 1 337 ? 28.770  66.404  39.467  1.00 12.61  ? 337 TYR A O    1 
ATOM   2545  C CB   . TYR A 1 337 ? 26.668  67.508  38.395  1.00 7.28   ? 337 TYR A CB   1 
ATOM   2546  C CG   . TYR A 1 337 ? 25.515  68.387  37.990  1.00 6.77   ? 337 TYR A CG   1 
ATOM   2547  C CD1  . TYR A 1 337 ? 24.313  67.862  37.606  1.00 11.45  ? 337 TYR A CD1  1 
ATOM   2548  C CD2  . TYR A 1 337 ? 25.665  69.752  37.944  1.00 4.80   ? 337 TYR A CD2  1 
ATOM   2549  C CE1  . TYR A 1 337 ? 23.268  68.671  37.230  1.00 9.42   ? 337 TYR A CE1  1 
ATOM   2550  C CE2  . TYR A 1 337 ? 24.630  70.566  37.562  1.00 4.69   ? 337 TYR A CE2  1 
ATOM   2551  C CZ   . TYR A 1 337 ? 23.436  70.016  37.204  1.00 4.72   ? 337 TYR A CZ   1 
ATOM   2552  O OH   . TYR A 1 337 ? 22.397  70.818  36.823  1.00 3.07   ? 337 TYR A OH   1 
ATOM   2553  N N    . SER A 1 338 ? 27.804  64.695  40.473  1.00 14.23  ? 338 SER A N    1 
ATOM   2554  C CA   . SER A 1 338 ? 29.029  64.114  41.007  1.00 10.99  ? 338 SER A CA   1 
ATOM   2555  C C    . SER A 1 338 ? 29.271  62.945  40.217  1.00 11.61  ? 338 SER A C    1 
ATOM   2556  O O    . SER A 1 338 ? 30.361  62.422  40.214  1.00 10.49  ? 338 SER A O    1 
ATOM   2557  C CB   . SER A 1 338 ? 28.804  63.661  42.438  1.00 9.88   ? 338 SER A CB   1 
ATOM   2558  O OG   . SER A 1 338 ? 28.536  64.737  43.316  1.00 17.14  ? 338 SER A OG   1 
ATOM   2559  N N    . VAL A 1 339 ? 28.244  62.530  39.494  1.00 15.02  ? 339 VAL A N    1 
ATOM   2560  C CA   . VAL A 1 339 ? 28.364  61.364  38.633  1.00 12.99  ? 339 VAL A CA   1 
ATOM   2561  C C    . VAL A 1 339 ? 29.057  61.842  37.399  1.00 11.21  ? 339 VAL A C    1 
ATOM   2562  O O    . VAL A 1 339 ? 29.915  61.171  36.865  1.00 11.32  ? 339 VAL A O    1 
ATOM   2563  C CB   . VAL A 1 339 ? 27.037  60.717  38.313  1.00 7.36   ? 339 VAL A CB   1 
ATOM   2564  C CG1  . VAL A 1 339 ? 27.246  59.482  37.493  1.00 6.88   ? 339 VAL A CG1  1 
ATOM   2565  C CG2  . VAL A 1 339 ? 26.223  60.461  39.555  1.00 7.45   ? 339 VAL A CG2  1 
ATOM   2566  N N    . TRP A 1 340 ? 28.742  63.056  36.974  1.00 9.90   ? 340 TRP A N    1 
ATOM   2567  C CA   . TRP A 1 340 ? 29.384  63.633  35.812  1.00 10.79  ? 340 TRP A CA   1 
ATOM   2568  C C    . TRP A 1 340 ? 30.814  63.965  36.110  1.00 9.75   ? 340 TRP A C    1 
ATOM   2569  O O    . TRP A 1 340 ? 31.676  63.569  35.386  1.00 9.73   ? 340 TRP A O    1 
ATOM   2570  C CB   . TRP A 1 340 ? 28.619  64.850  35.382  1.00 8.88   ? 340 TRP A CB   1 
ATOM   2571  C CG   . TRP A 1 340 ? 28.997  65.376  34.096  1.00 10.25  ? 340 TRP A CG   1 
ATOM   2572  C CD1  . TRP A 1 340 ? 28.448  65.064  32.917  1.00 12.29  ? 340 TRP A CD1  1 
ATOM   2573  C CD2  . TRP A 1 340 ? 30.018  66.343  33.832  1.00 13.15  ? 340 TRP A CD2  1 
ATOM   2574  N NE1  . TRP A 1 340 ? 29.059  65.764  31.921  1.00 20.28  ? 340 TRP A NE1  1 
ATOM   2575  C CE2  . TRP A 1 340 ? 30.029  66.560  32.462  1.00 13.92  ? 340 TRP A CE2  1 
ATOM   2576  C CE3  . TRP A 1 340 ? 30.919  67.045  34.627  1.00 14.97  ? 340 TRP A CE3  1 
ATOM   2577  C CZ2  . TRP A 1 340 ? 30.905  67.440  31.863  1.00 14.05  ? 340 TRP A CZ2  1 
ATOM   2578  C CZ3  . TRP A 1 340 ? 31.784  67.906  34.031  1.00 15.98  ? 340 TRP A CZ3  1 
ATOM   2579  C CH2  . TRP A 1 340 ? 31.777  68.096  32.664  1.00 15.04  ? 340 TRP A CH2  1 
ATOM   2580  N N    . ILE A 1 341 ? 31.065  64.695  37.189  1.00 10.26  ? 341 ILE A N    1 
ATOM   2581  C CA   . ILE A 1 341 ? 32.408  65.100  37.611  1.00 12.15  ? 341 ILE A CA   1 
ATOM   2582  C C    . ILE A 1 341 ? 33.182  63.894  37.991  1.00 13.51  ? 341 ILE A C    1 
ATOM   2583  O O    . ILE A 1 341 ? 34.355  63.928  38.325  1.00 10.75  ? 341 ILE A O    1 
ATOM   2584  C CB   . ILE A 1 341 ? 32.331  66.090  38.784  1.00 7.58   ? 341 ILE A CB   1 
ATOM   2585  C CG1  . ILE A 1 341 ? 31.481  67.280  38.413  1.00 10.76  ? 341 ILE A CG1  1 
ATOM   2586  C CG2  . ILE A 1 341 ? 33.658  66.751  39.104  1.00 7.46   ? 341 ILE A CG2  1 
ATOM   2587  C CD1  . ILE A 1 341 ? 31.585  68.391  39.426  1.00 10.07  ? 341 ILE A CD1  1 
ATOM   2588  N N    . GLY A 1 342 ? 32.518  62.767  37.916  1.00 11.35  ? 342 GLY A N    1 
ATOM   2589  C CA   . GLY A 1 342 ? 33.163  61.549  38.316  1.00 10.07  ? 342 GLY A CA   1 
ATOM   2590  C C    . GLY A 1 342 ? 33.834  61.111  37.115  1.00 10.42  ? 342 GLY A C    1 
ATOM   2591  O O    . GLY A 1 342 ? 34.935  60.703  37.227  1.00 9.66   ? 342 GLY A O    1 
ATOM   2592  N N    . GLY A 1 343 ? 33.149  61.198  35.988  1.00 10.84  ? 343 GLY A N    1 
ATOM   2593  C CA   . GLY A 1 343 ? 33.699  60.834  34.714  1.00 9.92   ? 343 GLY A CA   1 
ATOM   2594  C C    . GLY A 1 343 ? 34.526  61.919  34.132  1.00 11.25  ? 343 GLY A C    1 
ATOM   2595  O O    . GLY A 1 343 ? 35.444  61.646  33.462  1.00 12.79  ? 343 GLY A O    1 
ATOM   2596  N N    . SER A 1 344 ? 34.194  63.174  34.356  1.00 11.17  ? 344 SER A N    1 
ATOM   2597  C CA   . SER A 1 344 ? 35.016  64.275  33.897  1.00 10.35  ? 344 SER A CA   1 
ATOM   2598  C C    . SER A 1 344 ? 36.380  64.096  34.402  1.00 11.61  ? 344 SER A C    1 
ATOM   2599  O O    . SER A 1 344 ? 37.293  64.645  33.863  1.00 14.09  ? 344 SER A O    1 
ATOM   2600  C CB   . SER A 1 344 ? 34.457  65.593  34.353  1.00 10.02  ? 344 SER A CB   1 
ATOM   2601  O OG   . SER A 1 344 ? 35.329  66.654  34.108  1.00 11.69  ? 344 SER A OG   1 
ATOM   2602  N N    . ILE A 1 345 ? 36.537  63.294  35.433  1.00 13.57  ? 345 ILE A N    1 
ATOM   2603  C CA   . ILE A 1 345 ? 37.837  63.028  36.041  1.00 14.73  ? 345 ILE A CA   1 
ATOM   2604  C C    . ILE A 1 345 ? 38.291  61.613  35.754  1.00 14.34  ? 345 ILE A C    1 
ATOM   2605  O O    . ILE A 1 345 ? 39.424  61.430  35.490  1.00 15.05  ? 345 ILE A O    1 
ATOM   2606  C CB   . ILE A 1 345 ? 37.839  63.341  37.536  1.00 13.81  ? 345 ILE A CB   1 
ATOM   2607  C CG1  . ILE A 1 345 ? 37.607  64.822  37.775  1.00 20.12  ? 345 ILE A CG1  1 
ATOM   2608  C CG2  . ILE A 1 345 ? 39.147  62.951  38.203  1.00 22.22  ? 345 ILE A CG2  1 
ATOM   2609  C CD1  . ILE A 1 345 ? 37.556  65.165  39.245  1.00 35.84  ? 345 ILE A CD1  1 
ATOM   2610  N N    . LEU A 1 346 ? 37.406  60.641  35.696  1.00 10.29  ? 346 LEU A N    1 
ATOM   2611  C CA   . LEU A 1 346 ? 37.790  59.314  35.303  1.00 10.55  ? 346 LEU A CA   1 
ATOM   2612  C C    . LEU A 1 346 ? 38.330  59.395  33.936  1.00 13.82  ? 346 LEU A C    1 
ATOM   2613  O O    . LEU A 1 346 ? 39.419  58.949  33.685  1.00 18.26  ? 346 LEU A O    1 
ATOM   2614  C CB   . LEU A 1 346 ? 36.589  58.379  35.217  1.00 8.05   ? 346 LEU A CB   1 
ATOM   2615  C CG   . LEU A 1 346 ? 36.580  56.906  35.596  1.00 8.43   ? 346 LEU A CG   1 
ATOM   2616  C CD1  . LEU A 1 346 ? 35.711  56.184  34.592  1.00 8.58   ? 346 LEU A CD1  1 
ATOM   2617  C CD2  . LEU A 1 346 ? 37.953  56.274  35.660  1.00 12.79  ? 346 LEU A CD2  1 
ATOM   2618  N N    . ALA A 1 347 ? 37.596  59.976  33.023  1.00 13.37  ? 347 ALA A N    1 
ATOM   2619  C CA   . ALA A 1 347 ? 38.006  59.942  31.641  1.00 12.07  ? 347 ALA A CA   1 
ATOM   2620  C C    . ALA A 1 347 ? 39.198  60.742  31.345  1.00 11.37  ? 347 ALA A C    1 
ATOM   2621  O O    . ALA A 1 347 ? 39.929  60.432  30.438  1.00 13.98  ? 347 ALA A O    1 
ATOM   2622  C CB   . ALA A 1 347 ? 36.859  60.366  30.782  1.00 8.27   ? 347 ALA A CB   1 
ATOM   2623  N N    . SER A 1 348 ? 39.425  61.778  32.113  1.00 14.00  ? 348 SER A N    1 
ATOM   2624  C CA   . SER A 1 348 ? 40.547  62.657  31.925  1.00 15.11  ? 348 SER A CA   1 
ATOM   2625  C C    . SER A 1 348 ? 41.827  62.094  32.476  1.00 15.28  ? 348 SER A C    1 
ATOM   2626  O O    . SER A 1 348 ? 42.879  62.668  32.314  1.00 21.61  ? 348 SER A O    1 
ATOM   2627  C CB   . SER A 1 348 ? 40.229  63.946  32.620  1.00 13.56  ? 348 SER A CB   1 
ATOM   2628  O OG   . SER A 1 348 ? 40.345  63.799  34.012  1.00 20.72  ? 348 SER A OG   1 
ATOM   2629  N N    . LEU A 1 349 ? 41.737  60.966  33.130  1.00 14.05  ? 349 LEU A N    1 
ATOM   2630  C CA   . LEU A 1 349 ? 42.887  60.364  33.709  1.00 16.38  ? 349 LEU A CA   1 
ATOM   2631  C C    . LEU A 1 349 ? 43.741  59.788  32.659  1.00 18.42  ? 349 LEU A C    1 
ATOM   2632  O O    . LEU A 1 349 ? 43.252  59.192  31.727  1.00 23.37  ? 349 LEU A O    1 
ATOM   2633  C CB   . LEU A 1 349 ? 42.494  59.295  34.735  1.00 18.32  ? 349 LEU A CB   1 
ATOM   2634  C CG   . LEU A 1 349 ? 41.792  59.587  36.051  1.00 14.30  ? 349 LEU A CG   1 
ATOM   2635  C CD1  . LEU A 1 349 ? 41.547  58.294  36.793  1.00 15.60  ? 349 LEU A CD1  1 
ATOM   2636  C CD2  . LEU A 1 349 ? 42.592  60.545  36.902  1.00 23.61  ? 349 LEU A CD2  1 
ATOM   2637  N N    . SER A 1 350 ? 45.033  59.952  32.814  1.00 16.84  ? 350 SER A N    1 
ATOM   2638  C CA   . SER A 1 350 ? 45.990  59.458  31.875  1.00 20.14  ? 350 SER A CA   1 
ATOM   2639  C C    . SER A 1 350 ? 46.024  57.969  31.797  1.00 22.32  ? 350 SER A C    1 
ATOM   2640  O O    . SER A 1 350 ? 46.297  57.414  30.759  1.00 23.12  ? 350 SER A O    1 
ATOM   2641  C CB   . SER A 1 350 ? 47.325  59.997  32.304  1.00 23.55  ? 350 SER A CB   1 
ATOM   2642  O OG   . SER A 1 350 ? 47.269  61.399  32.453  1.00 27.16  ? 350 SER A OG   1 
ATOM   2643  N N    . THR A 1 351 ? 45.851  57.312  32.920  1.00 18.50  ? 351 THR A N    1 
ATOM   2644  C CA   . THR A 1 351 ? 45.834  55.860  32.960  1.00 20.64  ? 351 THR A CA   1 
ATOM   2645  C C    . THR A 1 351 ? 44.581  55.235  32.349  1.00 21.88  ? 351 THR A C    1 
ATOM   2646  O O    . THR A 1 351 ? 44.617  54.101  31.921  1.00 25.44  ? 351 THR A O    1 
ATOM   2647  C CB   . THR A 1 351 ? 46.152  55.354  34.373  1.00 22.91  ? 351 THR A CB   1 
ATOM   2648  O OG1  . THR A 1 351 ? 47.458  55.798  34.752  1.00 23.72  ? 351 THR A OG1  1 
ATOM   2649  C CG2  . THR A 1 351 ? 46.115  53.849  34.421  1.00 21.94  ? 351 THR A CG2  1 
ATOM   2650  N N    . PHE A 1 352 ? 43.481  55.964  32.305  1.00 15.13  ? 352 PHE A N    1 
ATOM   2651  C CA   . PHE A 1 352 ? 42.224  55.452  31.775  1.00 18.65  ? 352 PHE A CA   1 
ATOM   2652  C C    . PHE A 1 352 ? 42.156  55.192  30.310  1.00 23.94  ? 352 PHE A C    1 
ATOM   2653  O O    . PHE A 1 352 ? 41.370  54.367  29.872  1.00 20.10  ? 352 PHE A O    1 
ATOM   2654  C CB   . PHE A 1 352 ? 41.106  56.408  32.155  1.00 20.41  ? 352 PHE A CB   1 
ATOM   2655  C CG   . PHE A 1 352 ? 39.755  55.980  31.697  1.00 15.95  ? 352 PHE A CG   1 
ATOM   2656  C CD1  . PHE A 1 352 ? 39.147  54.885  32.252  1.00 15.22  ? 352 PHE A CD1  1 
ATOM   2657  C CD2  . PHE A 1 352 ? 39.098  56.676  30.712  1.00 10.61  ? 352 PHE A CD2  1 
ATOM   2658  C CE1  . PHE A 1 352 ? 37.912  54.483  31.823  1.00 19.16  ? 352 PHE A CE1  1 
ATOM   2659  C CE2  . PHE A 1 352 ? 37.856  56.285  30.288  1.00 10.74  ? 352 PHE A CE2  1 
ATOM   2660  C CZ   . PHE A 1 352 ? 37.265  55.185  30.839  1.00 14.08  ? 352 PHE A CZ   1 
ATOM   2661  N N    . GLN A 1 353 ? 43.017  55.804  29.529  1.00 21.55  ? 353 GLN A N    1 
ATOM   2662  C CA   . GLN A 1 353 ? 42.937  55.716  28.096  1.00 17.02  ? 353 GLN A CA   1 
ATOM   2663  C C    . GLN A 1 353 ? 42.921  54.291  27.641  1.00 21.60  ? 353 GLN A C    1 
ATOM   2664  O O    . GLN A 1 353 ? 42.321  53.978  26.623  1.00 19.43  ? 353 GLN A O    1 
ATOM   2665  C CB   . GLN A 1 353 ? 44.162  56.393  27.565  1.00 16.92  ? 353 GLN A CB   1 
ATOM   2666  C CG   . GLN A 1 353 ? 44.335  57.818  28.032  1.00 22.45  ? 353 GLN A CG   1 
ATOM   2667  C CD   . GLN A 1 353 ? 45.766  58.279  27.886  1.00 34.77  ? 353 GLN A CD   1 
ATOM   2668  O OE1  . GLN A 1 353 ? 46.057  59.474  27.885  1.00 47.67  ? 353 GLN A OE1  1 
ATOM   2669  N NE2  . GLN A 1 353 ? 46.674  57.328  27.764  1.00 32.63  ? 353 GLN A NE2  1 
ATOM   2670  N N    . GLN A 1 354 ? 43.582  53.414  28.369  1.00 22.16  ? 354 GLN A N    1 
ATOM   2671  C CA   . GLN A 1 354 ? 43.675  52.001  28.025  1.00 23.47  ? 354 GLN A CA   1 
ATOM   2672  C C    . GLN A 1 354 ? 42.479  51.133  28.323  1.00 17.29  ? 354 GLN A C    1 
ATOM   2673  O O    . GLN A 1 354 ? 42.444  49.982  27.945  1.00 18.79  ? 354 GLN A O    1 
ATOM   2674  C CB   . GLN A 1 354 ? 44.886  51.455  28.746  1.00 20.64  ? 354 GLN A CB   1 
ATOM   2675  C CG   . GLN A 1 354 ? 45.865  52.525  29.195  1.00 21.60  ? 354 GLN A CG   1 
ATOM   2676  C CD   . GLN A 1 354 ? 46.666  53.102  28.054  1.00 26.84  ? 354 GLN A CD   1 
ATOM   2677  O OE1  . GLN A 1 354 ? 46.948  54.290  28.028  1.00 29.29  ? 354 GLN A OE1  1 
ATOM   2678  N NE2  . GLN A 1 354 ? 47.026  52.260  27.099  1.00 28.66  ? 354 GLN A NE2  1 
ATOM   2679  N N    . MET A 1 355 ? 41.511  51.675  29.024  1.00 15.44  ? 355 MET A N    1 
ATOM   2680  C CA   . MET A 1 355 ? 40.359  50.893  29.419  1.00 19.75  ? 355 MET A CA   1 
ATOM   2681  C C    . MET A 1 355 ? 39.241  51.148  28.486  1.00 16.78  ? 355 MET A C    1 
ATOM   2682  O O    . MET A 1 355 ? 38.136  50.731  28.742  1.00 15.29  ? 355 MET A O    1 
ATOM   2683  C CB   . MET A 1 355 ? 39.990  51.260  30.834  1.00 30.19  ? 355 MET A CB   1 
ATOM   2684  C CG   . MET A 1 355 ? 41.176  51.513  31.741  1.00 24.16  ? 355 MET A CG   1 
ATOM   2685  S SD   . MET A 1 355 ? 40.630  51.807  33.417  1.00 16.13  ? 355 MET A SD   1 
ATOM   2686  C CE   . MET A 1 355 ? 42.148  52.406  34.137  1.00 30.16  ? 355 MET A CE   1 
ATOM   2687  N N    . TRP A 1 356 ? 39.521  51.876  27.421  1.00 19.83  ? 356 TRP A N    1 
ATOM   2688  C CA   . TRP A 1 356 ? 38.525  52.182  26.419  1.00 13.69  ? 356 TRP A CA   1 
ATOM   2689  C C    . TRP A 1 356 ? 38.256  50.982  25.561  1.00 12.93  ? 356 TRP A C    1 
ATOM   2690  O O    . TRP A 1 356 ? 39.137  50.169  25.339  1.00 14.22  ? 356 TRP A O    1 
ATOM   2691  C CB   . TRP A 1 356 ? 39.047  53.338  25.554  1.00 12.46  ? 356 TRP A CB   1 
ATOM   2692  C CG   . TRP A 1 356 ? 39.195  54.658  26.201  1.00 10.92  ? 356 TRP A CG   1 
ATOM   2693  C CD1  . TRP A 1 356 ? 40.314  55.169  26.749  1.00 20.46  ? 356 TRP A CD1  1 
ATOM   2694  C CD2  . TRP A 1 356 ? 38.166  55.613  26.434  1.00 7.33   ? 356 TRP A CD2  1 
ATOM   2695  N NE1  . TRP A 1 356 ? 40.068  56.400  27.292  1.00 21.77  ? 356 TRP A NE1  1 
ATOM   2696  C CE2  . TRP A 1 356 ? 38.748  56.694  27.108  1.00 12.84  ? 356 TRP A CE2  1 
ATOM   2697  C CE3  . TRP A 1 356 ? 36.811  55.665  26.123  1.00 9.07   ? 356 TRP A CE3  1 
ATOM   2698  C CZ2  . TRP A 1 356 ? 38.027  57.816  27.471  1.00 13.79  ? 356 TRP A CZ2  1 
ATOM   2699  C CZ3  . TRP A 1 356 ? 36.096  56.778  26.487  1.00 12.60  ? 356 TRP A CZ3  1 
ATOM   2700  C CH2  . TRP A 1 356 ? 36.703  57.839  27.152  1.00 13.79  ? 356 TRP A CH2  1 
ATOM   2701  N N    . ILE A 1 357 ? 37.032  50.847  25.111  1.00 12.93  ? 357 ILE A N    1 
ATOM   2702  C CA   . ILE A 1 357 ? 36.705  49.753  24.273  1.00 22.17  ? 357 ILE A CA   1 
ATOM   2703  C C    . ILE A 1 357 ? 36.986  50.387  22.961  1.00 27.25  ? 357 ILE A C    1 
ATOM   2704  O O    . ILE A 1 357 ? 36.290  51.309  22.585  1.00 22.90  ? 357 ILE A O    1 
ATOM   2705  C CB   . ILE A 1 357 ? 35.243  49.349  24.293  1.00 21.30  ? 357 ILE A CB   1 
ATOM   2706  C CG1  . ILE A 1 357 ? 34.856  48.856  25.675  1.00 19.50  ? 357 ILE A CG1  1 
ATOM   2707  C CG2  . ILE A 1 357 ? 34.962  48.289  23.245  1.00 20.99  ? 357 ILE A CG2  1 
ATOM   2708  C CD1  . ILE A 1 357 ? 33.435  48.383  25.733  1.00 23.18  ? 357 ILE A CD1  1 
ATOM   2709  N N    . SER A 1 358 ? 38.007  49.921  22.250  1.00 27.00  ? 358 SER A N    1 
ATOM   2710  C CA   . SER A 1 358 ? 38.411  50.543  21.025  1.00 21.53  ? 358 SER A CA   1 
ATOM   2711  C C    . SER A 1 358 ? 37.393  50.186  20.012  1.00 34.12  ? 358 SER A C    1 
ATOM   2712  O O    . SER A 1 358 ? 36.783  49.143  20.125  1.00 45.27  ? 358 SER A O    1 
ATOM   2713  C CB   . SER A 1 358 ? 39.759  50.031  20.637  1.00 22.95  ? 358 SER A CB   1 
ATOM   2714  O OG   . SER A 1 358 ? 39.654  48.851  19.900  1.00 34.71  ? 358 SER A OG   1 
ATOM   2715  N N    . LYS A 1 359 ? 37.189  51.015  19.004  1.00 30.02  ? 359 LYS A N    1 
ATOM   2716  C CA   . LYS A 1 359 ? 36.165  50.790  18.033  1.00 26.51  ? 359 LYS A CA   1 
ATOM   2717  C C    . LYS A 1 359 ? 36.529  49.555  17.425  1.00 33.60  ? 359 LYS A C    1 
ATOM   2718  O O    . LYS A 1 359 ? 35.689  48.737  17.131  1.00 39.44  ? 359 LYS A O    1 
ATOM   2719  C CB   . LYS A 1 359 ? 36.301  51.806  16.954  1.00 26.81  ? 359 LYS A CB   1 
ATOM   2720  C CG   . LYS A 1 359 ? 35.177  51.866  15.943  1.00 29.19  ? 359 LYS A CG   1 
ATOM   2721  C CD   . LYS A 1 359 ? 35.485  52.983  14.965  1.00 29.64  ? 359 LYS A CD   1 
ATOM   2722  C CE   . LYS A 1 359 ? 36.573  53.881  15.526  1.00 21.71  ? 359 LYS A CE   1 
ATOM   2723  N NZ   . LYS A 1 359 ? 36.715  55.155  14.777  1.00 21.71  ? 359 LYS A NZ   1 
ATOM   2724  N N    . GLN A 1 360 ? 37.813  49.377  17.232  1.00 35.01  ? 360 GLN A N    1 
ATOM   2725  C CA   . GLN A 1 360 ? 38.287  48.200  16.561  1.00 38.93  ? 360 GLN A CA   1 
ATOM   2726  C C    . GLN A 1 360 ? 37.888  47.005  17.294  1.00 32.06  ? 360 GLN A C    1 
ATOM   2727  O O    . GLN A 1 360 ? 37.358  46.117  16.708  1.00 39.67  ? 360 GLN A O    1 
ATOM   2728  C CB   . GLN A 1 360 ? 39.801  48.223  16.543  1.00 37.98  ? 360 GLN A CB   1 
ATOM   2729  C CG   . GLN A 1 360 ? 40.382  49.625  16.519  1.00 36.69  ? 360 GLN A CG   1 
ATOM   2730  C CD   . GLN A 1 360 ? 41.876  49.616  16.311  1.00 47.18  ? 360 GLN A CD   1 
ATOM   2731  O OE1  . GLN A 1 360 ? 42.436  48.642  15.809  1.00 46.74  ? 360 GLN A OE1  1 
ATOM   2732  N NE2  . GLN A 1 360 ? 42.532  50.705  16.691  1.00 34.84  ? 360 GLN A NE2  1 
ATOM   2733  N N    . GLU A 1 361 ? 38.030  47.017  18.595  1.00 27.08  ? 361 GLU A N    1 
ATOM   2734  C CA   . GLU A 1 361 ? 37.741  45.862  19.392  1.00 30.10  ? 361 GLU A CA   1 
ATOM   2735  C C    . GLU A 1 361 ? 36.321  45.396  19.299  1.00 27.73  ? 361 GLU A C    1 
ATOM   2736  O O    . GLU A 1 361 ? 36.074  44.227  19.321  1.00 26.83  ? 361 GLU A O    1 
ATOM   2737  C CB   . GLU A 1 361 ? 38.070  46.169  20.826  1.00 35.05  ? 361 GLU A CB   1 
ATOM   2738  C CG   . GLU A 1 361 ? 39.525  45.953  21.201  1.00 36.96  ? 361 GLU A CG   1 
ATOM   2739  C CD   . GLU A 1 361 ? 39.836  46.408  22.611  1.00 33.77  ? 361 GLU A CD   1 
ATOM   2740  O OE1  . GLU A 1 361 ? 38.892  46.606  23.392  1.00 35.89  ? 361 GLU A OE1  1 
ATOM   2741  O OE2  . GLU A 1 361 ? 41.024  46.560  22.939  1.00 27.77  ? 361 GLU A OE2  1 
ATOM   2742  N N    . TYR A 1 362 ? 35.378  46.296  19.230  1.00 23.43  ? 362 TYR A N    1 
ATOM   2743  C CA   . TYR A 1 362 ? 34.006  45.920  19.081  1.00 22.48  ? 362 TYR A CA   1 
ATOM   2744  C C    . TYR A 1 362 ? 33.745  45.221  17.823  1.00 22.20  ? 362 TYR A C    1 
ATOM   2745  O O    . TYR A 1 362 ? 33.067  44.225  17.784  1.00 22.19  ? 362 TYR A O    1 
ATOM   2746  C CB   . TYR A 1 362 ? 33.241  47.215  18.984  1.00 20.13  ? 362 TYR A CB   1 
ATOM   2747  C CG   . TYR A 1 362 ? 31.785  47.076  18.655  1.00 18.17  ? 362 TYR A CG   1 
ATOM   2748  C CD1  . TYR A 1 362 ? 30.883  46.668  19.605  1.00 19.90  ? 362 TYR A CD1  1 
ATOM   2749  C CD2  . TYR A 1 362 ? 31.309  47.382  17.399  1.00 17.19  ? 362 TYR A CD2  1 
ATOM   2750  C CE1  . TYR A 1 362 ? 29.555  46.550  19.308  1.00 15.57  ? 362 TYR A CE1  1 
ATOM   2751  C CE2  . TYR A 1 362 ? 29.982  47.259  17.098  1.00 15.20  ? 362 TYR A CE2  1 
ATOM   2752  C CZ   . TYR A 1 362 ? 29.119  46.842  18.063  1.00 14.10  ? 362 TYR A CZ   1 
ATOM   2753  O OH   . TYR A 1 362 ? 27.803  46.714  17.769  1.00 13.59  ? 362 TYR A OH   1 
ATOM   2754  N N    . ASP A 1 363 ? 34.296  45.737  16.766  1.00 28.98  ? 363 ASP A N    1 
ATOM   2755  C CA   . ASP A 1 363 ? 34.106  45.150  15.485  1.00 27.88  ? 363 ASP A CA   1 
ATOM   2756  C C    . ASP A 1 363 ? 34.556  43.729  15.605  1.00 34.32  ? 363 ASP A C    1 
ATOM   2757  O O    . ASP A 1 363 ? 33.861  42.820  15.176  1.00 31.51  ? 363 ASP A O    1 
ATOM   2758  C CB   . ASP A 1 363 ? 34.951  45.924  14.486  1.00 29.36  ? 363 ASP A CB   1 
ATOM   2759  C CG   . ASP A 1 363 ? 34.353  47.265  14.115  1.00 37.36  ? 363 ASP A CG   1 
ATOM   2760  O OD1  . ASP A 1 363 ? 33.712  47.906  14.967  1.00 42.84  ? 363 ASP A OD1  1 
ATOM   2761  O OD2  . ASP A 1 363 ? 34.522  47.683  12.955  1.00 41.50  ? 363 ASP A OD2  1 
ATOM   2762  N N    . GLU A 1 364 ? 35.741  43.519  16.154  1.00 33.79  ? 364 GLU A N    1 
ATOM   2763  C CA   . GLU A 1 364 ? 36.237  42.186  16.371  1.00 33.16  ? 364 GLU A CA   1 
ATOM   2764  C C    . GLU A 1 364 ? 35.515  41.287  17.364  1.00 30.21  ? 364 GLU A C    1 
ATOM   2765  O O    . GLU A 1 364 ? 35.207  40.158  17.053  1.00 40.82  ? 364 GLU A O    1 
ATOM   2766  C CB   . GLU A 1 364 ? 37.669  42.289  16.824  1.00 31.16  ? 364 GLU A CB   1 
ATOM   2767  C CG   . GLU A 1 364 ? 38.507  43.345  16.125  1.00 37.48  ? 364 GLU A CG   1 
ATOM   2768  C CD   . GLU A 1 364 ? 38.397  43.326  14.616  1.00 55.30  ? 364 GLU A CD   1 
ATOM   2769  O OE1  . GLU A 1 364 ? 38.478  42.237  14.014  1.00 74.34  ? 364 GLU A OE1  1 
ATOM   2770  O OE2  . GLU A 1 364 ? 38.226  44.411  14.028  1.00 55.93  ? 364 GLU A OE2  1 
ATOM   2771  N N    . SER A 1 365 ? 35.196  41.775  18.538  1.00 27.84  ? 365 SER A N    1 
ATOM   2772  C CA   . SER A 1 365 ? 34.609  40.928  19.559  1.00 36.74  ? 365 SER A CA   1 
ATOM   2773  C C    . SER A 1 365 ? 33.164  41.079  19.889  1.00 33.66  ? 365 SER A C    1 
ATOM   2774  O O    . SER A 1 365 ? 32.672  40.406  20.772  1.00 36.79  ? 365 SER A O    1 
ATOM   2775  C CB   . SER A 1 365 ? 35.338  41.160  20.854  1.00 44.39  ? 365 SER A CB   1 
ATOM   2776  O OG   . SER A 1 365 ? 36.701  41.446  20.612  1.00 69.82  ? 365 SER A OG   1 
ATOM   2777  N N    . GLY A 1 366 ? 32.483  41.971  19.230  1.00 26.21  ? 366 GLY A N    1 
ATOM   2778  C CA   . GLY A 1 366 ? 31.078  42.108  19.461  1.00 25.44  ? 366 GLY A CA   1 
ATOM   2779  C C    . GLY A 1 366 ? 30.762  42.991  20.600  1.00 25.83  ? 366 GLY A C    1 
ATOM   2780  O O    . GLY A 1 366 ? 31.648  43.519  21.216  1.00 25.41  ? 366 GLY A O    1 
ATOM   2781  N N    . PRO A 1 367 ? 29.489  43.139  20.899  1.00 25.18  ? 367 PRO A N    1 
ATOM   2782  C CA   . PRO A 1 367 ? 29.062  44.017  21.972  1.00 16.86  ? 367 PRO A CA   1 
ATOM   2783  C C    . PRO A 1 367 ? 29.093  43.303  23.272  1.00 21.82  ? 367 PRO A C    1 
ATOM   2784  O O    . PRO A 1 367 ? 28.679  43.872  24.244  1.00 23.72  ? 367 PRO A O    1 
ATOM   2785  C CB   . PRO A 1 367 ? 27.646  44.328  21.617  1.00 15.47  ? 367 PRO A CB   1 
ATOM   2786  C CG   . PRO A 1 367 ? 27.431  43.867  20.217  1.00 21.67  ? 367 PRO A CG   1 
ATOM   2787  C CD   . PRO A 1 367 ? 28.386  42.754  20.016  1.00 24.36  ? 367 PRO A CD   1 
ATOM   2788  N N    . SER A 1 368 ? 29.548  42.060  23.288  1.00 25.14  ? 368 SER A N    1 
ATOM   2789  C CA   . SER A 1 368 ? 29.663  41.274  24.486  1.00 19.69  ? 368 SER A CA   1 
ATOM   2790  C C    . SER A 1 368 ? 30.977  41.620  25.102  1.00 19.64  ? 368 SER A C    1 
ATOM   2791  O O    . SER A 1 368 ? 31.330  41.081  26.114  1.00 23.64  ? 368 SER A O    1 
ATOM   2792  C CB   . SER A 1 368 ? 29.625  39.844  24.067  1.00 27.17  ? 368 SER A CB   1 
ATOM   2793  O OG   . SER A 1 368 ? 28.845  39.683  22.901  1.00 37.42  ? 368 SER A OG   1 
ATOM   2794  N N    . ILE A 1 369 ? 31.731  42.490  24.461  1.00 18.63  ? 369 ILE A N    1 
ATOM   2795  C CA   . ILE A 1 369 ? 32.984  42.991  24.980  1.00 20.05  ? 369 ILE A CA   1 
ATOM   2796  C C    . ILE A 1 369 ? 32.874  43.824  26.225  1.00 19.68  ? 369 ILE A C    1 
ATOM   2797  O O    . ILE A 1 369 ? 33.724  43.770  27.076  1.00 21.95  ? 369 ILE A O    1 
ATOM   2798  C CB   . ILE A 1 369 ? 33.721  43.809  23.893  1.00 22.69  ? 369 ILE A CB   1 
ATOM   2799  C CG1  . ILE A 1 369 ? 35.160  44.081  24.303  1.00 27.78  ? 369 ILE A CG1  1 
ATOM   2800  C CG2  . ILE A 1 369 ? 33.017  45.105  23.536  1.00 18.53  ? 369 ILE A CG2  1 
ATOM   2801  C CD1  . ILE A 1 369 ? 35.958  44.735  23.212  1.00 27.66  ? 369 ILE A CD1  1 
ATOM   2802  N N    . VAL A 1 370 ? 31.856  44.643  26.312  1.00 16.81  ? 370 VAL A N    1 
ATOM   2803  C CA   . VAL A 1 370 ? 31.702  45.483  27.439  1.00 17.71  ? 370 VAL A CA   1 
ATOM   2804  C C    . VAL A 1 370 ? 31.826  44.696  28.674  1.00 20.39  ? 370 VAL A C    1 
ATOM   2805  O O    . VAL A 1 370 ? 32.245  45.217  29.663  1.00 22.17  ? 370 VAL A O    1 
ATOM   2806  C CB   . VAL A 1 370 ? 30.310  46.053  27.500  1.00 16.21  ? 370 VAL A CB   1 
ATOM   2807  C CG1  . VAL A 1 370 ? 30.033  46.952  26.323  1.00 12.73  ? 370 VAL A CG1  1 
ATOM   2808  C CG2  . VAL A 1 370 ? 29.254  45.001  27.721  1.00 18.70  ? 370 VAL A CG2  1 
ATOM   2809  N N    . HIS A 1 371 ? 31.470  43.435  28.653  1.00 16.77  ? 371 HIS A N    1 
ATOM   2810  C CA   . HIS A 1 371 ? 31.435  42.646  29.869  1.00 16.98  ? 371 HIS A CA   1 
ATOM   2811  C C    . HIS A 1 371 ? 32.796  42.292  30.273  1.00 16.35  ? 371 HIS A C    1 
ATOM   2812  O O    . HIS A 1 371 ? 32.995  41.880  31.383  1.00 15.87  ? 371 HIS A O    1 
ATOM   2813  C CB   . HIS A 1 371 ? 30.656  41.385  29.651  1.00 20.67  ? 371 HIS A CB   1 
ATOM   2814  C CG   . HIS A 1 371 ? 29.288  41.594  29.098  1.00 14.84  ? 371 HIS A CG   1 
ATOM   2815  N ND1  . HIS A 1 371 ? 28.284  42.205  29.808  1.00 14.60  ? 371 HIS A ND1  1 
ATOM   2816  C CD2  . HIS A 1 371 ? 28.742  41.220  27.922  1.00 17.40  ? 371 HIS A CD2  1 
ATOM   2817  C CE1  . HIS A 1 371 ? 27.184  42.224  29.084  1.00 12.66  ? 371 HIS A CE1  1 
ATOM   2818  N NE2  . HIS A 1 371 ? 27.434  41.629  27.937  1.00 17.53  ? 371 HIS A NE2  1 
ATOM   2819  N N    . ARG A 1 372 ? 33.748  42.482  29.382  1.00 15.44  ? 372 ARG A N    1 
ATOM   2820  C CA   . ARG A 1 372 ? 35.111  42.103  29.630  1.00 18.52  ? 372 ARG A CA   1 
ATOM   2821  C C    . ARG A 1 372 ? 35.987  43.290  29.663  1.00 15.35  ? 372 ARG A C    1 
ATOM   2822  O O    . ARG A 1 372 ? 37.184  43.166  29.654  1.00 20.26  ? 372 ARG A O    1 
ATOM   2823  C CB   . ARG A 1 372 ? 35.575  41.202  28.511  1.00 21.22  ? 372 ARG A CB   1 
ATOM   2824  C CG   . ARG A 1 372 ? 34.796  39.906  28.386  1.00 25.98  ? 372 ARG A CG   1 
ATOM   2825  C CD   . ARG A 1 372 ? 34.423  39.615  26.944  1.00 39.29  ? 372 ARG A CD   1 
ATOM   2826  N NE   . ARG A 1 372 ? 33.395  38.582  26.837  1.00 42.86  ? 372 ARG A NE   1 
ATOM   2827  C CZ   . ARG A 1 372 ? 32.934  38.112  25.683  1.00 39.23  ? 372 ARG A CZ   1 
ATOM   2828  N NH1  . ARG A 1 372 ? 33.397  38.594  24.542  1.00 40.15  ? 372 ARG A NH1  1 
ATOM   2829  N NH2  . ARG A 1 372 ? 32.002  37.171  25.668  1.00 36.34  ? 372 ARG A NH2  1 
ATOM   2830  N N    . LYS A 1 373 ? 35.415  44.460  29.688  1.00 13.86  ? 373 LYS A N    1 
ATOM   2831  C CA   . LYS A 1 373 ? 36.147  45.675  29.772  1.00 15.43  ? 373 LYS A CA   1 
ATOM   2832  C C    . LYS A 1 373 ? 35.485  46.462  30.828  1.00 16.58  ? 373 LYS A C    1 
ATOM   2833  O O    . LYS A 1 373 ? 36.077  46.825  31.811  1.00 17.42  ? 373 LYS A O    1 
ATOM   2834  C CB   . LYS A 1 373 ? 36.004  46.373  28.435  1.00 21.29  ? 373 LYS A CB   1 
ATOM   2835  C CG   . LYS A 1 373 ? 36.472  45.594  27.219  1.00 25.90  ? 373 LYS A CG   1 
ATOM   2836  C CD   . LYS A 1 373 ? 37.935  45.227  27.342  1.00 36.09  ? 373 LYS A CD   1 
ATOM   2837  C CE   . LYS A 1 373 ? 38.822  46.447  27.217  1.00 28.63  ? 373 LYS A CE   1 
ATOM   2838  N NZ   . LYS A 1 373 ? 40.257  46.063  27.170  1.00 34.09  ? 373 LYS A NZ   1 
ATOM   2839  N N    . CYS A 1 374 ? 34.208  46.711  30.632  1.00 18.01  ? 374 CYS A N    1 
ATOM   2840  C CA   . CYS A 1 374 ? 33.417  47.419  31.606  1.00 21.65  ? 374 CYS A CA   1 
ATOM   2841  C C    . CYS A 1 374 ? 32.942  46.533  32.724  1.00 17.24  ? 374 CYS A C    1 
ATOM   2842  O O    . CYS A 1 374 ? 32.532  45.416  32.504  1.00 16.09  ? 374 CYS A O    1 
ATOM   2843  C CB   . CYS A 1 374 ? 32.252  48.078  30.874  1.00 16.35  ? 374 CYS A CB   1 
ATOM   2844  S SG   . CYS A 1 374 ? 32.660  49.177  29.535  1.00 26.38  ? 374 CYS A SG   1 
ATOM   2845  N N    . PHE A 1 375 ? 32.994  47.039  33.939  1.00 16.31  ? 375 PHE A N    1 
ATOM   2846  C CA   . PHE A 1 375 ? 32.679  46.232  35.079  1.00 19.86  ? 375 PHE A CA   1 
ATOM   2847  C C    . PHE A 1 375 ? 31.758  46.993  36.013  1.00 22.93  ? 375 PHE A C    1 
ATOM   2848  O O    . PHE A 1 375 ? 31.765  46.788  37.230  1.00 23.81  ? 375 PHE A O    1 
ATOM   2849  C CB   . PHE A 1 375 ? 33.965  45.918  35.832  1.00 19.66  ? 375 PHE A CB   1 
ATOM   2850  C CG   . PHE A 1 375 ? 34.819  44.875  35.182  1.00 17.39  ? 375 PHE A CG   1 
ATOM   2851  C CD1  . PHE A 1 375 ? 34.264  43.726  34.676  1.00 18.52  ? 375 PHE A CD1  1 
ATOM   2852  C CD2  . PHE A 1 375 ? 36.178  45.043  35.100  1.00 14.92  ? 375 PHE A CD2  1 
ATOM   2853  C CE1  . PHE A 1 375 ? 35.051  42.769  34.087  1.00 17.15  ? 375 PHE A CE1  1 
ATOM   2854  C CE2  . PHE A 1 375 ? 36.968  44.087  34.516  1.00 18.00  ? 375 PHE A CE2  1 
ATOM   2855  C CZ   . PHE A 1 375 ? 36.404  42.947  34.011  1.00 17.53  ? 375 PHE A CZ   1 
ATOM   2856  N N    . ILE B 1 5   ? -13.887 101.925 -1.004  1.00 20.54  ? 5   ILE B N    1 
ATOM   2857  C CA   . ILE B 1 5   ? -12.767 101.047 -1.090  1.00 28.11  ? 5   ILE B CA   1 
ATOM   2858  C C    . ILE B 1 5   ? -12.196 101.135 0.291   1.00 33.11  ? 5   ILE B C    1 
ATOM   2859  O O    . ILE B 1 5   ? -12.710 101.887 1.116   1.00 29.65  ? 5   ILE B O    1 
ATOM   2860  C CB   . ILE B 1 5   ? -11.827 101.498 -2.205  1.00 29.43  ? 5   ILE B CB   1 
ATOM   2861  C CG1  . ILE B 1 5   ? -12.663 101.952 -3.401  1.00 29.46  ? 5   ILE B CG1  1 
ATOM   2862  C CG2  . ILE B 1 5   ? -10.916 100.368 -2.663  1.00 24.45  ? 5   ILE B CG2  1 
ATOM   2863  C CD1  . ILE B 1 5   ? -12.535 103.420 -3.743  1.00 45.66  ? 5   ILE B CD1  1 
ATOM   2864  N N    . ALA B 1 6   ? -11.114 100.418 0.576   1.00 27.35  ? 6   ALA B N    1 
ATOM   2865  C CA   . ALA B 1 6   ? -10.570 100.386 1.919   1.00 20.26  ? 6   ALA B CA   1 
ATOM   2866  C C    . ALA B 1 6   ? -9.466  101.328 1.972   1.00 22.23  ? 6   ALA B C    1 
ATOM   2867  O O    . ALA B 1 6   ? -9.009  101.762 0.946   1.00 20.02  ? 6   ALA B O    1 
ATOM   2868  C CB   . ALA B 1 6   ? -10.102 99.006  2.296   1.00 16.14  ? 6   ALA B CB   1 
ATOM   2869  N N    . ALA B 1 7   ? -9.012  101.635 3.175   1.00 23.61  ? 7   ALA B N    1 
ATOM   2870  C CA   . ALA B 1 7   ? -7.996  102.622 3.337   1.00 13.65  ? 7   ALA B CA   1 
ATOM   2871  C C    . ALA B 1 7   ? -6.678  102.036 3.567   1.00 12.53  ? 7   ALA B C    1 
ATOM   2872  O O    . ALA B 1 7   ? -6.552  100.882 3.906   1.00 11.03  ? 7   ALA B O    1 
ATOM   2873  C CB   . ALA B 1 7   ? -8.358  103.559 4.442   1.00 9.19   ? 7   ALA B CB   1 
ATOM   2874  N N    . LEU B 1 8   ? -5.675  102.860 3.378   1.00 12.92  ? 8   LEU B N    1 
ATOM   2875  C CA   . LEU B 1 8   ? -4.338  102.415 3.519   1.00 12.62  ? 8   LEU B CA   1 
ATOM   2876  C C    . LEU B 1 8   ? -3.882  103.299 4.596   1.00 10.70  ? 8   LEU B C    1 
ATOM   2877  O O    . LEU B 1 8   ? -4.291  104.422 4.657   1.00 10.90  ? 8   LEU B O    1 
ATOM   2878  C CB   . LEU B 1 8   ? -3.542  102.639 2.231   1.00 9.11   ? 8   LEU B CB   1 
ATOM   2879  C CG   . LEU B 1 8   ? -3.630  101.696 1.052   1.00 10.05  ? 8   LEU B CG   1 
ATOM   2880  C CD1  . LEU B 1 8   ? -2.885  102.322 -0.103  1.00 15.69  ? 8   LEU B CD1  1 
ATOM   2881  C CD2  . LEU B 1 8   ? -3.023  100.361 1.414   1.00 7.64   ? 8   LEU B CD2  1 
ATOM   2882  N N    . VAL B 1 9   ? -3.099  102.767 5.507   1.00 8.89   ? 9   VAL B N    1 
ATOM   2883  C CA   . VAL B 1 9   ? -2.590  103.522 6.621   1.00 9.51   ? 9   VAL B CA   1 
ATOM   2884  C C    . VAL B 1 9   ? -1.077  103.241 6.706   1.00 8.95   ? 9   VAL B C    1 
ATOM   2885  O O    . VAL B 1 9   ? -0.669  102.131 6.480   1.00 8.72   ? 9   VAL B O    1 
ATOM   2886  C CB   . VAL B 1 9   ? -3.355  103.167 7.920   1.00 13.74  ? 9   VAL B CB   1 
ATOM   2887  C CG1  . VAL B 1 9   ? -2.801  103.931 9.104   1.00 13.56  ? 9   VAL B CG1  1 
ATOM   2888  C CG2  . VAL B 1 9   ? -4.841  103.413 7.791   1.00 13.62  ? 9   VAL B CG2  1 
ATOM   2889  N N    . ILE B 1 10  ? -0.253  104.249 6.971   1.00 8.45   ? 10  ILE B N    1 
ATOM   2890  C CA   . ILE B 1 10  ? 1.194   104.045 7.108   1.00 9.79   ? 10  ILE B CA   1 
ATOM   2891  C C    . ILE B 1 10  ? 1.807   104.787 8.273   1.00 11.15  ? 10  ILE B C    1 
ATOM   2892  O O    . ILE B 1 10  ? 1.404   105.886 8.603   1.00 12.21  ? 10  ILE B O    1 
ATOM   2893  C CB   . ILE B 1 10  ? 2.014   104.248 5.810   1.00 9.89   ? 10  ILE B CB   1 
ATOM   2894  C CG1  . ILE B 1 10  ? 3.470   103.867 6.038   1.00 11.91  ? 10  ILE B CG1  1 
ATOM   2895  C CG2  . ILE B 1 10  ? 2.026   105.667 5.346   1.00 9.69   ? 10  ILE B CG2  1 
ATOM   2896  C CD1  . ILE B 1 10  ? 4.293   103.729 4.791   1.00 12.36  ? 10  ILE B CD1  1 
ATOM   2897  N N    . ASP B 1 11  ? 2.752   104.148 8.946   1.00 9.40   ? 11  ASP B N    1 
ATOM   2898  C CA   . ASP B 1 11  ? 3.441   104.794 10.029  1.00 8.79   ? 11  ASP B CA   1 
ATOM   2899  C C    . ASP B 1 11  ? 4.875   104.856 9.699   1.00 10.67  ? 11  ASP B C    1 
ATOM   2900  O O    . ASP B 1 11  ? 5.608   103.923 9.875   1.00 10.53  ? 11  ASP B O    1 
ATOM   2901  C CB   . ASP B 1 11  ? 3.146   104.157 11.395  1.00 8.93   ? 11  ASP B CB   1 
ATOM   2902  C CG   . ASP B 1 11  ? 3.825   104.851 12.538  1.00 9.15   ? 11  ASP B CG   1 
ATOM   2903  O OD1  . ASP B 1 11  ? 3.666   106.059 12.680  1.00 8.56   ? 11  ASP B OD1  1 
ATOM   2904  O OD2  . ASP B 1 11  ? 4.506   104.181 13.324  1.00 9.75   ? 11  ASP B OD2  1 
ATOM   2905  N N    . ASN B 1 12  ? 5.259   105.973 9.127   1.00 11.49  ? 12  ASN B N    1 
ATOM   2906  C CA   . ASN B 1 12  ? 6.593   106.209 8.744   1.00 13.66  ? 12  ASN B CA   1 
ATOM   2907  C C    . ASN B 1 12  ? 7.263   106.539 10.011  1.00 19.36  ? 12  ASN B C    1 
ATOM   2908  O O    . ASN B 1 12  ? 7.277   107.682 10.416  1.00 29.41  ? 12  ASN B O    1 
ATOM   2909  C CB   . ASN B 1 12  ? 6.588   107.489 7.948   1.00 8.88   ? 12  ASN B CB   1 
ATOM   2910  C CG   . ASN B 1 12  ? 5.433   107.600 7.014   1.00 9.83   ? 12  ASN B CG   1 
ATOM   2911  O OD1  . ASN B 1 12  ? 5.288   106.794 6.127   1.00 10.86  ? 12  ASN B OD1  1 
ATOM   2912  N ND2  . ASN B 1 12  ? 4.642   108.640 7.169   1.00 9.18   ? 12  ASN B ND2  1 
ATOM   2913  N N    . GLY B 1 13  ? 7.802   105.575 10.690  1.00 12.14  ? 13  GLY B N    1 
ATOM   2914  C CA   . GLY B 1 13  ? 8.425   105.985 11.888  1.00 13.54  ? 13  GLY B CA   1 
ATOM   2915  C C    . GLY B 1 13  ? 9.778   105.528 12.257  1.00 21.90  ? 13  GLY B C    1 
ATOM   2916  O O    . GLY B 1 13  ? 10.006  104.342 12.289  1.00 26.84  ? 13  GLY B O    1 
ATOM   2917  N N    . SER B 1 14  ? 10.681  106.443 12.537  1.00 20.43  ? 14  SER B N    1 
ATOM   2918  C CA   . SER B 1 14  ? 11.960  106.090 13.064  1.00 14.45  ? 14  SER B CA   1 
ATOM   2919  C C    . SER B 1 14  ? 12.488  105.088 12.165  1.00 17.56  ? 14  SER B C    1 
ATOM   2920  O O    . SER B 1 14  ? 12.342  105.204 10.976  1.00 42.36  ? 14  SER B O    1 
ATOM   2921  C CB   . SER B 1 14  ? 11.812  105.629 14.488  1.00 15.10  ? 14  SER B CB   1 
ATOM   2922  O OG   . SER B 1 14  ? 11.163  106.614 15.261  1.00 11.30  ? 14  SER B OG   1 
ATOM   2923  N N    . GLY B 1 15  ? 13.058  104.055 12.692  1.00 15.27  ? 15  GLY B N    1 
ATOM   2924  C CA   . GLY B 1 15  ? 13.544  102.975 11.866  1.00 22.28  ? 15  GLY B CA   1 
ATOM   2925  C C    . GLY B 1 15  ? 12.664  102.076 11.027  1.00 15.38  ? 15  GLY B C    1 
ATOM   2926  O O    . GLY B 1 15  ? 13.120  101.611 10.022  1.00 22.17  ? 15  GLY B O    1 
ATOM   2927  N N    . MET B 1 16  ? 11.478  101.726 11.483  1.00 10.47  ? 16  MET B N    1 
ATOM   2928  C CA   . MET B 1 16  ? 10.655  100.780 10.769  1.00 13.34  ? 16  MET B CA   1 
ATOM   2929  C C    . MET B 1 16  ? 9.301   101.272 10.355  1.00 13.00  ? 16  MET B C    1 
ATOM   2930  O O    . MET B 1 16  ? 8.633   101.934 11.115  1.00 13.08  ? 16  MET B O    1 
ATOM   2931  C CB   . MET B 1 16  ? 10.522  99.512  11.579  1.00 10.72  ? 16  MET B CB   1 
ATOM   2932  C CG   . MET B 1 16  ? 11.823  98.771  11.771  1.00 10.75  ? 16  MET B CG   1 
ATOM   2933  S SD   . MET B 1 16  ? 11.511  97.012  11.862  1.00 48.53  ? 16  MET B SD   1 
ATOM   2934  C CE   . MET B 1 16  ? 10.354  96.954  13.221  1.00 31.07  ? 16  MET B CE   1 
ATOM   2935  N N    . CYS B 1 17  ? 8.880   100.922 9.148   1.00 10.42  ? 17  CYS B N    1 
ATOM   2936  C CA   . CYS B 1 17  ? 7.630   101.415 8.628   1.00 11.87  ? 17  CYS B CA   1 
ATOM   2937  C C    . CYS B 1 17  ? 6.483   100.476 8.713   1.00 12.55  ? 17  CYS B C    1 
ATOM   2938  O O    . CYS B 1 17  ? 6.534   99.430  8.134   1.00 12.18  ? 17  CYS B O    1 
ATOM   2939  C CB   . CYS B 1 17  ? 7.784   101.961 7.221   1.00 15.91  ? 17  CYS B CB   1 
ATOM   2940  S SG   . CYS B 1 17  ? 8.896   103.367 7.020   1.00 32.49  ? 17  CYS B SG   1 
ATOM   2941  N N    . LYS B 1 18  ? 5.445   100.872 9.435   1.00 13.30  ? 18  LYS B N    1 
ATOM   2942  C CA   . LYS B 1 18  ? 4.329   100.037 9.675   1.00 10.23  ? 18  LYS B CA   1 
ATOM   2943  C C    . LYS B 1 18  ? 3.254   100.398 8.741   1.00 11.68  ? 18  LYS B C    1 
ATOM   2944  O O    . LYS B 1 18  ? 2.747   101.488 8.795   1.00 11.80  ? 18  LYS B O    1 
ATOM   2945  C CB   . LYS B 1 18  ? 3.918   100.288 11.087  1.00 9.06   ? 18  LYS B CB   1 
ATOM   2946  C CG   . LYS B 1 18  ? 5.086   100.665 11.979  1.00 9.46   ? 18  LYS B CG   1 
ATOM   2947  C CD   . LYS B 1 18  ? 4.781   100.536 13.456  1.00 8.09   ? 18  LYS B CD   1 
ATOM   2948  C CE   . LYS B 1 18  ? 3.463   101.186 13.821  1.00 10.73  ? 18  LYS B CE   1 
ATOM   2949  N NZ   . LYS B 1 18  ? 3.354   101.466 15.274  1.00 9.45   ? 18  LYS B NZ   1 
ATOM   2950  N N    . ALA B 1 19  ? 2.902   99.472  7.866   1.00 12.74  ? 19  ALA B N    1 
ATOM   2951  C CA   . ALA B 1 19  ? 1.909   99.734  6.871   1.00 10.71  ? 19  ALA B CA   1 
ATOM   2952  C C    . ALA B 1 19  ? 0.916   98.634  6.735   1.00 12.25  ? 19  ALA B C    1 
ATOM   2953  O O    . ALA B 1 19  ? 1.172   97.502  7.065   1.00 13.35  ? 19  ALA B O    1 
ATOM   2954  C CB   . ALA B 1 19  ? 2.554   99.991  5.551   1.00 9.13   ? 19  ALA B CB   1 
ATOM   2955  N N    . GLY B 1 20  ? -0.240  98.984  6.220   1.00 10.60  ? 20  GLY B N    1 
ATOM   2956  C CA   . GLY B 1 20  ? -1.283  98.028  6.059   1.00 11.11  ? 20  GLY B CA   1 
ATOM   2957  C C    . GLY B 1 20  ? -2.571  98.702  5.715   1.00 10.58  ? 20  GLY B C    1 
ATOM   2958  O O    . GLY B 1 20  ? -2.590  99.710  5.064   1.00 8.24   ? 20  GLY B O    1 
ATOM   2959  N N    . PHE B 1 21  ? -3.647  98.175  6.238   1.00 12.97  ? 21  PHE B N    1 
ATOM   2960  C CA   . PHE B 1 21  ? -4.945  98.660  5.896   1.00 16.05  ? 21  PHE B CA   1 
ATOM   2961  C C    . PHE B 1 21  ? -5.753  99.016  7.092   1.00 15.07  ? 21  PHE B C    1 
ATOM   2962  O O    . PHE B 1 21  ? -5.371  98.740  8.194   1.00 21.35  ? 21  PHE B O    1 
ATOM   2963  C CB   . PHE B 1 21  ? -5.710  97.545  5.166   1.00 23.54  ? 21  PHE B CB   1 
ATOM   2964  C CG   . PHE B 1 21  ? -4.940  96.885  4.063   1.00 20.44  ? 21  PHE B CG   1 
ATOM   2965  C CD1  . PHE B 1 21  ? -4.767  97.513  2.851   1.00 17.07  ? 21  PHE B CD1  1 
ATOM   2966  C CD2  . PHE B 1 21  ? -4.418  95.625  4.232   1.00 21.81  ? 21  PHE B CD2  1 
ATOM   2967  C CE1  . PHE B 1 21  ? -4.059  96.908  1.840   1.00 17.17  ? 21  PHE B CE1  1 
ATOM   2968  C CE2  . PHE B 1 21  ? -3.716  95.014  3.225   1.00 22.94  ? 21  PHE B CE2  1 
ATOM   2969  C CZ   . PHE B 1 21  ? -3.534  95.655  2.027   1.00 20.60  ? 21  PHE B CZ   1 
ATOM   2970  N N    . ALA B 1 22  ? -6.869  99.672  6.864   1.00 11.24  ? 22  ALA B N    1 
ATOM   2971  C CA   . ALA B 1 22  ? -7.748  100.034 7.942   1.00 13.50  ? 22  ALA B CA   1 
ATOM   2972  C C    . ALA B 1 22  ? -8.746  98.969  8.331   1.00 17.80  ? 22  ALA B C    1 
ATOM   2973  O O    . ALA B 1 22  ? -9.452  98.454  7.493   1.00 18.79  ? 22  ALA B O    1 
ATOM   2974  C CB   . ALA B 1 22  ? -8.444  101.334 7.637   1.00 10.18  ? 22  ALA B CB   1 
ATOM   2975  N N    . GLY B 1 23  ? -8.807  98.639  9.609   1.00 17.60  ? 23  GLY B N    1 
ATOM   2976  C CA   . GLY B 1 23  ? -9.739  97.676  10.108  1.00 14.87  ? 23  GLY B CA   1 
ATOM   2977  C C    . GLY B 1 23  ? -8.880  96.576  10.566  1.00 18.13  ? 23  GLY B C    1 
ATOM   2978  O O    . GLY B 1 23  ? -9.220  95.797  11.433  1.00 21.13  ? 23  GLY B O    1 
ATOM   2979  N N    . ASP B 1 24  ? -7.740  96.507  9.947   1.00 21.02  ? 24  ASP B N    1 
ATOM   2980  C CA   . ASP B 1 24  ? -6.834  95.463  10.274  1.00 27.93  ? 24  ASP B CA   1 
ATOM   2981  C C    . ASP B 1 24  ? -6.389  95.713  11.682  1.00 28.24  ? 24  ASP B C    1 
ATOM   2982  O O    . ASP B 1 24  ? -6.033  96.820  12.046  1.00 29.12  ? 24  ASP B O    1 
ATOM   2983  C CB   . ASP B 1 24  ? -5.696  95.435  9.261   1.00 22.88  ? 24  ASP B CB   1 
ATOM   2984  C CG   . ASP B 1 24  ? -6.057  94.678  8.016   1.00 28.71  ? 24  ASP B CG   1 
ATOM   2985  O OD1  . ASP B 1 24  ? -7.258  94.470  7.776   1.00 38.12  ? 24  ASP B OD1  1 
ATOM   2986  O OD2  . ASP B 1 24  ? -5.145  94.278  7.276   1.00 27.40  ? 24  ASP B OD2  1 
ATOM   2987  N N    . ASP B 1 25  ? -6.365  94.676  12.491  1.00 25.40  ? 25  ASP B N    1 
ATOM   2988  C CA   . ASP B 1 25  ? -6.028  94.843  13.873  1.00 23.28  ? 25  ASP B CA   1 
ATOM   2989  C C    . ASP B 1 25  ? -4.573  94.685  13.985  1.00 20.26  ? 25  ASP B C    1 
ATOM   2990  O O    . ASP B 1 25  ? -4.034  94.696  15.071  1.00 24.07  ? 25  ASP B O    1 
ATOM   2991  C CB   . ASP B 1 25  ? -6.733  93.771  14.686  1.00 31.71  ? 25  ASP B CB   1 
ATOM   2992  C CG   . ASP B 1 25  ? -8.239  93.946  14.718  1.00 33.20  ? 25  ASP B CG   1 
ATOM   2993  O OD1  . ASP B 1 25  ? -8.719  95.076  14.522  1.00 31.12  ? 25  ASP B OD1  1 
ATOM   2994  O OD2  . ASP B 1 25  ? -8.946  92.945  14.950  1.00 26.02  ? 25  ASP B OD2  1 
ATOM   2995  N N    . ALA B 1 26  ? -3.919  94.533  12.852  1.00 18.22  ? 26  ALA B N    1 
ATOM   2996  C CA   . ALA B 1 26  ? -2.473  94.409  12.839  1.00 18.44  ? 26  ALA B CA   1 
ATOM   2997  C C    . ALA B 1 26  ? -1.863  94.932  11.564  1.00 23.16  ? 26  ALA B C    1 
ATOM   2998  O O    . ALA B 1 26  ? -2.468  94.888  10.514  1.00 27.33  ? 26  ALA B O    1 
ATOM   2999  C CB   . ALA B 1 26  ? -2.057  92.971  13.059  1.00 13.78  ? 26  ALA B CB   1 
ATOM   3000  N N    . PRO B 1 27  ? -0.628  95.496  11.662  1.00 19.51  ? 27  PRO B N    1 
ATOM   3001  C CA   . PRO B 1 27  ? 0.001   95.889  10.418  1.00 16.18  ? 27  PRO B CA   1 
ATOM   3002  C C    . PRO B 1 27  ? 0.412   94.713  9.591   1.00 18.78  ? 27  PRO B C    1 
ATOM   3003  O O    . PRO B 1 27  ? 1.132   93.847  10.038  1.00 20.66  ? 27  PRO B O    1 
ATOM   3004  C CB   . PRO B 1 27  ? 1.252   96.599  10.887  1.00 14.82  ? 27  PRO B CB   1 
ATOM   3005  C CG   . PRO B 1 27  ? 1.011   97.013  12.268  1.00 17.36  ? 27  PRO B CG   1 
ATOM   3006  C CD   . PRO B 1 27  ? 0.236   95.872  12.806  1.00 20.67  ? 27  PRO B CD   1 
ATOM   3007  N N    . ARG B 1 28  ? -0.038  94.675  8.367   1.00 18.76  ? 28  ARG B N    1 
ATOM   3008  C CA   . ARG B 1 28  ? 0.379   93.621  7.475   1.00 22.68  ? 28  ARG B CA   1 
ATOM   3009  C C    . ARG B 1 28  ? 1.840   93.616  7.137   1.00 16.06  ? 28  ARG B C    1 
ATOM   3010  O O    . ARG B 1 28  ? 2.482   92.584  7.163   1.00 19.39  ? 28  ARG B O    1 
ATOM   3011  C CB   . ARG B 1 28  ? -0.455  93.670  6.190   1.00 22.30  ? 28  ARG B CB   1 
ATOM   3012  C CG   . ARG B 1 28  ? -0.043  92.672  5.137   1.00 22.05  ? 28  ARG B CG   1 
ATOM   3013  C CD   . ARG B 1 28  ? -1.034  92.642  3.999   1.00 20.65  ? 28  ARG B CD   1 
ATOM   3014  N NE   . ARG B 1 28  ? -0.554  91.767  2.945   1.00 34.55  ? 28  ARG B NE   1 
ATOM   3015  C CZ   . ARG B 1 28  ? -1.198  91.536  1.812   1.00 42.33  ? 28  ARG B CZ   1 
ATOM   3016  N NH1  . ARG B 1 28  ? -2.362  92.115  1.575   1.00 42.41  ? 28  ARG B NH1  1 
ATOM   3017  N NH2  . ARG B 1 28  ? -0.671  90.722  0.912   1.00 52.24  ? 28  ARG B NH2  1 
ATOM   3018  N N    . ALA B 1 29  ? 2.393   94.765  6.848   1.00 14.38  ? 29  ALA B N    1 
ATOM   3019  C CA   . ALA B 1 29  ? 3.802   94.820  6.596   1.00 17.19  ? 29  ALA B CA   1 
ATOM   3020  C C    . ALA B 1 29  ? 4.575   95.800  7.439   1.00 17.45  ? 29  ALA B C    1 
ATOM   3021  O O    . ALA B 1 29  ? 4.211   96.951  7.530   1.00 11.62  ? 29  ALA B O    1 
ATOM   3022  C CB   . ALA B 1 29  ? 4.029   95.086  5.153   1.00 19.69  ? 29  ALA B CB   1 
ATOM   3023  N N    . VAL B 1 30  ? 5.645   95.328  8.064   1.00 18.61  ? 30  VAL B N    1 
ATOM   3024  C CA   . VAL B 1 30  ? 6.494   96.162  8.891   1.00 14.50  ? 30  VAL B CA   1 
ATOM   3025  C C    . VAL B 1 30  ? 7.901   95.915  8.462   1.00 11.98  ? 30  VAL B C    1 
ATOM   3026  O O    . VAL B 1 30  ? 8.513   94.958  8.888   1.00 15.96  ? 30  VAL B O    1 
ATOM   3027  C CB   . VAL B 1 30  ? 6.327   95.948  10.398  1.00 13.63  ? 30  VAL B CB   1 
ATOM   3028  C CG1  . VAL B 1 30  ? 7.056   97.033  11.173  1.00 15.52  ? 30  VAL B CG1  1 
ATOM   3029  C CG2  . VAL B 1 30  ? 4.859   95.944  10.785  1.00 13.84  ? 30  VAL B CG2  1 
ATOM   3030  N N    . PHE B 1 31  ? 8.414   96.801  7.638   1.00 11.43  ? 31  PHE B N    1 
ATOM   3031  C CA   . PHE B 1 31  ? 9.743   96.712  7.079   1.00 13.82  ? 31  PHE B CA   1 
ATOM   3032  C C    . PHE B 1 31  ? 10.559  97.923  7.468   1.00 11.37  ? 31  PHE B C    1 
ATOM   3033  O O    . PHE B 1 31  ? 10.020  98.863  7.943   1.00 13.91  ? 31  PHE B O    1 
ATOM   3034  C CB   . PHE B 1 31  ? 9.604   96.612  5.548   1.00 16.15  ? 31  PHE B CB   1 
ATOM   3035  C CG   . PHE B 1 31  ? 9.073   97.840  4.880   1.00 13.91  ? 31  PHE B CG   1 
ATOM   3036  C CD1  . PHE B 1 31  ? 7.730   98.149  4.915   1.00 15.31  ? 31  PHE B CD1  1 
ATOM   3037  C CD2  . PHE B 1 31  ? 9.910   98.639  4.156   1.00 11.86  ? 31  PHE B CD2  1 
ATOM   3038  C CE1  . PHE B 1 31  ? 7.250   99.268  4.293   1.00 11.26  ? 31  PHE B CE1  1 
ATOM   3039  C CE2  . PHE B 1 31  ? 9.444   99.762  3.533   1.00 14.62  ? 31  PHE B CE2  1 
ATOM   3040  C CZ   . PHE B 1 31  ? 8.112   100.074 3.597   1.00 13.70  ? 31  PHE B CZ   1 
ATOM   3041  N N    . PRO B 1 32  ? 11.905  97.895  7.272   1.00 9.56   ? 32  PRO B N    1 
ATOM   3042  C CA   . PRO B 1 32  ? 12.637  99.118  7.557   1.00 10.41  ? 32  PRO B CA   1 
ATOM   3043  C C    . PRO B 1 32  ? 12.427  100.401 6.797   1.00 11.28  ? 32  PRO B C    1 
ATOM   3044  O O    . PRO B 1 32  ? 11.708  100.428 5.857   1.00 16.03  ? 32  PRO B O    1 
ATOM   3045  C CB   . PRO B 1 32  ? 14.044  98.689  7.328   1.00 11.33  ? 32  PRO B CB   1 
ATOM   3046  C CG   . PRO B 1 32  ? 14.088  97.335  7.870   1.00 11.67  ? 32  PRO B CG   1 
ATOM   3047  C CD   . PRO B 1 32  ? 12.884  96.774  7.214   1.00 12.41  ? 32  PRO B CD   1 
ATOM   3048  N N    . SER B 1 33  ? 13.127  101.457 7.180   1.00 12.58  ? 33  SER B N    1 
ATOM   3049  C CA   . SER B 1 33  ? 13.052  102.759 6.522   1.00 16.62  ? 33  SER B CA   1 
ATOM   3050  C C    . SER B 1 33  ? 14.429  102.996 6.073   1.00 17.13  ? 33  SER B C    1 
ATOM   3051  O O    . SER B 1 33  ? 15.089  103.902 6.537   1.00 20.07  ? 33  SER B O    1 
ATOM   3052  C CB   . SER B 1 33  ? 12.706  103.891 7.466   1.00 15.29  ? 33  SER B CB   1 
ATOM   3053  O OG   . SER B 1 33  ? 12.896  105.129 6.837   1.00 21.09  ? 33  SER B OG   1 
ATOM   3054  N N    . ILE B 1 34  ? 14.873  102.174 5.157   1.00 19.73  ? 34  ILE B N    1 
ATOM   3055  C CA   . ILE B 1 34  ? 16.199  102.266 4.683   1.00 20.15  ? 34  ILE B CA   1 
ATOM   3056  C C    . ILE B 1 34  ? 16.061  102.266 3.193   1.00 20.52  ? 34  ILE B C    1 
ATOM   3057  O O    . ILE B 1 34  ? 15.067  101.783 2.677   1.00 16.67  ? 34  ILE B O    1 
ATOM   3058  C CB   . ILE B 1 34  ? 16.993  101.054 5.208   1.00 13.85  ? 34  ILE B CB   1 
ATOM   3059  C CG1  . ILE B 1 34  ? 18.481  101.323 5.257   1.00 20.74  ? 34  ILE B CG1  1 
ATOM   3060  C CG2  . ILE B 1 34  ? 16.688  99.793  4.429   1.00 13.74  ? 34  ILE B CG2  1 
ATOM   3061  C CD1  . ILE B 1 34  ? 19.196  100.233 6.011   1.00 27.88  ? 34  ILE B CD1  1 
ATOM   3062  N N    . VAL B 1 35  ? 16.971  102.928 2.505   1.00 14.39  ? 35  VAL B N    1 
ATOM   3063  C CA   . VAL B 1 35  ? 16.992  102.916 1.079   1.00 15.55  ? 35  VAL B CA   1 
ATOM   3064  C C    . VAL B 1 35  ? 18.373  102.602 0.752   1.00 17.52  ? 35  VAL B C    1 
ATOM   3065  O O    . VAL B 1 35  ? 19.244  103.352 1.093   1.00 22.93  ? 35  VAL B O    1 
ATOM   3066  C CB   . VAL B 1 35  ? 16.830  104.322 0.560   1.00 20.15  ? 35  VAL B CB   1 
ATOM   3067  C CG1  . VAL B 1 35  ? 17.015  104.385 -0.945  1.00 19.99  ? 35  VAL B CG1  1 
ATOM   3068  C CG2  . VAL B 1 35  ? 15.476  104.878 0.956   1.00 19.79  ? 35  VAL B CG2  1 
ATOM   3069  N N    . GLY B 1 36  ? 18.613  101.565 -0.010  1.00 19.78  ? 36  GLY B N    1 
ATOM   3070  C CA   . GLY B 1 36  ? 19.966  101.285 -0.447  1.00 25.54  ? 36  GLY B CA   1 
ATOM   3071  C C    . GLY B 1 36  ? 20.323  101.453 -1.903  1.00 25.30  ? 36  GLY B C    1 
ATOM   3072  O O    . GLY B 1 36  ? 20.122  100.563 -2.690  1.00 30.90  ? 36  GLY B O    1 
ATOM   3073  N N    . ARG B 1 37  ? 20.881  102.580 -2.262  1.00 23.10  ? 37  ARG B N    1 
ATOM   3074  C CA   . ARG B 1 37  ? 21.282  102.849 -3.617  1.00 27.98  ? 37  ARG B CA   1 
ATOM   3075  C C    . ARG B 1 37  ? 22.651  102.209 -3.876  1.00 33.90  ? 37  ARG B C    1 
ATOM   3076  O O    . ARG B 1 37  ? 23.213  101.604 -2.995  1.00 33.05  ? 37  ARG B O    1 
ATOM   3077  C CB   . ARG B 1 37  ? 21.239  104.369 -3.874  1.00 22.98  ? 37  ARG B CB   1 
ATOM   3078  C CG   . ARG B 1 37  ? 19.861  104.940 -4.117  1.00 23.68  ? 37  ARG B CG   1 
ATOM   3079  C CD   . ARG B 1 37  ? 19.816  106.440 -3.912  1.00 23.39  ? 37  ARG B CD   1 
ATOM   3080  N NE   . ARG B 1 37  ? 20.303  107.193 -5.064  1.00 41.37  ? 37  ARG B NE   1 
ATOM   3081  C CZ   . ARG B 1 37  ? 19.534  107.641 -6.051  1.00 38.68  ? 37  ARG B CZ   1 
ATOM   3082  N NH1  . ARG B 1 37  ? 18.230  107.403 -6.043  1.00 45.07  ? 37  ARG B NH1  1 
ATOM   3083  N NH2  . ARG B 1 37  ? 20.066  108.327 -7.049  1.00 26.72  ? 37  ARG B NH2  1 
ATOM   3084  N N    . PRO B 1 38  ? 23.171  102.271 -5.107  1.00 31.07  ? 38  PRO B N    1 
ATOM   3085  C CA   . PRO B 1 38  ? 24.423  101.595 -5.414  1.00 26.85  ? 38  PRO B CA   1 
ATOM   3086  C C    . PRO B 1 38  ? 25.656  102.176 -4.846  1.00 28.76  ? 38  PRO B C    1 
ATOM   3087  O O    . PRO B 1 38  ? 25.676  103.330 -4.467  1.00 32.03  ? 38  PRO B O    1 
ATOM   3088  C CB   . PRO B 1 38  ? 24.513  101.760 -6.910  1.00 28.93  ? 38  PRO B CB   1 
ATOM   3089  C CG   . PRO B 1 38  ? 23.736  102.980 -7.220  1.00 28.36  ? 38  PRO B CG   1 
ATOM   3090  C CD   . PRO B 1 38  ? 22.559  102.800 -6.336  1.00 34.57  ? 38  PRO B CD   1 
ATOM   3091  N N    . ARG B 1 39  ? 26.690  101.365 -4.745  1.00 28.01  ? 39  ARG B N    1 
ATOM   3092  C CA   . ARG B 1 39  ? 27.931  101.898 -4.312  1.00 37.09  ? 39  ARG B CA   1 
ATOM   3093  C C    . ARG B 1 39  ? 28.685  102.460 -5.472  1.00 44.83  ? 39  ARG B C    1 
ATOM   3094  O O    . ARG B 1 39  ? 29.031  103.628 -5.490  1.00 60.97  ? 39  ARG B O    1 
ATOM   3095  C CB   . ARG B 1 39  ? 28.794  100.837 -3.688  1.00 40.91  ? 39  ARG B CB   1 
ATOM   3096  C CG   . ARG B 1 39  ? 30.229  101.305 -3.417  1.00 66.80  ? 39  ARG B CG   1 
ATOM   3097  C CD   . ARG B 1 39  ? 30.343  102.490 -2.452  1.00 78.37  ? 39  ARG B CD   1 
ATOM   3098  N NE   . ARG B 1 39  ? 30.692  103.763 -3.096  1.00 83.30  ? 39  ARG B NE   1 
ATOM   3099  C CZ   . ARG B 1 39  ? 29.976  104.885 -3.007  1.00 63.05  ? 39  ARG B CZ   1 
ATOM   3100  N NH1  . ARG B 1 39  ? 28.849  104.917 -2.311  1.00 51.98  ? 39  ARG B NH1  1 
ATOM   3101  N NH2  . ARG B 1 39  ? 30.378  105.977 -3.639  1.00 53.13  ? 39  ARG B NH2  1 
ATOM   3102  N N    . HIS B 1 40  ? 28.909  101.659 -6.481  1.00 41.28  ? 40  HIS B N    1 
ATOM   3103  C CA   . HIS B 1 40  ? 29.679  102.142 -7.583  1.00 44.03  ? 40  HIS B CA   1 
ATOM   3104  C C    . HIS B 1 40  ? 29.180  101.445 -8.820  1.00 46.05  ? 40  HIS B C    1 
ATOM   3105  O O    . HIS B 1 40  ? 28.664  100.356 -8.725  1.00 46.67  ? 40  HIS B O    1 
ATOM   3106  C CB   . HIS B 1 40  ? 31.168  101.921 -7.340  1.00 42.81  ? 40  HIS B CB   1 
ATOM   3107  C CG   . HIS B 1 40  ? 32.029  102.270 -8.518  1.00 56.27  ? 40  HIS B CG   1 
ATOM   3108  N ND1  . HIS B 1 40  ? 32.868  101.361 -9.125  1.00 61.20  ? 40  HIS B ND1  1 
ATOM   3109  C CD2  . HIS B 1 40  ? 32.149  103.420 -9.224  1.00 53.54  ? 40  HIS B CD2  1 
ATOM   3110  C CE1  . HIS B 1 40  ? 33.482  101.939 -10.142 1.00 49.07  ? 40  HIS B CE1  1 
ATOM   3111  N NE2  . HIS B 1 40  ? 33.062  103.188 -10.225 1.00 51.28  ? 40  HIS B NE2  1 
ATOM   3112  N N    . GLN B 1 41  ? 29.347  102.055 -9.983  1.00 40.22  ? 41  GLN B N    1 
ATOM   3113  C CA   . GLN B 1 41  ? 28.905  101.435 -11.177 1.00 31.61  ? 41  GLN B CA   1 
ATOM   3114  C C    . GLN B 1 41  ? 29.660  100.147 -11.142 1.00 33.35  ? 41  GLN B C    1 
ATOM   3115  O O    . GLN B 1 41  ? 30.862  100.137 -10.962 1.00 35.24  ? 41  GLN B O    1 
ATOM   3116  C CB   . GLN B 1 41  ? 29.291  102.295 -12.350 1.00 28.50  ? 41  GLN B CB   1 
ATOM   3117  N N    . GLY B 1 42  ? 28.986  99.041  -11.362 1.00 31.57  ? 42  GLY B N    1 
ATOM   3118  C CA   . GLY B 1 42  ? 29.611  97.749  -11.201 1.00 32.46  ? 42  GLY B CA   1 
ATOM   3119  C C    . GLY B 1 42  ? 28.674  96.950  -10.362 1.00 35.17  ? 42  GLY B C    1 
ATOM   3120  O O    . GLY B 1 42  ? 28.805  95.742  -10.279 1.00 38.87  ? 42  GLY B O    1 
ATOM   3121  N N    . VAL B 1 43  ? 27.737  97.615  -9.706  1.00 38.95  ? 43  VAL B N    1 
ATOM   3122  C CA   . VAL B 1 43  ? 26.707  96.932  -8.959  1.00 31.34  ? 43  VAL B CA   1 
ATOM   3123  C C    . VAL B 1 43  ? 25.461  97.350  -9.683  1.00 31.54  ? 43  VAL B C    1 
ATOM   3124  O O    . VAL B 1 43  ? 24.426  96.701  -9.575  1.00 27.49  ? 43  VAL B O    1 
ATOM   3125  C CB   . VAL B 1 43  ? 26.666  97.357  -7.497  1.00 29.76  ? 43  VAL B CB   1 
ATOM   3126  C CG1  . VAL B 1 43  ? 28.043  97.248  -6.871  1.00 40.24  ? 43  VAL B CG1  1 
ATOM   3127  C CG2  . VAL B 1 43  ? 26.138  98.762  -7.357  1.00 27.43  ? 43  VAL B CG2  1 
ATOM   3128  N N    . MET B 1 44  ? 25.570  98.417  -10.465 1.00 33.18  ? 44  MET B N    1 
ATOM   3129  C CA   . MET B 1 44  ? 24.453  98.896  -11.244 1.00 25.63  ? 44  MET B CA   1 
ATOM   3130  C C    . MET B 1 44  ? 24.751  98.116  -12.454 1.00 28.62  ? 44  MET B C    1 
ATOM   3131  O O    . MET B 1 44  ? 23.850  97.622  -13.121 1.00 28.18  ? 44  MET B O    1 
ATOM   3132  C CB   . MET B 1 44  ? 24.563  100.387 -11.484 1.00 16.73  ? 44  MET B CB   1 
ATOM   3133  C CG   . MET B 1 44  ? 23.295  101.153 -11.238 1.00 10.95  ? 44  MET B CG   1 
ATOM   3134  S SD   . MET B 1 44  ? 23.728  102.862 -11.496 1.00 23.05  ? 44  MET B SD   1 
ATOM   3135  C CE   . MET B 1 44  ? 25.369  102.879 -10.797 1.00 14.25  ? 44  MET B CE   1 
ATOM   3136  N N    . VAL B 1 45  ? 26.040  97.980  -12.739 1.00 31.86  ? 45  VAL B N    1 
ATOM   3137  C CA   . VAL B 1 45  ? 26.413  97.098  -13.828 1.00 33.68  ? 45  VAL B CA   1 
ATOM   3138  C C    . VAL B 1 45  ? 25.866  95.852  -13.331 1.00 30.92  ? 45  VAL B C    1 
ATOM   3139  O O    . VAL B 1 45  ? 25.998  95.515  -12.177 1.00 35.21  ? 45  VAL B O    1 
ATOM   3140  C CB   . VAL B 1 45  ? 27.927  96.996  -14.084 1.00 35.51  ? 45  VAL B CB   1 
ATOM   3141  C CG1  . VAL B 1 45  ? 28.216  95.974  -15.173 1.00 30.70  ? 45  VAL B CG1  1 
ATOM   3142  C CG2  . VAL B 1 45  ? 28.498  98.356  -14.453 1.00 32.65  ? 45  VAL B CG2  1 
ATOM   3143  N N    . GLY B 1 46  ? 25.246  95.124  -14.181 1.00 21.33  ? 46  GLY B N    1 
ATOM   3144  C CA   . GLY B 1 46  ? 24.619  93.994  -13.618 1.00 29.17  ? 46  GLY B CA   1 
ATOM   3145  C C    . GLY B 1 46  ? 23.306  93.996  -14.250 1.00 34.43  ? 46  GLY B C    1 
ATOM   3146  O O    . GLY B 1 46  ? 23.145  94.322  -15.413 1.00 39.83  ? 46  GLY B O    1 
ATOM   3147  N N    . MET B 1 47  ? 22.336  93.637  -13.482 1.00 26.18  ? 47  MET B N    1 
ATOM   3148  C CA   . MET B 1 47  ? 21.093  93.521  -14.082 1.00 32.23  ? 47  MET B CA   1 
ATOM   3149  C C    . MET B 1 47  ? 20.122  94.370  -13.379 1.00 30.47  ? 47  MET B C    1 
ATOM   3150  O O    . MET B 1 47  ? 20.191  94.570  -12.174 1.00 37.03  ? 47  MET B O    1 
ATOM   3151  C CB   . MET B 1 47  ? 20.685  92.054  -13.971 1.00 43.83  ? 47  MET B CB   1 
ATOM   3152  C CG   . MET B 1 47  ? 19.495  91.625  -14.800 1.00 52.53  ? 47  MET B CG   1 
ATOM   3153  S SD   . MET B 1 47  ? 19.323  89.845  -14.689 1.00 65.43  ? 47  MET B SD   1 
ATOM   3154  C CE   . MET B 1 47  ? 19.031  89.653  -12.937 1.00 36.63  ? 47  MET B CE   1 
ATOM   3155  N N    . GLY B 1 48  ? 19.213  94.908  -14.143 1.00 30.87  ? 48  GLY B N    1 
ATOM   3156  C CA   . GLY B 1 48  ? 18.164  95.611  -13.521 1.00 25.14  ? 48  GLY B CA   1 
ATOM   3157  C C    . GLY B 1 48  ? 17.830  96.923  -14.054 1.00 35.31  ? 48  GLY B C    1 
ATOM   3158  O O    . GLY B 1 48  ? 18.680  97.650  -14.537 1.00 39.74  ? 48  GLY B O    1 
ATOM   3159  N N    . GLN B 1 49  ? 16.558  97.230  -13.967 1.00 31.76  ? 49  GLN B N    1 
ATOM   3160  C CA   . GLN B 1 49  ? 16.143  98.525  -14.339 1.00 33.77  ? 49  GLN B CA   1 
ATOM   3161  C C    . GLN B 1 49  ? 16.013  99.169  -12.981 1.00 32.76  ? 49  GLN B C    1 
ATOM   3162  O O    . GLN B 1 49  ? 15.690  100.345 -12.884 1.00 25.11  ? 49  GLN B O    1 
ATOM   3163  C CB   . GLN B 1 49  ? 14.862  98.420  -15.129 1.00 28.50  ? 49  GLN B CB   1 
ATOM   3164  C CG   . GLN B 1 49  ? 14.767  99.439  -16.256 1.00 39.12  ? 49  GLN B CG   1 
ATOM   3165  C CD   . GLN B 1 49  ? 15.936  99.378  -17.230 1.00 38.13  ? 49  GLN B CD   1 
ATOM   3166  O OE1  . GLN B 1 49  ? 16.503  100.409 -17.598 1.00 28.05  ? 49  GLN B OE1  1 
ATOM   3167  N NE2  . GLN B 1 49  ? 16.296  98.173  -17.654 1.00 26.47  ? 49  GLN B NE2  1 
ATOM   3168  N N    . LYS B 1 50  ? 16.326  98.405  -11.938 1.00 28.13  ? 50  LYS B N    1 
ATOM   3169  C CA   . LYS B 1 50  ? 16.279  98.889  -10.566 1.00 26.73  ? 50  LYS B CA   1 
ATOM   3170  C C    . LYS B 1 50  ? 17.557  99.569  -10.027 1.00 32.87  ? 50  LYS B C    1 
ATOM   3171  O O    . LYS B 1 50  ? 18.632  98.977  -10.051 1.00 27.12  ? 50  LYS B O    1 
ATOM   3172  C CB   . LYS B 1 50  ? 15.920  97.701  -9.682  1.00 24.84  ? 50  LYS B CB   1 
ATOM   3173  C CG   . LYS B 1 50  ? 16.544  96.392  -10.104 1.00 24.16  ? 50  LYS B CG   1 
ATOM   3174  C CD   . LYS B 1 50  ? 16.166  95.283  -9.147  1.00 20.53  ? 50  LYS B CD   1 
ATOM   3175  C CE   . LYS B 1 50  ? 14.664  95.156  -9.018  1.00 17.30  ? 50  LYS B CE   1 
ATOM   3176  N NZ   . LYS B 1 50  ? 14.304  93.929  -8.258  1.00 26.88  ? 50  LYS B NZ   1 
ATOM   3177  N N    . ASP B 1 51  ? 17.445  100.785 -9.488  1.00 29.48  ? 51  ASP B N    1 
ATOM   3178  C CA   . ASP B 1 51  ? 18.605  101.523 -8.961  1.00 23.17  ? 51  ASP B CA   1 
ATOM   3179  C C    . ASP B 1 51  ? 18.909  101.213 -7.554  1.00 27.50  ? 51  ASP B C    1 
ATOM   3180  O O    . ASP B 1 51  ? 20.029  100.861 -7.225  1.00 27.25  ? 51  ASP B O    1 
ATOM   3181  C CB   . ASP B 1 51  ? 18.287  102.998 -8.939  1.00 24.05  ? 51  ASP B CB   1 
ATOM   3182  C CG   . ASP B 1 51  ? 19.520  103.868 -8.804  1.00 27.88  ? 51  ASP B CG   1 
ATOM   3183  O OD1  . ASP B 1 51  ? 20.638  103.371 -9.006  1.00 31.35  ? 51  ASP B OD1  1 
ATOM   3184  O OD2  . ASP B 1 51  ? 19.371  105.066 -8.513  1.00 29.49  ? 51  ASP B OD2  1 
ATOM   3185  N N    . SER B 1 52  ? 17.905  101.341 -6.703  1.00 34.85  ? 52  SER B N    1 
ATOM   3186  C CA   . SER B 1 52  ? 18.092  101.149 -5.291  1.00 27.44  ? 52  SER B CA   1 
ATOM   3187  C C    . SER B 1 52  ? 17.268  100.054 -4.789  1.00 24.54  ? 52  SER B C    1 
ATOM   3188  O O    . SER B 1 52  ? 16.230  99.742  -5.350  1.00 22.66  ? 52  SER B O    1 
ATOM   3189  C CB   . SER B 1 52  ? 17.628  102.373 -4.550  1.00 24.57  ? 52  SER B CB   1 
ATOM   3190  O OG   . SER B 1 52  ? 17.583  102.132 -3.169  1.00 27.16  ? 52  SER B OG   1 
ATOM   3191  N N    . TYR B 1 53  ? 17.720  99.467  -3.704  1.00 22.40  ? 53  TYR B N    1 
ATOM   3192  C CA   . TYR B 1 53  ? 16.989  98.401  -3.107  1.00 24.59  ? 53  TYR B CA   1 
ATOM   3193  C C    . TYR B 1 53  ? 16.492  99.026  -1.862  1.00 23.34  ? 53  TYR B C    1 
ATOM   3194  O O    . TYR B 1 53  ? 17.265  99.551  -1.102  1.00 19.75  ? 53  TYR B O    1 
ATOM   3195  C CB   . TYR B 1 53  ? 17.912  97.222  -2.840  1.00 24.53  ? 53  TYR B CB   1 
ATOM   3196  C CG   . TYR B 1 53  ? 18.234  96.366  -4.029  1.00 20.16  ? 53  TYR B CG   1 
ATOM   3197  C CD1  . TYR B 1 53  ? 19.233  96.721  -4.914  1.00 22.01  ? 53  TYR B CD1  1 
ATOM   3198  C CD2  . TYR B 1 53  ? 17.554  95.191  -4.250  1.00 23.13  ? 53  TYR B CD2  1 
ATOM   3199  C CE1  . TYR B 1 53  ? 19.537  95.928  -6.000  1.00 26.94  ? 53  TYR B CE1  1 
ATOM   3200  C CE2  . TYR B 1 53  ? 17.850  94.392  -5.332  1.00 31.79  ? 53  TYR B CE2  1 
ATOM   3201  C CZ   . TYR B 1 53  ? 18.844  94.766  -6.203  1.00 24.15  ? 53  TYR B CZ   1 
ATOM   3202  O OH   . TYR B 1 53  ? 19.136  93.967  -7.274  1.00 19.01  ? 53  TYR B OH   1 
ATOM   3203  N N    . VAL B 1 54  ? 15.188  99.001  -1.650  1.00 21.18  ? 54  VAL B N    1 
ATOM   3204  C CA   . VAL B 1 54  ? 14.623  99.694  -0.521  1.00 17.80  ? 54  VAL B CA   1 
ATOM   3205  C C    . VAL B 1 54  ? 13.965  98.762  0.421   1.00 18.54  ? 54  VAL B C    1 
ATOM   3206  O O    . VAL B 1 54  ? 13.242  97.888  0.020   1.00 17.29  ? 54  VAL B O    1 
ATOM   3207  C CB   . VAL B 1 54  ? 13.625  100.759 -0.968  1.00 11.77  ? 54  VAL B CB   1 
ATOM   3208  C CG1  . VAL B 1 54  ? 13.041  101.496 0.215   1.00 21.33  ? 54  VAL B CG1  1 
ATOM   3209  C CG2  . VAL B 1 54  ? 14.274  101.736 -1.918  1.00 14.54  ? 54  VAL B CG2  1 
ATOM   3210  N N    . GLY B 1 55  ? 14.274  98.903  1.686   1.00 16.84  ? 55  GLY B N    1 
ATOM   3211  C CA   . GLY B 1 55  ? 13.614  98.124  2.678   1.00 15.50  ? 55  GLY B CA   1 
ATOM   3212  C C    . GLY B 1 55  ? 14.234  96.875  3.172   1.00 15.17  ? 55  GLY B C    1 
ATOM   3213  O O    . GLY B 1 55  ? 15.404  96.812  3.459   1.00 17.03  ? 55  GLY B O    1 
ATOM   3214  N N    . ASP B 1 56  ? 13.418  95.850  3.254   1.00 16.29  ? 56  ASP B N    1 
ATOM   3215  C CA   . ASP B 1 56  ? 13.881  94.616  3.778   1.00 16.89  ? 56  ASP B CA   1 
ATOM   3216  C C    . ASP B 1 56  ? 15.145  94.034  3.121   1.00 27.15  ? 56  ASP B C    1 
ATOM   3217  O O    . ASP B 1 56  ? 16.009  93.426  3.712   1.00 28.43  ? 56  ASP B O    1 
ATOM   3218  C CB   . ASP B 1 56  ? 12.691  93.677  3.798   1.00 15.06  ? 56  ASP B CB   1 
ATOM   3219  C CG   . ASP B 1 56  ? 11.646  94.072  4.801   1.00 36.12  ? 56  ASP B CG   1 
ATOM   3220  O OD1  . ASP B 1 56  ? 11.937  94.900  5.686   1.00 42.66  ? 56  ASP B OD1  1 
ATOM   3221  O OD2  . ASP B 1 56  ? 10.513  93.575  4.687   1.00 45.52  ? 56  ASP B OD2  1 
ATOM   3222  N N    . GLU B 1 57  ? 15.319  94.283  1.828   1.00 30.21  ? 57  GLU B N    1 
ATOM   3223  C CA   . GLU B 1 57  ? 16.451  93.723  1.068   1.00 22.37  ? 57  GLU B CA   1 
ATOM   3224  C C    . GLU B 1 57  ? 17.619  94.614  0.931   1.00 23.75  ? 57  GLU B C    1 
ATOM   3225  O O    . GLU B 1 57  ? 18.627  94.212  0.385   1.00 23.66  ? 57  GLU B O    1 
ATOM   3226  C CB   . GLU B 1 57  ? 16.015  93.402  -0.340  1.00 27.99  ? 57  GLU B CB   1 
ATOM   3227  C CG   . GLU B 1 57  ? 15.354  92.050  -0.534  1.00 40.72  ? 57  GLU B CG   1 
ATOM   3228  C CD   . GLU B 1 57  ? 15.134  91.727  -2.001  1.00 40.43  ? 57  GLU B CD   1 
ATOM   3229  O OE1  . GLU B 1 57  ? 14.873  92.663  -2.782  1.00 30.73  ? 57  GLU B OE1  1 
ATOM   3230  O OE2  . GLU B 1 57  ? 15.219  90.540  -2.374  1.00 39.30  ? 57  GLU B OE2  1 
ATOM   3231  N N    . ALA B 1 58  ? 17.477  95.847  1.344   1.00 20.38  ? 58  ALA B N    1 
ATOM   3232  C CA   . ALA B 1 58  ? 18.600  96.740  1.360   1.00 24.67  ? 58  ALA B CA   1 
ATOM   3233  C C    . ALA B 1 58  ? 19.581  96.302  2.361   1.00 27.36  ? 58  ALA B C    1 
ATOM   3234  O O    . ALA B 1 58  ? 20.757  96.496  2.212   1.00 31.22  ? 58  ALA B O    1 
ATOM   3235  C CB   . ALA B 1 58  ? 18.160  98.112  1.698   1.00 24.70  ? 58  ALA B CB   1 
ATOM   3236  N N    . GLN B 1 59  ? 19.103  95.780  3.452   1.00 26.49  ? 59  GLN B N    1 
ATOM   3237  C CA   . GLN B 1 59  ? 19.997  95.440  4.494   1.00 32.60  ? 59  GLN B CA   1 
ATOM   3238  C C    . GLN B 1 59  ? 20.612  94.120  4.203   1.00 31.44  ? 59  GLN B C    1 
ATOM   3239  O O    . GLN B 1 59  ? 21.720  93.839  4.647   1.00 31.39  ? 59  GLN B O    1 
ATOM   3240  C CB   . GLN B 1 59  ? 19.245  95.489  5.822   1.00 43.94  ? 59  GLN B CB   1 
ATOM   3241  C CG   . GLN B 1 59  ? 19.602  94.422  6.857   1.00 51.89  ? 59  GLN B CG   1 
ATOM   3242  C CD   . GLN B 1 59  ? 20.893  94.698  7.603   1.00 39.10  ? 59  GLN B CD   1 
ATOM   3243  O OE1  . GLN B 1 59  ? 21.275  95.845  7.797   1.00 41.64  ? 59  GLN B OE1  1 
ATOM   3244  N NE2  . GLN B 1 59  ? 21.562  93.643  8.031   1.00 38.82  ? 59  GLN B NE2  1 
ATOM   3245  N N    . SER B 1 60  ? 19.922  93.303  3.428   1.00 30.35  ? 60  SER B N    1 
ATOM   3246  C CA   . SER B 1 60  ? 20.524  92.042  3.046   1.00 33.58  ? 60  SER B CA   1 
ATOM   3247  C C    . SER B 1 60  ? 21.773  92.218  2.222   1.00 30.07  ? 60  SER B C    1 
ATOM   3248  O O    . SER B 1 60  ? 22.783  91.582  2.467   1.00 25.32  ? 60  SER B O    1 
ATOM   3249  C CB   . SER B 1 60  ? 19.484  91.288  2.249   1.00 31.82  ? 60  SER B CB   1 
ATOM   3250  O OG   . SER B 1 60  ? 18.210  91.421  2.842   1.00 32.08  ? 60  SER B OG   1 
ATOM   3251  N N    . LYS B 1 61  ? 21.717  93.109  1.257   1.00 26.05  ? 61  LYS B N    1 
ATOM   3252  C CA   . LYS B 1 61  ? 22.868  93.425  0.482   1.00 27.78  ? 61  LYS B CA   1 
ATOM   3253  C C    . LYS B 1 61  ? 23.206  94.849  0.654   1.00 30.95  ? 61  LYS B C    1 
ATOM   3254  O O    . LYS B 1 61  ? 22.451  95.700  0.245   1.00 40.55  ? 61  LYS B O    1 
ATOM   3255  C CB   . LYS B 1 61  ? 22.478  93.227  -0.951  1.00 33.40  ? 61  LYS B CB   1 
ATOM   3256  C CG   . LYS B 1 61  ? 22.162  91.805  -1.372  1.00 31.38  ? 61  LYS B CG   1 
ATOM   3257  C CD   . LYS B 1 61  ? 21.833  91.753  -2.852  1.00 31.36  ? 61  LYS B CD   1 
ATOM   3258  C CE   . LYS B 1 61  ? 20.525  92.455  -3.136  1.00 22.67  ? 61  LYS B CE   1 
ATOM   3259  N NZ   . LYS B 1 61  ? 19.399  91.775  -2.450  1.00 24.57  ? 61  LYS B NZ   1 
ATOM   3260  N N    . ARG B 1 62  ? 24.278  95.154  1.350   1.00 27.07  ? 62  ARG B N    1 
ATOM   3261  C CA   . ARG B 1 62  ? 24.541  96.528  1.698   1.00 30.71  ? 62  ARG B CA   1 
ATOM   3262  C C    . ARG B 1 62  ? 25.980  96.830  1.797   1.00 32.77  ? 62  ARG B C    1 
ATOM   3263  O O    . ARG B 1 62  ? 26.390  97.899  2.234   1.00 31.16  ? 62  ARG B O    1 
ATOM   3264  C CB   . ARG B 1 62  ? 23.885  96.910  3.010   1.00 34.19  ? 62  ARG B CB   1 
ATOM   3265  C CG   . ARG B 1 62  ? 24.370  96.138  4.221   1.00 43.34  ? 62  ARG B CG   1 
ATOM   3266  C CD   . ARG B 1 62  ? 23.650  96.601  5.469   1.00 49.72  ? 62  ARG B CD   1 
ATOM   3267  N NE   . ARG B 1 62  ? 23.976  97.984  5.781   1.00 57.21  ? 62  ARG B NE   1 
ATOM   3268  C CZ   . ARG B 1 62  ? 25.043  98.361  6.475   1.00 55.70  ? 62  ARG B CZ   1 
ATOM   3269  N NH1  . ARG B 1 62  ? 25.886  97.453  6.935   1.00 54.14  ? 62  ARG B NH1  1 
ATOM   3270  N NH2  . ARG B 1 62  ? 25.269  99.642  6.701   1.00 67.55  ? 62  ARG B NH2  1 
ATOM   3271  N N    . GLY B 1 63  ? 26.763  95.842  1.455   1.00 28.81  ? 63  GLY B N    1 
ATOM   3272  C CA   . GLY B 1 63  ? 28.170  96.096  1.423   1.00 42.59  ? 63  GLY B CA   1 
ATOM   3273  C C    . GLY B 1 63  ? 28.369  96.364  -0.031  1.00 45.18  ? 63  GLY B C    1 
ATOM   3274  O O    . GLY B 1 63  ? 29.400  96.884  -0.459  1.00 48.22  ? 63  GLY B O    1 
ATOM   3275  N N    . ILE B 1 64  ? 27.383  95.971  -0.807  1.00 32.52  ? 64  ILE B N    1 
ATOM   3276  C CA   . ILE B 1 64  ? 27.466  96.222  -2.193  1.00 37.02  ? 64  ILE B CA   1 
ATOM   3277  C C    . ILE B 1 64  ? 26.652  97.431  -2.416  1.00 37.37  ? 64  ILE B C    1 
ATOM   3278  O O    . ILE B 1 64  ? 27.044  98.314  -3.142  1.00 45.17  ? 64  ILE B O    1 
ATOM   3279  C CB   . ILE B 1 64  ? 26.837  95.071  -2.949  1.00 46.35  ? 64  ILE B CB   1 
ATOM   3280  C CG1  . ILE B 1 64  ? 26.606  93.888  -2.010  1.00 49.23  ? 64  ILE B CG1  1 
ATOM   3281  C CG2  . ILE B 1 64  ? 27.718  94.648  -4.111  1.00 37.56  ? 64  ILE B CG2  1 
ATOM   3282  C CD1  . ILE B 1 64  ? 26.113  92.641  -2.707  1.00 49.37  ? 64  ILE B CD1  1 
ATOM   3283  N N    . LEU B 1 65  ? 25.507  97.493  -1.771  1.00 33.95  ? 65  LEU B N    1 
ATOM   3284  C CA   . LEU B 1 65  ? 24.606  98.607  -1.954  1.00 35.68  ? 65  LEU B CA   1 
ATOM   3285  C C    . LEU B 1 65  ? 24.612  99.578  -0.803  1.00 33.95  ? 65  LEU B C    1 
ATOM   3286  O O    . LEU B 1 65  ? 23.985  99.342  0.207   1.00 29.61  ? 65  LEU B O    1 
ATOM   3287  C CB   . LEU B 1 65  ? 23.219  98.056  -2.094  1.00 34.83  ? 65  LEU B CB   1 
ATOM   3288  C CG   . LEU B 1 65  ? 22.861  97.328  -3.389  1.00 46.18  ? 65  LEU B CG   1 
ATOM   3289  C CD1  . LEU B 1 65  ? 23.492  98.007  -4.590  1.00 42.71  ? 65  LEU B CD1  1 
ATOM   3290  C CD2  . LEU B 1 65  ? 23.199  95.847  -3.367  1.00 40.90  ? 65  LEU B CD2  1 
ATOM   3291  N N    . THR B 1 66  ? 25.252  100.714 -0.979  1.00 32.43  ? 66  THR B N    1 
ATOM   3292  C CA   . THR B 1 66  ? 25.382  101.658 0.092   1.00 26.85  ? 66  THR B CA   1 
ATOM   3293  C C    . THR B 1 66  ? 24.134  102.379 0.359   1.00 25.37  ? 66  THR B C    1 
ATOM   3294  O O    . THR B 1 66  ? 23.520  102.868 -0.552  1.00 24.79  ? 66  THR B O    1 
ATOM   3295  C CB   . THR B 1 66  ? 26.532  102.595 -0.162  1.00 34.77  ? 66  THR B CB   1 
ATOM   3296  O OG1  . THR B 1 66  ? 26.306  103.314 -1.377  1.00 38.51  ? 66  THR B OG1  1 
ATOM   3297  C CG2  . THR B 1 66  ? 27.794  101.780 -0.260  1.00 30.16  ? 66  THR B CG2  1 
ATOM   3298  N N    . LEU B 1 67  ? 23.806  102.550 1.627   1.00 27.32  ? 67  LEU B N    1 
ATOM   3299  C CA   . LEU B 1 67  ? 22.504  103.074 1.966   1.00 26.57  ? 67  LEU B CA   1 
ATOM   3300  C C    . LEU B 1 67  ? 22.233  104.331 2.679   1.00 22.05  ? 67  LEU B C    1 
ATOM   3301  O O    . LEU B 1 67  ? 23.107  104.917 3.295   1.00 20.38  ? 67  LEU B O    1 
ATOM   3302  C CB   . LEU B 1 67  ? 21.742  102.001 2.748   1.00 26.06  ? 67  LEU B CB   1 
ATOM   3303  C CG   . LEU B 1 67  ? 22.469  100.745 3.199   1.00 35.04  ? 67  LEU B CG   1 
ATOM   3304  C CD1  . LEU B 1 67  ? 23.220  101.023 4.479   1.00 28.02  ? 67  LEU B CD1  1 
ATOM   3305  C CD2  . LEU B 1 67  ? 21.454  99.651  3.423   1.00 29.02  ? 67  LEU B CD2  1 
ATOM   3306  N N    . LYS B 1 68  ? 20.979  104.745 2.581   1.00 19.95  ? 68  LYS B N    1 
ATOM   3307  C CA   . LYS B 1 68  ? 20.539  105.905 3.288   1.00 18.00  ? 68  LYS B CA   1 
ATOM   3308  C C    . LYS B 1 68  ? 19.455  105.545 4.230   1.00 16.03  ? 68  LYS B C    1 
ATOM   3309  O O    . LYS B 1 68  ? 18.652  104.693 3.952   1.00 15.86  ? 68  LYS B O    1 
ATOM   3310  C CB   . LYS B 1 68  ? 20.074  107.004 2.351   1.00 17.07  ? 68  LYS B CB   1 
ATOM   3311  C CG   . LYS B 1 68  ? 21.189  107.895 1.843   1.00 11.27  ? 68  LYS B CG   1 
ATOM   3312  C CD   . LYS B 1 68  ? 20.626  109.196 1.322   1.00 8.73   ? 68  LYS B CD   1 
ATOM   3313  C CE   . LYS B 1 68  ? 21.679  110.035 0.641   1.00 13.46  ? 68  LYS B CE   1 
ATOM   3314  N NZ   . LYS B 1 68  ? 21.121  111.350 0.231   1.00 25.59  ? 68  LYS B NZ   1 
ATOM   3315  N N    . TYR B 1 69  ? 19.468  106.190 5.378   1.00 20.03  ? 69  TYR B N    1 
ATOM   3316  C CA   . TYR B 1 69  ? 18.470  105.983 6.371   1.00 20.59  ? 69  TYR B CA   1 
ATOM   3317  C C    . TYR B 1 69  ? 17.761  107.296 6.514   1.00 16.32  ? 69  TYR B C    1 
ATOM   3318  O O    . TYR B 1 69  ? 18.286  108.204 7.128   1.00 13.70  ? 69  TYR B O    1 
ATOM   3319  C CB   . TYR B 1 69  ? 19.162  105.651 7.685   1.00 17.35  ? 69  TYR B CB   1 
ATOM   3320  C CG   . TYR B 1 69  ? 20.267  104.636 7.633   1.00 15.99  ? 69  TYR B CG   1 
ATOM   3321  C CD1  . TYR B 1 69  ? 21.549  104.997 7.264   1.00 21.47  ? 69  TYR B CD1  1 
ATOM   3322  C CD2  . TYR B 1 69  ? 20.044  103.338 8.016   1.00 12.68  ? 69  TYR B CD2  1 
ATOM   3323  C CE1  . TYR B 1 69  ? 22.565  104.074 7.230   1.00 22.92  ? 69  TYR B CE1  1 
ATOM   3324  C CE2  . TYR B 1 69  ? 21.058  102.412 7.992   1.00 19.33  ? 69  TYR B CE2  1 
ATOM   3325  C CZ   . TYR B 1 69  ? 22.313  102.786 7.598   1.00 25.10  ? 69  TYR B CZ   1 
ATOM   3326  O OH   . TYR B 1 69  ? 23.326  101.862 7.580   1.00 34.11  ? 69  TYR B OH   1 
ATOM   3327  N N    . PRO B 1 70  ? 16.573  107.405 5.933   1.00 14.67  ? 70  PRO B N    1 
ATOM   3328  C CA   . PRO B 1 70  ? 15.782  108.617 6.036   1.00 19.37  ? 70  PRO B CA   1 
ATOM   3329  C C    . PRO B 1 70  ? 14.893  108.568 7.261   1.00 31.55  ? 70  PRO B C    1 
ATOM   3330  O O    . PRO B 1 70  ? 14.804  107.466 7.800   1.00 42.33  ? 70  PRO B O    1 
ATOM   3331  C CB   . PRO B 1 70  ? 14.976  108.601 4.745   1.00 13.55  ? 70  PRO B CB   1 
ATOM   3332  C CG   . PRO B 1 70  ? 15.568  107.545 3.894   1.00 20.31  ? 70  PRO B CG   1 
ATOM   3333  C CD   . PRO B 1 70  ? 16.069  106.541 4.865   1.00 14.80  ? 70  PRO B CD   1 
ATOM   3334  N N    . ILE B 1 71  ? 14.262  109.636 7.715   1.00 21.64  ? 71  ILE B N    1 
ATOM   3335  C CA   . ILE B 1 71  ? 13.333  109.549 8.858   1.00 19.32  ? 71  ILE B CA   1 
ATOM   3336  C C    . ILE B 1 71  ? 13.777  108.718 10.038  1.00 20.82  ? 71  ILE B C    1 
ATOM   3337  O O    . ILE B 1 71  ? 13.015  107.935 10.534  1.00 28.08  ? 71  ILE B O    1 
ATOM   3338  C CB   . ILE B 1 71  ? 11.885  109.221 8.402   1.00 17.41  ? 71  ILE B CB   1 
ATOM   3339  C CG1  . ILE B 1 71  ? 10.838  109.510 9.464   1.00 22.88  ? 71  ILE B CG1  1 
ATOM   3340  C CG2  . ILE B 1 71  ? 11.702  107.825 7.835   1.00 22.24  ? 71  ILE B CG2  1 
ATOM   3341  C CD1  . ILE B 1 71  ? 9.444   109.400 8.914   1.00 27.36  ? 71  ILE B CD1  1 
ATOM   3342  N N    . GLU B 1 72  ? 14.976  108.921 10.570  1.00 22.95  ? 72  GLU B N    1 
ATOM   3343  C CA   . GLU B 1 72  ? 15.432  108.035 11.617  1.00 21.68  ? 72  GLU B CA   1 
ATOM   3344  C C    . GLU B 1 72  ? 15.160  108.726 12.907  1.00 21.41  ? 72  GLU B C    1 
ATOM   3345  O O    . GLU B 1 72  ? 15.357  108.141 13.954  1.00 23.28  ? 72  GLU B O    1 
ATOM   3346  C CB   . GLU B 1 72  ? 16.932  107.889 11.483  1.00 26.74  ? 72  GLU B CB   1 
ATOM   3347  C CG   . GLU B 1 72  ? 17.467  106.533 11.073  1.00 37.86  ? 72  GLU B CG   1 
ATOM   3348  C CD   . GLU B 1 72  ? 18.962  106.435 11.327  1.00 36.69  ? 72  GLU B CD   1 
ATOM   3349  O OE1  . GLU B 1 72  ? 19.589  107.489 11.545  1.00 26.57  ? 72  GLU B OE1  1 
ATOM   3350  O OE2  . GLU B 1 72  ? 19.508  105.314 11.318  1.00 31.84  ? 72  GLU B OE2  1 
ATOM   3351  N N    . HIS B 1 73  ? 14.772  109.987 12.846  1.00 15.17  ? 73  HIS B N    1 
ATOM   3352  C CA   . HIS B 1 73  ? 14.533  110.773 14.021  1.00 12.71  ? 73  HIS B CA   1 
ATOM   3353  C C    . HIS B 1 73  ? 13.140  111.259 13.935  1.00 11.41  ? 73  HIS B C    1 
ATOM   3354  O O    . HIS B 1 73  ? 12.789  112.240 14.541  1.00 10.84  ? 73  HIS B O    1 
ATOM   3355  C CB   . HIS B 1 73  ? 15.498  111.924 14.082  1.00 13.48  ? 73  HIS B CB   1 
ATOM   3356  C CG   . HIS B 1 73  ? 16.899  111.531 14.404  1.00 15.29  ? 73  HIS B CG   1 
ATOM   3357  N ND1  . HIS B 1 73  ? 17.288  111.137 15.663  1.00 24.45  ? 73  HIS B ND1  1 
ATOM   3358  C CD2  . HIS B 1 73  ? 18.011  111.492 13.637  1.00 21.61  ? 73  HIS B CD2  1 
ATOM   3359  C CE1  . HIS B 1 73  ? 18.578  110.858 15.655  1.00 28.92  ? 73  HIS B CE1  1 
ATOM   3360  N NE2  . HIS B 1 73  ? 19.040  111.064 14.437  1.00 26.02  ? 73  HIS B NE2  1 
ATOM   3361  N N    . GLY B 1 74  ? 12.351  110.640 13.101  1.00 12.40  ? 74  GLY B N    1 
ATOM   3362  C CA   . GLY B 1 74  ? 10.949  110.968 12.965  1.00 14.04  ? 74  GLY B CA   1 
ATOM   3363  C C    . GLY B 1 74  ? 10.602  111.977 11.926  1.00 9.94   ? 74  GLY B C    1 
ATOM   3364  O O    . GLY B 1 74  ? 9.503   111.973 11.424  1.00 10.60  ? 74  GLY B O    1 
ATOM   3365  N N    . ILE B 1 75  ? 11.568  112.752 11.503  1.00 9.87   ? 75  ILE B N    1 
ATOM   3366  C CA   . ILE B 1 75  ? 11.342  113.781 10.559  1.00 11.36  ? 75  ILE B CA   1 
ATOM   3367  C C    . ILE B 1 75  ? 11.990  113.239 9.349   1.00 18.32  ? 75  ILE B C    1 
ATOM   3368  O O    . ILE B 1 75  ? 13.084  112.718 9.431   1.00 20.71  ? 75  ILE B O    1 
ATOM   3369  C CB   . ILE B 1 75  ? 12.008  115.069 11.024  1.00 13.28  ? 75  ILE B CB   1 
ATOM   3370  C CG1  . ILE B 1 75  ? 13.313  114.752 11.753  1.00 14.20  ? 75  ILE B CG1  1 
ATOM   3371  C CG2  . ILE B 1 75  ? 11.066  115.866 11.910  1.00 8.79   ? 75  ILE B CG2  1 
ATOM   3372  C CD1  . ILE B 1 75  ? 14.205  115.946 11.989  1.00 19.00  ? 75  ILE B CD1  1 
ATOM   3373  N N    . VAL B 1 76  ? 11.359  113.381 8.200   1.00 16.15  ? 76  VAL B N    1 
ATOM   3374  C CA   . VAL B 1 76  ? 11.838  112.734 6.992   1.00 15.34  ? 76  VAL B CA   1 
ATOM   3375  C C    . VAL B 1 76  ? 13.208  112.993 6.363   1.00 16.68  ? 76  VAL B C    1 
ATOM   3376  O O    . VAL B 1 76  ? 13.859  112.012 6.038   1.00 22.61  ? 76  VAL B O    1 
ATOM   3377  C CB   . VAL B 1 76  ? 10.766  112.874 5.934   1.00 14.90  ? 76  VAL B CB   1 
ATOM   3378  C CG1  . VAL B 1 76  ? 11.125  112.108 4.687   1.00 19.59  ? 76  VAL B CG1  1 
ATOM   3379  C CG2  . VAL B 1 76  ? 9.433   112.413 6.489   1.00 14.30  ? 76  VAL B CG2  1 
ATOM   3380  N N    . THR B 1 77  ? 13.689  114.221 6.243   1.00 11.91  ? 77  THR B N    1 
ATOM   3381  C CA   . THR B 1 77  ? 15.044  114.507 5.722   1.00 15.24  ? 77  THR B CA   1 
ATOM   3382  C C    . THR B 1 77  ? 15.308  114.371 4.224   1.00 19.33  ? 77  THR B C    1 
ATOM   3383  O O    . THR B 1 77  ? 15.788  115.309 3.599   1.00 24.19  ? 77  THR B O    1 
ATOM   3384  C CB   . THR B 1 77  ? 16.151  113.698 6.418   1.00 15.24  ? 77  THR B CB   1 
ATOM   3385  O OG1  . THR B 1 77  ? 15.861  113.584 7.811   1.00 32.72  ? 77  THR B OG1  1 
ATOM   3386  C CG2  . THR B 1 77  ? 17.496  114.363 6.246   1.00 17.58  ? 77  THR B CG2  1 
ATOM   3387  N N    . ASN B 1 78  ? 15.056  113.204 3.647   1.00 20.77  ? 78  ASN B N    1 
ATOM   3388  C CA   . ASN B 1 78  ? 15.233  112.995 2.221   1.00 14.83  ? 78  ASN B CA   1 
ATOM   3389  C C    . ASN B 1 78  ? 13.886  112.797 1.692   1.00 13.14  ? 78  ASN B C    1 
ATOM   3390  O O    . ASN B 1 78  ? 13.209  111.868 2.053   1.00 15.25  ? 78  ASN B O    1 
ATOM   3391  C CB   . ASN B 1 78  ? 16.051  111.756 1.919   1.00 12.33  ? 78  ASN B CB   1 
ATOM   3392  C CG   . ASN B 1 78  ? 17.320  112.056 1.172   1.00 13.66  ? 78  ASN B CG   1 
ATOM   3393  O OD1  . ASN B 1 78  ? 17.357  112.002 -0.047  1.00 22.97  ? 78  ASN B OD1  1 
ATOM   3394  N ND2  . ASN B 1 78  ? 18.377  112.361 1.905   1.00 23.72  ? 78  ASN B ND2  1 
ATOM   3395  N N    . TRP B 1 79  ? 13.507  113.654 0.786   1.00 11.18  ? 79  TRP B N    1 
ATOM   3396  C CA   . TRP B 1 79  ? 12.207  113.572 0.233   1.00 14.21  ? 79  TRP B CA   1 
ATOM   3397  C C    . TRP B 1 79  ? 12.194  112.847 -1.088  1.00 15.42  ? 79  TRP B C    1 
ATOM   3398  O O    . TRP B 1 79  ? 11.162  112.712 -1.700  1.00 14.15  ? 79  TRP B O    1 
ATOM   3399  C CB   . TRP B 1 79  ? 11.651  114.965 0.119   1.00 13.01  ? 79  TRP B CB   1 
ATOM   3400  C CG   . TRP B 1 79  ? 11.039  115.426 1.337   1.00 11.49  ? 79  TRP B CG   1 
ATOM   3401  C CD1  . TRP B 1 79  ? 11.413  116.481 2.088   1.00 13.05  ? 79  TRP B CD1  1 
ATOM   3402  C CD2  . TRP B 1 79  ? 9.925   114.838 1.986   1.00 12.57  ? 79  TRP B CD2  1 
ATOM   3403  N NE1  . TRP B 1 79  ? 10.597  116.599 3.169   1.00 11.60  ? 79  TRP B NE1  1 
ATOM   3404  C CE2  . TRP B 1 79  ? 9.672   115.592 3.128   1.00 13.04  ? 79  TRP B CE2  1 
ATOM   3405  C CE3  . TRP B 1 79  ? 9.111   113.740 1.710   1.00 13.88  ? 79  TRP B CE3  1 
ATOM   3406  C CZ2  . TRP B 1 79  ? 8.650   115.290 3.988   1.00 14.70  ? 79  TRP B CZ2  1 
ATOM   3407  C CZ3  . TRP B 1 79  ? 8.106   113.448 2.559   1.00 13.14  ? 79  TRP B CZ3  1 
ATOM   3408  C CH2  . TRP B 1 79  ? 7.881   114.216 3.686   1.00 13.23  ? 79  TRP B CH2  1 
ATOM   3409  N N    . ASP B 1 80  ? 13.339  112.359 -1.514  1.00 12.93  ? 80  ASP B N    1 
ATOM   3410  C CA   . ASP B 1 80  ? 13.445  111.636 -2.742  1.00 13.62  ? 80  ASP B CA   1 
ATOM   3411  C C    . ASP B 1 80  ? 13.575  110.219 -2.367  1.00 14.33  ? 80  ASP B C    1 
ATOM   3412  O O    . ASP B 1 80  ? 13.090  109.344 -3.042  1.00 18.87  ? 80  ASP B O    1 
ATOM   3413  C CB   . ASP B 1 80  ? 14.711  112.054 -3.442  1.00 19.40  ? 80  ASP B CB   1 
ATOM   3414  C CG   . ASP B 1 80  ? 14.497  113.176 -4.438  1.00 32.29  ? 80  ASP B CG   1 
ATOM   3415  O OD1  . ASP B 1 80  ? 13.337  113.521 -4.726  1.00 32.07  ? 80  ASP B OD1  1 
ATOM   3416  O OD2  . ASP B 1 80  ? 15.501  113.710 -4.943  1.00 28.62  ? 80  ASP B OD2  1 
ATOM   3417  N N    . ASP B 1 81  ? 14.236  109.965 -1.273  1.00 15.32  ? 81  ASP B N    1 
ATOM   3418  C CA   . ASP B 1 81  ? 14.412  108.619 -0.788  1.00 19.33  ? 81  ASP B CA   1 
ATOM   3419  C C    . ASP B 1 81  ? 13.208  108.180 -0.015  1.00 16.28  ? 81  ASP B C    1 
ATOM   3420  O O    . ASP B 1 81  ? 13.068  107.030 0.269   1.00 17.18  ? 81  ASP B O    1 
ATOM   3421  C CB   . ASP B 1 81  ? 15.661  108.538 0.080   1.00 20.52  ? 81  ASP B CB   1 
ATOM   3422  C CG   . ASP B 1 81  ? 16.909  108.309 -0.703  1.00 29.19  ? 81  ASP B CG   1 
ATOM   3423  O OD1  . ASP B 1 81  ? 16.836  107.999 -1.907  1.00 31.33  ? 81  ASP B OD1  1 
ATOM   3424  O OD2  . ASP B 1 81  ? 17.980  108.432 -0.091  1.00 23.17  ? 81  ASP B OD2  1 
ATOM   3425  N N    . MET B 1 82  ? 12.310  109.076 0.310   1.00 13.57  ? 82  MET B N    1 
ATOM   3426  C CA   . MET B 1 82  ? 11.051  108.719 0.965   1.00 12.75  ? 82  MET B CA   1 
ATOM   3427  C C    . MET B 1 82  ? 9.935   108.457 -0.040  1.00 13.39  ? 82  MET B C    1 
ATOM   3428  O O    . MET B 1 82  ? 8.925   107.872 0.280   1.00 11.32  ? 82  MET B O    1 
ATOM   3429  C CB   . MET B 1 82  ? 10.667  109.812 1.936   1.00 10.09  ? 82  MET B CB   1 
ATOM   3430  C CG   . MET B 1 82  ? 9.403   109.595 2.752   1.00 13.75  ? 82  MET B CG   1 
ATOM   3431  S SD   . MET B 1 82  ? 9.467   108.375 4.067   1.00 9.38   ? 82  MET B SD   1 
ATOM   3432  C CE   . MET B 1 82  ? 8.382   109.200 5.200   1.00 14.64  ? 82  MET B CE   1 
ATOM   3433  N N    . GLU B 1 83  ? 10.129  108.823 -1.292  1.00 11.17  ? 83  GLU B N    1 
ATOM   3434  C CA   . GLU B 1 83  ? 9.169   108.510 -2.316  1.00 8.85   ? 83  GLU B CA   1 
ATOM   3435  C C    . GLU B 1 83  ? 9.380   107.066 -2.518  1.00 9.97   ? 83  GLU B C    1 
ATOM   3436  O O    . GLU B 1 83  ? 8.495   106.389 -2.979  1.00 9.39   ? 83  GLU B O    1 
ATOM   3437  C CB   . GLU B 1 83  ? 9.505   109.238 -3.598  1.00 8.69   ? 83  GLU B CB   1 
ATOM   3438  C CG   . GLU B 1 83  ? 9.227   110.730 -3.601  1.00 12.56  ? 83  GLU B CG   1 
ATOM   3439  C CD   . GLU B 1 83  ? 9.560   111.385 -4.927  1.00 9.53   ? 83  GLU B CD   1 
ATOM   3440  O OE1  . GLU B 1 83  ? 10.011  110.669 -5.830  1.00 10.58  ? 83  GLU B OE1  1 
ATOM   3441  O OE2  . GLU B 1 83  ? 9.379   112.608 -5.069  1.00 5.58   ? 83  GLU B OE2  1 
ATOM   3442  N N    . LYS B 1 84  ? 10.580  106.591 -2.256  1.00 8.03   ? 84  LYS B N    1 
ATOM   3443  C CA   . LYS B 1 84  ? 10.912  105.178 -2.343  1.00 8.72   ? 84  LYS B CA   1 
ATOM   3444  C C    . LYS B 1 84  ? 10.334  104.236 -1.318  1.00 10.85  ? 84  LYS B C    1 
ATOM   3445  O O    . LYS B 1 84  ? 10.008  103.115 -1.645  1.00 11.66  ? 84  LYS B O    1 
ATOM   3446  C CB   . LYS B 1 84  ? 12.412  105.066 -2.315  1.00 11.23  ? 84  LYS B CB   1 
ATOM   3447  C CG   . LYS B 1 84  ? 13.115  105.898 -3.371  1.00 15.14  ? 84  LYS B CG   1 
ATOM   3448  C CD   . LYS B 1 84  ? 14.115  105.070 -4.152  1.00 7.80   ? 84  LYS B CD   1 
ATOM   3449  C CE   . LYS B 1 84  ? 13.414  104.056 -5.034  1.00 4.84   ? 84  LYS B CE   1 
ATOM   3450  N NZ   . LYS B 1 84  ? 14.366  103.076 -5.600  1.00 8.64   ? 84  LYS B NZ   1 
ATOM   3451  N N    . ILE B 1 85  ? 10.187  104.680 -0.074  1.00 11.83  ? 85  ILE B N    1 
ATOM   3452  C CA   . ILE B 1 85  ? 9.722   103.827 1.000   1.00 7.78   ? 85  ILE B CA   1 
ATOM   3453  C C    . ILE B 1 85  ? 8.270   103.774 0.944   1.00 8.86   ? 85  ILE B C    1 
ATOM   3454  O O    . ILE B 1 85  ? 7.659   102.927 1.539   1.00 12.04  ? 85  ILE B O    1 
ATOM   3455  C CB   . ILE B 1 85  ? 10.198  104.326 2.349   1.00 8.85   ? 85  ILE B CB   1 
ATOM   3456  C CG1  . ILE B 1 85  ? 11.648  104.776 2.248   1.00 13.19  ? 85  ILE B CG1  1 
ATOM   3457  C CG2  . ILE B 1 85  ? 10.117  103.246 3.401   1.00 10.75  ? 85  ILE B CG2  1 
ATOM   3458  C CD1  . ILE B 1 85  ? 12.251  105.196 3.559   1.00 14.15  ? 85  ILE B CD1  1 
ATOM   3459  N N    . TRP B 1 86  ? 7.685   104.649 0.181   1.00 8.50   ? 86  TRP B N    1 
ATOM   3460  C CA   . TRP B 1 86  ? 6.267   104.609 -0.017  1.00 11.40  ? 86  TRP B CA   1 
ATOM   3461  C C    . TRP B 1 86  ? 5.969   103.880 -1.291  1.00 16.13  ? 86  TRP B C    1 
ATOM   3462  O O    . TRP B 1 86  ? 4.850   103.840 -1.749  1.00 16.08  ? 86  TRP B O    1 
ATOM   3463  C CB   . TRP B 1 86  ? 5.691   105.998 -0.055  1.00 12.84  ? 86  TRP B CB   1 
ATOM   3464  C CG   . TRP B 1 86  ? 5.587   106.674 1.243   1.00 9.98   ? 86  TRP B CG   1 
ATOM   3465  C CD1  . TRP B 1 86  ? 5.572   106.097 2.457   1.00 11.67  ? 86  TRP B CD1  1 
ATOM   3466  C CD2  . TRP B 1 86  ? 5.454   108.075 1.456   1.00 10.70  ? 86  TRP B CD2  1 
ATOM   3467  N NE1  . TRP B 1 86  ? 5.452   107.045 3.426   1.00 13.59  ? 86  TRP B NE1  1 
ATOM   3468  C CE2  . TRP B 1 86  ? 5.375   108.274 2.834   1.00 12.95  ? 86  TRP B CE2  1 
ATOM   3469  C CE3  . TRP B 1 86  ? 5.400   109.185 0.613   1.00 9.62   ? 86  TRP B CE3  1 
ATOM   3470  C CZ2  . TRP B 1 86  ? 5.242   109.534 3.396   1.00 10.75  ? 86  TRP B CZ2  1 
ATOM   3471  C CZ3  . TRP B 1 86  ? 5.268   110.427 1.170   1.00 10.94  ? 86  TRP B CZ3  1 
ATOM   3472  C CH2  . TRP B 1 86  ? 5.189   110.594 2.547   1.00 10.85  ? 86  TRP B CH2  1 
ATOM   3473  N N    . HIS B 1 87  ? 6.984   103.307 -1.884  1.00 15.93  ? 87  HIS B N    1 
ATOM   3474  C CA   . HIS B 1 87  ? 6.817   102.545 -3.081  1.00 14.97  ? 87  HIS B CA   1 
ATOM   3475  C C    . HIS B 1 87  ? 6.953   101.114 -2.664  1.00 15.72  ? 87  HIS B C    1 
ATOM   3476  O O    . HIS B 1 87  ? 6.486   100.230 -3.327  1.00 21.83  ? 87  HIS B O    1 
ATOM   3477  C CB   . HIS B 1 87  ? 7.966   102.916 -4.007  1.00 15.04  ? 87  HIS B CB   1 
ATOM   3478  C CG   . HIS B 1 87  ? 7.685   102.752 -5.469  1.00 22.15  ? 87  HIS B CG   1 
ATOM   3479  N ND1  . HIS B 1 87  ? 7.880   101.565 -6.137  1.00 16.39  ? 87  HIS B ND1  1 
ATOM   3480  C CD2  . HIS B 1 87  ? 7.284   103.645 -6.402  1.00 18.43  ? 87  HIS B CD2  1 
ATOM   3481  C CE1  . HIS B 1 87  ? 7.574   101.723 -7.410  1.00 11.82  ? 87  HIS B CE1  1 
ATOM   3482  N NE2  . HIS B 1 87  ? 7.210   102.976 -7.597  1.00 13.43  ? 87  HIS B NE2  1 
ATOM   3483  N N    . HIS B 1 88  ? 7.590   100.877 -1.545  1.00 10.97  ? 88  HIS B N    1 
ATOM   3484  C CA   . HIS B 1 88  ? 7.810   99.536  -1.085  1.00 13.59  ? 88  HIS B CA   1 
ATOM   3485  C C    . HIS B 1 88  ? 6.741   99.348  -0.119  1.00 12.64  ? 88  HIS B C    1 
ATOM   3486  O O    . HIS B 1 88  ? 6.760   98.453  0.672   1.00 15.71  ? 88  HIS B O    1 
ATOM   3487  C CB   . HIS B 1 88  ? 9.180   99.424  -0.411  1.00 14.27  ? 88  HIS B CB   1 
ATOM   3488  C CG   . HIS B 1 88  ? 9.715   98.035  -0.326  1.00 14.18  ? 88  HIS B CG   1 
ATOM   3489  N ND1  . HIS B 1 88  ? 10.332  97.414  -1.386  1.00 19.49  ? 88  HIS B ND1  1 
ATOM   3490  C CD2  . HIS B 1 88  ? 9.751   97.157  0.701   1.00 15.08  ? 88  HIS B CD2  1 
ATOM   3491  C CE1  . HIS B 1 88  ? 10.710  96.202  -1.021  1.00 25.17  ? 88  HIS B CE1  1 
ATOM   3492  N NE2  . HIS B 1 88  ? 10.371  96.023  0.241   1.00 21.11  ? 88  HIS B NE2  1 
ATOM   3493  N N    . THR B 1 89  ? 5.760   100.201 -0.207  1.00 11.57  ? 89  THR B N    1 
ATOM   3494  C CA   . THR B 1 89  ? 4.673   100.162 0.732   1.00 16.71  ? 89  THR B CA   1 
ATOM   3495  C C    . THR B 1 89  ? 3.415   99.954  -0.020  1.00 17.23  ? 89  THR B C    1 
ATOM   3496  O O    . THR B 1 89  ? 2.701   99.050  0.267   1.00 19.10  ? 89  THR B O    1 
ATOM   3497  C CB   . THR B 1 89  ? 4.555   101.452 1.571   1.00 14.86  ? 89  THR B CB   1 
ATOM   3498  O OG1  . THR B 1 89  ? 5.644   101.540 2.489   1.00 8.76   ? 89  THR B OG1  1 
ATOM   3499  C CG2  . THR B 1 89  ? 3.280   101.451 2.348   1.00 10.73  ? 89  THR B CG2  1 
ATOM   3500  N N    . PHE B 1 90  ? 3.095   100.785 -0.982  1.00 19.67  ? 90  PHE B N    1 
ATOM   3501  C CA   . PHE B 1 90  ? 1.894   100.489 -1.753  1.00 20.85  ? 90  PHE B CA   1 
ATOM   3502  C C    . PHE B 1 90  ? 2.136   99.916  -3.139  1.00 25.33  ? 90  PHE B C    1 
ATOM   3503  O O    . PHE B 1 90  ? 1.244   99.923  -3.961  1.00 29.11  ? 90  PHE B O    1 
ATOM   3504  C CB   . PHE B 1 90  ? 0.835   101.603 -1.821  1.00 12.59  ? 90  PHE B CB   1 
ATOM   3505  C CG   . PHE B 1 90  ? 1.164   102.871 -1.097  1.00 14.32  ? 90  PHE B CG   1 
ATOM   3506  C CD1  . PHE B 1 90  ? 0.844   103.024 0.226   1.00 22.11  ? 90  PHE B CD1  1 
ATOM   3507  C CD2  . PHE B 1 90  ? 1.683   103.947 -1.777  1.00 21.07  ? 90  PHE B CD2  1 
ATOM   3508  C CE1  . PHE B 1 90  ? 1.110   104.202 0.881   1.00 31.31  ? 90  PHE B CE1  1 
ATOM   3509  C CE2  . PHE B 1 90  ? 1.939   105.130 -1.135  1.00 19.64  ? 90  PHE B CE2  1 
ATOM   3510  C CZ   . PHE B 1 90  ? 1.659   105.256 0.197   1.00 20.22  ? 90  PHE B CZ   1 
ATOM   3511  N N    . TYR B 1 91  ? 3.342   99.459  -3.415  1.00 21.71  ? 91  TYR B N    1 
ATOM   3512  C CA   . TYR B 1 91  ? 3.624   98.898  -4.702  1.00 21.09  ? 91  TYR B CA   1 
ATOM   3513  C C    . TYR B 1 91  ? 4.287   97.563  -4.639  1.00 22.96  ? 91  TYR B C    1 
ATOM   3514  O O    . TYR B 1 91  ? 3.653   96.567  -4.948  1.00 21.66  ? 91  TYR B O    1 
ATOM   3515  C CB   . TYR B 1 91  ? 4.483   99.843  -5.514  1.00 15.42  ? 91  TYR B CB   1 
ATOM   3516  C CG   . TYR B 1 91  ? 3.744   100.932 -6.230  1.00 17.57  ? 91  TYR B CG   1 
ATOM   3517  C CD1  . TYR B 1 91  ? 2.676   100.646 -7.056  1.00 15.97  ? 91  TYR B CD1  1 
ATOM   3518  C CD2  . TYR B 1 91  ? 4.137   102.243 -6.107  1.00 15.98  ? 91  TYR B CD2  1 
ATOM   3519  C CE1  . TYR B 1 91  ? 2.009   101.645 -7.725  1.00 14.02  ? 91  TYR B CE1  1 
ATOM   3520  C CE2  . TYR B 1 91  ? 3.484   103.247 -6.774  1.00 14.29  ? 91  TYR B CE2  1 
ATOM   3521  C CZ   . TYR B 1 91  ? 2.421   102.943 -7.576  1.00 14.86  ? 91  TYR B CZ   1 
ATOM   3522  O OH   . TYR B 1 91  ? 1.773   103.962 -8.229  1.00 22.51  ? 91  TYR B OH   1 
ATOM   3523  N N    . ASN B 1 92  ? 5.557   97.525  -4.256  1.00 17.82  ? 92  ASN B N    1 
ATOM   3524  C CA   . ASN B 1 92  ? 6.328   96.298  -4.234  1.00 10.87  ? 92  ASN B CA   1 
ATOM   3525  C C    . ASN B 1 92  ? 6.203   95.515  -2.999  1.00 15.53  ? 92  ASN B C    1 
ATOM   3526  O O    . ASN B 1 92  ? 6.762   94.451  -2.912  1.00 24.32  ? 92  ASN B O    1 
ATOM   3527  C CB   . ASN B 1 92  ? 7.766   96.597  -4.476  1.00 18.96  ? 92  ASN B CB   1 
ATOM   3528  C CG   . ASN B 1 92  ? 8.066   96.910  -5.936  1.00 41.35  ? 92  ASN B CG   1 
ATOM   3529  O OD1  . ASN B 1 92  ? 9.118   97.458  -6.267  1.00 37.16  ? 92  ASN B OD1  1 
ATOM   3530  N ND2  . ASN B 1 92  ? 7.144   96.552  -6.818  1.00 39.94  ? 92  ASN B ND2  1 
ATOM   3531  N N    . GLU B 1 93  ? 5.478   96.004  -2.019  1.00 18.76  ? 93  GLU B N    1 
ATOM   3532  C CA   . GLU B 1 93  ? 5.168   95.227  -0.839  1.00 17.83  ? 93  GLU B CA   1 
ATOM   3533  C C    . GLU B 1 93  ? 3.828   95.775  -0.462  1.00 19.81  ? 93  GLU B C    1 
ATOM   3534  O O    . GLU B 1 93  ? 3.571   96.864  -0.862  1.00 26.36  ? 93  GLU B O    1 
ATOM   3535  C CB   . GLU B 1 93  ? 6.143   95.482  0.275   1.00 18.93  ? 93  GLU B CB   1 
ATOM   3536  C CG   . GLU B 1 93  ? 6.076   94.426  1.362   1.00 25.62  ? 93  GLU B CG   1 
ATOM   3537  C CD   . GLU B 1 93  ? 6.880   94.786  2.575   1.00 20.45  ? 93  GLU B CD   1 
ATOM   3538  O OE1  . GLU B 1 93  ? 7.502   95.852  2.570   1.00 16.66  ? 93  GLU B OE1  1 
ATOM   3539  O OE2  . GLU B 1 93  ? 6.885   93.995  3.531   1.00 28.88  ? 93  GLU B OE2  1 
ATOM   3540  N N    . LEU B 1 94  ? 2.961   95.062  0.244   1.00 16.91  ? 94  LEU B N    1 
ATOM   3541  C CA   . LEU B 1 94  ? 1.629   95.583  0.516   1.00 17.03  ? 94  LEU B CA   1 
ATOM   3542  C C    . LEU B 1 94  ? 1.162   96.049  -0.816  1.00 24.25  ? 94  LEU B C    1 
ATOM   3543  O O    . LEU B 1 94  ? 0.895   97.214  -1.035  1.00 24.51  ? 94  LEU B O    1 
ATOM   3544  C CB   . LEU B 1 94  ? 1.623   96.647  1.603   1.00 12.04  ? 94  LEU B CB   1 
ATOM   3545  C CG   . LEU B 1 94  ? 0.250   97.025  2.130   1.00 13.94  ? 94  LEU B CG   1 
ATOM   3546  C CD1  . LEU B 1 94  ? 0.072   96.294  3.437   1.00 22.76  ? 94  LEU B CD1  1 
ATOM   3547  C CD2  . LEU B 1 94  ? 0.161   98.524  2.331   1.00 16.89  ? 94  LEU B CD2  1 
ATOM   3548  N N    . ARG B 1 95  ? 0.975   95.129  -1.709  1.00 22.48  ? 95  ARG B N    1 
ATOM   3549  C CA   . ARG B 1 95  ? 0.766   95.460  -3.087  1.00 25.47  ? 95  ARG B CA   1 
ATOM   3550  C C    . ARG B 1 95  ? -0.277  96.319  -3.748  1.00 24.85  ? 95  ARG B C    1 
ATOM   3551  O O    . ARG B 1 95  ? 0.039   96.939  -4.734  1.00 36.39  ? 95  ARG B O    1 
ATOM   3552  C CB   . ARG B 1 95  ? 0.924   94.151  -3.814  1.00 29.72  ? 95  ARG B CB   1 
ATOM   3553  C CG   . ARG B 1 95  ? 2.240   93.473  -3.474  1.00 24.11  ? 95  ARG B CG   1 
ATOM   3554  C CD   . ARG B 1 95  ? 2.104   91.966  -3.386  1.00 34.78  ? 95  ARG B CD   1 
ATOM   3555  N NE   . ARG B 1 95  ? 2.598   91.295  -4.588  1.00 62.26  ? 95  ARG B NE   1 
ATOM   3556  C CZ   . ARG B 1 95  ? 1.828   90.771  -5.538  1.00 65.48  ? 95  ARG B CZ   1 
ATOM   3557  N NH1  . ARG B 1 95  ? 0.506   90.821  -5.442  1.00 65.12  ? 95  ARG B NH1  1 
ATOM   3558  N NH2  . ARG B 1 95  ? 2.386   90.186  -6.586  1.00 55.63  ? 95  ARG B NH2  1 
ATOM   3559  N N    . VAL B 1 96  ? -1.481  96.417  -3.279  1.00 19.89  ? 96  VAL B N    1 
ATOM   3560  C CA   . VAL B 1 96  ? -2.471  97.179  -4.022  1.00 22.06  ? 96  VAL B CA   1 
ATOM   3561  C C    . VAL B 1 96  ? -2.177  98.629  -4.285  1.00 22.47  ? 96  VAL B C    1 
ATOM   3562  O O    . VAL B 1 96  ? -1.577  99.267  -3.452  1.00 27.97  ? 96  VAL B O    1 
ATOM   3563  C CB   . VAL B 1 96  ? -3.765  97.188  -3.277  1.00 27.96  ? 96  VAL B CB   1 
ATOM   3564  C CG1  . VAL B 1 96  ? -4.586  95.968  -3.643  1.00 36.35  ? 96  VAL B CG1  1 
ATOM   3565  C CG2  . VAL B 1 96  ? -3.506  97.249  -1.782  1.00 25.98  ? 96  VAL B CG2  1 
ATOM   3566  N N    . ALA B 1 97  ? -2.651  99.177  -5.401  1.00 22.09  ? 97  ALA B N    1 
ATOM   3567  C CA   . ALA B 1 97  ? -2.382  100.551 -5.825  1.00 14.14  ? 97  ALA B CA   1 
ATOM   3568  C C    . ALA B 1 97  ? -2.768  101.710 -4.975  1.00 16.62  ? 97  ALA B C    1 
ATOM   3569  O O    . ALA B 1 97  ? -3.751  101.657 -4.269  1.00 17.73  ? 97  ALA B O    1 
ATOM   3570  C CB   . ALA B 1 97  ? -3.015  100.758 -7.156  1.00 12.81  ? 97  ALA B CB   1 
ATOM   3571  N N    . PRO B 1 98  ? -1.949  102.750 -4.971  1.00 19.20  ? 98  PRO B N    1 
ATOM   3572  C CA   . PRO B 1 98  ? -2.167  103.967 -4.215  1.00 12.24  ? 98  PRO B CA   1 
ATOM   3573  C C    . PRO B 1 98  ? -3.333  104.711 -4.688  1.00 13.24  ? 98  PRO B C    1 
ATOM   3574  O O    . PRO B 1 98  ? -3.980  105.371 -3.922  1.00 14.17  ? 98  PRO B O    1 
ATOM   3575  C CB   . PRO B 1 98  ? -0.959  104.756 -4.593  1.00 14.11  ? 98  PRO B CB   1 
ATOM   3576  C CG   . PRO B 1 98  ? 0.109   103.782 -4.829  1.00 18.69  ? 98  PRO B CG   1 
ATOM   3577  C CD   . PRO B 1 98  ? -0.578  102.648 -5.485  1.00 22.77  ? 98  PRO B CD   1 
ATOM   3578  N N    . GLU B 1 99  ? -3.541  104.698 -5.972  1.00 17.31  ? 99  GLU B N    1 
ATOM   3579  C CA   . GLU B 1 99  ? -4.636  105.370 -6.594  1.00 16.79  ? 99  GLU B CA   1 
ATOM   3580  C C    . GLU B 1 99  ? -5.975  104.853 -6.219  1.00 17.10  ? 99  GLU B C    1 
ATOM   3581  O O    . GLU B 1 99  ? -6.915  105.603 -6.196  1.00 17.49  ? 99  GLU B O    1 
ATOM   3582  C CB   . GLU B 1 99  ? -4.418  105.194 -8.092  1.00 14.94  ? 99  GLU B CB   1 
ATOM   3583  C CG   . GLU B 1 99  ? -2.936  105.226 -8.444  1.00 15.36  ? 99  GLU B CG   1 
ATOM   3584  C CD   . GLU B 1 99  ? -2.581  104.413 -9.666  1.00 15.90  ? 99  GLU B CD   1 
ATOM   3585  O OE1  . GLU B 1 99  ? -3.369  104.416 -10.624 1.00 21.56  ? 99  GLU B OE1  1 
ATOM   3586  O OE2  . GLU B 1 99  ? -1.504  103.789 -9.670  1.00 7.69   ? 99  GLU B OE2  1 
ATOM   3587  N N    . GLU B 1 100 ? -6.114  103.555 -6.085  1.00 16.07  ? 100 GLU B N    1 
ATOM   3588  C CA   . GLU B 1 100 ? -7.352  102.946 -5.654  1.00 16.78  ? 100 GLU B CA   1 
ATOM   3589  C C    . GLU B 1 100 ? -7.781  103.136 -4.217  1.00 15.77  ? 100 GLU B C    1 
ATOM   3590  O O    . GLU B 1 100 ? -8.962  103.265 -3.949  1.00 13.91  ? 100 GLU B O    1 
ATOM   3591  C CB   . GLU B 1 100 ? -7.261  101.473 -5.975  1.00 18.68  ? 100 GLU B CB   1 
ATOM   3592  C CG   . GLU B 1 100 ? -7.194  101.162 -7.453  1.00 19.20  ? 100 GLU B CG   1 
ATOM   3593  C CD   . GLU B 1 100 ? -7.058  99.684  -7.711  1.00 18.59  ? 100 GLU B CD   1 
ATOM   3594  O OE1  . GLU B 1 100 ? -6.835  98.937  -6.744  1.00 19.77  ? 100 GLU B OE1  1 
ATOM   3595  O OE2  . GLU B 1 100 ? -7.170  99.272  -8.878  1.00 29.83  ? 100 GLU B OE2  1 
ATOM   3596  N N    . HIS B 1 101 ? -6.842  103.126 -3.286  1.00 15.43  ? 101 HIS B N    1 
ATOM   3597  C CA   . HIS B 1 101 ? -7.135  103.207 -1.870  1.00 14.13  ? 101 HIS B CA   1 
ATOM   3598  C C    . HIS B 1 101 ? -6.713  104.491 -1.221  1.00 12.52  ? 101 HIS B C    1 
ATOM   3599  O O    . HIS B 1 101 ? -5.680  105.016 -1.538  1.00 13.80  ? 101 HIS B O    1 
ATOM   3600  C CB   . HIS B 1 101 ? -6.389  102.100 -1.172  1.00 11.23  ? 101 HIS B CB   1 
ATOM   3601  C CG   . HIS B 1 101 ? -6.636  100.741 -1.734  1.00 16.56  ? 101 HIS B CG   1 
ATOM   3602  N ND1  . HIS B 1 101 ? -6.179  100.353 -2.971  1.00 16.89  ? 101 HIS B ND1  1 
ATOM   3603  C CD2  . HIS B 1 101 ? -7.261  99.666  -1.206  1.00 24.10  ? 101 HIS B CD2  1 
ATOM   3604  C CE1  . HIS B 1 101 ? -6.545  99.107  -3.198  1.00 19.49  ? 101 HIS B CE1  1 
ATOM   3605  N NE2  . HIS B 1 101 ? -7.196  98.663  -2.142  1.00 29.33  ? 101 HIS B NE2  1 
ATOM   3606  N N    . PRO B 1 102 ? -7.531  105.022 -0.315  1.00 14.03  ? 102 PRO B N    1 
ATOM   3607  C CA   . PRO B 1 102 ? -7.236  106.258 0.400   1.00 12.50  ? 102 PRO B CA   1 
ATOM   3608  C C    . PRO B 1 102 ? -6.200  106.115 1.488   1.00 17.45  ? 102 PRO B C    1 
ATOM   3609  O O    . PRO B 1 102 ? -6.303  105.174 2.242   1.00 15.53  ? 102 PRO B O    1 
ATOM   3610  C CB   . PRO B 1 102 ? -8.585  106.621 0.978   1.00 9.97   ? 102 PRO B CB   1 
ATOM   3611  C CG   . PRO B 1 102 ? -9.582  106.008 0.078   1.00 10.38  ? 102 PRO B CG   1 
ATOM   3612  C CD   . PRO B 1 102 ? -8.963  104.695 -0.250  1.00 20.31  ? 102 PRO B CD   1 
ATOM   3613  N N    . VAL B 1 103 ? -5.237  107.034 1.600   1.00 16.56  ? 103 VAL B N    1 
ATOM   3614  C CA   . VAL B 1 103 ? -4.136  106.892 2.555   1.00 13.74  ? 103 VAL B CA   1 
ATOM   3615  C C    . VAL B 1 103 ? -4.147  107.735 3.833   1.00 13.84  ? 103 VAL B C    1 
ATOM   3616  O O    . VAL B 1 103 ? -4.454  108.897 3.780   1.00 12.83  ? 103 VAL B O    1 
ATOM   3617  C CB   . VAL B 1 103 ? -2.757  106.958 1.825   1.00 11.83  ? 103 VAL B CB   1 
ATOM   3618  C CG1  . VAL B 1 103 ? -1.649  106.382 2.681   1.00 11.15  ? 103 VAL B CG1  1 
ATOM   3619  C CG2  . VAL B 1 103 ? -2.802  106.173 0.533   1.00 13.73  ? 103 VAL B CG2  1 
ATOM   3620  N N    . LEU B 1 104 ? -3.879  107.135 4.996   1.00 13.44  ? 104 LEU B N    1 
ATOM   3621  C CA   . LEU B 1 104 ? -3.725  107.881 6.234   1.00 11.76  ? 104 LEU B CA   1 
ATOM   3622  C C    . LEU B 1 104 ? -2.273  107.821 6.570   1.00 11.74  ? 104 LEU B C    1 
ATOM   3623  O O    . LEU B 1 104 ? -1.664  106.778 6.499   1.00 8.64   ? 104 LEU B O    1 
ATOM   3624  C CB   . LEU B 1 104 ? -4.506  107.329 7.394   1.00 11.73  ? 104 LEU B CB   1 
ATOM   3625  C CG   . LEU B 1 104 ? -4.419  108.124 8.686   1.00 10.37  ? 104 LEU B CG   1 
ATOM   3626  C CD1  . LEU B 1 104 ? -5.585  109.053 8.755   1.00 15.12  ? 104 LEU B CD1  1 
ATOM   3627  C CD2  . LEU B 1 104 ? -4.448  107.241 9.896   1.00 8.59   ? 104 LEU B CD2  1 
ATOM   3628  N N    . LEU B 1 105 ? -1.706  108.968 6.922   1.00 11.93  ? 105 LEU B N    1 
ATOM   3629  C CA   . LEU B 1 105 ? -0.319  109.034 7.223   1.00 12.61  ? 105 LEU B CA   1 
ATOM   3630  C C    . LEU B 1 105 ? -0.103  109.519 8.612   1.00 14.69  ? 105 LEU B C    1 
ATOM   3631  O O    . LEU B 1 105 ? -0.984  110.110 9.187   1.00 13.91  ? 105 LEU B O    1 
ATOM   3632  C CB   . LEU B 1 105 ? 0.385   109.960 6.263   1.00 12.07  ? 105 LEU B CB   1 
ATOM   3633  C CG   . LEU B 1 105 ? 0.339   109.891 4.741   1.00 13.94  ? 105 LEU B CG   1 
ATOM   3634  C CD1  . LEU B 1 105 ? 0.767   111.236 4.189   1.00 10.89  ? 105 LEU B CD1  1 
ATOM   3635  C CD2  . LEU B 1 105 ? 1.278   108.819 4.243   1.00 10.81  ? 105 LEU B CD2  1 
ATOM   3636  N N    . THR B 1 106 ? 1.068   109.241 9.165   1.00 14.82  ? 106 THR B N    1 
ATOM   3637  C CA   . THR B 1 106 ? 1.424   109.646 10.509  1.00 10.14  ? 106 THR B CA   1 
ATOM   3638  C C    . THR B 1 106 ? 2.683   110.464 10.537  1.00 10.72  ? 106 THR B C    1 
ATOM   3639  O O    . THR B 1 106 ? 3.748   109.953 10.276  1.00 13.07  ? 106 THR B O    1 
ATOM   3640  C CB   . THR B 1 106 ? 1.698   108.460 11.378  1.00 10.01  ? 106 THR B CB   1 
ATOM   3641  O OG1  . THR B 1 106 ? 2.667   107.658 10.727  1.00 12.40  ? 106 THR B OG1  1 
ATOM   3642  C CG2  . THR B 1 106 ? 0.444   107.664 11.614  1.00 8.53   ? 106 THR B CG2  1 
ATOM   3643  N N    . GLU B 1 107 ? 2.587   111.731 10.910  1.00 8.04   ? 107 GLU B N    1 
ATOM   3644  C CA   . GLU B 1 107 ? 3.712   112.604 11.028  1.00 8.22   ? 107 GLU B CA   1 
ATOM   3645  C C    . GLU B 1 107 ? 4.291   112.583 12.394  1.00 11.71  ? 107 GLU B C    1 
ATOM   3646  O O    . GLU B 1 107 ? 3.698   112.085 13.315  1.00 13.27  ? 107 GLU B O    1 
ATOM   3647  C CB   . GLU B 1 107 ? 3.265   113.993 10.701  1.00 9.32   ? 107 GLU B CB   1 
ATOM   3648  C CG   . GLU B 1 107 ? 2.519   114.737 11.778  1.00 14.66  ? 107 GLU B CG   1 
ATOM   3649  C CD   . GLU B 1 107 ? 1.816   115.908 11.188  1.00 23.45  ? 107 GLU B CD   1 
ATOM   3650  O OE1  . GLU B 1 107 ? 2.382   116.451 10.236  1.00 18.18  ? 107 GLU B OE1  1 
ATOM   3651  O OE2  . GLU B 1 107 ? 0.711   116.256 11.631  1.00 24.54  ? 107 GLU B OE2  1 
ATOM   3652  N N    . ALA B 1 108 ? 5.485   113.100 12.547  1.00 15.30  ? 108 ALA B N    1 
ATOM   3653  C CA   . ALA B 1 108 ? 6.156   112.996 13.808  1.00 9.29   ? 108 ALA B CA   1 
ATOM   3654  C C    . ALA B 1 108 ? 5.690   114.038 14.656  1.00 8.86   ? 108 ALA B C    1 
ATOM   3655  O O    . ALA B 1 108 ? 5.111   115.012 14.210  1.00 12.10  ? 108 ALA B O    1 
ATOM   3656  C CB   . ALA B 1 108 ? 7.615   113.179 13.649  1.00 7.91   ? 108 ALA B CB   1 
ATOM   3657  N N    . PRO B 1 109 ? 5.938   113.842 15.928  1.00 7.25   ? 109 PRO B N    1 
ATOM   3658  C CA   . PRO B 1 109 ? 5.483   114.962 16.680  1.00 7.92   ? 109 PRO B CA   1 
ATOM   3659  C C    . PRO B 1 109 ? 6.229   116.216 16.302  1.00 6.99   ? 109 PRO B C    1 
ATOM   3660  O O    . PRO B 1 109 ? 7.430   116.194 16.147  1.00 6.74   ? 109 PRO B O    1 
ATOM   3661  C CB   . PRO B 1 109 ? 5.691   114.492 18.074  1.00 9.40   ? 109 PRO B CB   1 
ATOM   3662  C CG   . PRO B 1 109 ? 5.384   113.040 18.013  1.00 8.51   ? 109 PRO B CG   1 
ATOM   3663  C CD   . PRO B 1 109 ? 5.983   112.609 16.725  1.00 9.23   ? 109 PRO B CD   1 
ATOM   3664  N N    . LEU B 1 110 ? 5.517   117.313 16.193  1.00 5.36   ? 110 LEU B N    1 
ATOM   3665  C CA   . LEU B 1 110 ? 6.096   118.568 15.761  1.00 4.83   ? 110 LEU B CA   1 
ATOM   3666  C C    . LEU B 1 110 ? 6.736   118.615 14.374  1.00 7.69   ? 110 LEU B C    1 
ATOM   3667  O O    . LEU B 1 110 ? 7.819   119.137 14.220  1.00 11.08  ? 110 LEU B O    1 
ATOM   3668  C CB   . LEU B 1 110 ? 6.935   119.175 16.855  1.00 5.60   ? 110 LEU B CB   1 
ATOM   3669  C CG   . LEU B 1 110 ? 6.247   119.821 18.040  1.00 4.64   ? 110 LEU B CG   1 
ATOM   3670  C CD1  . LEU B 1 110 ? 7.292   120.557 18.852  1.00 3.98   ? 110 LEU B CD1  1 
ATOM   3671  C CD2  . LEU B 1 110 ? 5.211   120.797 17.528  1.00 9.21   ? 110 LEU B CD2  1 
ATOM   3672  N N    . ASN B 1 111 ? 5.970   118.136 13.393  1.00 10.46  ? 111 ASN B N    1 
ATOM   3673  C CA   . ASN B 1 111 ? 6.451   118.050 12.050  1.00 6.86   ? 111 ASN B CA   1 
ATOM   3674  C C    . ASN B 1 111 ? 6.431   119.383 11.440  1.00 6.54   ? 111 ASN B C    1 
ATOM   3675  O O    . ASN B 1 111 ? 5.489   120.131 11.619  1.00 6.49   ? 111 ASN B O    1 
ATOM   3676  C CB   . ASN B 1 111 ? 5.654   117.137 11.152  1.00 9.07   ? 111 ASN B CB   1 
ATOM   3677  C CG   . ASN B 1 111 ? 6.516   116.340 10.207  1.00 11.85  ? 111 ASN B CG   1 
ATOM   3678  O OD1  . ASN B 1 111 ? 6.202   116.206 9.040   1.00 12.16  ? 111 ASN B OD1  1 
ATOM   3679  N ND2  . ASN B 1 111 ? 7.602   115.803 10.712  1.00 15.02  ? 111 ASN B ND2  1 
ATOM   3680  N N    . PRO B 1 112 ? 7.504   119.708 10.717  1.00 7.93   ? 112 PRO B N    1 
ATOM   3681  C CA   . PRO B 1 112 ? 7.537   121.028 10.167  1.00 7.16   ? 112 PRO B CA   1 
ATOM   3682  C C    . PRO B 1 112 ? 6.485   121.269 9.122   1.00 8.53   ? 112 PRO B C    1 
ATOM   3683  O O    . PRO B 1 112 ? 6.176   120.383 8.367   1.00 10.14  ? 112 PRO B O    1 
ATOM   3684  C CB   . PRO B 1 112 ? 8.932   121.083 9.618   1.00 6.95   ? 112 PRO B CB   1 
ATOM   3685  C CG   . PRO B 1 112 ? 9.735   120.228 10.515  1.00 5.31   ? 112 PRO B CG   1 
ATOM   3686  C CD   . PRO B 1 112 ? 8.830   119.072 10.703  1.00 8.14   ? 112 PRO B CD   1 
ATOM   3687  N N    . LYS B 1 113 ? 5.942   122.468 9.073   1.00 8.57   ? 113 LYS B N    1 
ATOM   3688  C CA   . LYS B 1 113 ? 4.926   122.836 8.102   1.00 11.22  ? 113 LYS B CA   1 
ATOM   3689  C C    . LYS B 1 113 ? 5.354   122.525 6.707   1.00 12.33  ? 113 LYS B C    1 
ATOM   3690  O O    . LYS B 1 113 ? 4.555   122.371 5.826   1.00 12.72  ? 113 LYS B O    1 
ATOM   3691  C CB   . LYS B 1 113 ? 4.696   124.334 8.224   1.00 6.82   ? 113 LYS B CB   1 
ATOM   3692  C CG   . LYS B 1 113 ? 5.010   124.891 9.592   1.00 8.48   ? 113 LYS B CG   1 
ATOM   3693  C CD   . LYS B 1 113 ? 5.458   126.333 9.491   1.00 10.50  ? 113 LYS B CD   1 
ATOM   3694  C CE   . LYS B 1 113 ? 4.538   127.130 8.589   1.00 10.83  ? 113 LYS B CE   1 
ATOM   3695  N NZ   . LYS B 1 113 ? 4.863   128.581 8.610   1.00 8.13   ? 113 LYS B NZ   1 
ATOM   3696  N N    . ALA B 1 114 ? 6.623   122.429 6.500   1.00 9.63   ? 114 ALA B N    1 
ATOM   3697  C CA   . ALA B 1 114 ? 7.143   122.213 5.194   1.00 9.64   ? 114 ALA B CA   1 
ATOM   3698  C C    . ALA B 1 114 ? 7.360   120.789 4.846   1.00 12.29  ? 114 ALA B C    1 
ATOM   3699  O O    . ALA B 1 114 ? 7.368   120.440 3.680   1.00 20.16  ? 114 ALA B O    1 
ATOM   3700  C CB   . ALA B 1 114 ? 8.456   122.921 5.127   1.00 13.61  ? 114 ALA B CB   1 
ATOM   3701  N N    . ASN B 1 115 ? 7.593   119.954 5.844   1.00 11.21  ? 115 ASN B N    1 
ATOM   3702  C CA   . ASN B 1 115 ? 7.840   118.564 5.618   1.00 11.38  ? 115 ASN B CA   1 
ATOM   3703  C C    . ASN B 1 115 ? 6.493   117.994 5.440   1.00 12.36  ? 115 ASN B C    1 
ATOM   3704  O O    . ASN B 1 115 ? 6.330   116.957 4.889   1.00 12.34  ? 115 ASN B O    1 
ATOM   3705  C CB   . ASN B 1 115 ? 8.536   117.938 6.796   1.00 8.50   ? 115 ASN B CB   1 
ATOM   3706  C CG   . ASN B 1 115 ? 10.016  118.154 6.781   1.00 11.83  ? 115 ASN B CG   1 
ATOM   3707  O OD1  . ASN B 1 115 ? 10.486  119.247 6.504   1.00 15.12  ? 115 ASN B OD1  1 
ATOM   3708  N ND2  . ASN B 1 115 ? 10.762  117.110 7.089   1.00 14.22  ? 115 ASN B ND2  1 
ATOM   3709  N N    . ARG B 1 116 ? 5.496   118.718 5.881   1.00 11.70  ? 116 ARG B N    1 
ATOM   3710  C CA   . ARG B 1 116 ? 4.132   118.237 5.786   1.00 14.21  ? 116 ARG B CA   1 
ATOM   3711  C C    . ARG B 1 116 ? 3.599   118.434 4.427   1.00 14.47  ? 116 ARG B C    1 
ATOM   3712  O O    . ARG B 1 116 ? 2.867   117.617 3.923   1.00 16.59  ? 116 ARG B O    1 
ATOM   3713  C CB   . ARG B 1 116 ? 3.240   119.048 6.700   1.00 12.15  ? 116 ARG B CB   1 
ATOM   3714  C CG   . ARG B 1 116 ? 3.367   118.843 8.180   1.00 13.92  ? 116 ARG B CG   1 
ATOM   3715  C CD   . ARG B 1 116 ? 2.230   119.581 8.856   1.00 10.93  ? 116 ARG B CD   1 
ATOM   3716  N NE   . ARG B 1 116 ? 1.187   118.639 9.215   1.00 9.14   ? 116 ARG B NE   1 
ATOM   3717  C CZ   . ARG B 1 116 ? -0.067  118.953 9.475   1.00 9.54   ? 116 ARG B CZ   1 
ATOM   3718  N NH1  . ARG B 1 116 ? -0.466  120.202 9.407   1.00 11.99  ? 116 ARG B NH1  1 
ATOM   3719  N NH2  . ARG B 1 116 ? -0.922  118.005 9.793   1.00 8.75   ? 116 ARG B NH2  1 
ATOM   3720  N N    . GLU B 1 117 ? 3.952   119.536 3.824   1.00 12.04  ? 117 GLU B N    1 
ATOM   3721  C CA   . GLU B 1 117 ? 3.423   119.869 2.548   1.00 12.27  ? 117 GLU B CA   1 
ATOM   3722  C C    . GLU B 1 117 ? 3.949   119.000 1.497   1.00 12.16  ? 117 GLU B C    1 
ATOM   3723  O O    . GLU B 1 117 ? 3.500   119.021 0.391   1.00 16.83  ? 117 GLU B O    1 
ATOM   3724  C CB   . GLU B 1 117 ? 3.849   121.263 2.214   1.00 14.09  ? 117 GLU B CB   1 
ATOM   3725  C CG   . GLU B 1 117 ? 3.087   122.379 2.873   1.00 13.87  ? 117 GLU B CG   1 
ATOM   3726  C CD   . GLU B 1 117 ? 3.738   123.708 2.592   1.00 16.35  ? 117 GLU B CD   1 
ATOM   3727  O OE1  . GLU B 1 117 ? 3.988   123.986 1.410   1.00 21.52  ? 117 GLU B OE1  1 
ATOM   3728  O OE2  . GLU B 1 117 ? 4.016   124.466 3.537   1.00 14.54  ? 117 GLU B OE2  1 
ATOM   3729  N N    . LYS B 1 118 ? 4.933   118.203 1.796   1.00 11.97  ? 118 LYS B N    1 
ATOM   3730  C CA   . LYS B 1 118 ? 5.522   117.414 0.742   1.00 14.59  ? 118 LYS B CA   1 
ATOM   3731  C C    . LYS B 1 118 ? 4.868   116.105 0.752   1.00 13.19  ? 118 LYS B C    1 
ATOM   3732  O O    . LYS B 1 118 ? 4.711   115.502 -0.256  1.00 14.28  ? 118 LYS B O    1 
ATOM   3733  C CB   . LYS B 1 118 ? 7.006   117.287 0.925   1.00 13.53  ? 118 LYS B CB   1 
ATOM   3734  C CG   . LYS B 1 118 ? 7.776   116.953 -0.333  1.00 16.07  ? 118 LYS B CG   1 
ATOM   3735  C CD   . LYS B 1 118 ? 7.621   118.039 -1.369  1.00 19.90  ? 118 LYS B CD   1 
ATOM   3736  C CE   . LYS B 1 118 ? 8.055   117.542 -2.731  1.00 25.42  ? 118 LYS B CE   1 
ATOM   3737  N NZ   . LYS B 1 118 ? 7.549   118.446 -3.797  1.00 34.31  ? 118 LYS B NZ   1 
ATOM   3738  N N    . MET B 1 119 ? 4.485   115.642 1.902   1.00 11.00  ? 119 MET B N    1 
ATOM   3739  C CA   . MET B 1 119 ? 3.751   114.436 1.991   1.00 12.01  ? 119 MET B CA   1 
ATOM   3740  C C    . MET B 1 119 ? 2.432   114.630 1.304   1.00 16.12  ? 119 MET B C    1 
ATOM   3741  O O    . MET B 1 119 ? 1.934   113.730 0.666   1.00 16.18  ? 119 MET B O    1 
ATOM   3742  C CB   . MET B 1 119 ? 3.503   114.146 3.452   1.00 15.01  ? 119 MET B CB   1 
ATOM   3743  C CG   . MET B 1 119 ? 4.754   113.873 4.263   1.00 18.99  ? 119 MET B CG   1 
ATOM   3744  S SD   . MET B 1 119 ? 4.612   113.338 5.978   1.00 20.80  ? 119 MET B SD   1 
ATOM   3745  C CE   . MET B 1 119 ? 4.065   114.837 6.758   1.00 13.98  ? 119 MET B CE   1 
ATOM   3746  N N    . THR B 1 120 ? 1.819   115.791 1.461   1.00 14.69  ? 120 THR B N    1 
ATOM   3747  C CA   . THR B 1 120 ? 0.593   116.073 0.754   1.00 13.58  ? 120 THR B CA   1 
ATOM   3748  C C    . THR B 1 120 ? 0.844   116.067 -0.739  1.00 13.37  ? 120 THR B C    1 
ATOM   3749  O O    . THR B 1 120 ? 0.081   115.476 -1.470  1.00 13.26  ? 120 THR B O    1 
ATOM   3750  C CB   . THR B 1 120 ? 0.005   117.393 1.246   1.00 11.49  ? 120 THR B CB   1 
ATOM   3751  O OG1  . THR B 1 120 ? 0.095   117.441 2.668   1.00 12.76  ? 120 THR B OG1  1 
ATOM   3752  C CG2  . THR B 1 120 ? -1.432  117.550 0.831   1.00 10.56  ? 120 THR B CG2  1 
ATOM   3753  N N    . GLN B 1 121 ? 1.910   116.686 -1.205  1.00 10.11  ? 121 GLN B N    1 
ATOM   3754  C CA   . GLN B 1 121 ? 2.266   116.666 -2.605  1.00 10.43  ? 121 GLN B CA   1 
ATOM   3755  C C    . GLN B 1 121 ? 2.692   115.343 -3.136  1.00 12.45  ? 121 GLN B C    1 
ATOM   3756  O O    . GLN B 1 121 ? 2.196   114.903 -4.124  1.00 18.01  ? 121 GLN B O    1 
ATOM   3757  C CB   . GLN B 1 121 ? 3.449   117.569 -2.784  1.00 13.65  ? 121 GLN B CB   1 
ATOM   3758  C CG   . GLN B 1 121 ? 3.518   118.339 -4.078  1.00 17.27  ? 121 GLN B CG   1 
ATOM   3759  C CD   . GLN B 1 121 ? 4.216   119.659 -3.891  1.00 19.48  ? 121 GLN B CD   1 
ATOM   3760  O OE1  . GLN B 1 121 ? 4.909   119.862 -2.905  1.00 12.61  ? 121 GLN B OE1  1 
ATOM   3761  N NE2  . GLN B 1 121 ? 4.028   120.569 -4.831  1.00 24.39  ? 121 GLN B NE2  1 
ATOM   3762  N N    . ILE B 1 122 ? 3.676   114.734 -2.513  1.00 8.67   ? 122 ILE B N    1 
ATOM   3763  C CA   . ILE B 1 122 ? 4.101   113.437 -2.913  1.00 7.42   ? 122 ILE B CA   1 
ATOM   3764  C C    . ILE B 1 122 ? 2.932   112.476 -2.984  1.00 8.61   ? 122 ILE B C    1 
ATOM   3765  O O    . ILE B 1 122 ? 2.887   111.628 -3.816  1.00 11.74  ? 122 ILE B O    1 
ATOM   3766  C CB   . ILE B 1 122 ? 5.234   112.951 -2.017  1.00 7.08   ? 122 ILE B CB   1 
ATOM   3767  C CG1  . ILE B 1 122 ? 6.454   113.825 -2.201  1.00 9.25   ? 122 ILE B CG1  1 
ATOM   3768  C CG2  . ILE B 1 122 ? 5.629   111.526 -2.344  1.00 6.83   ? 122 ILE B CG2  1 
ATOM   3769  C CD1  . ILE B 1 122 ? 7.649   113.321 -1.441  1.00 10.10  ? 122 ILE B CD1  1 
ATOM   3770  N N    . MET B 1 123 ? 1.974   112.580 -2.118  1.00 8.77   ? 123 MET B N    1 
ATOM   3771  C CA   . MET B 1 123 ? 0.803   111.724 -2.194  1.00 10.56  ? 123 MET B CA   1 
ATOM   3772  C C    . MET B 1 123 ? -0.163  111.921 -3.324  1.00 13.28  ? 123 MET B C    1 
ATOM   3773  O O    . MET B 1 123 ? -0.788  110.989 -3.769  1.00 15.21  ? 123 MET B O    1 
ATOM   3774  C CB   . MET B 1 123 ? 0.054   111.631 -0.882  1.00 8.84   ? 123 MET B CB   1 
ATOM   3775  C CG   . MET B 1 123 ? 0.799   110.938 0.251   1.00 9.71   ? 123 MET B CG   1 
ATOM   3776  S SD   . MET B 1 123 ? 1.233   109.214 0.048   1.00 3.33   ? 123 MET B SD   1 
ATOM   3777  C CE   . MET B 1 123 ? -0.282  108.574 -0.617  1.00 10.50  ? 123 MET B CE   1 
ATOM   3778  N N    . PHE B 1 124 ? -0.355  113.145 -3.736  1.00 12.38  ? 124 PHE B N    1 
ATOM   3779  C CA   . PHE B 1 124 ? -1.282  113.439 -4.782  1.00 13.56  ? 124 PHE B CA   1 
ATOM   3780  C C    . PHE B 1 124 ? -0.550  113.620 -6.064  1.00 11.07  ? 124 PHE B C    1 
ATOM   3781  O O    . PHE B 1 124 ? -0.956  113.086 -7.080  1.00 12.63  ? 124 PHE B O    1 
ATOM   3782  C CB   . PHE B 1 124 ? -1.998  114.704 -4.414  1.00 17.94  ? 124 PHE B CB   1 
ATOM   3783  C CG   . PHE B 1 124 ? -3.057  114.523 -3.369  1.00 16.30  ? 124 PHE B CG   1 
ATOM   3784  C CD1  . PHE B 1 124 ? -4.175  113.763 -3.628  1.00 17.86  ? 124 PHE B CD1  1 
ATOM   3785  C CD2  . PHE B 1 124 ? -2.943  115.128 -2.141  1.00 14.42  ? 124 PHE B CD2  1 
ATOM   3786  C CE1  . PHE B 1 124 ? -5.151  113.601 -2.674  1.00 18.02  ? 124 PHE B CE1  1 
ATOM   3787  C CE2  . PHE B 1 124 ? -3.918  114.971 -1.184  1.00 21.64  ? 124 PHE B CE2  1 
ATOM   3788  C CZ   . PHE B 1 124 ? -5.023  114.206 -1.452  1.00 20.10  ? 124 PHE B CZ   1 
ATOM   3789  N N    . GLU B 1 125 ? 0.532   114.364 -6.038  1.00 10.26  ? 125 GLU B N    1 
ATOM   3790  C CA   . GLU B 1 125 ? 1.379   114.506 -7.221  1.00 9.31   ? 125 GLU B CA   1 
ATOM   3791  C C    . GLU B 1 125 ? 2.127   113.276 -7.735  1.00 7.91   ? 125 GLU B C    1 
ATOM   3792  O O    . GLU B 1 125 ? 2.339   113.168 -8.926  1.00 10.83  ? 125 GLU B O    1 
ATOM   3793  C CB   . GLU B 1 125 ? 2.297   115.709 -7.113  1.00 8.81   ? 125 GLU B CB   1 
ATOM   3794  C CG   . GLU B 1 125 ? 1.575   117.022 -7.277  1.00 13.77  ? 125 GLU B CG   1 
ATOM   3795  C CD   . GLU B 1 125 ? 2.520   118.149 -7.589  1.00 21.65  ? 125 GLU B CD   1 
ATOM   3796  O OE1  . GLU B 1 125 ? 3.670   117.865 -7.974  1.00 21.04  ? 125 GLU B OE1  1 
ATOM   3797  O OE2  . GLU B 1 125 ? 2.108   119.315 -7.453  1.00 18.47  ? 125 GLU B OE2  1 
ATOM   3798  N N    . THR B 1 126 ? 2.558   112.389 -6.856  1.00 5.63   ? 126 THR B N    1 
ATOM   3799  C CA   . THR B 1 126 ? 3.267   111.189 -7.258  1.00 6.12   ? 126 THR B CA   1 
ATOM   3800  C C    . THR B 1 126 ? 2.452   109.912 -7.144  1.00 6.57   ? 126 THR B C    1 
ATOM   3801  O O    . THR B 1 126 ? 2.646   109.003 -7.932  1.00 10.09  ? 126 THR B O    1 
ATOM   3802  C CB   . THR B 1 126 ? 4.681   111.050 -6.626  1.00 5.05   ? 126 THR B CB   1 
ATOM   3803  O OG1  . THR B 1 126 ? 4.626   110.303 -5.418  1.00 9.75   ? 126 THR B OG1  1 
ATOM   3804  C CG2  . THR B 1 126 ? 5.304   112.403 -6.360  1.00 5.94   ? 126 THR B CG2  1 
ATOM   3805  N N    . PHE B 1 127 ? 1.537   109.827 -6.198  1.00 5.89   ? 127 PHE B N    1 
ATOM   3806  C CA   . PHE B 1 127 ? 0.768   108.603 -5.991  1.00 7.52   ? 127 PHE B CA   1 
ATOM   3807  C C    . PHE B 1 127 ? -0.722  108.597 -6.351  1.00 8.01   ? 127 PHE B C    1 
ATOM   3808  O O    . PHE B 1 127 ? -1.381  107.608 -6.149  1.00 11.04  ? 127 PHE B O    1 
ATOM   3809  C CB   . PHE B 1 127 ? 0.977   108.157 -4.563  1.00 11.47  ? 127 PHE B CB   1 
ATOM   3810  C CG   . PHE B 1 127 ? 2.365   107.679 -4.268  1.00 9.11   ? 127 PHE B CG   1 
ATOM   3811  C CD1  . PHE B 1 127 ? 2.888   106.592 -4.925  1.00 9.60   ? 127 PHE B CD1  1 
ATOM   3812  C CD2  . PHE B 1 127 ? 3.133   108.299 -3.315  1.00 7.92   ? 127 PHE B CD2  1 
ATOM   3813  C CE1  . PHE B 1 127 ? 4.159   106.147 -4.653  1.00 10.02  ? 127 PHE B CE1  1 
ATOM   3814  C CE2  . PHE B 1 127 ? 4.403   107.859 -3.035  1.00 7.30   ? 127 PHE B CE2  1 
ATOM   3815  C CZ   . PHE B 1 127 ? 4.917   106.780 -3.706  1.00 7.19   ? 127 PHE B CZ   1 
ATOM   3816  N N    . ASN B 1 128 ? -1.232  109.652 -6.948  1.00 8.14   ? 128 ASN B N    1 
ATOM   3817  C CA   . ASN B 1 128 ? -2.660  109.798 -7.272  1.00 12.29  ? 128 ASN B CA   1 
ATOM   3818  C C    . ASN B 1 128 ? -3.607  109.249 -6.255  1.00 18.15  ? 128 ASN B C    1 
ATOM   3819  O O    . ASN B 1 128 ? -4.512  108.519 -6.590  1.00 17.83  ? 128 ASN B O    1 
ATOM   3820  C CB   . ASN B 1 128 ? -3.027  109.322 -8.666  1.00 11.83  ? 128 ASN B CB   1 
ATOM   3821  C CG   . ASN B 1 128 ? -4.275  109.971 -9.191  1.00 13.98  ? 128 ASN B CG   1 
ATOM   3822  O OD1  . ASN B 1 128 ? -4.566  111.120 -8.881  1.00 16.23  ? 128 ASN B OD1  1 
ATOM   3823  N ND2  . ASN B 1 128 ? -5.020  109.238 -9.993  1.00 15.24  ? 128 ASN B ND2  1 
ATOM   3824  N N    . THR B 1 129 ? -3.456  109.651 -5.014  1.00 16.63  ? 129 THR B N    1 
ATOM   3825  C CA   . THR B 1 129 ? -4.271  109.078 -3.996  1.00 13.37  ? 129 THR B CA   1 
ATOM   3826  C C    . THR B 1 129 ? -5.641  109.646 -4.094  1.00 13.64  ? 129 THR B C    1 
ATOM   3827  O O    . THR B 1 129 ? -5.814  110.757 -4.537  1.00 17.96  ? 129 THR B O    1 
ATOM   3828  C CB   . THR B 1 129 ? -3.586  109.166 -2.615  1.00 22.15  ? 129 THR B CB   1 
ATOM   3829  O OG1  . THR B 1 129 ? -4.074  108.136 -1.757  1.00 25.92  ? 129 THR B OG1  1 
ATOM   3830  C CG2  . THR B 1 129 ? -3.799  110.483 -1.955  1.00 21.36  ? 129 THR B CG2  1 
ATOM   3831  N N    . PRO B 1 130 ? -6.670  108.833 -3.707  1.00 11.55  ? 130 PRO B N    1 
ATOM   3832  C CA   . PRO B 1 130 ? -7.948  109.476 -3.778  1.00 10.73  ? 130 PRO B CA   1 
ATOM   3833  C C    . PRO B 1 130 ? -8.066  110.531 -2.749  1.00 15.30  ? 130 PRO B C    1 
ATOM   3834  O O    . PRO B 1 130 ? -8.483  111.645 -3.007  1.00 14.05  ? 130 PRO B O    1 
ATOM   3835  C CB   . PRO B 1 130 ? -8.869  108.342 -3.433  1.00 10.46  ? 130 PRO B CB   1 
ATOM   3836  C CG   . PRO B 1 130 ? -8.233  107.151 -3.973  1.00 12.56  ? 130 PRO B CG   1 
ATOM   3837  C CD   . PRO B 1 130 ? -6.873  107.379 -3.462  1.00 12.46  ? 130 PRO B CD   1 
ATOM   3838  N N    . ALA B 1 131 ? -7.701  110.170 -1.547  1.00 20.14  ? 131 ALA B N    1 
ATOM   3839  C CA   . ALA B 1 131 ? -7.773  111.088 -0.469  1.00 17.14  ? 131 ALA B CA   1 
ATOM   3840  C C    . ALA B 1 131 ? -6.631  110.892 0.489   1.00 20.04  ? 131 ALA B C    1 
ATOM   3841  O O    . ALA B 1 131 ? -6.076  109.808 0.555   1.00 17.79  ? 131 ALA B O    1 
ATOM   3842  C CB   . ALA B 1 131 ? -9.066  110.905 0.216   1.00 14.21  ? 131 ALA B CB   1 
ATOM   3843  N N    . MET B 1 132 ? -6.329  111.929 1.283   1.00 19.53  ? 132 MET B N    1 
ATOM   3844  C CA   . MET B 1 132 ? -5.224  111.865 2.245   1.00 17.18  ? 132 MET B CA   1 
ATOM   3845  C C    . MET B 1 132 ? -5.378  112.558 3.588   1.00 15.66  ? 132 MET B C    1 
ATOM   3846  O O    . MET B 1 132 ? -6.057  113.540 3.678   1.00 14.77  ? 132 MET B O    1 
ATOM   3847  C CB   . MET B 1 132 ? -3.987  112.430 1.566   1.00 14.97  ? 132 MET B CB   1 
ATOM   3848  C CG   . MET B 1 132 ? -2.646  112.063 2.135   1.00 21.58  ? 132 MET B CG   1 
ATOM   3849  S SD   . MET B 1 132 ? -1.642  113.522 1.881   1.00 25.98  ? 132 MET B SD   1 
ATOM   3850  C CE   . MET B 1 132 ? -2.537  114.692 2.870   1.00 13.50  ? 132 MET B CE   1 
ATOM   3851  N N    . TYR B 1 133 ? -4.724  112.044 4.630   1.00 13.72  ? 133 TYR B N    1 
ATOM   3852  C CA   . TYR B 1 133 ? -4.718  112.694 5.906   1.00 11.83  ? 133 TYR B CA   1 
ATOM   3853  C C    . TYR B 1 133 ? -3.370  112.496 6.519   1.00 16.88  ? 133 TYR B C    1 
ATOM   3854  O O    . TYR B 1 133 ? -2.817  111.445 6.372   1.00 15.63  ? 133 TYR B O    1 
ATOM   3855  C CB   . TYR B 1 133 ? -5.722  112.059 6.804   1.00 15.01  ? 133 TYR B CB   1 
ATOM   3856  C CG   . TYR B 1 133 ? -6.010  112.838 8.065   1.00 19.85  ? 133 TYR B CG   1 
ATOM   3857  C CD1  . TYR B 1 133 ? -6.885  113.892 8.060   1.00 19.44  ? 133 TYR B CD1  1 
ATOM   3858  C CD2  . TYR B 1 133 ? -5.404  112.508 9.259   1.00 17.50  ? 133 TYR B CD2  1 
ATOM   3859  C CE1  . TYR B 1 133 ? -7.142  114.601 9.207   1.00 20.15  ? 133 TYR B CE1  1 
ATOM   3860  C CE2  . TYR B 1 133 ? -5.657  113.214 10.403  1.00 21.89  ? 133 TYR B CE2  1 
ATOM   3861  C CZ   . TYR B 1 133 ? -6.525  114.262 10.373  1.00 26.25  ? 133 TYR B CZ   1 
ATOM   3862  O OH   . TYR B 1 133 ? -6.767  114.962 11.528  1.00 30.44  ? 133 TYR B OH   1 
ATOM   3863  N N    . VAL B 1 134 ? -2.820  113.500 7.206   1.00 18.28  ? 134 VAL B N    1 
ATOM   3864  C CA   . VAL B 1 134 ? -1.569  113.379 7.939   1.00 13.62  ? 134 VAL B CA   1 
ATOM   3865  C C    . VAL B 1 134 ? -1.864  113.667 9.375   1.00 13.93  ? 134 VAL B C    1 
ATOM   3866  O O    . VAL B 1 134 ? -2.294  114.733 9.692   1.00 19.70  ? 134 VAL B O    1 
ATOM   3867  C CB   . VAL B 1 134 ? -0.487  114.347 7.490   1.00 13.45  ? 134 VAL B CB   1 
ATOM   3868  C CG1  . VAL B 1 134 ? 0.849   113.771 7.851   1.00 18.48  ? 134 VAL B CG1  1 
ATOM   3869  C CG2  . VAL B 1 134 ? -0.535  114.570 5.994   1.00 17.80  ? 134 VAL B CG2  1 
ATOM   3870  N N    . ALA B 1 135 ? -1.639  112.713 10.261  1.00 17.79  ? 135 ALA B N    1 
ATOM   3871  C CA   . ALA B 1 135 ? -1.877  112.887 11.684  1.00 14.69  ? 135 ALA B CA   1 
ATOM   3872  C C    . ALA B 1 135 ? -0.641  112.669 12.474  1.00 10.37  ? 135 ALA B C    1 
ATOM   3873  O O    . ALA B 1 135 ? 0.356   112.384 11.929  1.00 9.17   ? 135 ALA B O    1 
ATOM   3874  C CB   . ALA B 1 135 ? -2.911  111.918 12.151  1.00 11.28  ? 135 ALA B CB   1 
ATOM   3875  N N    . ILE B 1 136 ? -0.716  112.793 13.781  1.00 8.86   ? 136 ILE B N    1 
ATOM   3876  C CA   . ILE B 1 136 ? 0.448   112.658 14.608  1.00 6.95   ? 136 ILE B CA   1 
ATOM   3877  C C    . ILE B 1 136 ? 0.426   111.292 15.156  1.00 7.27   ? 136 ILE B C    1 
ATOM   3878  O O    . ILE B 1 136 ? -0.602  110.769 15.487  1.00 9.77   ? 136 ILE B O    1 
ATOM   3879  C CB   . ILE B 1 136 ? 0.518   113.720 15.715  1.00 6.47   ? 136 ILE B CB   1 
ATOM   3880  C CG1  . ILE B 1 136 ? 0.354   115.114 15.131  1.00 9.49   ? 136 ILE B CG1  1 
ATOM   3881  C CG2  . ILE B 1 136 ? 1.822   113.669 16.475  1.00 7.79   ? 136 ILE B CG2  1 
ATOM   3882  C CD1  . ILE B 1 136 ? -0.507  116.034 15.961  1.00 5.62   ? 136 ILE B CD1  1 
ATOM   3883  N N    . GLN B 1 137 ? 1.574   110.683 15.218  1.00 6.41   ? 137 GLN B N    1 
ATOM   3884  C CA   . GLN B 1 137 ? 1.694   109.391 15.766  1.00 7.21   ? 137 GLN B CA   1 
ATOM   3885  C C    . GLN B 1 137 ? 1.058   109.262 17.116  1.00 8.22   ? 137 GLN B C    1 
ATOM   3886  O O    . GLN B 1 137 ? 0.351   108.325 17.368  1.00 9.64   ? 137 GLN B O    1 
ATOM   3887  C CB   . GLN B 1 137 ? 3.191   109.164 15.859  1.00 7.26   ? 137 GLN B CB   1 
ATOM   3888  C CG   . GLN B 1 137 ? 3.907   109.265 14.539  1.00 7.28   ? 137 GLN B CG   1 
ATOM   3889  C CD   . GLN B 1 137 ? 5.128   108.401 14.467  1.00 8.87   ? 137 GLN B CD   1 
ATOM   3890  O OE1  . GLN B 1 137 ? 5.418   107.651 15.384  1.00 6.65   ? 137 GLN B OE1  1 
ATOM   3891  N NE2  . GLN B 1 137 ? 5.848   108.495 13.369  1.00 14.42  ? 137 GLN B NE2  1 
ATOM   3892  N N    . ALA B 1 138 ? 1.318   110.194 18.010  1.00 7.63   ? 138 ALA B N    1 
ATOM   3893  C CA   . ALA B 1 138 ? 0.824   110.138 19.357  1.00 7.32   ? 138 ALA B CA   1 
ATOM   3894  C C    . ALA B 1 138 ? -0.624  110.410 19.578  1.00 9.76   ? 138 ALA B C    1 
ATOM   3895  O O    . ALA B 1 138 ? -1.193  109.942 20.528  1.00 11.01  ? 138 ALA B O    1 
ATOM   3896  C CB   . ALA B 1 138 ? 1.601   111.114 20.119  1.00 5.72   ? 138 ALA B CB   1 
ATOM   3897  N N    . VAL B 1 139 ? -1.245  111.189 18.726  1.00 7.27   ? 139 VAL B N    1 
ATOM   3898  C CA   . VAL B 1 139 ? -2.650  111.444 18.825  1.00 8.40   ? 139 VAL B CA   1 
ATOM   3899  C C    . VAL B 1 139 ? -3.341  110.147 18.532  1.00 13.43  ? 139 VAL B C    1 
ATOM   3900  O O    . VAL B 1 139 ? -4.362  109.862 19.121  1.00 11.87  ? 139 VAL B O    1 
ATOM   3901  C CB   . VAL B 1 139 ? -3.036  112.588 17.911  1.00 6.96   ? 139 VAL B CB   1 
ATOM   3902  C CG1  . VAL B 1 139 ? -4.526  112.777 17.849  1.00 9.76   ? 139 VAL B CG1  1 
ATOM   3903  C CG2  . VAL B 1 139 ? -2.413  113.865 18.419  1.00 8.85   ? 139 VAL B CG2  1 
ATOM   3904  N N    . LEU B 1 140 ? -2.738  109.301 17.703  1.00 13.57  ? 140 LEU B N    1 
ATOM   3905  C CA   . LEU B 1 140 ? -3.317  108.026 17.299  1.00 13.01  ? 140 LEU B CA   1 
ATOM   3906  C C    . LEU B 1 140 ? -2.959  106.905 18.209  1.00 14.15  ? 140 LEU B C    1 
ATOM   3907  O O    . LEU B 1 140 ? -3.611  105.907 18.215  1.00 17.59  ? 140 LEU B O    1 
ATOM   3908  C CB   . LEU B 1 140 ? -2.877  107.714 15.886  1.00 10.16  ? 140 LEU B CB   1 
ATOM   3909  C CG   . LEU B 1 140 ? -3.657  108.170 14.661  1.00 8.72   ? 140 LEU B CG   1 
ATOM   3910  C CD1  . LEU B 1 140 ? -4.292  109.529 14.817  1.00 11.02  ? 140 LEU B CD1  1 
ATOM   3911  C CD2  . LEU B 1 140 ? -2.747  108.172 13.464  1.00 9.31   ? 140 LEU B CD2  1 
ATOM   3912  N N    . SER B 1 141 ? -1.926  107.064 19.020  1.00 10.85  ? 141 SER B N    1 
ATOM   3913  C CA   . SER B 1 141 ? -1.561  106.058 19.997  1.00 12.30  ? 141 SER B CA   1 
ATOM   3914  C C    . SER B 1 141 ? -2.379  106.180 21.250  1.00 15.40  ? 141 SER B C    1 
ATOM   3915  O O    . SER B 1 141 ? -2.206  105.420 22.167  1.00 21.86  ? 141 SER B O    1 
ATOM   3916  C CB   . SER B 1 141 ? -0.096  106.159 20.348  1.00 11.76  ? 141 SER B CB   1 
ATOM   3917  O OG   . SER B 1 141 ? 0.655   106.786 19.351  1.00 17.93  ? 141 SER B OG   1 
ATOM   3918  N N    . LEU B 1 142 ? -3.308  107.109 21.267  1.00 16.06  ? 142 LEU B N    1 
ATOM   3919  C CA   . LEU B 1 142 ? -4.124  107.363 22.431  1.00 15.29  ? 142 LEU B CA   1 
ATOM   3920  C C    . LEU B 1 142 ? -5.499  107.046 22.041  1.00 15.43  ? 142 LEU B C    1 
ATOM   3921  O O    . LEU B 1 142 ? -6.329  106.821 22.877  1.00 17.18  ? 142 LEU B O    1 
ATOM   3922  C CB   . LEU B 1 142 ? -4.070  108.859 22.751  1.00 15.04  ? 142 LEU B CB   1 
ATOM   3923  C CG   . LEU B 1 142 ? -4.578  109.522 24.021  1.00 11.35  ? 142 LEU B CG   1 
ATOM   3924  C CD1  . LEU B 1 142 ? -3.552  109.412 25.127  1.00 8.10   ? 142 LEU B CD1  1 
ATOM   3925  C CD2  . LEU B 1 142 ? -4.855  110.975 23.715  1.00 8.40   ? 142 LEU B CD2  1 
ATOM   3926  N N    . TYR B 1 143 ? -5.765  107.059 20.761  1.00 13.55  ? 143 TYR B N    1 
ATOM   3927  C CA   . TYR B 1 143 ? -7.075  106.745 20.255  1.00 12.94  ? 143 TYR B CA   1 
ATOM   3928  C C    . TYR B 1 143 ? -7.191  105.273 20.244  1.00 16.37  ? 143 TYR B C    1 
ATOM   3929  O O    . TYR B 1 143 ? -8.284  104.750 20.186  1.00 14.16  ? 143 TYR B O    1 
ATOM   3930  C CB   . TYR B 1 143 ? -7.188  107.198 18.848  1.00 13.41  ? 143 TYR B CB   1 
ATOM   3931  C CG   . TYR B 1 143 ? -7.449  108.650 18.611  1.00 16.79  ? 143 TYR B CG   1 
ATOM   3932  C CD1  . TYR B 1 143 ? -8.035  109.442 19.570  1.00 17.86  ? 143 TYR B CD1  1 
ATOM   3933  C CD2  . TYR B 1 143 ? -7.115  109.227 17.409  1.00 15.81  ? 143 TYR B CD2  1 
ATOM   3934  C CE1  . TYR B 1 143 ? -8.289  110.771 19.344  1.00 17.89  ? 143 TYR B CE1  1 
ATOM   3935  C CE2  . TYR B 1 143 ? -7.344  110.557 17.180  1.00 15.25  ? 143 TYR B CE2  1 
ATOM   3936  C CZ   . TYR B 1 143 ? -7.939  111.319 18.151  1.00 16.06  ? 143 TYR B CZ   1 
ATOM   3937  O OH   . TYR B 1 143 ? -8.183  112.637 17.916  1.00 16.62  ? 143 TYR B OH   1 
ATOM   3938  N N    . ALA B 1 144 ? -6.066  104.570 20.287  1.00 13.74  ? 144 ALA B N    1 
ATOM   3939  C CA   . ALA B 1 144 ? -6.070  103.138 20.398  1.00 11.14  ? 144 ALA B CA   1 
ATOM   3940  C C    . ALA B 1 144 ? -6.618  102.813 21.732  1.00 14.95  ? 144 ALA B C    1 
ATOM   3941  O O    . ALA B 1 144 ? -7.533  102.026 21.843  1.00 16.93  ? 144 ALA B O    1 
ATOM   3942  C CB   . ALA B 1 144 ? -4.677  102.661 20.327  1.00 10.35  ? 144 ALA B CB   1 
ATOM   3943  N N    . SER B 1 145 ? -6.022  103.378 22.778  1.00 17.68  ? 145 SER B N    1 
ATOM   3944  C CA   . SER B 1 145 ? -6.462  103.208 24.165  1.00 14.83  ? 145 SER B CA   1 
ATOM   3945  C C    . SER B 1 145 ? -7.758  103.864 24.462  1.00 16.10  ? 145 SER B C    1 
ATOM   3946  O O    . SER B 1 145 ? -8.173  103.932 25.584  1.00 21.17  ? 145 SER B O    1 
ATOM   3947  C CB   . SER B 1 145 ? -5.459  103.897 25.040  1.00 14.35  ? 145 SER B CB   1 
ATOM   3948  O OG   . SER B 1 145 ? -5.445  105.277 24.783  1.00 18.97  ? 145 SER B OG   1 
ATOM   3949  N N    . GLY B 1 146 ? -8.389  104.422 23.469  1.00 14.30  ? 146 GLY B N    1 
ATOM   3950  C CA   . GLY B 1 146 ? -9.704  104.962 23.654  1.00 16.90  ? 146 GLY B CA   1 
ATOM   3951  C C    . GLY B 1 146 ? -9.809  106.267 24.285  1.00 16.24  ? 146 GLY B C    1 
ATOM   3952  O O    . GLY B 1 146 ? -10.831 106.630 24.835  1.00 18.26  ? 146 GLY B O    1 
ATOM   3953  N N    . ARG B 1 147 ? -8.759  107.038 24.146  1.00 15.37  ? 147 ARG B N    1 
ATOM   3954  C CA   . ARG B 1 147 ? -8.744  108.339 24.741  1.00 15.71  ? 147 ARG B CA   1 
ATOM   3955  C C    . ARG B 1 147 ? -8.621  109.404 23.738  1.00 12.57  ? 147 ARG B C    1 
ATOM   3956  O O    . ARG B 1 147 ? -8.164  109.177 22.668  1.00 15.02  ? 147 ARG B O    1 
ATOM   3957  C CB   . ARG B 1 147 ? -7.574  108.439 25.707  1.00 14.34  ? 147 ARG B CB   1 
ATOM   3958  C CG   . ARG B 1 147 ? -7.793  107.896 27.095  1.00 14.76  ? 147 ARG B CG   1 
ATOM   3959  C CD   . ARG B 1 147 ? -6.552  107.196 27.599  1.00 7.75   ? 147 ARG B CD   1 
ATOM   3960  N NE   . ARG B 1 147 ? -6.845  106.555 28.868  1.00 9.60   ? 147 ARG B NE   1 
ATOM   3961  C CZ   . ARG B 1 147 ? -7.045  105.256 29.022  1.00 9.98   ? 147 ARG B CZ   1 
ATOM   3962  N NH1  . ARG B 1 147 ? -6.960  104.445 27.997  1.00 10.84  ? 147 ARG B NH1  1 
ATOM   3963  N NH2  . ARG B 1 147 ? -7.318  104.762 30.205  1.00 9.81   ? 147 ARG B NH2  1 
ATOM   3964  N N    . THR B 1 148 ? -9.028  110.591 24.096  1.00 13.38  ? 148 THR B N    1 
ATOM   3965  C CA   . THR B 1 148 ? -8.933  111.726 23.237  1.00 14.04  ? 148 THR B CA   1 
ATOM   3966  C C    . THR B 1 148 ? -8.165  112.739 24.014  1.00 13.71  ? 148 THR B C    1 
ATOM   3967  O O    . THR B 1 148 ? -7.673  113.672 23.451  1.00 15.26  ? 148 THR B O    1 
ATOM   3968  C CB   . THR B 1 148 ? -10.315 112.244 22.932  1.00 15.76  ? 148 THR B CB   1 
ATOM   3969  O OG1  . THR B 1 148 ? -10.961 112.595 24.142  1.00 19.51  ? 148 THR B OG1  1 
ATOM   3970  C CG2  . THR B 1 148 ? -11.132 111.214 22.203  1.00 25.82  ? 148 THR B CG2  1 
ATOM   3971  N N    . THR B 1 149 ? -7.985  112.520 25.309  1.00 12.10  ? 149 THR B N    1 
ATOM   3972  C CA   . THR B 1 149 ? -7.210  113.407 26.172  1.00 10.12  ? 149 THR B CA   1 
ATOM   3973  C C    . THR B 1 149 ? -6.199  112.653 27.031  1.00 6.60   ? 149 THR B C    1 
ATOM   3974  O O    . THR B 1 149 ? -6.523  111.655 27.606  1.00 6.37   ? 149 THR B O    1 
ATOM   3975  C CB   . THR B 1 149 ? -8.103  114.342 27.024  1.00 12.33  ? 149 THR B CB   1 
ATOM   3976  O OG1  . THR B 1 149 ? -8.992  115.079 26.181  1.00 14.31  ? 149 THR B OG1  1 
ATOM   3977  C CG2  . THR B 1 149 ? -7.283  115.322 27.850  1.00 9.99   ? 149 THR B CG2  1 
ATOM   3978  N N    . GLY B 1 150 ? -4.963  113.128 27.085  1.00 6.31   ? 150 GLY B N    1 
ATOM   3979  C CA   . GLY B 1 150 ? -3.910  112.491 27.832  1.00 5.81   ? 150 GLY B CA   1 
ATOM   3980  C C    . GLY B 1 150 ? -2.519  112.786 27.344  1.00 5.71   ? 150 GLY B C    1 
ATOM   3981  O O    . GLY B 1 150 ? -2.358  113.593 26.488  1.00 5.54   ? 150 GLY B O    1 
ATOM   3982  N N    . ILE B 1 151 ? -1.514  112.147 27.920  1.00 5.44   ? 151 ILE B N    1 
ATOM   3983  C CA   . ILE B 1 151 ? -0.140  112.311 27.511  1.00 4.50   ? 151 ILE B CA   1 
ATOM   3984  C C    . ILE B 1 151 ? 0.400   111.004 26.968  1.00 4.62   ? 151 ILE B C    1 
ATOM   3985  O O    . ILE B 1 151 ? 0.114   109.975 27.478  1.00 4.05   ? 151 ILE B O    1 
ATOM   3986  C CB   . ILE B 1 151 ? 0.741   112.955 28.620  1.00 4.60   ? 151 ILE B CB   1 
ATOM   3987  C CG1  . ILE B 1 151 ? 2.210   113.055 28.227  1.00 4.71   ? 151 ILE B CG1  1 
ATOM   3988  C CG2  . ILE B 1 151 ? 0.595   112.250 29.935  1.00 7.80   ? 151 ILE B CG2  1 
ATOM   3989  C CD1  . ILE B 1 151 ? 2.874   114.304 28.728  1.00 5.03   ? 151 ILE B CD1  1 
ATOM   3990  N N    . VAL B 1 152 ? 1.117   111.048 25.854  1.00 4.28   ? 152 VAL B N    1 
ATOM   3991  C CA   . VAL B 1 152 ? 1.718   109.875 25.260  1.00 3.95   ? 152 VAL B CA   1 
ATOM   3992  C C    . VAL B 1 152 ? 3.227   109.885 25.337  1.00 4.15   ? 152 VAL B C    1 
ATOM   3993  O O    . VAL B 1 152 ? 3.825   110.917 25.264  1.00 3.95   ? 152 VAL B O    1 
ATOM   3994  C CB   . VAL B 1 152 ? 1.237   109.698 23.803  1.00 3.94   ? 152 VAL B CB   1 
ATOM   3995  C CG1  . VAL B 1 152 ? 2.093   108.751 22.992  1.00 6.15   ? 152 VAL B CG1  1 
ATOM   3996  C CG2  . VAL B 1 152 ? -0.178  109.187 23.776  1.00 7.19   ? 152 VAL B CG2  1 
ATOM   3997  N N    . MET B 1 153 ? 3.848   108.737 25.564  1.00 4.20   ? 153 MET B N    1 
ATOM   3998  C CA   . MET B 1 153 ? 5.274   108.639 25.525  1.00 3.67   ? 153 MET B CA   1 
ATOM   3999  C C    . MET B 1 153 ? 5.582   107.727 24.390  1.00 8.00   ? 153 MET B C    1 
ATOM   4000  O O    . MET B 1 153 ? 5.681   106.552 24.602  1.00 9.96   ? 153 MET B O    1 
ATOM   4001  C CB   . MET B 1 153 ? 5.848   108.013 26.779  1.00 3.47   ? 153 MET B CB   1 
ATOM   4002  C CG   . MET B 1 153 ? 7.232   108.457 27.137  1.00 3.71   ? 153 MET B CG   1 
ATOM   4003  S SD   . MET B 1 153 ? 8.255   107.024 26.917  1.00 10.18  ? 153 MET B SD   1 
ATOM   4004  C CE   . MET B 1 153 ? 7.579   105.954 28.151  1.00 8.10   ? 153 MET B CE   1 
ATOM   4005  N N    . ASP B 1 154 ? 5.774   108.260 23.190  1.00 5.56   ? 154 ASP B N    1 
ATOM   4006  C CA   . ASP B 1 154 ? 6.047   107.457 22.022  1.00 4.98   ? 154 ASP B CA   1 
ATOM   4007  C C    . ASP B 1 154 ? 7.498   107.205 21.868  1.00 6.47   ? 154 ASP B C    1 
ATOM   4008  O O    . ASP B 1 154 ? 8.268   108.107 21.713  1.00 5.98   ? 154 ASP B O    1 
ATOM   4009  C CB   . ASP B 1 154 ? 5.428   108.066 20.758  1.00 4.40   ? 154 ASP B CB   1 
ATOM   4010  C CG   . ASP B 1 154 ? 5.208   107.071 19.651  1.00 6.56   ? 154 ASP B CG   1 
ATOM   4011  O OD1  . ASP B 1 154 ? 5.227   105.854 19.880  1.00 8.34   ? 154 ASP B OD1  1 
ATOM   4012  O OD2  . ASP B 1 154 ? 5.000   107.527 18.518  1.00 5.82   ? 154 ASP B OD2  1 
ATOM   4013  N N    . SER B 1 155 ? 7.865   105.932 21.842  1.00 6.39   ? 155 SER B N    1 
ATOM   4014  C CA   . SER B 1 155 ? 9.223   105.543 21.634  1.00 7.20   ? 155 SER B CA   1 
ATOM   4015  C C    . SER B 1 155 ? 9.460   104.630 20.461  1.00 6.98   ? 155 SER B C    1 
ATOM   4016  O O    . SER B 1 155 ? 8.898   103.584 20.382  1.00 7.72   ? 155 SER B O    1 
ATOM   4017  C CB   . SER B 1 155 ? 9.720   104.868 22.852  1.00 6.98   ? 155 SER B CB   1 
ATOM   4018  O OG   . SER B 1 155 ? 9.146   103.598 22.939  1.00 10.14  ? 155 SER B OG   1 
ATOM   4019  N N    . GLY B 1 156 ? 10.327  105.021 19.553  1.00 6.28   ? 156 GLY B N    1 
ATOM   4020  C CA   . GLY B 1 156 ? 10.661  104.210 18.427  1.00 7.89   ? 156 GLY B CA   1 
ATOM   4021  C C    . GLY B 1 156 ? 12.103  103.849 18.429  1.00 9.13   ? 156 GLY B C    1 
ATOM   4022  O O    . GLY B 1 156 ? 12.661  103.768 19.484  1.00 8.54   ? 156 GLY B O    1 
ATOM   4023  N N    . ASP B 1 157 ? 12.676  103.522 17.277  1.00 11.82  ? 157 ASP B N    1 
ATOM   4024  C CA   . ASP B 1 157 ? 14.099  103.198 17.139  1.00 11.82  ? 157 ASP B CA   1 
ATOM   4025  C C    . ASP B 1 157 ? 15.023  104.363 17.426  1.00 9.39   ? 157 ASP B C    1 
ATOM   4026  O O    . ASP B 1 157 ? 16.100  104.182 17.935  1.00 8.89   ? 157 ASP B O    1 
ATOM   4027  C CB   . ASP B 1 157 ? 14.362  102.614 15.763  1.00 10.02  ? 157 ASP B CB   1 
ATOM   4028  C CG   . ASP B 1 157 ? 15.539  101.715 15.711  1.00 18.75  ? 157 ASP B CG   1 
ATOM   4029  O OD1  . ASP B 1 157 ? 15.965  101.224 16.767  1.00 30.02  ? 157 ASP B OD1  1 
ATOM   4030  O OD2  . ASP B 1 157 ? 16.028  101.479 14.593  1.00 22.57  ? 157 ASP B OD2  1 
ATOM   4031  N N    . GLY B 1 158 ? 14.637  105.552 17.023  1.00 7.16   ? 158 GLY B N    1 
ATOM   4032  C CA   . GLY B 1 158 ? 15.478  106.693 17.240  1.00 8.40   ? 158 GLY B CA   1 
ATOM   4033  C C    . GLY B 1 158 ? 14.985  107.944 17.857  1.00 11.01  ? 158 GLY B C    1 
ATOM   4034  O O    . GLY B 1 158 ? 15.763  108.817 18.188  1.00 8.25   ? 158 GLY B O    1 
ATOM   4035  N N    . VAL B 1 159 ? 13.685  108.048 17.983  1.00 12.25  ? 159 VAL B N    1 
ATOM   4036  C CA   . VAL B 1 159 ? 13.107  109.193 18.614  1.00 8.70   ? 159 VAL B CA   1 
ATOM   4037  C C    . VAL B 1 159 ? 12.048  108.864 19.650  1.00 8.12   ? 159 VAL B C    1 
ATOM   4038  O O    . VAL B 1 159 ? 11.166  108.076 19.402  1.00 9.06   ? 159 VAL B O    1 
ATOM   4039  C CB   . VAL B 1 159 ? 12.648  110.202 17.580  1.00 8.80   ? 159 VAL B CB   1 
ATOM   4040  C CG1  . VAL B 1 159 ? 11.355  109.790 16.909  1.00 10.37  ? 159 VAL B CG1  1 
ATOM   4041  C CG2  . VAL B 1 159 ? 12.564  111.573 18.192  1.00 10.01  ? 159 VAL B CG2  1 
ATOM   4042  N N    . THR B 1 160 ? 12.129  109.490 20.819  1.00 10.99  ? 160 THR B N    1 
ATOM   4043  C CA   . THR B 1 160 ? 11.168  109.284 21.887  1.00 9.11   ? 160 THR B CA   1 
ATOM   4044  C C    . THR B 1 160 ? 10.611  110.651 22.174  1.00 7.22   ? 160 THR B C    1 
ATOM   4045  O O    . THR B 1 160 ? 11.300  111.625 22.072  1.00 8.08   ? 160 THR B O    1 
ATOM   4046  C CB   . THR B 1 160 ? 11.816  108.625 23.127  1.00 6.51   ? 160 THR B CB   1 
ATOM   4047  O OG1  . THR B 1 160 ? 12.358  107.356 22.771  1.00 6.30   ? 160 THR B OG1  1 
ATOM   4048  C CG2  . THR B 1 160 ? 10.809  108.419 24.221  1.00 6.71   ? 160 THR B CG2  1 
ATOM   4049  N N    . HIS B 1 161 ? 9.346   110.739 22.496  1.00 4.91   ? 161 HIS B N    1 
ATOM   4050  C CA   . HIS B 1 161 ? 8.731   112.005 22.671  1.00 5.29   ? 161 HIS B CA   1 
ATOM   4051  C C    . HIS B 1 161 ? 7.690   111.921 23.716  1.00 5.51   ? 161 HIS B C    1 
ATOM   4052  O O    . HIS B 1 161 ? 7.166   110.869 23.942  1.00 5.27   ? 161 HIS B O    1 
ATOM   4053  C CB   . HIS B 1 161 ? 7.920   112.282 21.441  1.00 7.93   ? 161 HIS B CB   1 
ATOM   4054  C CG   . HIS B 1 161 ? 8.654   112.892 20.296  1.00 9.13   ? 161 HIS B CG   1 
ATOM   4055  N ND1  . HIS B 1 161 ? 9.166   112.146 19.261  1.00 7.76   ? 161 HIS B ND1  1 
ATOM   4056  C CD2  . HIS B 1 161 ? 8.852   114.184 19.958  1.00 8.36   ? 161 HIS B CD2  1 
ATOM   4057  C CE1  . HIS B 1 161 ? 9.697   112.951 18.364  1.00 7.71   ? 161 HIS B CE1  1 
ATOM   4058  N NE2  . HIS B 1 161 ? 9.530   114.192 18.768  1.00 9.19   ? 161 HIS B NE2  1 
ATOM   4059  N N    . THR B 1 162 ? 7.339   113.047 24.317  1.00 5.64   ? 162 THR B N    1 
ATOM   4060  C CA   . THR B 1 162 ? 6.279   113.104 25.288  1.00 5.28   ? 162 THR B CA   1 
ATOM   4061  C C    . THR B 1 162 ? 5.341   114.100 24.715  1.00 5.92   ? 162 THR B C    1 
ATOM   4062  O O    . THR B 1 162 ? 5.666   115.251 24.580  1.00 5.93   ? 162 THR B O    1 
ATOM   4063  C CB   . THR B 1 162 ? 6.785   113.476 26.664  1.00 5.81   ? 162 THR B CB   1 
ATOM   4064  O OG1  . THR B 1 162 ? 7.845   114.400 26.518  1.00 8.68   ? 162 THR B OG1  1 
ATOM   4065  C CG2  . THR B 1 162 ? 7.318   112.268 27.338  1.00 5.78   ? 162 THR B CG2  1 
ATOM   4066  N N    . VAL B 1 163 ? 4.159   113.652 24.361  1.00 5.62   ? 163 VAL B N    1 
ATOM   4067  C CA   . VAL B 1 163 ? 3.222   114.480 23.679  1.00 4.63   ? 163 VAL B CA   1 
ATOM   4068  C C    . VAL B 1 163 ? 1.947   114.610 24.445  1.00 6.37   ? 163 VAL B C    1 
ATOM   4069  O O    . VAL B 1 163 ? 1.254   113.642 24.616  1.00 4.25   ? 163 VAL B O    1 
ATOM   4070  C CB   . VAL B 1 163 ? 2.900   113.798 22.356  1.00 4.83   ? 163 VAL B CB   1 
ATOM   4071  C CG1  . VAL B 1 163 ? 1.872   114.549 21.562  1.00 6.26   ? 163 VAL B CG1  1 
ATOM   4072  C CG2  . VAL B 1 163 ? 4.155   113.583 21.546  1.00 5.15   ? 163 VAL B CG2  1 
ATOM   4073  N N    . PRO B 1 164 ? 1.651   115.852 24.981  1.00 5.91   ? 164 PRO B N    1 
ATOM   4074  C CA   . PRO B 1 164 ? 0.352   116.031 25.592  1.00 5.92   ? 164 PRO B CA   1 
ATOM   4075  C C    . PRO B 1 164 ? -0.752  116.298 24.616  1.00 6.81   ? 164 PRO B C    1 
ATOM   4076  O O    . PRO B 1 164 ? -0.581  117.069 23.722  1.00 8.35   ? 164 PRO B O    1 
ATOM   4077  C CB   . PRO B 1 164 ? 0.565   117.229 26.435  1.00 4.88   ? 164 PRO B CB   1 
ATOM   4078  C CG   . PRO B 1 164 ? 1.549   118.020 25.736  1.00 5.28   ? 164 PRO B CG   1 
ATOM   4079  C CD   . PRO B 1 164 ? 2.518   116.989 25.382  1.00 5.48   ? 164 PRO B CD   1 
ATOM   4080  N N    . ILE B 1 165 ? -1.905  115.680 24.787  1.00 7.39   ? 165 ILE B N    1 
ATOM   4081  C CA   . ILE B 1 165 ? -3.001  115.793 23.846  1.00 8.14   ? 165 ILE B CA   1 
ATOM   4082  C C    . ILE B 1 165 ? -4.256  116.197 24.578  1.00 8.59   ? 165 ILE B C    1 
ATOM   4083  O O    . ILE B 1 165 ? -4.731  115.476 25.403  1.00 7.96   ? 165 ILE B O    1 
ATOM   4084  C CB   . ILE B 1 165 ? -3.218  114.455 23.076  1.00 7.78   ? 165 ILE B CB   1 
ATOM   4085  C CG1  . ILE B 1 165 ? -1.941  113.958 22.423  1.00 7.07   ? 165 ILE B CG1  1 
ATOM   4086  C CG2  . ILE B 1 165 ? -4.303  114.569 22.033  1.00 8.22   ? 165 ILE B CG2  1 
ATOM   4087  C CD1  . ILE B 1 165 ? -1.562  112.577 22.862  1.00 6.40   ? 165 ILE B CD1  1 
ATOM   4088  N N    . TYR B 1 166 ? -4.771  117.377 24.302  1.00 11.24  ? 166 TYR B N    1 
ATOM   4089  C CA   . TYR B 1 166 ? -5.987  117.866 24.890  1.00 11.47  ? 166 TYR B CA   1 
ATOM   4090  C C    . TYR B 1 166 ? -7.023  117.937 23.846  1.00 14.94  ? 166 TYR B C    1 
ATOM   4091  O O    . TYR B 1 166 ? -7.107  118.932 23.151  1.00 14.71  ? 166 TYR B O    1 
ATOM   4092  C CB   . TYR B 1 166 ? -5.789  119.253 25.427  1.00 15.53  ? 166 TYR B CB   1 
ATOM   4093  C CG   . TYR B 1 166 ? -6.928  119.753 26.290  1.00 25.58  ? 166 TYR B CG   1 
ATOM   4094  C CD1  . TYR B 1 166 ? -7.509  118.944 27.253  1.00 23.06  ? 166 TYR B CD1  1 
ATOM   4095  C CD2  . TYR B 1 166 ? -7.424  121.031 26.134  1.00 23.48  ? 166 TYR B CD2  1 
ATOM   4096  C CE1  . TYR B 1 166 ? -8.554  119.396 28.031  1.00 20.90  ? 166 TYR B CE1  1 
ATOM   4097  C CE2  . TYR B 1 166 ? -8.468  121.492 26.908  1.00 25.39  ? 166 TYR B CE2  1 
ATOM   4098  C CZ   . TYR B 1 166 ? -9.030  120.673 27.853  1.00 25.48  ? 166 TYR B CZ   1 
ATOM   4099  O OH   . TYR B 1 166 ? -10.064 121.149 28.626  1.00 28.39  ? 166 TYR B OH   1 
ATOM   4100  N N    . GLU B 1 167 ? -7.820  116.898 23.736  1.00 13.44  ? 167 GLU B N    1 
ATOM   4101  C CA   . GLU B 1 167 ? -8.887  116.816 22.783  1.00 13.25  ? 167 GLU B CA   1 
ATOM   4102  C C    . GLU B 1 167 ? -8.448  116.714 21.382  1.00 14.15  ? 167 GLU B C    1 
ATOM   4103  O O    . GLU B 1 167 ? -8.828  117.483 20.531  1.00 19.72  ? 167 GLU B O    1 
ATOM   4104  C CB   . GLU B 1 167 ? -9.970  117.835 23.041  1.00 15.55  ? 167 GLU B CB   1 
ATOM   4105  C CG   . GLU B 1 167 ? -11.383 117.368 22.696  1.00 23.76  ? 167 GLU B CG   1 
ATOM   4106  C CD   . GLU B 1 167 ? -11.886 116.226 23.554  1.00 19.95  ? 167 GLU B CD   1 
ATOM   4107  O OE1  . GLU B 1 167 ? -11.591 116.202 24.758  1.00 24.82  ? 167 GLU B OE1  1 
ATOM   4108  O OE2  . GLU B 1 167 ? -12.598 115.355 23.020  1.00 13.51  ? 167 GLU B OE2  1 
ATOM   4109  N N    . GLY B 1 168 ? -7.612  115.747 21.123  1.00 11.09  ? 168 GLY B N    1 
ATOM   4110  C CA   . GLY B 1 168 ? -7.129  115.541 19.782  1.00 11.67  ? 168 GLY B CA   1 
ATOM   4111  C C    . GLY B 1 168 ? -6.024  116.436 19.361  1.00 11.32  ? 168 GLY B C    1 
ATOM   4112  O O    . GLY B 1 168 ? -5.529  116.344 18.259  1.00 12.62  ? 168 GLY B O    1 
ATOM   4113  N N    . TYR B 1 169 ? -5.609  117.300 20.247  1.00 10.77  ? 169 TYR B N    1 
ATOM   4114  C CA   . TYR B 1 169 ? -4.621  118.268 19.916  1.00 10.70  ? 169 TYR B CA   1 
ATOM   4115  C C    . TYR B 1 169 ? -3.455  118.121 20.760  1.00 10.18  ? 169 TYR B C    1 
ATOM   4116  O O    . TYR B 1 169 ? -3.500  118.272 21.935  1.00 9.88   ? 169 TYR B O    1 
ATOM   4117  C CB   . TYR B 1 169 ? -5.182  119.686 20.064  1.00 10.82  ? 169 TYR B CB   1 
ATOM   4118  C CG   . TYR B 1 169 ? -4.281  120.783 19.558  1.00 11.31  ? 169 TYR B CG   1 
ATOM   4119  C CD1  . TYR B 1 169 ? -3.766  120.750 18.282  1.00 12.06  ? 169 TYR B CD1  1 
ATOM   4120  C CD2  . TYR B 1 169 ? -3.951  121.850 20.362  1.00 12.93  ? 169 TYR B CD2  1 
ATOM   4121  C CE1  . TYR B 1 169 ? -2.931  121.742 17.828  1.00 13.01  ? 169 TYR B CE1  1 
ATOM   4122  C CE2  . TYR B 1 169 ? -3.120  122.847 19.915  1.00 14.85  ? 169 TYR B CE2  1 
ATOM   4123  C CZ   . TYR B 1 169 ? -2.617  122.788 18.646  1.00 13.04  ? 169 TYR B CZ   1 
ATOM   4124  O OH   . TYR B 1 169 ? -1.799  123.787 18.196  1.00 10.55  ? 169 TYR B OH   1 
ATOM   4125  N N    . ALA B 1 170 ? -2.358  117.860 20.124  1.00 8.91   ? 170 ALA B N    1 
ATOM   4126  C CA   . ALA B 1 170 ? -1.152  117.756 20.821  1.00 9.36   ? 170 ALA B CA   1 
ATOM   4127  C C    . ALA B 1 170 ? -0.809  119.155 20.969  1.00 12.05  ? 170 ALA B C    1 
ATOM   4128  O O    . ALA B 1 170 ? -0.979  119.913 20.053  1.00 13.61  ? 170 ALA B O    1 
ATOM   4129  C CB   . ALA B 1 170 ? -0.155  117.053 19.985  1.00 6.18   ? 170 ALA B CB   1 
ATOM   4130  N N    . LEU B 1 171 ? -0.310  119.519 22.120  1.00 11.47  ? 171 LEU B N    1 
ATOM   4131  C CA   . LEU B 1 171 ? -0.093  120.875 22.418  1.00 8.78   ? 171 LEU B CA   1 
ATOM   4132  C C    . LEU B 1 171 ? 1.288   121.222 22.162  1.00 7.47   ? 171 LEU B C    1 
ATOM   4133  O O    . LEU B 1 171 ? 2.141   120.848 22.900  1.00 8.51   ? 171 LEU B O    1 
ATOM   4134  C CB   . LEU B 1 171 ? -0.460  121.032 23.879  1.00 8.73   ? 171 LEU B CB   1 
ATOM   4135  C CG   . LEU B 1 171 ? -1.824  120.510 24.289  1.00 8.36   ? 171 LEU B CG   1 
ATOM   4136  C CD1  . LEU B 1 171 ? -1.882  120.344 25.785  1.00 7.80   ? 171 LEU B CD1  1 
ATOM   4137  C CD2  . LEU B 1 171 ? -2.883  121.475 23.827  1.00 10.48  ? 171 LEU B CD2  1 
ATOM   4138  N N    . PRO B 1 172 ? 1.524   122.065 21.121  1.00 6.15   ? 172 PRO B N    1 
ATOM   4139  C CA   . PRO B 1 172 ? 2.904   122.290 20.770  1.00 6.73   ? 172 PRO B CA   1 
ATOM   4140  C C    . PRO B 1 172 ? 3.810   123.008 21.728  1.00 8.50   ? 172 PRO B C    1 
ATOM   4141  O O    . PRO B 1 172 ? 5.012   123.040 21.525  1.00 7.04   ? 172 PRO B O    1 
ATOM   4142  C CB   . PRO B 1 172 ? 2.753   123.124 19.523  1.00 7.62   ? 172 PRO B CB   1 
ATOM   4143  C CG   . PRO B 1 172 ? 1.593   123.959 19.761  1.00 10.05  ? 172 PRO B CG   1 
ATOM   4144  C CD   . PRO B 1 172 ? 0.676   122.907 20.225  1.00 9.09   ? 172 PRO B CD   1 
ATOM   4145  N N    . HIS B 1 173 ? 3.255   123.608 22.752  1.00 9.19   ? 173 HIS B N    1 
ATOM   4146  C CA   . HIS B 1 173 ? 4.029   124.358 23.697  1.00 8.79   ? 173 HIS B CA   1 
ATOM   4147  C C    . HIS B 1 173 ? 4.573   123.419 24.689  1.00 8.68   ? 173 HIS B C    1 
ATOM   4148  O O    . HIS B 1 173 ? 5.389   123.794 25.513  1.00 6.84   ? 173 HIS B O    1 
ATOM   4149  C CB   . HIS B 1 173 ? 3.141   125.338 24.390  1.00 9.43   ? 173 HIS B CB   1 
ATOM   4150  C CG   . HIS B 1 173 ? 1.796   124.820 24.748  1.00 8.27   ? 173 HIS B CG   1 
ATOM   4151  N ND1  . HIS B 1 173 ? 1.552   124.150 25.922  1.00 8.29   ? 173 HIS B ND1  1 
ATOM   4152  C CD2  . HIS B 1 173 ? 0.606   124.932 24.121  1.00 10.95  ? 173 HIS B CD2  1 
ATOM   4153  C CE1  . HIS B 1 173 ? 0.275   123.838 25.988  1.00 12.88  ? 173 HIS B CE1  1 
ATOM   4154  N NE2  . HIS B 1 173 ? -0.321  124.302 24.908  1.00 17.28  ? 173 HIS B NE2  1 
ATOM   4155  N N    . ALA B 1 174 ? 4.149   122.166 24.591  1.00 6.27   ? 174 ALA B N    1 
ATOM   4156  C CA   . ALA B 1 174 ? 4.547   121.202 25.554  1.00 6.28   ? 174 ALA B CA   1 
ATOM   4157  C C    . ALA B 1 174 ? 4.966   119.915 25.024  1.00 7.08   ? 174 ALA B C    1 
ATOM   4158  O O    . ALA B 1 174 ? 5.029   118.976 25.759  1.00 7.67   ? 174 ALA B O    1 
ATOM   4159  C CB   . ALA B 1 174 ? 3.411   120.940 26.414  1.00 6.21   ? 174 ALA B CB   1 
ATOM   4160  N N    . ILE B 1 175 ? 5.262   119.827 23.744  1.00 6.48   ? 175 ILE B N    1 
ATOM   4161  C CA   . ILE B 1 175 ? 5.738   118.611 23.162  1.00 5.17   ? 175 ILE B CA   1 
ATOM   4162  C C    . ILE B 1 175 ? 7.185   118.620 23.456  1.00 6.88   ? 175 ILE B C    1 
ATOM   4163  O O    . ILE B 1 175 ? 7.859   119.608 23.245  1.00 4.60   ? 175 ILE B O    1 
ATOM   4164  C CB   . ILE B 1 175 ? 5.370   118.461 21.685  1.00 6.08   ? 175 ILE B CB   1 
ATOM   4165  C CG1  . ILE B 1 175 ? 3.868   118.300 21.540  1.00 6.54   ? 175 ILE B CG1  1 
ATOM   4166  C CG2  . ILE B 1 175 ? 6.030   117.248 21.061  1.00 5.06   ? 175 ILE B CG2  1 
ATOM   4167  C CD1  . ILE B 1 175 ? 3.440   117.998 20.130  1.00 9.93   ? 175 ILE B CD1  1 
ATOM   4168  N N    . LEU B 1 176 ? 7.670   117.516 23.981  1.00 0.82   ? 176 LEU B N    1 
ATOM   4169  C CA   . LEU B 1 176 ? 9.034   117.414 24.336  1.00 4.95   ? 176 LEU B CA   1 
ATOM   4170  C C    . LEU B 1 176 ? 9.613   116.227 23.662  1.00 6.36   ? 176 LEU B C    1 
ATOM   4171  O O    . LEU B 1 176 ? 8.985   115.207 23.629  1.00 5.03   ? 176 LEU B O    1 
ATOM   4172  C CB   . LEU B 1 176 ? 9.156   117.282 25.841  1.00 7.98   ? 176 LEU B CB   1 
ATOM   4173  C CG   . LEU B 1 176 ? 9.540   118.465 26.735  1.00 11.99  ? 176 LEU B CG   1 
ATOM   4174  C CD1  . LEU B 1 176 ? 8.356   119.374 26.980  1.00 8.57   ? 176 LEU B CD1  1 
ATOM   4175  C CD2  . LEU B 1 176 ? 10.095  117.989 28.061  1.00 6.93   ? 176 LEU B CD2  1 
ATOM   4176  N N    . ARG B 1 177 ? 10.819  116.358 23.131  1.00 6.10   ? 177 ARG B N    1 
ATOM   4177  C CA   . ARG B 1 177 ? 11.468  115.298 22.409  1.00 6.26   ? 177 ARG B CA   1 
ATOM   4178  C C    . ARG B 1 177 ? 12.749  114.834 22.990  1.00 7.65   ? 177 ARG B C    1 
ATOM   4179  O O    . ARG B 1 177 ? 13.633  115.627 23.243  1.00 8.51   ? 177 ARG B O    1 
ATOM   4180  C CB   . ARG B 1 177 ? 11.754  115.786 21.013  1.00 8.09   ? 177 ARG B CB   1 
ATOM   4181  C CG   . ARG B 1 177 ? 12.770  115.026 20.194  1.00 10.60  ? 177 ARG B CG   1 
ATOM   4182  C CD   . ARG B 1 177 ? 12.759  115.551 18.775  1.00 5.93   ? 177 ARG B CD   1 
ATOM   4183  N NE   . ARG B 1 177 ? 13.813  114.969 17.967  1.00 11.89  ? 177 ARG B NE   1 
ATOM   4184  C CZ   . ARG B 1 177 ? 13.795  114.918 16.643  1.00 15.78  ? 177 ARG B CZ   1 
ATOM   4185  N NH1  . ARG B 1 177 ? 12.769  115.395 15.967  1.00 13.15  ? 177 ARG B NH1  1 
ATOM   4186  N NH2  . ARG B 1 177 ? 14.801  114.371 15.998  1.00 11.34  ? 177 ARG B NH2  1 
ATOM   4187  N N    . LEU B 1 178 ? 12.891  113.515 23.182  1.00 9.63   ? 178 LEU B N    1 
ATOM   4188  C CA   . LEU B 1 178 ? 14.074  112.987 23.862  1.00 12.98  ? 178 LEU B CA   1 
ATOM   4189  C C    . LEU B 1 178 ? 15.199  112.556 22.971  1.00 16.69  ? 178 LEU B C    1 
ATOM   4190  O O    . LEU B 1 178 ? 16.351  112.770 23.318  1.00 27.83  ? 178 LEU B O    1 
ATOM   4191  C CB   . LEU B 1 178 ? 13.746  111.905 24.893  1.00 9.56   ? 178 LEU B CB   1 
ATOM   4192  C CG   . LEU B 1 178 ? 14.847  111.545 25.872  1.00 9.48   ? 178 LEU B CG   1 
ATOM   4193  C CD1  . LEU B 1 178 ? 15.271  112.798 26.607  1.00 7.73   ? 178 LEU B CD1  1 
ATOM   4194  C CD2  . LEU B 1 178 ? 14.392  110.463 26.832  1.00 6.85   ? 178 LEU B CD2  1 
ATOM   4195  N N    . ASP B 1 179 ? 14.898  111.990 21.824  1.00 9.93   ? 179 ASP B N    1 
ATOM   4196  C CA   . ASP B 1 179 ? 15.954  111.622 20.916  1.00 14.84  ? 179 ASP B CA   1 
ATOM   4197  C C    . ASP B 1 179 ? 16.872  110.546 21.494  1.00 13.20  ? 179 ASP B C    1 
ATOM   4198  O O    . ASP B 1 179 ? 18.066  110.520 21.214  1.00 10.41  ? 179 ASP B O    1 
ATOM   4199  C CB   . ASP B 1 179 ? 16.742  112.849 20.426  1.00 12.53  ? 179 ASP B CB   1 
ATOM   4200  C CG   . ASP B 1 179 ? 16.654  113.062 18.934  1.00 18.06  ? 179 ASP B CG   1 
ATOM   4201  O OD1  . ASP B 1 179 ? 15.641  112.687 18.333  1.00 19.89  ? 179 ASP B OD1  1 
ATOM   4202  O OD2  . ASP B 1 179 ? 17.600  113.627 18.357  1.00 20.13  ? 179 ASP B OD2  1 
ATOM   4203  N N    . LEU B 1 180 ? 16.321  109.646 22.292  1.00 9.48   ? 180 LEU B N    1 
ATOM   4204  C CA   . LEU B 1 180 ? 17.093  108.547 22.785  1.00 8.34   ? 180 LEU B CA   1 
ATOM   4205  C C    . LEU B 1 180 ? 16.059  107.542 22.620  1.00 8.19   ? 180 LEU B C    1 
ATOM   4206  O O    . LEU B 1 180 ? 14.922  107.804 22.943  1.00 6.23   ? 180 LEU B O    1 
ATOM   4207  C CB   . LEU B 1 180 ? 17.435  108.678 24.254  1.00 9.85   ? 180 LEU B CB   1 
ATOM   4208  C CG   . LEU B 1 180 ? 18.262  107.677 25.051  1.00 8.65   ? 180 LEU B CG   1 
ATOM   4209  C CD1  . LEU B 1 180 ? 18.722  108.393 26.298  1.00 7.12   ? 180 LEU B CD1  1 
ATOM   4210  C CD2  . LEU B 1 180 ? 17.431  106.484 25.465  1.00 9.94   ? 180 LEU B CD2  1 
ATOM   4211  N N    . ALA B 1 181 ? 16.451  106.384 22.116  1.00 9.57   ? 181 ALA B N    1 
ATOM   4212  C CA   . ALA B 1 181 ? 15.516  105.330 21.911  1.00 7.95   ? 181 ALA B CA   1 
ATOM   4213  C C    . ALA B 1 181 ? 16.062  104.019 21.659  1.00 7.41   ? 181 ALA B C    1 
ATOM   4214  O O    . ALA B 1 181 ? 17.031  103.636 22.240  1.00 8.91   ? 181 ALA B O    1 
ATOM   4215  C CB   . ALA B 1 181 ? 14.554  105.650 20.852  1.00 6.78   ? 181 ALA B CB   1 
ATOM   4216  N N    . GLY B 1 182 ? 15.438  103.290 20.781  1.00 6.20   ? 182 GLY B N    1 
ATOM   4217  C CA   . GLY B 1 182 ? 15.791  101.916 20.616  1.00 7.64   ? 182 GLY B CA   1 
ATOM   4218  C C    . GLY B 1 182 ? 17.135  101.522 20.247  1.00 9.83   ? 182 GLY B C    1 
ATOM   4219  O O    . GLY B 1 182 ? 17.610  100.530 20.735  1.00 12.51  ? 182 GLY B O    1 
ATOM   4220  N N    . ARG B 1 183 ? 17.809  102.328 19.487  1.00 11.24  ? 183 ARG B N    1 
ATOM   4221  C CA   . ARG B 1 183 ? 19.089  101.928 19.040  1.00 10.63  ? 183 ARG B CA   1 
ATOM   4222  C C    . ARG B 1 183 ? 20.072  102.263 20.074  1.00 8.48   ? 183 ARG B C    1 
ATOM   4223  O O    . ARG B 1 183 ? 21.022  101.551 20.262  1.00 11.74  ? 183 ARG B O    1 
ATOM   4224  C CB   . ARG B 1 183 ? 19.397  102.666 17.779  1.00 19.20  ? 183 ARG B CB   1 
ATOM   4225  C CG   . ARG B 1 183 ? 19.297  101.840 16.516  1.00 13.64  ? 183 ARG B CG   1 
ATOM   4226  C CD   . ARG B 1 183 ? 19.764  102.650 15.323  1.00 17.50  ? 183 ARG B CD   1 
ATOM   4227  N NE   . ARG B 1 183 ? 18.664  103.353 14.678  1.00 18.72  ? 183 ARG B NE   1 
ATOM   4228  C CZ   . ARG B 1 183 ? 18.432  104.654 14.778  1.00 23.66  ? 183 ARG B CZ   1 
ATOM   4229  N NH1  . ARG B 1 183 ? 19.232  105.427 15.494  1.00 24.52  ? 183 ARG B NH1  1 
ATOM   4230  N NH2  . ARG B 1 183 ? 17.396  105.177 14.153  1.00 24.09  ? 183 ARG B NH2  1 
ATOM   4231  N N    . ASP B 1 184 ? 19.854  103.353 20.753  1.00 7.33   ? 184 ASP B N    1 
ATOM   4232  C CA   . ASP B 1 184 ? 20.756  103.795 21.767  1.00 10.59  ? 184 ASP B CA   1 
ATOM   4233  C C    . ASP B 1 184 ? 20.886  102.765 22.852  1.00 11.80  ? 184 ASP B C    1 
ATOM   4234  O O    . ASP B 1 184 ? 21.890  102.707 23.524  1.00 10.42  ? 184 ASP B O    1 
ATOM   4235  C CB   . ASP B 1 184 ? 20.213  105.122 22.224  1.00 7.46   ? 184 ASP B CB   1 
ATOM   4236  C CG   . ASP B 1 184 ? 20.095  106.096 21.106  1.00 10.06  ? 184 ASP B CG   1 
ATOM   4237  O OD1  . ASP B 1 184 ? 19.053  106.103 20.437  1.00 10.64  ? 184 ASP B OD1  1 
ATOM   4238  O OD2  . ASP B 1 184 ? 21.052  106.853 20.883  1.00 13.69  ? 184 ASP B OD2  1 
ATOM   4239  N N    . LEU B 1 185 ? 19.885  101.940 23.029  1.00 7.87   ? 185 LEU B N    1 
ATOM   4240  C CA   . LEU B 1 185 ? 19.924  100.872 23.959  1.00 6.76   ? 185 LEU B CA   1 
ATOM   4241  C C    . LEU B 1 185 ? 20.615  99.661  23.493  1.00 8.86   ? 185 LEU B C    1 
ATOM   4242  O O    . LEU B 1 185 ? 21.420  99.119  24.170  1.00 15.13  ? 185 LEU B O    1 
ATOM   4243  C CB   . LEU B 1 185 ? 18.487  100.538 24.205  1.00 9.69   ? 185 LEU B CB   1 
ATOM   4244  C CG   . LEU B 1 185 ? 17.561  101.223 25.216  1.00 11.12  ? 185 LEU B CG   1 
ATOM   4245  C CD1  . LEU B 1 185 ? 17.675  102.724 25.337  1.00 8.18   ? 185 LEU B CD1  1 
ATOM   4246  C CD2  . LEU B 1 185 ? 16.143  100.852 24.879  1.00 8.11   ? 185 LEU B CD2  1 
ATOM   4247  N N    . THR B 1 186 ? 20.349  99.238  22.290  1.00 10.79  ? 186 THR B N    1 
ATOM   4248  C CA   . THR B 1 186 ? 20.959  98.053  21.732  1.00 11.81  ? 186 THR B CA   1 
ATOM   4249  C C    . THR B 1 186 ? 22.423  98.298  21.655  1.00 12.87  ? 186 THR B C    1 
ATOM   4250  O O    . THR B 1 186 ? 23.210  97.422  21.910  1.00 13.29  ? 186 THR B O    1 
ATOM   4251  C CB   . THR B 1 186 ? 20.463  97.837  20.312  1.00 9.42   ? 186 THR B CB   1 
ATOM   4252  O OG1  . THR B 1 186 ? 19.038  97.877  20.279  1.00 10.76  ? 186 THR B OG1  1 
ATOM   4253  C CG2  . THR B 1 186 ? 20.952  96.534  19.767  1.00 11.66  ? 186 THR B CG2  1 
ATOM   4254  N N    . ASP B 1 187 ? 22.802  99.496  21.286  1.00 9.82   ? 187 ASP B N    1 
ATOM   4255  C CA   . ASP B 1 187 ? 24.172  99.853  21.227  1.00 12.74  ? 187 ASP B CA   1 
ATOM   4256  C C    . ASP B 1 187 ? 24.793  99.934  22.597  1.00 19.79  ? 187 ASP B C    1 
ATOM   4257  O O    . ASP B 1 187 ? 25.975  99.699  22.732  1.00 23.98  ? 187 ASP B O    1 
ATOM   4258  C CB   . ASP B 1 187 ? 24.346  101.094 20.407  1.00 17.54  ? 187 ASP B CB   1 
ATOM   4259  C CG   . ASP B 1 187 ? 25.711  101.173 19.715  1.00 29.58  ? 187 ASP B CG   1 
ATOM   4260  O OD1  . ASP B 1 187 ? 26.721  100.691 20.266  1.00 23.98  ? 187 ASP B OD1  1 
ATOM   4261  O OD2  . ASP B 1 187 ? 25.777  101.744 18.608  1.00 24.86  ? 187 ASP B OD2  1 
ATOM   4262  N N    . TYR B 1 188 ? 24.076  100.379 23.614  1.00 14.24  ? 188 TYR B N    1 
ATOM   4263  C CA   . TYR B 1 188 ? 24.623  100.302 24.965  1.00 15.82  ? 188 TYR B CA   1 
ATOM   4264  C C    . TYR B 1 188 ? 24.748  98.867  25.331  1.00 16.08  ? 188 TYR B C    1 
ATOM   4265  O O    . TYR B 1 188 ? 25.770  98.459  25.790  1.00 21.61  ? 188 TYR B O    1 
ATOM   4266  C CB   . TYR B 1 188 ? 23.728  101.004 25.987  1.00 13.40  ? 188 TYR B CB   1 
ATOM   4267  C CG   . TYR B 1 188 ? 24.273  101.133 27.382  1.00 14.98  ? 188 TYR B CG   1 
ATOM   4268  C CD1  . TYR B 1 188 ? 25.476  101.757 27.618  1.00 17.20  ? 188 TYR B CD1  1 
ATOM   4269  C CD2  . TYR B 1 188 ? 23.561  100.667 28.463  1.00 14.54  ? 188 TYR B CD2  1 
ATOM   4270  C CE1  . TYR B 1 188 ? 25.973  101.889 28.894  1.00 19.26  ? 188 TYR B CE1  1 
ATOM   4271  C CE2  . TYR B 1 188 ? 24.052  100.790 29.740  1.00 19.15  ? 188 TYR B CE2  1 
ATOM   4272  C CZ   . TYR B 1 188 ? 25.260  101.405 29.951  1.00 23.99  ? 188 TYR B CZ   1 
ATOM   4273  O OH   . TYR B 1 188 ? 25.764  101.537 31.224  1.00 23.83  ? 188 TYR B OH   1 
ATOM   4274  N N    . LEU B 1 189 ? 23.736  98.076  25.051  1.00 11.91  ? 189 LEU B N    1 
ATOM   4275  C CA   . LEU B 1 189 ? 23.737  96.685  25.422  1.00 16.14  ? 189 LEU B CA   1 
ATOM   4276  C C    . LEU B 1 189 ? 24.782  95.976  24.667  1.00 20.27  ? 189 LEU B C    1 
ATOM   4277  O O    . LEU B 1 189 ? 25.375  95.050  25.172  1.00 21.65  ? 189 LEU B O    1 
ATOM   4278  C CB   . LEU B 1 189 ? 22.402  96.031  25.152  1.00 15.41  ? 189 LEU B CB   1 
ATOM   4279  C CG   . LEU B 1 189 ? 22.214  94.533  25.331  1.00 15.23  ? 189 LEU B CG   1 
ATOM   4280  C CD1  . LEU B 1 189 ? 22.433  94.152  26.773  1.00 19.30  ? 189 LEU B CD1  1 
ATOM   4281  C CD2  . LEU B 1 189 ? 20.820  94.146  24.898  1.00 14.30  ? 189 LEU B CD2  1 
ATOM   4282  N N    . MET B 1 190 ? 25.023  96.378  23.442  1.00 18.41  ? 190 MET B N    1 
ATOM   4283  C CA   . MET B 1 190 ? 26.130  95.791  22.724  1.00 22.78  ? 190 MET B CA   1 
ATOM   4284  C C    . MET B 1 190 ? 27.400  96.061  23.453  1.00 22.16  ? 190 MET B C    1 
ATOM   4285  O O    . MET B 1 190 ? 28.155  95.171  23.659  1.00 27.11  ? 190 MET B O    1 
ATOM   4286  C CB   . MET B 1 190 ? 26.207  96.317  21.319  1.00 22.84  ? 190 MET B CB   1 
ATOM   4287  C CG   . MET B 1 190 ? 26.825  95.376  20.321  1.00 33.18  ? 190 MET B CG   1 
ATOM   4288  S SD   . MET B 1 190 ? 27.214  96.293  18.836  1.00 49.14  ? 190 MET B SD   1 
ATOM   4289  C CE   . MET B 1 190 ? 28.963  96.558  19.066  1.00 53.66  ? 190 MET B CE   1 
ATOM   4290  N N    . LYS B 1 191 ? 27.644  97.294  23.839  1.00 16.20  ? 191 LYS B N    1 
ATOM   4291  C CA   . LYS B 1 191 ? 28.896  97.653  24.485  1.00 19.90  ? 191 LYS B CA   1 
ATOM   4292  C C    . LYS B 1 191 ? 29.096  97.127  25.884  1.00 26.81  ? 191 LYS B C    1 
ATOM   4293  O O    . LYS B 1 191 ? 30.218  96.843  26.273  1.00 30.71  ? 191 LYS B O    1 
ATOM   4294  C CB   . LYS B 1 191 ? 29.108  99.164  24.414  1.00 20.68  ? 191 LYS B CB   1 
ATOM   4295  C CG   . LYS B 1 191 ? 28.716  99.987  25.628  1.00 30.28  ? 191 LYS B CG   1 
ATOM   4296  C CD   . LYS B 1 191 ? 28.770  101.475 25.331  1.00 39.72  ? 191 LYS B CD   1 
ATOM   4297  C CE   . LYS B 1 191 ? 29.026  102.283 26.591  1.00 34.52  ? 191 LYS B CE   1 
ATOM   4298  N NZ   . LYS B 1 191 ? 28.727  103.728 26.400  1.00 30.12  ? 191 LYS B NZ   1 
ATOM   4299  N N    . ILE B 1 192 ? 28.021  96.993  26.646  1.00 25.50  ? 192 ILE B N    1 
ATOM   4300  C CA   . ILE B 1 192 ? 28.079  96.475  27.986  1.00 20.03  ? 192 ILE B CA   1 
ATOM   4301  C C    . ILE B 1 192 ? 28.076  94.987  27.948  1.00 22.38  ? 192 ILE B C    1 
ATOM   4302  O O    . ILE B 1 192 ? 28.296  94.352  28.937  1.00 19.86  ? 192 ILE B O    1 
ATOM   4303  C CB   . ILE B 1 192 ? 26.951  97.040  28.823  1.00 18.11  ? 192 ILE B CB   1 
ATOM   4304  C CG1  . ILE B 1 192 ? 25.594  96.502  28.420  1.00 14.41  ? 192 ILE B CG1  1 
ATOM   4305  C CG2  . ILE B 1 192 ? 26.978  98.529  28.704  1.00 17.78  ? 192 ILE B CG2  1 
ATOM   4306  C CD1  . ILE B 1 192 ? 24.457  97.136  29.176  1.00 12.78  ? 192 ILE B CD1  1 
ATOM   4307  N N    . LEU B 1 193 ? 27.887  94.408  26.782  1.00 24.81  ? 193 LEU B N    1 
ATOM   4308  C CA   . LEU B 1 193 ? 27.963  92.975  26.648  1.00 24.25  ? 193 LEU B CA   1 
ATOM   4309  C C    . LEU B 1 193 ? 29.288  92.716  26.010  1.00 25.83  ? 193 LEU B C    1 
ATOM   4310  O O    . LEU B 1 193 ? 29.877  91.695  26.240  1.00 30.22  ? 193 LEU B O    1 
ATOM   4311  C CB   . LEU B 1 193 ? 26.832  92.451  25.794  1.00 21.48  ? 193 LEU B CB   1 
ATOM   4312  C CG   . LEU B 1 193 ? 25.708  91.616  26.380  1.00 17.76  ? 193 LEU B CG   1 
ATOM   4313  C CD1  . LEU B 1 193 ? 24.794  91.256  25.230  1.00 16.43  ? 193 LEU B CD1  1 
ATOM   4314  C CD2  . LEU B 1 193 ? 26.241  90.361  27.043  1.00 22.34  ? 193 LEU B CD2  1 
ATOM   4315  N N    . THR B 1 194 ? 29.780  93.653  25.216  1.00 25.60  ? 194 THR B N    1 
ATOM   4316  C CA   . THR B 1 194 ? 31.080  93.533  24.583  1.00 29.15  ? 194 THR B CA   1 
ATOM   4317  C C    . THR B 1 194 ? 32.115  93.545  25.671  1.00 33.81  ? 194 THR B C    1 
ATOM   4318  O O    . THR B 1 194 ? 33.203  93.012  25.503  1.00 45.25  ? 194 THR B O    1 
ATOM   4319  C CB   . THR B 1 194 ? 31.276  94.645  23.556  1.00 28.22  ? 194 THR B CB   1 
ATOM   4320  O OG1  . THR B 1 194 ? 30.435  94.393  22.429  1.00 33.05  ? 194 THR B OG1  1 
ATOM   4321  C CG2  . THR B 1 194 ? 32.699  94.741  23.070  1.00 30.82  ? 194 THR B CG2  1 
ATOM   4322  N N    . GLU B 1 195 ? 31.778  94.060  26.829  1.00 29.45  ? 195 GLU B N    1 
ATOM   4323  C CA   . GLU B 1 195 ? 32.704  94.078  27.945  1.00 29.47  ? 195 GLU B CA   1 
ATOM   4324  C C    . GLU B 1 195 ? 32.589  92.884  28.832  1.00 30.03  ? 195 GLU B C    1 
ATOM   4325  O O    . GLU B 1 195 ? 33.461  92.653  29.652  1.00 35.46  ? 195 GLU B O    1 
ATOM   4326  C CB   . GLU B 1 195 ? 32.428  95.296  28.804  1.00 29.55  ? 195 GLU B CB   1 
ATOM   4327  C CG   . GLU B 1 195 ? 31.346  95.081  29.844  1.00 27.44  ? 195 GLU B CG   1 
ATOM   4328  C CD   . GLU B 1 195 ? 30.962  96.337  30.571  1.00 29.88  ? 195 GLU B CD   1 
ATOM   4329  O OE1  . GLU B 1 195 ? 31.488  97.412  30.231  1.00 38.25  ? 195 GLU B OE1  1 
ATOM   4330  O OE2  . GLU B 1 195 ? 30.118  96.242  31.477  1.00 31.47  ? 195 GLU B OE2  1 
ATOM   4331  N N    . ARG B 1 196 ? 31.540  92.112  28.686  1.00 22.85  ? 196 ARG B N    1 
ATOM   4332  C CA   . ARG B 1 196 ? 31.317  91.012  29.567  1.00 23.61  ? 196 ARG B CA   1 
ATOM   4333  C C    . ARG B 1 196 ? 32.144  89.884  29.034  1.00 30.31  ? 196 ARG B C    1 
ATOM   4334  O O    . ARG B 1 196 ? 32.190  88.804  29.611  1.00 26.92  ? 196 ARG B O    1 
ATOM   4335  C CB   . ARG B 1 196 ? 29.842  90.649  29.625  1.00 21.27  ? 196 ARG B CB   1 
ATOM   4336  C CG   . ARG B 1 196 ? 29.426  89.756  30.777  1.00 21.48  ? 196 ARG B CG   1 
ATOM   4337  C CD   . ARG B 1 196 ? 29.632  90.432  32.119  1.00 26.73  ? 196 ARG B CD   1 
ATOM   4338  N NE   . ARG B 1 196 ? 30.024  89.466  33.133  1.00 24.78  ? 196 ARG B NE   1 
ATOM   4339  C CZ   . ARG B 1 196 ? 31.269  89.292  33.557  1.00 29.75  ? 196 ARG B CZ   1 
ATOM   4340  N NH1  . ARG B 1 196 ? 32.250  90.044  33.081  1.00 31.11  ? 196 ARG B NH1  1 
ATOM   4341  N NH2  . ARG B 1 196 ? 31.532  88.379  34.473  1.00 41.80  ? 196 ARG B NH2  1 
ATOM   4342  N N    . GLY B 1 197 ? 32.853  90.130  27.951  1.00 31.03  ? 197 GLY B N    1 
ATOM   4343  C CA   . GLY B 1 197 ? 33.594  89.070  27.330  1.00 31.09  ? 197 GLY B CA   1 
ATOM   4344  C C    . GLY B 1 197 ? 32.760  88.375  26.298  1.00 36.84  ? 197 GLY B C    1 
ATOM   4345  O O    . GLY B 1 197 ? 33.075  87.265  25.887  1.00 44.18  ? 197 GLY B O    1 
ATOM   4346  N N    . TYR B 1 198 ? 31.673  88.998  25.893  1.00 31.52  ? 198 TYR B N    1 
ATOM   4347  C CA   . TYR B 1 198 ? 30.823  88.420  24.910  1.00 32.03  ? 198 TYR B CA   1 
ATOM   4348  C C    . TYR B 1 198 ? 30.714  89.497  23.906  1.00 38.38  ? 198 TYR B C    1 
ATOM   4349  O O    . TYR B 1 198 ? 29.697  90.143  23.834  1.00 40.63  ? 198 TYR B O    1 
ATOM   4350  C CB   . TYR B 1 198 ? 29.466  88.087  25.486  1.00 25.78  ? 198 TYR B CB   1 
ATOM   4351  C CG   . TYR B 1 198 ? 29.513  86.999  26.519  1.00 34.61  ? 198 TYR B CG   1 
ATOM   4352  C CD1  . TYR B 1 198 ? 29.929  85.726  26.188  1.00 35.79  ? 198 TYR B CD1  1 
ATOM   4353  C CD2  . TYR B 1 198 ? 29.151  87.243  27.827  1.00 47.72  ? 198 TYR B CD2  1 
ATOM   4354  C CE1  . TYR B 1 198 ? 29.980  84.722  27.131  1.00 46.87  ? 198 TYR B CE1  1 
ATOM   4355  C CE2  . TYR B 1 198 ? 29.201  86.246  28.779  1.00 48.34  ? 198 TYR B CE2  1 
ATOM   4356  C CZ   . TYR B 1 198 ? 29.614  84.988  28.422  1.00 47.65  ? 198 TYR B CZ   1 
ATOM   4357  O OH   . TYR B 1 198 ? 29.662  83.993  29.364  1.00 43.30  ? 198 TYR B OH   1 
ATOM   4358  N N    . SER B 1 199 ? 31.766  89.710  23.127  1.00 37.77  ? 199 SER B N    1 
ATOM   4359  C CA   . SER B 1 199 ? 31.796  90.765  22.120  1.00 36.09  ? 199 SER B CA   1 
ATOM   4360  C C    . SER B 1 199 ? 31.026  90.579  20.849  1.00 37.15  ? 199 SER B C    1 
ATOM   4361  O O    . SER B 1 199 ? 30.855  89.458  20.390  1.00 37.30  ? 199 SER B O    1 
ATOM   4362  C CB   . SER B 1 199 ? 33.226  91.141  21.786  1.00 35.53  ? 199 SER B CB   1 
ATOM   4363  O OG   . SER B 1 199 ? 33.283  92.053  20.709  1.00 37.03  ? 199 SER B OG   1 
ATOM   4364  N N    . PHE B 1 200 ? 30.583  91.685  20.275  1.00 35.48  ? 200 PHE B N    1 
ATOM   4365  C CA   . PHE B 1 200 ? 29.810  91.654  19.067  1.00 37.34  ? 200 PHE B CA   1 
ATOM   4366  C C    . PHE B 1 200 ? 30.343  92.770  18.204  1.00 38.42  ? 200 PHE B C    1 
ATOM   4367  O O    . PHE B 1 200 ? 30.776  93.791  18.700  1.00 32.68  ? 200 PHE B O    1 
ATOM   4368  C CB   . PHE B 1 200 ? 28.361  91.946  19.384  1.00 39.93  ? 200 PHE B CB   1 
ATOM   4369  C CG   . PHE B 1 200 ? 27.653  90.885  20.164  1.00 34.76  ? 200 PHE B CG   1 
ATOM   4370  C CD1  . PHE B 1 200 ? 27.032  89.837  19.518  1.00 42.39  ? 200 PHE B CD1  1 
ATOM   4371  C CD2  . PHE B 1 200 ? 27.537  90.977  21.533  1.00 28.73  ? 200 PHE B CD2  1 
ATOM   4372  C CE1  . PHE B 1 200 ? 26.346  88.875  20.224  1.00 37.08  ? 200 PHE B CE1  1 
ATOM   4373  C CE2  . PHE B 1 200 ? 26.858  90.016  22.247  1.00 32.93  ? 200 PHE B CE2  1 
ATOM   4374  C CZ   . PHE B 1 200 ? 26.260  88.963  21.592  1.00 33.16  ? 200 PHE B CZ   1 
ATOM   4375  N N    . THR B 1 201 ? 30.320  92.568  16.901  1.00 54.77  ? 201 THR B N    1 
ATOM   4376  C CA   . THR B 1 201 ? 30.733  93.612  15.952  1.00 64.37  ? 201 THR B CA   1 
ATOM   4377  C C    . THR B 1 201 ? 29.675  94.646  15.752  1.00 66.02  ? 201 THR B C    1 
ATOM   4378  O O    . THR B 1 201 ? 28.501  94.395  15.965  1.00 69.43  ? 201 THR B O    1 
ATOM   4379  C CB   . THR B 1 201 ? 31.004  93.034  14.558  1.00 53.99  ? 201 THR B CB   1 
ATOM   4380  O OG1  . THR B 1 201 ? 29.828  92.374  14.081  1.00 43.40  ? 201 THR B OG1  1 
ATOM   4381  C CG2  . THR B 1 201 ? 32.136  92.035  14.607  1.00 53.92  ? 201 THR B CG2  1 
ATOM   4382  N N    . THR B 1 202 ? 30.066  95.805  15.289  1.00 72.47  ? 202 THR B N    1 
ATOM   4383  C CA   . THR B 1 202 ? 29.117  96.856  15.104  1.00 78.80  ? 202 THR B CA   1 
ATOM   4384  C C    . THR B 1 202 ? 28.598  96.935  13.690  1.00 78.20  ? 202 THR B C    1 
ATOM   4385  O O    . THR B 1 202 ? 28.191  98.004  13.235  1.00 83.35  ? 202 THR B O    1 
ATOM   4386  C CB   . THR B 1 202 ? 29.798  98.189  15.420  1.00 77.68  ? 202 THR B CB   1 
ATOM   4387  O OG1  . THR B 1 202 ? 30.740  98.504  14.386  1.00 83.70  ? 202 THR B OG1  1 
ATOM   4388  C CG2  . THR B 1 202 ? 30.502  98.125  16.758  1.00 64.55  ? 202 THR B CG2  1 
ATOM   4389  N N    . THR B 1 203 ? 28.678  95.829  12.966  1.00 60.69  ? 203 THR B N    1 
ATOM   4390  C CA   . THR B 1 203 ? 28.169  95.833  11.635  1.00 63.65  ? 203 THR B CA   1 
ATOM   4391  C C    . THR B 1 203 ? 27.356  94.570  11.438  1.00 63.93  ? 203 THR B C    1 
ATOM   4392  O O    . THR B 1 203 ? 27.904  93.555  11.021  1.00 80.72  ? 203 THR B O    1 
ATOM   4393  C CB   . THR B 1 203 ? 29.297  96.060  10.607  1.00 65.32  ? 203 THR B CB   1 
ATOM   4394  O OG1  . THR B 1 203 ? 30.289  95.036  10.722  1.00 66.78  ? 203 THR B OG1  1 
ATOM   4395  C CG2  . THR B 1 203 ? 29.940  97.423  10.786  1.00 68.38  ? 203 THR B CG2  1 
ATOM   4396  N N    . ALA B 1 204 ? 26.094  94.573  11.848  1.00 46.57  ? 204 ALA B N    1 
ATOM   4397  C CA   . ALA B 1 204 ? 25.192  93.435  11.649  1.00 36.88  ? 204 ALA B CA   1 
ATOM   4398  C C    . ALA B 1 204 ? 25.283  92.157  12.469  1.00 32.21  ? 204 ALA B C    1 
ATOM   4399  O O    . ALA B 1 204 ? 24.569  91.210  12.218  1.00 26.95  ? 204 ALA B O    1 
ATOM   4400  C CB   . ALA B 1 204 ? 25.024  93.167  10.183  1.00 42.03  ? 204 ALA B CB   1 
ATOM   4401  N N    . GLU B 1 205 ? 26.141  92.116  13.465  1.00 46.10  ? 205 GLU B N    1 
ATOM   4402  C CA   . GLU B 1 205 ? 26.163  90.987  14.396  1.00 46.96  ? 205 GLU B CA   1 
ATOM   4403  C C    . GLU B 1 205 ? 25.498  91.602  15.560  1.00 48.16  ? 205 GLU B C    1 
ATOM   4404  O O    . GLU B 1 205 ? 25.385  90.990  16.607  1.00 43.10  ? 205 GLU B O    1 
ATOM   4405  C CB   . GLU B 1 205 ? 27.573  90.679  14.834  1.00 51.43  ? 205 GLU B CB   1 
ATOM   4406  C CG   . GLU B 1 205 ? 28.091  89.311  14.426  1.00 61.14  ? 205 GLU B CG   1 
ATOM   4407  C CD   . GLU B 1 205 ? 27.624  88.191  15.338  1.00 70.30  ? 205 GLU B CD   1 
ATOM   4408  O OE1  . GLU B 1 205 ? 27.224  88.475  16.485  1.00 68.36  ? 205 GLU B OE1  1 
ATOM   4409  O OE2  . GLU B 1 205 ? 27.663  87.021  14.904  1.00 68.62  ? 205 GLU B OE2  1 
ATOM   4410  N N    . ARG B 1 206 ? 25.066  92.841  15.391  1.00 50.16  ? 206 ARG B N    1 
ATOM   4411  C CA   . ARG B 1 206 ? 24.432  93.588  16.424  1.00 35.14  ? 206 ARG B CA   1 
ATOM   4412  C C    . ARG B 1 206 ? 22.944  93.527  16.296  1.00 31.71  ? 206 ARG B C    1 
ATOM   4413  O O    . ARG B 1 206 ? 22.258  94.384  16.809  1.00 36.26  ? 206 ARG B O    1 
ATOM   4414  C CB   . ARG B 1 206 ? 24.874  95.005  16.280  1.00 39.31  ? 206 ARG B CB   1 
ATOM   4415  C CG   . ARG B 1 206 ? 24.647  95.619  14.912  1.00 47.97  ? 206 ARG B CG   1 
ATOM   4416  C CD   . ARG B 1 206 ? 24.131  97.041  15.057  1.00 41.38  ? 206 ARG B CD   1 
ATOM   4417  N NE   . ARG B 1 206 ? 25.041  97.869  15.836  1.00 42.71  ? 206 ARG B NE   1 
ATOM   4418  C CZ   . ARG B 1 206 ? 25.824  98.796  15.309  1.00 48.26  ? 206 ARG B CZ   1 
ATOM   4419  N NH1  . ARG B 1 206 ? 25.790  99.024  14.007  1.00 50.22  ? 206 ARG B NH1  1 
ATOM   4420  N NH2  . ARG B 1 206 ? 26.625  99.507  16.083  1.00 48.40  ? 206 ARG B NH2  1 
ATOM   4421  N N    . GLU B 1 207 ? 22.432  92.565  15.558  1.00 32.15  ? 207 GLU B N    1 
ATOM   4422  C CA   . GLU B 1 207 ? 21.009  92.391  15.454  1.00 30.80  ? 207 GLU B CA   1 
ATOM   4423  C C    . GLU B 1 207 ? 20.735  91.291  16.371  1.00 27.22  ? 207 GLU B C    1 
ATOM   4424  O O    . GLU B 1 207 ? 19.626  91.089  16.786  1.00 34.08  ? 207 GLU B O    1 
ATOM   4425  C CB   . GLU B 1 207 ? 20.582  91.971  14.059  1.00 37.22  ? 207 GLU B CB   1 
ATOM   4426  C CG   . GLU B 1 207 ? 19.201  92.449  13.633  1.00 34.47  ? 207 GLU B CG   1 
ATOM   4427  C CD   . GLU B 1 207 ? 18.086  91.554  14.127  1.00 42.28  ? 207 GLU B CD   1 
ATOM   4428  O OE1  . GLU B 1 207 ? 18.128  90.344  13.831  1.00 44.36  ? 207 GLU B OE1  1 
ATOM   4429  O OE2  . GLU B 1 207 ? 17.162  92.056  14.802  1.00 36.33  ? 207 GLU B OE2  1 
ATOM   4430  N N    . ILE B 1 208 ? 21.745  90.530  16.678  1.00 23.89  ? 208 ILE B N    1 
ATOM   4431  C CA   . ILE B 1 208 ? 21.567  89.510  17.664  1.00 24.77  ? 208 ILE B CA   1 
ATOM   4432  C C    . ILE B 1 208 ? 21.400  90.243  18.968  1.00 28.32  ? 208 ILE B C    1 
ATOM   4433  O O    . ILE B 1 208 ? 20.639  89.822  19.825  1.00 22.98  ? 208 ILE B O    1 
ATOM   4434  C CB   . ILE B 1 208 ? 22.769  88.578  17.671  1.00 29.77  ? 208 ILE B CB   1 
ATOM   4435  C CG1  . ILE B 1 208 ? 23.030  88.047  16.271  1.00 37.75  ? 208 ILE B CG1  1 
ATOM   4436  C CG2  . ILE B 1 208 ? 22.551  87.416  18.610  1.00 37.10  ? 208 ILE B CG2  1 
ATOM   4437  C CD1  . ILE B 1 208 ? 24.126  87.014  16.228  1.00 48.01  ? 208 ILE B CD1  1 
ATOM   4438  N N    . VAL B 1 209 ? 22.118  91.339  19.135  1.00 25.55  ? 209 VAL B N    1 
ATOM   4439  C CA   . VAL B 1 209 ? 21.978  92.148  20.329  1.00 23.01  ? 209 VAL B CA   1 
ATOM   4440  C C    . VAL B 1 209 ? 20.684  92.938  20.401  1.00 21.74  ? 209 VAL B C    1 
ATOM   4441  O O    . VAL B 1 209 ? 20.339  93.451  21.440  1.00 20.73  ? 209 VAL B O    1 
ATOM   4442  C CB   . VAL B 1 209 ? 23.193  93.035  20.521  1.00 25.24  ? 209 VAL B CB   1 
ATOM   4443  C CG1  . VAL B 1 209 ? 22.995  93.960  21.699  1.00 30.45  ? 209 VAL B CG1  1 
ATOM   4444  C CG2  . VAL B 1 209 ? 24.403  92.184  20.791  1.00 27.42  ? 209 VAL B CG2  1 
ATOM   4445  N N    . ARG B 1 210 ? 19.979  93.084  19.297  1.00 20.95  ? 210 ARG B N    1 
ATOM   4446  C CA   . ARG B 1 210 ? 18.695  93.746  19.289  1.00 21.20  ? 210 ARG B CA   1 
ATOM   4447  C C    . ARG B 1 210 ? 17.653  92.783  19.644  1.00 22.30  ? 210 ARG B C    1 
ATOM   4448  O O    . ARG B 1 210 ? 16.529  93.141  19.811  1.00 22.26  ? 210 ARG B O    1 
ATOM   4449  C CB   . ARG B 1 210 ? 18.421  94.201  17.886  1.00 24.93  ? 210 ARG B CB   1 
ATOM   4450  C CG   . ARG B 1 210 ? 17.434  95.345  17.704  1.00 26.58  ? 210 ARG B CG   1 
ATOM   4451  C CD   . ARG B 1 210 ? 17.619  95.944  16.318  1.00 29.21  ? 210 ARG B CD   1 
ATOM   4452  N NE   . ARG B 1 210 ? 16.508  96.780  15.875  1.00 31.55  ? 210 ARG B NE   1 
ATOM   4453  C CZ   . ARG B 1 210 ? 16.413  97.270  14.643  1.00 27.43  ? 210 ARG B CZ   1 
ATOM   4454  N NH1  . ARG B 1 210 ? 17.363  97.001  13.763  1.00 21.11  ? 210 ARG B NH1  1 
ATOM   4455  N NH2  . ARG B 1 210 ? 15.376  98.020  14.286  1.00 18.43  ? 210 ARG B NH2  1 
ATOM   4456  N N    . ASP B 1 211 ? 18.017  91.531  19.718  1.00 20.80  ? 211 ASP B N    1 
ATOM   4457  C CA   . ASP B 1 211 ? 17.093  90.510  20.078  1.00 22.87  ? 211 ASP B CA   1 
ATOM   4458  C C    . ASP B 1 211 ? 17.234  90.190  21.528  1.00 25.09  ? 211 ASP B C    1 
ATOM   4459  O O    . ASP B 1 211 ? 16.299  89.732  22.137  1.00 28.43  ? 211 ASP B O    1 
ATOM   4460  C CB   . ASP B 1 211 ? 17.363  89.259  19.252  1.00 27.71  ? 211 ASP B CB   1 
ATOM   4461  C CG   . ASP B 1 211 ? 16.208  88.264  19.260  1.00 32.04  ? 211 ASP B CG   1 
ATOM   4462  O OD1  . ASP B 1 211 ? 15.059  88.658  18.957  1.00 35.20  ? 211 ASP B OD1  1 
ATOM   4463  O OD2  . ASP B 1 211 ? 16.460  87.073  19.534  1.00 20.26  ? 211 ASP B OD2  1 
ATOM   4464  N N    . ILE B 1 212 ? 18.381  90.427  22.121  1.00 23.90  ? 212 ILE B N    1 
ATOM   4465  C CA   . ILE B 1 212 ? 18.471  90.188  23.530  1.00 23.93  ? 212 ILE B CA   1 
ATOM   4466  C C    . ILE B 1 212 ? 17.714  91.291  24.218  1.00 20.62  ? 212 ILE B C    1 
ATOM   4467  O O    . ILE B 1 212 ? 17.168  91.093  25.268  1.00 18.75  ? 212 ILE B O    1 
ATOM   4468  C CB   . ILE B 1 212 ? 19.916  90.116  24.015  1.00 24.97  ? 212 ILE B CB   1 
ATOM   4469  C CG1  . ILE B 1 212 ? 20.795  89.433  22.982  1.00 25.77  ? 212 ILE B CG1  1 
ATOM   4470  C CG2  . ILE B 1 212 ? 19.994  89.365  25.324  1.00 33.14  ? 212 ILE B CG2  1 
ATOM   4471  C CD1  . ILE B 1 212 ? 22.208  89.203  23.450  1.00 20.90  ? 212 ILE B CD1  1 
ATOM   4472  N N    . LYS B 1 213 ? 17.667  92.456  23.619  1.00 19.95  ? 213 LYS B N    1 
ATOM   4473  C CA   . LYS B 1 213 ? 16.980  93.523  24.259  1.00 19.09  ? 213 LYS B CA   1 
ATOM   4474  C C    . LYS B 1 213 ? 15.492  93.404  24.285  1.00 23.75  ? 213 LYS B C    1 
ATOM   4475  O O    . LYS B 1 213 ? 14.886  93.509  25.313  1.00 38.66  ? 213 LYS B O    1 
ATOM   4476  C CB   . LYS B 1 213 ? 17.319  94.839  23.563  1.00 12.62  ? 213 LYS B CB   1 
ATOM   4477  C CG   . LYS B 1 213 ? 16.769  96.079  24.221  1.00 10.42  ? 213 LYS B CG   1 
ATOM   4478  C CD   . LYS B 1 213 ? 16.928  97.238  23.274  1.00 9.46   ? 213 LYS B CD   1 
ATOM   4479  C CE   . LYS B 1 213 ? 16.417  96.865  21.901  1.00 10.85  ? 213 LYS B CE   1 
ATOM   4480  N NZ   . LYS B 1 213 ? 16.400  98.054  21.017  1.00 7.83   ? 213 LYS B NZ   1 
ATOM   4481  N N    . GLU B 1 214 ? 14.852  93.159  23.177  1.00 19.97  ? 214 GLU B N    1 
ATOM   4482  C CA   . GLU B 1 214 ? 13.438  93.134  23.253  1.00 18.55  ? 214 GLU B CA   1 
ATOM   4483  C C    . GLU B 1 214 ? 13.057  91.914  24.024  1.00 23.54  ? 214 GLU B C    1 
ATOM   4484  O O    . GLU B 1 214 ? 12.206  91.980  24.898  1.00 25.73  ? 214 GLU B O    1 
ATOM   4485  C CB   . GLU B 1 214 ? 12.810  93.233  21.865  1.00 22.08  ? 214 GLU B CB   1 
ATOM   4486  C CG   . GLU B 1 214 ? 13.571  92.580  20.733  1.00 22.70  ? 214 GLU B CG   1 
ATOM   4487  C CD   . GLU B 1 214 ? 13.447  93.355  19.436  1.00 25.16  ? 214 GLU B CD   1 
ATOM   4488  O OE1  . GLU B 1 214 ? 13.223  94.578  19.492  1.00 17.92  ? 214 GLU B OE1  1 
ATOM   4489  O OE2  . GLU B 1 214 ? 13.591  92.750  18.355  1.00 29.83  ? 214 GLU B OE2  1 
ATOM   4490  N N    . LYS B 1 215 ? 13.686  90.796  23.709  1.00 22.05  ? 215 LYS B N    1 
ATOM   4491  C CA   . LYS B 1 215 ? 13.359  89.543  24.353  1.00 22.56  ? 215 LYS B CA   1 
ATOM   4492  C C    . LYS B 1 215 ? 13.723  89.283  25.779  1.00 25.85  ? 215 LYS B C    1 
ATOM   4493  O O    . LYS B 1 215 ? 12.909  88.797  26.547  1.00 23.84  ? 215 LYS B O    1 
ATOM   4494  C CB   . LYS B 1 215 ? 13.945  88.420  23.519  1.00 23.95  ? 215 LYS B CB   1 
ATOM   4495  C CG   . LYS B 1 215 ? 13.090  88.037  22.327  1.00 25.70  ? 215 LYS B CG   1 
ATOM   4496  C CD   . LYS B 1 215 ? 13.474  86.664  21.815  1.00 27.67  ? 215 LYS B CD   1 
ATOM   4497  C CE   . LYS B 1 215 ? 13.402  85.634  22.928  1.00 37.48  ? 215 LYS B CE   1 
ATOM   4498  N NZ   . LYS B 1 215 ? 12.029  85.501  23.491  1.00 35.62  ? 215 LYS B NZ   1 
ATOM   4499  N N    . LEU B 1 216 ? 14.930  89.624  26.153  1.00 25.60  ? 216 LEU B N    1 
ATOM   4500  C CA   . LEU B 1 216 ? 15.412  89.288  27.461  1.00 24.79  ? 216 LEU B CA   1 
ATOM   4501  C C    . LEU B 1 216 ? 15.931  90.533  28.114  1.00 25.56  ? 216 LEU B C    1 
ATOM   4502  O O    . LEU B 1 216 ? 17.120  90.655  28.298  1.00 28.00  ? 216 LEU B O    1 
ATOM   4503  C CB   . LEU B 1 216 ? 16.574  88.327  27.284  1.00 23.39  ? 216 LEU B CB   1 
ATOM   4504  C CG   . LEU B 1 216 ? 16.530  86.824  27.491  1.00 23.84  ? 216 LEU B CG   1 
ATOM   4505  C CD1  . LEU B 1 216 ? 15.653  86.153  26.457  1.00 28.75  ? 216 LEU B CD1  1 
ATOM   4506  C CD2  . LEU B 1 216 ? 17.954  86.318  27.374  1.00 20.95  ? 216 LEU B CD2  1 
ATOM   4507  N N    . CYS B 1 217 ? 15.047  91.457  28.476  1.00 23.94  ? 217 CYS B N    1 
ATOM   4508  C CA   . CYS B 1 217 ? 15.418  92.702  29.092  1.00 18.56  ? 217 CYS B CA   1 
ATOM   4509  C C    . CYS B 1 217 ? 14.148  93.222  29.647  1.00 22.50  ? 217 CYS B C    1 
ATOM   4510  O O    . CYS B 1 217 ? 13.076  92.899  29.136  1.00 18.49  ? 217 CYS B O    1 
ATOM   4511  C CB   . CYS B 1 217 ? 16.020  93.679  28.102  1.00 12.86  ? 217 CYS B CB   1 
ATOM   4512  S SG   . CYS B 1 217 ? 17.575  93.197  27.378  1.00 56.68  ? 217 CYS B SG   1 
ATOM   4513  N N    . TYR B 1 218 ? 14.242  94.000  30.714  1.00 19.48  ? 218 TYR B N    1 
ATOM   4514  C CA   . TYR B 1 218 ? 13.073  94.569  31.393  1.00 13.59  ? 218 TYR B CA   1 
ATOM   4515  C C    . TYR B 1 218 ? 13.469  95.832  32.093  1.00 16.47  ? 218 TYR B C    1 
ATOM   4516  O O    . TYR B 1 218 ? 14.633  96.028  32.361  1.00 18.32  ? 218 TYR B O    1 
ATOM   4517  C CB   . TYR B 1 218 ? 12.507  93.609  32.422  1.00 13.72  ? 218 TYR B CB   1 
ATOM   4518  C CG   . TYR B 1 218 ? 13.402  93.297  33.611  1.00 18.30  ? 218 TYR B CG   1 
ATOM   4519  C CD1  . TYR B 1 218 ? 14.570  92.565  33.461  1.00 23.41  ? 218 TYR B CD1  1 
ATOM   4520  C CD2  . TYR B 1 218 ? 13.063  93.715  34.885  1.00 12.00  ? 218 TYR B CD2  1 
ATOM   4521  C CE1  . TYR B 1 218 ? 15.378  92.283  34.529  1.00 18.19  ? 218 TYR B CE1  1 
ATOM   4522  C CE2  . TYR B 1 218 ? 13.870  93.434  35.960  1.00 17.65  ? 218 TYR B CE2  1 
ATOM   4523  C CZ   . TYR B 1 218 ? 15.022  92.717  35.767  1.00 24.28  ? 218 TYR B CZ   1 
ATOM   4524  O OH   . TYR B 1 218 ? 15.831  92.417  36.821  1.00 33.94  ? 218 TYR B OH   1 
ATOM   4525  N N    . VAL B 1 219 ? 12.512  96.663  32.491  1.00 13.94  ? 219 VAL B N    1 
ATOM   4526  C CA   . VAL B 1 219 ? 12.811  97.868  33.244  1.00 12.23  ? 219 VAL B CA   1 
ATOM   4527  C C    . VAL B 1 219 ? 12.816  97.509  34.697  1.00 15.31  ? 219 VAL B C    1 
ATOM   4528  O O    . VAL B 1 219 ? 11.913  96.830  35.146  1.00 15.87  ? 219 VAL B O    1 
ATOM   4529  C CB   . VAL B 1 219 ? 11.772  98.929  32.976  1.00 10.76  ? 219 VAL B CB   1 
ATOM   4530  C CG1  . VAL B 1 219 ? 11.919  100.096 33.925  1.00 12.81  ? 219 VAL B CG1  1 
ATOM   4531  C CG2  . VAL B 1 219 ? 11.860  99.400  31.542  1.00 14.68  ? 219 VAL B CG2  1 
ATOM   4532  N N    . ALA B 1 220 ? 13.798  97.974  35.463  1.00 14.14  ? 220 ALA B N    1 
ATOM   4533  C CA   . ALA B 1 220 ? 13.939  97.586  36.843  1.00 9.36   ? 220 ALA B CA   1 
ATOM   4534  C C    . ALA B 1 220 ? 13.448  98.616  37.748  1.00 8.83   ? 220 ALA B C    1 
ATOM   4535  O O    . ALA B 1 220 ? 13.930  99.714  37.707  1.00 8.32   ? 220 ALA B O    1 
ATOM   4536  C CB   . ALA B 1 220 ? 15.376  97.372  37.118  1.00 11.80  ? 220 ALA B CB   1 
ATOM   4537  N N    . LEU B 1 221 ? 12.519  98.265  38.614  1.00 10.86  ? 221 LEU B N    1 
ATOM   4538  C CA   . LEU B 1 221 ? 11.905  99.241  39.455  1.00 9.07   ? 221 LEU B CA   1 
ATOM   4539  C C    . LEU B 1 221 ? 12.850  99.891  40.395  1.00 13.02  ? 221 LEU B C    1 
ATOM   4540  O O    . LEU B 1 221 ? 12.778  101.090 40.572  1.00 20.86  ? 221 LEU B O    1 
ATOM   4541  C CB   . LEU B 1 221 ? 10.680  98.715  40.130  1.00 6.76   ? 221 LEU B CB   1 
ATOM   4542  C CG   . LEU B 1 221 ? 9.832   99.546  41.063  1.00 12.93  ? 221 LEU B CG   1 
ATOM   4543  C CD1  . LEU B 1 221 ? 9.555   100.870 40.405  1.00 16.30  ? 221 LEU B CD1  1 
ATOM   4544  C CD2  . LEU B 1 221 ? 8.538   98.798  41.318  1.00 12.79  ? 221 LEU B CD2  1 
ATOM   4545  N N    . ASP B 1 222 ? 13.744  99.171  41.041  1.00 9.14   ? 222 ASP B N    1 
ATOM   4546  C CA   . ASP B 1 222 ? 14.742  99.877  41.814  1.00 11.00  ? 222 ASP B CA   1 
ATOM   4547  C C    . ASP B 1 222 ? 16.015  99.369  41.248  1.00 14.44  ? 222 ASP B C    1 
ATOM   4548  O O    . ASP B 1 222 ? 16.381  98.249  41.509  1.00 18.82  ? 222 ASP B O    1 
ATOM   4549  C CB   . ASP B 1 222 ? 14.630  99.635  43.296  1.00 17.54  ? 222 ASP B CB   1 
ATOM   4550  C CG   . ASP B 1 222 ? 13.571  100.474 43.954  1.00 21.40  ? 222 ASP B CG   1 
ATOM   4551  O OD1  . ASP B 1 222 ? 13.103  101.450 43.347  1.00 20.25  ? 222 ASP B OD1  1 
ATOM   4552  O OD2  . ASP B 1 222 ? 13.216  100.158 45.103  1.00 20.64  ? 222 ASP B OD2  1 
ATOM   4553  N N    . PHE B 1 223 ? 16.714  100.184 40.489  1.00 9.94   ? 223 PHE B N    1 
ATOM   4554  C CA   . PHE B 1 223 ? 17.901  99.767  39.803  1.00 10.63  ? 223 PHE B CA   1 
ATOM   4555  C C    . PHE B 1 223 ? 18.899  99.398  40.792  1.00 15.05  ? 223 PHE B C    1 
ATOM   4556  O O    . PHE B 1 223 ? 19.727  98.538  40.568  1.00 15.64  ? 223 PHE B O    1 
ATOM   4557  C CB   . PHE B 1 223 ? 18.408  100.931 39.005  1.00 9.54   ? 223 PHE B CB   1 
ATOM   4558  C CG   . PHE B 1 223 ? 19.651  100.658 38.221  1.00 12.20  ? 223 PHE B CG   1 
ATOM   4559  C CD1  . PHE B 1 223 ? 19.695  99.641  37.292  1.00 15.15  ? 223 PHE B CD1  1 
ATOM   4560  C CD2  . PHE B 1 223 ? 20.760  101.460 38.382  1.00 12.50  ? 223 PHE B CD2  1 
ATOM   4561  C CE1  . PHE B 1 223 ? 20.834  99.406  36.562  1.00 15.03  ? 223 PHE B CE1  1 
ATOM   4562  C CE2  . PHE B 1 223 ? 21.901  101.230 37.656  1.00 12.35  ? 223 PHE B CE2  1 
ATOM   4563  C CZ   . PHE B 1 223 ? 21.935  100.205 36.743  1.00 14.36  ? 223 PHE B CZ   1 
ATOM   4564  N N    . GLU B 1 224 ? 18.873  100.094 41.892  1.00 14.48  ? 224 GLU B N    1 
ATOM   4565  C CA   . GLU B 1 224 ? 19.852  99.872  42.883  1.00 17.32  ? 224 GLU B CA   1 
ATOM   4566  C C    . GLU B 1 224 ? 19.581  98.595  43.640  1.00 21.29  ? 224 GLU B C    1 
ATOM   4567  O O    . GLU B 1 224 ? 20.523  97.942  44.050  1.00 22.77  ? 224 GLU B O    1 
ATOM   4568  C CB   . GLU B 1 224 ? 19.934  101.099 43.767  1.00 20.54  ? 224 GLU B CB   1 
ATOM   4569  C CG   . GLU B 1 224 ? 20.603  102.290 43.109  1.00 21.72  ? 224 GLU B CG   1 
ATOM   4570  C CD   . GLU B 1 224 ? 21.375  103.113 44.109  1.00 25.11  ? 224 GLU B CD   1 
ATOM   4571  O OE1  . GLU B 1 224 ? 21.374  102.736 45.289  1.00 25.26  ? 224 GLU B OE1  1 
ATOM   4572  O OE2  . GLU B 1 224 ? 21.983  104.126 43.728  1.00 31.38  ? 224 GLU B OE2  1 
ATOM   4573  N N    . GLN B 1 225 ? 18.324  98.191  43.799  1.00 19.96  ? 225 GLN B N    1 
ATOM   4574  C CA   . GLN B 1 225 ? 18.047  96.899  44.425  1.00 23.61  ? 225 GLN B CA   1 
ATOM   4575  C C    . GLN B 1 225 ? 18.366  95.886  43.421  1.00 26.18  ? 225 GLN B C    1 
ATOM   4576  O O    . GLN B 1 225 ? 18.823  94.809  43.719  1.00 26.62  ? 225 GLN B O    1 
ATOM   4577  C CB   . GLN B 1 225 ? 16.582  96.773  44.747  1.00 22.71  ? 225 GLN B CB   1 
ATOM   4578  C CG   . GLN B 1 225 ? 16.047  95.379  45.045  1.00 24.88  ? 225 GLN B CG   1 
ATOM   4579  C CD   . GLN B 1 225 ? 16.566  94.816  46.351  1.00 34.71  ? 225 GLN B CD   1 
ATOM   4580  O OE1  . GLN B 1 225 ? 16.221  95.300  47.429  1.00 26.35  ? 225 GLN B OE1  1 
ATOM   4581  N NE2  . GLN B 1 225 ? 17.398  93.788  46.262  1.00 34.85  ? 225 GLN B NE2  1 
ATOM   4582  N N    . GLU B 1 226 ? 18.093  96.219  42.184  1.00 25.06  ? 226 GLU B N    1 
ATOM   4583  C CA   . GLU B 1 226 ? 18.304  95.271  41.120  1.00 25.23  ? 226 GLU B CA   1 
ATOM   4584  C C    . GLU B 1 226 ? 19.761  94.989  40.963  1.00 21.95  ? 226 GLU B C    1 
ATOM   4585  O O    . GLU B 1 226 ? 20.152  93.881  40.705  1.00 25.24  ? 226 GLU B O    1 
ATOM   4586  C CB   . GLU B 1 226 ? 17.628  95.774  39.862  1.00 21.19  ? 226 GLU B CB   1 
ATOM   4587  C CG   . GLU B 1 226 ? 16.135  95.888  39.977  1.00 21.32  ? 226 GLU B CG   1 
ATOM   4588  C CD   . GLU B 1 226 ? 15.506  94.576  40.333  1.00 32.79  ? 226 GLU B CD   1 
ATOM   4589  O OE1  . GLU B 1 226 ? 15.948  93.541  39.802  1.00 20.84  ? 226 GLU B OE1  1 
ATOM   4590  O OE2  . GLU B 1 226 ? 14.570  94.587  41.155  1.00 48.95  ? 226 GLU B OE2  1 
ATOM   4591  N N    . MET B 1 227 ? 20.595  95.974  41.188  1.00 18.81  ? 227 MET B N    1 
ATOM   4592  C CA   . MET B 1 227 ? 22.012  95.667  41.183  1.00 24.44  ? 227 MET B CA   1 
ATOM   4593  C C    . MET B 1 227 ? 22.556  94.762  42.241  1.00 32.18  ? 227 MET B C    1 
ATOM   4594  O O    . MET B 1 227 ? 23.406  93.940  42.004  1.00 30.99  ? 227 MET B O    1 
ATOM   4595  C CB   . MET B 1 227 ? 22.772  96.974  41.056  1.00 28.90  ? 227 MET B CB   1 
ATOM   4596  C CG   . MET B 1 227 ? 22.544  97.737  39.773  1.00 21.98  ? 227 MET B CG   1 
ATOM   4597  S SD   . MET B 1 227 ? 22.998  96.849  38.284  1.00 27.27  ? 227 MET B SD   1 
ATOM   4598  C CE   . MET B 1 227 ? 24.765  96.746  38.471  1.00 19.16  ? 227 MET B CE   1 
ATOM   4599  N N    . ALA B 1 228 ? 21.971  94.877  43.416  1.00 32.58  ? 228 ALA B N    1 
ATOM   4600  C CA   . ALA B 1 228 ? 22.326  94.038  44.538  1.00 26.19  ? 228 ALA B CA   1 
ATOM   4601  C C    . ALA B 1 228 ? 21.892  92.624  44.390  1.00 32.20  ? 228 ALA B C    1 
ATOM   4602  O O    . ALA B 1 228 ? 22.581  91.746  44.855  1.00 42.23  ? 228 ALA B O    1 
ATOM   4603  C CB   . ALA B 1 228 ? 21.622  94.666  45.688  1.00 22.48  ? 228 ALA B CB   1 
ATOM   4604  N N    . THR B 1 229 ? 20.745  92.390  43.738  1.00 28.26  ? 229 THR B N    1 
ATOM   4605  C CA   . THR B 1 229 ? 20.208  91.054  43.507  1.00 27.39  ? 229 THR B CA   1 
ATOM   4606  C C    . THR B 1 229 ? 20.963  90.369  42.438  1.00 31.99  ? 229 THR B C    1 
ATOM   4607  O O    . THR B 1 229 ? 20.692  89.241  42.079  1.00 37.99  ? 229 THR B O    1 
ATOM   4608  C CB   . THR B 1 229 ? 18.764  91.121  43.008  1.00 29.96  ? 229 THR B CB   1 
ATOM   4609  O OG1  . THR B 1 229 ? 17.947  91.766  43.979  1.00 36.06  ? 229 THR B OG1  1 
ATOM   4610  C CG2  . THR B 1 229 ? 18.202  89.731  42.764  1.00 30.45  ? 229 THR B CG2  1 
ATOM   4611  N N    . ALA B 1 230 ? 21.949  91.047  41.903  1.00 32.35  ? 230 ALA B N    1 
ATOM   4612  C CA   . ALA B 1 230 ? 22.675  90.483  40.806  1.00 28.87  ? 230 ALA B CA   1 
ATOM   4613  C C    . ALA B 1 230 ? 24.019  90.045  41.233  1.00 34.42  ? 230 ALA B C    1 
ATOM   4614  O O    . ALA B 1 230 ? 24.619  89.188  40.604  1.00 37.35  ? 230 ALA B O    1 
ATOM   4615  C CB   . ALA B 1 230 ? 22.784  91.558  39.762  1.00 21.99  ? 230 ALA B CB   1 
ATOM   4616  N N    . ALA B 1 231 ? 24.515  90.628  42.313  1.00 30.82  ? 231 ALA B N    1 
ATOM   4617  C CA   . ALA B 1 231 ? 25.862  90.340  42.764  1.00 28.36  ? 231 ALA B CA   1 
ATOM   4618  C C    . ALA B 1 231 ? 25.832  89.497  43.966  1.00 33.71  ? 231 ALA B C    1 
ATOM   4619  O O    . ALA B 1 231 ? 26.814  89.344  44.648  1.00 31.83  ? 231 ALA B O    1 
ATOM   4620  C CB   . ALA B 1 231 ? 26.561  91.621  43.069  1.00 25.38  ? 231 ALA B CB   1 
ATOM   4621  N N    . SER B 1 232 ? 24.684  88.936  44.240  1.00 36.10  ? 232 SER B N    1 
ATOM   4622  C CA   . SER B 1 232 ? 24.569  88.040  45.333  1.00 40.45  ? 232 SER B CA   1 
ATOM   4623  C C    . SER B 1 232 ? 23.932  86.803  44.738  1.00 40.44  ? 232 SER B C    1 
ATOM   4624  O O    . SER B 1 232 ? 24.207  85.691  45.168  1.00 41.80  ? 232 SER B O    1 
ATOM   4625  C CB   . SER B 1 232 ? 23.693  88.648  46.407  1.00 29.68  ? 232 SER B CB   1 
ATOM   4626  O OG   . SER B 1 232 ? 22.406  88.951  45.914  1.00 40.81  ? 232 SER B OG   1 
ATOM   4627  N N    . SER B 1 233 ? 23.087  86.988  43.747  1.00 32.18  ? 233 SER B N    1 
ATOM   4628  C CA   . SER B 1 233 ? 22.402  85.873  43.177  1.00 31.00  ? 233 SER B CA   1 
ATOM   4629  C C    . SER B 1 233 ? 22.437  85.714  41.678  1.00 42.28  ? 233 SER B C    1 
ATOM   4630  O O    . SER B 1 233 ? 22.488  86.699  40.956  1.00 44.54  ? 233 SER B O    1 
ATOM   4631  C CB   . SER B 1 233 ? 20.961  86.056  43.596  1.00 21.14  ? 233 SER B CB   1 
ATOM   4632  O OG   . SER B 1 233 ? 20.825  85.971  44.992  1.00 29.53  ? 233 SER B OG   1 
ATOM   4633  N N    . SER B 1 234 ? 22.427  84.477  41.195  1.00 34.19  ? 234 SER B N    1 
ATOM   4634  C CA   . SER B 1 234 ? 22.405  84.211  39.774  1.00 33.64  ? 234 SER B CA   1 
ATOM   4635  C C    . SER B 1 234 ? 20.991  83.936  39.475  1.00 34.90  ? 234 SER B C    1 
ATOM   4636  O O    . SER B 1 234 ? 20.683  83.147  38.604  1.00 37.17  ? 234 SER B O    1 
ATOM   4637  C CB   . SER B 1 234 ? 23.168  82.973  39.416  1.00 45.25  ? 234 SER B CB   1 
ATOM   4638  O OG   . SER B 1 234 ? 23.016  81.988  40.419  1.00 48.76  ? 234 SER B OG   1 
ATOM   4639  N N    . SER B 1 235 ? 20.106  84.617  40.167  1.00 34.85  ? 235 SER B N    1 
ATOM   4640  C CA   . SER B 1 235 ? 18.689  84.418  40.003  1.00 34.23  ? 235 SER B CA   1 
ATOM   4641  C C    . SER B 1 235 ? 18.183  85.323  38.953  1.00 32.82  ? 235 SER B C    1 
ATOM   4642  O O    . SER B 1 235 ? 17.049  85.189  38.511  1.00 29.60  ? 235 SER B O    1 
ATOM   4643  C CB   . SER B 1 235 ? 18.016  84.802  41.303  1.00 35.69  ? 235 SER B CB   1 
ATOM   4644  O OG   . SER B 1 235 ? 17.425  86.080  41.228  1.00 46.80  ? 235 SER B OG   1 
ATOM   4645  N N    . LEU B 1 236 ? 19.009  86.273  38.547  1.00 36.09  ? 236 LEU B N    1 
ATOM   4646  C CA   . LEU B 1 236 ? 18.575  87.276  37.587  1.00 38.32  ? 236 LEU B CA   1 
ATOM   4647  C C    . LEU B 1 236 ? 19.255  87.089  36.273  1.00 28.71  ? 236 LEU B C    1 
ATOM   4648  O O    . LEU B 1 236 ? 19.107  87.881  35.363  1.00 28.52  ? 236 LEU B O    1 
ATOM   4649  C CB   . LEU B 1 236 ? 18.883  88.654  38.153  1.00 38.60  ? 236 LEU B CB   1 
ATOM   4650  C CG   . LEU B 1 236 ? 17.935  89.272  39.167  1.00 24.70  ? 236 LEU B CG   1 
ATOM   4651  C CD1  . LEU B 1 236 ? 18.352  90.711  39.338  1.00 31.09  ? 236 LEU B CD1  1 
ATOM   4652  C CD2  . LEU B 1 236 ? 16.500  89.188  38.683  1.00 19.10  ? 236 LEU B CD2  1 
ATOM   4653  N N    . GLU B 1 237 ? 19.972  86.003  36.150  1.00 30.02  ? 237 GLU B N    1 
ATOM   4654  C CA   . GLU B 1 237 ? 20.680  85.746  34.947  1.00 33.36  ? 237 GLU B CA   1 
ATOM   4655  C C    . GLU B 1 237 ? 19.796  84.973  34.031  1.00 33.68  ? 237 GLU B C    1 
ATOM   4656  O O    . GLU B 1 237 ? 18.905  84.276  34.486  1.00 32.12  ? 237 GLU B O    1 
ATOM   4657  C CB   . GLU B 1 237 ? 21.966  85.004  35.255  1.00 29.96  ? 237 GLU B CB   1 
ATOM   4658  C CG   . GLU B 1 237 ? 23.040  85.842  35.911  1.00 32.45  ? 237 GLU B CG   1 
ATOM   4659  C CD   . GLU B 1 237 ? 24.320  85.062  36.107  1.00 45.88  ? 237 GLU B CD   1 
ATOM   4660  O OE1  . GLU B 1 237 ? 24.501  84.046  35.418  1.00 54.41  ? 237 GLU B OE1  1 
ATOM   4661  O OE2  . GLU B 1 237 ? 25.146  85.456  36.952  1.00 49.88  ? 237 GLU B OE2  1 
ATOM   4662  N N    . LYS B 1 238 ? 20.005  85.128  32.732  1.00 30.24  ? 238 LYS B N    1 
ATOM   4663  C CA   . LYS B 1 238 ? 19.250  84.412  31.741  1.00 26.99  ? 238 LYS B CA   1 
ATOM   4664  C C    . LYS B 1 238 ? 20.268  84.029  30.702  1.00 34.89  ? 238 LYS B C    1 
ATOM   4665  O O    . LYS B 1 238 ? 21.403  84.478  30.776  1.00 35.51  ? 238 LYS B O    1 
ATOM   4666  C CB   . LYS B 1 238 ? 18.153  85.259  31.165  1.00 19.09  ? 238 LYS B CB   1 
ATOM   4667  C CG   . LYS B 1 238 ? 16.855  85.233  31.940  1.00 20.43  ? 238 LYS B CG   1 
ATOM   4668  C CD   . LYS B 1 238 ? 15.805  84.400  31.242  1.00 24.86  ? 238 LYS B CD   1 
ATOM   4669  C CE   . LYS B 1 238 ? 14.465  84.528  31.943  1.00 22.55  ? 238 LYS B CE   1 
ATOM   4670  N NZ   . LYS B 1 238 ? 14.369  83.670  33.154  1.00 26.38  ? 238 LYS B NZ   1 
ATOM   4671  N N    . SER B 1 239 ? 19.898  83.181  29.740  1.00 39.12  ? 239 SER B N    1 
ATOM   4672  C CA   . SER B 1 239 ? 20.855  82.661  28.760  1.00 30.49  ? 239 SER B CA   1 
ATOM   4673  C C    . SER B 1 239 ? 20.406  82.841  27.337  1.00 33.43  ? 239 SER B C    1 
ATOM   4674  O O    . SER B 1 239 ? 19.231  82.671  27.027  1.00 34.03  ? 239 SER B O    1 
ATOM   4675  C CB   . SER B 1 239 ? 21.120  81.170  29.009  1.00 28.26  ? 239 SER B CB   1 
ATOM   4676  O OG   . SER B 1 239 ? 21.779  80.944  30.236  1.00 35.36  ? 239 SER B OG   1 
ATOM   4677  N N    . TYR B 1 240 ? 21.347  83.171  26.466  1.00 33.64  ? 240 TYR B N    1 
ATOM   4678  C CA   . TYR B 1 240 ? 21.028  83.375  25.080  1.00 29.92  ? 240 TYR B CA   1 
ATOM   4679  C C    . TYR B 1 240 ? 21.842  82.465  24.221  1.00 39.97  ? 240 TYR B C    1 
ATOM   4680  O O    . TYR B 1 240 ? 23.042  82.421  24.359  1.00 38.79  ? 240 TYR B O    1 
ATOM   4681  C CB   . TYR B 1 240 ? 21.364  84.796  24.707  1.00 26.98  ? 240 TYR B CB   1 
ATOM   4682  C CG   . TYR B 1 240 ? 20.749  85.264  23.426  1.00 33.93  ? 240 TYR B CG   1 
ATOM   4683  C CD1  . TYR B 1 240 ? 19.419  85.634  23.374  1.00 35.73  ? 240 TYR B CD1  1 
ATOM   4684  C CD2  . TYR B 1 240 ? 21.502  85.350  22.271  1.00 35.20  ? 240 TYR B CD2  1 
ATOM   4685  C CE1  . TYR B 1 240 ? 18.850  86.067  22.200  1.00 38.74  ? 240 TYR B CE1  1 
ATOM   4686  C CE2  . TYR B 1 240 ? 20.945  85.780  21.097  1.00 37.94  ? 240 TYR B CE2  1 
ATOM   4687  C CZ   . TYR B 1 240 ? 19.621  86.139  21.067  1.00 44.26  ? 240 TYR B CZ   1 
ATOM   4688  O OH   . TYR B 1 240 ? 19.071  86.568  19.889  1.00 36.62  ? 240 TYR B OH   1 
ATOM   4689  N N    . GLU B 1 241 ? 21.203  81.754  23.300  1.00 49.90  ? 241 GLU B N    1 
ATOM   4690  C CA   . GLU B 1 241 ? 21.928  80.913  22.365  1.00 50.24  ? 241 GLU B CA   1 
ATOM   4691  C C    . GLU B 1 241 ? 22.082  81.710  21.106  1.00 46.67  ? 241 GLU B C    1 
ATOM   4692  O O    . GLU B 1 241 ? 21.098  82.110  20.487  1.00 41.79  ? 241 GLU B O    1 
ATOM   4693  C CB   . GLU B 1 241 ? 21.141  79.648  22.052  1.00 48.70  ? 241 GLU B CB   1 
ATOM   4694  C CG   . GLU B 1 241 ? 21.969  78.510  21.467  1.00 54.77  ? 241 GLU B CG   1 
ATOM   4695  C CD   . GLU B 1 241 ? 22.046  78.512  19.948  1.00 64.51  ? 241 GLU B CD   1 
ATOM   4696  O OE1  . GLU B 1 241 ? 21.057  78.906  19.296  1.00 63.27  ? 241 GLU B OE1  1 
ATOM   4697  O OE2  . GLU B 1 241 ? 23.095  78.105  19.404  1.00 56.50  ? 241 GLU B OE2  1 
ATOM   4698  N N    . LEU B 1 242 ? 23.323  81.949  20.720  1.00 44.83  ? 242 LEU B N    1 
ATOM   4699  C CA   . LEU B 1 242 ? 23.577  82.715  19.530  1.00 49.52  ? 242 LEU B CA   1 
ATOM   4700  C C    . LEU B 1 242 ? 23.300  81.911  18.307  1.00 50.84  ? 242 LEU B C    1 
ATOM   4701  O O    . LEU B 1 242 ? 23.475  80.706  18.296  1.00 51.74  ? 242 LEU B O    1 
ATOM   4702  C CB   . LEU B 1 242 ? 24.994  83.285  19.495  1.00 48.22  ? 242 LEU B CB   1 
ATOM   4703  C CG   . LEU B 1 242 ? 25.234  84.669  20.070  1.00 46.50  ? 242 LEU B CG   1 
ATOM   4704  C CD1  . LEU B 1 242 ? 25.380  84.556  21.567  1.00 45.30  ? 242 LEU B CD1  1 
ATOM   4705  C CD2  . LEU B 1 242 ? 26.496  85.257  19.476  1.00 44.75  ? 242 LEU B CD2  1 
ATOM   4706  N N    . PRO B 1 243 ? 22.928  82.583  17.237  1.00 47.76  ? 243 PRO B N    1 
ATOM   4707  C CA   . PRO B 1 243 ? 22.687  81.900  15.985  1.00 58.65  ? 243 PRO B CA   1 
ATOM   4708  C C    . PRO B 1 243 ? 23.956  81.253  15.461  1.00 62.10  ? 243 PRO B C    1 
ATOM   4709  O O    . PRO B 1 243 ? 23.897  80.457  14.529  1.00 58.15  ? 243 PRO B O    1 
ATOM   4710  C CB   . PRO B 1 243 ? 22.267  83.037  15.092  1.00 53.19  ? 243 PRO B CB   1 
ATOM   4711  C CG   . PRO B 1 243 ? 21.487  83.915  15.995  1.00 51.90  ? 243 PRO B CG   1 
ATOM   4712  C CD   . PRO B 1 243 ? 22.259  83.891  17.277  1.00 46.55  ? 243 PRO B CD   1 
ATOM   4713  N N    . ASP B 1 244 ? 25.094  81.612  16.026  1.00 61.42  ? 244 ASP B N    1 
ATOM   4714  C CA   . ASP B 1 244 ? 26.369  81.081  15.594  1.00 55.20  ? 244 ASP B CA   1 
ATOM   4715  C C    . ASP B 1 244 ? 26.905  79.969  16.475  1.00 53.73  ? 244 ASP B C    1 
ATOM   4716  O O    . ASP B 1 244 ? 28.100  79.745  16.523  1.00 57.96  ? 244 ASP B O    1 
ATOM   4717  C CB   . ASP B 1 244 ? 27.375  82.212  15.391  1.00 52.82  ? 244 ASP B CB   1 
ATOM   4718  C CG   . ASP B 1 244 ? 27.404  83.192  16.525  1.00 63.17  ? 244 ASP B CG   1 
ATOM   4719  O OD1  . ASP B 1 244 ? 27.794  82.802  17.641  1.00 61.69  ? 244 ASP B OD1  1 
ATOM   4720  O OD2  . ASP B 1 244 ? 27.079  84.368  16.283  1.00 64.40  ? 244 ASP B OD2  1 
ATOM   4721  N N    . GLY B 1 245 ? 26.035  79.294  17.208  1.00 48.32  ? 245 GLY B N    1 
ATOM   4722  C CA   . GLY B 1 245 ? 26.462  78.153  18.013  1.00 49.14  ? 245 GLY B CA   1 
ATOM   4723  C C    . GLY B 1 245 ? 27.009  78.415  19.400  1.00 61.94  ? 245 GLY B C    1 
ATOM   4724  O O    . GLY B 1 245 ? 27.448  77.485  20.058  1.00 66.81  ? 245 GLY B O    1 
ATOM   4725  N N    . GLN B 1 246 ? 26.953  79.657  19.863  1.00 62.38  ? 246 GLN B N    1 
ATOM   4726  C CA   . GLN B 1 246 ? 27.469  80.024  21.158  1.00 54.49  ? 246 GLN B CA   1 
ATOM   4727  C C    . GLN B 1 246 ? 26.346  80.388  22.100  1.00 57.21  ? 246 GLN B C    1 
ATOM   4728  O O    . GLN B 1 246 ? 25.491  81.164  21.760  1.00 51.24  ? 246 GLN B O    1 
ATOM   4729  C CB   . GLN B 1 246 ? 28.387  81.213  20.974  1.00 49.44  ? 246 GLN B CB   1 
ATOM   4730  C CG   . GLN B 1 246 ? 29.255  81.576  22.159  1.00 67.75  ? 246 GLN B CG   1 
ATOM   4731  C CD   . GLN B 1 246 ? 30.330  82.577  21.783  1.00 76.07  ? 246 GLN B CD   1 
ATOM   4732  O OE1  . GLN B 1 246 ? 30.651  82.739  20.608  1.00 66.88  ? 246 GLN B OE1  1 
ATOM   4733  N NE2  . GLN B 1 246 ? 30.897  83.247  22.779  1.00 68.74  ? 246 GLN B NE2  1 
ATOM   4734  N N    . VAL B 1 247 ? 26.341  79.825  23.301  1.00 61.82  ? 247 VAL B N    1 
ATOM   4735  C CA   . VAL B 1 247 ? 25.334  80.142  24.293  1.00 43.07  ? 247 VAL B CA   1 
ATOM   4736  C C    . VAL B 1 247 ? 26.005  81.080  25.264  1.00 43.30  ? 247 VAL B C    1 
ATOM   4737  O O    . VAL B 1 247 ? 27.172  80.876  25.594  1.00 35.06  ? 247 VAL B O    1 
ATOM   4738  C CB   . VAL B 1 247 ? 24.868  78.890  24.993  1.00 35.10  ? 247 VAL B CB   1 
ATOM   4739  C CG1  . VAL B 1 247 ? 23.670  79.190  25.873  1.00 49.46  ? 247 VAL B CG1  1 
ATOM   4740  C CG2  . VAL B 1 247 ? 24.518  77.827  23.973  1.00 47.80  ? 247 VAL B CG2  1 
ATOM   4741  N N    . ILE B 1 248 ? 25.316  82.141  25.684  1.00 42.42  ? 248 ILE B N    1 
ATOM   4742  C CA   . ILE B 1 248 ? 25.929  83.164  26.535  1.00 44.63  ? 248 ILE B CA   1 
ATOM   4743  C C    . ILE B 1 248 ? 25.149  83.473  27.783  1.00 42.86  ? 248 ILE B C    1 
ATOM   4744  O O    . ILE B 1 248 ? 24.105  82.888  28.018  1.00 38.50  ? 248 ILE B O    1 
ATOM   4745  C CB   . ILE B 1 248 ? 26.221  84.476  25.789  1.00 38.70  ? 248 ILE B CB   1 
ATOM   4746  C CG1  . ILE B 1 248 ? 24.948  85.116  25.259  1.00 34.29  ? 248 ILE B CG1  1 
ATOM   4747  C CG2  . ILE B 1 248 ? 27.205  84.245  24.660  1.00 51.60  ? 248 ILE B CG2  1 
ATOM   4748  C CD1  . ILE B 1 248 ? 25.175  86.498  24.699  1.00 30.53  ? 248 ILE B CD1  1 
ATOM   4749  N N    . THR B 1 249 ? 25.637  84.407  28.590  1.00 38.66  ? 249 THR B N    1 
ATOM   4750  C CA   . THR B 1 249 ? 24.966  84.759  29.831  1.00 40.88  ? 249 THR B CA   1 
ATOM   4751  C C    . THR B 1 249 ? 24.768  86.243  29.971  1.00 42.28  ? 249 THR B C    1 
ATOM   4752  O O    . THR B 1 249 ? 25.679  86.993  29.666  1.00 39.40  ? 249 THR B O    1 
ATOM   4753  C CB   . THR B 1 249 ? 25.765  84.304  31.053  1.00 47.53  ? 249 THR B CB   1 
ATOM   4754  O OG1  . THR B 1 249 ? 27.134  84.688  30.904  1.00 53.11  ? 249 THR B OG1  1 
ATOM   4755  C CG2  . THR B 1 249 ? 25.682  82.801  31.225  1.00 55.26  ? 249 THR B CG2  1 
ATOM   4756  N N    . ILE B 1 250 ? 23.596  86.682  30.445  1.00 35.50  ? 250 ILE B N    1 
ATOM   4757  C CA   . ILE B 1 250 ? 23.389  88.136  30.490  1.00 36.46  ? 250 ILE B CA   1 
ATOM   4758  C C    . ILE B 1 250 ? 23.347  88.889  31.845  1.00 33.32  ? 250 ILE B C    1 
ATOM   4759  O O    . ILE B 1 250 ? 24.223  89.699  32.108  1.00 31.74  ? 250 ILE B O    1 
ATOM   4760  C CB   . ILE B 1 250 ? 22.365  88.631  29.436  1.00 27.72  ? 250 ILE B CB   1 
ATOM   4761  C CG1  . ILE B 1 250 ? 22.350  90.152  29.384  1.00 20.19  ? 250 ILE B CG1  1 
ATOM   4762  C CG2  . ILE B 1 250 ? 21.012  87.976  29.646  1.00 31.73  ? 250 ILE B CG2  1 
ATOM   4763  C CD1  . ILE B 1 250 ? 22.155  90.691  27.997  1.00 21.68  ? 250 ILE B CD1  1 
ATOM   4764  N N    . GLY B 1 251 ? 22.436  88.607  32.744  1.00 21.21  ? 251 GLY B N    1 
ATOM   4765  C CA   . GLY B 1 251 ? 22.480  89.350  33.995  1.00 23.98  ? 251 GLY B CA   1 
ATOM   4766  C C    . GLY B 1 251 ? 22.307  90.844  34.106  1.00 20.18  ? 251 GLY B C    1 
ATOM   4767  O O    . GLY B 1 251 ? 21.311  91.376  33.693  1.00 19.97  ? 251 GLY B O    1 
ATOM   4768  N N    . ASN B 1 252 ? 23.265  91.533  34.683  1.00 18.52  ? 252 ASN B N    1 
ATOM   4769  C CA   . ASN B 1 252 ? 23.143  92.967  34.933  1.00 18.60  ? 252 ASN B CA   1 
ATOM   4770  C C    . ASN B 1 252 ? 22.957  93.804  33.708  1.00 22.53  ? 252 ASN B C    1 
ATOM   4771  O O    . ASN B 1 252 ? 22.360  94.858  33.774  1.00 22.33  ? 252 ASN B O    1 
ATOM   4772  C CB   . ASN B 1 252 ? 24.283  93.508  35.782  1.00 14.22  ? 252 ASN B CB   1 
ATOM   4773  C CG   . ASN B 1 252 ? 25.650  93.271  35.184  1.00 23.57  ? 252 ASN B CG   1 
ATOM   4774  O OD1  . ASN B 1 252 ? 26.288  94.201  34.708  1.00 25.39  ? 252 ASN B OD1  1 
ATOM   4775  N ND2  . ASN B 1 252 ? 26.131  92.035  35.246  1.00 24.98  ? 252 ASN B ND2  1 
ATOM   4776  N N    . GLU B 1 253 ? 23.464  93.363  32.586  1.00 22.02  ? 253 GLU B N    1 
ATOM   4777  C CA   . GLU B 1 253 ? 23.358  94.082  31.353  1.00 15.78  ? 253 GLU B CA   1 
ATOM   4778  C C    . GLU B 1 253 ? 21.968  94.068  30.839  1.00 14.33  ? 253 GLU B C    1 
ATOM   4779  O O    . GLU B 1 253 ? 21.628  94.823  29.961  1.00 13.23  ? 253 GLU B O    1 
ATOM   4780  C CB   . GLU B 1 253 ? 24.352  93.520  30.391  1.00 15.86  ? 253 GLU B CB   1 
ATOM   4781  C CG   . GLU B 1 253 ? 25.777  93.875  30.740  1.00 20.17  ? 253 GLU B CG   1 
ATOM   4782  C CD   . GLU B 1 253 ? 26.513  92.784  31.461  1.00 19.41  ? 253 GLU B CD   1 
ATOM   4783  O OE1  . GLU B 1 253 ? 26.083  91.631  31.379  1.00 21.41  ? 253 GLU B OE1  1 
ATOM   4784  O OE2  . GLU B 1 253 ? 27.528  93.084  32.109  1.00 18.88  ? 253 GLU B OE2  1 
ATOM   4785  N N    . ARG B 1 254 ? 21.152  93.176  31.346  1.00 15.05  ? 254 ARG B N    1 
ATOM   4786  C CA   . ARG B 1 254 ? 19.777  93.203  30.970  1.00 15.00  ? 254 ARG B CA   1 
ATOM   4787  C C    . ARG B 1 254 ? 19.056  94.431  31.454  1.00 16.87  ? 254 ARG B C    1 
ATOM   4788  O O    . ARG B 1 254 ? 18.448  95.112  30.668  1.00 20.85  ? 254 ARG B O    1 
ATOM   4789  C CB   . ARG B 1 254 ? 19.066  92.026  31.588  1.00 13.68  ? 254 ARG B CB   1 
ATOM   4790  C CG   . ARG B 1 254 ? 19.217  90.704  30.893  1.00 19.87  ? 254 ARG B CG   1 
ATOM   4791  C CD   . ARG B 1 254 ? 18.509  89.629  31.690  1.00 19.64  ? 254 ARG B CD   1 
ATOM   4792  N NE   . ARG B 1 254 ? 17.109  89.514  31.320  1.00 20.69  ? 254 ARG B NE   1 
ATOM   4793  C CZ   . ARG B 1 254 ? 16.178  88.984  32.099  1.00 19.46  ? 254 ARG B CZ   1 
ATOM   4794  N NH1  . ARG B 1 254 ? 16.500  88.547  33.305  1.00 23.49  ? 254 ARG B NH1  1 
ATOM   4795  N NH2  . ARG B 1 254 ? 14.926  88.912  31.683  1.00 18.99  ? 254 ARG B NH2  1 
ATOM   4796  N N    . PHE B 1 255 ? 19.181  94.787  32.720  1.00 17.19  ? 255 PHE B N    1 
ATOM   4797  C CA   . PHE B 1 255 ? 18.402  95.890  33.260  1.00 17.23  ? 255 PHE B CA   1 
ATOM   4798  C C    . PHE B 1 255 ? 19.135  97.184  33.215  1.00 15.77  ? 255 PHE B C    1 
ATOM   4799  O O    . PHE B 1 255 ? 18.595  98.242  33.507  1.00 13.92  ? 255 PHE B O    1 
ATOM   4800  C CB   . PHE B 1 255 ? 17.867  95.581  34.654  1.00 16.45  ? 255 PHE B CB   1 
ATOM   4801  C CG   . PHE B 1 255 ? 18.883  95.022  35.603  1.00 19.52  ? 255 PHE B CG   1 
ATOM   4802  C CD1  . PHE B 1 255 ? 19.757  95.851  36.265  1.00 16.79  ? 255 PHE B CD1  1 
ATOM   4803  C CD2  . PHE B 1 255 ? 18.925  93.672  35.866  1.00 20.30  ? 255 PHE B CD2  1 
ATOM   4804  C CE1  . PHE B 1 255 ? 20.679  95.345  37.143  1.00 15.57  ? 255 PHE B CE1  1 
ATOM   4805  C CE2  . PHE B 1 255 ? 19.842  93.158  36.746  1.00 22.13  ? 255 PHE B CE2  1 
ATOM   4806  C CZ   . PHE B 1 255 ? 20.722  93.997  37.385  1.00 21.19  ? 255 PHE B CZ   1 
ATOM   4807  N N    . ARG B 1 256 ? 20.369  97.106  32.804  1.00 14.40  ? 256 ARG B N    1 
ATOM   4808  C CA   . ARG B 1 256 ? 21.128  98.298  32.669  1.00 16.30  ? 256 ARG B CA   1 
ATOM   4809  C C    . ARG B 1 256 ? 20.741  98.888  31.364  1.00 17.25  ? 256 ARG B C    1 
ATOM   4810  O O    . ARG B 1 256 ? 20.893  100.069 31.183  1.00 22.37  ? 256 ARG B O    1 
ATOM   4811  C CB   . ARG B 1 256 ? 22.633  98.015  32.707  1.00 14.76  ? 256 ARG B CB   1 
ATOM   4812  C CG   . ARG B 1 256 ? 23.291  97.941  34.063  1.00 11.51  ? 256 ARG B CG   1 
ATOM   4813  C CD   . ARG B 1 256 ? 24.630  97.247  33.921  1.00 11.86  ? 256 ARG B CD   1 
ATOM   4814  N NE   . ARG B 1 256 ? 25.595  98.016  33.151  1.00 10.46  ? 256 ARG B NE   1 
ATOM   4815  C CZ   . ARG B 1 256 ? 26.768  97.543  32.746  1.00 10.72  ? 256 ARG B CZ   1 
ATOM   4816  N NH1  . ARG B 1 256 ? 27.111  96.305  33.024  1.00 12.04  ? 256 ARG B NH1  1 
ATOM   4817  N NH2  . ARG B 1 256 ? 27.595  98.308  32.064  1.00 10.87  ? 256 ARG B NH2  1 
ATOM   4818  N N    . CYS B 1 257 ? 20.239  98.086  30.438  1.00 20.10  ? 257 CYS B N    1 
ATOM   4819  C CA   . CYS B 1 257 ? 19.932  98.616  29.085  1.00 19.65  ? 257 CYS B CA   1 
ATOM   4820  C C    . CYS B 1 257 ? 18.699  99.475  28.982  1.00 16.65  ? 257 CYS B C    1 
ATOM   4821  O O    . CYS B 1 257 ? 18.767  100.559 28.464  1.00 13.47  ? 257 CYS B O    1 
ATOM   4822  C CB   . CYS B 1 257 ? 20.091  97.550  28.008  1.00 16.24  ? 257 CYS B CB   1 
ATOM   4823  S SG   . CYS B 1 257 ? 19.866  98.066  26.322  1.00 40.03  ? 257 CYS B SG   1 
ATOM   4824  N N    . PRO B 1 258 ? 17.529  99.004  29.508  1.00 12.58  ? 258 PRO B N    1 
ATOM   4825  C CA   . PRO B 1 258 ? 16.439  99.966  29.513  1.00 10.04  ? 258 PRO B CA   1 
ATOM   4826  C C    . PRO B 1 258 ? 16.460  101.002 30.614  1.00 14.23  ? 258 PRO B C    1 
ATOM   4827  O O    . PRO B 1 258 ? 15.412  101.471 30.999  1.00 16.97  ? 258 PRO B O    1 
ATOM   4828  C CB   . PRO B 1 258 ? 15.294  99.035  29.699  1.00 6.70   ? 258 PRO B CB   1 
ATOM   4829  C CG   . PRO B 1 258 ? 15.831  97.926  30.428  1.00 10.10  ? 258 PRO B CG   1 
ATOM   4830  C CD   . PRO B 1 258 ? 17.081  97.692  29.732  1.00 12.89  ? 258 PRO B CD   1 
ATOM   4831  N N    . GLU B 1 259 ? 17.633  101.410 31.086  1.00 11.96  ? 259 GLU B N    1 
ATOM   4832  C CA   . GLU B 1 259 ? 17.761  102.395 32.169  1.00 11.08  ? 259 GLU B CA   1 
ATOM   4833  C C    . GLU B 1 259 ? 18.219  103.623 31.559  1.00 10.36  ? 259 GLU B C    1 
ATOM   4834  O O    . GLU B 1 259 ? 18.209  104.650 32.163  1.00 9.12   ? 259 GLU B O    1 
ATOM   4835  C CB   . GLU B 1 259 ? 18.776  101.967 33.221  1.00 9.75   ? 259 GLU B CB   1 
ATOM   4836  C CG   . GLU B 1 259 ? 18.896  102.830 34.456  1.00 10.64  ? 259 GLU B CG   1 
ATOM   4837  C CD   . GLU B 1 259 ? 17.911  102.477 35.527  1.00 10.20  ? 259 GLU B CD   1 
ATOM   4838  O OE1  . GLU B 1 259 ? 17.365  101.366 35.496  1.00 12.48  ? 259 GLU B OE1  1 
ATOM   4839  O OE2  . GLU B 1 259 ? 17.682  103.321 36.398  1.00 6.96   ? 259 GLU B OE2  1 
ATOM   4840  N N    . ALA B 1 260 ? 18.627  103.528 30.325  1.00 10.82  ? 260 ALA B N    1 
ATOM   4841  C CA   . ALA B 1 260 ? 19.069  104.676 29.600  1.00 9.92   ? 260 ALA B CA   1 
ATOM   4842  C C    . ALA B 1 260 ? 17.877  105.557 29.407  1.00 11.09  ? 260 ALA B C    1 
ATOM   4843  O O    . ALA B 1 260 ? 18.010  106.740 29.209  1.00 10.56  ? 260 ALA B O    1 
ATOM   4844  C CB   . ALA B 1 260 ? 19.719  104.261 28.313  1.00 5.75   ? 260 ALA B CB   1 
ATOM   4845  N N    . LEU B 1 261 ? 16.703  104.975 29.361  1.00 11.25  ? 261 LEU B N    1 
ATOM   4846  C CA   . LEU B 1 261 ? 15.498  105.745 29.268  1.00 8.54   ? 261 LEU B CA   1 
ATOM   4847  C C    . LEU B 1 261 ? 15.190  106.528 30.486  1.00 7.60   ? 261 LEU B C    1 
ATOM   4848  O O    . LEU B 1 261 ? 14.817  107.658 30.388  1.00 6.93   ? 261 LEU B O    1 
ATOM   4849  C CB   . LEU B 1 261 ? 14.374  104.769 28.984  1.00 7.89   ? 261 LEU B CB   1 
ATOM   4850  C CG   . LEU B 1 261 ? 14.446  103.931 27.724  1.00 6.80   ? 261 LEU B CG   1 
ATOM   4851  C CD1  . LEU B 1 261 ? 13.353  102.884 27.795  1.00 4.87   ? 261 LEU B CD1  1 
ATOM   4852  C CD2  . LEU B 1 261 ? 14.278  104.829 26.512  1.00 5.19   ? 261 LEU B CD2  1 
ATOM   4853  N N    . PHE B 1 262 ? 15.272  105.908 31.645  1.00 11.14  ? 262 PHE B N    1 
ATOM   4854  C CA   . PHE B 1 262 ? 15.084  106.608 32.908  1.00 9.20   ? 262 PHE B CA   1 
ATOM   4855  C C    . PHE B 1 262 ? 16.274  107.412 33.326  1.00 9.88   ? 262 PHE B C    1 
ATOM   4856  O O    . PHE B 1 262 ? 16.142  108.539 33.765  1.00 9.28   ? 262 PHE B O    1 
ATOM   4857  C CB   . PHE B 1 262 ? 14.622  105.652 33.992  1.00 5.78   ? 262 PHE B CB   1 
ATOM   4858  C CG   . PHE B 1 262 ? 13.224  105.201 33.810  1.00 5.48   ? 262 PHE B CG   1 
ATOM   4859  C CD1  . PHE B 1 262 ? 12.188  105.987 34.233  1.00 7.48   ? 262 PHE B CD1  1 
ATOM   4860  C CD2  . PHE B 1 262 ? 12.953  104.013 33.177  1.00 6.95   ? 262 PHE B CD2  1 
ATOM   4861  C CE1  . PHE B 1 262 ? 10.896  105.589 34.048  1.00 5.29   ? 262 PHE B CE1  1 
ATOM   4862  C CE2  . PHE B 1 262 ? 11.660  103.608 32.987  1.00 5.66   ? 262 PHE B CE2  1 
ATOM   4863  C CZ   . PHE B 1 262 ? 10.631  104.398 33.421  1.00 6.00   ? 262 PHE B CZ   1 
ATOM   4864  N N    . GLN B 1 263 ? 17.453  106.840 33.191  1.00 8.73   ? 263 GLN B N    1 
ATOM   4865  C CA   . GLN B 1 263 ? 18.639  107.579 33.476  1.00 8.98   ? 263 GLN B CA   1 
ATOM   4866  C C    . GLN B 1 263 ? 19.482  107.610 32.241  1.00 11.39  ? 263 GLN B C    1 
ATOM   4867  O O    . GLN B 1 263 ? 20.229  106.691 32.011  1.00 11.68  ? 263 GLN B O    1 
ATOM   4868  C CB   . GLN B 1 263 ? 19.381  106.883 34.587  1.00 9.31   ? 263 GLN B CB   1 
ATOM   4869  C CG   . GLN B 1 263 ? 18.685  106.899 35.927  1.00 9.67   ? 263 GLN B CG   1 
ATOM   4870  C CD   . GLN B 1 263 ? 19.491  106.209 36.993  1.00 9.63   ? 263 GLN B CD   1 
ATOM   4871  O OE1  . GLN B 1 263 ? 20.525  105.613 36.713  1.00 5.52   ? 263 GLN B OE1  1 
ATOM   4872  N NE2  . GLN B 1 263 ? 19.026  106.292 38.231  1.00 9.36   ? 263 GLN B NE2  1 
ATOM   4873  N N    . PRO B 1 264 ? 19.454  108.707 31.485  1.00 10.32  ? 264 PRO B N    1 
ATOM   4874  C CA   . PRO B 1 264 ? 20.167  108.831 30.216  1.00 10.16  ? 264 PRO B CA   1 
ATOM   4875  C C    . PRO B 1 264 ? 21.680  108.979 30.313  1.00 14.17  ? 264 PRO B C    1 
ATOM   4876  O O    . PRO B 1 264 ? 22.355  108.901 29.307  1.00 12.97  ? 264 PRO B O    1 
ATOM   4877  C CB   . PRO B 1 264 ? 19.540  110.072 29.642  1.00 10.13  ? 264 PRO B CB   1 
ATOM   4878  C CG   . PRO B 1 264 ? 18.209  110.153 30.251  1.00 8.59   ? 264 PRO B CG   1 
ATOM   4879  C CD   . PRO B 1 264 ? 18.505  109.804 31.661  1.00 10.06  ? 264 PRO B CD   1 
ATOM   4880  N N    . SER B 1 265 ? 22.214  109.155 31.503  1.00 17.42  ? 265 SER B N    1 
ATOM   4881  C CA   . SER B 1 265 ? 23.625  109.390 31.736  1.00 15.53  ? 265 SER B CA   1 
ATOM   4882  C C    . SER B 1 265 ? 24.468  108.226 31.384  1.00 16.12  ? 265 SER B C    1 
ATOM   4883  O O    . SER B 1 265 ? 25.683  108.309 31.404  1.00 14.84  ? 265 SER B O    1 
ATOM   4884  C CB   . SER B 1 265 ? 23.749  109.733 33.192  1.00 14.58  ? 265 SER B CB   1 
ATOM   4885  O OG   . SER B 1 265 ? 23.085  110.947 33.485  1.00 25.99  ? 265 SER B OG   1 
ATOM   4886  N N    . PHE B 1 266 ? 23.836  107.097 31.171  1.00 17.49  ? 266 PHE B N    1 
ATOM   4887  C CA   . PHE B 1 266 ? 24.509  105.874 30.775  1.00 19.28  ? 266 PHE B CA   1 
ATOM   4888  C C    . PHE B 1 266 ? 25.202  105.970 29.432  1.00 21.69  ? 266 PHE B C    1 
ATOM   4889  O O    . PHE B 1 266 ? 26.243  105.364 29.228  1.00 19.47  ? 266 PHE B O    1 
ATOM   4890  C CB   . PHE B 1 266 ? 23.426  104.818 30.731  1.00 22.81  ? 266 PHE B CB   1 
ATOM   4891  C CG   . PHE B 1 266 ? 23.046  104.267 32.073  1.00 20.03  ? 266 PHE B CG   1 
ATOM   4892  C CD1  . PHE B 1 266 ? 22.746  105.097 33.127  1.00 12.44  ? 266 PHE B CD1  1 
ATOM   4893  C CD2  . PHE B 1 266 ? 22.963  102.903 32.264  1.00 20.99  ? 266 PHE B CD2  1 
ATOM   4894  C CE1  . PHE B 1 266 ? 22.397  104.579 34.350  1.00 19.04  ? 266 PHE B CE1  1 
ATOM   4895  C CE2  . PHE B 1 266 ? 22.614  102.376 33.483  1.00 14.21  ? 266 PHE B CE2  1 
ATOM   4896  C CZ   . PHE B 1 266 ? 22.332  103.217 34.528  1.00 18.18  ? 266 PHE B CZ   1 
ATOM   4897  N N    . LEU B 1 267 ? 24.604  106.701 28.496  1.00 24.39  ? 267 LEU B N    1 
ATOM   4898  C CA   . LEU B 1 267 ? 25.150  106.902 27.169  1.00 20.04  ? 267 LEU B CA   1 
ATOM   4899  C C    . LEU B 1 267 ? 26.021  108.143 27.057  1.00 17.55  ? 267 LEU B C    1 
ATOM   4900  O O    . LEU B 1 267 ? 26.465  108.480 25.985  1.00 29.23  ? 267 LEU B O    1 
ATOM   4901  C CB   . LEU B 1 267 ? 23.986  107.000 26.198  1.00 14.83  ? 267 LEU B CB   1 
ATOM   4902  C CG   . LEU B 1 267 ? 23.062  105.808 26.136  1.00 15.72  ? 267 LEU B CG   1 
ATOM   4903  C CD1  . LEU B 1 267 ? 21.786  106.247 25.456  1.00 18.70  ? 267 LEU B CD1  1 
ATOM   4904  C CD2  . LEU B 1 267 ? 23.752  104.714 25.347  1.00 21.17  ? 267 LEU B CD2  1 
ATOM   4905  N N    . GLY B 1 268 ? 26.270  108.824 28.147  1.00 14.25  ? 268 GLY B N    1 
ATOM   4906  C CA   . GLY B 1 268 ? 27.092  110.012 28.150  1.00 12.56  ? 268 GLY B CA   1 
ATOM   4907  C C    . GLY B 1 268 ? 26.286  111.248 27.996  1.00 16.82  ? 268 GLY B C    1 
ATOM   4908  O O    . GLY B 1 268 ? 26.837  112.327 28.020  1.00 16.44  ? 268 GLY B O    1 
ATOM   4909  N N    . MET B 1 269 ? 24.984  111.095 27.824  1.00 17.12  ? 269 MET B N    1 
ATOM   4910  C CA   . MET B 1 269 ? 24.091  112.227 27.647  1.00 13.45  ? 269 MET B CA   1 
ATOM   4911  C C    . MET B 1 269 ? 23.766  112.990 28.897  1.00 18.01  ? 269 MET B C    1 
ATOM   4912  O O    . MET B 1 269 ? 23.742  112.449 29.979  1.00 17.08  ? 269 MET B O    1 
ATOM   4913  C CB   . MET B 1 269 ? 22.787  111.814 26.978  1.00 9.03   ? 269 MET B CB   1 
ATOM   4914  C CG   . MET B 1 269 ? 22.890  111.221 25.604  1.00 17.63  ? 269 MET B CG   1 
ATOM   4915  S SD   . MET B 1 269 ? 21.193  111.073 25.075  1.00 16.25  ? 269 MET B SD   1 
ATOM   4916  C CE   . MET B 1 269 ? 20.744  112.794 25.044  1.00 9.85   ? 269 MET B CE   1 
ATOM   4917  N N    . GLU B 1 270 ? 23.484  114.268 28.741  1.00 18.76  ? 270 GLU B N    1 
ATOM   4918  C CA   . GLU B 1 270 ? 23.140  115.080 29.863  1.00 20.35  ? 270 GLU B CA   1 
ATOM   4919  C C    . GLU B 1 270 ? 21.737  115.515 29.695  1.00 19.57  ? 270 GLU B C    1 
ATOM   4920  O O    . GLU B 1 270 ? 21.419  116.668 29.920  1.00 23.04  ? 270 GLU B O    1 
ATOM   4921  C CB   . GLU B 1 270 ? 24.046  116.267 29.933  1.00 23.51  ? 270 GLU B CB   1 
ATOM   4922  C CG   . GLU B 1 270 ? 25.487  115.888 30.226  1.00 30.16  ? 270 GLU B CG   1 
ATOM   4923  C CD   . GLU B 1 270 ? 26.335  117.061 30.659  1.00 37.29  ? 270 GLU B CD   1 
ATOM   4924  O OE1  . GLU B 1 270 ? 25.798  118.178 30.779  1.00 50.92  ? 270 GLU B OE1  1 
ATOM   4925  O OE2  . GLU B 1 270 ? 27.541  116.861 30.880  1.00 28.85  ? 270 GLU B OE2  1 
ATOM   4926  N N    . SER B 1 271 ? 20.884  114.588 29.308  1.00 13.01  ? 271 SER B N    1 
ATOM   4927  C CA   . SER B 1 271 ? 19.503  114.878 29.162  1.00 11.03  ? 271 SER B CA   1 
ATOM   4928  C C    . SER B 1 271 ? 18.773  114.319 30.301  1.00 10.85  ? 271 SER B C    1 
ATOM   4929  O O    . SER B 1 271 ? 19.365  113.914 31.282  1.00 18.29  ? 271 SER B O    1 
ATOM   4930  C CB   . SER B 1 271 ? 18.965  114.299 27.900  1.00 14.47  ? 271 SER B CB   1 
ATOM   4931  O OG   . SER B 1 271 ? 18.710  112.919 28.026  1.00 22.10  ? 271 SER B OG   1 
ATOM   4932  N N    . CYS B 1 272 ? 17.465  114.268 30.195  1.00 7.53   ? 272 CYS B N    1 
ATOM   4933  C CA   . CYS B 1 272 ? 16.671  113.849 31.272  1.00 7.04   ? 272 CYS B CA   1 
ATOM   4934  C C    . CYS B 1 272 ? 15.793  112.744 30.839  1.00 9.18   ? 272 CYS B C    1 
ATOM   4935  O O    . CYS B 1 272 ? 15.264  112.794 29.767  1.00 11.39  ? 272 CYS B O    1 
ATOM   4936  C CB   . CYS B 1 272 ? 15.837  115.026 31.634  1.00 10.10  ? 272 CYS B CB   1 
ATOM   4937  S SG   . CYS B 1 272 ? 16.666  116.630 31.734  1.00 30.73  ? 272 CYS B SG   1 
ATOM   4938  N N    . GLY B 1 273 ? 15.586  111.754 31.688  1.00 10.37  ? 273 GLY B N    1 
ATOM   4939  C CA   . GLY B 1 273 ? 14.836  110.580 31.332  1.00 6.97   ? 273 GLY B CA   1 
ATOM   4940  C C    . GLY B 1 273 ? 13.398  110.712 31.241  1.00 6.82   ? 273 GLY B C    1 
ATOM   4941  O O    . GLY B 1 273 ? 12.892  111.675 31.672  1.00 11.36  ? 273 GLY B O    1 
ATOM   4942  N N    . ILE B 1 274 ? 12.718  109.712 30.730  1.00 6.54   ? 274 ILE B N    1 
ATOM   4943  C CA   . ILE B 1 274 ? 11.297  109.783 30.477  1.00 6.02   ? 274 ILE B CA   1 
ATOM   4944  C C    . ILE B 1 274 ? 10.391  110.208 31.576  1.00 7.71   ? 274 ILE B C    1 
ATOM   4945  O O    . ILE B 1 274 ? 9.319   110.657 31.300  1.00 8.06   ? 274 ILE B O    1 
ATOM   4946  C CB   . ILE B 1 274 ? 10.790  108.494 29.842  1.00 4.11   ? 274 ILE B CB   1 
ATOM   4947  C CG1  . ILE B 1 274 ? 11.094  107.291 30.702  1.00 6.43   ? 274 ILE B CG1  1 
ATOM   4948  C CG2  . ILE B 1 274 ? 11.442  108.297 28.493  1.00 7.44   ? 274 ILE B CG2  1 
ATOM   4949  C CD1  . ILE B 1 274 ? 11.039  106.008 29.920  1.00 7.39   ? 274 ILE B CD1  1 
ATOM   4950  N N    . HIS B 1 275 ? 10.818  110.115 32.815  1.00 7.09   ? 275 HIS B N    1 
ATOM   4951  C CA   . HIS B 1 275 ? 9.972   110.443 33.920  1.00 6.62   ? 275 HIS B CA   1 
ATOM   4952  C C    . HIS B 1 275 ? 10.085  111.882 34.153  1.00 8.30   ? 275 HIS B C    1 
ATOM   4953  O O    . HIS B 1 275 ? 9.122   112.516 34.496  1.00 7.59   ? 275 HIS B O    1 
ATOM   4954  C CB   . HIS B 1 275 ? 10.377  109.630 35.113  1.00 7.05   ? 275 HIS B CB   1 
ATOM   4955  C CG   . HIS B 1 275 ? 11.766  109.852 35.610  1.00 6.92   ? 275 HIS B CG   1 
ATOM   4956  N ND1  . HIS B 1 275 ? 12.875  109.340 34.982  1.00 7.98   ? 275 HIS B ND1  1 
ATOM   4957  C CD2  . HIS B 1 275 ? 12.215  110.457 36.731  1.00 6.87   ? 275 HIS B CD2  1 
ATOM   4958  C CE1  . HIS B 1 275 ? 13.952  109.666 35.668  1.00 8.98   ? 275 HIS B CE1  1 
ATOM   4959  N NE2  . HIS B 1 275 ? 13.579  110.344 36.734  1.00 7.83   ? 275 HIS B NE2  1 
ATOM   4960  N N    . GLU B 1 276 ? 11.272  112.424 33.931  1.00 8.51   ? 276 GLU B N    1 
ATOM   4961  C CA   . GLU B 1 276 ? 11.530  113.819 34.088  1.00 9.40   ? 276 GLU B CA   1 
ATOM   4962  C C    . GLU B 1 276 ? 10.896  114.469 32.913  1.00 12.61  ? 276 GLU B C    1 
ATOM   4963  O O    . GLU B 1 276 ? 10.118  115.376 33.070  1.00 10.76  ? 276 GLU B O    1 
ATOM   4964  C CB   . GLU B 1 276 ? 13.021  114.015 34.046  1.00 7.09   ? 276 GLU B CB   1 
ATOM   4965  C CG   . GLU B 1 276 ? 13.754  113.636 35.321  1.00 11.93  ? 276 GLU B CG   1 
ATOM   4966  C CD   . GLU B 1 276 ? 15.267  113.544 35.167  1.00 12.76  ? 276 GLU B CD   1 
ATOM   4967  O OE1  . GLU B 1 276 ? 15.946  114.575 35.283  1.00 13.32  ? 276 GLU B OE1  1 
ATOM   4968  O OE2  . GLU B 1 276 ? 15.795  112.441 34.954  1.00 8.55   ? 276 GLU B OE2  1 
ATOM   4969  N N    . THR B 1 277 ? 11.178  113.987 31.718  1.00 13.23  ? 277 THR B N    1 
ATOM   4970  C CA   . THR B 1 277 ? 10.621  114.493 30.489  1.00 8.83   ? 277 THR B CA   1 
ATOM   4971  C C    . THR B 1 277 ? 9.128   114.492 30.482  1.00 10.52  ? 277 THR B C    1 
ATOM   4972  O O    . THR B 1 277 ? 8.536   115.395 29.961  1.00 14.06  ? 277 THR B O    1 
ATOM   4973  C CB   . THR B 1 277 ? 11.154  113.624 29.370  1.00 8.76   ? 277 THR B CB   1 
ATOM   4974  O OG1  . THR B 1 277 ? 12.569  113.521 29.493  1.00 9.26   ? 277 THR B OG1  1 
ATOM   4975  C CG2  . THR B 1 277 ? 10.858  114.193 28.020  1.00 12.32  ? 277 THR B CG2  1 
ATOM   4976  N N    . THR B 1 278 ? 8.474   113.515 31.081  1.00 10.02  ? 278 THR B N    1 
ATOM   4977  C CA   . THR B 1 278 ? 7.007   113.538 31.189  1.00 11.04  ? 278 THR B CA   1 
ATOM   4978  C C    . THR B 1 278 ? 6.506   114.619 32.123  1.00 12.31  ? 278 THR B C    1 
ATOM   4979  O O    . THR B 1 278 ? 5.605   115.317 31.770  1.00 11.89  ? 278 THR B O    1 
ATOM   4980  C CB   . THR B 1 278 ? 6.435   112.152 31.531  1.00 11.95  ? 278 THR B CB   1 
ATOM   4981  O OG1  . THR B 1 278 ? 6.828   111.216 30.525  1.00 7.83   ? 278 THR B OG1  1 
ATOM   4982  C CG2  . THR B 1 278 ? 4.938   112.159 31.594  1.00 13.19  ? 278 THR B CG2  1 
ATOM   4983  N N    . PHE B 1 279 ? 7.134   114.825 33.275  1.00 11.63  ? 279 PHE B N    1 
ATOM   4984  C CA   . PHE B 1 279 ? 6.766   115.864 34.258  1.00 11.69  ? 279 PHE B CA   1 
ATOM   4985  C C    . PHE B 1 279 ? 6.929   117.217 33.725  1.00 12.21  ? 279 PHE B C    1 
ATOM   4986  O O    . PHE B 1 279 ? 6.136   118.084 33.963  1.00 13.31  ? 279 PHE B O    1 
ATOM   4987  C CB   . PHE B 1 279 ? 7.775   115.799 35.385  1.00 13.18  ? 279 PHE B CB   1 
ATOM   4988  C CG   . PHE B 1 279 ? 7.502   116.711 36.540  1.00 14.05  ? 279 PHE B CG   1 
ATOM   4989  C CD1  . PHE B 1 279 ? 6.309   116.657 37.224  1.00 12.38  ? 279 PHE B CD1  1 
ATOM   4990  C CD2  . PHE B 1 279 ? 8.472   117.584 36.969  1.00 10.68  ? 279 PHE B CD2  1 
ATOM   4991  C CE1  . PHE B 1 279 ? 6.076   117.490 38.290  1.00 12.61  ? 279 PHE B CE1  1 
ATOM   4992  C CE2  . PHE B 1 279 ? 8.243   118.420 38.032  1.00 8.97   ? 279 PHE B CE2  1 
ATOM   4993  C CZ   . PHE B 1 279 ? 7.045   118.372 38.695  1.00 8.36   ? 279 PHE B CZ   1 
ATOM   4994  N N    . ASN B 1 280 ? 8.009   117.423 33.018  1.00 9.74   ? 280 ASN B N    1 
ATOM   4995  C CA   . ASN B 1 280 ? 8.269   118.701 32.450  1.00 8.98   ? 280 ASN B CA   1 
ATOM   4996  C C    . ASN B 1 280 ? 7.310   119.036 31.368  1.00 9.94   ? 280 ASN B C    1 
ATOM   4997  O O    . ASN B 1 280 ? 7.064   120.169 31.157  1.00 11.36  ? 280 ASN B O    1 
ATOM   4998  C CB   . ASN B 1 280 ? 9.687   118.701 31.961  1.00 8.50   ? 280 ASN B CB   1 
ATOM   4999  C CG   . ASN B 1 280 ? 10.693  118.665 33.089  1.00 12.15  ? 280 ASN B CG   1 
ATOM   5000  O OD1  . ASN B 1 280 ? 11.661  117.916 33.041  1.00 9.27   ? 280 ASN B OD1  1 
ATOM   5001  N ND2  . ASN B 1 280 ? 10.477  119.490 34.101  1.00 14.80  ? 280 ASN B ND2  1 
ATOM   5002  N N    . SER B 1 281 ? 6.700   118.067 30.722  1.00 10.90  ? 281 SER B N    1 
ATOM   5003  C CA   . SER B 1 281 ? 5.761   118.285 29.622  1.00 8.91   ? 281 SER B CA   1 
ATOM   5004  C C    . SER B 1 281 ? 4.385   118.456 30.103  1.00 9.50   ? 281 SER B C    1 
ATOM   5005  O O    . SER B 1 281 ? 3.528   118.896 29.387  1.00 8.47   ? 281 SER B O    1 
ATOM   5006  C CB   . SER B 1 281 ? 5.773   117.085 28.721  1.00 7.95   ? 281 SER B CB   1 
ATOM   5007  O OG   . SER B 1 281 ? 4.814   117.187 27.710  1.00 10.30  ? 281 SER B OG   1 
ATOM   5008  N N    . ILE B 1 282 ? 4.142   118.061 31.329  1.00 11.04  ? 282 ILE B N    1 
ATOM   5009  C CA   . ILE B 1 282 ? 2.824   118.140 31.921  1.00 13.02  ? 282 ILE B CA   1 
ATOM   5010  C C    . ILE B 1 282 ? 2.722   119.471 32.575  1.00 10.92  ? 282 ILE B C    1 
ATOM   5011  O O    . ILE B 1 282 ? 1.688   120.075 32.647  1.00 11.59  ? 282 ILE B O    1 
ATOM   5012  C CB   . ILE B 1 282 ? 2.629   116.974 32.923  1.00 11.73  ? 282 ILE B CB   1 
ATOM   5013  C CG1  . ILE B 1 282 ? 2.415   115.660 32.201  1.00 12.07  ? 282 ILE B CG1  1 
ATOM   5014  C CG2  . ILE B 1 282 ? 1.427   117.167 33.804  1.00 15.22  ? 282 ILE B CG2  1 
ATOM   5015  C CD1  . ILE B 1 282 ? 2.239   114.488 33.127  1.00 9.74   ? 282 ILE B CD1  1 
ATOM   5016  N N    . MET B 1 283 ? 3.843   119.983 32.974  1.00 11.12  ? 283 MET B N    1 
ATOM   5017  C CA   . MET B 1 283 ? 3.876   121.251 33.630  1.00 14.34  ? 283 MET B CA   1 
ATOM   5018  C C    . MET B 1 283 ? 4.119   122.376 32.691  1.00 13.21  ? 283 MET B C    1 
ATOM   5019  O O    . MET B 1 283 ? 4.274   123.491 33.120  1.00 14.34  ? 283 MET B O    1 
ATOM   5020  C CB   . MET B 1 283 ? 4.953   121.231 34.703  1.00 15.67  ? 283 MET B CB   1 
ATOM   5021  C CG   . MET B 1 283 ? 4.637   120.324 35.872  1.00 15.95  ? 283 MET B CG   1 
ATOM   5022  S SD   . MET B 1 283 ? 3.999   121.227 37.279  1.00 27.46  ? 283 MET B SD   1 
ATOM   5023  C CE   . MET B 1 283 ? 3.079   119.946 38.115  1.00 20.44  ? 283 MET B CE   1 
ATOM   5024  N N    . LYS B 1 284 ? 4.166   122.102 31.404  1.00 9.81   ? 284 LYS B N    1 
ATOM   5025  C CA   . LYS B 1 284 ? 4.361   123.116 30.410  1.00 8.15   ? 284 LYS B CA   1 
ATOM   5026  C C    . LYS B 1 284 ? 3.009   123.244 29.929  1.00 8.51   ? 284 LYS B C    1 
ATOM   5027  O O    . LYS B 1 284 ? 2.798   123.647 28.823  1.00 12.05  ? 284 LYS B O    1 
ATOM   5028  C CB   . LYS B 1 284 ? 5.271   122.639 29.331  1.00 6.57   ? 284 LYS B CB   1 
ATOM   5029  C CG   . LYS B 1 284 ? 6.569   123.400 29.253  1.00 6.97   ? 284 LYS B CG   1 
ATOM   5030  C CD   . LYS B 1 284 ? 7.705   122.506 28.813  1.00 9.01   ? 284 LYS B CD   1 
ATOM   5031  C CE   . LYS B 1 284 ? 9.048   123.126 29.158  1.00 21.65  ? 284 LYS B CE   1 
ATOM   5032  N NZ   . LYS B 1 284 ? 10.000  122.172 29.798  1.00 28.65  ? 284 LYS B NZ   1 
ATOM   5033  N N    . CYS B 1 285 ? 2.054   122.931 30.793  1.00 10.31  ? 285 CYS B N    1 
ATOM   5034  C CA   . CYS B 1 285 ? 0.648   122.974 30.438  1.00 13.04  ? 285 CYS B CA   1 
ATOM   5035  C C    . CYS B 1 285 ? -0.025  123.665 31.594  1.00 17.32  ? 285 CYS B C    1 
ATOM   5036  O O    . CYS B 1 285 ? 0.625   124.044 32.543  1.00 19.75  ? 285 CYS B O    1 
ATOM   5037  C CB   . CYS B 1 285 ? 0.106   121.574 30.154  1.00 10.42  ? 285 CYS B CB   1 
ATOM   5038  S SG   . CYS B 1 285 ? 0.703   120.653 28.738  1.00 11.48  ? 285 CYS B SG   1 
ATOM   5039  N N    . ASP B 1 286 ? -1.327  123.855 31.509  1.00 18.07  ? 286 ASP B N    1 
ATOM   5040  C CA   . ASP B 1 286 ? -2.010  124.560 32.564  1.00 21.57  ? 286 ASP B CA   1 
ATOM   5041  C C    . ASP B 1 286 ? -2.556  123.657 33.558  1.00 22.63  ? 286 ASP B C    1 
ATOM   5042  O O    . ASP B 1 286 ? -2.854  122.547 33.255  1.00 22.69  ? 286 ASP B O    1 
ATOM   5043  C CB   . ASP B 1 286 ? -3.031  125.514 32.029  1.00 18.08  ? 286 ASP B CB   1 
ATOM   5044  C CG   . ASP B 1 286 ? -3.692  126.293 33.118  1.00 32.27  ? 286 ASP B CG   1 
ATOM   5045  O OD1  . ASP B 1 286 ? -3.320  126.084 34.284  1.00 46.36  ? 286 ASP B OD1  1 
ATOM   5046  O OD2  . ASP B 1 286 ? -4.566  127.122 32.820  1.00 40.19  ? 286 ASP B OD2  1 
ATOM   5047  N N    . VAL B 1 287 ? -2.702  124.122 34.782  1.00 23.91  ? 287 VAL B N    1 
ATOM   5048  C CA   . VAL B 1 287 ? -3.049  123.266 35.864  1.00 17.66  ? 287 VAL B CA   1 
ATOM   5049  C C    . VAL B 1 287 ? -4.360  122.645 35.759  1.00 16.32  ? 287 VAL B C    1 
ATOM   5050  O O    . VAL B 1 287 ? -4.681  121.720 36.478  1.00 18.73  ? 287 VAL B O    1 
ATOM   5051  C CB   . VAL B 1 287 ? -2.986  124.199 37.051  1.00 19.12  ? 287 VAL B CB   1 
ATOM   5052  C CG1  . VAL B 1 287 ? -1.573  124.704 37.256  1.00 16.24  ? 287 VAL B CG1  1 
ATOM   5053  C CG2  . VAL B 1 287 ? -3.943  125.358 36.871  1.00 21.14  ? 287 VAL B CG2  1 
ATOM   5054  N N    . ASP B 1 288 ? -5.133  123.113 34.817  1.00 16.12  ? 288 ASP B N    1 
ATOM   5055  C CA   . ASP B 1 288 ? -6.476  122.621 34.674  1.00 17.41  ? 288 ASP B CA   1 
ATOM   5056  C C    . ASP B 1 288 ? -6.538  121.330 33.902  1.00 18.17  ? 288 ASP B C    1 
ATOM   5057  O O    . ASP B 1 288 ? -7.487  120.583 34.037  1.00 16.53  ? 288 ASP B O    1 
ATOM   5058  C CB   . ASP B 1 288 ? -7.291  123.711 34.017  1.00 15.63  ? 288 ASP B CB   1 
ATOM   5059  C CG   . ASP B 1 288 ? -6.830  125.093 34.391  1.00 21.55  ? 288 ASP B CG   1 
ATOM   5060  O OD1  . ASP B 1 288 ? -6.649  125.363 35.589  1.00 23.50  ? 288 ASP B OD1  1 
ATOM   5061  O OD2  . ASP B 1 288 ? -6.668  125.925 33.482  1.00 27.55  ? 288 ASP B OD2  1 
ATOM   5062  N N    . ILE B 1 289 ? -5.527  121.056 33.086  1.00 20.35  ? 289 ILE B N    1 
ATOM   5063  C CA   . ILE B 1 289 ? -5.475  119.872 32.246  1.00 13.93  ? 289 ILE B CA   1 
ATOM   5064  C C    . ILE B 1 289 ? -4.483  118.829 32.765  1.00 15.44  ? 289 ILE B C    1 
ATOM   5065  O O    . ILE B 1 289 ? -4.597  117.665 32.440  1.00 13.52  ? 289 ILE B O    1 
ATOM   5066  C CB   . ILE B 1 289 ? -5.156  120.308 30.817  1.00 14.65  ? 289 ILE B CB   1 
ATOM   5067  C CG1  . ILE B 1 289 ? -3.676  120.569 30.620  1.00 13.60  ? 289 ILE B CG1  1 
ATOM   5068  C CG2  . ILE B 1 289 ? -5.936  121.553 30.448  1.00 17.40  ? 289 ILE B CG2  1 
ATOM   5069  C CD1  . ILE B 1 289 ? -3.248  120.359 29.196  1.00 16.01  ? 289 ILE B CD1  1 
ATOM   5070  N N    . ARG B 1 290 ? -3.543  119.229 33.615  1.00 15.37  ? 290 ARG B N    1 
ATOM   5071  C CA   . ARG B 1 290 ? -2.547  118.339 34.184  1.00 13.62  ? 290 ARG B CA   1 
ATOM   5072  C C    . ARG B 1 290 ? -3.076  117.134 34.885  1.00 14.65  ? 290 ARG B C    1 
ATOM   5073  O O    . ARG B 1 290 ? -2.434  116.118 34.930  1.00 12.22  ? 290 ARG B O    1 
ATOM   5074  C CB   . ARG B 1 290 ? -1.742  119.135 35.167  1.00 9.15   ? 290 ARG B CB   1 
ATOM   5075  C CG   . ARG B 1 290 ? -0.872  120.168 34.524  1.00 12.66  ? 290 ARG B CG   1 
ATOM   5076  C CD   . ARG B 1 290 ? 0.032   120.826 35.532  1.00 15.26  ? 290 ARG B CD   1 
ATOM   5077  N NE   . ARG B 1 290 ? 0.506   122.099 35.026  1.00 15.73  ? 290 ARG B NE   1 
ATOM   5078  C CZ   . ARG B 1 290 ? 1.055   123.034 35.782  1.00 15.62  ? 290 ARG B CZ   1 
ATOM   5079  N NH1  . ARG B 1 290 ? 1.201   122.827 37.072  1.00 16.26  ? 290 ARG B NH1  1 
ATOM   5080  N NH2  . ARG B 1 290 ? 1.462   124.167 35.248  1.00 20.47  ? 290 ARG B NH2  1 
ATOM   5081  N N    . LYS B 1 291 ? -4.260  117.227 35.435  1.00 18.73  ? 291 LYS B N    1 
ATOM   5082  C CA   . LYS B 1 291 ? -4.873  116.133 36.174  1.00 17.10  ? 291 LYS B CA   1 
ATOM   5083  C C    . LYS B 1 291 ? -5.352  115.050 35.295  1.00 16.82  ? 291 LYS B C    1 
ATOM   5084  O O    . LYS B 1 291 ? -5.403  113.909 35.715  1.00 15.53  ? 291 LYS B O    1 
ATOM   5085  C CB   . LYS B 1 291 ? -6.087  116.681 36.901  1.00 16.50  ? 291 LYS B CB   1 
ATOM   5086  C CG   . LYS B 1 291 ? -5.831  117.955 37.680  1.00 19.23  ? 291 LYS B CG   1 
ATOM   5087  C CD   . LYS B 1 291 ? -6.524  117.877 39.028  1.00 18.90  ? 291 LYS B CD   1 
ATOM   5088  C CE   . LYS B 1 291 ? -6.304  119.125 39.865  1.00 15.39  ? 291 LYS B CE   1 
ATOM   5089  N NZ   . LYS B 1 291 ? -6.430  118.829 41.315  1.00 11.40  ? 291 LYS B NZ   1 
ATOM   5090  N N    . ASP B 1 292 ? -5.723  115.399 34.073  1.00 16.72  ? 292 ASP B N    1 
ATOM   5091  C CA   . ASP B 1 292 ? -6.287  114.451 33.144  1.00 17.01  ? 292 ASP B CA   1 
ATOM   5092  C C    . ASP B 1 292 ? -5.196  113.802 32.353  1.00 14.33  ? 292 ASP B C    1 
ATOM   5093  O O    . ASP B 1 292 ? -5.458  113.016 31.497  1.00 14.95  ? 292 ASP B O    1 
ATOM   5094  C CB   . ASP B 1 292 ? -7.202  115.225 32.216  1.00 14.17  ? 292 ASP B CB   1 
ATOM   5095  C CG   . ASP B 1 292 ? -8.652  114.994 32.493  1.00 23.42  ? 292 ASP B CG   1 
ATOM   5096  O OD1  . ASP B 1 292 ? -8.981  114.459 33.569  1.00 33.91  ? 292 ASP B OD1  1 
ATOM   5097  O OD2  . ASP B 1 292 ? -9.470  115.355 31.626  1.00 20.14  ? 292 ASP B OD2  1 
ATOM   5098  N N    . LEU B 1 293 ? -3.957  114.162 32.623  1.00 12.74  ? 293 LEU B N    1 
ATOM   5099  C CA   . LEU B 1 293 ? -2.830  113.655 31.888  1.00 12.00  ? 293 LEU B CA   1 
ATOM   5100  C C    . LEU B 1 293 ? -2.045  112.772 32.782  1.00 11.43  ? 293 LEU B C    1 
ATOM   5101  O O    . LEU B 1 293 ? -1.435  111.836 32.344  1.00 11.32  ? 293 LEU B O    1 
ATOM   5102  C CB   . LEU B 1 293 ? -1.910  114.795 31.500  1.00 13.97  ? 293 LEU B CB   1 
ATOM   5103  C CG   . LEU B 1 293 ? -2.304  116.079 30.774  1.00 15.57  ? 293 LEU B CG   1 
ATOM   5104  C CD1  . LEU B 1 293 ? -1.056  116.886 30.461  1.00 10.30  ? 293 LEU B CD1  1 
ATOM   5105  C CD2  . LEU B 1 293 ? -3.091  115.822 29.509  1.00 11.94  ? 293 LEU B CD2  1 
ATOM   5106  N N    . TYR B 1 294 ? -2.044  113.067 34.050  1.00 10.03  ? 294 TYR B N    1 
ATOM   5107  C CA   . TYR B 1 294 ? -1.279  112.296 34.988  1.00 10.15  ? 294 TYR B CA   1 
ATOM   5108  C C    . TYR B 1 294 ? -1.987  111.031 35.094  1.00 10.26  ? 294 TYR B C    1 
ATOM   5109  O O    . TYR B 1 294 ? -1.391  110.006 35.248  1.00 10.54  ? 294 TYR B O    1 
ATOM   5110  C CB   . TYR B 1 294 ? -1.250  112.973 36.331  1.00 10.80  ? 294 TYR B CB   1 
ATOM   5111  C CG   . TYR B 1 294 ? -0.075  113.863 36.614  1.00 10.23  ? 294 TYR B CG   1 
ATOM   5112  C CD1  . TYR B 1 294 ? 1.212   113.381 36.583  1.00 6.99   ? 294 TYR B CD1  1 
ATOM   5113  C CD2  . TYR B 1 294 ? -0.268  115.184 36.947  1.00 8.87   ? 294 TYR B CD2  1 
ATOM   5114  C CE1  . TYR B 1 294 ? 2.278   114.202 36.855  1.00 8.89   ? 294 TYR B CE1  1 
ATOM   5115  C CE2  . TYR B 1 294 ? 0.784   116.015 37.220  1.00 7.93   ? 294 TYR B CE2  1 
ATOM   5116  C CZ   . TYR B 1 294 ? 2.054   115.518 37.173  1.00 12.34  ? 294 TYR B CZ   1 
ATOM   5117  O OH   . TYR B 1 294 ? 3.097   116.350 37.446  1.00 10.52  ? 294 TYR B OH   1 
ATOM   5118  N N    . ALA B 1 295 ? -3.285  111.082 34.934  1.00 11.56  ? 295 ALA B N    1 
ATOM   5119  C CA   . ALA B 1 295 ? -4.110  109.914 35.038  1.00 12.15  ? 295 ALA B CA   1 
ATOM   5120  C C    . ALA B 1 295 ? -4.349  109.315 33.728  1.00 11.85  ? 295 ALA B C    1 
ATOM   5121  O O    . ALA B 1 295 ? -5.191  108.475 33.598  1.00 10.64  ? 295 ALA B O    1 
ATOM   5122  C CB   . ALA B 1 295 ? -5.422  110.321 35.569  1.00 12.37  ? 295 ALA B CB   1 
ATOM   5123  N N    . ASN B 1 296 ? -3.650  109.781 32.718  1.00 11.32  ? 296 ASN B N    1 
ATOM   5124  C CA   . ASN B 1 296 ? -3.819  109.280 31.358  1.00 11.28  ? 296 ASN B CA   1 
ATOM   5125  C C    . ASN B 1 296 ? -2.523  109.265 30.570  1.00 8.02   ? 296 ASN B C    1 
ATOM   5126  O O    . ASN B 1 296 ? -2.469  109.805 29.501  1.00 7.32   ? 296 ASN B O    1 
ATOM   5127  C CB   . ASN B 1 296 ? -4.919  110.028 30.621  1.00 10.83  ? 296 ASN B CB   1 
ATOM   5128  C CG   . ASN B 1 296 ? -6.311  109.609 31.032  1.00 9.67   ? 296 ASN B CG   1 
ATOM   5129  O OD1  . ASN B 1 296 ? -6.671  108.448 30.941  1.00 11.43  ? 296 ASN B OD1  1 
ATOM   5130  N ND2  . ASN B 1 296 ? -7.098  110.558 31.502  1.00 8.48   ? 296 ASN B ND2  1 
ATOM   5131  N N    . THR B 1 297 ? -1.513  108.576 31.076  1.00 5.44   ? 297 THR B N    1 
ATOM   5132  C CA   . THR B 1 297 ? -0.243  108.470 30.409  1.00 6.15   ? 297 THR B CA   1 
ATOM   5133  C C    . THR B 1 297 ? -0.083  107.203 29.619  1.00 7.49   ? 297 THR B C    1 
ATOM   5134  O O    . THR B 1 297 ? 0.148   106.173 30.192  1.00 10.88  ? 297 THR B O    1 
ATOM   5135  C CB   . THR B 1 297 ? 0.920   108.545 31.407  1.00 8.10   ? 297 THR B CB   1 
ATOM   5136  O OG1  . THR B 1 297 ? 0.669   109.565 32.375  1.00 7.83   ? 297 THR B OG1  1 
ATOM   5137  C CG2  . THR B 1 297 ? 2.246   108.837 30.704  1.00 4.46   ? 297 THR B CG2  1 
ATOM   5138  N N    . VAL B 1 298 ? -0.164  107.271 28.295  1.00 5.53   ? 298 VAL B N    1 
ATOM   5139  C CA   . VAL B 1 298 ? -0.039  106.102 27.432  1.00 6.22   ? 298 VAL B CA   1 
ATOM   5140  C C    . VAL B 1 298 ? 1.371   105.852 26.963  1.00 7.17   ? 298 VAL B C    1 
ATOM   5141  O O    . VAL B 1 298 ? 1.975   106.675 26.321  1.00 8.33   ? 298 VAL B O    1 
ATOM   5142  C CB   . VAL B 1 298 ? -1.027  106.123 26.263  1.00 6.08   ? 298 VAL B CB   1 
ATOM   5143  C CG1  . VAL B 1 298 ? -0.839  104.929 25.352  1.00 9.14   ? 298 VAL B CG1  1 
ATOM   5144  C CG2  . VAL B 1 298 ? -2.443  106.157 26.785  1.00 6.66   ? 298 VAL B CG2  1 
ATOM   5145  N N    . LEU B 1 299 ? 1.919   104.707 27.306  1.00 5.72   ? 299 LEU B N    1 
ATOM   5146  C CA   . LEU B 1 299 ? 3.221   104.383 26.897  1.00 5.85   ? 299 LEU B CA   1 
ATOM   5147  C C    . LEU B 1 299 ? 2.974   103.736 25.589  1.00 8.31   ? 299 LEU B C    1 
ATOM   5148  O O    . LEU B 1 299 ? 2.335   102.724 25.535  1.00 12.75  ? 299 LEU B O    1 
ATOM   5149  C CB   . LEU B 1 299 ? 3.826   103.456 27.891  1.00 6.24   ? 299 LEU B CB   1 
ATOM   5150  C CG   . LEU B 1 299 ? 3.982   103.874 29.343  1.00 7.17   ? 299 LEU B CG   1 
ATOM   5151  C CD1  . LEU B 1 299 ? 5.144   103.107 29.911  1.00 7.66   ? 299 LEU B CD1  1 
ATOM   5152  C CD2  . LEU B 1 299 ? 4.202   105.357 29.546  1.00 11.13  ? 299 LEU B CD2  1 
ATOM   5153  N N    . SER B 1 300 ? 3.440   104.346 24.503  1.00 6.43   ? 300 SER B N    1 
ATOM   5154  C CA   . SER B 1 300 ? 3.222   103.862 23.166  1.00 6.60   ? 300 SER B CA   1 
ATOM   5155  C C    . SER B 1 300 ? 4.547   103.731 22.599  1.00 5.71   ? 300 SER B C    1 
ATOM   5156  O O    . SER B 1 300 ? 5.455   104.333 23.045  1.00 6.02   ? 300 SER B O    1 
ATOM   5157  C CB   . SER B 1 300 ? 2.444   104.847 22.348  1.00 8.18   ? 300 SER B CB   1 
ATOM   5158  O OG   . SER B 1 300 ? 2.576   104.595 20.971  1.00 10.41  ? 300 SER B OG   1 
ATOM   5159  N N    . GLY B 1 301 ? 4.674   102.921 21.593  1.00 6.86   ? 301 GLY B N    1 
ATOM   5160  C CA   . GLY B 1 301 ? 5.952   102.639 21.033  1.00 5.84   ? 301 GLY B CA   1 
ATOM   5161  C C    . GLY B 1 301 ? 6.472   101.286 21.385  1.00 6.35   ? 301 GLY B C    1 
ATOM   5162  O O    . GLY B 1 301 ? 5.880   100.571 22.133  1.00 7.91   ? 301 GLY B O    1 
ATOM   5163  N N    . GLY B 1 302 ? 7.624   100.935 20.876  1.00 7.80   ? 302 GLY B N    1 
ATOM   5164  C CA   . GLY B 1 302 ? 8.168   99.622  21.091  1.00 10.65  ? 302 GLY B CA   1 
ATOM   5165  C C    . GLY B 1 302 ? 9.354   99.585  21.976  1.00 8.87   ? 302 GLY B C    1 
ATOM   5166  O O    . GLY B 1 302 ? 9.885   98.524  22.249  1.00 10.16  ? 302 GLY B O    1 
ATOM   5167  N N    . THR B 1 303 ? 9.805   100.747 22.390  1.00 7.58   ? 303 THR B N    1 
ATOM   5168  C CA   . THR B 1 303 ? 10.872  100.796 23.338  1.00 9.52   ? 303 THR B CA   1 
ATOM   5169  C C    . THR B 1 303 ? 10.130  100.919 24.635  1.00 8.41   ? 303 THR B C    1 
ATOM   5170  O O    . THR B 1 303 ? 10.651  100.691 25.702  1.00 10.70  ? 303 THR B O    1 
ATOM   5171  C CB   . THR B 1 303 ? 11.888  101.914 22.990  1.00 7.18   ? 303 THR B CB   1 
ATOM   5172  O OG1  . THR B 1 303 ? 12.615  101.543 21.817  1.00 7.94   ? 303 THR B OG1  1 
ATOM   5173  C CG2  . THR B 1 303 ? 12.867  102.161 24.085  1.00 6.70   ? 303 THR B CG2  1 
ATOM   5174  N N    . THR B 1 304 ? 8.872   101.250 24.546  1.00 6.85   ? 304 THR B N    1 
ATOM   5175  C CA   . THR B 1 304 ? 8.077   101.264 25.725  1.00 7.75   ? 304 THR B CA   1 
ATOM   5176  C C    . THR B 1 304 ? 7.453   99.930  25.844  1.00 12.04  ? 304 THR B C    1 
ATOM   5177  O O    . THR B 1 304 ? 6.290   99.861  26.136  1.00 11.63  ? 304 THR B O    1 
ATOM   5178  C CB   . THR B 1 304 ? 6.891   102.152 25.606  1.00 7.00   ? 304 THR B CB   1 
ATOM   5179  O OG1  . THR B 1 304 ? 6.162   101.786 24.445  1.00 11.71  ? 304 THR B OG1  1 
ATOM   5180  C CG2  . THR B 1 304 ? 7.314   103.569 25.499  1.00 7.24   ? 304 THR B CG2  1 
ATOM   5181  N N    . MET B 1 305 ? 8.212   98.863  25.615  1.00 13.43  ? 305 MET B N    1 
ATOM   5182  C CA   . MET B 1 305 ? 7.642   97.525  25.622  1.00 13.96  ? 305 MET B CA   1 
ATOM   5183  C C    . MET B 1 305 ? 8.526   96.594  26.333  1.00 12.69  ? 305 MET B C    1 
ATOM   5184  O O    . MET B 1 305 ? 8.790   95.494  25.877  1.00 14.28  ? 305 MET B O    1 
ATOM   5185  C CB   . MET B 1 305 ? 7.459   96.973  24.207  1.00 13.79  ? 305 MET B CB   1 
ATOM   5186  C CG   . MET B 1 305 ? 6.181   97.344  23.508  1.00 13.66  ? 305 MET B CG   1 
ATOM   5187  S SD   . MET B 1 305 ? 4.905   96.127  23.782  1.00 23.12  ? 305 MET B SD   1 
ATOM   5188  C CE   . MET B 1 305 ? 5.773   94.613  23.429  1.00 31.90  ? 305 MET B CE   1 
ATOM   5189  N N    . TYR B 1 306 ? 9.038   97.061  27.438  1.00 10.82  ? 306 TYR B N    1 
ATOM   5190  C CA   . TYR B 1 306 ? 9.886   96.234  28.232  1.00 11.82  ? 306 TYR B CA   1 
ATOM   5191  C C    . TYR B 1 306 ? 9.044   95.977  29.453  1.00 13.32  ? 306 TYR B C    1 
ATOM   5192  O O    . TYR B 1 306 ? 8.438   96.854  29.989  1.00 13.40  ? 306 TYR B O    1 
ATOM   5193  C CB   . TYR B 1 306 ? 11.224  96.915  28.500  1.00 7.89   ? 306 TYR B CB   1 
ATOM   5194  C CG   . TYR B 1 306 ? 11.972  97.353  27.270  1.00 9.76   ? 306 TYR B CG   1 
ATOM   5195  C CD1  . TYR B 1 306 ? 12.009  96.567  26.135  1.00 17.75  ? 306 TYR B CD1  1 
ATOM   5196  C CD2  . TYR B 1 306 ? 12.641  98.555  27.242  1.00 8.61   ? 306 TYR B CD2  1 
ATOM   5197  C CE1  . TYR B 1 306 ? 12.674  96.975  25.003  1.00 14.93  ? 306 TYR B CE1  1 
ATOM   5198  C CE2  . TYR B 1 306 ? 13.321  98.963  26.120  1.00 8.19   ? 306 TYR B CE2  1 
ATOM   5199  C CZ   . TYR B 1 306 ? 13.326  98.166  25.004  1.00 10.20  ? 306 TYR B CZ   1 
ATOM   5200  O OH   . TYR B 1 306 ? 13.979  98.557  23.874  1.00 12.73  ? 306 TYR B OH   1 
ATOM   5201  N N    . PRO B 1 307 ? 8.962   94.705  29.904  1.00 12.95  ? 307 PRO B N    1 
ATOM   5202  C CA   . PRO B 1 307 ? 8.088   94.519  31.043  1.00 10.00  ? 307 PRO B CA   1 
ATOM   5203  C C    . PRO B 1 307 ? 8.471   95.246  32.329  1.00 16.00  ? 307 PRO B C    1 
ATOM   5204  O O    . PRO B 1 307 ? 9.540   95.021  32.863  1.00 20.35  ? 307 PRO B O    1 
ATOM   5205  C CB   . PRO B 1 307 ? 8.219   93.022  31.288  1.00 8.12   ? 307 PRO B CB   1 
ATOM   5206  C CG   . PRO B 1 307 ? 8.539   92.437  29.982  1.00 12.55  ? 307 PRO B CG   1 
ATOM   5207  C CD   . PRO B 1 307 ? 9.577   93.395  29.554  1.00 19.53  ? 307 PRO B CD   1 
ATOM   5208  N N    . GLY B 1 308 ? 7.585   96.062  32.871  1.00 15.63  ? 308 GLY B N    1 
ATOM   5209  C CA   . GLY B 1 308 ? 7.862   96.777  34.093  1.00 13.38  ? 308 GLY B CA   1 
ATOM   5210  C C    . GLY B 1 308 ? 7.984   98.241  33.874  1.00 14.37  ? 308 GLY B C    1 
ATOM   5211  O O    . GLY B 1 308 ? 8.216   98.979  34.795  1.00 17.10  ? 308 GLY B O    1 
ATOM   5212  N N    . ILE B 1 309 ? 7.786   98.685  32.661  1.00 13.38  ? 309 ILE B N    1 
ATOM   5213  C CA   . ILE B 1 309 ? 8.001   100.057 32.335  1.00 11.79  ? 309 ILE B CA   1 
ATOM   5214  C C    . ILE B 1 309 ? 6.973   100.934 32.945  1.00 11.74  ? 309 ILE B C    1 
ATOM   5215  O O    . ILE B 1 309 ? 7.246   102.070 33.220  1.00 13.21  ? 309 ILE B O    1 
ATOM   5216  C CB   . ILE B 1 309 ? 8.102   100.223 30.793  1.00 14.33  ? 309 ILE B CB   1 
ATOM   5217  C CG1  . ILE B 1 309 ? 8.520   101.642 30.381  1.00 12.90  ? 309 ILE B CG1  1 
ATOM   5218  C CG2  . ILE B 1 309 ? 6.830   99.783  30.087  1.00 13.03  ? 309 ILE B CG2  1 
ATOM   5219  C CD1  . ILE B 1 309 ? 9.648   101.693 29.385  1.00 12.68  ? 309 ILE B CD1  1 
ATOM   5220  N N    . ALA B 1 310 ? 5.797   100.422 33.227  1.00 9.55   ? 310 ALA B N    1 
ATOM   5221  C CA   . ALA B 1 310 ? 4.714   101.264 33.697  1.00 12.66  ? 310 ALA B CA   1 
ATOM   5222  C C    . ALA B 1 310 ? 4.598   101.174 35.148  1.00 15.23  ? 310 ALA B C    1 
ATOM   5223  O O    . ALA B 1 310 ? 3.653   101.644 35.726  1.00 17.13  ? 310 ALA B O    1 
ATOM   5224  C CB   . ALA B 1 310 ? 3.438   100.815 33.075  1.00 8.25   ? 310 ALA B CB   1 
ATOM   5225  N N    . ASP B 1 311 ? 5.573   100.562 35.766  1.00 11.74  ? 311 ASP B N    1 
ATOM   5226  C CA   . ASP B 1 311 ? 5.502   100.326 37.162  1.00 13.21  ? 311 ASP B CA   1 
ATOM   5227  C C    . ASP B 1 311 ? 6.634   101.070 37.683  1.00 13.35  ? 311 ASP B C    1 
ATOM   5228  O O    . ASP B 1 311 ? 6.794   101.222 38.872  1.00 13.94  ? 311 ASP B O    1 
ATOM   5229  C CB   . ASP B 1 311 ? 5.657   98.835  37.367  1.00 22.95  ? 311 ASP B CB   1 
ATOM   5230  C CG   . ASP B 1 311 ? 4.495   98.033  36.786  1.00 27.98  ? 311 ASP B CG   1 
ATOM   5231  O OD1  . ASP B 1 311 ? 3.349   98.235  37.217  1.00 39.64  ? 311 ASP B OD1  1 
ATOM   5232  O OD2  . ASP B 1 311 ? 4.717   97.191  35.899  1.00 22.65  ? 311 ASP B OD2  1 
ATOM   5233  N N    . ARG B 1 312 ? 7.425   101.582 36.770  1.00 11.81  ? 312 ARG B N    1 
ATOM   5234  C CA   . ARG B 1 312 ? 8.536   102.398 37.139  1.00 10.63  ? 312 ARG B CA   1 
ATOM   5235  C C    . ARG B 1 312 ? 8.114   103.736 36.698  1.00 9.83   ? 312 ARG B C    1 
ATOM   5236  O O    . ARG B 1 312 ? 8.563   104.695 37.177  1.00 8.77   ? 312 ARG B O    1 
ATOM   5237  C CB   . ARG B 1 312 ? 9.810   101.933 36.464  1.00 9.51   ? 312 ARG B CB   1 
ATOM   5238  C CG   . ARG B 1 312 ? 11.015  102.826 36.645  1.00 8.14   ? 312 ARG B CG   1 
ATOM   5239  C CD   . ARG B 1 312 ? 11.991  102.361 37.692  1.00 6.88   ? 312 ARG B CD   1 
ATOM   5240  N NE   . ARG B 1 312 ? 13.090  103.294 37.794  1.00 5.31   ? 312 ARG B NE   1 
ATOM   5241  C CZ   . ARG B 1 312 ? 14.265  103.124 37.213  1.00 5.83   ? 312 ARG B CZ   1 
ATOM   5242  N NH1  . ARG B 1 312 ? 14.500  102.039 36.504  1.00 5.44   ? 312 ARG B NH1  1 
ATOM   5243  N NH2  . ARG B 1 312 ? 15.203  104.043 37.345  1.00 5.88   ? 312 ARG B NH2  1 
ATOM   5244  N N    . MET B 1 313 ? 7.147   103.822 35.829  1.00 8.73   ? 313 MET B N    1 
ATOM   5245  C CA   . MET B 1 313 ? 6.653   105.110 35.434  1.00 10.18  ? 313 MET B CA   1 
ATOM   5246  C C    . MET B 1 313 ? 5.563   105.516 36.314  1.00 9.28   ? 313 MET B C    1 
ATOM   5247  O O    . MET B 1 313 ? 4.896   106.458 36.080  1.00 8.63   ? 313 MET B O    1 
ATOM   5248  C CB   . MET B 1 313 ? 6.164   105.117 33.995  1.00 10.60  ? 313 MET B CB   1 
ATOM   5249  C CG   . MET B 1 313 ? 7.220   105.336 32.932  1.00 9.92   ? 313 MET B CG   1 
ATOM   5250  S SD   . MET B 1 313 ? 7.800   107.021 32.829  1.00 8.13   ? 313 MET B SD   1 
ATOM   5251  C CE   . MET B 1 313 ? 6.681   107.678 31.614  1.00 9.46   ? 313 MET B CE   1 
ATOM   5252  N N    . GLN B 1 314 ? 5.364   104.780 37.352  1.00 10.81  ? 314 GLN B N    1 
ATOM   5253  C CA   . GLN B 1 314 ? 4.356   105.103 38.306  1.00 11.15  ? 314 GLN B CA   1 
ATOM   5254  C C    . GLN B 1 314 ? 5.120   105.548 39.454  1.00 8.49   ? 314 GLN B C    1 
ATOM   5255  O O    . GLN B 1 314 ? 4.884   106.565 39.951  1.00 7.72   ? 314 GLN B O    1 
ATOM   5256  C CB   . GLN B 1 314 ? 3.585   103.863 38.634  1.00 12.22  ? 314 GLN B CB   1 
ATOM   5257  C CG   . GLN B 1 314 ? 2.688   103.981 39.848  1.00 20.81  ? 314 GLN B CG   1 
ATOM   5258  C CD   . GLN B 1 314 ? 1.297   104.462 39.520  1.00 9.87   ? 314 GLN B CD   1 
ATOM   5259  O OE1  . GLN B 1 314 ? 0.624   105.039 40.362  1.00 13.98  ? 314 GLN B OE1  1 
ATOM   5260  N NE2  . GLN B 1 314 ? 0.856   104.218 38.303  1.00 7.98   ? 314 GLN B NE2  1 
ATOM   5261  N N    . LYS B 1 315 ? 6.152   104.822 39.806  1.00 9.35   ? 315 LYS B N    1 
ATOM   5262  C CA   . LYS B 1 315 ? 7.024   105.173 40.898  1.00 12.59  ? 315 LYS B CA   1 
ATOM   5263  C C    . LYS B 1 315 ? 7.837   106.388 40.649  1.00 12.42  ? 315 LYS B C    1 
ATOM   5264  O O    . LYS B 1 315 ? 8.200   107.071 41.584  1.00 15.28  ? 315 LYS B O    1 
ATOM   5265  C CB   . LYS B 1 315 ? 7.978   104.036 41.163  1.00 10.45  ? 315 LYS B CB   1 
ATOM   5266  C CG   . LYS B 1 315 ? 7.329   102.737 41.589  1.00 21.90  ? 315 LYS B CG   1 
ATOM   5267  C CD   . LYS B 1 315 ? 6.699   102.844 42.965  1.00 35.51  ? 315 LYS B CD   1 
ATOM   5268  C CE   . LYS B 1 315 ? 6.047   101.542 43.394  1.00 38.07  ? 315 LYS B CE   1 
ATOM   5269  N NZ   . LYS B 1 315 ? 7.022   100.430 43.574  1.00 16.91  ? 315 LYS B NZ   1 
ATOM   5270  N N    . GLU B 1 316 ? 8.115   106.694 39.396  1.00 9.60   ? 316 GLU B N    1 
ATOM   5271  C CA   . GLU B 1 316 ? 8.986   107.810 39.076  1.00 8.39   ? 316 GLU B CA   1 
ATOM   5272  C C    . GLU B 1 316 ? 8.267   109.054 38.753  1.00 8.38   ? 316 GLU B C    1 
ATOM   5273  O O    . GLU B 1 316 ? 8.877   110.078 38.677  1.00 8.42   ? 316 GLU B O    1 
ATOM   5274  C CB   . GLU B 1 316 ? 9.980   107.438 38.011  1.00 7.04   ? 316 GLU B CB   1 
ATOM   5275  C CG   . GLU B 1 316 ? 10.958  106.348 38.418  1.00 6.50   ? 316 GLU B CG   1 
ATOM   5276  C CD   . GLU B 1 316 ? 12.264  106.861 38.974  1.00 8.06   ? 316 GLU B CD   1 
ATOM   5277  O OE1  . GLU B 1 316 ? 12.260  107.702 39.887  1.00 7.25   ? 316 GLU B OE1  1 
ATOM   5278  O OE2  . GLU B 1 316 ? 13.311  106.405 38.505  1.00 10.87  ? 316 GLU B OE2  1 
ATOM   5279  N N    . ILE B 1 317 ? 6.958   108.983 38.586  1.00 10.42  ? 317 ILE B N    1 
ATOM   5280  C CA   . ILE B 1 317 ? 6.129   110.135 38.320  1.00 10.45  ? 317 ILE B CA   1 
ATOM   5281  C C    . ILE B 1 317 ? 5.288   110.382 39.525  1.00 8.47   ? 317 ILE B C    1 
ATOM   5282  O O    . ILE B 1 317 ? 4.727   111.405 39.641  1.00 8.03   ? 317 ILE B O    1 
ATOM   5283  C CB   . ILE B 1 317 ? 5.290   109.922 37.073  1.00 5.66   ? 317 ILE B CB   1 
ATOM   5284  C CG1  . ILE B 1 317 ? 6.135   109.357 35.961  1.00 8.40   ? 317 ILE B CG1  1 
ATOM   5285  C CG2  . ILE B 1 317 ? 4.784   111.235 36.512  1.00 5.39   ? 317 ILE B CG2  1 
ATOM   5286  C CD1  . ILE B 1 317 ? 5.757   109.943 34.632  1.00 10.78  ? 317 ILE B CD1  1 
ATOM   5287  N N    . THR B 1 318 ? 5.244   109.460 40.469  1.00 9.73   ? 318 THR B N    1 
ATOM   5288  C CA   . THR B 1 318 ? 4.508   109.633 41.723  1.00 12.69  ? 318 THR B CA   1 
ATOM   5289  C C    . THR B 1 318 ? 5.433   110.320 42.646  1.00 12.19  ? 318 THR B C    1 
ATOM   5290  O O    . THR B 1 318 ? 5.010   111.081 43.502  1.00 9.82   ? 318 THR B O    1 
ATOM   5291  C CB   . THR B 1 318 ? 4.068   108.276 42.324  1.00 10.51  ? 318 THR B CB   1 
ATOM   5292  O OG1  . THR B 1 318 ? 3.120   107.643 41.464  1.00 13.33  ? 318 THR B OG1  1 
ATOM   5293  C CG2  . THR B 1 318 ? 3.434   108.415 43.683  1.00 9.31   ? 318 THR B CG2  1 
ATOM   5294  N N    . ALA B 1 319 ? 6.721   110.141 42.420  1.00 13.44  ? 319 ALA B N    1 
ATOM   5295  C CA   . ALA B 1 319 ? 7.728   110.741 43.245  1.00 8.29   ? 319 ALA B CA   1 
ATOM   5296  C C    . ALA B 1 319 ? 8.001   112.110 42.802  1.00 10.47  ? 319 ALA B C    1 
ATOM   5297  O O    . ALA B 1 319 ? 8.196   112.988 43.608  1.00 14.64  ? 319 ALA B O    1 
ATOM   5298  C CB   . ALA B 1 319 ? 8.956   109.940 43.144  1.00 5.28   ? 319 ALA B CB   1 
ATOM   5299  N N    . LEU B 1 320 ? 7.924   112.351 41.518  1.00 10.81  ? 320 LEU B N    1 
ATOM   5300  C CA   . LEU B 1 320 ? 8.209   113.662 40.975  1.00 13.19  ? 320 LEU B CA   1 
ATOM   5301  C C    . LEU B 1 320 ? 7.059   114.574 41.111  1.00 12.30  ? 320 LEU B C    1 
ATOM   5302  O O    . LEU B 1 320 ? 7.233   115.769 41.141  1.00 13.82  ? 320 LEU B O    1 
ATOM   5303  C CB   . LEU B 1 320 ? 8.613   113.559 39.515  1.00 10.53  ? 320 LEU B CB   1 
ATOM   5304  C CG   . LEU B 1 320 ? 10.075  113.403 39.150  1.00 8.99   ? 320 LEU B CG   1 
ATOM   5305  C CD1  . LEU B 1 320 ? 10.165  113.472 37.648  1.00 7.89   ? 320 LEU B CD1  1 
ATOM   5306  C CD2  . LEU B 1 320 ? 10.877  114.528 39.769  1.00 20.31  ? 320 LEU B CD2  1 
ATOM   5307  N N    . ALA B 1 321 ? 5.876   114.037 41.258  1.00 10.69  ? 321 ALA B N    1 
ATOM   5308  C CA   . ALA B 1 321 ? 4.680   114.850 41.286  1.00 12.50  ? 321 ALA B CA   1 
ATOM   5309  C C    . ALA B 1 321 ? 3.986   115.160 42.569  1.00 13.50  ? 321 ALA B C    1 
ATOM   5310  O O    . ALA B 1 321 ? 4.230   114.532 43.588  1.00 9.49   ? 321 ALA B O    1 
ATOM   5311  C CB   . ALA B 1 321 ? 3.668   114.211 40.376  1.00 8.82   ? 321 ALA B CB   1 
ATOM   5312  N N    . PRO B 1 322 ? 3.090   116.200 42.526  1.00 10.89  ? 322 PRO B N    1 
ATOM   5313  C CA   . PRO B 1 322 ? 2.273   116.408 43.698  1.00 10.60  ? 322 PRO B CA   1 
ATOM   5314  C C    . PRO B 1 322 ? 1.619   115.202 44.299  1.00 16.65  ? 322 PRO B C    1 
ATOM   5315  O O    . PRO B 1 322 ? 1.278   114.268 43.611  1.00 17.55  ? 322 PRO B O    1 
ATOM   5316  C CB   . PRO B 1 322 ? 1.166   117.269 43.152  1.00 12.56  ? 322 PRO B CB   1 
ATOM   5317  C CG   . PRO B 1 322 ? 1.654   117.905 41.906  1.00 18.13  ? 322 PRO B CG   1 
ATOM   5318  C CD   . PRO B 1 322 ? 3.055   117.470 41.750  1.00 15.09  ? 322 PRO B CD   1 
ATOM   5319  N N    . SER B 1 323 ? 1.310   115.260 45.576  1.00 23.28  ? 323 SER B N    1 
ATOM   5320  C CA   . SER B 1 323 ? 0.783   114.119 46.289  1.00 17.44  ? 323 SER B CA   1 
ATOM   5321  C C    . SER B 1 323 ? -0.664  113.843 46.119  1.00 21.43  ? 323 SER B C    1 
ATOM   5322  O O    . SER B 1 323 ? -1.162  112.790 46.507  1.00 16.63  ? 323 SER B O    1 
ATOM   5323  C CB   . SER B 1 323 ? 0.994   114.380 47.744  1.00 15.64  ? 323 SER B CB   1 
ATOM   5324  O OG   . SER B 1 323 ? 0.065   115.342 48.206  1.00 21.09  ? 323 SER B OG   1 
ATOM   5325  N N    . THR B 1 324 ? -1.367  114.777 45.528  1.00 22.82  ? 324 THR B N    1 
ATOM   5326  C CA   . THR B 1 324 ? -2.786  114.628 45.339  1.00 24.54  ? 324 THR B CA   1 
ATOM   5327  C C    . THR B 1 324 ? -3.059  114.053 44.000  1.00 29.43  ? 324 THR B C    1 
ATOM   5328  O O    . THR B 1 324 ? -4.201  114.011 43.565  1.00 27.13  ? 324 THR B O    1 
ATOM   5329  C CB   . THR B 1 324 ? -3.341  116.023 45.259  1.00 27.70  ? 324 THR B CB   1 
ATOM   5330  O OG1  . THR B 1 324 ? -2.815  116.673 44.098  1.00 26.98  ? 324 THR B OG1  1 
ATOM   5331  C CG2  . THR B 1 324 ? -2.931  116.810 46.484  1.00 22.29  ? 324 THR B CG2  1 
ATOM   5332  N N    . MET B 1 325 ? -2.028  113.577 43.324  1.00 22.31  ? 325 MET B N    1 
ATOM   5333  C CA   . MET B 1 325 ? -2.195  113.179 41.957  1.00 15.03  ? 325 MET B CA   1 
ATOM   5334  C C    . MET B 1 325 ? -2.294  111.754 41.713  1.00 14.85  ? 325 MET B C    1 
ATOM   5335  O O    . MET B 1 325 ? -1.532  110.982 42.258  1.00 15.28  ? 325 MET B O    1 
ATOM   5336  C CB   . MET B 1 325 ? -1.058  113.743 41.143  1.00 19.54  ? 325 MET B CB   1 
ATOM   5337  C CG   . MET B 1 325 ? -1.134  115.233 40.884  1.00 20.41  ? 325 MET B CG   1 
ATOM   5338  S SD   . MET B 1 325 ? -2.501  115.735 39.836  1.00 14.05  ? 325 MET B SD   1 
ATOM   5339  C CE   . MET B 1 325 ? -2.290  117.503 39.856  1.00 8.99   ? 325 MET B CE   1 
ATOM   5340  N N    . LYS B 1 326 ? -3.232  111.396 40.851  1.00 15.63  ? 326 LYS B N    1 
ATOM   5341  C CA   . LYS B 1 326 ? -3.397  110.025 40.484  1.00 13.13  ? 326 LYS B CA   1 
ATOM   5342  C C    . LYS B 1 326 ? -2.629  109.864 39.227  1.00 12.71  ? 326 LYS B C    1 
ATOM   5343  O O    . LYS B 1 326 ? -2.712  110.673 38.338  1.00 13.42  ? 326 LYS B O    1 
ATOM   5344  C CB   . LYS B 1 326 ? -4.860  109.597 40.435  1.00 10.82  ? 326 LYS B CB   1 
ATOM   5345  C CG   . LYS B 1 326 ? -5.737  110.116 39.321  1.00 23.03  ? 326 LYS B CG   1 
ATOM   5346  C CD   . LYS B 1 326 ? -6.678  109.007 38.866  1.00 23.68  ? 326 LYS B CD   1 
ATOM   5347  C CE   . LYS B 1 326 ? -8.029  109.548 38.430  1.00 16.86  ? 326 LYS B CE   1 
ATOM   5348  N NZ   . LYS B 1 326 ? -8.849  108.511 37.749  1.00 11.29  ? 326 LYS B NZ   1 
ATOM   5349  N N    . ILE B 1 327 ? -1.799  108.845 39.180  1.00 10.86  ? 327 ILE B N    1 
ATOM   5350  C CA   . ILE B 1 327 ? -0.960  108.625 38.062  1.00 9.38   ? 327 ILE B CA   1 
ATOM   5351  C C    . ILE B 1 327 ? -1.407  107.321 37.554  1.00 11.25  ? 327 ILE B C    1 
ATOM   5352  O O    . ILE B 1 327 ? -1.259  106.331 38.232  1.00 10.47  ? 327 ILE B O    1 
ATOM   5353  C CB   . ILE B 1 327 ? 0.522   108.536 38.479  1.00 6.50   ? 327 ILE B CB   1 
ATOM   5354  C CG1  . ILE B 1 327 ? 0.811   109.445 39.663  1.00 6.41   ? 327 ILE B CG1  1 
ATOM   5355  C CG2  . ILE B 1 327 ? 1.430   108.893 37.324  1.00 8.44   ? 327 ILE B CG2  1 
ATOM   5356  C CD1  . ILE B 1 327 ? 1.314   110.811 39.281  1.00 6.62   ? 327 ILE B CD1  1 
ATOM   5357  N N    . LYS B 1 328 ? -2.018  107.289 36.380  1.00 13.23  ? 328 LYS B N    1 
ATOM   5358  C CA   . LYS B 1 328 ? -2.375  106.029 35.764  1.00 13.02  ? 328 LYS B CA   1 
ATOM   5359  C C    . LYS B 1 328 ? -1.525  105.879 34.563  1.00 11.25  ? 328 LYS B C    1 
ATOM   5360  O O    . LYS B 1 328 ? -1.496  106.757 33.732  1.00 9.71   ? 328 LYS B O    1 
ATOM   5361  C CB   . LYS B 1 328 ? -3.851  105.916 35.401  1.00 10.57  ? 328 LYS B CB   1 
ATOM   5362  C CG   . LYS B 1 328 ? -4.274  104.539 34.931  1.00 11.73  ? 328 LYS B CG   1 
ATOM   5363  C CD   . LYS B 1 328 ? -5.778  104.408 34.846  1.00 14.40  ? 328 LYS B CD   1 
ATOM   5364  C CE   . LYS B 1 328 ? -6.384  105.475 33.960  1.00 13.02  ? 328 LYS B CE   1 
ATOM   5365  N NZ   . LYS B 1 328 ? -7.732  105.109 33.448  1.00 11.99  ? 328 LYS B NZ   1 
ATOM   5366  N N    . ILE B 1 329 ? -0.783  104.780 34.503  1.00 11.08  ? 329 ILE B N    1 
ATOM   5367  C CA   . ILE B 1 329 ? 0.047   104.477 33.376  1.00 11.76  ? 329 ILE B CA   1 
ATOM   5368  C C    . ILE B 1 329 ? -0.631  103.386 32.564  1.00 7.82   ? 329 ILE B C    1 
ATOM   5369  O O    . ILE B 1 329 ? -1.007  102.358 33.087  1.00 7.23   ? 329 ILE B O    1 
ATOM   5370  C CB   . ILE B 1 329 ? 1.467   104.181 33.824  1.00 9.46   ? 329 ILE B CB   1 
ATOM   5371  C CG1  . ILE B 1 329 ? 1.867   105.145 34.914  1.00 6.83   ? 329 ILE B CG1  1 
ATOM   5372  C CG2  . ILE B 1 329 ? 2.413   104.417 32.679  1.00 8.59   ? 329 ILE B CG2  1 
ATOM   5373  C CD1  . ILE B 1 329 ? 2.218   106.499 34.355  1.00 8.73   ? 329 ILE B CD1  1 
ATOM   5374  N N    . ILE B 1 330 ? -0.847  103.653 31.288  1.00 6.05   ? 330 ILE B N    1 
ATOM   5375  C CA   . ILE B 1 330 ? -1.561  102.752 30.402  1.00 8.60   ? 330 ILE B CA   1 
ATOM   5376  C C    . ILE B 1 330 ? -0.674  102.254 29.296  1.00 7.96   ? 330 ILE B C    1 
ATOM   5377  O O    . ILE B 1 330 ? -0.429  102.925 28.334  1.00 5.85   ? 330 ILE B O    1 
ATOM   5378  C CB   . ILE B 1 330 ? -2.772  103.485 29.806  1.00 8.56   ? 330 ILE B CB   1 
ATOM   5379  C CG1  . ILE B 1 330 ? -3.568  104.187 30.896  1.00 7.26   ? 330 ILE B CG1  1 
ATOM   5380  C CG2  . ILE B 1 330 ? -3.682  102.519 29.068  1.00 11.42  ? 330 ILE B CG2  1 
ATOM   5381  C CD1  . ILE B 1 330 ? -3.730  105.659 30.676  1.00 6.81   ? 330 ILE B CD1  1 
ATOM   5382  N N    . ALA B 1 331 ? -0.174  101.055 29.450  1.00 7.30   ? 331 ALA B N    1 
ATOM   5383  C CA   . ALA B 1 331 ? 0.702   100.490 28.497  1.00 8.75   ? 331 ALA B CA   1 
ATOM   5384  C C    . ALA B 1 331 ? 0.015   99.309  27.913  1.00 10.78  ? 331 ALA B C    1 
ATOM   5385  O O    . ALA B 1 331 ? 0.192   98.199  28.375  1.00 11.01  ? 331 ALA B O    1 
ATOM   5386  C CB   . ALA B 1 331 ? 1.916   100.051 29.210  1.00 8.96   ? 331 ALA B CB   1 
ATOM   5387  N N    . PRO B 1 332 ? -0.803  99.538  26.838  1.00 11.83  ? 332 PRO B N    1 
ATOM   5388  C CA   . PRO B 1 332 ? -1.525  98.390  26.376  1.00 13.97  ? 332 PRO B CA   1 
ATOM   5389  C C    . PRO B 1 332 ? -0.562  97.457  25.750  1.00 19.78  ? 332 PRO B C    1 
ATOM   5390  O O    . PRO B 1 332 ? 0.399   97.900  25.235  1.00 21.92  ? 332 PRO B O    1 
ATOM   5391  C CB   . PRO B 1 332 ? -2.402  98.989  25.308  1.00 13.11  ? 332 PRO B CB   1 
ATOM   5392  C CG   . PRO B 1 332 ? -2.616  100.387 25.696  1.00 11.51  ? 332 PRO B CG   1 
ATOM   5393  C CD   . PRO B 1 332 ? -1.208  100.702 26.001  1.00 19.39  ? 332 PRO B CD   1 
ATOM   5394  N N    . PRO B 1 333 ? -0.829  96.107  25.727  1.00 23.42  ? 333 PRO B N    1 
ATOM   5395  C CA   . PRO B 1 333 ? 0.238   95.243  25.187  1.00 19.48  ? 333 PRO B CA   1 
ATOM   5396  C C    . PRO B 1 333 ? 0.558   95.502  23.746  1.00 21.02  ? 333 PRO B C    1 
ATOM   5397  O O    . PRO B 1 333 ? 1.538   95.005  23.227  1.00 19.25  ? 333 PRO B O    1 
ATOM   5398  C CB   . PRO B 1 333 ? -0.374  93.857  25.302  1.00 19.89  ? 333 PRO B CB   1 
ATOM   5399  C CG   . PRO B 1 333 ? -1.439  93.956  26.324  1.00 20.58  ? 333 PRO B CG   1 
ATOM   5400  C CD   . PRO B 1 333 ? -2.029  95.276  26.022  1.00 15.52  ? 333 PRO B CD   1 
ATOM   5401  N N    . GLU B 1 334 ? -0.252  96.304  23.097  1.00 23.69  ? 334 GLU B N    1 
ATOM   5402  C CA   . GLU B 1 334 ? -0.090  96.592  21.698  1.00 21.03  ? 334 GLU B CA   1 
ATOM   5403  C C    . GLU B 1 334 ? 0.370   97.951  21.552  1.00 23.07  ? 334 GLU B C    1 
ATOM   5404  O O    . GLU B 1 334 ? -0.194  98.699  20.803  1.00 28.33  ? 334 GLU B O    1 
ATOM   5405  C CB   . GLU B 1 334 ? -1.442  96.554  21.014  1.00 23.99  ? 334 GLU B CB   1 
ATOM   5406  C CG   . GLU B 1 334 ? -2.140  95.200  21.005  1.00 26.30  ? 334 GLU B CG   1 
ATOM   5407  C CD   . GLU B 1 334 ? -2.931  94.934  22.253  1.00 28.98  ? 334 GLU B CD   1 
ATOM   5408  O OE1  . GLU B 1 334 ? -2.888  95.786  23.152  1.00 29.48  ? 334 GLU B OE1  1 
ATOM   5409  O OE2  . GLU B 1 334 ? -3.578  93.878  22.337  1.00 46.55  ? 334 GLU B OE2  1 
ATOM   5410  N N    . ARG B 1 335 ? 1.415   98.292  22.277  1.00 17.01  ? 335 ARG B N    1 
ATOM   5411  C CA   . ARG B 1 335 ? 1.968   99.605  22.196  1.00 13.83  ? 335 ARG B CA   1 
ATOM   5412  C C    . ARG B 1 335 ? 2.937   99.619  21.108  1.00 12.93  ? 335 ARG B C    1 
ATOM   5413  O O    . ARG B 1 335 ? 3.293   100.654 20.637  1.00 14.93  ? 335 ARG B O    1 
ATOM   5414  C CB   . ARG B 1 335 ? 2.523   100.083 23.516  1.00 12.88  ? 335 ARG B CB   1 
ATOM   5415  C CG   . ARG B 1 335 ? 3.306   99.115  24.339  1.00 14.21  ? 335 ARG B CG   1 
ATOM   5416  C CD   . ARG B 1 335 ? 3.144   99.428  25.804  1.00 11.34  ? 335 ARG B CD   1 
ATOM   5417  N NE   . ARG B 1 335 ? 4.088   98.718  26.656  1.00 14.82  ? 335 ARG B NE   1 
ATOM   5418  C CZ   . ARG B 1 335 ? 3.898   97.518  27.187  1.00 14.88  ? 335 ARG B CZ   1 
ATOM   5419  N NH1  . ARG B 1 335 ? 2.786   96.852  26.961  1.00 14.44  ? 335 ARG B NH1  1 
ATOM   5420  N NH2  . ARG B 1 335 ? 4.831   96.985  27.953  1.00 15.84  ? 335 ARG B NH2  1 
ATOM   5421  N N    . LYS B 1 336 ? 3.308   98.463  20.629  1.00 13.41  ? 336 LYS B N    1 
ATOM   5422  C CA   . LYS B 1 336 ? 4.317   98.390  19.610  1.00 14.14  ? 336 LYS B CA   1 
ATOM   5423  C C    . LYS B 1 336 ? 3.689   99.006  18.439  1.00 11.78  ? 336 LYS B C    1 
ATOM   5424  O O    . LYS B 1 336 ? 4.337   99.733  17.699  1.00 11.01  ? 336 LYS B O    1 
ATOM   5425  C CB   . LYS B 1 336 ? 4.712   96.944  19.352  1.00 13.74  ? 336 LYS B CB   1 
ATOM   5426  C CG   . LYS B 1 336 ? 6.205   96.733  19.224  1.00 20.56  ? 336 LYS B CG   1 
ATOM   5427  C CD   . LYS B 1 336 ? 6.592   95.301  19.553  1.00 34.22  ? 336 LYS B CD   1 
ATOM   5428  C CE   . LYS B 1 336 ? 8.066   95.195  19.934  1.00 53.71  ? 336 LYS B CE   1 
ATOM   5429  N NZ   . LYS B 1 336 ? 8.376   94.056  20.852  1.00 26.41  ? 336 LYS B NZ   1 
ATOM   5430  N N    . TYR B 1 337 ? 2.404   98.759  18.281  1.00 10.29  ? 337 TYR B N    1 
ATOM   5431  C CA   . TYR B 1 337 ? 1.687   99.244  17.141  1.00 15.02  ? 337 TYR B CA   1 
ATOM   5432  C C    . TYR B 1 337 ? 0.411   99.884  17.558  1.00 19.65  ? 337 TYR B C    1 
ATOM   5433  O O    . TYR B 1 337 ? -0.636  99.383  17.245  1.00 20.67  ? 337 TYR B O    1 
ATOM   5434  C CB   . TYR B 1 337 ? 1.333   98.019  16.344  1.00 14.75  ? 337 TYR B CB   1 
ATOM   5435  C CG   . TYR B 1 337 ? 2.478   97.159  15.880  1.00 9.10   ? 337 TYR B CG   1 
ATOM   5436  C CD1  . TYR B 1 337 ? 3.409   97.630  14.996  1.00 8.42   ? 337 TYR B CD1  1 
ATOM   5437  C CD2  . TYR B 1 337 ? 2.598   95.860  16.304  1.00 11.30  ? 337 TYR B CD2  1 
ATOM   5438  C CE1  . TYR B 1 337 ? 4.450   96.846  14.572  1.00 9.12   ? 337 TYR B CE1  1 
ATOM   5439  C CE2  . TYR B 1 337 ? 3.635   95.068  15.880  1.00 8.35   ? 337 TYR B CE2  1 
ATOM   5440  C CZ   . TYR B 1 337 ? 4.556   95.572  15.015  1.00 7.06   ? 337 TYR B CZ   1 
ATOM   5441  O OH   . TYR B 1 337 ? 5.591   94.782  14.595  1.00 8.37   ? 337 TYR B OH   1 
ATOM   5442  N N    . SER B 1 338 ? 0.496   101.024 18.235  1.00 17.02  ? 338 SER B N    1 
ATOM   5443  C CA   . SER B 1 338 ? -0.677  101.702 18.736  1.00 18.64  ? 338 SER B CA   1 
ATOM   5444  C C    . SER B 1 338 ? -0.890  102.882 17.901  1.00 19.99  ? 338 SER B C    1 
ATOM   5445  O O    . SER B 1 338 ? -1.971  103.412 17.845  1.00 16.17  ? 338 SER B O    1 
ATOM   5446  C CB   . SER B 1 338 ? -0.417  102.155 20.138  1.00 20.53  ? 338 SER B CB   1 
ATOM   5447  O OG   . SER B 1 338 ? -1.155  101.393 21.076  1.00 30.64  ? 338 SER B OG   1 
ATOM   5448  N N    . VAL B 1 339 ? 0.146   103.288 17.194  1.00 21.58  ? 339 VAL B N    1 
ATOM   5449  C CA   . VAL B 1 339 ? 0.048   104.417 16.310  1.00 13.04  ? 339 VAL B CA   1 
ATOM   5450  C C    . VAL B 1 339 ? -0.637  103.842 15.153  1.00 12.95  ? 339 VAL B C    1 
ATOM   5451  O O    . VAL B 1 339 ? -1.350  104.508 14.441  1.00 14.72  ? 339 VAL B O    1 
ATOM   5452  C CB   . VAL B 1 339 ? 1.422   104.908 15.939  1.00 8.59   ? 339 VAL B CB   1 
ATOM   5453  C CG1  . VAL B 1 339 ? 1.329   106.043 14.974  1.00 14.48  ? 339 VAL B CG1  1 
ATOM   5454  C CG2  . VAL B 1 339 ? 2.261   105.242 17.147  1.00 6.79   ? 339 VAL B CG2  1 
ATOM   5455  N N    . TRP B 1 340 ? -0.449  102.555 14.980  1.00 11.94  ? 340 TRP B N    1 
ATOM   5456  C CA   . TRP B 1 340 ? -1.056  101.858 13.883  1.00 15.96  ? 340 TRP B CA   1 
ATOM   5457  C C    . TRP B 1 340 ? -2.457  101.555 14.143  1.00 16.36  ? 340 TRP B C    1 
ATOM   5458  O O    . TRP B 1 340 ? -3.300  101.876 13.366  1.00 12.77  ? 340 TRP B O    1 
ATOM   5459  C CB   . TRP B 1 340 ? -0.414  100.522 13.720  1.00 18.26  ? 340 TRP B CB   1 
ATOM   5460  C CG   . TRP B 1 340 ? -1.103  99.733  12.733  1.00 17.33  ? 340 TRP B CG   1 
ATOM   5461  C CD1  . TRP B 1 340 ? -1.889  98.635  12.930  1.00 21.04  ? 340 TRP B CD1  1 
ATOM   5462  C CD2  . TRP B 1 340 ? -1.141  100.013 11.360  1.00 12.43  ? 340 TRP B CD2  1 
ATOM   5463  N NE1  . TRP B 1 340 ? -2.408  98.217  11.744  1.00 13.97  ? 340 TRP B NE1  1 
ATOM   5464  C CE2  . TRP B 1 340 ? -1.953  99.050  10.762  1.00 14.02  ? 340 TRP B CE2  1 
ATOM   5465  C CE3  . TRP B 1 340 ? -0.556  100.989 10.568  1.00 14.20  ? 340 TRP B CE3  1 
ATOM   5466  C CZ2  . TRP B 1 340 ? -2.185  99.040  9.435   1.00 18.82  ? 340 TRP B CZ2  1 
ATOM   5467  C CZ3  . TRP B 1 340 ? -0.783  100.968 9.278   1.00 15.94  ? 340 TRP B CZ3  1 
ATOM   5468  C CH2  . TRP B 1 340 ? -1.603  100.025 8.712   1.00 17.48  ? 340 TRP B CH2  1 
ATOM   5469  N N    . ILE B 1 341 ? -2.705  100.837 15.218  1.00 17.43  ? 341 ILE B N    1 
ATOM   5470  C CA   . ILE B 1 341 ? -4.030  100.405 15.544  1.00 13.90  ? 341 ILE B CA   1 
ATOM   5471  C C    . ILE B 1 341 ? -4.937  101.577 15.548  1.00 13.61  ? 341 ILE B C    1 
ATOM   5472  O O    . ILE B 1 341 ? -6.003  101.489 15.053  1.00 16.71  ? 341 ILE B O    1 
ATOM   5473  C CB   . ILE B 1 341 ? -4.026  99.539  16.801  1.00 9.04   ? 341 ILE B CB   1 
ATOM   5474  C CG1  . ILE B 1 341 ? -3.763  98.089  16.433  1.00 10.87  ? 341 ILE B CG1  1 
ATOM   5475  C CG2  . ILE B 1 341 ? -5.326  99.636  17.572  1.00 10.13  ? 341 ILE B CG2  1 
ATOM   5476  C CD1  . ILE B 1 341 ? -3.949  97.141  17.590  1.00 13.66  ? 341 ILE B CD1  1 
ATOM   5477  N N    . GLY B 1 342 ? -4.459  102.725 15.933  1.00 11.34  ? 342 GLY B N    1 
ATOM   5478  C CA   . GLY B 1 342 ? -5.296  103.899 16.014  1.00 13.90  ? 342 GLY B CA   1 
ATOM   5479  C C    . GLY B 1 342 ? -5.369  104.665 14.759  1.00 14.70  ? 342 GLY B C    1 
ATOM   5480  O O    . GLY B 1 342 ? -6.103  105.615 14.646  1.00 14.51  ? 342 GLY B O    1 
ATOM   5481  N N    . GLY B 1 343 ? -4.579  104.255 13.802  1.00 14.60  ? 343 GLY B N    1 
ATOM   5482  C CA   . GLY B 1 343 ? -4.628  104.878 12.518  1.00 15.33  ? 343 GLY B CA   1 
ATOM   5483  C C    . GLY B 1 343 ? -5.601  104.029 11.798  1.00 20.48  ? 343 GLY B C    1 
ATOM   5484  O O    . GLY B 1 343 ? -6.413  104.545 11.071  1.00 21.92  ? 343 GLY B O    1 
ATOM   5485  N N    . SER B 1 344 ? -5.546  102.723 12.006  1.00 20.77  ? 344 SER B N    1 
ATOM   5486  C CA   . SER B 1 344 ? -6.552  101.845 11.451  1.00 18.21  ? 344 SER B CA   1 
ATOM   5487  C C    . SER B 1 344 ? -7.919  102.314 11.929  1.00 17.90  ? 344 SER B C    1 
ATOM   5488  O O    . SER B 1 344 ? -8.799  102.467 11.131  1.00 18.18  ? 344 SER B O    1 
ATOM   5489  C CB   . SER B 1 344 ? -6.269  100.415 11.833  1.00 13.17  ? 344 SER B CB   1 
ATOM   5490  O OG   . SER B 1 344 ? -5.087  99.949  11.230  1.00 13.18  ? 344 SER B OG   1 
ATOM   5491  N N    . ILE B 1 345 ? -8.095  102.603 13.204  1.00 13.83  ? 345 ILE B N    1 
ATOM   5492  C CA   . ILE B 1 345 ? -9.359  103.118 13.736  1.00 15.09  ? 345 ILE B CA   1 
ATOM   5493  C C    . ILE B 1 345 ? -9.843  104.413 13.167  1.00 17.98  ? 345 ILE B C    1 
ATOM   5494  O O    . ILE B 1 345 ? -10.952 104.484 12.705  1.00 20.22  ? 345 ILE B O    1 
ATOM   5495  C CB   . ILE B 1 345 ? -9.302  103.307 15.248  1.00 17.93  ? 345 ILE B CB   1 
ATOM   5496  C CG1  . ILE B 1 345 ? -8.955  102.012 15.960  1.00 19.93  ? 345 ILE B CG1  1 
ATOM   5497  C CG2  . ILE B 1 345 ? -10.647 103.737 15.796  1.00 29.18  ? 345 ILE B CG2  1 
ATOM   5498  C CD1  . ILE B 1 345 ? -8.641  102.222 17.421  1.00 18.07  ? 345 ILE B CD1  1 
ATOM   5499  N N    . LEU B 1 346 ? -9.038  105.457 13.201  1.00 16.03  ? 346 LEU B N    1 
ATOM   5500  C CA   . LEU B 1 346 ? -9.406  106.746 12.657  1.00 14.24  ? 346 LEU B CA   1 
ATOM   5501  C C    . LEU B 1 346 ? -9.870  106.539 11.278  1.00 19.28  ? 346 LEU B C    1 
ATOM   5502  O O    . LEU B 1 346 ? -10.917 106.998 10.933  1.00 24.54  ? 346 LEU B O    1 
ATOM   5503  C CB   . LEU B 1 346 ? -8.236  107.703 12.688  1.00 11.46  ? 346 LEU B CB   1 
ATOM   5504  C CG   . LEU B 1 346 ? -8.320  109.069 12.050  1.00 13.61  ? 346 LEU B CG   1 
ATOM   5505  C CD1  . LEU B 1 346 ? -9.564  109.765 12.515  1.00 11.04  ? 346 LEU B CD1  1 
ATOM   5506  C CD2  . LEU B 1 346 ? -7.103  109.907 12.363  1.00 16.23  ? 346 LEU B CD2  1 
ATOM   5507  N N    . ALA B 1 347 ? -9.153  105.777 10.485  1.00 16.77  ? 347 ALA B N    1 
ATOM   5508  C CA   . ALA B 1 347 ? -9.503  105.592 9.088   1.00 14.93  ? 347 ALA B CA   1 
ATOM   5509  C C    . ALA B 1 347 ? -10.715 104.730 8.831   1.00 17.72  ? 347 ALA B C    1 
ATOM   5510  O O    . ALA B 1 347 ? -11.261 104.749 7.745   1.00 16.25  ? 347 ALA B O    1 
ATOM   5511  C CB   . ALA B 1 347 ? -8.317  105.032 8.388   1.00 14.01  ? 347 ALA B CB   1 
ATOM   5512  N N    . SER B 1 348 ? -11.130 103.953 9.821   1.00 18.84  ? 348 SER B N    1 
ATOM   5513  C CA   . SER B 1 348 ? -12.265 103.057 9.712   1.00 15.43  ? 348 SER B CA   1 
ATOM   5514  C C    . SER B 1 348 ? -13.462 103.653 10.371  1.00 11.88  ? 348 SER B C    1 
ATOM   5515  O O    . SER B 1 348 ? -14.498 103.046 10.490  1.00 10.63  ? 348 SER B O    1 
ATOM   5516  C CB   . SER B 1 348 ? -11.911 101.789 10.442  1.00 13.28  ? 348 SER B CB   1 
ATOM   5517  O OG   . SER B 1 348 ? -12.071 101.954 11.826  1.00 28.95  ? 348 SER B OG   1 
ATOM   5518  N N    . LEU B 1 349 ? -13.323 104.870 10.806  1.00 15.08  ? 349 LEU B N    1 
ATOM   5519  C CA   . LEU B 1 349 ? -14.400 105.529 11.455  1.00 24.65  ? 349 LEU B CA   1 
ATOM   5520  C C    . LEU B 1 349 ? -15.209 106.079 10.363  1.00 20.64  ? 349 LEU B C    1 
ATOM   5521  O O    . LEU B 1 349 ? -14.728 106.314 9.291   1.00 24.13  ? 349 LEU B O    1 
ATOM   5522  C CB   . LEU B 1 349 ? -13.899 106.627 12.395  1.00 27.29  ? 349 LEU B CB   1 
ATOM   5523  C CG   . LEU B 1 349 ? -13.393 106.299 13.789  1.00 22.37  ? 349 LEU B CG   1 
ATOM   5524  C CD1  . LEU B 1 349 ? -13.334 107.580 14.575  1.00 19.89  ? 349 LEU B CD1  1 
ATOM   5525  C CD2  . LEU B 1 349 ? -14.231 105.253 14.493  1.00 24.80  ? 349 LEU B CD2  1 
ATOM   5526  N N    . SER B 1 350 ? -16.450 106.376 10.632  1.00 20.61  ? 350 SER B N    1 
ATOM   5527  C CA   . SER B 1 350 ? -17.328 106.774 9.590   1.00 25.86  ? 350 SER B CA   1 
ATOM   5528  C C    . SER B 1 350 ? -17.589 108.222 9.536   1.00 28.65  ? 350 SER B C    1 
ATOM   5529  O O    . SER B 1 350 ? -18.315 108.689 8.680   1.00 28.41  ? 350 SER B O    1 
ATOM   5530  C CB   . SER B 1 350 ? -18.613 106.061 9.849   1.00 34.47  ? 350 SER B CB   1 
ATOM   5531  O OG   . SER B 1 350 ? -18.393 104.874 10.588  1.00 30.54  ? 350 SER B OG   1 
ATOM   5532  N N    . THR B 1 351 ? -17.006 108.963 10.456  1.00 33.73  ? 351 THR B N    1 
ATOM   5533  C CA   . THR B 1 351 ? -17.164 110.404 10.485  1.00 32.96  ? 351 THR B CA   1 
ATOM   5534  C C    . THR B 1 351 ? -15.957 110.964 9.821   1.00 29.24  ? 351 THR B C    1 
ATOM   5535  O O    . THR B 1 351 ? -15.865 112.151 9.597   1.00 29.54  ? 351 THR B O    1 
ATOM   5536  C CB   . THR B 1 351 ? -17.262 110.898 11.926  1.00 21.31  ? 351 THR B CB   1 
ATOM   5537  O OG1  . THR B 1 351 ? -16.182 110.355 12.680  1.00 28.47  ? 351 THR B OG1  1 
ATOM   5538  C CG2  . THR B 1 351 ? -18.545 110.426 12.541  1.00 24.59  ? 351 THR B CG2  1 
ATOM   5539  N N    . PHE B 1 352 ? -15.043 110.093 9.452   1.00 25.33  ? 352 PHE B N    1 
ATOM   5540  C CA   . PHE B 1 352 ? -13.783 110.529 8.916   1.00 28.17  ? 352 PHE B CA   1 
ATOM   5541  C C    . PHE B 1 352 ? -13.880 110.759 7.461   1.00 31.93  ? 352 PHE B C    1 
ATOM   5542  O O    . PHE B 1 352 ? -12.979 111.307 6.855   1.00 29.38  ? 352 PHE B O    1 
ATOM   5543  C CB   . PHE B 1 352 ? -12.738 109.444 9.207   1.00 19.43  ? 352 PHE B CB   1 
ATOM   5544  C CG   . PHE B 1 352 ? -11.324 109.880 8.995   1.00 16.95  ? 352 PHE B CG   1 
ATOM   5545  C CD1  . PHE B 1 352 ? -10.892 111.117 9.420   1.00 17.80  ? 352 PHE B CD1  1 
ATOM   5546  C CD2  . PHE B 1 352 ? -10.425 109.041 8.384   1.00 12.59  ? 352 PHE B CD2  1 
ATOM   5547  C CE1  . PHE B 1 352 ? -9.595  111.512 9.218   1.00 15.70  ? 352 PHE B CE1  1 
ATOM   5548  C CE2  . PHE B 1 352 ? -9.126  109.428 8.185   1.00 11.54  ? 352 PHE B CE2  1 
ATOM   5549  C CZ   . PHE B 1 352 ? -8.714  110.665 8.599   1.00 14.73  ? 352 PHE B CZ   1 
ATOM   5550  N N    . GLN B 1 353 ? -15.006 110.432 6.884   1.00 27.42  ? 353 GLN B N    1 
ATOM   5551  C CA   . GLN B 1 353 ? -15.078 110.499 5.470   1.00 22.80  ? 353 GLN B CA   1 
ATOM   5552  C C    . GLN B 1 353 ? -14.810 111.890 5.054   1.00 32.19  ? 353 GLN B C    1 
ATOM   5553  O O    . GLN B 1 353 ? -14.262 112.122 3.994   1.00 42.52  ? 353 GLN B O    1 
ATOM   5554  C CB   . GLN B 1 353 ? -16.378 109.974 4.999   1.00 23.71  ? 353 GLN B CB   1 
ATOM   5555  C CG   . GLN B 1 353 ? -16.634 108.547 5.456   1.00 34.70  ? 353 GLN B CG   1 
ATOM   5556  C CD   . GLN B 1 353 ? -15.490 107.595 5.146   1.00 27.42  ? 353 GLN B CD   1 
ATOM   5557  O OE1  . GLN B 1 353 ? -15.048 107.488 4.007   1.00 31.10  ? 353 GLN B OE1  1 
ATOM   5558  N NE2  . GLN B 1 353 ? -15.028 106.877 6.160   1.00 20.00  ? 353 GLN B NE2  1 
ATOM   5559  N N    . GLN B 1 354 ? -15.230 112.847 5.833   1.00 30.37  ? 354 GLN B N    1 
ATOM   5560  C CA   . GLN B 1 354 ? -14.854 114.206 5.503   1.00 36.96  ? 354 GLN B CA   1 
ATOM   5561  C C    . GLN B 1 354 ? -13.394 114.671 5.582   1.00 31.33  ? 354 GLN B C    1 
ATOM   5562  O O    . GLN B 1 354 ? -12.926 115.335 4.672   1.00 33.68  ? 354 GLN B O    1 
ATOM   5563  C CB   . GLN B 1 354 ? -15.740 115.195 6.247   1.00 35.10  ? 354 GLN B CB   1 
ATOM   5564  C CG   . GLN B 1 354 ? -15.511 116.616 5.808   1.00 36.56  ? 354 GLN B CG   1 
ATOM   5565  C CD   . GLN B 1 354 ? -16.053 116.888 4.429   1.00 42.29  ? 354 GLN B CD   1 
ATOM   5566  O OE1  . GLN B 1 354 ? -16.988 116.234 3.993   1.00 53.60  ? 354 GLN B OE1  1 
ATOM   5567  N NE2  . GLN B 1 354 ? -15.477 117.861 3.740   1.00 39.41  ? 354 GLN B NE2  1 
ATOM   5568  N N    . MET B 1 355 ? -12.643 114.332 6.617   1.00 28.73  ? 355 MET B N    1 
ATOM   5569  C CA   . MET B 1 355 ? -11.285 114.927 6.726   1.00 31.40  ? 355 MET B CA   1 
ATOM   5570  C C    . MET B 1 355 ? -10.253 114.479 5.765   1.00 20.75  ? 355 MET B C    1 
ATOM   5571  O O    . MET B 1 355 ? -9.274  115.154 5.581   1.00 22.84  ? 355 MET B O    1 
ATOM   5572  C CB   . MET B 1 355 ? -10.709 115.065 8.146   1.00 26.52  ? 355 MET B CB   1 
ATOM   5573  C CG   . MET B 1 355 ? -11.113 116.346 8.857   1.00 28.47  ? 355 MET B CG   1 
ATOM   5574  S SD   . MET B 1 355 ? -10.197 116.667 10.376  1.00 50.84  ? 355 MET B SD   1 
ATOM   5575  C CE   . MET B 1 355 ? -10.630 115.240 11.362  1.00 49.60  ? 355 MET B CE   1 
ATOM   5576  N N    . TRP B 1 356 ? -10.467 113.342 5.149   1.00 19.39  ? 356 TRP B N    1 
ATOM   5577  C CA   . TRP B 1 356 ? -9.556  112.926 4.155   1.00 19.28  ? 356 TRP B CA   1 
ATOM   5578  C C    . TRP B 1 356 ? -9.567  114.102 3.193   1.00 19.72  ? 356 TRP B C    1 
ATOM   5579  O O    . TRP B 1 356 ? -10.606 114.589 2.811   1.00 20.23  ? 356 TRP B O    1 
ATOM   5580  C CB   . TRP B 1 356 ? -10.088 111.721 3.412   1.00 13.24  ? 356 TRP B CB   1 
ATOM   5581  C CG   . TRP B 1 356 ? -10.350 110.475 4.075   1.00 10.57  ? 356 TRP B CG   1 
ATOM   5582  C CD1  . TRP B 1 356 ? -11.553 110.006 4.468   1.00 14.24  ? 356 TRP B CD1  1 
ATOM   5583  C CD2  . TRP B 1 356 ? -9.417  109.434 4.303   1.00 10.88  ? 356 TRP B CD2  1 
ATOM   5584  N NE1  . TRP B 1 356 ? -11.424 108.753 4.992   1.00 16.66  ? 356 TRP B NE1  1 
ATOM   5585  C CE2  . TRP B 1 356 ? -10.113 108.377 4.895   1.00 14.90  ? 356 TRP B CE2  1 
ATOM   5586  C CE3  . TRP B 1 356 ? -8.052  109.306 4.095   1.00 12.66  ? 356 TRP B CE3  1 
ATOM   5587  C CZ2  . TRP B 1 356 ? -9.489  107.214 5.288   1.00 13.52  ? 356 TRP B CZ2  1 
ATOM   5588  C CZ3  . TRP B 1 356 ? -7.445  108.160 4.478   1.00 14.65  ? 356 TRP B CZ3  1 
ATOM   5589  C CH2  . TRP B 1 356 ? -8.154  107.124 5.070   1.00 12.39  ? 356 TRP B CH2  1 
ATOM   5590  N N    . ILE B 1 357 ? -8.408  114.539 2.768   1.00 17.49  ? 357 ILE B N    1 
ATOM   5591  C CA   . ILE B 1 357 ? -8.310  115.668 1.904   1.00 22.72  ? 357 ILE B CA   1 
ATOM   5592  C C    . ILE B 1 357 ? -8.551  115.065 0.590   1.00 29.32  ? 357 ILE B C    1 
ATOM   5593  O O    . ILE B 1 357 ? -8.028  114.013 0.342   1.00 29.13  ? 357 ILE B O    1 
ATOM   5594  C CB   . ILE B 1 357 ? -6.865  116.210 1.930   1.00 23.70  ? 357 ILE B CB   1 
ATOM   5595  C CG1  . ILE B 1 357 ? -6.527  116.805 3.296   1.00 17.98  ? 357 ILE B CG1  1 
ATOM   5596  C CG2  . ILE B 1 357 ? -6.620  117.227 0.831   1.00 19.04  ? 357 ILE B CG2  1 
ATOM   5597  C CD1  . ILE B 1 357 ? -5.097  117.264 3.424   1.00 14.47  ? 357 ILE B CD1  1 
ATOM   5598  N N    . SER B 1 358 ? -9.317  115.710 -0.274  1.00 28.66  ? 358 SER B N    1 
ATOM   5599  C CA   . SER B 1 358 ? -9.650  115.123 -1.519  1.00 22.72  ? 358 SER B CA   1 
ATOM   5600  C C    . SER B 1 358 ? -8.730  115.650 -2.542  1.00 26.82  ? 358 SER B C    1 
ATOM   5601  O O    . SER B 1 358 ? -8.061  116.627 -2.338  1.00 27.74  ? 358 SER B O    1 
ATOM   5602  C CB   . SER B 1 358 ? -11.074 115.425 -1.848  1.00 23.95  ? 358 SER B CB   1 
ATOM   5603  O OG   . SER B 1 358 ? -11.769 115.860 -0.702  1.00 37.18  ? 358 SER B OG   1 
ATOM   5604  N N    . LYS B 1 359 ? -8.662  114.969 -3.666  1.00 29.02  ? 359 LYS B N    1 
ATOM   5605  C CA   . LYS B 1 359 ? -7.772  115.349 -4.705  1.00 25.84  ? 359 LYS B CA   1 
ATOM   5606  C C    . LYS B 1 359 ? -8.369  116.483 -5.401  1.00 30.07  ? 359 LYS B C    1 
ATOM   5607  O O    . LYS B 1 359 ? -7.784  117.034 -6.312  1.00 37.69  ? 359 LYS B O    1 
ATOM   5608  C CB   . LYS B 1 359 ? -7.629  114.200 -5.669  1.00 23.47  ? 359 LYS B CB   1 
ATOM   5609  C CG   . LYS B 1 359 ? -8.906  113.466 -6.014  1.00 24.84  ? 359 LYS B CG   1 
ATOM   5610  C CD   . LYS B 1 359 ? -8.700  112.651 -7.279  1.00 21.74  ? 359 LYS B CD   1 
ATOM   5611  C CE   . LYS B 1 359 ? -8.294  113.546 -8.437  1.00 27.57  ? 359 LYS B CE   1 
ATOM   5612  N NZ   . LYS B 1 359 ? -8.183  112.803 -9.723  1.00 18.01  ? 359 LYS B NZ   1 
ATOM   5613  N N    . GLN B 1 360 ? -9.545  116.869 -4.972  1.00 29.21  ? 360 GLN B N    1 
ATOM   5614  C CA   . GLN B 1 360 ? -10.234 117.947 -5.593  1.00 28.46  ? 360 GLN B CA   1 
ATOM   5615  C C    . GLN B 1 360 ? -9.975  119.162 -4.841  1.00 30.60  ? 360 GLN B C    1 
ATOM   5616  O O    . GLN B 1 360 ? -10.167 120.238 -5.343  1.00 36.23  ? 360 GLN B O    1 
ATOM   5617  C CB   . GLN B 1 360 ? -11.702 117.687 -5.543  1.00 33.49  ? 360 GLN B CB   1 
ATOM   5618  C CG   . GLN B 1 360 ? -12.227 116.984 -6.775  1.00 42.36  ? 360 GLN B CG   1 
ATOM   5619  C CD   . GLN B 1 360 ? -12.194 117.874 -7.989  1.00 31.92  ? 360 GLN B CD   1 
ATOM   5620  O OE1  . GLN B 1 360 ? -12.903 118.874 -8.056  1.00 29.17  ? 360 GLN B OE1  1 
ATOM   5621  N NE2  . GLN B 1 360 ? -11.360 117.520 -8.958  1.00 30.94  ? 360 GLN B NE2  1 
ATOM   5622  N N    . GLU B 1 361 ? -9.579  119.006 -3.599  1.00 29.21  ? 361 GLU B N    1 
ATOM   5623  C CA   . GLU B 1 361 ? -9.244  120.149 -2.792  1.00 25.26  ? 361 GLU B CA   1 
ATOM   5624  C C    . GLU B 1 361 ? -7.769  120.298 -2.818  1.00 23.36  ? 361 GLU B C    1 
ATOM   5625  O O    . GLU B 1 361 ? -7.241  121.265 -2.377  1.00 22.85  ? 361 GLU B O    1 
ATOM   5626  C CB   . GLU B 1 361 ? -9.694  119.939 -1.388  1.00 28.09  ? 361 GLU B CB   1 
ATOM   5627  C CG   . GLU B 1 361 ? -11.081 119.379 -1.189  1.00 36.74  ? 361 GLU B CG   1 
ATOM   5628  C CD   . GLU B 1 361 ? -11.267 118.875 0.225   1.00 32.68  ? 361 GLU B CD   1 
ATOM   5629  O OE1  . GLU B 1 361 ? -10.251 118.602 0.882   1.00 28.05  ? 361 GLU B OE1  1 
ATOM   5630  O OE2  . GLU B 1 361 ? -12.420 118.745 0.675   1.00 25.46  ? 361 GLU B OE2  1 
ATOM   5631  N N    . TYR B 1 362 ? -7.083  119.292 -3.309  1.00 20.91  ? 362 TYR B N    1 
ATOM   5632  C CA   . TYR B 1 362 ? -5.671  119.408 -3.452  1.00 21.11  ? 362 TYR B CA   1 
ATOM   5633  C C    . TYR B 1 362 ? -5.444  120.282 -4.622  1.00 32.01  ? 362 TYR B C    1 
ATOM   5634  O O    . TYR B 1 362 ? -4.647  121.191 -4.558  1.00 34.84  ? 362 TYR B O    1 
ATOM   5635  C CB   . TYR B 1 362 ? -5.016  118.089 -3.712  1.00 19.04  ? 362 TYR B CB   1 
ATOM   5636  C CG   . TYR B 1 362 ? -3.555  118.244 -4.018  1.00 18.91  ? 362 TYR B CG   1 
ATOM   5637  C CD1  . TYR B 1 362 ? -2.666  118.595 -3.028  1.00 21.13  ? 362 TYR B CD1  1 
ATOM   5638  C CD2  . TYR B 1 362 ? -3.070  118.077 -5.299  1.00 16.88  ? 362 TYR B CD2  1 
ATOM   5639  C CE1  . TYR B 1 362 ? -1.336  118.748 -3.299  1.00 18.58  ? 362 TYR B CE1  1 
ATOM   5640  C CE2  . TYR B 1 362 ? -1.739  118.248 -5.573  1.00 18.43  ? 362 TYR B CE2  1 
ATOM   5641  C CZ   . TYR B 1 362 ? -0.885  118.583 -4.565  1.00 19.92  ? 362 TYR B CZ   1 
ATOM   5642  O OH   . TYR B 1 362 ? 0.436   118.750 -4.832  1.00 18.04  ? 362 TYR B OH   1 
ATOM   5643  N N    . ASP B 1 363 ? -6.131  120.029 -5.724  1.00 32.15  ? 363 ASP B N    1 
ATOM   5644  C CA   . ASP B 1 363 ? -5.863  120.798 -6.908  1.00 24.93  ? 363 ASP B CA   1 
ATOM   5645  C C    . ASP B 1 363 ? -6.316  122.225 -6.757  1.00 30.17  ? 363 ASP B C    1 
ATOM   5646  O O    . ASP B 1 363 ? -5.725  123.125 -7.322  1.00 31.37  ? 363 ASP B O    1 
ATOM   5647  C CB   . ASP B 1 363 ? -6.367  120.094 -8.154  1.00 26.10  ? 363 ASP B CB   1 
ATOM   5648  C CG   . ASP B 1 363 ? -7.849  119.809 -8.150  1.00 45.98  ? 363 ASP B CG   1 
ATOM   5649  O OD1  . ASP B 1 363 ? -8.656  120.657 -7.732  1.00 47.28  ? 363 ASP B OD1  1 
ATOM   5650  O OD2  . ASP B 1 363 ? -8.218  118.728 -8.654  1.00 53.63  ? 363 ASP B OD2  1 
ATOM   5651  N N    . GLU B 1 364 ? -7.310  122.455 -5.923  1.00 28.54  ? 364 GLU B N    1 
ATOM   5652  C CA   . GLU B 1 364 ? -7.847  123.785 -5.725  1.00 26.76  ? 364 GLU B CA   1 
ATOM   5653  C C    . GLU B 1 364 ? -7.099  124.603 -4.731  1.00 32.07  ? 364 GLU B C    1 
ATOM   5654  O O    . GLU B 1 364 ? -7.097  125.820 -4.813  1.00 36.22  ? 364 GLU B O    1 
ATOM   5655  C CB   . GLU B 1 364 ? -9.281  123.660 -5.254  1.00 22.71  ? 364 GLU B CB   1 
ATOM   5656  C CG   . GLU B 1 364 ? -10.125 124.907 -5.380  1.00 35.60  ? 364 GLU B CG   1 
ATOM   5657  C CD   . GLU B 1 364 ? -11.227 124.954 -4.348  1.00 58.31  ? 364 GLU B CD   1 
ATOM   5658  O OE1  . GLU B 1 364 ? -12.062 124.028 -4.337  1.00 58.42  ? 364 GLU B OE1  1 
ATOM   5659  O OE2  . GLU B 1 364 ? -11.261 125.913 -3.549  1.00 62.43  ? 364 GLU B OE2  1 
ATOM   5660  N N    . SER B 1 365 ? -6.407  123.966 -3.801  1.00 30.72  ? 365 SER B N    1 
ATOM   5661  C CA   . SER B 1 365 ? -5.769  124.716 -2.720  1.00 31.40  ? 365 SER B CA   1 
ATOM   5662  C C    . SER B 1 365 ? -4.306  124.530 -2.604  1.00 27.56  ? 365 SER B C    1 
ATOM   5663  O O    . SER B 1 365 ? -3.593  125.451 -2.248  1.00 27.27  ? 365 SER B O    1 
ATOM   5664  C CB   . SER B 1 365 ? -6.406  124.360 -1.401  1.00 31.45  ? 365 SER B CB   1 
ATOM   5665  O OG   . SER B 1 365 ? -7.794  124.103 -1.525  1.00 35.31  ? 365 SER B OG   1 
ATOM   5666  N N    . GLY B 1 366 ? -3.836  123.336 -2.878  1.00 25.60  ? 366 GLY B N    1 
ATOM   5667  C CA   . GLY B 1 366 ? -2.423  123.146 -2.907  1.00 20.32  ? 366 GLY B CA   1 
ATOM   5668  C C    . GLY B 1 366 ? -2.057  122.237 -1.838  1.00 20.88  ? 366 GLY B C    1 
ATOM   5669  O O    . GLY B 1 366 ? -2.908  121.664 -1.222  1.00 24.19  ? 366 GLY B O    1 
ATOM   5670  N N    . PRO B 1 367 ? -0.715  122.030 -1.653  1.00 19.18  ? 367 PRO B N    1 
ATOM   5671  C CA   . PRO B 1 367 ? -0.384  121.220 -0.502  1.00 20.56  ? 367 PRO B CA   1 
ATOM   5672  C C    . PRO B 1 367 ? -0.362  122.001 0.763   1.00 15.89  ? 367 PRO B C    1 
ATOM   5673  O O    . PRO B 1 367 ? 0.081   121.522 1.777   1.00 14.10  ? 367 PRO B O    1 
ATOM   5674  C CB   . PRO B 1 367 ? 0.979   120.712 -0.844  1.00 19.33  ? 367 PRO B CB   1 
ATOM   5675  C CG   . PRO B 1 367 ? 1.608   121.775 -1.624  1.00 20.94  ? 367 PRO B CG   1 
ATOM   5676  C CD   . PRO B 1 367 ? 0.495   122.158 -2.520  1.00 16.97  ? 367 PRO B CD   1 
ATOM   5677  N N    . SER B 1 368 ? -0.900  123.197 0.714   1.00 17.02  ? 368 SER B N    1 
ATOM   5678  C CA   . SER B 1 368 ? -0.963  124.027 1.875   1.00 21.05  ? 368 SER B CA   1 
ATOM   5679  C C    . SER B 1 368 ? -2.368  123.913 2.378   1.00 22.81  ? 368 SER B C    1 
ATOM   5680  O O    . SER B 1 368 ? -2.994  124.894 2.737   1.00 18.69  ? 368 SER B O    1 
ATOM   5681  C CB   . SER B 1 368 ? -0.593  125.428 1.487   1.00 22.23  ? 368 SER B CB   1 
ATOM   5682  O OG   . SER B 1 368 ? 0.109   125.438 0.263   1.00 33.68  ? 368 SER B OG   1 
ATOM   5683  N N    . ILE B 1 369 ? -2.885  122.693 2.370   1.00 22.31  ? 369 ILE B N    1 
ATOM   5684  C CA   . ILE B 1 369 ? -4.230  122.419 2.832   1.00 22.92  ? 369 ILE B CA   1 
ATOM   5685  C C    . ILE B 1 369 ? -4.085  121.481 4.003   1.00 21.25  ? 369 ILE B C    1 
ATOM   5686  O O    . ILE B 1 369 ? -4.937  121.432 4.830   1.00 19.14  ? 369 ILE B O    1 
ATOM   5687  C CB   . ILE B 1 369 ? -5.108  121.820 1.695   1.00 18.26  ? 369 ILE B CB   1 
ATOM   5688  C CG1  . ILE B 1 369 ? -6.582  121.822 2.058   1.00 18.77  ? 369 ILE B CG1  1 
ATOM   5689  C CG2  . ILE B 1 369 ? -4.656  120.434 1.286   1.00 17.92  ? 369 ILE B CG2  1 
ATOM   5690  C CD1  . ILE B 1 369 ? -7.353  120.774 1.313   1.00 14.08  ? 369 ILE B CD1  1 
ATOM   5691  N N    . VAL B 1 370 ? -2.966  120.792 4.123   1.00 18.02  ? 370 VAL B N    1 
ATOM   5692  C CA   . VAL B 1 370 ? -2.718  119.906 5.226   1.00 15.03  ? 370 VAL B CA   1 
ATOM   5693  C C    . VAL B 1 370 ? -2.883  120.658 6.480   1.00 17.93  ? 370 VAL B C    1 
ATOM   5694  O O    . VAL B 1 370 ? -3.448  120.161 7.414   1.00 18.65  ? 370 VAL B O    1 
ATOM   5695  C CB   . VAL B 1 370 ? -1.308  119.309 5.134   1.00 14.31  ? 370 VAL B CB   1 
ATOM   5696  C CG1  . VAL B 1 370 ? -0.197  120.320 4.949   1.00 16.08  ? 370 VAL B CG1  1 
ATOM   5697  C CG2  . VAL B 1 370 ? -1.037  118.284 6.202   1.00 15.01  ? 370 VAL B CG2  1 
ATOM   5698  N N    . HIS B 1 371 ? -2.451  121.897 6.509   1.00 19.02  ? 371 HIS B N    1 
ATOM   5699  C CA   . HIS B 1 371 ? -2.525  122.729 7.702   1.00 23.10  ? 371 HIS B CA   1 
ATOM   5700  C C    . HIS B 1 371 ? -3.938  123.072 8.075   1.00 19.35  ? 371 HIS B C    1 
ATOM   5701  O O    . HIS B 1 371 ? -4.288  123.095 9.237   1.00 16.48  ? 371 HIS B O    1 
ATOM   5702  C CB   . HIS B 1 371 ? -1.769  123.990 7.404   1.00 16.82  ? 371 HIS B CB   1 
ATOM   5703  C CG   . HIS B 1 371 ? -0.412  123.769 6.838   1.00 13.78  ? 371 HIS B CG   1 
ATOM   5704  N ND1  . HIS B 1 371 ? 0.516   122.955 7.435   1.00 13.97  ? 371 HIS B ND1  1 
ATOM   5705  C CD2  . HIS B 1 371 ? 0.186   124.282 5.740   1.00 19.23  ? 371 HIS B CD2  1 
ATOM   5706  C CE1  . HIS B 1 371 ? 1.625   122.964 6.726   1.00 13.98  ? 371 HIS B CE1  1 
ATOM   5707  N NE2  . HIS B 1 371 ? 1.453   123.765 5.695   1.00 16.68  ? 371 HIS B NE2  1 
ATOM   5708  N N    . ARG B 1 372 ? -4.774  123.277 7.080   1.00 17.67  ? 372 ARG B N    1 
ATOM   5709  C CA   . ARG B 1 372 ? -6.153  123.609 7.301   1.00 18.46  ? 372 ARG B CA   1 
ATOM   5710  C C    . ARG B 1 372 ? -7.089  122.448 7.217   1.00 13.88  ? 372 ARG B C    1 
ATOM   5711  O O    . ARG B 1 372 ? -8.253  122.634 6.995   1.00 15.37  ? 372 ARG B O    1 
ATOM   5712  C CB   . ARG B 1 372 ? -6.538  124.645 6.279   1.00 22.96  ? 372 ARG B CB   1 
ATOM   5713  C CG   . ARG B 1 372 ? -5.574  125.814 6.198   1.00 28.39  ? 372 ARG B CG   1 
ATOM   5714  C CD   . ARG B 1 372 ? -5.695  126.537 4.872   1.00 34.84  ? 372 ARG B CD   1 
ATOM   5715  N NE   . ARG B 1 372 ? -6.270  125.673 3.849   1.00 36.50  ? 372 ARG B NE   1 
ATOM   5716  C CZ   . ARG B 1 372 ? -7.324  125.993 3.113   1.00 33.61  ? 372 ARG B CZ   1 
ATOM   5717  N NH1  . ARG B 1 372 ? -7.921  127.159 3.291   1.00 34.14  ? 372 ARG B NH1  1 
ATOM   5718  N NH2  . ARG B 1 372 ? -7.785  125.142 2.215   1.00 32.28  ? 372 ARG B NH2  1 
ATOM   5719  N N    . LYS B 1 373 ? -6.604  121.243 7.404   1.00 12.29  ? 373 LYS B N    1 
ATOM   5720  C CA   . LYS B 1 373 ? -7.441  120.079 7.321   1.00 13.71  ? 373 LYS B CA   1 
ATOM   5721  C C    . LYS B 1 373 ? -7.047  119.062 8.327   1.00 13.26  ? 373 LYS B C    1 
ATOM   5722  O O    . LYS B 1 373 ? -7.879  118.372 8.866   1.00 15.62  ? 373 LYS B O    1 
ATOM   5723  C CB   . LYS B 1 373 ? -7.347  119.481 5.930   1.00 17.64  ? 373 LYS B CB   1 
ATOM   5724  C CG   . LYS B 1 373 ? -8.540  119.706 5.035   1.00 15.76  ? 373 LYS B CG   1 
ATOM   5725  C CD   . LYS B 1 373 ? -9.532  118.582 5.183   1.00 18.53  ? 373 LYS B CD   1 
ATOM   5726  C CE   . LYS B 1 373 ? -10.703 118.816 4.264   1.00 24.49  ? 373 LYS B CE   1 
ATOM   5727  N NZ   . LYS B 1 373 ? -11.681 117.708 4.350   1.00 27.66  ? 373 LYS B NZ   1 
ATOM   5728  N N    . CYS B 1 374 ? -5.773  118.985 8.600   1.00 12.72  ? 374 CYS B N    1 
ATOM   5729  C CA   . CYS B 1 374 ? -5.290  118.037 9.538   1.00 15.54  ? 374 CYS B CA   1 
ATOM   5730  C C    . CYS B 1 374 ? -4.939  118.681 10.879  1.00 13.02  ? 374 CYS B C    1 
ATOM   5731  O O    . CYS B 1 374 ? -4.336  119.732 10.925  1.00 10.99  ? 374 CYS B O    1 
ATOM   5732  C CB   . CYS B 1 374 ? -4.186  117.256 8.882   1.00 14.74  ? 374 CYS B CB   1 
ATOM   5733  S SG   . CYS B 1 374 ? -4.591  116.525 7.290   1.00 24.23  ? 374 CYS B SG   1 
ATOM   5734  N N    . PHE B 1 375 ? -5.348  118.059 11.976  1.00 14.63  ? 375 PHE B N    1 
ATOM   5735  C CA   . PHE B 1 375 ? -5.202  118.662 13.317  1.00 22.59  ? 375 PHE B CA   1 
ATOM   5736  C C    . PHE B 1 375 ? -4.701  117.769 14.449  1.00 15.85  ? 375 PHE B C    1 
ATOM   5737  O O    . PHE B 1 375 ? -4.813  118.112 15.613  1.00 7.21   ? 375 PHE B O    1 
ATOM   5738  C CB   . PHE B 1 375 ? -6.574  119.143 13.769  1.00 21.82  ? 375 PHE B CB   1 
ATOM   5739  C CG   . PHE B 1 375 ? -7.101  120.272 12.963  1.00 21.64  ? 375 PHE B CG   1 
ATOM   5740  C CD1  . PHE B 1 375 ? -6.536  121.517 13.066  1.00 18.34  ? 375 PHE B CD1  1 
ATOM   5741  C CD2  . PHE B 1 375 ? -8.132  120.081 12.081  1.00 19.89  ? 375 PHE B CD2  1 
ATOM   5742  C CE1  . PHE B 1 375 ? -7.002  122.554 12.314  1.00 12.25  ? 375 PHE B CE1  1 
ATOM   5743  C CE2  . PHE B 1 375 ? -8.593  121.121 11.315  1.00 21.15  ? 375 PHE B CE2  1 
ATOM   5744  C CZ   . PHE B 1 375 ? -8.032  122.360 11.438  1.00 11.93  ? 375 PHE B CZ   1 
ATOM   5745  N N    . GLU C 2 7   ? 7.186   131.669 87.935  1.00 42.28  ? 25  GLU C N    1 
ATOM   5746  C CA   . GLU C 2 7   ? 6.274   130.711 87.346  1.00 40.45  ? 25  GLU C CA   1 
ATOM   5747  C C    . GLU C 2 7   ? 5.210   131.322 86.495  1.00 36.74  ? 25  GLU C C    1 
ATOM   5748  O O    . GLU C 2 7   ? 4.069   130.899 86.498  1.00 41.26  ? 25  GLU C O    1 
ATOM   5749  C CB   . GLU C 2 7   ? 5.632   129.859 88.415  1.00 38.39  ? 25  GLU C CB   1 
ATOM   5750  C CG   . GLU C 2 7   ? 6.635   129.031 89.180  1.00 49.11  ? 25  GLU C CG   1 
ATOM   5751  C CD   . GLU C 2 7   ? 6.791   127.659 88.586  1.00 57.35  ? 25  GLU C CD   1 
ATOM   5752  O OE1  . GLU C 2 7   ? 5.820   126.893 88.664  1.00 58.97  ? 25  GLU C OE1  1 
ATOM   5753  O OE2  . GLU C 2 7   ? 7.870   127.357 88.037  1.00 63.37  ? 25  GLU C OE2  1 
ATOM   5754  N N    . LEU C 2 8   ? 5.578   132.312 85.722  1.00 39.34  ? 26  LEU C N    1 
ATOM   5755  C CA   . LEU C 2 8   ? 4.657   132.936 84.813  1.00 48.24  ? 26  LEU C CA   1 
ATOM   5756  C C    . LEU C 2 8   ? 5.432   132.938 83.556  1.00 45.30  ? 26  LEU C C    1 
ATOM   5757  O O    . LEU C 2 8   ? 4.981   133.415 82.536  1.00 47.40  ? 26  LEU C O    1 
ATOM   5758  C CB   . LEU C 2 8   ? 4.472   134.392 85.166  1.00 49.83  ? 26  LEU C CB   1 
ATOM   5759  C CG   . LEU C 2 8   ? 5.711   135.284 85.100  1.00 46.90  ? 26  LEU C CG   1 
ATOM   5760  C CD1  . LEU C 2 8   ? 6.000   135.694 83.666  1.00 42.16  ? 26  LEU C CD1  1 
ATOM   5761  C CD2  . LEU C 2 8   ? 5.554   136.501 86.000  1.00 48.90  ? 26  LEU C CD2  1 
ATOM   5762  N N    . SER C 2 9   ? 6.638   132.422 83.651  1.00 47.07  ? 27  SER C N    1 
ATOM   5763  C CA   . SER C 2 9   ? 7.498   132.315 82.517  1.00 45.86  ? 27  SER C CA   1 
ATOM   5764  C C    . SER C 2 9   ? 7.459   130.876 82.095  1.00 38.55  ? 27  SER C C    1 
ATOM   5765  O O    . SER C 2 9   ? 8.093   130.507 81.160  1.00 35.66  ? 27  SER C O    1 
ATOM   5766  C CB   . SER C 2 9   ? 8.900   132.701 82.883  1.00 49.27  ? 27  SER C CB   1 
ATOM   5767  O OG   . SER C 2 9   ? 9.391   131.874 83.925  1.00 52.68  ? 27  SER C OG   1 
ATOM   5768  N N    . ILE C 2 10  ? 6.720   130.057 82.793  1.00 35.15  ? 28  ILE C N    1 
ATOM   5769  C CA   . ILE C 2 10  ? 6.582   128.675 82.442  1.00 36.59  ? 28  ILE C CA   1 
ATOM   5770  C C    . ILE C 2 10  ? 5.388   128.701 81.569  1.00 40.36  ? 28  ILE C C    1 
ATOM   5771  O O    . ILE C 2 10  ? 4.919   127.683 81.087  1.00 41.02  ? 28  ILE C O    1 
ATOM   5772  C CB   . ILE C 2 10  ? 6.351   127.844 83.685  1.00 38.89  ? 28  ILE C CB   1 
ATOM   5773  C CG1  . ILE C 2 10  ? 7.466   128.030 84.708  1.00 46.47  ? 28  ILE C CG1  1 
ATOM   5774  C CG2  . ILE C 2 10  ? 6.103   126.400 83.310  1.00 28.67  ? 28  ILE C CG2  1 
ATOM   5775  C CD1  . ILE C 2 10  ? 8.821   127.651 84.155  1.00 51.01  ? 28  ILE C CD1  1 
ATOM   5776  N N    . SER C 2 11  ? 4.846   129.886 81.401  1.00 44.00  ? 29  SER C N    1 
ATOM   5777  C CA   . SER C 2 11  ? 3.749   130.052 80.499  1.00 48.95  ? 29  SER C CA   1 
ATOM   5778  C C    . SER C 2 11  ? 4.242   130.802 79.316  1.00 43.65  ? 29  SER C C    1 
ATOM   5779  O O    . SER C 2 11  ? 3.864   130.505 78.212  1.00 50.07  ? 29  SER C O    1 
ATOM   5780  C CB   . SER C 2 11  ? 2.695   130.874 81.212  1.00 60.99  ? 29  SER C CB   1 
ATOM   5781  O OG   . SER C 2 11  ? 3.035   132.241 81.274  1.00 58.57  ? 29  SER C OG   1 
ATOM   5782  N N    . LEU C 2 12  ? 5.093   131.791 79.540  1.00 38.83  ? 30  LEU C N    1 
ATOM   5783  C CA   . LEU C 2 12  ? 5.594   132.598 78.459  1.00 39.67  ? 30  LEU C CA   1 
ATOM   5784  C C    . LEU C 2 12  ? 6.462   131.681 77.676  1.00 41.27  ? 30  LEU C C    1 
ATOM   5785  O O    . LEU C 2 12  ? 6.599   131.800 76.468  1.00 40.00  ? 30  LEU C O    1 
ATOM   5786  C CB   . LEU C 2 12  ? 6.327   133.841 78.956  1.00 29.41  ? 30  LEU C CB   1 
ATOM   5787  C CG   . LEU C 2 12  ? 7.784   133.991 79.379  1.00 32.43  ? 30  LEU C CG   1 
ATOM   5788  C CD1  . LEU C 2 12  ? 8.704   134.125 78.184  1.00 44.02  ? 30  LEU C CD1  1 
ATOM   5789  C CD2  . LEU C 2 12  ? 7.893   135.247 80.220  1.00 33.22  ? 30  LEU C CD2  1 
ATOM   5790  N N    . SER C 2 13  ? 7.013   130.710 78.357  1.00 34.45  ? 31  SER C N    1 
ATOM   5791  C CA   . SER C 2 13  ? 7.832   129.768 77.684  1.00 35.94  ? 31  SER C CA   1 
ATOM   5792  C C    . SER C 2 13  ? 7.032   129.000 76.668  1.00 35.35  ? 31  SER C C    1 
ATOM   5793  O O    . SER C 2 13  ? 7.523   128.716 75.624  1.00 35.25  ? 31  SER C O    1 
ATOM   5794  C CB   . SER C 2 13  ? 8.464   128.838 78.695  1.00 33.54  ? 31  SER C CB   1 
ATOM   5795  O OG   . SER C 2 13  ? 9.659   129.365 79.224  1.00 33.21  ? 31  SER C OG   1 
ATOM   5796  N N    . LEU C 2 14  ? 5.830   128.599 77.001  1.00 40.00  ? 32  LEU C N    1 
ATOM   5797  C CA   . LEU C 2 14  ? 4.969   127.852 76.098  1.00 44.71  ? 32  LEU C CA   1 
ATOM   5798  C C    . LEU C 2 14  ? 4.384   128.498 74.859  1.00 53.21  ? 32  LEU C C    1 
ATOM   5799  O O    . LEU C 2 14  ? 4.196   127.839 73.847  1.00 66.68  ? 32  LEU C O    1 
ATOM   5800  C CB   . LEU C 2 14  ? 3.790   127.297 76.872  1.00 42.19  ? 32  LEU C CB   1 
ATOM   5801  C CG   . LEU C 2 14  ? 3.984   126.493 78.135  1.00 45.43  ? 32  LEU C CG   1 
ATOM   5802  C CD1  . LEU C 2 14  ? 2.766   126.791 78.978  1.00 48.74  ? 32  LEU C CD1  1 
ATOM   5803  C CD2  . LEU C 2 14  ? 4.086   125.012 77.817  1.00 40.15  ? 32  LEU C CD2  1 
ATOM   5804  N N    . ASP C 2 15  ? 3.968   129.739 74.944  1.00 44.47  ? 33  ASP C N    1 
ATOM   5805  C CA   . ASP C 2 15  ? 3.284   130.325 73.821  1.00 49.53  ? 33  ASP C CA   1 
ATOM   5806  C C    . ASP C 2 15  ? 4.064   130.586 72.531  1.00 51.26  ? 33  ASP C C    1 
ATOM   5807  O O    . ASP C 2 15  ? 3.616   130.227 71.449  1.00 42.85  ? 33  ASP C O    1 
ATOM   5808  C CB   . ASP C 2 15  ? 2.748   131.653 74.320  1.00 55.82  ? 33  ASP C CB   1 
ATOM   5809  C CG   . ASP C 2 15  ? 2.272   131.598 75.749  1.00 55.44  ? 33  ASP C CG   1 
ATOM   5810  O OD1  . ASP C 2 15  ? 1.755   130.552 76.181  1.00 52.15  ? 33  ASP C OD1  1 
ATOM   5811  O OD2  . ASP C 2 15  ? 2.415   132.619 76.447  1.00 63.36  ? 33  ASP C OD2  1 
ATOM   5812  N N    . SER C 2 16  ? 5.220   131.215 72.644  1.00 48.65  ? 34  SER C N    1 
ATOM   5813  C CA   . SER C 2 16  ? 6.046   131.551 71.476  1.00 43.79  ? 34  SER C CA   1 
ATOM   5814  C C    . SER C 2 16  ? 6.780   130.508 70.663  1.00 49.28  ? 34  SER C C    1 
ATOM   5815  O O    . SER C 2 16  ? 6.847   130.589 69.442  1.00 57.01  ? 34  SER C O    1 
ATOM   5816  C CB   . SER C 2 16  ? 7.054   132.645 71.833  1.00 53.71  ? 34  SER C CB   1 
ATOM   5817  O OG   . SER C 2 16  ? 7.949   132.893 70.763  1.00 45.05  ? 34  SER C OG   1 
ATOM   5818  N N    . PRO C 2 17  ? 7.345   129.518 71.312  1.00 43.73  ? 35  PRO C N    1 
ATOM   5819  C CA   . PRO C 2 17  ? 8.168   128.613 70.550  1.00 41.80  ? 35  PRO C CA   1 
ATOM   5820  C C    . PRO C 2 17  ? 7.523   127.586 69.686  1.00 50.14  ? 35  PRO C C    1 
ATOM   5821  O O    . PRO C 2 17  ? 6.311   127.478 69.642  1.00 60.64  ? 35  PRO C O    1 
ATOM   5822  C CB   . PRO C 2 17  ? 8.899   127.877 71.662  1.00 34.04  ? 35  PRO C CB   1 
ATOM   5823  C CG   . PRO C 2 17  ? 7.912   127.796 72.733  1.00 40.12  ? 35  PRO C CG   1 
ATOM   5824  C CD   . PRO C 2 17  ? 7.421   129.199 72.740  1.00 47.16  ? 35  PRO C CD   1 
ATOM   5825  N N    . LYS C 2 18  ? 8.331   126.869 68.930  1.00 39.30  ? 36  LYS C N    1 
ATOM   5826  C CA   . LYS C 2 18  ? 7.842   125.730 68.220  1.00 27.86  ? 36  LYS C CA   1 
ATOM   5827  C C    . LYS C 2 18  ? 7.915   124.621 69.243  1.00 28.06  ? 36  LYS C C    1 
ATOM   5828  O O    . LYS C 2 18  ? 8.679   123.689 69.107  1.00 27.77  ? 36  LYS C O    1 
ATOM   5829  C CB   . LYS C 2 18  ? 8.872   125.411 67.191  1.00 29.04  ? 36  LYS C CB   1 
ATOM   5830  C CG   . LYS C 2 18  ? 10.177  126.163 67.403  1.00 27.68  ? 36  LYS C CG   1 
ATOM   5831  C CD   . LYS C 2 18  ? 11.181  125.876 66.303  1.00 32.28  ? 36  LYS C CD   1 
ATOM   5832  C CE   . LYS C 2 18  ? 12.427  126.730 66.455  1.00 27.19  ? 36  LYS C CE   1 
ATOM   5833  N NZ   . LYS C 2 18  ? 13.375  126.532 65.326  1.00 20.92  ? 36  LYS C NZ   1 
ATOM   5834  N N    . LEU C 2 19  ? 7.163   124.740 70.308  1.00 29.08  ? 37  LEU C N    1 
ATOM   5835  C CA   . LEU C 2 19  ? 7.246   123.738 71.320  1.00 25.06  ? 37  LEU C CA   1 
ATOM   5836  C C    . LEU C 2 19  ? 6.540   122.516 70.860  1.00 23.54  ? 37  LEU C C    1 
ATOM   5837  O O    . LEU C 2 19  ? 5.586   122.577 70.105  1.00 30.14  ? 37  LEU C O    1 
ATOM   5838  C CB   . LEU C 2 19  ? 6.772   124.223 72.703  1.00 30.98  ? 37  LEU C CB   1 
ATOM   5839  C CG   . LEU C 2 19  ? 5.381   124.418 73.312  1.00 33.61  ? 37  LEU C CG   1 
ATOM   5840  C CD1  . LEU C 2 19  ? 4.295   124.927 72.379  1.00 33.27  ? 37  LEU C CD1  1 
ATOM   5841  C CD2  . LEU C 2 19  ? 4.928   123.239 74.149  1.00 36.48  ? 37  LEU C CD2  1 
ATOM   5842  N N    . ASP C 2 20  ? 6.993   121.391 71.322  1.00 18.40  ? 38  ASP C N    1 
ATOM   5843  C CA   . ASP C 2 20  ? 6.469   120.164 70.875  1.00 20.77  ? 38  ASP C CA   1 
ATOM   5844  C C    . ASP C 2 20  ? 6.027   119.403 72.053  1.00 22.38  ? 38  ASP C C    1 
ATOM   5845  O O    . ASP C 2 20  ? 5.929   119.943 73.123  1.00 27.64  ? 38  ASP C O    1 
ATOM   5846  C CB   . ASP C 2 20  ? 7.555   119.437 70.077  1.00 26.48  ? 38  ASP C CB   1 
ATOM   5847  C CG   . ASP C 2 20  ? 8.758   118.966 70.916  1.00 30.04  ? 38  ASP C CG   1 
ATOM   5848  O OD1  . ASP C 2 20  ? 8.936   119.379 72.068  1.00 31.84  ? 38  ASP C OD1  1 
ATOM   5849  O OD2  . ASP C 2 20  ? 9.560   118.165 70.395  1.00 18.88  ? 38  ASP C OD2  1 
ATOM   5850  N N    . GLU C 2 21  ? 5.741   118.145 71.868  1.00 18.57  ? 39  GLU C N    1 
ATOM   5851  C CA   . GLU C 2 21  ? 5.267   117.349 72.934  1.00 21.93  ? 39  GLU C CA   1 
ATOM   5852  C C    . GLU C 2 21  ? 6.232   117.076 74.031  1.00 28.07  ? 39  GLU C C    1 
ATOM   5853  O O    . GLU C 2 21  ? 5.850   117.110 75.182  1.00 30.83  ? 39  GLU C O    1 
ATOM   5854  C CB   . GLU C 2 21  ? 4.699   116.090 72.339  1.00 26.44  ? 39  GLU C CB   1 
ATOM   5855  C CG   . GLU C 2 21  ? 3.683   116.394 71.257  1.00 25.34  ? 39  GLU C CG   1 
ATOM   5856  C CD   . GLU C 2 21  ? 2.719   115.271 71.027  1.00 23.09  ? 39  GLU C CD   1 
ATOM   5857  O OE1  . GLU C 2 21  ? 2.590   114.424 71.921  1.00 31.04  ? 39  GLU C OE1  1 
ATOM   5858  O OE2  . GLU C 2 21  ? 2.091   115.253 69.959  1.00 17.81  ? 39  GLU C OE2  1 
ATOM   5859  N N    . SER C 2 22  ? 7.500   116.879 73.718  1.00 31.88  ? 40  SER C N    1 
ATOM   5860  C CA   . SER C 2 22  ? 8.522   116.712 74.758  1.00 33.33  ? 40  SER C CA   1 
ATOM   5861  C C    . SER C 2 22  ? 8.735   117.968 75.552  1.00 28.98  ? 40  SER C C    1 
ATOM   5862  O O    . SER C 2 22  ? 8.951   117.914 76.735  1.00 28.60  ? 40  SER C O    1 
ATOM   5863  C CB   . SER C 2 22  ? 9.831   116.264 74.153  1.00 27.71  ? 40  SER C CB   1 
ATOM   5864  O OG   . SER C 2 22  ? 9.696   115.009 73.524  1.00 34.75  ? 40  SER C OG   1 
ATOM   5865  N N    . ASP C 2 23  ? 8.665   119.108 74.907  1.00 22.91  ? 41  ASP C N    1 
ATOM   5866  C CA   . ASP C 2 23  ? 8.809   120.351 75.589  1.00 23.12  ? 41  ASP C CA   1 
ATOM   5867  C C    . ASP C 2 23  ? 7.706   120.519 76.557  1.00 24.71  ? 41  ASP C C    1 
ATOM   5868  O O    . ASP C 2 23  ? 7.924   120.946 77.663  1.00 30.31  ? 41  ASP C O    1 
ATOM   5869  C CB   . ASP C 2 23  ? 8.710   121.471 74.586  1.00 30.25  ? 41  ASP C CB   1 
ATOM   5870  C CG   . ASP C 2 23  ? 9.999   121.749 73.847  1.00 38.93  ? 41  ASP C CG   1 
ATOM   5871  O OD1  . ASP C 2 23  ? 11.044  121.837 74.495  1.00 49.97  ? 41  ASP C OD1  1 
ATOM   5872  O OD2  . ASP C 2 23  ? 9.967   121.942 72.615  1.00 30.88  ? 41  ASP C OD2  1 
ATOM   5873  N N    . PHE C 2 24  ? 6.503   120.170 76.160  1.00 21.17  ? 42  PHE C N    1 
ATOM   5874  C CA   . PHE C 2 24  ? 5.352   120.316 77.019  1.00 22.57  ? 42  PHE C CA   1 
ATOM   5875  C C    . PHE C 2 24  ? 5.436   119.500 78.265  1.00 24.97  ? 42  PHE C C    1 
ATOM   5876  O O    . PHE C 2 24  ? 5.166   119.969 79.351  1.00 22.90  ? 42  PHE C O    1 
ATOM   5877  C CB   . PHE C 2 24  ? 4.165   119.769 76.286  1.00 21.86  ? 42  PHE C CB   1 
ATOM   5878  C CG   . PHE C 2 24  ? 2.849   120.187 76.858  1.00 22.87  ? 42  PHE C CG   1 
ATOM   5879  C CD1  . PHE C 2 24  ? 2.282   121.383 76.491  1.00 15.85  ? 42  PHE C CD1  1 
ATOM   5880  C CD2  . PHE C 2 24  ? 2.173   119.372 77.742  1.00 25.23  ? 42  PHE C CD2  1 
ATOM   5881  C CE1  . PHE C 2 24  ? 1.074   121.763 77.007  1.00 22.74  ? 42  PHE C CE1  1 
ATOM   5882  C CE2  . PHE C 2 24  ? 0.965   119.749 78.266  1.00 26.42  ? 42  PHE C CE2  1 
ATOM   5883  C CZ   . PHE C 2 24  ? 0.416   120.947 77.896  1.00 29.95  ? 42  PHE C CZ   1 
ATOM   5884  N N    . ILE C 2 25  ? 5.834   118.266 78.114  1.00 23.47  ? 43  ILE C N    1 
ATOM   5885  C CA   . ILE C 2 25  ? 5.918   117.422 79.246  1.00 24.79  ? 43  ILE C CA   1 
ATOM   5886  C C    . ILE C 2 25  ? 6.898   117.952 80.218  1.00 24.94  ? 43  ILE C C    1 
ATOM   5887  O O    . ILE C 2 25  ? 6.581   118.128 81.360  1.00 30.82  ? 43  ILE C O    1 
ATOM   5888  C CB   . ILE C 2 25  ? 6.434   116.078 78.781  1.00 23.54  ? 43  ILE C CB   1 
ATOM   5889  C CG1  . ILE C 2 25  ? 5.390   115.440 77.870  1.00 23.88  ? 43  ILE C CG1  1 
ATOM   5890  C CG2  . ILE C 2 25  ? 6.727   115.171 79.960  1.00 23.18  ? 43  ILE C CG2  1 
ATOM   5891  C CD1  . ILE C 2 25  ? 5.895   114.279 77.056  1.00 26.28  ? 43  ILE C CD1  1 
ATOM   5892  N N    . LEU C 2 26  ? 8.085   118.278 79.779  1.00 24.58  ? 44  LEU C N    1 
ATOM   5893  C CA   . LEU C 2 26  ? 9.122   118.744 80.664  1.00 22.73  ? 44  LEU C CA   1 
ATOM   5894  C C    . LEU C 2 26  ? 8.852   120.084 81.311  1.00 22.61  ? 44  LEU C C    1 
ATOM   5895  O O    . LEU C 2 26  ? 9.113   120.261 82.479  1.00 28.26  ? 44  LEU C O    1 
ATOM   5896  C CB   . LEU C 2 26  ? 10.414  118.798 79.879  1.00 23.54  ? 44  LEU C CB   1 
ATOM   5897  C CG   . LEU C 2 26  ? 10.886  117.533 79.187  1.00 24.27  ? 44  LEU C CG   1 
ATOM   5898  C CD1  . LEU C 2 26  ? 11.908  117.879 78.127  1.00 20.30  ? 44  LEU C CD1  1 
ATOM   5899  C CD2  . LEU C 2 26  ? 11.453  116.560 80.192  1.00 27.87  ? 44  LEU C CD2  1 
ATOM   5900  N N    . LEU C 2 27  ? 8.351   121.036 80.557  1.00 20.73  ? 45  LEU C N    1 
ATOM   5901  C CA   . LEU C 2 27  ? 8.083   122.353 81.095  1.00 23.08  ? 45  LEU C CA   1 
ATOM   5902  C C    . LEU C 2 27  ? 6.972   122.277 82.099  1.00 31.64  ? 45  LEU C C    1 
ATOM   5903  O O    . LEU C 2 27  ? 7.017   122.946 83.119  1.00 38.32  ? 45  LEU C O    1 
ATOM   5904  C CB   . LEU C 2 27  ? 7.755   123.340 79.981  1.00 20.09  ? 45  LEU C CB   1 
ATOM   5905  C CG   . LEU C 2 27  ? 8.006   124.825 80.117  1.00 20.48  ? 45  LEU C CG   1 
ATOM   5906  C CD1  . LEU C 2 27  ? 9.428   125.026 80.582  1.00 35.55  ? 45  LEU C CD1  1 
ATOM   5907  C CD2  . LEU C 2 27  ? 7.814   125.413 78.742  1.00 18.71  ? 45  LEU C CD2  1 
ATOM   5908  N N    . SER C 2 28  ? 5.939   121.503 81.815  1.00 30.26  ? 46  SER C N    1 
ATOM   5909  C CA   . SER C 2 28  ? 4.876   121.307 82.778  1.00 28.23  ? 46  SER C CA   1 
ATOM   5910  C C    . SER C 2 28  ? 5.232   120.550 84.045  1.00 24.76  ? 46  SER C C    1 
ATOM   5911  O O    . SER C 2 28  ? 4.813   120.937 85.106  1.00 27.48  ? 46  SER C O    1 
ATOM   5912  C CB   . SER C 2 28  ? 3.728   120.616 82.093  1.00 27.48  ? 46  SER C CB   1 
ATOM   5913  O OG   . SER C 2 28  ? 4.045   119.280 81.765  1.00 34.24  ? 46  SER C OG   1 
ATOM   5914  N N    . VAL C 2 29  ? 5.998   119.478 83.960  1.00 19.43  ? 47  VAL C N    1 
ATOM   5915  C CA   . VAL C 2 29  ? 6.260   118.693 85.135  1.00 21.45  ? 47  VAL C CA   1 
ATOM   5916  C C    . VAL C 2 29  ? 7.144   119.429 86.086  1.00 30.55  ? 47  VAL C C    1 
ATOM   5917  O O    . VAL C 2 29  ? 7.045   119.207 87.262  1.00 37.07  ? 47  VAL C O    1 
ATOM   5918  C CB   . VAL C 2 29  ? 6.728   117.298 84.815  1.00 20.89  ? 47  VAL C CB   1 
ATOM   5919  C CG1  . VAL C 2 29  ? 5.606   116.520 84.159  1.00 20.26  ? 47  VAL C CG1  1 
ATOM   5920  C CG2  . VAL C 2 29  ? 7.948   117.331 83.946  1.00 24.42  ? 47  VAL C CG2  1 
ATOM   5921  N N    . LYS C 2 30  ? 8.035   120.274 85.616  1.00 27.77  ? 48  LYS C N    1 
ATOM   5922  C CA   . LYS C 2 30  ? 8.798   121.169 86.493  1.00 30.39  ? 48  LYS C CA   1 
ATOM   5923  C C    . LYS C 2 30  ? 7.932   122.284 87.060  1.00 35.05  ? 48  LYS C C    1 
ATOM   5924  O O    . LYS C 2 30  ? 8.121   122.684 88.182  1.00 41.93  ? 48  LYS C O    1 
ATOM   5925  C CB   . LYS C 2 30  ? 10.056  121.693 85.820  1.00 29.62  ? 48  LYS C CB   1 
ATOM   5926  C CG   . LYS C 2 30  ? 10.959  122.516 86.720  1.00 35.46  ? 48  LYS C CG   1 
ATOM   5927  C CD   . LYS C 2 30  ? 12.409  122.071 86.677  1.00 29.99  ? 48  LYS C CD   1 
ATOM   5928  C CE   . LYS C 2 30  ? 12.597  120.749 87.396  1.00 31.13  ? 48  LYS C CE   1 
ATOM   5929  N NZ   . LYS C 2 30  ? 11.949  120.738 88.735  1.00 40.52  ? 48  LYS C NZ   1 
ATOM   5930  N N    . TYR C 2 31  ? 6.986   122.807 86.303  1.00 23.56  ? 49  TYR C N    1 
ATOM   5931  C CA   . TYR C 2 31  ? 6.084   123.776 86.859  1.00 29.33  ? 49  TYR C CA   1 
ATOM   5932  C C    . TYR C 2 31  ? 5.326   123.160 87.983  1.00 39.11  ? 49  TYR C C    1 
ATOM   5933  O O    . TYR C 2 31  ? 5.141   123.771 89.019  1.00 39.42  ? 49  TYR C O    1 
ATOM   5934  C CB   . TYR C 2 31  ? 5.065   124.158 85.811  1.00 36.04  ? 49  TYR C CB   1 
ATOM   5935  C CG   . TYR C 2 31  ? 3.810   124.844 86.324  1.00 44.59  ? 49  TYR C CG   1 
ATOM   5936  C CD1  . TYR C 2 31  ? 3.815   126.184 86.642  1.00 46.43  ? 49  TYR C CD1  1 
ATOM   5937  C CD2  . TYR C 2 31  ? 2.620   124.150 86.469  1.00 44.08  ? 49  TYR C CD2  1 
ATOM   5938  C CE1  . TYR C 2 31  ? 2.687   126.814 87.112  1.00 53.34  ? 49  TYR C CE1  1 
ATOM   5939  C CE2  . TYR C 2 31  ? 1.484   124.772 86.944  1.00 51.35  ? 49  TYR C CE2  1 
ATOM   5940  C CZ   . TYR C 2 31  ? 1.524   126.105 87.262  1.00 55.00  ? 49  TYR C CZ   1 
ATOM   5941  O OH   . TYR C 2 31  ? 0.402   126.742 87.728  1.00 55.32  ? 49  TYR C OH   1 
ATOM   5942  N N    . LEU C 2 32  ? 4.863   121.945 87.793  1.00 37.83  ? 50  LEU C N    1 
ATOM   5943  C CA   . LEU C 2 32  ? 4.066   121.288 88.804  1.00 30.30  ? 50  LEU C CA   1 
ATOM   5944  C C    . LEU C 2 32  ? 4.971   120.885 89.935  1.00 32.64  ? 50  LEU C C    1 
ATOM   5945  O O    . LEU C 2 32  ? 4.637   121.083 91.086  1.00 43.65  ? 50  LEU C O    1 
ATOM   5946  C CB   . LEU C 2 32  ? 3.372   120.055 88.239  1.00 21.40  ? 50  LEU C CB   1 
ATOM   5947  C CG   . LEU C 2 32  ? 2.329   120.150 87.138  1.00 28.29  ? 50  LEU C CG   1 
ATOM   5948  C CD1  . LEU C 2 32  ? 1.847   118.753 86.788  1.00 20.58  ? 50  LEU C CD1  1 
ATOM   5949  C CD2  . LEU C 2 32  ? 1.175   121.008 87.609  1.00 43.64  ? 50  LEU C CD2  1 
ATOM   5950  N N    . GLU C 2 33  ? 6.120   120.322 89.621  1.00 29.84  ? 51  GLU C N    1 
ATOM   5951  C CA   . GLU C 2 33  ? 7.049   119.882 90.643  1.00 34.33  ? 51  GLU C CA   1 
ATOM   5952  C C    . GLU C 2 33  ? 7.385   121.043 91.490  1.00 37.64  ? 51  GLU C C    1 
ATOM   5953  O O    . GLU C 2 33  ? 7.700   120.905 92.653  1.00 46.47  ? 51  GLU C O    1 
ATOM   5954  C CB   . GLU C 2 33  ? 8.324   119.350 90.017  1.00 31.16  ? 51  GLU C CB   1 
ATOM   5955  C CG   . GLU C 2 33  ? 8.879   118.085 90.622  1.00 27.06  ? 51  GLU C CG   1 
ATOM   5956  C CD   . GLU C 2 33  ? 9.716   117.331 89.628  1.00 36.35  ? 51  GLU C CD   1 
ATOM   5957  O OE1  . GLU C 2 33  ? 10.605  117.960 89.024  1.00 33.53  ? 51  GLU C OE1  1 
ATOM   5958  O OE2  . GLU C 2 33  ? 9.478   116.124 89.444  1.00 39.90  ? 51  GLU C OE2  1 
ATOM   5959  N N    . LYS C 2 34  ? 7.333   122.208 90.904  1.00 30.29  ? 52  LYS C N    1 
ATOM   5960  C CA   . LYS C 2 34  ? 7.686   123.368 91.641  1.00 34.27  ? 52  LYS C CA   1 
ATOM   5961  C C    . LYS C 2 34  ? 6.448   124.175 91.930  1.00 38.32  ? 52  LYS C C    1 
ATOM   5962  O O    . LYS C 2 34  ? 5.532   123.707 92.600  1.00 42.95  ? 52  LYS C O    1 
ATOM   5963  C CB   . LYS C 2 34  ? 8.671   124.192 90.849  1.00 40.15  ? 52  LYS C CB   1 
ATOM   5964  C CG   . LYS C 2 34  ? 10.065  123.603 90.796  1.00 49.97  ? 52  LYS C CG   1 
ATOM   5965  C CD   . LYS C 2 34  ? 11.092  124.670 90.466  1.00 51.90  ? 52  LYS C CD   1 
ATOM   5966  C CE   . LYS C 2 34  ? 10.821  125.297 89.112  1.00 50.30  ? 52  LYS C CE   1 
ATOM   5967  N NZ   . LYS C 2 34  ? 12.088  125.534 88.372  1.00 50.05  ? 52  LYS C NZ   1 
ATOM   5968  N N    . GLY C 2 44  ? 4.618   109.508 92.743  1.00 45.07  ? 62  GLY C N    1 
ATOM   5969  C CA   . GLY C 2 44  ? 4.028   108.325 92.157  1.00 34.23  ? 62  GLY C CA   1 
ATOM   5970  C C    . GLY C 2 44  ? 3.409   108.680 90.849  1.00 36.81  ? 62  GLY C C    1 
ATOM   5971  O O    . GLY C 2 44  ? 3.233   107.828 90.006  1.00 41.43  ? 62  GLY C O    1 
ATOM   5972  N N    . PHE C 2 45  ? 3.073   109.945 90.672  1.00 36.38  ? 63  PHE C N    1 
ATOM   5973  C CA   . PHE C 2 45  ? 2.483   110.421 89.433  1.00 37.43  ? 63  PHE C CA   1 
ATOM   5974  C C    . PHE C 2 45  ? 3.595   110.879 88.577  1.00 37.68  ? 63  PHE C C    1 
ATOM   5975  O O    . PHE C 2 45  ? 3.581   110.655 87.393  1.00 37.76  ? 63  PHE C O    1 
ATOM   5976  C CB   . PHE C 2 45  ? 1.560   111.569 89.768  1.00 37.97  ? 63  PHE C CB   1 
ATOM   5977  C CG   . PHE C 2 45  ? 0.916   112.225 88.594  1.00 51.95  ? 63  PHE C CG   1 
ATOM   5978  C CD1  . PHE C 2 45  ? -0.186  111.662 87.993  1.00 63.43  ? 63  PHE C CD1  1 
ATOM   5979  C CD2  . PHE C 2 45  ? 1.369   113.448 88.140  1.00 38.52  ? 63  PHE C CD2  1 
ATOM   5980  C CE1  . PHE C 2 45  ? -0.795  112.284 86.931  1.00 61.75  ? 63  PHE C CE1  1 
ATOM   5981  C CE2  . PHE C 2 45  ? 0.770   114.071 87.077  1.00 44.75  ? 63  PHE C CE2  1 
ATOM   5982  C CZ   . PHE C 2 45  ? -0.315  113.492 86.479  1.00 55.26  ? 63  PHE C CZ   1 
ATOM   5983  N N    . PHE C 2 46  ? 4.599   111.468 89.185  1.00 39.55  ? 64  PHE C N    1 
ATOM   5984  C CA   . PHE C 2 46  ? 5.732   111.987 88.473  1.00 36.35  ? 64  PHE C CA   1 
ATOM   5985  C C    . PHE C 2 46  ? 6.667   110.939 87.983  1.00 33.62  ? 64  PHE C C    1 
ATOM   5986  O O    . PHE C 2 46  ? 7.196   111.047 86.898  1.00 33.78  ? 64  PHE C O    1 
ATOM   5987  C CB   . PHE C 2 46  ? 6.470   112.838 89.469  1.00 39.54  ? 64  PHE C CB   1 
ATOM   5988  C CG   . PHE C 2 46  ? 6.059   114.272 89.464  1.00 40.34  ? 64  PHE C CG   1 
ATOM   5989  C CD1  . PHE C 2 46  ? 5.949   114.967 88.281  1.00 43.94  ? 64  PHE C CD1  1 
ATOM   5990  C CD2  . PHE C 2 46  ? 5.795   114.924 90.647  1.00 37.90  ? 64  PHE C CD2  1 
ATOM   5991  C CE1  . PHE C 2 46  ? 5.571   116.288 88.279  1.00 43.54  ? 64  PHE C CE1  1 
ATOM   5992  C CE2  . PHE C 2 46  ? 5.417   116.244 90.651  1.00 33.67  ? 64  PHE C CE2  1 
ATOM   5993  C CZ   . PHE C 2 46  ? 5.301   116.925 89.465  1.00 34.58  ? 64  PHE C CZ   1 
ATOM   5994  N N    . GLU C 2 47  ? 6.931   109.945 88.806  1.00 29.24  ? 65  GLU C N    1 
ATOM   5995  C CA   . GLU C 2 47  ? 7.768   108.853 88.405  1.00 29.87  ? 65  GLU C CA   1 
ATOM   5996  C C    . GLU C 2 47  ? 7.059   108.054 87.365  1.00 37.79  ? 65  GLU C C    1 
ATOM   5997  O O    . GLU C 2 47  ? 7.680   107.400 86.571  1.00 42.28  ? 65  GLU C O    1 
ATOM   5998  C CB   . GLU C 2 47  ? 8.123   107.956 89.570  1.00 28.16  ? 65  GLU C CB   1 
ATOM   5999  C CG   . GLU C 2 47  ? 9.327   107.069 89.294  1.00 28.93  ? 65  GLU C CG   1 
ATOM   6000  C CD   . GLU C 2 47  ? 10.156  106.777 90.517  1.00 40.33  ? 65  GLU C CD   1 
ATOM   6001  O OE1  . GLU C 2 47  ? 9.754   107.189 91.621  1.00 45.87  ? 65  GLU C OE1  1 
ATOM   6002  O OE2  . GLU C 2 47  ? 11.212  106.133 90.370  1.00 29.02  ? 65  GLU C OE2  1 
ATOM   6003  N N    . ASP C 2 48  ? 5.741   108.100 87.331  1.00 37.86  ? 66  ASP C N    1 
ATOM   6004  C CA   . ASP C 2 48  ? 4.984   107.381 86.308  1.00 35.84  ? 66  ASP C CA   1 
ATOM   6005  C C    . ASP C 2 48  ? 5.199   108.071 85.041  1.00 34.03  ? 66  ASP C C    1 
ATOM   6006  O O    . ASP C 2 48  ? 5.533   107.444 84.097  1.00 36.47  ? 66  ASP C O    1 
ATOM   6007  C CB   . ASP C 2 48  ? 3.505   107.310 86.595  1.00 35.00  ? 66  ASP C CB   1 
ATOM   6008  C CG   . ASP C 2 48  ? 2.816   106.192 85.856  1.00 40.08  ? 66  ASP C CG   1 
ATOM   6009  O OD1  . ASP C 2 48  ? 3.489   105.376 85.199  1.00 36.45  ? 66  ASP C OD1  1 
ATOM   6010  O OD2  . ASP C 2 48  ? 1.577   106.129 85.940  1.00 43.70  ? 66  ASP C OD2  1 
ATOM   6011  N N    . ILE C 2 49  ? 5.034   109.384 84.996  1.00 34.15  ? 67  ILE C N    1 
ATOM   6012  C CA   . ILE C 2 49  ? 5.283   110.168 83.778  1.00 29.70  ? 67  ILE C CA   1 
ATOM   6013  C C    . ILE C 2 49  ? 6.700   109.948 83.262  1.00 26.84  ? 67  ILE C C    1 
ATOM   6014  O O    . ILE C 2 49  ? 7.002   110.192 82.125  1.00 24.12  ? 67  ILE C O    1 
ATOM   6015  C CB   . ILE C 2 49  ? 4.939   111.653 83.997  1.00 18.60  ? 67  ILE C CB   1 
ATOM   6016  C CG1  . ILE C 2 49  ? 3.522   111.761 84.460  1.00 24.82  ? 67  ILE C CG1  1 
ATOM   6017  C CG2  . ILE C 2 49  ? 5.001   112.464 82.718  1.00 26.73  ? 67  ILE C CG2  1 
ATOM   6018  C CD1  . ILE C 2 49  ? 2.604   111.119 83.475  1.00 33.70  ? 67  ILE C CD1  1 
ATOM   6019  N N    . GLU C 2 50  ? 7.572   109.420 84.082  1.00 20.26  ? 68  GLU C N    1 
ATOM   6020  C CA   . GLU C 2 50  ? 8.940   109.287 83.672  1.00 25.35  ? 68  GLU C CA   1 
ATOM   6021  C C    . GLU C 2 50  ? 9.146   107.912 83.202  1.00 33.18  ? 68  GLU C C    1 
ATOM   6022  O O    . GLU C 2 50  ? 10.221  107.549 82.755  1.00 34.67  ? 68  GLU C O    1 
ATOM   6023  C CB   . GLU C 2 50  ? 9.812   109.468 84.878  1.00 28.36  ? 68  GLU C CB   1 
ATOM   6024  C CG   . GLU C 2 50  ? 10.586  110.745 84.978  1.00 29.90  ? 68  GLU C CG   1 
ATOM   6025  C CD   . GLU C 2 50  ? 11.720  110.592 85.954  1.00 35.16  ? 68  GLU C CD   1 
ATOM   6026  O OE1  . GLU C 2 50  ? 11.915  109.474 86.460  1.00 31.14  ? 68  GLU C OE1  1 
ATOM   6027  O OE2  . GLU C 2 50  ? 12.412  111.581 86.217  1.00 40.28  ? 68  GLU C OE2  1 
ATOM   6028  N N    . LYS C 2 51  ? 8.113   107.108 83.315  1.00 32.97  ? 69  LYS C N    1 
ATOM   6029  C CA   . LYS C 2 51  ? 8.180   105.727 82.865  1.00 32.12  ? 69  LYS C CA   1 
ATOM   6030  C C    . LYS C 2 51  ? 7.412   105.723 81.609  1.00 27.81  ? 69  LYS C C    1 
ATOM   6031  O O    . LYS C 2 51  ? 7.301   104.716 80.951  1.00 32.06  ? 69  LYS C O    1 
ATOM   6032  C CB   . LYS C 2 51  ? 7.507   104.808 83.862  1.00 24.98  ? 69  LYS C CB   1 
ATOM   6033  C CG   . LYS C 2 51  ? 8.261   104.569 85.148  1.00 24.73  ? 69  LYS C CG   1 
ATOM   6034  C CD   . LYS C 2 51  ? 7.294   104.056 86.194  1.00 36.34  ? 69  LYS C CD   1 
ATOM   6035  C CE   . LYS C 2 51  ? 7.950   103.892 87.549  1.00 35.94  ? 69  LYS C CE   1 
ATOM   6036  N NZ   . LYS C 2 51  ? 6.945   103.993 88.640  1.00 38.58  ? 69  LYS C NZ   1 
ATOM   6037  N N    . LEU C 2 52  ? 6.896   106.880 81.253  1.00 23.91  ? 70  LEU C N    1 
ATOM   6038  C CA   . LEU C 2 52  ? 6.112   107.002 80.063  1.00 24.66  ? 70  LEU C CA   1 
ATOM   6039  C C    . LEU C 2 52  ? 6.878   107.817 79.053  1.00 28.43  ? 70  LEU C C    1 
ATOM   6040  O O    . LEU C 2 52  ? 6.816   107.539 77.888  1.00 27.83  ? 70  LEU C O    1 
ATOM   6041  C CB   . LEU C 2 52  ? 4.782   107.641 80.408  1.00 14.52  ? 70  LEU C CB   1 
ATOM   6042  C CG   . LEU C 2 52  ? 3.894   106.942 81.409  1.00 19.29  ? 70  LEU C CG   1 
ATOM   6043  C CD1  . LEU C 2 52  ? 2.684   107.811 81.612  1.00 30.31  ? 70  LEU C CD1  1 
ATOM   6044  C CD2  . LEU C 2 52  ? 3.497   105.554 80.959  1.00 26.89  ? 70  LEU C CD2  1 
ATOM   6045  N N    . TYR C 2 53  ? 7.634   108.811 79.492  1.00 23.91  ? 71  TYR C N    1 
ATOM   6046  C CA   . TYR C 2 53  ? 8.456   109.624 78.590  1.00 22.47  ? 71  TYR C CA   1 
ATOM   6047  C C    . TYR C 2 53  ? 9.466   108.797 77.945  1.00 23.19  ? 71  TYR C C    1 
ATOM   6048  O O    . TYR C 2 53  ? 9.617   108.819 76.757  1.00 22.34  ? 71  TYR C O    1 
ATOM   6049  C CB   . TYR C 2 53  ? 9.228   110.689 79.342  1.00 22.51  ? 71  TYR C CB   1 
ATOM   6050  C CG   . TYR C 2 53  ? 9.828   111.786 78.521  1.00 19.70  ? 71  TYR C CG   1 
ATOM   6051  C CD1  . TYR C 2 53  ? 9.077   112.846 78.079  1.00 19.88  ? 71  TYR C CD1  1 
ATOM   6052  C CD2  . TYR C 2 53  ? 11.156  111.783 78.234  1.00 19.79  ? 71  TYR C CD2  1 
ATOM   6053  C CE1  . TYR C 2 53  ? 9.647   113.856 77.341  1.00 25.54  ? 71  TYR C CE1  1 
ATOM   6054  C CE2  . TYR C 2 53  ? 11.730  112.778 77.505  1.00 25.50  ? 71  TYR C CE2  1 
ATOM   6055  C CZ   . TYR C 2 53  ? 10.984  113.809 77.062  1.00 29.54  ? 71  TYR C CZ   1 
ATOM   6056  O OH   . TYR C 2 53  ? 11.626  114.773 76.339  1.00 21.92  ? 71  TYR C OH   1 
ATOM   6057  N N    . PHE C 2 54  ? 10.190  108.048 78.732  1.00 21.68  ? 72  PHE C N    1 
ATOM   6058  C CA   . PHE C 2 54  ? 11.155  107.159 78.173  1.00 23.47  ? 72  PHE C CA   1 
ATOM   6059  C C    . PHE C 2 54  ? 10.568  106.270 77.114  1.00 27.44  ? 72  PHE C C    1 
ATOM   6060  O O    . PHE C 2 54  ? 11.219  105.977 76.130  1.00 29.00  ? 72  PHE C O    1 
ATOM   6061  C CB   . PHE C 2 54  ? 11.753  106.324 79.250  1.00 19.01  ? 72  PHE C CB   1 
ATOM   6062  C CG   . PHE C 2 54  ? 12.946  105.585 78.808  1.00 19.27  ? 72  PHE C CG   1 
ATOM   6063  C CD1  . PHE C 2 54  ? 14.117  106.246 78.603  1.00 13.64  ? 72  PHE C CD1  1 
ATOM   6064  C CD2  . PHE C 2 54  ? 12.878  104.244 78.550  1.00 24.66  ? 72  PHE C CD2  1 
ATOM   6065  C CE1  . PHE C 2 54  ? 15.211  105.580 78.167  1.00 14.46  ? 72  PHE C CE1  1 
ATOM   6066  C CE2  . PHE C 2 54  ? 13.975  103.569 78.114  1.00 22.69  ? 72  PHE C CE2  1 
ATOM   6067  C CZ   . PHE C 2 54  ? 15.142  104.240 77.927  1.00 16.90  ? 72  PHE C CZ   1 
ATOM   6068  N N    . LYS C 2 55  ? 9.318   105.868 77.260  1.00 27.52  ? 73  LYS C N    1 
ATOM   6069  C CA   . LYS C 2 55  ? 8.743   104.917 76.318  1.00 33.43  ? 73  LYS C CA   1 
ATOM   6070  C C    . LYS C 2 55  ? 7.937   105.548 75.225  1.00 33.87  ? 73  LYS C C    1 
ATOM   6071  O O    . LYS C 2 55  ? 7.047   104.914 74.686  1.00 41.34  ? 73  LYS C O    1 
ATOM   6072  C CB   . LYS C 2 55  ? 7.898   103.883 77.057  1.00 32.97  ? 73  LYS C CB   1 
ATOM   6073  C CG   . LYS C 2 55  ? 8.638   103.142 78.153  1.00 38.78  ? 73  LYS C CG   1 
ATOM   6074  C CD   . LYS C 2 55  ? 7.882   101.901 78.589  1.00 34.82  ? 73  LYS C CD   1 
ATOM   6075  C CE   . LYS C 2 55  ? 6.386   102.149 78.633  1.00 40.31  ? 73  LYS C CE   1 
ATOM   6076  N NZ   . LYS C 2 55  ? 5.847   102.136 80.021  1.00 44.91  ? 73  LYS C NZ   1 
ATOM   6077  N N    . GLN C 2 56  ? 8.272   106.769 74.859  1.00 26.20  ? 74  GLN C N    1 
ATOM   6078  C CA   . GLN C 2 56  ? 7.552   107.520 73.837  1.00 28.77  ? 74  GLN C CA   1 
ATOM   6079  C C    . GLN C 2 56  ? 6.053   107.327 73.869  1.00 26.98  ? 74  GLN C C    1 
ATOM   6080  O O    . GLN C 2 56  ? 5.426   107.186 72.835  1.00 27.77  ? 74  GLN C O    1 
ATOM   6081  C CB   . GLN C 2 56  ? 8.247   107.402 72.499  1.00 34.57  ? 74  GLN C CB   1 
ATOM   6082  C CG   . GLN C 2 56  ? 9.604   108.073 72.439  1.00 25.13  ? 74  GLN C CG   1 
ATOM   6083  C CD   . GLN C 2 56  ? 10.265  107.857 71.117  1.00 28.51  ? 74  GLN C CD   1 
ATOM   6084  O OE1  . GLN C 2 56  ? 9.974   106.893 70.440  1.00 33.67  ? 74  GLN C OE1  1 
ATOM   6085  N NE2  . GLN C 2 56  ? 11.156  108.757 70.735  1.00 44.56  ? 74  GLN C NE2  1 
ATOM   6086  N N    . ASN C 2 57  ? 5.474   107.378 75.071  1.00 34.27  ? 75  ASN C N    1 
ATOM   6087  C CA   . ASN C 2 57  ? 4.032   107.222 75.317  1.00 37.49  ? 75  ASN C CA   1 
ATOM   6088  C C    . ASN C 2 57  ? 3.540   108.560 75.708  1.00 28.73  ? 75  ASN C C    1 
ATOM   6089  O O    . ASN C 2 57  ? 3.048   108.735 76.791  1.00 26.23  ? 75  ASN C O    1 
ATOM   6090  C CB   . ASN C 2 57  ? 3.875   106.364 76.554  1.00 31.09  ? 75  ASN C CB   1 
ATOM   6091  C CG   . ASN C 2 57  ? 3.230   105.036 76.285  1.00 42.95  ? 75  ASN C CG   1 
ATOM   6092  O OD1  . ASN C 2 57  ? 2.307   104.926 75.480  1.00 47.94  ? 75  ASN C OD1  1 
ATOM   6093  N ND2  . ASN C 2 57  ? 3.696   104.013 76.985  1.00 40.45  ? 75  ASN C ND2  1 
ATOM   6094  N N    . TYR C 2 58  ? 3.591   109.504 74.801  1.00 30.07  ? 76  TYR C N    1 
ATOM   6095  C CA   . TYR C 2 58  ? 3.276   110.873 75.127  1.00 31.30  ? 76  TYR C CA   1 
ATOM   6096  C C    . TYR C 2 58  ? 1.859   111.310 75.149  1.00 33.29  ? 76  TYR C C    1 
ATOM   6097  O O    . TYR C 2 58  ? 1.598   112.386 75.625  1.00 43.34  ? 76  TYR C O    1 
ATOM   6098  C CB   . TYR C 2 58  ? 3.952   111.790 74.104  1.00 31.52  ? 76  TYR C CB   1 
ATOM   6099  C CG   . TYR C 2 58  ? 5.469   111.847 74.054  1.00 29.03  ? 76  TYR C CG   1 
ATOM   6100  C CD1  . TYR C 2 58  ? 6.270   111.091 74.897  1.00 27.18  ? 76  TYR C CD1  1 
ATOM   6101  C CD2  . TYR C 2 58  ? 6.093   112.680 73.147  1.00 30.23  ? 76  TYR C CD2  1 
ATOM   6102  C CE1  . TYR C 2 58  ? 7.645   111.158 74.821  1.00 34.83  ? 76  TYR C CE1  1 
ATOM   6103  C CE2  . TYR C 2 58  ? 7.464   112.755 73.068  1.00 38.61  ? 76  TYR C CE2  1 
ATOM   6104  C CZ   . TYR C 2 58  ? 8.234   111.991 73.904  1.00 36.70  ? 76  TYR C CZ   1 
ATOM   6105  O OH   . TYR C 2 58  ? 9.593   112.073 73.812  1.00 21.80  ? 76  TYR C OH   1 
ATOM   6106  N N    . LYS C 2 59  ? 0.919   110.526 74.648  1.00 33.80  ? 77  LYS C N    1 
ATOM   6107  C CA   . LYS C 2 59  ? -0.468  110.997 74.585  1.00 28.26  ? 77  LYS C CA   1 
ATOM   6108  C C    . LYS C 2 59  ? -1.190  110.509 75.790  1.00 30.34  ? 77  LYS C C    1 
ATOM   6109  O O    . LYS C 2 59  ? -2.199  111.061 76.176  1.00 35.73  ? 77  LYS C O    1 
ATOM   6110  C CB   . LYS C 2 59  ? -1.166  110.575 73.307  1.00 26.45  ? 77  LYS C CB   1 
ATOM   6111  C CG   . LYS C 2 59  ? -0.466  111.036 72.033  1.00 25.79  ? 77  LYS C CG   1 
ATOM   6112  C CD   . LYS C 2 59  ? -0.384  112.550 71.923  1.00 24.81  ? 77  LYS C CD   1 
ATOM   6113  C CE   . LYS C 2 59  ? -1.674  113.155 71.395  1.00 25.77  ? 77  LYS C CE   1 
ATOM   6114  N NZ   . LYS C 2 59  ? -1.573  114.625 71.190  1.00 13.58  ? 77  LYS C NZ   1 
ATOM   6115  N N    . GLU C 2 60  ? -0.688  109.457 76.385  1.00 36.94  ? 78  GLU C N    1 
ATOM   6116  C CA   . GLU C 2 60  ? -1.241  108.979 77.616  1.00 33.36  ? 78  GLU C CA   1 
ATOM   6117  C C    . GLU C 2 60  ? -0.999  110.072 78.576  1.00 36.69  ? 78  GLU C C    1 
ATOM   6118  O O    . GLU C 2 60  ? -1.893  110.493 79.283  1.00 40.55  ? 78  GLU C O    1 
ATOM   6119  C CB   . GLU C 2 60  ? -0.367  107.797 78.054  1.00 27.98  ? 78  GLU C CB   1 
ATOM   6120  C CG   . GLU C 2 60  ? -0.892  106.949 79.183  1.00 41.90  ? 78  GLU C CG   1 
ATOM   6121  C CD   . GLU C 2 60  ? -0.019  105.734 79.371  1.00 55.03  ? 78  GLU C CD   1 
ATOM   6122  O OE1  . GLU C 2 60  ? 0.907   105.585 78.559  1.00 50.24  ? 78  GLU C OE1  1 
ATOM   6123  O OE2  . GLU C 2 60  ? -0.246  104.942 80.309  1.00 62.65  ? 78  GLU C OE2  1 
ATOM   6124  N N    . ALA C 2 61  ? 0.212   110.570 78.589  1.00 31.76  ? 79  ALA C N    1 
ATOM   6125  C CA   . ALA C 2 61  ? 0.588   111.571 79.522  1.00 30.01  ? 79  ALA C CA   1 
ATOM   6126  C C    . ALA C 2 61  ? 0.006   112.919 79.372  1.00 34.50  ? 79  ALA C C    1 
ATOM   6127  O O    . ALA C 2 61  ? -0.288  113.534 80.351  1.00 38.30  ? 79  ALA C O    1 
ATOM   6128  C CB   . ALA C 2 61  ? 2.072   111.646 79.559  1.00 32.76  ? 79  ALA C CB   1 
ATOM   6129  N N    . ILE C 2 62  ? -0.141  113.425 78.167  1.00 30.83  ? 80  ILE C N    1 
ATOM   6130  C CA   . ILE C 2 62  ? -0.596  114.783 78.035  1.00 27.89  ? 80  ILE C CA   1 
ATOM   6131  C C    . ILE C 2 62  ? -1.936  114.844 78.616  1.00 31.00  ? 80  ILE C C    1 
ATOM   6132  O O    . ILE C 2 62  ? -2.257  115.766 79.322  1.00 38.00  ? 80  ILE C O    1 
ATOM   6133  C CB   . ILE C 2 62  ? -0.611  115.277 76.585  1.00 34.79  ? 80  ILE C CB   1 
ATOM   6134  C CG1  . ILE C 2 62  ? -1.227  116.665 76.467  1.00 35.61  ? 80  ILE C CG1  1 
ATOM   6135  C CG2  . ILE C 2 62  ? -1.331  114.322 75.645  1.00 33.17  ? 80  ILE C CG2  1 
ATOM   6136  C CD1  . ILE C 2 62  ? -1.592  117.000 75.045  1.00 25.47  ? 80  ILE C CD1  1 
ATOM   6137  N N    . GLU C 2 63  ? -2.755  113.871 78.325  1.00 32.04  ? 81  GLU C N    1 
ATOM   6138  C CA   . GLU C 2 63  ? -4.043  113.811 78.975  1.00 43.59  ? 81  GLU C CA   1 
ATOM   6139  C C    . GLU C 2 63  ? -4.025  113.469 80.474  1.00 42.85  ? 81  GLU C C    1 
ATOM   6140  O O    . GLU C 2 63  ? -4.819  113.994 81.234  1.00 41.54  ? 81  GLU C O    1 
ATOM   6141  C CB   . GLU C 2 63  ? -5.016  113.005 78.154  1.00 41.12  ? 81  GLU C CB   1 
ATOM   6142  C CG   . GLU C 2 63  ? -5.510  113.777 76.941  1.00 44.77  ? 81  GLU C CG   1 
ATOM   6143  C CD   . GLU C 2 63  ? -6.175  115.103 77.292  1.00 38.34  ? 81  GLU C CD   1 
ATOM   6144  O OE1  . GLU C 2 63  ? -6.714  115.256 78.404  1.00 34.99  ? 81  GLU C OE1  1 
ATOM   6145  O OE2  . GLU C 2 63  ? -6.180  115.996 76.426  1.00 35.57  ? 81  GLU C OE2  1 
ATOM   6146  N N    . LYS C 2 64  ? -3.138  112.590 80.903  1.00 36.94  ? 82  LYS C N    1 
ATOM   6147  C CA   . LYS C 2 64  ? -3.016  112.311 82.309  1.00 37.15  ? 82  LYS C CA   1 
ATOM   6148  C C    . LYS C 2 64  ? -2.613  113.571 83.051  1.00 41.95  ? 82  LYS C C    1 
ATOM   6149  O O    . LYS C 2 64  ? -3.164  113.859 84.097  1.00 46.03  ? 82  LYS C O    1 
ATOM   6150  C CB   . LYS C 2 64  ? -1.965  111.219 82.500  1.00 28.94  ? 82  LYS C CB   1 
ATOM   6151  C CG   . LYS C 2 64  ? -1.799  110.714 83.917  1.00 41.24  ? 82  LYS C CG   1 
ATOM   6152  C CD   . LYS C 2 64  ? -0.656  109.718 84.033  1.00 37.53  ? 82  LYS C CD   1 
ATOM   6153  C CE   . LYS C 2 64  ? -0.884  108.468 83.203  1.00 30.55  ? 82  LYS C CE   1 
ATOM   6154  N NZ   . LYS C 2 64  ? -0.026  107.345 83.672  1.00 15.79  ? 82  LYS C NZ   1 
ATOM   6155  N N    . ILE C 2 65  ? -1.658  114.329 82.527  1.00 35.95  ? 83  ILE C N    1 
ATOM   6156  C CA   . ILE C 2 65  ? -1.215  115.568 83.151  1.00 35.15  ? 83  ILE C CA   1 
ATOM   6157  C C    . ILE C 2 65  ? -2.331  116.538 83.112  1.00 38.23  ? 83  ILE C C    1 
ATOM   6158  O O    . ILE C 2 65  ? -2.551  117.263 84.049  1.00 45.11  ? 83  ILE C O    1 
ATOM   6159  C CB   . ILE C 2 65  ? -0.038  116.179 82.403  1.00 30.40  ? 83  ILE C CB   1 
ATOM   6160  C CG1  . ILE C 2 65  ? 1.137   115.213 82.344  1.00 36.19  ? 83  ILE C CG1  1 
ATOM   6161  C CG2  . ILE C 2 65  ? 0.410   117.482 83.043  1.00 30.19  ? 83  ILE C CG2  1 
ATOM   6162  C CD1  . ILE C 2 65  ? 1.746   114.910 83.681  1.00 37.56  ? 83  ILE C CD1  1 
ATOM   6163  N N    . LEU C 2 66  ? -3.040  116.574 82.002  1.00 33.26  ? 84  LEU C N    1 
ATOM   6164  C CA   . LEU C 2 66  ? -4.145  117.497 81.850  1.00 38.12  ? 84  LEU C CA   1 
ATOM   6165  C C    . LEU C 2 66  ? -5.283  117.223 82.824  1.00 46.03  ? 84  LEU C C    1 
ATOM   6166  O O    . LEU C 2 66  ? -5.865  118.152 83.361  1.00 48.83  ? 84  LEU C O    1 
ATOM   6167  C CB   . LEU C 2 66  ? -4.582  117.530 80.408  1.00 40.59  ? 84  LEU C CB   1 
ATOM   6168  C CG   . LEU C 2 66  ? -4.089  118.747 79.627  1.00 45.19  ? 84  LEU C CG   1 
ATOM   6169  C CD1  . LEU C 2 66  ? -2.612  119.001 79.859  1.00 41.35  ? 84  LEU C CD1  1 
ATOM   6170  C CD2  . LEU C 2 66  ? -4.400  118.624 78.148  1.00 37.47  ? 84  LEU C CD2  1 
ATOM   6171  N N    . ASP C 2 67  ? -5.625  115.971 83.054  1.00 45.17  ? 85  ASP C N    1 
ATOM   6172  C CA   . ASP C 2 67  ? -6.587  115.639 84.095  1.00 44.98  ? 85  ASP C CA   1 
ATOM   6173  C C    . ASP C 2 67  ? -5.978  116.019 85.428  1.00 48.09  ? 85  ASP C C    1 
ATOM   6174  O O    . ASP C 2 67  ? -6.693  116.394 86.327  1.00 51.81  ? 85  ASP C O    1 
ATOM   6175  C CB   . ASP C 2 67  ? -6.913  114.157 84.117  1.00 43.61  ? 85  ASP C CB   1 
ATOM   6176  C CG   . ASP C 2 67  ? -8.094  113.802 83.262  1.00 55.08  ? 85  ASP C CG   1 
ATOM   6177  O OD1  . ASP C 2 67  ? -9.066  114.579 83.228  1.00 55.85  ? 85  ASP C OD1  1 
ATOM   6178  O OD2  . ASP C 2 67  ? -8.060  112.723 82.638  1.00 64.23  ? 85  ASP C OD2  1 
ATOM   6179  N N    . PHE C 2 68  ? -4.675  115.847 85.602  1.00 42.20  ? 86  PHE C N    1 
ATOM   6180  C CA   . PHE C 2 68  ? -3.989  116.198 86.848  1.00 45.78  ? 86  PHE C CA   1 
ATOM   6181  C C    . PHE C 2 68  ? -4.047  117.663 87.145  1.00 47.92  ? 86  PHE C C    1 
ATOM   6182  O O    . PHE C 2 68  ? -4.107  118.060 88.289  1.00 48.78  ? 86  PHE C O    1 
ATOM   6183  C CB   . PHE C 2 68  ? -2.537  115.766 86.822  1.00 45.11  ? 86  PHE C CB   1 
ATOM   6184  C CG   . PHE C 2 68  ? -1.914  115.627 88.174  1.00 40.68  ? 86  PHE C CG   1 
ATOM   6185  C CD1  . PHE C 2 68  ? -2.086  114.474 88.907  1.00 46.71  ? 86  PHE C CD1  1 
ATOM   6186  C CD2  . PHE C 2 68  ? -1.139  116.637 88.696  1.00 40.22  ? 86  PHE C CD2  1 
ATOM   6187  C CE1  . PHE C 2 68  ? -1.509  114.333 90.151  1.00 48.23  ? 86  PHE C CE1  1 
ATOM   6188  C CE2  . PHE C 2 68  ? -0.558  116.507 89.936  1.00 47.65  ? 86  PHE C CE2  1 
ATOM   6189  C CZ   . PHE C 2 68  ? -0.742  115.353 90.665  1.00 50.66  ? 86  PHE C CZ   1 
ATOM   6190  N N    . CYS C 2 69  ? -3.983  118.487 86.119  1.00 47.32  ? 87  CYS C N    1 
ATOM   6191  C CA   . CYS C 2 69  ? -4.039  119.922 86.307  1.00 51.41  ? 87  CYS C CA   1 
ATOM   6192  C C    . CYS C 2 69  ? -5.450  120.251 86.777  1.00 50.22  ? 87  CYS C C    1 
ATOM   6193  O O    . CYS C 2 69  ? -5.708  121.359 87.218  1.00 55.47  ? 87  CYS C O    1 
ATOM   6194  C CB   . CYS C 2 69  ? -3.611  120.677 85.036  1.00 43.51  ? 87  CYS C CB   1 
ATOM   6195  S SG   . CYS C 2 69  ? -3.543  122.474 85.114  1.00 60.02  ? 87  CYS C SG   1 
ATOM   6196  N N    . LYS C 2 70  ? -6.374  119.317 86.641  1.00 46.48  ? 88  LYS C N    1 
ATOM   6197  C CA   . LYS C 2 70  ? -7.717  119.497 87.163  1.00 49.72  ? 88  LYS C CA   1 
ATOM   6198  C C    . LYS C 2 70  ? -7.873  118.816 88.519  1.00 51.13  ? 88  LYS C C    1 
ATOM   6199  O O    . LYS C 2 70  ? -8.605  119.302 89.370  1.00 51.32  ? 88  LYS C O    1 
ATOM   6200  C CB   . LYS C 2 70  ? -8.758  118.865 86.255  1.00 54.56  ? 88  LYS C CB   1 
ATOM   6201  C CG   . LYS C 2 70  ? -8.738  119.276 84.796  1.00 61.44  ? 88  LYS C CG   1 
ATOM   6202  C CD   . LYS C 2 70  ? -10.014 118.784 84.124  1.00 51.35  ? 88  LYS C CD   1 
ATOM   6203  C CE   . LYS C 2 70  ? -9.912  118.774 82.611  1.00 39.51  ? 88  LYS C CE   1 
ATOM   6204  N NZ   . LYS C 2 70  ? -9.107  117.622 82.127  1.00 45.43  ? 88  LYS C NZ   1 
ATOM   6205  N N    . LYS C 2 71  ? -7.238  117.670 88.714  1.00 49.22  ? 89  LYS C N    1 
ATOM   6206  C CA   . LYS C 2 71  ? -7.406  116.953 89.952  1.00 44.57  ? 89  LYS C CA   1 
ATOM   6207  C C    . LYS C 2 71  ? -6.924  117.868 91.015  1.00 49.03  ? 89  LYS C C    1 
ATOM   6208  O O    . LYS C 2 71  ? -7.547  118.007 92.057  1.00 60.23  ? 89  LYS C O    1 
ATOM   6209  C CB   . LYS C 2 71  ? -6.591  115.681 89.982  1.00 40.12  ? 89  LYS C CB   1 
ATOM   6210  C CG   . LYS C 2 71  ? -7.049  114.681 91.022  1.00 32.40  ? 89  LYS C CG   1 
ATOM   6211  C CD   . LYS C 2 71  ? -6.011  113.594 91.224  1.00 40.91  ? 89  LYS C CD   1 
ATOM   6212  C CE   . LYS C 2 71  ? -6.642  112.211 91.168  1.00 41.39  ? 89  LYS C CE   1 
ATOM   6213  N NZ   . LYS C 2 71  ? -5.714  111.185 90.615  1.00 40.22  ? 89  LYS C NZ   1 
ATOM   6214  N N    . ASN C 2 72  ? -5.771  118.460 90.794  1.00 45.03  ? 90  ASN C N    1 
ATOM   6215  C CA   . ASN C 2 72  ? -5.207  119.285 91.803  1.00 39.84  ? 90  ASN C CA   1 
ATOM   6216  C C    . ASN C 2 72  ? -5.052  120.695 91.309  1.00 43.90  ? 90  ASN C C    1 
ATOM   6217  O O    . ASN C 2 72  ? -3.953  121.170 91.154  1.00 55.32  ? 90  ASN C O    1 
ATOM   6218  C CB   . ASN C 2 72  ? -3.890  118.687 92.208  1.00 41.48  ? 90  ASN C CB   1 
ATOM   6219  C CG   . ASN C 2 72  ? -4.021  117.266 92.682  1.00 47.10  ? 90  ASN C CG   1 
ATOM   6220  O OD1  . ASN C 2 72  ? -3.787  116.332 91.936  1.00 41.64  ? 90  ASN C OD1  1 
ATOM   6221  N ND2  . ASN C 2 72  ? -4.401  117.098 93.933  1.00 68.46  ? 90  ASN C ND2  1 
ATOM   6222  N N    . GLU C 2 73  ? -6.144  121.409 91.119  1.00 43.03  ? 91  GLU C N    1 
ATOM   6223  C CA   . GLU C 2 73  ? -6.027  122.803 90.729  1.00 53.81  ? 91  GLU C CA   1 
ATOM   6224  C C    . GLU C 2 73  ? -5.670  123.631 91.916  1.00 57.05  ? 91  GLU C C    1 
ATOM   6225  O O    . GLU C 2 73  ? -5.506  124.833 91.828  1.00 54.20  ? 91  GLU C O    1 
ATOM   6226  C CB   . GLU C 2 73  ? -7.302  123.378 90.138  1.00 52.11  ? 91  GLU C CB   1 
ATOM   6227  C CG   . GLU C 2 73  ? -8.116  122.467 89.260  1.00 57.00  ? 91  GLU C CG   1 
ATOM   6228  C CD   . GLU C 2 73  ? -8.539  123.138 87.976  1.00 60.75  ? 91  GLU C CD   1 
ATOM   6229  O OE1  . GLU C 2 73  ? -7.948  124.176 87.642  1.00 56.19  ? 91  GLU C OE1  1 
ATOM   6230  O OE2  . GLU C 2 73  ? -9.453  122.632 87.297  1.00 67.08  ? 91  GLU C OE2  1 
ATOM   6231  N N    . SER C 2 74  ? -5.589  122.995 93.063  1.00 62.04  ? 92  SER C N    1 
ATOM   6232  C CA   . SER C 2 74  ? -5.174  123.700 94.254  1.00 61.50  ? 92  SER C CA   1 
ATOM   6233  C C    . SER C 2 74  ? -3.687  123.806 94.190  1.00 58.57  ? 92  SER C C    1 
ATOM   6234  O O    . SER C 2 74  ? -3.030  122.905 93.679  1.00 55.80  ? 92  SER C O    1 
ATOM   6235  C CB   . SER C 2 74  ? -5.645  122.981 95.502  1.00 55.74  ? 92  SER C CB   1 
ATOM   6236  O OG   . SER C 2 74  ? -7.020  122.661 95.409  1.00 50.96  ? 92  SER C OG   1 
ATOM   6237  N N    . LEU C 2 75  ? -3.152  124.919 94.652  1.00 63.69  ? 93  LEU C N    1 
ATOM   6238  C CA   . LEU C 2 75  ? -1.720  125.191 94.540  1.00 69.42  ? 93  LEU C CA   1 
ATOM   6239  C C    . LEU C 2 75  ? -1.256  125.244 93.087  1.00 71.26  ? 93  LEU C C    1 
ATOM   6240  O O    . LEU C 2 75  ? -0.088  124.992 92.807  1.00 71.47  ? 93  LEU C O    1 
ATOM   6241  C CB   . LEU C 2 75  ? -0.853  124.288 95.423  1.00 64.44  ? 93  LEU C CB   1 
ATOM   6242  C CG   . LEU C 2 75  ? -1.055  124.464 96.930  1.00 65.93  ? 93  LEU C CG   1 
ATOM   6243  C CD1  . LEU C 2 75  ? -0.269  123.434 97.725  1.00 68.03  ? 93  LEU C CD1  1 
ATOM   6244  C CD2  . LEU C 2 75  ? -0.687  125.870 97.364  1.00 54.39  ? 93  LEU C CD2  1 
ATOM   6245  N N    . LEU C 2 76  ? -2.156  125.594 92.162  1.00 71.60  ? 94  LEU C N    1 
ATOM   6246  C CA   . LEU C 2 76  ? -1.784  125.775 90.756  1.00 60.03  ? 94  LEU C CA   1 
ATOM   6247  C C    . LEU C 2 76  ? -2.372  127.122 90.468  1.00 58.91  ? 94  LEU C C    1 
ATOM   6248  O O    . LEU C 2 76  ? -3.397  127.470 91.018  1.00 62.93  ? 94  LEU C O    1 
ATOM   6249  C CB   . LEU C 2 76  ? -2.426  124.773 89.836  1.00 53.74  ? 94  LEU C CB   1 
ATOM   6250  C CG   . LEU C 2 76  ? -1.644  123.590 89.299  1.00 56.95  ? 94  LEU C CG   1 
ATOM   6251  C CD1  . LEU C 2 76  ? -1.007  122.733 90.377  1.00 58.86  ? 94  LEU C CD1  1 
ATOM   6252  C CD2  . LEU C 2 76  ? -2.651  122.772 88.538  1.00 59.21  ? 94  LEU C CD2  1 
ATOM   6253  N N    . SER C 2 77  ? -1.723  127.887 89.601  1.00 55.98  ? 95  SER C N    1 
ATOM   6254  C CA   . SER C 2 77  ? -2.249  129.168 89.195  1.00 54.03  ? 95  SER C CA   1 
ATOM   6255  C C    . SER C 2 77  ? -3.110  128.878 88.039  1.00 60.47  ? 95  SER C C    1 
ATOM   6256  O O    . SER C 2 77  ? -2.908  127.905 87.334  1.00 62.01  ? 95  SER C O    1 
ATOM   6257  C CB   . SER C 2 77  ? -1.142  130.076 88.736  1.00 58.81  ? 95  SER C CB   1 
ATOM   6258  O OG   . SER C 2 77  ? -1.656  131.199 88.046  1.00 69.32  ? 95  SER C OG   1 
ATOM   6259  N N    . GLU C 2 78  ? -4.089  129.715 87.820  1.00 64.14  ? 96  GLU C N    1 
ATOM   6260  C CA   . GLU C 2 78  ? -5.032  129.413 86.788  1.00 57.91  ? 96  GLU C CA   1 
ATOM   6261  C C    . GLU C 2 78  ? -4.719  130.006 85.477  1.00 59.75  ? 96  GLU C C    1 
ATOM   6262  O O    . GLU C 2 78  ? -5.500  129.842 84.565  1.00 67.56  ? 96  GLU C O    1 
ATOM   6263  C CB   . GLU C 2 78  ? -6.439  129.782 87.203  1.00 61.90  ? 96  GLU C CB   1 
ATOM   6264  C CG   . GLU C 2 78  ? -6.831  129.234 88.566  1.00 61.44  ? 96  GLU C CG   1 
ATOM   6265  C CD   . GLU C 2 78  ? -6.792  127.726 88.620  1.00 60.54  ? 96  GLU C CD   1 
ATOM   6266  O OE1  . GLU C 2 78  ? -7.279  127.094 87.670  1.00 68.22  ? 96  GLU C OE1  1 
ATOM   6267  O OE2  . GLU C 2 78  ? -6.285  127.174 89.614  1.00 60.20  ? 96  GLU C OE2  1 
ATOM   6268  N N    . GLN C 2 79  ? -3.648  130.768 85.359  1.00 55.76  ? 97  GLN C N    1 
ATOM   6269  C CA   . GLN C 2 79  ? -3.267  131.206 84.034  1.00 51.70  ? 97  GLN C CA   1 
ATOM   6270  C C    . GLN C 2 79  ? -2.797  129.977 83.299  1.00 42.63  ? 97  GLN C C    1 
ATOM   6271  O O    . GLN C 2 79  ? -3.097  129.788 82.141  1.00 47.80  ? 97  GLN C O    1 
ATOM   6272  C CB   . GLN C 2 79  ? -2.204  132.288 84.082  1.00 48.00  ? 97  GLN C CB   1 
ATOM   6273  C CG   . GLN C 2 79  ? -1.973  132.969 82.744  1.00 58.17  ? 97  GLN C CG   1 
ATOM   6274  C CD   . GLN C 2 79  ? -0.573  133.528 82.590  1.00 68.39  ? 97  GLN C CD   1 
ATOM   6275  O OE1  . GLN C 2 79  ? 0.153   133.700 83.568  1.00 64.54  ? 97  GLN C OE1  1 
ATOM   6276  N NE2  . GLN C 2 79  ? -0.185  133.812 81.354  1.00 68.70  ? 97  GLN C NE2  1 
ATOM   6277  N N    . VAL C 2 80  ? -2.064  129.134 83.980  1.00 44.15  ? 98  VAL C N    1 
ATOM   6278  C CA   . VAL C 2 80  ? -1.507  127.932 83.376  1.00 54.48  ? 98  VAL C CA   1 
ATOM   6279  C C    . VAL C 2 80  ? -2.473  126.836 82.948  1.00 51.03  ? 98  VAL C C    1 
ATOM   6280  O O    . VAL C 2 80  ? -2.345  126.263 81.891  1.00 49.17  ? 98  VAL C O    1 
ATOM   6281  C CB   . VAL C 2 80  ? -0.365  127.396 84.268  1.00 51.89  ? 98  VAL C CB   1 
ATOM   6282  C CG1  . VAL C 2 80  ? 0.331   126.210 83.641  1.00 42.78  ? 98  VAL C CG1  1 
ATOM   6283  C CG2  . VAL C 2 80  ? 0.639   128.510 84.508  1.00 48.31  ? 98  VAL C CG2  1 
ATOM   6284  N N    . VAL C 2 81  ? -3.465  126.561 83.747  1.00 46.49  ? 99  VAL C N    1 
ATOM   6285  C CA   . VAL C 2 81  ? -4.443  125.578 83.358  1.00 46.78  ? 99  VAL C CA   1 
ATOM   6286  C C    . VAL C 2 81  ? -5.112  126.088 82.120  1.00 54.55  ? 99  VAL C C    1 
ATOM   6287  O O    . VAL C 2 81  ? -5.424  125.341 81.221  1.00 60.09  ? 99  VAL C O    1 
ATOM   6288  C CB   . VAL C 2 81  ? -5.511  125.464 84.440  1.00 58.57  ? 99  VAL C CB   1 
ATOM   6289  C CG1  . VAL C 2 81  ? -6.507  124.361 84.121  1.00 60.48  ? 99  VAL C CG1  1 
ATOM   6290  C CG2  . VAL C 2 81  ? -4.863  125.240 85.796  1.00 60.46  ? 99  VAL C CG2  1 
ATOM   6291  N N    . GLN C 2 82  ? -5.365  127.377 82.075  1.00 57.47  ? 100 GLN C N    1 
ATOM   6292  C CA   . GLN C 2 82  ? -5.967  127.980 80.917  1.00 54.17  ? 100 GLN C CA   1 
ATOM   6293  C C    . GLN C 2 82  ? -5.036  128.106 79.741  1.00 54.03  ? 100 GLN C C    1 
ATOM   6294  O O    . GLN C 2 82  ? -5.492  128.455 78.672  1.00 62.20  ? 100 GLN C O    1 
ATOM   6295  C CB   . GLN C 2 82  ? -6.579  129.303 81.288  1.00 57.70  ? 100 GLN C CB   1 
ATOM   6296  C CG   . GLN C 2 82  ? -7.636  129.190 82.375  1.00 60.87  ? 100 GLN C CG   1 
ATOM   6297  C CD   . GLN C 2 82  ? -8.789  128.288 81.993  1.00 68.70  ? 100 GLN C CD   1 
ATOM   6298  O OE1  . GLN C 2 82  ? -8.997  127.238 82.598  1.00 63.88  ? 100 GLN C OE1  1 
ATOM   6299  N NE2  . GLN C 2 82  ? -9.550  128.695 80.984  1.00 66.18  ? 100 GLN C NE2  1 
ATOM   6300  N N    . ARG C 2 83  ? -3.732  127.919 79.917  1.00 51.34  ? 101 ARG C N    1 
ATOM   6301  C CA   . ARG C 2 83  ? -2.829  127.865 78.767  1.00 49.90  ? 101 ARG C CA   1 
ATOM   6302  C C    . ARG C 2 83  ? -2.440  126.449 78.389  1.00 43.42  ? 101 ARG C C    1 
ATOM   6303  O O    . ARG C 2 83  ? -2.472  126.082 77.239  1.00 44.53  ? 101 ARG C O    1 
ATOM   6304  C CB   . ARG C 2 83  ? -1.560  128.636 79.034  1.00 46.05  ? 101 ARG C CB   1 
ATOM   6305  C CG   . ARG C 2 83  ? -1.417  129.907 78.218  1.00 42.50  ? 101 ARG C CG   1 
ATOM   6306  C CD   . ARG C 2 83  ? -1.251  129.578 76.748  1.00 40.88  ? 101 ARG C CD   1 
ATOM   6307  N NE   . ARG C 2 83  ? -1.323  130.764 75.905  1.00 47.36  ? 101 ARG C NE   1 
ATOM   6308  C CZ   . ARG C 2 83  ? -1.138  130.751 74.589  1.00 55.52  ? 101 ARG C CZ   1 
ATOM   6309  N NH1  . ARG C 2 83  ? -0.852  129.617 73.967  1.00 54.07  ? 101 ARG C NH1  1 
ATOM   6310  N NH2  . ARG C 2 83  ? -1.227  131.874 73.893  1.00 51.41  ? 101 ARG C NH2  1 
ATOM   6311  N N    . LEU C 2 84  ? -2.078  125.645 79.358  1.00 38.51  ? 102 LEU C N    1 
ATOM   6312  C CA   . LEU C 2 84  ? -1.621  124.298 79.085  1.00 39.01  ? 102 LEU C CA   1 
ATOM   6313  C C    . LEU C 2 84  ? -2.702  123.474 78.488  1.00 44.21  ? 102 LEU C C    1 
ATOM   6314  O O    . LEU C 2 84  ? -2.419  122.572 77.737  1.00 50.86  ? 102 LEU C O    1 
ATOM   6315  C CB   . LEU C 2 84  ? -1.078  123.618 80.329  1.00 38.48  ? 102 LEU C CB   1 
ATOM   6316  C CG   . LEU C 2 84  ? 0.287   123.920 80.921  1.00 30.03  ? 102 LEU C CG   1 
ATOM   6317  C CD1  . LEU C 2 84  ? 0.597   122.866 81.963  1.00 27.17  ? 102 LEU C CD1  1 
ATOM   6318  C CD2  . LEU C 2 84  ? 1.327   123.870 79.832  1.00 34.09  ? 102 LEU C CD2  1 
ATOM   6319  N N    . ALA C 2 85  ? -3.934  123.667 78.904  1.00 46.73  ? 103 ALA C N    1 
ATOM   6320  C CA   . ALA C 2 85  ? -5.048  122.989 78.255  1.00 49.35  ? 103 ALA C CA   1 
ATOM   6321  C C    . ALA C 2 85  ? -5.176  123.491 76.840  1.00 51.70  ? 103 ALA C C    1 
ATOM   6322  O O    . ALA C 2 85  ? -5.505  122.729 75.933  1.00 40.08  ? 103 ALA C O    1 
ATOM   6323  C CB   . ALA C 2 85  ? -6.329  123.244 79.000  1.00 36.83  ? 103 ALA C CB   1 
ATOM   6324  N N    . GLU C 2 86  ? -4.966  124.781 76.654  1.00 41.21  ? 104 GLU C N    1 
ATOM   6325  C CA   . GLU C 2 86  ? -5.103  125.376 75.354  1.00 43.41  ? 104 GLU C CA   1 
ATOM   6326  C C    . GLU C 2 86  ? -4.128  124.969 74.313  1.00 46.09  ? 104 GLU C C    1 
ATOM   6327  O O    . GLU C 2 86  ? -4.504  124.752 73.166  1.00 39.34  ? 104 GLU C O    1 
ATOM   6328  C CB   . GLU C 2 86  ? -4.982  126.886 75.528  1.00 43.44  ? 104 GLU C CB   1 
ATOM   6329  C CG   . GLU C 2 86  ? -4.963  127.714 74.256  1.00 55.71  ? 104 GLU C CG   1 
ATOM   6330  C CD   . GLU C 2 86  ? -4.791  129.186 74.538  1.00 47.03  ? 104 GLU C CD   1 
ATOM   6331  O OE1  . GLU C 2 86  ? -4.705  129.557 75.719  1.00 25.82  ? 104 GLU C OE1  1 
ATOM   6332  O OE2  . GLU C 2 86  ? -4.743  129.974 73.575  1.00 60.65  ? 104 GLU C OE2  1 
ATOM   6333  N N    . VAL C 2 87  ? -2.870  124.864 74.680  1.00 46.35  ? 105 VAL C N    1 
ATOM   6334  C CA   . VAL C 2 87  ? -1.852  124.643 73.683  1.00 40.36  ? 105 VAL C CA   1 
ATOM   6335  C C    . VAL C 2 87  ? -1.569  123.205 73.474  1.00 35.84  ? 105 VAL C C    1 
ATOM   6336  O O    . VAL C 2 87  ? -1.129  122.793 72.412  1.00 40.86  ? 105 VAL C O    1 
ATOM   6337  C CB   . VAL C 2 87  ? -0.603  125.419 74.070  1.00 42.71  ? 105 VAL C CB   1 
ATOM   6338  C CG1  . VAL C 2 87  ? 0.149   124.754 75.213  1.00 41.38  ? 105 VAL C CG1  1 
ATOM   6339  C CG2  . VAL C 2 87  ? 0.280   125.671 72.860  1.00 56.17  ? 105 VAL C CG2  1 
ATOM   6340  N N    . ALA C 2 88  ? -1.853  122.418 74.464  1.00 26.04  ? 106 ALA C N    1 
ATOM   6341  C CA   . ALA C 2 88  ? -1.688  121.034 74.287  1.00 25.17  ? 106 ALA C CA   1 
ATOM   6342  C C    . ALA C 2 88  ? -2.440  120.598 73.080  1.00 30.42  ? 106 ALA C C    1 
ATOM   6343  O O    . ALA C 2 88  ? -2.230  119.503 72.584  1.00 34.40  ? 106 ALA C O    1 
ATOM   6344  C CB   . ALA C 2 88  ? -2.225  120.354 75.481  1.00 26.18  ? 106 ALA C CB   1 
ATOM   6345  N N    . LYS C 2 92  ? 2.603   119.025 68.774  1.00 9.75   ? 110 LYS C N    1 
ATOM   6346  C CA   . LYS C 2 92  ? 3.156   118.375 67.606  1.00 20.76  ? 110 LYS C CA   1 
ATOM   6347  C C    . LYS C 2 92  ? 4.649   118.156 67.644  1.00 23.89  ? 110 LYS C C    1 
ATOM   6348  O O    . LYS C 2 92  ? 5.412   119.102 67.693  1.00 23.19  ? 110 LYS C O    1 
ATOM   6349  C CB   . LYS C 2 92  ? 2.747   119.120 66.352  1.00 21.87  ? 110 LYS C CB   1 
ATOM   6350  C CG   . LYS C 2 92  ? 1.626   118.458 65.564  1.00 13.79  ? 110 LYS C CG   1 
ATOM   6351  C CD   . LYS C 2 92  ? 0.352   119.285 65.600  1.00 11.95  ? 110 LYS C CD   1 
ATOM   6352  C CE   . LYS C 2 92  ? -0.824  118.515 65.029  1.00 9.78   ? 110 LYS C CE   1 
ATOM   6353  N NZ   . LYS C 2 92  ? -2.092  118.785 65.758  1.00 8.48   ? 110 LYS C NZ   1 
ATOM   6354  N N    . SER C 2 93  ? 5.075   116.902 67.555  1.00 23.63  ? 111 SER C N    1 
ATOM   6355  C CA   . SER C 2 93  ? 6.482   116.555 67.605  1.00 21.73  ? 111 SER C CA   1 
ATOM   6356  C C    . SER C 2 93  ? 7.048   116.300 66.220  1.00 27.11  ? 111 SER C C    1 
ATOM   6357  O O    . SER C 2 93  ? 6.713   115.312 65.607  1.00 31.51  ? 111 SER C O    1 
ATOM   6358  C CB   . SER C 2 93  ? 6.643   115.283 68.412  1.00 18.50  ? 111 SER C CB   1 
ATOM   6359  O OG   . SER C 2 93  ? 6.886   115.532 69.776  1.00 26.24  ? 111 SER C OG   1 
ATOM   6360  N N    . ASN C 2 94  ? 7.927   117.164 65.732  1.00 25.03  ? 112 ASN C N    1 
ATOM   6361  C CA   . ASN C 2 94  ? 8.522   116.971 64.428  1.00 24.35  ? 112 ASN C CA   1 
ATOM   6362  C C    . ASN C 2 94  ? 9.809   116.224 64.595  1.00 21.25  ? 112 ASN C C    1 
ATOM   6363  O O    . ASN C 2 94  ? 10.702  116.710 65.258  1.00 19.13  ? 112 ASN C O    1 
ATOM   6364  C CB   . ASN C 2 94  ? 8.779   118.314 63.761  1.00 24.48  ? 112 ASN C CB   1 
ATOM   6365  C CG   . ASN C 2 94  ? 8.999   118.219 62.264  1.00 25.31  ? 112 ASN C CG   1 
ATOM   6366  O OD1  . ASN C 2 94  ? 8.441   117.363 61.584  1.00 27.51  ? 112 ASN C OD1  1 
ATOM   6367  N ND2  . ASN C 2 94  ? 9.788   119.141 61.738  1.00 18.46  ? 112 ASN C ND2  1 
ATOM   6368  N N    . PRO C 2 95  ? 9.928   115.064 63.953  1.00 15.72  ? 113 PRO C N    1 
ATOM   6369  C CA   . PRO C 2 95  ? 11.093  114.233 64.127  1.00 16.55  ? 113 PRO C CA   1 
ATOM   6370  C C    . PRO C 2 95  ? 12.349  114.934 63.685  1.00 21.86  ? 113 PRO C C    1 
ATOM   6371  O O    . PRO C 2 95  ? 13.423  114.629 64.168  1.00 22.22  ? 113 PRO C O    1 
ATOM   6372  C CB   . PRO C 2 95  ? 10.774  113.047 63.264  1.00 13.39  ? 113 PRO C CB   1 
ATOM   6373  C CG   . PRO C 2 95  ? 9.716   113.481 62.330  1.00 19.75  ? 113 PRO C CG   1 
ATOM   6374  C CD   . PRO C 2 95  ? 8.900   114.397 63.153  1.00 16.34  ? 113 PRO C CD   1 
ATOM   6375  N N    . LYS C 2 96  ? 12.247  115.839 62.749  1.00 22.22  ? 114 LYS C N    1 
ATOM   6376  C CA   . LYS C 2 96  ? 13.393  116.511 62.199  1.00 23.60  ? 114 LYS C CA   1 
ATOM   6377  C C    . LYS C 2 96  ? 14.120  117.357 63.193  1.00 30.43  ? 114 LYS C C    1 
ATOM   6378  O O    . LYS C 2 96  ? 15.333  117.445 63.176  1.00 35.24  ? 114 LYS C O    1 
ATOM   6379  C CB   . LYS C 2 96  ? 12.836  117.390 61.102  1.00 21.02  ? 114 LYS C CB   1 
ATOM   6380  C CG   . LYS C 2 96  ? 13.801  117.818 60.024  1.00 45.52  ? 114 LYS C CG   1 
ATOM   6381  C CD   . LYS C 2 96  ? 13.081  118.659 58.980  1.00 45.06  ? 114 LYS C CD   1 
ATOM   6382  C CE   . LYS C 2 96  ? 13.940  118.832 57.739  1.00 45.69  ? 114 LYS C CE   1 
ATOM   6383  N NZ   . LYS C 2 96  ? 13.435  119.896 56.832  1.00 44.40  ? 114 LYS C NZ   1 
ATOM   6384  N N    . ASP C 2 97  ? 13.375  118.037 64.038  1.00 23.64  ? 115 ASP C N    1 
ATOM   6385  C CA   . ASP C 2 97  ? 13.962  118.947 64.964  1.00 19.01  ? 115 ASP C CA   1 
ATOM   6386  C C    . ASP C 2 97  ? 13.563  118.787 66.399  1.00 26.07  ? 115 ASP C C    1 
ATOM   6387  O O    . ASP C 2 97  ? 13.688  119.731 67.148  1.00 38.83  ? 115 ASP C O    1 
ATOM   6388  C CB   . ASP C 2 97  ? 13.626  120.361 64.500  1.00 15.54  ? 115 ASP C CB   1 
ATOM   6389  C CG   . ASP C 2 97  ? 12.186  120.547 64.140  1.00 20.13  ? 115 ASP C CG   1 
ATOM   6390  O OD1  . ASP C 2 97  ? 11.318  120.237 64.968  1.00 32.28  ? 115 ASP C OD1  1 
ATOM   6391  O OD2  . ASP C 2 97  ? 11.923  121.055 63.036  1.00 22.65  ? 115 ASP C OD2  1 
ATOM   6392  N N    . ASN C 2 98  ? 13.112  117.631 66.838  1.00 22.33  ? 116 ASN C N    1 
ATOM   6393  C CA   . ASN C 2 98  ? 12.627  117.561 68.206  1.00 23.84  ? 116 ASN C CA   1 
ATOM   6394  C C    . ASN C 2 98  ? 13.793  117.417 69.111  1.00 19.97  ? 116 ASN C C    1 
ATOM   6395  O O    . ASN C 2 98  ? 14.265  116.332 69.344  1.00 22.86  ? 116 ASN C O    1 
ATOM   6396  C CB   . ASN C 2 98  ? 11.524  116.495 68.429  1.00 18.13  ? 116 ASN C CB   1 
ATOM   6397  C CG   . ASN C 2 98  ? 11.898  115.123 67.966  1.00 20.03  ? 116 ASN C CG   1 
ATOM   6398  O OD1  . ASN C 2 98  ? 12.898  114.929 67.297  1.00 25.81  ? 116 ASN C OD1  1 
ATOM   6399  N ND2  . ASN C 2 98  ? 11.078  114.155 68.319  1.00 14.61  ? 116 ASN C ND2  1 
ATOM   6400  N N    . GLU C 2 99  ? 14.250  118.526 69.668  1.00 20.15  ? 117 GLU C N    1 
ATOM   6401  C CA   . GLU C 2 99  ? 15.476  118.493 70.451  1.00 25.02  ? 117 GLU C CA   1 
ATOM   6402  C C    . GLU C 2 99  ? 15.352  118.182 71.878  1.00 20.04  ? 117 GLU C C    1 
ATOM   6403  O O    . GLU C 2 99  ? 16.331  117.913 72.540  1.00 21.74  ? 117 GLU C O    1 
ATOM   6404  C CB   . GLU C 2 99  ? 16.232  119.808 70.312  1.00 22.91  ? 117 GLU C CB   1 
ATOM   6405  C CG   . GLU C 2 99  ? 17.117  119.935 69.093  1.00 20.43  ? 117 GLU C CG   1 
ATOM   6406  C CD   . GLU C 2 99  ? 17.477  121.374 68.816  1.00 26.14  ? 117 GLU C CD   1 
ATOM   6407  O OE1  . GLU C 2 99  ? 16.592  122.235 68.963  1.00 28.40  ? 117 GLU C OE1  1 
ATOM   6408  O OE2  . GLU C 2 99  ? 18.633  121.647 68.449  1.00 21.09  ? 117 GLU C OE2  1 
ATOM   6409  N N    . SER C 2 100 ? 14.152  118.196 72.371  1.00 20.49  ? 118 SER C N    1 
ATOM   6410  C CA   . SER C 2 100 ? 14.016  118.030 73.776  1.00 20.62  ? 118 SER C CA   1 
ATOM   6411  C C    . SER C 2 100 ? 14.147  116.578 74.107  1.00 24.75  ? 118 SER C C    1 
ATOM   6412  O O    . SER C 2 100 ? 14.362  116.243 75.255  1.00 29.03  ? 118 SER C O    1 
ATOM   6413  C CB   . SER C 2 100 ? 12.720  118.659 74.257  1.00 17.74  ? 118 SER C CB   1 
ATOM   6414  O OG   . SER C 2 100 ? 12.623  119.969 73.776  1.00 23.04  ? 118 SER C OG   1 
ATOM   6415  N N    . ARG C 2 101 ? 14.041  115.705 73.104  1.00 21.53  ? 119 ARG C N    1 
ATOM   6416  C CA   . ARG C 2 101 ? 14.171  114.267 73.329  1.00 18.67  ? 119 ARG C CA   1 
ATOM   6417  C C    . ARG C 2 101 ? 15.550  113.926 72.971  1.00 18.15  ? 119 ARG C C    1 
ATOM   6418  O O    . ARG C 2 101 ? 16.069  112.927 73.351  1.00 18.86  ? 119 ARG C O    1 
ATOM   6419  C CB   . ARG C 2 101 ? 13.252  113.527 72.417  1.00 15.20  ? 119 ARG C CB   1 
ATOM   6420  C CG   . ARG C 2 101 ? 13.035  112.062 72.722  1.00 12.99  ? 119 ARG C CG   1 
ATOM   6421  C CD   . ARG C 2 101 ? 12.833  111.818 74.193  1.00 17.45  ? 119 ARG C CD   1 
ATOM   6422  N NE   . ARG C 2 101 ? 13.165  110.454 74.532  1.00 16.54  ? 119 ARG C NE   1 
ATOM   6423  C CZ   . ARG C 2 101 ? 12.278  109.496 74.715  1.00 22.73  ? 119 ARG C CZ   1 
ATOM   6424  N NH1  . ARG C 2 101 ? 10.999  109.766 74.591  1.00 29.03  ? 119 ARG C NH1  1 
ATOM   6425  N NH2  . ARG C 2 101 ? 12.675  108.273 75.011  1.00 19.86  ? 119 ARG C NH2  1 
ATOM   6426  N N    . ARG C 2 102 ? 16.194  114.818 72.270  1.00 14.79  ? 120 ARG C N    1 
ATOM   6427  C CA   . ARG C 2 102 ? 17.494  114.525 71.791  1.00 17.34  ? 120 ARG C CA   1 
ATOM   6428  C C    . ARG C 2 102 ? 18.446  114.574 72.890  1.00 17.28  ? 120 ARG C C    1 
ATOM   6429  O O    . ARG C 2 102 ? 19.352  113.804 72.927  1.00 17.09  ? 120 ARG C O    1 
ATOM   6430  C CB   . ARG C 2 102 ? 17.864  115.542 70.760  1.00 19.49  ? 120 ARG C CB   1 
ATOM   6431  C CG   . ARG C 2 102 ? 17.185  115.315 69.442  1.00 17.89  ? 120 ARG C CG   1 
ATOM   6432  C CD   . ARG C 2 102 ? 17.640  116.288 68.384  1.00 18.30  ? 120 ARG C CD   1 
ATOM   6433  N NE   . ARG C 2 102 ? 16.905  116.031 67.167  1.00 23.69  ? 120 ARG C NE   1 
ATOM   6434  C CZ   . ARG C 2 102 ? 17.341  115.253 66.194  1.00 22.68  ? 120 ARG C CZ   1 
ATOM   6435  N NH1  . ARG C 2 102 ? 18.528  114.678 66.266  1.00 16.07  ? 120 ARG C NH1  1 
ATOM   6436  N NH2  . ARG C 2 102 ? 16.587  115.064 65.137  1.00 36.02  ? 120 ARG C NH2  1 
ATOM   6437  N N    . LEU C 2 103 ? 18.245  115.477 73.819  1.00 13.53  ? 121 LEU C N    1 
ATOM   6438  C CA   . LEU C 2 103 ? 19.138  115.602 74.927  1.00 13.45  ? 121 LEU C CA   1 
ATOM   6439  C C    . LEU C 2 103 ? 18.876  114.508 75.866  1.00 15.96  ? 121 LEU C C    1 
ATOM   6440  O O    . LEU C 2 103 ? 19.784  113.820 76.257  1.00 18.25  ? 121 LEU C O    1 
ATOM   6441  C CB   . LEU C 2 103 ? 18.903  116.908 75.629  1.00 15.87  ? 121 LEU C CB   1 
ATOM   6442  C CG   . LEU C 2 103 ? 19.954  117.362 76.633  1.00 22.87  ? 121 LEU C CG   1 
ATOM   6443  C CD1  . LEU C 2 103 ? 20.946  118.353 76.057  1.00 25.29  ? 121 LEU C CD1  1 
ATOM   6444  C CD2  . LEU C 2 103 ? 19.261  117.945 77.834  1.00 18.95  ? 121 LEU C CD2  1 
ATOM   6445  N N    . TYR C 2 104 ? 17.627  114.315 76.232  1.00 11.98  ? 122 TYR C N    1 
ATOM   6446  C CA   . TYR C 2 104 ? 17.275  113.315 77.202  1.00 12.96  ? 122 TYR C CA   1 
ATOM   6447  C C    . TYR C 2 104 ? 17.893  112.020 76.879  1.00 13.43  ? 122 TYR C C    1 
ATOM   6448  O O    . TYR C 2 104 ? 18.398  111.359 77.749  1.00 15.16  ? 122 TYR C O    1 
ATOM   6449  C CB   . TYR C 2 104 ? 15.790  113.186 77.217  1.00 18.23  ? 122 TYR C CB   1 
ATOM   6450  C CG   . TYR C 2 104 ? 15.191  112.123 78.114  1.00 21.88  ? 122 TYR C CG   1 
ATOM   6451  C CD1  . TYR C 2 104 ? 14.902  112.392 79.431  1.00 22.51  ? 122 TYR C CD1  1 
ATOM   6452  C CD2  . TYR C 2 104 ? 14.853  110.869 77.624  1.00 17.16  ? 122 TYR C CD2  1 
ATOM   6453  C CE1  . TYR C 2 104 ? 14.338  111.433 80.246  1.00 23.21  ? 122 TYR C CE1  1 
ATOM   6454  C CE2  . TYR C 2 104 ? 14.294  109.912 78.435  1.00 16.49  ? 122 TYR C CE2  1 
ATOM   6455  C CZ   . TYR C 2 104 ? 14.037  110.206 79.747  1.00 16.94  ? 122 TYR C CZ   1 
ATOM   6456  O OH   . TYR C 2 104 ? 13.476  109.271 80.569  1.00 20.91  ? 122 TYR C OH   1 
ATOM   6457  N N    . GLU C 2 105 ? 17.888  111.644 75.627  1.00 10.85  ? 123 GLU C N    1 
ATOM   6458  C CA   . GLU C 2 105 ? 18.390  110.369 75.207  1.00 12.16  ? 123 GLU C CA   1 
ATOM   6459  C C    . GLU C 2 105 ? 19.855  110.283 75.091  1.00 12.40  ? 123 GLU C C    1 
ATOM   6460  O O    . GLU C 2 105 ? 20.388  109.223 75.245  1.00 9.77   ? 123 GLU C O    1 
ATOM   6461  C CB   . GLU C 2 105 ? 17.786  110.091 73.874  1.00 17.14  ? 123 GLU C CB   1 
ATOM   6462  C CG   . GLU C 2 105 ? 16.404  109.497 73.945  1.00 24.11  ? 123 GLU C CG   1 
ATOM   6463  C CD   . GLU C 2 105 ? 15.928  109.024 72.606  1.00 16.43  ? 123 GLU C CD   1 
ATOM   6464  O OE1  . GLU C 2 105 ? 16.737  108.444 71.891  1.00 14.72  ? 123 GLU C OE1  1 
ATOM   6465  O OE2  . GLU C 2 105 ? 14.754  109.219 72.272  1.00 17.77  ? 123 GLU C OE2  1 
ATOM   6466  N N    . THR C 2 106 ? 20.520  111.382 74.789  1.00 12.76  ? 124 THR C N    1 
ATOM   6467  C CA   . THR C 2 106 ? 21.983  111.436 74.742  1.00 13.05  ? 124 THR C CA   1 
ATOM   6468  C C    . THR C 2 106 ? 22.505  111.308 76.169  1.00 18.33  ? 124 THR C C    1 
ATOM   6469  O O    . THR C 2 106 ? 23.584  110.788 76.408  1.00 18.60  ? 124 THR C O    1 
ATOM   6470  C CB   . THR C 2 106 ? 22.413  112.763 74.116  1.00 14.37  ? 124 THR C CB   1 
ATOM   6471  O OG1  . THR C 2 106 ? 21.934  112.829 72.775  1.00 20.18  ? 124 THR C OG1  1 
ATOM   6472  C CG2  . THR C 2 106 ? 23.903  112.932 74.121  1.00 14.73  ? 124 THR C CG2  1 
ATOM   6473  N N    . LEU C 2 107 ? 21.717  111.750 77.143  1.00 15.36  ? 125 LEU C N    1 
ATOM   6474  C CA   . LEU C 2 107 ? 22.084  111.626 78.545  1.00 11.93  ? 125 LEU C CA   1 
ATOM   6475  C C    . LEU C 2 107 ? 21.779  110.260 79.079  1.00 13.31  ? 125 LEU C C    1 
ATOM   6476  O O    . LEU C 2 107 ? 22.444  109.802 79.970  1.00 13.94  ? 125 LEU C O    1 
ATOM   6477  C CB   . LEU C 2 107 ? 21.315  112.659 79.332  1.00 9.62   ? 125 LEU C CB   1 
ATOM   6478  C CG   . LEU C 2 107 ? 21.578  114.138 79.058  1.00 10.24  ? 125 LEU C CG   1 
ATOM   6479  C CD1  . LEU C 2 107 ? 20.602  114.981 79.846  1.00 11.91  ? 125 LEU C CD1  1 
ATOM   6480  C CD2  . LEU C 2 107 ? 23.002  114.523 79.405  1.00 10.13  ? 125 LEU C CD2  1 
ATOM   6481  N N    . TYR C 2 108 ? 20.766  109.604 78.548  1.00 13.49  ? 126 TYR C N    1 
ATOM   6482  C CA   . TYR C 2 108 ? 20.412  108.270 78.949  1.00 13.96  ? 126 TYR C CA   1 
ATOM   6483  C C    . TYR C 2 108 ? 21.372  107.343 78.356  1.00 14.31  ? 126 TYR C C    1 
ATOM   6484  O O    . TYR C 2 108 ? 21.694  106.354 78.937  1.00 17.91  ? 126 TYR C O    1 
ATOM   6485  C CB   . TYR C 2 108 ? 18.989  107.905 78.512  1.00 12.71  ? 126 TYR C CB   1 
ATOM   6486  C CG   . TYR C 2 108 ? 18.770  106.456 78.172  1.00 14.45  ? 126 TYR C CG   1 
ATOM   6487  C CD1  . TYR C 2 108 ? 18.713  105.487 79.164  1.00 14.41  ? 126 TYR C CD1  1 
ATOM   6488  C CD2  . TYR C 2 108 ? 18.625  106.054 76.853  1.00 19.34  ? 126 TYR C CD2  1 
ATOM   6489  C CE1  . TYR C 2 108 ? 18.544  104.159 78.847  1.00 12.77  ? 126 TYR C CE1  1 
ATOM   6490  C CE2  . TYR C 2 108 ? 18.456  104.726 76.533  1.00 23.61  ? 126 TYR C CE2  1 
ATOM   6491  C CZ   . TYR C 2 108 ? 18.417  103.790 77.534  1.00 19.38  ? 126 TYR C CZ   1 
ATOM   6492  O OH   . TYR C 2 108 ? 18.226  102.486 77.207  1.00 24.26  ? 126 TYR C OH   1 
ATOM   6493  N N    . ALA C 2 109 ? 21.864  107.632 77.184  1.00 9.33   ? 127 ALA C N    1 
ATOM   6494  C CA   . ALA C 2 109 ? 22.865  106.793 76.585  1.00 12.02  ? 127 ALA C CA   1 
ATOM   6495  C C    . ALA C 2 109 ? 24.038  106.628 77.451  1.00 18.24  ? 127 ALA C C    1 
ATOM   6496  O O    . ALA C 2 109 ? 24.697  105.637 77.369  1.00 18.58  ? 127 ALA C O    1 
ATOM   6497  C CB   . ALA C 2 109 ? 23.325  107.471 75.379  1.00 15.54  ? 127 ALA C CB   1 
ATOM   6498  N N    . ASP C 2 110 ? 24.347  107.627 78.259  1.00 21.05  ? 128 ASP C N    1 
ATOM   6499  C CA   . ASP C 2 110 ? 25.499  107.619 79.130  1.00 18.98  ? 128 ASP C CA   1 
ATOM   6500  C C    . ASP C 2 110 ? 25.084  107.123 80.460  1.00 19.73  ? 128 ASP C C    1 
ATOM   6501  O O    . ASP C 2 110 ? 25.891  106.703 81.247  1.00 21.58  ? 128 ASP C O    1 
ATOM   6502  C CB   . ASP C 2 110 ? 25.934  109.041 79.314  1.00 23.07  ? 128 ASP C CB   1 
ATOM   6503  C CG   . ASP C 2 110 ? 27.004  109.475 78.338  1.00 32.29  ? 128 ASP C CG   1 
ATOM   6504  O OD1  . ASP C 2 110 ? 27.938  108.708 78.071  1.00 29.67  ? 128 ASP C OD1  1 
ATOM   6505  O OD2  . ASP C 2 110 ? 26.929  110.623 77.862  1.00 38.93  ? 128 ASP C OD2  1 
ATOM   6506  N N    . HIS C 2 111 ? 23.796  107.163 80.730  1.00 17.26  ? 129 HIS C N    1 
ATOM   6507  C CA   . HIS C 2 111 ? 23.285  106.607 81.963  1.00 17.80  ? 129 HIS C CA   1 
ATOM   6508  C C    . HIS C 2 111 ? 23.354  105.135 81.861  1.00 19.19  ? 129 HIS C C    1 
ATOM   6509  O O    . HIS C 2 111 ? 23.985  104.524 82.681  1.00 23.98  ? 129 HIS C O    1 
ATOM   6510  C CB   . HIS C 2 111 ? 21.866  107.052 82.206  1.00 18.97  ? 129 HIS C CB   1 
ATOM   6511  C CG   . HIS C 2 111 ? 21.425  106.909 83.621  1.00 23.07  ? 129 HIS C CG   1 
ATOM   6512  N ND1  . HIS C 2 111 ? 22.279  107.067 84.688  1.00 20.39  ? 129 HIS C ND1  1 
ATOM   6513  C CD2  . HIS C 2 111 ? 20.217  106.609 84.145  1.00 19.30  ? 129 HIS C CD2  1 
ATOM   6514  C CE1  . HIS C 2 111 ? 21.615  106.871 85.809  1.00 24.97  ? 129 HIS C CE1  1 
ATOM   6515  N NE2  . HIS C 2 111 ? 20.363  106.589 85.507  1.00 18.31  ? 129 HIS C NE2  1 
ATOM   6516  N N    . LEU C 2 112 ? 22.743  104.539 80.854  1.00 15.88  ? 130 LEU C N    1 
ATOM   6517  C CA   . LEU C 2 112 ? 22.874  103.104 80.637  1.00 17.89  ? 130 LEU C CA   1 
ATOM   6518  C C    . LEU C 2 112 ? 24.299  102.657 80.585  1.00 20.10  ? 130 LEU C C    1 
ATOM   6519  O O    . LEU C 2 112 ? 24.608  101.546 80.898  1.00 24.32  ? 130 LEU C O    1 
ATOM   6520  C CB   . LEU C 2 112 ? 22.202  102.721 79.347  1.00 13.17  ? 130 LEU C CB   1 
ATOM   6521  C CG   . LEU C 2 112 ? 21.879  101.265 79.086  1.00 14.82  ? 130 LEU C CG   1 
ATOM   6522  C CD1  . LEU C 2 112 ? 21.180  100.617 80.262  1.00 26.83  ? 130 LEU C CD1  1 
ATOM   6523  C CD2  . LEU C 2 112 ? 21.013  101.205 77.861  1.00 14.44  ? 130 LEU C CD2  1 
ATOM   6524  N N    . GLU C 2 113 ? 25.182  103.528 80.172  1.00 19.24  ? 131 GLU C N    1 
ATOM   6525  C CA   . GLU C 2 113 ? 26.559  103.182 80.015  1.00 22.68  ? 131 GLU C CA   1 
ATOM   6526  C C    . GLU C 2 113 ? 27.202  103.019 81.336  1.00 31.98  ? 131 GLU C C    1 
ATOM   6527  O O    . GLU C 2 113 ? 27.869  102.031 81.557  1.00 36.74  ? 131 GLU C O    1 
ATOM   6528  C CB   . GLU C 2 113 ? 27.245  104.297 79.263  1.00 27.99  ? 131 GLU C CB   1 
ATOM   6529  C CG   . GLU C 2 113 ? 28.709  104.070 78.936  1.00 41.95  ? 131 GLU C CG   1 
ATOM   6530  C CD   . GLU C 2 113 ? 29.606  105.160 79.496  1.00 53.47  ? 131 GLU C CD   1 
ATOM   6531  O OE1  . GLU C 2 113 ? 29.087  106.103 80.127  1.00 36.81  ? 131 GLU C OE1  1 
ATOM   6532  O OE2  . GLU C 2 113 ? 30.835  105.071 79.305  1.00 67.52  ? 131 GLU C OE2  1 
ATOM   6533  N N    . SER C 2 114 ? 26.998  103.975 82.243  1.00 23.70  ? 132 SER C N    1 
ATOM   6534  C CA   . SER C 2 114 ? 27.577  103.921 83.584  1.00 22.38  ? 132 SER C CA   1 
ATOM   6535  C C    . SER C 2 114 ? 27.202  102.675 84.244  1.00 22.38  ? 132 SER C C    1 
ATOM   6536  O O    . SER C 2 114 ? 28.017  102.055 84.880  1.00 23.10  ? 132 SER C O    1 
ATOM   6537  C CB   . SER C 2 114 ? 27.062  105.061 84.416  1.00 24.02  ? 132 SER C CB   1 
ATOM   6538  O OG   . SER C 2 114 ? 25.782  104.822 84.948  1.00 30.70  ? 132 SER C OG   1 
ATOM   6539  N N    . VAL C 2 115 ? 25.956  102.287 84.081  1.00 20.48  ? 133 VAL C N    1 
ATOM   6540  C CA   . VAL C 2 115 ? 25.442  101.090 84.660  1.00 20.00  ? 133 VAL C CA   1 
ATOM   6541  C C    . VAL C 2 115 ? 26.168  99.908  84.161  1.00 22.11  ? 133 VAL C C    1 
ATOM   6542  O O    . VAL C 2 115 ? 26.630  99.199  84.924  1.00 29.52  ? 133 VAL C O    1 
ATOM   6543  C CB   . VAL C 2 115 ? 23.946  100.961 84.393  1.00 17.60  ? 133 VAL C CB   1 
ATOM   6544  C CG1  . VAL C 2 115 ? 23.380  99.717  85.045  1.00 25.70  ? 133 VAL C CG1  1 
ATOM   6545  C CG2  . VAL C 2 115 ? 23.212  102.179 84.914  1.00 15.36  ? 133 VAL C CG2  1 
ATOM   6546  N N    . ILE C 2 116 ? 26.342  99.695  82.879  1.00 19.80  ? 134 ILE C N    1 
ATOM   6547  C CA   . ILE C 2 116 ? 26.933  98.444  82.389  1.00 20.98  ? 134 ILE C CA   1 
ATOM   6548  C C    . ILE C 2 116 ? 28.360  98.251  82.856  1.00 26.12  ? 134 ILE C C    1 
ATOM   6549  O O    . ILE C 2 116 ? 28.923  97.165  82.792  1.00 27.84  ? 134 ILE C O    1 
ATOM   6550  C CB   . ILE C 2 116 ? 26.650  98.257  80.892  1.00 18.91  ? 134 ILE C CB   1 
ATOM   6551  C CG1  . ILE C 2 116 ? 25.156  98.277  80.679  1.00 21.18  ? 134 ILE C CG1  1 
ATOM   6552  C CG2  . ILE C 2 116 ? 27.101  96.924  80.333  1.00 23.19  ? 134 ILE C CG2  1 
ATOM   6553  C CD1  . ILE C 2 116 ? 24.803  98.744  79.308  1.00 19.42  ? 134 ILE C CD1  1 
ATOM   6554  N N    . LYS C 2 117 ? 28.975  99.300  83.366  1.00 22.93  ? 135 LYS C N    1 
ATOM   6555  C CA   . LYS C 2 117 ? 30.305  99.147  83.914  1.00 22.55  ? 135 LYS C CA   1 
ATOM   6556  C C    . LYS C 2 117 ? 30.202  98.805  85.373  1.00 35.58  ? 135 LYS C C    1 
ATOM   6557  O O    . LYS C 2 117 ? 31.200  98.594  86.048  1.00 37.18  ? 135 LYS C O    1 
ATOM   6558  C CB   . LYS C 2 117 ? 31.151  100.376 83.647  1.00 20.14  ? 135 LYS C CB   1 
ATOM   6559  C CG   . LYS C 2 117 ? 31.387  100.734 82.208  1.00 33.13  ? 135 LYS C CG   1 
ATOM   6560  C CD   . LYS C 2 117 ? 32.303  101.933 82.116  1.00 37.04  ? 135 LYS C CD   1 
ATOM   6561  C CE   . LYS C 2 117 ? 33.709  101.540 82.519  1.00 38.24  ? 135 LYS C CE   1 
ATOM   6562  N NZ   . LYS C 2 117 ? 34.329  100.614 81.535  1.00 37.28  ? 135 LYS C NZ   1 
ATOM   6563  N N    . GLN C 2 118 ? 28.990  98.851  85.901  1.00 33.43  ? 136 GLN C N    1 
ATOM   6564  C CA   . GLN C 2 118 ? 28.759  98.580  87.300  1.00 22.63  ? 136 GLN C CA   1 
ATOM   6565  C C    . GLN C 2 118 ? 27.735  97.504  87.343  1.00 29.73  ? 136 GLN C C    1 
ATOM   6566  O O    . GLN C 2 118 ? 27.233  97.143  88.392  1.00 40.00  ? 136 GLN C O    1 
ATOM   6567  C CB   . GLN C 2 118 ? 28.312  99.883  87.943  1.00 17.16  ? 136 GLN C CB   1 
ATOM   6568  C CG   . GLN C 2 118 ? 26.842  100.214 87.913  1.00 23.53  ? 136 GLN C CG   1 
ATOM   6569  C CD   . GLN C 2 118 ? 26.590  101.600 88.440  1.00 31.96  ? 136 GLN C CD   1 
ATOM   6570  O OE1  . GLN C 2 118 ? 27.524  102.375 88.631  1.00 27.44  ? 136 GLN C OE1  1 
ATOM   6571  N NE2  . GLN C 2 118 ? 25.329  101.923 88.677  1.00 35.34  ? 136 GLN C NE2  1 
ATOM   6572  N N    . GLU C 2 119 ? 27.406  96.966  86.188  1.00 31.46  ? 137 GLU C N    1 
ATOM   6573  C CA   . GLU C 2 119 ? 26.517  95.830  86.104  1.00 37.08  ? 137 GLU C CA   1 
ATOM   6574  C C    . GLU C 2 119 ? 27.584  95.110  85.359  1.00 36.54  ? 137 GLU C C    1 
ATOM   6575  O O    . GLU C 2 119 ? 27.419  94.780  84.197  1.00 32.49  ? 137 GLU C O    1 
ATOM   6576  C CB   . GLU C 2 119 ? 25.330  96.165  85.223  1.00 40.02  ? 137 GLU C CB   1 
ATOM   6577  C CG   . GLU C 2 119 ? 24.094  95.302  85.386  1.00 41.55  ? 137 GLU C CG   1 
ATOM   6578  C CD   . GLU C 2 119 ? 22.985  95.691  84.427  1.00 43.75  ? 137 GLU C CD   1 
ATOM   6579  O OE1  . GLU C 2 119 ? 23.254  96.407  83.443  1.00 37.62  ? 137 GLU C OE1  1 
ATOM   6580  O OE2  . GLU C 2 119 ? 21.836  95.276  84.653  1.00 46.90  ? 137 GLU C OE2  1 
ATOM   6581  N N    . SER C 2 120 ? 28.706  94.887  86.019  1.00 39.62  ? 138 SER C N    1 
ATOM   6582  C CA   . SER C 2 120 ? 29.883  94.344  85.363  1.00 35.00  ? 138 SER C CA   1 
ATOM   6583  C C    . SER C 2 120 ? 29.955  93.067  84.616  1.00 27.09  ? 138 SER C C    1 
ATOM   6584  O O    . SER C 2 120 ? 29.088  92.213  84.685  1.00 24.94  ? 138 SER C O    1 
ATOM   6585  C CB   . SER C 2 120 ? 31.066  94.421  86.330  1.00 37.55  ? 138 SER C CB   1 
ATOM   6586  O OG   . SER C 2 120 ? 31.330  95.747  86.735  1.00 36.74  ? 138 SER C OG   1 
ATOM   6587  N N    . ASP C 2 121 ? 31.056  92.936  83.924  1.00 27.08  ? 139 ASP C N    1 
ATOM   6588  C CA   . ASP C 2 121 ? 31.257  91.802  83.117  1.00 36.39  ? 139 ASP C CA   1 
ATOM   6589  C C    . ASP C 2 121 ? 32.690  91.467  83.149  1.00 40.04  ? 139 ASP C C    1 
ATOM   6590  O O    . ASP C 2 121 ? 33.518  92.293  83.476  1.00 38.06  ? 139 ASP C O    1 
ATOM   6591  C CB   . ASP C 2 121 ? 30.913  92.173  81.679  1.00 40.69  ? 139 ASP C CB   1 
ATOM   6592  C CG   . ASP C 2 121 ? 31.633  93.414  81.198  1.00 48.61  ? 139 ASP C CG   1 
ATOM   6593  O OD1  . ASP C 2 121 ? 31.263  94.522  81.637  1.00 48.39  ? 139 ASP C OD1  1 
ATOM   6594  O OD2  . ASP C 2 121 ? 32.561  93.287  80.369  1.00 40.90  ? 139 ASP C OD2  1 
ATOM   6595  N N    . LEU C 2 122 ? 33.003  90.228  82.874  1.00 46.83  ? 140 LEU C N    1 
ATOM   6596  C CA   . LEU C 2 122 ? 34.371  89.860  82.715  1.00 46.77  ? 140 LEU C CA   1 
ATOM   6597  C C    . LEU C 2 122 ? 34.422  89.367  81.297  1.00 47.75  ? 140 LEU C C    1 
ATOM   6598  O O    . LEU C 2 122 ? 35.291  89.741  80.539  1.00 55.22  ? 140 LEU C O    1 
ATOM   6599  C CB   . LEU C 2 122 ? 34.788  88.796  83.746  1.00 47.91  ? 140 LEU C CB   1 
ATOM   6600  C CG   . LEU C 2 122 ? 34.150  87.399  83.778  1.00 47.73  ? 140 LEU C CG   1 
ATOM   6601  C CD1  . LEU C 2 122 ? 34.747  86.482  82.726  1.00 50.02  ? 140 LEU C CD1  1 
ATOM   6602  C CD2  . LEU C 2 122 ? 34.223  86.760  85.155  1.00 19.89  ? 140 LEU C CD2  1 
ATOM   6603  N N    . SER C 2 123 ? 33.484  88.512  80.933  1.00 47.87  ? 141 SER C N    1 
ATOM   6604  C CA   . SER C 2 123 ? 33.476  87.947  79.612  1.00 47.04  ? 141 SER C CA   1 
ATOM   6605  C C    . SER C 2 123 ? 32.117  87.586  79.101  1.00 43.13  ? 141 SER C C    1 
ATOM   6606  O O    . SER C 2 123 ? 31.864  86.427  78.844  1.00 52.98  ? 141 SER C O    1 
ATOM   6607  C CB   . SER C 2 123 ? 34.254  86.631  79.680  1.00 50.63  ? 141 SER C CB   1 
ATOM   6608  O OG   . SER C 2 123 ? 33.760  85.797  80.708  1.00 58.95  ? 141 SER C OG   1 
ATOM   6609  N N    . VAL C 2 124 ? 31.233  88.529  78.918  1.00 32.10  ? 142 VAL C N    1 
ATOM   6610  C CA   . VAL C 2 124 ? 29.972  88.175  78.339  1.00 34.72  ? 142 VAL C CA   1 
ATOM   6611  C C    . VAL C 2 124 ? 30.046  88.482  76.879  1.00 30.34  ? 142 VAL C C    1 
ATOM   6612  O O    . VAL C 2 124 ? 29.117  88.196  76.145  1.00 22.88  ? 142 VAL C O    1 
ATOM   6613  C CB   . VAL C 2 124 ? 28.880  88.960  79.035  1.00 34.23  ? 142 VAL C CB   1 
ATOM   6614  C CG1  . VAL C 2 124 ? 29.163  89.018  80.525  1.00 28.70  ? 142 VAL C CG1  1 
ATOM   6615  C CG2  . VAL C 2 124 ? 28.747  90.360  78.488  1.00 34.65  ? 142 VAL C CG2  1 
ATOM   6616  N N    . PHE C 2 125 ? 31.160  89.071  76.460  1.00 30.27  ? 143 PHE C N    1 
ATOM   6617  C CA   . PHE C 2 125 ? 31.357  89.473  75.088  1.00 23.64  ? 143 PHE C CA   1 
ATOM   6618  C C    . PHE C 2 125 ? 32.505  88.682  74.582  1.00 24.46  ? 143 PHE C C    1 
ATOM   6619  O O    . PHE C 2 125 ? 32.633  88.470  73.399  1.00 25.63  ? 143 PHE C O    1 
ATOM   6620  C CB   . PHE C 2 125 ? 31.734  90.938  75.067  1.00 19.50  ? 143 PHE C CB   1 
ATOM   6621  C CG   . PHE C 2 125 ? 30.704  91.844  75.653  1.00 17.80  ? 143 PHE C CG   1 
ATOM   6622  C CD1  . PHE C 2 125 ? 29.490  92.018  75.040  1.00 22.76  ? 143 PHE C CD1  1 
ATOM   6623  C CD2  . PHE C 2 125 ? 30.970  92.553  76.798  1.00 22.62  ? 143 PHE C CD2  1 
ATOM   6624  C CE1  . PHE C 2 125 ? 28.547  92.868  75.568  1.00 23.66  ? 143 PHE C CE1  1 
ATOM   6625  C CE2  . PHE C 2 125 ? 30.032  93.406  77.338  1.00 27.29  ? 143 PHE C CE2  1 
ATOM   6626  C CZ   . PHE C 2 125 ? 28.813  93.559  76.722  1.00 22.48  ? 143 PHE C CZ   1 
ATOM   6627  N N    . ASN C 2 126 ? 33.366  88.264  75.488  1.00 34.99  ? 144 ASN C N    1 
ATOM   6628  C CA   . ASN C 2 126 ? 34.504  87.428  75.136  1.00 32.96  ? 144 ASN C CA   1 
ATOM   6629  C C    . ASN C 2 126 ? 33.964  86.087  74.665  1.00 32.02  ? 144 ASN C C    1 
ATOM   6630  O O    . ASN C 2 126 ? 34.629  85.394  73.898  1.00 30.64  ? 144 ASN C O    1 
ATOM   6631  C CB   . ASN C 2 126 ? 35.522  87.335  76.260  1.00 33.57  ? 144 ASN C CB   1 
ATOM   6632  C CG   . ASN C 2 126 ? 36.066  88.664  76.677  1.00 34.74  ? 144 ASN C CG   1 
ATOM   6633  O OD1  . ASN C 2 126 ? 35.339  89.531  77.138  1.00 45.48  ? 144 ASN C OD1  1 
ATOM   6634  N ND2  . ASN C 2 126 ? 37.366  88.811  76.566  1.00 36.49  ? 144 ASN C ND2  1 
ATOM   6635  N N    . GLU C 2 127 ? 32.855  85.625  75.224  1.00 29.48  ? 145 GLU C N    1 
ATOM   6636  C CA   . GLU C 2 127 ? 32.185  84.440  74.680  1.00 30.97  ? 145 GLU C CA   1 
ATOM   6637  C C    . GLU C 2 127 ? 31.558  84.720  73.326  1.00 31.53  ? 145 GLU C C    1 
ATOM   6638  O O    . GLU C 2 127 ? 31.763  83.965  72.420  1.00 28.28  ? 145 GLU C O    1 
ATOM   6639  C CB   . GLU C 2 127 ? 31.089  83.959  75.622  1.00 31.62  ? 145 GLU C CB   1 
ATOM   6640  C CG   . GLU C 2 127 ? 31.540  83.291  76.901  1.00 42.29  ? 145 GLU C CG   1 
ATOM   6641  C CD   . GLU C 2 127 ? 30.420  83.197  77.911  1.00 39.31  ? 145 GLU C CD   1 
ATOM   6642  O OE1  . GLU C 2 127 ? 29.507  84.036  77.853  1.00 36.10  ? 145 GLU C OE1  1 
ATOM   6643  O OE2  . GLU C 2 127 ? 30.457  82.294  78.766  1.00 41.56  ? 145 GLU C OE2  1 
ATOM   6644  N N    . LEU C 2 128 ? 30.915  85.859  73.132  1.00 27.48  ? 146 LEU C N    1 
ATOM   6645  C CA   . LEU C 2 128 ? 30.170  86.164  71.918  1.00 27.46  ? 146 LEU C CA   1 
ATOM   6646  C C    . LEU C 2 128 ? 31.057  86.268  70.744  1.00 28.76  ? 146 LEU C C    1 
ATOM   6647  O O    . LEU C 2 128 ? 30.610  86.347  69.619  1.00 29.80  ? 146 LEU C O    1 
ATOM   6648  C CB   . LEU C 2 128 ? 29.337  87.430  72.090  1.00 19.42  ? 146 LEU C CB   1 
ATOM   6649  C CG   . LEU C 2 128 ? 28.538  88.165  71.025  1.00 14.44  ? 146 LEU C CG   1 
ATOM   6650  C CD1  . LEU C 2 128 ? 27.371  87.332  70.562  1.00 22.96  ? 146 LEU C CD1  1 
ATOM   6651  C CD2  . LEU C 2 128 ? 28.033  89.456  71.630  1.00 13.67  ? 146 LEU C CD2  1 
ATOM   6652  N N    . ARG C 2 129 ? 32.332  86.300  70.983  1.00 23.93  ? 147 ARG C N    1 
ATOM   6653  C CA   . ARG C 2 129 ? 33.240  86.297  69.882  1.00 31.02  ? 147 ARG C CA   1 
ATOM   6654  C C    . ARG C 2 129 ? 33.056  85.041  69.088  1.00 25.17  ? 147 ARG C C    1 
ATOM   6655  O O    . ARG C 2 129 ? 33.147  85.055  67.887  1.00 20.83  ? 147 ARG C O    1 
ATOM   6656  C CB   . ARG C 2 129 ? 34.684  86.465  70.379  1.00 32.48  ? 147 ARG C CB   1 
ATOM   6657  C CG   . ARG C 2 129 ? 35.010  87.894  70.762  1.00 28.04  ? 147 ARG C CG   1 
ATOM   6658  C CD   . ARG C 2 129 ? 36.135  88.000  71.763  1.00 26.91  ? 147 ARG C CD   1 
ATOM   6659  N NE   . ARG C 2 129 ? 37.185  87.033  71.509  1.00 42.51  ? 147 ARG C NE   1 
ATOM   6660  C CZ   . ARG C 2 129 ? 38.376  87.061  72.093  1.00 44.32  ? 147 ARG C CZ   1 
ATOM   6661  N NH1  . ARG C 2 129 ? 38.676  88.021  72.953  1.00 36.99  ? 147 ARG C NH1  1 
ATOM   6662  N NH2  . ARG C 2 129 ? 39.270  86.132  71.806  1.00 52.64  ? 147 ARG C NH2  1 
ATOM   6663  N N    . ASP C 2 130 ? 32.807  83.944  69.755  1.00 24.79  ? 148 ASP C N    1 
ATOM   6664  C CA   . ASP C 2 130 ? 32.687  82.681  69.072  1.00 26.33  ? 148 ASP C CA   1 
ATOM   6665  C C    . ASP C 2 130 ? 31.623  82.690  68.058  1.00 26.72  ? 148 ASP C C    1 
ATOM   6666  O O    . ASP C 2 130 ? 31.615  81.850  67.181  1.00 25.73  ? 148 ASP C O    1 
ATOM   6667  C CB   . ASP C 2 130 ? 32.461  81.546  70.074  1.00 27.27  ? 148 ASP C CB   1 
ATOM   6668  C CG   . ASP C 2 130 ? 31.161  81.639  70.866  1.00 32.84  ? 148 ASP C CG   1 
ATOM   6669  O OD1  . ASP C 2 130 ? 30.282  82.471  70.596  1.00 41.57  ? 148 ASP C OD1  1 
ATOM   6670  O OD2  . ASP C 2 130 ? 31.022  80.840  71.810  1.00 33.66  ? 148 ASP C OD2  1 
ATOM   6671  N N    . SER C 2 131 ? 30.700  83.624  68.167  1.00 28.71  ? 149 SER C N    1 
ATOM   6672  C CA   . SER C 2 131 ? 29.573  83.676  67.285  1.00 23.95  ? 149 SER C CA   1 
ATOM   6673  C C    . SER C 2 131 ? 29.863  84.624  66.156  1.00 28.93  ? 149 SER C C    1 
ATOM   6674  O O    . SER C 2 131 ? 29.310  84.481  65.107  1.00 28.09  ? 149 SER C O    1 
ATOM   6675  C CB   . SER C 2 131 ? 28.389  84.141  68.086  1.00 22.29  ? 149 SER C CB   1 
ATOM   6676  O OG   . SER C 2 131 ? 28.206  83.372  69.252  1.00 24.99  ? 149 SER C OG   1 
ATOM   6677  N N    . TYR C 2 132 ? 30.692  85.636  66.370  1.00 31.15  ? 150 TYR C N    1 
ATOM   6678  C CA   . TYR C 2 132 ? 31.089  86.530  65.302  1.00 28.76  ? 150 TYR C CA   1 
ATOM   6679  C C    . TYR C 2 132 ? 31.925  85.820  64.354  1.00 28.05  ? 150 TYR C C    1 
ATOM   6680  O O    . TYR C 2 132 ? 31.722  85.856  63.159  1.00 31.67  ? 150 TYR C O    1 
ATOM   6681  C CB   . TYR C 2 132 ? 32.016  87.592  65.879  1.00 24.52  ? 150 TYR C CB   1 
ATOM   6682  C CG   . TYR C 2 132 ? 32.442  88.734  64.967  1.00 26.95  ? 150 TYR C CG   1 
ATOM   6683  C CD1  . TYR C 2 132 ? 33.192  88.519  63.828  1.00 26.67  ? 150 TYR C CD1  1 
ATOM   6684  C CD2  . TYR C 2 132 ? 32.144  90.040  65.287  1.00 31.90  ? 150 TYR C CD2  1 
ATOM   6685  C CE1  . TYR C 2 132 ? 33.565  89.553  63.011  1.00 26.49  ? 150 TYR C CE1  1 
ATOM   6686  C CE2  . TYR C 2 132 ? 32.545  91.086  64.481  1.00 28.56  ? 150 TYR C CE2  1 
ATOM   6687  C CZ   . TYR C 2 132 ? 33.257  90.827  63.342  1.00 21.92  ? 150 TYR C CZ   1 
ATOM   6688  O OH   . TYR C 2 132 ? 33.654  91.845  62.525  1.00 19.66  ? 150 TYR C OH   1 
ATOM   6689  N N    . ASN C 2 133 ? 32.894  85.134  64.888  1.00 22.20  ? 151 ASN C N    1 
ATOM   6690  C CA   . ASN C 2 133 ? 33.827  84.509  64.030  1.00 23.68  ? 151 ASN C CA   1 
ATOM   6691  C C    . ASN C 2 133 ? 33.148  83.462  63.242  1.00 23.39  ? 151 ASN C C    1 
ATOM   6692  O O    . ASN C 2 133 ? 33.492  83.249  62.114  1.00 31.64  ? 151 ASN C O    1 
ATOM   6693  C CB   . ASN C 2 133 ? 34.998  83.991  64.845  1.00 30.95  ? 151 ASN C CB   1 
ATOM   6694  C CG   . ASN C 2 133 ? 35.612  85.042  65.756  1.00 31.98  ? 151 ASN C CG   1 
ATOM   6695  O OD1  . ASN C 2 133 ? 35.305  86.222  65.672  1.00 38.35  ? 151 ASN C OD1  1 
ATOM   6696  N ND2  . ASN C 2 133 ? 36.501  84.602  66.632  1.00 27.25  ? 151 ASN C ND2  1 
ATOM   6697  N N    . ALA C 2 134 ? 32.258  82.717  63.848  1.00 16.59  ? 152 ALA C N    1 
ATOM   6698  C CA   . ALA C 2 134 ? 31.469  81.751  63.121  1.00 18.19  ? 152 ALA C CA   1 
ATOM   6699  C C    . ALA C 2 134 ? 30.375  82.218  62.218  1.00 23.96  ? 152 ALA C C    1 
ATOM   6700  O O    . ALA C 2 134 ? 30.292  81.794  61.090  1.00 30.97  ? 152 ALA C O    1 
ATOM   6701  C CB   . ALA C 2 134 ? 30.833  80.879  64.131  1.00 28.10  ? 152 ALA C CB   1 
ATOM   6702  N N    . VAL C 2 135 ? 29.518  83.078  62.714  1.00 24.02  ? 153 VAL C N    1 
ATOM   6703  C CA   . VAL C 2 135 ? 28.398  83.597  61.950  1.00 25.23  ? 153 VAL C CA   1 
ATOM   6704  C C    . VAL C 2 135 ? 28.803  84.476  60.794  1.00 37.10  ? 153 VAL C C    1 
ATOM   6705  O O    . VAL C 2 135 ? 28.192  84.428  59.730  1.00 45.48  ? 153 VAL C O    1 
ATOM   6706  C CB   . VAL C 2 135 ? 27.359  84.289  62.853  1.00 23.13  ? 153 VAL C CB   1 
ATOM   6707  C CG1  . VAL C 2 135 ? 26.978  85.662  62.351  1.00 28.40  ? 153 VAL C CG1  1 
ATOM   6708  C CG2  . VAL C 2 135 ? 26.142  83.411  63.051  1.00 24.67  ? 153 VAL C CG2  1 
ATOM   6709  N N    . LYS C 2 136 ? 29.823  85.299  60.989  1.00 37.55  ? 154 LYS C N    1 
ATOM   6710  C CA   . LYS C 2 136 ? 30.297  86.166  59.927  1.00 39.10  ? 154 LYS C CA   1 
ATOM   6711  C C    . LYS C 2 136 ? 31.780  86.115  59.742  1.00 39.46  ? 154 LYS C C    1 
ATOM   6712  O O    . LYS C 2 136 ? 32.507  86.938  60.270  1.00 39.15  ? 154 LYS C O    1 
ATOM   6713  C CB   . LYS C 2 136 ? 29.857  87.593  60.160  1.00 39.75  ? 154 LYS C CB   1 
ATOM   6714  C CG   . LYS C 2 136 ? 29.798  88.004  61.605  1.00 40.16  ? 154 LYS C CG   1 
ATOM   6715  C CD   . LYS C 2 136 ? 29.913  89.501  61.663  1.00 43.30  ? 154 LYS C CD   1 
ATOM   6716  C CE   . LYS C 2 136 ? 29.416  90.027  62.981  1.00 40.63  ? 154 LYS C CE   1 
ATOM   6717  N NZ   . LYS C 2 136 ? 29.512  91.494  62.885  1.00 34.30  ? 154 LYS C NZ   1 
ATOM   6718  N N    . PRO C 2 137 ? 32.246  85.119  59.011  1.00 47.52  ? 155 PRO C N    1 
ATOM   6719  C CA   . PRO C 2 137 ? 33.685  84.969  58.860  1.00 50.72  ? 155 PRO C CA   1 
ATOM   6720  C C    . PRO C 2 137 ? 34.205  85.206  57.511  1.00 52.34  ? 155 PRO C C    1 
ATOM   6721  O O    . PRO C 2 137 ? 35.367  84.916  57.257  1.00 68.16  ? 155 PRO C O    1 
ATOM   6722  C CB   . PRO C 2 137 ? 33.861  83.459  58.953  1.00 39.94  ? 155 PRO C CB   1 
ATOM   6723  C CG   . PRO C 2 137 ? 32.587  82.888  58.413  1.00 35.74  ? 155 PRO C CG   1 
ATOM   6724  C CD   . PRO C 2 137 ? 31.521  83.948  58.487  1.00 38.01  ? 155 PRO C CD   1 
ATOM   6725  N N    . GLU C 2 138 ? 33.408  85.765  56.634  1.00 39.92  ? 156 GLU C N    1 
ATOM   6726  C CA   . GLU C 2 138 ? 33.841  85.826  55.289  1.00 32.49  ? 156 GLU C CA   1 
ATOM   6727  C C    . GLU C 2 138 ? 35.008  86.699  54.847  1.00 31.01  ? 156 GLU C C    1 
ATOM   6728  O O    . GLU C 2 138 ? 35.820  86.277  54.039  1.00 37.33  ? 156 GLU C O    1 
ATOM   6729  C CB   . GLU C 2 138 ? 32.641  86.430  54.623  1.00 27.46  ? 156 GLU C CB   1 
ATOM   6730  C CG   . GLU C 2 138 ? 32.479  87.888  55.017  1.00 36.21  ? 156 GLU C CG   1 
ATOM   6731  C CD   . GLU C 2 138 ? 31.864  88.075  56.370  1.00 39.72  ? 156 GLU C CD   1 
ATOM   6732  O OE1  . GLU C 2 138 ? 31.637  87.077  57.066  1.00 36.25  ? 156 GLU C OE1  1 
ATOM   6733  O OE2  . GLU C 2 138 ? 31.601  89.222  56.734  1.00 48.37  ? 156 GLU C OE2  1 
ATOM   6734  N N    . TYR C 2 139 ? 35.172  87.846  55.482  1.00 31.74  ? 157 TYR C N    1 
ATOM   6735  C CA   . TYR C 2 139 ? 36.318  88.708  55.278  1.00 29.00  ? 157 TYR C CA   1 
ATOM   6736  C C    . TYR C 2 139 ? 36.593  89.257  56.587  1.00 35.79  ? 157 TYR C C    1 
ATOM   6737  O O    . TYR C 2 139 ? 37.733  89.380  56.989  1.00 37.42  ? 157 TYR C O    1 
ATOM   6738  C CB   . TYR C 2 139 ? 36.142  89.666  54.136  1.00 22.50  ? 157 TYR C CB   1 
ATOM   6739  C CG   . TYR C 2 139 ? 34.756  90.210  53.931  1.00 28.16  ? 157 TYR C CG   1 
ATOM   6740  C CD1  . TYR C 2 139 ? 34.261  91.236  54.712  1.00 23.48  ? 157 TYR C CD1  1 
ATOM   6741  C CD2  . TYR C 2 139 ? 33.957  89.720  52.920  1.00 31.87  ? 157 TYR C CD2  1 
ATOM   6742  C CE1  . TYR C 2 139 ? 32.996  91.730  54.512  1.00 22.59  ? 157 TYR C CE1  1 
ATOM   6743  C CE2  . TYR C 2 139 ? 32.697  90.214  52.711  1.00 22.33  ? 157 TYR C CE2  1 
ATOM   6744  C CZ   . TYR C 2 139 ? 32.232  91.216  53.509  1.00 17.58  ? 157 TYR C CZ   1 
ATOM   6745  O OH   . TYR C 2 139 ? 30.986  91.694  53.290  1.00 17.08  ? 157 TYR C OH   1 
ATOM   6746  N N    . ALA C 2 140 ? 35.626  89.412  57.382  1.00 37.72  ? 158 ALA C N    1 
ATOM   6747  C CA   . ALA C 2 140 ? 35.564  90.332  58.441  1.00 30.09  ? 158 ALA C CA   1 
ATOM   6748  C C    . ALA C 2 140 ? 36.618  90.013  59.404  1.00 31.40  ? 158 ALA C C    1 
ATOM   6749  O O    . ALA C 2 140 ? 37.225  88.964  59.347  1.00 30.93  ? 158 ALA C O    1 
ATOM   6750  C CB   . ALA C 2 140 ? 34.205  90.322  59.073  1.00 25.38  ? 158 ALA C CB   1 
ATOM   6751  N N    . VAL C 2 141 ? 36.873  90.954  60.281  1.00 29.77  ? 159 VAL C N    1 
ATOM   6752  C CA   . VAL C 2 141 ? 37.899  90.787  61.241  1.00 27.40  ? 159 VAL C CA   1 
ATOM   6753  C C    . VAL C 2 141 ? 37.517  89.636  62.091  1.00 30.16  ? 159 VAL C C    1 
ATOM   6754  O O    . VAL C 2 141 ? 36.373  89.415  62.364  1.00 38.22  ? 159 VAL C O    1 
ATOM   6755  C CB   . VAL C 2 141 ? 38.027  92.096  62.032  1.00 30.14  ? 159 VAL C CB   1 
ATOM   6756  C CG1  . VAL C 2 141 ? 37.120  93.161  61.442  1.00 21.64  ? 159 VAL C CG1  1 
ATOM   6757  C CG2  . VAL C 2 141 ? 37.745  91.918  63.517  1.00 41.85  ? 159 VAL C CG2  1 
ATOM   6758  N N    . THR C 2 142 ? 38.472  88.835  62.479  1.00 29.50  ? 160 THR C N    1 
ATOM   6759  C CA   . THR C 2 142 ? 38.138  87.777  63.388  1.00 38.98  ? 160 THR C CA   1 
ATOM   6760  C C    . THR C 2 142 ? 38.764  88.146  64.715  1.00 42.40  ? 160 THR C C    1 
ATOM   6761  O O    . THR C 2 142 ? 39.980  88.208  64.830  1.00 47.68  ? 160 THR C O    1 
ATOM   6762  C CB   . THR C 2 142 ? 38.580  86.416  62.840  1.00 41.89  ? 160 THR C CB   1 
ATOM   6763  O OG1  . THR C 2 142 ? 37.666  86.001  61.817  1.00 28.91  ? 160 THR C OG1  1 
ATOM   6764  C CG2  . THR C 2 142 ? 38.609  85.377  63.930  1.00 46.98  ? 160 THR C CG2  1 
ATOM   6765  N N    . HIS C 2 143 ? 37.933  88.439  65.709  1.00 31.58  ? 161 HIS C N    1 
ATOM   6766  C CA   . HIS C 2 143 ? 38.459  88.856  66.978  1.00 36.39  ? 161 HIS C CA   1 
ATOM   6767  C C    . HIS C 2 143 ? 39.246  87.743  67.645  1.00 41.92  ? 161 HIS C C    1 
ATOM   6768  O O    . HIS C 2 143 ? 38.784  86.622  67.708  1.00 51.73  ? 161 HIS C O    1 
ATOM   6769  C CB   . HIS C 2 143 ? 37.333  89.340  67.858  1.00 31.83  ? 161 HIS C CB   1 
ATOM   6770  C CG   . HIS C 2 143 ? 37.728  90.444  68.780  1.00 31.82  ? 161 HIS C CG   1 
ATOM   6771  N ND1  . HIS C 2 143 ? 37.091  91.662  68.791  1.00 30.43  ? 161 HIS C ND1  1 
ATOM   6772  C CD2  . HIS C 2 143 ? 38.711  90.523  69.704  1.00 36.98  ? 161 HIS C CD2  1 
ATOM   6773  C CE1  . HIS C 2 143 ? 37.655  92.442  69.692  1.00 30.60  ? 161 HIS C CE1  1 
ATOM   6774  N NE2  . HIS C 2 143 ? 38.642  91.776  70.260  1.00 44.65  ? 161 HIS C NE2  1 
ATOM   6775  N N    . GLU C 2 144 ? 40.419  88.047  68.173  1.00 39.37  ? 162 GLU C N    1 
ATOM   6776  C CA   . GLU C 2 144 ? 41.240  87.050  68.855  1.00 47.45  ? 162 GLU C CA   1 
ATOM   6777  C C    . GLU C 2 144 ? 41.806  87.536  70.171  1.00 51.71  ? 162 GLU C C    1 
ATOM   6778  O O    . GLU C 2 144 ? 42.445  86.769  70.885  1.00 55.08  ? 162 GLU C O    1 
ATOM   6779  C CB   . GLU C 2 144 ? 42.400  86.591  67.985  1.00 47.92  ? 162 GLU C CB   1 
ATOM   6780  C CG   . GLU C 2 144 ? 43.381  87.663  67.573  1.00 52.91  ? 162 GLU C CG   1 
ATOM   6781  C CD   . GLU C 2 144 ? 44.528  87.073  66.788  1.00 57.78  ? 162 GLU C CD   1 
ATOM   6782  O OE1  . GLU C 2 144 ? 44.470  85.865  66.495  1.00 54.42  ? 162 GLU C OE1  1 
ATOM   6783  O OE2  . GLU C 2 144 ? 45.485  87.806  66.478  1.00 72.30  ? 162 GLU C OE2  1 
ATOM   6784  N N    . ILE C 2 147 ? 38.961  90.882  75.033  1.00 17.21  ? 165 ILE C N    1 
ATOM   6785  C CA   . ILE C 2 147 ? 38.200  92.055  75.459  1.00 25.29  ? 165 ILE C CA   1 
ATOM   6786  C C    . ILE C 2 147 ? 38.269  92.209  76.952  1.00 28.29  ? 165 ILE C C    1 
ATOM   6787  O O    . ILE C 2 147 ? 37.822  91.359  77.689  1.00 32.65  ? 165 ILE C O    1 
ATOM   6788  C CB   . ILE C 2 147 ? 36.736  92.043  74.981  1.00 27.63  ? 165 ILE C CB   1 
ATOM   6789  C CG1  . ILE C 2 147 ? 36.640  92.162  73.470  1.00 25.80  ? 165 ILE C CG1  1 
ATOM   6790  C CG2  . ILE C 2 147 ? 35.911  93.118  75.661  1.00 26.06  ? 165 ILE C CG2  1 
ATOM   6791  C CD1  . ILE C 2 147 ? 35.447  91.429  72.918  1.00 24.92  ? 165 ILE C CD1  1 
ATOM   6792  N N    . LYS C 2 148 ? 38.858  93.298  77.410  1.00 28.05  ? 166 LYS C N    1 
ATOM   6793  C CA   . LYS C 2 148 ? 39.024  93.541  78.820  1.00 33.25  ? 166 LYS C CA   1 
ATOM   6794  C C    . LYS C 2 148 ? 38.418  94.831  79.289  1.00 29.68  ? 166 LYS C C    1 
ATOM   6795  O O    . LYS C 2 148 ? 38.511  95.142  80.472  1.00 26.37  ? 166 LYS C O    1 
ATOM   6796  C CB   . LYS C 2 148 ? 40.500  93.557  79.156  1.00 34.73  ? 166 LYS C CB   1 
ATOM   6797  C CG   . LYS C 2 148 ? 41.109  92.189  79.410  1.00 32.82  ? 166 LYS C CG   1 
ATOM   6798  C CD   . LYS C 2 148 ? 40.617  91.593  80.718  1.00 33.88  ? 166 LYS C CD   1 
ATOM   6799  C CE   . LYS C 2 148 ? 39.982  90.230  80.505  1.00 37.28  ? 166 LYS C CE   1 
ATOM   6800  N NZ   . LYS C 2 148 ? 38.656  90.148  81.166  1.00 41.42  ? 166 LYS C NZ   1 
ATOM   6801  N N    . THR C 2 149 ? 37.782  95.590  78.394  1.00 25.83  ? 167 THR C N    1 
ATOM   6802  C CA   . THR C 2 149 ? 37.088  96.804  78.798  1.00 23.65  ? 167 THR C CA   1 
ATOM   6803  C C    . THR C 2 149 ? 35.737  96.856  78.190  1.00 24.62  ? 167 THR C C    1 
ATOM   6804  O O    . THR C 2 149 ? 35.320  95.909  77.578  1.00 29.14  ? 167 THR C O    1 
ATOM   6805  C CB   . THR C 2 149 ? 37.811  98.106  78.388  1.00 26.28  ? 167 THR C CB   1 
ATOM   6806  O OG1  . THR C 2 149 ? 37.772  98.258  76.974  1.00 32.85  ? 167 THR C OG1  1 
ATOM   6807  C CG2  . THR C 2 149 ? 39.252  98.144  78.852  1.00 28.93  ? 167 THR C CG2  1 
ATOM   6808  N N    . LEU C 2 150 ? 35.040  97.977  78.350  1.00 25.61  ? 168 LEU C N    1 
ATOM   6809  C CA   . LEU C 2 150 ? 33.704  98.163  77.783  1.00 21.42  ? 168 LEU C CA   1 
ATOM   6810  C C    . LEU C 2 150 ? 33.711  99.134  76.670  1.00 21.03  ? 168 LEU C C    1 
ATOM   6811  O O    . LEU C 2 150 ? 32.746  99.823  76.424  1.00 29.80  ? 168 LEU C O    1 
ATOM   6812  C CB   . LEU C 2 150 ? 32.715  98.682  78.823  1.00 18.66  ? 168 LEU C CB   1 
ATOM   6813  C CG   . LEU C 2 150 ? 31.252  98.276  78.761  1.00 17.01  ? 168 LEU C CG   1 
ATOM   6814  C CD1  . LEU C 2 150 ? 31.063  96.817  79.111  1.00 21.11  ? 168 LEU C CD1  1 
ATOM   6815  C CD2  . LEU C 2 150 ? 30.438  99.181  79.658  1.00 13.38  ? 168 LEU C CD2  1 
ATOM   6816  N N    . ASP C 2 151 ? 34.825  99.234  75.993  1.00 18.87  ? 169 ASP C N    1 
ATOM   6817  C CA   . ASP C 2 151 ? 34.922  100.092 74.870  1.00 20.77  ? 169 ASP C CA   1 
ATOM   6818  C C    . ASP C 2 151 ? 35.511  99.220  73.835  1.00 21.60  ? 169 ASP C C    1 
ATOM   6819  O O    . ASP C 2 151 ? 35.539  99.548  72.674  1.00 21.83  ? 169 ASP C O    1 
ATOM   6820  C CB   . ASP C 2 151 ? 35.868  101.235 75.125  1.00 17.92  ? 169 ASP C CB   1 
ATOM   6821  C CG   . ASP C 2 151 ? 35.322  102.240 76.099  1.00 34.09  ? 169 ASP C CG   1 
ATOM   6822  O OD1  . ASP C 2 151 ? 34.109  102.217 76.368  1.00 50.08  ? 169 ASP C OD1  1 
ATOM   6823  O OD2  . ASP C 2 151 ? 36.108  103.055 76.604  1.00 48.74  ? 169 ASP C OD2  1 
ATOM   6824  N N    . GLU C 2 152 ? 36.036  98.092  74.274  1.00 24.09  ? 170 GLU C N    1 
ATOM   6825  C CA   . GLU C 2 152 ? 36.589  97.104  73.374  1.00 25.00  ? 170 GLU C CA   1 
ATOM   6826  C C    . GLU C 2 152 ? 35.440  96.164  73.196  1.00 22.65  ? 170 GLU C C    1 
ATOM   6827  O O    . GLU C 2 152 ? 35.469  95.345  72.318  1.00 21.42  ? 170 GLU C O    1 
ATOM   6828  C CB   . GLU C 2 152 ? 37.808  96.352  73.866  1.00 22.19  ? 170 GLU C CB   1 
ATOM   6829  C CG   . GLU C 2 152 ? 39.051  97.161  74.135  1.00 27.13  ? 170 GLU C CG   1 
ATOM   6830  C CD   . GLU C 2 152 ? 39.947  96.439  75.115  1.00 35.88  ? 170 GLU C CD   1 
ATOM   6831  O OE1  . GLU C 2 152 ? 39.555  95.349  75.545  1.00 30.45  ? 170 GLU C OE1  1 
ATOM   6832  O OE2  . GLU C 2 152 ? 41.029  96.950  75.460  1.00 44.99  ? 170 GLU C OE2  1 
ATOM   6833  N N    . ALA C 2 153 ? 34.428  96.265  74.039  1.00 20.15  ? 171 ALA C N    1 
ATOM   6834  C CA   . ALA C 2 153 ? 33.231  95.463  73.911  1.00 21.73  ? 171 ALA C CA   1 
ATOM   6835  C C    . ALA C 2 153 ? 32.431  96.200  72.962  1.00 25.04  ? 171 ALA C C    1 
ATOM   6836  O O    . ALA C 2 153 ? 31.700  95.614  72.233  1.00 25.37  ? 171 ALA C O    1 
ATOM   6837  C CB   . ALA C 2 153 ? 32.487  95.444  75.191  1.00 16.47  ? 171 ALA C CB   1 
ATOM   6838  N N    . LYS C 2 154 ? 32.518  97.514  73.012  1.00 26.13  ? 172 LYS C N    1 
ATOM   6839  C CA   . LYS C 2 154 ? 31.814  98.381  72.114  1.00 22.52  ? 172 LYS C CA   1 
ATOM   6840  C C    . LYS C 2 154 ? 32.463  98.169  70.832  1.00 21.83  ? 172 LYS C C    1 
ATOM   6841  O O    . LYS C 2 154 ? 31.828  97.780  69.929  1.00 22.45  ? 172 LYS C O    1 
ATOM   6842  C CB   . LYS C 2 154 ? 32.092  99.795  72.533  1.00 22.03  ? 172 LYS C CB   1 
ATOM   6843  C CG   . LYS C 2 154 ? 31.099  100.843 72.127  1.00 24.03  ? 172 LYS C CG   1 
ATOM   6844  C CD   . LYS C 2 154 ? 31.207  102.001 73.092  1.00 22.29  ? 172 LYS C CD   1 
ATOM   6845  C CE   . LYS C 2 154 ? 31.662  103.262 72.403  1.00 21.55  ? 172 LYS C CE   1 
ATOM   6846  N NZ   . LYS C 2 154 ? 31.061  104.434 73.082  1.00 17.75  ? 172 LYS C NZ   1 
ATOM   6847  N N    . GLN C 2 155 ? 33.754  98.421  70.740  1.00 17.37  ? 173 GLN C N    1 
ATOM   6848  C CA   . GLN C 2 155 ? 34.489  98.247  69.511  1.00 17.12  ? 173 GLN C CA   1 
ATOM   6849  C C    . GLN C 2 155 ? 34.149  96.940  68.850  1.00 25.44  ? 173 GLN C C    1 
ATOM   6850  O O    . GLN C 2 155 ? 34.053  96.881  67.641  1.00 26.66  ? 173 GLN C O    1 
ATOM   6851  C CB   . GLN C 2 155 ? 35.978  98.402  69.777  1.00 15.23  ? 173 GLN C CB   1 
ATOM   6852  C CG   . GLN C 2 155 ? 36.876  98.456  68.555  1.00 22.94  ? 173 GLN C CG   1 
ATOM   6853  C CD   . GLN C 2 155 ? 38.193  99.140  68.843  1.00 18.43  ? 173 GLN C CD   1 
ATOM   6854  O OE1  . GLN C 2 155 ? 38.307  99.907  69.787  1.00 19.63  ? 173 GLN C OE1  1 
ATOM   6855  N NE2  . GLN C 2 155 ? 39.187  98.876  68.019  1.00 18.44  ? 173 GLN C NE2  1 
ATOM   6856  N N    . PHE C 2 156 ? 34.011  95.868  69.597  1.00 24.32  ? 174 PHE C N    1 
ATOM   6857  C CA   . PHE C 2 156 ? 33.548  94.602  69.027  1.00 25.25  ? 174 PHE C CA   1 
ATOM   6858  C C    . PHE C 2 156 ? 32.129  94.551  68.525  1.00 21.11  ? 174 PHE C C    1 
ATOM   6859  O O    . PHE C 2 156 ? 31.892  94.157  67.409  1.00 22.20  ? 174 PHE C O    1 
ATOM   6860  C CB   . PHE C 2 156 ? 33.716  93.548  70.119  1.00 27.41  ? 174 PHE C CB   1 
ATOM   6861  C CG   . PHE C 2 156 ? 33.179  92.190  69.786  1.00 29.89  ? 174 PHE C CG   1 
ATOM   6862  C CD1  . PHE C 2 156 ? 33.752  91.423  68.795  1.00 26.49  ? 174 PHE C CD1  1 
ATOM   6863  C CD2  . PHE C 2 156 ? 32.139  91.654  70.518  1.00 26.52  ? 174 PHE C CD2  1 
ATOM   6864  C CE1  . PHE C 2 156 ? 33.267  90.172  68.509  1.00 25.51  ? 174 PHE C CE1  1 
ATOM   6865  C CE2  . PHE C 2 156 ? 31.652  90.403  70.235  1.00 27.18  ? 174 PHE C CE2  1 
ATOM   6866  C CZ   . PHE C 2 156 ? 32.216  89.663  69.227  1.00 24.67  ? 174 PHE C CZ   1 
ATOM   6867  N N    . ILE C 2 157 ? 31.189  94.993  69.330  1.00 16.46  ? 175 ILE C N    1 
ATOM   6868  C CA   . ILE C 2 157 ? 29.800  94.956  68.957  1.00 19.49  ? 175 ILE C CA   1 
ATOM   6869  C C    . ILE C 2 157 ? 29.448  96.033  67.964  1.00 22.40  ? 175 ILE C C    1 
ATOM   6870  O O    . ILE C 2 157 ? 28.393  95.997  67.364  1.00 22.64  ? 175 ILE C O    1 
ATOM   6871  C CB   . ILE C 2 157 ? 28.891  95.060  70.191  1.00 19.04  ? 175 ILE C CB   1 
ATOM   6872  C CG1  . ILE C 2 157 ? 29.110  96.380  70.919  1.00 22.39  ? 175 ILE C CG1  1 
ATOM   6873  C CG2  . ILE C 2 157 ? 29.060  93.890  71.144  1.00 26.14  ? 175 ILE C CG2  1 
ATOM   6874  C CD1  . ILE C 2 157 ? 28.057  97.411  70.601  1.00 21.51  ? 175 ILE C CD1  1 
ATOM   6875  N N    . LEU C 2 158 ? 30.323  97.007  67.791  1.00 20.90  ? 176 LEU C N    1 
ATOM   6876  C CA   . LEU C 2 158 ? 30.081  98.117  66.896  1.00 17.25  ? 176 LEU C CA   1 
ATOM   6877  C C    . LEU C 2 158 ? 30.656  97.714  65.574  1.00 19.44  ? 176 LEU C C    1 
ATOM   6878  O O    . LEU C 2 158 ? 30.518  98.421  64.595  1.00 19.24  ? 176 LEU C O    1 
ATOM   6879  C CB   . LEU C 2 158 ? 30.647  99.433  67.436  1.00 11.86  ? 176 LEU C CB   1 
ATOM   6880  C CG   . LEU C 2 158 ? 29.671  100.481 67.947  1.00 11.52  ? 176 LEU C CG   1 
ATOM   6881  C CD1  . LEU C 2 158 ? 28.783  99.893  69.018  1.00 17.90  ? 176 LEU C CD1  1 
ATOM   6882  C CD2  . LEU C 2 158 ? 30.410  101.688 68.475  1.00 12.23  ? 176 LEU C CD2  1 
ATOM   6883  N N    . SER C 2 159 ? 31.265  96.546  65.528  1.00 19.73  ? 177 SER C N    1 
ATOM   6884  C CA   . SER C 2 159 ? 31.849  96.017  64.314  1.00 22.17  ? 177 SER C CA   1 
ATOM   6885  C C    . SER C 2 159 ? 30.874  94.986  63.795  1.00 20.11  ? 177 SER C C    1 
ATOM   6886  O O    . SER C 2 159 ? 31.238  94.016  63.167  1.00 20.24  ? 177 SER C O    1 
ATOM   6887  C CB   . SER C 2 159 ? 33.231  95.462  64.574  1.00 18.34  ? 177 SER C CB   1 
ATOM   6888  O OG   . SER C 2 159 ? 34.100  96.491  64.978  1.00 24.63  ? 177 SER C OG   1 
ATOM   6889  N N    . PHE C 2 160 ? 29.615  95.218  64.071  1.00 18.58  ? 178 PHE C N    1 
ATOM   6890  C CA   . PHE C 2 160 ? 28.596  94.347  63.579  1.00 24.34  ? 178 PHE C CA   1 
ATOM   6891  C C    . PHE C 2 160 ? 27.974  95.031  62.412  1.00 25.00  ? 178 PHE C C    1 
ATOM   6892  O O    . PHE C 2 160 ? 26.845  94.767  62.095  1.00 27.17  ? 178 PHE C O    1 
ATOM   6893  C CB   . PHE C 2 160 ? 27.530  94.111  64.642  1.00 30.08  ? 178 PHE C CB   1 
ATOM   6894  C CG   . PHE C 2 160 ? 27.909  93.097  65.697  1.00 31.87  ? 178 PHE C CG   1 
ATOM   6895  C CD1  . PHE C 2 160 ? 29.219  92.690  65.878  1.00 29.37  ? 178 PHE C CD1  1 
ATOM   6896  C CD2  . PHE C 2 160 ? 26.942  92.563  66.517  1.00 20.93  ? 178 PHE C CD2  1 
ATOM   6897  C CE1  . PHE C 2 160 ? 29.552  91.769  66.848  1.00 22.45  ? 178 PHE C CE1  1 
ATOM   6898  C CE2  . PHE C 2 160 ? 27.269  91.645  67.489  1.00 20.79  ? 178 PHE C CE2  1 
ATOM   6899  C CZ   . PHE C 2 160 ? 28.575  91.247  67.655  1.00 21.09  ? 178 PHE C CZ   1 
ATOM   6900  N N    . VAL C 2 161 ? 28.718  95.896  61.761  1.00 21.97  ? 179 VAL C N    1 
ATOM   6901  C CA   . VAL C 2 161 ? 28.240  96.552  60.585  1.00 15.34  ? 179 VAL C CA   1 
ATOM   6902  C C    . VAL C 2 161 ? 28.924  95.788  59.529  1.00 16.05  ? 179 VAL C C    1 
ATOM   6903  O O    . VAL C 2 161 ? 28.541  95.829  58.388  1.00 19.44  ? 179 VAL C O    1 
ATOM   6904  C CB   . VAL C 2 161 ? 28.680  98.008  60.589  1.00 16.61  ? 179 VAL C CB   1 
ATOM   6905  C CG1  . VAL C 2 161 ? 30.191  98.151  60.541  1.00 17.60  ? 179 VAL C CG1  1 
ATOM   6906  C CG2  . VAL C 2 161 ? 27.976  98.816  59.515  1.00 15.18  ? 179 VAL C CG2  1 
ATOM   6907  N N    . MET C 2 162 ? 29.934  95.055  59.921  1.00 15.42  ? 180 MET C N    1 
ATOM   6908  C CA   . MET C 2 162 ? 30.687  94.244  58.993  1.00 20.70  ? 180 MET C CA   1 
ATOM   6909  C C    . MET C 2 162 ? 29.915  93.029  58.651  1.00 24.98  ? 180 MET C C    1 
ATOM   6910  O O    . MET C 2 162 ? 30.404  92.138  58.006  1.00 30.52  ? 180 MET C O    1 
ATOM   6911  C CB   . MET C 2 162 ? 31.995  93.843  59.614  1.00 23.39  ? 180 MET C CB   1 
ATOM   6912  C CG   . MET C 2 162 ? 32.897  95.004  59.967  1.00 22.01  ? 180 MET C CG   1 
ATOM   6913  S SD   . MET C 2 162 ? 33.479  95.856  58.500  1.00 42.26  ? 180 MET C SD   1 
ATOM   6914  C CE   . MET C 2 162 ? 33.975  97.412  59.223  1.00 27.13  ? 180 MET C CE   1 
ATOM   6915  N N    . LEU C 2 163 ? 28.699  92.972  59.099  1.00 22.75  ? 181 LEU C N    1 
ATOM   6916  C CA   . LEU C 2 163 ? 27.870  91.910  58.704  1.00 25.64  ? 181 LEU C CA   1 
ATOM   6917  C C    . LEU C 2 163 ? 27.017  92.913  58.056  1.00 24.29  ? 181 LEU C C    1 
ATOM   6918  O O    . LEU C 2 163 ? 26.296  93.643  58.706  1.00 30.06  ? 181 LEU C O    1 
ATOM   6919  C CB   . LEU C 2 163 ? 27.172  91.366  59.922  1.00 27.12  ? 181 LEU C CB   1 
ATOM   6920  C CG   . LEU C 2 163 ? 26.452  90.032  59.770  1.00 44.62  ? 181 LEU C CG   1 
ATOM   6921  C CD1  . LEU C 2 163 ? 26.205  89.398  61.123  1.00 35.98  ? 181 LEU C CD1  1 
ATOM   6922  C CD2  . LEU C 2 163 ? 25.144  90.211  59.024  1.00 48.34  ? 181 LEU C CD2  1 
ATOM   6923  N N    . ASN C 2 164 ? 27.036  92.943  56.759  1.00 18.21  ? 182 ASN C N    1 
ATOM   6924  C CA   . ASN C 2 164 ? 26.334  93.964  56.069  1.00 27.13  ? 182 ASN C CA   1 
ATOM   6925  C C    . ASN C 2 164 ? 25.574  93.624  54.868  1.00 31.10  ? 182 ASN C C    1 
ATOM   6926  O O    . ASN C 2 164 ? 26.143  93.233  53.878  1.00 35.50  ? 182 ASN C O    1 
ATOM   6927  C CB   . ASN C 2 164 ? 27.455  94.710  55.413  1.00 41.76  ? 182 ASN C CB   1 
ATOM   6928  C CG   . ASN C 2 164 ? 28.236  93.853  54.401  1.00 47.70  ? 182 ASN C CG   1 
ATOM   6929  O OD1  . ASN C 2 164 ? 28.086  92.638  54.369  1.00 38.70  ? 182 ASN C OD1  1 
ATOM   6930  N ND2  . ASN C 2 164 ? 29.087  94.481  53.600  1.00 54.69  ? 182 ASN C ND2  1 
ATOM   6931  N N    . ASP C 2 165 ? 24.281  93.719  54.901  1.00 30.14  ? 183 ASP C N    1 
ATOM   6932  C CA   . ASP C 2 165 ? 23.533  93.505  53.679  1.00 30.88  ? 183 ASP C CA   1 
ATOM   6933  C C    . ASP C 2 165 ? 23.666  92.193  52.932  1.00 27.73  ? 183 ASP C C    1 
ATOM   6934  O O    . ASP C 2 165 ? 23.649  92.177  51.717  1.00 35.16  ? 183 ASP C O    1 
ATOM   6935  C CB   . ASP C 2 165 ? 23.862  94.647  52.710  1.00 32.89  ? 183 ASP C CB   1 
ATOM   6936  C CG   . ASP C 2 165 ? 23.709  96.023  53.329  1.00 27.09  ? 183 ASP C CG   1 
ATOM   6937  O OD1  . ASP C 2 165 ? 22.570  96.468  53.531  1.00 25.95  ? 183 ASP C OD1  1 
ATOM   6938  O OD2  . ASP C 2 165 ? 24.734  96.668  53.589  1.00 23.58  ? 183 ASP C OD2  1 
ATOM   6939  N N    . ASN C 2 166 ? 24.006  91.163  53.714  1.00 28.97  ? 184 ASN C N    1 
ATOM   6940  C CA   . ASN C 2 166 ? 24.157  89.811  53.210  1.00 29.73  ? 184 ASN C CA   1 
ATOM   6941  C C    . ASN C 2 166 ? 23.429  88.901  54.188  1.00 29.79  ? 184 ASN C C    1 
ATOM   6942  O O    . ASN C 2 166 ? 22.308  88.528  53.934  1.00 26.57  ? 184 ASN C O    1 
ATOM   6943  C CB   . ASN C 2 166 ? 25.625  89.370  52.964  1.00 21.04  ? 184 ASN C CB   1 
ATOM   6944  C CG   . ASN C 2 166 ? 26.557  89.618  54.116  1.00 31.28  ? 184 ASN C CG   1 
ATOM   6945  O OD1  . ASN C 2 166 ? 26.161  90.056  55.185  1.00 46.95  ? 184 ASN C OD1  1 
ATOM   6946  N ND2  . ASN C 2 166 ? 27.826  89.319  53.896  1.00 30.60  ? 184 ASN C ND2  1 
ATOM   6947  N N    . VAL C 2 167 ? 24.054  88.552  55.302  1.00 31.93  ? 185 VAL C N    1 
ATOM   6948  C CA   . VAL C 2 167 ? 23.433  87.701  56.313  1.00 28.22  ? 185 VAL C CA   1 
ATOM   6949  C C    . VAL C 2 167 ? 22.295  88.401  57.033  1.00 23.51  ? 185 VAL C C    1 
ATOM   6950  O O    . VAL C 2 167 ? 21.424  87.744  57.573  1.00 19.44  ? 185 VAL C O    1 
ATOM   6951  C CB   . VAL C 2 167 ? 24.468  87.091  57.247  1.00 25.57  ? 185 VAL C CB   1 
ATOM   6952  C CG1  . VAL C 2 167 ? 24.156  85.629  57.470  1.00 37.36  ? 185 VAL C CG1  1 
ATOM   6953  C CG2  . VAL C 2 167 ? 25.856  87.218  56.664  1.00 25.75  ? 185 VAL C CG2  1 
ATOM   6954  N N    . GLU C 2 168 ? 22.328  89.718  57.106  1.00 21.02  ? 186 GLU C N    1 
ATOM   6955  C CA   . GLU C 2 168 ? 21.250  90.512  57.678  1.00 21.07  ? 186 GLU C CA   1 
ATOM   6956  C C    . GLU C 2 168 ? 19.973  90.389  56.894  1.00 25.24  ? 186 GLU C C    1 
ATOM   6957  O O    . GLU C 2 168 ? 18.895  90.415  57.455  1.00 21.19  ? 186 GLU C O    1 
ATOM   6958  C CB   . GLU C 2 168 ? 21.695  91.953  57.590  1.00 20.82  ? 186 GLU C CB   1 
ATOM   6959  C CG   . GLU C 2 168 ? 20.615  93.002  57.672  1.00 23.87  ? 186 GLU C CG   1 
ATOM   6960  C CD   . GLU C 2 168 ? 21.144  94.365  57.325  1.00 25.70  ? 186 GLU C CD   1 
ATOM   6961  O OE1  . GLU C 2 168 ? 22.355  94.481  57.088  1.00 30.61  ? 186 GLU C OE1  1 
ATOM   6962  O OE2  . GLU C 2 168 ? 20.353  95.317  57.286  1.00 29.31  ? 186 GLU C OE2  1 
ATOM   6963  N N    . LEU C 2 169 ? 20.081  90.274  55.583  1.00 30.14  ? 187 LEU C N    1 
ATOM   6964  C CA   . LEU C 2 169 ? 18.928  90.237  54.674  1.00 25.95  ? 187 LEU C CA   1 
ATOM   6965  C C    . LEU C 2 169 ? 17.931  89.146  54.782  1.00 25.98  ? 187 LEU C C    1 
ATOM   6966  O O    . LEU C 2 169 ? 16.769  89.361  54.486  1.00 29.58  ? 187 LEU C O    1 
ATOM   6967  C CB   . LEU C 2 169 ? 19.387  90.307  53.222  1.00 26.17  ? 187 LEU C CB   1 
ATOM   6968  C CG   . LEU C 2 169 ? 19.606  91.619  52.495  1.00 24.35  ? 187 LEU C CG   1 
ATOM   6969  C CD1  . LEU C 2 169 ? 20.268  91.260  51.184  1.00 23.86  ? 187 LEU C CD1  1 
ATOM   6970  C CD2  . LEU C 2 169 ? 18.254  92.250  52.231  1.00 22.11  ? 187 LEU C CD2  1 
ATOM   6971  N N    . PRO C 2 170 ? 18.356  87.959  55.164  1.00 22.11  ? 188 PRO C N    1 
ATOM   6972  C CA   . PRO C 2 170 ? 17.305  86.988  55.322  1.00 23.99  ? 188 PRO C CA   1 
ATOM   6973  C C    . PRO C 2 170 ? 16.187  87.407  56.275  1.00 26.76  ? 188 PRO C C    1 
ATOM   6974  O O    . PRO C 2 170 ? 15.044  87.205  55.926  1.00 24.90  ? 188 PRO C O    1 
ATOM   6975  C CB   . PRO C 2 170 ? 18.076  85.865  55.945  1.00 23.66  ? 188 PRO C CB   1 
ATOM   6976  C CG   . PRO C 2 170 ? 19.371  85.869  55.228  1.00 20.35  ? 188 PRO C CG   1 
ATOM   6977  C CD   . PRO C 2 170 ? 19.616  87.287  54.825  1.00 19.48  ? 188 PRO C CD   1 
ATOM   6978  N N    . LEU C 2 171 ? 16.490  88.006  57.411  1.00 28.29  ? 189 LEU C N    1 
ATOM   6979  C CA   . LEU C 2 171 ? 15.497  88.465  58.383  1.00 24.38  ? 189 LEU C CA   1 
ATOM   6980  C C    . LEU C 2 171 ? 15.061  89.922  58.298  1.00 24.66  ? 189 LEU C C    1 
ATOM   6981  O O    . LEU C 2 171 ? 14.375  90.381  59.176  1.00 28.22  ? 189 LEU C O    1 
ATOM   6982  C CB   . LEU C 2 171 ? 15.956  88.140  59.795  1.00 22.11  ? 189 LEU C CB   1 
ATOM   6983  C CG   . LEU C 2 171 ? 17.399  87.729  60.044  1.00 32.79  ? 189 LEU C CG   1 
ATOM   6984  C CD1  . LEU C 2 171 ? 18.236  88.968  60.268  1.00 34.60  ? 189 LEU C CD1  1 
ATOM   6985  C CD2  . LEU C 2 171 ? 17.466  86.846  61.275  1.00 36.20  ? 189 LEU C CD2  1 
ATOM   6986  N N    . LYS C 2 172 ? 15.450  90.645  57.260  1.00 20.80  ? 190 LYS C N    1 
ATOM   6987  C CA   . LYS C 2 172 ? 15.114  92.043  57.118  1.00 23.70  ? 190 LYS C CA   1 
ATOM   6988  C C    . LYS C 2 172 ? 13.934  92.075  56.303  1.00 23.67  ? 190 LYS C C    1 
ATOM   6989  O O    . LYS C 2 172 ? 13.333  93.113  56.130  1.00 26.84  ? 190 LYS C O    1 
ATOM   6990  C CB   . LYS C 2 172 ? 16.159  92.754  56.300  1.00 24.33  ? 190 LYS C CB   1 
ATOM   6991  C CG   . LYS C 2 172 ? 16.238  94.244  56.538  1.00 23.15  ? 190 LYS C CG   1 
ATOM   6992  C CD   . LYS C 2 172 ? 17.480  94.830  55.910  1.00 16.79  ? 190 LYS C CD   1 
ATOM   6993  C CE   . LYS C 2 172 ? 17.317  94.995  54.418  1.00 22.74  ? 190 LYS C CE   1 
ATOM   6994  N NZ   . LYS C 2 172 ? 18.525  95.635  53.843  1.00 31.12  ? 190 LYS C NZ   1 
ATOM   6995  N N    . ALA C 2 173 ? 13.563  90.930  55.789  1.00 27.09  ? 191 ALA C N    1 
ATOM   6996  C CA   . ALA C 2 173 ? 12.460  90.870  54.848  1.00 29.92  ? 191 ALA C CA   1 
ATOM   6997  C C    . ALA C 2 173 ? 11.302  90.309  55.558  1.00 30.23  ? 191 ALA C C    1 
ATOM   6998  O O    . ALA C 2 173 ? 10.197  90.358  55.054  1.00 34.81  ? 191 ALA C O    1 
ATOM   6999  C CB   . ALA C 2 173 ? 12.760  90.027  53.642  1.00 21.60  ? 191 ALA C CB   1 
ATOM   7000  N N    . GLN C 2 174 ? 11.546  89.793  56.753  1.00 29.15  ? 192 GLN C N    1 
ATOM   7001  C CA   . GLN C 2 174 ? 10.495  89.237  57.551  1.00 30.03  ? 192 GLN C CA   1 
ATOM   7002  C C    . GLN C 2 174 ? 9.958   90.400  58.320  1.00 27.75  ? 192 GLN C C    1 
ATOM   7003  O O    . GLN C 2 174 ? 9.117   90.233  59.176  1.00 36.52  ? 192 GLN C O    1 
ATOM   7004  C CB   . GLN C 2 174 ? 11.031  88.137  58.460  1.00 25.92  ? 192 GLN C CB   1 
ATOM   7005  C CG   . GLN C 2 174 ? 11.916  87.107  57.799  1.00 27.25  ? 192 GLN C CG   1 
ATOM   7006  C CD   . GLN C 2 174 ? 12.444  86.120  58.813  1.00 30.61  ? 192 GLN C CD   1 
ATOM   7007  O OE1  . GLN C 2 174 ? 11.977  86.088  59.946  1.00 20.47  ? 192 GLN C OE1  1 
ATOM   7008  N NE2  . GLN C 2 174 ? 13.420  85.313  58.416  1.00 34.55  ? 192 GLN C NE2  1 
ATOM   7009  N N    . SER C 2 175 ? 10.376  91.598  57.952  1.00 21.81  ? 193 SER C N    1 
ATOM   7010  C CA   . SER C 2 175 ? 9.958   92.778  58.678  1.00 25.98  ? 193 SER C CA   1 
ATOM   7011  C C    . SER C 2 175 ? 8.862   93.616  58.086  1.00 24.76  ? 193 SER C C    1 
ATOM   7012  O O    . SER C 2 175 ? 8.946   94.026  56.948  1.00 35.17  ? 193 SER C O    1 
ATOM   7013  C CB   . SER C 2 175 ? 11.132  93.692  58.869  1.00 29.15  ? 193 SER C CB   1 
ATOM   7014  O OG   . SER C 2 175 ? 10.784  94.787  59.691  1.00 28.82  ? 193 SER C OG   1 
ATOM   7015  N N    . GLU C 2 176 ? 7.799   93.830  58.833  1.00 18.79  ? 194 GLU C N    1 
ATOM   7016  C CA   . GLU C 2 176 ? 6.758   94.708  58.384  1.00 21.02  ? 194 GLU C CA   1 
ATOM   7017  C C    . GLU C 2 176 ? 7.227   96.090  58.588  1.00 23.44  ? 194 GLU C C    1 
ATOM   7018  O O    . GLU C 2 176 ? 7.022   96.944  57.749  1.00 29.22  ? 194 GLU C O    1 
ATOM   7019  C CB   . GLU C 2 176 ? 5.562   94.606  59.323  1.00 18.70  ? 194 GLU C CB   1 
ATOM   7020  C CG   . GLU C 2 176 ? 4.272   95.199  58.770  1.00 18.32  ? 194 GLU C CG   1 
ATOM   7021  C CD   . GLU C 2 176 ? 3.533   96.060  59.773  1.00 20.35  ? 194 GLU C CD   1 
ATOM   7022  O OE1  . GLU C 2 176 ? 4.045   96.264  60.886  1.00 28.66  ? 194 GLU C OE1  1 
ATOM   7023  O OE2  . GLU C 2 176 ? 2.435   96.540  59.446  1.00 19.79  ? 194 GLU C OE2  1 
ATOM   7024  N N    . ARG C 2 177 ? 7.894   96.411  59.668  1.00 28.41  ? 195 ARG C N    1 
ATOM   7025  C CA   . ARG C 2 177 ? 8.264   97.807  59.906  1.00 30.15  ? 195 ARG C CA   1 
ATOM   7026  C C    . ARG C 2 177 ? 9.343   98.346  58.987  1.00 24.78  ? 195 ARG C C    1 
ATOM   7027  O O    . ARG C 2 177 ? 9.252   99.456  58.522  1.00 23.48  ? 195 ARG C O    1 
ATOM   7028  C CB   . ARG C 2 177 ? 8.742   97.974  61.344  1.00 32.40  ? 195 ARG C CB   1 
ATOM   7029  C CG   . ARG C 2 177 ? 7.668   97.847  62.398  1.00 38.87  ? 195 ARG C CG   1 
ATOM   7030  C CD   . ARG C 2 177 ? 8.212   97.134  63.623  1.00 34.04  ? 195 ARG C CD   1 
ATOM   7031  N NE   . ARG C 2 177 ? 7.246   97.113  64.712  1.00 36.26  ? 195 ARG C NE   1 
ATOM   7032  C CZ   . ARG C 2 177 ? 6.255   96.238  64.816  1.00 39.06  ? 195 ARG C CZ   1 
ATOM   7033  N NH1  . ARG C 2 177 ? 6.085   95.303  63.896  1.00 33.44  ? 195 ARG C NH1  1 
ATOM   7034  N NH2  . ARG C 2 177 ? 5.428   96.300  65.844  1.00 54.50  ? 195 ARG C NH2  1 
ATOM   7035  N N    . TYR C 2 178 ? 10.337  97.553  58.711  1.00 21.51  ? 196 TYR C N    1 
ATOM   7036  C CA   . TYR C 2 178 ? 11.445  98.060  57.975  1.00 20.36  ? 196 TYR C CA   1 
ATOM   7037  C C    . TYR C 2 178 ? 11.272  98.833  56.713  1.00 21.81  ? 196 TYR C C    1 
ATOM   7038  O O    . TYR C 2 178 ? 11.906  99.863  56.563  1.00 27.20  ? 196 TYR C O    1 
ATOM   7039  C CB   . TYR C 2 178 ? 12.481  96.985  57.764  1.00 18.85  ? 196 TYR C CB   1 
ATOM   7040  C CG   . TYR C 2 178 ? 13.863  97.539  57.563  1.00 16.96  ? 196 TYR C CG   1 
ATOM   7041  C CD1  . TYR C 2 178 ? 14.594  98.018  58.626  1.00 15.71  ? 196 TYR C CD1  1 
ATOM   7042  C CD2  . TYR C 2 178 ? 14.426  97.598  56.310  1.00 24.76  ? 196 TYR C CD2  1 
ATOM   7043  C CE1  . TYR C 2 178 ? 15.855  98.533  58.447  1.00 18.43  ? 196 TYR C CE1  1 
ATOM   7044  C CE2  . TYR C 2 178 ? 15.683  98.115  56.122  1.00 27.42  ? 196 TYR C CE2  1 
ATOM   7045  C CZ   . TYR C 2 178 ? 16.392  98.575  57.196  1.00 18.80  ? 196 TYR C CZ   1 
ATOM   7046  O OH   . TYR C 2 178 ? 17.647  99.083  57.007  1.00 19.40  ? 196 TYR C OH   1 
ATOM   7047  N N    . PRO C 2 179 ? 10.461  98.348  55.762  1.00 23.54  ? 197 PRO C N    1 
ATOM   7048  C CA   . PRO C 2 179 ? 10.506  99.147  54.550  1.00 24.08  ? 197 PRO C CA   1 
ATOM   7049  C C    . PRO C 2 179 ? 9.747   100.431 54.683  1.00 22.94  ? 197 PRO C C    1 
ATOM   7050  O O    . PRO C 2 179 ? 8.946   100.735 53.818  1.00 24.48  ? 197 PRO C O    1 
ATOM   7051  C CB   . PRO C 2 179 ? 9.860   98.246  53.535  1.00 25.89  ? 197 PRO C CB   1 
ATOM   7052  C CG   . PRO C 2 179 ? 9.001   97.323  54.314  1.00 29.76  ? 197 PRO C CG   1 
ATOM   7053  C CD   . PRO C 2 179 ? 9.825   97.047  55.516  1.00 29.01  ? 197 PRO C CD   1 
ATOM   7054  N N    . LYS C 2 180 ? 10.031  101.199 55.724  1.00 19.99  ? 198 LYS C N    1 
ATOM   7055  C CA   . LYS C 2 180 ? 9.375   102.454 55.978  1.00 17.99  ? 198 LYS C CA   1 
ATOM   7056  C C    . LYS C 2 180 ? 10.457  103.386 56.441  1.00 14.22  ? 198 LYS C C    1 
ATOM   7057  O O    . LYS C 2 180 ? 10.209  104.365 57.107  1.00 12.15  ? 198 LYS C O    1 
ATOM   7058  C CB   . LYS C 2 180 ? 8.275   102.240 57.000  1.00 20.32  ? 198 LYS C CB   1 
ATOM   7059  C CG   . LYS C 2 180 ? 7.107   101.421 56.461  1.00 18.50  ? 198 LYS C CG   1 
ATOM   7060  C CD   . LYS C 2 180 ? 6.089   101.063 57.523  1.00 32.09  ? 198 LYS C CD   1 
ATOM   7061  C CE   . LYS C 2 180 ? 4.792   100.582 56.893  1.00 25.56  ? 198 LYS C CE   1 
ATOM   7062  N NZ   . LYS C 2 180 ? 3.649   100.626 57.846  1.00 21.03  ? 198 LYS C NZ   1 
ATOM   7063  N N    . LYS C 2 181 ? 11.681  103.046 56.108  1.00 17.46  ? 199 LYS C N    1 
ATOM   7064  C CA   . LYS C 2 181 ? 12.811  103.859 56.468  1.00 14.44  ? 199 LYS C CA   1 
ATOM   7065  C C    . LYS C 2 181 ? 12.644  105.090 55.682  1.00 15.29  ? 199 LYS C C    1 
ATOM   7066  O O    . LYS C 2 181 ? 12.545  105.047 54.475  1.00 13.51  ? 199 LYS C O    1 
ATOM   7067  C CB   . LYS C 2 181 ? 14.085  103.103 56.095  1.00 10.48  ? 199 LYS C CB   1 
ATOM   7068  C CG   . LYS C 2 181 ? 15.355  103.443 56.822  1.00 12.54  ? 199 LYS C CG   1 
ATOM   7069  C CD   . LYS C 2 181 ? 16.219  102.200 56.918  1.00 15.76  ? 199 LYS C CD   1 
ATOM   7070  C CE   . LYS C 2 181 ? 17.700  102.523 57.006  1.00 18.53  ? 199 LYS C CE   1 
ATOM   7071  N NZ   . LYS C 2 181 ? 18.436  101.614 57.924  1.00 12.15  ? 199 LYS C NZ   1 
ATOM   7072  N N    . ASP C 2 182 ? 12.693  106.210 56.361  1.00 18.77  ? 200 ASP C N    1 
ATOM   7073  C CA   . ASP C 2 182 ? 12.440  107.481 55.736  1.00 25.30  ? 200 ASP C CA   1 
ATOM   7074  C C    . ASP C 2 182 ? 13.731  108.184 55.522  1.00 16.91  ? 200 ASP C C    1 
ATOM   7075  O O    . ASP C 2 182 ? 13.795  109.379 55.497  1.00 16.43  ? 200 ASP C O    1 
ATOM   7076  C CB   . ASP C 2 182 ? 11.560  108.307 56.689  1.00 22.99  ? 200 ASP C CB   1 
ATOM   7077  C CG   . ASP C 2 182 ? 10.525  109.102 55.979  1.00 31.61  ? 200 ASP C CG   1 
ATOM   7078  O OD1  . ASP C 2 182 ? 10.743  109.418 54.800  1.00 32.63  ? 200 ASP C OD1  1 
ATOM   7079  O OD2  . ASP C 2 182 ? 9.491   109.416 56.595  1.00 26.53  ? 200 ASP C OD2  1 
ATOM   7080  N N    . ARG C 2 183 ? 14.770  107.409 55.351  1.00 14.35  ? 201 ARG C N    1 
ATOM   7081  C CA   . ARG C 2 183 ? 16.076  107.993 55.141  1.00 20.60  ? 201 ARG C CA   1 
ATOM   7082  C C    . ARG C 2 183 ? 16.223  108.317 53.682  1.00 22.33  ? 201 ARG C C    1 
ATOM   7083  O O    . ARG C 2 183 ? 15.713  107.579 52.863  1.00 23.89  ? 201 ARG C O    1 
ATOM   7084  C CB   . ARG C 2 183 ? 17.153  106.998 55.540  1.00 11.82  ? 201 ARG C CB   1 
ATOM   7085  C CG   . ARG C 2 183 ? 18.553  107.516 55.359  1.00 15.76  ? 201 ARG C CG   1 
ATOM   7086  C CD   . ARG C 2 183 ? 19.552  106.498 55.846  1.00 10.93  ? 201 ARG C CD   1 
ATOM   7087  N NE   . ARG C 2 183 ? 20.910  106.987 55.703  1.00 10.97  ? 201 ARG C NE   1 
ATOM   7088  C CZ   . ARG C 2 183 ? 21.962  106.383 56.222  1.00 14.97  ? 201 ARG C CZ   1 
ATOM   7089  N NH1  . ARG C 2 183 ? 21.803  105.272 56.918  1.00 16.15  ? 201 ARG C NH1  1 
ATOM   7090  N NH2  . ARG C 2 183 ? 23.170  106.888 56.045  1.00 21.84  ? 201 ARG C NH2  1 
ATOM   7091  N N    . SER C 2 184 ? 16.966  109.363 53.320  1.00 11.47  ? 202 SER C N    1 
ATOM   7092  C CA   . SER C 2 184 ? 17.175  109.667 51.947  1.00 11.74  ? 202 SER C CA   1 
ATOM   7093  C C    . SER C 2 184 ? 18.402  109.014 51.541  1.00 23.14  ? 202 SER C C    1 
ATOM   7094  O O    . SER C 2 184 ? 19.137  108.510 52.371  1.00 17.98  ? 202 SER C O    1 
ATOM   7095  C CB   . SER C 2 184 ? 17.385  111.135 51.851  1.00 14.61  ? 202 SER C CB   1 
ATOM   7096  O OG   . SER C 2 184 ? 17.652  111.540 50.530  1.00 32.39  ? 202 SER C OG   1 
ATOM   7097  N N    . ARG C 2 185 ? 18.675  109.037 50.241  1.00 26.88  ? 203 ARG C N    1 
ATOM   7098  C CA   . ARG C 2 185 ? 19.920  108.494 49.715  1.00 18.35  ? 203 ARG C CA   1 
ATOM   7099  C C    . ARG C 2 185 ? 20.774  109.662 49.399  1.00 16.57  ? 203 ARG C C    1 
ATOM   7100  O O    . ARG C 2 185 ? 21.939  109.501 49.130  1.00 25.22  ? 203 ARG C O    1 
ATOM   7101  C CB   . ARG C 2 185 ? 19.670  107.703 48.447  1.00 19.40  ? 203 ARG C CB   1 
ATOM   7102  C CG   . ARG C 2 185 ? 20.531  106.465 48.324  1.00 24.14  ? 203 ARG C CG   1 
ATOM   7103  C CD   . ARG C 2 185 ? 20.094  105.566 47.188  1.00 24.79  ? 203 ARG C CD   1 
ATOM   7104  N NE   . ARG C 2 185 ? 18.660  105.342 47.158  1.00 23.47  ? 203 ARG C NE   1 
ATOM   7105  C CZ   . ARG C 2 185 ? 18.088  104.171 46.919  1.00 22.11  ? 203 ARG C CZ   1 
ATOM   7106  N NH1  . ARG C 2 185 ? 18.823  103.098 46.708  1.00 20.31  ? 203 ARG C NH1  1 
ATOM   7107  N NH2  . ARG C 2 185 ? 16.774  104.076 46.891  1.00 23.87  ? 203 ARG C NH2  1 
ATOM   7108  N N    . GLU C 2 186 ? 20.190  110.847 49.422  1.00 11.34  ? 204 GLU C N    1 
ATOM   7109  C CA   . GLU C 2 186 ? 20.943  112.044 49.196  1.00 13.02  ? 204 GLU C CA   1 
ATOM   7110  C C    . GLU C 2 186 ? 21.788  112.090 50.387  1.00 22.80  ? 204 GLU C C    1 
ATOM   7111  O O    . GLU C 2 186 ? 21.336  112.414 51.458  1.00 32.64  ? 204 GLU C O    1 
ATOM   7112  C CB   . GLU C 2 186 ? 20.096  113.279 49.243  1.00 13.37  ? 204 GLU C CB   1 
ATOM   7113  C CG   . GLU C 2 186 ? 20.757  114.462 48.560  1.00 19.30  ? 204 GLU C CG   1 
ATOM   7114  C CD   . GLU C 2 186 ? 20.186  115.794 48.979  1.00 16.96  ? 204 GLU C CD   1 
ATOM   7115  O OE1  . GLU C 2 186 ? 19.225  115.823 49.768  1.00 15.70  ? 204 GLU C OE1  1 
ATOM   7116  O OE2  . GLU C 2 186 ? 20.702  116.819 48.507  1.00 13.88  ? 204 GLU C OE2  1 
ATOM   7117  N N    . GLU C 2 187 ? 23.051  111.797 50.203  1.00 24.30  ? 205 GLU C N    1 
ATOM   7118  C CA   . GLU C 2 187 ? 23.962  111.825 51.296  1.00 28.91  ? 205 GLU C CA   1 
ATOM   7119  C C    . GLU C 2 187 ? 24.444  113.197 51.209  1.00 28.43  ? 205 GLU C C    1 
ATOM   7120  O O    . GLU C 2 187 ? 24.638  113.686 50.110  1.00 30.28  ? 205 GLU C O    1 
ATOM   7121  C CB   . GLU C 2 187 ? 25.071  110.847 50.949  1.00 30.94  ? 205 GLU C CB   1 
ATOM   7122  C CG   . GLU C 2 187 ? 25.863  111.200 49.717  1.00 26.64  ? 205 GLU C CG   1 
ATOM   7123  C CD   . GLU C 2 187 ? 26.847  110.115 49.395  1.00 37.38  ? 205 GLU C CD   1 
ATOM   7124  O OE1  . GLU C 2 187 ? 27.152  109.287 50.274  1.00 24.33  ? 205 GLU C OE1  1 
ATOM   7125  O OE2  . GLU C 2 187 ? 27.316  110.109 48.246  1.00 52.16  ? 205 GLU C OE2  1 
ATOM   7126  N N    . LEU C 2 188 ? 24.516  113.895 52.327  1.00 26.66  ? 206 LEU C N    1 
ATOM   7127  C CA   . LEU C 2 188 ? 24.822  115.300 52.276  1.00 26.95  ? 206 LEU C CA   1 
ATOM   7128  C C    . LEU C 2 188 ? 26.138  115.508 52.949  1.00 20.43  ? 206 LEU C C    1 
ATOM   7129  O O    . LEU C 2 188 ? 26.558  116.627 53.156  1.00 21.88  ? 206 LEU C O    1 
ATOM   7130  C CB   . LEU C 2 188 ? 23.649  115.923 53.008  1.00 19.48  ? 206 LEU C CB   1 
ATOM   7131  C CG   . LEU C 2 188 ? 22.398  116.192 52.207  1.00 24.57  ? 206 LEU C CG   1 
ATOM   7132  C CD1  . LEU C 2 188 ? 21.310  116.626 53.160  1.00 22.86  ? 206 LEU C CD1  1 
ATOM   7133  C CD2  . LEU C 2 188 ? 22.734  117.303 51.240  1.00 33.10  ? 206 LEU C CD2  1 
ATOM   7134  N N    . GLY C 2 189 ? 26.805  114.439 53.314  1.00 14.52  ? 207 GLY C N    1 
ATOM   7135  C CA   . GLY C 2 189 ? 28.122  114.578 53.865  1.00 16.60  ? 207 GLY C CA   1 
ATOM   7136  C C    . GLY C 2 189 ? 28.326  114.614 55.340  1.00 18.91  ? 207 GLY C C    1 
ATOM   7137  O O    . GLY C 2 189 ? 27.464  114.226 56.071  1.00 23.10  ? 207 GLY C O    1 
ATOM   7138  N N    . ASN C 2 190 ? 29.484  115.074 55.781  1.00 18.90  ? 208 ASN C N    1 
ATOM   7139  C CA   . ASN C 2 190 ? 29.787  115.167 57.192  1.00 15.09  ? 208 ASN C CA   1 
ATOM   7140  C C    . ASN C 2 190 ? 29.880  116.627 57.594  1.00 15.24  ? 208 ASN C C    1 
ATOM   7141  O O    . ASN C 2 190 ? 30.554  117.387 56.937  1.00 20.17  ? 208 ASN C O    1 
ATOM   7142  C CB   . ASN C 2 190 ? 31.085  114.430 57.522  1.00 11.04  ? 208 ASN C CB   1 
ATOM   7143  C CG   . ASN C 2 190 ? 30.930  112.938 57.543  1.00 13.86  ? 208 ASN C CG   1 
ATOM   7144  O OD1  . ASN C 2 190 ? 29.975  112.396 57.010  1.00 25.32  ? 208 ASN C OD1  1 
ATOM   7145  N ND2  . ASN C 2 190 ? 31.882  112.260 58.152  1.00 13.23  ? 208 ASN C ND2  1 
ATOM   7146  N N    . THR C 2 191 ? 29.193  117.025 58.657  1.00 14.22  ? 209 THR C N    1 
ATOM   7147  C CA   . THR C 2 191 ? 29.208  118.400 59.145  1.00 15.83  ? 209 THR C CA   1 
ATOM   7148  C C    . THR C 2 191 ? 29.897  118.392 60.483  1.00 14.80  ? 209 THR C C    1 
ATOM   7149  O O    . THR C 2 191 ? 29.769  117.448 61.195  1.00 21.77  ? 209 THR C O    1 
ATOM   7150  C CB   . THR C 2 191 ? 27.796  118.879 59.468  1.00 15.66  ? 209 THR C CB   1 
ATOM   7151  O OG1  . THR C 2 191 ? 26.916  118.523 58.402  1.00 29.68  ? 209 THR C OG1  1 
ATOM   7152  C CG2  . THR C 2 191 ? 27.757  120.377 59.679  1.00 11.31  ? 209 THR C CG2  1 
ATOM   7153  N N    . PRO C 2 192 ? 30.652  119.419 60.845  1.00 11.14  ? 210 PRO C N    1 
ATOM   7154  C CA   . PRO C 2 192 ? 31.188  119.354 62.196  1.00 13.30  ? 210 PRO C CA   1 
ATOM   7155  C C    . PRO C 2 192 ? 30.222  119.708 63.323  1.00 11.24  ? 210 PRO C C    1 
ATOM   7156  O O    . PRO C 2 192 ? 29.380  120.554 63.129  1.00 8.77   ? 210 PRO C O    1 
ATOM   7157  C CB   . PRO C 2 192 ? 32.412  120.262 62.128  1.00 14.36  ? 210 PRO C CB   1 
ATOM   7158  C CG   . PRO C 2 192 ? 32.796  120.273 60.697  1.00 15.75  ? 210 PRO C CG   1 
ATOM   7159  C CD   . PRO C 2 192 ? 31.467  120.340 60.024  1.00 17.78  ? 210 PRO C CD   1 
ATOM   7160  N N    . SER C 2 193 ? 30.335  119.041 64.471  1.00 12.44  ? 211 SER C N    1 
ATOM   7161  C CA   . SER C 2 193 ? 29.486  119.289 65.631  1.00 12.51  ? 211 SER C CA   1 
ATOM   7162  C C    . SER C 2 193 ? 30.196  118.982 66.898  1.00 12.08  ? 211 SER C C    1 
ATOM   7163  O O    . SER C 2 193 ? 30.974  118.066 66.943  1.00 15.86  ? 211 SER C O    1 
ATOM   7164  C CB   . SER C 2 193 ? 28.230  118.434 65.621  1.00 14.36  ? 211 SER C CB   1 
ATOM   7165  O OG   . SER C 2 193 ? 27.446  118.657 66.768  1.00 17.86  ? 211 SER C OG   1 
ATOM   7166  N N    . ALA C 2 194 ? 29.933  119.756 67.938  1.00 12.04  ? 212 ALA C N    1 
ATOM   7167  C CA   . ALA C 2 194 ? 30.507  119.527 69.249  1.00 12.47  ? 212 ALA C CA   1 
ATOM   7168  C C    . ALA C 2 194 ? 29.415  119.262 70.207  1.00 10.27  ? 212 ALA C C    1 
ATOM   7169  O O    . ALA C 2 194 ? 29.236  120.002 71.110  1.00 11.69  ? 212 ALA C O    1 
ATOM   7170  C CB   . ALA C 2 194 ? 31.244  120.720 69.737  1.00 11.29  ? 212 ALA C CB   1 
ATOM   7171  N N    . ASN C 2 195 ? 28.613  118.291 69.920  1.00 12.96  ? 213 ASN C N    1 
ATOM   7172  C CA   . ASN C 2 195 ? 27.517  118.029 70.731  1.00 13.63  ? 213 ASN C CA   1 
ATOM   7173  C C    . ASN C 2 195 ? 27.626  116.546 70.708  1.00 15.48  ? 213 ASN C C    1 
ATOM   7174  O O    . ASN C 2 195 ? 27.993  115.980 69.689  1.00 18.51  ? 213 ASN C O    1 
ATOM   7175  C CB   . ASN C 2 195 ? 26.244  118.552 70.096  1.00 10.15  ? 213 ASN C CB   1 
ATOM   7176  C CG   . ASN C 2 195 ? 26.208  120.058 70.019  1.00 12.24  ? 213 ASN C CG   1 
ATOM   7177  O OD1  . ASN C 2 195 ? 26.343  120.743 71.022  1.00 16.53  ? 213 ASN C OD1  1 
ATOM   7178  N ND2  . ASN C 2 195 ? 26.030  120.579 68.825  1.00 17.17  ? 213 ASN C ND2  1 
ATOM   7179  N N    . PRO C 2 196 ? 27.381  115.894 71.839  1.00 12.26  ? 214 PRO C N    1 
ATOM   7180  C CA   . PRO C 2 196 ? 27.547  114.466 71.712  1.00 15.42  ? 214 PRO C CA   1 
ATOM   7181  C C    . PRO C 2 196 ? 26.211  113.816 71.465  1.00 24.34  ? 214 PRO C C    1 
ATOM   7182  O O    . PRO C 2 196 ? 25.205  114.479 71.609  1.00 38.23  ? 214 PRO C O    1 
ATOM   7183  C CB   . PRO C 2 196 ? 28.118  114.099 73.041  1.00 17.16  ? 214 PRO C CB   1 
ATOM   7184  C CG   . PRO C 2 196 ? 27.550  115.091 73.994  1.00 25.12  ? 214 PRO C CG   1 
ATOM   7185  C CD   . PRO C 2 196 ? 27.179  116.318 73.226  1.00 14.90  ? 214 PRO C CD   1 
ATOM   7186  N N    . GLY C 2 197 ? 26.168  112.597 70.997  1.00 17.08  ? 215 GLY C N    1 
ATOM   7187  C CA   . GLY C 2 197 ? 24.890  111.924 70.848  1.00 20.06  ? 215 GLY C CA   1 
ATOM   7188  C C    . GLY C 2 197 ? 23.911  112.180 69.742  1.00 14.56  ? 215 GLY C C    1 
ATOM   7189  O O    . GLY C 2 197 ? 24.293  112.586 68.687  1.00 17.95  ? 215 GLY C O    1 
ATOM   7190  N N    . ILE C 2 198 ? 22.660  111.813 69.935  1.00 12.27  ? 216 ILE C N    1 
ATOM   7191  C CA   . ILE C 2 198 ? 21.611  112.150 69.008  1.00 12.31  ? 216 ILE C CA   1 
ATOM   7192  C C    . ILE C 2 198 ? 21.738  113.580 69.256  1.00 18.68  ? 216 ILE C C    1 
ATOM   7193  O O    . ILE C 2 198 ? 21.641  113.995 70.381  1.00 34.84  ? 216 ILE C O    1 
ATOM   7194  C CB   . ILE C 2 198 ? 20.288  111.716 69.576  1.00 12.09  ? 216 ILE C CB   1 
ATOM   7195  C CG1  . ILE C 2 198 ? 20.238  110.215 69.677  1.00 14.52  ? 216 ILE C CG1  1 
ATOM   7196  C CG2  . ILE C 2 198 ? 19.133  112.199 68.729  1.00 24.74  ? 216 ILE C CG2  1 
ATOM   7197  C CD1  . ILE C 2 198 ? 18.996  109.785 70.379  1.00 19.14  ? 216 ILE C CD1  1 
ATOM   7198  N N    . MET C 2 199 ? 21.873  114.389 68.246  1.00 18.43  ? 217 MET C N    1 
ATOM   7199  C CA   . MET C 2 199 ? 22.241  115.736 68.472  1.00 18.42  ? 217 MET C CA   1 
ATOM   7200  C C    . MET C 2 199 ? 21.796  116.566 67.397  1.00 25.77  ? 217 MET C C    1 
ATOM   7201  O O    . MET C 2 199 ? 21.171  116.082 66.480  1.00 43.41  ? 217 MET C O    1 
ATOM   7202  C CB   . MET C 2 199 ? 23.753  115.824 68.344  1.00 20.22  ? 217 MET C CB   1 
ATOM   7203  C CG   . MET C 2 199 ? 24.382  115.600 66.958  1.00 24.03  ? 217 MET C CG   1 
ATOM   7204  S SD   . MET C 2 199 ? 26.146  115.335 66.687  1.00 108.37 ? 217 MET C SD   1 
ATOM   7205  C CE   . MET C 2 199 ? 26.275  113.559 66.867  1.00 51.41  ? 217 MET C CE   1 
ATOM   7206  N N    . LYS C 2 200 ? 22.128  117.831 67.475  1.00 21.46  ? 218 LYS C N    1 
ATOM   7207  C CA   . LYS C 2 200 ? 21.809  118.671 66.396  1.00 22.63  ? 218 LYS C CA   1 
ATOM   7208  C C    . LYS C 2 200 ? 23.084  119.451 66.214  1.00 20.59  ? 218 LYS C C    1 
ATOM   7209  O O    . LYS C 2 200 ? 23.711  119.786 67.176  1.00 16.83  ? 218 LYS C O    1 
ATOM   7210  C CB   . LYS C 2 200 ? 20.564  119.500 66.638  1.00 20.74  ? 218 LYS C CB   1 
ATOM   7211  C CG   . LYS C 2 200 ? 19.648  119.644 65.437  1.00 17.76  ? 218 LYS C CG   1 
ATOM   7212  C CD   . LYS C 2 200 ? 19.235  118.290 64.899  1.00 20.23  ? 218 LYS C CD   1 
ATOM   7213  C CE   . LYS C 2 200 ? 18.640  118.399 63.507  1.00 45.72  ? 218 LYS C CE   1 
ATOM   7214  N NZ   . LYS C 2 200 ? 18.478  117.080 62.832  1.00 40.41  ? 218 LYS C NZ   1 
ATOM   7215  N N    . PRO C 2 201 ? 23.519  119.681 64.960  1.00 21.20  ? 219 PRO C N    1 
ATOM   7216  C CA   . PRO C 2 201 ? 24.813  120.338 64.858  1.00 18.69  ? 219 PRO C CA   1 
ATOM   7217  C C    . PRO C 2 201 ? 24.888  121.712 65.435  1.00 20.27  ? 219 PRO C C    1 
ATOM   7218  O O    . PRO C 2 201 ? 25.821  122.021 66.149  1.00 16.19  ? 219 PRO C O    1 
ATOM   7219  C CB   . PRO C 2 201 ? 25.022  120.408 63.352  1.00 21.97  ? 219 PRO C CB   1 
ATOM   7220  C CG   . PRO C 2 201 ? 23.684  120.386 62.736  1.00 18.03  ? 219 PRO C CG   1 
ATOM   7221  C CD   . PRO C 2 201 ? 23.007  119.389 63.586  1.00 22.61  ? 219 PRO C CD   1 
ATOM   7222  N N    . ASN C 2 202 ? 23.900  122.537 65.153  1.00 22.65  ? 220 ASN C N    1 
ATOM   7223  C CA   . ASN C 2 202 ? 23.862  123.887 65.625  1.00 22.88  ? 220 ASN C CA   1 
ATOM   7224  C C    . ASN C 2 202 ? 22.870  123.827 66.738  1.00 17.89  ? 220 ASN C C    1 
ATOM   7225  O O    . ASN C 2 202 ? 21.818  124.415 66.670  1.00 23.50  ? 220 ASN C O    1 
ATOM   7226  C CB   . ASN C 2 202 ? 23.428  124.816 64.495  1.00 14.01  ? 220 ASN C CB   1 
ATOM   7227  C CG   . ASN C 2 202 ? 23.946  124.385 63.142  1.00 20.30  ? 220 ASN C CG   1 
ATOM   7228  O OD1  . ASN C 2 202 ? 23.172  123.980 62.284  1.00 33.16  ? 220 ASN C OD1  1 
ATOM   7229  N ND2  . ASN C 2 202 ? 25.250  124.486 62.940  1.00 15.03  ? 220 ASN C ND2  1 
ATOM   7230  N N    . SER C 2 203 ? 23.206  123.087 67.768  1.00 13.95  ? 221 SER C N    1 
ATOM   7231  C CA   . SER C 2 203 ? 22.302  122.896 68.862  1.00 17.85  ? 221 SER C CA   1 
ATOM   7232  C C    . SER C 2 203 ? 22.726  123.547 70.096  1.00 14.94  ? 221 SER C C    1 
ATOM   7233  O O    . SER C 2 203 ? 23.856  123.424 70.499  1.00 13.20  ? 221 SER C O    1 
ATOM   7234  C CB   . SER C 2 203 ? 22.249  121.427 69.214  1.00 20.75  ? 221 SER C CB   1 
ATOM   7235  O OG   . SER C 2 203 ? 21.001  121.040 69.750  1.00 27.78  ? 221 SER C OG   1 
ATOM   7236  N N    . PRO C 2 204 ? 21.751  124.231 70.780  1.00 14.27  ? 222 PRO C N    1 
ATOM   7237  C CA   . PRO C 2 204 ? 22.200  124.745 72.043  1.00 10.17  ? 222 PRO C CA   1 
ATOM   7238  C C    . PRO C 2 204 ? 22.567  123.641 72.933  1.00 10.73  ? 222 PRO C C    1 
ATOM   7239  O O    . PRO C 2 204 ? 21.986  122.593 72.893  1.00 15.04  ? 222 PRO C O    1 
ATOM   7240  C CB   . PRO C 2 204 ? 20.975  125.399 72.567  1.00 10.43  ? 222 PRO C CB   1 
ATOM   7241  C CG   . PRO C 2 204 ? 20.331  125.951 71.371  1.00 14.73  ? 222 PRO C CG   1 
ATOM   7242  C CD   . PRO C 2 204 ? 20.395  124.777 70.486  1.00 14.27  ? 222 PRO C CD   1 
ATOM   7243  N N    . ASN C 2 205 ? 23.533  123.880 73.778  1.00 9.93   ? 223 ASN C N    1 
ATOM   7244  C CA   . ASN C 2 205 ? 23.996  122.854 74.644  1.00 12.57  ? 223 ASN C CA   1 
ATOM   7245  C C    . ASN C 2 205 ? 24.692  123.421 75.802  1.00 13.22  ? 223 ASN C C    1 
ATOM   7246  O O    . ASN C 2 205 ? 25.025  124.585 75.814  1.00 14.49  ? 223 ASN C O    1 
ATOM   7247  C CB   . ASN C 2 205 ? 24.963  121.908 73.936  1.00 14.18  ? 223 ASN C CB   1 
ATOM   7248  C CG   . ASN C 2 205 ? 25.254  120.653 74.712  1.00 15.30  ? 223 ASN C CG   1 
ATOM   7249  O OD1  . ASN C 2 205 ? 24.408  120.174 75.450  1.00 25.34  ? 223 ASN C OD1  1 
ATOM   7250  N ND2  . ASN C 2 205 ? 26.459  120.134 74.577  1.00 11.59  ? 223 ASN C ND2  1 
ATOM   7251  N N    . PHE C 2 206 ? 24.987  122.567 76.756  1.00 11.71  ? 224 PHE C N    1 
ATOM   7252  C CA   . PHE C 2 206 ? 25.600  122.972 77.957  1.00 10.81  ? 224 PHE C CA   1 
ATOM   7253  C C    . PHE C 2 206 ? 27.061  122.867 77.729  1.00 12.93  ? 224 PHE C C    1 
ATOM   7254  O O    . PHE C 2 206 ? 27.482  122.052 76.953  1.00 14.53  ? 224 PHE C O    1 
ATOM   7255  C CB   . PHE C 2 206 ? 25.212  121.971 79.015  1.00 14.40  ? 224 PHE C CB   1 
ATOM   7256  C CG   . PHE C 2 206 ? 23.728  121.842 79.273  1.00 12.75  ? 224 PHE C CG   1 
ATOM   7257  C CD1  . PHE C 2 206 ? 22.869  122.918 79.174  1.00 12.89  ? 224 PHE C CD1  1 
ATOM   7258  C CD2  . PHE C 2 206 ? 23.209  120.628 79.681  1.00 10.99  ? 224 PHE C CD2  1 
ATOM   7259  C CE1  . PHE C 2 206 ? 21.523  122.775 79.441  1.00 11.26  ? 224 PHE C CE1  1 
ATOM   7260  C CE2  . PHE C 2 206 ? 21.868  120.482 79.950  1.00 9.59   ? 224 PHE C CE2  1 
ATOM   7261  C CZ   . PHE C 2 206 ? 21.027  121.558 79.835  1.00 11.84  ? 224 PHE C CZ   1 
ATOM   7262  N N    . THR C 2 207 ? 27.858  123.677 78.416  1.00 13.91  ? 225 THR C N    1 
ATOM   7263  C CA   . THR C 2 207 ? 29.299  123.689 78.243  1.00 11.10  ? 225 THR C CA   1 
ATOM   7264  C C    . THR C 2 207 ? 29.888  122.525 78.957  1.00 16.72  ? 225 THR C C    1 
ATOM   7265  O O    . THR C 2 207 ? 31.076  122.283 78.891  1.00 22.86  ? 225 THR C O    1 
ATOM   7266  C CB   . THR C 2 207 ? 29.814  124.972 78.809  1.00 10.60  ? 225 THR C CB   1 
ATOM   7267  O OG1  . THR C 2 207 ? 29.216  126.046 78.078  1.00 11.65  ? 225 THR C OG1  1 
ATOM   7268  C CG2  . THR C 2 207 ? 31.311  125.059 78.670  1.00 16.25  ? 225 THR C CG2  1 
ATOM   7269  N N    . ASP C 2 208 ? 29.031  121.725 79.561  1.00 19.18  ? 226 ASP C N    1 
ATOM   7270  C CA   . ASP C 2 208 ? 29.454  120.593 80.336  1.00 15.70  ? 226 ASP C CA   1 
ATOM   7271  C C    . ASP C 2 208 ? 29.256  119.333 79.530  1.00 15.14  ? 226 ASP C C    1 
ATOM   7272  O O    . ASP C 2 208 ? 29.722  118.282 79.922  1.00 15.38  ? 226 ASP C O    1 
ATOM   7273  C CB   . ASP C 2 208 ? 28.547  120.581 81.562  1.00 15.73  ? 226 ASP C CB   1 
ATOM   7274  C CG   . ASP C 2 208 ? 29.237  120.115 82.815  1.00 31.08  ? 226 ASP C CG   1 
ATOM   7275  O OD1  . ASP C 2 208 ? 30.362  119.589 82.740  1.00 42.39  ? 226 ASP C OD1  1 
ATOM   7276  O OD2  . ASP C 2 208 ? 28.632  120.265 83.893  1.00 27.23  ? 226 ASP C OD2  1 
ATOM   7277  N N    . ASN C 2 209 ? 28.573  119.416 78.398  1.00 14.82  ? 227 ASN C N    1 
ATOM   7278  C CA   . ASN C 2 209 ? 28.256  118.226 77.595  1.00 16.42  ? 227 ASN C CA   1 
ATOM   7279  C C    . ASN C 2 209 ? 28.970  118.208 76.272  1.00 10.41  ? 227 ASN C C    1 
ATOM   7280  O O    . ASN C 2 209 ? 29.183  117.175 75.691  1.00 10.66  ? 227 ASN C O    1 
ATOM   7281  C CB   . ASN C 2 209 ? 26.733  118.115 77.373  1.00 10.91  ? 227 ASN C CB   1 
ATOM   7282  C CG   . ASN C 2 209 ? 26.281  116.720 77.043  1.00 13.39  ? 227 ASN C CG   1 
ATOM   7283  O OD1  . ASN C 2 209 ? 26.867  115.740 77.480  1.00 21.91  ? 227 ASN C OD1  1 
ATOM   7284  N ND2  . ASN C 2 209 ? 25.212  116.624 76.279  1.00 16.41  ? 227 ASN C ND2  1 
ATOM   7285  N N    . LEU C 2 210 ? 29.380  119.350 75.808  1.00 8.73   ? 228 LEU C N    1 
ATOM   7286  C CA   . LEU C 2 210 ? 29.997  119.427 74.543  1.00 7.90   ? 228 LEU C CA   1 
ATOM   7287  C C    . LEU C 2 210 ? 31.196  118.548 74.516  1.00 10.72  ? 228 LEU C C    1 
ATOM   7288  O O    . LEU C 2 210 ? 31.909  118.464 75.499  1.00 13.06  ? 228 LEU C O    1 
ATOM   7289  C CB   . LEU C 2 210 ? 30.222  120.897 74.176  1.00 7.84   ? 228 LEU C CB   1 
ATOM   7290  C CG   . LEU C 2 210 ? 31.282  121.936 74.521  1.00 13.52  ? 228 LEU C CG   1 
ATOM   7291  C CD1  . LEU C 2 210 ? 30.569  123.271 74.552  1.00 8.71   ? 228 LEU C CD1  1 
ATOM   7292  C CD2  . LEU C 2 210 ? 32.062  121.704 75.802  1.00 13.69  ? 228 LEU C CD2  1 
ATOM   7293  N N    . VAL C 2 211 ? 31.453  117.894 73.395  1.00 12.06  ? 229 VAL C N    1 
ATOM   7294  C CA   . VAL C 2 211 ? 32.498  116.931 73.282  1.00 9.76   ? 229 VAL C CA   1 
ATOM   7295  C C    . VAL C 2 211 ? 33.430  117.433 72.236  1.00 9.28   ? 229 VAL C C    1 
ATOM   7296  O O    . VAL C 2 211 ? 33.091  118.316 71.483  1.00 8.26   ? 229 VAL C O    1 
ATOM   7297  C CB   . VAL C 2 211 ? 31.873  115.585 72.916  1.00 10.45  ? 229 VAL C CB   1 
ATOM   7298  C CG1  . VAL C 2 211 ? 31.728  115.401 71.420  1.00 14.22  ? 229 VAL C CG1  1 
ATOM   7299  C CG2  . VAL C 2 211 ? 32.571  114.412 73.584  1.00 8.75   ? 229 VAL C CG2  1 
ATOM   7300  N N    . PRO C 2 212 ? 34.647  116.901 72.219  1.00 9.85   ? 230 PRO C N    1 
ATOM   7301  C CA   . PRO C 2 212 ? 35.564  117.301 71.201  1.00 10.31  ? 230 PRO C CA   1 
ATOM   7302  C C    . PRO C 2 212 ? 34.957  117.222 69.820  1.00 14.88  ? 230 PRO C C    1 
ATOM   7303  O O    . PRO C 2 212 ? 34.333  116.244 69.477  1.00 16.80  ? 230 PRO C O    1 
ATOM   7304  C CB   . PRO C 2 212 ? 36.633  116.282 71.400  1.00 7.54   ? 230 PRO C CB   1 
ATOM   7305  C CG   . PRO C 2 212 ? 36.549  115.957 72.844  1.00 6.12   ? 230 PRO C CG   1 
ATOM   7306  C CD   . PRO C 2 212 ? 35.092  115.975 73.187  1.00 10.75  ? 230 PRO C CD   1 
ATOM   7307  N N    . VAL C 2 213 ? 35.163  118.251 69.017  1.00 18.40  ? 231 VAL C N    1 
ATOM   7308  C CA   . VAL C 2 213 ? 34.557  118.353 67.714  1.00 12.56  ? 231 VAL C CA   1 
ATOM   7309  C C    . VAL C 2 213 ? 34.988  117.316 66.790  1.00 12.95  ? 231 VAL C C    1 
ATOM   7310  O O    . VAL C 2 213 ? 36.147  116.956 66.759  1.00 15.10  ? 231 VAL C O    1 
ATOM   7311  C CB   . VAL C 2 213 ? 34.756  119.804 67.177  1.00 13.39  ? 231 VAL C CB   1 
ATOM   7312  C CG1  . VAL C 2 213 ? 36.184  120.280 67.350  1.00 18.45  ? 231 VAL C CG1  1 
ATOM   7313  C CG2  . VAL C 2 213 ? 34.245  119.993 65.762  1.00 16.39  ? 231 VAL C CG2  1 
ATOM   7314  N N    . ARG C 2 214 ? 34.052  116.853 66.001  1.00 16.31  ? 232 ARG C N    1 
ATOM   7315  C CA   . ARG C 2 214 ? 34.293  115.755 65.145  1.00 18.38  ? 232 ARG C CA   1 
ATOM   7316  C C    . ARG C 2 214 ? 33.435  116.139 64.033  1.00 17.77  ? 232 ARG C C    1 
ATOM   7317  O O    . ARG C 2 214 ? 32.723  117.111 64.114  1.00 17.58  ? 232 ARG C O    1 
ATOM   7318  C CB   . ARG C 2 214 ? 33.740  114.507 65.809  1.00 14.89  ? 232 ARG C CB   1 
ATOM   7319  C CG   . ARG C 2 214 ? 32.328  114.698 66.339  1.00 15.17  ? 232 ARG C CG   1 
ATOM   7320  C CD   . ARG C 2 214 ? 31.770  113.454 66.990  1.00 16.57  ? 232 ARG C CD   1 
ATOM   7321  N NE   . ARG C 2 214 ? 31.502  112.392 66.028  1.00 27.25  ? 232 ARG C NE   1 
ATOM   7322  C CZ   . ARG C 2 214 ? 30.663  111.386 66.248  1.00 31.45  ? 232 ARG C CZ   1 
ATOM   7323  N NH1  . ARG C 2 214 ? 30.001  111.312 67.394  1.00 28.77  ? 232 ARG C NH1  1 
ATOM   7324  N NH2  . ARG C 2 214 ? 30.469  110.466 65.322  1.00 29.62  ? 232 ARG C NH2  1 
ATOM   7325  N N    . ASP C 2 215 ? 33.510  115.303 63.015  1.00 16.82  ? 233 ASP C N    1 
ATOM   7326  C CA   . ASP C 2 215 ? 32.699  115.462 61.877  1.00 18.77  ? 233 ASP C CA   1 
ATOM   7327  C C    . ASP C 2 215 ? 31.566  114.508 62.066  1.00 12.04  ? 233 ASP C C    1 
ATOM   7328  O O    . ASP C 2 215 ? 31.735  113.314 62.208  1.00 10.01  ? 233 ASP C O    1 
ATOM   7329  C CB   . ASP C 2 215 ? 33.516  115.164 60.636  1.00 18.27  ? 233 ASP C CB   1 
ATOM   7330  C CG   . ASP C 2 215 ? 34.669  114.200 60.899  1.00 34.03  ? 233 ASP C CG   1 
ATOM   7331  O OD1  . ASP C 2 215 ? 35.599  114.553 61.651  1.00 37.78  ? 233 ASP C OD1  1 
ATOM   7332  O OD2  . ASP C 2 215 ? 34.672  113.090 60.331  1.00 45.10  ? 233 ASP C OD2  1 
ATOM   7333  N N    . VAL C 2 216 ? 30.390  115.064 62.086  1.00 10.19  ? 234 VAL C N    1 
ATOM   7334  C CA   . VAL C 2 216 ? 29.247  114.282 62.248  1.00 14.88  ? 234 VAL C CA   1 
ATOM   7335  C C    . VAL C 2 216 ? 28.455  114.242 60.957  1.00 18.13  ? 234 VAL C C    1 
ATOM   7336  O O    . VAL C 2 216 ? 28.331  115.216 60.258  1.00 14.00  ? 234 VAL C O    1 
ATOM   7337  C CB   . VAL C 2 216 ? 28.439  114.777 63.423  1.00 14.67  ? 234 VAL C CB   1 
ATOM   7338  C CG1  . VAL C 2 216 ? 27.661  116.029 63.088  1.00 11.82  ? 234 VAL C CG1  1 
ATOM   7339  C CG2  . VAL C 2 216 ? 27.487  113.683 63.829  1.00 18.65  ? 234 VAL C CG2  1 
ATOM   7340  N N    . PRO C 2 217 ? 27.966  113.064 60.603  1.00 18.05  ? 235 PRO C N    1 
ATOM   7341  C CA   . PRO C 2 217 ? 27.251  112.903 59.364  1.00 11.09  ? 235 PRO C CA   1 
ATOM   7342  C C    . PRO C 2 217 ? 25.940  113.550 59.216  1.00 10.40  ? 235 PRO C C    1 
ATOM   7343  O O    . PRO C 2 217 ? 25.210  113.713 60.165  1.00 13.52  ? 235 PRO C O    1 
ATOM   7344  C CB   . PRO C 2 217 ? 27.064  111.422 59.315  1.00 11.20  ? 235 PRO C CB   1 
ATOM   7345  C CG   . PRO C 2 217 ? 28.283  110.872 59.934  1.00 20.24  ? 235 PRO C CG   1 
ATOM   7346  C CD   . PRO C 2 217 ? 28.476  111.777 61.102  1.00 16.66  ? 235 PRO C CD   1 
ATOM   7347  N N    . LYS C 2 218 ? 25.618  113.897 57.995  1.00 10.15  ? 236 LYS C N    1 
ATOM   7348  C CA   . LYS C 2 218 ? 24.364  114.505 57.710  1.00 13.05  ? 236 LYS C CA   1 
ATOM   7349  C C    . LYS C 2 218 ? 23.643  113.548 56.826  1.00 13.95  ? 236 LYS C C    1 
ATOM   7350  O O    . LYS C 2 218 ? 24.200  113.040 55.869  1.00 18.72  ? 236 LYS C O    1 
ATOM   7351  C CB   . LYS C 2 218 ? 24.604  115.818 56.985  1.00 17.73  ? 236 LYS C CB   1 
ATOM   7352  C CG   . LYS C 2 218 ? 23.401  116.721 56.798  1.00 17.37  ? 236 LYS C CG   1 
ATOM   7353  C CD   . LYS C 2 218 ? 23.819  118.031 56.153  1.00 16.30  ? 236 LYS C CD   1 
ATOM   7354  C CE   . LYS C 2 218 ? 22.632  118.961 55.958  1.00 22.01  ? 236 LYS C CE   1 
ATOM   7355  N NZ   . LYS C 2 218 ? 22.984  120.231 55.258  1.00 17.51  ? 236 LYS C NZ   1 
ATOM   7356  N N    . ILE C 2 219 ? 22.413  113.241 57.162  1.00 14.02  ? 237 ILE C N    1 
ATOM   7357  C CA   . ILE C 2 219 ? 21.609  112.347 56.376  1.00 15.43  ? 237 ILE C CA   1 
ATOM   7358  C C    . ILE C 2 219 ? 20.346  113.158 56.339  1.00 21.13  ? 237 ILE C C    1 
ATOM   7359  O O    . ILE C 2 219 ? 20.244  114.130 57.084  1.00 26.65  ? 237 ILE C O    1 
ATOM   7360  C CB   . ILE C 2 219 ? 21.350  111.016 57.094  1.00 8.93   ? 237 ILE C CB   1 
ATOM   7361  C CG1  . ILE C 2 219 ? 20.287  111.154 58.166  1.00 12.98  ? 237 ILE C CG1  1 
ATOM   7362  C CG2  . ILE C 2 219 ? 22.619  110.445 57.697  1.00 12.23  ? 237 ILE C CG2  1 
ATOM   7363  C CD1  . ILE C 2 219 ? 19.195  110.132 58.005  1.00 18.02  ? 237 ILE C CD1  1 
ATOM   7364  N N    . ALA C 2 220 ? 19.389  112.832 55.486  1.00 15.75  ? 238 ALA C N    1 
ATOM   7365  C CA   . ALA C 2 220 ? 18.117  113.535 55.530  1.00 12.88  ? 238 ALA C CA   1 
ATOM   7366  C C    . ALA C 2 220 ? 16.957  112.604 55.397  1.00 13.60  ? 238 ALA C C    1 
ATOM   7367  O O    . ALA C 2 220 ? 17.149  111.420 55.282  1.00 20.26  ? 238 ALA C O    1 
ATOM   7368  C CB   . ALA C 2 220 ? 18.069  114.620 54.506  1.00 16.36  ? 238 ALA C CB   1 
ATOM   7369  N N    . ILE C 2 221 ? 15.748  113.115 55.481  1.00 11.37  ? 239 ILE C N    1 
ATOM   7370  C CA   . ILE C 2 221 ? 14.555  112.293 55.355  1.00 17.79  ? 239 ILE C CA   1 
ATOM   7371  C C    . ILE C 2 221 ? 13.987  112.199 53.932  1.00 21.65  ? 239 ILE C C    1 
ATOM   7372  O O    . ILE C 2 221 ? 13.969  113.182 53.223  1.00 25.57  ? 239 ILE C O    1 
ATOM   7373  C CB   . ILE C 2 221 ? 13.516  112.769 56.382  1.00 19.41  ? 239 ILE C CB   1 
ATOM   7374  C CG1  . ILE C 2 221 ? 12.158  112.140 56.180  1.00 28.32  ? 239 ILE C CG1  1 
ATOM   7375  C CG2  . ILE C 2 221 ? 13.388  114.282 56.339  1.00 27.92  ? 239 ILE C CG2  1 
ATOM   7376  C CD1  . ILE C 2 221 ? 11.098  112.757 57.057  1.00 25.99  ? 239 ILE C CD1  1 
ATOM   7377  N N    . ASN C 2 222 ? 13.561  111.009 53.492  1.00 21.34  ? 240 ASN C N    1 
ATOM   7378  C CA   . ASN C 2 222 ? 12.953  110.865 52.178  1.00 27.54  ? 240 ASN C CA   1 
ATOM   7379  C C    . ASN C 2 222 ? 11.600  111.506 52.164  1.00 32.75  ? 240 ASN C C    1 
ATOM   7380  O O    . ASN C 2 222 ? 11.281  112.156 51.186  1.00 33.37  ? 240 ASN C O    1 
ATOM   7381  C CB   . ASN C 2 222 ? 12.832  109.422 51.735  1.00 20.76  ? 240 ASN C CB   1 
ATOM   7382  C CG   . ASN C 2 222 ? 12.805  109.287 50.244  1.00 27.05  ? 240 ASN C CG   1 
ATOM   7383  O OD1  . ASN C 2 222 ? 13.824  109.429 49.579  1.00 24.44  ? 240 ASN C OD1  1 
ATOM   7384  N ND2  . ASN C 2 222 ? 11.635  109.016 49.705  1.00 42.60  ? 240 ASN C ND2  1 
ATOM   7385  N N    . GLU C 2 223 ? 10.749  111.249 53.134  1.00 24.13  ? 241 GLU C N    1 
ATOM   7386  C CA   . GLU C 2 223 ? 9.505   111.954 53.275  1.00 21.59  ? 241 GLU C CA   1 
ATOM   7387  C C    . GLU C 2 223 ? 8.620   111.873 52.086  1.00 28.50  ? 241 GLU C C    1 
ATOM   7388  O O    . GLU C 2 223 ? 7.677   112.630 51.925  1.00 29.06  ? 241 GLU C O    1 
ATOM   7389  C CB   . GLU C 2 223 ? 9.727   113.405 53.713  1.00 23.56  ? 241 GLU C CB   1 
ATOM   7390  C CG   . GLU C 2 223 ? 10.484  114.327 52.769  1.00 27.23  ? 241 GLU C CG   1 
ATOM   7391  C CD   . GLU C 2 223 ? 10.736  115.691 53.373  1.00 42.59  ? 241 GLU C CD   1 
ATOM   7392  O OE1  . GLU C 2 223 ? 10.052  116.044 54.357  1.00 49.77  ? 241 GLU C OE1  1 
ATOM   7393  O OE2  . GLU C 2 223 ? 11.608  116.412 52.847  1.00 52.88  ? 241 GLU C OE2  1 
ATOM   7394  N N    . LYS C 2 224 ? 8.904   110.901 51.252  1.00 29.03  ? 242 LYS C N    1 
ATOM   7395  C CA   . LYS C 2 224 ? 8.102   110.676 50.078  1.00 27.29  ? 242 LYS C CA   1 
ATOM   7396  C C    . LYS C 2 224 ? 7.672   109.259 50.308  1.00 24.93  ? 242 LYS C C    1 
ATOM   7397  O O    . LYS C 2 224 ? 6.911   108.701 49.546  1.00 24.40  ? 242 LYS C O    1 
ATOM   7398  C CB   . LYS C 2 224 ? 8.822   110.909 48.750  1.00 34.72  ? 242 LYS C CB   1 
ATOM   7399  C CG   . LYS C 2 224 ? 8.585   112.294 48.173  1.00 21.35  ? 242 LYS C CG   1 
ATOM   7400  C CD   . LYS C 2 224 ? 9.755   112.750 47.328  1.00 14.72  ? 242 LYS C CD   1 
ATOM   7401  C CE   . LYS C 2 224 ? 9.676   114.245 47.074  1.00 19.97  ? 242 LYS C CE   1 
ATOM   7402  N NZ   . LYS C 2 224 ? 10.933  114.803 46.500  1.00 18.58  ? 242 LYS C NZ   1 
ATOM   7403  N N    . VAL C 2 225 ? 8.154   108.666 51.377  1.00 27.88  ? 243 VAL C N    1 
ATOM   7404  C CA   . VAL C 2 225 ? 7.701   107.356 51.739  1.00 26.69  ? 243 VAL C CA   1 
ATOM   7405  C C    . VAL C 2 225 ? 6.322   107.477 52.317  1.00 22.34  ? 243 VAL C C    1 
ATOM   7406  O O    . VAL C 2 225 ? 5.916   108.529 52.789  1.00 22.59  ? 243 VAL C O    1 
ATOM   7407  C CB   . VAL C 2 225 ? 8.632   106.642 52.734  1.00 18.12  ? 243 VAL C CB   1 
ATOM   7408  C CG1  . VAL C 2 225 ? 10.063  106.683 52.249  1.00 23.92  ? 243 VAL C CG1  1 
ATOM   7409  C CG2  . VAL C 2 225 ? 8.527   107.272 54.086  1.00 23.57  ? 243 VAL C CG2  1 
ATOM   7410  N N    . ALA C 2 226 ? 5.576   106.397 52.246  1.00 19.18  ? 244 ALA C N    1 
ATOM   7411  C CA   . ALA C 2 226 ? 4.258   106.404 52.799  1.00 21.88  ? 244 ALA C CA   1 
ATOM   7412  C C    . ALA C 2 226 ? 4.250   105.514 54.000  1.00 22.31  ? 244 ALA C C    1 
ATOM   7413  O O    . ALA C 2 226 ? 4.703   104.380 53.939  1.00 22.45  ? 244 ALA C O    1 
ATOM   7414  C CB   . ALA C 2 226 ? 3.268   105.933 51.779  1.00 20.95  ? 244 ALA C CB   1 
ATOM   7415  N N    . GLY C 2 227 ? 3.769   106.040 55.111  1.00 21.24  ? 245 GLY C N    1 
ATOM   7416  C CA   . GLY C 2 227 ? 3.748   105.283 56.324  1.00 17.48  ? 245 GLY C CA   1 
ATOM   7417  C C    . GLY C 2 227 ? 5.136   105.104 56.826  1.00 17.44  ? 245 GLY C C    1 
ATOM   7418  O O    . GLY C 2 227 ? 5.446   104.106 57.426  1.00 21.08  ? 245 GLY C O    1 
ATOM   7419  N N    . GLY C 2 228 ? 5.970   106.084 56.606  1.00 13.29  ? 246 GLY C N    1 
ATOM   7420  C CA   . GLY C 2 228 ? 7.338   105.994 57.014  1.00 12.02  ? 246 GLY C CA   1 
ATOM   7421  C C    . GLY C 2 228 ? 7.434   106.161 58.474  1.00 21.61  ? 246 GLY C C    1 
ATOM   7422  O O    . GLY C 2 228 ? 6.574   106.740 59.077  1.00 28.73  ? 246 GLY C O    1 
ATOM   7423  N N    . TYR C 2 229 ? 8.518   105.742 59.060  1.00 18.63  ? 247 TYR C N    1 
ATOM   7424  C CA   . TYR C 2 229 ? 8.633   105.767 60.475  1.00 14.48  ? 247 TYR C CA   1 
ATOM   7425  C C    . TYR C 2 229 ? 8.459   107.136 60.891  1.00 15.27  ? 247 TYR C C    1 
ATOM   7426  O O    . TYR C 2 229 ? 7.714   107.388 61.773  1.00 18.86  ? 247 TYR C O    1 
ATOM   7427  C CB   . TYR C 2 229 ? 10.074  105.410 60.781  1.00 20.85  ? 247 TYR C CB   1 
ATOM   7428  C CG   . TYR C 2 229 ? 10.397  105.001 62.184  1.00 22.02  ? 247 TYR C CG   1 
ATOM   7429  C CD1  . TYR C 2 229 ? 9.960   103.796 62.685  1.00 24.99  ? 247 TYR C CD1  1 
ATOM   7430  C CD2  . TYR C 2 229 ? 11.178  105.796 62.989  1.00 16.05  ? 247 TYR C CD2  1 
ATOM   7431  C CE1  . TYR C 2 229 ? 10.265  103.407 63.962  1.00 19.13  ? 247 TYR C CE1  1 
ATOM   7432  C CE2  . TYR C 2 229 ? 11.486  105.410 64.266  1.00 16.68  ? 247 TYR C CE2  1 
ATOM   7433  C CZ   . TYR C 2 229 ? 11.029  104.221 64.740  1.00 17.01  ? 247 TYR C CZ   1 
ATOM   7434  O OH   . TYR C 2 229 ? 11.323  103.833 66.004  1.00 17.63  ? 247 TYR C OH   1 
ATOM   7435  N N    . SER C 2 230 ? 9.077   108.067 60.218  1.00 20.03  ? 248 SER C N    1 
ATOM   7436  C CA   . SER C 2 230 ? 9.054   109.440 60.641  1.00 16.08  ? 248 SER C CA   1 
ATOM   7437  C C    . SER C 2 230 ? 7.655   109.984 60.698  1.00 18.38  ? 248 SER C C    1 
ATOM   7438  O O    . SER C 2 230 ? 7.382   110.827 61.524  1.00 20.67  ? 248 SER C O    1 
ATOM   7439  C CB   . SER C 2 230 ? 9.954   110.237 59.746  1.00 20.03  ? 248 SER C CB   1 
ATOM   7440  O OG   . SER C 2 230 ? 11.286  109.812 59.909  1.00 33.24  ? 248 SER C OG   1 
ATOM   7441  N N    . LYS C 2 231 ? 6.790   109.602 59.769  1.00 21.30  ? 249 LYS C N    1 
ATOM   7442  C CA   . LYS C 2 231 ? 5.380   109.977 59.799  1.00 16.59  ? 249 LYS C CA   1 
ATOM   7443  C C    . LYS C 2 231 ? 4.579   109.335 60.888  1.00 15.16  ? 249 LYS C C    1 
ATOM   7444  O O    . LYS C 2 231 ? 3.744   109.979 61.493  1.00 18.63  ? 249 LYS C O    1 
ATOM   7445  C CB   . LYS C 2 231 ? 4.776   109.624 58.456  1.00 22.91  ? 249 LYS C CB   1 
ATOM   7446  C CG   . LYS C 2 231 ? 5.276   110.463 57.296  1.00 17.74  ? 249 LYS C CG   1 
ATOM   7447  C CD   . LYS C 2 231 ? 4.384   111.674 57.070  1.00 15.51  ? 249 LYS C CD   1 
ATOM   7448  C CE   . LYS C 2 231 ? 5.045   112.676 56.136  1.00 25.17  ? 249 LYS C CE   1 
ATOM   7449  N NZ   . LYS C 2 231 ? 5.529   112.054 54.873  1.00 33.30  ? 249 LYS C NZ   1 
ATOM   7450  N N    . THR C 2 232 ? 4.815   108.060 61.128  1.00 13.95  ? 250 THR C N    1 
ATOM   7451  C CA   . THR C 2 232 ? 4.111   107.321 62.158  1.00 19.07  ? 250 THR C CA   1 
ATOM   7452  C C    . THR C 2 232 ? 4.722   107.307 63.550  1.00 15.89  ? 250 THR C C    1 
ATOM   7453  O O    . THR C 2 232 ? 4.041   106.953 64.494  1.00 18.82  ? 250 THR C O    1 
ATOM   7454  C CB   . THR C 2 232 ? 3.937   105.873 61.713  1.00 22.49  ? 250 THR C CB   1 
ATOM   7455  O OG1  . THR C 2 232 ? 5.142   105.140 61.949  1.00 28.65  ? 250 THR C OG1  1 
ATOM   7456  C CG2  . THR C 2 232 ? 3.569   105.808 60.250  1.00 14.19  ? 250 THR C CG2  1 
ATOM   7457  N N    . LYS C 2 233 ? 5.990   107.643 63.694  1.00 15.68  ? 251 LYS C N    1 
ATOM   7458  C CA   . LYS C 2 233 ? 6.652   107.733 64.975  1.00 14.76  ? 251 LYS C CA   1 
ATOM   7459  C C    . LYS C 2 233 ? 7.251   109.054 64.854  1.00 14.92  ? 251 LYS C C    1 
ATOM   7460  O O    . LYS C 2 233 ? 8.384   109.185 64.469  1.00 13.65  ? 251 LYS C O    1 
ATOM   7461  C CB   . LYS C 2 233 ? 7.762   106.725 65.146  1.00 13.08  ? 251 LYS C CB   1 
ATOM   7462  C CG   . LYS C 2 233 ? 8.231   106.571 66.575  1.00 12.16  ? 251 LYS C CG   1 
ATOM   7463  C CD   . LYS C 2 233 ? 7.924   105.196 67.124  1.00 11.80  ? 251 LYS C CD   1 
ATOM   7464  C CE   . LYS C 2 233 ? 8.241   105.143 68.606  1.00 18.80  ? 251 LYS C CE   1 
ATOM   7465  N NZ   . LYS C 2 233 ? 7.831   103.859 69.236  1.00 27.44  ? 251 LYS C NZ   1 
ATOM   7466  N N    . PRO C 2 234 ? 6.482   110.072 65.144  1.00 20.32  ? 252 PRO C N    1 
ATOM   7467  C CA   . PRO C 2 234 ? 6.946   111.439 65.056  1.00 20.45  ? 252 PRO C CA   1 
ATOM   7468  C C    . PRO C 2 234 ? 7.589   111.832 66.352  1.00 21.63  ? 252 PRO C C    1 
ATOM   7469  O O    . PRO C 2 234 ? 7.968   112.970 66.531  1.00 22.51  ? 252 PRO C O    1 
ATOM   7470  C CB   . PRO C 2 234 ? 5.638   112.195 64.872  1.00 18.30  ? 252 PRO C CB   1 
ATOM   7471  C CG   . PRO C 2 234 ? 4.512   111.235 65.032  1.00 19.05  ? 252 PRO C CG   1 
ATOM   7472  C CD   . PRO C 2 234 ? 5.095   110.006 65.622  1.00 23.51  ? 252 PRO C CD   1 
ATOM   7473  N N    . THR C 2 235 ? 7.704   110.895 67.262  1.00 15.96  ? 253 THR C N    1 
ATOM   7474  C CA   . THR C 2 235 ? 8.201   111.158 68.555  1.00 13.25  ? 253 THR C CA   1 
ATOM   7475  C C    . THR C 2 235 ? 9.649   110.816 68.649  1.00 11.95  ? 253 THR C C    1 
ATOM   7476  O O    . THR C 2 235 ? 10.319  111.183 69.589  1.00 17.48  ? 253 THR C O    1 
ATOM   7477  C CB   . THR C 2 235 ? 7.394   110.323 69.528  1.00 15.79  ? 253 THR C CB   1 
ATOM   7478  O OG1  . THR C 2 235 ? 7.325   108.977 69.062  1.00 15.04  ? 253 THR C OG1  1 
ATOM   7479  C CG2  . THR C 2 235 ? 6.001   110.869 69.642  1.00 15.31  ? 253 THR C CG2  1 
ATOM   7480  N N    . THR C 2 236 ? 10.152  110.114 67.664  1.00 12.73  ? 254 THR C N    1 
ATOM   7481  C CA   . THR C 2 236 ? 11.530  109.723 67.678  1.00 15.78  ? 254 THR C CA   1 
ATOM   7482  C C    . THR C 2 236 ? 12.315  110.681 66.921  1.00 18.84  ? 254 THR C C    1 
ATOM   7483  O O    . THR C 2 236 ? 12.016  110.955 65.781  1.00 17.75  ? 254 THR C O    1 
ATOM   7484  C CB   . THR C 2 236 ? 11.822  108.399 67.002  1.00 16.15  ? 254 THR C CB   1 
ATOM   7485  O OG1  . THR C 2 236 ? 11.004  108.270 65.842  1.00 22.28  ? 254 THR C OG1  1 
ATOM   7486  C CG2  . THR C 2 236 ? 11.611  107.271 67.933  1.00 11.90  ? 254 THR C CG2  1 
ATOM   7487  N N    . PRO C 2 237 ? 13.365  111.241 67.577  1.00 16.89  ? 255 PRO C N    1 
ATOM   7488  C CA   . PRO C 2 237 ? 14.249  112.091 66.827  1.00 15.15  ? 255 PRO C CA   1 
ATOM   7489  C C    . PRO C 2 237 ? 14.857  111.408 65.638  1.00 17.15  ? 255 PRO C C    1 
ATOM   7490  O O    . PRO C 2 237 ? 14.917  110.198 65.582  1.00 16.52  ? 255 PRO C O    1 
ATOM   7491  C CB   . PRO C 2 237 ? 15.296  112.404 67.860  1.00 15.43  ? 255 PRO C CB   1 
ATOM   7492  C CG   . PRO C 2 237 ? 14.545  112.562 69.093  1.00 18.33  ? 255 PRO C CG   1 
ATOM   7493  C CD   . PRO C 2 237 ? 13.688  111.357 69.028  1.00 14.75  ? 255 PRO C CD   1 
ATOM   7494  N N    . PHE C 2 238 ? 15.395  112.181 64.711  1.00 15.31  ? 256 PHE C N    1 
ATOM   7495  C CA   . PHE C 2 238 ? 15.922  111.648 63.476  1.00 12.47  ? 256 PHE C CA   1 
ATOM   7496  C C    . PHE C 2 238 ? 17.390  111.756 63.313  1.00 12.74  ? 256 PHE C C    1 
ATOM   7497  O O    . PHE C 2 238 ? 17.928  112.832 63.338  1.00 18.20  ? 256 PHE C O    1 
ATOM   7498  C CB   . PHE C 2 238 ? 15.292  112.423 62.339  1.00 15.98  ? 256 PHE C CB   1 
ATOM   7499  C CG   . PHE C 2 238 ? 15.265  111.693 61.037  1.00 17.83  ? 256 PHE C CG   1 
ATOM   7500  C CD1  . PHE C 2 238 ? 14.278  110.776 60.779  1.00 17.96  ? 256 PHE C CD1  1 
ATOM   7501  C CD2  . PHE C 2 238 ? 16.206  111.945 60.068  1.00 11.29  ? 256 PHE C CD2  1 
ATOM   7502  C CE1  . PHE C 2 238 ? 14.240  110.108 59.588  1.00 18.42  ? 256 PHE C CE1  1 
ATOM   7503  C CE2  . PHE C 2 238 ? 16.171  111.279 58.879  1.00 14.11  ? 256 PHE C CE2  1 
ATOM   7504  C CZ   . PHE C 2 238 ? 15.190  110.358 58.637  1.00 19.06  ? 256 PHE C CZ   1 
ATOM   7505  N N    . VAL C 2 239 ? 18.049  110.628 63.189  1.00 11.90  ? 257 VAL C N    1 
ATOM   7506  C CA   . VAL C 2 239 ? 19.460  110.579 62.995  1.00 16.12  ? 257 VAL C CA   1 
ATOM   7507  C C    . VAL C 2 239 ? 19.852  109.633 61.860  1.00 15.39  ? 257 VAL C C    1 
ATOM   7508  O O    . VAL C 2 239 ? 20.857  109.871 61.225  1.00 15.95  ? 257 VAL C O    1 
ATOM   7509  C CB   . VAL C 2 239 ? 20.110  110.173 64.315  1.00 19.71  ? 257 VAL C CB   1 
ATOM   7510  C CG1  . VAL C 2 239 ? 19.861  111.235 65.371  1.00 12.35  ? 257 VAL C CG1  1 
ATOM   7511  C CG2  . VAL C 2 239 ? 19.570  108.840 64.785  1.00 21.25  ? 257 VAL C CG2  1 
ATOM   7512  N N    . ALA C 2 240 ? 19.096  108.563 61.615  1.00 17.66  ? 258 ALA C N    1 
ATOM   7513  C CA   . ALA C 2 240 ? 19.280  107.621 60.477  1.00 17.73  ? 258 ALA C CA   1 
ATOM   7514  C C    . ALA C 2 240 ? 17.859  107.280 60.556  1.00 22.50  ? 258 ALA C C    1 
ATOM   7515  O O    . ALA C 2 240 ? 17.215  107.863 61.364  1.00 39.70  ? 258 ALA C O    1 
ATOM   7516  C CB   . ALA C 2 240 ? 20.099  106.438 60.771  1.00 19.19  ? 258 ALA C CB   1 
ATOM   7517  N N    . SER C 2 241 ? 17.268  106.494 59.684  1.00 14.11  ? 259 SER C N    1 
ATOM   7518  C CA   . SER C 2 241 ? 15.815  106.308 59.877  1.00 15.01  ? 259 SER C CA   1 
ATOM   7519  C C    . SER C 2 241 ? 15.263  105.103 60.554  1.00 20.91  ? 259 SER C C    1 
ATOM   7520  O O    . SER C 2 241 ? 14.144  105.131 61.002  1.00 35.99  ? 259 SER C O    1 
ATOM   7521  C CB   . SER C 2 241 ? 14.937  106.720 58.726  1.00 12.51  ? 259 SER C CB   1 
ATOM   7522  O OG   . SER C 2 241 ? 13.587  106.778 59.121  1.00 14.91  ? 259 SER C OG   1 
ATOM   7523  N N    . LEU C 2 242 ? 16.004  104.043 60.640  1.00 16.72  ? 260 LEU C N    1 
ATOM   7524  C CA   . LEU C 2 242 ? 15.543  102.928 61.389  1.00 16.45  ? 260 LEU C CA   1 
ATOM   7525  C C    . LEU C 2 242 ? 16.872  102.310 61.340  1.00 23.95  ? 260 LEU C C    1 
ATOM   7526  O O    . LEU C 2 242 ? 17.712  102.839 60.654  1.00 35.89  ? 260 LEU C O    1 
ATOM   7527  C CB   . LEU C 2 242 ? 14.513  102.128 60.625  1.00 14.98  ? 260 LEU C CB   1 
ATOM   7528  C CG   . LEU C 2 242 ? 13.671  101.140 61.424  1.00 24.25  ? 260 LEU C CG   1 
ATOM   7529  C CD1  . LEU C 2 242 ? 13.258  101.735 62.756  1.00 22.15  ? 260 LEU C CD1  1 
ATOM   7530  C CD2  . LEU C 2 242 ? 12.457  100.718 60.626  1.00 21.11  ? 260 LEU C CD2  1 
ATOM   7531  N N    . SER C 2 243 ? 17.128  101.230 62.043  1.00 19.28  ? 261 SER C N    1 
ATOM   7532  C CA   . SER C 2 243 ? 18.455  100.725 62.032  1.00 21.31  ? 261 SER C CA   1 
ATOM   7533  C C    . SER C 2 243 ? 18.586  99.341  61.593  1.00 30.17  ? 261 SER C C    1 
ATOM   7534  O O    . SER C 2 243 ? 17.902  98.471  62.094  1.00 31.83  ? 261 SER C O    1 
ATOM   7535  C CB   . SER C 2 243 ? 19.054  100.630 63.416  1.00 16.61  ? 261 SER C CB   1 
ATOM   7536  O OG   . SER C 2 243 ? 20.352  100.082 63.388  1.00 17.40  ? 261 SER C OG   1 
ATOM   7537  N N    . GLY C 2 244 ? 19.534  99.104  60.708  1.00 27.58  ? 262 GLY C N    1 
ATOM   7538  C CA   . GLY C 2 244 ? 19.669  97.801  60.163  1.00 23.01  ? 262 GLY C CA   1 
ATOM   7539  C C    . GLY C 2 244 ? 20.984  97.213  60.340  1.00 27.02  ? 262 GLY C C    1 
ATOM   7540  O O    . GLY C 2 244 ? 21.572  96.738  59.410  1.00 42.92  ? 262 GLY C O    1 
ATOM   7541  N N    . THR C 2 245 ? 21.553  97.375  61.490  1.00 22.76  ? 263 THR C N    1 
ATOM   7542  C CA   . THR C 2 245 ? 22.757  96.668  61.761  1.00 23.54  ? 263 THR C CA   1 
ATOM   7543  C C    . THR C 2 245 ? 22.217  95.820  62.861  1.00 25.80  ? 263 THR C C    1 
ATOM   7544  O O    . THR C 2 245 ? 22.845  94.892  63.311  1.00 24.71  ? 263 THR C O    1 
ATOM   7545  C CB   . THR C 2 245 ? 23.756  97.707  62.205  1.00 19.03  ? 263 THR C CB   1 
ATOM   7546  O OG1  . THR C 2 245 ? 23.925  98.656  61.152  1.00 24.96  ? 263 THR C OG1  1 
ATOM   7547  C CG2  . THR C 2 245 ? 25.064  97.113  62.496  1.00 19.29  ? 263 THR C CG2  1 
ATOM   7548  N N    . THR C 2 246 ? 21.018  96.150  63.307  1.00 24.06  ? 264 THR C N    1 
ATOM   7549  C CA   . THR C 2 246 ? 20.398  95.449  64.395  1.00 16.92  ? 264 THR C CA   1 
ATOM   7550  C C    . THR C 2 246 ? 20.053  94.067  64.020  1.00 17.47  ? 264 THR C C    1 
ATOM   7551  O O    . THR C 2 246 ? 20.129  93.180  64.820  1.00 18.12  ? 264 THR C O    1 
ATOM   7552  C CB   . THR C 2 246 ? 19.211  96.242  64.889  1.00 15.74  ? 264 THR C CB   1 
ATOM   7553  O OG1  . THR C 2 246 ? 18.258  96.391  63.837  1.00 32.19  ? 264 THR C OG1  1 
ATOM   7554  C CG2  . THR C 2 246 ? 19.663  97.596  65.338  1.00 10.69  ? 264 THR C CG2  1 
ATOM   7555  N N    . TYR C 2 247 ? 19.626  93.884  62.804  1.00 17.55  ? 265 TYR C N    1 
ATOM   7556  C CA   . TYR C 2 247 ? 19.309  92.576  62.300  1.00 20.31  ? 265 TYR C CA   1 
ATOM   7557  C C    . TYR C 2 247 ? 20.569  91.783  62.255  1.00 21.52  ? 265 TYR C C    1 
ATOM   7558  O O    . TYR C 2 247 ? 20.563  90.595  62.480  1.00 22.02  ? 265 TYR C O    1 
ATOM   7559  C CB   . TYR C 2 247 ? 18.665  92.689  60.934  1.00 20.79  ? 265 TYR C CB   1 
ATOM   7560  C CG   . TYR C 2 247 ? 17.295  93.288  60.929  1.00 18.29  ? 265 TYR C CG   1 
ATOM   7561  C CD1  . TYR C 2 247 ? 16.232  92.617  61.487  1.00 17.97  ? 265 TYR C CD1  1 
ATOM   7562  C CD2  . TYR C 2 247 ? 17.059  94.516  60.351  1.00 16.36  ? 265 TYR C CD2  1 
ATOM   7563  C CE1  . TYR C 2 247 ? 14.971  93.157  61.482  1.00 17.83  ? 265 TYR C CE1  1 
ATOM   7564  C CE2  . TYR C 2 247 ? 15.802  95.060  60.343  1.00 15.81  ? 265 TYR C CE2  1 
ATOM   7565  C CZ   . TYR C 2 247 ? 14.766  94.371  60.908  1.00 18.70  ? 265 TYR C CZ   1 
ATOM   7566  O OH   . TYR C 2 247 ? 13.511  94.906  60.906  1.00 23.29  ? 265 TYR C OH   1 
ATOM   7567  N N    . SER C 2 248 ? 21.660  92.416  61.914  1.00 21.53  ? 266 SER C N    1 
ATOM   7568  C CA   . SER C 2 248 ? 22.935  91.757  61.967  1.00 24.68  ? 266 SER C CA   1 
ATOM   7569  C C    . SER C 2 248 ? 23.296  91.355  63.400  1.00 22.95  ? 266 SER C C    1 
ATOM   7570  O O    . SER C 2 248 ? 23.887  90.321  63.609  1.00 25.96  ? 266 SER C O    1 
ATOM   7571  C CB   . SER C 2 248 ? 23.993  92.688  61.388  1.00 24.14  ? 266 SER C CB   1 
ATOM   7572  O OG   . SER C 2 248 ? 23.649  93.135  60.098  1.00 25.33  ? 266 SER C OG   1 
ATOM   7573  N N    . LEU C 2 249 ? 22.986  92.178  64.387  1.00 17.00  ? 267 LEU C N    1 
ATOM   7574  C CA   . LEU C 2 249 ? 23.234  91.818  65.770  1.00 18.38  ? 267 LEU C CA   1 
ATOM   7575  C C    . LEU C 2 249 ? 22.436  90.612  66.089  1.00 21.64  ? 267 LEU C C    1 
ATOM   7576  O O    . LEU C 2 249 ? 22.926  89.698  66.717  1.00 21.81  ? 267 LEU C O    1 
ATOM   7577  C CB   . LEU C 2 249 ? 22.813  92.940  66.705  1.00 15.02  ? 267 LEU C CB   1 
ATOM   7578  C CG   . LEU C 2 249 ? 22.714  92.816  68.223  1.00 13.68  ? 267 LEU C CG   1 
ATOM   7579  C CD1  . LEU C 2 249 ? 24.059  92.960  68.900  1.00 12.17  ? 267 LEU C CD1  1 
ATOM   7580  C CD2  . LEU C 2 249 ? 21.752  93.856  68.762  1.00 11.34  ? 267 LEU C CD2  1 
ATOM   7581  N N    . MET C 2 250 ? 21.204  90.586  65.643  1.00 18.57  ? 268 MET C N    1 
ATOM   7582  C CA   . MET C 2 250 ? 20.346  89.462  65.876  1.00 19.57  ? 268 MET C CA   1 
ATOM   7583  C C    . MET C 2 250 ? 20.791  88.213  65.114  1.00 22.35  ? 268 MET C C    1 
ATOM   7584  O O    . MET C 2 250 ? 20.352  87.138  65.430  1.00 25.08  ? 268 MET C O    1 
ATOM   7585  C CB   . MET C 2 250 ? 18.919  89.921  65.742  1.00 14.10  ? 268 MET C CB   1 
ATOM   7586  C CG   . MET C 2 250 ? 18.644  91.106  66.631  1.00 14.43  ? 268 MET C CG   1 
ATOM   7587  S SD   . MET C 2 250 ? 17.053  90.935  67.406  1.00 22.85  ? 268 MET C SD   1 
ATOM   7588  C CE   . MET C 2 250 ? 17.111  89.187  67.735  1.00 31.96  ? 268 MET C CE   1 
ATOM   7589  N N    . VAL C 2 251 ? 21.577  88.345  64.059  1.00 18.65  ? 269 VAL C N    1 
ATOM   7590  C CA   . VAL C 2 251 ? 22.203  87.209  63.390  1.00 20.61  ? 269 VAL C CA   1 
ATOM   7591  C C    . VAL C 2 251 ? 23.274  86.604  64.278  1.00 23.42  ? 269 VAL C C    1 
ATOM   7592  O O    . VAL C 2 251 ? 23.463  85.399  64.272  1.00 23.71  ? 269 VAL C O    1 
ATOM   7593  C CB   . VAL C 2 251 ? 22.830  87.649  62.064  1.00 22.50  ? 269 VAL C CB   1 
ATOM   7594  C CG1  . VAL C 2 251 ? 23.598  86.526  61.406  1.00 31.23  ? 269 VAL C CG1  1 
ATOM   7595  C CG2  . VAL C 2 251 ? 21.758  88.131  61.115  1.00 28.46  ? 269 VAL C CG2  1 
ATOM   7596  N N    . VAL C 2 252 ? 24.011  87.430  65.024  1.00 24.03  ? 270 VAL C N    1 
ATOM   7597  C CA   . VAL C 2 252 ? 25.114  86.961  65.902  1.00 23.08  ? 270 VAL C CA   1 
ATOM   7598  C C    . VAL C 2 252 ? 24.571  86.527  67.224  1.00 20.65  ? 270 VAL C C    1 
ATOM   7599  O O    . VAL C 2 252 ? 25.127  85.661  67.868  1.00 24.10  ? 270 VAL C O    1 
ATOM   7600  C CB   . VAL C 2 252 ? 26.162  88.055  66.134  1.00 15.45  ? 270 VAL C CB   1 
ATOM   7601  C CG1  . VAL C 2 252 ? 27.420  87.505  66.761  1.00 18.26  ? 270 VAL C CG1  1 
ATOM   7602  C CG2  . VAL C 2 252 ? 26.517  88.714  64.822  1.00 23.60  ? 270 VAL C CG2  1 
ATOM   7603  N N    . LEU C 2 253 ? 23.462  87.106  67.621  1.00 16.46  ? 271 LEU C N    1 
ATOM   7604  C CA   . LEU C 2 253 ? 22.817  86.723  68.852  1.00 19.16  ? 271 LEU C CA   1 
ATOM   7605  C C    . LEU C 2 253 ? 22.109  85.427  68.808  1.00 19.56  ? 271 LEU C C    1 
ATOM   7606  O O    . LEU C 2 253 ? 22.031  84.763  69.813  1.00 19.96  ? 271 LEU C O    1 
ATOM   7607  C CB   . LEU C 2 253 ? 21.886  87.799  69.359  1.00 22.00  ? 271 LEU C CB   1 
ATOM   7608  C CG   . LEU C 2 253 ? 22.448  89.077  69.974  1.00 17.55  ? 271 LEU C CG   1 
ATOM   7609  C CD1  . LEU C 2 253 ? 21.292  89.970  70.370  1.00 12.49  ? 271 LEU C CD1  1 
ATOM   7610  C CD2  . LEU C 2 253 ? 23.312  88.772  71.180  1.00 16.62  ? 271 LEU C CD2  1 
ATOM   7611  N N    . THR C 2 254 ? 21.594  85.028  67.668  1.00 15.92  ? 272 THR C N    1 
ATOM   7612  C CA   . THR C 2 254 ? 21.003  83.728  67.592  1.00 15.76  ? 272 THR C CA   1 
ATOM   7613  C C    . THR C 2 254 ? 22.004  82.658  67.848  1.00 19.91  ? 272 THR C C    1 
ATOM   7614  O O    . THR C 2 254 ? 21.715  81.766  68.602  1.00 32.07  ? 272 THR C O    1 
ATOM   7615  C CB   . THR C 2 254 ? 20.449  83.453  66.231  1.00 19.33  ? 272 THR C CB   1 
ATOM   7616  O OG1  . THR C 2 254 ? 21.450  83.714  65.243  1.00 24.24  ? 272 THR C OG1  1 
ATOM   7617  C CG2  . THR C 2 254 ? 19.257  84.307  65.963  1.00 22.27  ? 272 THR C CG2  1 
ATOM   7618  N N    . ASP C 2 255 ? 23.196  82.742  67.284  1.00 16.74  ? 273 ASP C N    1 
ATOM   7619  C CA   . ASP C 2 255 ? 24.256  81.772  67.546  1.00 23.94  ? 273 ASP C CA   1 
ATOM   7620  C C    . ASP C 2 255 ? 24.686  81.776  69.000  1.00 27.50  ? 273 ASP C C    1 
ATOM   7621  O O    . ASP C 2 255 ? 25.081  80.759  69.530  1.00 30.72  ? 273 ASP C O    1 
ATOM   7622  C CB   . ASP C 2 255 ? 25.433  82.006  66.632  1.00 25.38  ? 273 ASP C CB   1 
ATOM   7623  C CG   . ASP C 2 255 ? 26.316  80.799  66.480  1.00 29.56  ? 273 ASP C CG   1 
ATOM   7624  O OD1  . ASP C 2 255 ? 25.840  79.761  65.992  1.00 35.21  ? 273 ASP C OD1  1 
ATOM   7625  O OD2  . ASP C 2 255 ? 27.507  80.899  66.808  1.00 27.12  ? 273 ASP C OD2  1 
ATOM   7626  N N    . TYR C 2 256 ? 24.701  82.924  69.637  1.00 22.56  ? 274 TYR C N    1 
ATOM   7627  C CA   . TYR C 2 256 ? 25.000  82.981  71.042  1.00 25.88  ? 274 TYR C CA   1 
ATOM   7628  C C    . TYR C 2 256 ? 23.952  82.313  71.848  1.00 25.28  ? 274 TYR C C    1 
ATOM   7629  O O    . TYR C 2 256 ? 24.251  81.586  72.752  1.00 30.81  ? 274 TYR C O    1 
ATOM   7630  C CB   . TYR C 2 256 ? 25.098  84.435  71.487  1.00 27.26  ? 274 TYR C CB   1 
ATOM   7631  C CG   . TYR C 2 256 ? 25.729  84.669  72.833  1.00 20.38  ? 274 TYR C CG   1 
ATOM   7632  C CD1  . TYR C 2 256 ? 27.069  84.424  73.038  1.00 22.58  ? 274 TYR C CD1  1 
ATOM   7633  C CD2  . TYR C 2 256 ? 24.992  85.162  73.880  1.00 13.87  ? 274 TYR C CD2  1 
ATOM   7634  C CE1  . TYR C 2 256 ? 27.650  84.638  74.262  1.00 20.93  ? 274 TYR C CE1  1 
ATOM   7635  C CE2  . TYR C 2 256 ? 25.567  85.378  75.105  1.00 18.74  ? 274 TYR C CE2  1 
ATOM   7636  C CZ   . TYR C 2 256 ? 26.894  85.114  75.286  1.00 21.10  ? 274 TYR C CZ   1 
ATOM   7637  O OH   . TYR C 2 256 ? 27.465  85.334  76.506  1.00 24.51  ? 274 TYR C OH   1 
ATOM   7638  N N    . ILE C 2 257 ? 22.709  82.549  71.517  1.00 17.81  ? 275 ILE C N    1 
ATOM   7639  C CA   . ILE C 2 257 ? 21.649  81.953  72.269  1.00 24.25  ? 275 ILE C CA   1 
ATOM   7640  C C    . ILE C 2 257 ? 21.755  80.482  72.123  1.00 26.79  ? 275 ILE C C    1 
ATOM   7641  O O    . ILE C 2 257 ? 21.642  79.755  73.074  1.00 32.76  ? 275 ILE C O    1 
ATOM   7642  C CB   . ILE C 2 257 ? 20.286  82.411  71.800  1.00 24.70  ? 275 ILE C CB   1 
ATOM   7643  C CG1  . ILE C 2 257 ? 20.032  83.842  72.269  1.00 22.73  ? 275 ILE C CG1  1 
ATOM   7644  C CG2  . ILE C 2 257 ? 19.197  81.498  72.324  1.00 26.25  ? 275 ILE C CG2  1 
ATOM   7645  C CD1  . ILE C 2 257 ? 18.637  84.337  71.988  1.00 17.36  ? 275 ILE C CD1  1 
ATOM   7646  N N    . GLU C 2 258 ? 22.051  80.033  70.937  1.00 20.46  ? 276 GLU C N    1 
ATOM   7647  C CA   . GLU C 2 258 ? 22.171  78.629  70.693  1.00 25.01  ? 276 GLU C CA   1 
ATOM   7648  C C    . GLU C 2 258 ? 23.263  77.965  71.471  1.00 26.36  ? 276 GLU C C    1 
ATOM   7649  O O    . GLU C 2 258 ? 23.075  76.921  72.063  1.00 28.26  ? 276 GLU C O    1 
ATOM   7650  C CB   . GLU C 2 258 ? 22.479  78.454  69.219  1.00 24.58  ? 276 GLU C CB   1 
ATOM   7651  C CG   . GLU C 2 258 ? 21.288  78.692  68.301  1.00 29.69  ? 276 GLU C CG   1 
ATOM   7652  C CD   . GLU C 2 258 ? 21.689  78.931  66.858  1.00 27.27  ? 276 GLU C CD   1 
ATOM   7653  O OE1  . GLU C 2 258 ? 22.887  78.821  66.557  1.00 29.55  ? 276 GLU C OE1  1 
ATOM   7654  O OE2  . GLU C 2 258 ? 20.808  79.230  66.026  1.00 20.17  ? 276 GLU C OE2  1 
ATOM   7655  N N    . LYS C 2 259 ? 24.415  78.569  71.494  1.00 25.38  ? 277 LYS C N    1 
ATOM   7656  C CA   . LYS C 2 259 ? 25.537  77.970  72.167  1.00 29.59  ? 277 LYS C CA   1 
ATOM   7657  C C    . LYS C 2 259 ? 25.644  78.328  73.626  1.00 33.89  ? 277 LYS C C    1 
ATOM   7658  O O    . LYS C 2 259 ? 26.518  77.814  74.304  1.00 40.05  ? 277 LYS C O    1 
ATOM   7659  C CB   . LYS C 2 259 ? 26.833  78.414  71.501  1.00 31.94  ? 277 LYS C CB   1 
ATOM   7660  C CG   . LYS C 2 259 ? 27.031  78.107  70.034  1.00 25.51  ? 277 LYS C CG   1 
ATOM   7661  C CD   . LYS C 2 259 ? 28.227  78.918  69.552  1.00 27.74  ? 277 LYS C CD   1 
ATOM   7662  C CE   . LYS C 2 259 ? 28.858  78.363  68.290  1.00 33.71  ? 277 LYS C CE   1 
ATOM   7663  N NZ   . LYS C 2 259 ? 29.901  79.279  67.758  1.00 18.50  ? 277 LYS C NZ   1 
ATOM   7664  N N    . HIS C 2 260 ? 24.825  79.260  74.093  1.00 33.43  ? 278 HIS C N    1 
ATOM   7665  C CA   . HIS C 2 260 ? 24.885  79.699  75.477  1.00 33.37  ? 278 HIS C CA   1 
ATOM   7666  C C    . HIS C 2 260 ? 23.567  79.836  76.256  1.00 28.07  ? 278 HIS C C    1 
ATOM   7667  O O    . HIS C 2 260 ? 23.476  80.612  77.166  1.00 30.47  ? 278 HIS C O    1 
ATOM   7668  C CB   . HIS C 2 260 ? 25.681  80.990  75.578  1.00 34.26  ? 278 HIS C CB   1 
ATOM   7669  C CG   . HIS C 2 260 ? 27.018  80.956  74.913  1.00 33.11  ? 278 HIS C CG   1 
ATOM   7670  N ND1  . HIS C 2 260 ? 28.178  80.685  75.598  1.00 38.08  ? 278 HIS C ND1  1 
ATOM   7671  C CD2  . HIS C 2 260 ? 27.387  81.203  73.635  1.00 29.67  ? 278 HIS C CD2  1 
ATOM   7672  C CE1  . HIS C 2 260 ? 29.201  80.745  74.766  1.00 44.28  ? 278 HIS C CE1  1 
ATOM   7673  N NE2  . HIS C 2 260 ? 28.748  81.059  73.569  1.00 36.07  ? 278 HIS C NE2  1 
ATOM   7674  N N    . LYS C 2 261 ? 22.549  79.103  75.899  1.00 28.10  ? 279 LYS C N    1 
ATOM   7675  C CA   . LYS C 2 261 ? 21.283  79.189  76.599  1.00 35.11  ? 279 LYS C CA   1 
ATOM   7676  C C    . LYS C 2 261 ? 21.188  78.251  77.770  1.00 36.55  ? 279 LYS C C    1 
ATOM   7677  O O    . LYS C 2 261 ? 20.205  78.285  78.489  1.00 36.53  ? 279 LYS C O    1 
ATOM   7678  C CB   . LYS C 2 261 ? 20.149  78.854  75.647  1.00 36.24  ? 279 LYS C CB   1 
ATOM   7679  C CG   . LYS C 2 261 ? 20.206  77.458  75.056  1.00 29.59  ? 279 LYS C CG   1 
ATOM   7680  C CD   . LYS C 2 261 ? 19.066  77.244  74.083  1.00 29.15  ? 279 LYS C CD   1 
ATOM   7681  C CE   . LYS C 2 261 ? 19.157  75.874  73.454  1.00 31.35  ? 279 LYS C CE   1 
ATOM   7682  N NZ   . LYS C 2 261 ? 20.524  75.631  72.929  1.00 29.94  ? 279 LYS C NZ   1 
ATOM   7683  N N    . THR C 2 262 ? 22.187  77.396  77.952  1.00 36.54  ? 280 THR C N    1 
ATOM   7684  C CA   . THR C 2 262 ? 22.227  76.446  79.039  1.00 26.50  ? 280 THR C CA   1 
ATOM   7685  C C    . THR C 2 262 ? 23.014  77.129  80.086  1.00 25.81  ? 280 THR C C    1 
ATOM   7686  O O    . THR C 2 262 ? 23.318  76.547  81.110  1.00 22.66  ? 280 THR C O    1 
ATOM   7687  C CB   . THR C 2 262 ? 22.984  75.239  78.569  1.00 26.84  ? 280 THR C CB   1 
ATOM   7688  O OG1  . THR C 2 262 ? 23.961  75.654  77.609  1.00 29.96  ? 280 THR C OG1  1 
ATOM   7689  C CG2  . THR C 2 262 ? 22.047  74.284  77.879  1.00 28.70  ? 280 THR C CG2  1 
ATOM   7690  N N    . ASP C 2 263 ? 23.337  78.391  79.834  1.00 27.31  ? 281 ASP C N    1 
ATOM   7691  C CA   . ASP C 2 263 ? 24.145  79.162  80.736  1.00 27.41  ? 281 ASP C CA   1 
ATOM   7692  C C    . ASP C 2 263 ? 23.281  79.969  81.612  1.00 24.20  ? 281 ASP C C    1 
ATOM   7693  O O    . ASP C 2 263 ? 22.436  80.699  81.154  1.00 22.61  ? 281 ASP C O    1 
ATOM   7694  C CB   . ASP C 2 263 ? 25.088  80.049  79.958  1.00 34.61  ? 281 ASP C CB   1 
ATOM   7695  C CG   . ASP C 2 263 ? 26.181  79.274  79.228  1.00 33.55  ? 281 ASP C CG   1 
ATOM   7696  O OD1  . ASP C 2 263 ? 26.199  78.034  79.290  1.00 38.91  ? 281 ASP C OD1  1 
ATOM   7697  O OD2  . ASP C 2 263 ? 27.035  79.915  78.584  1.00 27.24  ? 281 ASP C OD2  1 
ATOM   7698  N N    . LYS C 2 264 ? 23.538  79.894  82.889  1.00 23.11  ? 282 LYS C N    1 
ATOM   7699  C CA   . LYS C 2 264 ? 22.663  80.498  83.847  1.00 28.23  ? 282 LYS C CA   1 
ATOM   7700  C C    . LYS C 2 264 ? 22.284  81.920  83.799  1.00 30.54  ? 282 LYS C C    1 
ATOM   7701  O O    . LYS C 2 264 ? 21.163  82.252  84.139  1.00 37.33  ? 282 LYS C O    1 
ATOM   7702  C CB   . LYS C 2 264 ? 23.195  80.206  85.256  1.00 32.58  ? 282 LYS C CB   1 
ATOM   7703  C CG   . LYS C 2 264 ? 24.667  80.480  85.473  1.00 36.82  ? 282 LYS C CG   1 
ATOM   7704  C CD   . LYS C 2 264 ? 24.880  80.925  86.904  1.00 30.91  ? 282 LYS C CD   1 
ATOM   7705  C CE   . LYS C 2 264 ? 23.888  80.237  87.821  1.00 35.73  ? 282 LYS C CE   1 
ATOM   7706  N NZ   . LYS C 2 264 ? 23.984  80.756  89.211  1.00 52.89  ? 282 LYS C NZ   1 
ATOM   7707  N N    . ASP C 2 265 ? 23.189  82.774  83.394  1.00 31.68  ? 283 ASP C N    1 
ATOM   7708  C CA   . ASP C 2 265 ? 22.908  84.172  83.489  1.00 30.82  ? 283 ASP C CA   1 
ATOM   7709  C C    . ASP C 2 265 ? 23.042  84.844  82.180  1.00 35.11  ? 283 ASP C C    1 
ATOM   7710  O O    . ASP C 2 265 ? 23.250  86.007  82.132  1.00 38.74  ? 283 ASP C O    1 
ATOM   7711  C CB   . ASP C 2 265 ? 23.892  84.761  84.464  1.00 31.96  ? 283 ASP C CB   1 
ATOM   7712  C CG   . ASP C 2 265 ? 23.356  84.808  85.867  1.00 43.17  ? 283 ASP C CG   1 
ATOM   7713  O OD1  . ASP C 2 265 ? 22.197  85.222  86.040  1.00 57.48  ? 283 ASP C OD1  1 
ATOM   7714  O OD2  . ASP C 2 265 ? 24.087  84.437  86.801  1.00 41.86  ? 283 ASP C OD2  1 
ATOM   7715  N N    . ILE C 2 266 ? 22.927  84.097  81.100  1.00 30.67  ? 284 ILE C N    1 
ATOM   7716  C CA   . ILE C 2 266 ? 23.023  84.637  79.767  1.00 25.32  ? 284 ILE C CA   1 
ATOM   7717  C C    . ILE C 2 266 ? 21.886  85.570  79.589  1.00 22.77  ? 284 ILE C C    1 
ATOM   7718  O O    . ILE C 2 266 ? 21.908  86.384  78.726  1.00 25.86  ? 284 ILE C O    1 
ATOM   7719  C CB   . ILE C 2 266 ? 22.974  83.523  78.710  1.00 27.96  ? 284 ILE C CB   1 
ATOM   7720  C CG1  . ILE C 2 266 ? 23.214  84.058  77.301  1.00 25.31  ? 284 ILE C CG1  1 
ATOM   7721  C CG2  . ILE C 2 266 ? 21.667  82.749  78.769  1.00 32.87  ? 284 ILE C CG2  1 
ATOM   7722  C CD1  . ILE C 2 266 ? 23.486  82.975  76.282  1.00 32.98  ? 284 ILE C CD1  1 
ATOM   7723  N N    . GLU C 2 267 ? 20.893  85.498  80.445  1.00 24.65  ? 285 GLU C N    1 
ATOM   7724  C CA   . GLU C 2 267 ? 19.733  86.338  80.354  1.00 22.74  ? 285 GLU C CA   1 
ATOM   7725  C C    . GLU C 2 267 ? 20.122  87.684  80.843  1.00 29.07  ? 285 GLU C C    1 
ATOM   7726  O O    . GLU C 2 267 ? 19.511  88.675  80.497  1.00 24.99  ? 285 GLU C O    1 
ATOM   7727  C CB   . GLU C 2 267 ? 18.628  85.749  81.186  1.00 28.86  ? 285 GLU C CB   1 
ATOM   7728  C CG   . GLU C 2 267 ? 18.843  85.655  82.687  1.00 36.92  ? 285 GLU C CG   1 
ATOM   7729  C CD   . GLU C 2 267 ? 17.718  84.939  83.399  1.00 56.21  ? 285 GLU C CD   1 
ATOM   7730  O OE1  . GLU C 2 267 ? 16.629  84.816  82.811  1.00 72.51  ? 285 GLU C OE1  1 
ATOM   7731  O OE2  . GLU C 2 267 ? 17.923  84.503  84.546  1.00 58.74  ? 285 GLU C OE2  1 
ATOM   7732  N N    . LYS C 2 268 ? 21.185  87.729  81.638  1.00 37.08  ? 286 LYS C N    1 
ATOM   7733  C CA   . LYS C 2 268 ? 21.705  88.975  82.159  1.00 29.77  ? 286 LYS C CA   1 
ATOM   7734  C C    . LYS C 2 268 ? 22.682  89.450  81.166  1.00 29.99  ? 286 LYS C C    1 
ATOM   7735  O O    . LYS C 2 268 ? 22.693  90.605  80.810  1.00 29.72  ? 286 LYS C O    1 
ATOM   7736  C CB   . LYS C 2 268 ? 22.407  88.666  83.462  1.00 24.62  ? 286 LYS C CB   1 
ATOM   7737  C CG   . LYS C 2 268 ? 22.528  89.839  84.412  1.00 32.44  ? 286 LYS C CG   1 
ATOM   7738  C CD   . LYS C 2 268 ? 23.750  89.698  85.300  1.00 32.62  ? 286 LYS C CD   1 
ATOM   7739  C CE   . LYS C 2 268 ? 24.173  91.041  85.870  1.00 40.47  ? 286 LYS C CE   1 
ATOM   7740  N NZ   . LYS C 2 268 ? 25.648  91.153  86.040  1.00 38.45  ? 286 LYS C NZ   1 
ATOM   7741  N N    . LYS C 2 269 ? 23.499  88.538  80.691  1.00 28.47  ? 287 LYS C N    1 
ATOM   7742  C CA   . LYS C 2 269 ? 24.476  88.859  79.688  1.00 27.68  ? 287 LYS C CA   1 
ATOM   7743  C C    . LYS C 2 269 ? 23.862  89.493  78.485  1.00 23.00  ? 287 LYS C C    1 
ATOM   7744  O O    . LYS C 2 269 ? 24.301  90.543  78.086  1.00 22.74  ? 287 LYS C O    1 
ATOM   7745  C CB   . LYS C 2 269 ? 25.224  87.592  79.268  1.00 23.25  ? 287 LYS C CB   1 
ATOM   7746  C CG   . LYS C 2 269 ? 25.978  86.881  80.366  1.00 17.14  ? 287 LYS C CG   1 
ATOM   7747  C CD   . LYS C 2 269 ? 26.653  85.653  79.794  1.00 20.41  ? 287 LYS C CD   1 
ATOM   7748  C CE   . LYS C 2 269 ? 26.927  84.614  80.860  1.00 30.55  ? 287 LYS C CE   1 
ATOM   7749  N NZ   . LYS C 2 269 ? 27.090  83.261  80.272  1.00 30.22  ? 287 LYS C NZ   1 
ATOM   7750  N N    . VAL C 2 270 ? 22.852  88.883  77.900  1.00 18.77  ? 288 VAL C N    1 
ATOM   7751  C CA   . VAL C 2 270 ? 22.274  89.364  76.658  1.00 15.69  ? 288 VAL C CA   1 
ATOM   7752  C C    . VAL C 2 270 ? 21.622  90.686  76.807  1.00 14.25  ? 288 VAL C C    1 
ATOM   7753  O O    . VAL C 2 270 ? 21.475  91.441  75.874  1.00 10.81  ? 288 VAL C O    1 
ATOM   7754  C CB   . VAL C 2 270 ? 21.367  88.287  76.043  1.00 15.04  ? 288 VAL C CB   1 
ATOM   7755  C CG1  . VAL C 2 270 ? 20.376  88.803  75.018  1.00 17.52  ? 288 VAL C CG1  1 
ATOM   7756  C CG2  . VAL C 2 270 ? 22.208  87.207  75.409  1.00 14.17  ? 288 VAL C CG2  1 
ATOM   7757  N N    . ASN C 2 271 ? 21.312  91.041  78.015  1.00 14.90  ? 289 ASN C N    1 
ATOM   7758  C CA   . ASN C 2 271 ? 20.591  92.266  78.159  1.00 18.61  ? 289 ASN C CA   1 
ATOM   7759  C C    . ASN C 2 271 ? 21.591  93.346  77.997  1.00 19.33  ? 289 ASN C C    1 
ATOM   7760  O O    . ASN C 2 271 ? 21.394  94.204  77.187  1.00 18.23  ? 289 ASN C O    1 
ATOM   7761  C CB   . ASN C 2 271 ? 19.849  92.325  79.474  1.00 20.10  ? 289 ASN C CB   1 
ATOM   7762  C CG   . ASN C 2 271 ? 18.352  92.202  79.300  1.00 21.19  ? 289 ASN C CG   1 
ATOM   7763  O OD1  . ASN C 2 271 ? 17.740  92.994  78.604  1.00 21.25  ? 289 ASN C OD1  1 
ATOM   7764  N ND2  . ASN C 2 271 ? 17.760  91.202  79.929  1.00 21.91  ? 289 ASN C ND2  1 
ATOM   7765  N N    . GLN C 2 272 ? 22.694  93.298  78.729  1.00 20.18  ? 290 GLN C N    1 
ATOM   7766  C CA   . GLN C 2 272 ? 23.781  94.253  78.577  1.00 16.53  ? 290 GLN C CA   1 
ATOM   7767  C C    . GLN C 2 272 ? 24.328  94.304  77.188  1.00 13.51  ? 290 GLN C C    1 
ATOM   7768  O O    . GLN C 2 272 ? 24.743  95.313  76.763  1.00 13.20  ? 290 GLN C O    1 
ATOM   7769  C CB   . GLN C 2 272 ? 24.890  93.896  79.523  1.00 18.51  ? 290 GLN C CB   1 
ATOM   7770  C CG   . GLN C 2 272 ? 24.473  93.422  80.894  1.00 27.02  ? 290 GLN C CG   1 
ATOM   7771  C CD   . GLN C 2 272 ? 25.517  92.517  81.509  1.00 32.61  ? 290 GLN C CD   1 
ATOM   7772  O OE1  . GLN C 2 272 ? 26.269  91.852  80.806  1.00 17.92  ? 290 GLN C OE1  1 
ATOM   7773  N NE2  . GLN C 2 272 ? 25.570  92.491  82.827  1.00 38.01  ? 290 GLN C NE2  1 
ATOM   7774  N N    . ILE C 2 273 ? 24.354  93.212  76.472  1.00 13.25  ? 291 ILE C N    1 
ATOM   7775  C CA   . ILE C 2 273 ? 24.760  93.216  75.084  1.00 12.50  ? 291 ILE C CA   1 
ATOM   7776  C C    . ILE C 2 273 ? 23.932  94.165  74.284  1.00 12.02  ? 291 ILE C C    1 
ATOM   7777  O O    . ILE C 2 273 ? 24.468  94.931  73.532  1.00 12.40  ? 291 ILE C O    1 
ATOM   7778  C CB   . ILE C 2 273 ? 24.667  91.799  74.475  1.00 11.91  ? 291 ILE C CB   1 
ATOM   7779  C CG1  . ILE C 2 273 ? 25.677  90.851  75.108  1.00 16.84  ? 291 ILE C CG1  1 
ATOM   7780  C CG2  . ILE C 2 273 ? 24.835  91.803  72.973  1.00 10.94  ? 291 ILE C CG2  1 
ATOM   7781  C CD1  . ILE C 2 273 ? 25.592  89.437  74.598  1.00 16.36  ? 291 ILE C CD1  1 
ATOM   7782  N N    . ILE C 2 274 ? 22.617  94.132  74.435  1.00 10.31  ? 292 ILE C N    1 
ATOM   7783  C CA   . ILE C 2 274 ? 21.736  94.937  73.620  1.00 11.06  ? 292 ILE C CA   1 
ATOM   7784  C C    . ILE C 2 274 ? 21.519  96.251  74.283  1.00 13.32  ? 292 ILE C C    1 
ATOM   7785  O O    . ILE C 2 274 ? 21.200  97.217  73.643  1.00 10.30  ? 292 ILE C O    1 
ATOM   7786  C CB   . ILE C 2 274 ? 20.424  94.223  73.488  1.00 10.25  ? 292 ILE C CB   1 
ATOM   7787  C CG1  . ILE C 2 274 ? 20.622  92.948  72.691  1.00 18.81  ? 292 ILE C CG1  1 
ATOM   7788  C CG2  . ILE C 2 274 ? 19.358  95.058  72.803  1.00 10.63  ? 292 ILE C CG2  1 
ATOM   7789  C CD1  . ILE C 2 274 ? 19.417  92.047  72.739  1.00 25.66  ? 292 ILE C CD1  1 
ATOM   7790  N N    . ASN C 2 275 ? 21.770  96.302  75.580  1.00 15.72  ? 293 ASN C N    1 
ATOM   7791  C CA   . ASN C 2 275 ? 21.693  97.540  76.343  1.00 13.28  ? 293 ASN C CA   1 
ATOM   7792  C C    . ASN C 2 275 ? 22.968  98.366  76.101  1.00 13.96  ? 293 ASN C C    1 
ATOM   7793  O O    . ASN C 2 275 ? 22.892  99.540  76.114  1.00 13.79  ? 293 ASN C O    1 
ATOM   7794  C CB   . ASN C 2 275 ? 21.408  97.338  77.834  1.00 9.80   ? 293 ASN C CB   1 
ATOM   7795  C CG   . ASN C 2 275 ? 20.027  96.848  78.122  1.00 12.55  ? 293 ASN C CG   1 
ATOM   7796  O OD1  . ASN C 2 275 ? 19.803  96.264  79.162  1.00 16.24  ? 293 ASN C OD1  1 
ATOM   7797  N ND2  . ASN C 2 275 ? 19.098  97.087  77.225  1.00 20.78  ? 293 ASN C ND2  1 
ATOM   7798  N N    . LEU C 2 276 ? 24.135  97.785  75.851  1.00 13.13  ? 294 LEU C N    1 
ATOM   7799  C CA   . LEU C 2 276 ? 25.338  98.533  75.489  1.00 11.87  ? 294 LEU C CA   1 
ATOM   7800  C C    . LEU C 2 276 ? 25.220  98.944  74.081  1.00 11.99  ? 294 LEU C C    1 
ATOM   7801  O O    . LEU C 2 276 ? 25.629  99.989  73.715  1.00 12.67  ? 294 LEU C O    1 
ATOM   7802  C CB   . LEU C 2 276 ? 26.613  97.720  75.640  1.00 13.16  ? 294 LEU C CB   1 
ATOM   7803  C CG   . LEU C 2 276 ? 27.961  98.094  75.040  1.00 13.74  ? 294 LEU C CG   1 
ATOM   7804  C CD1  . LEU C 2 276 ? 28.726  99.014  75.961  1.00 8.59   ? 294 LEU C CD1  1 
ATOM   7805  C CD2  . LEU C 2 276 ? 28.750  96.831  74.785  1.00 16.54  ? 294 LEU C CD2  1 
ATOM   7806  N N    . TRP C 2 277 ? 24.663  98.119  73.251  1.00 12.31  ? 295 TRP C N    1 
ATOM   7807  C CA   . TRP C 2 277 ? 24.408  98.510  71.873  1.00 16.18  ? 295 TRP C CA   1 
ATOM   7808  C C    . TRP C 2 277 ? 23.516  99.749  71.769  1.00 16.37  ? 295 TRP C C    1 
ATOM   7809  O O    . TRP C 2 277 ? 23.829  100.643 71.018  1.00 17.61  ? 295 TRP C O    1 
ATOM   7810  C CB   . TRP C 2 277 ? 23.829  97.302  71.119  1.00 13.04  ? 295 TRP C CB   1 
ATOM   7811  C CG   . TRP C 2 277 ? 23.277  97.491  69.783  1.00 11.92  ? 295 TRP C CG   1 
ATOM   7812  C CD1  . TRP C 2 277 ? 22.051  97.973  69.461  1.00 13.99  ? 295 TRP C CD1  1 
ATOM   7813  C CD2  . TRP C 2 277 ? 23.893  97.115  68.565  1.00 12.93  ? 295 TRP C CD2  1 
ATOM   7814  N NE1  . TRP C 2 277 ? 21.884  97.963  68.105  1.00 15.50  ? 295 TRP C NE1  1 
ATOM   7815  C CE2  . TRP C 2 277 ? 23.007  97.435  67.534  1.00 13.12  ? 295 TRP C CE2  1 
ATOM   7816  C CE3  . TRP C 2 277 ? 25.125  96.554  68.245  1.00 15.05  ? 295 TRP C CE3  1 
ATOM   7817  C CZ2  . TRP C 2 277 ? 23.312  97.218  66.216  1.00 10.93  ? 295 TRP C CZ2  1 
ATOM   7818  C CZ3  . TRP C 2 277 ? 25.418  96.340  66.941  1.00 15.20  ? 295 TRP C CZ3  1 
ATOM   7819  C CH2  . TRP C 2 277 ? 24.519  96.664  65.942  1.00 15.20  ? 295 TRP C CH2  1 
ATOM   7820  N N    . ILE C 2 278 ? 22.414  99.810  72.503  1.00 11.70  ? 296 ILE C N    1 
ATOM   7821  C CA   . ILE C 2 278 ? 21.551  100.970 72.462  1.00 10.80  ? 296 ILE C CA   1 
ATOM   7822  C C    . ILE C 2 278 ? 22.289  102.081 73.169  1.00 10.94  ? 296 ILE C C    1 
ATOM   7823  O O    . ILE C 2 278 ? 22.137  103.216 72.856  1.00 9.05   ? 296 ILE C O    1 
ATOM   7824  C CB   . ILE C 2 278 ? 20.146  100.639 72.991  1.00 10.25  ? 296 ILE C CB   1 
ATOM   7825  C CG1  . ILE C 2 278 ? 19.229  101.842 72.978  1.00 12.73  ? 296 ILE C CG1  1 
ATOM   7826  C CG2  . ILE C 2 278 ? 20.164  100.138 74.402  1.00 14.99  ? 296 ILE C CG2  1 
ATOM   7827  C CD1  . ILE C 2 278 ? 18.858  102.303 71.601  1.00 19.74  ? 296 ILE C CD1  1 
ATOM   7828  N N    . SER C 2 279 ? 23.165  101.759 74.091  1.00 13.31  ? 297 SER C N    1 
ATOM   7829  C CA   . SER C 2 279 ? 23.969  102.750 74.768  1.00 14.19  ? 297 SER C CA   1 
ATOM   7830  C C    . SER C 2 279 ? 24.822  103.381 73.759  1.00 14.08  ? 297 SER C C    1 
ATOM   7831  O O    . SER C 2 279 ? 24.750  104.555 73.546  1.00 16.52  ? 297 SER C O    1 
ATOM   7832  C CB   . SER C 2 279 ? 24.830  102.086 75.817  1.00 13.93  ? 297 SER C CB   1 
ATOM   7833  O OG   . SER C 2 279 ? 25.643  103.006 76.494  1.00 26.37  ? 297 SER C OG   1 
ATOM   7834  N N    . SER C 2 280 ? 25.582  102.589 73.042  1.00 11.33  ? 298 SER C N    1 
ATOM   7835  C CA   . SER C 2 280 ? 26.490  103.095 72.048  1.00 12.99  ? 298 SER C CA   1 
ATOM   7836  C C    . SER C 2 280 ? 26.004  103.575 70.703  1.00 11.07  ? 298 SER C C    1 
ATOM   7837  O O    . SER C 2 280 ? 26.779  104.030 69.917  1.00 12.05  ? 298 SER C O    1 
ATOM   7838  C CB   . SER C 2 280 ? 27.439  101.957 71.881  1.00 15.08  ? 298 SER C CB   1 
ATOM   7839  O OG   . SER C 2 280 ? 27.832  101.462 73.135  1.00 17.18  ? 298 SER C OG   1 
ATOM   7840  N N    . TYR C 2 281 ? 24.716  103.495 70.433  1.00 11.57  ? 299 TYR C N    1 
ATOM   7841  C CA   . TYR C 2 281 ? 24.154  103.887 69.157  1.00 9.62   ? 299 TYR C CA   1 
ATOM   7842  C C    . TYR C 2 281 ? 23.434  105.160 69.324  1.00 8.06   ? 299 TYR C C    1 
ATOM   7843  O O    . TYR C 2 281 ? 22.953  105.719 68.391  1.00 10.93  ? 299 TYR C O    1 
ATOM   7844  C CB   . TYR C 2 281 ? 23.266  102.773 68.609  1.00 8.29   ? 299 TYR C CB   1 
ATOM   7845  C CG   . TYR C 2 281 ? 23.999  101.868 67.646  1.00 10.43  ? 299 TYR C CG   1 
ATOM   7846  C CD1  . TYR C 2 281 ? 25.180  101.258 68.007  1.00 13.30  ? 299 TYR C CD1  1 
ATOM   7847  C CD2  . TYR C 2 281 ? 23.524  101.651 66.371  1.00 9.74   ? 299 TYR C CD2  1 
ATOM   7848  C CE1  . TYR C 2 281 ? 25.866  100.460 67.131  1.00 11.16  ? 299 TYR C CE1  1 
ATOM   7849  C CE2  . TYR C 2 281 ? 24.203  100.846 65.488  1.00 10.18  ? 299 TYR C CE2  1 
ATOM   7850  C CZ   . TYR C 2 281 ? 25.376  100.257 65.879  1.00 12.09  ? 299 TYR C CZ   1 
ATOM   7851  O OH   . TYR C 2 281 ? 26.075  99.453  65.017  1.00 20.59  ? 299 TYR C OH   1 
ATOM   7852  N N    . ILE C 2 282 ? 23.430  105.671 70.518  1.00 7.67   ? 300 ILE C N    1 
ATOM   7853  C CA   . ILE C 2 282 ? 22.789  106.908 70.799  1.00 8.48   ? 300 ILE C CA   1 
ATOM   7854  C C    . ILE C 2 282 ? 23.784  107.971 71.105  1.00 10.11  ? 300 ILE C C    1 
ATOM   7855  O O    . ILE C 2 282 ? 23.553  109.118 70.881  1.00 13.50  ? 300 ILE C O    1 
ATOM   7856  C CB   . ILE C 2 282 ? 21.845  106.702 71.978  1.00 10.64  ? 300 ILE C CB   1 
ATOM   7857  C CG1  . ILE C 2 282 ? 20.636  105.875 71.592  1.00 13.80  ? 300 ILE C CG1  1 
ATOM   7858  C CG2  . ILE C 2 282 ? 21.217  107.979 72.441  1.00 10.81  ? 300 ILE C CG2  1 
ATOM   7859  C CD1  . ILE C 2 282 ? 19.534  106.003 72.614  1.00 9.67   ? 300 ILE C CD1  1 
ATOM   7860  N N    . LYS C 2 283 ? 24.950  107.588 71.546  1.00 10.26  ? 301 LYS C N    1 
ATOM   7861  C CA   . LYS C 2 283 ? 25.974  108.533 71.913  1.00 11.28  ? 301 LYS C CA   1 
ATOM   7862  C C    . LYS C 2 283 ? 27.062  108.612 70.908  1.00 11.11  ? 301 LYS C C    1 
ATOM   7863  O O    . LYS C 2 283 ? 27.931  109.443 70.998  1.00 14.54  ? 301 LYS C O    1 
ATOM   7864  C CB   . LYS C 2 283 ? 26.619  108.099 73.219  1.00 19.89  ? 301 LYS C CB   1 
ATOM   7865  C CG   . LYS C 2 283 ? 27.351  106.775 73.159  1.00 19.28  ? 301 LYS C CG   1 
ATOM   7866  C CD   . LYS C 2 283 ? 27.988  106.411 74.481  1.00 20.78  ? 301 LYS C CD   1 
ATOM   7867  C CE   . LYS C 2 283 ? 28.702  105.094 74.378  1.00 32.93  ? 301 LYS C CE   1 
ATOM   7868  N NZ   . LYS C 2 283 ? 29.338  104.717 75.670  1.00 37.26  ? 301 LYS C NZ   1 
ATOM   7869  N N    . GLU C 2 284 ? 27.002  107.746 69.915  1.00 13.47  ? 302 GLU C N    1 
ATOM   7870  C CA   . GLU C 2 284 ? 27.998  107.703 68.867  1.00 12.03  ? 302 GLU C CA   1 
ATOM   7871  C C    . GLU C 2 284 ? 27.308  108.197 67.665  1.00 12.43  ? 302 GLU C C    1 
ATOM   7872  O O    . GLU C 2 284 ? 27.756  107.983 66.570  1.00 14.73  ? 302 GLU C O    1 
ATOM   7873  C CB   . GLU C 2 284 ? 28.669  106.376 68.634  1.00 9.34   ? 302 GLU C CB   1 
ATOM   7874  C CG   . GLU C 2 284 ? 29.516  105.857 69.776  1.00 11.69  ? 302 GLU C CG   1 
ATOM   7875  C CD   . GLU C 2 284 ? 30.672  106.765 70.104  1.00 15.03  ? 302 GLU C CD   1 
ATOM   7876  O OE1  . GLU C 2 284 ? 31.562  106.908 69.251  1.00 14.02  ? 302 GLU C OE1  1 
ATOM   7877  O OE2  . GLU C 2 284 ? 30.692  107.333 71.213  1.00 18.31  ? 302 GLU C OE2  1 
ATOM   7878  N N    . GLY C 2 285 ? 26.184  108.841 67.861  1.00 11.77  ? 303 GLY C N    1 
ATOM   7879  C CA   . GLY C 2 285 ? 25.490  109.500 66.784  1.00 12.33  ? 303 GLY C CA   1 
ATOM   7880  C C    . GLY C 2 285 ? 24.823  108.786 65.680  1.00 12.12  ? 303 GLY C C    1 
ATOM   7881  O O    . GLY C 2 285 ? 24.757  109.297 64.572  1.00 16.71  ? 303 GLY C O    1 
ATOM   7882  N N    . TYR C 2 286 ? 24.326  107.606 65.953  1.00 9.00   ? 304 TYR C N    1 
ATOM   7883  C CA   . TYR C 2 286 ? 23.738  106.854 64.914  1.00 7.98   ? 304 TYR C CA   1 
ATOM   7884  C C    . TYR C 2 286 ? 22.255  106.831 65.011  1.00 9.23   ? 304 TYR C C    1 
ATOM   7885  O O    . TYR C 2 286 ? 21.605  107.248 64.076  1.00 13.83  ? 304 TYR C O    1 
ATOM   7886  C CB   . TYR C 2 286 ? 24.230  105.429 64.999  1.00 7.39   ? 304 TYR C CB   1 
ATOM   7887  C CG   . TYR C 2 286 ? 25.706  105.137 64.996  1.00 6.61   ? 304 TYR C CG   1 
ATOM   7888  C CD1  . TYR C 2 286 ? 26.535  105.629 64.017  1.00 6.37   ? 304 TYR C CD1  1 
ATOM   7889  C CD2  . TYR C 2 286 ? 26.245  104.290 65.936  1.00 6.16   ? 304 TYR C CD2  1 
ATOM   7890  C CE1  . TYR C 2 286 ? 27.879  105.326 64.012  1.00 6.95   ? 304 TYR C CE1  1 
ATOM   7891  C CE2  . TYR C 2 286 ? 27.577  103.976 65.936  1.00 6.03   ? 304 TYR C CE2  1 
ATOM   7892  C CZ   . TYR C 2 286 ? 28.393  104.498 64.971  1.00 6.18   ? 304 TYR C CZ   1 
ATOM   7893  O OH   . TYR C 2 286 ? 29.731  104.192 64.971  1.00 4.51   ? 304 TYR C OH   1 
ATOM   7894  N N    . HIS C 2 287 ? 21.699  106.446 66.157  1.00 12.17  ? 305 HIS C N    1 
ATOM   7895  C CA   . HIS C 2 287 ? 20.243  106.247 66.309  1.00 9.02   ? 305 HIS C CA   1 
ATOM   7896  C C    . HIS C 2 287 ? 19.448  106.720 67.519  1.00 9.18   ? 305 HIS C C    1 
ATOM   7897  O O    . HIS C 2 287 ? 20.005  106.945 68.545  1.00 11.33  ? 305 HIS C O    1 
ATOM   7898  C CB   . HIS C 2 287 ? 19.971  104.775 66.120  1.00 6.84   ? 305 HIS C CB   1 
ATOM   7899  C CG   . HIS C 2 287 ? 20.350  104.254 64.774  1.00 9.94   ? 305 HIS C CG   1 
ATOM   7900  N ND1  . HIS C 2 287 ? 21.471  103.488 64.560  1.00 11.08  ? 305 HIS C ND1  1 
ATOM   7901  C CD2  . HIS C 2 287 ? 19.754  104.390 63.570  1.00 10.51  ? 305 HIS C CD2  1 
ATOM   7902  C CE1  . HIS C 2 287 ? 21.553  103.176 63.280  1.00 12.78  ? 305 HIS C CE1  1 
ATOM   7903  N NE2  . HIS C 2 287 ? 20.519  103.708 62.659  1.00 11.65  ? 305 HIS C NE2  1 
ATOM   7904  N N    . SER C 2 288 ? 18.152  106.928 67.362  1.00 11.48  ? 306 SER C N    1 
ATOM   7905  C CA   . SER C 2 288 ? 17.230  107.328 68.422  1.00 13.79  ? 306 SER C CA   1 
ATOM   7906  C C    . SER C 2 288 ? 16.868  106.076 69.144  1.00 17.14  ? 306 SER C C    1 
ATOM   7907  O O    . SER C 2 288 ? 17.140  105.015 68.641  1.00 27.61  ? 306 SER C O    1 
ATOM   7908  C CB   . SER C 2 288 ? 16.025  107.992 67.837  1.00 11.71  ? 306 SER C CB   1 
ATOM   7909  O OG   . SER C 2 288 ? 15.166  108.420 68.858  1.00 18.55  ? 306 SER C OG   1 
ATOM   7910  N N    . TYR C 2 289 ? 16.229  106.135 70.298  1.00 13.59  ? 307 TYR C N    1 
ATOM   7911  C CA   . TYR C 2 289 ? 16.060  104.931 71.087  1.00 13.88  ? 307 TYR C CA   1 
ATOM   7912  C C    . TYR C 2 289 ? 15.341  103.943 70.328  1.00 16.26  ? 307 TYR C C    1 
ATOM   7913  O O    . TYR C 2 289 ? 15.795  102.820 70.182  1.00 13.53  ? 307 TYR C O    1 
ATOM   7914  C CB   . TYR C 2 289 ? 15.247  105.240 72.344  1.00 10.43  ? 307 TYR C CB   1 
ATOM   7915  C CG   . TYR C 2 289 ? 14.954  104.098 73.258  1.00 10.87  ? 307 TYR C CG   1 
ATOM   7916  C CD1  . TYR C 2 289 ? 15.965  103.376 73.845  1.00 13.60  ? 307 TYR C CD1  1 
ATOM   7917  C CD2  . TYR C 2 289 ? 13.654  103.772 73.564  1.00 14.14  ? 307 TYR C CD2  1 
ATOM   7918  C CE1  . TYR C 2 289 ? 15.688  102.333 74.689  1.00 13.52  ? 307 TYR C CE1  1 
ATOM   7919  C CE2  . TYR C 2 289 ? 13.368  102.728 74.405  1.00 21.94  ? 307 TYR C CE2  1 
ATOM   7920  C CZ   . TYR C 2 289 ? 14.392  102.017 74.960  1.00 17.19  ? 307 TYR C CZ   1 
ATOM   7921  O OH   . TYR C 2 289 ? 14.093  100.993 75.799  1.00 13.35  ? 307 TYR C OH   1 
ATOM   7922  N N    . SER C 2 290 ? 14.262  104.368 69.726  1.00 16.36  ? 308 SER C N    1 
ATOM   7923  C CA   . SER C 2 290 ? 13.421  103.437 69.061  1.00 17.23  ? 308 SER C CA   1 
ATOM   7924  C C    . SER C 2 290 ? 13.835  103.208 67.614  1.00 21.00  ? 308 SER C C    1 
ATOM   7925  O O    . SER C 2 290 ? 13.246  102.383 66.939  1.00 19.60  ? 308 SER C O    1 
ATOM   7926  C CB   . SER C 2 290 ? 12.002  103.911 69.226  1.00 13.10  ? 308 SER C CB   1 
ATOM   7927  O OG   . SER C 2 290 ? 11.574  103.701 70.550  1.00 10.11  ? 308 SER C OG   1 
ATOM   7928  N N    . GLU C 2 291 ? 14.852  103.908 67.123  1.00 15.10  ? 309 GLU C N    1 
ATOM   7929  C CA   . GLU C 2 291 ? 15.271  103.663 65.787  1.00 13.35  ? 309 GLU C CA   1 
ATOM   7930  C C    . GLU C 2 291 ? 16.095  102.444 65.841  1.00 13.92  ? 309 GLU C C    1 
ATOM   7931  O O    . GLU C 2 291 ? 16.253  101.782 64.853  1.00 14.58  ? 309 GLU C O    1 
ATOM   7932  C CB   . GLU C 2 291 ? 15.988  104.845 65.201  1.00 16.21  ? 309 GLU C CB   1 
ATOM   7933  C CG   . GLU C 2 291 ? 15.066  105.895 64.612  1.00 18.46  ? 309 GLU C CG   1 
ATOM   7934  C CD   . GLU C 2 291 ? 15.790  106.891 63.744  1.00 11.77  ? 309 GLU C CD   1 
ATOM   7935  O OE1  . GLU C 2 291 ? 17.017  106.803 63.630  1.00 11.99  ? 309 GLU C OE1  1 
ATOM   7936  O OE2  . GLU C 2 291 ? 15.129  107.765 63.170  1.00 9.65   ? 309 GLU C OE2  1 
ATOM   7937  N N    . VAL C 2 292 ? 16.574  102.100 67.022  1.00 15.40  ? 310 VAL C N    1 
ATOM   7938  C CA   . VAL C 2 292 ? 17.326  100.849 67.191  1.00 19.21  ? 310 VAL C CA   1 
ATOM   7939  C C    . VAL C 2 292 ? 16.448  99.782  67.827  1.00 13.75  ? 310 VAL C C    1 
ATOM   7940  O O    . VAL C 2 292 ? 16.489  98.637  67.445  1.00 13.72  ? 310 VAL C O    1 
ATOM   7941  C CB   . VAL C 2 292 ? 18.660  101.071 67.990  1.00 12.98  ? 310 VAL C CB   1 
ATOM   7942  C CG1  . VAL C 2 292 ? 19.000  99.886  68.873  1.00 12.86  ? 310 VAL C CG1  1 
ATOM   7943  C CG2  . VAL C 2 292 ? 19.820  101.287 67.055  1.00 12.04  ? 310 VAL C CG2  1 
ATOM   7944  N N    . VAL C 2 293 ? 15.607  100.177 68.764  1.00 12.14  ? 311 VAL C N    1 
ATOM   7945  C CA   . VAL C 2 293 ? 14.781  99.234  69.510  1.00 15.12  ? 311 VAL C CA   1 
ATOM   7946  C C    . VAL C 2 293 ? 13.455  98.821  68.968  1.00 17.07  ? 311 VAL C C    1 
ATOM   7947  O O    . VAL C 2 293 ? 13.055  97.710  69.229  1.00 19.97  ? 311 VAL C O    1 
ATOM   7948  C CB   . VAL C 2 293 ? 14.628  99.679  70.987  1.00 16.25  ? 311 VAL C CB   1 
ATOM   7949  C CG1  . VAL C 2 293 ? 13.197  99.912  71.434  1.00 16.52  ? 311 VAL C CG1  1 
ATOM   7950  C CG2  . VAL C 2 293 ? 15.375  98.748  71.909  1.00 18.75  ? 311 VAL C CG2  1 
ATOM   7951  N N    . ASP C 2 294 ? 12.767  99.638  68.177  1.00 16.19  ? 312 ASP C N    1 
ATOM   7952  C CA   . ASP C 2 294 ? 11.443  99.230  67.733  1.00 18.67  ? 312 ASP C CA   1 
ATOM   7953  C C    . ASP C 2 294 ? 11.587  98.441  66.460  1.00 19.47  ? 312 ASP C C    1 
ATOM   7954  O O    . ASP C 2 294 ? 10.676  98.308  65.665  1.00 23.42  ? 312 ASP C O    1 
ATOM   7955  C CB   . ASP C 2 294 ? 10.493  100.372 67.478  1.00 11.18  ? 312 ASP C CB   1 
ATOM   7956  C CG   . ASP C 2 294 ? 10.037  101.041 68.725  1.00 24.10  ? 312 ASP C CG   1 
ATOM   7957  O OD1  . ASP C 2 294 ? 10.212  100.481 69.815  1.00 30.41  ? 312 ASP C OD1  1 
ATOM   7958  O OD2  . ASP C 2 294 ? 9.509   102.153 68.605  1.00 25.30  ? 312 ASP C OD2  1 
ATOM   7959  N N    . VAL C 2 295 ? 12.757  97.857  66.296  1.00 12.95  ? 313 VAL C N    1 
ATOM   7960  C CA   . VAL C 2 295 ? 13.029  97.056  65.149  1.00 11.73  ? 313 VAL C CA   1 
ATOM   7961  C C    . VAL C 2 295 ? 13.129  95.753  65.809  1.00 14.38  ? 313 VAL C C    1 
ATOM   7962  O O    . VAL C 2 295 ? 12.807  94.762  65.228  1.00 19.46  ? 313 VAL C O    1 
ATOM   7963  C CB   . VAL C 2 295 ? 14.300  97.351  64.334  1.00 22.16  ? 313 VAL C CB   1 
ATOM   7964  C CG1  . VAL C 2 295 ? 14.190  98.700  63.642  1.00 27.29  ? 313 VAL C CG1  1 
ATOM   7965  C CG2  . VAL C 2 295 ? 15.531  97.299  65.227  1.00 22.62  ? 313 VAL C CG2  1 
ATOM   7966  N N    . LEU C 2 296 ? 13.567  95.757  67.049  1.00 15.88  ? 314 LEU C N    1 
ATOM   7967  C CA   . LEU C 2 296 ? 13.799  94.538  67.818  1.00 21.79  ? 314 LEU C CA   1 
ATOM   7968  C C    . LEU C 2 296 ? 12.585  94.197  68.611  1.00 19.72  ? 314 LEU C C    1 
ATOM   7969  O O    . LEU C 2 296 ? 12.498  93.119  69.169  1.00 18.28  ? 314 LEU C O    1 
ATOM   7970  C CB   . LEU C 2 296 ? 14.993  94.748  68.770  1.00 19.11  ? 314 LEU C CB   1 
ATOM   7971  C CG   . LEU C 2 296 ? 16.464  94.572  68.434  1.00 11.09  ? 314 LEU C CG   1 
ATOM   7972  C CD1  . LEU C 2 296 ? 16.953  95.581  67.422  1.00 18.46  ? 314 LEU C CD1  1 
ATOM   7973  C CD2  . LEU C 2 296 ? 17.252  94.654  69.721  1.00 6.19   ? 314 LEU C CD2  1 
ATOM   7974  N N    . THR C 2 297 ? 11.669  95.148  68.718  1.00 21.35  ? 315 THR C N    1 
ATOM   7975  C CA   . THR C 2 297 ? 10.398  94.941  69.370  1.00 22.10  ? 315 THR C CA   1 
ATOM   7976  C C    . THR C 2 297 ? 9.461   94.556  68.264  1.00 27.97  ? 315 THR C C    1 
ATOM   7977  O O    . THR C 2 297 ? 8.396   95.122  68.143  1.00 38.25  ? 315 THR C O    1 
ATOM   7978  C CB   . THR C 2 297 ? 9.816   96.233  69.966  1.00 17.08  ? 315 THR C CB   1 
ATOM   7979  O OG1  . THR C 2 297 ? 9.698   97.236  68.959  1.00 13.65  ? 315 THR C OG1  1 
ATOM   7980  C CG2  . THR C 2 297 ? 10.663  96.739  71.096  1.00 22.68  ? 315 THR C CG2  1 
ATOM   7981  N N    . GLU C 2 298 ? 9.850   93.609  67.433  1.00 25.59  ? 316 GLU C N    1 
ATOM   7982  C CA   . GLU C 2 298 ? 9.035   93.178  66.347  1.00 18.93  ? 316 GLU C CA   1 
ATOM   7983  C C    . GLU C 2 298 ? 8.851   91.805  66.743  1.00 23.63  ? 316 GLU C C    1 
ATOM   7984  O O    . GLU C 2 298 ? 9.752   91.188  67.243  1.00 29.62  ? 316 GLU C O    1 
ATOM   7985  C CB   . GLU C 2 298 ? 9.764   93.221  65.033  1.00 19.25  ? 316 GLU C CB   1 
ATOM   7986  C CG   . GLU C 2 298 ? 8.909   92.815  63.851  1.00 25.44  ? 316 GLU C CG   1 
ATOM   7987  C CD   . GLU C 2 298 ? 9.038   93.730  62.666  1.00 25.32  ? 316 GLU C CD   1 
ATOM   7988  O OE1  . GLU C 2 298 ? 10.111  94.324  62.478  1.00 22.81  ? 316 GLU C OE1  1 
ATOM   7989  O OE2  . GLU C 2 298 ? 8.053   93.843  61.922  1.00 24.38  ? 316 GLU C OE2  1 
ATOM   7990  N N    . PRO C 2 299 ? 7.701   91.262  66.464  1.00 25.32  ? 317 PRO C N    1 
ATOM   7991  C CA   . PRO C 2 299 ? 7.442   89.958  67.003  1.00 25.18  ? 317 PRO C CA   1 
ATOM   7992  C C    . PRO C 2 299 ? 8.432   88.872  66.683  1.00 21.07  ? 317 PRO C C    1 
ATOM   7993  O O    . PRO C 2 299 ? 8.724   88.063  67.549  1.00 18.83  ? 317 PRO C O    1 
ATOM   7994  C CB   . PRO C 2 299 ? 6.116   89.655  66.364  1.00 22.46  ? 317 PRO C CB   1 
ATOM   7995  C CG   . PRO C 2 299 ? 5.399   90.950  66.403  1.00 18.84  ? 317 PRO C CG   1 
ATOM   7996  C CD   . PRO C 2 299 ? 6.454   91.967  66.126  1.00 25.09  ? 317 PRO C CD   1 
ATOM   7997  N N    . PHE C 2 300 ? 8.936   88.836  65.480  1.00 18.38  ? 318 PHE C N    1 
ATOM   7998  C CA   . PHE C 2 300 ? 9.824   87.769  65.077  1.00 23.24  ? 318 PHE C CA   1 
ATOM   7999  C C    . PHE C 2 300 ? 11.169  87.726  65.758  1.00 26.13  ? 318 PHE C C    1 
ATOM   8000  O O    . PHE C 2 300 ? 11.823  86.698  65.738  1.00 27.56  ? 318 PHE C O    1 
ATOM   8001  C CB   . PHE C 2 300 ? 9.907   87.676  63.545  1.00 20.32  ? 318 PHE C CB   1 
ATOM   8002  C CG   . PHE C 2 300 ? 10.765  88.708  62.886  1.00 25.02  ? 318 PHE C CG   1 
ATOM   8003  C CD1  . PHE C 2 300 ? 10.242  89.918  62.517  1.00 23.96  ? 318 PHE C CD1  1 
ATOM   8004  C CD2  . PHE C 2 300 ? 12.074  88.427  62.562  1.00 28.35  ? 318 PHE C CD2  1 
ATOM   8005  C CE1  . PHE C 2 300 ? 11.027  90.856  61.890  1.00 22.94  ? 318 PHE C CE1  1 
ATOM   8006  C CE2  . PHE C 2 300 ? 12.858  89.359  61.931  1.00 27.32  ? 318 PHE C CE2  1 
ATOM   8007  C CZ   . PHE C 2 300 ? 12.333  90.577  61.594  1.00 23.87  ? 318 PHE C CZ   1 
ATOM   8008  N N    . LEU C 2 301 ? 11.625  88.849  66.285  1.00 24.77  ? 319 LEU C N    1 
ATOM   8009  C CA   . LEU C 2 301 ? 12.910  88.928  66.923  1.00 22.24  ? 319 LEU C CA   1 
ATOM   8010  C C    . LEU C 2 301 ? 12.877  88.690  68.401  1.00 22.79  ? 319 LEU C C    1 
ATOM   8011  O O    . LEU C 2 301 ? 13.865  88.307  68.976  1.00 24.50  ? 319 LEU C O    1 
ATOM   8012  C CB   . LEU C 2 301 ? 13.487  90.292  66.601  1.00 25.59  ? 319 LEU C CB   1 
ATOM   8013  C CG   . LEU C 2 301 ? 13.857  90.557  65.148  1.00 26.55  ? 319 LEU C CG   1 
ATOM   8014  C CD1  . LEU C 2 301 ? 14.208  92.012  64.960  1.00 24.41  ? 319 LEU C CD1  1 
ATOM   8015  C CD2  . LEU C 2 301 ? 15.010  89.678  64.695  1.00 25.25  ? 319 LEU C CD2  1 
ATOM   8016  N N    . GLN C 2 302 ? 11.766  88.970  69.041  1.00 24.26  ? 320 GLN C N    1 
ATOM   8017  C CA   . GLN C 2 302 ? 11.586  88.641  70.431  1.00 23.08  ? 320 GLN C CA   1 
ATOM   8018  C C    . GLN C 2 302 ? 11.485  87.162  70.482  1.00 24.85  ? 320 GLN C C    1 
ATOM   8019  O O    . GLN C 2 302 ? 11.952  86.542  71.384  1.00 28.17  ? 320 GLN C O    1 
ATOM   8020  C CB   . GLN C 2 302 ? 10.246  89.175  70.898  1.00 20.82  ? 320 GLN C CB   1 
ATOM   8021  C CG   . GLN C 2 302 ? 10.122  90.681  70.953  1.00 20.88  ? 320 GLN C CG   1 
ATOM   8022  C CD   . GLN C 2 302 ? 8.738   91.123  71.357  1.00 27.25  ? 320 GLN C CD   1 
ATOM   8023  O OE1  . GLN C 2 302 ? 7.778   90.401  71.165  1.00 53.44  ? 320 GLN C OE1  1 
ATOM   8024  N NE2  . GLN C 2 302 ? 8.632   92.319  71.909  1.00 24.14  ? 320 GLN C NE2  1 
ATOM   8025  N N    . SER C 2 303 ? 10.876  86.580  69.480  1.00 23.89  ? 321 SER C N    1 
ATOM   8026  C CA   . SER C 2 303 ? 10.740  85.147  69.409  1.00 22.88  ? 321 SER C CA   1 
ATOM   8027  C C    . SER C 2 303 ? 12.031  84.420  69.602  1.00 20.39  ? 321 SER C C    1 
ATOM   8028  O O    . SER C 2 303 ? 12.048  83.371  70.195  1.00 26.15  ? 321 SER C O    1 
ATOM   8029  C CB   . SER C 2 303 ? 10.153  84.701  68.098  1.00 27.28  ? 321 SER C CB   1 
ATOM   8030  O OG   . SER C 2 303 ? 8.838   85.199  67.954  1.00 37.05  ? 321 SER C OG   1 
ATOM   8031  N N    . ILE C 2 304 ? 13.115  84.950  69.112  1.00 19.22  ? 322 ILE C N    1 
ATOM   8032  C CA   . ILE C 2 304 ? 14.359  84.298  69.327  1.00 22.74  ? 322 ILE C CA   1 
ATOM   8033  C C    . ILE C 2 304 ? 14.624  84.312  70.784  1.00 23.85  ? 322 ILE C C    1 
ATOM   8034  O O    . ILE C 2 304 ? 15.015  83.302  71.343  1.00 31.70  ? 322 ILE C O    1 
ATOM   8035  C CB   . ILE C 2 304 ? 15.467  85.068  68.602  1.00 25.79  ? 322 ILE C CB   1 
ATOM   8036  C CG1  . ILE C 2 304 ? 15.051  85.292  67.150  1.00 22.11  ? 322 ILE C CG1  1 
ATOM   8037  C CG2  . ILE C 2 304 ? 16.788  84.327  68.694  1.00 18.21  ? 322 ILE C CG2  1 
ATOM   8038  C CD1  . ILE C 2 304 ? 16.055  86.042  66.314  1.00 19.94  ? 322 ILE C CD1  1 
ATOM   8039  N N    . PHE C 2 305 ? 14.430  85.450  71.407  1.00 22.15  ? 323 PHE C N    1 
ATOM   8040  C CA   . PHE C 2 305 ? 14.616  85.589  72.827  1.00 23.74  ? 323 PHE C CA   1 
ATOM   8041  C C    . PHE C 2 305 ? 13.586  84.954  73.698  1.00 27.18  ? 323 PHE C C    1 
ATOM   8042  O O    . PHE C 2 305 ? 13.922  84.316  74.679  1.00 34.34  ? 323 PHE C O    1 
ATOM   8043  C CB   . PHE C 2 305 ? 14.663  87.062  73.177  1.00 24.14  ? 323 PHE C CB   1 
ATOM   8044  C CG   . PHE C 2 305 ? 15.767  87.818  72.528  1.00 22.49  ? 323 PHE C CG   1 
ATOM   8045  C CD1  . PHE C 2 305 ? 17.075  87.536  72.816  1.00 21.08  ? 323 PHE C CD1  1 
ATOM   8046  C CD2  . PHE C 2 305 ? 15.484  88.849  71.669  1.00 19.06  ? 323 PHE C CD2  1 
ATOM   8047  C CE1  . PHE C 2 305 ? 18.088  88.241  72.228  1.00 17.08  ? 323 PHE C CE1  1 
ATOM   8048  C CE2  . PHE C 2 305 ? 16.487  89.565  71.079  1.00 16.77  ? 323 PHE C CE2  1 
ATOM   8049  C CZ   . PHE C 2 305 ? 17.793  89.256  71.359  1.00 20.04  ? 323 PHE C CZ   1 
ATOM   8050  N N    . ASP C 2 306 ? 12.323  85.169  73.391  1.00 24.15  ? 324 ASP C N    1 
ATOM   8051  C CA   . ASP C 2 306 ? 11.247  84.654  74.195  1.00 22.97  ? 324 ASP C CA   1 
ATOM   8052  C C    . ASP C 2 306 ? 11.245  83.162  74.378  1.00 29.68  ? 324 ASP C C    1 
ATOM   8053  O O    . ASP C 2 306 ? 10.925  82.689  75.450  1.00 40.58  ? 324 ASP C O    1 
ATOM   8054  C CB   . ASP C 2 306 ? 9.936   85.117  73.613  1.00 21.25  ? 324 ASP C CB   1 
ATOM   8055  C CG   . ASP C 2 306 ? 9.554   86.498  74.079  1.00 35.62  ? 324 ASP C CG   1 
ATOM   8056  O OD1  . ASP C 2 306 ? 10.247  87.028  74.967  1.00 39.88  ? 324 ASP C OD1  1 
ATOM   8057  O OD2  . ASP C 2 306 ? 8.558   87.046  73.572  1.00 28.81  ? 324 ASP C OD2  1 
ATOM   8058  N N    . LYS C 2 307 ? 11.654  82.420  73.378  1.00 21.43  ? 325 LYS C N    1 
ATOM   8059  C CA   . LYS C 2 307 ? 11.684  80.972  73.451  1.00 21.36  ? 325 LYS C CA   1 
ATOM   8060  C C    . LYS C 2 307 ? 12.941  80.453  74.053  1.00 27.11  ? 325 LYS C C    1 
ATOM   8061  O O    . LYS C 2 307 ? 13.180  79.265  74.024  1.00 33.99  ? 325 LYS C O    1 
ATOM   8062  C CB   . LYS C 2 307 ? 11.529  80.371  72.077  1.00 21.34  ? 325 LYS C CB   1 
ATOM   8063  C CG   . LYS C 2 307 ? 10.307  80.848  71.321  1.00 45.49  ? 325 LYS C CG   1 
ATOM   8064  C CD   . LYS C 2 307 ? 10.120  80.088  70.019  1.00 38.66  ? 325 LYS C CD   1 
ATOM   8065  C CE   . LYS C 2 307 ? 11.317  80.232  69.105  1.00 23.83  ? 325 LYS C CE   1 
ATOM   8066  N NZ   . LYS C 2 307 ? 11.116  79.454  67.857  1.00 22.78  ? 325 LYS C NZ   1 
ATOM   8067  N N    . ALA C 2 308 ? 13.813  81.338  74.480  1.00 23.76  ? 326 ALA C N    1 
ATOM   8068  C CA   . ALA C 2 308 ? 15.013  80.940  75.158  1.00 27.54  ? 326 ALA C CA   1 
ATOM   8069  C C    . ALA C 2 308 ? 14.994  81.504  76.542  1.00 37.64  ? 326 ALA C C    1 
ATOM   8070  O O    . ALA C 2 308 ? 16.000  81.411  77.238  1.00 47.14  ? 326 ALA C O    1 
ATOM   8071  C CB   . ALA C 2 308 ? 16.199  81.473  74.436  1.00 28.29  ? 326 ALA C CB   1 
ATOM   8072  N N    . ASN C 2 309 ? 13.858  82.041  76.972  1.00 37.84  ? 327 ASN C N    1 
ATOM   8073  C CA   . ASN C 2 309 ? 13.719  82.679  78.289  1.00 39.82  ? 327 ASN C CA   1 
ATOM   8074  C C    . ASN C 2 309 ? 14.642  83.859  78.500  1.00 33.80  ? 327 ASN C C    1 
ATOM   8075  O O    . ASN C 2 309 ? 15.289  83.967  79.529  1.00 25.95  ? 327 ASN C O    1 
ATOM   8076  C CB   . ASN C 2 309 ? 13.795  81.650  79.434  1.00 31.51  ? 327 ASN C CB   1 
ATOM   8077  C CG   . ASN C 2 309 ? 12.635  81.742  80.398  1.00 30.16  ? 327 ASN C CG   1 
ATOM   8078  O OD1  . ASN C 2 309 ? 11.579  82.270  80.077  1.00 32.87  ? 327 ASN C OD1  1 
ATOM   8079  N ND2  . ASN C 2 309 ? 12.829  81.208  81.591  1.00 33.29  ? 327 ASN C ND2  1 
ATOM   8080  N N    . ILE C 2 310 ? 14.696  84.753  77.519  1.00 28.74  ? 328 ILE C N    1 
ATOM   8081  C CA   . ILE C 2 310 ? 15.531  85.936  77.627  1.00 27.83  ? 328 ILE C CA   1 
ATOM   8082  C C    . ILE C 2 310 ? 14.677  87.159  77.389  1.00 27.39  ? 328 ILE C C    1 
ATOM   8083  O O    . ILE C 2 310 ? 14.791  87.816  76.378  1.00 33.45  ? 328 ILE C O    1 
ATOM   8084  C CB   . ILE C 2 310 ? 16.691  85.912  76.626  1.00 22.49  ? 328 ILE C CB   1 
ATOM   8085  C CG1  . ILE C 2 310 ? 17.347  84.540  76.589  1.00 22.12  ? 328 ILE C CG1  1 
ATOM   8086  C CG2  . ILE C 2 310 ? 17.731  86.946  77.002  1.00 22.34  ? 328 ILE C CG2  1 
ATOM   8087  C CD1  . ILE C 2 310 ? 18.644  84.506  75.834  1.00 19.33  ? 328 ILE C CD1  1 
ATOM   8088  N N    . LYS C 2 311 ? 13.808  87.471  78.339  1.00 23.95  ? 329 LYS C N    1 
ATOM   8089  C CA   . LYS C 2 311 ? 12.958  88.637  78.222  1.00 26.53  ? 329 LYS C CA   1 
ATOM   8090  C C    . LYS C 2 311 ? 13.791  89.838  78.254  1.00 25.27  ? 329 LYS C C    1 
ATOM   8091  O O    . LYS C 2 311 ? 14.619  89.988  79.129  1.00 25.14  ? 329 LYS C O    1 
ATOM   8092  C CB   . LYS C 2 311 ? 11.978  88.731  79.369  1.00 23.76  ? 329 LYS C CB   1 
ATOM   8093  C CG   . LYS C 2 311 ? 10.986  89.882  79.269  1.00 27.00  ? 329 LYS C CG   1 
ATOM   8094  C CD   . LYS C 2 311 ? 10.062  89.725  78.070  1.00 37.39  ? 329 LYS C CD   1 
ATOM   8095  C CE   . LYS C 2 311 ? 9.482   91.058  77.634  1.00 31.30  ? 329 LYS C CE   1 
ATOM   8096  N NZ   . LYS C 2 311 ? 8.862   91.798  78.763  1.00 27.16  ? 329 LYS C NZ   1 
ATOM   8097  N N    . LEU C 2 312 ? 13.512  90.761  77.361  1.00 28.21  ? 330 LEU C N    1 
ATOM   8098  C CA   . LEU C 2 312 ? 14.358  91.902  77.240  1.00 32.25  ? 330 LEU C CA   1 
ATOM   8099  C C    . LEU C 2 312 ? 13.834  93.227  77.682  1.00 25.24  ? 330 LEU C C    1 
ATOM   8100  O O    . LEU C 2 312 ? 12.814  93.683  77.228  1.00 29.78  ? 330 LEU C O    1 
ATOM   8101  C CB   . LEU C 2 312 ? 14.873  92.001  75.794  1.00 30.15  ? 330 LEU C CB   1 
ATOM   8102  C CG   . LEU C 2 312 ? 15.959  91.091  75.233  1.00 23.29  ? 330 LEU C CG   1 
ATOM   8103  C CD1  . LEU C 2 312 ? 16.528  91.790  74.022  1.00 16.36  ? 330 LEU C CD1  1 
ATOM   8104  C CD2  . LEU C 2 312 ? 17.072  90.833  76.221  1.00 18.15  ? 330 LEU C CD2  1 
ATOM   8105  N N    . ASN C 2 313 ? 14.580  93.858  78.567  1.00 22.04  ? 331 ASN C N    1 
ATOM   8106  C CA   . ASN C 2 313 ? 14.249  95.173  78.967  1.00 24.80  ? 331 ASN C CA   1 
ATOM   8107  C C    . ASN C 2 313 ? 15.019  95.814  77.941  1.00 29.03  ? 331 ASN C C    1 
ATOM   8108  O O    . ASN C 2 313 ? 16.184  95.528  77.758  1.00 32.46  ? 331 ASN C O    1 
ATOM   8109  C CB   . ASN C 2 313 ? 14.844  95.567  80.294  1.00 33.39  ? 331 ASN C CB   1 
ATOM   8110  C CG   . ASN C 2 313 ? 16.353  95.581  80.314  1.00 33.80  ? 331 ASN C CG   1 
ATOM   8111  O OD1  . ASN C 2 313 ? 16.988  95.071  79.404  1.00 30.16  ? 331 ASN C OD1  1 
ATOM   8112  N ND2  . ASN C 2 313 ? 16.930  96.235  81.310  1.00 42.49  ? 331 ASN C ND2  1 
ATOM   8113  N N    . TYR C 2 314 ? 14.386  96.709  77.244  1.00 24.61  ? 332 TYR C N    1 
ATOM   8114  C CA   . TYR C 2 314 ? 15.038  97.298  76.146  1.00 21.24  ? 332 TYR C CA   1 
ATOM   8115  C C    . TYR C 2 314 ? 15.805  98.494  76.591  1.00 20.33  ? 332 TYR C C    1 
ATOM   8116  O O    . TYR C 2 314 ? 16.039  99.389  75.815  1.00 17.50  ? 332 TYR C O    1 
ATOM   8117  C CB   . TYR C 2 314 ? 13.944  97.599  75.168  1.00 19.19  ? 332 TYR C CB   1 
ATOM   8118  C CG   . TYR C 2 314 ? 13.348  96.344  74.592  1.00 25.65  ? 332 TYR C CG   1 
ATOM   8119  C CD1  . TYR C 2 314 ? 14.123  95.466  73.853  1.00 30.64  ? 332 TYR C CD1  1 
ATOM   8120  C CD2  . TYR C 2 314 ? 12.017  96.031  74.794  1.00 26.64  ? 332 TYR C CD2  1 
ATOM   8121  C CE1  . TYR C 2 314 ? 13.591  94.312  73.326  1.00 27.96  ? 332 TYR C CE1  1 
ATOM   8122  C CE2  . TYR C 2 314 ? 11.475  94.873  74.274  1.00 29.58  ? 332 TYR C CE2  1 
ATOM   8123  C CZ   . TYR C 2 314 ? 12.270  94.025  73.541  1.00 33.35  ? 332 TYR C CZ   1 
ATOM   8124  O OH   . TYR C 2 314 ? 11.732  92.882  73.023  1.00 39.66  ? 332 TYR C OH   1 
ATOM   8125  N N    . GLY C 2 315 ? 16.243  98.475  77.842  1.00 21.14  ? 333 GLY C N    1 
ATOM   8126  C CA   . GLY C 2 315 ? 16.981  99.585  78.399  1.00 21.11  ? 333 GLY C CA   1 
ATOM   8127  C C    . GLY C 2 315 ? 16.147  100.555 79.201  1.00 21.59  ? 333 GLY C C    1 
ATOM   8128  O O    . GLY C 2 315 ? 16.543  101.680 79.430  1.00 17.97  ? 333 GLY C O    1 
ATOM   8129  N N    . VAL C 2 316 ? 14.991  100.138 79.666  1.00 14.05  ? 334 VAL C N    1 
ATOM   8130  C CA   . VAL C 2 316 ? 14.188  101.049 80.399  1.00 14.07  ? 334 VAL C CA   1 
ATOM   8131  C C    . VAL C 2 316 ? 14.770  101.030 81.751  1.00 21.23  ? 334 VAL C C    1 
ATOM   8132  O O    . VAL C 2 316 ? 14.962  99.972  82.333  1.00 17.37  ? 334 VAL C O    1 
ATOM   8133  C CB   . VAL C 2 316 ? 12.731  100.660 80.411  1.00 15.72  ? 334 VAL C CB   1 
ATOM   8134  C CG1  . VAL C 2 316 ? 12.548  99.314  81.095  1.00 29.32  ? 334 VAL C CG1  1 
ATOM   8135  C CG2  . VAL C 2 316 ? 11.891  101.736 81.077  1.00 13.96  ? 334 VAL C CG2  1 
ATOM   8136  N N    . LEU C 2 317 ? 15.105  102.205 82.250  1.00 22.84  ? 335 LEU C N    1 
ATOM   8137  C CA   . LEU C 2 317 ? 15.769  102.309 83.522  1.00 18.08  ? 335 LEU C CA   1 
ATOM   8138  C C    . LEU C 2 317 ? 14.943  102.855 84.646  1.00 25.20  ? 335 LEU C C    1 
ATOM   8139  O O    . LEU C 2 317 ? 13.849  103.353 84.423  1.00 19.67  ? 335 LEU C O    1 
ATOM   8140  C CB   . LEU C 2 317 ? 17.012  103.163 83.295  1.00 15.26  ? 335 LEU C CB   1 
ATOM   8141  C CG   . LEU C 2 317 ? 18.188  102.552 82.534  1.00 12.89  ? 335 LEU C CG   1 
ATOM   8142  C CD1  . LEU C 2 317 ? 19.378  103.481 82.586  1.00 11.48  ? 335 LEU C CD1  1 
ATOM   8143  C CD2  . LEU C 2 317 ? 18.572  101.202 83.100  1.00 10.94  ? 335 LEU C CD2  1 
ATOM   8144  N N    . ASP C 2 318 ? 15.424  102.702 85.875  1.00 26.77  ? 336 ASP C N    1 
ATOM   8145  C CA   . ASP C 2 318 ? 14.743  103.174 87.044  1.00 15.11  ? 336 ASP C CA   1 
ATOM   8146  C C    . ASP C 2 318 ? 15.050  104.618 87.497  1.00 23.25  ? 336 ASP C C    1 
ATOM   8147  O O    . ASP C 2 318 ? 14.193  105.466 87.676  1.00 26.45  ? 336 ASP C O    1 
ATOM   8148  C CB   . ASP C 2 318 ? 14.962  102.121 88.111  1.00 19.58  ? 336 ASP C CB   1 
ATOM   8149  C CG   . ASP C 2 318 ? 14.298  100.790 87.794  1.00 31.51  ? 336 ASP C CG   1 
ATOM   8150  O OD1  . ASP C 2 318 ? 13.436  100.756 86.893  1.00 36.47  ? 336 ASP C OD1  1 
ATOM   8151  O OD2  . ASP C 2 318 ? 14.605  99.780  88.459  1.00 36.04  ? 336 ASP C OD2  1 
ATOM   8152  N N    . ASP C 2 319 ? 16.340  104.906 87.528  1.00 25.21  ? 337 ASP C N    1 
ATOM   8153  C CA   . ASP C 2 319 ? 16.812  106.269 87.754  1.00 30.57  ? 337 ASP C CA   1 
ATOM   8154  C C    . ASP C 2 319 ? 16.790  107.168 86.553  1.00 32.66  ? 337 ASP C C    1 
ATOM   8155  O O    . ASP C 2 319 ? 17.813  107.589 86.069  1.00 33.52  ? 337 ASP C O    1 
ATOM   8156  C CB   . ASP C 2 319 ? 18.253  106.035 88.196  1.00 28.81  ? 337 ASP C CB   1 
ATOM   8157  C CG   . ASP C 2 319 ? 18.749  107.057 89.184  1.00 36.96  ? 337 ASP C CG   1 
ATOM   8158  O OD1  . ASP C 2 319 ? 17.996  107.986 89.526  1.00 47.22  ? 337 ASP C OD1  1 
ATOM   8159  O OD2  . ASP C 2 319 ? 19.908  106.921 89.621  1.00 29.11  ? 337 ASP C OD2  1 
ATOM   8160  N N    . THR C 2 320 ? 15.621  107.488 86.070  1.00 29.17  ? 338 THR C N    1 
ATOM   8161  C CA   . THR C 2 320 ? 15.526  108.252 84.861  1.00 28.35  ? 338 THR C CA   1 
ATOM   8162  C C    . THR C 2 320 ? 15.499  109.705 85.280  1.00 33.80  ? 338 THR C C    1 
ATOM   8163  O O    . THR C 2 320 ? 15.307  110.588 84.466  1.00 31.55  ? 338 THR C O    1 
ATOM   8164  C CB   . THR C 2 320 ? 14.283  107.783 84.112  1.00 29.32  ? 338 THR C CB   1 
ATOM   8165  O OG1  . THR C 2 320 ? 13.303  107.352 85.060  1.00 32.35  ? 338 THR C OG1  1 
ATOM   8166  C CG2  . THR C 2 320 ? 14.619  106.628 83.200  1.00 21.69  ? 338 THR C CG2  1 
ATOM   8167  N N    . HIS C 2 321 ? 15.597  109.960 86.562  1.00 42.36  ? 339 HIS C N    1 
ATOM   8168  C CA   . HIS C 2 321 ? 15.639  111.317 87.078  1.00 36.25  ? 339 HIS C CA   1 
ATOM   8169  C C    . HIS C 2 321 ? 16.774  112.146 86.508  1.00 32.41  ? 339 HIS C C    1 
ATOM   8170  O O    . HIS C 2 321 ? 16.649  113.258 86.042  1.00 26.40  ? 339 HIS C O    1 
ATOM   8171  C CB   . HIS C 2 321 ? 15.600  111.302 88.615  1.00 38.12  ? 339 HIS C CB   1 
ATOM   8172  C CG   . HIS C 2 321 ? 14.425  110.589 89.199  1.00 37.95  ? 339 HIS C CG   1 
ATOM   8173  N ND1  . HIS C 2 321 ? 13.140  111.072 89.102  1.00 43.52  ? 339 HIS C ND1  1 
ATOM   8174  C CD2  . HIS C 2 321 ? 14.334  109.408 89.849  1.00 41.36  ? 339 HIS C CD2  1 
ATOM   8175  C CE1  . HIS C 2 321 ? 12.311  110.235 89.695  1.00 49.74  ? 339 HIS C CE1  1 
ATOM   8176  N NE2  . HIS C 2 321 ? 13.011  109.215 90.156  1.00 48.08  ? 339 HIS C NE2  1 
ATOM   8177  N N    . ALA C 2 322 ? 17.905  111.491 86.455  1.00 28.13  ? 340 ALA C N    1 
ATOM   8178  C CA   . ALA C 2 322 ? 19.069  112.180 85.979  1.00 34.43  ? 340 ALA C CA   1 
ATOM   8179  C C    . ALA C 2 322 ? 18.971  112.910 84.681  1.00 38.87  ? 340 ALA C C    1 
ATOM   8180  O O    . ALA C 2 322 ? 19.430  114.039 84.606  1.00 42.93  ? 340 ALA C O    1 
ATOM   8181  C CB   . ALA C 2 322 ? 20.140  111.133 85.911  1.00 26.63  ? 340 ALA C CB   1 
ATOM   8182  N N    . GLU C 2 323 ? 18.434  112.284 83.644  1.00 33.22  ? 341 GLU C N    1 
ATOM   8183  C CA   . GLU C 2 323 ? 18.168  112.918 82.364  1.00 22.76  ? 341 GLU C CA   1 
ATOM   8184  C C    . GLU C 2 323 ? 17.055  113.908 82.284  1.00 19.52  ? 341 GLU C C    1 
ATOM   8185  O O    . GLU C 2 323 ? 17.196  114.912 81.635  1.00 20.18  ? 341 GLU C O    1 
ATOM   8186  C CB   . GLU C 2 323 ? 17.762  111.797 81.468  1.00 22.46  ? 341 GLU C CB   1 
ATOM   8187  C CG   . GLU C 2 323 ? 18.772  110.675 81.396  1.00 28.97  ? 341 GLU C CG   1 
ATOM   8188  C CD   . GLU C 2 323 ? 18.372  109.451 82.175  1.00 30.00  ? 341 GLU C CD   1 
ATOM   8189  O OE1  . GLU C 2 323 ? 17.502  108.695 81.706  1.00 31.20  ? 341 GLU C OE1  1 
ATOM   8190  O OE2  . GLU C 2 323 ? 18.948  109.240 83.251  1.00 29.33  ? 341 GLU C OE2  1 
ATOM   8191  N N    . PHE C 2 324 ? 15.925  113.610 82.892  1.00 21.01  ? 342 PHE C N    1 
ATOM   8192  C CA   . PHE C 2 324 ? 14.716  114.420 82.800  1.00 20.00  ? 342 PHE C CA   1 
ATOM   8193  C C    . PHE C 2 324 ? 14.907  115.708 83.432  1.00 24.68  ? 342 PHE C C    1 
ATOM   8194  O O    . PHE C 2 324 ? 14.276  116.663 83.068  1.00 21.88  ? 342 PHE C O    1 
ATOM   8195  C CB   . PHE C 2 324 ? 13.672  113.681 83.596  1.00 21.13  ? 342 PHE C CB   1 
ATOM   8196  C CG   . PHE C 2 324 ? 12.256  113.914 83.197  1.00 21.87  ? 342 PHE C CG   1 
ATOM   8197  C CD1  . PHE C 2 324 ? 11.733  113.327 82.074  1.00 27.01  ? 342 PHE C CD1  1 
ATOM   8198  C CD2  . PHE C 2 324 ? 11.414  114.615 84.027  1.00 20.07  ? 342 PHE C CD2  1 
ATOM   8199  C CE1  . PHE C 2 324 ? 10.412  113.505 81.741  1.00 28.26  ? 342 PHE C CE1  1 
ATOM   8200  C CE2  . PHE C 2 324 ? 10.096  114.794 83.702  1.00 20.35  ? 342 PHE C CE2  1 
ATOM   8201  C CZ   . PHE C 2 324 ? 9.590   114.245 82.555  1.00 21.99  ? 342 PHE C CZ   1 
ATOM   8202  N N    . ARG C 2 325 ? 15.743  115.738 84.442  1.00 32.40  ? 343 ARG C N    1 
ATOM   8203  C CA   . ARG C 2 325 ? 16.013  116.970 85.170  1.00 35.78  ? 343 ARG C CA   1 
ATOM   8204  C C    . ARG C 2 325 ? 16.721  118.008 84.347  1.00 36.13  ? 343 ARG C C    1 
ATOM   8205  O O    . ARG C 2 325 ? 16.455  119.188 84.477  1.00 34.16  ? 343 ARG C O    1 
ATOM   8206  C CB   . ARG C 2 325 ? 16.789  116.646 86.430  1.00 40.79  ? 343 ARG C CB   1 
ATOM   8207  C CG   . ARG C 2 325 ? 17.352  117.858 87.160  1.00 51.59  ? 343 ARG C CG   1 
ATOM   8208  C CD   . ARG C 2 325 ? 17.477  117.645 88.661  1.00 71.72  ? 343 ARG C CD   1 
ATOM   8209  N NE   . ARG C 2 325 ? 17.896  116.292 89.015  1.00 86.78  ? 343 ARG C NE   1 
ATOM   8210  C CZ   . ARG C 2 325 ? 19.159  115.913 89.172  1.00 80.64  ? 343 ARG C CZ   1 
ATOM   8211  N NH1  . ARG C 2 325 ? 20.141  116.786 88.998  1.00 72.47  ? 343 ARG C NH1  1 
ATOM   8212  N NH2  . ARG C 2 325 ? 19.440  114.657 89.497  1.00 64.50  ? 343 ARG C NH2  1 
ATOM   8213  N N    . LYS C 2 326 ? 17.637  117.575 83.500  1.00 32.96  ? 344 LYS C N    1 
ATOM   8214  C CA   . LYS C 2 326 ? 18.409  118.478 82.713  1.00 22.94  ? 344 LYS C CA   1 
ATOM   8215  C C    . LYS C 2 326 ? 17.720  118.859 81.455  1.00 17.75  ? 344 LYS C C    1 
ATOM   8216  O O    . LYS C 2 326 ? 18.017  119.880 80.898  1.00 19.28  ? 344 LYS C O    1 
ATOM   8217  C CB   . LYS C 2 326 ? 19.726  117.811 82.438  1.00 20.89  ? 344 LYS C CB   1 
ATOM   8218  C CG   . LYS C 2 326 ? 20.561  117.592 83.679  1.00 24.12  ? 344 LYS C CG   1 
ATOM   8219  C CD   . LYS C 2 326 ? 21.088  118.917 84.199  1.00 30.25  ? 344 LYS C CD   1 
ATOM   8220  C CE   . LYS C 2 326 ? 21.681  118.796 85.589  1.00 31.18  ? 344 LYS C CE   1 
ATOM   8221  N NZ   . LYS C 2 326 ? 20.633  118.800 86.637  1.00 35.10  ? 344 LYS C NZ   1 
ATOM   8222  N N    . ALA C 2 327 ? 16.796  118.050 80.991  1.00 17.45  ? 345 ALA C N    1 
ATOM   8223  C CA   . ALA C 2 327 ? 16.048  118.382 79.811  1.00 18.94  ? 345 ALA C CA   1 
ATOM   8224  C C    . ALA C 2 327 ? 15.166  119.550 80.043  1.00 22.63  ? 345 ALA C C    1 
ATOM   8225  O O    . ALA C 2 327 ? 14.962  120.351 79.166  1.00 18.60  ? 345 ALA C O    1 
ATOM   8226  C CB   . ALA C 2 327 ? 15.239  117.212 79.383  1.00 15.61  ? 345 ALA C CB   1 
ATOM   8227  N N    . GLN C 2 328 ? 14.582  119.628 81.212  1.00 23.50  ? 346 GLN C N    1 
ATOM   8228  C CA   . GLN C 2 328 ? 13.743  120.735 81.575  1.00 20.80  ? 346 GLN C CA   1 
ATOM   8229  C C    . GLN C 2 328 ? 14.530  121.997 81.627  1.00 20.11  ? 346 GLN C C    1 
ATOM   8230  O O    . GLN C 2 328 ? 14.033  123.046 81.284  1.00 22.38  ? 346 GLN C O    1 
ATOM   8231  C CB   . GLN C 2 328 ? 13.169  120.413 82.917  1.00 20.29  ? 346 GLN C CB   1 
ATOM   8232  C CG   . GLN C 2 328 ? 12.409  119.098 82.932  1.00 21.25  ? 346 GLN C CG   1 
ATOM   8233  C CD   . GLN C 2 328 ? 12.016  118.632 84.313  1.00 21.58  ? 346 GLN C CD   1 
ATOM   8234  O OE1  . GLN C 2 328 ? 12.855  118.272 85.122  1.00 23.82  ? 346 GLN C OE1  1 
ATOM   8235  N NE2  . GLN C 2 328 ? 10.730  118.616 84.578  1.00 22.52  ? 346 GLN C NE2  1 
ATOM   8236  N N    . ASP C 2 329 ? 15.743  121.933 82.126  1.00 21.17  ? 347 ASP C N    1 
ATOM   8237  C CA   . ASP C 2 329 ? 16.637  123.078 82.120  1.00 26.11  ? 347 ASP C CA   1 
ATOM   8238  C C    . ASP C 2 329 ? 17.010  123.476 80.706  1.00 23.07  ? 347 ASP C C    1 
ATOM   8239  O O    . ASP C 2 329 ? 17.138  124.647 80.418  1.00 23.40  ? 347 ASP C O    1 
ATOM   8240  C CB   . ASP C 2 329 ? 17.881  122.763 82.952  1.00 25.69  ? 347 ASP C CB   1 
ATOM   8241  C CG   . ASP C 2 329 ? 17.562  122.259 84.344  1.00 27.11  ? 347 ASP C CG   1 
ATOM   8242  O OD1  . ASP C 2 329 ? 16.465  122.531 84.857  1.00 30.51  ? 347 ASP C OD1  1 
ATOM   8243  O OD2  . ASP C 2 329 ? 18.430  121.597 84.939  1.00 23.62  ? 347 ASP C OD2  1 
ATOM   8244  N N    . TYR C 2 330 ? 17.230  122.522 79.830  1.00 20.10  ? 348 TYR C N    1 
ATOM   8245  C CA   . TYR C 2 330 ? 17.486  122.808 78.440  1.00 18.82  ? 348 TYR C CA   1 
ATOM   8246  C C    . TYR C 2 330 ? 16.301  123.452 77.800  1.00 22.17  ? 348 TYR C C    1 
ATOM   8247  O O    . TYR C 2 330 ? 16.447  124.431 77.109  1.00 23.95  ? 348 TYR C O    1 
ATOM   8248  C CB   . TYR C 2 330 ? 17.721  121.477 77.753  1.00 17.28  ? 348 TYR C CB   1 
ATOM   8249  C CG   . TYR C 2 330 ? 18.114  121.511 76.318  1.00 20.09  ? 348 TYR C CG   1 
ATOM   8250  C CD1  . TYR C 2 330 ? 19.179  122.271 75.894  1.00 18.80  ? 348 TYR C CD1  1 
ATOM   8251  C CD2  . TYR C 2 330 ? 17.442  120.739 75.385  1.00 21.88  ? 348 TYR C CD2  1 
ATOM   8252  C CE1  . TYR C 2 330 ? 19.544  122.293 74.572  1.00 22.45  ? 348 TYR C CE1  1 
ATOM   8253  C CE2  . TYR C 2 330 ? 17.807  120.753 74.058  1.00 26.13  ? 348 TYR C CE2  1 
ATOM   8254  C CZ   . TYR C 2 330 ? 18.862  121.535 73.661  1.00 22.11  ? 348 TYR C CZ   1 
ATOM   8255  O OH   . TYR C 2 330 ? 19.235  121.564 72.349  1.00 15.99  ? 348 TYR C OH   1 
ATOM   8256  N N    . VAL C 2 331 ? 15.112  122.931 78.035  1.00 17.07  ? 349 VAL C N    1 
ATOM   8257  C CA   . VAL C 2 331 ? 13.925  123.451 77.405  1.00 17.58  ? 349 VAL C CA   1 
ATOM   8258  C C    . VAL C 2 331 ? 13.694  124.845 77.861  1.00 21.43  ? 349 VAL C C    1 
ATOM   8259  O O    . VAL C 2 331 ? 13.352  125.695 77.081  1.00 19.86  ? 349 VAL C O    1 
ATOM   8260  C CB   . VAL C 2 331 ? 12.714  122.597 77.742  1.00 18.19  ? 349 VAL C CB   1 
ATOM   8261  C CG1  . VAL C 2 331 ? 11.415  123.278 77.381  1.00 18.42  ? 349 VAL C CG1  1 
ATOM   8262  C CG2  . VAL C 2 331 ? 12.811  121.259 77.047  1.00 23.73  ? 349 VAL C CG2  1 
ATOM   8263  N N    . PHE C 2 332 ? 13.901  125.108 79.130  1.00 19.84  ? 350 PHE C N    1 
ATOM   8264  C CA   . PHE C 2 332 ? 13.613  126.411 79.630  1.00 22.31  ? 350 PHE C CA   1 
ATOM   8265  C C    . PHE C 2 332 ? 14.481  127.437 78.991  1.00 26.88  ? 350 PHE C C    1 
ATOM   8266  O O    . PHE C 2 332 ? 14.026  128.484 78.609  1.00 25.06  ? 350 PHE C O    1 
ATOM   8267  C CB   . PHE C 2 332 ? 13.835  126.429 81.106  1.00 21.96  ? 350 PHE C CB   1 
ATOM   8268  C CG   . PHE C 2 332 ? 13.074  127.510 81.806  1.00 36.49  ? 350 PHE C CG   1 
ATOM   8269  C CD1  . PHE C 2 332 ? 11.697  127.452 81.893  1.00 38.58  ? 350 PHE C CD1  1 
ATOM   8270  C CD2  . PHE C 2 332 ? 13.725  128.587 82.366  1.00 29.80  ? 350 PHE C CD2  1 
ATOM   8271  C CE1  . PHE C 2 332 ? 10.983  128.441 82.528  1.00 41.24  ? 350 PHE C CE1  1 
ATOM   8272  C CE2  . PHE C 2 332 ? 13.015  129.579 83.001  1.00 36.67  ? 350 PHE C CE2  1 
ATOM   8273  C CZ   . PHE C 2 332 ? 11.643  129.506 83.085  1.00 36.73  ? 350 PHE C CZ   1 
ATOM   8274  N N    . GLY C 2 333 ? 15.749  127.132 78.838  1.00 29.62  ? 351 GLY C N    1 
ATOM   8275  C CA   . GLY C 2 333 ? 16.696  128.051 78.242  1.00 25.87  ? 351 GLY C CA   1 
ATOM   8276  C C    . GLY C 2 333 ? 16.478  128.179 76.772  1.00 27.53  ? 351 GLY C C    1 
ATOM   8277  O O    . GLY C 2 333 ? 17.102  128.998 76.142  1.00 25.65  ? 351 GLY C O    1 
ATOM   8278  N N    . LEU C 2 334 ? 15.546  127.411 76.240  1.00 23.41  ? 352 LEU C N    1 
ATOM   8279  C CA   . LEU C 2 334 ? 15.271  127.456 74.833  1.00 23.58  ? 352 LEU C CA   1 
ATOM   8280  C C    . LEU C 2 334 ? 13.977  128.142 74.638  1.00 23.52  ? 352 LEU C C    1 
ATOM   8281  O O    . LEU C 2 334 ? 13.826  128.985 73.781  1.00 24.90  ? 352 LEU C O    1 
ATOM   8282  C CB   . LEU C 2 334 ? 15.231  126.052 74.261  1.00 21.48  ? 352 LEU C CB   1 
ATOM   8283  C CG   . LEU C 2 334 ? 16.497  125.324 73.841  1.00 14.83  ? 352 LEU C CG   1 
ATOM   8284  C CD1  . LEU C 2 334 ? 16.120  123.897 73.517  1.00 15.89  ? 352 LEU C CD1  1 
ATOM   8285  C CD2  . LEU C 2 334 ? 17.038  125.995 72.605  1.00 14.66  ? 352 LEU C CD2  1 
ATOM   8286  N N    . THR C 2 335 ? 13.021  127.780 75.443  1.00 18.34  ? 353 THR C N    1 
ATOM   8287  C CA   . THR C 2 335 ? 11.748  128.437 75.361  1.00 25.14  ? 353 THR C CA   1 
ATOM   8288  C C    . THR C 2 335 ? 11.828  129.902 75.755  1.00 26.91  ? 353 THR C C    1 
ATOM   8289  O O    . THR C 2 335 ? 11.219  130.747 75.103  1.00 25.37  ? 353 THR C O    1 
ATOM   8290  C CB   . THR C 2 335 ? 10.721  127.635 76.167  1.00 18.99  ? 353 THR C CB   1 
ATOM   8291  O OG1  . THR C 2 335 ? 11.274  127.301 77.438  1.00 25.80  ? 353 THR C OG1  1 
ATOM   8292  C CG2  . THR C 2 335 ? 10.368  126.364 75.441  1.00 16.58  ? 353 THR C CG2  1 
ATOM   8293  N N    . ILE C 2 336 ? 12.554  130.205 76.825  1.00 24.33  ? 354 ILE C N    1 
ATOM   8294  C CA   . ILE C 2 336 ? 12.731  131.567 77.316  1.00 23.75  ? 354 ILE C CA   1 
ATOM   8295  C C    . ILE C 2 336 ? 13.463  132.518 76.428  1.00 23.87  ? 354 ILE C C    1 
ATOM   8296  O O    . ILE C 2 336 ? 13.097  133.670 76.319  1.00 25.28  ? 354 ILE C O    1 
ATOM   8297  C CB   . ILE C 2 336 ? 13.289  131.552 78.755  1.00 22.70  ? 354 ILE C CB   1 
ATOM   8298  C CG1  . ILE C 2 336 ? 12.632  132.631 79.608  1.00 25.55  ? 354 ILE C CG1  1 
ATOM   8299  C CG2  . ILE C 2 336 ? 14.800  131.684 78.808  1.00 23.38  ? 354 ILE C CG2  1 
ATOM   8300  C CD1  . ILE C 2 336 ? 11.224  132.291 80.017  1.00 30.49  ? 354 ILE C CD1  1 
ATOM   8301  N N    . GLN C 2 337 ? 14.515  132.042 75.802  1.00 22.13  ? 355 GLN C N    1 
ATOM   8302  C CA   . GLN C 2 337 ? 15.226  132.836 74.857  1.00 25.36  ? 355 GLN C CA   1 
ATOM   8303  C C    . GLN C 2 337 ? 14.493  133.067 73.556  1.00 29.17  ? 355 GLN C C    1 
ATOM   8304  O O    . GLN C 2 337 ? 14.581  134.105 72.940  1.00 29.29  ? 355 GLN C O    1 
ATOM   8305  C CB   . GLN C 2 337 ? 16.454  132.042 74.447  1.00 21.79  ? 355 GLN C CB   1 
ATOM   8306  C CG   . GLN C 2 337 ? 16.174  130.734 73.731  1.00 21.24  ? 355 GLN C CG   1 
ATOM   8307  C CD   . GLN C 2 337 ? 17.411  129.969 73.336  1.00 36.27  ? 355 GLN C CD   1 
ATOM   8308  O OE1  . GLN C 2 337 ? 18.485  130.183 73.882  1.00 67.12  ? 355 GLN C OE1  1 
ATOM   8309  N NE2  . GLN C 2 337 ? 17.269  129.086 72.359  1.00 26.49  ? 355 GLN C NE2  1 
ATOM   8310  N N    . SER C 2 338 ? 13.633  132.139 73.198  1.00 23.25  ? 356 SER C N    1 
ATOM   8311  C CA   . SER C 2 338 ? 12.938  132.252 71.957  1.00 22.16  ? 356 SER C CA   1 
ATOM   8312  C C    . SER C 2 338 ? 12.201  133.517 72.164  1.00 26.52  ? 356 SER C C    1 
ATOM   8313  O O    . SER C 2 338 ? 12.072  134.316 71.268  1.00 32.37  ? 356 SER C O    1 
ATOM   8314  C CB   . SER C 2 338 ? 12.000  131.119 71.640  1.00 24.16  ? 356 SER C CB   1 
ATOM   8315  O OG   . SER C 2 338 ? 12.713  129.913 71.477  1.00 28.65  ? 356 SER C OG   1 
ATOM   8316  N N    . ALA C 2 339 ? 11.690  133.718 73.346  1.00 24.92  ? 357 ALA C N    1 
ATOM   8317  C CA   . ALA C 2 339 ? 10.877  134.867 73.591  1.00 27.39  ? 357 ALA C CA   1 
ATOM   8318  C C    . ALA C 2 339 ? 11.577  136.175 73.752  1.00 31.90  ? 357 ALA C C    1 
ATOM   8319  O O    . ALA C 2 339 ? 10.963  137.215 73.546  1.00 35.92  ? 357 ALA C O    1 
ATOM   8320  C CB   . ALA C 2 339 ? 10.045  134.600 74.795  1.00 22.77  ? 357 ALA C CB   1 
ATOM   8321  N N    . MET C 2 340 ? 12.831  136.161 74.170  1.00 30.33  ? 358 MET C N    1 
ATOM   8322  C CA   . MET C 2 340 ? 13.554  137.393 74.423  1.00 30.16  ? 358 MET C CA   1 
ATOM   8323  C C    . MET C 2 340 ? 13.990  137.766 73.078  1.00 29.50  ? 358 MET C C    1 
ATOM   8324  O O    . MET C 2 340 ? 14.375  138.882 72.826  1.00 30.23  ? 358 MET C O    1 
ATOM   8325  C CB   . MET C 2 340 ? 14.799  137.120 75.268  1.00 22.63  ? 358 MET C CB   1 
ATOM   8326  C CG   . MET C 2 340 ? 15.897  136.379 74.547  1.00 19.60  ? 358 MET C CG   1 
ATOM   8327  S SD   . MET C 2 340 ? 17.540  137.014 74.815  1.00 64.54  ? 358 MET C SD   1 
ATOM   8328  C CE   . MET C 2 340 ? 17.227  138.759 74.983  1.00 16.72  ? 358 MET C CE   1 
ATOM   8329  N N    . HIS C 2 341 ? 13.912  136.826 72.178  1.00 28.75  ? 359 HIS C N    1 
ATOM   8330  C CA   . HIS C 2 341 ? 14.426  137.046 70.859  1.00 30.76  ? 359 HIS C CA   1 
ATOM   8331  C C    . HIS C 2 341 ? 13.341  137.783 70.202  1.00 34.36  ? 359 HIS C C    1 
ATOM   8332  O O    . HIS C 2 341 ? 13.568  138.630 69.382  1.00 32.37  ? 359 HIS C O    1 
ATOM   8333  C CB   . HIS C 2 341 ? 14.618  135.730 70.131  1.00 29.79  ? 359 HIS C CB   1 
ATOM   8334  C CG   . HIS C 2 341 ? 15.859  134.983 70.498  1.00 21.56  ? 359 HIS C CG   1 
ATOM   8335  N ND1  . HIS C 2 341 ? 16.759  135.433 71.433  1.00 20.89  ? 359 HIS C ND1  1 
ATOM   8336  C CD2  . HIS C 2 341 ? 16.339  133.801 70.054  1.00 18.33  ? 359 HIS C CD2  1 
ATOM   8337  C CE1  . HIS C 2 341 ? 17.745  134.562 71.545  1.00 17.46  ? 359 HIS C CE1  1 
ATOM   8338  N NE2  . HIS C 2 341 ? 17.514  133.565 70.717  1.00 12.04  ? 359 HIS C NE2  1 
ATOM   8339  N N    . HIS C 2 342 ? 12.118  137.436 70.537  1.00 34.89  ? 360 HIS C N    1 
ATOM   8340  C CA   . HIS C 2 342 ? 10.980  138.112 69.964  1.00 40.56  ? 360 HIS C CA   1 
ATOM   8341  C C    . HIS C 2 342 ? 10.848  139.448 70.551  1.00 40.94  ? 360 HIS C C    1 
ATOM   8342  O O    . HIS C 2 342 ? 10.407  140.315 69.877  1.00 41.86  ? 360 HIS C O    1 
ATOM   8343  C CB   . HIS C 2 342 ? 9.717   137.339 70.170  1.00 43.73  ? 360 HIS C CB   1 
ATOM   8344  C CG   . HIS C 2 342 ? 8.697   137.576 69.108  1.00 46.30  ? 360 HIS C CG   1 
ATOM   8345  N ND1  . HIS C 2 342 ? 7.356   137.719 69.381  1.00 51.66  ? 360 HIS C ND1  1 
ATOM   8346  C CD2  . HIS C 2 342 ? 8.825   137.711 67.768  1.00 47.00  ? 360 HIS C CD2  1 
ATOM   8347  C CE1  . HIS C 2 342 ? 6.699   137.926 68.254  1.00 60.43  ? 360 HIS C CE1  1 
ATOM   8348  N NE2  . HIS C 2 342 ? 7.567   137.924 67.260  1.00 55.49  ? 360 HIS C NE2  1 
ATOM   8349  N N    . GLU C 2 343 ? 11.247  139.639 71.801  1.00 33.73  ? 361 GLU C N    1 
ATOM   8350  C CA   . GLU C 2 343 ? 11.253  140.966 72.423  1.00 32.92  ? 361 GLU C CA   1 
ATOM   8351  C C    . GLU C 2 343 ? 12.435  141.823 72.068  1.00 30.91  ? 361 GLU C C    1 
ATOM   8352  O O    . GLU C 2 343 ? 12.486  142.964 72.426  1.00 35.99  ? 361 GLU C O    1 
ATOM   8353  C CB   . GLU C 2 343 ? 11.241  140.839 73.918  1.00 36.63  ? 361 GLU C CB   1 
ATOM   8354  C CG   . GLU C 2 343 ? 10.301  141.769 74.645  1.00 39.10  ? 361 GLU C CG   1 
ATOM   8355  C CD   . GLU C 2 343 ? 10.640  141.842 76.106  1.00 32.77  ? 361 GLU C CD   1 
ATOM   8356  O OE1  . GLU C 2 343 ? 10.702  140.775 76.742  1.00 26.87  ? 361 GLU C OE1  1 
ATOM   8357  O OE2  . GLU C 2 343 ? 10.861  142.957 76.603  1.00 33.99  ? 361 GLU C OE2  1 
ATOM   8358  N N    . LEU C 2 344 ? 13.394  141.276 71.352  1.00 30.93  ? 362 LEU C N    1 
ATOM   8359  C CA   . LEU C 2 344 ? 14.542  142.031 70.939  1.00 28.49  ? 362 LEU C CA   1 
ATOM   8360  C C    . LEU C 2 344 ? 14.195  142.471 69.593  1.00 32.84  ? 362 LEU C C    1 
ATOM   8361  O O    . LEU C 2 344 ? 14.658  143.477 69.125  1.00 38.48  ? 362 LEU C O    1 
ATOM   8362  C CB   . LEU C 2 344 ? 15.745  141.130 70.822  1.00 22.82  ? 362 LEU C CB   1 
ATOM   8363  C CG   . LEU C 2 344 ? 16.837  141.143 71.876  1.00 27.88  ? 362 LEU C CG   1 
ATOM   8364  C CD1  . LEU C 2 344 ? 17.819  140.055 71.499  1.00 27.55  ? 362 LEU C CD1  1 
ATOM   8365  C CD2  . LEU C 2 344 ? 17.524  142.495 71.915  1.00 28.22  ? 362 LEU C CD2  1 
ATOM   8366  N N    . GLN C 2 345 ? 13.375  141.691 68.933  1.00 29.16  ? 363 GLN C N    1 
ATOM   8367  C CA   . GLN C 2 345 ? 12.980  142.023 67.597  1.00 34.87  ? 363 GLN C CA   1 
ATOM   8368  C C    . GLN C 2 345 ? 11.575  142.484 67.642  1.00 40.24  ? 363 GLN C C    1 
ATOM   8369  O O    . GLN C 2 345 ? 10.777  142.117 66.795  1.00 43.52  ? 363 GLN C O    1 
ATOM   8370  C CB   . GLN C 2 345 ? 13.139  140.844 66.667  1.00 39.91  ? 363 GLN C CB   1 
ATOM   8371  C CG   . GLN C 2 345 ? 14.517  140.203 66.669  1.00 35.62  ? 363 GLN C CG   1 
ATOM   8372  C CD   . GLN C 2 345 ? 14.495  138.736 66.279  1.00 29.16  ? 363 GLN C CD   1 
ATOM   8373  O OE1  . GLN C 2 345 ? 13.507  138.038 66.483  1.00 27.71  ? 363 GLN C OE1  1 
ATOM   8374  N NE2  . GLN C 2 345 ? 15.592  138.267 65.712  1.00 25.73  ? 363 GLN C NE2  1 
ATOM   8375  N N    . GLU C 2 346 ? 11.236  143.249 68.665  1.00 43.81  ? 364 GLU C N    1 
ATOM   8376  C CA   . GLU C 2 346 ? 9.931   143.882 68.754  1.00 41.69  ? 364 GLU C CA   1 
ATOM   8377  C C    . GLU C 2 346 ? 10.356  145.085 69.494  1.00 41.28  ? 364 GLU C C    1 
ATOM   8378  O O    . GLU C 2 346 ? 9.559   145.825 70.015  1.00 50.26  ? 364 GLU C O    1 
ATOM   8379  C CB   . GLU C 2 346 ? 8.850   143.039 69.424  1.00 44.48  ? 364 GLU C CB   1 
ATOM   8380  C CG   . GLU C 2 346 ? 8.710   143.007 70.937  1.00 48.00  ? 364 GLU C CG   1 
ATOM   8381  C CD   . GLU C 2 346 ? 7.711   141.949 71.379  1.00 50.53  ? 364 GLU C CD   1 
ATOM   8382  O OE1  . GLU C 2 346 ? 7.254   141.168 70.520  1.00 43.89  ? 364 GLU C OE1  1 
ATOM   8383  O OE2  . GLU C 2 346 ? 7.376   141.893 72.578  1.00 51.40  ? 364 GLU C OE2  1 
ATOM   8384  N N    . ARG C 2 347 ? 11.652  145.311 69.511  1.00 36.96  ? 365 ARG C N    1 
ATOM   8385  C CA   . ARG C 2 347 ? 12.190  146.479 70.144  1.00 41.31  ? 365 ARG C CA   1 
ATOM   8386  C C    . ARG C 2 347 ? 13.161  147.035 69.149  1.00 41.38  ? 365 ARG C C    1 
ATOM   8387  O O    . ARG C 2 347 ? 13.573  148.181 69.233  1.00 43.27  ? 365 ARG C O    1 
ATOM   8388  C CB   . ARG C 2 347 ? 12.938  146.091 71.388  1.00 37.87  ? 365 ARG C CB   1 
ATOM   8389  C CG   . ARG C 2 347 ? 12.299  146.473 72.706  1.00 41.20  ? 365 ARG C CG   1 
ATOM   8390  C CD   . ARG C 2 347 ? 13.361  146.480 73.793  1.00 42.07  ? 365 ARG C CD   1 
ATOM   8391  N NE   . ARG C 2 347 ? 14.200  147.672 73.702  1.00 52.07  ? 365 ARG C NE   1 
ATOM   8392  C CZ   . ARG C 2 347 ? 15.448  147.687 73.250  1.00 42.69  ? 365 ARG C CZ   1 
ATOM   8393  N NH1  . ARG C 2 347 ? 16.021  146.567 72.846  1.00 42.61  ? 365 ARG C NH1  1 
ATOM   8394  N NH2  . ARG C 2 347 ? 16.116  148.824 73.196  1.00 39.90  ? 365 ARG C NH2  1 
ATOM   8395  N N    . PHE C 2 348 ? 13.553  146.215 68.194  1.00 35.36  ? 366 PHE C N    1 
ATOM   8396  C CA   . PHE C 2 348 ? 14.460  146.663 67.162  1.00 38.41  ? 366 PHE C CA   1 
ATOM   8397  C C    . PHE C 2 348 ? 13.635  146.689 65.924  1.00 38.55  ? 366 PHE C C    1 
ATOM   8398  O O    . PHE C 2 348 ? 13.999  147.293 64.928  1.00 38.12  ? 366 PHE C O    1 
ATOM   8399  C CB   . PHE C 2 348 ? 15.632  145.711 67.006  1.00 36.14  ? 366 PHE C CB   1 
ATOM   8400  C CG   . PHE C 2 348 ? 16.898  146.210 67.621  1.00 37.38  ? 366 PHE C CG   1 
ATOM   8401  C CD1  . PHE C 2 348 ? 17.716  147.077 66.928  1.00 35.98  ? 366 PHE C CD1  1 
ATOM   8402  C CD2  . PHE C 2 348 ? 17.267  145.814 68.891  1.00 37.23  ? 366 PHE C CD2  1 
ATOM   8403  C CE1  . PHE C 2 348 ? 18.885  147.538 67.494  1.00 32.92  ? 366 PHE C CE1  1 
ATOM   8404  C CE2  . PHE C 2 348 ? 18.431  146.274 69.462  1.00 32.48  ? 366 PHE C CE2  1 
ATOM   8405  C CZ   . PHE C 2 348 ? 19.242  147.136 68.762  1.00 31.12  ? 366 PHE C CZ   1 
ATOM   8406  N N    . LYS C 2 349 ? 12.520  145.998 65.961  1.00 39.79  ? 367 LYS C N    1 
ATOM   8407  C CA   . LYS C 2 349 ? 11.622  146.035 64.841  1.00 44.57  ? 367 LYS C CA   1 
ATOM   8408  C C    . LYS C 2 349 ? 11.011  147.369 64.993  1.00 48.29  ? 367 LYS C C    1 
ATOM   8409  O O    . LYS C 2 349 ? 10.868  148.120 64.034  1.00 51.21  ? 367 LYS C O    1 
ATOM   8410  C CB   . LYS C 2 349 ? 10.565  144.946 64.914  1.00 42.99  ? 367 LYS C CB   1 
ATOM   8411  C CG   . LYS C 2 349 ? 9.595   144.942 63.748  1.00 33.89  ? 367 LYS C CG   1 
ATOM   8412  C CD   . LYS C 2 349 ? 10.318  144.687 62.439  1.00 36.56  ? 367 LYS C CD   1 
ATOM   8413  C CE   . LYS C 2 349 ? 9.351   144.506 61.279  1.00 51.62  ? 367 LYS C CE   1 
ATOM   8414  N NZ   . LYS C 2 349 ? 10.021  144.466 59.947  1.00 45.37  ? 367 LYS C NZ   1 
ATOM   8415  N N    . ASN C 2 350 ? 10.636  147.687 66.218  1.00 45.98  ? 368 ASN C N    1 
ATOM   8416  C CA   . ASN C 2 350 ? 10.122  148.991 66.505  1.00 46.07  ? 368 ASN C CA   1 
ATOM   8417  C C    . ASN C 2 350 ? 11.258  149.979 66.662  1.00 49.14  ? 368 ASN C C    1 
ATOM   8418  O O    . ASN C 2 350 ? 11.701  150.259 67.766  1.00 36.93  ? 368 ASN C O    1 
ATOM   8419  C CB   . ASN C 2 350 ? 9.331   148.855 67.771  1.00 45.34  ? 368 ASN C CB   1 
ATOM   8420  C CG   . ASN C 2 350 ? 8.176   147.893 67.635  1.00 50.31  ? 368 ASN C CG   1 
ATOM   8421  O OD1  . ASN C 2 350 ? 7.939   147.332 66.571  1.00 53.10  ? 368 ASN C OD1  1 
ATOM   8422  N ND2  . ASN C 2 350 ? 7.444   147.697 68.723  1.00 55.22  ? 368 ASN C ND2  1 
ATOM   8423  N N    . LYS C 2 351 ? 11.746  150.499 65.549  1.00 54.83  ? 369 LYS C N    1 
ATOM   8424  C CA   . LYS C 2 351 ? 12.828  151.455 65.569  1.00 54.29  ? 369 LYS C CA   1 
ATOM   8425  C C    . LYS C 2 351 ? 12.423  152.633 64.726  1.00 63.34  ? 369 LYS C C    1 
ATOM   8426  O O    . LYS C 2 351 ? 12.163  152.490 63.539  1.00 59.88  ? 369 LYS C O    1 
ATOM   8427  C CB   . LYS C 2 351 ? 14.067  150.854 64.938  1.00 54.56  ? 369 LYS C CB   1 
ATOM   8428  C CG   . LYS C 2 351 ? 15.261  151.792 64.878  1.00 57.53  ? 369 LYS C CG   1 
ATOM   8429  C CD   . LYS C 2 351 ? 16.411  151.319 65.753  1.00 48.02  ? 369 LYS C CD   1 
ATOM   8430  C CE   . LYS C 2 351 ? 17.515  152.363 65.806  1.00 37.74  ? 369 LYS C CE   1 
ATOM   8431  N NZ   . LYS C 2 351 ? 18.871  151.775 65.628  1.00 35.02  ? 369 LYS C NZ   1 
ATOM   8432  N N    . GLN D 2 4   ? -25.764 115.560 -2.643  1.00 32.40  ? 22  GLN D N    1 
ATOM   8433  C CA   . GLN D 2 4   ? -25.938 115.594 -1.214  1.00 36.56  ? 22  GLN D CA   1 
ATOM   8434  C C    . GLN D 2 4   ? -25.045 114.568 -0.605  1.00 42.10  ? 22  GLN D C    1 
ATOM   8435  O O    . GLN D 2 4   ? -25.519 113.574 -0.074  1.00 46.26  ? 22  GLN D O    1 
ATOM   8436  C CB   . GLN D 2 4   ? -27.385 115.316 -0.839  1.00 44.46  ? 22  GLN D CB   1 
ATOM   8437  C CG   . GLN D 2 4   ? -28.349 116.478 -1.024  1.00 44.70  ? 22  GLN D CG   1 
ATOM   8438  C CD   . GLN D 2 4   ? -28.863 116.620 -2.440  1.00 46.43  ? 22  GLN D CD   1 
ATOM   8439  O OE1  . GLN D 2 4   ? -28.853 115.673 -3.215  1.00 53.25  ? 22  GLN D OE1  1 
ATOM   8440  N NE2  . GLN D 2 4   ? -29.331 117.813 -2.778  1.00 50.21  ? 22  GLN D NE2  1 
ATOM   8441  N N    . LYS D 2 5   ? -23.741 114.798 -0.684  1.00 42.83  ? 23  LYS D N    1 
ATOM   8442  C CA   . LYS D 2 5   ? -22.789 113.842 -0.165  1.00 42.72  ? 23  LYS D CA   1 
ATOM   8443  C C    . LYS D 2 5   ? -21.939 114.467 0.863   1.00 40.49  ? 23  LYS D C    1 
ATOM   8444  O O    . LYS D 2 5   ? -21.806 113.957 1.957   1.00 32.84  ? 23  LYS D O    1 
ATOM   8445  C CB   . LYS D 2 5   ? -21.833 113.476 -1.285  1.00 50.47  ? 23  LYS D CB   1 
ATOM   8446  C CG   . LYS D 2 5   ? -20.794 112.436 -0.891  1.00 63.39  ? 23  LYS D CG   1 
ATOM   8447  C CD   . LYS D 2 5   ? -19.426 112.741 -1.484  1.00 55.86  ? 23  LYS D CD   1 
ATOM   8448  C CE   . LYS D 2 5   ? -18.375 111.795 -0.935  1.00 48.80  ? 23  LYS D CE   1 
ATOM   8449  N NZ   . LYS D 2 5   ? -18.338 111.798 0.552   1.00 40.67  ? 23  LYS D NZ   1 
ATOM   8450  N N    . ILE D 2 6   ? -21.391 115.611 0.536   1.00 52.23  ? 24  ILE D N    1 
ATOM   8451  C CA   . ILE D 2 6   ? -20.468 116.276 1.420   1.00 44.03  ? 24  ILE D CA   1 
ATOM   8452  C C    . ILE D 2 6   ? -21.188 117.160 2.414   1.00 35.21  ? 24  ILE D C    1 
ATOM   8453  O O    . ILE D 2 6   ? -20.623 117.964 3.127   1.00 38.32  ? 24  ILE D O    1 
ATOM   8454  C CB   . ILE D 2 6   ? -19.383 116.969 0.593   1.00 45.04  ? 24  ILE D CB   1 
ATOM   8455  C CG1  . ILE D 2 6   ? -18.548 115.944 -0.158  1.00 51.40  ? 24  ILE D CG1  1 
ATOM   8456  C CG2  . ILE D 2 6   ? -18.462 117.762 1.497   1.00 43.22  ? 24  ILE D CG2  1 
ATOM   8457  C CD1  . ILE D 2 6   ? -17.636 116.565 -1.193  1.00 51.57  ? 24  ILE D CD1  1 
ATOM   8458  N N    . GLU D 2 7   ? -22.494 117.065 2.359   1.00 31.17  ? 25  GLU D N    1 
ATOM   8459  C CA   . GLU D 2 7   ? -23.303 117.740 3.304   1.00 32.15  ? 25  GLU D CA   1 
ATOM   8460  C C    . GLU D 2 7   ? -23.549 116.897 4.558   1.00 38.35  ? 25  GLU D C    1 
ATOM   8461  O O    . GLU D 2 7   ? -24.101 117.405 5.519   1.00 37.07  ? 25  GLU D O    1 
ATOM   8462  C CB   . GLU D 2 7   ? -24.549 118.042 2.534   1.00 36.78  ? 25  GLU D CB   1 
ATOM   8463  C CG   . GLU D 2 7   ? -24.262 118.697 1.197   1.00 43.29  ? 25  GLU D CG   1 
ATOM   8464  C CD   . GLU D 2 7   ? -25.520 118.896 0.394   1.00 52.21  ? 25  GLU D CD   1 
ATOM   8465  O OE1  . GLU D 2 7   ? -26.574 118.449 0.875   1.00 51.31  ? 25  GLU D OE1  1 
ATOM   8466  O OE2  . GLU D 2 7   ? -25.463 119.493 -0.700  1.00 49.12  ? 25  GLU D OE2  1 
ATOM   8467  N N    . LEU D 2 8   ? -23.135 115.628 4.582   1.00 36.92  ? 26  LEU D N    1 
ATOM   8468  C CA   . LEU D 2 8   ? -23.225 114.792 5.789   1.00 30.39  ? 26  LEU D CA   1 
ATOM   8469  C C    . LEU D 2 8   ? -22.424 115.445 6.832   1.00 32.15  ? 26  LEU D C    1 
ATOM   8470  O O    . LEU D 2 8   ? -22.788 115.458 7.985   1.00 34.15  ? 26  LEU D O    1 
ATOM   8471  C CB   . LEU D 2 8   ? -22.745 113.378 5.564   1.00 25.53  ? 26  LEU D CB   1 
ATOM   8472  C CG   . LEU D 2 8   ? -22.682 112.304 6.645   1.00 36.20  ? 26  LEU D CG   1 
ATOM   8473  C CD1  . LEU D 2 8   ? -24.082 112.014 7.154   1.00 50.76  ? 26  LEU D CD1  1 
ATOM   8474  C CD2  . LEU D 2 8   ? -22.006 111.030 6.162   1.00 46.10  ? 26  LEU D CD2  1 
ATOM   8475  N N    . SER D 2 9   ? -21.290 115.978 6.431   1.00 36.51  ? 27  SER D N    1 
ATOM   8476  C CA   . SER D 2 9   ? -20.419 116.687 7.319   1.00 37.10  ? 27  SER D CA   1 
ATOM   8477  C C    . SER D 2 9   ? -20.980 117.898 7.996   1.00 31.40  ? 27  SER D C    1 
ATOM   8478  O O    . SER D 2 9   ? -20.727 118.132 9.160   1.00 29.66  ? 27  SER D O    1 
ATOM   8479  C CB   . SER D 2 9   ? -19.281 117.118 6.438   1.00 33.28  ? 27  SER D CB   1 
ATOM   8480  O OG   . SER D 2 9   ? -19.732 118.003 5.450   1.00 33.13  ? 27  SER D OG   1 
ATOM   8481  N N    . ILE D 2 10  ? -21.764 118.673 7.288   1.00 23.53  ? 28  ILE D N    1 
ATOM   8482  C CA   . ILE D 2 10  ? -22.289 119.877 7.849   1.00 27.49  ? 28  ILE D CA   1 
ATOM   8483  C C    . ILE D 2 10  ? -23.495 119.537 8.666   1.00 32.40  ? 28  ILE D C    1 
ATOM   8484  O O    . ILE D 2 10  ? -24.111 120.400 9.252   1.00 30.82  ? 28  ILE D O    1 
ATOM   8485  C CB   . ILE D 2 10  ? -22.582 120.879 6.751   1.00 31.68  ? 28  ILE D CB   1 
ATOM   8486  C CG1  . ILE D 2 10  ? -21.456 120.851 5.725   1.00 35.64  ? 28  ILE D CG1  1 
ATOM   8487  C CG2  . ILE D 2 10  ? -22.734 122.287 7.299   1.00 33.57  ? 28  ILE D CG2  1 
ATOM   8488  C CD1  . ILE D 2 10  ? -21.128 122.198 5.127   1.00 33.21  ? 28  ILE D CD1  1 
ATOM   8489  N N    . SER D 2 11  ? -23.878 118.276 8.677   1.00 35.01  ? 29  SER D N    1 
ATOM   8490  C CA   . SER D 2 11  ? -24.961 117.847 9.530   1.00 28.31  ? 29  SER D CA   1 
ATOM   8491  C C    . SER D 2 11  ? -24.438 117.098 10.716  1.00 28.55  ? 29  SER D C    1 
ATOM   8492  O O    . SER D 2 11  ? -25.113 117.049 11.718  1.00 31.23  ? 29  SER D O    1 
ATOM   8493  C CB   . SER D 2 11  ? -25.887 116.946 8.738   1.00 31.93  ? 29  SER D CB   1 
ATOM   8494  O OG   . SER D 2 11  ? -26.233 117.516 7.490   1.00 33.90  ? 29  SER D OG   1 
ATOM   8495  N N    . LEU D 2 12  ? -23.227 116.542 10.624  1.00 28.97  ? 30  LEU D N    1 
ATOM   8496  C CA   . LEU D 2 12  ? -22.575 115.836 11.734  1.00 30.20  ? 30  LEU D CA   1 
ATOM   8497  C C    . LEU D 2 12  ? -21.864 116.832 12.576  1.00 23.34  ? 30  LEU D C    1 
ATOM   8498  O O    . LEU D 2 12  ? -21.251 116.502 13.551  1.00 23.36  ? 30  LEU D O    1 
ATOM   8499  C CB   . LEU D 2 12  ? -21.559 114.852 11.213  1.00 23.42  ? 30  LEU D CB   1 
ATOM   8500  C CG   . LEU D 2 12  ? -22.035 113.666 10.393  1.00 36.15  ? 30  LEU D CG   1 
ATOM   8501  C CD1  . LEU D 2 12  ? -20.847 112.895 9.851   1.00 33.88  ? 30  LEU D CD1  1 
ATOM   8502  C CD2  . LEU D 2 12  ? -22.875 112.779 11.284  1.00 35.78  ? 30  LEU D CD2  1 
ATOM   8503  N N    . SER D 2 13  ? -21.947 118.067 12.186  1.00 23.10  ? 31  SER D N    1 
ATOM   8504  C CA   . SER D 2 13  ? -21.355 119.128 12.906  1.00 23.99  ? 31  SER D CA   1 
ATOM   8505  C C    . SER D 2 13  ? -22.397 119.712 13.740  1.00 25.34  ? 31  SER D C    1 
ATOM   8506  O O    . SER D 2 13  ? -22.145 120.622 14.495  1.00 24.84  ? 31  SER D O    1 
ATOM   8507  C CB   . SER D 2 13  ? -21.007 120.191 11.917  1.00 25.93  ? 31  SER D CB   1 
ATOM   8508  O OG   . SER D 2 13  ? -22.163 120.625 11.256  1.00 29.19  ? 31  SER D OG   1 
ATOM   8509  N N    . LEU D 2 14  ? -23.599 119.219 13.589  1.00 27.20  ? 32  LEU D N    1 
ATOM   8510  C CA   . LEU D 2 14  ? -24.707 119.790 14.306  1.00 34.68  ? 32  LEU D CA   1 
ATOM   8511  C C    . LEU D 2 14  ? -25.085 118.777 15.334  1.00 32.40  ? 32  LEU D C    1 
ATOM   8512  O O    . LEU D 2 14  ? -25.863 119.056 16.227  1.00 28.89  ? 32  LEU D O    1 
ATOM   8513  C CB   . LEU D 2 14  ? -25.793 120.098 13.295  1.00 32.48  ? 32  LEU D CB   1 
ATOM   8514  C CG   . LEU D 2 14  ? -25.521 121.183 12.254  1.00 21.85  ? 32  LEU D CG   1 
ATOM   8515  C CD1  . LEU D 2 14  ? -26.498 121.083 11.111  1.00 27.39  ? 32  LEU D CD1  1 
ATOM   8516  C CD2  . LEU D 2 14  ? -25.590 122.566 12.853  1.00 16.97  ? 32  LEU D CD2  1 
ATOM   8517  N N    . ASP D 2 15  ? -24.491 117.592 15.238  1.00 33.92  ? 33  ASP D N    1 
ATOM   8518  C CA   . ASP D 2 15  ? -24.671 116.550 16.237  1.00 34.54  ? 33  ASP D CA   1 
ATOM   8519  C C    . ASP D 2 15  ? -23.709 116.923 17.324  1.00 34.09  ? 33  ASP D C    1 
ATOM   8520  O O    . ASP D 2 15  ? -23.669 116.258 18.351  1.00 22.02  ? 33  ASP D O    1 
ATOM   8521  C CB   . ASP D 2 15  ? -24.213 115.207 15.688  1.00 29.52  ? 33  ASP D CB   1 
ATOM   8522  C CG   . ASP D 2 15  ? -25.070 114.705 14.558  1.00 43.13  ? 33  ASP D CG   1 
ATOM   8523  O OD1  . ASP D 2 15  ? -26.066 115.364 14.219  1.00 52.81  ? 33  ASP D OD1  1 
ATOM   8524  O OD2  . ASP D 2 15  ? -24.747 113.631 14.013  1.00 37.84  ? 33  ASP D OD2  1 
ATOM   8525  N N    . SER D 2 16  ? -22.911 117.978 17.096  1.00 41.00  ? 34  SER D N    1 
ATOM   8526  C CA   . SER D 2 16  ? -21.912 118.452 18.053  1.00 27.38  ? 34  SER D CA   1 
ATOM   8527  C C    . SER D 2 16  ? -22.584 119.331 19.045  1.00 23.89  ? 34  SER D C    1 
ATOM   8528  O O    . SER D 2 16  ? -23.249 120.291 18.695  1.00 22.67  ? 34  SER D O    1 
ATOM   8529  C CB   . SER D 2 16  ? -20.812 119.226 17.349  1.00 17.53  ? 34  SER D CB   1 
ATOM   8530  O OG   . SER D 2 16  ? -21.279 120.468 16.874  1.00 21.37  ? 34  SER D OG   1 
ATOM   8531  N N    . PRO D 2 17  ? -22.415 119.004 20.298  1.00 19.51  ? 35  PRO D N    1 
ATOM   8532  C CA   . PRO D 2 17  ? -23.085 119.749 21.336  1.00 24.66  ? 35  PRO D CA   1 
ATOM   8533  C C    . PRO D 2 17  ? -22.597 121.172 21.531  1.00 28.27  ? 35  PRO D C    1 
ATOM   8534  O O    . PRO D 2 17  ? -23.322 121.988 22.086  1.00 28.55  ? 35  PRO D O    1 
ATOM   8535  C CB   . PRO D 2 17  ? -22.801 118.908 22.568  1.00 24.36  ? 35  PRO D CB   1 
ATOM   8536  C CG   . PRO D 2 17  ? -22.449 117.554 22.073  1.00 25.63  ? 35  PRO D CG   1 
ATOM   8537  C CD   . PRO D 2 17  ? -21.701 117.834 20.823  1.00 20.47  ? 35  PRO D CD   1 
ATOM   8538  N N    . LYS D 2 18  ? -21.398 121.479 21.091  1.00 22.67  ? 36  LYS D N    1 
ATOM   8539  C CA   . LYS D 2 18  ? -20.836 122.776 21.346  1.00 21.74  ? 36  LYS D CA   1 
ATOM   8540  C C    . LYS D 2 18  ? -20.957 123.772 20.214  1.00 26.10  ? 36  LYS D C    1 
ATOM   8541  O O    . LYS D 2 18  ? -20.218 124.747 20.165  1.00 26.41  ? 36  LYS D O    1 
ATOM   8542  C CB   . LYS D 2 18  ? -19.408 122.630 21.813  1.00 18.44  ? 36  LYS D CB   1 
ATOM   8543  C CG   . LYS D 2 18  ? -19.000 123.549 22.945  1.00 16.59  ? 36  LYS D CG   1 
ATOM   8544  C CD   . LYS D 2 18  ? -17.545 123.316 23.310  1.00 21.02  ? 36  LYS D CD   1 
ATOM   8545  C CE   . LYS D 2 18  ? -17.304 121.866 23.677  1.00 15.81  ? 36  LYS D CE   1 
ATOM   8546  N NZ   . LYS D 2 18  ? -15.871 121.587 23.948  1.00 11.76  ? 36  LYS D NZ   1 
ATOM   8547  N N    . LEU D 2 19  ? -21.866 123.540 19.286  1.00 21.66  ? 37  LEU D N    1 
ATOM   8548  C CA   . LEU D 2 19  ? -22.085 124.525 18.245  1.00 24.28  ? 37  LEU D CA   1 
ATOM   8549  C C    . LEU D 2 19  ? -22.673 125.782 18.795  1.00 21.95  ? 37  LEU D C    1 
ATOM   8550  O O    . LEU D 2 19  ? -23.618 125.754 19.556  1.00 22.65  ? 37  LEU D O    1 
ATOM   8551  C CB   . LEU D 2 19  ? -22.957 123.983 17.116  1.00 20.09  ? 37  LEU D CB   1 
ATOM   8552  C CG   . LEU D 2 19  ? -22.984 124.776 15.824  1.00 23.42  ? 37  LEU D CG   1 
ATOM   8553  C CD1  . LEU D 2 19  ? -22.241 124.018 14.745  1.00 24.85  ? 37  LEU D CD1  1 
ATOM   8554  C CD2  . LEU D 2 19  ? -24.425 124.969 15.430  1.00 32.54  ? 37  LEU D CD2  1 
ATOM   8555  N N    . ASP D 2 20  ? -22.121 126.901 18.383  1.00 21.82  ? 38  ASP D N    1 
ATOM   8556  C CA   . ASP D 2 20  ? -22.593 128.162 18.844  1.00 24.67  ? 38  ASP D CA   1 
ATOM   8557  C C    . ASP D 2 20  ? -23.100 128.973 17.741  1.00 28.26  ? 38  ASP D C    1 
ATOM   8558  O O    . ASP D 2 20  ? -23.408 128.478 16.683  1.00 36.88  ? 38  ASP D O    1 
ATOM   8559  C CB   . ASP D 2 20  ? -21.525 128.926 19.621  1.00 28.14  ? 38  ASP D CB   1 
ATOM   8560  C CG   . ASP D 2 20  ? -20.365 129.348 18.812  1.00 30.52  ? 38  ASP D CG   1 
ATOM   8561  O OD1  . ASP D 2 20  ? -20.168 128.786 17.750  1.00 34.95  ? 38  ASP D OD1  1 
ATOM   8562  O OD2  . ASP D 2 20  ? -19.623 130.241 19.265  1.00 27.76  ? 38  ASP D OD2  1 
ATOM   8563  N N    . GLU D 2 21  ? -23.302 130.221 18.017  1.00 25.23  ? 39  GLU D N    1 
ATOM   8564  C CA   . GLU D 2 21  ? -23.747 131.099 17.015  1.00 26.39  ? 39  GLU D CA   1 
ATOM   8565  C C    . GLU D 2 21  ? -22.718 131.298 15.945  1.00 31.57  ? 39  GLU D C    1 
ATOM   8566  O O    . GLU D 2 21  ? -23.059 131.349 14.780  1.00 35.26  ? 39  GLU D O    1 
ATOM   8567  C CB   . GLU D 2 21  ? -24.102 132.384 17.701  1.00 31.49  ? 39  GLU D CB   1 
ATOM   8568  C CG   . GLU D 2 21  ? -24.993 132.161 18.905  1.00 41.27  ? 39  GLU D CG   1 
ATOM   8569  C CD   . GLU D 2 21  ? -26.100 133.183 19.020  1.00 46.48  ? 39  GLU D CD   1 
ATOM   8570  O OE1  . GLU D 2 21  ? -25.821 134.386 18.868  1.00 52.59  ? 39  GLU D OE1  1 
ATOM   8571  O OE2  . GLU D 2 21  ? -27.248 132.783 19.275  1.00 33.32  ? 39  GLU D OE2  1 
ATOM   8572  N N    . SER D 2 22  ? -21.467 131.338 16.312  1.00 28.11  ? 40  SER D N    1 
ATOM   8573  C CA   . SER D 2 22  ? -20.464 131.623 15.337  1.00 26.62  ? 40  SER D CA   1 
ATOM   8574  C C    . SER D 2 22  ? -20.194 130.470 14.501  1.00 24.72  ? 40  SER D C    1 
ATOM   8575  O O    . SER D 2 22  ? -20.002 130.594 13.330  1.00 32.07  ? 40  SER D O    1 
ATOM   8576  C CB   . SER D 2 22  ? -19.217 131.884 16.024  1.00 29.70  ? 40  SER D CB   1 
ATOM   8577  O OG   . SER D 2 22  ? -18.234 131.806 15.040  1.00 35.26  ? 40  SER D OG   1 
ATOM   8578  N N    . ASP D 2 23  ? -20.160 129.326 15.101  1.00 22.32  ? 41  ASP D N    1 
ATOM   8579  C CA   . ASP D 2 23  ? -19.972 128.125 14.367  1.00 27.42  ? 41  ASP D CA   1 
ATOM   8580  C C    . ASP D 2 23  ? -21.101 127.916 13.373  1.00 33.29  ? 41  ASP D C    1 
ATOM   8581  O O    . ASP D 2 23  ? -20.886 127.443 12.272  1.00 39.05  ? 41  ASP D O    1 
ATOM   8582  C CB   . ASP D 2 23  ? -19.860 126.949 15.334  1.00 27.12  ? 41  ASP D CB   1 
ATOM   8583  C CG   . ASP D 2 23  ? -18.607 126.982 16.173  1.00 31.05  ? 41  ASP D CG   1 
ATOM   8584  O OD1  . ASP D 2 23  ? -17.628 127.633 15.778  1.00 30.99  ? 41  ASP D OD1  1 
ATOM   8585  O OD2  . ASP D 2 23  ? -18.610 126.351 17.246  1.00 23.31  ? 41  ASP D OD2  1 
ATOM   8586  N N    . PHE D 2 24  ? -22.306 128.245 13.749  1.00 26.43  ? 42  PHE D N    1 
ATOM   8587  C CA   . PHE D 2 24  ? -23.407 128.055 12.871  1.00 27.97  ? 42  PHE D CA   1 
ATOM   8588  C C    . PHE D 2 24  ? -23.273 128.845 11.610  1.00 29.30  ? 42  PHE D C    1 
ATOM   8589  O O    . PHE D 2 24  ? -23.329 128.289 10.550  1.00 29.55  ? 42  PHE D O    1 
ATOM   8590  C CB   . PHE D 2 24  ? -24.559 128.692 13.590  1.00 29.55  ? 42  PHE D CB   1 
ATOM   8591  C CG   . PHE D 2 24  ? -25.910 128.269 13.128  1.00 35.01  ? 42  PHE D CG   1 
ATOM   8592  C CD1  . PHE D 2 24  ? -26.371 126.998 13.376  1.00 35.72  ? 42  PHE D CD1  1 
ATOM   8593  C CD2  . PHE D 2 24  ? -26.749 129.178 12.524  1.00 32.34  ? 42  PHE D CD2  1 
ATOM   8594  C CE1  . PHE D 2 24  ? -27.627 126.621 12.988  1.00 31.68  ? 42  PHE D CE1  1 
ATOM   8595  C CE2  . PHE D 2 24  ? -28.008 128.809 12.131  1.00 39.60  ? 42  PHE D CE2  1 
ATOM   8596  C CZ   . PHE D 2 24  ? -28.445 127.531 12.367  1.00 35.91  ? 42  PHE D CZ   1 
ATOM   8597  N N    . ILE D 2 25  ? -22.988 130.129 11.707  1.00 29.42  ? 43  ILE D N    1 
ATOM   8598  C CA   . ILE D 2 25  ? -22.934 130.972 10.534  1.00 32.52  ? 43  ILE D CA   1 
ATOM   8599  C C    . ILE D 2 25  ? -21.790 130.578 9.661   1.00 35.52  ? 43  ILE D C    1 
ATOM   8600  O O    . ILE D 2 25  ? -21.930 130.435 8.468   1.00 36.90  ? 43  ILE D O    1 
ATOM   8601  C CB   . ILE D 2 25  ? -22.721 132.415 10.932  1.00 28.54  ? 43  ILE D CB   1 
ATOM   8602  C CG1  . ILE D 2 25  ? -23.766 132.837 11.957  1.00 31.12  ? 43  ILE D CG1  1 
ATOM   8603  C CG2  . ILE D 2 25  ? -22.787 133.318 9.717   1.00 31.03  ? 43  ILE D CG2  1 
ATOM   8604  C CD1  . ILE D 2 25  ? -23.513 134.208 12.537  1.00 31.27  ? 43  ILE D CD1  1 
ATOM   8605  N N    . LEU D 2 26  ? -20.638 130.400 10.255  1.00 31.10  ? 44  LEU D N    1 
ATOM   8606  C CA   . LEU D 2 26  ? -19.471 129.983 9.504   1.00 29.78  ? 44  LEU D CA   1 
ATOM   8607  C C    . LEU D 2 26  ? -19.643 128.650 8.781   1.00 33.06  ? 44  LEU D C    1 
ATOM   8608  O O    . LEU D 2 26  ? -18.901 128.363 7.866   1.00 34.33  ? 44  LEU D O    1 
ATOM   8609  C CB   . LEU D 2 26  ? -18.270 129.991 10.438  1.00 28.44  ? 44  LEU D CB   1 
ATOM   8610  C CG   . LEU D 2 26  ? -17.769 131.340 10.927  1.00 24.70  ? 44  LEU D CG   1 
ATOM   8611  C CD1  . LEU D 2 26  ? -16.651 131.110 11.919  1.00 20.37  ? 44  LEU D CD1  1 
ATOM   8612  C CD2  . LEU D 2 26  ? -17.289 132.191 9.771   1.00 20.61  ? 44  LEU D CD2  1 
ATOM   8613  N N    . LEU D 2 27  ? -20.592 127.821 9.185   1.00 31.52  ? 45  LEU D N    1 
ATOM   8614  C CA   . LEU D 2 27  ? -20.888 126.567 8.462   1.00 36.81  ? 45  LEU D CA   1 
ATOM   8615  C C    . LEU D 2 27  ? -22.059 126.704 7.555   1.00 31.17  ? 45  LEU D C    1 
ATOM   8616  O O    . LEU D 2 27  ? -22.111 126.117 6.505   1.00 34.42  ? 45  LEU D O    1 
ATOM   8617  C CB   . LEU D 2 27  ? -21.303 125.491 9.439   1.00 33.25  ? 45  LEU D CB   1 
ATOM   8618  C CG   . LEU D 2 27  ? -20.633 124.136 9.539   1.00 33.42  ? 45  LEU D CG   1 
ATOM   8619  C CD1  . LEU D 2 27  ? -19.128 124.287 9.497   1.00 37.57  ? 45  LEU D CD1  1 
ATOM   8620  C CD2  . LEU D 2 27  ? -21.079 123.539 10.853  1.00 18.41  ? 45  LEU D CD2  1 
ATOM   8621  N N    . SER D 2 28  ? -23.035 127.464 7.992   1.00 32.28  ? 46  SER D N    1 
ATOM   8622  C CA   . SER D 2 28  ? -24.229 127.621 7.226   1.00 32.14  ? 46  SER D CA   1 
ATOM   8623  C C    . SER D 2 28  ? -23.875 128.293 5.966   1.00 34.97  ? 46  SER D C    1 
ATOM   8624  O O    . SER D 2 28  ? -24.344 127.925 4.921   1.00 39.02  ? 46  SER D O    1 
ATOM   8625  C CB   . SER D 2 28  ? -25.235 128.430 8.010   1.00 23.74  ? 46  SER D CB   1 
ATOM   8626  O OG   . SER D 2 28  ? -25.445 127.868 9.284   1.00 25.46  ? 46  SER D OG   1 
ATOM   8627  N N    . VAL D 2 29  ? -23.033 129.290 6.051   1.00 28.51  ? 47  VAL D N    1 
ATOM   8628  C CA   . VAL D 2 29  ? -22.618 129.985 4.880   1.00 29.22  ? 47  VAL D CA   1 
ATOM   8629  C C    . VAL D 2 29  ? -21.833 129.118 3.939   1.00 35.04  ? 47  VAL D C    1 
ATOM   8630  O O    . VAL D 2 29  ? -22.108 129.120 2.763   1.00 45.74  ? 47  VAL D O    1 
ATOM   8631  C CB   . VAL D 2 29  ? -21.854 131.245 5.235   1.00 31.97  ? 47  VAL D CB   1 
ATOM   8632  C CG1  . VAL D 2 29  ? -20.906 131.660 4.125   1.00 32.03  ? 47  VAL D CG1  1 
ATOM   8633  C CG2  . VAL D 2 29  ? -22.821 132.361 5.571   1.00 36.79  ? 47  VAL D CG2  1 
ATOM   8634  N N    . LYS D 2 30  ? -20.902 128.320 4.418   1.00 33.14  ? 48  LYS D N    1 
ATOM   8635  C CA   . LYS D 2 30  ? -20.193 127.394 3.523   1.00 44.36  ? 48  LYS D CA   1 
ATOM   8636  C C    . LYS D 2 30  ? -21.062 126.303 2.911   1.00 39.93  ? 48  LYS D C    1 
ATOM   8637  O O    . LYS D 2 30  ? -20.835 125.903 1.796   1.00 46.26  ? 48  LYS D O    1 
ATOM   8638  C CB   . LYS D 2 30  ? -18.897 126.845 4.127   1.00 47.06  ? 48  LYS D CB   1 
ATOM   8639  C CG   . LYS D 2 30  ? -19.055 125.709 5.125   1.00 49.52  ? 48  LYS D CG   1 
ATOM   8640  C CD   . LYS D 2 30  ? -17.717 125.072 5.461   1.00 40.76  ? 48  LYS D CD   1 
ATOM   8641  C CE   . LYS D 2 30  ? -17.116 124.378 4.253   1.00 35.51  ? 48  LYS D CE   1 
ATOM   8642  N NZ   . LYS D 2 30  ? -15.796 123.762 4.553   1.00 24.72  ? 48  LYS D NZ   1 
ATOM   8643  N N    . TYR D 2 31  ? -22.027 125.798 3.649   1.00 35.08  ? 49  TYR D N    1 
ATOM   8644  C CA   . TYR D 2 31  ? -22.920 124.813 3.123   1.00 32.83  ? 49  TYR D CA   1 
ATOM   8645  C C    . TYR D 2 31  ? -23.643 125.431 1.980   1.00 41.89  ? 49  TYR D C    1 
ATOM   8646  O O    . TYR D 2 31  ? -23.842 124.812 0.967   1.00 41.85  ? 49  TYR D O    1 
ATOM   8647  C CB   . TYR D 2 31  ? -23.943 124.484 4.179   1.00 27.54  ? 49  TYR D CB   1 
ATOM   8648  C CG   . TYR D 2 31  ? -24.891 123.401 3.792   1.00 35.86  ? 49  TYR D CG   1 
ATOM   8649  C CD1  . TYR D 2 31  ? -24.564 122.092 4.004   1.00 40.72  ? 49  TYR D CD1  1 
ATOM   8650  C CD2  . TYR D 2 31  ? -26.120 123.685 3.223   1.00 41.91  ? 49  TYR D CD2  1 
ATOM   8651  C CE1  . TYR D 2 31  ? -25.414 121.085 3.667   1.00 42.85  ? 49  TYR D CE1  1 
ATOM   8652  C CE2  . TYR D 2 31  ? -26.980 122.676 2.869   1.00 42.69  ? 49  TYR D CE2  1 
ATOM   8653  C CZ   . TYR D 2 31  ? -26.607 121.378 3.100   1.00 45.71  ? 49  TYR D CZ   1 
ATOM   8654  O OH   . TYR D 2 31  ? -27.423 120.335 2.781   1.00 47.64  ? 49  TYR D OH   1 
ATOM   8655  N N    . LEU D 2 32  ? -24.087 126.654 2.150   1.00 41.73  ? 50  LEU D N    1 
ATOM   8656  C CA   . LEU D 2 32  ? -24.826 127.319 1.113   1.00 39.56  ? 50  LEU D CA   1 
ATOM   8657  C C    . LEU D 2 32  ? -23.950 127.605 -0.049  1.00 37.79  ? 50  LEU D C    1 
ATOM   8658  O O    . LEU D 2 32  ? -24.256 127.236 -1.141  1.00 44.51  ? 50  LEU D O    1 
ATOM   8659  C CB   . LEU D 2 32  ? -25.393 128.636 1.668   1.00 37.85  ? 50  LEU D CB   1 
ATOM   8660  C CG   . LEU D 2 32  ? -26.740 128.738 2.389   1.00 33.51  ? 50  LEU D CG   1 
ATOM   8661  C CD1  . LEU D 2 32  ? -27.047 127.552 3.283   1.00 30.75  ? 50  LEU D CD1  1 
ATOM   8662  C CD2  . LEU D 2 32  ? -26.846 130.036 3.163   1.00 22.70  ? 50  LEU D CD2  1 
ATOM   8663  N N    . GLU D 2 33  ? -22.791 128.154 0.191   1.00 31.58  ? 51  GLU D N    1 
ATOM   8664  C CA   . GLU D 2 33  ? -21.938 128.563 -0.893  1.00 37.36  ? 51  GLU D CA   1 
ATOM   8665  C C    . GLU D 2 33  ? -21.527 127.387 -1.696  1.00 41.60  ? 51  GLU D C    1 
ATOM   8666  O O    . GLU D 2 33  ? -21.487 127.462 -2.901  1.00 43.98  ? 51  GLU D O    1 
ATOM   8667  C CB   . GLU D 2 33  ? -20.707 129.234 -0.310  1.00 41.95  ? 51  GLU D CB   1 
ATOM   8668  C CG   . GLU D 2 33  ? -20.143 130.417 -1.064  1.00 45.14  ? 51  GLU D CG   1 
ATOM   8669  C CD   . GLU D 2 33  ? -19.068 131.119 -0.261  1.00 37.37  ? 51  GLU D CD   1 
ATOM   8670  O OE1  . GLU D 2 33  ? -18.965 130.841 0.946   1.00 36.34  ? 51  GLU D OE1  1 
ATOM   8671  O OE2  . GLU D 2 33  ? -18.323 131.938 -0.831  1.00 30.75  ? 51  GLU D OE2  1 
ATOM   8672  N N    . LYS D 2 34  ? -21.234 126.281 -1.042  1.00 42.60  ? 52  LYS D N    1 
ATOM   8673  C CA   . LYS D 2 34  ? -20.757 125.097 -1.721  1.00 38.34  ? 52  LYS D CA   1 
ATOM   8674  C C    . LYS D 2 34  ? -21.872 124.283 -2.223  1.00 39.01  ? 52  LYS D C    1 
ATOM   8675  O O    . LYS D 2 34  ? -21.656 123.209 -2.746  1.00 51.03  ? 52  LYS D O    1 
ATOM   8676  C CB   . LYS D 2 34  ? -19.891 124.258 -0.822  1.00 39.13  ? 52  LYS D CB   1 
ATOM   8677  C CG   . LYS D 2 34  ? -18.517 124.862 -0.579  1.00 40.89  ? 52  LYS D CG   1 
ATOM   8678  C CD   . LYS D 2 34  ? -17.552 123.855 0.024   1.00 37.06  ? 52  LYS D CD   1 
ATOM   8679  C CE   . LYS D 2 34  ? -16.133 124.395 0.010   1.00 32.91  ? 52  LYS D CE   1 
ATOM   8680  N NZ   . LYS D 2 34  ? -15.114 123.371 0.363   1.00 22.60  ? 52  LYS D NZ   1 
ATOM   8681  N N    . SER D 2 35  ? -23.085 124.743 -2.015  1.00 39.51  ? 53  SER D N    1 
ATOM   8682  C CA   . SER D 2 35  ? -24.205 124.060 -2.592  1.00 43.38  ? 53  SER D CA   1 
ATOM   8683  C C    . SER D 2 35  ? -24.967 124.938 -3.567  1.00 39.80  ? 53  SER D C    1 
ATOM   8684  O O    . SER D 2 35  ? -25.674 124.440 -4.420  1.00 42.74  ? 53  SER D O    1 
ATOM   8685  C CB   . SER D 2 35  ? -25.107 123.583 -1.472  1.00 45.50  ? 53  SER D CB   1 
ATOM   8686  O OG   . SER D 2 35  ? -24.407 122.749 -0.565  1.00 38.35  ? 53  SER D OG   1 
ATOM   8687  N N    . LEU D 2 36  ? -24.820 126.245 -3.450  1.00 36.79  ? 54  LEU D N    1 
ATOM   8688  C CA   . LEU D 2 36  ? -25.525 127.173 -4.318  1.00 38.15  ? 54  LEU D CA   1 
ATOM   8689  C C    . LEU D 2 36  ? -24.717 127.350 -5.552  1.00 42.97  ? 54  LEU D C    1 
ATOM   8690  O O    . LEU D 2 36  ? -25.265 127.421 -6.649  1.00 50.31  ? 54  LEU D O    1 
ATOM   8691  C CB   . LEU D 2 36  ? -25.679 128.540 -3.666  1.00 32.80  ? 54  LEU D CB   1 
ATOM   8692  C CG   . LEU D 2 36  ? -26.579 128.702 -2.456  1.00 42.62  ? 54  LEU D CG   1 
ATOM   8693  C CD1  . LEU D 2 36  ? -26.488 130.130 -1.972  1.00 52.22  ? 54  LEU D CD1  1 
ATOM   8694  C CD2  . LEU D 2 36  ? -28.013 128.299 -2.725  1.00 42.51  ? 54  LEU D CD2  1 
ATOM   8695  N N    . GLY D 2 37  ? -23.411 127.460 -5.388  1.00 41.05  ? 55  GLY D N    1 
ATOM   8696  C CA   . GLY D 2 37  ? -22.514 127.607 -6.515  1.00 35.49  ? 55  GLY D CA   1 
ATOM   8697  C C    . GLY D 2 37  ? -21.062 127.742 -6.122  1.00 38.82  ? 55  GLY D C    1 
ATOM   8698  O O    . GLY D 2 37  ? -20.323 126.760 -6.019  1.00 35.52  ? 55  GLY D O    1 
ATOM   8699  N N    . LYS D 2 40  ? -24.360 133.090 -7.867  1.00 36.47  ? 58  LYS D N    1 
ATOM   8700  C CA   . LYS D 2 40  ? -25.399 133.702 -8.684  1.00 49.30  ? 58  LYS D CA   1 
ATOM   8701  C C    . LYS D 2 40  ? -25.821 135.071 -8.182  1.00 45.20  ? 58  LYS D C    1 
ATOM   8702  O O    . LYS D 2 40  ? -25.005 135.979 -8.087  1.00 42.35  ? 58  LYS D O    1 
ATOM   8703  C CB   . LYS D 2 40  ? -26.603 132.776 -8.707  1.00 56.36  ? 58  LYS D CB   1 
ATOM   8704  C CG   . LYS D 2 40  ? -27.328 132.685 -10.036 1.00 79.56  ? 58  LYS D CG   1 
ATOM   8705  C CD   . LYS D 2 40  ? -28.455 131.670 -9.958  1.00 82.86  ? 58  LYS D CD   1 
ATOM   8706  C CE   . LYS D 2 40  ? -29.502 132.077 -8.936  1.00 67.24  ? 58  LYS D CE   1 
ATOM   8707  N NZ   . LYS D 2 40  ? -30.494 130.990 -8.705  1.00 59.16  ? 58  LYS D NZ   1 
ATOM   8708  N N    . GLU D 2 41  ? -27.092 135.230 -7.861  1.00 45.45  ? 59  GLU D N    1 
ATOM   8709  C CA   . GLU D 2 41  ? -27.571 136.479 -7.288  1.00 57.39  ? 59  GLU D CA   1 
ATOM   8710  C C    . GLU D 2 41  ? -27.129 136.588 -5.848  1.00 55.59  ? 59  GLU D C    1 
ATOM   8711  O O    . GLU D 2 41  ? -27.285 137.623 -5.208  1.00 44.24  ? 59  GLU D O    1 
ATOM   8712  C CB   . GLU D 2 41  ? -29.087 136.549 -7.359  1.00 52.89  ? 59  GLU D CB   1 
ATOM   8713  C CG   . GLU D 2 41  ? -29.625 137.963 -7.509  1.00 55.47  ? 59  GLU D CG   1 
ATOM   8714  C CD   . GLU D 2 41  ? -30.983 138.010 -8.172  1.00 57.85  ? 59  GLU D CD   1 
ATOM   8715  O OE1  . GLU D 2 41  ? -31.935 137.408 -7.641  1.00 57.08  ? 59  GLU D OE1  1 
ATOM   8716  O OE2  . GLU D 2 41  ? -31.094 138.647 -9.236  1.00 53.94  ? 59  GLU D OE2  1 
ATOM   8717  N N    . PHE D 2 42  ? -26.593 135.503 -5.327  1.00 52.13  ? 60  PHE D N    1 
ATOM   8718  C CA   . PHE D 2 42  ? -26.185 135.470 -3.952  1.00 48.20  ? 60  PHE D CA   1 
ATOM   8719  C C    . PHE D 2 42  ? -24.831 135.993 -3.619  1.00 46.22  ? 60  PHE D C    1 
ATOM   8720  O O    . PHE D 2 42  ? -23.995 135.226 -3.212  1.00 57.43  ? 60  PHE D O    1 
ATOM   8721  C CB   . PHE D 2 42  ? -26.169 134.018 -3.540  1.00 47.17  ? 60  PHE D CB   1 
ATOM   8722  C CG   . PHE D 2 42  ? -27.239 133.195 -4.184  1.00 52.79  ? 60  PHE D CG   1 
ATOM   8723  C CD1  . PHE D 2 42  ? -28.572 133.506 -4.005  1.00 59.42  ? 60  PHE D CD1  1 
ATOM   8724  C CD2  . PHE D 2 42  ? -26.913 132.103 -4.947  1.00 54.14  ? 60  PHE D CD2  1 
ATOM   8725  C CE1  . PHE D 2 42  ? -29.558 132.746 -4.587  1.00 58.83  ? 60  PHE D CE1  1 
ATOM   8726  C CE2  . PHE D 2 42  ? -27.893 131.337 -5.531  1.00 65.28  ? 60  PHE D CE2  1 
ATOM   8727  C CZ   . PHE D 2 42  ? -29.216 131.658 -5.352  1.00 66.72  ? 60  PHE D CZ   1 
ATOM   8728  N N    . SER D 2 43  ? -24.558 137.263 -3.818  1.00 37.66  ? 61  SER D N    1 
ATOM   8729  C CA   . SER D 2 43  ? -23.284 137.785 -3.333  1.00 47.08  ? 61  SER D CA   1 
ATOM   8730  C C    . SER D 2 43  ? -23.557 139.039 -2.573  1.00 47.77  ? 61  SER D C    1 
ATOM   8731  O O    . SER D 2 43  ? -22.689 139.894 -2.401  1.00 41.25  ? 61  SER D O    1 
ATOM   8732  C CB   . SER D 2 43  ? -22.194 137.923 -4.384  1.00 53.17  ? 61  SER D CB   1 
ATOM   8733  O OG   . SER D 2 43  ? -21.534 136.688 -4.598  1.00 50.68  ? 61  SER D OG   1 
ATOM   8734  N N    . GLY D 2 44  ? -24.804 139.178 -2.165  1.00 44.74  ? 62  GLY D N    1 
ATOM   8735  C CA   . GLY D 2 44  ? -25.167 140.301 -1.353  1.00 36.79  ? 62  GLY D CA   1 
ATOM   8736  C C    . GLY D 2 44  ? -25.601 139.607 -0.109  1.00 41.63  ? 62  GLY D C    1 
ATOM   8737  O O    . GLY D 2 44  ? -25.926 140.244 0.879   1.00 51.46  ? 62  GLY D O    1 
ATOM   8738  N N    . PHE D 2 45  ? -25.656 138.292 -0.148  1.00 35.99  ? 63  PHE D N    1 
ATOM   8739  C CA   . PHE D 2 45  ? -25.940 137.603 1.077   1.00 40.63  ? 63  PHE D CA   1 
ATOM   8740  C C    . PHE D 2 45  ? -24.635 137.463 1.744   1.00 38.41  ? 63  PHE D C    1 
ATOM   8741  O O    . PHE D 2 45  ? -24.414 137.958 2.821   1.00 39.78  ? 63  PHE D O    1 
ATOM   8742  C CB   . PHE D 2 45  ? -26.425 136.197 0.767   1.00 35.61  ? 63  PHE D CB   1 
ATOM   8743  C CG   . PHE D 2 45  ? -26.766 135.391 1.972   1.00 27.69  ? 63  PHE D CG   1 
ATOM   8744  C CD1  . PHE D 2 45  ? -27.840 135.722 2.757   1.00 39.18  ? 63  PHE D CD1  1 
ATOM   8745  C CD2  . PHE D 2 45  ? -26.027 134.284 2.300   1.00 31.24  ? 63  PHE D CD2  1 
ATOM   8746  C CE1  . PHE D 2 45  ? -28.160 134.970 3.862   1.00 48.41  ? 63  PHE D CE1  1 
ATOM   8747  C CE2  . PHE D 2 45  ? -26.335 133.529 3.403   1.00 39.90  ? 63  PHE D CE2  1 
ATOM   8748  C CZ   . PHE D 2 45  ? -27.405 133.871 4.184   1.00 43.70  ? 63  PHE D CZ   1 
ATOM   8749  N N    . PHE D 2 46  ? -23.722 136.859 1.040   1.00 36.43  ? 64  PHE D N    1 
ATOM   8750  C CA   . PHE D 2 46  ? -22.463 136.580 1.621   1.00 34.36  ? 64  PHE D CA   1 
ATOM   8751  C C    . PHE D 2 46  ? -21.670 137.794 1.972   1.00 42.09  ? 64  PHE D C    1 
ATOM   8752  O O    . PHE D 2 46  ? -21.066 137.813 3.020   1.00 58.67  ? 64  PHE D O    1 
ATOM   8753  C CB   . PHE D 2 46  ? -21.682 135.652 0.714   1.00 34.26  ? 64  PHE D CB   1 
ATOM   8754  C CG   . PHE D 2 46  ? -22.338 134.326 0.499   1.00 35.93  ? 64  PHE D CG   1 
ATOM   8755  C CD1  . PHE D 2 46  ? -22.652 133.520 1.566   1.00 35.67  ? 64  PHE D CD1  1 
ATOM   8756  C CD2  . PHE D 2 46  ? -22.618 133.882 -0.771  1.00 38.23  ? 64  PHE D CD2  1 
ATOM   8757  C CE1  . PHE D 2 46  ? -23.251 132.297 1.368   1.00 39.09  ? 64  PHE D CE1  1 
ATOM   8758  C CE2  . PHE D 2 46  ? -23.221 132.661 -0.978  1.00 34.67  ? 64  PHE D CE2  1 
ATOM   8759  C CZ   . PHE D 2 46  ? -23.537 131.867 0.095   1.00 35.27  ? 64  PHE D CZ   1 
ATOM   8760  N N    . GLU D 2 47  ? -21.636 138.817 1.158   1.00 34.63  ? 65  GLU D N    1 
ATOM   8761  C CA   . GLU D 2 47  ? -20.894 139.978 1.574   1.00 43.27  ? 65  GLU D CA   1 
ATOM   8762  C C    . GLU D 2 47  ? -21.521 140.588 2.820   1.00 52.77  ? 65  GLU D C    1 
ATOM   8763  O O    . GLU D 2 47  ? -20.817 141.083 3.681   1.00 47.35  ? 65  GLU D O    1 
ATOM   8764  C CB   . GLU D 2 47  ? -20.753 140.976 0.435   1.00 43.28  ? 65  GLU D CB   1 
ATOM   8765  C CG   . GLU D 2 47  ? -19.543 141.885 0.528   1.00 52.14  ? 65  GLU D CG   1 
ATOM   8766  C CD   . GLU D 2 47  ? -18.293 141.272 -0.070  1.00 54.09  ? 65  GLU D CD   1 
ATOM   8767  O OE1  . GLU D 2 47  ? -18.406 140.263 -0.793  1.00 61.20  ? 65  GLU D OE1  1 
ATOM   8768  O OE2  . GLU D 2 47  ? -17.194 141.807 0.168   1.00 54.66  ? 65  GLU D OE2  1 
ATOM   8769  N N    . ASP D 2 48  ? -22.840 140.628 2.902   1.00 54.00  ? 66  ASP D N    1 
ATOM   8770  C CA   . ASP D 2 48  ? -23.511 141.101 4.108   1.00 46.90  ? 66  ASP D CA   1 
ATOM   8771  C C    . ASP D 2 48  ? -23.381 140.204 5.315   1.00 44.20  ? 66  ASP D C    1 
ATOM   8772  O O    . ASP D 2 48  ? -23.266 140.717 6.403   1.00 50.29  ? 66  ASP D O    1 
ATOM   8773  C CB   . ASP D 2 48  ? -24.968 141.440 3.864   1.00 51.57  ? 66  ASP D CB   1 
ATOM   8774  C CG   . ASP D 2 48  ? -25.151 142.763 3.140   1.00 56.27  ? 66  ASP D CG   1 
ATOM   8775  O OD1  . ASP D 2 48  ? -24.612 142.924 2.028   1.00 53.18  ? 66  ASP D OD1  1 
ATOM   8776  O OD2  . ASP D 2 48  ? -25.850 143.643 3.685   1.00 53.17  ? 66  ASP D OD2  1 
ATOM   8777  N N    . ILE D 2 49  ? -23.422 138.882 5.169   1.00 39.61  ? 67  ILE D N    1 
ATOM   8778  C CA   . ILE D 2 49  ? -23.196 138.007 6.333   1.00 38.44  ? 67  ILE D CA   1 
ATOM   8779  C C    . ILE D 2 49  ? -21.816 138.241 6.899   1.00 35.74  ? 67  ILE D C    1 
ATOM   8780  O O    . ILE D 2 49  ? -21.584 138.060 8.077   1.00 29.35  ? 67  ILE D O    1 
ATOM   8781  C CB   . ILE D 2 49  ? -23.504 136.533 6.056   1.00 31.22  ? 67  ILE D CB   1 
ATOM   8782  C CG1  . ILE D 2 49  ? -24.899 136.388 5.483   1.00 40.67  ? 67  ILE D CG1  1 
ATOM   8783  C CG2  . ILE D 2 49  ? -23.483 135.730 7.329   1.00 33.38  ? 67  ILE D CG2  1 
ATOM   8784  C CD1  . ILE D 2 49  ? -25.984 136.808 6.439   1.00 45.60  ? 67  ILE D CD1  1 
ATOM   8785  N N    . GLU D 2 50  ? -20.916 138.736 6.091   1.00 32.54  ? 68  GLU D N    1 
ATOM   8786  C CA   . GLU D 2 50  ? -19.614 139.058 6.603   1.00 37.13  ? 68  GLU D CA   1 
ATOM   8787  C C    . GLU D 2 50  ? -19.706 140.225 7.485   1.00 36.99  ? 68  GLU D C    1 
ATOM   8788  O O    . GLU D 2 50  ? -19.186 140.209 8.577   1.00 39.87  ? 68  GLU D O    1 
ATOM   8789  C CB   . GLU D 2 50  ? -18.653 139.399 5.480   1.00 42.96  ? 68  GLU D CB   1 
ATOM   8790  C CG   . GLU D 2 50  ? -18.202 138.220 4.639   1.00 40.21  ? 68  GLU D CG   1 
ATOM   8791  C CD   . GLU D 2 50  ? -17.239 138.631 3.554   1.00 38.64  ? 68  GLU D CD   1 
ATOM   8792  O OE1  . GLU D 2 50  ? -16.865 139.818 3.511   1.00 41.34  ? 68  GLU D OE1  1 
ATOM   8793  O OE2  . GLU D 2 50  ? -16.858 137.767 2.749   1.00 38.06  ? 68  GLU D OE2  1 
ATOM   8794  N N    . LYS D 2 51  ? -20.362 141.259 7.011   1.00 42.20  ? 69  LYS D N    1 
ATOM   8795  C CA   . LYS D 2 51  ? -20.532 142.468 7.802   1.00 46.50  ? 69  LYS D CA   1 
ATOM   8796  C C    . LYS D 2 51  ? -21.319 142.174 9.059   1.00 37.52  ? 69  LYS D C    1 
ATOM   8797  O O    . LYS D 2 51  ? -21.006 142.679 10.122  1.00 34.37  ? 69  LYS D O    1 
ATOM   8798  C CB   . LYS D 2 51  ? -21.219 143.534 6.964   1.00 39.85  ? 69  LYS D CB   1 
ATOM   8799  C CG   . LYS D 2 51  ? -20.648 143.708 5.571   1.00 45.17  ? 69  LYS D CG   1 
ATOM   8800  C CD   . LYS D 2 51  ? -21.584 144.527 4.699   1.00 56.34  ? 69  LYS D CD   1 
ATOM   8801  C CE   . LYS D 2 51  ? -21.144 144.523 3.244   1.00 52.93  ? 69  LYS D CE   1 
ATOM   8802  N NZ   . LYS D 2 51  ? -22.100 145.236 2.354   1.00 38.88  ? 69  LYS D NZ   1 
ATOM   8803  N N    . LEU D 2 52  ? -22.340 141.363 8.956   1.00 30.00  ? 70  LEU D N    1 
ATOM   8804  C CA   . LEU D 2 52  ? -23.046 140.968 10.136  1.00 30.86  ? 70  LEU D CA   1 
ATOM   8805  C C    . LEU D 2 52  ? -22.250 140.107 11.126  1.00 28.35  ? 70  LEU D C    1 
ATOM   8806  O O    . LEU D 2 52  ? -22.346 140.302 12.313  1.00 34.20  ? 70  LEU D O    1 
ATOM   8807  C CB   . LEU D 2 52  ? -24.347 140.309 9.734   1.00 32.62  ? 70  LEU D CB   1 
ATOM   8808  C CG   . LEU D 2 52  ? -25.268 141.141 8.865   1.00 32.84  ? 70  LEU D CG   1 
ATOM   8809  C CD1  . LEU D 2 52  ? -26.527 140.331 8.688   1.00 39.80  ? 70  LEU D CD1  1 
ATOM   8810  C CD2  . LEU D 2 52  ? -25.583 142.476 9.506   1.00 28.76  ? 70  LEU D CD2  1 
ATOM   8811  N N    . TYR D 2 53  ? -21.474 139.153 10.665  1.00 24.72  ? 71  TYR D N    1 
ATOM   8812  C CA   . TYR D 2 53  ? -20.652 138.349 11.573  1.00 28.84  ? 71  TYR D CA   1 
ATOM   8813  C C    . TYR D 2 53  ? -19.593 139.169 12.262  1.00 27.99  ? 71  TYR D C    1 
ATOM   8814  O O    . TYR D 2 53  ? -19.248 138.939 13.408  1.00 24.45  ? 71  TYR D O    1 
ATOM   8815  C CB   . TYR D 2 53  ? -20.010 137.160 10.851  1.00 32.62  ? 71  TYR D CB   1 
ATOM   8816  C CG   . TYR D 2 53  ? -19.150 136.255 11.703  1.00 27.96  ? 71  TYR D CG   1 
ATOM   8817  C CD1  . TYR D 2 53  ? -19.719 135.288 12.510  1.00 24.59  ? 71  TYR D CD1  1 
ATOM   8818  C CD2  . TYR D 2 53  ? -17.771 136.352 11.679  1.00 26.60  ? 71  TYR D CD2  1 
ATOM   8819  C CE1  . TYR D 2 53  ? -18.940 134.463 13.290  1.00 21.99  ? 71  TYR D CE1  1 
ATOM   8820  C CE2  . TYR D 2 53  ? -16.990 135.528 12.457  1.00 28.27  ? 71  TYR D CE2  1 
ATOM   8821  C CZ   . TYR D 2 53  ? -17.580 134.588 13.260  1.00 21.12  ? 71  TYR D CZ   1 
ATOM   8822  O OH   . TYR D 2 53  ? -16.799 133.770 14.029  1.00 12.32  ? 71  TYR D OH   1 
ATOM   8823  N N    . PHE D 2 54  ? -19.035 140.101 11.541  1.00 25.01  ? 72  PHE D N    1 
ATOM   8824  C CA   . PHE D 2 54  ? -18.068 140.960 12.132  1.00 27.31  ? 72  PHE D CA   1 
ATOM   8825  C C    . PHE D 2 54  ? -18.640 141.828 13.224  1.00 28.36  ? 72  PHE D C    1 
ATOM   8826  O O    . PHE D 2 54  ? -17.969 142.088 14.197  1.00 36.06  ? 72  PHE D O    1 
ATOM   8827  C CB   . PHE D 2 54  ? -17.405 141.762 11.048  1.00 29.85  ? 72  PHE D CB   1 
ATOM   8828  C CG   . PHE D 2 54  ? -16.849 143.051 11.509  1.00 32.67  ? 72  PHE D CG   1 
ATOM   8829  C CD1  . PHE D 2 54  ? -15.636 143.095 12.146  1.00 20.80  ? 72  PHE D CD1  1 
ATOM   8830  C CD2  . PHE D 2 54  ? -17.541 144.221 11.289  1.00 43.62  ? 72  PHE D CD2  1 
ATOM   8831  C CE1  . PHE D 2 54  ? -15.128 144.285 12.570  1.00 22.20  ? 72  PHE D CE1  1 
ATOM   8832  C CE2  . PHE D 2 54  ? -17.038 145.417 11.715  1.00 43.69  ? 72  PHE D CE2  1 
ATOM   8833  C CZ   . PHE D 2 54  ? -15.823 145.447 12.342  1.00 33.68  ? 72  PHE D CZ   1 
ATOM   8834  N N    . LYS D 2 55  ? -19.870 142.284 13.076  1.00 27.16  ? 73  LYS D N    1 
ATOM   8835  C CA   . LYS D 2 55  ? -20.492 143.147 14.058  1.00 24.76  ? 73  LYS D CA   1 
ATOM   8836  C C    . LYS D 2 55  ? -21.078 142.372 15.179  1.00 26.54  ? 73  LYS D C    1 
ATOM   8837  O O    . LYS D 2 55  ? -21.672 142.942 16.063  1.00 30.31  ? 73  LYS D O    1 
ATOM   8838  C CB   . LYS D 2 55  ? -21.552 144.009 13.414  1.00 27.21  ? 73  LYS D CB   1 
ATOM   8839  C CG   . LYS D 2 55  ? -22.837 143.322 13.042  1.00 26.34  ? 73  LYS D CG   1 
ATOM   8840  C CD   . LYS D 2 55  ? -23.657 144.152 12.075  1.00 33.93  ? 73  LYS D CD   1 
ATOM   8841  C CE   . LYS D 2 55  ? -24.640 145.062 12.777  1.00 33.92  ? 73  LYS D CE   1 
ATOM   8842  N NZ   . LYS D 2 55  ? -25.573 145.669 11.790  1.00 35.52  ? 73  LYS D NZ   1 
ATOM   8843  N N    . GLN D 2 56  ? -20.948 141.075 15.135  1.00 23.58  ? 74  GLN D N    1 
ATOM   8844  C CA   . GLN D 2 56  ? -21.409 140.222 16.180  1.00 19.92  ? 74  GLN D CA   1 
ATOM   8845  C C    . GLN D 2 56  ? -22.859 140.331 16.283  1.00 26.20  ? 74  GLN D C    1 
ATOM   8846  O O    . GLN D 2 56  ? -23.399 140.246 17.365  1.00 42.05  ? 74  GLN D O    1 
ATOM   8847  C CB   . GLN D 2 56  ? -20.702 140.484 17.478  1.00 23.60  ? 74  GLN D CB   1 
ATOM   8848  C CG   . GLN D 2 56  ? -19.214 140.681 17.304  1.00 23.40  ? 74  GLN D CG   1 
ATOM   8849  C CD   . GLN D 2 56  ? -18.437 140.544 18.573  1.00 23.03  ? 74  GLN D CD   1 
ATOM   8850  O OE1  . GLN D 2 56  ? -18.920 140.002 19.552  1.00 27.83  ? 74  GLN D OE1  1 
ATOM   8851  N NE2  . GLN D 2 56  ? -17.214 141.024 18.559  1.00 27.10  ? 74  GLN D NE2  1 
ATOM   8852  N N    . ASN D 2 57  ? -23.521 140.535 15.161  1.00 29.00  ? 75  ASN D N    1 
ATOM   8853  C CA   . ASN D 2 57  ? -24.981 140.547 15.140  1.00 30.24  ? 75  ASN D CA   1 
ATOM   8854  C C    . ASN D 2 57  ? -25.357 139.237 14.601  1.00 24.33  ? 75  ASN D C    1 
ATOM   8855  O O    . ASN D 2 57  ? -25.848 139.131 13.501  1.00 29.75  ? 75  ASN D O    1 
ATOM   8856  C CB   . ASN D 2 57  ? -25.531 141.660 14.285  1.00 34.29  ? 75  ASN D CB   1 
ATOM   8857  C CG   . ASN D 2 57  ? -25.996 142.841 15.107  1.00 47.39  ? 75  ASN D CG   1 
ATOM   8858  O OD1  . ASN D 2 57  ? -25.220 143.427 15.857  1.00 53.79  ? 75  ASN D OD1  1 
ATOM   8859  N ND2  . ASN D 2 57  ? -27.266 143.195 14.972  1.00 47.62  ? 75  ASN D ND2  1 
ATOM   8860  N N    . TYR D 2 58  ? -25.140 138.226 15.395  1.00 18.45  ? 76  TYR D N    1 
ATOM   8861  C CA   . TYR D 2 58  ? -25.338 136.894 14.926  1.00 27.23  ? 76  TYR D CA   1 
ATOM   8862  C C    . TYR D 2 58  ? -26.718 136.467 14.518  1.00 33.80  ? 76  TYR D C    1 
ATOM   8863  O O    . TYR D 2 58  ? -26.837 135.706 13.585  1.00 34.59  ? 76  TYR D O    1 
ATOM   8864  C CB   . TYR D 2 58  ? -24.756 135.890 15.919  1.00 29.80  ? 76  TYR D CB   1 
ATOM   8865  C CG   . TYR D 2 58  ? -23.258 135.943 16.185  1.00 30.47  ? 76  TYR D CG   1 
ATOM   8866  C CD1  . TYR D 2 58  ? -22.375 136.541 15.306  1.00 29.66  ? 76  TYR D CD1  1 
ATOM   8867  C CD2  . TYR D 2 58  ? -22.733 135.361 17.323  1.00 31.89  ? 76  TYR D CD2  1 
ATOM   8868  C CE1  . TYR D 2 58  ? -21.017 136.573 15.573  1.00 33.39  ? 76  TYR D CE1  1 
ATOM   8869  C CE2  . TYR D 2 58  ? -21.383 135.374 17.588  1.00 24.39  ? 76  TYR D CE2  1 
ATOM   8870  C CZ   . TYR D 2 58  ? -20.530 135.984 16.717  1.00 25.42  ? 76  TYR D CZ   1 
ATOM   8871  O OH   . TYR D 2 58  ? -19.194 135.993 17.007  1.00 21.65  ? 76  TYR D OH   1 
ATOM   8872  N N    . LYS D 2 59  ? -27.769 136.858 15.213  1.00 35.22  ? 77  LYS D N    1 
ATOM   8873  C CA   . LYS D 2 59  ? -29.085 136.359 14.809  1.00 33.70  ? 77  LYS D CA   1 
ATOM   8874  C C    . LYS D 2 59  ? -29.716 137.239 13.774  1.00 37.63  ? 77  LYS D C    1 
ATOM   8875  O O    . LYS D 2 59  ? -30.664 136.828 13.149  1.00 40.58  ? 77  LYS D O    1 
ATOM   8876  C CB   . LYS D 2 59  ? -30.029 136.088 15.980  1.00 36.03  ? 77  LYS D CB   1 
ATOM   8877  C CG   . LYS D 2 59  ? -29.627 134.946 16.888  1.00 34.68  ? 77  LYS D CG   1 
ATOM   8878  C CD   . LYS D 2 59  ? -30.851 134.144 17.284  1.00 38.49  ? 77  LYS D CD   1 
ATOM   8879  C CE   . LYS D 2 59  ? -30.543 133.150 18.387  1.00 43.19  ? 77  LYS D CE   1 
ATOM   8880  N NZ   . LYS D 2 59  ? -30.172 133.850 19.647  1.00 41.64  ? 77  LYS D NZ   1 
ATOM   8881  N N    . GLU D 2 60  ? -29.216 138.455 13.581  1.00 37.79  ? 78  GLU D N    1 
ATOM   8882  C CA   . GLU D 2 60  ? -29.704 139.272 12.481  1.00 39.66  ? 78  GLU D CA   1 
ATOM   8883  C C    . GLU D 2 60  ? -29.272 138.493 11.287  1.00 40.49  ? 78  GLU D C    1 
ATOM   8884  O O    . GLU D 2 60  ? -29.982 138.417 10.303  1.00 40.98  ? 78  GLU D O    1 
ATOM   8885  C CB   . GLU D 2 60  ? -29.089 140.652 12.459  1.00 36.34  ? 78  GLU D CB   1 
ATOM   8886  C CG   . GLU D 2 60  ? -29.643 141.539 11.356  1.00 43.80  ? 78  GLU D CG   1 
ATOM   8887  C CD   . GLU D 2 60  ? -29.079 142.941 11.382  1.00 46.45  ? 78  GLU D CD   1 
ATOM   8888  O OE1  . GLU D 2 60  ? -28.590 143.360 12.444  1.00 49.70  ? 78  GLU D OE1  1 
ATOM   8889  O OE2  . GLU D 2 60  ? -29.135 143.628 10.344  1.00 39.96  ? 78  GLU D OE2  1 
ATOM   8890  N N    . ALA D 2 61  ? -28.072 137.955 11.336  1.00 36.36  ? 79  ALA D N    1 
ATOM   8891  C CA   . ALA D 2 61  ? -27.612 137.070 10.288  1.00 35.71  ? 79  ALA D CA   1 
ATOM   8892  C C    . ALA D 2 61  ? -28.341 135.730 10.219  1.00 34.26  ? 79  ALA D C    1 
ATOM   8893  O O    . ALA D 2 61  ? -28.586 135.225 9.158   1.00 45.01  ? 79  ALA D O    1 
ATOM   8894  C CB   . ALA D 2 61  ? -26.131 136.856 10.409  1.00 31.99  ? 79  ALA D CB   1 
ATOM   8895  N N    . ILE D 2 62  ? -28.659 135.131 11.336  1.00 29.84  ? 80  ILE D N    1 
ATOM   8896  C CA   . ILE D 2 62  ? -29.319 133.853 11.308  1.00 32.40  ? 80  ILE D CA   1 
ATOM   8897  C C    . ILE D 2 62  ? -30.681 133.931 10.708  1.00 35.69  ? 80  ILE D C    1 
ATOM   8898  O O    . ILE D 2 62  ? -31.175 132.965 10.159  1.00 42.39  ? 80  ILE D O    1 
ATOM   8899  C CB   . ILE D 2 62  ? -29.325 133.167 12.685  1.00 37.65  ? 80  ILE D CB   1 
ATOM   8900  C CG1  . ILE D 2 62  ? -27.895 132.809 13.092  1.00 31.53  ? 80  ILE D CG1  1 
ATOM   8901  C CG2  . ILE D 2 62  ? -30.146 131.894 12.706  1.00 33.39  ? 80  ILE D CG2  1 
ATOM   8902  C CD1  . ILE D 2 62  ? -27.733 132.461 14.554  1.00 31.51  ? 80  ILE D CD1  1 
ATOM   8903  N N    . GLU D 2 63  ? -31.323 135.075 10.841  1.00 39.38  ? 81  GLU D N    1 
ATOM   8904  C CA   . GLU D 2 63  ? -32.652 135.272 10.262  1.00 49.16  ? 81  GLU D CA   1 
ATOM   8905  C C    . GLU D 2 63  ? -32.579 135.311 8.776   1.00 48.01  ? 81  GLU D C    1 
ATOM   8906  O O    . GLU D 2 63  ? -33.499 134.906 8.086   1.00 46.59  ? 81  GLU D O    1 
ATOM   8907  C CB   . GLU D 2 63  ? -33.248 136.592 10.703  1.00 51.41  ? 81  GLU D CB   1 
ATOM   8908  C CG   . GLU D 2 63  ? -33.542 136.677 12.197  1.00 62.74  ? 81  GLU D CG   1 
ATOM   8909  C CD   . GLU D 2 63  ? -34.490 135.603 12.705  1.00 72.20  ? 81  GLU D CD   1 
ATOM   8910  O OE1  . GLU D 2 63  ? -35.470 135.285 11.994  1.00 79.78  ? 81  GLU D OE1  1 
ATOM   8911  O OE2  . GLU D 2 63  ? -34.244 135.049 13.799  1.00 57.55  ? 81  GLU D OE2  1 
ATOM   8912  N N    . LYS D 2 64  ? -31.473 135.818 8.273   1.00 41.68  ? 82  LYS D N    1 
ATOM   8913  C CA   . LYS D 2 64  ? -31.241 135.766 6.857   1.00 40.58  ? 82  LYS D CA   1 
ATOM   8914  C C    . LYS D 2 64  ? -31.033 134.324 6.405   1.00 39.48  ? 82  LYS D C    1 
ATOM   8915  O O    . LYS D 2 64  ? -31.615 133.910 5.437   1.00 49.83  ? 82  LYS D O    1 
ATOM   8916  C CB   . LYS D 2 64  ? -30.104 136.655 6.416   1.00 34.20  ? 82  LYS D CB   1 
ATOM   8917  C CG   . LYS D 2 64  ? -30.284 138.101 6.844   1.00 33.08  ? 82  LYS D CG   1 
ATOM   8918  C CD   . LYS D 2 64  ? -29.151 138.973 6.339   1.00 34.38  ? 82  LYS D CD   1 
ATOM   8919  C CE   . LYS D 2 64  ? -29.427 140.440 6.602   1.00 33.08  ? 82  LYS D CE   1 
ATOM   8920  N NZ   . LYS D 2 64  ? -28.347 141.311 6.068   1.00 34.43  ? 82  LYS D NZ   1 
ATOM   8921  N N    . ILE D 2 65  ? -30.230 133.557 7.105   1.00 35.52  ? 83  ILE D N    1 
ATOM   8922  C CA   . ILE D 2 65  ? -29.963 132.185 6.723   1.00 38.94  ? 83  ILE D CA   1 
ATOM   8923  C C    . ILE D 2 65  ? -31.168 131.343 6.802   1.00 39.52  ? 83  ILE D C    1 
ATOM   8924  O O    . ILE D 2 65  ? -31.439 130.568 5.916   1.00 43.14  ? 83  ILE D O    1 
ATOM   8925  C CB   . ILE D 2 65  ? -28.899 131.524 7.622   1.00 42.51  ? 83  ILE D CB   1 
ATOM   8926  C CG1  . ILE D 2 65  ? -27.613 132.349 7.622   1.00 44.42  ? 83  ILE D CG1  1 
ATOM   8927  C CG2  . ILE D 2 65  ? -28.590 130.111 7.174   1.00 39.51  ? 83  ILE D CG2  1 
ATOM   8928  C CD1  . ILE D 2 65  ? -26.623 131.922 8.676   1.00 40.33  ? 83  ILE D CD1  1 
ATOM   8929  N N    . LEU D 2 66  ? -31.912 131.480 7.871   1.00 42.51  ? 84  LEU D N    1 
ATOM   8930  C CA   . LEU D 2 66  ? -33.065 130.619 8.046   1.00 50.28  ? 84  LEU D CA   1 
ATOM   8931  C C    . LEU D 2 66  ? -34.104 130.894 6.964   1.00 50.32  ? 84  LEU D C    1 
ATOM   8932  O O    . LEU D 2 66  ? -34.752 129.978 6.496   1.00 47.14  ? 84  LEU D O    1 
ATOM   8933  C CB   . LEU D 2 66  ? -33.589 130.720 9.469   1.00 45.67  ? 84  LEU D CB   1 
ATOM   8934  C CG   . LEU D 2 66  ? -32.752 130.065 10.555  1.00 45.92  ? 84  LEU D CG   1 
ATOM   8935  C CD1  . LEU D 2 66  ? -33.391 130.370 11.895  1.00 58.77  ? 84  LEU D CD1  1 
ATOM   8936  C CD2  . LEU D 2 66  ? -32.693 128.567 10.331  1.00 43.93  ? 84  LEU D CD2  1 
ATOM   8937  N N    . ASP D 2 67  ? -34.310 132.156 6.619   1.00 48.34  ? 85  ASP D N    1 
ATOM   8938  C CA   . ASP D 2 67  ? -35.196 132.520 5.517   1.00 50.31  ? 85  ASP D CA   1 
ATOM   8939  C C    . ASP D 2 67  ? -34.659 132.166 4.156   1.00 45.27  ? 85  ASP D C    1 
ATOM   8940  O O    . ASP D 2 67  ? -35.401 131.758 3.302   1.00 47.93  ? 85  ASP D O    1 
ATOM   8941  C CB   . ASP D 2 67  ? -35.469 134.016 5.551   1.00 56.51  ? 85  ASP D CB   1 
ATOM   8942  C CG   . ASP D 2 67  ? -36.909 134.358 5.218   1.00 62.25  ? 85  ASP D CG   1 
ATOM   8943  O OD1  . ASP D 2 67  ? -37.700 133.432 4.945   1.00 58.34  ? 85  ASP D OD1  1 
ATOM   8944  O OD2  . ASP D 2 67  ? -37.250 135.560 5.233   1.00 57.93  ? 85  ASP D OD2  1 
ATOM   8945  N N    . PHE D 2 68  ? -33.372 132.355 3.933   1.00 41.81  ? 86  PHE D N    1 
ATOM   8946  C CA   . PHE D 2 68  ? -32.767 132.082 2.648   1.00 47.37  ? 86  PHE D CA   1 
ATOM   8947  C C    . PHE D 2 68  ? -33.009 130.650 2.454   1.00 45.56  ? 86  PHE D C    1 
ATOM   8948  O O    . PHE D 2 68  ? -33.369 130.218 1.388   1.00 50.49  ? 86  PHE D O    1 
ATOM   8949  C CB   . PHE D 2 68  ? -31.258 132.252 2.756   1.00 41.03  ? 86  PHE D CB   1 
ATOM   8950  C CG   . PHE D 2 68  ? -30.578 132.678 1.503   1.00 38.46  ? 86  PHE D CG   1 
ATOM   8951  C CD1  . PHE D 2 68  ? -30.866 133.894 0.930   1.00 44.87  ? 86  PHE D CD1  1 
ATOM   8952  C CD2  . PHE D 2 68  ? -29.606 131.888 0.939   1.00 36.47  ? 86  PHE D CD2  1 
ATOM   8953  C CE1  . PHE D 2 68  ? -30.224 134.300 -0.215  1.00 41.90  ? 86  PHE D CE1  1 
ATOM   8954  C CE2  . PHE D 2 68  ? -28.958 132.285 -0.201  1.00 38.84  ? 86  PHE D CE2  1 
ATOM   8955  C CZ   . PHE D 2 68  ? -29.265 133.493 -0.776  1.00 42.64  ? 86  PHE D CZ   1 
ATOM   8956  N N    . CYS D 2 69  ? -32.832 129.900 3.506   1.00 42.53  ? 87  CYS D N    1 
ATOM   8957  C CA   . CYS D 2 69  ? -33.017 128.498 3.410   1.00 45.34  ? 87  CYS D CA   1 
ATOM   8958  C C    . CYS D 2 69  ? -34.446 128.257 3.038   1.00 47.60  ? 87  CYS D C    1 
ATOM   8959  O O    . CYS D 2 69  ? -34.725 127.280 2.395   1.00 57.07  ? 87  CYS D O    1 
ATOM   8960  C CB   . CYS D 2 69  ? -32.604 127.828 4.703   1.00 54.29  ? 87  CYS D CB   1 
ATOM   8961  S SG   . CYS D 2 69  ? -30.812 127.655 4.902   1.00 53.92  ? 87  CYS D SG   1 
ATOM   8962  N N    . LYS D 2 70  ? -35.377 129.053 3.537   1.00 48.09  ? 88  LYS D N    1 
ATOM   8963  C CA   . LYS D 2 70  ? -36.774 128.958 3.092   1.00 49.59  ? 88  LYS D CA   1 
ATOM   8964  C C    . LYS D 2 70  ? -37.074 129.422 1.652   1.00 50.02  ? 88  LYS D C    1 
ATOM   8965  O O    . LYS D 2 70  ? -37.833 128.786 0.936   1.00 51.35  ? 88  LYS D O    1 
ATOM   8966  C CB   . LYS D 2 70  ? -37.673 129.722 4.057   1.00 49.14  ? 88  LYS D CB   1 
ATOM   8967  C CG   . LYS D 2 70  ? -37.706 129.189 5.475   1.00 51.82  ? 88  LYS D CG   1 
ATOM   8968  C CD   . LYS D 2 70  ? -38.328 130.219 6.407   1.00 54.91  ? 88  LYS D CD   1 
ATOM   8969  C CE   . LYS D 2 70  ? -37.963 129.970 7.861   1.00 55.13  ? 88  LYS D CE   1 
ATOM   8970  N NZ   . LYS D 2 70  ? -38.374 131.091 8.754   1.00 40.55  ? 88  LYS D NZ   1 
ATOM   8971  N N    . LYS D 2 71  ? -36.491 130.521 1.215   1.00 44.34  ? 89  LYS D N    1 
ATOM   8972  C CA   . LYS D 2 71  ? -36.764 131.053 -0.119  1.00 40.00  ? 89  LYS D CA   1 
ATOM   8973  C C    . LYS D 2 71  ? -36.078 130.237 -1.165  1.00 39.87  ? 89  LYS D C    1 
ATOM   8974  O O    . LYS D 2 71  ? -36.535 130.122 -2.297  1.00 43.16  ? 89  LYS D O    1 
ATOM   8975  C CB   . LYS D 2 71  ? -36.242 132.485 -0.203  1.00 30.80  ? 89  LYS D CB   1 
ATOM   8976  C CG   . LYS D 2 71  ? -36.810 133.356 -1.304  1.00 30.35  ? 89  LYS D CG   1 
ATOM   8977  C CD   . LYS D 2 71  ? -36.059 134.676 -1.344  1.00 31.41  ? 89  LYS D CD   1 
ATOM   8978  C CE   . LYS D 2 71  ? -36.694 135.677 -2.295  1.00 28.68  ? 89  LYS D CE   1 
ATOM   8979  N NZ   . LYS D 2 71  ? -37.995 136.195 -1.792  1.00 35.22  ? 89  LYS D NZ   1 
ATOM   8980  N N    . ASN D 2 72  ? -34.968 129.656 -0.797  1.00 42.57  ? 90  ASN D N    1 
ATOM   8981  C CA   . ASN D 2 72  ? -34.193 128.919 -1.751  1.00 47.71  ? 90  ASN D CA   1 
ATOM   8982  C C    . ASN D 2 72  ? -34.186 127.463 -1.373  1.00 45.50  ? 90  ASN D C    1 
ATOM   8983  O O    . ASN D 2 72  ? -33.205 126.774 -1.555  1.00 45.24  ? 90  ASN D O    1 
ATOM   8984  C CB   . ASN D 2 72  ? -32.777 129.480 -1.859  1.00 47.26  ? 90  ASN D CB   1 
ATOM   8985  C CG   . ASN D 2 72  ? -32.745 130.933 -2.295  1.00 45.35  ? 90  ASN D CG   1 
ATOM   8986  O OD1  . ASN D 2 72  ? -32.511 131.236 -3.459  1.00 40.46  ? 90  ASN D OD1  1 
ATOM   8987  N ND2  . ASN D 2 72  ? -32.962 131.839 -1.357  1.00 45.20  ? 90  ASN D ND2  1 
ATOM   8988  N N    . GLU D 2 73  ? -35.282 127.003 -0.808  1.00 34.60  ? 91  GLU D N    1 
ATOM   8989  C CA   . GLU D 2 73  ? -35.423 125.600 -0.502  1.00 36.43  ? 91  GLU D CA   1 
ATOM   8990  C C    . GLU D 2 73  ? -35.552 124.774 -1.756  1.00 47.17  ? 91  GLU D C    1 
ATOM   8991  O O    . GLU D 2 73  ? -35.391 123.556 -1.712  1.00 50.26  ? 91  GLU D O    1 
ATOM   8992  C CB   . GLU D 2 73  ? -36.644 125.369 0.353   1.00 42.94  ? 91  GLU D CB   1 
ATOM   8993  C CG   . GLU D 2 73  ? -36.546 125.950 1.751   1.00 56.35  ? 91  GLU D CG   1 
ATOM   8994  C CD   . GLU D 2 73  ? -37.822 125.754 2.540   1.00 57.45  ? 91  GLU D CD   1 
ATOM   8995  O OE1  . GLU D 2 73  ? -38.837 125.340 1.946   1.00 71.39  ? 91  GLU D OE1  1 
ATOM   8996  O OE2  . GLU D 2 73  ? -37.801 125.993 3.760   1.00 48.78  ? 91  GLU D OE2  1 
ATOM   8997  N N    . SER D 2 74  ? -35.884 125.409 -2.877  1.00 49.77  ? 92  SER D N    1 
ATOM   8998  C CA   . SER D 2 74  ? -35.915 124.694 -4.139  1.00 49.28  ? 92  SER D CA   1 
ATOM   8999  C C    . SER D 2 74  ? -34.507 124.262 -4.377  1.00 50.13  ? 92  SER D C    1 
ATOM   9000  O O    . SER D 2 74  ? -34.251 123.092 -4.646  1.00 44.76  ? 92  SER D O    1 
ATOM   9001  C CB   . SER D 2 74  ? -36.269 125.647 -5.260  1.00 46.69  ? 92  SER D CB   1 
ATOM   9002  O OG   . SER D 2 74  ? -35.660 126.909 -5.086  1.00 45.71  ? 92  SER D OG   1 
ATOM   9003  N N    . LEU D 2 75  ? -33.580 125.192 -4.243  1.00 51.12  ? 93  LEU D N    1 
ATOM   9004  C CA   . LEU D 2 75  ? -32.167 124.902 -4.375  1.00 41.74  ? 93  LEU D CA   1 
ATOM   9005  C C    . LEU D 2 75  ? -31.604 124.063 -3.247  1.00 42.33  ? 93  LEU D C    1 
ATOM   9006  O O    . LEU D 2 75  ? -30.734 123.243 -3.482  1.00 47.63  ? 93  LEU D O    1 
ATOM   9007  C CB   . LEU D 2 75  ? -31.435 126.233 -4.439  1.00 42.54  ? 93  LEU D CB   1 
ATOM   9008  C CG   . LEU D 2 75  ? -31.799 127.213 -5.539  1.00 47.20  ? 93  LEU D CG   1 
ATOM   9009  C CD1  . LEU D 2 75  ? -31.047 128.505 -5.295  1.00 44.67  ? 93  LEU D CD1  1 
ATOM   9010  C CD2  . LEU D 2 75  ? -31.421 126.624 -6.885  1.00 54.37  ? 93  LEU D CD2  1 
ATOM   9011  N N    . LEU D 2 76  ? -32.056 124.292 -2.019  1.00 39.88  ? 94  LEU D N    1 
ATOM   9012  C CA   . LEU D 2 76  ? -31.512 123.610 -0.846  1.00 38.85  ? 94  LEU D CA   1 
ATOM   9013  C C    . LEU D 2 76  ? -31.741 122.137 -0.685  1.00 43.86  ? 94  LEU D C    1 
ATOM   9014  O O    . LEU D 2 76  ? -32.737 121.598 -1.144  1.00 42.76  ? 94  LEU D O    1 
ATOM   9015  C CB   . LEU D 2 76  ? -32.021 124.291 0.400   1.00 32.15  ? 94  LEU D CB   1 
ATOM   9016  C CG   . LEU D 2 76  ? -31.613 123.888 1.804   1.00 42.17  ? 94  LEU D CG   1 
ATOM   9017  C CD1  . LEU D 2 76  ? -30.324 124.593 2.171   1.00 69.77  ? 94  LEU D CD1  1 
ATOM   9018  C CD2  . LEU D 2 76  ? -32.719 124.236 2.781   1.00 49.91  ? 94  LEU D CD2  1 
ATOM   9019  N N    . SER D 2 77  ? -30.789 121.474 -0.051  1.00 50.01  ? 95  SER D N    1 
ATOM   9020  C CA   . SER D 2 77  ? -30.926 120.071 0.241   1.00 57.56  ? 95  SER D CA   1 
ATOM   9021  C C    . SER D 2 77  ? -32.032 119.997 1.256   1.00 60.23  ? 95  SER D C    1 
ATOM   9022  O O    . SER D 2 77  ? -32.085 120.798 2.175   1.00 55.38  ? 95  SER D O    1 
ATOM   9023  C CB   . SER D 2 77  ? -29.624 119.582 0.826   1.00 49.98  ? 95  SER D CB   1 
ATOM   9024  O OG   . SER D 2 77  ? -28.539 120.264 0.232   1.00 43.68  ? 95  SER D OG   1 
ATOM   9025  N N    . GLU D 2 78  ? -32.900 119.021 1.149   1.00 63.83  ? 96  GLU D N    1 
ATOM   9026  C CA   . GLU D 2 78  ? -34.081 119.027 1.990   1.00 66.82  ? 96  GLU D CA   1 
ATOM   9027  C C    . GLU D 2 78  ? -34.022 118.910 3.472   1.00 61.09  ? 96  GLU D C    1 
ATOM   9028  O O    . GLU D 2 78  ? -34.661 119.686 4.158   1.00 67.52  ? 96  GLU D O    1 
ATOM   9029  C CB   . GLU D 2 78  ? -35.048 117.962 1.469   1.00 71.71  ? 96  GLU D CB   1 
ATOM   9030  C CG   . GLU D 2 78  ? -35.054 117.802 -0.047  1.00 59.23  ? 96  GLU D CG   1 
ATOM   9031  C CD   . GLU D 2 78  ? -35.844 118.877 -0.769  1.00 61.08  ? 96  GLU D CD   1 
ATOM   9032  O OE1  . GLU D 2 78  ? -36.750 119.473 -0.156  1.00 67.15  ? 96  GLU D OE1  1 
ATOM   9033  O OE2  . GLU D 2 78  ? -35.571 119.113 -1.963  1.00 60.28  ? 96  GLU D OE2  1 
ATOM   9034  N N    . GLN D 2 79  ? -33.255 117.977 3.992   1.00 61.95  ? 97  GLN D N    1 
ATOM   9035  C CA   . GLN D 2 79  ? -33.284 117.754 5.436   1.00 60.57  ? 97  GLN D CA   1 
ATOM   9036  C C    . GLN D 2 79  ? -32.197 118.448 6.206   1.00 58.55  ? 97  GLN D C    1 
ATOM   9037  O O    . GLN D 2 79  ? -32.059 118.236 7.394   1.00 64.26  ? 97  GLN D O    1 
ATOM   9038  C CB   . GLN D 2 79  ? -33.341 116.262 5.779   1.00 59.31  ? 97  GLN D CB   1 
ATOM   9039  C CG   . GLN D 2 79  ? -34.633 115.566 5.402   1.00 61.24  ? 97  GLN D CG   1 
ATOM   9040  C CD   . GLN D 2 79  ? -34.646 115.094 3.965   1.00 59.85  ? 97  GLN D CD   1 
ATOM   9041  O OE1  . GLN D 2 79  ? -33.648 115.210 3.256   1.00 57.14  ? 97  GLN D OE1  1 
ATOM   9042  N NE2  . GLN D 2 79  ? -35.780 114.553 3.528   1.00 50.56  ? 97  GLN D NE2  1 
ATOM   9043  N N    . VAL D 2 80  ? -31.381 119.232 5.541   1.00 55.76  ? 98  VAL D N    1 
ATOM   9044  C CA   . VAL D 2 80  ? -30.408 119.995 6.261   1.00 54.06  ? 98  VAL D CA   1 
ATOM   9045  C C    . VAL D 2 80  ? -31.039 120.989 7.154   1.00 56.37  ? 98  VAL D C    1 
ATOM   9046  O O    . VAL D 2 80  ? -30.576 121.193 8.244   1.00 54.48  ? 98  VAL D O    1 
ATOM   9047  C CB   . VAL D 2 80  ? -29.368 120.684 5.386   1.00 49.85  ? 98  VAL D CB   1 
ATOM   9048  C CG1  . VAL D 2 80  ? -29.965 121.825 4.586   1.00 50.84  ? 98  VAL D CG1  1 
ATOM   9049  C CG2  . VAL D 2 80  ? -28.209 121.174 6.241   1.00 47.92  ? 98  VAL D CG2  1 
ATOM   9050  N N    . VAL D 2 81  ? -32.099 121.630 6.691   1.00 54.25  ? 99  VAL D N    1 
ATOM   9051  C CA   . VAL D 2 81  ? -32.744 122.645 7.507   1.00 59.34  ? 99  VAL D CA   1 
ATOM   9052  C C    . VAL D 2 81  ? -33.512 122.076 8.720   1.00 60.95  ? 99  VAL D C    1 
ATOM   9053  O O    . VAL D 2 81  ? -33.797 122.743 9.687   1.00 60.84  ? 99  VAL D O    1 
ATOM   9054  C CB   . VAL D 2 81  ? -33.676 123.553 6.713   1.00 49.65  ? 99  VAL D CB   1 
ATOM   9055  C CG1  . VAL D 2 81  ? -32.922 124.378 5.686   1.00 41.75  ? 99  VAL D CG1  1 
ATOM   9056  C CG2  . VAL D 2 81  ? -34.775 122.729 6.064   1.00 57.14  ? 99  VAL D CG2  1 
ATOM   9057  N N    . GLN D 2 82  ? -33.791 120.788 8.660   1.00 57.72  ? 100 GLN D N    1 
ATOM   9058  C CA   . GLN D 2 82  ? -34.338 120.106 9.812   1.00 56.69  ? 100 GLN D CA   1 
ATOM   9059  C C    . GLN D 2 82  ? -33.307 120.236 10.880  1.00 56.45  ? 100 GLN D C    1 
ATOM   9060  O O    . GLN D 2 82  ? -33.636 120.547 12.005  1.00 62.60  ? 100 GLN D O    1 
ATOM   9061  C CB   . GLN D 2 82  ? -34.666 118.644 9.607   1.00 56.90  ? 100 GLN D CB   1 
ATOM   9062  C CG   . GLN D 2 82  ? -36.127 118.375 9.252   1.00 75.99  ? 100 GLN D CG   1 
ATOM   9063  C CD   . GLN D 2 82  ? -36.619 119.110 8.008   1.00 76.45  ? 100 GLN D CD   1 
ATOM   9064  O OE1  . GLN D 2 82  ? -37.186 120.199 8.099   1.00 69.04  ? 100 GLN D OE1  1 
ATOM   9065  N NE2  . GLN D 2 82  ? -36.430 118.501 6.845   1.00 56.36  ? 100 GLN D NE2  1 
ATOM   9066  N N    . ARG D 2 83  ? -32.065 119.912 10.571  1.00 59.10  ? 101 ARG D N    1 
ATOM   9067  C CA   . ARG D 2 83  ? -30.942 120.142 11.502  1.00 60.05  ? 101 ARG D CA   1 
ATOM   9068  C C    . ARG D 2 83  ? -30.218 121.498 11.608  1.00 51.23  ? 101 ARG D C    1 
ATOM   9069  O O    . ARG D 2 83  ? -29.645 121.833 12.616  1.00 58.43  ? 101 ARG D O    1 
ATOM   9070  C CB   . ARG D 2 83  ? -29.842 119.120 11.239  1.00 52.78  ? 101 ARG D CB   1 
ATOM   9071  C CG   . ARG D 2 83  ? -30.249 117.685 11.527  1.00 46.90  ? 101 ARG D CG   1 
ATOM   9072  C CD   . ARG D 2 83  ? -30.317 117.428 13.017  1.00 36.74  ? 101 ARG D CD   1 
ATOM   9073  N NE   . ARG D 2 83  ? -29.000 117.497 13.633  1.00 44.94  ? 101 ARG D NE   1 
ATOM   9074  C CZ   . ARG D 2 83  ? -28.794 117.463 14.942  1.00 58.09  ? 101 ARG D CZ   1 
ATOM   9075  N NH1  . ARG D 2 83  ? -29.818 117.371 15.773  1.00 59.91  ? 101 ARG D NH1  1 
ATOM   9076  N NH2  . ARG D 2 83  ? -27.564 117.534 15.423  1.00 60.41  ? 101 ARG D NH2  1 
ATOM   9077  N N    . LEU D 2 84  ? -30.261 122.270 10.536  1.00 41.89  ? 102 LEU D N    1 
ATOM   9078  C CA   . LEU D 2 84  ? -29.746 123.629 10.559  1.00 43.26  ? 102 LEU D CA   1 
ATOM   9079  C C    . LEU D 2 84  ? -30.728 124.322 11.457  1.00 53.39  ? 102 LEU D C    1 
ATOM   9080  O O    . LEU D 2 84  ? -30.333 125.089 12.316  1.00 56.53  ? 102 LEU D O    1 
ATOM   9081  C CB   . LEU D 2 84  ? -29.557 124.381 9.251   1.00 37.94  ? 102 LEU D CB   1 
ATOM   9082  C CG   . LEU D 2 84  ? -28.703 125.640 9.218   1.00 30.17  ? 102 LEU D CG   1 
ATOM   9083  C CD1  . LEU D 2 84  ? -27.665 125.510 8.124   1.00 29.21  ? 102 LEU D CD1  1 
ATOM   9084  C CD2  . LEU D 2 84  ? -29.574 126.857 8.976   1.00 35.09  ? 102 LEU D CD2  1 
ATOM   9085  N N    . ALA D 2 85  ? -32.016 124.069 11.275  1.00 45.85  ? 103 ALA D N    1 
ATOM   9086  C CA   . ALA D 2 85  ? -33.006 124.621 12.178  1.00 46.03  ? 103 ALA D CA   1 
ATOM   9087  C C    . ALA D 2 85  ? -33.111 123.636 13.269  1.00 46.59  ? 103 ALA D C    1 
ATOM   9088  O O    . ALA D 2 85  ? -32.388 122.672 13.267  1.00 57.21  ? 103 ALA D O    1 
ATOM   9089  C CB   . ALA D 2 85  ? -34.334 124.774 11.512  1.00 50.55  ? 103 ALA D CB   1 
ATOM   9090  N N    . GLU D 2 86  ? -33.992 123.859 14.216  1.00 47.21  ? 104 GLU D N    1 
ATOM   9091  C CA   . GLU D 2 86  ? -34.075 122.981 15.370  1.00 47.67  ? 104 GLU D CA   1 
ATOM   9092  C C    . GLU D 2 86  ? -32.761 122.925 16.068  1.00 49.56  ? 104 GLU D C    1 
ATOM   9093  O O    . GLU D 2 86  ? -32.576 122.076 16.925  1.00 48.01  ? 104 GLU D O    1 
ATOM   9094  C CB   . GLU D 2 86  ? -34.527 121.578 15.005  1.00 47.45  ? 104 GLU D CB   1 
ATOM   9095  C CG   . GLU D 2 86  ? -36.031 121.418 14.793  1.00 58.18  ? 104 GLU D CG   1 
ATOM   9096  C CD   . GLU D 2 86  ? -36.547 122.024 13.497  1.00 49.89  ? 104 GLU D CD   1 
ATOM   9097  O OE1  . GLU D 2 86  ? -36.730 123.253 13.446  1.00 44.18  ? 104 GLU D OE1  1 
ATOM   9098  O OE2  . GLU D 2 86  ? -36.795 121.269 12.537  1.00 45.35  ? 104 GLU D OE2  1 
ATOM   9099  N N    . VAL D 2 87  ? -31.834 123.809 15.696  1.00 45.25  ? 105 VAL D N    1 
ATOM   9100  C CA   . VAL D 2 87  ? -30.587 123.887 16.385  1.00 42.21  ? 105 VAL D CA   1 
ATOM   9101  C C    . VAL D 2 87  ? -30.441 125.345 16.677  1.00 40.99  ? 105 VAL D C    1 
ATOM   9102  O O    . VAL D 2 87  ? -29.920 125.721 17.702  1.00 51.53  ? 105 VAL D O    1 
ATOM   9103  C CB   . VAL D 2 87  ? -29.464 123.348 15.495  1.00 33.61  ? 105 VAL D CB   1 
ATOM   9104  C CG1  . VAL D 2 87  ? -28.131 123.980 15.826  1.00 41.76  ? 105 VAL D CG1  1 
ATOM   9105  C CG2  . VAL D 2 87  ? -29.378 121.841 15.617  1.00 27.71  ? 105 VAL D CG2  1 
ATOM   9106  N N    . ALA D 2 88  ? -30.986 126.180 15.814  1.00 38.06  ? 106 ALA D N    1 
ATOM   9107  C CA   . ALA D 2 88  ? -30.847 127.637 15.969  1.00 42.44  ? 106 ALA D CA   1 
ATOM   9108  C C    . ALA D 2 88  ? -31.450 128.284 17.190  1.00 38.90  ? 106 ALA D C    1 
ATOM   9109  O O    . ALA D 2 88  ? -30.948 129.282 17.672  1.00 33.67  ? 106 ALA D O    1 
ATOM   9110  C CB   . ALA D 2 88  ? -31.223 128.376 14.705  1.00 38.83  ? 106 ALA D CB   1 
ATOM   9111  N N    . PRO D 2 89  ? -32.588 127.782 17.646  1.00 42.31  ? 107 PRO D N    1 
ATOM   9112  C CA   . PRO D 2 89  ? -33.124 128.291 18.902  1.00 44.99  ? 107 PRO D CA   1 
ATOM   9113  C C    . PRO D 2 89  ? -32.241 128.022 20.099  1.00 46.26  ? 107 PRO D C    1 
ATOM   9114  O O    . PRO D 2 89  ? -32.385 128.700 21.102  1.00 49.31  ? 107 PRO D O    1 
ATOM   9115  C CB   . PRO D 2 89  ? -34.401 127.466 19.076  1.00 44.26  ? 107 PRO D CB   1 
ATOM   9116  C CG   . PRO D 2 89  ? -34.434 126.463 17.973  1.00 45.16  ? 107 PRO D CG   1 
ATOM   9117  C CD   . PRO D 2 89  ? -33.644 127.100 16.887  1.00 45.26  ? 107 PRO D CD   1 
ATOM   9118  N N    . ARG D 2 90  ? -31.382 127.030 20.041  1.00 45.54  ? 108 ARG D N    1 
ATOM   9119  C CA   . ARG D 2 90  ? -30.592 126.630 21.179  1.00 44.13  ? 108 ARG D CA   1 
ATOM   9120  C C    . ARG D 2 90  ? -29.227 127.271 21.206  1.00 43.23  ? 108 ARG D C    1 
ATOM   9121  O O    . ARG D 2 90  ? -28.404 126.946 22.041  1.00 50.57  ? 108 ARG D O    1 
ATOM   9122  C CB   . ARG D 2 90  ? -30.457 125.114 21.092  1.00 47.50  ? 108 ARG D CB   1 
ATOM   9123  C CG   . ARG D 2 90  ? -30.113 124.382 22.374  1.00 56.85  ? 108 ARG D CG   1 
ATOM   9124  C CD   . ARG D 2 90  ? -29.107 123.276 22.093  1.00 54.10  ? 108 ARG D CD   1 
ATOM   9125  N NE   . ARG D 2 90  ? -29.491 122.474 20.936  1.00 63.78  ? 108 ARG D NE   1 
ATOM   9126  C CZ   . ARG D 2 90  ? -30.107 121.299 21.007  1.00 66.23  ? 108 ARG D CZ   1 
ATOM   9127  N NH1  . ARG D 2 90  ? -30.401 120.773 22.186  1.00 51.02  ? 108 ARG D NH1  1 
ATOM   9128  N NH2  . ARG D 2 90  ? -30.413 120.644 19.896  1.00 64.22  ? 108 ARG D NH2  1 
ATOM   9129  N N    . LEU D 2 91  ? -28.972 128.192 20.311  1.00 36.97  ? 109 LEU D N    1 
ATOM   9130  C CA   . LEU D 2 91  ? -27.650 128.762 20.216  1.00 39.71  ? 109 LEU D CA   1 
ATOM   9131  C C    . LEU D 2 91  ? -27.243 129.843 21.168  1.00 38.43  ? 109 LEU D C    1 
ATOM   9132  O O    . LEU D 2 91  ? -27.918 130.853 21.255  1.00 35.37  ? 109 LEU D O    1 
ATOM   9133  C CB   . LEU D 2 91  ? -27.441 129.292 18.816  1.00 48.22  ? 109 LEU D CB   1 
ATOM   9134  C CG   . LEU D 2 91  ? -27.637 128.368 17.625  1.00 46.50  ? 109 LEU D CG   1 
ATOM   9135  C CD1  . LEU D 2 91  ? -27.232 129.105 16.367  1.00 36.97  ? 109 LEU D CD1  1 
ATOM   9136  C CD2  . LEU D 2 91  ? -26.873 127.067 17.770  1.00 40.10  ? 109 LEU D CD2  1 
ATOM   9137  N N    . LYS D 2 92  ? -26.100 129.653 21.840  1.00 39.41  ? 110 LYS D N    1 
ATOM   9138  C CA   . LYS D 2 92  ? -25.576 130.614 22.755  1.00 35.38  ? 110 LYS D CA   1 
ATOM   9139  C C    . LYS D 2 92  ? -24.155 130.727 22.486  1.00 32.71  ? 110 LYS D C    1 
ATOM   9140  O O    . LYS D 2 92  ? -23.615 129.939 21.764  1.00 30.40  ? 110 LYS D O    1 
ATOM   9141  C CB   . LYS D 2 92  ? -25.732 130.126 24.174  1.00 31.14  ? 110 LYS D CB   1 
ATOM   9142  C CG   . LYS D 2 92  ? -25.359 128.683 24.422  1.00 37.00  ? 110 LYS D CG   1 
ATOM   9143  C CD   . LYS D 2 92  ? -25.062 128.469 25.895  1.00 40.67  ? 110 LYS D CD   1 
ATOM   9144  C CE   . LYS D 2 92  ? -23.757 129.131 26.303  1.00 44.19  ? 110 LYS D CE   1 
ATOM   9145  N NZ   . LYS D 2 92  ? -22.568 128.441 25.727  1.00 40.72  ? 110 LYS D NZ   1 
ATOM   9146  N N    . SER D 2 93  ? -23.524 131.706 23.097  1.00 34.66  ? 111 SER D N    1 
ATOM   9147  C CA   . SER D 2 93  ? -22.097 131.843 23.032  1.00 36.42  ? 111 SER D CA   1 
ATOM   9148  C C    . SER D 2 93  ? -21.406 131.981 24.383  1.00 33.79  ? 111 SER D C    1 
ATOM   9149  O O    . SER D 2 93  ? -21.740 132.877 25.118  1.00 34.54  ? 111 SER D O    1 
ATOM   9150  C CB   . SER D 2 93  ? -21.818 133.107 22.230  1.00 32.89  ? 111 SER D CB   1 
ATOM   9151  O OG   . SER D 2 93  ? -22.284 133.022 20.899  1.00 39.56  ? 111 SER D OG   1 
ATOM   9152  N N    . ASN D 2 94  ? -20.524 131.061 24.755  1.00 33.37  ? 112 ASN D N    1 
ATOM   9153  C CA   . ASN D 2 94  ? -19.779 131.172 26.009  1.00 27.55  ? 112 ASN D CA   1 
ATOM   9154  C C    . ASN D 2 94  ? -18.629 132.013 25.659  1.00 22.89  ? 112 ASN D C    1 
ATOM   9155  O O    . ASN D 2 94  ? -17.809 131.600 24.914  1.00 27.14  ? 112 ASN D O    1 
ATOM   9156  C CB   . ASN D 2 94  ? -19.226 129.868 26.551  1.00 23.97  ? 112 ASN D CB   1 
ATOM   9157  C CG   . ASN D 2 94  ? -18.989 129.890 28.041  1.00 32.79  ? 112 ASN D CG   1 
ATOM   9158  O OD1  . ASN D 2 94  ? -18.600 130.899 28.610  1.00 40.24  ? 112 ASN D OD1  1 
ATOM   9159  N ND2  . ASN D 2 94  ? -19.205 128.755 28.680  1.00 37.07  ? 112 ASN D ND2  1 
ATOM   9160  N N    . PRO D 2 95  ? -18.520 133.236 26.268  1.00 19.19  ? 113 PRO D N    1 
ATOM   9161  C CA   . PRO D 2 95  ? -17.327 133.994 25.921  1.00 21.74  ? 113 PRO D CA   1 
ATOM   9162  C C    . PRO D 2 95  ? -16.048 133.541 26.537  1.00 20.15  ? 113 PRO D C    1 
ATOM   9163  O O    . PRO D 2 95  ? -15.153 134.309 26.769  1.00 18.92  ? 113 PRO D O    1 
ATOM   9164  C CB   . PRO D 2 95  ? -17.669 135.368 26.437  1.00 23.44  ? 113 PRO D CB   1 
ATOM   9165  C CG   . PRO D 2 95  ? -18.505 135.130 27.605  1.00 26.10  ? 113 PRO D CG   1 
ATOM   9166  C CD   . PRO D 2 95  ? -19.420 134.100 27.085  1.00 21.85  ? 113 PRO D CD   1 
ATOM   9167  N N    . LYS D 2 96  ? -15.970 132.293 26.898  1.00 24.11  ? 114 LYS D N    1 
ATOM   9168  C CA   . LYS D 2 96  ? -14.740 131.770 27.411  1.00 25.74  ? 114 LYS D CA   1 
ATOM   9169  C C    . LYS D 2 96  ? -14.396 131.006 26.236  1.00 25.84  ? 114 LYS D C    1 
ATOM   9170  O O    . LYS D 2 96  ? -13.475 131.337 25.528  1.00 31.01  ? 114 LYS D O    1 
ATOM   9171  C CB   . LYS D 2 96  ? -15.034 130.818 28.546  1.00 25.20  ? 114 LYS D CB   1 
ATOM   9172  C CG   . LYS D 2 96  ? -13.823 130.250 29.249  1.00 32.89  ? 114 LYS D CG   1 
ATOM   9173  C CD   . LYS D 2 96  ? -14.259 129.539 30.515  1.00 34.33  ? 114 LYS D CD   1 
ATOM   9174  C CE   . LYS D 2 96  ? -14.989 128.251 30.185  1.00 32.65  ? 114 LYS D CE   1 
ATOM   9175  N NZ   . LYS D 2 96  ? -15.265 127.430 31.396  1.00 51.82  ? 114 LYS D NZ   1 
ATOM   9176  N N    . ASP D 2 97  ? -15.219 130.030 25.944  1.00 21.64  ? 115 ASP D N    1 
ATOM   9177  C CA   . ASP D 2 97  ? -14.985 129.190 24.838  1.00 20.95  ? 115 ASP D CA   1 
ATOM   9178  C C    . ASP D 2 97  ? -15.635 129.668 23.570  1.00 24.39  ? 115 ASP D C    1 
ATOM   9179  O O    . ASP D 2 97  ? -16.694 129.180 23.217  1.00 29.18  ? 115 ASP D O    1 
ATOM   9180  C CB   . ASP D 2 97  ? -15.525 127.850 25.251  1.00 23.47  ? 115 ASP D CB   1 
ATOM   9181  C CG   . ASP D 2 97  ? -14.794 127.263 26.430  1.00 33.89  ? 115 ASP D CG   1 
ATOM   9182  O OD1  . ASP D 2 97  ? -13.646 127.659 26.684  1.00 38.10  ? 115 ASP D OD1  1 
ATOM   9183  O OD2  . ASP D 2 97  ? -15.362 126.389 27.106  1.00 44.33  ? 115 ASP D OD2  1 
ATOM   9184  N N    . ASN D 2 98  ? -15.028 130.619 22.873  1.00 17.49  ? 116 ASN D N    1 
ATOM   9185  C CA   . ASN D 2 98  ? -15.542 131.114 21.608  1.00 18.49  ? 116 ASN D CA   1 
ATOM   9186  C C    . ASN D 2 98  ? -14.398 131.407 20.743  1.00 21.19  ? 116 ASN D C    1 
ATOM   9187  O O    . ASN D 2 98  ? -14.198 132.537 20.409  1.00 26.44  ? 116 ASN D O    1 
ATOM   9188  C CB   . ASN D 2 98  ? -16.094 132.501 21.759  1.00 25.23  ? 116 ASN D CB   1 
ATOM   9189  C CG   . ASN D 2 98  ? -17.576 132.532 22.006  1.00 25.67  ? 116 ASN D CG   1 
ATOM   9190  O OD1  . ASN D 2 98  ? -18.270 131.546 21.822  1.00 30.69  ? 116 ASN D OD1  1 
ATOM   9191  N ND2  . ASN D 2 98  ? -18.066 133.666 22.446  1.00 20.12  ? 116 ASN D ND2  1 
ATOM   9192  N N    . GLU D 2 99  ? -13.670 130.385 20.305  1.00 25.04  ? 117 GLU D N    1 
ATOM   9193  C CA   . GLU D 2 99  ? -12.451 130.583 19.525  1.00 26.15  ? 117 GLU D CA   1 
ATOM   9194  C C    . GLU D 2 99  ? -12.428 130.430 18.006  1.00 18.89  ? 117 GLU D C    1 
ATOM   9195  O O    . GLU D 2 99  ? -11.429 130.356 17.326  1.00 21.42  ? 117 GLU D O    1 
ATOM   9196  C CB   . GLU D 2 99  ? -11.435 129.558 19.947  1.00 25.07  ? 117 GLU D CB   1 
ATOM   9197  C CG   . GLU D 2 99  ? -11.767 128.157 19.515  1.00 29.94  ? 117 GLU D CG   1 
ATOM   9198  C CD   . GLU D 2 99  ? -12.798 127.517 20.398  1.00 29.57  ? 117 GLU D CD   1 
ATOM   9199  O OE1  . GLU D 2 99  ? -13.320 128.209 21.293  1.00 29.57  ? 117 GLU D OE1  1 
ATOM   9200  O OE2  . GLU D 2 99  ? -13.079 126.325 20.194  1.00 39.83  ? 117 GLU D OE2  1 
ATOM   9201  N N    . SER D 2 100 ? -13.622 130.483 17.494  1.00 14.08  ? 118 SER D N    1 
ATOM   9202  C CA   . SER D 2 100 ? -13.833 130.375 16.095  1.00 16.67  ? 118 SER D CA   1 
ATOM   9203  C C    . SER D 2 100 ? -13.712 131.790 15.794  1.00 20.91  ? 118 SER D C    1 
ATOM   9204  O O    . SER D 2 100 ? -13.363 132.157 14.694  1.00 27.25  ? 118 SER D O    1 
ATOM   9205  C CB   . SER D 2 100 ? -15.251 129.978 15.722  1.00 16.65  ? 118 SER D CB   1 
ATOM   9206  O OG   . SER D 2 100 ? -16.192 130.952 16.109  1.00 17.65  ? 118 SER D OG   1 
ATOM   9207  N N    . ARG D 2 101 ? -14.011 132.624 16.761  1.00 16.63  ? 119 ARG D N    1 
ATOM   9208  C CA   . ARG D 2 101 ? -14.080 134.036 16.512  1.00 19.53  ? 119 ARG D CA   1 
ATOM   9209  C C    . ARG D 2 101 ? -12.795 134.554 16.922  1.00 19.04  ? 119 ARG D C    1 
ATOM   9210  O O    . ARG D 2 101 ? -12.419 135.659 16.605  1.00 17.38  ? 119 ARG D O    1 
ATOM   9211  C CB   . ARG D 2 101 ? -15.190 134.584 17.374  1.00 16.50  ? 119 ARG D CB   1 
ATOM   9212  C CG   . ARG D 2 101 ? -15.463 136.065 17.241  1.00 19.38  ? 119 ARG D CG   1 
ATOM   9213  C CD   . ARG D 2 101 ? -15.637 136.467 15.803  1.00 28.51  ? 119 ARG D CD   1 
ATOM   9214  N NE   . ARG D 2 101 ? -15.480 137.898 15.656  1.00 24.84  ? 119 ARG D NE   1 
ATOM   9215  C CZ   . ARG D 2 101 ? -16.488 138.735 15.540  1.00 22.68  ? 119 ARG D CZ   1 
ATOM   9216  N NH1  . ARG D 2 101 ? -17.722 138.266 15.544  1.00 20.11  ? 119 ARG D NH1  1 
ATOM   9217  N NH2  . ARG D 2 101 ? -16.254 140.027 15.408  1.00 25.31  ? 119 ARG D NH2  1 
ATOM   9218  N N    . ARG D 2 102 ? -12.083 133.720 17.633  1.00 18.75  ? 120 ARG D N    1 
ATOM   9219  C CA   . ARG D 2 102 ? -10.808 134.117 18.100  1.00 22.11  ? 120 ARG D CA   1 
ATOM   9220  C C    . ARG D 2 102 ? -9.886  133.939 16.966  1.00 23.38  ? 120 ARG D C    1 
ATOM   9221  O O    . ARG D 2 102 ? -9.084  134.803 16.714  1.00 21.26  ? 120 ARG D O    1 
ATOM   9222  C CB   . ARG D 2 102 ? -10.460 133.258 19.274  1.00 21.51  ? 120 ARG D CB   1 
ATOM   9223  C CG   . ARG D 2 102 ? -11.107 133.677 20.580  1.00 22.43  ? 120 ARG D CG   1 
ATOM   9224  C CD   . ARG D 2 102 ? -10.859 132.650 21.668  1.00 20.85  ? 120 ARG D CD   1 
ATOM   9225  N NE   . ARG D 2 102 ? -11.554 132.907 22.918  1.00 13.70  ? 120 ARG D NE   1 
ATOM   9226  C CZ   . ARG D 2 102 ? -11.032 133.587 23.924  1.00 18.61  ? 120 ARG D CZ   1 
ATOM   9227  N NH1  . ARG D 2 102 ? -9.825  134.106 23.827  1.00 21.73  ? 120 ARG D NH1  1 
ATOM   9228  N NH2  . ARG D 2 102 ? -11.720 133.758 25.029  1.00 22.73  ? 120 ARG D NH2  1 
ATOM   9229  N N    . LEU D 2 103 ? -10.000 132.827 16.249  1.00 20.49  ? 121 LEU D N    1 
ATOM   9230  C CA   . LEU D 2 103 ? -9.227  132.643 15.036  1.00 22.31  ? 121 LEU D CA   1 
ATOM   9231  C C    . LEU D 2 103 ? -9.591  133.779 14.130  1.00 24.56  ? 121 LEU D C    1 
ATOM   9232  O O    . LEU D 2 103 ? -8.746  134.450 13.641  1.00 24.21  ? 121 LEU D O    1 
ATOM   9233  C CB   . LEU D 2 103 ? -9.524  131.310 14.344  1.00 20.11  ? 121 LEU D CB   1 
ATOM   9234  C CG   . LEU D 2 103 ? -8.585  130.909 13.203  1.00 20.05  ? 121 LEU D CG   1 
ATOM   9235  C CD1  . LEU D 2 103 ? -7.448  130.018 13.645  1.00 27.99  ? 121 LEU D CD1  1 
ATOM   9236  C CD2  . LEU D 2 103 ? -9.318  130.246 12.068  1.00 20.03  ? 121 LEU D CD2  1 
ATOM   9237  N N    . TYR D 2 104 ? -10.859 134.021 13.916  1.00 20.86  ? 122 TYR D N    1 
ATOM   9238  C CA   . TYR D 2 104 ? -11.228 135.034 12.983  1.00 19.33  ? 122 TYR D CA   1 
ATOM   9239  C C    . TYR D 2 104 ? -10.543 136.317 13.264  1.00 24.36  ? 122 TYR D C    1 
ATOM   9240  O O    . TYR D 2 104 ? -9.935  136.889 12.379  1.00 26.25  ? 122 TYR D O    1 
ATOM   9241  C CB   . TYR D 2 104 ? -12.717 135.242 13.005  1.00 15.18  ? 122 TYR D CB   1 
ATOM   9242  C CG   . TYR D 2 104 ? -13.216 136.350 12.121  1.00 17.60  ? 122 TYR D CG   1 
ATOM   9243  C CD1  . TYR D 2 104 ? -13.334 136.171 10.763  1.00 14.55  ? 122 TYR D CD1  1 
ATOM   9244  C CD2  . TYR D 2 104 ? -13.587 137.570 12.651  1.00 17.96  ? 122 TYR D CD2  1 
ATOM   9245  C CE1  . TYR D 2 104 ? -13.785 137.181 9.952   1.00 21.03  ? 122 TYR D CE1  1 
ATOM   9246  C CE2  . TYR D 2 104 ? -14.046 138.586 11.848  1.00 20.46  ? 122 TYR D CE2  1 
ATOM   9247  C CZ   . TYR D 2 104 ? -14.144 138.382 10.498  1.00 24.24  ? 122 TYR D CZ   1 
ATOM   9248  O OH   . TYR D 2 104 ? -14.600 139.386 9.686   1.00 31.55  ? 122 TYR D OH   1 
ATOM   9249  N N    . GLU D 2 105 ? -10.589 136.780 14.496  1.00 25.91  ? 123 GLU D N    1 
ATOM   9250  C CA   . GLU D 2 105 ? -10.068 138.102 14.823  1.00 22.62  ? 123 GLU D CA   1 
ATOM   9251  C C    . GLU D 2 105 ? -8.606  138.222 14.879  1.00 20.94  ? 123 GLU D C    1 
ATOM   9252  O O    . GLU D 2 105 ? -8.142  139.314 14.861  1.00 20.41  ? 123 GLU D O    1 
ATOM   9253  C CB   . GLU D 2 105 ? -10.675 138.612 16.124  1.00 25.76  ? 123 GLU D CB   1 
ATOM   9254  C CG   . GLU D 2 105 ? -12.149 138.958 16.085  1.00 26.46  ? 123 GLU D CG   1 
ATOM   9255  C CD   . GLU D 2 105 ? -12.689 139.265 17.461  1.00 21.62  ? 123 GLU D CD   1 
ATOM   9256  O OE1  . GLU D 2 105 ? -11.876 139.341 18.390  1.00 23.91  ? 123 GLU D OE1  1 
ATOM   9257  O OE2  . GLU D 2 105 ? -13.910 139.438 17.612  1.00 15.94  ? 123 GLU D OE2  1 
ATOM   9258  N N    . THR D 2 106 ? -7.870  137.127 15.032  1.00 22.59  ? 124 THR D N    1 
ATOM   9259  C CA   . THR D 2 106 ? -6.405  137.164 14.994  1.00 23.81  ? 124 THR D CA   1 
ATOM   9260  C C    . THR D 2 106 ? -5.968  137.128 13.572  1.00 26.51  ? 124 THR D C    1 
ATOM   9261  O O    . THR D 2 106 ? -4.850  137.481 13.267  1.00 27.04  ? 124 THR D O    1 
ATOM   9262  C CB   . THR D 2 106 ? -5.738  136.083 15.832  1.00 23.65  ? 124 THR D CB   1 
ATOM   9263  O OG1  . THR D 2 106 ? -4.350  136.399 15.966  1.00 25.43  ? 124 THR D OG1  1 
ATOM   9264  C CG2  . THR D 2 106 ? -5.855  134.730 15.196  1.00 29.62  ? 124 THR D CG2  1 
ATOM   9265  N N    . LEU D 2 107 ? -6.873  136.762 12.675  1.00 32.20  ? 125 LEU D N    1 
ATOM   9266  C CA   . LEU D 2 107 ? -6.616  136.769 11.234  1.00 26.95  ? 125 LEU D CA   1 
ATOM   9267  C C    . LEU D 2 107 ? -6.981  138.137 10.768  1.00 22.39  ? 125 LEU D C    1 
ATOM   9268  O O    . LEU D 2 107 ? -6.246  138.755 10.033  1.00 24.22  ? 125 LEU D O    1 
ATOM   9269  C CB   . LEU D 2 107 ? -7.547  135.775 10.550  1.00 23.92  ? 125 LEU D CB   1 
ATOM   9270  C CG   . LEU D 2 107 ? -7.355  134.273 10.673  1.00 24.22  ? 125 LEU D CG   1 
ATOM   9271  C CD1  . LEU D 2 107 ? -8.576  133.602 10.072  1.00 28.12  ? 125 LEU D CD1  1 
ATOM   9272  C CD2  . LEU D 2 107 ? -6.089  133.838 9.968   1.00 26.73  ? 125 LEU D CD2  1 
ATOM   9273  N N    . TYR D 2 108 ? -8.099  138.627 11.260  1.00 18.82  ? 126 TYR D N    1 
ATOM   9274  C CA   . TYR D 2 108 ? -8.541  139.950 10.947  1.00 20.09  ? 126 TYR D CA   1 
ATOM   9275  C C    . TYR D 2 108 ? -7.620  140.972 11.473  1.00 23.93  ? 126 TYR D C    1 
ATOM   9276  O O    . TYR D 2 108 ? -7.739  142.110 11.103  1.00 24.12  ? 126 TYR D O    1 
ATOM   9277  C CB   . TYR D 2 108 ? -9.851  140.112 11.643  1.00 25.86  ? 126 TYR D CB   1 
ATOM   9278  C CG   . TYR D 2 108 ? -10.739 141.242 11.234  1.00 28.10  ? 126 TYR D CG   1 
ATOM   9279  C CD1  . TYR D 2 108 ? -11.207 141.340 9.948   1.00 30.90  ? 126 TYR D CD1  1 
ATOM   9280  C CD2  . TYR D 2 108 ? -11.169 142.171 12.162  1.00 22.95  ? 126 TYR D CD2  1 
ATOM   9281  C CE1  . TYR D 2 108 ? -12.041 142.365 9.579   1.00 33.15  ? 126 TYR D CE1  1 
ATOM   9282  C CE2  . TYR D 2 108 ? -12.004 143.199 11.800  1.00 20.05  ? 126 TYR D CE2  1 
ATOM   9283  C CZ   . TYR D 2 108 ? -12.436 143.284 10.502  1.00 33.29  ? 126 TYR D CZ   1 
ATOM   9284  O OH   . TYR D 2 108 ? -13.267 144.292 10.103  1.00 33.89  ? 126 TYR D OH   1 
ATOM   9285  N N    . ALA D 2 109 ? -6.704  140.592 12.349  1.00 22.73  ? 127 ALA D N    1 
ATOM   9286  C CA   . ALA D 2 109 ? -5.772  141.536 12.958  1.00 20.88  ? 127 ALA D CA   1 
ATOM   9287  C C    . ALA D 2 109 ? -4.565  141.655 12.194  1.00 22.13  ? 127 ALA D C    1 
ATOM   9288  O O    . ALA D 2 109 ? -3.866  142.636 12.299  1.00 24.32  ? 127 ALA D O    1 
ATOM   9289  C CB   . ALA D 2 109 ? -5.369  141.066 14.285  1.00 18.80  ? 127 ALA D CB   1 
ATOM   9290  N N    . ASP D 2 110 ? -4.265  140.621 11.436  1.00 24.81  ? 128 ASP D N    1 
ATOM   9291  C CA   . ASP D 2 110 ? -3.058  140.616 10.638  1.00 31.11  ? 128 ASP D CA   1 
ATOM   9292  C C    . ASP D 2 110 ? -3.435  141.249 9.324   1.00 31.24  ? 128 ASP D C    1 
ATOM   9293  O O    . ASP D 2 110 ? -2.556  141.684 8.608   1.00 28.29  ? 128 ASP D O    1 
ATOM   9294  C CB   . ASP D 2 110 ? -2.529  139.202 10.468  1.00 28.71  ? 128 ASP D CB   1 
ATOM   9295  C CG   . ASP D 2 110 ? -1.718  138.734 11.639  1.00 28.14  ? 128 ASP D CG   1 
ATOM   9296  O OD1  . ASP D 2 110 ? -1.986  139.174 12.762  1.00 30.94  ? 128 ASP D OD1  1 
ATOM   9297  O OD2  . ASP D 2 110 ? -0.813  137.908 11.435  1.00 36.50  ? 128 ASP D OD2  1 
ATOM   9298  N N    . HIS D 2 111 ? -4.726  141.285 8.990   1.00 25.44  ? 129 HIS D N    1 
ATOM   9299  C CA   . HIS D 2 111 ? -5.205  141.938 7.778   1.00 24.03  ? 129 HIS D CA   1 
ATOM   9300  C C    . HIS D 2 111 ? -5.553  143.377 8.019   1.00 26.63  ? 129 HIS D C    1 
ATOM   9301  O O    . HIS D 2 111 ? -5.876  144.091 7.114   1.00 35.59  ? 129 HIS D O    1 
ATOM   9302  C CB   . HIS D 2 111 ? -6.419  141.231 7.223   1.00 23.00  ? 129 HIS D CB   1 
ATOM   9303  C CG   . HIS D 2 111 ? -6.645  141.463 5.767   1.00 26.78  ? 129 HIS D CG   1 
ATOM   9304  N ND1  . HIS D 2 111 ? -5.706  141.155 4.809   1.00 30.58  ? 129 HIS D ND1  1 
ATOM   9305  C CD2  . HIS D 2 111 ? -7.698  141.987 5.102   1.00 27.62  ? 129 HIS D CD2  1 
ATOM   9306  C CE1  . HIS D 2 111 ? -6.174  141.475 3.619   1.00 32.81  ? 129 HIS D CE1  1 
ATOM   9307  N NE2  . HIS D 2 111 ? -7.381  141.983 3.769   1.00 34.02  ? 129 HIS D NE2  1 
ATOM   9308  N N    . LEU D 2 112 ? -5.504  143.824 9.247   1.00 21.47  ? 130 LEU D N    1 
ATOM   9309  C CA   . LEU D 2 112 ? -5.798  145.193 9.550   1.00 24.12  ? 130 LEU D CA   1 
ATOM   9310  C C    . LEU D 2 112 ? -4.495  145.802 9.616   1.00 28.14  ? 130 LEU D C    1 
ATOM   9311  O O    . LEU D 2 112 ? -4.375  147.006 9.492   1.00 31.41  ? 130 LEU D O    1 
ATOM   9312  C CB   . LEU D 2 112 ? -6.427  145.313 10.911  1.00 28.50  ? 130 LEU D CB   1 
ATOM   9313  C CG   . LEU D 2 112 ? -7.888  145.705 11.178  1.00 30.97  ? 130 LEU D CG   1 
ATOM   9314  C CD1  . LEU D 2 112 ? -8.861  144.891 10.358  1.00 30.29  ? 130 LEU D CD1  1 
ATOM   9315  C CD2  . LEU D 2 112 ? -8.226  145.553 12.650  1.00 23.52  ? 130 LEU D CD2  1 
ATOM   9316  N N    . GLU D 2 113 ? -3.512  145.006 9.962   1.00 30.67  ? 131 GLU D N    1 
ATOM   9317  C CA   . GLU D 2 113 ? -2.156  145.465 9.969   1.00 26.20  ? 131 GLU D CA   1 
ATOM   9318  C C    . GLU D 2 113 ? -1.822  145.520 8.542   1.00 30.42  ? 131 GLU D C    1 
ATOM   9319  O O    . GLU D 2 113 ? -1.157  146.425 8.112   1.00 36.42  ? 131 GLU D O    1 
ATOM   9320  C CB   . GLU D 2 113 ? -1.285  144.450 10.664  1.00 30.49  ? 131 GLU D CB   1 
ATOM   9321  C CG   . GLU D 2 113 ? 0.209   144.761 10.666  1.00 46.43  ? 131 GLU D CG   1 
ATOM   9322  C CD   . GLU D 2 113 ? 1.103   143.523 10.589  1.00 43.72  ? 131 GLU D CD   1 
ATOM   9323  O OE1  . GLU D 2 113 ? 0.589   142.395 10.467  1.00 45.63  ? 131 GLU D OE1  1 
ATOM   9324  O OE2  . GLU D 2 113 ? 2.336   143.682 10.644  1.00 33.20  ? 131 GLU D OE2  1 
ATOM   9325  N N    . SER D 2 114 ? -2.319  144.575 7.766   1.00 28.99  ? 132 SER D N    1 
ATOM   9326  C CA   . SER D 2 114 ? -1.947  144.528 6.366   1.00 26.61  ? 132 SER D CA   1 
ATOM   9327  C C    . SER D 2 114 ? -2.232  145.819 5.689   1.00 26.41  ? 132 SER D C    1 
ATOM   9328  O O    . SER D 2 114 ? -1.363  146.444 5.134   1.00 32.00  ? 132 SER D O    1 
ATOM   9329  C CB   . SER D 2 114 ? -2.700  143.418 5.666   1.00 29.50  ? 132 SER D CB   1 
ATOM   9330  O OG   . SER D 2 114 ? -2.366  143.354 4.293   1.00 36.47  ? 132 SER D OG   1 
ATOM   9331  N N    . VAL D 2 115 ? -3.454  146.262 5.791   1.00 24.03  ? 133 VAL D N    1 
ATOM   9332  C CA   . VAL D 2 115 ? -3.817  147.527 5.232   1.00 26.13  ? 133 VAL D CA   1 
ATOM   9333  C C    . VAL D 2 115 ? -3.113  148.764 5.793   1.00 28.49  ? 133 VAL D C    1 
ATOM   9334  O O    . VAL D 2 115 ? -2.890  149.725 5.077   1.00 33.62  ? 133 VAL D O    1 
ATOM   9335  C CB   . VAL D 2 115 ? -5.332  147.563 5.296   1.00 20.53  ? 133 VAL D CB   1 
ATOM   9336  C CG1  . VAL D 2 115 ? -5.868  148.722 4.484   1.00 28.32  ? 133 VAL D CG1  1 
ATOM   9337  C CG2  . VAL D 2 115 ? -5.890  146.264 4.753   1.00 17.87  ? 133 VAL D CG2  1 
ATOM   9338  N N    . ILE D 2 116 ? -2.743  148.752 7.051   1.00 26.69  ? 134 ILE D N    1 
ATOM   9339  C CA   . ILE D 2 116 ? -1.993  149.866 7.628   1.00 28.70  ? 134 ILE D CA   1 
ATOM   9340  C C    . ILE D 2 116 ? -0.595  150.027 7.108   1.00 31.76  ? 134 ILE D C    1 
ATOM   9341  O O    . ILE D 2 116 ? -0.130  151.128 6.975   1.00 31.79  ? 134 ILE D O    1 
ATOM   9342  C CB   . ILE D 2 116 ? -2.092  149.927 9.170   1.00 29.77  ? 134 ILE D CB   1 
ATOM   9343  C CG1  . ILE D 2 116 ? -2.320  151.360 9.653   1.00 30.39  ? 134 ILE D CG1  1 
ATOM   9344  C CG2  . ILE D 2 116 ? -0.904  149.299 9.852   1.00 30.28  ? 134 ILE D CG2  1 
ATOM   9345  C CD1  . ILE D 2 116 ? -3.753  151.815 9.503   1.00 29.98  ? 134 ILE D CD1  1 
ATOM   9346  N N    . LYS D 2 117 ? 0.099   148.939 6.838   1.00 31.60  ? 135 LYS D N    1 
ATOM   9347  C CA   . LYS D 2 117 ? 1.440   149.001 6.268   1.00 33.23  ? 135 LYS D CA   1 
ATOM   9348  C C    . LYS D 2 117 ? 1.358   149.634 4.889   1.00 47.86  ? 135 LYS D C    1 
ATOM   9349  O O    . LYS D 2 117 ? 2.283   150.330 4.473   1.00 44.29  ? 135 LYS D O    1 
ATOM   9350  C CB   . LYS D 2 117 ? 2.045   147.620 6.184   1.00 31.74  ? 135 LYS D CB   1 
ATOM   9351  C CG   . LYS D 2 117 ? 2.035   146.826 7.466   1.00 38.82  ? 135 LYS D CG   1 
ATOM   9352  C CD   . LYS D 2 117 ? 2.052   145.342 7.148   1.00 40.33  ? 135 LYS D CD   1 
ATOM   9353  C CE   . LYS D 2 117 ? 3.233   144.977 6.266   1.00 40.14  ? 135 LYS D CE   1 
ATOM   9354  N NZ   . LYS D 2 117 ? 4.545   145.136 6.958   1.00 38.62  ? 135 LYS D NZ   1 
ATOM   9355  N N    . GLN D 2 118 ? 0.275   149.368 4.155   1.00 46.85  ? 136 GLN D N    1 
ATOM   9356  C CA   . GLN D 2 118 ? 0.064   149.995 2.861   1.00 36.99  ? 136 GLN D CA   1 
ATOM   9357  C C    . GLN D 2 118 ? 0.003   151.498 3.024   1.00 44.36  ? 136 GLN D C    1 
ATOM   9358  O O    . GLN D 2 118 ? 0.544   152.209 2.201   1.00 52.89  ? 136 GLN D O    1 
ATOM   9359  C CB   . GLN D 2 118 ? -1.192  149.460 2.215   1.00 32.72  ? 136 GLN D CB   1 
ATOM   9360  C CG   . GLN D 2 118 ? -1.115  148.000 1.822   1.00 30.04  ? 136 GLN D CG   1 
ATOM   9361  C CD   . GLN D 2 118 ? -2.405  147.465 1.244   1.00 43.02  ? 136 GLN D CD   1 
ATOM   9362  O OE1  . GLN D 2 118 ? -3.483  147.986 1.525   1.00 43.16  ? 136 GLN D OE1  1 
ATOM   9363  N NE2  . GLN D 2 118 ? -2.305  146.428 0.419   1.00 49.66  ? 136 GLN D NE2  1 
ATOM   9364  N N    . GLU D 2 119 ? -0.641  152.011 4.064   1.00 43.90  ? 137 GLU D N    1 
ATOM   9365  C CA   . GLU D 2 119 ? -0.590  153.442 4.307   1.00 48.10  ? 137 GLU D CA   1 
ATOM   9366  C C    . GLU D 2 119 ? 0.642   153.665 5.102   1.00 51.83  ? 137 GLU D C    1 
ATOM   9367  O O    . GLU D 2 119 ? 0.610   153.650 6.319   1.00 47.76  ? 137 GLU D O    1 
ATOM   9368  C CB   . GLU D 2 119 ? -1.774  153.899 5.105   1.00 49.92  ? 137 GLU D CB   1 
ATOM   9369  C CG   . GLU D 2 119 ? -2.306  155.248 4.644   1.00 61.86  ? 137 GLU D CG   1 
ATOM   9370  C CD   . GLU D 2 119 ? -1.225  156.309 4.548   1.00 64.25  ? 137 GLU D CD   1 
ATOM   9371  O OE1  . GLU D 2 119 ? -0.563  156.571 5.568   1.00 55.89  ? 137 GLU D OE1  1 
ATOM   9372  O OE2  . GLU D 2 119 ? -1.046  156.888 3.457   1.00 59.51  ? 137 GLU D OE2  1 
ATOM   9373  N N    . SER D 2 120 ? 1.727   153.997 4.433   1.00 51.35  ? 138 SER D N    1 
ATOM   9374  C CA   . SER D 2 120 ? 3.003   154.090 5.092   1.00 50.92  ? 138 SER D CA   1 
ATOM   9375  C C    . SER D 2 120 ? 3.290   155.345 5.787   1.00 50.12  ? 138 SER D C    1 
ATOM   9376  O O    . SER D 2 120 ? 4.358   155.511 6.328   1.00 54.84  ? 138 SER D O    1 
ATOM   9377  C CB   . SER D 2 120 ? 4.057   153.947 4.017   1.00 44.62  ? 138 SER D CB   1 
ATOM   9378  O OG   . SER D 2 120 ? 3.674   154.661 2.858   1.00 45.13  ? 138 SER D OG   1 
ATOM   9379  N N    . ASP D 2 121 ? 2.387   156.285 5.740   1.00 51.73  ? 139 ASP D N    1 
ATOM   9380  C CA   . ASP D 2 121 ? 2.727   157.575 6.285   1.00 50.40  ? 139 ASP D CA   1 
ATOM   9381  C C    . ASP D 2 121 ? 2.688   157.662 7.786   1.00 57.42  ? 139 ASP D C    1 
ATOM   9382  O O    . ASP D 2 121 ? 1.728   158.177 8.360   1.00 55.70  ? 139 ASP D O    1 
ATOM   9383  C CB   . ASP D 2 121 ? 1.992   158.647 5.517   1.00 58.86  ? 139 ASP D CB   1 
ATOM   9384  C CG   . ASP D 2 121 ? 2.511   158.805 4.095   1.00 61.63  ? 139 ASP D CG   1 
ATOM   9385  O OD1  . ASP D 2 121 ? 3.707   158.542 3.860   1.00 52.08  ? 139 ASP D OD1  1 
ATOM   9386  O OD2  . ASP D 2 121 ? 1.725   159.204 3.210   1.00 51.57  ? 139 ASP D OD2  1 
ATOM   9387  N N    . LEU D 2 122 ? 3.750   157.196 8.429   1.00 59.37  ? 140 LEU D N    1 
ATOM   9388  C CA   . LEU D 2 122 ? 3.825   157.232 9.874   1.00 44.58  ? 140 LEU D CA   1 
ATOM   9389  C C    . LEU D 2 122 ? 4.157   158.578 10.437  1.00 45.74  ? 140 LEU D C    1 
ATOM   9390  O O    . LEU D 2 122 ? 5.070   158.751 11.221  1.00 46.45  ? 140 LEU D O    1 
ATOM   9391  C CB   . LEU D 2 122 ? 4.963   156.326 10.268  1.00 42.29  ? 140 LEU D CB   1 
ATOM   9392  C CG   . LEU D 2 122 ? 4.848   154.847 9.931   1.00 35.17  ? 140 LEU D CG   1 
ATOM   9393  C CD1  . LEU D 2 122 ? 6.129   154.118 10.262  1.00 29.87  ? 140 LEU D CD1  1 
ATOM   9394  C CD2  . LEU D 2 122 ? 3.663   154.205 10.620  1.00 38.96  ? 140 LEU D CD2  1 
ATOM   9395  N N    . SER D 2 123 ? 3.404   159.554 9.983   1.00 48.06  ? 141 SER D N    1 
ATOM   9396  C CA   . SER D 2 123 ? 3.704   160.914 10.307  1.00 40.10  ? 141 SER D CA   1 
ATOM   9397  C C    . SER D 2 123 ? 3.002   161.164 11.554  1.00 37.18  ? 141 SER D C    1 
ATOM   9398  O O    . SER D 2 123 ? 3.518   161.797 12.448  1.00 39.45  ? 141 SER D O    1 
ATOM   9399  C CB   . SER D 2 123 ? 3.231   161.881 9.227   1.00 41.06  ? 141 SER D CB   1 
ATOM   9400  O OG   . SER D 2 123 ? 1.846   161.765 8.972   1.00 40.56  ? 141 SER D OG   1 
ATOM   9401  N N    . VAL D 2 124 ? 1.809   160.622 11.629  1.00 38.57  ? 142 VAL D N    1 
ATOM   9402  C CA   . VAL D 2 124 ? 1.017   160.839 12.812  1.00 40.56  ? 142 VAL D CA   1 
ATOM   9403  C C    . VAL D 2 124 ? 1.676   160.300 14.028  1.00 37.28  ? 142 VAL D C    1 
ATOM   9404  O O    . VAL D 2 124 ? 1.563   160.872 15.045  1.00 31.97  ? 142 VAL D O    1 
ATOM   9405  C CB   . VAL D 2 124 ? -0.382  160.264 12.692  1.00 35.77  ? 142 VAL D CB   1 
ATOM   9406  C CG1  . VAL D 2 124 ? -0.400  158.798 12.328  1.00 36.00  ? 142 VAL D CG1  1 
ATOM   9407  C CG2  . VAL D 2 124 ? -1.230  160.636 13.885  1.00 32.72  ? 142 VAL D CG2  1 
ATOM   9408  N N    . PHE D 2 125 ? 2.343   159.161 13.940  1.00 36.47  ? 143 PHE D N    1 
ATOM   9409  C CA   . PHE D 2 125 ? 2.912   158.546 15.104  1.00 33.70  ? 143 PHE D CA   1 
ATOM   9410  C C    . PHE D 2 125 ? 4.117   159.351 15.489  1.00 33.33  ? 143 PHE D C    1 
ATOM   9411  O O    . PHE D 2 125 ? 4.563   159.303 16.604  1.00 35.58  ? 143 PHE D O    1 
ATOM   9412  C CB   . PHE D 2 125 ? 3.283   157.100 14.822  1.00 27.92  ? 143 PHE D CB   1 
ATOM   9413  C CG   . PHE D 2 125 ? 2.207   156.285 14.191  1.00 24.75  ? 143 PHE D CG   1 
ATOM   9414  C CD1  . PHE D 2 125 ? 0.922   156.327 14.639  1.00 26.75  ? 143 PHE D CD1  1 
ATOM   9415  C CD2  . PHE D 2 125 ? 2.512   155.418 13.182  1.00 29.83  ? 143 PHE D CD2  1 
ATOM   9416  C CE1  . PHE D 2 125 ? -0.056  155.555 14.050  1.00 33.06  ? 143 PHE D CE1  1 
ATOM   9417  C CE2  . PHE D 2 125 ? 1.550   154.644 12.579  1.00 38.98  ? 143 PHE D CE2  1 
ATOM   9418  C CZ   . PHE D 2 125 ? 0.255   154.714 13.014  1.00 39.52  ? 143 PHE D CZ   1 
ATOM   9419  N N    . ASN D 2 126 ? 4.653   160.103 14.554  1.00 34.67  ? 144 ASN D N    1 
ATOM   9420  C CA   . ASN D 2 126 ? 5.861   160.870 14.800  1.00 38.69  ? 144 ASN D CA   1 
ATOM   9421  C C    . ASN D 2 126 ? 5.424   162.229 15.232  1.00 44.17  ? 144 ASN D C    1 
ATOM   9422  O O    . ASN D 2 126 ? 6.236   163.052 15.638  1.00 43.79  ? 144 ASN D O    1 
ATOM   9423  C CB   . ASN D 2 126 ? 6.709   160.942 13.555  1.00 39.37  ? 144 ASN D CB   1 
ATOM   9424  C CG   . ASN D 2 126 ? 8.063   160.320 13.723  1.00 42.73  ? 144 ASN D CG   1 
ATOM   9425  O OD1  . ASN D 2 126 ? 8.692   160.447 14.761  1.00 47.54  ? 144 ASN D OD1  1 
ATOM   9426  N ND2  . ASN D 2 126 ? 8.536   159.667 12.683  1.00 45.63  ? 144 ASN D ND2  1 
ATOM   9427  N N    . GLU D 2 127 ? 4.124   162.474 15.173  1.00 39.07  ? 145 GLU D N    1 
ATOM   9428  C CA   . GLU D 2 127 ? 3.595   163.715 15.712  1.00 41.36  ? 145 GLU D CA   1 
ATOM   9429  C C    . GLU D 2 127 ? 2.541   163.406 16.749  1.00 39.91  ? 145 GLU D C    1 
ATOM   9430  O O    . GLU D 2 127 ? 1.760   164.251 17.080  1.00 37.28  ? 145 GLU D O    1 
ATOM   9431  C CB   . GLU D 2 127 ? 3.092   164.673 14.641  1.00 44.75  ? 145 GLU D CB   1 
ATOM   9432  C CG   . GLU D 2 127 ? 1.834   164.262 13.909  1.00 44.48  ? 145 GLU D CG   1 
ATOM   9433  C CD   . GLU D 2 127 ? 1.634   165.035 12.635  1.00 47.51  ? 145 GLU D CD   1 
ATOM   9434  O OE1  . GLU D 2 127 ? 2.634   165.326 11.957  1.00 55.84  ? 145 GLU D OE1  1 
ATOM   9435  O OE2  . GLU D 2 127 ? 0.481   165.349 12.311  1.00 47.36  ? 145 GLU D OE2  1 
ATOM   9436  N N    . LEU D 2 128 ? 2.473   162.180 17.257  1.00 33.69  ? 146 LEU D N    1 
ATOM   9437  C CA   . LEU D 2 128 ? 1.578   161.894 18.359  1.00 28.51  ? 146 LEU D CA   1 
ATOM   9438  C C    . LEU D 2 128 ? 2.617   161.778 19.376  1.00 33.20  ? 146 LEU D C    1 
ATOM   9439  O O    . LEU D 2 128 ? 2.346   161.573 20.528  1.00 36.91  ? 146 LEU D O    1 
ATOM   9440  C CB   . LEU D 2 128 ? 0.885   160.588 18.207  1.00 23.97  ? 146 LEU D CB   1 
ATOM   9441  C CG   . LEU D 2 128 ? -0.263  160.156 19.093  1.00 21.45  ? 146 LEU D CG   1 
ATOM   9442  C CD1  . LEU D 2 128 ? -1.578  160.680 18.565  1.00 24.55  ? 146 LEU D CD1  1 
ATOM   9443  C CD2  . LEU D 2 128 ? -0.246  158.649 19.050  1.00 21.37  ? 146 LEU D CD2  1 
ATOM   9444  N N    . ARG D 2 129 ? 3.851   161.860 18.938  1.00 31.81  ? 147 ARG D N    1 
ATOM   9445  C CA   . ARG D 2 129 ? 4.934   161.812 19.877  1.00 37.23  ? 147 ARG D CA   1 
ATOM   9446  C C    . ARG D 2 129 ? 5.045   163.154 20.563  1.00 41.02  ? 147 ARG D C    1 
ATOM   9447  O O    . ARG D 2 129 ? 6.005   163.441 21.255  1.00 40.95  ? 147 ARG D O    1 
ATOM   9448  C CB   . ARG D 2 129 ? 6.229   161.223 19.275  1.00 32.16  ? 147 ARG D CB   1 
ATOM   9449  C CG   . ARG D 2 129 ? 7.141   162.112 18.482  1.00 40.37  ? 147 ARG D CG   1 
ATOM   9450  C CD   . ARG D 2 129 ? 8.219   161.250 17.852  1.00 38.35  ? 147 ARG D CD   1 
ATOM   9451  N NE   . ARG D 2 129 ? 9.327   160.954 18.749  1.00 49.25  ? 147 ARG D NE   1 
ATOM   9452  C CZ   . ARG D 2 129 ? 10.482  161.615 18.743  1.00 55.49  ? 147 ARG D CZ   1 
ATOM   9453  N NH1  . ARG D 2 129 ? 10.672  162.600 17.882  1.00 57.55  ? 147 ARG D NH1  1 
ATOM   9454  N NH2  . ARG D 2 129 ? 11.450  161.286 19.584  1.00 55.32  ? 147 ARG D NH2  1 
ATOM   9455  N N    . ASP D 2 130 ? 4.008   163.964 20.418  1.00 40.42  ? 148 ASP D N    1 
ATOM   9456  C CA   . ASP D 2 130 ? 4.000   165.253 21.059  1.00 38.37  ? 148 ASP D CA   1 
ATOM   9457  C C    . ASP D 2 130 ? 2.872   165.327 22.012  1.00 36.58  ? 148 ASP D C    1 
ATOM   9458  O O    . ASP D 2 130 ? 2.946   166.012 23.017  1.00 43.23  ? 148 ASP D O    1 
ATOM   9459  C CB   . ASP D 2 130 ? 3.997   166.394 20.033  1.00 41.23  ? 148 ASP D CB   1 
ATOM   9460  C CG   . ASP D 2 130 ? 2.689   166.552 19.261  1.00 43.69  ? 148 ASP D CG   1 
ATOM   9461  O OD1  . ASP D 2 130 ? 1.776   165.721 19.347  1.00 42.92  ? 148 ASP D OD1  1 
ATOM   9462  O OD2  . ASP D 2 130 ? 2.585   167.554 18.527  1.00 45.71  ? 148 ASP D OD2  1 
ATOM   9463  N N    . SER D 2 131 ? 1.796   164.657 21.683  1.00 33.02  ? 149 SER D N    1 
ATOM   9464  C CA   . SER D 2 131 ? 0.691   164.597 22.592  1.00 39.84  ? 149 SER D CA   1 
ATOM   9465  C C    . SER D 2 131 ? 1.072   163.733 23.758  1.00 42.89  ? 149 SER D C    1 
ATOM   9466  O O    . SER D 2 131 ? 0.705   163.999 24.877  1.00 45.28  ? 149 SER D O    1 
ATOM   9467  C CB   . SER D 2 131 ? -0.591  164.164 21.919  1.00 35.93  ? 149 SER D CB   1 
ATOM   9468  O OG   . SER D 2 131 ? -0.984  165.135 20.983  1.00 39.03  ? 149 SER D OG   1 
ATOM   9469  N N    . TYR D 2 132 ? 1.833   162.696 23.506  1.00 36.46  ? 150 TYR D N    1 
ATOM   9470  C CA   . TYR D 2 132 ? 2.288   161.869 24.582  1.00 33.80  ? 150 TYR D CA   1 
ATOM   9471  C C    . TYR D 2 132 ? 3.022   162.695 25.569  1.00 32.59  ? 150 TYR D C    1 
ATOM   9472  O O    . TYR D 2 132 ? 2.571   162.864 26.671  1.00 34.59  ? 150 TYR D O    1 
ATOM   9473  C CB   . TYR D 2 132 ? 3.228   160.794 24.055  1.00 30.89  ? 150 TYR D CB   1 
ATOM   9474  C CG   . TYR D 2 132 ? 3.426   159.684 25.027  1.00 33.28  ? 150 TYR D CG   1 
ATOM   9475  C CD1  . TYR D 2 132 ? 2.339   159.099 25.642  1.00 36.98  ? 150 TYR D CD1  1 
ATOM   9476  C CD2  . TYR D 2 132 ? 4.688   159.231 25.348  1.00 30.35  ? 150 TYR D CD2  1 
ATOM   9477  C CE1  . TYR D 2 132 ? 2.499   158.090 26.552  1.00 43.32  ? 150 TYR D CE1  1 
ATOM   9478  C CE2  . TYR D 2 132 ? 4.855   158.216 26.253  1.00 28.47  ? 150 TYR D CE2  1 
ATOM   9479  C CZ   . TYR D 2 132 ? 3.754   157.654 26.852  1.00 41.48  ? 150 TYR D CZ   1 
ATOM   9480  O OH   . TYR D 2 132 ? 3.881   156.641 27.766  1.00 46.04  ? 150 TYR D OH   1 
ATOM   9481  N N    . ASN D 2 133 ? 4.162   163.214 25.188  1.00 35.94  ? 151 ASN D N    1 
ATOM   9482  C CA   . ASN D 2 133 ? 5.007   163.929 26.095  1.00 34.08  ? 151 ASN D CA   1 
ATOM   9483  C C    . ASN D 2 133 ? 4.266   164.938 26.885  1.00 39.01  ? 151 ASN D C    1 
ATOM   9484  O O    . ASN D 2 133 ? 4.498   165.096 28.068  1.00 49.11  ? 151 ASN D O    1 
ATOM   9485  C CB   . ASN D 2 133 ? 6.115   164.625 25.333  1.00 31.09  ? 151 ASN D CB   1 
ATOM   9486  C CG   . ASN D 2 133 ? 6.894   163.706 24.432  1.00 54.06  ? 151 ASN D CG   1 
ATOM   9487  O OD1  . ASN D 2 133 ? 6.421   162.650 24.026  1.00 62.61  ? 151 ASN D OD1  1 
ATOM   9488  N ND2  . ASN D 2 133 ? 8.107   164.122 24.093  1.00 61.20  ? 151 ASN D ND2  1 
ATOM   9489  N N    . ALA D 2 134 ? 3.399   165.678 26.248  1.00 36.63  ? 152 ALA D N    1 
ATOM   9490  C CA   . ALA D 2 134 ? 2.726   166.721 26.955  1.00 42.26  ? 152 ALA D CA   1 
ATOM   9491  C C    . ALA D 2 134 ? 1.541   166.218 27.763  1.00 41.56  ? 152 ALA D C    1 
ATOM   9492  O O    . ALA D 2 134 ? 1.351   166.632 28.898  1.00 36.44  ? 152 ALA D O    1 
ATOM   9493  C CB   . ALA D 2 134 ? 2.325   167.787 25.965  1.00 51.93  ? 152 ALA D CB   1 
ATOM   9494  N N    . VAL D 2 135 ? 0.733   165.352 27.181  1.00 34.79  ? 153 VAL D N    1 
ATOM   9495  C CA   . VAL D 2 135 ? -0.366  164.761 27.913  1.00 32.72  ? 153 VAL D CA   1 
ATOM   9496  C C    . VAL D 2 135 ? 0.009   163.864 29.093  1.00 41.50  ? 153 VAL D C    1 
ATOM   9497  O O    . VAL D 2 135 ? -0.602  163.960 30.143  1.00 52.14  ? 153 VAL D O    1 
ATOM   9498  C CB   . VAL D 2 135 ? -1.382  164.119 26.973  1.00 40.60  ? 153 VAL D CB   1 
ATOM   9499  C CG1  . VAL D 2 135 ? -2.486  163.403 27.724  1.00 41.45  ? 153 VAL D CG1  1 
ATOM   9500  C CG2  . VAL D 2 135 ? -1.963  165.173 26.060  1.00 47.99  ? 153 VAL D CG2  1 
ATOM   9501  N N    . LYS D 2 136 ? 0.995   162.989 28.943  1.00 38.59  ? 154 LYS D N    1 
ATOM   9502  C CA   . LYS D 2 136 ? 1.443   162.189 30.057  1.00 38.24  ? 154 LYS D CA   1 
ATOM   9503  C C    . LYS D 2 136 ? 2.815   162.586 30.409  1.00 39.98  ? 154 LYS D C    1 
ATOM   9504  O O    . LYS D 2 136 ? 3.753   162.241 29.710  1.00 38.60  ? 154 LYS D O    1 
ATOM   9505  C CB   . LYS D 2 136 ? 1.485   160.746 29.607  1.00 38.48  ? 154 LYS D CB   1 
ATOM   9506  C CG   . LYS D 2 136 ? 1.927   159.756 30.674  1.00 46.41  ? 154 LYS D CG   1 
ATOM   9507  C CD   . LYS D 2 136 ? 1.288   160.065 32.014  1.00 43.38  ? 154 LYS D CD   1 
ATOM   9508  C CE   . LYS D 2 136 ? 1.969   159.323 33.144  1.00 39.51  ? 154 LYS D CE   1 
ATOM   9509  N NZ   . LYS D 2 136 ? 1.692   159.998 34.437  1.00 48.57  ? 154 LYS D NZ   1 
ATOM   9510  N N    . PRO D 2 137 ? 2.963   163.308 31.506  1.00 49.17  ? 155 PRO D N    1 
ATOM   9511  C CA   . PRO D 2 137 ? 4.314   163.625 31.928  1.00 55.30  ? 155 PRO D CA   1 
ATOM   9512  C C    . PRO D 2 137 ? 5.222   162.536 32.509  1.00 55.20  ? 155 PRO D C    1 
ATOM   9513  O O    . PRO D 2 137 ? 6.370   162.539 32.081  1.00 72.75  ? 155 PRO D O    1 
ATOM   9514  C CB   . PRO D 2 137 ? 4.146   164.846 32.841  1.00 44.13  ? 155 PRO D CB   1 
ATOM   9515  C CG   . PRO D 2 137 ? 2.718   165.267 32.698  1.00 57.96  ? 155 PRO D CG   1 
ATOM   9516  C CD   . PRO D 2 137 ? 1.966   164.032 32.303  1.00 61.48  ? 155 PRO D CD   1 
ATOM   9517  N N    . GLU D 2 138 ? 4.792   161.592 33.343  1.00 32.60  ? 156 GLU D N    1 
ATOM   9518  C CA   . GLU D 2 138 ? 5.774   160.642 33.917  1.00 37.02  ? 156 GLU D CA   1 
ATOM   9519  C C    . GLU D 2 138 ? 6.147   159.339 33.183  1.00 46.51  ? 156 GLU D C    1 
ATOM   9520  O O    . GLU D 2 138 ? 5.671   158.271 33.519  1.00 52.14  ? 156 GLU D O    1 
ATOM   9521  C CB   . GLU D 2 138 ? 5.470   160.368 35.385  1.00 36.84  ? 156 GLU D CB   1 
ATOM   9522  C CG   . GLU D 2 138 ? 6.455   159.478 36.126  1.00 34.31  ? 156 GLU D CG   1 
ATOM   9523  C CD   . GLU D 2 138 ? 5.833   158.162 36.553  1.00 25.76  ? 156 GLU D CD   1 
ATOM   9524  O OE1  . GLU D 2 138 ? 4.593   158.042 36.553  1.00 14.36  ? 156 GLU D OE1  1 
ATOM   9525  O OE2  . GLU D 2 138 ? 6.591   157.242 36.885  1.00 28.62  ? 156 GLU D OE2  1 
ATOM   9526  N N    . TYR D 2 139 ? 7.055   159.409 32.225  1.00 48.80  ? 157 TYR D N    1 
ATOM   9527  C CA   . TYR D 2 139 ? 7.501   158.239 31.488  1.00 44.24  ? 157 TYR D CA   1 
ATOM   9528  C C    . TYR D 2 139 ? 8.705   158.711 30.698  1.00 47.45  ? 157 TYR D C    1 
ATOM   9529  O O    . TYR D 2 139 ? 8.955   159.903 30.636  1.00 44.60  ? 157 TYR D O    1 
ATOM   9530  C CB   . TYR D 2 139 ? 6.413   157.737 30.552  1.00 43.81  ? 157 TYR D CB   1 
ATOM   9531  C CG   . TYR D 2 139 ? 6.861   156.592 29.657  1.00 53.89  ? 157 TYR D CG   1 
ATOM   9532  C CD1  . TYR D 2 139 ? 7.309   155.400 30.190  1.00 52.71  ? 157 TYR D CD1  1 
ATOM   9533  C CD2  . TYR D 2 139 ? 6.862   156.719 28.284  1.00 58.23  ? 157 TYR D CD2  1 
ATOM   9534  C CE1  . TYR D 2 139 ? 7.732   154.372 29.377  1.00 53.97  ? 157 TYR D CE1  1 
ATOM   9535  C CE2  . TYR D 2 139 ? 7.281   155.693 27.462  1.00 62.00  ? 157 TYR D CE2  1 
ATOM   9536  C CZ   . TYR D 2 139 ? 7.719   154.519 28.017  1.00 56.84  ? 157 TYR D CZ   1 
ATOM   9537  O OH   . TYR D 2 139 ? 8.141   153.484 27.210  1.00 46.97  ? 157 TYR D OH   1 
ATOM   9538  N N    . ALA D 2 140 ? 9.466   157.805 30.106  1.00 44.14  ? 158 ALA D N    1 
ATOM   9539  C CA   . ALA D 2 140 ? 10.559  158.234 29.289  1.00 50.51  ? 158 ALA D CA   1 
ATOM   9540  C C    . ALA D 2 140 ? 9.958   158.928 28.118  1.00 57.85  ? 158 ALA D C    1 
ATOM   9541  O O    . ALA D 2 140 ? 9.161   158.357 27.410  1.00 56.55  ? 158 ALA D O    1 
ATOM   9542  C CB   . ALA D 2 140 ? 11.369  157.063 28.841  1.00 47.41  ? 158 ALA D CB   1 
ATOM   9543  N N    . VAL D 2 141 ? 10.415  160.129 27.826  1.00 58.06  ? 159 VAL D N    1 
ATOM   9544  C CA   . VAL D 2 141 ? 9.784   160.924 26.801  1.00 56.36  ? 159 VAL D CA   1 
ATOM   9545  C C    . VAL D 2 141 ? 9.733   160.345 25.422  1.00 67.52  ? 159 VAL D C    1 
ATOM   9546  O O    . VAL D 2 141 ? 10.729  159.809 24.946  1.00 74.54  ? 159 VAL D O    1 
ATOM   9547  C CB   . VAL D 2 141 ? 10.449  162.293 26.775  1.00 55.03  ? 159 VAL D CB   1 
ATOM   9548  C CG1  . VAL D 2 141 ? 10.029  163.103 27.986  1.00 69.46  ? 159 VAL D CG1  1 
ATOM   9549  C CG2  . VAL D 2 141 ? 11.960  162.149 26.749  1.00 55.68  ? 159 VAL D CG2  1 
ATOM   9550  N N    . THR D 2 142 ? 8.566   160.364 24.802  1.00 58.75  ? 160 THR D N    1 
ATOM   9551  C CA   . THR D 2 142 ? 8.469   159.934 23.416  1.00 49.68  ? 160 THR D CA   1 
ATOM   9552  C C    . THR D 2 142 ? 8.951   158.593 23.081  1.00 57.10  ? 160 THR D C    1 
ATOM   9553  O O    . THR D 2 142 ? 8.821   157.668 23.864  1.00 67.46  ? 160 THR D O    1 
ATOM   9554  C CB   . THR D 2 142 ? 9.179   160.977 22.533  1.00 54.13  ? 160 THR D CB   1 
ATOM   9555  O OG1  . THR D 2 142 ? 8.898   160.711 21.155  1.00 69.74  ? 160 THR D OG1  1 
ATOM   9556  C CG2  . THR D 2 142 ? 10.689  160.812 22.620  1.00 54.47  ? 160 THR D CG2  1 
ATOM   9557  N N    . HIS D 2 143 ? 9.535   158.470 21.911  1.00 54.18  ? 161 HIS D N    1 
ATOM   9558  C CA   . HIS D 2 143 ? 10.090  157.210 21.507  1.00 54.15  ? 161 HIS D CA   1 
ATOM   9559  C C    . HIS D 2 143 ? 11.595  157.220 21.620  1.00 64.33  ? 161 HIS D C    1 
ATOM   9560  O O    . HIS D 2 143 ? 12.222  156.201 21.349  1.00 65.83  ? 161 HIS D O    1 
ATOM   9561  C CB   . HIS D 2 143 ? 9.610   156.898 20.098  1.00 52.80  ? 161 HIS D CB   1 
ATOM   9562  C CG   . HIS D 2 143 ? 9.949   155.521 19.620  1.00 66.74  ? 161 HIS D CG   1 
ATOM   9563  N ND1  . HIS D 2 143 ? 10.840  155.290 18.597  1.00 64.77  ? 161 HIS D ND1  1 
ATOM   9564  C CD2  . HIS D 2 143 ? 9.524   154.303 20.032  1.00 59.79  ? 161 HIS D CD2  1 
ATOM   9565  C CE1  . HIS D 2 143 ? 10.950  153.990 18.397  1.00 58.25  ? 161 HIS D CE1  1 
ATOM   9566  N NE2  . HIS D 2 143 ? 10.164  153.368 19.256  1.00 57.66  ? 161 HIS D NE2  1 
ATOM   9567  N N    . GLU D 2 144 ? 12.175  158.334 22.081  1.00 66.13  ? 162 GLU D N    1 
ATOM   9568  C CA   . GLU D 2 144 ? 13.643  158.519 22.135  1.00 67.82  ? 162 GLU D CA   1 
ATOM   9569  C C    . GLU D 2 144 ? 14.191  158.751 20.741  1.00 67.92  ? 162 GLU D C    1 
ATOM   9570  O O    . GLU D 2 144 ? 15.330  159.175 20.591  1.00 71.46  ? 162 GLU D O    1 
ATOM   9571  C CB   . GLU D 2 144 ? 14.397  157.395 22.856  1.00 60.77  ? 162 GLU D CB   1 
ATOM   9572  C CG   . GLU D 2 144 ? 14.243  157.311 24.360  1.00 68.21  ? 162 GLU D CG   1 
ATOM   9573  C CD   . GLU D 2 144 ? 15.097  156.196 24.930  1.00 73.61  ? 162 GLU D CD   1 
ATOM   9574  O OE1  . GLU D 2 144 ? 15.814  155.542 24.144  1.00 57.03  ? 162 GLU D OE1  1 
ATOM   9575  O OE2  . GLU D 2 144 ? 15.057  155.971 26.155  1.00 73.25  ? 162 GLU D OE2  1 
ATOM   9576  N N    . THR D 2 145 ? 13.371  158.506 19.725  1.00 59.94  ? 163 THR D N    1 
ATOM   9577  C CA   . THR D 2 145 ? 13.752  158.640 18.359  1.00 64.51  ? 163 THR D CA   1 
ATOM   9578  C C    . THR D 2 145 ? 12.484  158.609 17.549  1.00 62.99  ? 163 THR D C    1 
ATOM   9579  O O    . THR D 2 145 ? 11.410  158.629 18.113  1.00 52.33  ? 163 THR D O    1 
ATOM   9580  C CB   . THR D 2 145 ? 14.718  157.567 17.864  1.00 68.41  ? 163 THR D CB   1 
ATOM   9581  O OG1  . THR D 2 145 ? 15.243  157.918 16.578  1.00 83.62  ? 163 THR D OG1  1 
ATOM   9582  C CG2  . THR D 2 145 ? 14.023  156.219 17.784  1.00 64.83  ? 163 THR D CG2  1 
ATOM   9583  N N    . GLU D 2 146 ? 12.586  158.561 16.233  1.00 62.18  ? 164 GLU D N    1 
ATOM   9584  C CA   . GLU D 2 146 ? 11.410  158.619 15.417  1.00 51.69  ? 164 GLU D CA   1 
ATOM   9585  C C    . GLU D 2 146 ? 10.769  157.337 15.136  1.00 47.55  ? 164 GLU D C    1 
ATOM   9586  O O    . GLU D 2 146 ? 11.341  156.289 15.336  1.00 49.96  ? 164 GLU D O    1 
ATOM   9587  C CB   . GLU D 2 146 ? 11.844  159.215 14.094  1.00 59.79  ? 164 GLU D CB   1 
ATOM   9588  C CG   . GLU D 2 146 ? 12.560  160.553 14.205  1.00 71.45  ? 164 GLU D CG   1 
ATOM   9589  C CD   . GLU D 2 146 ? 12.534  161.345 12.911  1.00 67.90  ? 164 GLU D CD   1 
ATOM   9590  O OE1  . GLU D 2 146 ? 11.602  161.144 12.104  1.00 57.13  ? 164 GLU D OE1  1 
ATOM   9591  O OE2  . GLU D 2 146 ? 13.448  162.170 12.697  1.00 63.96  ? 164 GLU D OE2  1 
ATOM   9592  N N    . ILE D 2 147 ? 9.563   157.414 14.633  1.00 43.17  ? 165 ILE D N    1 
ATOM   9593  C CA   . ILE D 2 147 ? 8.881   156.221 14.293  1.00 42.18  ? 165 ILE D CA   1 
ATOM   9594  C C    . ILE D 2 147 ? 9.231   156.029 12.862  1.00 40.20  ? 165 ILE D C    1 
ATOM   9595  O O    . ILE D 2 147 ? 8.791   156.788 12.018  1.00 43.31  ? 165 ILE D O    1 
ATOM   9596  C CB   . ILE D 2 147 ? 7.377   156.400 14.435  1.00 37.22  ? 165 ILE D CB   1 
ATOM   9597  C CG1  . ILE D 2 147 ? 7.033   156.935 15.823  1.00 32.16  ? 165 ILE D CG1  1 
ATOM   9598  C CG2  . ILE D 2 147 ? 6.667   155.095 14.189  1.00 43.59  ? 165 ILE D CG2  1 
ATOM   9599  C CD1  . ILE D 2 147 ? 7.244   155.946 16.938  1.00 35.54  ? 165 ILE D CD1  1 
ATOM   9600  N N    . LYS D 2 148 ? 10.023  155.010 12.576  1.00 39.58  ? 166 LYS D N    1 
ATOM   9601  C CA   . LYS D 2 148 ? 10.446  154.734 11.217  1.00 43.81  ? 166 LYS D CA   1 
ATOM   9602  C C    . LYS D 2 148 ? 9.679   153.566 10.672  1.00 36.96  ? 166 LYS D C    1 
ATOM   9603  O O    . LYS D 2 148 ? 9.325   153.547 9.504   1.00 31.36  ? 166 LYS D O    1 
ATOM   9604  C CB   . LYS D 2 148 ? 11.930  154.408 11.225  1.00 40.96  ? 166 LYS D CB   1 
ATOM   9605  C CG   . LYS D 2 148 ? 12.826  155.617 11.393  1.00 51.44  ? 166 LYS D CG   1 
ATOM   9606  C CD   . LYS D 2 148 ? 12.938  156.388 10.092  1.00 52.41  ? 166 LYS D CD   1 
ATOM   9607  C CE   . LYS D 2 148 ? 13.149  157.870 10.335  1.00 57.86  ? 166 LYS D CE   1 
ATOM   9608  N NZ   . LYS D 2 148 ? 11.857  158.571 10.561  1.00 57.62  ? 166 LYS D NZ   1 
ATOM   9609  N N    . THR D 2 149 ? 9.425   152.583 11.519  1.00 32.19  ? 167 THR D N    1 
ATOM   9610  C CA   . THR D 2 149 ? 8.686   151.417 11.132  1.00 27.69  ? 167 THR D CA   1 
ATOM   9611  C C    . THR D 2 149 ? 7.376   151.377 11.842  1.00 29.34  ? 167 THR D C    1 
ATOM   9612  O O    . THR D 2 149 ? 7.047   152.285 12.560  1.00 32.90  ? 167 THR D O    1 
ATOM   9613  C CB   . THR D 2 149 ? 9.459   150.154 11.469  1.00 29.01  ? 167 THR D CB   1 
ATOM   9614  O OG1  . THR D 2 149 ? 9.381   149.893 12.869  1.00 35.12  ? 167 THR D OG1  1 
ATOM   9615  C CG2  . THR D 2 149 ? 10.909  150.274 11.059  1.00 26.85  ? 167 THR D CG2  1 
ATOM   9616  N N    . LEU D 2 150 ? 6.607   150.324 11.634  1.00 27.75  ? 168 LEU D N    1 
ATOM   9617  C CA   . LEU D 2 150 ? 5.285   150.223 12.226  1.00 27.80  ? 168 LEU D CA   1 
ATOM   9618  C C    . LEU D 2 150 ? 5.328   149.273 13.353  1.00 30.42  ? 168 LEU D C    1 
ATOM   9619  O O    . LEU D 2 150 ? 4.325   148.957 13.958  1.00 33.62  ? 168 LEU D O    1 
ATOM   9620  C CB   . LEU D 2 150 ? 4.266   149.749 11.208  1.00 20.55  ? 168 LEU D CB   1 
ATOM   9621  C CG   . LEU D 2 150 ? 2.764   149.904 11.373  1.00 17.79  ? 168 LEU D CG   1 
ATOM   9622  C CD1  . LEU D 2 150 ? 2.240   151.009 10.485  1.00 21.28  ? 168 LEU D CD1  1 
ATOM   9623  C CD2  . LEU D 2 150 ? 2.192   148.566 10.965  1.00 20.74  ? 168 LEU D CD2  1 
ATOM   9624  N N    . ASP D 2 151 ? 6.506   148.804 13.673  1.00 26.45  ? 169 ASP D N    1 
ATOM   9625  C CA   . ASP D 2 151 ? 6.584   147.837 14.718  1.00 28.81  ? 169 ASP D CA   1 
ATOM   9626  C C    . ASP D 2 151 ? 7.108   148.615 15.841  1.00 30.18  ? 169 ASP D C    1 
ATOM   9627  O O    . ASP D 2 151 ? 7.131   148.145 16.950  1.00 39.40  ? 169 ASP D O    1 
ATOM   9628  C CB   . ASP D 2 151 ? 7.459   146.650 14.349  1.00 26.29  ? 169 ASP D CB   1 
ATOM   9629  C CG   . ASP D 2 151 ? 6.893   145.347 14.798  1.00 24.60  ? 169 ASP D CG   1 
ATOM   9630  O OD1  . ASP D 2 151 ? 6.804   145.128 16.015  1.00 29.13  ? 169 ASP D OD1  1 
ATOM   9631  O OD2  . ASP D 2 151 ? 6.556   144.532 13.927  1.00 23.24  ? 169 ASP D OD2  1 
ATOM   9632  N N    . GLU D 2 152 ? 7.522   149.827 15.583  1.00 27.09  ? 170 GLU D N    1 
ATOM   9633  C CA   . GLU D 2 152 ? 7.981   150.690 16.646  1.00 32.39  ? 170 GLU D CA   1 
ATOM   9634  C C    . GLU D 2 152 ? 6.947   151.730 16.792  1.00 30.81  ? 170 GLU D C    1 
ATOM   9635  O O    . GLU D 2 152 ? 7.116   152.694 17.516  1.00 31.16  ? 170 GLU D O    1 
ATOM   9636  C CB   . GLU D 2 152 ? 9.352   151.273 16.360  1.00 34.26  ? 170 GLU D CB   1 
ATOM   9637  C CG   . GLU D 2 152 ? 9.469   152.288 15.252  1.00 37.67  ? 170 GLU D CG   1 
ATOM   9638  C CD   . GLU D 2 152 ? 10.865  152.290 14.696  1.00 41.72  ? 170 GLU D CD   1 
ATOM   9639  O OE1  . GLU D 2 152 ? 11.433  151.196 14.556  1.00 37.10  ? 170 GLU D OE1  1 
ATOM   9640  O OE2  . GLU D 2 152 ? 11.403  153.369 14.419  1.00 44.40  ? 170 GLU D OE2  1 
ATOM   9641  N N    . ALA D 2 153 ? 5.846   151.525 16.096  1.00 28.36  ? 171 ALA D N    1 
ATOM   9642  C CA   . ALA D 2 153 ? 4.754   152.442 16.188  1.00 27.78  ? 171 ALA D CA   1 
ATOM   9643  C C    . ALA D 2 153 ? 3.878   151.734 17.087  1.00 29.62  ? 171 ALA D C    1 
ATOM   9644  O O    . ALA D 2 153 ? 3.111   152.331 17.761  1.00 35.47  ? 171 ALA D O    1 
ATOM   9645  C CB   . ALA D 2 153 ? 4.064   152.606 14.884  1.00 20.90  ? 171 ALA D CB   1 
ATOM   9646  N N    . LYS D 2 154 ? 3.999   150.431 17.128  1.00 23.29  ? 172 LYS D N    1 
ATOM   9647  C CA   . LYS D 2 154 ? 3.178   149.632 17.973  1.00 19.57  ? 172 LYS D CA   1 
ATOM   9648  C C    . LYS D 2 154 ? 3.736   149.894 19.271  1.00 23.54  ? 172 LYS D C    1 
ATOM   9649  O O    . LYS D 2 154 ? 3.055   149.944 20.210  1.00 25.99  ? 172 LYS D O    1 
ATOM   9650  C CB   . LYS D 2 154 ? 3.428   148.189 17.638  1.00 22.03  ? 172 LYS D CB   1 
ATOM   9651  C CG   . LYS D 2 154 ? 2.623   147.172 18.408  1.00 19.06  ? 172 LYS D CG   1 
ATOM   9652  C CD   . LYS D 2 154 ? 3.124   145.774 18.118  1.00 15.84  ? 172 LYS D CD   1 
ATOM   9653  C CE   . LYS D 2 154 ? 3.023   145.467 16.641  1.00 18.30  ? 172 LYS D CE   1 
ATOM   9654  N NZ   . LYS D 2 154 ? 2.344   144.167 16.425  1.00 19.32  ? 172 LYS D NZ   1 
ATOM   9655  N N    . GLN D 2 155 ? 5.015   150.126 19.339  1.00 26.88  ? 173 GLN D N    1 
ATOM   9656  C CA   . GLN D 2 155 ? 5.668   150.304 20.613  1.00 23.78  ? 173 GLN D CA   1 
ATOM   9657  C C    . GLN D 2 155 ? 5.220   151.540 21.259  1.00 23.36  ? 173 GLN D C    1 
ATOM   9658  O O    . GLN D 2 155 ? 5.043   151.563 22.437  1.00 27.64  ? 173 GLN D O    1 
ATOM   9659  C CB   . GLN D 2 155 ? 7.167   150.303 20.416  1.00 22.73  ? 173 GLN D CB   1 
ATOM   9660  C CG   . GLN D 2 155 ? 7.740   148.909 20.276  1.00 28.23  ? 173 GLN D CG   1 
ATOM   9661  C CD   . GLN D 2 155 ? 9.224   148.913 20.015  1.00 33.16  ? 173 GLN D CD   1 
ATOM   9662  O OE1  . GLN D 2 155 ? 9.871   149.956 20.066  1.00 30.25  ? 173 GLN D OE1  1 
ATOM   9663  N NE2  . GLN D 2 155 ? 9.775   147.743 19.730  1.00 28.23  ? 173 GLN D NE2  1 
ATOM   9664  N N    . PHE D 2 156 ? 5.014   152.587 20.506  1.00 29.14  ? 174 PHE D N    1 
ATOM   9665  C CA   . PHE D 2 156 ? 4.507   153.829 21.047  1.00 28.05  ? 174 PHE D CA   1 
ATOM   9666  C C    . PHE D 2 156 ? 3.111   153.620 21.520  1.00 27.88  ? 174 PHE D C    1 
ATOM   9667  O O    . PHE D 2 156 ? 2.818   153.893 22.656  1.00 29.74  ? 174 PHE D O    1 
ATOM   9668  C CB   . PHE D 2 156 ? 4.492   154.893 19.966  1.00 29.50  ? 174 PHE D CB   1 
ATOM   9669  C CG   . PHE D 2 156 ? 4.664   156.268 20.491  1.00 29.90  ? 174 PHE D CG   1 
ATOM   9670  C CD1  . PHE D 2 156 ? 5.789   156.595 21.202  1.00 33.17  ? 174 PHE D CD1  1 
ATOM   9671  C CD2  . PHE D 2 156 ? 3.706   157.224 20.275  1.00 25.29  ? 174 PHE D CD2  1 
ATOM   9672  C CE1  . PHE D 2 156 ? 5.958   157.854 21.700  1.00 37.30  ? 174 PHE D CE1  1 
ATOM   9673  C CE2  . PHE D 2 156 ? 3.864   158.487 20.773  1.00 29.35  ? 174 PHE D CE2  1 
ATOM   9674  C CZ   . PHE D 2 156 ? 4.991   158.801 21.487  1.00 38.96  ? 174 PHE D CZ   1 
ATOM   9675  N N    . ILE D 2 157 ? 2.236   153.181 20.651  1.00 24.92  ? 175 ILE D N    1 
ATOM   9676  C CA   . ILE D 2 157 ? 0.866   152.893 20.995  1.00 22.93  ? 175 ILE D CA   1 
ATOM   9677  C C    . ILE D 2 157 ? 0.758   151.985 22.211  1.00 28.24  ? 175 ILE D C    1 
ATOM   9678  O O    . ILE D 2 157 ? -0.205  152.014 22.949  1.00 29.95  ? 175 ILE D O    1 
ATOM   9679  C CB   . ILE D 2 157 ? 0.250   152.276 19.738  1.00 19.59  ? 175 ILE D CB   1 
ATOM   9680  C CG1  . ILE D 2 157 ? -0.245  153.377 18.823  1.00 25.34  ? 175 ILE D CG1  1 
ATOM   9681  C CG2  . ILE D 2 157 ? -0.835  151.249 20.005  1.00 24.00  ? 175 ILE D CG2  1 
ATOM   9682  C CD1  . ILE D 2 157 ? -1.242  154.268 19.496  1.00 34.47  ? 175 ILE D CD1  1 
ATOM   9683  N N    . LEU D 2 158 ? 1.774   151.184 22.459  1.00 26.08  ? 176 LEU D N    1 
ATOM   9684  C CA   . LEU D 2 158 ? 1.734   150.247 23.557  1.00 22.87  ? 176 LEU D CA   1 
ATOM   9685  C C    . LEU D 2 158 ? 2.565   150.797 24.692  1.00 27.28  ? 176 LEU D C    1 
ATOM   9686  O O    . LEU D 2 158 ? 3.110   150.045 25.488  1.00 28.32  ? 176 LEU D O    1 
ATOM   9687  C CB   . LEU D 2 158 ? 2.277   148.904 23.092  1.00 21.25  ? 176 LEU D CB   1 
ATOM   9688  C CG   . LEU D 2 158 ? 1.569   147.940 22.131  1.00 19.38  ? 176 LEU D CG   1 
ATOM   9689  C CD1  . LEU D 2 158 ? 1.949   146.491 22.356  1.00 21.15  ? 176 LEU D CD1  1 
ATOM   9690  C CD2  . LEU D 2 158 ? 0.075   148.090 22.062  1.00 12.14  ? 176 LEU D CD2  1 
ATOM   9691  N N    . SER D 2 159 ? 2.642   152.116 24.787  1.00 27.72  ? 177 SER D N    1 
ATOM   9692  C CA   . SER D 2 159 ? 3.387   152.778 25.825  1.00 23.40  ? 177 SER D CA   1 
ATOM   9693  C C    . SER D 2 159 ? 2.331   153.679 26.360  1.00 29.43  ? 177 SER D C    1 
ATOM   9694  O O    . SER D 2 159 ? 2.524   154.393 27.315  1.00 35.27  ? 177 SER D O    1 
ATOM   9695  C CB   . SER D 2 159 ? 4.585   153.533 25.274  1.00 19.14  ? 177 SER D CB   1 
ATOM   9696  O OG   . SER D 2 159 ? 4.295   154.867 24.940  1.00 29.77  ? 177 SER D OG   1 
ATOM   9697  N N    . PHE D 2 160 ? 1.173   153.646 25.743  1.00 23.39  ? 178 PHE D N    1 
ATOM   9698  C CA   . PHE D 2 160 ? 0.083   154.435 26.227  1.00 26.73  ? 178 PHE D CA   1 
ATOM   9699  C C    . PHE D 2 160 ? -0.570  153.573 27.269  1.00 35.70  ? 178 PHE D C    1 
ATOM   9700  O O    . PHE D 2 160 ? -1.721  153.780 27.603  1.00 36.54  ? 178 PHE D O    1 
ATOM   9701  C CB   . PHE D 2 160 ? -0.910  154.784 25.126  1.00 21.97  ? 178 PHE D CB   1 
ATOM   9702  C CG   . PHE D 2 160 ? -0.362  155.641 24.037  1.00 24.54  ? 178 PHE D CG   1 
ATOM   9703  C CD1  . PHE D 2 160 ? 0.931   156.108 24.066  1.00 28.14  ? 178 PHE D CD1  1 
ATOM   9704  C CD2  . PHE D 2 160 ? -1.161  155.978 22.977  1.00 21.00  ? 178 PHE D CD2  1 
ATOM   9705  C CE1  . PHE D 2 160 ? 1.425   156.890 23.055  1.00 25.05  ? 178 PHE D CE1  1 
ATOM   9706  C CE2  . PHE D 2 160 ? -0.679  156.762 21.963  1.00 24.42  ? 178 PHE D CE2  1 
ATOM   9707  C CZ   . PHE D 2 160 ? 0.618   157.217 22.002  1.00 27.28  ? 178 PHE D CZ   1 
ATOM   9708  N N    . VAL D 2 161 ? 0.119   152.537 27.737  1.00 35.93  ? 179 VAL D N    1 
ATOM   9709  C CA   . VAL D 2 161 ? -0.400  151.677 28.798  1.00 27.51  ? 179 VAL D CA   1 
ATOM   9710  C C    . VAL D 2 161 ? 0.245   152.149 30.020  1.00 25.56  ? 179 VAL D C    1 
ATOM   9711  O O    . VAL D 2 161 ? -0.245  151.930 31.093  1.00 31.29  ? 179 VAL D O    1 
ATOM   9712  C CB   . VAL D 2 161 ? 0.063   150.252 28.658  1.00 33.67  ? 179 VAL D CB   1 
ATOM   9713  C CG1  . VAL D 2 161 ? -0.790  149.323 29.510  1.00 24.92  ? 179 VAL D CG1  1 
ATOM   9714  C CG2  . VAL D 2 161 ? 0.018   149.833 27.199  1.00 41.53  ? 179 VAL D CG2  1 
ATOM   9715  N N    . MET D 2 162 ? 1.386   152.766 29.854  1.00 21.61  ? 180 MET D N    1 
ATOM   9716  C CA   . MET D 2 162 ? 2.087   153.311 30.966  1.00 25.57  ? 180 MET D CA   1 
ATOM   9717  C C    . MET D 2 162 ? 1.390   154.557 31.461  1.00 27.69  ? 180 MET D C    1 
ATOM   9718  O O    . MET D 2 162 ? 1.739   155.118 32.487  1.00 22.78  ? 180 MET D O    1 
ATOM   9719  C CB   . MET D 2 162 ? 3.510   153.599 30.537  1.00 27.42  ? 180 MET D CB   1 
ATOM   9720  C CG   . MET D 2 162 ? 4.479   152.460 30.740  1.00 31.79  ? 180 MET D CG   1 
ATOM   9721  S SD   . MET D 2 162 ? 4.871   152.294 32.481  1.00 50.15  ? 180 MET D SD   1 
ATOM   9722  C CE   . MET D 2 162 ? 5.549   153.912 32.812  1.00 27.76  ? 180 MET D CE   1 
ATOM   9723  N N    . LEU D 2 163 ? 0.411   155.007 30.715  1.00 31.54  ? 181 LEU D N    1 
ATOM   9724  C CA   . LEU D 2 163 ? -0.358  156.148 31.115  1.00 32.46  ? 181 LEU D CA   1 
ATOM   9725  C C    . LEU D 2 163 ? -1.516  155.462 31.680  1.00 30.78  ? 181 LEU D C    1 
ATOM   9726  O O    . LEU D 2 163 ? -2.416  155.090 30.953  1.00 37.11  ? 181 LEU D O    1 
ATOM   9727  C CB   . LEU D 2 163 ? -0.796  156.908 29.861  1.00 29.40  ? 181 LEU D CB   1 
ATOM   9728  C CG   . LEU D 2 163 ? -1.553  158.233 29.834  1.00 29.48  ? 181 LEU D CG   1 
ATOM   9729  C CD1  . LEU D 2 163 ? -1.362  158.859 28.468  1.00 27.73  ? 181 LEU D CD1  1 
ATOM   9730  C CD2  . LEU D 2 163 ? -3.031  158.075 30.131  1.00 32.87  ? 181 LEU D CD2  1 
ATOM   9731  N N    . ASN D 2 164 ? -1.515  155.256 32.974  1.00 25.94  ? 182 ASN D N    1 
ATOM   9732  C CA   . ASN D 2 164 ? -2.585  154.490 33.526  1.00 28.85  ? 182 ASN D CA   1 
ATOM   9733  C C    . ASN D 2 164 ? -2.858  154.693 34.979  1.00 33.29  ? 182 ASN D C    1 
ATOM   9734  O O    . ASN D 2 164 ? -1.932  154.897 35.745  1.00 27.56  ? 182 ASN D O    1 
ATOM   9735  C CB   . ASN D 2 164 ? -2.274  153.013 33.302  1.00 30.38  ? 182 ASN D CB   1 
ATOM   9736  C CG   . ASN D 2 164 ? -3.449  152.124 33.587  1.00 41.94  ? 182 ASN D CG   1 
ATOM   9737  O OD1  . ASN D 2 164 ? -4.585  152.518 33.407  1.00 49.24  ? 182 ASN D OD1  1 
ATOM   9738  N ND2  . ASN D 2 164 ? -3.182  150.913 34.017  1.00 36.49  ? 182 ASN D ND2  1 
ATOM   9739  N N    . ASP D 2 165 ? -4.123  154.675 35.362  1.00 31.69  ? 183 ASP D N    1 
ATOM   9740  C CA   . ASP D 2 165 ? -4.511  154.730 36.746  1.00 23.09  ? 183 ASP D CA   1 
ATOM   9741  C C    . ASP D 2 165 ? -4.382  156.121 37.253  1.00 26.03  ? 183 ASP D C    1 
ATOM   9742  O O    . ASP D 2 165 ? -4.710  156.399 38.385  1.00 34.84  ? 183 ASP D O    1 
ATOM   9743  C CB   . ASP D 2 165 ? -3.735  153.677 37.509  1.00 22.18  ? 183 ASP D CB   1 
ATOM   9744  C CG   . ASP D 2 165 ? -4.124  152.270 37.108  1.00 27.32  ? 183 ASP D CG   1 
ATOM   9745  O OD1  . ASP D 2 165 ? -5.321  152.031 36.866  1.00 25.35  ? 183 ASP D OD1  1 
ATOM   9746  O OD2  . ASP D 2 165 ? -3.238  151.402 37.035  1.00 24.10  ? 183 ASP D OD2  1 
ATOM   9747  N N    . ASN D 2 166 ? -3.952  157.024 36.394  1.00 32.24  ? 184 ASN D N    1 
ATOM   9748  C CA   . ASN D 2 166 ? -3.829  158.413 36.747  1.00 26.90  ? 184 ASN D CA   1 
ATOM   9749  C C    . ASN D 2 166 ? -4.596  159.223 35.722  1.00 35.90  ? 184 ASN D C    1 
ATOM   9750  O O    . ASN D 2 166 ? -5.757  159.537 35.949  1.00 38.28  ? 184 ASN D O    1 
ATOM   9751  C CB   . ASN D 2 166 ? -2.377  158.882 36.746  1.00 19.71  ? 184 ASN D CB   1 
ATOM   9752  C CG   . ASN D 2 166 ? -1.427  157.865 37.328  1.00 28.41  ? 184 ASN D CG   1 
ATOM   9753  O OD1  . ASN D 2 166 ? -1.663  157.322 38.399  1.00 29.37  ? 184 ASN D OD1  1 
ATOM   9754  N ND2  . ASN D 2 166 ? -0.325  157.619 36.627  1.00 27.64  ? 184 ASN D ND2  1 
ATOM   9755  N N    . VAL D 2 167 ? -4.013  159.492 34.561  1.00 28.51  ? 185 VAL D N    1 
ATOM   9756  C CA   . VAL D 2 167 ? -4.642  160.402 33.595  1.00 23.52  ? 185 VAL D CA   1 
ATOM   9757  C C    . VAL D 2 167 ? -5.970  160.008 32.968  1.00 27.13  ? 185 VAL D C    1 
ATOM   9758  O O    . VAL D 2 167 ? -6.683  160.855 32.472  1.00 25.34  ? 185 VAL D O    1 
ATOM   9759  C CB   . VAL D 2 167 ? -3.631  160.868 32.562  1.00 24.59  ? 185 VAL D CB   1 
ATOM   9760  C CG1  . VAL D 2 167 ? -4.309  161.706 31.499  1.00 32.35  ? 185 VAL D CG1  1 
ATOM   9761  C CG2  . VAL D 2 167 ? -2.539  161.667 33.247  1.00 29.19  ? 185 VAL D CG2  1 
ATOM   9762  N N    . GLU D 2 168 ? -6.278  158.729 32.931  1.00 27.78  ? 186 GLU D N    1 
ATOM   9763  C CA   . GLU D 2 168 ? -7.564  158.269 32.411  1.00 30.18  ? 186 GLU D CA   1 
ATOM   9764  C C    . GLU D 2 168 ? -8.658  157.987 33.388  1.00 27.96  ? 186 GLU D C    1 
ATOM   9765  O O    . GLU D 2 168 ? -9.746  157.630 32.986  1.00 23.85  ? 186 GLU D O    1 
ATOM   9766  C CB   . GLU D 2 168 ? -7.367  156.962 31.687  1.00 33.28  ? 186 GLU D CB   1 
ATOM   9767  C CG   . GLU D 2 168 ? -7.513  155.728 32.540  1.00 26.43  ? 186 GLU D CG   1 
ATOM   9768  C CD   . GLU D 2 168 ? -6.196  155.227 33.042  1.00 28.68  ? 186 GLU D CD   1 
ATOM   9769  O OE1  . GLU D 2 168 ? -5.201  155.952 32.904  1.00 24.67  ? 186 GLU D OE1  1 
ATOM   9770  O OE2  . GLU D 2 168 ? -6.161  154.108 33.566  1.00 38.22  ? 186 GLU D OE2  1 
ATOM   9771  N N    . LEU D 2 169 ? -8.379  158.101 34.669  1.00 31.31  ? 187 LEU D N    1 
ATOM   9772  C CA   . LEU D 2 169 ? -9.367  157.768 35.653  1.00 28.05  ? 187 LEU D CA   1 
ATOM   9773  C C    . LEU D 2 169 ? -10.524 158.713 35.498  1.00 30.97  ? 187 LEU D C    1 
ATOM   9774  O O    . LEU D 2 169 ? -11.667 158.315 35.672  1.00 27.63  ? 187 LEU D O    1 
ATOM   9775  C CB   . LEU D 2 169 ? -8.745  157.740 37.036  1.00 21.50  ? 187 LEU D CB   1 
ATOM   9776  C CG   . LEU D 2 169 ? -8.562  156.367 37.666  1.00 28.53  ? 187 LEU D CG   1 
ATOM   9777  C CD1  . LEU D 2 169 ? -7.859  156.515 39.000  1.00 37.47  ? 187 LEU D CD1  1 
ATOM   9778  C CD2  . LEU D 2 169 ? -9.909  155.690 37.848  1.00 23.63  ? 187 LEU D CD2  1 
ATOM   9779  N N    . PRO D 2 170 ? -10.244 159.982 35.212  1.00 33.49  ? 188 PRO D N    1 
ATOM   9780  C CA   . PRO D 2 170 ? -11.319 160.907 34.915  1.00 27.88  ? 188 PRO D CA   1 
ATOM   9781  C C    . PRO D 2 170 ? -12.207 160.424 33.795  1.00 30.05  ? 188 PRO D C    1 
ATOM   9782  O O    . PRO D 2 170 ? -13.407 160.545 33.935  1.00 34.08  ? 188 PRO D O    1 
ATOM   9783  C CB   . PRO D 2 170 ? -10.558 162.112 34.435  1.00 28.27  ? 188 PRO D CB   1 
ATOM   9784  C CG   . PRO D 2 170 ? -9.332  162.129 35.269  1.00 32.15  ? 188 PRO D CG   1 
ATOM   9785  C CD   . PRO D 2 170 ? -9.043  160.709 35.657  1.00 30.44  ? 188 PRO D CD   1 
ATOM   9786  N N    . LEU D 2 171 ? -11.652 159.898 32.707  1.00 29.86  ? 189 LEU D N    1 
ATOM   9787  C CA   . LEU D 2 171 ? -12.429 159.405 31.557  1.00 26.75  ? 189 LEU D CA   1 
ATOM   9788  C C    . LEU D 2 171 ? -13.068 158.063 31.715  1.00 24.64  ? 189 LEU D C    1 
ATOM   9789  O O    . LEU D 2 171 ? -13.913 157.681 30.953  1.00 29.15  ? 189 LEU D O    1 
ATOM   9790  C CB   . LEU D 2 171 ? -11.556 159.397 30.328  1.00 27.47  ? 189 LEU D CB   1 
ATOM   9791  C CG   . LEU D 2 171 ? -11.363 160.633 29.475  1.00 26.53  ? 189 LEU D CG   1 
ATOM   9792  C CD1  . LEU D 2 171 ? -10.616 161.678 30.290  1.00 38.20  ? 189 LEU D CD1  1 
ATOM   9793  C CD2  . LEU D 2 171 ? -10.570 160.245 28.244  1.00 30.22  ? 189 LEU D CD2  1 
ATOM   9794  N N    . LYS D 2 172 ? -12.666 157.338 32.724  1.00 22.32  ? 190 LYS D N    1 
ATOM   9795  C CA   . LYS D 2 172 ? -13.231 156.051 32.979  1.00 22.86  ? 190 LYS D CA   1 
ATOM   9796  C C    . LYS D 2 172 ? -14.486 156.213 33.755  1.00 29.64  ? 190 LYS D C    1 
ATOM   9797  O O    . LYS D 2 172 ? -15.278 155.289 33.887  1.00 27.94  ? 190 LYS D O    1 
ATOM   9798  C CB   . LYS D 2 172 ? -12.212 155.242 33.737  1.00 23.83  ? 190 LYS D CB   1 
ATOM   9799  C CG   . LYS D 2 172 ? -11.023 154.758 32.944  1.00 26.40  ? 190 LYS D CG   1 
ATOM   9800  C CD   . LYS D 2 172 ? -10.080 154.000 33.858  1.00 30.42  ? 190 LYS D CD   1 
ATOM   9801  C CE   . LYS D 2 172 ? -9.142  153.099 33.077  1.00 28.88  ? 190 LYS D CE   1 
ATOM   9802  N NZ   . LYS D 2 172 ? -8.341  152.240 33.989  1.00 39.14  ? 190 LYS D NZ   1 
ATOM   9803  N N    . ALA D 2 173 ? -14.658 157.396 34.323  1.00 34.01  ? 191 ALA D N    1 
ATOM   9804  C CA   . ALA D 2 173 ? -15.889 157.719 35.019  1.00 32.45  ? 191 ALA D CA   1 
ATOM   9805  C C    . ALA D 2 173 ? -16.449 158.314 33.806  1.00 38.88  ? 191 ALA D C    1 
ATOM   9806  O O    . ALA D 2 173 ? -15.707 158.596 32.895  1.00 36.95  ? 191 ALA D O    1 
ATOM   9807  C CB   . ALA D 2 173 ? -15.674 158.800 36.035  1.00 22.45  ? 191 ALA D CB   1 
ATOM   9808  N N    . GLN D 2 174 ? -17.742 158.504 33.752  1.00 33.70  ? 192 GLN D N    1 
ATOM   9809  C CA   . GLN D 2 174 ? -18.403 158.997 32.556  1.00 28.48  ? 192 GLN D CA   1 
ATOM   9810  C C    . GLN D 2 174 ? -18.644 157.883 31.603  1.00 31.81  ? 192 GLN D C    1 
ATOM   9811  O O    . GLN D 2 174 ? -19.315 158.001 30.607  1.00 44.57  ? 192 GLN D O    1 
ATOM   9812  C CB   . GLN D 2 174 ? -17.923 160.387 32.053  1.00 36.58  ? 192 GLN D CB   1 
ATOM   9813  C CG   . GLN D 2 174 ? -16.506 160.618 31.571  1.00 41.87  ? 192 GLN D CG   1 
ATOM   9814  C CD   . GLN D 2 174 ? -16.272 162.050 31.130  1.00 50.58  ? 192 GLN D CD   1 
ATOM   9815  O OE1  . GLN D 2 174 ? -17.013 162.947 31.508  1.00 54.35  ? 192 GLN D OE1  1 
ATOM   9816  N NE2  . GLN D 2 174 ? -15.242 162.267 30.324  1.00 43.63  ? 192 GLN D NE2  1 
ATOM   9817  N N    . SER D 2 175 ? -18.136 156.740 31.989  1.00 26.78  ? 193 SER D N    1 
ATOM   9818  C CA   . SER D 2 175 ? -18.387 155.571 31.232  1.00 26.45  ? 193 SER D CA   1 
ATOM   9819  C C    . SER D 2 175 ? -19.376 154.782 31.930  1.00 26.82  ? 193 SER D C    1 
ATOM   9820  O O    . SER D 2 175 ? -19.192 154.469 33.061  1.00 40.10  ? 193 SER D O    1 
ATOM   9821  C CB   . SER D 2 175 ? -17.170 154.756 31.206  1.00 30.52  ? 193 SER D CB   1 
ATOM   9822  O OG   . SER D 2 175 ? -17.463 153.516 30.614  1.00 37.62  ? 193 SER D OG   1 
ATOM   9823  N N    . GLU D 2 176 ? -20.443 154.428 31.274  1.00 25.60  ? 194 GLU D N    1 
ATOM   9824  C CA   . GLU D 2 176 ? -21.494 153.683 31.874  1.00 31.25  ? 194 GLU D CA   1 
ATOM   9825  C C    . GLU D 2 176 ? -21.199 152.220 31.764  1.00 32.38  ? 194 GLU D C    1 
ATOM   9826  O O    . GLU D 2 176 ? -21.986 151.409 32.210  1.00 29.42  ? 194 GLU D O    1 
ATOM   9827  C CB   . GLU D 2 176 ? -22.721 153.995 31.078  1.00 30.55  ? 194 GLU D CB   1 
ATOM   9828  C CG   . GLU D 2 176 ? -22.494 153.875 29.583  1.00 45.06  ? 194 GLU D CG   1 
ATOM   9829  C CD   . GLU D 2 176 ? -22.351 155.216 28.910  1.00 48.43  ? 194 GLU D CD   1 
ATOM   9830  O OE1  . GLU D 2 176 ? -23.320 155.987 28.951  1.00 65.46  ? 194 GLU D OE1  1 
ATOM   9831  O OE2  . GLU D 2 176 ? -21.275 155.502 28.348  1.00 38.45  ? 194 GLU D OE2  1 
ATOM   9832  N N    . ARG D 2 177 ? -20.047 151.868 31.194  1.00 34.19  ? 195 ARG D N    1 
ATOM   9833  C CA   . ARG D 2 177 ? -19.719 150.467 30.934  1.00 32.75  ? 195 ARG D CA   1 
ATOM   9834  C C    . ARG D 2 177 ? -18.470 149.895 31.533  1.00 27.19  ? 195 ARG D C    1 
ATOM   9835  O O    . ARG D 2 177 ? -18.411 148.720 31.784  1.00 26.80  ? 195 ARG D O    1 
ATOM   9836  C CB   . ARG D 2 177 ? -19.608 150.262 29.446  1.00 38.69  ? 195 ARG D CB   1 
ATOM   9837  C CG   . ARG D 2 177 ? -20.894 150.464 28.658  1.00 44.72  ? 195 ARG D CG   1 
ATOM   9838  C CD   . ARG D 2 177 ? -22.115 149.815 29.287  1.00 46.60  ? 195 ARG D CD   1 
ATOM   9839  N NE   . ARG D 2 177 ? -23.346 150.379 28.737  1.00 50.24  ? 195 ARG D NE   1 
ATOM   9840  C CZ   . ARG D 2 177 ? -24.422 150.693 29.451  1.00 47.35  ? 195 ARG D CZ   1 
ATOM   9841  N NH1  . ARG D 2 177 ? -24.439 150.496 30.757  1.00 37.49  ? 195 ARG D NH1  1 
ATOM   9842  N NH2  . ARG D 2 177 ? -25.488 151.201 28.855  1.00 48.16  ? 195 ARG D NH2  1 
ATOM   9843  N N    . TYR D 2 178 ? -17.444 150.702 31.696  1.00 26.38  ? 196 TYR D N    1 
ATOM   9844  C CA   . TYR D 2 178 ? -16.233 150.237 32.359  1.00 28.73  ? 196 TYR D CA   1 
ATOM   9845  C C    . TYR D 2 178 ? -16.459 149.909 33.778  1.00 31.15  ? 196 TYR D C    1 
ATOM   9846  O O    . TYR D 2 178 ? -15.674 149.181 34.369  1.00 35.55  ? 196 TYR D O    1 
ATOM   9847  C CB   . TYR D 2 178 ? -15.056 151.201 32.262  1.00 22.00  ? 196 TYR D CB   1 
ATOM   9848  C CG   . TYR D 2 178 ? -13.707 150.567 32.501  1.00 21.28  ? 196 TYR D CG   1 
ATOM   9849  C CD1  . TYR D 2 178 ? -13.489 149.226 32.229  1.00 26.66  ? 196 TYR D CD1  1 
ATOM   9850  C CD2  . TYR D 2 178 ? -12.659 151.302 33.008  1.00 21.11  ? 196 TYR D CD2  1 
ATOM   9851  C CE1  . TYR D 2 178 ? -12.262 148.640 32.457  1.00 22.46  ? 196 TYR D CE1  1 
ATOM   9852  C CE2  . TYR D 2 178 ? -11.432 150.720 33.242  1.00 19.76  ? 196 TYR D CE2  1 
ATOM   9853  C CZ   . TYR D 2 178 ? -11.244 149.393 32.962  1.00 20.65  ? 196 TYR D CZ   1 
ATOM   9854  O OH   . TYR D 2 178 ? -10.030 148.815 33.194  1.00 29.06  ? 196 TYR D OH   1 
ATOM   9855  N N    . PRO D 2 179 ? -17.487 150.532 34.452  1.00 30.72  ? 197 PRO D N    1 
ATOM   9856  C CA   . PRO D 2 179 ? -17.767 150.005 35.783  1.00 32.98  ? 197 PRO D CA   1 
ATOM   9857  C C    . PRO D 2 179 ? -18.229 148.604 35.687  1.00 25.99  ? 197 PRO D C    1 
ATOM   9858  O O    . PRO D 2 179 ? -18.248 147.868 36.653  1.00 23.69  ? 197 PRO D O    1 
ATOM   9859  C CB   . PRO D 2 179 ? -18.973 150.797 36.176  1.00 36.40  ? 197 PRO D CB   1 
ATOM   9860  C CG   . PRO D 2 179 ? -18.807 152.065 35.465  1.00 35.33  ? 197 PRO D CG   1 
ATOM   9861  C CD   . PRO D 2 179 ? -18.219 151.724 34.137  1.00 29.94  ? 197 PRO D CD   1 
ATOM   9862  N N    . LYS D 2 180 ? -18.596 148.215 34.498  1.00 18.60  ? 198 LYS D N    1 
ATOM   9863  C CA   . LYS D 2 180 ? -19.118 146.907 34.314  1.00 21.88  ? 198 LYS D CA   1 
ATOM   9864  C C    . LYS D 2 180 ? -18.087 146.061 33.656  1.00 22.32  ? 198 LYS D C    1 
ATOM   9865  O O    . LYS D 2 180 ? -18.246 145.634 32.537  1.00 27.15  ? 198 LYS D O    1 
ATOM   9866  C CB   . LYS D 2 180 ? -20.443 146.960 33.607  1.00 31.40  ? 198 LYS D CB   1 
ATOM   9867  C CG   . LYS D 2 180 ? -21.570 147.581 34.401  1.00 27.75  ? 198 LYS D CG   1 
ATOM   9868  C CD   . LYS D 2 180 ? -22.862 147.359 33.650  1.00 32.30  ? 198 LYS D CD   1 
ATOM   9869  C CE   . LYS D 2 180 ? -22.854 148.166 32.372  1.00 39.52  ? 198 LYS D CE   1 
ATOM   9870  N NZ   . LYS D 2 180 ? -24.150 148.081 31.650  1.00 49.07  ? 198 LYS D NZ   1 
ATOM   9871  N N    . LYS D 2 181 ? -17.008 145.813 34.365  1.00 26.47  ? 199 LYS D N    1 
ATOM   9872  C CA   . LYS D 2 181 ? -16.008 144.906 33.888  1.00 20.57  ? 199 LYS D CA   1 
ATOM   9873  C C    . LYS D 2 181 ? -16.174 143.541 34.496  1.00 28.08  ? 199 LYS D C    1 
ATOM   9874  O O    . LYS D 2 181 ? -16.575 143.429 35.636  1.00 37.50  ? 199 LYS D O    1 
ATOM   9875  C CB   . LYS D 2 181 ? -14.663 145.494 34.222  1.00 21.58  ? 199 LYS D CB   1 
ATOM   9876  C CG   . LYS D 2 181 ? -13.471 144.732 33.681  1.00 27.05  ? 199 LYS D CG   1 
ATOM   9877  C CD   . LYS D 2 181 ? -12.165 145.402 34.070  1.00 31.78  ? 199 LYS D CD   1 
ATOM   9878  C CE   . LYS D 2 181 ? -11.929 145.299 35.568  1.00 29.65  ? 199 LYS D CE   1 
ATOM   9879  N NZ   . LYS D 2 181 ? -11.741 143.893 36.002  1.00 25.97  ? 199 LYS D NZ   1 
ATOM   9880  N N    . ASP D 2 182 ? -15.913 142.483 33.759  1.00 25.51  ? 200 ASP D N    1 
ATOM   9881  C CA   . ASP D 2 182 ? -16.170 141.142 34.219  1.00 20.24  ? 200 ASP D CA   1 
ATOM   9882  C C    . ASP D 2 182 ? -14.891 140.462 34.529  1.00 20.58  ? 200 ASP D C    1 
ATOM   9883  O O    . ASP D 2 182 ? -14.792 139.264 34.456  1.00 25.64  ? 200 ASP D O    1 
ATOM   9884  C CB   . ASP D 2 182 ? -16.873 140.319 33.168  1.00 26.38  ? 200 ASP D CB   1 
ATOM   9885  C CG   . ASP D 2 182 ? -16.238 140.443 31.796  1.00 28.36  ? 200 ASP D CG   1 
ATOM   9886  O OD1  . ASP D 2 182 ? -16.638 141.319 31.015  1.00 24.52  ? 200 ASP D OD1  1 
ATOM   9887  O OD2  . ASP D 2 182 ? -15.345 139.644 31.484  1.00 32.82  ? 200 ASP D OD2  1 
ATOM   9888  N N    . ARG D 2 183 ? -13.902 141.203 34.945  1.00 16.68  ? 201 ARG D N    1 
ATOM   9889  C CA   . ARG D 2 183 ? -12.630 140.612 35.138  1.00 14.89  ? 201 ARG D CA   1 
ATOM   9890  C C    . ARG D 2 183 ? -12.458 140.168 36.521  1.00 18.60  ? 201 ARG D C    1 
ATOM   9891  O O    . ARG D 2 183 ? -13.360 140.272 37.319  1.00 23.26  ? 201 ARG D O    1 
ATOM   9892  C CB   . ARG D 2 183 ? -11.558 141.599 34.797  1.00 14.74  ? 201 ARG D CB   1 
ATOM   9893  C CG   . ARG D 2 183 ? -10.295 141.031 34.179  1.00 14.79  ? 201 ARG D CG   1 
ATOM   9894  C CD   . ARG D 2 183 ? -9.148  141.941 34.560  1.00 11.72  ? 201 ARG D CD   1 
ATOM   9895  N NE   . ARG D 2 183 ? -7.861  141.534 34.025  1.00 10.50  ? 201 ARG D NE   1 
ATOM   9896  C CZ   . ARG D 2 183 ? -7.256  142.166 33.034  1.00 14.54  ? 201 ARG D CZ   1 
ATOM   9897  N NH1  . ARG D 2 183 ? -7.844  143.202 32.468  1.00 13.66  ? 201 ARG D NH1  1 
ATOM   9898  N NH2  . ARG D 2 183 ? -6.079  141.756 32.603  1.00 13.56  ? 201 ARG D NH2  1 
ATOM   9899  N N    . SER D 2 184 ? -11.289 139.640 36.829  1.00 16.78  ? 202 SER D N    1 
ATOM   9900  C CA   . SER D 2 184 ? -11.044 139.109 38.109  1.00 16.80  ? 202 SER D CA   1 
ATOM   9901  C C    . SER D 2 184 ? -9.710  139.491 38.591  1.00 17.15  ? 202 SER D C    1 
ATOM   9902  O O    . SER D 2 184 ? -8.902  140.016 37.851  1.00 12.07  ? 202 SER D O    1 
ATOM   9903  C CB   . SER D 2 184 ? -11.071 137.619 38.016  1.00 21.77  ? 202 SER D CB   1 
ATOM   9904  O OG   . SER D 2 184 ? -12.388 137.138 37.905  1.00 25.60  ? 202 SER D OG   1 
ATOM   9905  N N    . ARG D 2 185 ? -9.472  139.245 39.867  1.00 17.06  ? 203 ARG D N    1 
ATOM   9906  C CA   . ARG D 2 185 ? -8.225  139.567 40.482  1.00 15.67  ? 203 ARG D CA   1 
ATOM   9907  C C    . ARG D 2 185 ? -7.830  138.317 41.117  1.00 21.56  ? 203 ARG D C    1 
ATOM   9908  O O    . ARG D 2 185 ? -7.052  138.328 42.044  1.00 30.30  ? 203 ARG D O    1 
ATOM   9909  C CB   . ARG D 2 185 ? -8.467  140.529 41.606  1.00 19.68  ? 203 ARG D CB   1 
ATOM   9910  C CG   . ARG D 2 185 ? -9.275  141.769 41.265  1.00 25.47  ? 203 ARG D CG   1 
ATOM   9911  C CD   . ARG D 2 185 ? -9.948  142.313 42.505  1.00 25.34  ? 203 ARG D CD   1 
ATOM   9912  N NE   . ARG D 2 185 ? -9.302  143.518 42.997  1.00 26.24  ? 203 ARG D NE   1 
ATOM   9913  C CZ   . ARG D 2 185 ? -9.947  144.523 43.574  1.00 31.05  ? 203 ARG D CZ   1 
ATOM   9914  N NH1  . ARG D 2 185 ? -11.256 144.473 43.729  1.00 32.06  ? 203 ARG D NH1  1 
ATOM   9915  N NH2  . ARG D 2 185 ? -9.285  145.589 43.986  1.00 32.40  ? 203 ARG D NH2  1 
ATOM   9916  N N    . GLU D 2 186 ? -8.345  137.207 40.609  1.00 18.70  ? 204 GLU D N    1 
ATOM   9917  C CA   . GLU D 2 186 ? -8.005  135.901 41.131  1.00 24.06  ? 204 GLU D CA   1 
ATOM   9918  C C    . GLU D 2 186 ? -6.604  135.703 40.783  1.00 27.42  ? 204 GLU D C    1 
ATOM   9919  O O    . GLU D 2 186 ? -5.968  134.795 41.278  1.00 41.84  ? 204 GLU D O    1 
ATOM   9920  C CB   . GLU D 2 186 ? -8.768  134.812 40.431  1.00 19.97  ? 204 GLU D CB   1 
ATOM   9921  C CG   . GLU D 2 186 ? -8.502  133.427 40.980  1.00 22.49  ? 204 GLU D CG   1 
ATOM   9922  C CD   . GLU D 2 186 ? -9.316  132.355 40.295  1.00 29.18  ? 204 GLU D CD   1 
ATOM   9923  O OE1  . GLU D 2 186 ? -10.066 132.681 39.357  1.00 47.13  ? 204 GLU D OE1  1 
ATOM   9924  O OE2  . GLU D 2 186 ? -9.220  131.187 40.708  1.00 24.18  ? 204 GLU D OE2  1 
ATOM   9925  N N    . GLU D 2 187 ? -6.104  136.539 39.917  1.00 20.87  ? 205 GLU D N    1 
ATOM   9926  C CA   . GLU D 2 187 ? -4.708  136.494 39.575  1.00 24.70  ? 205 GLU D CA   1 
ATOM   9927  C C    . GLU D 2 187 ? -4.092  135.207 39.170  1.00 28.86  ? 205 GLU D C    1 
ATOM   9928  O O    . GLU D 2 187 ? -3.126  134.774 39.779  1.00 27.34  ? 205 GLU D O    1 
ATOM   9929  C CB   . GLU D 2 187 ? -3.878  137.206 40.630  1.00 23.92  ? 205 GLU D CB   1 
ATOM   9930  C CG   . GLU D 2 187 ? -3.742  138.698 40.408  1.00 24.74  ? 205 GLU D CG   1 
ATOM   9931  C CD   . GLU D 2 187 ? -2.469  139.052 39.677  1.00 30.88  ? 205 GLU D CD   1 
ATOM   9932  O OE1  . GLU D 2 187 ? -1.596  138.171 39.552  1.00 30.88  ? 205 GLU D OE1  1 
ATOM   9933  O OE2  . GLU D 2 187 ? -2.333  140.209 39.238  1.00 35.97  ? 205 GLU D OE2  1 
ATOM   9934  N N    . LEU D 2 188 ? -4.669  134.556 38.180  1.00 29.51  ? 206 LEU D N    1 
ATOM   9935  C CA   . LEU D 2 188 ? -4.029  133.401 37.605  1.00 26.03  ? 206 LEU D CA   1 
ATOM   9936  C C    . LEU D 2 188 ? -2.879  134.036 36.821  1.00 22.40  ? 206 LEU D C    1 
ATOM   9937  O O    . LEU D 2 188 ? -2.994  135.170 36.376  1.00 23.97  ? 206 LEU D O    1 
ATOM   9938  C CB   . LEU D 2 188 ? -5.002  132.679 36.699  1.00 19.08  ? 206 LEU D CB   1 
ATOM   9939  C CG   . LEU D 2 188 ? -6.152  131.843 37.223  1.00 26.56  ? 206 LEU D CG   1 
ATOM   9940  C CD1  . LEU D 2 188 ? -5.831  131.334 38.616  1.00 46.41  ? 206 LEU D CD1  1 
ATOM   9941  C CD2  . LEU D 2 188 ? -7.428  132.656 37.211  1.00 28.49  ? 206 LEU D CD2  1 
ATOM   9942  N N    . GLY D 2 189 ? -1.785  133.337 36.609  1.00 17.17  ? 207 GLY D N    1 
ATOM   9943  C CA   . GLY D 2 189 ? -0.635  133.968 35.988  1.00 22.51  ? 207 GLY D CA   1 
ATOM   9944  C C    . GLY D 2 189 ? -0.090  133.287 34.783  1.00 23.95  ? 207 GLY D C    1 
ATOM   9945  O O    . GLY D 2 189 ? -0.369  132.141 34.635  1.00 39.60  ? 207 GLY D O    1 
ATOM   9946  N N    . ASN D 2 190 ? 0.860   133.848 34.060  1.00 15.28  ? 208 ASN D N    1 
ATOM   9947  C CA   . ASN D 2 190 ? 1.272   133.299 32.758  1.00 19.56  ? 208 ASN D CA   1 
ATOM   9948  C C    . ASN D 2 190 ? 1.423   131.785 32.456  1.00 20.09  ? 208 ASN D C    1 
ATOM   9949  O O    . ASN D 2 190 ? 1.952   131.055 33.269  1.00 19.38  ? 208 ASN D O    1 
ATOM   9950  C CB   . ASN D 2 190 ? 2.589   133.972 32.393  1.00 14.30  ? 208 ASN D CB   1 
ATOM   9951  C CG   . ASN D 2 190 ? 2.482   135.473 32.325  1.00 23.96  ? 208 ASN D CG   1 
ATOM   9952  O OD1  . ASN D 2 190 ? 1.494   136.062 32.753  1.00 26.15  ? 208 ASN D OD1  1 
ATOM   9953  N ND2  . ASN D 2 190 ? 3.514   136.106 31.786  1.00 24.93  ? 208 ASN D ND2  1 
ATOM   9954  N N    . THR D 2 191 ? 0.883   131.313 31.315  1.00 18.45  ? 209 THR D N    1 
ATOM   9955  C CA   . THR D 2 191 ? 0.984   129.911 30.859  1.00 16.51  ? 209 THR D CA   1 
ATOM   9956  C C    . THR D 2 191 ? 1.535   129.934 29.448  1.00 16.05  ? 209 THR D C    1 
ATOM   9957  O O    . THR D 2 191 ? 1.456   130.934 28.792  1.00 17.08  ? 209 THR D O    1 
ATOM   9958  C CB   . THR D 2 191 ? -0.377  129.205 30.779  1.00 19.43  ? 209 THR D CB   1 
ATOM   9959  O OG1  . THR D 2 191 ? -0.216  127.837 30.393  1.00 17.98  ? 209 THR D OG1  1 
ATOM   9960  C CG2  . THR D 2 191 ? -1.295  129.884 29.788  1.00 18.35  ? 209 THR D CG2  1 
ATOM   9961  N N    . PRO D 2 192 ? 2.157   128.846 28.988  1.00 18.96  ? 210 PRO D N    1 
ATOM   9962  C CA   . PRO D 2 192 ? 2.649   128.775 27.613  1.00 17.80  ? 210 PRO D CA   1 
ATOM   9963  C C    . PRO D 2 192 ? 1.611   128.684 26.510  1.00 16.33  ? 210 PRO D C    1 
ATOM   9964  O O    . PRO D 2 192 ? 0.609   128.051 26.717  1.00 23.72  ? 210 PRO D O    1 
ATOM   9965  C CB   . PRO D 2 192 ? 3.484   127.508 27.643  1.00 13.49  ? 210 PRO D CB   1 
ATOM   9966  C CG   . PRO D 2 192 ? 4.008   127.444 29.021  1.00 13.98  ? 210 PRO D CG   1 
ATOM   9967  C CD   . PRO D 2 192 ? 2.837   127.865 29.849  1.00 17.41  ? 210 PRO D CD   1 
ATOM   9968  N N    . SER D 2 193 ? 1.846   129.289 25.359  1.00 13.58  ? 211 SER D N    1 
ATOM   9969  C CA   . SER D 2 193 ? 0.929   129.155 24.248  1.00 19.66  ? 211 SER D CA   1 
ATOM   9970  C C    . SER D 2 193 ? 1.623   129.304 22.961  1.00 19.59  ? 211 SER D C    1 
ATOM   9971  O O    . SER D 2 193 ? 2.686   129.857 22.901  1.00 19.69  ? 211 SER D O    1 
ATOM   9972  C CB   . SER D 2 193 ? -0.124  130.209 24.287  1.00 17.85  ? 211 SER D CB   1 
ATOM   9973  O OG   . SER D 2 193 ? -0.922  130.242 23.127  1.00 21.44  ? 211 SER D OG   1 
ATOM   9974  N N    . ALA D 2 194 ? 0.977   128.871 21.908  1.00 17.91  ? 212 ALA D N    1 
ATOM   9975  C CA   . ALA D 2 194 ? 1.538   128.993 20.608  1.00 20.24  ? 212 ALA D CA   1 
ATOM   9976  C C    . ALA D 2 194 ? 0.416   129.398 19.705  1.00 21.19  ? 212 ALA D C    1 
ATOM   9977  O O    . ALA D 2 194 ? 0.645   129.899 18.630  1.00 22.36  ? 212 ALA D O    1 
ATOM   9978  C CB   . ALA D 2 194 ? 2.113   127.682 20.195  1.00 24.22  ? 212 ALA D CB   1 
ATOM   9979  N N    . ASN D 2 195 ? -0.806  129.192 20.154  1.00 18.17  ? 213 ASN D N    1 
ATOM   9980  C CA   . ASN D 2 195 ? -1.943  129.613 19.399  1.00 17.63  ? 213 ASN D CA   1 
ATOM   9981  C C    . ASN D 2 195 ? -1.807  131.105 19.371  1.00 23.87  ? 213 ASN D C    1 
ATOM   9982  O O    . ASN D 2 195 ? -1.526  131.699 20.384  1.00 26.31  ? 213 ASN D O    1 
ATOM   9983  C CB   . ASN D 2 195 ? -3.268  129.155 20.011  1.00 17.51  ? 213 ASN D CB   1 
ATOM   9984  C CG   . ASN D 2 195 ? -3.412  127.646 20.030  1.00 32.26  ? 213 ASN D CG   1 
ATOM   9985  O OD1  . ASN D 2 195 ? -3.771  127.058 21.049  1.00 44.60  ? 213 ASN D OD1  1 
ATOM   9986  N ND2  . ASN D 2 195 ? -3.134  127.012 18.897  1.00 28.00  ? 213 ASN D ND2  1 
ATOM   9987  N N    . PRO D 2 196 ? -2.013  131.739 18.222  1.00 24.08  ? 214 PRO D N    1 
ATOM   9988  C CA   . PRO D 2 196 ? -1.738  133.155 18.110  1.00 17.05  ? 214 PRO D CA   1 
ATOM   9989  C C    . PRO D 2 196 ? -2.769  134.122 18.602  1.00 23.88  ? 214 PRO D C    1 
ATOM   9990  O O    . PRO D 2 196 ? -3.926  133.776 18.693  1.00 26.85  ? 214 PRO D O    1 
ATOM   9991  C CB   . PRO D 2 196 ? -1.561  133.317 16.630  1.00 18.45  ? 214 PRO D CB   1 
ATOM   9992  C CG   . PRO D 2 196 ? -2.516  132.364 16.038  1.00 22.88  ? 214 PRO D CG   1 
ATOM   9993  C CD   . PRO D 2 196 ? -2.541  131.193 16.966  1.00 23.19  ? 214 PRO D CD   1 
ATOM   9994  N N    . GLY D 2 197 ? -2.357  135.330 18.960  1.00 21.71  ? 215 GLY D N    1 
ATOM   9995  C CA   . GLY D 2 197 ? -3.297  136.356 19.337  1.00 16.51  ? 215 GLY D CA   1 
ATOM   9996  C C    . GLY D 2 197 ? -4.235  136.040 20.434  1.00 18.81  ? 215 GLY D C    1 
ATOM   9997  O O    . GLY D 2 197 ? -3.803  135.635 21.490  1.00 19.01  ? 215 GLY D O    1 
ATOM   9998  N N    . ILE D 2 198 ? -5.517  136.284 20.219  1.00 16.38  ? 216 ILE D N    1 
ATOM   9999  C CA   . ILE D 2 198 ? -6.482  135.886 21.186  1.00 12.22  ? 216 ILE D CA   1 
ATOM   10000 C C    . ILE D 2 198 ? -7.075  134.628 20.732  1.00 20.65  ? 216 ILE D C    1 
ATOM   10001 O O    . ILE D 2 198 ? -7.856  134.633 19.839  1.00 39.32  ? 216 ILE D O    1 
ATOM   10002 C CB   . ILE D 2 198 ? -7.643  136.825 21.289  1.00 11.32  ? 216 ILE D CB   1 
ATOM   10003 C CG1  . ILE D 2 198 ? -8.049  137.425 19.958  1.00 20.01  ? 216 ILE D CG1  1 
ATOM   10004 C CG2  . ILE D 2 198 ? -7.301  137.895 22.287  1.00 20.06  ? 216 ILE D CG2  1 
ATOM   10005 C CD1  . ILE D 2 198 ? -9.548  137.372 19.766  1.00 23.80  ? 216 ILE D CD1  1 
ATOM   10006 N N    . MET D 2 199 ? -6.713  133.520 21.320  1.00 14.20  ? 217 MET D N    1 
ATOM   10007 C CA   . MET D 2 199 ? -7.268  132.260 20.973  1.00 13.93  ? 217 MET D CA   1 
ATOM   10008 C C    . MET D 2 199 ? -6.748  131.628 22.173  1.00 14.45  ? 217 MET D C    1 
ATOM   10009 O O    . MET D 2 199 ? -6.053  132.263 22.912  1.00 28.14  ? 217 MET D O    1 
ATOM   10010 C CB   . MET D 2 199 ? -6.570  131.659 19.778  1.00 23.99  ? 217 MET D CB   1 
ATOM   10011 C CG   . MET D 2 199 ? -7.119  131.934 18.402  1.00 18.46  ? 217 MET D CG   1 
ATOM   10012 S SD   . MET D 2 199 ? -6.257  130.886 17.232  1.00 11.11  ? 217 MET D SD   1 
ATOM   10013 C CE   . MET D 2 199 ? -6.769  129.289 17.819  1.00 16.13  ? 217 MET D CE   1 
ATOM   10014 N N    . LYS D 2 200 ? -7.043  130.385 22.408  1.00 11.39  ? 218 LYS D N    1 
ATOM   10015 C CA   . LYS D 2 200 ? -6.625  129.816 23.652  1.00 14.07  ? 218 LYS D CA   1 
ATOM   10016 C C    . LYS D 2 200 ? -5.395  128.895 23.590  1.00 15.70  ? 218 LYS D C    1 
ATOM   10017 O O    . LYS D 2 200 ? -5.279  128.164 22.647  1.00 21.10  ? 218 LYS D O    1 
ATOM   10018 C CB   . LYS D 2 200 ? -7.828  129.148 24.314  1.00 15.69  ? 218 LYS D CB   1 
ATOM   10019 C CG   . LYS D 2 200 ? -8.804  130.134 24.932  1.00 17.22  ? 218 LYS D CG   1 
ATOM   10020 C CD   . LYS D 2 200 ? -10.017 129.421 25.491  1.00 15.62  ? 218 LYS D CD   1 
ATOM   10021 C CE   . LYS D 2 200 ? -10.792 128.759 24.376  1.00 18.40  ? 218 LYS D CE   1 
ATOM   10022 N NZ   . LYS D 2 200 ? -11.625 127.619 24.836  1.00 20.64  ? 218 LYS D NZ   1 
ATOM   10023 N N    . PRO D 2 201 ? -4.468  128.920 24.593  1.00 16.53  ? 219 PRO D N    1 
ATOM   10024 C CA   . PRO D 2 201 ? -3.263  128.099 24.490  1.00 16.34  ? 219 PRO D CA   1 
ATOM   10025 C C    . PRO D 2 201 ? -3.432  126.663 24.197  1.00 15.76  ? 219 PRO D C    1 
ATOM   10026 O O    . PRO D 2 201 ? -2.595  126.059 23.554  1.00 16.95  ? 219 PRO D O    1 
ATOM   10027 C CB   . PRO D 2 201 ? -2.671  128.213 25.876  1.00 11.69  ? 219 PRO D CB   1 
ATOM   10028 C CG   . PRO D 2 201 ? -3.094  129.526 26.358  1.00 12.99  ? 219 PRO D CG   1 
ATOM   10029 C CD   . PRO D 2 201 ? -4.517  129.498 25.966  1.00 15.35  ? 219 PRO D CD   1 
ATOM   10030 N N    . ASN D 2 202 ? -4.498  126.092 24.684  1.00 12.57  ? 220 ASN D N    1 
ATOM   10031 C CA   . ASN D 2 202 ? -4.703  124.705 24.540  1.00 12.93  ? 220 ASN D CA   1 
ATOM   10032 C C    . ASN D 2 202 ? -5.913  124.493 23.690  1.00 15.18  ? 220 ASN D C    1 
ATOM   10033 O O    . ASN D 2 202 ? -6.789  123.741 24.049  1.00 20.26  ? 220 ASN D O    1 
ATOM   10034 C CB   . ASN D 2 202 ? -4.953  124.110 25.907  1.00 13.49  ? 220 ASN D CB   1 
ATOM   10035 C CG   . ASN D 2 202 ? -3.761  124.205 26.838  1.00 12.78  ? 220 ASN D CG   1 
ATOM   10036 O OD1  . ASN D 2 202 ? -2.917  123.329 26.866  1.00 12.37  ? 220 ASN D OD1  1 
ATOM   10037 N ND2  . ASN D 2 202 ? -3.721  125.246 27.640  1.00 13.58  ? 220 ASN D ND2  1 
ATOM   10038 N N    . SER D 2 203 ? -5.967  125.156 22.543  1.00 14.64  ? 221 SER D N    1 
ATOM   10039 C CA   . SER D 2 203 ? -7.082  125.032 21.641  1.00 16.41  ? 221 SER D CA   1 
ATOM   10040 C C    . SER D 2 203 ? -6.541  124.902 20.287  1.00 14.33  ? 221 SER D C    1 
ATOM   10041 O O    . SER D 2 203 ? -5.527  125.492 19.994  1.00 11.97  ? 221 SER D O    1 
ATOM   10042 C CB   . SER D 2 203 ? -8.061  126.197 21.747  1.00 19.09  ? 221 SER D CB   1 
ATOM   10043 O OG   . SER D 2 203 ? -7.484  127.427 21.374  1.00 18.79  ? 221 SER D OG   1 
ATOM   10044 N N    . PRO D 2 204 ? -7.246  124.127 19.397  1.00 16.11  ? 222 PRO D N    1 
ATOM   10045 C CA   . PRO D 2 204 ? -6.621  123.916 18.113  1.00 14.66  ? 222 PRO D CA   1 
ATOM   10046 C C    . PRO D 2 204 ? -6.249  125.080 17.302  1.00 20.85  ? 222 PRO D C    1 
ATOM   10047 O O    . PRO D 2 204 ? -6.864  126.112 17.365  1.00 28.50  ? 222 PRO D O    1 
ATOM   10048 C CB   . PRO D 2 204 ? -7.712  123.190 17.418  1.00 13.45  ? 222 PRO D CB   1 
ATOM   10049 C CG   . PRO D 2 204 ? -8.306  122.385 18.481  1.00 15.76  ? 222 PRO D CG   1 
ATOM   10050 C CD   . PRO D 2 204 ? -8.504  123.458 19.478  1.00 17.77  ? 222 PRO D CD   1 
ATOM   10051 N N    . ASN D 2 205 ? -5.236  124.914 16.486  1.00 22.08  ? 223 ASN D N    1 
ATOM   10052 C CA   . ASN D 2 205 ? -4.767  125.978 15.658  1.00 19.68  ? 223 ASN D CA   1 
ATOM   10053 C C    . ASN D 2 205 ? -4.243  125.283 14.443  1.00 20.45  ? 223 ASN D C    1 
ATOM   10054 O O    . ASN D 2 205 ? -4.045  124.074 14.451  1.00 16.40  ? 223 ASN D O    1 
ATOM   10055 C CB   . ASN D 2 205 ? -3.667  126.738 16.383  1.00 17.75  ? 223 ASN D CB   1 
ATOM   10056 C CG   . ASN D 2 205 ? -3.326  128.045 15.738  1.00 23.31  ? 223 ASN D CG   1 
ATOM   10057 O OD1  . ASN D 2 205 ? -2.165  128.397 15.634  1.00 23.43  ? 223 ASN D OD1  1 
ATOM   10058 N ND2  . ASN D 2 205 ? -4.332  128.773 15.305  1.00 28.13  ? 223 ASN D ND2  1 
ATOM   10059 N N    . PHE D 2 206 ? -4.020  126.025 13.385  1.00 21.21  ? 224 PHE D N    1 
ATOM   10060 C CA   . PHE D 2 206 ? -3.539  125.470 12.172  1.00 14.89  ? 224 PHE D CA   1 
ATOM   10061 C C    . PHE D 2 206 ? -2.065  125.517 12.317  1.00 16.03  ? 224 PHE D C    1 
ATOM   10062 O O    . PHE D 2 206 ? -1.543  126.349 13.009  1.00 20.72  ? 224 PHE D O    1 
ATOM   10063 C CB   . PHE D 2 206 ? -3.903  126.359 11.015  1.00 16.68  ? 224 PHE D CB   1 
ATOM   10064 C CG   . PHE D 2 206 ? -5.366  126.417 10.670  1.00 15.49  ? 224 PHE D CG   1 
ATOM   10065 C CD1  . PHE D 2 206 ? -6.311  125.690 11.346  1.00 18.22  ? 224 PHE D CD1  1 
ATOM   10066 C CD2  . PHE D 2 206 ? -5.785  127.216 9.642   1.00 19.12  ? 224 PHE D CD2  1 
ATOM   10067 C CE1  . PHE D 2 206 ? -7.642  125.762 11.003  1.00 13.67  ? 224 PHE D CE1  1 
ATOM   10068 C CE2  . PHE D 2 206 ? -7.110  127.279 9.296   1.00 15.97  ? 224 PHE D CE2  1 
ATOM   10069 C CZ   . PHE D 2 206 ? -8.039  126.553 9.975   1.00 11.83  ? 224 PHE D CZ   1 
ATOM   10070 N N    . THR D 2 207 ? -1.380  124.629 11.634  1.00 12.63  ? 225 THR D N    1 
ATOM   10071 C CA   . THR D 2 207 ? 0.048   124.547 11.706  1.00 13.22  ? 225 THR D CA   1 
ATOM   10072 C C    . THR D 2 207 ? 0.688   125.720 11.034  1.00 16.40  ? 225 THR D C    1 
ATOM   10073 O O    . THR D 2 207 ? 1.884   125.889 11.063  1.00 12.98  ? 225 THR D O    1 
ATOM   10074 C CB   . THR D 2 207 ? 0.442   123.242 11.069  1.00 11.18  ? 225 THR D CB   1 
ATOM   10075 O OG1  . THR D 2 207 ? -0.165  122.177 11.812  1.00 10.51  ? 225 THR D OG1  1 
ATOM   10076 C CG2  . THR D 2 207 ? 1.951   123.069 11.057  1.00 8.31   ? 225 THR D CG2  1 
ATOM   10077 N N    . ASP D 2 208 ? -0.122  126.558 10.424  1.00 17.66  ? 226 ASP D N    1 
ATOM   10078 C CA   . ASP D 2 208 ? 0.396   127.682 9.691   1.00 18.83  ? 226 ASP D CA   1 
ATOM   10079 C C    . ASP D 2 208 ? 0.058   129.027 10.301  1.00 25.82  ? 226 ASP D C    1 
ATOM   10080 O O    . ASP D 2 208 ? 0.452   130.060 9.774   1.00 24.46  ? 226 ASP D O    1 
ATOM   10081 C CB   . ASP D 2 208 ? -0.063  127.554 8.231   1.00 17.53  ? 226 ASP D CB   1 
ATOM   10082 C CG   . ASP D 2 208 ? -1.577  127.672 8.015   1.00 23.55  ? 226 ASP D CG   1 
ATOM   10083 O OD1  . ASP D 2 208 ? -2.341  128.105 8.884   1.00 27.15  ? 226 ASP D OD1  1 
ATOM   10084 O OD2  . ASP D 2 208 ? -2.016  127.347 6.900   1.00 23.53  ? 226 ASP D OD2  1 
ATOM   10085 N N    . ASN D 2 209 ? -0.662  129.016 11.418  1.00 22.55  ? 227 ASN D N    1 
ATOM   10086 C CA   . ASN D 2 209 ? -1.050  130.232 12.092  1.00 19.59  ? 227 ASN D CA   1 
ATOM   10087 C C    . ASN D 2 209 ? -0.229  130.311 13.337  1.00 17.70  ? 227 ASN D C    1 
ATOM   10088 O O    . ASN D 2 209 ? -0.013  131.367 13.873  1.00 17.63  ? 227 ASN D O    1 
ATOM   10089 C CB   . ASN D 2 209 ? -2.495  130.109 12.483  1.00 15.85  ? 227 ASN D CB   1 
ATOM   10090 C CG   . ASN D 2 209 ? -3.438  130.638 11.442  1.00 43.32  ? 227 ASN D CG   1 
ATOM   10091 O OD1  . ASN D 2 209 ? -4.610  130.864 11.728  1.00 49.13  ? 227 ASN D OD1  1 
ATOM   10092 N ND2  . ASN D 2 209 ? -2.946  130.836 10.227  1.00 55.70  ? 227 ASN D ND2  1 
ATOM   10093 N N    . LEU D 2 210 ? 0.253   129.190 13.802  1.00 20.02  ? 228 LEU D N    1 
ATOM   10094 C CA   . LEU D 2 210 ? 1.028   129.126 15.006  1.00 18.56  ? 228 LEU D CA   1 
ATOM   10095 C C    . LEU D 2 210 ? 2.103   130.153 14.952  1.00 21.63  ? 228 LEU D C    1 
ATOM   10096 O O    . LEU D 2 210 ? 2.754   130.319 13.932  1.00 20.88  ? 228 LEU D O    1 
ATOM   10097 C CB   . LEU D 2 210 ? 1.707   127.758 15.092  1.00 15.52  ? 228 LEU D CB   1 
ATOM   10098 C CG   . LEU D 2 210 ? 0.938   126.509 15.475  1.00 11.66  ? 228 LEU D CG   1 
ATOM   10099 C CD1  . LEU D 2 210 ? 1.897   125.346 15.416  1.00 12.74  ? 228 LEU D CD1  1 
ATOM   10100 C CD2  . LEU D 2 210 ? 0.394   126.645 16.875  1.00 19.20  ? 228 LEU D CD2  1 
ATOM   10101 N N    . VAL D 2 211 ? 2.354   130.812 16.074  1.00 23.85  ? 229 VAL D N    1 
ATOM   10102 C CA   . VAL D 2 211 ? 3.450   131.732 16.187  1.00 22.50  ? 229 VAL D CA   1 
ATOM   10103 C C    . VAL D 2 211 ? 4.326   131.068 17.168  1.00 16.37  ? 229 VAL D C    1 
ATOM   10104 O O    . VAL D 2 211 ? 3.925   130.063 17.722  1.00 14.03  ? 229 VAL D O    1 
ATOM   10105 C CB   . VAL D 2 211 ? 3.042   133.144 16.647  1.00 21.57  ? 229 VAL D CB   1 
ATOM   10106 C CG1  . VAL D 2 211 ? 2.434   133.096 18.041  1.00 16.67  ? 229 VAL D CG1  1 
ATOM   10107 C CG2  . VAL D 2 211 ? 4.238   134.083 16.612  1.00 27.61  ? 229 VAL D CG2  1 
ATOM   10108 N N    . PRO D 2 212 ? 5.564   131.579 17.417  1.00 12.89  ? 230 PRO D N    1 
ATOM   10109 C CA   . PRO D 2 212 ? 6.290   130.868 18.459  1.00 9.53   ? 230 PRO D CA   1 
ATOM   10110 C C    . PRO D 2 212 ? 5.809   130.777 19.879  1.00 11.70  ? 230 PRO D C    1 
ATOM   10111 O O    . PRO D 2 212 ? 4.937   131.514 20.279  1.00 16.90  ? 230 PRO D O    1 
ATOM   10112 C CB   . PRO D 2 212 ? 7.558   131.665 18.400  1.00 8.98   ? 230 PRO D CB   1 
ATOM   10113 C CG   . PRO D 2 212 ? 7.586   132.194 17.032  1.00 12.04  ? 230 PRO D CG   1 
ATOM   10114 C CD   . PRO D 2 212 ? 6.196   132.696 16.917  1.00 15.27  ? 230 PRO D CD   1 
ATOM   10115 N N    . VAL D 2 213 ? 6.403   129.905 20.674  1.00 10.84  ? 231 VAL D N    1 
ATOM   10116 C CA   . VAL D 2 213 ? 5.927   129.695 22.029  1.00 12.42  ? 231 VAL D CA   1 
ATOM   10117 C C    . VAL D 2 213 ? 6.293   130.807 22.913  1.00 13.59  ? 231 VAL D C    1 
ATOM   10118 O O    . VAL D 2 213 ? 7.456   131.146 23.049  1.00 12.10  ? 231 VAL D O    1 
ATOM   10119 C CB   . VAL D 2 213 ? 6.155   128.268 22.587  1.00 11.57  ? 231 VAL D CB   1 
ATOM   10120 C CG1  . VAL D 2 213 ? 7.527   127.743 22.226  1.00 10.80  ? 231 VAL D CG1  1 
ATOM   10121 C CG2  . VAL D 2 213 ? 5.871   128.156 24.069  1.00 11.30  ? 231 VAL D CG2  1 
ATOM   10122 N N    . ARG D 2 214 ? 5.274   131.418 23.486  1.00 23.34  ? 232 ARG D N    1 
ATOM   10123 C CA   . ARG D 2 214 ? 5.386   132.453 24.431  1.00 19.99  ? 232 ARG D CA   1 
ATOM   10124 C C    . ARG D 2 214 ? 4.513   132.232 25.580  1.00 24.57  ? 232 ARG D C    1 
ATOM   10125 O O    . ARG D 2 214 ? 3.551   131.506 25.462  1.00 25.86  ? 232 ARG D O    1 
ATOM   10126 C CB   . ARG D 2 214 ? 4.881   133.697 23.718  1.00 21.37  ? 232 ARG D CB   1 
ATOM   10127 C CG   . ARG D 2 214 ? 3.391   133.748 23.415  1.00 20.46  ? 232 ARG D CG   1 
ATOM   10128 C CD   . ARG D 2 214 ? 3.000   134.979 22.622  1.00 24.48  ? 232 ARG D CD   1 
ATOM   10129 N NE   . ARG D 2 214 ? 1.568   135.029 22.385  1.00 23.96  ? 232 ARG D NE   1 
ATOM   10130 C CZ   . ARG D 2 214 ? 0.961   134.381 21.404  1.00 36.80  ? 232 ARG D CZ   1 
ATOM   10131 N NH1  . ARG D 2 214 ? 1.673   133.647 20.579  1.00 52.80  ? 232 ARG D NH1  1 
ATOM   10132 N NH2  . ARG D 2 214 ? -0.347  134.474 21.248  1.00 37.21  ? 232 ARG D NH2  1 
ATOM   10133 N N    . ASP D 2 215 ? 4.831   132.813 26.713  1.00 21.63  ? 233 ASP D N    1 
ATOM   10134 C CA   . ASP D 2 215 ? 4.077   132.609 27.894  1.00 17.04  ? 233 ASP D CA   1 
ATOM   10135 C C    . ASP D 2 215 ? 3.119   133.725 27.855  1.00 14.80  ? 233 ASP D C    1 
ATOM   10136 O O    . ASP D 2 215 ? 3.495   134.872 27.854  1.00 15.38  ? 233 ASP D O    1 
ATOM   10137 C CB   . ASP D 2 215 ? 4.904   132.679 29.150  1.00 23.61  ? 233 ASP D CB   1 
ATOM   10138 C CG   . ASP D 2 215 ? 6.042   131.683 29.167  1.00 25.25  ? 233 ASP D CG   1 
ATOM   10139 O OD1  . ASP D 2 215 ? 5.981   130.667 28.451  1.00 22.72  ? 233 ASP D OD1  1 
ATOM   10140 O OD2  . ASP D 2 215 ? 7.003   131.916 29.921  1.00 26.77  ? 233 ASP D OD2  1 
ATOM   10141 N N    . VAL D 2 216 ? 1.853   133.398 27.823  1.00 15.22  ? 234 VAL D N    1 
ATOM   10142 C CA   . VAL D 2 216 ? 0.816   134.384 27.805  1.00 13.12  ? 234 VAL D CA   1 
ATOM   10143 C C    . VAL D 2 216 ? -0.017  134.336 29.061  1.00 13.59  ? 234 VAL D C    1 
ATOM   10144 O O    . VAL D 2 216 ? -0.105  133.331 29.711  1.00 15.09  ? 234 VAL D O    1 
ATOM   10145 C CB   . VAL D 2 216 ? -0.117  134.148 26.627  1.00 10.15  ? 234 VAL D CB   1 
ATOM   10146 C CG1  . VAL D 2 216 ? 0.583   134.428 25.328  1.00 21.27  ? 234 VAL D CG1  1 
ATOM   10147 C CG2  . VAL D 2 216 ? -0.735  132.769 26.656  1.00 13.04  ? 234 VAL D CG2  1 
ATOM   10148 N N    . PRO D 2 217 ? -0.702  135.462 29.406  1.00 11.26  ? 235 PRO D N    1 
ATOM   10149 C CA   . PRO D 2 217 ? -1.441  135.382 30.646  1.00 11.59  ? 235 PRO D CA   1 
ATOM   10150 C C    . PRO D 2 217 ? -2.672  134.598 30.792  1.00 11.99  ? 235 PRO D C    1 
ATOM   10151 O O    . PRO D 2 217 ? -3.297  134.210 29.827  1.00 15.35  ? 235 PRO D O    1 
ATOM   10152 C CB   . PRO D 2 217 ? -1.894  136.794 30.829  1.00 12.30  ? 235 PRO D CB   1 
ATOM   10153 C CG   . PRO D 2 217 ? -0.855  137.620 30.197  1.00 13.60  ? 235 PRO D CG   1 
ATOM   10154 C CD   . PRO D 2 217 ? -0.738  136.874 28.933  1.00 12.21  ? 235 PRO D CD   1 
ATOM   10155 N N    . LYS D 2 218 ? -3.049  134.381 32.039  1.00 14.22  ? 236 LYS D N    1 
ATOM   10156 C CA   . LYS D 2 218 ? -4.251  133.669 32.343  1.00 14.37  ? 236 LYS D CA   1 
ATOM   10157 C C    . LYS D 2 218 ? -5.231  134.534 33.093  1.00 13.62  ? 236 LYS D C    1 
ATOM   10158 O O    . LYS D 2 218 ? -4.978  134.920 34.203  1.00 19.55  ? 236 LYS D O    1 
ATOM   10159 C CB   . LYS D 2 218 ? -3.888  132.458 33.189  1.00 16.52  ? 236 LYS D CB   1 
ATOM   10160 C CG   . LYS D 2 218 ? -3.099  131.365 32.521  1.00 14.18  ? 236 LYS D CG   1 
ATOM   10161 C CD   . LYS D 2 218 ? -2.745  130.368 33.594  1.00 23.64  ? 236 LYS D CD   1 
ATOM   10162 C CE   . LYS D 2 218 ? -4.021  129.736 34.113  1.00 27.44  ? 236 LYS D CE   1 
ATOM   10163 N NZ   . LYS D 2 218 ? -3.767  128.651 35.093  1.00 39.99  ? 236 LYS D NZ   1 
ATOM   10164 N N    . ILE D 2 219 ? -6.318  134.910 32.464  1.00 10.75  ? 237 ILE D N    1 
ATOM   10165 C CA   . ILE D 2 219 ? -7.230  135.847 33.058  1.00 10.84  ? 237 ILE D CA   1 
ATOM   10166 C C    . ILE D 2 219 ? -8.603  135.256 33.027  1.00 12.82  ? 237 ILE D C    1 
ATOM   10167 O O    . ILE D 2 219 ? -9.028  134.727 32.016  1.00 14.68  ? 237 ILE D O    1 
ATOM   10168 C CB   . ILE D 2 219 ? -7.185  137.224 32.361  1.00 10.72  ? 237 ILE D CB   1 
ATOM   10169 C CG1  . ILE D 2 219 ? -5.821  137.878 32.500  1.00 10.41  ? 237 ILE D CG1  1 
ATOM   10170 C CG2  . ILE D 2 219 ? -8.251  138.156 32.900  1.00 12.94  ? 237 ILE D CG2  1 
ATOM   10171 C CD1  . ILE D 2 219 ? -5.345  138.519 31.224  1.00 14.32  ? 237 ILE D CD1  1 
ATOM   10172 N N    . ALA D 2 220 ? -9.331  135.368 34.125  1.00 12.23  ? 238 ALA D N    1 
ATOM   10173 C CA   . ALA D 2 220 ? -10.620 134.758 34.227  1.00 12.77  ? 238 ALA D CA   1 
ATOM   10174 C C    . ALA D 2 220 ? -11.795 135.663 34.319  1.00 16.00  ? 238 ALA D C    1 
ATOM   10175 O O    . ALA D 2 220 ? -11.671 136.861 34.285  1.00 23.76  ? 238 ALA D O    1 
ATOM   10176 C CB   . ALA D 2 220 ? -10.605 133.862 35.408  1.00 11.96  ? 238 ALA D CB   1 
ATOM   10177 N N    . ILE D 2 221 ? -12.964 135.074 34.435  1.00 13.86  ? 239 ILE D N    1 
ATOM   10178 C CA   . ILE D 2 221 ? -14.187 135.839 34.482  1.00 21.69  ? 239 ILE D CA   1 
ATOM   10179 C C    . ILE D 2 221 ? -14.931 135.815 35.823  1.00 31.69  ? 239 ILE D C    1 
ATOM   10180 O O    . ILE D 2 221 ? -15.171 134.746 36.392  1.00 23.81  ? 239 ILE D O    1 
ATOM   10181 C CB   . ILE D 2 221 ? -15.170 135.313 33.412  1.00 16.74  ? 239 ILE D CB   1 
ATOM   10182 C CG1  . ILE D 2 221 ? -14.491 135.146 32.062  1.00 20.55  ? 239 ILE D CG1  1 
ATOM   10183 C CG2  . ILE D 2 221 ? -16.373 136.216 33.290  1.00 16.77  ? 239 ILE D CG2  1 
ATOM   10184 C CD1  . ILE D 2 221 ? -15.354 134.458 31.034  1.00 25.31  ? 239 ILE D CD1  1 
ATOM   10185 N N    . ASN D 2 222 ? -15.263 136.989 36.355  1.00 26.36  ? 240 ASN D N    1 
ATOM   10186 C CA   . ASN D 2 222 ? -16.086 137.069 37.538  1.00 30.49  ? 240 ASN D CA   1 
ATOM   10187 C C    . ASN D 2 222 ? -17.483 136.928 37.056  1.00 27.11  ? 240 ASN D C    1 
ATOM   10188 O O    . ASN D 2 222 ? -18.002 137.786 36.374  1.00 23.82  ? 240 ASN D O    1 
ATOM   10189 C CB   . ASN D 2 222 ? -15.967 138.432 38.196  1.00 32.00  ? 240 ASN D CB   1 
ATOM   10190 C CG   . ASN D 2 222 ? -16.231 138.396 39.677  1.00 36.59  ? 240 ASN D CG   1 
ATOM   10191 O OD1  . ASN D 2 222 ? -15.630 137.615 40.408  1.00 41.29  ? 240 ASN D OD1  1 
ATOM   10192 N ND2  . ASN D 2 222 ? -17.123 139.256 40.130  1.00 34.49  ? 240 ASN D ND2  1 
ATOM   10193 N N    . GLU D 2 223 ? -18.114 135.836 37.435  1.00 32.45  ? 241 GLU D N    1 
ATOM   10194 C CA   . GLU D 2 223 ? -19.498 135.654 37.087  1.00 40.43  ? 241 GLU D CA   1 
ATOM   10195 C C    . GLU D 2 223 ? -20.456 135.954 38.192  1.00 40.09  ? 241 GLU D C    1 
ATOM   10196 O O    . GLU D 2 223 ? -21.286 135.129 38.550  1.00 34.41  ? 241 GLU D O    1 
ATOM   10197 C CB   . GLU D 2 223 ? -19.780 134.247 36.604  1.00 36.93  ? 241 GLU D CB   1 
ATOM   10198 C CG   . GLU D 2 223 ? -19.941 134.169 35.091  1.00 35.37  ? 241 GLU D CG   1 
ATOM   10199 C CD   . GLU D 2 223 ? -20.851 135.253 34.534  1.00 32.64  ? 241 GLU D CD   1 
ATOM   10200 O OE1  . GLU D 2 223 ? -22.069 135.197 34.791  1.00 41.71  ? 241 GLU D OE1  1 
ATOM   10201 O OE2  . GLU D 2 223 ? -20.360 136.157 33.829  1.00 28.15  ? 241 GLU D OE2  1 
ATOM   10202 N N    . LYS D 2 224 ? -20.348 137.158 38.724  1.00 37.39  ? 242 LYS D N    1 
ATOM   10203 C CA   . LYS D 2 224 ? -21.213 137.644 39.735  1.00 35.73  ? 242 LYS D CA   1 
ATOM   10204 C C    . LYS D 2 224 ? -21.187 139.162 39.596  1.00 35.92  ? 242 LYS D C    1 
ATOM   10205 O O    . LYS D 2 224 ? -21.271 139.946 40.520  1.00 41.27  ? 242 LYS D O    1 
ATOM   10206 C CB   . LYS D 2 224 ? -20.596 137.394 41.090  1.00 43.80  ? 242 LYS D CB   1 
ATOM   10207 C CG   . LYS D 2 224 ? -20.424 135.927 41.430  1.00 43.63  ? 242 LYS D CG   1 
ATOM   10208 C CD   . LYS D 2 224 ? -19.801 135.747 42.799  1.00 29.94  ? 242 LYS D CD   1 
ATOM   10209 C CE   . LYS D 2 224 ? -19.600 134.273 43.084  1.00 33.37  ? 242 LYS D CE   1 
ATOM   10210 N NZ   . LYS D 2 224 ? -20.906 133.563 43.123  1.00 26.29  ? 242 LYS D NZ   1 
ATOM   10211 N N    . VAL D 2 225 ? -21.102 139.567 38.341  1.00 37.99  ? 243 VAL D N    1 
ATOM   10212 C CA   . VAL D 2 225 ? -20.973 140.967 38.010  1.00 25.59  ? 243 VAL D CA   1 
ATOM   10213 C C    . VAL D 2 225 ? -22.347 141.325 37.553  1.00 28.06  ? 243 VAL D C    1 
ATOM   10214 O O    . VAL D 2 225 ? -23.148 140.461 37.249  1.00 36.28  ? 243 VAL D O    1 
ATOM   10215 C CB   . VAL D 2 225 ? -19.946 141.323 36.940  1.00 26.75  ? 243 VAL D CB   1 
ATOM   10216 C CG1  . VAL D 2 225 ? -20.369 140.805 35.581  1.00 38.42  ? 243 VAL D CG1  1 
ATOM   10217 C CG2  . VAL D 2 225 ? -19.618 142.806 36.917  1.00 26.38  ? 243 VAL D CG2  1 
ATOM   10218 N N    . ALA D 2 226 ? -22.645 142.602 37.552  1.00 27.82  ? 244 ALA D N    1 
ATOM   10219 C CA   . ALA D 2 226 ? -23.917 143.094 37.138  1.00 35.80  ? 244 ALA D CA   1 
ATOM   10220 C C    . ALA D 2 226 ? -23.976 143.363 35.662  1.00 45.13  ? 244 ALA D C    1 
ATOM   10221 O O    . ALA D 2 226 ? -23.905 144.507 35.253  1.00 46.91  ? 244 ALA D O    1 
ATOM   10222 C CB   . ALA D 2 226 ? -24.097 144.397 37.841  1.00 36.08  ? 244 ALA D CB   1 
ATOM   10223 N N    . GLY D 2 227 ? -24.127 142.333 34.847  1.00 42.86  ? 245 GLY D N    1 
ATOM   10224 C CA   . GLY D 2 227 ? -24.164 142.493 33.407  1.00 41.24  ? 245 GLY D CA   1 
ATOM   10225 C C    . GLY D 2 227 ? -22.984 143.150 32.756  1.00 35.17  ? 245 GLY D C    1 
ATOM   10226 O O    . GLY D 2 227 ? -23.128 143.947 31.869  1.00 39.54  ? 245 GLY D O    1 
ATOM   10227 N N    . GLY D 2 228 ? -21.808 142.850 33.220  1.00 29.05  ? 246 GLY D N    1 
ATOM   10228 C CA   . GLY D 2 228 ? -20.678 143.525 32.679  1.00 31.43  ? 246 GLY D CA   1 
ATOM   10229 C C    . GLY D 2 228 ? -19.989 142.896 31.529  1.00 38.89  ? 246 GLY D C    1 
ATOM   10230 O O    . GLY D 2 228 ? -18.843 142.605 31.675  1.00 57.21  ? 246 GLY D O    1 
ATOM   10231 N N    . TYR D 2 229 ? -20.655 142.636 30.431  1.00 33.08  ? 247 TYR D N    1 
ATOM   10232 C CA   . TYR D 2 229 ? -20.041 142.128 29.188  1.00 34.26  ? 247 TYR D CA   1 
ATOM   10233 C C    . TYR D 2 229 ? -19.756 140.683 28.913  1.00 28.20  ? 247 TYR D C    1 
ATOM   10234 O O    . TYR D 2 229 ? -19.439 140.352 27.795  1.00 30.82  ? 247 TYR D O    1 
ATOM   10235 C CB   . TYR D 2 229 ? -18.890 142.993 28.702  1.00 35.45  ? 247 TYR D CB   1 
ATOM   10236 C CG   . TYR D 2 229 ? -19.256 143.917 27.590  1.00 42.25  ? 247 TYR D CG   1 
ATOM   10237 C CD1  . TYR D 2 229 ? -20.080 144.991 27.823  1.00 52.92  ? 247 TYR D CD1  1 
ATOM   10238 C CD2  . TYR D 2 229 ? -18.777 143.720 26.307  1.00 39.47  ? 247 TYR D CD2  1 
ATOM   10239 C CE1  . TYR D 2 229 ? -20.431 145.847 26.810  1.00 65.53  ? 247 TYR D CE1  1 
ATOM   10240 C CE2  . TYR D 2 229 ? -19.121 144.576 25.284  1.00 43.87  ? 247 TYR D CE2  1 
ATOM   10241 C CZ   . TYR D 2 229 ? -19.952 145.638 25.549  1.00 63.53  ? 247 TYR D CZ   1 
ATOM   10242 O OH   . TYR D 2 229 ? -20.325 146.515 24.564  1.00 65.92  ? 247 TYR D OH   1 
ATOM   10243 N N    . SER D 2 230 ? -19.917 139.800 29.862  1.00 23.66  ? 248 SER D N    1 
ATOM   10244 C CA   . SER D 2 230 ? -19.726 138.422 29.511  1.00 26.39  ? 248 SER D CA   1 
ATOM   10245 C C    . SER D 2 230 ? -21.084 137.968 29.369  1.00 29.49  ? 248 SER D C    1 
ATOM   10246 O O    . SER D 2 230 ? -21.330 136.875 28.894  1.00 28.80  ? 248 SER D O    1 
ATOM   10247 C CB   . SER D 2 230 ? -19.021 137.635 30.590  1.00 29.75  ? 248 SER D CB   1 
ATOM   10248 O OG   . SER D 2 230 ? -17.617 137.700 30.442  1.00 23.63  ? 248 SER D OG   1 
ATOM   10249 N N    . LYS D 2 231 ? -21.998 138.792 29.843  1.00 32.56  ? 249 LYS D N    1 
ATOM   10250 C CA   . LYS D 2 231 ? -23.394 138.480 29.709  1.00 28.28  ? 249 LYS D CA   1 
ATOM   10251 C C    . LYS D 2 231 ? -24.074 139.502 28.855  1.00 23.04  ? 249 LYS D C    1 
ATOM   10252 O O    . LYS D 2 231 ? -24.996 139.195 28.142  1.00 24.65  ? 249 LYS D O    1 
ATOM   10253 C CB   . LYS D 2 231 ? -24.019 138.380 31.080  1.00 26.79  ? 249 LYS D CB   1 
ATOM   10254 C CG   . LYS D 2 231 ? -24.111 136.957 31.607  1.00 29.34  ? 249 LYS D CG   1 
ATOM   10255 C CD   . LYS D 2 231 ? -24.609 135.998 30.532  1.00 25.24  ? 249 LYS D CD   1 
ATOM   10256 C CE   . LYS D 2 231 ? -26.074 136.222 30.187  1.00 29.00  ? 249 LYS D CE   1 
ATOM   10257 N NZ   . LYS D 2 231 ? -26.366 135.860 28.776  1.00 17.58  ? 249 LYS D NZ   1 
ATOM   10258 N N    . THR D 2 232 ? -23.599 140.720 28.890  1.00 22.90  ? 250 THR D N    1 
ATOM   10259 C CA   . THR D 2 232 ? -24.135 141.720 28.023  1.00 29.49  ? 250 THR D CA   1 
ATOM   10260 C C    . THR D 2 232 ? -23.855 141.293 26.641  1.00 29.44  ? 250 THR D C    1 
ATOM   10261 O O    . THR D 2 232 ? -24.719 141.320 25.778  1.00 27.59  ? 250 THR D O    1 
ATOM   10262 C CB   . THR D 2 232 ? -23.436 143.058 28.237  1.00 28.33  ? 250 THR D CB   1 
ATOM   10263 O OG1  . THR D 2 232 ? -23.906 143.632 29.451  1.00 40.00  ? 250 THR D OG1  1 
ATOM   10264 C CG2  . THR D 2 232 ? -23.744 144.030 27.118  1.00 29.68  ? 250 THR D CG2  1 
ATOM   10265 N N    . LYS D 2 233 ? -22.630 140.898 26.407  1.00 31.42  ? 251 LYS D N    1 
ATOM   10266 C CA   . LYS D 2 233 ? -22.227 140.439 25.112  1.00 26.12  ? 251 LYS D CA   1 
ATOM   10267 C C    . LYS D 2 233 ? -21.679 139.085 25.284  1.00 20.54  ? 251 LYS D C    1 
ATOM   10268 O O    . LYS D 2 233 ? -20.504 138.938 25.496  1.00 23.32  ? 251 LYS D O    1 
ATOM   10269 C CB   . LYS D 2 233 ? -21.160 141.340 24.530  1.00 28.21  ? 251 LYS D CB   1 
ATOM   10270 C CG   . LYS D 2 233 ? -21.681 142.673 24.024  1.00 30.82  ? 251 LYS D CG   1 
ATOM   10271 C CD   . LYS D 2 233 ? -20.850 143.209 22.870  1.00 29.02  ? 251 LYS D CD   1 
ATOM   10272 C CE   . LYS D 2 233 ? -21.403 142.759 21.528  1.00 28.29  ? 251 LYS D CE   1 
ATOM   10273 N NZ   . LYS D 2 233 ? -20.895 143.613 20.421  1.00 22.01  ? 251 LYS D NZ   1 
ATOM   10274 N N    . PRO D 2 234 ? -22.538 138.086 25.221  1.00 17.09  ? 252 PRO D N    1 
ATOM   10275 C CA   . PRO D 2 234 ? -22.127 136.704 25.341  1.00 22.02  ? 252 PRO D CA   1 
ATOM   10276 C C    . PRO D 2 234 ? -21.310 136.318 24.141  1.00 25.20  ? 252 PRO D C    1 
ATOM   10277 O O    . PRO D 2 234 ? -20.559 135.367 24.188  1.00 24.58  ? 252 PRO D O    1 
ATOM   10278 C CB   . PRO D 2 234 ? -23.448 135.979 25.377  1.00 19.47  ? 252 PRO D CB   1 
ATOM   10279 C CG   . PRO D 2 234 ? -24.380 136.829 24.607  1.00 22.53  ? 252 PRO D CG   1 
ATOM   10280 C CD   . PRO D 2 234 ? -23.976 138.221 24.948  1.00 17.94  ? 252 PRO D CD   1 
ATOM   10281 N N    . THR D 2 235 ? -21.520 136.998 23.038  1.00 29.19  ? 253 THR D N    1 
ATOM   10282 C CA   . THR D 2 235 ? -20.816 136.744 21.808  1.00 23.89  ? 253 THR D CA   1 
ATOM   10283 C C    . THR D 2 235 ? -19.345 137.022 21.760  1.00 23.71  ? 253 THR D C    1 
ATOM   10284 O O    . THR D 2 235 ? -18.577 136.208 21.288  1.00 26.44  ? 253 THR D O    1 
ATOM   10285 C CB   . THR D 2 235 ? -21.453 137.649 20.743  1.00 19.48  ? 253 THR D CB   1 
ATOM   10286 O OG1  . THR D 2 235 ? -21.467 139.008 21.185  1.00 15.68  ? 253 THR D OG1  1 
ATOM   10287 C CG2  . THR D 2 235 ? -22.867 137.212 20.457  1.00 15.88  ? 253 THR D CG2  1 
ATOM   10288 N N    . THR D 2 236 ? -18.930 138.165 22.262  1.00 23.24  ? 254 THR D N    1 
ATOM   10289 C CA   . THR D 2 236 ? -17.558 138.542 22.181  1.00 25.16  ? 254 THR D CA   1 
ATOM   10290 C C    . THR D 2 236 ? -16.741 137.586 22.943  1.00 31.99  ? 254 THR D C    1 
ATOM   10291 O O    . THR D 2 236 ? -17.042 137.291 24.077  1.00 29.90  ? 254 THR D O    1 
ATOM   10292 C CB   . THR D 2 236 ? -17.366 139.867 22.847  1.00 32.17  ? 254 THR D CB   1 
ATOM   10293 O OG1  . THR D 2 236 ? -18.324 140.791 22.330  1.00 37.98  ? 254 THR D OG1  1 
ATOM   10294 C CG2  . THR D 2 236 ? -15.963 140.386 22.590  1.00 28.50  ? 254 THR D CG2  1 
ATOM   10295 N N    . PRO D 2 237 ? -15.658 137.125 22.343  1.00 34.24  ? 255 PRO D N    1 
ATOM   10296 C CA   . PRO D 2 237 ? -14.786 136.166 22.973  1.00 26.06  ? 255 PRO D CA   1 
ATOM   10297 C C    . PRO D 2 237 ? -13.723 136.977 23.522  1.00 30.11  ? 255 PRO D C    1 
ATOM   10298 O O    . PRO D 2 237 ? -13.022 137.625 22.773  1.00 36.83  ? 255 PRO D O    1 
ATOM   10299 C CB   . PRO D 2 237 ? -14.159 135.472 21.790  1.00 22.80  ? 255 PRO D CB   1 
ATOM   10300 C CG   . PRO D 2 237 ? -14.631 136.132 20.549  1.00 27.69  ? 255 PRO D CG   1 
ATOM   10301 C CD   . PRO D 2 237 ? -15.296 137.393 20.948  1.00 32.98  ? 255 PRO D CD   1 
ATOM   10302 N N    . PHE D 2 238 ? -13.512 136.950 24.807  1.00 23.41  ? 256 PHE D N    1 
ATOM   10303 C CA   . PHE D 2 238 ? -12.440 137.781 25.223  1.00 25.05  ? 256 PHE D CA   1 
ATOM   10304 C C    . PHE D 2 238 ? -11.641 137.388 26.395  1.00 25.34  ? 256 PHE D C    1 
ATOM   10305 O O    . PHE D 2 238 ? -12.090 136.622 27.226  1.00 29.29  ? 256 PHE D O    1 
ATOM   10306 C CB   . PHE D 2 238 ? -12.917 139.210 25.334  1.00 31.79  ? 256 PHE D CB   1 
ATOM   10307 C CG   . PHE D 2 238 ? -14.032 139.422 26.306  1.00 35.95  ? 256 PHE D CG   1 
ATOM   10308 C CD1  . PHE D 2 238 ? -13.764 139.679 27.626  1.00 29.36  ? 256 PHE D CD1  1 
ATOM   10309 C CD2  . PHE D 2 238 ? -15.345 139.412 25.887  1.00 35.12  ? 256 PHE D CD2  1 
ATOM   10310 C CE1  . PHE D 2 238 ? -14.787 139.888 28.518  1.00 32.21  ? 256 PHE D CE1  1 
ATOM   10311 C CE2  . PHE D 2 238 ? -16.371 139.621 26.771  1.00 29.31  ? 256 PHE D CE2  1 
ATOM   10312 C CZ   . PHE D 2 238 ? -16.090 139.860 28.091  1.00 28.96  ? 256 PHE D CZ   1 
ATOM   10313 N N    . VAL D 2 239 ? -10.440 137.935 26.457  1.00 22.86  ? 257 VAL D N    1 
ATOM   10314 C CA   . VAL D 2 239 ? -9.567  137.585 27.521  1.00 20.61  ? 257 VAL D CA   1 
ATOM   10315 C C    . VAL D 2 239 ? -9.651  138.396 28.794  1.00 28.33  ? 257 VAL D C    1 
ATOM   10316 O O    . VAL D 2 239 ? -9.976  137.846 29.828  1.00 38.22  ? 257 VAL D O    1 
ATOM   10317 C CB   . VAL D 2 239 ? -8.161  137.681 27.017  1.00 24.51  ? 257 VAL D CB   1 
ATOM   10318 C CG1  . VAL D 2 239 ? -7.919  139.010 26.321  1.00 22.68  ? 257 VAL D CG1  1 
ATOM   10319 C CG2  . VAL D 2 239 ? -7.162  137.395 28.126  1.00 21.36  ? 257 VAL D CG2  1 
ATOM   10320 N N    . ALA D 2 240 ? -9.447  139.698 28.746  1.00 25.64  ? 258 ALA D N    1 
ATOM   10321 C CA   . ALA D 2 240 ? -9.540  140.489 29.928  1.00 19.16  ? 258 ALA D CA   1 
ATOM   10322 C C    . ALA D 2 240 ? -10.417 141.596 29.604  1.00 26.06  ? 258 ALA D C    1 
ATOM   10323 O O    . ALA D 2 240 ? -9.905  142.528 29.085  1.00 38.44  ? 258 ALA D O    1 
ATOM   10324 C CB   . ALA D 2 240 ? -8.207  141.051 30.139  1.00 17.16  ? 258 ALA D CB   1 
ATOM   10325 N N    . SER D 2 241 ? -11.603 141.702 30.141  1.00 15.40  ? 259 SER D N    1 
ATOM   10326 C CA   . SER D 2 241 ? -12.562 142.671 29.661  1.00 19.60  ? 259 SER D CA   1 
ATOM   10327 C C    . SER D 2 241 ? -12.418 144.166 29.615  1.00 21.21  ? 259 SER D C    1 
ATOM   10328 O O    . SER D 2 241 ? -11.578 144.747 30.267  1.00 33.12  ? 259 SER D O    1 
ATOM   10329 C CB   . SER D 2 241 ? -13.852 142.409 30.440  1.00 23.91  ? 259 SER D CB   1 
ATOM   10330 O OG   . SER D 2 241 ? -14.861 143.338 30.086  1.00 32.58  ? 259 SER D OG   1 
ATOM   10331 N N    . LEU D 2 242 ? -13.132 144.778 28.718  1.00 15.63  ? 260 LEU D N    1 
ATOM   10332 C CA   . LEU D 2 242 ? -13.207 146.233 28.638  1.00 22.85  ? 260 LEU D CA   1 
ATOM   10333 C C    . LEU D 2 242 ? -12.029 147.107 28.552  1.00 23.53  ? 260 LEU D C    1 
ATOM   10334 O O    . LEU D 2 242 ? -12.073 148.227 29.012  1.00 31.17  ? 260 LEU D O    1 
ATOM   10335 C CB   . LEU D 2 242 ? -14.315 146.862 29.485  1.00 20.77  ? 260 LEU D CB   1 
ATOM   10336 C CG   . LEU D 2 242 ? -15.479 147.281 28.603  1.00 22.43  ? 260 LEU D CG   1 
ATOM   10337 C CD1  . LEU D 2 242 ? -16.217 146.054 28.093  1.00 34.65  ? 260 LEU D CD1  1 
ATOM   10338 C CD2  . LEU D 2 242 ? -16.407 148.191 29.371  1.00 24.89  ? 260 LEU D CD2  1 
ATOM   10339 N N    . SER D 2 243 ? -11.003 146.657 27.906  1.00 24.90  ? 261 SER D N    1 
ATOM   10340 C CA   . SER D 2 243 ? -9.873  147.501 27.667  1.00 30.86  ? 261 SER D CA   1 
ATOM   10341 C C    . SER D 2 243 ? -9.473  148.113 28.936  1.00 35.70  ? 261 SER D C    1 
ATOM   10342 O O    . SER D 2 243 ? -9.521  147.489 29.956  1.00 49.81  ? 261 SER D O    1 
ATOM   10343 C CB   . SER D 2 243 ? -10.111 148.474 26.571  1.00 25.26  ? 261 SER D CB   1 
ATOM   10344 O OG   . SER D 2 243 ? -8.980  149.302 26.408  1.00 33.21  ? 261 SER D OG   1 
ATOM   10345 N N    . GLY D 2 244 ? -9.140  149.354 28.942  1.00 28.85  ? 262 GLY D N    1 
ATOM   10346 C CA   . GLY D 2 244 ? -8.664  149.858 30.186  1.00 31.43  ? 262 GLY D CA   1 
ATOM   10347 C C    . GLY D 2 244 ? -7.698  150.874 29.795  1.00 35.11  ? 262 GLY D C    1 
ATOM   10348 O O    . GLY D 2 244 ? -7.543  151.866 30.480  1.00 35.93  ? 262 GLY D O    1 
ATOM   10349 N N    . THR D 2 245 ? -7.009  150.608 28.711  1.00 29.21  ? 263 THR D N    1 
ATOM   10350 C CA   . THR D 2 245 ? -6.159  151.629 28.181  1.00 22.48  ? 263 THR D CA   1 
ATOM   10351 C C    . THR D 2 245 ? -6.680  152.417 27.020  1.00 27.51  ? 263 THR D C    1 
ATOM   10352 O O    . THR D 2 245 ? -5.977  153.237 26.475  1.00 31.38  ? 263 THR D O    1 
ATOM   10353 C CB   . THR D 2 245 ? -4.800  151.054 27.830  1.00 27.44  ? 263 THR D CB   1 
ATOM   10354 O OG1  . THR D 2 245 ? -4.194  150.520 29.008  1.00 35.93  ? 263 THR D OG1  1 
ATOM   10355 C CG2  . THR D 2 245 ? -3.922  152.136 27.271  1.00 34.33  ? 263 THR D CG2  1 
ATOM   10356 N N    . THR D 2 246 ? -7.916  152.218 26.637  1.00 26.49  ? 264 THR D N    1 
ATOM   10357 C CA   . THR D 2 246 ? -8.472  152.989 25.566  1.00 26.29  ? 264 THR D CA   1 
ATOM   10358 C C    . THR D 2 246 ? -8.842  154.321 26.047  1.00 25.15  ? 264 THR D C    1 
ATOM   10359 O O    . THR D 2 246 ? -8.939  155.227 25.276  1.00 26.62  ? 264 THR D O    1 
ATOM   10360 C CB   . THR D 2 246 ? -9.761  152.406 25.110  1.00 24.73  ? 264 THR D CB   1 
ATOM   10361 O OG1  . THR D 2 246 ? -10.624 152.386 26.234  1.00 37.05  ? 264 THR D OG1  1 
ATOM   10362 C CG2  . THR D 2 246 ? -9.548  151.022 24.594  1.00 20.75  ? 264 THR D CG2  1 
ATOM   10363 N N    . TYR D 2 247 ? -9.049  154.453 27.337  1.00 24.11  ? 265 TYR D N    1 
ATOM   10364 C CA   . TYR D 2 247 ? -9.451  155.713 27.926  1.00 22.95  ? 265 TYR D CA   1 
ATOM   10365 C C    . TYR D 2 247 ? -8.199  156.486 28.053  1.00 22.95  ? 265 TYR D C    1 
ATOM   10366 O O    . TYR D 2 247 ? -8.254  157.669 28.248  1.00 24.58  ? 265 TYR D O    1 
ATOM   10367 C CB   . TYR D 2 247 ? -10.064 155.525 29.282  1.00 19.61  ? 265 TYR D CB   1 
ATOM   10368 C CG   . TYR D 2 247 ? -11.377 154.806 29.276  1.00 19.45  ? 265 TYR D CG   1 
ATOM   10369 C CD1  . TYR D 2 247 ? -12.520 155.425 28.828  1.00 17.93  ? 265 TYR D CD1  1 
ATOM   10370 C CD2  . TYR D 2 247 ? -11.481 153.511 29.739  1.00 21.45  ? 265 TYR D CD2  1 
ATOM   10371 C CE1  . TYR D 2 247 ? -13.729 154.777 28.837  1.00 18.12  ? 265 TYR D CE1  1 
ATOM   10372 C CE2  . TYR D 2 247 ? -12.690 152.861 29.756  1.00 20.23  ? 265 TYR D CE2  1 
ATOM   10373 C CZ   . TYR D 2 247 ? -13.810 153.506 29.306  1.00 18.45  ? 265 TYR D CZ   1 
ATOM   10374 O OH   . TYR D 2 247 ? -15.015 152.862 29.294  1.00 16.71  ? 265 TYR D OH   1 
ATOM   10375 N N    . SER D 2 248 ? -7.060  155.821 27.915  1.00 24.48  ? 266 SER D N    1 
ATOM   10376 C CA   . SER D 2 248 ? -5.766  156.464 27.994  1.00 22.06  ? 266 SER D CA   1 
ATOM   10377 C C    . SER D 2 248 ? -5.262  156.788 26.614  1.00 21.39  ? 266 SER D C    1 
ATOM   10378 O O    . SER D 2 248 ? -4.304  157.512 26.466  1.00 25.40  ? 266 SER D O    1 
ATOM   10379 C CB   . SER D 2 248 ? -4.812  155.553 28.720  1.00 24.74  ? 266 SER D CB   1 
ATOM   10380 O OG   . SER D 2 248 ? -5.447  154.878 29.779  1.00 26.19  ? 266 SER D OG   1 
ATOM   10381 N N    . LEU D 2 249 ? -5.873  156.230 25.585  1.00 20.23  ? 267 LEU D N    1 
ATOM   10382 C CA   . LEU D 2 249 ? -5.524  156.594 24.220  1.00 23.40  ? 267 LEU D CA   1 
ATOM   10383 C C    . LEU D 2 249 ? -6.158  157.910 24.015  1.00 27.95  ? 267 LEU D C    1 
ATOM   10384 O O    . LEU D 2 249 ? -5.544  158.802 23.503  1.00 24.42  ? 267 LEU D O    1 
ATOM   10385 C CB   . LEU D 2 249 ? -6.113  155.639 23.200  1.00 16.46  ? 267 LEU D CB   1 
ATOM   10386 C CG   . LEU D 2 249 ? -5.928  155.902 21.716  1.00 15.70  ? 267 LEU D CG   1 
ATOM   10387 C CD1  . LEU D 2 249 ? -4.476  156.059 21.323  1.00 13.53  ? 267 LEU D CD1  1 
ATOM   10388 C CD2  . LEU D 2 249 ? -6.611  154.835 20.891  1.00 17.30  ? 267 LEU D CD2  1 
ATOM   10389 N N    . MET D 2 250 ? -7.406  158.045 24.435  1.00 29.38  ? 268 MET D N    1 
ATOM   10390 C CA   . MET D 2 250 ? -8.141  159.269 24.271  1.00 24.84  ? 268 MET D CA   1 
ATOM   10391 C C    . MET D 2 250 ? -7.582  160.453 25.021  1.00 31.18  ? 268 MET D C    1 
ATOM   10392 O O    . MET D 2 250 ? -7.969  161.551 24.766  1.00 30.30  ? 268 MET D O    1 
ATOM   10393 C CB   . MET D 2 250 ? -9.562  159.016 24.653  1.00 25.00  ? 268 MET D CB   1 
ATOM   10394 C CG   . MET D 2 250 ? -10.118 157.725 24.122  1.00 24.79  ? 268 MET D CG   1 
ATOM   10395 S SD   . MET D 2 250 ? -10.303 157.721 22.349  1.00 41.87  ? 268 MET D SD   1 
ATOM   10396 C CE   . MET D 2 250 ? -11.365 159.141 22.186  1.00 40.28  ? 268 MET D CE   1 
ATOM   10397 N N    . VAL D 2 251 ? -6.661  160.254 25.945  1.00 30.08  ? 269 VAL D N    1 
ATOM   10398 C CA   . VAL D 2 251 ? -6.024  161.350 26.632  1.00 23.89  ? 269 VAL D CA   1 
ATOM   10399 C C    . VAL D 2 251 ? -5.011  161.905 25.682  1.00 32.85  ? 269 VAL D C    1 
ATOM   10400 O O    . VAL D 2 251 ? -4.880  163.103 25.550  1.00 38.99  ? 269 VAL D O    1 
ATOM   10401 C CB   . VAL D 2 251 ? -5.342  160.865 27.881  1.00 21.97  ? 269 VAL D CB   1 
ATOM   10402 C CG1  . VAL D 2 251 ? -4.689  161.999 28.639  1.00 26.47  ? 269 VAL D CG1  1 
ATOM   10403 C CG2  . VAL D 2 251 ? -6.344  160.180 28.769  1.00 29.81  ? 269 VAL D CG2  1 
ATOM   10404 N N    . VAL D 2 252 ? -4.299  161.040 24.976  1.00 36.89  ? 270 VAL D N    1 
ATOM   10405 C CA   . VAL D 2 252 ? -3.283  161.456 24.009  1.00 32.70  ? 270 VAL D CA   1 
ATOM   10406 C C    . VAL D 2 252 ? -3.981  161.940 22.789  1.00 29.94  ? 270 VAL D C    1 
ATOM   10407 O O    . VAL D 2 252 ? -3.702  162.990 22.276  1.00 30.35  ? 270 VAL D O    1 
ATOM   10408 C CB   . VAL D 2 252 ? -2.410  160.256 23.636  1.00 24.54  ? 270 VAL D CB   1 
ATOM   10409 C CG1  . VAL D 2 252 ? -1.384  160.615 22.593  1.00 25.25  ? 270 VAL D CG1  1 
ATOM   10410 C CG2  . VAL D 2 252 ? -1.733  159.693 24.862  1.00 28.26  ? 270 VAL D CG2  1 
ATOM   10411 N N    . LEU D 2 253 ? -4.928  161.175 22.324  1.00 25.82  ? 271 LEU D N    1 
ATOM   10412 C CA   . LEU D 2 253 ? -5.598  161.517 21.112  1.00 31.20  ? 271 LEU D CA   1 
ATOM   10413 C C    . LEU D 2 253 ? -6.313  162.823 21.255  1.00 34.93  ? 271 LEU D C    1 
ATOM   10414 O O    . LEU D 2 253 ? -6.271  163.597 20.357  1.00 37.04  ? 271 LEU D O    1 
ATOM   10415 C CB   . LEU D 2 253 ? -6.552  160.391 20.698  1.00 25.10  ? 271 LEU D CB   1 
ATOM   10416 C CG   . LEU D 2 253 ? -6.112  159.361 19.675  1.00 22.95  ? 271 LEU D CG   1 
ATOM   10417 C CD1  . LEU D 2 253 ? -7.335  158.623 19.177  1.00 18.37  ? 271 LEU D CD1  1 
ATOM   10418 C CD2  . LEU D 2 253 ? -5.395  160.039 18.527  1.00 35.64  ? 271 LEU D CD2  1 
ATOM   10419 N N    . THR D 2 254 ? -6.968  163.105 22.374  1.00 33.27  ? 272 THR D N    1 
ATOM   10420 C CA   . THR D 2 254 ? -7.787  164.330 22.473  1.00 38.39  ? 272 THR D CA   1 
ATOM   10421 C C    . THR D 2 254 ? -7.027  165.598 22.316  1.00 35.82  ? 272 THR D C    1 
ATOM   10422 O O    . THR D 2 254 ? -7.406  166.428 21.543  1.00 41.22  ? 272 THR D O    1 
ATOM   10423 C CB   . THR D 2 254 ? -8.682  164.370 23.724  1.00 39.55  ? 272 THR D CB   1 
ATOM   10424 O OG1  . THR D 2 254 ? -9.689  163.356 23.624  1.00 38.47  ? 272 THR D OG1  1 
ATOM   10425 C CG2  . THR D 2 254 ? -9.369  165.708 23.892  1.00 35.72  ? 272 THR D CG2  1 
ATOM   10426 N N    . ASP D 2 255 ? -5.923  165.739 23.011  1.00 29.92  ? 273 ASP D N    1 
ATOM   10427 C CA   . ASP D 2 255 ? -5.074  166.891 22.829  1.00 41.56  ? 273 ASP D CA   1 
ATOM   10428 C C    . ASP D 2 255 ? -4.448  166.894 21.452  1.00 46.75  ? 273 ASP D C    1 
ATOM   10429 O O    . ASP D 2 255 ? -4.311  167.928 20.866  1.00 46.71  ? 273 ASP D O    1 
ATOM   10430 C CB   . ASP D 2 255 ? -3.979  166.910 23.859  1.00 35.14  ? 273 ASP D CB   1 
ATOM   10431 C CG   . ASP D 2 255 ? -4.489  167.240 25.226  1.00 56.44  ? 273 ASP D CG   1 
ATOM   10432 O OD1  . ASP D 2 255 ? -5.629  167.728 25.331  1.00 72.22  ? 273 ASP D OD1  1 
ATOM   10433 O OD2  . ASP D 2 255 ? -3.751  167.007 26.202  1.00 64.78  ? 273 ASP D OD2  1 
ATOM   10434 N N    . TYR D 2 256 ? -4.088  165.741 20.914  1.00 42.29  ? 274 TYR D N    1 
ATOM   10435 C CA   . TYR D 2 256 ? -3.596  165.656 19.536  1.00 40.07  ? 274 TYR D CA   1 
ATOM   10436 C C    . TYR D 2 256 ? -4.652  166.183 18.630  1.00 37.40  ? 274 TYR D C    1 
ATOM   10437 O O    . TYR D 2 256 ? -4.437  167.149 17.978  1.00 41.96  ? 274 TYR D O    1 
ATOM   10438 C CB   . TYR D 2 256 ? -3.275  164.248 19.063  1.00 36.41  ? 274 TYR D CB   1 
ATOM   10439 C CG   . TYR D 2 256 ? -2.852  164.152 17.629  1.00 30.39  ? 274 TYR D CG   1 
ATOM   10440 C CD1  . TYR D 2 256 ? -1.611  164.576 17.245  1.00 34.35  ? 274 TYR D CD1  1 
ATOM   10441 C CD2  . TYR D 2 256 ? -3.688  163.616 16.666  1.00 27.94  ? 274 TYR D CD2  1 
ATOM   10442 C CE1  . TYR D 2 256 ? -1.214  164.492 15.941  1.00 38.89  ? 274 TYR D CE1  1 
ATOM   10443 C CE2  . TYR D 2 256 ? -3.295  163.541 15.355  1.00 32.39  ? 274 TYR D CE2  1 
ATOM   10444 C CZ   . TYR D 2 256 ? -2.050  163.982 15.009  1.00 36.57  ? 274 TYR D CZ   1 
ATOM   10445 O OH   . TYR D 2 256 ? -1.612  163.918 13.724  1.00 37.24  ? 274 TYR D OH   1 
ATOM   10446 N N    . ILE D 2 257 ? -5.777  165.504 18.546  1.00 31.12  ? 275 ILE D N    1 
ATOM   10447 C CA   . ILE D 2 257 ? -6.846  165.905 17.676  1.00 33.60  ? 275 ILE D CA   1 
ATOM   10448 C C    . ILE D 2 257 ? -7.143  167.376 17.779  1.00 42.45  ? 275 ILE D C    1 
ATOM   10449 O O    . ILE D 2 257 ? -7.255  168.025 16.795  1.00 49.61  ? 275 ILE D O    1 
ATOM   10450 C CB   . ILE D 2 257 ? -8.090  165.059 17.942  1.00 33.10  ? 275 ILE D CB   1 
ATOM   10451 C CG1  . ILE D 2 257 ? -7.902  163.649 17.410  1.00 31.76  ? 275 ILE D CG1  1 
ATOM   10452 C CG2  . ILE D 2 257 ? -9.348  165.681 17.360  1.00 36.17  ? 275 ILE D CG2  1 
ATOM   10453 C CD1  . ILE D 2 257 ? -8.823  162.663 18.078  1.00 28.45  ? 275 ILE D CD1  1 
ATOM   10454 N N    . GLU D 2 258 ? -7.169  167.948 18.965  1.00 43.84  ? 276 GLU D N    1 
ATOM   10455 C CA   . GLU D 2 258 ? -7.381  169.398 19.115  1.00 46.94  ? 276 GLU D CA   1 
ATOM   10456 C C    . GLU D 2 258 ? -6.254  170.324 18.660  1.00 44.99  ? 276 GLU D C    1 
ATOM   10457 O O    . GLU D 2 258 ? -6.492  171.459 18.278  1.00 49.76  ? 276 GLU D O    1 
ATOM   10458 C CB   . GLU D 2 258 ? -7.786  169.728 20.550  1.00 45.17  ? 276 GLU D CB   1 
ATOM   10459 C CG   . GLU D 2 258 ? -8.109  171.175 20.882  1.00 48.36  ? 276 GLU D CG   1 
ATOM   10460 C CD   . GLU D 2 258 ? -8.539  171.349 22.324  1.00 68.22  ? 276 GLU D CD   1 
ATOM   10461 O OE1  . GLU D 2 258 ? -8.548  170.352 23.069  1.00 78.78  ? 276 GLU D OE1  1 
ATOM   10462 O OE2  . GLU D 2 258 ? -8.864  172.485 22.717  1.00 58.34  ? 276 GLU D OE2  1 
ATOM   10463 N N    . LYS D 2 259 ? -5.027  169.829 18.648  1.00 41.13  ? 277 LYS D N    1 
ATOM   10464 C CA   . LYS D 2 259 ? -3.912  170.632 18.214  1.00 41.53  ? 277 LYS D CA   1 
ATOM   10465 C C    . LYS D 2 259 ? -3.842  170.467 16.751  1.00 41.73  ? 277 LYS D C    1 
ATOM   10466 O O    . LYS D 2 259 ? -3.646  171.417 16.017  1.00 47.67  ? 277 LYS D O    1 
ATOM   10467 C CB   . LYS D 2 259 ? -2.605  170.139 18.787  1.00 40.71  ? 277 LYS D CB   1 
ATOM   10468 C CG   . LYS D 2 259 ? -2.384  170.372 20.268  1.00 51.44  ? 277 LYS D CG   1 
ATOM   10469 C CD   . LYS D 2 259 ? -1.215  169.525 20.754  1.00 52.48  ? 277 LYS D CD   1 
ATOM   10470 C CE   . LYS D 2 259 ? -1.152  169.466 22.269  1.00 38.45  ? 277 LYS D CE   1 
ATOM   10471 N NZ   . LYS D 2 259 ? -0.512  168.214 22.749  1.00 37.65  ? 277 LYS D NZ   1 
ATOM   10472 N N    . HIS D 2 260 ? -3.989  169.241 16.301  1.00 41.25  ? 278 HIS D N    1 
ATOM   10473 C CA   . HIS D 2 260 ? -3.925  168.948 14.893  1.00 41.13  ? 278 HIS D CA   1 
ATOM   10474 C C    . HIS D 2 260 ? -5.306  168.648 14.386  1.00 46.24  ? 278 HIS D C    1 
ATOM   10475 O O    . HIS D 2 260 ? -5.518  167.619 13.801  1.00 44.30  ? 278 HIS D O    1 
ATOM   10476 C CB   . HIS D 2 260 ? -3.031  167.767 14.632  1.00 34.09  ? 278 HIS D CB   1 
ATOM   10477 C CG   . HIS D 2 260 ? -1.630  167.930 15.130  1.00 42.82  ? 278 HIS D CG   1 
ATOM   10478 N ND1  . HIS D 2 260 ? -0.557  168.080 14.282  1.00 40.10  ? 278 HIS D ND1  1 
ATOM   10479 C CD2  . HIS D 2 260 ? -1.117  167.927 16.382  1.00 48.82  ? 278 HIS D CD2  1 
ATOM   10480 C CE1  . HIS D 2 260 ? 0.552   168.183 14.988  1.00 41.25  ? 278 HIS D CE1  1 
ATOM   10481 N NE2  . HIS D 2 260 ? 0.240   168.091 16.266  1.00 49.30  ? 278 HIS D NE2  1 
ATOM   10482 N N    . LYS D 2 261 ? -6.260  169.540 14.619  1.00 41.56  ? 279 LYS D N    1 
ATOM   10483 C CA   . LYS D 2 261 ? -7.599  169.367 14.123  1.00 41.39  ? 279 LYS D CA   1 
ATOM   10484 C C    . LYS D 2 261 ? -7.679  169.963 12.787  1.00 50.63  ? 279 LYS D C    1 
ATOM   10485 O O    . LYS D 2 261 ? -8.513  169.590 11.976  1.00 49.61  ? 279 LYS D O    1 
ATOM   10486 C CB   . LYS D 2 261 ? -8.524  170.164 14.996  1.00 37.08  ? 279 LYS D CB   1 
ATOM   10487 C CG   . LYS D 2 261 ? -9.922  169.590 15.110  1.00 41.85  ? 279 LYS D CG   1 
ATOM   10488 C CD   . LYS D 2 261 ? -10.363 169.539 16.557  1.00 49.37  ? 279 LYS D CD   1 
ATOM   10489 C CE   . LYS D 2 261 ? -11.421 170.579 16.852  1.00 48.44  ? 279 LYS D CE   1 
ATOM   10490 N NZ   . LYS D 2 261 ? -12.657 169.946 17.384  1.00 41.60  ? 279 LYS D NZ   1 
ATOM   10491 N N    . THR D 2 262 ? -6.849  170.960 12.545  1.00 56.80  ? 280 THR D N    1 
ATOM   10492 C CA   . THR D 2 262 ? -6.923  171.692 11.311  1.00 45.96  ? 280 THR D CA   1 
ATOM   10493 C C    . THR D 2 262 ? -6.223  170.975 10.241  1.00 48.96  ? 280 THR D C    1 
ATOM   10494 O O    . THR D 2 262 ? -6.559  171.129 9.084   1.00 63.18  ? 280 THR D O    1 
ATOM   10495 C CB   . THR D 2 262 ? -6.231  173.032 11.465  1.00 38.20  ? 280 THR D CB   1 
ATOM   10496 O OG1  . THR D 2 262 ? -4.906  172.822 11.961  1.00 39.51  ? 280 THR D OG1  1 
ATOM   10497 C CG2  . THR D 2 262 ? -6.994  173.896 12.440  1.00 45.50  ? 280 THR D CG2  1 
ATOM   10498 N N    . ASP D 2 263 ? -5.249  170.167 10.595  1.00 44.81  ? 281 ASP D N    1 
ATOM   10499 C CA   . ASP D 2 263 ? -4.477  169.557 9.558   1.00 51.17  ? 281 ASP D CA   1 
ATOM   10500 C C    . ASP D 2 263 ? -5.476  168.782 8.754   1.00 57.71  ? 281 ASP D C    1 
ATOM   10501 O O    . ASP D 2 263 ? -6.310  168.103 9.315   1.00 66.36  ? 281 ASP D O    1 
ATOM   10502 C CB   . ASP D 2 263 ? -3.407  168.673 10.148  1.00 48.26  ? 281 ASP D CB   1 
ATOM   10503 C CG   . ASP D 2 263 ? -2.428  169.439 11.006  1.00 48.90  ? 281 ASP D CG   1 
ATOM   10504 O OD1  . ASP D 2 263 ? -2.648  170.642 11.244  1.00 48.77  ? 281 ASP D OD1  1 
ATOM   10505 O OD2  . ASP D 2 263 ? -1.430  168.835 11.447  1.00 49.23  ? 281 ASP D OD2  1 
ATOM   10506 N N    . LYS D 2 264 ? -5.411  168.877 7.438   1.00 48.89  ? 282 LYS D N    1 
ATOM   10507 C CA   . LYS D 2 264 ? -6.384  168.230 6.566   1.00 56.75  ? 282 LYS D CA   1 
ATOM   10508 C C    . LYS D 2 264 ? -6.538  166.746 6.507   1.00 59.45  ? 282 LYS D C    1 
ATOM   10509 O O    . LYS D 2 264 ? -7.585  166.240 6.126   1.00 64.21  ? 282 LYS D O    1 
ATOM   10510 C CB   . LYS D 2 264 ? -6.163  168.693 5.133   1.00 69.35  ? 282 LYS D CB   1 
ATOM   10511 C CG   . LYS D 2 264 ? -7.406  169.242 4.446   1.00 72.45  ? 282 LYS D CG   1 
ATOM   10512 C CD   . LYS D 2 264 ? -7.919  170.500 5.131   1.00 80.72  ? 282 LYS D CD   1 
ATOM   10513 C CE   . LYS D 2 264 ? -9.302  170.890 4.629   1.00 68.77  ? 282 LYS D CE   1 
ATOM   10514 N NZ   . LYS D 2 264 ? -9.831  172.084 5.345   1.00 52.86  ? 282 LYS D NZ   1 
ATOM   10515 N N    . ASP D 2 265 ? -5.492  166.033 6.861   1.00 53.65  ? 283 ASP D N    1 
ATOM   10516 C CA   . ASP D 2 265 ? -5.551  164.596 6.852   1.00 56.84  ? 283 ASP D CA   1 
ATOM   10517 C C    . ASP D 2 265 ? -5.637  163.981 8.312   1.00 61.15  ? 283 ASP D C    1 
ATOM   10518 O O    . ASP D 2 265 ? -5.139  162.945 8.703   1.00 60.92  ? 283 ASP D O    1 
ATOM   10519 C CB   . ASP D 2 265 ? -4.259  163.985 6.315   1.00 52.47  ? 283 ASP D CB   1 
ATOM   10520 C CG   . ASP D 2 265 ? -3.044  164.334 7.134   1.00 56.94  ? 283 ASP D CG   1 
ATOM   10521 O OD1  . ASP D 2 265 ? -3.155  165.115 8.093   1.00 58.86  ? 283 ASP D OD1  1 
ATOM   10522 O OD2  . ASP D 2 265 ? -1.966  163.791 6.835   1.00 64.68  ? 283 ASP D OD2  1 
ATOM   10523 N N    . ILE D 2 266 ? -6.387  164.733 9.108   1.00 56.07  ? 284 ILE D N    1 
ATOM   10524 C CA   . ILE D 2 266 ? -6.484  164.430 10.529  1.00 50.43  ? 284 ILE D CA   1 
ATOM   10525 C C    . ILE D 2 266 ? -7.217  163.108 10.513  1.00 47.22  ? 284 ILE D C    1 
ATOM   10526 O O    . ILE D 2 266 ? -6.878  162.248 11.292  1.00 53.93  ? 284 ILE D O    1 
ATOM   10527 C CB   . ILE D 2 266 ? -7.270  165.471 11.353  1.00 45.31  ? 284 ILE D CB   1 
ATOM   10528 C CG1  . ILE D 2 266 ? -7.728  164.920 12.705  1.00 44.41  ? 284 ILE D CG1  1 
ATOM   10529 C CG2  . ILE D 2 266 ? -8.480  165.967 10.581  1.00 50.82  ? 284 ILE D CG2  1 
ATOM   10530 C CD1  . ILE D 2 266 ? -6.604  164.621 13.670  1.00 47.51  ? 284 ILE D CD1  1 
ATOM   10531 N N    . GLU D 2 267 ? -8.177  162.881 9.647   1.00 39.98  ? 285 GLU D N    1 
ATOM   10532 C CA   . GLU D 2 267 ? -8.808  161.572 9.647   1.00 43.98  ? 285 GLU D CA   1 
ATOM   10533 C C    . GLU D 2 267 ? -7.825  160.561 9.166   1.00 40.93  ? 285 GLU D C    1 
ATOM   10534 O O    . GLU D 2 267 ? -7.781  159.437 9.622   1.00 35.59  ? 285 GLU D O    1 
ATOM   10535 C CB   . GLU D 2 267 ? -9.991  161.551 8.709   1.00 57.42  ? 285 GLU D CB   1 
ATOM   10536 C CG   . GLU D 2 267 ? -11.014 160.487 9.034   1.00 54.90  ? 285 GLU D CG   1 
ATOM   10537 C CD   . GLU D 2 267 ? -11.902 160.210 7.856   1.00 59.02  ? 285 GLU D CD   1 
ATOM   10538 O OE1  . GLU D 2 267 ? -11.369 160.090 6.736   1.00 36.76  ? 285 GLU D OE1  1 
ATOM   10539 O OE2  . GLU D 2 267 ? -13.126 160.136 8.051   1.00 73.62  ? 285 GLU D OE2  1 
ATOM   10540 N N    . LYS D 2 268 ? -7.031  160.966 8.220   1.00 44.01  ? 286 LYS D N    1 
ATOM   10541 C CA   . LYS D 2 268 ? -6.102  160.050 7.647   1.00 47.05  ? 286 LYS D CA   1 
ATOM   10542 C C    . LYS D 2 268 ? -5.063  159.657 8.643   1.00 41.15  ? 286 LYS D C    1 
ATOM   10543 O O    . LYS D 2 268 ? -4.372  158.662 8.512   1.00 40.45  ? 286 LYS D O    1 
ATOM   10544 C CB   . LYS D 2 268 ? -5.504  160.612 6.364   1.00 51.15  ? 286 LYS D CB   1 
ATOM   10545 C CG   . LYS D 2 268 ? -6.517  160.851 5.254   1.00 61.33  ? 286 LYS D CG   1 
ATOM   10546 C CD   . LYS D 2 268 ? -7.097  159.559 4.698   1.00 57.65  ? 286 LYS D CD   1 
ATOM   10547 C CE   . LYS D 2 268 ? -8.028  159.825 3.527   1.00 38.40  ? 286 LYS D CE   1 
ATOM   10548 N NZ   . LYS D 2 268 ? -9.303  160.461 3.953   1.00 53.21  ? 286 LYS D NZ   1 
ATOM   10549 N N    . LYS D 2 269 ? -4.904  160.501 9.623   1.00 35.31  ? 287 LYS D N    1 
ATOM   10550 C CA   . LYS D 2 269 ? -4.009  160.170 10.682  1.00 39.44  ? 287 LYS D CA   1 
ATOM   10551 C C    . LYS D 2 269 ? -4.614  159.749 12.029  1.00 34.16  ? 287 LYS D C    1 
ATOM   10552 O O    . LYS D 2 269 ? -3.881  159.492 12.947  1.00 30.73  ? 287 LYS D O    1 
ATOM   10553 C CB   . LYS D 2 269 ? -3.146  161.416 10.812  1.00 43.93  ? 287 LYS D CB   1 
ATOM   10554 C CG   . LYS D 2 269 ? -2.313  161.768 9.600   1.00 39.96  ? 287 LYS D CG   1 
ATOM   10555 C CD   . LYS D 2 269 ? -1.552  163.047 9.874   1.00 43.29  ? 287 LYS D CD   1 
ATOM   10556 C CE   . LYS D 2 269 ? -2.443  164.059 10.574  1.00 46.33  ? 287 LYS D CE   1 
ATOM   10557 N NZ   . LYS D 2 269 ? -1.800  165.396 10.714  1.00 39.04  ? 287 LYS D NZ   1 
ATOM   10558 N N    . VAL D 2 270 ? -5.936  159.677 12.148  1.00 30.73  ? 288 VAL D N    1 
ATOM   10559 C CA   . VAL D 2 270 ? -6.560  159.269 13.394  1.00 28.53  ? 288 VAL D CA   1 
ATOM   10560 C C    . VAL D 2 270 ? -7.086  157.881 13.333  1.00 28.27  ? 288 VAL D C    1 
ATOM   10561 O O    . VAL D 2 270 ? -7.076  157.163 14.306  1.00 35.44  ? 288 VAL D O    1 
ATOM   10562 C CB   . VAL D 2 270 ? -7.661  160.233 13.881  1.00 29.69  ? 288 VAL D CB   1 
ATOM   10563 C CG1  . VAL D 2 270 ? -8.966  160.056 13.130  1.00 34.67  ? 288 VAL D CG1  1 
ATOM   10564 C CG2  . VAL D 2 270 ? -7.885  160.082 15.369  1.00 31.19  ? 288 VAL D CG2  1 
ATOM   10565 N N    . ASN D 2 271 ? -7.550  157.479 12.183  1.00 27.43  ? 289 ASN D N    1 
ATOM   10566 C CA   . ASN D 2 271 ? -8.009  156.139 12.031  1.00 31.95  ? 289 ASN D CA   1 
ATOM   10567 C C    . ASN D 2 271 ? -6.787  155.269 12.093  1.00 30.55  ? 289 ASN D C    1 
ATOM   10568 O O    . ASN D 2 271 ? -6.851  154.136 12.506  1.00 29.55  ? 289 ASN D O    1 
ATOM   10569 C CB   . ASN D 2 271 ? -8.814  155.988 10.753  1.00 27.83  ? 289 ASN D CB   1 
ATOM   10570 C CG   . ASN D 2 271 ? -10.297 155.937 11.005  1.00 31.66  ? 289 ASN D CG   1 
ATOM   10571 O OD1  . ASN D 2 271 ? -10.729 155.599 12.095  1.00 42.80  ? 289 ASN D OD1  1 
ATOM   10572 N ND2  . ASN D 2 271 ? -11.083 156.258 9.990   1.00 22.59  ? 289 ASN D ND2  1 
ATOM   10573 N N    . GLN D 2 272 ? -5.663  155.782 11.648  1.00 25.60  ? 290 GLN D N    1 
ATOM   10574 C CA   . GLN D 2 272 ? -4.443  155.034 11.741  1.00 26.11  ? 290 GLN D CA   1 
ATOM   10575 C C    . GLN D 2 272 ? -4.063  154.731 13.163  1.00 27.89  ? 290 GLN D C    1 
ATOM   10576 O O    . GLN D 2 272 ? -3.668  153.623 13.447  1.00 31.41  ? 290 GLN D O    1 
ATOM   10577 C CB   . GLN D 2 272 ? -3.334  155.827 11.099  1.00 35.51  ? 290 GLN D CB   1 
ATOM   10578 C CG   . GLN D 2 272 ? -3.172  155.621 9.603   1.00 37.48  ? 290 GLN D CG   1 
ATOM   10579 C CD   . GLN D 2 272 ? -1.788  156.005 9.112   1.00 40.35  ? 290 GLN D CD   1 
ATOM   10580 O OE1  . GLN D 2 272 ? -1.046  155.174 8.605   1.00 40.28  ? 290 GLN D OE1  1 
ATOM   10581 N NE2  . GLN D 2 272 ? -1.431  157.265 9.282   1.00 40.37  ? 290 GLN D NE2  1 
ATOM   10582 N N    . ILE D 2 273 ? -4.173  155.687 14.066  1.00 26.13  ? 291 ILE D N    1 
ATOM   10583 C CA   . ILE D 2 273 ? -3.916  155.453 15.480  1.00 24.64  ? 291 ILE D CA   1 
ATOM   10584 C C    . ILE D 2 273 ? -4.900  154.499 16.109  1.00 26.71  ? 291 ILE D C    1 
ATOM   10585 O O    . ILE D 2 273 ? -4.510  153.661 16.902  1.00 26.38  ? 291 ILE D O    1 
ATOM   10586 C CB   . ILE D 2 273 ? -4.001  156.740 16.266  1.00 23.47  ? 291 ILE D CB   1 
ATOM   10587 C CG1  . ILE D 2 273 ? -3.281  157.854 15.551  1.00 31.59  ? 291 ILE D CG1  1 
ATOM   10588 C CG2  . ILE D 2 273 ? -3.356  156.577 17.624  1.00 27.13  ? 291 ILE D CG2  1 
ATOM   10589 C CD1  . ILE D 2 273 ? -1.869  157.985 16.025  1.00 35.04  ? 291 ILE D CD1  1 
ATOM   10590 N N    . ILE D 2 274 ? -6.175  154.614 15.768  1.00 23.77  ? 292 ILE D N    1 
ATOM   10591 C CA   . ILE D 2 274 ? -7.192  153.768 16.362  1.00 21.16  ? 292 ILE D CA   1 
ATOM   10592 C C    . ILE D 2 274 ? -7.071  152.383 15.832  1.00 22.69  ? 292 ILE D C    1 
ATOM   10593 O O    . ILE D 2 274 ? -7.183  151.430 16.570  1.00 19.75  ? 292 ILE D O    1 
ATOM   10594 C CB   . ILE D 2 274 ? -8.604  154.301 16.098  1.00 24.64  ? 292 ILE D CB   1 
ATOM   10595 C CG1  . ILE D 2 274 ? -8.834  155.599 16.861  1.00 30.12  ? 292 ILE D CG1  1 
ATOM   10596 C CG2  . ILE D 2 274 ? -9.670  153.303 16.504  1.00 17.57  ? 292 ILE D CG2  1 
ATOM   10597 C CD1  . ILE D 2 274 ? -9.277  155.389 18.288  1.00 25.40  ? 292 ILE D CD1  1 
ATOM   10598 N N    . ASN D 2 275 ? -6.797  152.261 14.546  1.00 27.82  ? 293 ASN D N    1 
ATOM   10599 C CA   . ASN D 2 275 ? -6.735  150.930 13.937  1.00 25.77  ? 293 ASN D CA   1 
ATOM   10600 C C    . ASN D 2 275 ? -5.440  150.206 14.144  1.00 22.42  ? 293 ASN D C    1 
ATOM   10601 O O    . ASN D 2 275 ? -5.396  149.005 14.001  1.00 20.84  ? 293 ASN D O    1 
ATOM   10602 C CB   . ASN D 2 275 ? -7.134  150.986 12.478  1.00 26.54  ? 293 ASN D CB   1 
ATOM   10603 C CG   . ASN D 2 275 ? -8.510  151.556 12.272  1.00 27.21  ? 293 ASN D CG   1 
ATOM   10604 O OD1  . ASN D 2 275 ? -9.368  151.475 13.137  1.00 26.97  ? 293 ASN D OD1  1 
ATOM   10605 N ND2  . ASN D 2 275 ? -8.717  152.154 11.121  1.00 21.31  ? 293 ASN D ND2  1 
ATOM   10606 N N    . LEU D 2 276 ? -4.381  150.915 14.481  1.00 21.01  ? 294 LEU D N    1 
ATOM   10607 C CA   . LEU D 2 276 ? -3.150  150.262 14.833  1.00 21.13  ? 294 LEU D CA   1 
ATOM   10608 C C    . LEU D 2 276 ? -3.405  149.680 16.174  1.00 20.89  ? 294 LEU D C    1 
ATOM   10609 O O    . LEU D 2 276 ? -3.027  148.587 16.430  1.00 23.29  ? 294 LEU D O    1 
ATOM   10610 C CB   . LEU D 2 276 ? -2.017  151.246 14.940  1.00 20.48  ? 294 LEU D CB   1 
ATOM   10611 C CG   . LEU D 2 276 ? -0.615  150.692 15.154  1.00 22.55  ? 294 LEU D CG   1 
ATOM   10612 C CD1  . LEU D 2 276 ? -0.209  149.789 14.009  1.00 19.83  ? 294 LEU D CD1  1 
ATOM   10613 C CD2  . LEU D 2 276 ? 0.362   151.832 15.305  1.00 20.58  ? 294 LEU D CD2  1 
ATOM   10614 N N    . TRP D 2 277 ? -4.071  150.401 17.042  1.00 21.67  ? 295 TRP D N    1 
ATOM   10615 C CA   . TRP D 2 277 ? -4.398  149.940 18.388  1.00 20.56  ? 295 TRP D CA   1 
ATOM   10616 C C    . TRP D 2 277 ? -5.286  148.740 18.360  1.00 20.08  ? 295 TRP D C    1 
ATOM   10617 O O    . TRP D 2 277 ? -4.983  147.753 18.960  1.00 18.42  ? 295 TRP D O    1 
ATOM   10618 C CB   . TRP D 2 277 ? -5.125  151.093 19.097  1.00 19.42  ? 295 TRP D CB   1 
ATOM   10619 C CG   . TRP D 2 277 ? -5.450  150.967 20.523  1.00 18.44  ? 295 TRP D CG   1 
ATOM   10620 C CD1  . TRP D 2 277 ? -6.491  150.306 21.067  1.00 18.34  ? 295 TRP D CD1  1 
ATOM   10621 C CD2  . TRP D 2 277 ? -4.770  151.593 21.597  1.00 21.39  ? 295 TRP D CD2  1 
ATOM   10622 N NE1  . TRP D 2 277 ? -6.485  150.447 22.423  1.00 18.33  ? 295 TRP D NE1  1 
ATOM   10623 C CE2  . TRP D 2 277 ? -5.432  151.243 22.769  1.00 19.29  ? 295 TRP D CE2  1 
ATOM   10624 C CE3  . TRP D 2 277 ? -3.649  152.409 21.682  1.00 19.29  ? 295 TRP D CE3  1 
ATOM   10625 C CZ2  . TRP D 2 277 ? -5.014  151.668 23.998  1.00 19.96  ? 295 TRP D CZ2  1 
ATOM   10626 C CZ3  . TRP D 2 277 ? -3.239  152.827 22.902  1.00 19.91  ? 295 TRP D CZ3  1 
ATOM   10627 C CH2  . TRP D 2 277 ? -3.912  152.462 24.045  1.00 19.40  ? 295 TRP D CH2  1 
ATOM   10628 N N    . ILE D 2 278 ? -6.406  148.833 17.676  1.00 17.52  ? 296 ILE D N    1 
ATOM   10629 C CA   . ILE D 2 278 ? -7.364  147.765 17.670  1.00 16.15  ? 296 ILE D CA   1 
ATOM   10630 C C    . ILE D 2 278 ? -6.673  146.525 17.271  1.00 19.43  ? 296 ILE D C    1 
ATOM   10631 O O    . ILE D 2 278 ? -6.839  145.527 17.911  1.00 20.40  ? 296 ILE D O    1 
ATOM   10632 C CB   . ILE D 2 278 ? -8.542  148.093 16.752  1.00 18.21  ? 296 ILE D CB   1 
ATOM   10633 C CG1  . ILE D 2 278 ? -9.337  149.249 17.329  1.00 16.18  ? 296 ILE D CG1  1 
ATOM   10634 C CG2  . ILE D 2 278 ? -9.477  146.915 16.605  1.00 16.18  ? 296 ILE D CG2  1 
ATOM   10635 C CD1  . ILE D 2 278 ? -10.548 149.605 16.514  1.00 21.35  ? 296 ILE D CD1  1 
ATOM   10636 N N    . SER D 2 279 ? -5.842  146.596 16.245  1.00 20.98  ? 297 SER D N    1 
ATOM   10637 C CA   . SER D 2 279 ? -5.177  145.431 15.710  1.00 18.09  ? 297 SER D CA   1 
ATOM   10638 C C    . SER D 2 279 ? -4.062  144.925 16.529  1.00 15.40  ? 297 SER D C    1 
ATOM   10639 O O    . SER D 2 279 ? -3.933  143.767 16.626  1.00 16.31  ? 297 SER D O    1 
ATOM   10640 C CB   . SER D 2 279 ? -4.681  145.736 14.321  1.00 18.38  ? 297 SER D CB   1 
ATOM   10641 O OG   . SER D 2 279 ? -3.547  146.564 14.318  1.00 20.73  ? 297 SER D OG   1 
ATOM   10642 N N    . SER D 2 280 ? -3.269  145.780 17.139  1.00 13.78  ? 298 SER D N    1 
ATOM   10643 C CA   . SER D 2 280 ? -2.098  145.381 17.874  1.00 15.89  ? 298 SER D CA   1 
ATOM   10644 C C    . SER D 2 280 ? -2.436  144.916 19.244  1.00 17.28  ? 298 SER D C    1 
ATOM   10645 O O    . SER D 2 280 ? -1.561  144.635 20.027  1.00 22.20  ? 298 SER D O    1 
ATOM   10646 C CB   . SER D 2 280 ? -1.118  146.536 17.927  1.00 13.16  ? 298 SER D CB   1 
ATOM   10647 O OG   . SER D 2 280 ? -0.694  146.919 16.639  1.00 15.68  ? 298 SER D OG   1 
ATOM   10648 N N    . TYR D 2 281 ? -3.714  144.767 19.522  1.00 14.94  ? 299 TYR D N    1 
ATOM   10649 C CA   . TYR D 2 281 ? -4.180  144.288 20.801  1.00 15.10  ? 299 TYR D CA   1 
ATOM   10650 C C    . TYR D 2 281 ? -4.721  142.902 20.564  1.00 16.08  ? 299 TYR D C    1 
ATOM   10651 O O    . TYR D 2 281 ? -4.368  141.997 21.260  1.00 21.24  ? 299 TYR D O    1 
ATOM   10652 C CB   . TYR D 2 281 ? -5.250  145.230 21.295  1.00 18.07  ? 299 TYR D CB   1 
ATOM   10653 C CG   . TYR D 2 281 ? -4.757  146.259 22.280  1.00 17.99  ? 299 TYR D CG   1 
ATOM   10654 C CD1  . TYR D 2 281 ? -3.714  147.107 21.963  1.00 17.43  ? 299 TYR D CD1  1 
ATOM   10655 C CD2  . TYR D 2 281 ? -5.331  146.377 23.530  1.00 20.58  ? 299 TYR D CD2  1 
ATOM   10656 C CE1  . TYR D 2 281 ? -3.255  148.039 22.864  1.00 13.73  ? 299 TYR D CE1  1 
ATOM   10657 C CE2  . TYR D 2 281 ? -4.876  147.305 24.437  1.00 20.56  ? 299 TYR D CE2  1 
ATOM   10658 C CZ   . TYR D 2 281 ? -3.840  148.131 24.096  1.00 17.69  ? 299 TYR D CZ   1 
ATOM   10659 O OH   . TYR D 2 281 ? -3.384  149.053 24.994  1.00 18.50  ? 299 TYR D OH   1 
ATOM   10660 N N    . ILE D 2 282 ? -5.504  142.684 19.527  1.00 15.68  ? 300 ILE D N    1 
ATOM   10661 C CA   . ILE D 2 282 ? -5.947  141.336 19.170  1.00 17.57  ? 300 ILE D CA   1 
ATOM   10662 C C    . ILE D 2 282 ? -4.835  140.544 18.520  1.00 13.95  ? 300 ILE D C    1 
ATOM   10663 O O    . ILE D 2 282 ? -4.955  139.358 18.329  1.00 17.51  ? 300 ILE D O    1 
ATOM   10664 C CB   . ILE D 2 282 ? -7.114  141.379 18.196  1.00 13.98  ? 300 ILE D CB   1 
ATOM   10665 C CG1  . ILE D 2 282 ? -7.891  142.665 18.317  1.00 14.63  ? 300 ILE D CG1  1 
ATOM   10666 C CG2  . ILE D 2 282 ? -8.111  140.307 18.490  1.00 13.33  ? 300 ILE D CG2  1 
ATOM   10667 C CD1  . ILE D 2 282 ? -8.763  142.916 17.113  1.00 15.94  ? 300 ILE D CD1  1 
ATOM   10668 N N    . LYS D 2 283 ? -3.739  141.198 18.212  1.00 10.22  ? 301 LYS D N    1 
ATOM   10669 C CA   . LYS D 2 283 ? -2.600  140.523 17.621  1.00 14.66  ? 301 LYS D CA   1 
ATOM   10670 C C    . LYS D 2 283 ? -1.600  140.186 18.667  1.00 15.16  ? 301 LYS D C    1 
ATOM   10671 O O    . LYS D 2 283 ? -0.880  139.219 18.544  1.00 18.13  ? 301 LYS D O    1 
ATOM   10672 C CB   . LYS D 2 283 ? -1.931  141.418 16.598  1.00 17.19  ? 301 LYS D CB   1 
ATOM   10673 C CG   . LYS D 2 283 ? -0.853  140.740 15.780  1.00 20.13  ? 301 LYS D CG   1 
ATOM   10674 C CD   . LYS D 2 283 ? -0.314  141.660 14.706  1.00 27.06  ? 301 LYS D CD   1 
ATOM   10675 C CE   . LYS D 2 283 ? 0.837   141.008 13.956  1.00 36.67  ? 301 LYS D CE   1 
ATOM   10676 N NZ   . LYS D 2 283 ? 2.039   140.829 14.817  1.00 29.52  ? 301 LYS D NZ   1 
ATOM   10677 N N    . GLU D 2 284 ? -1.578  140.949 19.734  1.00 17.56  ? 302 GLU D N    1 
ATOM   10678 C CA   . GLU D 2 284 ? -0.649  140.720 20.818  1.00 19.51  ? 302 GLU D CA   1 
ATOM   10679 C C    . GLU D 2 284 ? -1.343  140.052 21.952  1.00 16.19  ? 302 GLU D C    1 
ATOM   10680 O O    . GLU D 2 284 ? -0.722  139.732 22.938  1.00 22.23  ? 302 GLU D O    1 
ATOM   10681 C CB   . GLU D 2 284 ? 0.014   142.019 21.233  1.00 20.72  ? 302 GLU D CB   1 
ATOM   10682 C CG   . GLU D 2 284 ? 0.983   142.551 20.196  1.00 28.90  ? 302 GLU D CG   1 
ATOM   10683 C CD   . GLU D 2 284 ? 2.202   141.667 20.041  1.00 37.12  ? 302 GLU D CD   1 
ATOM   10684 O OE1  . GLU D 2 284 ? 2.776   141.274 21.072  1.00 47.09  ? 302 GLU D OE1  1 
ATOM   10685 O OE2  . GLU D 2 284 ? 2.591   141.368 18.896  1.00 24.40  ? 302 GLU D OE2  1 
ATOM   10686 N N    . GLY D 2 285 ? -2.628  139.817 21.821  1.00 15.63  ? 303 GLY D N    1 
ATOM   10687 C CA   . GLY D 2 285 ? -3.359  139.063 22.802  1.00 13.63  ? 303 GLY D CA   1 
ATOM   10688 C C    . GLY D 2 285 ? -3.984  139.793 23.908  1.00 15.38  ? 303 GLY D C    1 
ATOM   10689 O O    . GLY D 2 285 ? -4.698  139.216 24.693  1.00 20.12  ? 303 GLY D O    1 
ATOM   10690 N N    . TYR D 2 286 ? -3.747  141.074 23.970  1.00 17.38  ? 304 TYR D N    1 
ATOM   10691 C CA   . TYR D 2 286 ? -4.282  141.892 25.029  1.00 18.93  ? 304 TYR D CA   1 
ATOM   10692 C C    . TYR D 2 286 ? -5.784  141.984 25.045  1.00 20.14  ? 304 TYR D C    1 
ATOM   10693 O O    . TYR D 2 286 ? -6.372  141.978 26.100  1.00 37.67  ? 304 TYR D O    1 
ATOM   10694 C CB   . TYR D 2 286 ? -3.633  143.257 25.036  1.00 17.75  ? 304 TYR D CB   1 
ATOM   10695 C CG   . TYR D 2 286 ? -2.142  143.180 25.122  1.00 18.47  ? 304 TYR D CG   1 
ATOM   10696 C CD1  . TYR D 2 286 ? -1.532  142.194 25.870  1.00 17.83  ? 304 TYR D CD1  1 
ATOM   10697 C CD2  . TYR D 2 286 ? -1.342  144.087 24.460  1.00 18.58  ? 304 TYR D CD2  1 
ATOM   10698 C CE1  . TYR D 2 286 ? -0.164  142.110 25.957  1.00 21.89  ? 304 TYR D CE1  1 
ATOM   10699 C CE2  . TYR D 2 286 ? 0.027   144.011 24.543  1.00 24.13  ? 304 TYR D CE2  1 
ATOM   10700 C CZ   . TYR D 2 286 ? 0.605   143.019 25.296  1.00 26.04  ? 304 TYR D CZ   1 
ATOM   10701 O OH   . TYR D 2 286 ? 1.968   142.933 25.390  1.00 44.46  ? 304 TYR D OH   1 
ATOM   10702 N N    . HIS D 2 287 ? -6.417  142.044 23.901  1.00 14.19  ? 305 HIS D N    1 
ATOM   10703 C CA   . HIS D 2 287 ? -7.836  142.171 23.876  1.00 14.95  ? 305 HIS D CA   1 
ATOM   10704 C C    . HIS D 2 287 ? -8.565  141.543 22.718  1.00 15.47  ? 305 HIS D C    1 
ATOM   10705 O O    . HIS D 2 287 ? -8.020  140.745 22.006  1.00 16.05  ? 305 HIS D O    1 
ATOM   10706 C CB   . HIS D 2 287 ? -8.190  143.629 23.969  1.00 15.29  ? 305 HIS D CB   1 
ATOM   10707 C CG   . HIS D 2 287 ? -8.080  144.205 25.348  1.00 21.39  ? 305 HIS D CG   1 
ATOM   10708 N ND1  . HIS D 2 287 ? -8.839  143.762 26.406  1.00 16.20  ? 305 HIS D ND1  1 
ATOM   10709 C CD2  . HIS D 2 287 ? -7.306  145.200 25.836  1.00 24.80  ? 305 HIS D CD2  1 
ATOM   10710 C CE1  . HIS D 2 287 ? -8.533  144.454 27.485  1.00 14.30  ? 305 HIS D CE1  1 
ATOM   10711 N NE2  . HIS D 2 287 ? -7.604  145.330 27.168  1.00 13.32  ? 305 HIS D NE2  1 
ATOM   10712 N N    . SER D 2 288 ? -9.820  141.878 22.559  1.00 16.38  ? 306 SER D N    1 
ATOM   10713 C CA   . SER D 2 288 ? -10.633 141.379 21.493  1.00 17.94  ? 306 SER D CA   1 
ATOM   10714 C C    . SER D 2 288 ? -11.180 142.645 20.896  1.00 18.80  ? 306 SER D C    1 
ATOM   10715 O O    . SER D 2 288 ? -11.086 143.676 21.507  1.00 19.76  ? 306 SER D O    1 
ATOM   10716 C CB   . SER D 2 288 ? -11.735 140.519 22.047  1.00 18.02  ? 306 SER D CB   1 
ATOM   10717 O OG   . SER D 2 288 ? -12.785 140.334 21.119  1.00 26.60  ? 306 SER D OG   1 
ATOM   10718 N N    . TYR D 2 289 ? -11.714 142.592 19.692  1.00 15.96  ? 307 TYR D N    1 
ATOM   10719 C CA   . TYR D 2 289 ? -12.195 143.769 19.002  1.00 21.30  ? 307 TYR D CA   1 
ATOM   10720 C C    . TYR D 2 289 ? -13.179 144.482 19.826  1.00 28.32  ? 307 TYR D C    1 
ATOM   10721 O O    . TYR D 2 289 ? -13.075 145.674 20.039  1.00 34.08  ? 307 TYR D O    1 
ATOM   10722 C CB   . TYR D 2 289 ? -12.885 143.335 17.731  1.00 23.70  ? 307 TYR D CB   1 
ATOM   10723 C CG   . TYR D 2 289 ? -13.493 144.407 16.884  1.00 22.25  ? 307 TYR D CG   1 
ATOM   10724 C CD1  . TYR D 2 289 ? -12.718 145.175 16.039  1.00 23.19  ? 307 TYR D CD1  1 
ATOM   10725 C CD2  . TYR D 2 289 ? -14.853 144.608 16.886  1.00 23.71  ? 307 TYR D CD2  1 
ATOM   10726 C CE1  . TYR D 2 289 ? -13.283 146.145 15.251  1.00 18.79  ? 307 TYR D CE1  1 
ATOM   10727 C CE2  . TYR D 2 289 ? -15.429 145.577 16.107  1.00 29.96  ? 307 TYR D CE2  1 
ATOM   10728 C CZ   . TYR D 2 289 ? -14.640 146.344 15.294  1.00 22.18  ? 307 TYR D CZ   1 
ATOM   10729 O OH   . TYR D 2 289 ? -15.242 147.306 14.529  1.00 13.28  ? 307 TYR D OH   1 
ATOM   10730 N N    . SER D 2 290 ? -14.164 143.759 20.299  1.00 27.29  ? 308 SER D N    1 
ATOM   10731 C CA   . SER D 2 290 ? -15.193 144.353 21.109  1.00 27.54  ? 308 SER D CA   1 
ATOM   10732 C C    . SER D 2 290 ? -14.655 144.992 22.372  1.00 22.94  ? 308 SER D C    1 
ATOM   10733 O O    . SER D 2 290 ? -15.151 146.013 22.797  1.00 24.20  ? 308 SER D O    1 
ATOM   10734 C CB   . SER D 2 290 ? -16.269 143.340 21.369  1.00 27.49  ? 308 SER D CB   1 
ATOM   10735 O OG   . SER D 2 290 ? -16.950 143.040 20.172  1.00 23.60  ? 308 SER D OG   1 
ATOM   10736 N N    . GLU D 2 291 ? -13.652 144.399 22.985  1.00 20.00  ? 309 GLU D N    1 
ATOM   10737 C CA   . GLU D 2 291 ? -13.032 144.961 24.169  1.00 22.59  ? 309 GLU D CA   1 
ATOM   10738 C C    . GLU D 2 291 ? -12.350 146.300 23.901  1.00 27.57  ? 309 GLU D C    1 
ATOM   10739 O O    . GLU D 2 291 ? -12.091 147.052 24.815  1.00 22.67  ? 309 GLU D O    1 
ATOM   10740 C CB   . GLU D 2 291 ? -12.055 143.983 24.744  1.00 15.11  ? 309 GLU D CB   1 
ATOM   10741 C CG   . GLU D 2 291 ? -12.655 142.845 25.503  1.00 20.16  ? 309 GLU D CG   1 
ATOM   10742 C CD   . GLU D 2 291 ? -11.578 141.945 26.028  1.00 23.81  ? 309 GLU D CD   1 
ATOM   10743 O OE1  . GLU D 2 291 ? -10.577 141.732 25.347  1.00 34.29  ? 309 GLU D OE1  1 
ATOM   10744 O OE2  . GLU D 2 291 ? -11.720 141.450 27.131  1.00 23.96  ? 309 GLU D OE2  1 
ATOM   10745 N N    . VAL D 2 292 ? -12.004 146.573 22.656  1.00 24.99  ? 310 VAL D N    1 
ATOM   10746 C CA   . VAL D 2 292 ? -11.368 147.826 22.291  1.00 23.16  ? 310 VAL D CA   1 
ATOM   10747 C C    . VAL D 2 292 ? -12.369 148.773 21.652  1.00 29.70  ? 310 VAL D C    1 
ATOM   10748 O O    . VAL D 2 292 ? -12.334 149.964 21.907  1.00 32.42  ? 310 VAL D O    1 
ATOM   10749 C CB   . VAL D 2 292 ? -10.194 147.584 21.338  1.00 17.51  ? 310 VAL D CB   1 
ATOM   10750 C CG1  . VAL D 2 292 ? -9.495  148.888 21.019  1.00 19.63  ? 310 VAL D CG1  1 
ATOM   10751 C CG2  . VAL D 2 292 ? -9.215  146.602 21.949  1.00 19.10  ? 310 VAL D CG2  1 
ATOM   10752 N N    . VAL D 2 293 ? -13.261 148.255 20.817  1.00 31.95  ? 311 VAL D N    1 
ATOM   10753 C CA   . VAL D 2 293 ? -14.261 149.080 20.150  1.00 32.06  ? 311 VAL D CA   1 
ATOM   10754 C C    . VAL D 2 293 ? -15.416 149.495 21.008  1.00 32.33  ? 311 VAL D C    1 
ATOM   10755 O O    . VAL D 2 293 ? -15.792 150.646 21.011  1.00 33.19  ? 311 VAL D O    1 
ATOM   10756 C CB   . VAL D 2 293 ? -14.764 148.410 18.859  1.00 21.42  ? 311 VAL D CB   1 
ATOM   10757 C CG1  . VAL D 2 293 ? -16.149 148.872 18.457  1.00 17.36  ? 311 VAL D CG1  1 
ATOM   10758 C CG2  . VAL D 2 293 ? -13.770 148.676 17.753  1.00 23.21  ? 311 VAL D CG2  1 
ATOM   10759 N N    . ASP D 2 294 ? -15.997 148.574 21.751  1.00 27.33  ? 312 ASP D N    1 
ATOM   10760 C CA   . ASP D 2 294 ? -17.189 148.904 22.491  1.00 26.45  ? 312 ASP D CA   1 
ATOM   10761 C C    . ASP D 2 294 ? -16.877 149.936 23.552  1.00 29.86  ? 312 ASP D C    1 
ATOM   10762 O O    . ASP D 2 294 ? -17.773 150.493 24.157  1.00 28.11  ? 312 ASP D O    1 
ATOM   10763 C CB   . ASP D 2 294 ? -17.858 147.633 22.966  1.00 22.29  ? 312 ASP D CB   1 
ATOM   10764 C CG   . ASP D 2 294 ? -18.698 146.994 21.907  1.00 31.44  ? 312 ASP D CG   1 
ATOM   10765 O OD1  . ASP D 2 294 ? -19.231 147.720 21.051  1.00 40.73  ? 312 ASP D OD1  1 
ATOM   10766 O OD2  . ASP D 2 294 ? -18.852 145.763 21.941  1.00 34.39  ? 312 ASP D OD2  1 
ATOM   10767 N N    . VAL D 2 295 ? -15.616 150.123 23.861  1.00 25.82  ? 313 VAL D N    1 
ATOM   10768 C CA   . VAL D 2 295 ? -15.221 151.193 24.737  1.00 23.03  ? 313 VAL D CA   1 
ATOM   10769 C C    . VAL D 2 295 ? -15.329 152.481 23.984  1.00 30.81  ? 313 VAL D C    1 
ATOM   10770 O O    . VAL D 2 295 ? -15.611 153.509 24.552  1.00 29.73  ? 313 VAL D O    1 
ATOM   10771 C CB   . VAL D 2 295 ? -13.780 151.048 25.158  1.00 23.46  ? 313 VAL D CB   1 
ATOM   10772 C CG1  . VAL D 2 295 ? -13.484 151.944 26.329  1.00 27.68  ? 313 VAL D CG1  1 
ATOM   10773 C CG2  . VAL D 2 295 ? -13.520 149.621 25.530  1.00 33.28  ? 313 VAL D CG2  1 
ATOM   10774 N N    . LEU D 2 296 ? -15.008 152.454 22.699  1.00 31.83  ? 314 LEU D N    1 
ATOM   10775 C CA   . LEU D 2 296 ? -15.037 153.651 21.874  1.00 28.57  ? 314 LEU D CA   1 
ATOM   10776 C C    . LEU D 2 296 ? -16.397 153.916 21.243  1.00 27.17  ? 314 LEU D C    1 
ATOM   10777 O O    . LEU D 2 296 ? -16.647 155.010 20.766  1.00 22.65  ? 314 LEU D O    1 
ATOM   10778 C CB   . LEU D 2 296 ? -13.930 153.558 20.838  1.00 26.91  ? 314 LEU D CB   1 
ATOM   10779 C CG   . LEU D 2 296 ? -12.496 153.375 21.307  1.00 30.30  ? 314 LEU D CG   1 
ATOM   10780 C CD1  . LEU D 2 296 ? -11.611 153.028 20.127  1.00 30.12  ? 314 LEU D CD1  1 
ATOM   10781 C CD2  . LEU D 2 296 ? -12.008 154.635 21.984  1.00 29.52  ? 314 LEU D CD2  1 
ATOM   10782 N N    . THR D 2 297 ? -17.306 152.957 21.308  1.00 26.10  ? 315 THR D N    1 
ATOM   10783 C CA   . THR D 2 297 ? -18.671 153.141 20.837  1.00 27.32  ? 315 THR D CA   1 
ATOM   10784 C C    . THR D 2 297 ? -19.427 153.841 21.928  1.00 35.23  ? 315 THR D C    1 
ATOM   10785 O O    . THR D 2 297 ? -20.633 154.010 21.839  1.00 35.04  ? 315 THR D O    1 
ATOM   10786 C CB   . THR D 2 297 ? -19.390 151.820 20.598  1.00 25.00  ? 315 THR D CB   1 
ATOM   10787 O OG1  . THR D 2 297 ? -19.437 151.070 21.812  1.00 36.79  ? 315 THR D OG1  1 
ATOM   10788 C CG2  . THR D 2 297 ? -18.717 151.028 19.520  1.00 31.20  ? 315 THR D CG2  1 
ATOM   10789 N N    . GLU D 2 298 ? -18.749 154.152 23.012  1.00 42.29  ? 316 GLU D N    1 
ATOM   10790 C CA   . GLU D 2 298 ? -19.333 154.889 24.088  1.00 35.17  ? 316 GLU D CA   1 
ATOM   10791 C C    . GLU D 2 298 ? -19.504 156.283 23.617  1.00 38.24  ? 316 GLU D C    1 
ATOM   10792 O O    . GLU D 2 298 ? -18.581 156.869 23.086  1.00 42.24  ? 316 GLU D O    1 
ATOM   10793 C CB   . GLU D 2 298 ? -18.398 154.841 25.280  1.00 31.46  ? 316 GLU D CB   1 
ATOM   10794 C CG   . GLU D 2 298 ? -18.286 153.471 25.922  1.00 38.27  ? 316 GLU D CG   1 
ATOM   10795 C CD   . GLU D 2 298 ? -19.244 153.259 27.063  1.00 36.32  ? 316 GLU D CD   1 
ATOM   10796 O OE1  . GLU D 2 298 ? -20.444 153.055 26.808  1.00 37.17  ? 316 GLU D OE1  1 
ATOM   10797 O OE2  . GLU D 2 298 ? -18.784 153.275 28.215  1.00 30.21  ? 316 GLU D OE2  1 
ATOM   10798 N N    . PRO D 2 299 ? -20.663 156.865 23.883  1.00 36.44  ? 317 PRO D N    1 
ATOM   10799 C CA   . PRO D 2 299 ? -20.964 158.180 23.341  1.00 33.25  ? 317 PRO D CA   1 
ATOM   10800 C C    . PRO D 2 299 ? -20.022 159.287 23.755  1.00 38.49  ? 317 PRO D C    1 
ATOM   10801 O O    . PRO D 2 299 ? -19.770 160.177 22.958  1.00 40.08  ? 317 PRO D O    1 
ATOM   10802 C CB   . PRO D 2 299 ? -22.362 158.440 23.857  1.00 27.36  ? 317 PRO D CB   1 
ATOM   10803 C CG   . PRO D 2 299 ? -22.544 157.536 25.024  1.00 30.14  ? 317 PRO D CG   1 
ATOM   10804 C CD   . PRO D 2 299 ? -21.786 156.312 24.651  1.00 33.50  ? 317 PRO D CD   1 
ATOM   10805 N N    . PHE D 2 300 ? -19.546 159.278 24.981  1.00 37.66  ? 318 PHE D N    1 
ATOM   10806 C CA   . PHE D 2 300 ? -18.703 160.341 25.467  1.00 33.82  ? 318 PHE D CA   1 
ATOM   10807 C C    . PHE D 2 300 ? -17.427 160.376 24.702  1.00 29.49  ? 318 PHE D C    1 
ATOM   10808 O O    . PHE D 2 300 ? -16.817 161.409 24.555  1.00 28.70  ? 318 PHE D O    1 
ATOM   10809 C CB   . PHE D 2 300 ? -18.504 160.269 26.986  1.00 36.67  ? 318 PHE D CB   1 
ATOM   10810 C CG   . PHE D 2 300 ? -17.732 159.090 27.471  1.00 30.81  ? 318 PHE D CG   1 
ATOM   10811 C CD1  . PHE D 2 300 ? -18.294 157.836 27.500  1.00 36.50  ? 318 PHE D CD1  1 
ATOM   10812 C CD2  . PHE D 2 300 ? -16.456 159.256 27.957  1.00 28.04  ? 318 PHE D CD2  1 
ATOM   10813 C CE1  . PHE D 2 300 ? -17.580 156.759 27.961  1.00 35.37  ? 318 PHE D CE1  1 
ATOM   10814 C CE2  . PHE D 2 300 ? -15.741 158.186 28.420  1.00 34.90  ? 318 PHE D CE2  1 
ATOM   10815 C CZ   . PHE D 2 300 ? -16.303 156.934 28.422  1.00 32.39  ? 318 PHE D CZ   1 
ATOM   10816 N N    . LEU D 2 301 ? -16.945 159.218 24.338  1.00 32.05  ? 319 LEU D N    1 
ATOM   10817 C CA   . LEU D 2 301 ? -15.742 159.144 23.545  1.00 43.42  ? 319 LEU D CA   1 
ATOM   10818 C C    . LEU D 2 301 ? -15.935 159.633 22.120  1.00 41.45  ? 319 LEU D C    1 
ATOM   10819 O O    . LEU D 2 301 ? -15.055 160.234 21.544  1.00 40.29  ? 319 LEU D O    1 
ATOM   10820 C CB   . LEU D 2 301 ? -15.124 157.739 23.640  1.00 41.79  ? 319 LEU D CB   1 
ATOM   10821 C CG   . LEU D 2 301 ? -14.505 157.434 24.997  1.00 27.93  ? 319 LEU D CG   1 
ATOM   10822 C CD1  . LEU D 2 301 ? -13.826 156.086 25.002  1.00 27.95  ? 319 LEU D CD1  1 
ATOM   10823 C CD2  . LEU D 2 301 ? -13.504 158.514 25.331  1.00 26.45  ? 319 LEU D CD2  1 
ATOM   10824 N N    . GLN D 2 302 ? -17.079 159.340 21.537  1.00 33.35  ? 320 GLN D N    1 
ATOM   10825 C CA   . GLN D 2 302 ? -17.349 159.774 20.195  1.00 35.17  ? 320 GLN D CA   1 
ATOM   10826 C C    . GLN D 2 302 ? -17.411 161.261 20.128  1.00 37.01  ? 320 GLN D C    1 
ATOM   10827 O O    . GLN D 2 302 ? -17.163 161.842 19.102  1.00 39.25  ? 320 GLN D O    1 
ATOM   10828 C CB   . GLN D 2 302 ? -18.604 159.126 19.671  1.00 37.47  ? 320 GLN D CB   1 
ATOM   10829 C CG   . GLN D 2 302 ? -18.378 157.813 18.939  1.00 42.70  ? 320 GLN D CG   1 
ATOM   10830 C CD   . GLN D 2 302 ? -17.711 157.985 17.581  1.00 46.71  ? 320 GLN D CD   1 
ATOM   10831 O OE1  . GLN D 2 302 ? -16.498 158.161 17.486  1.00 45.07  ? 320 GLN D OE1  1 
ATOM   10832 N NE2  . GLN D 2 302 ? -18.504 157.911 16.519  1.00 50.64  ? 320 GLN D NE2  1 
ATOM   10833 N N    . SER D 2 303 ? -17.793 161.895 21.208  1.00 33.93  ? 321 SER D N    1 
ATOM   10834 C CA   . SER D 2 303 ? -17.831 163.338 21.269  1.00 28.98  ? 321 SER D CA   1 
ATOM   10835 C C    . SER D 2 303 ? -16.774 164.146 20.602  1.00 32.40  ? 321 SER D C    1 
ATOM   10836 O O    . SER D 2 303 ? -17.107 164.962 19.785  1.00 35.99  ? 321 SER D O    1 
ATOM   10837 C CB   . SER D 2 303 ? -17.947 163.762 22.713  1.00 29.12  ? 321 SER D CB   1 
ATOM   10838 O OG   . SER D 2 303 ? -16.697 163.777 23.360  1.00 53.35  ? 321 SER D OG   1 
ATOM   10839 N N    . ILE D 2 304 ? -15.509 163.938 20.923  1.00 31.58  ? 322 ILE D N    1 
ATOM   10840 C CA   . ILE D 2 304 ? -14.460 164.767 20.371  1.00 35.32  ? 322 ILE D CA   1 
ATOM   10841 C C    . ILE D 2 304 ? -14.204 164.411 18.950  1.00 36.22  ? 322 ILE D C    1 
ATOM   10842 O O    . ILE D 2 304 ? -13.802 165.217 18.131  1.00 39.00  ? 322 ILE D O    1 
ATOM   10843 C CB   . ILE D 2 304 ? -13.173 164.509 21.148  1.00 33.29  ? 322 ILE D CB   1 
ATOM   10844 C CG1  . ILE D 2 304 ? -12.027 165.436 20.730  1.00 41.96  ? 322 ILE D CG1  1 
ATOM   10845 C CG2  . ILE D 2 304 ? -12.781 163.043 21.075  1.00 33.43  ? 322 ILE D CG2  1 
ATOM   10846 C CD1  . ILE D 2 304 ? -10.858 165.409 21.686  1.00 45.54  ? 322 ILE D CD1  1 
ATOM   10847 N N    . PHE D 2 305 ? -14.511 163.178 18.641  1.00 39.62  ? 323 PHE D N    1 
ATOM   10848 C CA   . PHE D 2 305 ? -14.309 162.671 17.318  1.00 37.51  ? 323 PHE D CA   1 
ATOM   10849 C C    . PHE D 2 305 ? -15.361 163.383 16.542  1.00 41.41  ? 323 PHE D C    1 
ATOM   10850 O O    . PHE D 2 305 ? -15.084 164.151 15.653  1.00 42.45  ? 323 PHE D O    1 
ATOM   10851 C CB   . PHE D 2 305 ? -14.521 161.163 17.195  1.00 33.51  ? 323 PHE D CB   1 
ATOM   10852 C CG   . PHE D 2 305 ? -13.344 160.342 17.588  1.00 33.38  ? 323 PHE D CG   1 
ATOM   10853 C CD1  . PHE D 2 305 ? -12.092 160.624 17.101  1.00 34.00  ? 323 PHE D CD1  1 
ATOM   10854 C CD2  . PHE D 2 305 ? -13.499 159.265 18.425  1.00 32.73  ? 323 PHE D CD2  1 
ATOM   10855 C CE1  . PHE D 2 305 ? -11.009 159.858 17.451  1.00 30.25  ? 323 PHE D CE1  1 
ATOM   10856 C CE2  . PHE D 2 305 ? -12.421 158.495 18.783  1.00 37.48  ? 323 PHE D CE2  1 
ATOM   10857 C CZ   . PHE D 2 305 ? -11.172 158.794 18.295  1.00 31.90  ? 323 PHE D CZ   1 
ATOM   10858 N N    . ASP D 2 306 ? -16.605 163.128 16.868  1.00 38.40  ? 324 ASP D N    1 
ATOM   10859 C CA   . ASP D 2 306 ? -17.673 163.696 16.086  1.00 40.91  ? 324 ASP D CA   1 
ATOM   10860 C C    . ASP D 2 306 ? -17.781 165.226 16.112  1.00 40.74  ? 324 ASP D C    1 
ATOM   10861 O O    . ASP D 2 306 ? -18.615 165.779 15.424  1.00 44.89  ? 324 ASP D O    1 
ATOM   10862 C CB   . ASP D 2 306 ? -18.969 162.957 16.406  1.00 38.68  ? 324 ASP D CB   1 
ATOM   10863 C CG   . ASP D 2 306 ? -19.045 161.612 15.748  1.00 39.48  ? 324 ASP D CG   1 
ATOM   10864 O OD1  . ASP D 2 306 ? -18.253 161.346 14.829  1.00 40.30  ? 324 ASP D OD1  1 
ATOM   10865 O OD2  . ASP D 2 306 ? -19.909 160.817 16.147  1.00 40.65  ? 324 ASP D OD2  1 
ATOM   10866 N N    . LYS D 2 307 ? -16.935 165.915 16.861  1.00 37.90  ? 325 LYS D N    1 
ATOM   10867 C CA   . LYS D 2 307 ? -16.896 167.385 16.855  1.00 37.12  ? 325 LYS D CA   1 
ATOM   10868 C C    . LYS D 2 307 ? -15.613 167.830 16.206  1.00 37.50  ? 325 LYS D C    1 
ATOM   10869 O O    . LYS D 2 307 ? -15.157 168.953 16.387  1.00 29.90  ? 325 LYS D O    1 
ATOM   10870 C CB   . LYS D 2 307 ? -17.054 167.999 18.238  1.00 33.33  ? 325 LYS D CB   1 
ATOM   10871 C CG   . LYS D 2 307 ? -15.889 167.843 19.202  1.00 35.49  ? 325 LYS D CG   1 
ATOM   10872 C CD   . LYS D 2 307 ? -16.153 168.567 20.514  1.00 38.02  ? 325 LYS D CD   1 
ATOM   10873 C CE   . LYS D 2 307 ? -17.281 167.928 21.306  1.00 34.17  ? 325 LYS D CE   1 
ATOM   10874 N NZ   . LYS D 2 307 ? -16.984 167.896 22.762  1.00 35.22  ? 325 LYS D NZ   1 
ATOM   10875 N N    . ALA D 2 308 ? -14.922 166.927 15.545  1.00 38.18  ? 326 ALA D N    1 
ATOM   10876 C CA   . ALA D 2 308 ? -13.717 167.315 14.856  1.00 41.47  ? 326 ALA D CA   1 
ATOM   10877 C C    . ALA D 2 308 ? -13.994 166.881 13.506  1.00 47.27  ? 326 ALA D C    1 
ATOM   10878 O O    . ALA D 2 308 ? -13.108 166.875 12.664  1.00 45.26  ? 326 ALA D O    1 
ATOM   10879 C CB   . ALA D 2 308 ? -12.529 166.595 15.387  1.00 38.58  ? 326 ALA D CB   1 
ATOM   10880 N N    . ASN D 2 309 ? -15.225 166.470 13.302  1.00 47.38  ? 327 ASN D N    1 
ATOM   10881 C CA   . ASN D 2 309 ? -15.666 166.056 11.998  1.00 49.21  ? 327 ASN D CA   1 
ATOM   10882 C C    . ASN D 2 309 ? -14.894 164.847 11.566  1.00 50.49  ? 327 ASN D C    1 
ATOM   10883 O O    . ASN D 2 309 ? -14.658 164.649 10.374  1.00 51.45  ? 327 ASN D O    1 
ATOM   10884 C CB   . ASN D 2 309 ? -15.665 167.222 11.000  1.00 49.75  ? 327 ASN D CB   1 
ATOM   10885 C CG   . ASN D 2 309 ? -16.548 168.371 11.441  1.00 50.88  ? 327 ASN D CG   1 
ATOM   10886 O OD1  . ASN D 2 309 ? -17.617 168.167 12.008  1.00 62.06  ? 327 ASN D OD1  1 
ATOM   10887 N ND2  . ASN D 2 309 ? -16.099 169.587 11.184  1.00 43.80  ? 327 ASN D ND2  1 
ATOM   10888 N N    . ILE D 2 310 ? -14.491 164.023 12.538  1.00 48.54  ? 328 ILE D N    1 
ATOM   10889 C CA   . ILE D 2 310 ? -13.810 162.778 12.222  1.00 39.04  ? 328 ILE D CA   1 
ATOM   10890 C C    . ILE D 2 310 ? -14.700 161.633 12.565  1.00 37.22  ? 328 ILE D C    1 
ATOM   10891 O O    . ILE D 2 310 ? -15.461 161.707 13.499  1.00 37.88  ? 328 ILE D O    1 
ATOM   10892 C CB   . ILE D 2 310 ? -12.413 162.644 12.852  1.00 33.20  ? 328 ILE D CB   1 
ATOM   10893 C CG1  . ILE D 2 310 ? -12.366 163.107 14.279  1.00 34.62  ? 328 ILE D CG1  1 
ATOM   10894 C CG2  . ILE D 2 310 ? -11.408 163.446 12.055  1.00 39.04  ? 328 ILE D CG2  1 
ATOM   10895 C CD1  . ILE D 2 310 ? -10.957 163.293 14.761  1.00 37.26  ? 328 ILE D CD1  1 
ATOM   10896 N N    . LYS D 2 311 ? -14.623 160.563 11.791  1.00 41.33  ? 329 LYS D N    1 
ATOM   10897 C CA   . LYS D 2 311 ? -15.375 159.365 12.060  1.00 40.77  ? 329 LYS D CA   1 
ATOM   10898 C C    . LYS D 2 311 ? -14.459 158.268 12.360  1.00 44.71  ? 329 LYS D C    1 
ATOM   10899 O O    . LYS D 2 311 ? -13.256 158.448 12.262  1.00 48.30  ? 329 LYS D O    1 
ATOM   10900 C CB   . LYS D 2 311 ? -16.087 158.968 10.782  1.00 41.99  ? 329 LYS D CB   1 
ATOM   10901 C CG   . LYS D 2 311 ? -17.063 157.806 10.905  1.00 53.46  ? 329 LYS D CG   1 
ATOM   10902 C CD   . LYS D 2 311 ? -17.648 157.386 9.561   1.00 53.66  ? 329 LYS D CD   1 
ATOM   10903 C CE   . LYS D 2 311 ? -18.842 156.453 9.737   1.00 52.77  ? 329 LYS D CE   1 
ATOM   10904 N NZ   . LYS D 2 311 ? -18.515 155.208 10.481  1.00 44.19  ? 329 LYS D NZ   1 
ATOM   10905 N N    . LEU D 2 312 ? -14.997 157.112 12.707  1.00 43.41  ? 330 LEU D N    1 
ATOM   10906 C CA   . LEU D 2 312 ? -14.161 155.967 12.979  1.00 38.46  ? 330 LEU D CA   1 
ATOM   10907 C C    . LEU D 2 312 ? -14.688 154.783 12.225  1.00 34.90  ? 330 LEU D C    1 
ATOM   10908 O O    . LEU D 2 312 ? -15.867 154.497 12.289  1.00 32.84  ? 330 LEU D O    1 
ATOM   10909 C CB   . LEU D 2 312 ? -13.972 155.657 14.452  1.00 34.82  ? 330 LEU D CB   1 
ATOM   10910 C CG   . LEU D 2 312 ? -12.658 155.805 15.187  1.00 34.44  ? 330 LEU D CG   1 
ATOM   10911 C CD1  . LEU D 2 312 ? -12.003 157.148 14.941  1.00 33.69  ? 330 LEU D CD1  1 
ATOM   10912 C CD2  . LEU D 2 312 ? -12.990 155.658 16.653  1.00 35.90  ? 330 LEU D CD2  1 
ATOM   10913 N N    . ASN D 2 313 ? -13.814 154.100 11.489  1.00 28.97  ? 331 ASN D N    1 
ATOM   10914 C CA   . ASN D 2 313 ? -14.194 152.918 10.738  1.00 28.48  ? 331 ASN D CA   1 
ATOM   10915 C C    . ASN D 2 313 ? -14.276 151.789 11.665  1.00 26.58  ? 331 ASN D C    1 
ATOM   10916 O O    . ASN D 2 313 ? -14.986 150.842 11.395  1.00 24.86  ? 331 ASN D O    1 
ATOM   10917 C CB   . ASN D 2 313 ? -13.222 152.609 9.588   1.00 28.62  ? 331 ASN D CB   1 
ATOM   10918 C CG   . ASN D 2 313 ? -11.776 152.613 9.975   1.00 27.05  ? 331 ASN D CG   1 
ATOM   10919 O OD1  . ASN D 2 313 ? -11.417 152.766 11.127  1.00 32.78  ? 331 ASN D OD1  1 
ATOM   10920 N ND2  . ASN D 2 313 ? -10.925 152.429 8.984   1.00 26.17  ? 331 ASN D ND2  1 
ATOM   10921 N N    . TYR D 2 314 ? -13.535 151.879 12.751  1.00 27.38  ? 332 TYR D N    1 
ATOM   10922 C CA   . TYR D 2 314 ? -13.507 150.852 13.764  1.00 24.39  ? 332 TYR D CA   1 
ATOM   10923 C C    . TYR D 2 314 ? -12.895 149.619 13.224  1.00 20.06  ? 332 TYR D C    1 
ATOM   10924 O O    . TYR D 2 314 ? -13.333 148.537 13.490  1.00 20.43  ? 332 TYR D O    1 
ATOM   10925 C CB   . TYR D 2 314 ? -14.883 150.615 14.361  1.00 27.94  ? 332 TYR D CB   1 
ATOM   10926 C CG   . TYR D 2 314 ? -15.418 151.743 15.207  1.00 29.01  ? 332 TYR D CG   1 
ATOM   10927 C CD1  . TYR D 2 314 ? -14.809 152.097 16.396  1.00 35.08  ? 332 TYR D CD1  1 
ATOM   10928 C CD2  . TYR D 2 314 ? -16.552 152.431 14.829  1.00 28.87  ? 332 TYR D CD2  1 
ATOM   10929 C CE1  . TYR D 2 314 ? -15.307 153.119 17.175  1.00 33.21  ? 332 TYR D CE1  1 
ATOM   10930 C CE2  . TYR D 2 314 ? -17.055 153.457 15.600  1.00 42.51  ? 332 TYR D CE2  1 
ATOM   10931 C CZ   . TYR D 2 314 ? -16.428 153.797 16.771  1.00 33.75  ? 332 TYR D CZ   1 
ATOM   10932 O OH   . TYR D 2 314 ? -16.934 154.815 17.533  1.00 22.84  ? 332 TYR D OH   1 
ATOM   10933 N N    . GLY D 2 315 ? -11.850 149.794 12.469  1.00 17.43  ? 333 GLY D N    1 
ATOM   10934 C CA   . GLY D 2 315 ? -11.173 148.667 11.897  1.00 23.24  ? 333 GLY D CA   1 
ATOM   10935 C C    . GLY D 2 315 ? -11.993 147.794 10.997  1.00 28.25  ? 333 GLY D C    1 
ATOM   10936 O O    . GLY D 2 315 ? -11.784 146.599 10.969  1.00 33.42  ? 333 GLY D O    1 
ATOM   10937 N N    . VAL D 2 316 ? -12.905 148.372 10.242  1.00 26.98  ? 334 VAL D N    1 
ATOM   10938 C CA   . VAL D 2 316 ? -13.777 147.594 9.415   1.00 24.73  ? 334 VAL D CA   1 
ATOM   10939 C C    . VAL D 2 316 ? -13.107 147.539 8.105   1.00 27.77  ? 334 VAL D C    1 
ATOM   10940 O O    . VAL D 2 316 ? -12.390 148.456 7.736   1.00 24.04  ? 334 VAL D O    1 
ATOM   10941 C CB   . VAL D 2 316 ? -15.184 148.181 9.310   1.00 21.31  ? 334 VAL D CB   1 
ATOM   10942 C CG1  . VAL D 2 316 ? -15.201 149.435 8.463   1.00 25.96  ? 334 VAL D CG1  1 
ATOM   10943 C CG2  . VAL D 2 316 ? -16.151 147.158 8.749   1.00 23.43  ? 334 VAL D CG2  1 
ATOM   10944 N N    . LEU D 2 317 ? -13.309 146.448 7.398   1.00 31.34  ? 335 LEU D N    1 
ATOM   10945 C CA   . LEU D 2 317 ? -12.659 146.246 6.146   1.00 33.79  ? 335 LEU D CA   1 
ATOM   10946 C C    . LEU D 2 317 ? -13.608 145.563 5.207   1.00 35.25  ? 335 LEU D C    1 
ATOM   10947 O O    . LEU D 2 317 ? -14.650 145.096 5.626   1.00 28.04  ? 335 LEU D O    1 
ATOM   10948 C CB   . LEU D 2 317 ? -11.412 145.408 6.358   1.00 30.23  ? 335 LEU D CB   1 
ATOM   10949 C CG   . LEU D 2 317 ? -10.147 146.126 6.820   1.00 26.23  ? 335 LEU D CG   1 
ATOM   10950 C CD1  . LEU D 2 317 ? -9.004  145.140 6.815   1.00 25.91  ? 335 LEU D CD1  1 
ATOM   10951 C CD2  . LEU D 2 317 ? -9.839  147.275 5.879   1.00 36.55  ? 335 LEU D CD2  1 
ATOM   10952 N N    . ASP D 2 318 ? -13.314 145.611 3.921   1.00 40.90  ? 336 ASP D N    1 
ATOM   10953 C CA   . ASP D 2 318 ? -14.117 144.929 2.932   1.00 36.56  ? 336 ASP D CA   1 
ATOM   10954 C C    . ASP D 2 318 ? -13.923 143.440 2.583   1.00 41.00  ? 336 ASP D C    1 
ATOM   10955 O O    . ASP D 2 318 ? -14.879 142.677 2.566   1.00 42.22  ? 336 ASP D O    1 
ATOM   10956 C CB   . ASP D 2 318 ? -14.038 145.754 1.671   1.00 30.08  ? 336 ASP D CB   1 
ATOM   10957 C CG   . ASP D 2 318 ? -14.299 147.216 1.919   1.00 37.02  ? 336 ASP D CG   1 
ATOM   10958 O OD1  . ASP D 2 318 ? -13.398 147.902 2.435   1.00 38.28  ? 336 ASP D OD1  1 
ATOM   10959 O OD2  . ASP D 2 318 ? -15.404 147.683 1.587   1.00 34.80  ? 336 ASP D OD2  1 
ATOM   10960 N N    . ASP D 2 319 ? -12.700 143.009 2.342   1.00 35.62  ? 337 ASP D N    1 
ATOM   10961 C CA   . ASP D 2 319 ? -12.464 141.622 1.937   1.00 37.42  ? 337 ASP D CA   1 
ATOM   10962 C C    . ASP D 2 319 ? -11.980 140.676 3.020   1.00 42.15  ? 337 ASP D C    1 
ATOM   10963 O O    . ASP D 2 319 ? -10.812 140.340 3.129   1.00 43.54  ? 337 ASP D O    1 
ATOM   10964 C CB   . ASP D 2 319 ? -11.212 141.648 1.100   1.00 48.71  ? 337 ASP D CB   1 
ATOM   10965 C CG   . ASP D 2 319 ? -10.010 142.166 1.866   1.00 49.55  ? 337 ASP D CG   1 
ATOM   10966 O OD1  . ASP D 2 319 ? -10.167 142.578 3.032   1.00 47.13  ? 337 ASP D OD1  1 
ATOM   10967 O OD2  . ASP D 2 319 ? -8.895  142.148 1.310   1.00 68.57  ? 337 ASP D OD2  1 
ATOM   10968 N N    . THR D 2 320 ? -12.910 140.228 3.833   1.00 40.44  ? 338 THR D N    1 
ATOM   10969 C CA   . THR D 2 320 ? -12.536 139.482 5.015   1.00 36.44  ? 338 THR D CA   1 
ATOM   10970 C C    . THR D 2 320 ? -12.901 138.065 4.674   1.00 33.27  ? 338 THR D C    1 
ATOM   10971 O O    . THR D 2 320 ? -13.038 137.244 5.536   1.00 25.19  ? 338 THR D O    1 
ATOM   10972 C CB   . THR D 2 320 ? -13.301 139.882 6.251   1.00 36.06  ? 338 THR D CB   1 
ATOM   10973 O OG1  . THR D 2 320 ? -14.699 139.696 6.031   1.00 49.24  ? 338 THR D OG1  1 
ATOM   10974 C CG2  . THR D 2 320 ? -13.039 141.336 6.580   1.00 37.40  ? 338 THR D CG2  1 
ATOM   10975 N N    . HIS D 2 321 ? -13.007 137.779 3.383   1.00 40.13  ? 339 HIS D N    1 
ATOM   10976 C CA   . HIS D 2 321 ? -13.397 136.451 2.906   1.00 36.73  ? 339 HIS D CA   1 
ATOM   10977 C C    . HIS D 2 321 ? -12.270 135.571 3.227   1.00 36.97  ? 339 HIS D C    1 
ATOM   10978 O O    . HIS D 2 321 ? -12.466 134.394 3.400   1.00 32.62  ? 339 HIS D O    1 
ATOM   10979 C CB   . HIS D 2 321 ? -13.687 136.418 1.413   1.00 39.06  ? 339 HIS D CB   1 
ATOM   10980 C CG   . HIS D 2 321 ? -12.663 137.108 0.567   1.00 55.73  ? 339 HIS D CG   1 
ATOM   10981 N ND1  . HIS D 2 321 ? -12.797 138.415 0.155   1.00 58.53  ? 339 HIS D ND1  1 
ATOM   10982 C CD2  . HIS D 2 321 ? -11.502 136.663 0.028   1.00 62.79  ? 339 HIS D CD2  1 
ATOM   10983 C CE1  . HIS D 2 321 ? -11.756 138.752 -0.583  1.00 64.19  ? 339 HIS D CE1  1 
ATOM   10984 N NE2  . HIS D 2 321 ? -10.954 137.707 -0.675  1.00 59.52  ? 339 HIS D NE2  1 
ATOM   10985 N N    . ALA D 2 322 ? -11.079 136.120 3.242   1.00 34.01  ? 340 ALA D N    1 
ATOM   10986 C CA   . ALA D 2 322 ? -9.911  135.385 3.632   1.00 30.82  ? 340 ALA D CA   1 
ATOM   10987 C C    . ALA D 2 322 ? -9.980  135.091 5.073   1.00 30.02  ? 340 ALA D C    1 
ATOM   10988 O O    . ALA D 2 322 ? -9.501  134.060 5.494   1.00 28.60  ? 340 ALA D O    1 
ATOM   10989 C CB   . ALA D 2 322 ? -8.709  136.248 3.370   1.00 36.25  ? 340 ALA D CB   1 
ATOM   10990 N N    . GLU D 2 323 ? -10.543 136.003 5.845   1.00 23.69  ? 341 GLU D N    1 
ATOM   10991 C CA   . GLU D 2 323 ? -10.636 135.830 7.258   1.00 20.43  ? 341 GLU D CA   1 
ATOM   10992 C C    . GLU D 2 323 ? -11.862 135.046 7.645   1.00 24.55  ? 341 GLU D C    1 
ATOM   10993 O O    . GLU D 2 323 ? -11.813 134.286 8.589   1.00 29.23  ? 341 GLU D O    1 
ATOM   10994 C CB   . GLU D 2 323 ? -10.610 137.175 7.890   1.00 23.38  ? 341 GLU D CB   1 
ATOM   10995 C CG   . GLU D 2 323 ? -9.255  137.831 7.848   1.00 25.72  ? 341 GLU D CG   1 
ATOM   10996 C CD   . GLU D 2 323 ? -9.177  138.935 6.833   1.00 26.21  ? 341 GLU D CD   1 
ATOM   10997 O OE1  . GLU D 2 323 ? -9.844  139.966 7.019   1.00 29.93  ? 341 GLU D OE1  1 
ATOM   10998 O OE2  . GLU D 2 323 ? -8.441  138.771 5.853   1.00 31.39  ? 341 GLU D OE2  1 
ATOM   10999 N N    . PHE D 2 324 ? -12.961 135.178 6.925   1.00 17.90  ? 342 PHE D N    1 
ATOM   11000 C CA   . PHE D 2 324 ? -14.138 134.374 7.166   1.00 18.98  ? 342 PHE D CA   1 
ATOM   11001 C C    . PHE D 2 324 ? -13.701 132.994 6.920   1.00 23.68  ? 342 PHE D C    1 
ATOM   11002 O O    . PHE D 2 324 ? -13.940 132.105 7.690   1.00 25.19  ? 342 PHE D O    1 
ATOM   11003 C CB   . PHE D 2 324 ? -15.164 134.702 6.115   1.00 21.44  ? 342 PHE D CB   1 
ATOM   11004 C CG   . PHE D 2 324 ? -16.587 134.593 6.570   1.00 18.99  ? 342 PHE D CG   1 
ATOM   11005 C CD1  . PHE D 2 324 ? -17.142 135.556 7.385   1.00 22.40  ? 342 PHE D CD1  1 
ATOM   11006 C CD2  . PHE D 2 324 ? -17.385 133.557 6.131   1.00 17.83  ? 342 PHE D CD2  1 
ATOM   11007 C CE1  . PHE D 2 324 ? -18.455 135.459 7.789   1.00 33.55  ? 342 PHE D CE1  1 
ATOM   11008 C CE2  . PHE D 2 324 ? -18.700 133.456 6.526   1.00 19.84  ? 342 PHE D CE2  1 
ATOM   11009 C CZ   . PHE D 2 324 ? -19.238 134.410 7.354   1.00 29.14  ? 342 PHE D CZ   1 
ATOM   11010 N N    . ARG D 2 325 ? -13.078 132.788 5.796   1.00 24.86  ? 343 ARG D N    1 
ATOM   11011 C CA   . ARG D 2 325 ? -12.586 131.488 5.444   1.00 28.09  ? 343 ARG D CA   1 
ATOM   11012 C C    . ARG D 2 325 ? -11.401 131.198 6.279   1.00 27.26  ? 343 ARG D C    1 
ATOM   11013 O O    . ARG D 2 325 ? -10.780 132.118 6.724   1.00 26.60  ? 343 ARG D O    1 
ATOM   11014 C CB   . ARG D 2 325 ? -12.255 131.449 3.963   1.00 35.67  ? 343 ARG D CB   1 
ATOM   11015 C CG   . ARG D 2 325 ? -11.888 130.092 3.391   1.00 44.98  ? 343 ARG D CG   1 
ATOM   11016 C CD   . ARG D 2 325 ? -12.125 130.026 1.889   1.00 37.08  ? 343 ARG D CD   1 
ATOM   11017 N NE   . ARG D 2 325 ? -11.976 131.314 1.222   1.00 32.94  ? 343 ARG D NE   1 
ATOM   11018 C CZ   . ARG D 2 325 ? -12.120 131.495 -0.087  1.00 49.67  ? 343 ARG D CZ   1 
ATOM   11019 N NH1  . ARG D 2 325 ? -12.408 130.469 -0.871  1.00 40.71  ? 343 ARG D NH1  1 
ATOM   11020 N NH2  . ARG D 2 325 ? -11.974 132.699 -0.617  1.00 53.10  ? 343 ARG D NH2  1 
ATOM   11021 N N    . LYS D 2 326 ? -11.129 129.940 6.557   1.00 32.70  ? 344 LYS D N    1 
ATOM   11022 C CA   . LYS D 2 326 ? -10.049 129.490 7.424   1.00 27.34  ? 344 LYS D CA   1 
ATOM   11023 C C    . LYS D 2 326 ? -10.606 129.615 8.804   1.00 27.78  ? 344 LYS D C    1 
ATOM   11024 O O    . LYS D 2 326 ? -9.913  129.400 9.757   1.00 37.80  ? 344 LYS D O    1 
ATOM   11025 C CB   . LYS D 2 326 ? -8.763  130.339 7.429   1.00 19.62  ? 344 LYS D CB   1 
ATOM   11026 C CG   . LYS D 2 326 ? -7.782  129.994 6.332   1.00 29.38  ? 344 LYS D CG   1 
ATOM   11027 C CD   . LYS D 2 326 ? -6.442  130.676 6.531   1.00 21.71  ? 344 LYS D CD   1 
ATOM   11028 C CE   . LYS D 2 326 ? -5.475  130.235 5.445   1.00 33.33  ? 344 LYS D CE   1 
ATOM   11029 N NZ   . LYS D 2 326 ? -4.168  130.941 5.480   1.00 34.98  ? 344 LYS D NZ   1 
ATOM   11030 N N    . ALA D 2 327 ? -11.897 129.896 8.908   1.00 27.18  ? 345 ALA D N    1 
ATOM   11031 C CA   . ALA D 2 327 ? -12.529 130.005 10.187  1.00 26.47  ? 345 ALA D CA   1 
ATOM   11032 C C    . ALA D 2 327 ? -13.604 129.052 9.926   1.00 31.23  ? 345 ALA D C    1 
ATOM   11033 O O    . ALA D 2 327 ? -14.096 128.424 10.834  1.00 33.25  ? 345 ALA D O    1 
ATOM   11034 C CB   . ALA D 2 327 ? -13.063 131.343 10.553  1.00 17.85  ? 345 ALA D CB   1 
ATOM   11035 N N    . GLN D 2 328 ? -14.027 128.957 8.688   1.00 29.85  ? 346 GLN D N    1 
ATOM   11036 C CA   . GLN D 2 328 ? -14.985 127.933 8.321   1.00 30.35  ? 346 GLN D CA   1 
ATOM   11037 C C    . GLN D 2 328 ? -14.352 126.563 8.387   1.00 21.80  ? 346 GLN D C    1 
ATOM   11038 O O    . GLN D 2 328 ? -14.987 125.602 8.782   1.00 17.55  ? 346 GLN D O    1 
ATOM   11039 C CB   . GLN D 2 328 ? -15.490 128.227 6.924   1.00 40.09  ? 346 GLN D CB   1 
ATOM   11040 C CG   . GLN D 2 328 ? -15.996 129.651 6.731   1.00 37.02  ? 346 GLN D CG   1 
ATOM   11041 C CD   . GLN D 2 328 ? -16.384 129.960 5.300   1.00 36.17  ? 346 GLN D CD   1 
ATOM   11042 O OE1  . GLN D 2 328 ? -15.605 129.758 4.376   1.00 40.15  ? 346 GLN D OE1  1 
ATOM   11043 N NE2  . GLN D 2 328 ? -17.587 130.467 5.114   1.00 26.80  ? 346 GLN D NE2  1 
ATOM   11044 N N    . ASP D 2 329 ? -13.102 126.470 7.974   1.00 21.42  ? 347 ASP D N    1 
ATOM   11045 C CA   . ASP D 2 329 ? -12.389 125.224 7.979   1.00 20.22  ? 347 ASP D CA   1 
ATOM   11046 C C    . ASP D 2 329 ? -11.995 124.845 9.379   1.00 21.86  ? 347 ASP D C    1 
ATOM   11047 O O    . ASP D 2 329 ? -11.743 123.687 9.646   1.00 23.41  ? 347 ASP D O    1 
ATOM   11048 C CB   . ASP D 2 329 ? -11.139 125.392 7.150   1.00 24.61  ? 347 ASP D CB   1 
ATOM   11049 C CG   . ASP D 2 329 ? -11.411 125.903 5.760   1.00 36.66  ? 347 ASP D CG   1 
ATOM   11050 O OD1  . ASP D 2 329 ? -12.454 125.545 5.183   1.00 40.50  ? 347 ASP D OD1  1 
ATOM   11051 O OD2  . ASP D 2 329 ? -10.557 126.645 5.233   1.00 27.38  ? 347 ASP D OD2  1 
ATOM   11052 N N    . TYR D 2 330 ? -11.884 125.808 10.273  1.00 21.93  ? 348 TYR D N    1 
ATOM   11053 C CA   . TYR D 2 330 ? -11.619 125.535 11.669  1.00 14.84  ? 348 TYR D CA   1 
ATOM   11054 C C    . TYR D 2 330 ? -12.774 124.929 12.334  1.00 18.52  ? 348 TYR D C    1 
ATOM   11055 O O    . TYR D 2 330 ? -12.620 123.951 13.031  1.00 21.70  ? 348 TYR D O    1 
ATOM   11056 C CB   . TYR D 2 330 ? -11.404 126.868 12.333  1.00 16.50  ? 348 TYR D CB   1 
ATOM   11057 C CG   . TYR D 2 330 ? -10.918 126.859 13.744  1.00 23.74  ? 348 TYR D CG   1 
ATOM   11058 C CD1  . TYR D 2 330 ? -9.639  126.439 14.050  1.00 27.87  ? 348 TYR D CD1  1 
ATOM   11059 C CD2  . TYR D 2 330 ? -11.719 127.318 14.767  1.00 20.94  ? 348 TYR D CD2  1 
ATOM   11060 C CE1  . TYR D 2 330 ? -9.187  126.441 15.346  1.00 27.90  ? 348 TYR D CE1  1 
ATOM   11061 C CE2  . TYR D 2 330 ? -11.273 127.321 16.065  1.00 21.52  ? 348 TYR D CE2  1 
ATOM   11062 C CZ   . TYR D 2 330 ? -10.007 126.884 16.348  1.00 24.51  ? 348 TYR D CZ   1 
ATOM   11063 O OH   . TYR D 2 330 ? -9.559  126.893 17.640  1.00 23.71  ? 348 TYR D OH   1 
ATOM   11064 N N    . VAL D 2 331 ? -13.951 125.483 12.108  1.00 18.89  ? 349 VAL D N    1 
ATOM   11065 C CA   . VAL D 2 331 ? -15.169 124.986 12.707  1.00 17.64  ? 349 VAL D CA   1 
ATOM   11066 C C    . VAL D 2 331 ? -15.411 123.612 12.234  1.00 14.98  ? 349 VAL D C    1 
ATOM   11067 O O    . VAL D 2 331 ? -15.799 122.773 12.986  1.00 14.41  ? 349 VAL D O    1 
ATOM   11068 C CB   . VAL D 2 331 ? -16.331 125.857 12.271  1.00 21.20  ? 349 VAL D CB   1 
ATOM   11069 C CG1  . VAL D 2 331 ? -17.658 125.265 12.698  1.00 23.60  ? 349 VAL D CG1  1 
ATOM   11070 C CG2  . VAL D 2 331 ? -16.171 127.262 12.818  1.00 19.57  ? 349 VAL D CG2  1 
ATOM   11071 N N    . PHE D 2 332 ? -15.155 123.370 10.978  1.00 16.08  ? 350 PHE D N    1 
ATOM   11072 C CA   . PHE D 2 332 ? -15.300 122.070 10.421  1.00 18.69  ? 350 PHE D CA   1 
ATOM   11073 C C    . PHE D 2 332 ? -14.339 121.130 11.037  1.00 20.53  ? 350 PHE D C    1 
ATOM   11074 O O    . PHE D 2 332 ? -14.686 120.017 11.364  1.00 18.69  ? 350 PHE D O    1 
ATOM   11075 C CB   . PHE D 2 332 ? -14.961 122.189 8.973   1.00 20.41  ? 350 PHE D CB   1 
ATOM   11076 C CG   . PHE D 2 332 ? -14.991 120.903 8.240   1.00 32.66  ? 350 PHE D CG   1 
ATOM   11077 C CD1  . PHE D 2 332 ? -16.181 120.376 7.824   1.00 21.67  ? 350 PHE D CD1  1 
ATOM   11078 C CD2  . PHE D 2 332 ? -13.832 120.234 7.962   1.00 52.01  ? 350 PHE D CD2  1 
ATOM   11079 C CE1  . PHE D 2 332 ? -16.223 119.195 7.143   1.00 34.28  ? 350 PHE D CE1  1 
ATOM   11080 C CE2  . PHE D 2 332 ? -13.867 119.054 7.280   1.00 56.25  ? 350 PHE D CE2  1 
ATOM   11081 C CZ   . PHE D 2 332 ? -15.062 118.534 6.864   1.00 55.08  ? 350 PHE D CZ   1 
ATOM   11082 N N    . GLY D 2 333 ? -13.104 121.561 11.170  1.00 22.32  ? 351 GLY D N    1 
ATOM   11083 C CA   . GLY D 2 333 ? -12.078 120.739 11.789  1.00 26.40  ? 351 GLY D CA   1 
ATOM   11084 C C    . GLY D 2 333 ? -12.382 120.421 13.219  1.00 27.57  ? 351 GLY D C    1 
ATOM   11085 O O    . GLY D 2 333 ? -12.163 119.317 13.645  1.00 31.03  ? 351 GLY D O    1 
ATOM   11086 N N    . LEU D 2 334 ? -12.825 121.389 13.984  1.00 20.00  ? 352 LEU D N    1 
ATOM   11087 C CA   . LEU D 2 334 ? -13.303 121.126 15.323  1.00 17.56  ? 352 LEU D CA   1 
ATOM   11088 C C    . LEU D 2 334 ? -14.646 120.378 15.489  1.00 15.69  ? 352 LEU D C    1 
ATOM   11089 O O    . LEU D 2 334 ? -14.762 119.560 16.368  1.00 23.09  ? 352 LEU D O    1 
ATOM   11090 C CB   . LEU D 2 334 ? -13.279 122.433 16.086  1.00 22.72  ? 352 LEU D CB   1 
ATOM   11091 C CG   . LEU D 2 334 ? -11.952 122.779 16.728  1.00 18.92  ? 352 LEU D CG   1 
ATOM   11092 C CD1  . LEU D 2 334 ? -12.095 124.124 17.409  1.00 26.07  ? 352 LEU D CD1  1 
ATOM   11093 C CD2  . LEU D 2 334 ? -11.658 121.700 17.750  1.00 21.16  ? 352 LEU D CD2  1 
ATOM   11094 N N    . THR D 2 335 ? -15.661 120.668 14.699  1.00 12.16  ? 353 THR D N    1 
ATOM   11095 C CA   . THR D 2 335 ? -16.975 120.002 14.784  1.00 14.82  ? 353 THR D CA   1 
ATOM   11096 C C    . THR D 2 335 ? -17.063 118.550 14.438  1.00 14.50  ? 353 THR D C    1 
ATOM   11097 O O    . THR D 2 335 ? -17.757 117.788 15.075  1.00 14.17  ? 353 THR D O    1 
ATOM   11098 C CB   . THR D 2 335 ? -18.041 120.722 13.955  1.00 13.84  ? 353 THR D CB   1 
ATOM   11099 O OG1  . THR D 2 335 ? -17.572 120.917 12.625  1.00 23.75  ? 353 THR D OG1  1 
ATOM   11100 C CG2  . THR D 2 335 ? -18.395 122.055 14.568  1.00 12.84  ? 353 THR D CG2  1 
ATOM   11101 N N    . ILE D 2 336 ? -16.391 118.159 13.394  1.00 17.31  ? 354 ILE D N    1 
ATOM   11102 C CA   . ILE D 2 336 ? -16.364 116.772 13.012  1.00 18.77  ? 354 ILE D CA   1 
ATOM   11103 C C    . ILE D 2 336 ? -15.230 116.200 13.836  1.00 22.15  ? 354 ILE D C    1 
ATOM   11104 O O    . ILE D 2 336 ? -15.072 115.006 13.900  1.00 21.76  ? 354 ILE D O    1 
ATOM   11105 C CB   . ILE D 2 336 ? -16.196 116.647 11.498  1.00 19.94  ? 354 ILE D CB   1 
ATOM   11106 C CG1  . ILE D 2 336 ? -16.995 117.718 10.792  1.00 20.21  ? 354 ILE D CG1  1 
ATOM   11107 C CG2  . ILE D 2 336 ? -16.689 115.302 10.996  1.00 26.89  ? 354 ILE D CG2  1 
ATOM   11108 C CD1  . ILE D 2 336 ? -17.220 117.363 9.356   1.00 23.04  ? 354 ILE D CD1  1 
ATOM   11109 N N    . GLN D 2 337 ? -14.392 117.032 14.424  1.00 21.22  ? 355 GLN D N    1 
ATOM   11110 C CA   . GLN D 2 337 ? -13.423 116.546 15.381  1.00 16.02  ? 355 GLN D CA   1 
ATOM   11111 C C    . GLN D 2 337 ? -14.102 115.831 16.507  1.00 18.40  ? 355 GLN D C    1 
ATOM   11112 O O    . GLN D 2 337 ? -13.790 114.726 16.862  1.00 16.77  ? 355 GLN D O    1 
ATOM   11113 C CB   . GLN D 2 337 ? -12.497 117.634 15.868  1.00 18.76  ? 355 GLN D CB   1 
ATOM   11114 C CG   . GLN D 2 337 ? -11.386 117.097 16.754  1.00 23.32  ? 355 GLN D CG   1 
ATOM   11115 C CD   . GLN D 2 337 ? -10.434 116.180 16.034  1.00 27.42  ? 355 GLN D CD   1 
ATOM   11116 O OE1  . GLN D 2 337 ? -10.534 114.964 16.141  1.00 45.19  ? 355 GLN D OE1  1 
ATOM   11117 N NE2  . GLN D 2 337 ? -9.502  116.756 15.303  1.00 24.16  ? 355 GLN D NE2  1 
ATOM   11118 N N    . SER D 2 338 ? -15.092 116.492 17.064  1.00 21.15  ? 356 SER D N    1 
ATOM   11119 C CA   . SER D 2 338 ? -15.914 115.881 18.081  1.00 18.88  ? 356 SER D CA   1 
ATOM   11120 C C    . SER D 2 338 ? -16.583 114.626 17.655  1.00 20.57  ? 356 SER D C    1 
ATOM   11121 O O    . SER D 2 338 ? -16.757 113.722 18.431  1.00 18.90  ? 356 SER D O    1 
ATOM   11122 C CB   . SER D 2 338 ? -16.930 116.899 18.485  1.00 12.50  ? 356 SER D CB   1 
ATOM   11123 O OG   . SER D 2 338 ? -17.699 116.407 19.560  1.00 12.80  ? 356 SER D OG   1 
ATOM   11124 N N    . ALA D 2 339 ? -16.979 114.571 16.411  1.00 16.77  ? 357 ALA D N    1 
ATOM   11125 C CA   . ALA D 2 339 ? -17.606 113.406 15.900  1.00 15.25  ? 357 ALA D CA   1 
ATOM   11126 C C    . ALA D 2 339 ? -16.756 112.185 15.894  1.00 18.07  ? 357 ALA D C    1 
ATOM   11127 O O    . ALA D 2 339 ? -17.202 111.135 16.294  1.00 21.10  ? 357 ALA D O    1 
ATOM   11128 C CB   . ALA D 2 339 ? -17.982 113.716 14.503  1.00 19.18  ? 357 ALA D CB   1 
ATOM   11129 N N    . MET D 2 340 ? -15.528 112.306 15.441  1.00 20.03  ? 358 MET D N    1 
ATOM   11130 C CA   . MET D 2 340 ? -14.622 111.193 15.414  1.00 18.55  ? 358 MET D CA   1 
ATOM   11131 C C    . MET D 2 340 ? -14.364 110.812 16.804  1.00 20.44  ? 358 MET D C    1 
ATOM   11132 O O    . MET D 2 340 ? -14.162 109.668 17.091  1.00 22.34  ? 358 MET D O    1 
ATOM   11133 C CB   . MET D 2 340 ? -13.348 111.526 14.683  1.00 18.44  ? 358 MET D CB   1 
ATOM   11134 C CG   . MET D 2 340 ? -12.459 112.623 15.226  1.00 25.96  ? 358 MET D CG   1 
ATOM   11135 S SD   . MET D 2 340 ? -10.710 112.368 14.897  1.00 31.43  ? 358 MET D SD   1 
ATOM   11136 C CE   . MET D 2 340 ? -10.526 110.776 15.678  1.00 14.35  ? 358 MET D CE   1 
ATOM   11137 N N    . HIS D 2 341 ? -14.282 111.792 17.672  1.00 17.94  ? 359 HIS D N    1 
ATOM   11138 C CA   . HIS D 2 341 ? -14.108 111.534 19.061  1.00 17.98  ? 359 HIS D CA   1 
ATOM   11139 C C    . HIS D 2 341 ? -15.299 110.883 19.694  1.00 24.10  ? 359 HIS D C    1 
ATOM   11140 O O    . HIS D 2 341 ? -15.159 109.949 20.445  1.00 32.99  ? 359 HIS D O    1 
ATOM   11141 C CB   . HIS D 2 341 ? -13.813 112.849 19.722  1.00 19.67  ? 359 HIS D CB   1 
ATOM   11142 C CG   . HIS D 2 341 ? -12.442 113.369 19.458  1.00 19.49  ? 359 HIS D CG   1 
ATOM   11143 N ND1  . HIS D 2 341 ? -12.183 114.706 19.276  1.00 15.03  ? 359 HIS D ND1  1 
ATOM   11144 C CD2  . HIS D 2 341 ? -11.253 112.735 19.356  1.00 19.88  ? 359 HIS D CD2  1 
ATOM   11145 C CE1  . HIS D 2 341 ? -10.892 114.873 19.067  1.00 19.74  ? 359 HIS D CE1  1 
ATOM   11146 N NE2  . HIS D 2 341 ? -10.305 113.694 19.115  1.00 17.06  ? 359 HIS D NE2  1 
ATOM   11147 N N    . HIS D 2 342 ? -16.491 111.344 19.384  1.00 21.02  ? 360 HIS D N    1 
ATOM   11148 C CA   . HIS D 2 342 ? -17.690 110.684 19.899  1.00 30.64  ? 360 HIS D CA   1 
ATOM   11149 C C    . HIS D 2 342 ? -17.838 109.286 19.352  1.00 30.70  ? 360 HIS D C    1 
ATOM   11150 O O    . HIS D 2 342 ? -18.191 108.387 20.089  1.00 36.74  ? 360 HIS D O    1 
ATOM   11151 C CB   . HIS D 2 342 ? -18.939 111.508 19.600  1.00 34.04  ? 360 HIS D CB   1 
ATOM   11152 C CG   . HIS D 2 342 ? -20.169 111.078 20.336  1.00 42.07  ? 360 HIS D CG   1 
ATOM   11153 N ND1  . HIS D 2 342 ? -20.748 111.848 21.320  1.00 43.43  ? 360 HIS D ND1  1 
ATOM   11154 C CD2  . HIS D 2 342 ? -20.955 109.982 20.207  1.00 46.97  ? 360 HIS D CD2  1 
ATOM   11155 C CE1  . HIS D 2 342 ? -21.823 111.234 21.782  1.00 49.02  ? 360 HIS D CE1  1 
ATOM   11156 N NE2  . HIS D 2 342 ? -21.972 110.100 21.123  1.00 45.77  ? 360 HIS D NE2  1 
ATOM   11157 N N    . GLU D 2 343 ? -17.565 109.086 18.071  1.00 24.47  ? 361 GLU D N    1 
ATOM   11158 C CA   . GLU D 2 343 ? -17.613 107.764 17.508  1.00 28.40  ? 361 GLU D CA   1 
ATOM   11159 C C    . GLU D 2 343 ? -16.411 106.961 17.927  1.00 25.42  ? 361 GLU D C    1 
ATOM   11160 O O    . GLU D 2 343 ? -16.382 105.774 17.734  1.00 30.87  ? 361 GLU D O    1 
ATOM   11161 C CB   . GLU D 2 343 ? -17.651 107.840 16.002  1.00 26.77  ? 361 GLU D CB   1 
ATOM   11162 C CG   . GLU D 2 343 ? -18.342 106.663 15.340  1.00 28.47  ? 361 GLU D CG   1 
ATOM   11163 C CD   . GLU D 2 343 ? -17.886 106.451 13.920  1.00 30.92  ? 361 GLU D CD   1 
ATOM   11164 O OE1  . GLU D 2 343 ? -17.461 107.428 13.284  1.00 25.56  ? 361 GLU D OE1  1 
ATOM   11165 O OE2  . GLU D 2 343 ? -17.938 105.298 13.453  1.00 36.84  ? 361 GLU D OE2  1 
ATOM   11166 N N    . LEU D 2 344 ? -15.417 107.579 18.513  1.00 20.20  ? 362 LEU D N    1 
ATOM   11167 C CA   . LEU D 2 344 ? -14.298 106.773 18.881  1.00 22.74  ? 362 LEU D CA   1 
ATOM   11168 C C    . LEU D 2 344 ? -14.629 106.224 20.191  1.00 29.85  ? 362 LEU D C    1 
ATOM   11169 O O    . LEU D 2 344 ? -14.236 105.130 20.546  1.00 35.39  ? 362 LEU D O    1 
ATOM   11170 C CB   . LEU D 2 344 ? -13.074 107.635 19.017  1.00 17.71  ? 362 LEU D CB   1 
ATOM   11171 C CG   . LEU D 2 344 ? -11.727 106.985 19.193  1.00 19.35  ? 362 LEU D CG   1 
ATOM   11172 C CD1  . LEU D 2 344 ? -10.971 107.105 17.886  1.00 23.66  ? 362 LEU D CD1  1 
ATOM   11173 C CD2  . LEU D 2 344 ? -11.054 107.756 20.305  1.00 24.94  ? 362 LEU D CD2  1 
ATOM   11174 N N    . GLN D 2 345 ? -15.358 107.002 20.955  1.00 26.32  ? 363 GLN D N    1 
ATOM   11175 C CA   . GLN D 2 345 ? -15.668 106.602 22.294  1.00 31.39  ? 363 GLN D CA   1 
ATOM   11176 C C    . GLN D 2 345 ? -16.985 105.881 22.399  1.00 46.37  ? 363 GLN D C    1 
ATOM   11177 O O    . GLN D 2 345 ? -17.314 105.349 23.447  1.00 53.75  ? 363 GLN D O    1 
ATOM   11178 C CB   . GLN D 2 345 ? -15.657 107.825 23.152  1.00 35.02  ? 363 GLN D CB   1 
ATOM   11179 C CG   . GLN D 2 345 ? -14.261 108.347 23.449  1.00 39.49  ? 363 GLN D CG   1 
ATOM   11180 C CD   . GLN D 2 345 ? -14.240 109.362 24.571  1.00 37.25  ? 363 GLN D CD   1 
ATOM   11181 O OE1  . GLN D 2 345 ? -13.420 109.272 25.482  1.00 36.89  ? 363 GLN D OE1  1 
ATOM   11182 N NE2  . GLN D 2 345 ? -15.145 110.335 24.514  1.00 20.41  ? 363 GLN D NE2  1 
ATOM   11183 N N    . GLU D 2 346 ? -17.768 105.855 21.332  1.00 44.76  ? 364 GLU D N    1 
ATOM   11184 C CA   . GLU D 2 346 ? -18.978 105.079 21.325  1.00 38.73  ? 364 GLU D CA   1 
ATOM   11185 C C    . GLU D 2 346 ? -18.598 103.881 20.535  1.00 43.73  ? 364 GLU D C    1 
ATOM   11186 O O    . GLU D 2 346 ? -19.411 103.320 19.824  1.00 47.74  ? 364 GLU D O    1 
ATOM   11187 C CB   . GLU D 2 346 ? -20.101 105.838 20.688  1.00 37.03  ? 364 GLU D CB   1 
ATOM   11188 C CG   . GLU D 2 346 ? -21.143 106.340 21.668  1.00 38.56  ? 364 GLU D CG   1 
ATOM   11189 C CD   . GLU D 2 346 ? -22.280 105.362 21.865  1.00 35.39  ? 364 GLU D CD   1 
ATOM   11190 O OE1  . GLU D 2 346 ? -23.140 105.257 20.970  1.00 33.92  ? 364 GLU D OE1  1 
ATOM   11191 O OE2  . GLU D 2 346 ? -22.317 104.703 22.920  1.00 30.55  ? 364 GLU D OE2  1 
ATOM   11192 N N    . ARG D 2 347 ? -17.342 103.478 20.638  1.00 44.55  ? 365 ARG D N    1 
ATOM   11193 C CA   . ARG D 2 347 ? -16.854 102.289 19.969  1.00 42.95  ? 365 ARG D CA   1 
ATOM   11194 C C    . ARG D 2 347 ? -15.884 101.711 20.930  1.00 47.26  ? 365 ARG D C    1 
ATOM   11195 O O    . ARG D 2 347 ? -15.402 100.606 20.757  1.00 49.71  ? 365 ARG D O    1 
ATOM   11196 C CB   . ARG D 2 347 ? -16.096 102.641 18.704  1.00 42.52  ? 365 ARG D CB   1 
ATOM   11197 C CG   . ARG D 2 347 ? -16.950 102.748 17.455  1.00 53.57  ? 365 ARG D CG   1 
ATOM   11198 C CD   . ARG D 2 347 ? -16.575 101.712 16.412  1.00 55.72  ? 365 ARG D CD   1 
ATOM   11199 N NE   . ARG D 2 347 ? -17.116 100.403 16.752  1.00 64.94  ? 365 ARG D NE   1 
ATOM   11200 C CZ   . ARG D 2 347 ? -18.323 99.973  16.409  1.00 59.83  ? 365 ARG D CZ   1 
ATOM   11201 N NH1  . ARG D 2 347 ? -19.133 100.737 15.694  1.00 48.26  ? 365 ARG D NH1  1 
ATOM   11202 N NH2  . ARG D 2 347 ? -18.715 98.766  16.780  1.00 68.32  ? 365 ARG D NH2  1 
ATOM   11203 N N    . PHE D 2 348 ? -15.534 102.488 21.933  1.00 45.38  ? 366 PHE D N    1 
ATOM   11204 C CA   . PHE D 2 348 ? -14.574 102.048 22.916  1.00 45.70  ? 366 PHE D CA   1 
ATOM   11205 C C    . PHE D 2 348 ? -15.492 101.450 23.900  1.00 47.73  ? 366 PHE D C    1 
ATOM   11206 O O    . PHE D 2 348 ? -15.167 100.483 24.572  1.00 45.50  ? 366 PHE D O    1 
ATOM   11207 C CB   . PHE D 2 348 ? -13.880 103.273 23.504  1.00 41.87  ? 366 PHE D CB   1 
ATOM   11208 C CG   . PHE D 2 348 ? -13.086 102.999 24.744  1.00 52.90  ? 366 PHE D CG   1 
ATOM   11209 C CD1  . PHE D 2 348 ? -11.921 102.252 24.687  1.00 52.28  ? 366 PHE D CD1  1 
ATOM   11210 C CD2  . PHE D 2 348 ? -13.494 103.501 25.966  1.00 45.21  ? 366 PHE D CD2  1 
ATOM   11211 C CE1  . PHE D 2 348 ? -11.184 102.003 25.829  1.00 43.76  ? 366 PHE D CE1  1 
ATOM   11212 C CE2  . PHE D 2 348 ? -12.765 103.252 27.108  1.00 38.36  ? 366 PHE D CE2  1 
ATOM   11213 C CZ   . PHE D 2 348 ? -11.607 102.504 27.042  1.00 34.83  ? 366 PHE D CZ   1 
ATOM   11214 N N    . LYS D 2 349 ? -16.667 102.034 23.992  1.00 49.65  ? 367 LYS D N    1 
ATOM   11215 C CA   . LYS D 2 349 ? -17.664 101.516 24.892  1.00 56.40  ? 367 LYS D CA   1 
ATOM   11216 C C    . LYS D 2 349 ? -18.402 100.510 24.016  1.00 56.12  ? 367 LYS D C    1 
ATOM   11217 O O    . LYS D 2 349 ? -19.536 100.728 23.592  1.00 55.80  ? 367 LYS D O    1 
ATOM   11218 C CB   . LYS D 2 349 ? -18.581 102.653 25.286  1.00 60.46  ? 367 LYS D CB   1 
ATOM   11219 C CG   . LYS D 2 349 ? -17.903 103.703 26.153  1.00 64.90  ? 367 LYS D CG   1 
ATOM   11220 C CD   . LYS D 2 349 ? -18.805 104.904 26.409  1.00 64.12  ? 367 LYS D CD   1 
ATOM   11221 C CE   . LYS D 2 349 ? -20.032 104.524 27.231  1.00 58.21  ? 367 LYS D CE   1 
ATOM   11222 N NZ   . LYS D 2 349 ? -20.867 105.700 27.595  1.00 59.34  ? 367 LYS D NZ   1 
ATOM   11223 N N    . ASN D 2 350 ? -17.744 99.397  23.752  1.00 45.06  ? 368 ASN D N    1 
ATOM   11224 C CA   . ASN D 2 350 ? -18.285 98.405  22.882  1.00 46.38  ? 368 ASN D CA   1 
ATOM   11225 C C    . ASN D 2 350 ? -17.191 97.388  22.774  1.00 45.55  ? 368 ASN D C    1 
ATOM   11226 O O    . ASN D 2 350 ? -16.594 97.243  21.717  1.00 38.78  ? 368 ASN D O    1 
ATOM   11227 C CB   . ASN D 2 350 ? -18.553 98.905  21.478  1.00 54.47  ? 368 ASN D CB   1 
ATOM   11228 C CG   . ASN D 2 350 ? -19.968 99.376  21.268  1.00 53.81  ? 368 ASN D CG   1 
ATOM   11229 O OD1  . ASN D 2 350 ? -20.877 98.998  21.997  1.00 63.77  ? 368 ASN D OD1  1 
ATOM   11230 N ND2  . ASN D 2 350 ? -20.163 100.203 20.250  1.00 43.07  ? 368 ASN D ND2  1 
ATOM   11231 N N    . GLY E 3 1   ? 18.555  146.806 55.488  1.00 25.94  ? -1  GLY E N    1 
ATOM   11232 C CA   . GLY E 3 1   ? 18.950  148.073 56.076  1.00 38.63  ? -1  GLY E CA   1 
ATOM   11233 C C    . GLY E 3 1   ? 20.093  148.863 55.463  1.00 32.36  ? -1  GLY E C    1 
ATOM   11234 O O    . GLY E 3 1   ? 20.559  149.805 56.068  1.00 43.58  ? -1  GLY E O    1 
ATOM   11235 N N    . SER E 3 2   ? 20.529  148.518 54.263  1.00 28.14  ? 0   SER E N    1 
ATOM   11236 C CA   . SER E 3 2   ? 21.643  149.197 53.624  1.00 31.11  ? 0   SER E CA   1 
ATOM   11237 C C    . SER E 3 2   ? 21.435  149.748 52.224  1.00 29.72  ? 0   SER E C    1 
ATOM   11238 O O    . SER E 3 2   ? 22.399  149.860 51.485  1.00 31.32  ? 0   SER E O    1 
ATOM   11239 C CB   . SER E 3 2   ? 22.879  148.309 53.628  1.00 32.11  ? 0   SER E CB   1 
ATOM   11240 O OG   . SER E 3 2   ? 23.965  148.921 54.304  1.00 27.37  ? 0   SER E OG   1 
ATOM   11241 N N    . MET E 3 3   ? 20.215  150.105 51.849  1.00 26.48  ? 1   MET E N    1 
ATOM   11242 C CA   . MET E 3 3   ? 20.008  150.767 50.569  1.00 33.31  ? 1   MET E CA   1 
ATOM   11243 C C    . MET E 3 3   ? 18.747  151.601 50.528  1.00 32.13  ? 1   MET E C    1 
ATOM   11244 O O    . MET E 3 3   ? 17.872  151.342 49.736  1.00 36.90  ? 1   MET E O    1 
ATOM   11245 C CB   . MET E 3 3   ? 20.003  149.779 49.392  1.00 29.52  ? 1   MET E CB   1 
ATOM   11246 C CG   . MET E 3 3   ? 21.052  150.032 48.332  1.00 28.32  ? 1   MET E CG   1 
ATOM   11247 S SD   . MET E 3 3   ? 20.678  149.232 46.776  1.00 19.73  ? 1   MET E SD   1 
ATOM   11248 C CE   . MET E 3 3   ? 18.915  149.427 46.727  1.00 28.04  ? 1   MET E CE   1 
ATOM   11249 N N    . GLN E 3 4   ? 18.654  152.625 51.347  1.00 21.11  ? 2   GLN E N    1 
ATOM   11250 C CA   . GLN E 3 4   ? 17.481  153.495 51.342  1.00 29.15  ? 2   GLN E CA   1 
ATOM   11251 C C    . GLN E 3 4   ? 17.067  153.906 49.966  1.00 31.20  ? 2   GLN E C    1 
ATOM   11252 O O    . GLN E 3 4   ? 17.865  154.388 49.238  1.00 28.14  ? 2   GLN E O    1 
ATOM   11253 C CB   . GLN E 3 4   ? 17.726  154.760 52.147  1.00 27.87  ? 2   GLN E CB   1 
ATOM   11254 C CG   . GLN E 3 4   ? 16.714  155.024 53.231  1.00 33.88  ? 2   GLN E CG   1 
ATOM   11255 C CD   . GLN E 3 4   ? 17.076  156.241 54.041  1.00 37.40  ? 2   GLN E CD   1 
ATOM   11256 O OE1  . GLN E 3 4   ? 17.708  157.162 53.536  1.00 34.07  ? 2   GLN E OE1  1 
ATOM   11257 N NE2  . GLN E 3 4   ? 16.684  156.250 55.306  1.00 38.70  ? 2   GLN E NE2  1 
ATOM   11258 N N    . ILE E 3 5   ? 15.810  153.721 49.607  1.00 25.33  ? 3   ILE E N    1 
ATOM   11259 C CA   . ILE E 3 5   ? 15.317  154.110 48.315  1.00 19.56  ? 3   ILE E CA   1 
ATOM   11260 C C    . ILE E 3 5   ? 14.080  154.852 48.614  1.00 17.76  ? 3   ILE E C    1 
ATOM   11261 O O    . ILE E 3 5   ? 13.717  154.992 49.761  1.00 21.04  ? 3   ILE E O    1 
ATOM   11262 C CB   . ILE E 3 5   ? 14.986  152.943 47.376  1.00 19.77  ? 3   ILE E CB   1 
ATOM   11263 C CG1  . ILE E 3 5   ? 14.223  151.850 48.098  1.00 21.23  ? 3   ILE E CG1  1 
ATOM   11264 C CG2  . ILE E 3 5   ? 16.238  152.402 46.711  1.00 25.09  ? 3   ILE E CG2  1 
ATOM   11265 C CD1  . ILE E 3 5   ? 13.257  151.126 47.200  1.00 17.56  ? 3   ILE E CD1  1 
ATOM   11266 N N    . PHE E 3 6   ? 13.408  155.329 47.581  1.00 15.11  ? 4   PHE E N    1 
ATOM   11267 C CA   . PHE E 3 6   ? 12.230  156.113 47.764  1.00 13.67  ? 4   PHE E CA   1 
ATOM   11268 C C    . PHE E 3 6   ? 11.164  155.757 46.780  1.00 13.74  ? 4   PHE E C    1 
ATOM   11269 O O    . PHE E 3 6   ? 11.443  155.481 45.647  1.00 12.94  ? 4   PHE E O    1 
ATOM   11270 C CB   . PHE E 3 6   ? 12.579  157.582 47.615  1.00 18.01  ? 4   PHE E CB   1 
ATOM   11271 C CG   . PHE E 3 6   ? 13.717  158.039 48.479  1.00 15.30  ? 4   PHE E CG   1 
ATOM   11272 C CD1  . PHE E 3 6   ? 13.564  158.148 49.840  1.00 15.36  ? 4   PHE E CD1  1 
ATOM   11273 C CD2  . PHE E 3 6   ? 14.931  158.355 47.925  1.00 15.20  ? 4   PHE E CD2  1 
ATOM   11274 C CE1  . PHE E 3 6   ? 14.608  158.544 50.636  1.00 14.35  ? 4   PHE E CE1  1 
ATOM   11275 C CE2  . PHE E 3 6   ? 15.974  158.765 48.714  1.00 13.00  ? 4   PHE E CE2  1 
ATOM   11276 C CZ   . PHE E 3 6   ? 15.814  158.858 50.071  1.00 11.88  ? 4   PHE E CZ   1 
ATOM   11277 N N    . VAL E 3 7   ? 9.923   155.758 47.231  1.00 13.43  ? 5   VAL E N    1 
ATOM   11278 C CA   . VAL E 3 7   ? 8.806   155.455 46.371  1.00 16.33  ? 5   VAL E CA   1 
ATOM   11279 C C    . VAL E 3 7   ? 7.832   156.591 46.389  1.00 15.90  ? 5   VAL E C    1 
ATOM   11280 O O    . VAL E 3 7   ? 7.159   156.782 47.373  1.00 15.02  ? 5   VAL E O    1 
ATOM   11281 C CB   . VAL E 3 7   ? 8.096   154.120 46.714  1.00 17.84  ? 5   VAL E CB   1 
ATOM   11282 C CG1  . VAL E 3 7   ? 7.442   153.518 45.491  1.00 12.79  ? 5   VAL E CG1  1 
ATOM   11283 C CG2  . VAL E 3 7   ? 9.072   153.105 47.283  1.00 16.08  ? 5   VAL E CG2  1 
ATOM   11284 N N    . LYS E 3 8   ? 7.702   157.314 45.272  1.00 16.11  ? 6   LYS E N    1 
ATOM   11285 C CA   . LYS E 3 8   ? 6.814   158.460 45.179  1.00 18.74  ? 6   LYS E CA   1 
ATOM   11286 C C    . LYS E 3 8   ? 5.562   158.077 44.516  1.00 18.96  ? 6   LYS E C    1 
ATOM   11287 O O    . LYS E 3 8   ? 5.571   157.316 43.589  1.00 16.73  ? 6   LYS E O    1 
ATOM   11288 C CB   . LYS E 3 8   ? 7.454   159.610 44.445  1.00 17.63  ? 6   LYS E CB   1 
ATOM   11289 C CG   . LYS E 3 8   ? 6.928   160.980 44.776  1.00 24.05  ? 6   LYS E CG   1 
ATOM   11290 C CD   . LYS E 3 8   ? 7.843   162.042 44.208  1.00 21.26  ? 6   LYS E CD   1 
ATOM   11291 C CE   . LYS E 3 8   ? 9.290   161.727 44.543  1.00 36.05  ? 6   LYS E CE   1 
ATOM   11292 N NZ   . LYS E 3 8   ? 9.932   162.694 45.478  1.00 30.85  ? 6   LYS E NZ   1 
ATOM   11293 N N    . THR E 3 9   ? 4.452   158.582 45.013  1.00 21.87  ? 7   THR E N    1 
ATOM   11294 C CA   . THR E 3 9   ? 3.186   158.199 44.493  1.00 19.81  ? 7   THR E CA   1 
ATOM   11295 C C    . THR E 3 9   ? 2.648   159.361 43.772  1.00 20.04  ? 7   THR E C    1 
ATOM   11296 O O    . THR E 3 9   ? 3.396   160.181 43.272  1.00 20.93  ? 7   THR E O    1 
ATOM   11297 C CB   . THR E 3 9   ? 2.284   157.611 45.599  1.00 20.66  ? 7   THR E CB   1 
ATOM   11298 O OG1  . THR E 3 9   ? 0.967   157.319 45.114  1.00 26.38  ? 7   THR E OG1  1 
ATOM   11299 C CG2  . THR E 3 9   ? 2.214   158.485 46.759  1.00 21.61  ? 7   THR E CG2  1 
ATOM   11300 N N    . LEU E 3 10  ? 1.346   159.425 43.639  1.00 21.67  ? 8   LEU E N    1 
ATOM   11301 C CA   . LEU E 3 10  ? 0.732   160.452 42.861  1.00 22.24  ? 8   LEU E CA   1 
ATOM   11302 C C    . LEU E 3 10  ? 0.233   161.560 43.742  1.00 22.64  ? 8   LEU E C    1 
ATOM   11303 O O    . LEU E 3 10  ? -0.418  162.476 43.276  1.00 22.16  ? 8   LEU E O    1 
ATOM   11304 C CB   . LEU E 3 10  ? -0.362  159.770 42.075  1.00 22.65  ? 8   LEU E CB   1 
ATOM   11305 C CG   . LEU E 3 10  ? 0.040   158.377 41.603  1.00 23.11  ? 8   LEU E CG   1 
ATOM   11306 C CD1  . LEU E 3 10  ? -1.142  157.439 41.482  1.00 20.85  ? 8   LEU E CD1  1 
ATOM   11307 C CD2  . LEU E 3 10  ? 0.852   158.437 40.323  1.00 20.81  ? 8   LEU E CD2  1 
ATOM   11308 N N    . THR E 3 11  ? 0.593   161.513 45.012  1.00 27.86  ? 9   THR E N    1 
ATOM   11309 C CA   . THR E 3 11  ? 0.195   162.509 45.944  1.00 22.33  ? 9   THR E CA   1 
ATOM   11310 C C    . THR E 3 11  ? 1.449   163.266 46.170  1.00 25.65  ? 9   THR E C    1 
ATOM   11311 O O    . THR E 3 11  ? 1.419   164.417 46.570  1.00 32.57  ? 9   THR E O    1 
ATOM   11312 C CB   . THR E 3 11  ? -0.262  161.866 47.234  1.00 20.65  ? 9   THR E CB   1 
ATOM   11313 O OG1  . THR E 3 11  ? -0.207  160.452 47.124  1.00 27.69  ? 9   THR E OG1  1 
ATOM   11314 C CG2  . THR E 3 11  ? -1.688  162.253 47.512  1.00 28.11  ? 9   THR E CG2  1 
ATOM   11315 N N    . GLY E 3 12  ? 2.579   162.641 45.895  1.00 25.69  ? 10  GLY E N    1 
ATOM   11316 C CA   . GLY E 3 12  ? 3.865   163.270 46.084  1.00 22.33  ? 10  GLY E CA   1 
ATOM   11317 C C    . GLY E 3 12  ? 4.406   162.699 47.335  1.00 24.44  ? 10  GLY E C    1 
ATOM   11318 O O    . GLY E 3 12  ? 5.433   163.125 47.829  1.00 30.91  ? 10  GLY E O    1 
ATOM   11319 N N    . LYS E 3 13  ? 3.730   161.700 47.851  1.00 20.12  ? 11  LYS E N    1 
ATOM   11320 C CA   . LYS E 3 13  ? 4.121   161.159 49.102  1.00 18.50  ? 11  LYS E CA   1 
ATOM   11321 C C    . LYS E 3 13  ? 5.179   160.223 48.859  1.00 22.56  ? 11  LYS E C    1 
ATOM   11322 O O    . LYS E 3 13  ? 4.969   159.174 48.301  1.00 25.14  ? 11  LYS E O    1 
ATOM   11323 C CB   . LYS E 3 13  ? 2.979   160.493 49.780  1.00 25.40  ? 11  LYS E CB   1 
ATOM   11324 C CG   . LYS E 3 13  ? 2.043   161.481 50.451  1.00 34.00  ? 11  LYS E CG   1 
ATOM   11325 C CD   . LYS E 3 13  ? 0.738   160.835 50.875  1.00 33.91  ? 11  LYS E CD   1 
ATOM   11326 C CE   . LYS E 3 13  ? -0.051  161.772 51.769  1.00 35.59  ? 11  LYS E CE   1 
ATOM   11327 N NZ   . LYS E 3 13  ? -1.518  161.616 51.595  1.00 40.39  ? 11  LYS E NZ   1 
ATOM   11328 N N    . THR E 3 14  ? 6.361   160.622 49.266  1.00 19.91  ? 12  THR E N    1 
ATOM   11329 C CA   . THR E 3 14  ? 7.498   159.823 49.074  1.00 18.22  ? 12  THR E CA   1 
ATOM   11330 C C    . THR E 3 14  ? 7.652   158.968 50.269  1.00 19.12  ? 12  THR E C    1 
ATOM   11331 O O    . THR E 3 14  ? 7.832   159.471 51.356  1.00 21.56  ? 12  THR E O    1 
ATOM   11332 C CB   . THR E 3 14  ? 8.688   160.718 48.913  1.00 22.20  ? 12  THR E CB   1 
ATOM   11333 O OG1  . THR E 3 14  ? 8.279   161.891 48.208  1.00 24.66  ? 12  THR E OG1  1 
ATOM   11334 C CG2  . THR E 3 14  ? 9.759   160.024 48.118  1.00 25.57  ? 12  THR E CG2  1 
ATOM   11335 N N    . ILE E 3 15  ? 7.566   157.657 50.080  1.00 20.61  ? 13  ILE E N    1 
ATOM   11336 C CA   . ILE E 3 15  ? 7.750   156.713 51.161  1.00 16.53  ? 13  ILE E CA   1 
ATOM   11337 C C    . ILE E 3 15  ? 9.185   156.334 51.180  1.00 16.14  ? 13  ILE E C    1 
ATOM   11338 O O    . ILE E 3 15  ? 9.890   156.519 50.210  1.00 22.61  ? 13  ILE E O    1 
ATOM   11339 C CB   . ILE E 3 15  ? 6.806   155.506 51.052  1.00 21.52  ? 13  ILE E CB   1 
ATOM   11340 C CG1  . ILE E 3 15  ? 7.460   154.264 50.465  1.00 22.46  ? 13  ILE E CG1  1 
ATOM   11341 C CG2  . ILE E 3 15  ? 5.560   155.865 50.256  1.00 20.41  ? 13  ILE E CG2  1 
ATOM   11342 C CD1  . ILE E 3 15  ? 6.573   153.051 50.557  1.00 17.27  ? 13  ILE E CD1  1 
ATOM   11343 N N    . THR E 3 16  ? 9.653   155.826 52.301  1.00 13.83  ? 14  THR E N    1 
ATOM   11344 C CA   . THR E 3 16  ? 11.059  155.532 52.438  1.00 22.12  ? 14  THR E CA   1 
ATOM   11345 C C    . THR E 3 16  ? 11.249  154.077 52.725  1.00 22.95  ? 14  THR E C    1 
ATOM   11346 O O    . THR E 3 16  ? 10.667  153.562 53.649  1.00 24.55  ? 14  THR E O    1 
ATOM   11347 C CB   . THR E 3 16  ? 11.709  156.437 53.522  1.00 25.43  ? 14  THR E CB   1 
ATOM   11348 O OG1  . THR E 3 16  ? 11.261  157.788 53.366  1.00 23.57  ? 14  THR E OG1  1 
ATOM   11349 C CG2  . THR E 3 16  ? 13.208  156.416 53.420  1.00 21.89  ? 14  THR E CG2  1 
ATOM   11350 N N    . LEU E 3 17  ? 12.063  153.409 51.922  1.00 21.73  ? 15  LEU E N    1 
ATOM   11351 C CA   . LEU E 3 17  ? 12.289  151.990 52.077  1.00 27.33  ? 15  LEU E CA   1 
ATOM   11352 C C    . LEU E 3 17  ? 13.739  151.593 52.294  1.00 31.06  ? 15  LEU E C    1 
ATOM   11353 O O    . LEU E 3 17  ? 14.609  152.215 51.760  1.00 26.00  ? 15  LEU E O    1 
ATOM   11354 C CB   . LEU E 3 17  ? 11.687  151.249 50.888  1.00 20.26  ? 15  LEU E CB   1 
ATOM   11355 C CG   . LEU E 3 17  ? 10.794  150.063 51.211  1.00 17.82  ? 15  LEU E CG   1 
ATOM   11356 C CD1  . LEU E 3 17  ? 9.346   150.480 51.102  1.00 17.26  ? 15  LEU E CD1  1 
ATOM   11357 C CD2  . LEU E 3 17  ? 11.096  148.949 50.240  1.00 19.37  ? 15  LEU E CD2  1 
ATOM   11358 N N    . GLU E 3 18  ? 13.984  150.569 53.107  1.00 31.59  ? 16  GLU E N    1 
ATOM   11359 C CA   . GLU E 3 18  ? 15.325  150.089 53.388  1.00 31.29  ? 16  GLU E CA   1 
ATOM   11360 C C    . GLU E 3 18  ? 15.422  148.731 52.824  1.00 27.63  ? 16  GLU E C    1 
ATOM   11361 O O    . GLU E 3 18  ? 14.835  147.804 53.353  1.00 29.28  ? 16  GLU E O    1 
ATOM   11362 C CB   . GLU E 3 18  ? 15.586  150.051 54.877  1.00 30.89  ? 16  GLU E CB   1 
ATOM   11363 C CG   . GLU E 3 18  ? 15.508  151.408 55.554  1.00 36.81  ? 16  GLU E CG   1 
ATOM   11364 C CD   . GLU E 3 18  ? 16.862  151.951 55.946  1.00 38.38  ? 16  GLU E CD   1 
ATOM   11365 O OE1  . GLU E 3 18  ? 17.803  151.867 55.136  1.00 33.83  ? 16  GLU E OE1  1 
ATOM   11366 O OE2  . GLU E 3 18  ? 16.982  152.470 57.070  1.00 46.45  ? 16  GLU E OE2  1 
ATOM   11367 N N    . VAL E 3 19  ? 16.214  148.584 51.767  1.00 25.04  ? 17  VAL E N    1 
ATOM   11368 C CA   . VAL E 3 19  ? 16.316  147.341 51.054  1.00 28.45  ? 17  VAL E CA   1 
ATOM   11369 C C    . VAL E 3 19  ? 17.745  146.990 50.777  1.00 27.73  ? 17  VAL E C    1 
ATOM   11370 O O    . VAL E 3 19  ? 18.631  147.634 51.287  1.00 29.23  ? 17  VAL E O    1 
ATOM   11371 C CB   . VAL E 3 19  ? 15.696  147.527 49.680  1.00 23.17  ? 17  VAL E CB   1 
ATOM   11372 C CG1  . VAL E 3 19  ? 14.248  147.103 49.663  1.00 27.13  ? 17  VAL E CG1  1 
ATOM   11373 C CG2  . VAL E 3 19  ? 15.850  148.939 49.203  1.00 17.43  ? 17  VAL E CG2  1 
ATOM   11374 N N    . GLU E 3 20  ? 17.984  145.962 49.969  1.00 22.52  ? 18  GLU E N    1 
ATOM   11375 C CA   . GLU E 3 20  ? 19.319  145.567 49.579  1.00 20.37  ? 18  GLU E CA   1 
ATOM   11376 C C    . GLU E 3 20  ? 19.228  145.331 48.115  1.00 20.61  ? 18  GLU E C    1 
ATOM   11377 O O    . GLU E 3 20  ? 18.151  145.177 47.606  1.00 25.51  ? 18  GLU E O    1 
ATOM   11378 C CB   . GLU E 3 20  ? 19.708  144.283 50.270  1.00 21.28  ? 18  GLU E CB   1 
ATOM   11379 C CG   . GLU E 3 20  ? 19.654  144.283 51.795  1.00 24.61  ? 18  GLU E CG   1 
ATOM   11380 C CD   . GLU E 3 20  ? 20.708  145.144 52.467  1.00 22.72  ? 18  GLU E CD   1 
ATOM   11381 O OE1  . GLU E 3 20  ? 21.766  145.423 51.869  1.00 20.46  ? 18  GLU E OE1  1 
ATOM   11382 O OE2  . GLU E 3 20  ? 20.474  145.535 53.621  1.00 19.57  ? 18  GLU E OE2  1 
ATOM   11383 N N    . PRO E 3 21  ? 20.386  145.307 47.381  1.00 16.72  ? 19  PRO E N    1 
ATOM   11384 C CA   . PRO E 3 21  ? 20.208  145.210 45.931  1.00 16.68  ? 19  PRO E CA   1 
ATOM   11385 C C    . PRO E 3 21  ? 19.909  143.888 45.357  1.00 16.96  ? 19  PRO E C    1 
ATOM   11386 O O    . PRO E 3 21  ? 20.051  143.702 44.175  1.00 17.62  ? 19  PRO E O    1 
ATOM   11387 C CB   . PRO E 3 21  ? 21.555  145.624 45.406  1.00 14.25  ? 19  PRO E CB   1 
ATOM   11388 C CG   . PRO E 3 21  ? 22.508  145.136 46.401  1.00 20.14  ? 19  PRO E CG   1 
ATOM   11389 C CD   . PRO E 3 21  ? 21.840  145.465 47.684  1.00 16.97  ? 19  PRO E CD   1 
ATOM   11390 N N    . SER E 3 22  ? 19.508  142.957 46.171  1.00 19.11  ? 20  SER E N    1 
ATOM   11391 C CA   . SER E 3 22  ? 19.292  141.617 45.717  1.00 25.18  ? 20  SER E CA   1 
ATOM   11392 C C    . SER E 3 22  ? 17.881  141.269 46.027  1.00 22.21  ? 20  SER E C    1 
ATOM   11393 O O    . SER E 3 22  ? 17.495  140.108 45.942  1.00 18.76  ? 20  SER E O    1 
ATOM   11394 C CB   . SER E 3 22  ? 20.208  140.718 46.512  1.00 23.93  ? 20  SER E CB   1 
ATOM   11395 O OG   . SER E 3 22  ? 20.645  141.341 47.702  1.00 16.92  ? 20  SER E OG   1 
ATOM   11396 N N    . ASP E 3 23  ? 17.093  142.267 46.382  1.00 16.50  ? 21  ASP E N    1 
ATOM   11397 C CA   . ASP E 3 23  ? 15.751  142.030 46.799  1.00 18.01  ? 21  ASP E CA   1 
ATOM   11398 C C    . ASP E 3 23  ? 14.872  142.147 45.624  1.00 20.57  ? 21  ASP E C    1 
ATOM   11399 O O    . ASP E 3 23  ? 15.081  142.993 44.800  1.00 19.98  ? 21  ASP E O    1 
ATOM   11400 C CB   . ASP E 3 23  ? 15.386  143.058 47.836  1.00 20.19  ? 21  ASP E CB   1 
ATOM   11401 C CG   . ASP E 3 23  ? 16.019  142.790 49.168  1.00 29.68  ? 21  ASP E CG   1 
ATOM   11402 O OD1  . ASP E 3 23  ? 16.481  141.656 49.377  1.00 36.02  ? 21  ASP E OD1  1 
ATOM   11403 O OD2  . ASP E 3 23  ? 16.046  143.708 50.011  1.00 23.59  ? 21  ASP E OD2  1 
ATOM   11404 N N    . THR E 3 24  ? 13.848  141.316 45.538  1.00 21.56  ? 22  THR E N    1 
ATOM   11405 C CA   . THR E 3 24  ? 13.010  141.291 44.368  1.00 20.83  ? 22  THR E CA   1 
ATOM   11406 C C    . THR E 3 24  ? 11.959  142.343 44.459  1.00 19.48  ? 22  THR E C    1 
ATOM   11407 O O    . THR E 3 24  ? 11.812  142.949 45.486  1.00 19.05  ? 22  THR E O    1 
ATOM   11408 C CB   . THR E 3 24  ? 12.434  139.900 44.173  1.00 19.21  ? 22  THR E CB   1 
ATOM   11409 O OG1  . THR E 3 24  ? 11.228  139.765 44.925  1.00 23.89  ? 22  THR E OG1  1 
ATOM   11410 C CG2  . THR E 3 24  ? 13.417  138.866 44.629  1.00 17.81  ? 22  THR E CG2  1 
ATOM   11411 N N    . ILE E 3 25  ? 11.247  142.604 43.370  1.00 18.35  ? 23  ILE E N    1 
ATOM   11412 C CA   . ILE E 3 25  ? 10.245  143.673 43.346  1.00 19.78  ? 23  ILE E CA   1 
ATOM   11413 C C    . ILE E 3 25  ? 9.032   143.263 44.121  1.00 20.72  ? 23  ILE E C    1 
ATOM   11414 O O    . ILE E 3 25  ? 8.282   144.087 44.557  1.00 21.17  ? 23  ILE E O    1 
ATOM   11415 C CB   . ILE E 3 25  ? 9.897   144.107 41.923  1.00 17.98  ? 23  ILE E CB   1 
ATOM   11416 C CG1  . ILE E 3 25  ? 11.156  144.488 41.169  1.00 18.90  ? 23  ILE E CG1  1 
ATOM   11417 C CG2  . ILE E 3 25  ? 8.996   145.328 41.871  1.00 17.88  ? 23  ILE E CG2  1 
ATOM   11418 C CD1  . ILE E 3 25  ? 11.816  145.743 41.669  1.00 18.54  ? 23  ILE E CD1  1 
ATOM   11419 N N    . GLU E 3 26  ? 8.873   141.983 44.373  1.00 21.27  ? 24  GLU E N    1 
ATOM   11420 C CA   . GLU E 3 26  ? 7.775   141.514 45.174  1.00 20.00  ? 24  GLU E CA   1 
ATOM   11421 C C    . GLU E 3 26  ? 8.100   141.707 46.606  1.00 18.79  ? 24  GLU E C    1 
ATOM   11422 O O    . GLU E 3 26  ? 7.217   141.761 47.432  1.00 15.56  ? 24  GLU E O    1 
ATOM   11423 C CB   . GLU E 3 26  ? 7.593   140.050 44.935  1.00 25.82  ? 24  GLU E CB   1 
ATOM   11424 C CG   . GLU E 3 26  ? 6.223   139.628 44.454  1.00 35.43  ? 24  GLU E CG   1 
ATOM   11425 C CD   . GLU E 3 26  ? 6.238   138.222 43.893  1.00 38.03  ? 24  GLU E CD   1 
ATOM   11426 O OE1  . GLU E 3 26  ? 7.313   137.768 43.461  1.00 31.21  ? 24  GLU E OE1  1 
ATOM   11427 O OE2  . GLU E 3 26  ? 5.181   137.566 43.883  1.00 37.28  ? 24  GLU E OE2  1 
ATOM   11428 N N    . ASN E 3 27  ? 9.382   141.803 46.916  1.00 19.55  ? 25  ASN E N    1 
ATOM   11429 C CA   . ASN E 3 27  ? 9.814   142.032 48.279  1.00 21.76  ? 25  ASN E CA   1 
ATOM   11430 C C    . ASN E 3 27  ? 9.626   143.482 48.555  1.00 23.83  ? 25  ASN E C    1 
ATOM   11431 O O    . ASN E 3 27  ? 9.212   143.842 49.607  1.00 28.75  ? 25  ASN E O    1 
ATOM   11432 C CB   . ASN E 3 27  ? 11.259  141.634 48.502  1.00 17.34  ? 25  ASN E CB   1 
ATOM   11433 C CG   . ASN E 3 27  ? 11.595  141.429 49.954  1.00 22.70  ? 25  ASN E CG   1 
ATOM   11434 O OD1  . ASN E 3 27  ? 12.722  141.668 50.369  1.00 26.07  ? 25  ASN E OD1  1 
ATOM   11435 N ND2  . ASN E 3 27  ? 10.624  140.981 50.733  1.00 21.53  ? 25  ASN E ND2  1 
ATOM   11436 N N    . VAL E 3 28  ? 9.927   144.341 47.614  1.00 20.81  ? 26  VAL E N    1 
ATOM   11437 C CA   . VAL E 3 28  ? 9.691   145.742 47.799  1.00 16.87  ? 26  VAL E CA   1 
ATOM   11438 C C    . VAL E 3 28  ? 8.227   145.932 47.935  1.00 15.50  ? 26  VAL E C    1 
ATOM   11439 O O    . VAL E 3 28  ? 7.794   146.546 48.854  1.00 17.38  ? 26  VAL E O    1 
ATOM   11440 C CB   . VAL E 3 28  ? 10.257  146.526 46.624  1.00 19.43  ? 26  VAL E CB   1 
ATOM   11441 C CG1  . VAL E 3 28  ? 10.083  148.015 46.822  1.00 18.33  ? 26  VAL E CG1  1 
ATOM   11442 C CG2  . VAL E 3 28  ? 11.726  146.200 46.470  1.00 19.71  ? 26  VAL E CG2  1 
ATOM   11443 N N    . LYS E 3 29  ? 7.442   145.345 47.060  1.00 18.68  ? 27  LYS E N    1 
ATOM   11444 C CA   . LYS E 3 29  ? 5.982   145.451 47.095  1.00 17.74  ? 27  LYS E CA   1 
ATOM   11445 C C    . LYS E 3 29  ? 5.346   144.937 48.357  1.00 19.15  ? 27  LYS E C    1 
ATOM   11446 O O    . LYS E 3 29  ? 4.222   145.271 48.664  1.00 19.40  ? 27  LYS E O    1 
ATOM   11447 C CB   . LYS E 3 29  ? 5.371   144.742 45.899  1.00 14.08  ? 27  LYS E CB   1 
ATOM   11448 C CG   . LYS E 3 29  ? 5.320   145.525 44.620  1.00 13.50  ? 27  LYS E CG   1 
ATOM   11449 C CD   . LYS E 3 29  ? 4.653   144.679 43.567  1.00 13.12  ? 27  LYS E CD   1 
ATOM   11450 C CE   . LYS E 3 29  ? 5.383   144.822 42.257  1.00 23.53  ? 27  LYS E CE   1 
ATOM   11451 N NZ   . LYS E 3 29  ? 4.525   144.519 41.086  1.00 29.30  ? 27  LYS E NZ   1 
ATOM   11452 N N    . ALA E 3 30  ? 6.061   144.125 49.107  1.00 17.49  ? 28  ALA E N    1 
ATOM   11453 C CA   . ALA E 3 30  ? 5.567   143.615 50.361  1.00 15.36  ? 28  ALA E CA   1 
ATOM   11454 C C    . ALA E 3 30  ? 5.772   144.628 51.392  1.00 16.95  ? 28  ALA E C    1 
ATOM   11455 O O    . ALA E 3 30  ? 4.932   144.810 52.202  1.00 22.18  ? 28  ALA E O    1 
ATOM   11456 C CB   . ALA E 3 30  ? 6.369   142.425 50.729  1.00 14.92  ? 28  ALA E CB   1 
ATOM   11457 N N    . LYS E 3 31  ? 6.901   145.310 51.369  1.00 14.52  ? 29  LYS E N    1 
ATOM   11458 C CA   . LYS E 3 31  ? 7.211   146.354 52.313  1.00 15.01  ? 29  LYS E CA   1 
ATOM   11459 C C    . LYS E 3 31  ? 6.409   147.583 52.113  1.00 15.66  ? 29  LYS E C    1 
ATOM   11460 O O    . LYS E 3 31  ? 6.207   148.317 53.040  1.00 15.09  ? 29  LYS E O    1 
ATOM   11461 C CB   . LYS E 3 31  ? 8.663   146.660 52.200  1.00 12.10  ? 29  LYS E CB   1 
ATOM   11462 C CG   . LYS E 3 31  ? 9.550   145.449 52.371  1.00 13.05  ? 29  LYS E CG   1 
ATOM   11463 C CD   . LYS E 3 31  ? 10.841  145.806 53.067  1.00 12.22  ? 29  LYS E CD   1 
ATOM   11464 C CE   . LYS E 3 31  ? 12.014  145.286 52.274  1.00 17.09  ? 29  LYS E CE   1 
ATOM   11465 N NZ   . LYS E 3 31  ? 11.606  145.083 50.866  1.00 19.00  ? 29  LYS E NZ   1 
ATOM   11466 N N    . ILE E 3 32  ? 5.905   147.809 50.923  1.00 17.28  ? 30  ILE E N    1 
ATOM   11467 C CA   . ILE E 3 32  ? 5.014   148.920 50.655  1.00 19.33  ? 30  ILE E CA   1 
ATOM   11468 C C    . ILE E 3 32  ? 3.589   148.515 51.076  1.00 22.52  ? 30  ILE E C    1 
ATOM   11469 O O    . ILE E 3 32  ? 2.633   149.234 50.844  1.00 22.79  ? 30  ILE E O    1 
ATOM   11470 C CB   . ILE E 3 32  ? 5.101   149.306 49.159  1.00 13.65  ? 30  ILE E CB   1 
ATOM   11471 C CG1  . ILE E 3 32  ? 6.534   149.410 48.694  1.00 13.98  ? 30  ILE E CG1  1 
ATOM   11472 C CG2  . ILE E 3 32  ? 4.470   150.648 48.849  1.00 14.79  ? 30  ILE E CG2  1 
ATOM   11473 C CD1  . ILE E 3 32  ? 6.626   149.747 47.232  1.00 17.46  ? 30  ILE E CD1  1 
ATOM   11474 N N    . GLN E 3 33  ? 3.426   147.339 51.683  1.00 20.06  ? 31  GLN E N    1 
ATOM   11475 C CA   . GLN E 3 33  ? 2.122   146.897 52.177  1.00 20.04  ? 31  GLN E CA   1 
ATOM   11476 C C    . GLN E 3 33  ? 2.218   146.870 53.652  1.00 18.47  ? 31  GLN E C    1 
ATOM   11477 O O    . GLN E 3 33  ? 1.272   147.099 54.376  1.00 18.59  ? 31  GLN E O    1 
ATOM   11478 C CB   . GLN E 3 33  ? 1.769   145.505 51.719  1.00 17.95  ? 31  GLN E CB   1 
ATOM   11479 C CG   . GLN E 3 33  ? 0.409   145.031 52.213  1.00 19.35  ? 31  GLN E CG   1 
ATOM   11480 C CD   . GLN E 3 33  ? 0.132   143.572 51.965  1.00 20.37  ? 31  GLN E CD   1 
ATOM   11481 O OE1  . GLN E 3 33  ? 1.031   142.738 52.003  1.00 23.82  ? 31  GLN E OE1  1 
ATOM   11482 N NE2  . GLN E 3 33  ? -1.128  143.254 51.724  1.00 15.10  ? 31  GLN E NE2  1 
ATOM   11483 N N    . ASP E 3 34  ? 3.398   146.574 54.121  1.00 17.32  ? 32  ASP E N    1 
ATOM   11484 C CA   . ASP E 3 34  ? 3.616   146.498 55.535  1.00 20.84  ? 32  ASP E CA   1 
ATOM   11485 C C    . ASP E 3 34  ? 3.613   147.876 56.082  1.00 25.43  ? 32  ASP E C    1 
ATOM   11486 O O    . ASP E 3 34  ? 3.335   148.074 57.250  1.00 30.33  ? 32  ASP E O    1 
ATOM   11487 C CB   . ASP E 3 34  ? 4.956   145.845 55.836  1.00 20.27  ? 32  ASP E CB   1 
ATOM   11488 C CG   . ASP E 3 34  ? 5.046   144.423 55.340  1.00 27.50  ? 32  ASP E CG   1 
ATOM   11489 O OD1  . ASP E 3 34  ? 3.992   143.787 55.144  1.00 33.43  ? 32  ASP E OD1  1 
ATOM   11490 O OD2  . ASP E 3 34  ? 6.179   143.938 55.152  1.00 19.40  ? 32  ASP E OD2  1 
ATOM   11491 N N    . LYS E 3 35  ? 3.910   148.852 55.250  1.00 20.87  ? 33  LYS E N    1 
ATOM   11492 C CA   . LYS E 3 35  ? 4.007   150.190 55.756  1.00 16.84  ? 33  LYS E CA   1 
ATOM   11493 C C    . LYS E 3 35  ? 2.917   151.050 55.269  1.00 18.63  ? 33  LYS E C    1 
ATOM   11494 O O    . LYS E 3 35  ? 2.724   152.123 55.800  1.00 27.26  ? 33  LYS E O    1 
ATOM   11495 C CB   . LYS E 3 35  ? 5.388   150.787 55.501  1.00 15.68  ? 33  LYS E CB   1 
ATOM   11496 C CG   . LYS E 3 35  ? 5.649   151.420 54.157  1.00 25.66  ? 33  LYS E CG   1 
ATOM   11497 C CD   . LYS E 3 35  ? 7.079   151.920 54.112  1.00 23.82  ? 33  LYS E CD   1 
ATOM   11498 C CE   . LYS E 3 35  ? 7.943   151.202 55.129  1.00 16.01  ? 33  LYS E CE   1 
ATOM   11499 N NZ   . LYS E 3 35  ? 9.372   151.123 54.720  1.00 12.53  ? 33  LYS E NZ   1 
ATOM   11500 N N    . GLU E 3 36  ? 2.144   150.580 54.301  1.00 18.18  ? 34  GLU E N    1 
ATOM   11501 C CA   . GLU E 3 36  ? 1.101   151.406 53.706  1.00 20.91  ? 34  GLU E CA   1 
ATOM   11502 C C    . GLU E 3 36  ? -0.292  150.813 53.608  1.00 15.65  ? 34  GLU E C    1 
ATOM   11503 O O    . GLU E 3 36  ? -1.269  151.529 53.587  1.00 13.28  ? 34  GLU E O    1 
ATOM   11504 C CB   . GLU E 3 36  ? 1.559   151.888 52.353  1.00 20.05  ? 34  GLU E CB   1 
ATOM   11505 C CG   . GLU E 3 36  ? 2.759   152.822 52.325  1.00 22.17  ? 34  GLU E CG   1 
ATOM   11506 C CD   . GLU E 3 36  ? 2.473   154.203 52.873  1.00 22.62  ? 34  GLU E CD   1 
ATOM   11507 O OE1  . GLU E 3 36  ? 1.386   154.740 52.611  1.00 22.14  ? 34  GLU E OE1  1 
ATOM   11508 O OE2  . GLU E 3 36  ? 3.348   154.762 53.560  1.00 23.81  ? 34  GLU E OE2  1 
ATOM   11509 N N    . GLY E 3 37  ? -0.392  149.513 53.514  1.00 11.25  ? 35  GLY E N    1 
ATOM   11510 C CA   . GLY E 3 37  ? -1.671  148.858 53.485  1.00 9.80   ? 35  GLY E CA   1 
ATOM   11511 C C    . GLY E 3 37  ? -2.142  148.509 52.141  1.00 11.23  ? 35  GLY E C    1 
ATOM   11512 O O    . GLY E 3 37  ? -3.269  148.117 51.982  1.00 13.06  ? 35  GLY E O    1 
ATOM   11513 N N    . ILE E 3 38  ? -1.276  148.597 51.161  1.00 14.51  ? 36  ILE E N    1 
ATOM   11514 C CA   . ILE E 3 38  ? -1.649  148.379 49.785  1.00 12.05  ? 36  ILE E CA   1 
ATOM   11515 C C    . ILE E 3 38  ? -1.303  147.023 49.325  1.00 12.07  ? 36  ILE E C    1 
ATOM   11516 O O    . ILE E 3 38  ? -0.193  146.609 49.430  1.00 13.14  ? 36  ILE E O    1 
ATOM   11517 C CB   . ILE E 3 38  ? -0.983  149.407 48.875  1.00 10.43  ? 36  ILE E CB   1 
ATOM   11518 C CG1  . ILE E 3 38  ? -1.349  150.816 49.307  1.00 11.97  ? 36  ILE E CG1  1 
ATOM   11519 C CG2  . ILE E 3 38  ? -1.428  149.194 47.456  1.00 14.06  ? 36  ILE E CG2  1 
ATOM   11520 C CD1  . ILE E 3 38  ? -0.221  151.796 49.135  1.00 16.95  ? 36  ILE E CD1  1 
ATOM   11521 N N    . PRO E 3 39  ? -2.333  146.277 48.827  1.00 11.87  ? 37  PRO E N    1 
ATOM   11522 C CA   . PRO E 3 39  ? -1.962  144.932 48.485  1.00 12.86  ? 37  PRO E CA   1 
ATOM   11523 C C    . PRO E 3 39  ? -0.992  144.913 47.376  1.00 17.83  ? 37  PRO E C    1 
ATOM   11524 O O    . PRO E 3 39  ? -1.054  145.739 46.501  1.00 19.83  ? 37  PRO E O    1 
ATOM   11525 C CB   . PRO E 3 39  ? -3.262  144.362 48.007  1.00 13.78  ? 37  PRO E CB   1 
ATOM   11526 C CG   . PRO E 3 39  ? -4.280  145.026 48.831  1.00 13.86  ? 37  PRO E CG   1 
ATOM   11527 C CD   . PRO E 3 39  ? -3.811  146.415 48.663  1.00 12.88  ? 37  PRO E CD   1 
ATOM   11528 N N    . PRO E 3 40  ? -0.070  143.945 47.406  1.00 17.07  ? 38  PRO E N    1 
ATOM   11529 C CA   . PRO E 3 40  ? 0.946   143.966 46.396  1.00 15.14  ? 38  PRO E CA   1 
ATOM   11530 C C    . PRO E 3 40  ? 0.452   143.858 44.966  1.00 20.32  ? 38  PRO E C    1 
ATOM   11531 O O    . PRO E 3 40  ? 1.241   143.965 44.062  1.00 22.62  ? 38  PRO E O    1 
ATOM   11532 C CB   . PRO E 3 40  ? 1.790   142.798 46.813  1.00 15.71  ? 38  PRO E CB   1 
ATOM   11533 C CG   . PRO E 3 40  ? 1.711   142.792 48.282  1.00 14.97  ? 38  PRO E CG   1 
ATOM   11534 C CD   . PRO E 3 40  ? 0.247   142.938 48.432  1.00 16.40  ? 38  PRO E CD   1 
ATOM   11535 N N    . ASP E 3 41  ? -0.844  143.699 44.764  1.00 21.88  ? 39  ASP E N    1 
ATOM   11536 C CA   . ASP E 3 41  ? -1.415  143.542 43.432  1.00 20.64  ? 39  ASP E CA   1 
ATOM   11537 C C    . ASP E 3 41  ? -2.112  144.770 42.961  1.00 23.11  ? 39  ASP E C    1 
ATOM   11538 O O    . ASP E 3 41  ? -2.879  144.710 42.026  1.00 25.25  ? 39  ASP E O    1 
ATOM   11539 C CB   . ASP E 3 41  ? -2.389  142.393 43.398  1.00 21.60  ? 39  ASP E CB   1 
ATOM   11540 C CG   . ASP E 3 41  ? -1.757  141.065 43.758  1.00 29.80  ? 39  ASP E CG   1 
ATOM   11541 O OD1  . ASP E 3 41  ? -0.517  140.948 43.754  1.00 33.43  ? 39  ASP E OD1  1 
ATOM   11542 O OD2  . ASP E 3 41  ? -2.515  140.118 44.040  1.00 32.82  ? 39  ASP E OD2  1 
ATOM   11543 N N    . GLN E 3 42  ? -1.885  145.884 43.623  1.00 20.88  ? 40  GLN E N    1 
ATOM   11544 C CA   . GLN E 3 42  ? -2.415  147.134 43.169  1.00 22.06  ? 40  GLN E CA   1 
ATOM   11545 C C    . GLN E 3 42  ? -1.197  147.883 42.837  1.00 17.78  ? 40  GLN E C    1 
ATOM   11546 O O    . GLN E 3 42  ? -1.199  148.762 42.026  1.00 19.00  ? 40  GLN E O    1 
ATOM   11547 C CB   . GLN E 3 42  ? -3.111  147.831 44.319  1.00 19.37  ? 40  GLN E CB   1 
ATOM   11548 C CG   . GLN E 3 42  ? -3.891  149.065 43.940  1.00 18.65  ? 40  GLN E CG   1 
ATOM   11549 C CD   . GLN E 3 42  ? -4.636  149.651 45.106  1.00 16.93  ? 40  GLN E CD   1 
ATOM   11550 O OE1  . GLN E 3 42  ? -5.324  150.654 44.975  1.00 24.46  ? 40  GLN E OE1  1 
ATOM   11551 N NE2  . GLN E 3 42  ? -4.507  149.024 46.253  1.00 19.36  ? 40  GLN E NE2  1 
ATOM   11552 N N    . GLN E 3 43  ? -0.114  147.505 43.446  1.00 14.72  ? 41  GLN E N    1 
ATOM   11553 C CA   . GLN E 3 43  ? 1.112   148.201 43.246  1.00 17.55  ? 41  GLN E CA   1 
ATOM   11554 C C    . GLN E 3 43  ? 1.685   147.983 41.894  1.00 25.30  ? 41  GLN E C    1 
ATOM   11555 O O    . GLN E 3 43  ? 1.584   146.903 41.351  1.00 37.70  ? 41  GLN E O    1 
ATOM   11556 C CB   . GLN E 3 43  ? 2.095   147.845 44.343  1.00 16.17  ? 41  GLN E CB   1 
ATOM   11557 C CG   . GLN E 3 43  ? 1.495   147.908 45.726  1.00 17.03  ? 41  GLN E CG   1 
ATOM   11558 C CD   . GLN E 3 43  ? 2.536   147.684 46.775  1.00 14.92  ? 41  GLN E CD   1 
ATOM   11559 O OE1  . GLN E 3 43  ? 3.682   147.445 46.462  1.00 13.20  ? 41  GLN E OE1  1 
ATOM   11560 N NE2  . GLN E 3 43  ? 2.148   147.773 48.023  1.00 17.80  ? 41  GLN E NE2  1 
ATOM   11561 N N    . ARG E 3 44  ? 2.285   149.010 41.330  1.00 21.46  ? 42  ARG E N    1 
ATOM   11562 C CA   . ARG E 3 44  ? 2.825   148.956 40.016  1.00 14.76  ? 42  ARG E CA   1 
ATOM   11563 C C    . ARG E 3 44  ? 3.989   149.813 40.179  1.00 15.08  ? 42  ARG E C    1 
ATOM   11564 O O    . ARG E 3 44  ? 3.846   151.007 40.281  1.00 12.72  ? 42  ARG E O    1 
ATOM   11565 C CB   . ARG E 3 44  ? 1.887   149.665 39.079  1.00 15.60  ? 42  ARG E CB   1 
ATOM   11566 C CG   . ARG E 3 44  ? 0.685   148.861 38.637  1.00 20.89  ? 42  ARG E CG   1 
ATOM   11567 C CD   . ARG E 3 44  ? -0.106  149.614 37.587  1.00 20.84  ? 42  ARG E CD   1 
ATOM   11568 N NE   . ARG E 3 44  ? 0.179   149.145 36.238  1.00 25.82  ? 42  ARG E NE   1 
ATOM   11569 C CZ   . ARG E 3 44  ? 0.751   149.875 35.289  1.00 29.07  ? 42  ARG E CZ   1 
ATOM   11570 N NH1  . ARG E 3 44  ? 1.104   151.126 35.526  1.00 27.71  ? 42  ARG E NH1  1 
ATOM   11571 N NH2  . ARG E 3 44  ? 0.959   149.355 34.088  1.00 26.19  ? 42  ARG E NH2  1 
ATOM   11572 N N    . LEU E 3 45  ? 5.159   149.223 40.190  1.00 16.07  ? 43  LEU E N    1 
ATOM   11573 C CA   . LEU E 3 45  ? 6.367   149.969 40.452  1.00 12.00  ? 43  LEU E CA   1 
ATOM   11574 C C    . LEU E 3 45  ? 7.071   150.362 39.172  1.00 10.92  ? 43  LEU E C    1 
ATOM   11575 O O    . LEU E 3 45  ? 7.209   149.560 38.304  1.00 12.53  ? 43  LEU E O    1 
ATOM   11576 C CB   . LEU E 3 45  ? 7.224   149.238 41.462  1.00 12.51  ? 43  LEU E CB   1 
ATOM   11577 C CG   . LEU E 3 45  ? 7.225   149.662 42.913  1.00 12.34  ? 43  LEU E CG   1 
ATOM   11578 C CD1  . LEU E 3 45  ? 6.072   148.988 43.610  1.00 16.13  ? 43  LEU E CD1  1 
ATOM   11579 C CD2  . LEU E 3 45  ? 8.529   149.189 43.512  1.00 16.40  ? 43  LEU E CD2  1 
ATOM   11580 N N    . ILE E 3 46  ? 7.450   151.619 39.038  1.00 10.67  ? 44  ILE E N    1 
ATOM   11581 C CA   . ILE E 3 46  ? 8.005   152.149 37.805  1.00 15.95  ? 44  ILE E CA   1 
ATOM   11582 C C    . ILE E 3 46  ? 9.265   152.930 38.048  1.00 14.98  ? 44  ILE E C    1 
ATOM   11583 O O    . ILE E 3 46  ? 9.264   153.928 38.717  1.00 16.01  ? 44  ILE E O    1 
ATOM   11584 C CB   . ILE E 3 46  ? 6.976   153.084 37.098  1.00 16.70  ? 44  ILE E CB   1 
ATOM   11585 C CG1  . ILE E 3 46  ? 5.748   152.319 36.638  1.00 17.89  ? 44  ILE E CG1  1 
ATOM   11586 C CG2  . ILE E 3 46  ? 7.588   153.789 35.906  1.00 18.56  ? 44  ILE E CG2  1 
ATOM   11587 C CD1  . ILE E 3 46  ? 4.464   152.995 37.026  1.00 14.95  ? 44  ILE E CD1  1 
ATOM   11588 N N    . PHE E 3 47  ? 10.365  152.460 37.518  1.00 17.29  ? 45  PHE E N    1 
ATOM   11589 C CA   . PHE E 3 47  ? 11.616  153.142 37.635  1.00 19.09  ? 45  PHE E CA   1 
ATOM   11590 C C    . PHE E 3 47  ? 11.957  152.935 36.218  1.00 24.69  ? 45  PHE E C    1 
ATOM   11591 O O    . PHE E 3 47  ? 11.589  151.906 35.689  1.00 30.10  ? 45  PHE E O    1 
ATOM   11592 C CB   . PHE E 3 47  ? 12.549  152.327 38.500  1.00 19.56  ? 45  PHE E CB   1 
ATOM   11593 C CG   . PHE E 3 47  ? 13.987  152.738 38.437  1.00 28.19  ? 45  PHE E CG   1 
ATOM   11594 C CD1  . PHE E 3 47  ? 14.429  153.853 39.107  1.00 23.92  ? 45  PHE E CD1  1 
ATOM   11595 C CD2  . PHE E 3 47  ? 14.904  151.978 37.742  1.00 30.36  ? 45  PHE E CD2  1 
ATOM   11596 C CE1  . PHE E 3 47  ? 15.752  154.220 39.073  1.00 22.60  ? 45  PHE E CE1  1 
ATOM   11597 C CE2  . PHE E 3 47  ? 16.228  152.342 37.697  1.00 27.23  ? 45  PHE E CE2  1 
ATOM   11598 C CZ   . PHE E 3 47  ? 16.653  153.462 38.367  1.00 27.52  ? 45  PHE E CZ   1 
ATOM   11599 N N    . ALA E 3 48  ? 12.594  153.907 35.582  1.00 19.28  ? 46  ALA E N    1 
ATOM   11600 C CA   . ALA E 3 48  ? 13.001  153.807 34.196  1.00 22.51  ? 46  ALA E CA   1 
ATOM   11601 C C    . ALA E 3 48  ? 11.905  153.678 33.218  1.00 19.05  ? 46  ALA E C    1 
ATOM   11602 O O    . ALA E 3 48  ? 12.076  153.060 32.195  1.00 24.64  ? 46  ALA E O    1 
ATOM   11603 C CB   . ALA E 3 48  ? 13.958  152.660 34.008  1.00 34.87  ? 46  ALA E CB   1 
ATOM   11604 N N    . GLY E 3 49  ? 10.764  154.244 33.517  1.00 18.84  ? 47  GLY E N    1 
ATOM   11605 C CA   . GLY E 3 49  ? 9.623   154.163 32.639  1.00 20.90  ? 47  GLY E CA   1 
ATOM   11606 C C    . GLY E 3 49  ? 9.229   152.749 32.405  1.00 23.20  ? 47  GLY E C    1 
ATOM   11607 O O    . GLY E 3 49  ? 8.741   152.405 31.359  1.00 31.73  ? 47  GLY E O    1 
ATOM   11608 N N    . LYS E 3 50  ? 9.403   151.905 33.392  1.00 25.11  ? 48  LYS E N    1 
ATOM   11609 C CA   . LYS E 3 50  ? 9.143   150.514 33.182  1.00 28.65  ? 48  LYS E CA   1 
ATOM   11610 C C    . LYS E 3 50  ? 8.350   149.942 34.277  1.00 23.21  ? 48  LYS E C    1 
ATOM   11611 O O    . LYS E 3 50  ? 8.641   150.199 35.412  1.00 22.67  ? 48  LYS E O    1 
ATOM   11612 C CB   . LYS E 3 50  ? 10.483  149.788 33.166  1.00 27.69  ? 48  LYS E CB   1 
ATOM   11613 C CG   . LYS E 3 50  ? 10.805  149.041 31.891  1.00 37.37  ? 48  LYS E CG   1 
ATOM   11614 C CD   . LYS E 3 50  ? 11.813  147.943 32.165  1.00 54.27  ? 48  LYS E CD   1 
ATOM   11615 C CE   . LYS E 3 50  ? 13.182  148.519 32.494  1.00 59.67  ? 48  LYS E CE   1 
ATOM   11616 N NZ   . LYS E 3 50  ? 14.287  147.535 32.299  1.00 44.88  ? 48  LYS E NZ   1 
ATOM   11617 N N    . GLN E 3 51  ? 7.342   149.154 33.963  1.00 20.55  ? 49  GLN E N    1 
ATOM   11618 C CA   . GLN E 3 51  ? 6.641   148.481 35.000  1.00 16.68  ? 49  GLN E CA   1 
ATOM   11619 C C    . GLN E 3 51  ? 7.565   147.367 35.294  1.00 17.44  ? 49  GLN E C    1 
ATOM   11620 O O    . GLN E 3 51  ? 7.824   146.515 34.465  1.00 18.37  ? 49  GLN E O    1 
ATOM   11621 C CB   . GLN E 3 51  ? 5.252   148.025 34.610  1.00 16.11  ? 49  GLN E CB   1 
ATOM   11622 C CG   . GLN E 3 51  ? 4.223   148.237 35.693  1.00 19.55  ? 49  GLN E CG   1 
ATOM   11623 C CD   . GLN E 3 51  ? 3.633   146.932 36.157  1.00 37.58  ? 49  GLN E CD   1 
ATOM   11624 O OE1  . GLN E 3 51  ? 2.975   146.239 35.390  1.00 38.06  ? 49  GLN E OE1  1 
ATOM   11625 N NE2  . GLN E 3 51  ? 3.873   146.582 37.416  1.00 40.18  ? 49  GLN E NE2  1 
ATOM   11626 N N    . LEU E 3 52  ? 8.082   147.387 36.498  1.00 20.50  ? 50  LEU E N    1 
ATOM   11627 C CA   . LEU E 3 52  ? 9.044   146.437 36.906  1.00 18.88  ? 50  LEU E CA   1 
ATOM   11628 C C    . LEU E 3 52  ? 8.426   145.118 37.145  1.00 16.55  ? 50  LEU E C    1 
ATOM   11629 O O    . LEU E 3 52  ? 7.271   145.042 37.509  1.00 20.31  ? 50  LEU E O    1 
ATOM   11630 C CB   . LEU E 3 52  ? 9.723   147.004 38.148  1.00 16.86  ? 50  LEU E CB   1 
ATOM   11631 C CG   . LEU E 3 52  ? 10.252  148.431 38.156  1.00 14.56  ? 50  LEU E CG   1 
ATOM   11632 C CD1  . LEU E 3 52  ? 10.765  148.819 39.527  1.00 13.83  ? 50  LEU E CD1  1 
ATOM   11633 C CD2  . LEU E 3 52  ? 11.291  148.692 37.086  1.00 21.78  ? 50  LEU E CD2  1 
ATOM   11634 N N    . GLU E 3 53  ? 9.200   144.057 36.980  1.00 15.14  ? 51  GLU E N    1 
ATOM   11635 C CA   . GLU E 3 53  ? 8.661   142.737 37.079  1.00 14.31  ? 51  GLU E CA   1 
ATOM   11636 C C    . GLU E 3 53  ? 8.868   142.222 38.427  1.00 13.50  ? 51  GLU E C    1 
ATOM   11637 O O    . GLU E 3 53  ? 9.751   142.655 39.077  1.00 17.48  ? 51  GLU E O    1 
ATOM   11638 C CB   . GLU E 3 53  ? 9.221   141.845 36.000  1.00 14.25  ? 51  GLU E CB   1 
ATOM   11639 C CG   . GLU E 3 53  ? 8.673   142.142 34.624  1.00 16.23  ? 51  GLU E CG   1 
ATOM   11640 C CD   . GLU E 3 53  ? 9.414   141.414 33.533  1.00 27.87  ? 51  GLU E CD   1 
ATOM   11641 O OE1  . GLU E 3 53  ? 9.790   140.250 33.753  1.00 30.96  ? 51  GLU E OE1  1 
ATOM   11642 O OE2  . GLU E 3 53  ? 9.610   142.004 32.456  1.00 27.99  ? 51  GLU E OE2  1 
ATOM   11643 N N    . ASP E 3 54  ? 8.092   141.250 38.849  1.00 13.58  ? 52  ASP E N    1 
ATOM   11644 C CA   . ASP E 3 54  ? 8.099   140.811 40.221  1.00 18.70  ? 52  ASP E CA   1 
ATOM   11645 C C    . ASP E 3 54  ? 9.123   139.807 40.578  1.00 15.44  ? 52  ASP E C    1 
ATOM   11646 O O    . ASP E 3 54  ? 9.288   139.464 41.727  1.00 17.57  ? 52  ASP E O    1 
ATOM   11647 C CB   . ASP E 3 54  ? 6.703   140.268 40.548  1.00 22.52  ? 52  ASP E CB   1 
ATOM   11648 C CG   . ASP E 3 54  ? 5.694   141.342 40.758  1.00 25.44  ? 52  ASP E CG   1 
ATOM   11649 O OD1  . ASP E 3 54  ? 5.603   142.244 39.915  1.00 33.50  ? 52  ASP E OD1  1 
ATOM   11650 O OD2  . ASP E 3 54  ? 4.974   141.279 41.765  1.00 24.52  ? 52  ASP E OD2  1 
ATOM   11651 N N    . GLY E 3 55  ? 9.844   139.348 39.597  1.00 10.95  ? 53  GLY E N    1 
ATOM   11652 C CA   . GLY E 3 55  ? 10.907  138.417 39.872  1.00 16.22  ? 53  GLY E CA   1 
ATOM   11653 C C    . GLY E 3 55  ? 12.259  139.027 39.754  1.00 12.75  ? 53  GLY E C    1 
ATOM   11654 O O    . GLY E 3 55  ? 13.240  138.456 40.191  1.00 13.81  ? 53  GLY E O    1 
ATOM   11655 N N    . ARG E 3 56  ? 12.301  140.202 39.167  1.00 11.74  ? 54  ARG E N    1 
ATOM   11656 C CA   . ARG E 3 56  ? 13.537  140.882 38.979  1.00 15.82  ? 54  ARG E CA   1 
ATOM   11657 C C    . ARG E 3 56  ? 13.983  141.607 40.199  1.00 19.38  ? 54  ARG E C    1 
ATOM   11658 O O    . ARG E 3 56  ? 13.190  142.133 40.922  1.00 18.45  ? 54  ARG E O    1 
ATOM   11659 C CB   . ARG E 3 56  ? 13.437  141.746 37.772  1.00 14.47  ? 54  ARG E CB   1 
ATOM   11660 C CG   . ARG E 3 56  ? 12.737  141.064 36.626  1.00 17.73  ? 54  ARG E CG   1 
ATOM   11661 C CD   . ARG E 3 56  ? 13.715  140.254 35.811  1.00 20.93  ? 54  ARG E CD   1 
ATOM   11662 N NE   . ARG E 3 56  ? 13.220  139.999 34.472  1.00 15.92  ? 54  ARG E NE   1 
ATOM   11663 C CZ   . ARG E 3 56  ? 13.485  140.765 33.425  1.00 21.45  ? 54  ARG E CZ   1 
ATOM   11664 N NH1  . ARG E 3 56  ? 14.238  141.847 33.561  1.00 24.31  ? 54  ARG E NH1  1 
ATOM   11665 N NH2  . ARG E 3 56  ? 12.993  140.448 32.242  1.00 26.51  ? 54  ARG E NH2  1 
ATOM   11666 N N    . THR E 3 57  ? 15.278  141.610 40.447  1.00 16.69  ? 55  THR E N    1 
ATOM   11667 C CA   . THR E 3 57  ? 15.810  142.181 41.622  1.00 12.95  ? 55  THR E CA   1 
ATOM   11668 C C    . THR E 3 57  ? 16.037  143.583 41.353  1.00 17.92  ? 55  THR E C    1 
ATOM   11669 O O    . THR E 3 57  ? 15.807  144.049 40.264  1.00 24.23  ? 55  THR E O    1 
ATOM   11670 C CB   . THR E 3 57  ? 17.132  141.557 41.936  1.00 15.14  ? 55  THR E CB   1 
ATOM   11671 O OG1  . THR E 3 57  ? 18.125  142.078 41.064  1.00 17.42  ? 55  THR E OG1  1 
ATOM   11672 C CG2  . THR E 3 57  ? 17.049  140.075 41.738  1.00 18.81  ? 55  THR E CG2  1 
ATOM   11673 N N    . LEU E 3 58  ? 16.482  144.311 42.355  1.00 15.96  ? 56  LEU E N    1 
ATOM   11674 C CA   . LEU E 3 58  ? 16.634  145.721 42.212  1.00 13.92  ? 56  LEU E CA   1 
ATOM   11675 C C    . LEU E 3 58  ? 17.789  145.963 41.339  1.00 16.55  ? 56  LEU E C    1 
ATOM   11676 O O    . LEU E 3 58  ? 17.862  146.958 40.681  1.00 21.44  ? 56  LEU E O    1 
ATOM   11677 C CB   . LEU E 3 58  ? 16.838  146.320 43.569  1.00 14.68  ? 56  LEU E CB   1 
ATOM   11678 C CG   . LEU E 3 58  ? 15.711  146.276 44.580  1.00 14.23  ? 56  LEU E CG   1 
ATOM   11679 C CD1  . LEU E 3 58  ? 16.082  147.131 45.762  1.00 12.90  ? 56  LEU E CD1  1 
ATOM   11680 C CD2  . LEU E 3 58  ? 14.444  146.806 43.959  1.00 15.67  ? 56  LEU E CD2  1 
ATOM   11681 N N    . SER E 3 59  ? 18.687  145.009 41.259  1.00 18.49  ? 57  SER E N    1 
ATOM   11682 C CA   . SER E 3 59  ? 19.863  145.116 40.410  1.00 22.62  ? 57  SER E CA   1 
ATOM   11683 C C    . SER E 3 59  ? 19.716  144.278 39.197  1.00 22.03  ? 57  SER E C    1 
ATOM   11684 O O    . SER E 3 59  ? 20.650  143.625 38.779  1.00 27.29  ? 57  SER E O    1 
ATOM   11685 C CB   . SER E 3 59  ? 21.046  144.591 41.141  1.00 24.61  ? 57  SER E CB   1 
ATOM   11686 O OG   . SER E 3 59  ? 20.832  143.242 41.497  1.00 27.67  ? 57  SER E OG   1 
ATOM   11687 N N    . ASP E 3 60  ? 18.530  144.253 38.634  1.00 17.26  ? 58  ASP E N    1 
ATOM   11688 C CA   . ASP E 3 60  ? 18.313  143.572 37.397  1.00 23.07  ? 58  ASP E CA   1 
ATOM   11689 C C    . ASP E 3 60  ? 17.767  144.757 36.700  1.00 26.48  ? 58  ASP E C    1 
ATOM   11690 O O    . ASP E 3 60  ? 17.426  144.690 35.531  1.00 29.19  ? 58  ASP E O    1 
ATOM   11691 C CB   . ASP E 3 60  ? 17.235  142.519 37.519  1.00 21.00  ? 58  ASP E CB   1 
ATOM   11692 C CG   . ASP E 3 60  ? 17.788  141.113 37.615  1.00 26.12  ? 58  ASP E CG   1 
ATOM   11693 O OD1  . ASP E 3 60  ? 19.008  140.961 37.790  1.00 36.59  ? 58  ASP E OD1  1 
ATOM   11694 O OD2  . ASP E 3 60  ? 17.004  140.149 37.518  1.00 21.42  ? 58  ASP E OD2  1 
ATOM   11695 N N    . TYR E 3 61  ? 17.734  145.881 37.410  1.00 17.53  ? 59  TYR E N    1 
ATOM   11696 C CA   . TYR E 3 61  ? 17.169  147.105 36.866  1.00 22.85  ? 59  TYR E CA   1 
ATOM   11697 C C    . TYR E 3 61  ? 17.970  148.377 37.140  1.00 21.35  ? 59  TYR E C    1 
ATOM   11698 O O    . TYR E 3 61  ? 17.558  149.426 36.698  1.00 18.81  ? 59  TYR E O    1 
ATOM   11699 C CB   . TYR E 3 61  ? 15.782  147.289 37.478  1.00 18.71  ? 59  TYR E CB   1 
ATOM   11700 C CG   . TYR E 3 61  ? 14.656  146.478 36.916  1.00 16.68  ? 59  TYR E CG   1 
ATOM   11701 C CD1  . TYR E 3 61  ? 14.449  146.402 35.564  1.00 23.62  ? 59  TYR E CD1  1 
ATOM   11702 C CD2  . TYR E 3 61  ? 13.778  145.820 37.748  1.00 16.18  ? 59  TYR E CD2  1 
ATOM   11703 C CE1  . TYR E 3 61  ? 13.414  145.668 35.044  1.00 26.65  ? 59  TYR E CE1  1 
ATOM   11704 C CE2  . TYR E 3 61  ? 12.735  145.091 37.234  1.00 15.16  ? 59  TYR E CE2  1 
ATOM   11705 C CZ   . TYR E 3 61  ? 12.566  145.019 35.879  1.00 20.54  ? 59  TYR E CZ   1 
ATOM   11706 O OH   . TYR E 3 61  ? 11.546  144.304 35.334  1.00 18.50  ? 59  TYR E OH   1 
ATOM   11707 N N    . ASN E 3 62  ? 19.077  148.301 37.860  1.00 21.52  ? 60  ASN E N    1 
ATOM   11708 C CA   . ASN E 3 62  ? 19.911  149.466 38.266  1.00 23.16  ? 60  ASN E CA   1 
ATOM   11709 C C    . ASN E 3 62  ? 19.340  150.360 39.320  1.00 23.94  ? 60  ASN E C    1 
ATOM   11710 O O    . ASN E 3 62  ? 19.788  151.479 39.481  1.00 24.48  ? 60  ASN E O    1 
ATOM   11711 C CB   . ASN E 3 62  ? 20.541  150.265 37.133  1.00 22.86  ? 60  ASN E CB   1 
ATOM   11712 C CG   . ASN E 3 62  ? 22.048  150.324 37.230  1.00 29.66  ? 60  ASN E CG   1 
ATOM   11713 O OD1  . ASN E 3 62  ? 22.633  149.968 38.250  1.00 32.00  ? 60  ASN E OD1  1 
ATOM   11714 N ND2  . ASN E 3 62  ? 22.689  150.773 36.162  1.00 39.06  ? 60  ASN E ND2  1 
ATOM   11715 N N    . ILE E 3 63  ? 18.351  149.859 40.039  1.00 23.45  ? 61  ILE E N    1 
ATOM   11716 C CA   . ILE E 3 63  ? 17.796  150.592 41.143  1.00 24.09  ? 61  ILE E CA   1 
ATOM   11717 C C    . ILE E 3 63  ? 18.888  150.583 42.173  1.00 30.67  ? 61  ILE E C    1 
ATOM   11718 O O    . ILE E 3 63  ? 19.163  149.573 42.814  1.00 27.84  ? 61  ILE E O    1 
ATOM   11719 C CB   . ILE E 3 63  ? 16.553  149.902 41.664  1.00 23.62  ? 61  ILE E CB   1 
ATOM   11720 C CG1  . ILE E 3 63  ? 15.510  149.799 40.559  1.00 22.49  ? 61  ILE E CG1  1 
ATOM   11721 C CG2  . ILE E 3 63  ? 16.016  150.610 42.891  1.00 26.15  ? 61  ILE E CG2  1 
ATOM   11722 C CD1  . ILE E 3 63  ? 14.347  148.899 40.879  1.00 18.18  ? 61  ILE E CD1  1 
ATOM   11723 N N    . GLN E 3 64  ? 19.545  151.717 42.331  1.00 31.94  ? 62  GLN E N    1 
ATOM   11724 C CA   . GLN E 3 64  ? 20.622  151.799 43.260  1.00 32.13  ? 62  GLN E CA   1 
ATOM   11725 C C    . GLN E 3 64  ? 20.210  152.553 44.439  1.00 33.41  ? 62  GLN E C    1 
ATOM   11726 O O    . GLN E 3 64  ? 19.053  152.604 44.783  1.00 36.17  ? 62  GLN E O    1 
ATOM   11727 C CB   . GLN E 3 64  ? 21.830  152.451 42.646  1.00 36.54  ? 62  GLN E CB   1 
ATOM   11728 C CG   . GLN E 3 64  ? 23.022  151.523 42.499  1.00 50.27  ? 62  GLN E CG   1 
ATOM   11729 C CD   . GLN E 3 64  ? 24.339  152.268 42.502  1.00 50.87  ? 62  GLN E CD   1 
ATOM   11730 O OE1  . GLN E 3 64  ? 25.379  151.725 42.874  1.00 47.35  ? 62  GLN E OE1  1 
ATOM   11731 N NE2  . GLN E 3 64  ? 24.300  153.524 42.087  1.00 53.25  ? 62  GLN E NE2  1 
ATOM   11732 N N    . LYS E 3 65  ? 21.164  153.143 45.119  1.00 36.91  ? 63  LYS E N    1 
ATOM   11733 C CA   . LYS E 3 65  ? 20.860  153.779 46.371  1.00 38.32  ? 63  LYS E CA   1 
ATOM   11734 C C    . LYS E 3 65  ? 20.224  155.102 46.266  1.00 32.94  ? 63  LYS E C    1 
ATOM   11735 O O    . LYS E 3 65  ? 20.688  155.949 45.525  1.00 29.81  ? 63  LYS E O    1 
ATOM   11736 C CB   . LYS E 3 65  ? 22.114  153.828 47.234  1.00 38.78  ? 63  LYS E CB   1 
ATOM   11737 C CG   . LYS E 3 65  ? 23.131  152.759 46.882  1.00 43.56  ? 63  LYS E CG   1 
ATOM   11738 C CD   . LYS E 3 65  ? 24.532  153.152 47.307  1.00 41.39  ? 63  LYS E CD   1 
ATOM   11739 C CE   . LYS E 3 65  ? 25.008  154.385 46.564  1.00 44.14  ? 63  LYS E CE   1 
ATOM   11740 N NZ   . LYS E 3 65  ? 25.539  154.061 45.215  1.00 40.32  ? 63  LYS E NZ   1 
ATOM   11741 N N    . GLU E 3 66  ? 19.143  155.266 46.995  1.00 28.72  ? 64  GLU E N    1 
ATOM   11742 C CA   . GLU E 3 66  ? 18.420  156.492 47.008  1.00 26.73  ? 64  GLU E CA   1 
ATOM   11743 C C    . GLU E 3 66  ? 17.955  156.771 45.633  1.00 26.73  ? 64  GLU E C    1 
ATOM   11744 O O    . GLU E 3 66  ? 18.122  157.853 45.115  1.00 27.32  ? 64  GLU E O    1 
ATOM   11745 C CB   . GLU E 3 66  ? 19.214  157.587 47.693  1.00 31.15  ? 64  GLU E CB   1 
ATOM   11746 C CG   . GLU E 3 66  ? 19.511  157.324 49.164  1.00 35.88  ? 64  GLU E CG   1 
ATOM   11747 C CD   . GLU E 3 66  ? 20.971  157.004 49.422  1.00 49.62  ? 64  GLU E CD   1 
ATOM   11748 O OE1  . GLU E 3 66  ? 21.833  157.686 48.835  1.00 50.27  ? 64  GLU E OE1  1 
ATOM   11749 O OE2  . GLU E 3 66  ? 21.260  156.070 50.203  1.00 46.50  ? 64  GLU E OE2  1 
ATOM   11750 N N    . SER E 3 67  ? 17.285  155.791 45.050  1.00 21.73  ? 65  SER E N    1 
ATOM   11751 C CA   . SER E 3 67  ? 16.756  155.939 43.738  1.00 21.16  ? 65  SER E CA   1 
ATOM   11752 C C    . SER E 3 67  ? 15.310  156.065 43.901  1.00 19.79  ? 65  SER E C    1 
ATOM   11753 O O    . SER E 3 67  ? 14.756  155.519 44.820  1.00 19.47  ? 65  SER E O    1 
ATOM   11754 C CB   . SER E 3 67  ? 17.045  154.709 42.940  1.00 26.86  ? 65  SER E CB   1 
ATOM   11755 O OG   . SER E 3 67  ? 15.901  153.901 42.880  1.00 37.33  ? 65  SER E OG   1 
ATOM   11756 N N    . THR E 3 68  ? 14.671  156.802 43.008  1.00 19.86  ? 66  THR E N    1 
ATOM   11757 C CA   . THR E 3 68  ? 13.266  157.038 43.136  1.00 15.78  ? 66  THR E CA   1 
ATOM   11758 C C    . THR E 3 68  ? 12.475  156.186 42.228  1.00 15.31  ? 66  THR E C    1 
ATOM   11759 O O    . THR E 3 68  ? 12.685  156.188 41.027  1.00 15.66  ? 66  THR E O    1 
ATOM   11760 C CB   . THR E 3 68  ? 12.892  158.516 43.030  1.00 18.22  ? 66  THR E CB   1 
ATOM   11761 O OG1  . THR E 3 68  ? 13.753  159.287 43.872  1.00 24.17  ? 66  THR E OG1  1 
ATOM   11762 C CG2  . THR E 3 68  ? 11.462  158.744 43.468  1.00 14.79  ? 66  THR E CG2  1 
ATOM   11763 N N    . LEU E 3 69  ? 11.544  155.440 42.814  1.00 17.61  ? 67  LEU E N    1 
ATOM   11764 C CA   . LEU E 3 69  ? 10.686  154.552 42.072  1.00 16.64  ? 67  LEU E CA   1 
ATOM   11765 C C    . LEU E 3 69  ? 9.313   155.083 42.199  1.00 12.34  ? 67  LEU E C    1 
ATOM   11766 O O    . LEU E 3 69  ? 9.059   155.905 43.037  1.00 14.08  ? 67  LEU E O    1 
ATOM   11767 C CB   . LEU E 3 69  ? 10.724  153.171 42.708  1.00 15.56  ? 67  LEU E CB   1 
ATOM   11768 C CG   . LEU E 3 69  ? 12.003  152.632 43.304  1.00 14.98  ? 67  LEU E CG   1 
ATOM   11769 C CD1  . LEU E 3 69  ? 11.659  151.308 43.935  1.00 18.80  ? 67  LEU E CD1  1 
ATOM   11770 C CD2  . LEU E 3 69  ? 12.965  152.412 42.172  1.00 15.86  ? 67  LEU E CD2  1 
ATOM   11771 N N    . HIS E 3 70  ? 8.397   154.617 41.382  1.00 10.35  ? 68  HIS E N    1 
ATOM   11772 C CA   . HIS E 3 70  ? 7.055   155.157 41.398  1.00 11.41  ? 68  HIS E CA   1 
ATOM   11773 C C    . HIS E 3 70  ? 5.974   154.156 41.603  1.00 10.07  ? 68  HIS E C    1 
ATOM   11774 O O    . HIS E 3 70  ? 6.038   153.080 41.106  1.00 12.57  ? 68  HIS E O    1 
ATOM   11775 C CB   . HIS E 3 70  ? 6.777   156.010 40.165  1.00 15.10  ? 68  HIS E CB   1 
ATOM   11776 C CG   . HIS E 3 70  ? 7.508   157.315 40.151  1.00 16.08  ? 68  HIS E CG   1 
ATOM   11777 N ND1  . HIS E 3 70  ? 8.820   157.430 39.752  1.00 14.20  ? 68  HIS E ND1  1 
ATOM   11778 C CD2  . HIS E 3 70  ? 7.109   158.562 40.488  1.00 17.49  ? 68  HIS E CD2  1 
ATOM   11779 C CE1  . HIS E 3 70  ? 9.200   158.689 39.852  1.00 11.85  ? 68  HIS E CE1  1 
ATOM   11780 N NE2  . HIS E 3 70  ? 8.180   159.397 40.295  1.00 11.96  ? 68  HIS E NE2  1 
ATOM   11781 N N    . LEU E 3 71  ? 4.949   154.537 42.336  1.00 11.69  ? 69  LEU E N    1 
ATOM   11782 C CA   . LEU E 3 71  ? 3.875   153.630 42.666  1.00 14.89  ? 69  LEU E CA   1 
ATOM   11783 C C    . LEU E 3 71  ? 2.564   154.078 42.129  1.00 14.67  ? 69  LEU E C    1 
ATOM   11784 O O    . LEU E 3 71  ? 2.066   155.115 42.492  1.00 14.72  ? 69  LEU E O    1 
ATOM   11785 C CB   . LEU E 3 71  ? 3.758   153.525 44.168  1.00 17.83  ? 69  LEU E CB   1 
ATOM   11786 C CG   . LEU E 3 71  ? 2.810   152.513 44.782  1.00 12.50  ? 69  LEU E CG   1 
ATOM   11787 C CD1  . LEU E 3 71  ? 3.417   151.158 44.619  1.00 10.54  ? 69  LEU E CD1  1 
ATOM   11788 C CD2  . LEU E 3 71  ? 2.604   152.813 46.253  1.00 12.57  ? 69  LEU E CD2  1 
ATOM   11789 N N    . VAL E 3 72  ? 1.982   153.266 41.274  1.00 13.24  ? 70  VAL E N    1 
ATOM   11790 C CA   . VAL E 3 72  ? 0.727   153.571 40.727  1.00 13.12  ? 70  VAL E CA   1 
ATOM   11791 C C    . VAL E 3 72  ? -0.089  152.448 41.173  1.00 14.92  ? 70  VAL E C    1 
ATOM   11792 O O    . VAL E 3 72  ? 0.181   151.329 40.875  1.00 18.21  ? 70  VAL E O    1 
ATOM   11793 C CB   . VAL E 3 72  ? 0.762   153.579 39.225  1.00 14.85  ? 70  VAL E CB   1 
ATOM   11794 C CG1  . VAL E 3 72  ? -0.633  153.743 38.663  1.00 18.78  ? 70  VAL E CG1  1 
ATOM   11795 C CG2  . VAL E 3 72  ? 1.689   154.667 38.716  1.00 13.68  ? 70  VAL E CG2  1 
ATOM   11796 N N    . LEU E 3 73  ? -1.095  152.757 41.931  1.00 15.46  ? 71  LEU E N    1 
ATOM   11797 C CA   . LEU E 3 73  ? -1.956  151.770 42.452  1.00 18.91  ? 71  LEU E CA   1 
ATOM   11798 C C    . LEU E 3 73  ? -3.027  151.515 41.479  1.00 16.02  ? 71  LEU E C    1 
ATOM   11799 O O    . LEU E 3 73  ? -3.591  152.438 40.938  1.00 17.39  ? 71  LEU E O    1 
ATOM   11800 C CB   . LEU E 3 73  ? -2.513  152.277 43.773  1.00 19.11  ? 71  LEU E CB   1 
ATOM   11801 C CG   . LEU E 3 73  ? -1.513  152.418 44.907  1.00 17.34  ? 71  LEU E CG   1 
ATOM   11802 C CD1  . LEU E 3 73  ? -2.268  152.364 46.213  1.00 15.82  ? 71  LEU E CD1  1 
ATOM   11803 C CD2  . LEU E 3 73  ? -0.490  151.303 44.843  1.00 21.56  ? 71  LEU E CD2  1 
ATOM   11804 N N    . ARG E 3 74  ? -3.328  150.259 41.287  1.00 12.12  ? 72  ARG E N    1 
ATOM   11805 C CA   . ARG E 3 74  ? -4.274  149.881 40.313  1.00 17.59  ? 72  ARG E CA   1 
ATOM   11806 C C    . ARG E 3 74  ? -5.701  149.908 40.779  1.00 17.39  ? 72  ARG E C    1 
ATOM   11807 O O    . ARG E 3 74  ? -6.063  149.405 41.808  1.00 15.16  ? 72  ARG E O    1 
ATOM   11808 C CB   . ARG E 3 74  ? -3.892  148.499 39.844  1.00 24.68  ? 72  ARG E CB   1 
ATOM   11809 C CG   . ARG E 3 74  ? -3.360  148.396 38.438  1.00 23.25  ? 72  ARG E CG   1 
ATOM   11810 C CD   . ARG E 3 74  ? -3.796  147.074 37.845  1.00 24.98  ? 72  ARG E CD   1 
ATOM   11811 N NE   . ARG E 3 74  ? -3.076  145.947 38.412  1.00 25.37  ? 72  ARG E NE   1 
ATOM   11812 C CZ   . ARG E 3 74  ? -3.246  144.689 38.026  1.00 27.70  ? 72  ARG E CZ   1 
ATOM   11813 N NH1  . ARG E 3 74  ? -4.118  144.397 37.073  1.00 22.95  ? 72  ARG E NH1  1 
ATOM   11814 N NH2  . ARG E 3 74  ? -2.548  143.724 38.595  1.00 29.34  ? 72  ARG E NH2  1 
ATOM   11815 N N    . LEU E 3 75  ? -6.542  150.520 39.990  1.00 16.38  ? 73  LEU E N    1 
ATOM   11816 C CA   . LEU E 3 75  ? -7.924  150.541 40.316  1.00 19.99  ? 73  LEU E CA   1 
ATOM   11817 C C    . LEU E 3 75  ? -8.607  149.411 39.592  1.00 27.39  ? 73  LEU E C    1 
ATOM   11818 O O    . LEU E 3 75  ? -9.332  149.610 38.619  1.00 23.83  ? 73  LEU E O    1 
ATOM   11819 C CB   . LEU E 3 75  ? -8.529  151.885 39.962  1.00 25.72  ? 73  LEU E CB   1 
ATOM   11820 C CG   . LEU E 3 75  ? -9.641  152.267 40.952  1.00 25.40  ? 73  LEU E CG   1 
ATOM   11821 C CD1  . LEU E 3 75  ? -9.405  153.637 41.553  1.00 25.82  ? 73  LEU E CD1  1 
ATOM   11822 C CD2  . LEU E 3 75  ? -11.039 152.170 40.363  1.00 19.69  ? 73  LEU E CD2  1 
ATOM   11823 N N    . ARG E 3 76  ? -8.328  148.199 40.032  1.00 29.54  ? 74  ARG E N    1 
ATOM   11824 C CA   . ARG E 3 76  ? -8.951  147.043 39.470  1.00 21.93  ? 74  ARG E CA   1 
ATOM   11825 C C    . ARG E 3 76  ? -10.183 147.150 40.238  1.00 19.42  ? 74  ARG E C    1 
ATOM   11826 O O    . ARG E 3 76  ? -10.203 146.929 41.422  1.00 25.02  ? 74  ARG E O    1 
ATOM   11827 C CB   . ARG E 3 76  ? -8.173  145.815 39.913  1.00 20.05  ? 74  ARG E CB   1 
ATOM   11828 C CG   . ARG E 3 76  ? -6.918  146.123 40.696  1.00 18.69  ? 74  ARG E CG   1 
ATOM   11829 C CD   . ARG E 3 76  ? -6.328  144.855 41.252  1.00 22.67  ? 74  ARG E CD   1 
ATOM   11830 N NE   . ARG E 3 76  ? -6.040  143.911 40.186  1.00 29.61  ? 74  ARG E NE   1 
ATOM   11831 C CZ   . ARG E 3 76  ? -5.656  142.657 40.376  1.00 29.70  ? 74  ARG E CZ   1 
ATOM   11832 N NH1  . ARG E 3 76  ? -5.518  142.185 41.599  1.00 27.61  ? 74  ARG E NH1  1 
ATOM   11833 N NH2  . ARG E 3 76  ? -5.418  141.876 39.337  1.00 27.60  ? 74  ARG E NH2  1 
ATOM   11834 N N    . GLY E 3 77  ? -11.219 147.602 39.593  1.00 15.29  ? 75  GLY E N    1 
ATOM   11835 C CA   . GLY E 3 77  ? -12.458 147.829 40.293  1.00 16.15  ? 75  GLY E CA   1 
ATOM   11836 C C    . GLY E 3 77  ? -13.184 146.557 40.506  1.00 19.93  ? 75  GLY E C    1 
ATOM   11837 O O    . GLY E 3 77  ? -14.338 146.549 40.903  1.00 24.38  ? 75  GLY E O    1 
ATOM   11838 N N    . GLY E 3 78  ? -12.502 145.469 40.266  1.00 16.42  ? 76  GLY E N    1 
ATOM   11839 C CA   . GLY E 3 78  ? -13.153 144.204 40.372  1.00 19.30  ? 76  GLY E CA   1 
ATOM   11840 C C    . GLY E 3 78  ? -14.327 144.152 39.421  1.00 37.42  ? 76  GLY E C    1 
ATOM   11841 O O    . GLY E 3 78  ? -14.243 144.530 38.253  1.00 44.35  ? 76  GLY E O    1 
ATOM   11842 N N    . SER F 3 2   ? 49.094  100.112 35.186  1.00 14.34  ? 0   SER F N    1 
ATOM   11843 C CA   . SER F 3 2   ? 50.197  99.773  36.050  1.00 16.45  ? 0   SER F CA   1 
ATOM   11844 C C    . SER F 3 2   ? 49.895  98.484  36.790  1.00 30.76  ? 0   SER F C    1 
ATOM   11845 O O    . SER F 3 2   ? 50.116  97.408  36.247  1.00 32.99  ? 0   SER F O    1 
ATOM   11846 C CB   . SER F 3 2   ? 50.490  100.911 36.998  1.00 13.67  ? 0   SER F CB   1 
ATOM   11847 O OG   . SER F 3 2   ? 51.594  100.640 37.826  1.00 29.09  ? 0   SER F OG   1 
ATOM   11848 N N    . MET F 3 3   ? 49.404  98.567  38.023  1.00 36.10  ? 1   MET F N    1 
ATOM   11849 C CA   . MET F 3 3   ? 49.020  97.376  38.779  1.00 31.95  ? 1   MET F CA   1 
ATOM   11850 C C    . MET F 3 3   ? 47.661  96.885  38.461  1.00 29.94  ? 1   MET F C    1 
ATOM   11851 O O    . MET F 3 3   ? 46.946  97.508  37.709  1.00 28.07  ? 1   MET F O    1 
ATOM   11852 C CB   . MET F 3 3   ? 49.187  97.528  40.289  1.00 27.39  ? 1   MET F CB   1 
ATOM   11853 C CG   . MET F 3 3   ? 48.285  98.502  41.000  1.00 32.89  ? 1   MET F CG   1 
ATOM   11854 S SD   . MET F 3 3   ? 48.781  98.566  42.724  1.00 47.72  ? 1   MET F SD   1 
ATOM   11855 C CE   . MET F 3 3   ? 47.638  99.768  43.370  1.00 26.59  ? 1   MET F CE   1 
ATOM   11856 N N    . GLN F 3 4   ? 47.332  95.716  38.967  1.00 31.78  ? 2   GLN F N    1 
ATOM   11857 C CA   . GLN F 3 4   ? 46.025  95.160  38.768  1.00 33.13  ? 2   GLN F CA   1 
ATOM   11858 C C    . GLN F 3 4   ? 45.500  94.708  40.113  1.00 31.92  ? 2   GLN F C    1 
ATOM   11859 O O    . GLN F 3 4   ? 46.170  93.963  40.774  1.00 34.70  ? 2   GLN F O    1 
ATOM   11860 C CB   . GLN F 3 4   ? 46.142  93.949  37.850  1.00 33.22  ? 2   GLN F CB   1 
ATOM   11861 C CG   . GLN F 3 4   ? 46.703  94.212  36.471  1.00 31.87  ? 2   GLN F CG   1 
ATOM   11862 C CD   . GLN F 3 4   ? 47.084  92.932  35.778  1.00 34.13  ? 2   GLN F CD   1 
ATOM   11863 O OE1  . GLN F 3 4   ? 46.999  91.854  36.362  1.00 38.74  ? 2   GLN F OE1  1 
ATOM   11864 N NE2  . GLN F 3 4   ? 47.514  93.037  34.532  1.00 30.95  ? 2   GLN F NE2  1 
ATOM   11865 N N    . ILE F 3 5   ? 44.283  95.069  40.488  1.00 27.20  ? 3   ILE F N    1 
ATOM   11866 C CA   . ILE F 3 5   ? 43.719  94.717  41.784  1.00 24.53  ? 3   ILE F CA   1 
ATOM   11867 C C    . ILE F 3 5   ? 42.471  93.930  41.511  1.00 25.11  ? 3   ILE F C    1 
ATOM   11868 O O    . ILE F 3 5   ? 41.932  94.000  40.430  1.00 28.35  ? 3   ILE F O    1 
ATOM   11869 C CB   . ILE F 3 5   ? 43.451  95.969  42.622  1.00 19.72  ? 3   ILE F CB   1 
ATOM   11870 C CG1  . ILE F 3 5   ? 44.282  95.944  43.890  1.00 29.24  ? 3   ILE F CG1  1 
ATOM   11871 C CG2  . ILE F 3 5   ? 41.978  96.183  42.912  1.00 20.82  ? 3   ILE F CG2  1 
ATOM   11872 C CD1  . ILE F 3 5   ? 45.719  96.343  43.661  1.00 36.09  ? 3   ILE F CD1  1 
ATOM   11873 N N    . PHE F 3 6   ? 42.048  93.107  42.450  1.00 20.44  ? 4   PHE F N    1 
ATOM   11874 C CA   . PHE F 3 6   ? 40.870  92.285  42.266  1.00 21.41  ? 4   PHE F CA   1 
ATOM   11875 C C    . PHE F 3 6   ? 39.803  92.620  43.290  1.00 19.12  ? 4   PHE F C    1 
ATOM   11876 O O    . PHE F 3 6   ? 40.118  93.044  44.364  1.00 17.69  ? 4   PHE F O    1 
ATOM   11877 C CB   . PHE F 3 6   ? 41.247  90.831  42.365  1.00 19.50  ? 4   PHE F CB   1 
ATOM   11878 C CG   . PHE F 3 6   ? 42.091  90.338  41.235  1.00 29.08  ? 4   PHE F CG   1 
ATOM   11879 C CD1  . PHE F 3 6   ? 43.448  90.579  41.204  1.00 29.29  ? 4   PHE F CD1  1 
ATOM   11880 C CD2  . PHE F 3 6   ? 41.526  89.603  40.219  1.00 28.47  ? 4   PHE F CD2  1 
ATOM   11881 C CE1  . PHE F 3 6   ? 44.222  90.121  40.166  1.00 31.47  ? 4   PHE F CE1  1 
ATOM   11882 C CE2  . PHE F 3 6   ? 42.294  89.132  39.180  1.00 31.28  ? 4   PHE F CE2  1 
ATOM   11883 C CZ   . PHE F 3 6   ? 43.646  89.394  39.153  1.00 38.06  ? 4   PHE F CZ   1 
ATOM   11884 N N    . VAL F 3 7   ? 38.538  92.467  42.939  1.00 17.49  ? 5   VAL F N    1 
ATOM   11885 C CA   . VAL F 3 7   ? 37.459  92.767  43.847  1.00 15.32  ? 5   VAL F CA   1 
ATOM   11886 C C    . VAL F 3 7   ? 36.484  91.609  43.746  1.00 18.19  ? 5   VAL F C    1 
ATOM   11887 O O    . VAL F 3 7   ? 35.992  91.329  42.679  1.00 18.59  ? 5   VAL F O    1 
ATOM   11888 C CB   . VAL F 3 7   ? 36.729  94.089  43.513  1.00 14.37  ? 5   VAL F CB   1 
ATOM   11889 C CG1  . VAL F 3 7   ? 35.763  94.481  44.599  1.00 13.69  ? 5   VAL F CG1  1 
ATOM   11890 C CG2  . VAL F 3 7   ? 37.688  95.224  43.220  1.00 16.57  ? 5   VAL F CG2  1 
ATOM   11891 N N    . LYS F 3 8   ? 36.180  90.944  44.863  1.00 19.11  ? 6   LYS F N    1 
ATOM   11892 C CA   . LYS F 3 8   ? 35.245  89.826  44.889  1.00 18.59  ? 6   LYS F CA   1 
ATOM   11893 C C    . LYS F 3 8   ? 33.883  90.074  45.532  1.00 20.18  ? 6   LYS F C    1 
ATOM   11894 O O    . LYS F 3 8   ? 33.795  90.623  46.609  1.00 17.54  ? 6   LYS F O    1 
ATOM   11895 C CB   . LYS F 3 8   ? 35.920  88.641  45.519  1.00 15.46  ? 6   LYS F CB   1 
ATOM   11896 C CG   . LYS F 3 8   ? 37.056  88.076  44.694  1.00 14.51  ? 6   LYS F CG   1 
ATOM   11897 C CD   . LYS F 3 8   ? 37.003  86.564  44.686  1.00 20.66  ? 6   LYS F CD   1 
ATOM   11898 C CE   . LYS F 3 8   ? 38.240  85.960  44.057  1.00 13.40  ? 6   LYS F CE   1 
ATOM   11899 N NZ   . LYS F 3 8   ? 38.202  84.478  44.156  1.00 10.92  ? 6   LYS F NZ   1 
ATOM   11900 N N    . THR F 3 9   ? 32.823  89.678  44.844  1.00 20.71  ? 7   THR F N    1 
ATOM   11901 C CA   . THR F 3 9   ? 31.472  89.897  45.319  1.00 20.65  ? 7   THR F CA   1 
ATOM   11902 C C    . THR F 3 9   ? 30.904  88.707  46.030  1.00 28.13  ? 7   THR F C    1 
ATOM   11903 O O    . THR F 3 9   ? 31.548  87.677  46.139  1.00 30.98  ? 7   THR F O    1 
ATOM   11904 C CB   . THR F 3 9   ? 30.593  90.381  44.171  1.00 22.64  ? 7   THR F CB   1 
ATOM   11905 O OG1  . THR F 3 9   ? 29.213  90.292  44.500  1.00 21.54  ? 7   THR F OG1  1 
ATOM   11906 C CG2  . THR F 3 9   ? 30.864  89.629  42.937  1.00 20.23  ? 7   THR F CG2  1 
ATOM   11907 N N    . LEU F 3 10  ? 29.706  88.833  46.555  1.00 27.67  ? 8   LEU F N    1 
ATOM   11908 C CA   . LEU F 3 10  ? 29.099  87.779  47.334  1.00 26.04  ? 8   LEU F CA   1 
ATOM   11909 C C    . LEU F 3 10  ? 28.520  86.637  46.525  1.00 34.07  ? 8   LEU F C    1 
ATOM   11910 O O    . LEU F 3 10  ? 27.795  85.826  47.072  1.00 33.98  ? 8   LEU F O    1 
ATOM   11911 C CB   . LEU F 3 10  ? 28.029  88.425  48.189  1.00 24.97  ? 8   LEU F CB   1 
ATOM   11912 C CG   . LEU F 3 10  ? 28.340  89.830  48.712  1.00 22.05  ? 8   LEU F CG   1 
ATOM   11913 C CD1  . LEU F 3 10  ? 27.059  90.510  49.155  1.00 27.32  ? 8   LEU F CD1  1 
ATOM   11914 C CD2  . LEU F 3 10  ? 29.332  89.789  49.858  1.00 23.06  ? 8   LEU F CD2  1 
ATOM   11915 N N    . THR F 3 11  ? 28.810  86.579  45.226  1.00 36.20  ? 9   THR F N    1 
ATOM   11916 C CA   . THR F 3 11  ? 28.366  85.496  44.374  1.00 29.14  ? 9   THR F CA   1 
ATOM   11917 C C    . THR F 3 11  ? 29.625  84.777  44.087  1.00 30.73  ? 9   THR F C    1 
ATOM   11918 O O    . THR F 3 11  ? 29.626  83.585  43.823  1.00 36.34  ? 9   THR F O    1 
ATOM   11919 C CB   . THR F 3 11  ? 27.711  85.981  43.091  1.00 34.51  ? 9   THR F CB   1 
ATOM   11920 O OG1  . THR F 3 11  ? 27.902  85.003  42.065  1.00 50.72  ? 9   THR F OG1  1 
ATOM   11921 C CG2  . THR F 3 11  ? 28.276  87.266  42.632  1.00 34.42  ? 9   THR F CG2  1 
ATOM   11922 N N    . GLY F 3 12  ? 30.731  85.483  44.167  1.00 31.98  ? 10  GLY F N    1 
ATOM   11923 C CA   . GLY F 3 12  ? 32.024  84.855  44.015  1.00 35.00  ? 10  GLY F CA   1 
ATOM   11924 C C    . GLY F 3 12  ? 32.692  85.248  42.763  1.00 31.50  ? 10  GLY F C    1 
ATOM   11925 O O    . GLY F 3 12  ? 33.512  84.519  42.224  1.00 32.98  ? 10  GLY F O    1 
ATOM   11926 N N    . LYS F 3 13  ? 32.425  86.446  42.307  1.00 27.73  ? 11  LYS F N    1 
ATOM   11927 C CA   . LYS F 3 13  ? 32.955  86.842  41.048  1.00 25.01  ? 11  LYS F CA   1 
ATOM   11928 C C    . LYS F 3 13  ? 34.019  87.890  41.152  1.00 23.24  ? 11  LYS F C    1 
ATOM   11929 O O    . LYS F 3 13  ? 33.888  88.812  41.911  1.00 29.73  ? 11  LYS F O    1 
ATOM   11930 C CB   . LYS F 3 13  ? 31.809  87.242  40.142  1.00 25.51  ? 11  LYS F CB   1 
ATOM   11931 C CG   . LYS F 3 13  ? 30.748  86.173  39.959  1.00 26.33  ? 11  LYS F CG   1 
ATOM   11932 C CD   . LYS F 3 13  ? 30.169  86.199  38.557  1.00 39.92  ? 11  LYS F CD   1 
ATOM   11933 C CE   . LYS F 3 13  ? 29.017  87.182  38.443  1.00 45.03  ? 11  LYS F CE   1 
ATOM   11934 N NZ   . LYS F 3 13  ? 28.411  87.163  37.084  1.00 45.95  ? 11  LYS F NZ   1 
ATOM   11935 N N    . THR F 3 14  ? 35.083  87.756  40.371  1.00 18.72  ? 12  THR F N    1 
ATOM   11936 C CA   . THR F 3 14  ? 36.184  88.676  40.438  1.00 18.37  ? 12  THR F CA   1 
ATOM   11937 C C    . THR F 3 14  ? 36.112  89.649  39.331  1.00 25.11  ? 12  THR F C    1 
ATOM   11938 O O    . THR F 3 14  ? 35.873  89.275  38.195  1.00 25.27  ? 12  THR F O    1 
ATOM   11939 C CB   . THR F 3 14  ? 37.529  87.972  40.409  1.00 14.92  ? 12  THR F CB   1 
ATOM   11940 O OG1  . THR F 3 14  ? 38.310  88.482  39.331  1.00 30.67  ? 12  THR F OG1  1 
ATOM   11941 C CG2  . THR F 3 14  ? 37.351  86.492  40.237  1.00 23.07  ? 12  THR F CG2  1 
ATOM   11942 N N    . ILE F 3 15  ? 36.272  90.931  39.665  1.00 23.33  ? 13  ILE F N    1 
ATOM   11943 C CA   . ILE F 3 15  ? 36.237  91.993  38.694  1.00 22.01  ? 13  ILE F CA   1 
ATOM   11944 C C    . ILE F 3 15  ? 37.669  92.390  38.747  1.00 22.84  ? 13  ILE F C    1 
ATOM   11945 O O    . ILE F 3 15  ? 38.312  92.223  39.761  1.00 21.56  ? 13  ILE F O    1 
ATOM   11946 C CB   . ILE F 3 15  ? 35.243  93.107  39.094  1.00 15.78  ? 13  ILE F CB   1 
ATOM   11947 C CG1  . ILE F 3 15  ? 35.928  94.305  39.727  1.00 23.15  ? 13  ILE F CG1  1 
ATOM   11948 C CG2  . ILE F 3 15  ? 34.133  92.573  39.979  1.00 12.30  ? 13  ILE F CG2  1 
ATOM   11949 C CD1  . ILE F 3 15  ? 35.315  95.612  39.310  1.00 22.48  ? 13  ILE F CD1  1 
ATOM   11950 N N    . THR F 3 16  ? 38.225  92.824  37.634  1.00 22.90  ? 14  THR F N    1 
ATOM   11951 C CA   . THR F 3 16  ? 39.643  93.117  37.612  1.00 31.75  ? 14  THR F CA   1 
ATOM   11952 C C    . THR F 3 16  ? 39.812  94.565  37.343  1.00 32.51  ? 14  THR F C    1 
ATOM   11953 O O    . THR F 3 16  ? 39.135  95.103  36.492  1.00 34.18  ? 14  THR F O    1 
ATOM   11954 C CB   . THR F 3 16  ? 40.415  92.263  36.593  1.00 30.57  ? 14  THR F CB   1 
ATOM   11955 O OG1  . THR F 3 16  ? 40.003  90.893  36.691  1.00 26.06  ? 14  THR F OG1  1 
ATOM   11956 C CG2  . THR F 3 16  ? 41.912  92.341  36.843  1.00 29.38  ? 14  THR F CG2  1 
ATOM   11957 N N    . LEU F 3 17  ? 40.693  95.214  38.089  1.00 32.83  ? 15  LEU F N    1 
ATOM   11958 C CA   . LEU F 3 17  ? 40.882  96.636  37.964  1.00 33.60  ? 15  LEU F CA   1 
ATOM   11959 C C    . LEU F 3 17  ? 42.323  96.975  37.690  1.00 31.10  ? 15  LEU F C    1 
ATOM   11960 O O    . LEU F 3 17  ? 43.201  96.347  38.208  1.00 29.40  ? 15  LEU F O    1 
ATOM   11961 C CB   . LEU F 3 17  ? 40.376  97.302  39.241  1.00 25.10  ? 15  LEU F CB   1 
ATOM   11962 C CG   . LEU F 3 17  ? 39.239  98.322  39.218  1.00 25.03  ? 15  LEU F CG   1 
ATOM   11963 C CD1  . LEU F 3 17  ? 38.120  97.926  38.279  1.00 25.86  ? 15  LEU F CD1  1 
ATOM   11964 C CD2  . LEU F 3 17  ? 38.697  98.490  40.617  1.00 26.52  ? 15  LEU F CD2  1 
ATOM   11965 N N    . GLU F 3 18  ? 42.560  97.936  36.814  1.00 29.67  ? 16  GLU F N    1 
ATOM   11966 C CA   . GLU F 3 18  ? 43.921  98.380  36.520  1.00 35.99  ? 16  GLU F CA   1 
ATOM   11967 C C    . GLU F 3 18  ? 44.107  99.699  37.168  1.00 33.19  ? 16  GLU F C    1 
ATOM   11968 O O    . GLU F 3 18  ? 43.627  100.707 36.687  1.00 34.81  ? 16  GLU F O    1 
ATOM   11969 C CB   . GLU F 3 18  ? 44.183  98.434  35.025  1.00 40.56  ? 16  GLU F CB   1 
ATOM   11970 C CG   . GLU F 3 18  ? 43.591  97.268  34.254  1.00 37.01  ? 16  GLU F CG   1 
ATOM   11971 C CD   . GLU F 3 18  ? 44.650  96.331  33.728  1.00 41.50  ? 16  GLU F CD   1 
ATOM   11972 O OE1  . GLU F 3 18  ? 45.765  96.805  33.443  1.00 47.78  ? 16  GLU F OE1  1 
ATOM   11973 O OE2  . GLU F 3 18  ? 44.367  95.126  33.598  1.00 39.01  ? 16  GLU F OE2  1 
ATOM   11974 N N    . VAL F 3 19  ? 44.871  99.721  38.239  1.00 32.16  ? 17  VAL F N    1 
ATOM   11975 C CA   . VAL F 3 19  ? 44.983  100.898 39.039  1.00 31.27  ? 17  VAL F CA   1 
ATOM   11976 C C    . VAL F 3 19  ? 46.394  101.299 39.323  1.00 30.71  ? 17  VAL F C    1 
ATOM   11977 O O    . VAL F 3 19  ? 47.310  100.727 38.782  1.00 32.40  ? 17  VAL F O    1 
ATOM   11978 C CB   . VAL F 3 19  ? 44.322  100.572 40.380  1.00 25.49  ? 17  VAL F CB   1 
ATOM   11979 C CG1  . VAL F 3 19  ? 42.835  100.875 40.327  1.00 27.88  ? 17  VAL F CG1  1 
ATOM   11980 C CG2  . VAL F 3 19  ? 44.517  99.113  40.717  1.00 23.88  ? 17  VAL F CG2  1 
ATOM   11981 N N    . GLU F 3 20  ? 46.583  102.283 40.174  1.00 26.80  ? 18  GLU F N    1 
ATOM   11982 C CA   . GLU F 3 20  ? 47.906  102.783 40.480  1.00 29.84  ? 18  GLU F CA   1 
ATOM   11983 C C    . GLU F 3 20  ? 47.879  102.997 41.967  1.00 37.90  ? 18  GLU F C    1 
ATOM   11984 O O    . GLU F 3 20  ? 46.817  103.126 42.532  1.00 38.02  ? 18  GLU F O    1 
ATOM   11985 C CB   . GLU F 3 20  ? 48.174  104.121 39.760  1.00 21.93  ? 18  GLU F CB   1 
ATOM   11986 C CG   . GLU F 3 20  ? 49.011  104.043 38.500  1.00 26.12  ? 18  GLU F CG   1 
ATOM   11987 C CD   . GLU F 3 20  ? 48.192  104.228 37.242  1.00 26.28  ? 18  GLU F CD   1 
ATOM   11988 O OE1  . GLU F 3 20  ? 47.297  105.086 37.241  1.00 32.80  ? 18  GLU F OE1  1 
ATOM   11989 O OE2  . GLU F 3 20  ? 48.438  103.519 36.255  1.00 20.45  ? 18  GLU F OE2  1 
ATOM   11990 N N    . PRO F 3 21  ? 49.076  103.106 42.643  1.00 32.16  ? 19  PRO F N    1 
ATOM   11991 C CA   . PRO F 3 21  ? 49.015  103.248 44.088  1.00 22.92  ? 19  PRO F CA   1 
ATOM   11992 C C    . PRO F 3 21  ? 48.414  104.524 44.568  1.00 20.85  ? 19  PRO F C    1 
ATOM   11993 O O    . PRO F 3 21  ? 48.318  104.772 45.751  1.00 23.39  ? 19  PRO F O    1 
ATOM   11994 C CB   . PRO F 3 21  ? 50.494  103.308 44.422  1.00 22.21  ? 19  PRO F CB   1 
ATOM   11995 C CG   . PRO F 3 21  ? 51.139  102.429 43.447  1.00 24.49  ? 19  PRO F CG   1 
ATOM   11996 C CD   . PRO F 3 21  ? 50.509  102.987 42.240  1.00 28.52  ? 19  PRO F CD   1 
ATOM   11997 N N    . SER F 3 22  ? 47.994  105.352 43.659  1.00 19.02  ? 20  SER F N    1 
ATOM   11998 C CA   . SER F 3 22  ? 47.538  106.677 44.015  1.00 30.21  ? 20  SER F CA   1 
ATOM   11999 C C    . SER F 3 22  ? 46.100  106.891 43.679  1.00 26.52  ? 20  SER F C    1 
ATOM   12000 O O    . SER F 3 22  ? 45.495  107.889 44.038  1.00 24.94  ? 20  SER F O    1 
ATOM   12001 C CB   . SER F 3 22  ? 48.403  107.700 43.243  1.00 29.66  ? 20  SER F CB   1 
ATOM   12002 O OG   . SER F 3 22  ? 49.753  107.286 43.139  1.00 22.70  ? 20  SER F OG   1 
ATOM   12003 N N    . ASP F 3 23  ? 45.539  105.942 42.985  1.00 21.16  ? 21  ASP F N    1 
ATOM   12004 C CA   . ASP F 3 23  ? 44.185  106.060 42.630  1.00 21.32  ? 21  ASP F CA   1 
ATOM   12005 C C    . ASP F 3 23  ? 43.380  106.028 43.886  1.00 29.30  ? 21  ASP F C    1 
ATOM   12006 O O    . ASP F 3 23  ? 43.622  105.225 44.758  1.00 28.64  ? 21  ASP F O    1 
ATOM   12007 C CB   . ASP F 3 23  ? 43.832  104.975 41.646  1.00 24.76  ? 21  ASP F CB   1 
ATOM   12008 C CG   . ASP F 3 23  ? 44.246  105.315 40.247  1.00 34.32  ? 21  ASP F CG   1 
ATOM   12009 O OD1  . ASP F 3 23  ? 44.806  106.408 40.053  1.00 37.03  ? 21  ASP F OD1  1 
ATOM   12010 O OD2  . ASP F 3 23  ? 44.005  104.501 39.338  1.00 31.95  ? 21  ASP F OD2  1 
ATOM   12011 N N    . THR F 3 24  ? 42.418  106.934 43.986  1.00 34.59  ? 22  THR F N    1 
ATOM   12012 C CA   . THR F 3 24  ? 41.584  107.052 45.157  1.00 26.52  ? 22  THR F CA   1 
ATOM   12013 C C    . THR F 3 24  ? 40.652  105.875 45.219  1.00 29.32  ? 22  THR F C    1 
ATOM   12014 O O    . THR F 3 24  ? 40.569  105.114 44.296  1.00 30.20  ? 22  THR F O    1 
ATOM   12015 C CB   . THR F 3 24  ? 40.810  108.351 45.056  1.00 21.96  ? 22  THR F CB   1 
ATOM   12016 O OG1  . THR F 3 24  ? 40.943  108.871 43.736  1.00 24.97  ? 22  THR F OG1  1 
ATOM   12017 C CG2  . THR F 3 24  ? 41.363  109.356 46.016  1.00 31.80  ? 22  THR F CG2  1 
ATOM   12018 N N    . ILE F 3 25  ? 39.920  105.711 46.305  1.00 29.60  ? 23  ILE F N    1 
ATOM   12019 C CA   . ILE F 3 25  ? 39.010  104.582 46.436  1.00 26.46  ? 23  ILE F CA   1 
ATOM   12020 C C    . ILE F 3 25  ? 37.719  104.999 45.811  1.00 23.18  ? 23  ILE F C    1 
ATOM   12021 O O    . ILE F 3 25  ? 36.831  104.220 45.604  1.00 20.62  ? 23  ILE F O    1 
ATOM   12022 C CB   . ILE F 3 25  ? 38.906  104.104 47.887  1.00 23.64  ? 23  ILE F CB   1 
ATOM   12023 C CG1  . ILE F 3 25  ? 40.283  103.716 48.406  1.00 25.81  ? 23  ILE F CG1  1 
ATOM   12024 C CG2  . ILE F 3 25  ? 38.044  102.867 48.048  1.00 23.81  ? 23  ILE F CG2  1 
ATOM   12025 C CD1  . ILE F 3 25  ? 40.837  102.476 47.758  1.00 25.18  ? 23  ILE F CD1  1 
ATOM   12026 N N    . GLU F 3 26  ? 37.649  106.238 45.417  1.00 25.36  ? 24  GLU F N    1 
ATOM   12027 C CA   . GLU F 3 26  ? 36.470  106.769 44.796  1.00 24.32  ? 24  GLU F CA   1 
ATOM   12028 C C    . GLU F 3 26  ? 36.739  106.695 43.368  1.00 25.07  ? 24  GLU F C    1 
ATOM   12029 O O    . GLU F 3 26  ? 35.867  106.944 42.569  1.00 23.80  ? 24  GLU F O    1 
ATOM   12030 C CB   . GLU F 3 26  ? 36.416  108.214 45.134  1.00 28.72  ? 24  GLU F CB   1 
ATOM   12031 C CG   . GLU F 3 26  ? 35.074  108.858 45.390  1.00 39.27  ? 24  GLU F CG   1 
ATOM   12032 C CD   . GLU F 3 26  ? 35.250  110.264 45.939  1.00 45.04  ? 24  GLU F CD   1 
ATOM   12033 O OE1  . GLU F 3 26  ? 36.369  110.808 45.815  1.00 31.31  ? 24  GLU F OE1  1 
ATOM   12034 O OE2  . GLU F 3 26  ? 34.286  110.826 46.496  1.00 44.07  ? 24  GLU F OE2  1 
ATOM   12035 N N    . ASN F 3 27  ? 37.973  106.363 43.023  1.00 25.24  ? 25  ASN F N    1 
ATOM   12036 C CA   . ASN F 3 27  ? 38.357  106.222 41.630  1.00 28.17  ? 25  ASN F CA   1 
ATOM   12037 C C    . ASN F 3 27  ? 38.190  104.808 41.320  1.00 28.33  ? 25  ASN F C    1 
ATOM   12038 O O    . ASN F 3 27  ? 37.776  104.469 40.249  1.00 26.75  ? 25  ASN F O    1 
ATOM   12039 C CB   . ASN F 3 27  ? 39.798  106.579 41.382  1.00 27.82  ? 25  ASN F CB   1 
ATOM   12040 C CG   . ASN F 3 27  ? 39.974  107.524 40.229  1.00 36.24  ? 25  ASN F CG   1 
ATOM   12041 O OD1  . ASN F 3 27  ? 39.442  107.306 39.141  1.00 32.16  ? 25  ASN F OD1  1 
ATOM   12042 N ND2  . ASN F 3 27  ? 40.727  108.586 40.457  1.00 48.19  ? 25  ASN F ND2  1 
ATOM   12043 N N    . VAL F 3 28  ? 38.485  103.951 42.277  1.00 26.25  ? 26  VAL F N    1 
ATOM   12044 C CA   . VAL F 3 28  ? 38.264  102.544 42.071  1.00 24.95  ? 26  VAL F CA   1 
ATOM   12045 C C    . VAL F 3 28  ? 36.795  102.316 42.078  1.00 20.66  ? 26  VAL F C    1 
ATOM   12046 O O    . VAL F 3 28  ? 36.316  101.523 41.328  1.00 23.03  ? 26  VAL F O    1 
ATOM   12047 C CB   . VAL F 3 28  ? 39.089  101.639 43.007  1.00 19.45  ? 26  VAL F CB   1 
ATOM   12048 C CG1  . VAL F 3 28  ? 40.507  102.129 43.092  1.00 19.95  ? 26  VAL F CG1  1 
ATOM   12049 C CG2  . VAL F 3 28  ? 38.472  101.467 44.371  1.00 25.00  ? 26  VAL F CG2  1 
ATOM   12050 N N    . LYS F 3 29  ? 36.063  103.087 42.859  1.00 20.24  ? 27  LYS F N    1 
ATOM   12051 C CA   . LYS F 3 29  ? 34.624  102.931 42.960  1.00 23.27  ? 27  LYS F CA   1 
ATOM   12052 C C    . LYS F 3 29  ? 33.969  103.511 41.738  1.00 25.10  ? 27  LYS F C    1 
ATOM   12053 O O    . LYS F 3 29  ? 32.806  103.296 41.469  1.00 25.77  ? 27  LYS F O    1 
ATOM   12054 C CB   . LYS F 3 29  ? 34.080  103.578 44.229  1.00 18.37  ? 27  LYS F CB   1 
ATOM   12055 C CG   . LYS F 3 29  ? 33.795  102.666 45.391  1.00 17.78  ? 27  LYS F CG   1 
ATOM   12056 C CD   . LYS F 3 29  ? 33.410  103.468 46.612  1.00 16.39  ? 27  LYS F CD   1 
ATOM   12057 C CE   . LYS F 3 29  ? 34.104  102.939 47.851  1.00 18.97  ? 27  LYS F CE   1 
ATOM   12058 N NZ   . LYS F 3 29  ? 33.953  103.841 49.022  1.00 18.03  ? 27  LYS F NZ   1 
ATOM   12059 N N    . ALA F 3 30  ? 34.731  104.220 40.947  1.00 20.48  ? 28  ALA F N    1 
ATOM   12060 C CA   . ALA F 3 30  ? 34.205  104.784 39.745  1.00 18.59  ? 28  ALA F CA   1 
ATOM   12061 C C    . ALA F 3 30  ? 34.471  103.899 38.590  1.00 23.06  ? 28  ALA F C    1 
ATOM   12062 O O    . ALA F 3 30  ? 33.834  104.040 37.579  1.00 26.19  ? 28  ALA F O    1 
ATOM   12063 C CB   . ALA F 3 30  ? 34.854  106.097 39.507  1.00 21.37  ? 28  ALA F CB   1 
ATOM   12064 N N    . LYS F 3 31  ? 35.397  102.961 38.728  1.00 21.96  ? 29  LYS F N    1 
ATOM   12065 C CA   . LYS F 3 31  ? 35.771  102.067 37.650  1.00 19.30  ? 29  LYS F CA   1 
ATOM   12066 C C    . LYS F 3 31  ? 34.909  100.882 37.691  1.00 19.16  ? 29  LYS F C    1 
ATOM   12067 O O    . LYS F 3 31  ? 34.797  100.171 36.723  1.00 21.27  ? 29  LYS F O    1 
ATOM   12068 C CB   . LYS F 3 31  ? 37.201  101.654 37.817  1.00 17.31  ? 29  LYS F CB   1 
ATOM   12069 C CG   . LYS F 3 31  ? 38.215  102.730 37.486  1.00 19.34  ? 29  LYS F CG   1 
ATOM   12070 C CD   . LYS F 3 31  ? 39.602  102.326 37.947  1.00 22.38  ? 29  LYS F CD   1 
ATOM   12071 C CE   . LYS F 3 31  ? 40.443  103.531 38.314  1.00 24.32  ? 29  LYS F CE   1 
ATOM   12072 N NZ   . LYS F 3 31  ? 41.211  104.048 37.152  1.00 28.14  ? 29  LYS F NZ   1 
ATOM   12073 N N    . ILE F 3 32  ? 34.282  100.651 38.821  1.00 19.75  ? 30  ILE F N    1 
ATOM   12074 C CA   . ILE F 3 32  ? 33.354  99.555  38.976  1.00 22.49  ? 30  ILE F CA   1 
ATOM   12075 C C    . ILE F 3 32  ? 31.943  100.009 38.568  1.00 29.89  ? 30  ILE F C    1 
ATOM   12076 O O    . ILE F 3 32  ? 31.024  99.220  38.522  1.00 24.85  ? 30  ILE F O    1 
ATOM   12077 C CB   . ILE F 3 32  ? 33.364  99.084  40.443  1.00 20.77  ? 30  ILE F CB   1 
ATOM   12078 C CG1  . ILE F 3 32  ? 34.771  98.905  40.964  1.00 23.43  ? 30  ILE F CG1  1 
ATOM   12079 C CG2  . ILE F 3 32  ? 32.673  97.746  40.644  1.00 21.71  ? 30  ILE F CG2  1 
ATOM   12080 C CD1  . ILE F 3 32  ? 34.813  98.449  42.401  1.00 17.13  ? 30  ILE F CD1  1 
ATOM   12081 N N    . GLN F 3 33  ? 31.753  101.284 38.241  1.00 25.82  ? 31  GLN F N    1 
ATOM   12082 C CA   . GLN F 3 33  ? 30.464  101.781 37.805  1.00 17.10  ? 31  GLN F CA   1 
ATOM   12083 C C    . GLN F 3 33  ? 30.508  101.730 36.355  1.00 20.96  ? 31  GLN F C    1 
ATOM   12084 O O    . GLN F 3 33  ? 29.515  101.626 35.666  1.00 24.71  ? 31  GLN F O    1 
ATOM   12085 C CB   . GLN F 3 33  ? 30.289  103.228 38.157  1.00 17.76  ? 31  GLN F CB   1 
ATOM   12086 C CG   . GLN F 3 33  ? 28.907  103.770 37.825  1.00 14.80  ? 31  GLN F CG   1 
ATOM   12087 C CD   . GLN F 3 33  ? 28.731  105.230 38.132  1.00 11.83  ? 31  GLN F CD   1 
ATOM   12088 O OE1  . GLN F 3 33  ? 29.695  105.965 38.299  1.00 14.46  ? 31  GLN F OE1  1 
ATOM   12089 N NE2  . GLN F 3 33  ? 27.489  105.658 38.215  1.00 11.38  ? 31  GLN F NE2  1 
ATOM   12090 N N    . ASP F 3 34  ? 31.702  101.839 35.844  1.00 23.77  ? 32  ASP F N    1 
ATOM   12091 C CA   . ASP F 3 34  ? 31.860  101.848 34.422  1.00 24.89  ? 32  ASP F CA   1 
ATOM   12092 C C    . ASP F 3 34  ? 31.736  100.432 33.964  1.00 31.24  ? 32  ASP F C    1 
ATOM   12093 O O    . ASP F 3 34  ? 30.904  100.115 33.136  1.00 31.20  ? 32  ASP F O    1 
ATOM   12094 C CB   . ASP F 3 34  ? 33.238  102.412 34.078  1.00 22.45  ? 32  ASP F CB   1 
ATOM   12095 C CG   . ASP F 3 34  ? 33.384  103.857 34.429  1.00 28.95  ? 32  ASP F CG   1 
ATOM   12096 O OD1  . ASP F 3 34  ? 32.360  104.546 34.561  1.00 37.48  ? 32  ASP F OD1  1 
ATOM   12097 O OD2  . ASP F 3 34  ? 34.535  104.309 34.567  1.00 24.63  ? 32  ASP F OD2  1 
ATOM   12098 N N    . LYS F 3 35  ? 32.522  99.554  34.550  1.00 27.20  ? 33  LYS F N    1 
ATOM   12099 C CA   . LYS F 3 35  ? 32.564  98.178  34.132  1.00 20.34  ? 33  LYS F CA   1 
ATOM   12100 C C    . LYS F 3 35  ? 31.479  97.281  34.592  1.00 16.75  ? 33  LYS F C    1 
ATOM   12101 O O    . LYS F 3 35  ? 31.355  96.185  34.121  1.00 17.95  ? 33  LYS F O    1 
ATOM   12102 C CB   . LYS F 3 35  ? 33.947  97.634  34.494  1.00 16.12  ? 33  LYS F CB   1 
ATOM   12103 C CG   . LYS F 3 35  ? 34.107  96.861  35.777  1.00 24.84  ? 33  LYS F CG   1 
ATOM   12104 C CD   . LYS F 3 35  ? 35.282  95.915  35.617  1.00 25.10  ? 33  LYS F CD   1 
ATOM   12105 C CE   . LYS F 3 35  ? 34.887  94.657  34.870  1.00 14.82  ? 33  LYS F CE   1 
ATOM   12106 N NZ   . LYS F 3 35  ? 35.894  93.581  35.064  1.00 18.27  ? 33  LYS F NZ   1 
ATOM   12107 N N    . GLU F 3 36  ? 30.659  97.725  35.496  1.00 17.60  ? 34  GLU F N    1 
ATOM   12108 C CA   . GLU F 3 36  ? 29.663  96.844  36.046  1.00 23.88  ? 34  GLU F CA   1 
ATOM   12109 C C    . GLU F 3 36  ? 28.318  97.521  36.253  1.00 18.39  ? 34  GLU F C    1 
ATOM   12110 O O    . GLU F 3 36  ? 27.305  96.856  36.343  1.00 12.61  ? 34  GLU F O    1 
ATOM   12111 C CB   . GLU F 3 36  ? 30.192  96.196  37.329  1.00 22.02  ? 34  GLU F CB   1 
ATOM   12112 C CG   . GLU F 3 36  ? 31.097  94.986  37.195  1.00 15.42  ? 34  GLU F CG   1 
ATOM   12113 C CD   . GLU F 3 36  ? 30.412  93.815  36.545  1.00 18.71  ? 34  GLU F CD   1 
ATOM   12114 O OE1  . GLU F 3 36  ? 29.298  93.466  36.971  1.00 20.84  ? 34  GLU F OE1  1 
ATOM   12115 O OE2  . GLU F 3 36  ? 30.991  93.242  35.608  1.00 25.48  ? 34  GLU F OE2  1 
ATOM   12116 N N    . GLY F 3 37  ? 28.317  98.837  36.359  1.00 14.98  ? 35  GLY F N    1 
ATOM   12117 C CA   . GLY F 3 37  ? 27.091  99.583  36.489  1.00 14.66  ? 35  GLY F CA   1 
ATOM   12118 C C    . GLY F 3 37  ? 26.704  100.013 37.853  1.00 21.49  ? 35  GLY F C    1 
ATOM   12119 O O    . GLY F 3 37  ? 25.784  100.793 38.001  1.00 25.65  ? 35  GLY F O    1 
ATOM   12120 N N    . ILE F 3 38  ? 27.411  99.564  38.867  1.00 24.85  ? 36  ILE F N    1 
ATOM   12121 C CA   . ILE F 3 38  ? 27.033  99.839  40.222  1.00 18.77  ? 36  ILE F CA   1 
ATOM   12122 C C    . ILE F 3 38  ? 27.226  101.274 40.550  1.00 15.35  ? 36  ILE F C    1 
ATOM   12123 O O    . ILE F 3 38  ? 28.288  101.796 40.392  1.00 15.05  ? 36  ILE F O    1 
ATOM   12124 C CB   . ILE F 3 38  ? 27.787  98.925  41.176  1.00 16.01  ? 36  ILE F CB   1 
ATOM   12125 C CG1  . ILE F 3 38  ? 27.872  97.529  40.598  1.00 16.39  ? 36  ILE F CG1  1 
ATOM   12126 C CG2  . ILE F 3 38  ? 27.077  98.894  42.493  1.00 16.51  ? 36  ILE F CG2  1 
ATOM   12127 C CD1  . ILE F 3 38  ? 29.121  96.801  40.989  1.00 21.10  ? 36  ILE F CD1  1 
ATOM   12128 N N    . PRO F 3 39  ? 26.131  101.942 41.025  1.00 14.83  ? 37  PRO F N    1 
ATOM   12129 C CA   . PRO F 3 39  ? 26.407  103.309 41.401  1.00 17.43  ? 37  PRO F CA   1 
ATOM   12130 C C    . PRO F 3 39  ? 27.495  103.339 42.400  1.00 18.47  ? 37  PRO F C    1 
ATOM   12131 O O    . PRO F 3 39  ? 27.515  102.505 43.268  1.00 21.68  ? 37  PRO F O    1 
ATOM   12132 C CB   . PRO F 3 39  ? 25.108  103.725 42.047  1.00 21.76  ? 37  PRO F CB   1 
ATOM   12133 C CG   . PRO F 3 39  ? 24.084  103.034 41.248  1.00 21.43  ? 37  PRO F CG   1 
ATOM   12134 C CD   . PRO F 3 39  ? 24.667  101.678 41.179  1.00 16.16  ? 37  PRO F CD   1 
ATOM   12135 N N    . PRO F 3 40  ? 28.380  104.374 42.350  1.00 16.10  ? 38  PRO F N    1 
ATOM   12136 C CA   . PRO F 3 40  ? 29.501  104.269 43.255  1.00 15.93  ? 38  PRO F CA   1 
ATOM   12137 C C    . PRO F 3 40  ? 29.200  104.518 44.715  1.00 17.70  ? 38  PRO F C    1 
ATOM   12138 O O    . PRO F 3 40  ? 30.132  104.628 45.493  1.00 19.35  ? 38  PRO F O    1 
ATOM   12139 C CB   . PRO F 3 40  ? 30.422  105.316 42.695  1.00 15.79  ? 38  PRO F CB   1 
ATOM   12140 C CG   . PRO F 3 40  ? 29.543  106.419 42.348  1.00 18.32  ? 38  PRO F CG   1 
ATOM   12141 C CD   . PRO F 3 40  ? 28.374  105.738 41.743  1.00 18.01  ? 38  PRO F CD   1 
ATOM   12142 N N    . ASP F 3 41  ? 27.929  104.581 45.100  1.00 16.47  ? 39  ASP F N    1 
ATOM   12143 C CA   . ASP F 3 41  ? 27.542  104.895 46.452  1.00 14.19  ? 39  ASP F CA   1 
ATOM   12144 C C    . ASP F 3 41  ? 27.048  103.648 47.058  1.00 16.94  ? 39  ASP F C    1 
ATOM   12145 O O    . ASP F 3 41  ? 27.123  103.470 48.256  1.00 29.77  ? 39  ASP F O    1 
ATOM   12146 C CB   . ASP F 3 41  ? 26.443  105.925 46.444  1.00 14.08  ? 39  ASP F CB   1 
ATOM   12147 C CG   . ASP F 3 41  ? 26.789  107.142 45.640  1.00 23.58  ? 39  ASP F CG   1 
ATOM   12148 O OD1  . ASP F 3 41  ? 27.657  107.921 46.074  1.00 25.53  ? 39  ASP F OD1  1 
ATOM   12149 O OD2  . ASP F 3 41  ? 26.181  107.333 44.573  1.00 23.07  ? 39  ASP F OD2  1 
ATOM   12150 N N    . GLN F 3 42  ? 26.551  102.746 46.242  1.00 15.64  ? 40  GLN F N    1 
ATOM   12151 C CA   . GLN F 3 42  ? 26.103  101.464 46.712  1.00 15.27  ? 40  GLN F CA   1 
ATOM   12152 C C    . GLN F 3 42  ? 27.304  100.676 47.045  1.00 16.75  ? 40  GLN F C    1 
ATOM   12153 O O    . GLN F 3 42  ? 27.274  99.825  47.892  1.00 18.05  ? 40  GLN F O    1 
ATOM   12154 C CB   . GLN F 3 42  ? 25.371  100.776 45.590  1.00 14.33  ? 40  GLN F CB   1 
ATOM   12155 C CG   . GLN F 3 42  ? 23.886  100.660 45.759  1.00 18.89  ? 40  GLN F CG   1 
ATOM   12156 C CD   . GLN F 3 42  ? 23.333  99.472  45.026  1.00 17.91  ? 40  GLN F CD   1 
ATOM   12157 O OE1  . GLN F 3 42  ? 23.566  99.298  43.841  1.00 16.94  ? 40  GLN F OE1  1 
ATOM   12158 N NE2  . GLN F 3 42  ? 22.600  98.643  45.732  1.00 22.03  ? 40  GLN F NE2  1 
ATOM   12159 N N    . GLN F 3 43  ? 28.392  100.955 46.376  1.00 17.13  ? 41  GLN F N    1 
ATOM   12160 C CA   . GLN F 3 43  ? 29.625  100.237 46.562  1.00 16.20  ? 41  GLN F CA   1 
ATOM   12161 C C    . GLN F 3 43  ? 30.314  100.544 47.829  1.00 14.66  ? 41  GLN F C    1 
ATOM   12162 O O    . GLN F 3 43  ? 30.561  101.681 48.145  1.00 19.31  ? 41  GLN F O    1 
ATOM   12163 C CB   . GLN F 3 43  ? 30.560  100.559 45.427  1.00 15.09  ? 41  GLN F CB   1 
ATOM   12164 C CG   . GLN F 3 43  ? 29.988  100.443 44.046  1.00 14.20  ? 41  GLN F CG   1 
ATOM   12165 C CD   . GLN F 3 43  ? 31.035  100.728 43.017  1.00 21.82  ? 41  GLN F CD   1 
ATOM   12166 O OE1  . GLN F 3 43  ? 32.204  100.566 43.285  1.00 26.33  ? 41  GLN F OE1  1 
ATOM   12167 N NE2  . GLN F 3 43  ? 30.630  101.163 41.846  1.00 18.98  ? 41  GLN F NE2  1 
ATOM   12168 N N    . ARG F 3 44  ? 30.639  99.510  48.573  1.00 14.09  ? 42  ARG F N    1 
ATOM   12169 C CA   . ARG F 3 44  ? 31.298  99.656  49.828  1.00 15.25  ? 42  ARG F CA   1 
ATOM   12170 C C    . ARG F 3 44  ? 32.395  98.725  49.636  1.00 14.41  ? 42  ARG F C    1 
ATOM   12171 O O    . ARG F 3 44  ? 32.173  97.603  49.270  1.00 12.09  ? 42  ARG F O    1 
ATOM   12172 C CB   . ARG F 3 44  ? 30.439  99.114  50.941  1.00 16.82  ? 42  ARG F CB   1 
ATOM   12173 C CG   . ARG F 3 44  ? 29.225  99.940  51.298  1.00 26.88  ? 42  ARG F CG   1 
ATOM   12174 C CD   . ARG F 3 44  ? 28.075  99.027  51.663  1.00 30.48  ? 42  ARG F CD   1 
ATOM   12175 N NE   . ARG F 3 44  ? 28.455  98.067  52.687  1.00 28.40  ? 42  ARG F NE   1 
ATOM   12176 C CZ   . ARG F 3 44  ? 27.969  98.066  53.920  1.00 32.74  ? 42  ARG F CZ   1 
ATOM   12177 N NH1  . ARG F 3 44  ? 27.081  98.980  54.283  1.00 27.89  ? 42  ARG F NH1  1 
ATOM   12178 N NH2  . ARG F 3 44  ? 28.374  97.157  54.791  1.00 31.86  ? 42  ARG F NH2  1 
ATOM   12179 N N    . LEU F 3 45  ? 33.601  99.179  49.894  1.00 15.43  ? 43  LEU F N    1 
ATOM   12180 C CA   . LEU F 3 45  ? 34.742  98.362  49.632  1.00 13.36  ? 43  LEU F CA   1 
ATOM   12181 C C    . LEU F 3 45  ? 35.438  98.055  50.891  1.00 13.50  ? 43  LEU F C    1 
ATOM   12182 O O    . LEU F 3 45  ? 35.587  98.911  51.701  1.00 14.50  ? 43  LEU F O    1 
ATOM   12183 C CB   . LEU F 3 45  ? 35.614  99.010  48.573  1.00 15.88  ? 43  LEU F CB   1 
ATOM   12184 C CG   . LEU F 3 45  ? 35.495  98.422  47.178  1.00 15.05  ? 43  LEU F CG   1 
ATOM   12185 C CD1  . LEU F 3 45  ? 35.514  99.522  46.148  1.00 13.53  ? 43  LEU F CD1  1 
ATOM   12186 C CD2  . LEU F 3 45  ? 36.637  97.470  46.936  1.00 15.64  ? 43  LEU F CD2  1 
ATOM   12187 N N    . ILE F 3 46  ? 35.810  96.801  51.079  1.00 13.47  ? 44  ILE F N    1 
ATOM   12188 C CA   . ILE F 3 46  ? 36.373  96.347  52.322  1.00 16.89  ? 44  ILE F CA   1 
ATOM   12189 C C    . ILE F 3 46  ? 37.617  95.561  52.112  1.00 18.93  ? 44  ILE F C    1 
ATOM   12190 O O    . ILE F 3 46  ? 37.599  94.539  51.482  1.00 24.69  ? 44  ILE F O    1 
ATOM   12191 C CB   . ILE F 3 46  ? 35.423  95.377  53.045  1.00 12.47  ? 44  ILE F CB   1 
ATOM   12192 C CG1  . ILE F 3 46  ? 33.987  95.511  52.550  1.00 18.96  ? 44  ILE F CG1  1 
ATOM   12193 C CG2  . ILE F 3 46  ? 35.462  95.583  54.541  1.00 18.88  ? 44  ILE F CG2  1 
ATOM   12194 C CD1  . ILE F 3 46  ? 32.987  95.745  53.654  1.00 21.72  ? 44  ILE F CD1  1 
ATOM   12195 N N    . PHE F 3 47  ? 38.713  96.036  52.636  1.00 17.06  ? 45  PHE F N    1 
ATOM   12196 C CA   . PHE F 3 47  ? 39.937  95.325  52.547  1.00 20.28  ? 45  PHE F CA   1 
ATOM   12197 C C    . PHE F 3 47  ? 40.380  95.454  53.956  1.00 28.24  ? 45  PHE F C    1 
ATOM   12198 O O    . PHE F 3 47  ? 40.127  96.482  54.557  1.00 32.91  ? 45  PHE F O    1 
ATOM   12199 C CB   . PHE F 3 47  ? 40.896  96.048  51.638  1.00 22.96  ? 45  PHE F CB   1 
ATOM   12200 C CG   . PHE F 3 47  ? 42.243  95.400  51.523  1.00 30.42  ? 45  PHE F CG   1 
ATOM   12201 C CD1  . PHE F 3 47  ? 42.377  94.144  50.964  1.00 29.17  ? 45  PHE F CD1  1 
ATOM   12202 C CD2  . PHE F 3 47  ? 43.372  96.048  51.972  1.00 29.70  ? 45  PHE F CD2  1 
ATOM   12203 C CE1  . PHE F 3 47  ? 43.609  93.548  50.846  1.00 23.67  ? 45  PHE F CE1  1 
ATOM   12204 C CE2  . PHE F 3 47  ? 44.613  95.458  51.860  1.00 32.12  ? 45  PHE F CE2  1 
ATOM   12205 C CZ   . PHE F 3 47  ? 44.730  94.206  51.296  1.00 31.47  ? 45  PHE F CZ   1 
ATOM   12206 N N    . ALA F 3 48  ? 41.004  94.427  54.507  1.00 26.28  ? 46  ALA F N    1 
ATOM   12207 C CA   . ALA F 3 48  ? 41.497  94.422  55.876  1.00 22.35  ? 46  ALA F CA   1 
ATOM   12208 C C    . ALA F 3 48  ? 40.489  94.395  57.000  1.00 24.17  ? 46  ALA F C    1 
ATOM   12209 O O    . ALA F 3 48  ? 40.875  94.395  58.156  1.00 30.50  ? 46  ALA F O    1 
ATOM   12210 C CB   . ALA F 3 48  ? 42.548  95.472  56.090  1.00 22.45  ? 46  ALA F CB   1 
ATOM   12211 N N    . GLY F 3 49  ? 39.208  94.308  56.689  1.00 22.38  ? 47  GLY F N    1 
ATOM   12212 C CA   . GLY F 3 49  ? 38.186  94.194  57.700  1.00 18.80  ? 47  GLY F CA   1 
ATOM   12213 C C    . GLY F 3 49  ? 37.769  95.580  57.932  1.00 22.34  ? 47  GLY F C    1 
ATOM   12214 O O    . GLY F 3 49  ? 37.035  95.859  58.850  1.00 27.11  ? 47  GLY F O    1 
ATOM   12215 N N    . LYS F 3 50  ? 38.272  96.473  57.105  1.00 26.71  ? 48  LYS F N    1 
ATOM   12216 C CA   . LYS F 3 50  ? 37.980  97.883  57.259  1.00 30.92  ? 48  LYS F CA   1 
ATOM   12217 C C    . LYS F 3 50  ? 37.303  98.379  56.020  1.00 24.94  ? 48  LYS F C    1 
ATOM   12218 O O    . LYS F 3 50  ? 37.786  98.168  54.938  1.00 21.55  ? 48  LYS F O    1 
ATOM   12219 C CB   . LYS F 3 50  ? 39.277  98.677  57.453  1.00 25.95  ? 48  LYS F CB   1 
ATOM   12220 C CG   . LYS F 3 50  ? 40.225  98.139  58.500  1.00 24.51  ? 48  LYS F CG   1 
ATOM   12221 C CD   . LYS F 3 50  ? 41.455  99.015  58.596  1.00 21.00  ? 48  LYS F CD   1 
ATOM   12222 C CE   . LYS F 3 50  ? 42.701  98.184  58.819  1.00 24.67  ? 48  LYS F CE   1 
ATOM   12223 N NZ   . LYS F 3 50  ? 43.723  98.422  57.762  1.00 31.35  ? 48  LYS F NZ   1 
ATOM   12224 N N    . GLN F 3 51  ? 36.183  99.060  56.165  1.00 21.87  ? 49  GLN F N    1 
ATOM   12225 C CA   . GLN F 3 51  ? 35.563  99.637  55.012  1.00 19.70  ? 49  GLN F CA   1 
ATOM   12226 C C    . GLN F 3 51  ? 36.447  100.741 54.563  1.00 21.88  ? 49  GLN F C    1 
ATOM   12227 O O    . GLN F 3 51  ? 36.925  101.514 55.369  1.00 32.21  ? 49  GLN F O    1 
ATOM   12228 C CB   . GLN F 3 51  ? 34.166  100.131 55.302  1.00 21.69  ? 49  GLN F CB   1 
ATOM   12229 C CG   . GLN F 3 51  ? 33.215  99.041  55.750  1.00 26.21  ? 49  GLN F CG   1 
ATOM   12230 C CD   . GLN F 3 51  ? 31.818  99.240  55.228  1.00 21.88  ? 49  GLN F CD   1 
ATOM   12231 O OE1  . GLN F 3 51  ? 31.573  99.078  54.047  1.00 22.54  ? 49  GLN F OE1  1 
ATOM   12232 N NE2  . GLN F 3 51  ? 30.895  99.596  56.109  1.00 21.89  ? 49  GLN F NE2  1 
ATOM   12233 N N    . LEU F 3 52  ? 36.660  100.855 53.272  1.00 19.39  ? 50  LEU F N    1 
ATOM   12234 C CA   . LEU F 3 52  ? 37.608  101.807 52.787  1.00 21.81  ? 50  LEU F CA   1 
ATOM   12235 C C    . LEU F 3 52  ? 37.027  103.175 52.596  1.00 21.35  ? 50  LEU F C    1 
ATOM   12236 O O    . LEU F 3 52  ? 35.836  103.318 52.391  1.00 15.21  ? 50  LEU F O    1 
ATOM   12237 C CB   . LEU F 3 52  ? 38.286  101.250 51.545  1.00 20.77  ? 50  LEU F CB   1 
ATOM   12238 C CG   . LEU F 3 52  ? 38.832  99.832  51.548  1.00 21.75  ? 50  LEU F CG   1 
ATOM   12239 C CD1  . LEU F 3 52  ? 39.353  99.451  50.180  1.00 15.50  ? 50  LEU F CD1  1 
ATOM   12240 C CD2  . LEU F 3 52  ? 39.895  99.653  52.607  1.00 26.14  ? 50  LEU F CD2  1 
ATOM   12241 N N    . GLU F 3 53  ? 37.880  104.195 52.661  1.00 20.97  ? 51  GLU F N    1 
ATOM   12242 C CA   . GLU F 3 53  ? 37.426  105.565 52.575  1.00 16.95  ? 51  GLU F CA   1 
ATOM   12243 C C    . GLU F 3 53  ? 37.529  106.089 51.225  1.00 20.44  ? 51  GLU F C    1 
ATOM   12244 O O    . GLU F 3 53  ? 38.431  105.757 50.521  1.00 26.64  ? 51  GLU F O    1 
ATOM   12245 C CB   . GLU F 3 53  ? 38.232  106.430 53.492  1.00 22.42  ? 51  GLU F CB   1 
ATOM   12246 C CG   . GLU F 3 53  ? 37.572  106.717 54.825  1.00 27.26  ? 51  GLU F CG   1 
ATOM   12247 C CD   . GLU F 3 53  ? 37.883  108.105 55.335  1.00 29.92  ? 51  GLU F CD   1 
ATOM   12248 O OE1  . GLU F 3 53  ? 37.674  109.074 54.582  1.00 40.74  ? 51  GLU F OE1  1 
ATOM   12249 O OE2  . GLU F 3 53  ? 38.340  108.227 56.485  1.00 24.73  ? 51  GLU F OE2  1 
ATOM   12250 N N    . ASP F 3 54  ? 36.634  106.975 50.872  1.00 20.44  ? 52  ASP F N    1 
ATOM   12251 C CA   . ASP F 3 54  ? 36.553  107.467 49.526  1.00 25.28  ? 52  ASP F CA   1 
ATOM   12252 C C    . ASP F 3 54  ? 37.582  108.500 49.187  1.00 27.63  ? 52  ASP F C    1 
ATOM   12253 O O    . ASP F 3 54  ? 37.858  108.738 48.032  1.00 27.86  ? 52  ASP F O    1 
ATOM   12254 C CB   . ASP F 3 54  ? 35.155  108.032 49.344  1.00 24.33  ? 52  ASP F CB   1 
ATOM   12255 C CG   . ASP F 3 54  ? 34.317  107.217 48.453  1.00 24.22  ? 52  ASP F CG   1 
ATOM   12256 O OD1  . ASP F 3 54  ? 34.821  106.202 47.988  1.00 35.57  ? 52  ASP F OD1  1 
ATOM   12257 O OD2  . ASP F 3 54  ? 33.164  107.601 48.204  1.00 18.23  ? 52  ASP F OD2  1 
ATOM   12258 N N    . GLY F 3 55  ? 38.149  109.143 50.187  1.00 28.01  ? 53  GLY F N    1 
ATOM   12259 C CA   . GLY F 3 55  ? 39.188  110.125 49.959  1.00 28.46  ? 53  GLY F CA   1 
ATOM   12260 C C    . GLY F 3 55  ? 40.573  109.571 50.132  1.00 22.27  ? 53  GLY F C    1 
ATOM   12261 O O    . GLY F 3 55  ? 41.548  110.298 50.032  1.00 20.64  ? 53  GLY F O    1 
ATOM   12262 N N    . ARG F 3 56  ? 40.666  108.279 50.371  1.00 20.15  ? 54  ARG F N    1 
ATOM   12263 C CA   . ARG F 3 56  ? 41.944  107.662 50.585  1.00 22.27  ? 54  ARG F CA   1 
ATOM   12264 C C    . ARG F 3 56  ? 42.385  106.848 49.425  1.00 24.70  ? 54  ARG F C    1 
ATOM   12265 O O    . ARG F 3 56  ? 41.587  106.542 48.575  1.00 19.91  ? 54  ARG F O    1 
ATOM   12266 C CB   . ARG F 3 56  ? 42.015  106.910 51.896  1.00 22.03  ? 54  ARG F CB   1 
ATOM   12267 C CG   . ARG F 3 56  ? 42.226  107.804 53.100  1.00 31.58  ? 54  ARG F CG   1 
ATOM   12268 C CD   . ARG F 3 56  ? 41.784  107.144 54.396  1.00 25.40  ? 54  ARG F CD   1 
ATOM   12269 N NE   . ARG F 3 56  ? 42.514  105.922 54.700  1.00 24.18  ? 54  ARG F NE   1 
ATOM   12270 C CZ   . ARG F 3 56  ? 43.610  105.873 55.447  1.00 35.19  ? 54  ARG F CZ   1 
ATOM   12271 N NH1  . ARG F 3 56  ? 44.112  106.981 55.961  1.00 44.34  ? 54  ARG F NH1  1 
ATOM   12272 N NH2  . ARG F 3 56  ? 44.210  104.716 55.679  1.00 28.19  ? 54  ARG F NH2  1 
ATOM   12273 N N    . THR F 3 57  ? 43.676  106.569 49.349  1.00 27.22  ? 55  THR F N    1 
ATOM   12274 C CA   . THR F 3 57  ? 44.254  105.895 48.216  1.00 23.98  ? 55  THR F CA   1 
ATOM   12275 C C    . THR F 3 57  ? 44.567  104.466 48.444  1.00 23.94  ? 55  THR F C    1 
ATOM   12276 O O    . THR F 3 57  ? 44.563  103.999 49.556  1.00 27.23  ? 55  THR F O    1 
ATOM   12277 C CB   . THR F 3 57  ? 45.559  106.569 47.826  1.00 24.83  ? 55  THR F CB   1 
ATOM   12278 O OG1  . THR F 3 57  ? 46.653  105.919 48.474  1.00 31.85  ? 55  THR F OG1  1 
ATOM   12279 C CG2  . THR F 3 57  ? 45.536  108.029 48.204  1.00 27.14  ? 55  THR F CG2  1 
ATOM   12280 N N    . LEU F 3 58  ? 44.833  103.756 47.380  1.00 17.06  ? 56  LEU F N    1 
ATOM   12281 C CA   . LEU F 3 58  ? 45.117  102.366 47.486  1.00 17.26  ? 56  LEU F CA   1 
ATOM   12282 C C    . LEU F 3 58  ? 46.358  102.063 48.308  1.00 26.78  ? 56  LEU F C    1 
ATOM   12283 O O    . LEU F 3 58  ? 46.459  101.001 48.862  1.00 33.53  ? 56  LEU F O    1 
ATOM   12284 C CB   . LEU F 3 58  ? 45.146  101.759 46.106  1.00 17.86  ? 56  LEU F CB   1 
ATOM   12285 C CG   . LEU F 3 58  ? 43.863  101.628 45.303  1.00 18.44  ? 56  LEU F CG   1 
ATOM   12286 C CD1  . LEU F 3 58  ? 44.191  101.797 43.843  1.00 22.33  ? 56  LEU F CD1  1 
ATOM   12287 C CD2  . LEU F 3 58  ? 43.215  100.279 45.522  1.00 16.62  ? 56  LEU F CD2  1 
ATOM   12288 N N    . SER F 3 59  ? 47.331  102.964 48.362  1.00 32.40  ? 57  SER F N    1 
ATOM   12289 C CA   . SER F 3 59  ? 48.540  102.798 49.205  1.00 31.43  ? 57  SER F CA   1 
ATOM   12290 C C    . SER F 3 59  ? 48.427  103.345 50.600  1.00 20.34  ? 57  SER F C    1 
ATOM   12291 O O    . SER F 3 59  ? 49.360  103.228 51.367  1.00 19.14  ? 57  SER F O    1 
ATOM   12292 C CB   . SER F 3 59  ? 49.756  103.387 48.530  1.00 25.62  ? 57  SER F CB   1 
ATOM   12293 O OG   . SER F 3 59  ? 50.362  102.443 47.669  1.00 21.64  ? 57  SER F OG   1 
ATOM   12294 N N    . ASP F 3 60  ? 47.311  103.974 50.923  1.00 20.04  ? 58  ASP F N    1 
ATOM   12295 C CA   . ASP F 3 60  ? 47.058  104.424 52.271  1.00 28.36  ? 58  ASP F CA   1 
ATOM   12296 C C    . ASP F 3 60  ? 46.459  103.270 53.009  1.00 30.75  ? 58  ASP F C    1 
ATOM   12297 O O    . ASP F 3 60  ? 46.314  103.317 54.223  1.00 22.79  ? 58  ASP F O    1 
ATOM   12298 C CB   . ASP F 3 60  ? 46.060  105.554 52.263  1.00 25.96  ? 58  ASP F CB   1 
ATOM   12299 C CG   . ASP F 3 60  ? 46.654  106.860 51.800  1.00 34.12  ? 58  ASP F CG   1 
ATOM   12300 O OD1  . ASP F 3 60  ? 47.841  106.875 51.425  1.00 37.42  ? 58  ASP F OD1  1 
ATOM   12301 O OD2  . ASP F 3 60  ? 45.930  107.876 51.814  1.00 31.34  ? 58  ASP F OD2  1 
ATOM   12302 N N    . TYR F 3 61  ? 46.085  102.234 52.270  1.00 24.43  ? 59  TYR F N    1 
ATOM   12303 C CA   . TYR F 3 61  ? 45.528  101.037 52.865  1.00 28.01  ? 59  TYR F CA   1 
ATOM   12304 C C    . TYR F 3 61  ? 46.396  99.855  52.616  1.00 24.99  ? 59  TYR F C    1 
ATOM   12305 O O    . TYR F 3 61  ? 46.074  98.771  53.050  1.00 30.03  ? 59  TYR F O    1 
ATOM   12306 C CB   . TYR F 3 61  ? 44.144  100.773 52.316  1.00 27.10  ? 59  TYR F CB   1 
ATOM   12307 C CG   . TYR F 3 61  ? 43.073  101.646 52.887  1.00 25.45  ? 59  TYR F CG   1 
ATOM   12308 C CD1  . TYR F 3 61  ? 42.756  101.581 54.229  1.00 23.12  ? 59  TYR F CD1  1 
ATOM   12309 C CD2  . TYR F 3 61  ? 42.359  102.514 52.085  1.00 23.75  ? 59  TYR F CD2  1 
ATOM   12310 C CE1  . TYR F 3 61  ? 41.773  102.371 54.764  1.00 25.70  ? 59  TYR F CE1  1 
ATOM   12311 C CE2  . TYR F 3 61  ? 41.368  103.308 52.612  1.00 25.57  ? 59  TYR F CE2  1 
ATOM   12312 C CZ   . TYR F 3 61  ? 41.083  103.228 53.951  1.00 28.56  ? 59  TYR F CZ   1 
ATOM   12313 O OH   . TYR F 3 61  ? 40.102  104.011 54.497  1.00 27.05  ? 59  TYR F OH   1 
ATOM   12314 N N    . ASN F 3 62  ? 47.506  100.059 51.955  1.00 22.64  ? 60  ASN F N    1 
ATOM   12315 C CA   . ASN F 3 62  ? 48.429  98.988  51.605  1.00 27.51  ? 60  ASN F CA   1 
ATOM   12316 C C    . ASN F 3 62  ? 47.816  97.948  50.711  1.00 30.71  ? 60  ASN F C    1 
ATOM   12317 O O    . ASN F 3 62  ? 48.069  96.764  50.850  1.00 33.67  ? 60  ASN F O    1 
ATOM   12318 C CB   . ASN F 3 62  ? 49.131  98.401  52.823  1.00 31.49  ? 60  ASN F CB   1 
ATOM   12319 C CG   . ASN F 3 62  ? 50.530  97.914  52.520  1.00 35.12  ? 60  ASN F CG   1 
ATOM   12320 O OD1  . ASN F 3 62  ? 51.170  98.374  51.578  1.00 34.92  ? 60  ASN F OD1  1 
ATOM   12321 N ND2  . ASN F 3 62  ? 51.017  96.984  53.329  1.00 36.63  ? 60  ASN F ND2  1 
ATOM   12322 N N    . ILE F 3 63  ? 47.008  98.388  49.771  1.00 30.56  ? 61  ILE F N    1 
ATOM   12323 C CA   . ILE F 3 63  ? 46.462  97.487  48.799  1.00 32.05  ? 61  ILE F CA   1 
ATOM   12324 C C    . ILE F 3 63  ? 47.549  97.579  47.772  1.00 38.39  ? 61  ILE F C    1 
ATOM   12325 O O    . ILE F 3 63  ? 48.041  98.671  47.490  1.00 35.23  ? 61  ILE F O    1 
ATOM   12326 C CB   . ILE F 3 63  ? 45.149  98.013  48.241  1.00 24.57  ? 61  ILE F CB   1 
ATOM   12327 C CG1  . ILE F 3 63  ? 44.164  98.272  49.371  1.00 29.29  ? 61  ILE F CG1  1 
ATOM   12328 C CG2  . ILE F 3 63  ? 44.595  97.049  47.229  1.00 20.76  ? 61  ILE F CG2  1 
ATOM   12329 C CD1  . ILE F 3 63  ? 42.936  99.045  48.960  1.00 24.85  ? 61  ILE F CD1  1 
ATOM   12330 N N    . GLN F 3 64  ? 47.946  96.459  47.206  1.00 33.83  ? 62  GLN F N    1 
ATOM   12331 C CA   . GLN F 3 64  ? 49.057  96.463  46.320  1.00 38.80  ? 62  GLN F CA   1 
ATOM   12332 C C    . GLN F 3 64  ? 48.925  95.229  45.587  1.00 44.75  ? 62  GLN F C    1 
ATOM   12333 O O    . GLN F 3 64  ? 48.012  94.497  45.856  1.00 56.44  ? 62  GLN F O    1 
ATOM   12334 C CB   . GLN F 3 64  ? 50.290  96.267  47.164  1.00 44.33  ? 62  GLN F CB   1 
ATOM   12335 C CG   . GLN F 3 64  ? 51.558  96.879  46.602  1.00 51.14  ? 62  GLN F CG   1 
ATOM   12336 C CD   . GLN F 3 64  ? 52.689  96.855  47.599  1.00 42.35  ? 62  GLN F CD   1 
ATOM   12337 O OE1  . GLN F 3 64  ? 52.469  96.731  48.803  1.00 40.09  ? 62  GLN F OE1  1 
ATOM   12338 N NE2  . GLN F 3 64  ? 53.909  96.979  47.105  1.00 55.04  ? 62  GLN F NE2  1 
ATOM   12339 N N    . LYS F 3 65  ? 49.786  94.973  44.623  1.00 46.22  ? 63  LYS F N    1 
ATOM   12340 C CA   . LYS F 3 65  ? 49.805  93.667  43.969  1.00 44.41  ? 63  LYS F CA   1 
ATOM   12341 C C    . LYS F 3 65  ? 48.534  93.251  43.386  1.00 42.88  ? 63  LYS F C    1 
ATOM   12342 O O    . LYS F 3 65  ? 47.928  93.988  42.666  1.00 55.81  ? 63  LYS F O    1 
ATOM   12343 C CB   . LYS F 3 65  ? 50.260  92.588  44.924  1.00 48.47  ? 63  LYS F CB   1 
ATOM   12344 C CG   . LYS F 3 65  ? 51.727  92.737  45.299  1.00 71.77  ? 63  LYS F CG   1 
ATOM   12345 C CD   . LYS F 3 65  ? 52.625  92.617  44.073  1.00 58.89  ? 63  LYS F CD   1 
ATOM   12346 C CE   . LYS F 3 65  ? 53.553  93.810  43.919  1.00 42.34  ? 63  LYS F CE   1 
ATOM   12347 N NZ   . LYS F 3 65  ? 52.838  95.049  43.515  1.00 36.16  ? 63  LYS F NZ   1 
ATOM   12348 N N    . GLU F 3 66  ? 48.096  92.071  43.711  1.00 32.74  ? 64  GLU F N    1 
ATOM   12349 C CA   . GLU F 3 66  ? 46.914  91.611  43.074  1.00 38.42  ? 64  GLU F CA   1 
ATOM   12350 C C    . GLU F 3 66  ? 46.109  91.285  44.240  1.00 35.15  ? 64  GLU F C    1 
ATOM   12351 O O    . GLU F 3 66  ? 45.842  90.129  44.510  1.00 35.93  ? 64  GLU F O    1 
ATOM   12352 C CB   . GLU F 3 66  ? 47.245  90.384  42.281  1.00 46.00  ? 64  GLU F CB   1 
ATOM   12353 C CG   . GLU F 3 66  ? 48.271  90.625  41.187  1.00 49.93  ? 64  GLU F CG   1 
ATOM   12354 C CD   . GLU F 3 66  ? 48.730  89.350  40.524  1.00 63.45  ? 64  GLU F CD   1 
ATOM   12355 O OE1  . GLU F 3 66  ? 48.557  88.273  41.126  1.00 63.92  ? 64  GLU F OE1  1 
ATOM   12356 O OE2  . GLU F 3 66  ? 49.270  89.425  39.406  1.00 73.53  ? 64  GLU F OE2  1 
ATOM   12357 N N    . SER F 3 67  ? 45.672  92.317  44.922  1.00 26.35  ? 65  SER F N    1 
ATOM   12358 C CA   . SER F 3 67  ? 44.996  92.126  46.143  1.00 20.54  ? 65  SER F CA   1 
ATOM   12359 C C    . SER F 3 67  ? 43.571  92.019  45.974  1.00 19.52  ? 65  SER F C    1 
ATOM   12360 O O    . SER F 3 67  ? 42.979  92.794  45.273  1.00 23.68  ? 65  SER F O    1 
ATOM   12361 C CB   . SER F 3 67  ? 45.304  93.295  47.041  1.00 25.01  ? 65  SER F CB   1 
ATOM   12362 O OG   . SER F 3 67  ? 46.562  93.148  47.663  1.00 32.71  ? 65  SER F OG   1 
ATOM   12363 N N    . THR F 3 68  ? 42.995  91.041  46.639  1.00 17.34  ? 66  THR F N    1 
ATOM   12364 C CA   . THR F 3 68  ? 41.571  90.856  46.558  1.00 19.02  ? 66  THR F CA   1 
ATOM   12365 C C    . THR F 3 68  ? 40.896  91.771  47.546  1.00 18.01  ? 66  THR F C    1 
ATOM   12366 O O    . THR F 3 68  ? 41.252  91.801  48.709  1.00 21.03  ? 66  THR F O    1 
ATOM   12367 C CB   . THR F 3 68  ? 41.149  89.376  46.661  1.00 13.10  ? 66  THR F CB   1 
ATOM   12368 O OG1  . THR F 3 68  ? 41.523  88.681  45.468  1.00 14.59  ? 66  THR F OG1  1 
ATOM   12369 C CG2  . THR F 3 68  ? 39.669  89.253  46.853  1.00 11.53  ? 66  THR F CG2  1 
ATOM   12370 N N    . LEU F 3 69  ? 39.966  92.573  47.066  1.00 14.39  ? 67  LEU F N    1 
ATOM   12371 C CA   . LEU F 3 69  ? 39.253  93.481  47.890  1.00 14.63  ? 67  LEU F CA   1 
ATOM   12372 C C    . LEU F 3 69  ? 37.875  92.970  47.803  1.00 13.46  ? 67  LEU F C    1 
ATOM   12373 O O    . LEU F 3 69  ? 37.621  92.045  47.087  1.00 14.07  ? 67  LEU F O    1 
ATOM   12374 C CB   . LEU F 3 69  ? 39.350  94.881  47.324  1.00 17.27  ? 67  LEU F CB   1 
ATOM   12375 C CG   . LEU F 3 69  ? 40.586  95.451  46.664  1.00 15.55  ? 67  LEU F CG   1 
ATOM   12376 C CD1  . LEU F 3 69  ? 40.297  96.892  46.320  1.00 12.77  ? 67  LEU F CD1  1 
ATOM   12377 C CD2  . LEU F 3 69  ? 41.697  95.392  47.670  1.00 24.24  ? 67  LEU F CD2  1 
ATOM   12378 N N    . HIS F 3 70  ? 36.945  93.561  48.515  1.00 11.59  ? 68  HIS F N    1 
ATOM   12379 C CA   . HIS F 3 70  ? 35.619  93.009  48.586  1.00 12.02  ? 68  HIS F CA   1 
ATOM   12380 C C    . HIS F 3 70  ? 34.510  93.987  48.412  1.00 12.60  ? 68  HIS F C    1 
ATOM   12381 O O    . HIS F 3 70  ? 34.635  95.102  48.819  1.00 12.91  ? 68  HIS F O    1 
ATOM   12382 C CB   . HIS F 3 70  ? 35.474  92.333  49.939  1.00 15.67  ? 68  HIS F CB   1 
ATOM   12383 C CG   . HIS F 3 70  ? 36.182  91.018  50.045  1.00 16.76  ? 68  HIS F CG   1 
ATOM   12384 N ND1  . HIS F 3 70  ? 35.689  89.859  49.492  1.00 20.39  ? 68  HIS F ND1  1 
ATOM   12385 C CD2  . HIS F 3 70  ? 37.348  90.682  50.639  1.00 14.62  ? 68  HIS F CD2  1 
ATOM   12386 C CE1  . HIS F 3 70  ? 36.522  88.867  49.738  1.00 13.59  ? 68  HIS F CE1  1 
ATOM   12387 N NE2  . HIS F 3 70  ? 37.538  89.341  50.431  1.00 11.77  ? 68  HIS F NE2  1 
ATOM   12388 N N    . LEU F 3 71  ? 33.392  93.555  47.856  1.00 9.96   ? 69  LEU F N    1 
ATOM   12389 C CA   . LEU F 3 71  ? 32.310  94.454  47.562  1.00 11.18  ? 69  LEU F CA   1 
ATOM   12390 C C    . LEU F 3 71  ? 30.923  94.046  47.937  1.00 14.06  ? 69  LEU F C    1 
ATOM   12391 O O    . LEU F 3 71  ? 30.468  92.990  47.577  1.00 21.01  ? 69  LEU F O    1 
ATOM   12392 C CB   . LEU F 3 71  ? 32.326  94.793  46.093  1.00 13.13  ? 69  LEU F CB   1 
ATOM   12393 C CG   . LEU F 3 71  ? 31.474  95.928  45.534  1.00 13.18  ? 69  LEU F CG   1 
ATOM   12394 C CD1  . LEU F 3 71  ? 32.252  97.220  45.487  1.00 13.17  ? 69  LEU F CD1  1 
ATOM   12395 C CD2  . LEU F 3 71  ? 31.014  95.545  44.144  1.00 13.67  ? 69  LEU F CD2  1 
ATOM   12396 N N    . VAL F 3 72  ? 30.237  94.920  48.660  1.00 13.05  ? 70  VAL F N    1 
ATOM   12397 C CA   . VAL F 3 72  ? 28.873  94.695  49.022  1.00 15.71  ? 70  VAL F CA   1 
ATOM   12398 C C    . VAL F 3 72  ? 28.101  95.859  48.494  1.00 19.84  ? 70  VAL F C    1 
ATOM   12399 O O    . VAL F 3 72  ? 28.640  96.924  48.303  1.00 15.78  ? 70  VAL F O    1 
ATOM   12400 C CB   . VAL F 3 72  ? 28.666  94.662  50.518  1.00 17.90  ? 70  VAL F CB   1 
ATOM   12401 C CG1  . VAL F 3 72  ? 27.417  93.882  50.871  1.00 18.36  ? 70  VAL F CG1  1 
ATOM   12402 C CG2  . VAL F 3 72  ? 29.894  94.140  51.225  1.00 23.24  ? 70  VAL F CG2  1 
ATOM   12403 N N    . LEU F 3 73  ? 26.810  95.655  48.257  1.00 25.43  ? 71  LEU F N    1 
ATOM   12404 C CA   . LEU F 3 73  ? 25.959  96.682  47.715  1.00 19.14  ? 71  LEU F CA   1 
ATOM   12405 C C    . LEU F 3 73  ? 24.939  97.073  48.711  1.00 19.02  ? 71  LEU F C    1 
ATOM   12406 O O    . LEU F 3 73  ? 24.235  96.252  49.213  1.00 18.10  ? 71  LEU F O    1 
ATOM   12407 C CB   . LEU F 3 73  ? 25.366  96.270  46.382  1.00 16.64  ? 71  LEU F CB   1 
ATOM   12408 C CG   . LEU F 3 73  ? 26.182  96.466  45.113  1.00 16.48  ? 71  LEU F CG   1 
ATOM   12409 C CD1  . LEU F 3 73  ? 27.298  95.462  44.968  1.00 17.85  ? 71  LEU F CD1  1 
ATOM   12410 C CD2  . LEU F 3 73  ? 25.251  96.294  43.948  1.00 18.39  ? 71  LEU F CD2  1 
ATOM   12411 N N    . ARG F 3 74  ? 24.903  98.349  49.020  1.00 19.56  ? 72  ARG F N    1 
ATOM   12412 C CA   . ARG F 3 74  ? 24.006  98.891  49.978  1.00 20.32  ? 72  ARG F CA   1 
ATOM   12413 C C    . ARG F 3 74  ? 22.633  98.809  49.502  1.00 23.84  ? 72  ARG F C    1 
ATOM   12414 O O    . ARG F 3 74  ? 22.259  99.356  48.489  1.00 19.32  ? 72  ARG F O    1 
ATOM   12415 C CB   . ARG F 3 74  ? 24.353  100.331 50.173  1.00 24.27  ? 72  ARG F CB   1 
ATOM   12416 C CG   . ARG F 3 74  ? 24.858  100.764 51.528  1.00 32.12  ? 72  ARG F CG   1 
ATOM   12417 C CD   . ARG F 3 74  ? 25.903  101.854 51.350  1.00 26.74  ? 72  ARG F CD   1 
ATOM   12418 N NE   . ARG F 3 74  ? 25.378  103.187 51.605  1.00 40.69  ? 72  ARG F NE   1 
ATOM   12419 C CZ   . ARG F 3 74  ? 25.895  104.039 52.483  1.00 48.38  ? 72  ARG F CZ   1 
ATOM   12420 N NH1  . ARG F 3 74  ? 26.955  103.696 53.194  1.00 36.46  ? 72  ARG F NH1  1 
ATOM   12421 N NH2  . ARG F 3 74  ? 25.345  105.233 52.651  1.00 47.21  ? 72  ARG F NH2  1 
ATOM   12422 N N    . LEU F 3 75  ? 21.849  98.097  50.266  1.00 31.22  ? 73  LEU F N    1 
ATOM   12423 C CA   . LEU F 3 75  ? 20.499  97.882  49.913  1.00 28.03  ? 73  LEU F CA   1 
ATOM   12424 C C    . LEU F 3 75  ? 19.759  98.960  50.651  1.00 27.39  ? 73  LEU F C    1 
ATOM   12425 O O    . LEU F 3 75  ? 19.738  98.987  51.867  1.00 34.98  ? 73  LEU F O    1 
ATOM   12426 C CB   . LEU F 3 75  ? 20.141  96.471  50.349  1.00 19.23  ? 73  LEU F CB   1 
ATOM   12427 C CG   . LEU F 3 75  ? 20.335  95.403  49.296  1.00 19.37  ? 73  LEU F CG   1 
ATOM   12428 C CD1  . LEU F 3 75  ? 21.483  94.497  49.678  1.00 20.57  ? 73  LEU F CD1  1 
ATOM   12429 C CD2  . LEU F 3 75  ? 19.057  94.609  49.190  1.00 24.51  ? 73  LEU F CD2  1 
ATOM   12430 N N    . ARG F 3 76  ? 19.186  99.885  49.909  1.00 22.41  ? 74  ARG F N    1 
ATOM   12431 C CA   . ARG F 3 76  ? 18.487  100.973 50.493  1.00 21.97  ? 74  ARG F CA   1 
ATOM   12432 C C    . ARG F 3 76  ? 17.273  101.100 49.671  1.00 24.85  ? 74  ARG F C    1 
ATOM   12433 O O    . ARG F 3 76  ? 17.079  100.325 48.756  1.00 35.20  ? 74  ARG F O    1 
ATOM   12434 C CB   . ARG F 3 76  ? 19.275  102.224 50.252  1.00 23.51  ? 74  ARG F CB   1 
ATOM   12435 C CG   . ARG F 3 76  ? 20.625  102.329 50.922  1.00 27.03  ? 74  ARG F CG   1 
ATOM   12436 C CD   . ARG F 3 76  ? 21.146  103.730 50.696  1.00 21.89  ? 74  ARG F CD   1 
ATOM   12437 N NE   . ARG F 3 76  ? 22.489  103.805 50.134  1.00 23.42  ? 74  ARG F NE   1 
ATOM   12438 C CZ   . ARG F 3 76  ? 22.821  103.521 48.882  1.00 22.55  ? 74  ARG F CZ   1 
ATOM   12439 N NH1  . ARG F 3 76  ? 21.934  103.093 48.019  1.00 19.55  ? 74  ARG F NH1  1 
ATOM   12440 N NH2  . ARG F 3 76  ? 24.063  103.655 48.494  1.00 26.83  ? 74  ARG F NH2  1 
ATOM   12441 N N    . GLY F 3 77  ? 16.459  102.100 49.949  1.00 19.05  ? 75  GLY F N    1 
ATOM   12442 C CA   . GLY F 3 77  ? 15.266  102.341 49.175  1.00 28.41  ? 75  GLY F CA   1 
ATOM   12443 C C    . GLY F 3 77  ? 14.334  101.170 49.135  1.00 41.91  ? 75  GLY F C    1 
ATOM   12444 O O    . GLY F 3 77  ? 13.968  100.709 48.067  1.00 48.08  ? 75  GLY F O    1 
ATOM   12445 N N    . GLY F 3 78  ? 13.922  100.688 50.295  1.00 37.21  ? 76  GLY F N    1 
ATOM   12446 C CA   . GLY F 3 78  ? 13.082  99.508  50.350  1.00 36.28  ? 76  GLY F CA   1 
ATOM   12447 C C    . GLY F 3 78  ? 13.319  98.621  51.558  1.00 49.82  ? 76  GLY F C    1 
ATOM   12448 O O    . GLY F 3 78  ? 14.438  98.251  51.876  1.00 55.05  ? 76  GLY F O    1 
ATOM   12449 O OXT  . GLY F 3 78  ? 12.388  98.239  52.246  1.00 44.48  ? 76  GLY F OXT  1 
HETATM 12450 P P    . PO4 G 4 .   ? 22.396  101.338 59.266  1.00 63.60  ? 401 PO4 C P    1 
HETATM 12451 O O1   . PO4 G 4 .   ? 23.665  101.655 58.528  1.00 66.89  ? 401 PO4 C O1   1 
HETATM 12452 O O2   . PO4 G 4 .   ? 21.415  102.469 59.110  1.00 50.21  ? 401 PO4 C O2   1 
HETATM 12453 O O3   . PO4 G 4 .   ? 21.804  100.095 58.674  1.00 48.35  ? 401 PO4 C O3   1 
HETATM 12454 O O4   . PO4 G 4 .   ? 22.725  101.137 60.715  1.00 28.50  ? 401 PO4 C O4   1 
HETATM 12455 P PB   . AR6 H 5 .   ? -6.329  146.426 30.520  1.00 38.84  ? 401 AR6 D PB   1 
HETATM 12456 O O1B  . AR6 H 5 .   ? -7.674  146.287 31.155  1.00 31.25  ? 401 AR6 D O1B  1 
HETATM 12457 C C1D  . AR6 H 5 .   ? -4.505  147.910 34.289  1.00 43.99  ? 401 AR6 D C1D  1 
HETATM 12458 O O1D  . AR6 H 5 .   ? -4.649  148.768 35.418  1.00 59.17  ? 401 AR6 D O1D  1 
HETATM 12459 O O2B  . AR6 H 5 .   ? -6.124  146.977 29.148  1.00 33.49  ? 401 AR6 D O2B  1 
HETATM 12460 C C2D  . AR6 H 5 .   ? -3.207  147.155 34.303  1.00 31.76  ? 401 AR6 D C2D  1 
HETATM 12461 O O2D  . AR6 H 5 .   ? -2.211  147.929 34.940  1.00 45.35  ? 401 AR6 D O2D  1 
HETATM 12462 O O3A  . AR6 H 5 .   ? -5.522  145.057 30.701  1.00 47.72  ? 401 AR6 D O3A  1 
HETATM 12463 C C3D  . AR6 H 5 .   ? -2.828  147.004 32.872  1.00 30.54  ? 401 AR6 D C3D  1 
HETATM 12464 O O3D  . AR6 H 5 .   ? -1.417  147.057 32.722  1.00 54.55  ? 401 AR6 D O3D  1 
HETATM 12465 C C4D  . AR6 H 5 .   ? -3.470  148.196 32.215  1.00 37.54  ? 401 AR6 D C4D  1 
HETATM 12466 O O4D  . AR6 H 5 .   ? -4.459  148.685 33.104  1.00 35.98  ? 401 AR6 D O4D  1 
HETATM 12467 C C5D  . AR6 H 5 .   ? -4.200  147.825 30.956  1.00 58.53  ? 401 AR6 D C5D  1 
HETATM 12468 O O5D  . AR6 H 5 .   ? -5.484  147.417 31.400  1.00 59.97  ? 401 AR6 D O5D  1 
HETATM 12469 H H1D  . AR6 H 5 .   ? -5.335  147.193 34.245  1.00 52.62  ? 401 AR6 D H1D  1 
HETATM 12470 H H2D  . AR6 H 5 .   ? -3.327  146.169 34.757  1.00 37.94  ? 401 AR6 D H2D  1 
HETATM 12471 H HO2D . AR6 H 5 .   ? -1.500  147.338 35.219  1.00 54.26  ? 401 AR6 D HO2D 1 
HETATM 12472 H H3D  . AR6 H 5 .   ? -3.238  146.056 32.496  1.00 36.48  ? 401 AR6 D H3D  1 
HETATM 12473 H HO3D . AR6 H 5 .   ? -1.186  146.850 31.807  1.00 65.30  ? 401 AR6 D HO3D 1 
HETATM 12474 H H4D  . AR6 H 5 .   ? -2.718  148.968 32.007  1.00 44.89  ? 401 AR6 D H4D  1 
HETATM 12475 H H5D  . AR6 H 5 .   ? -4.298  148.690 30.315  1.00 70.07  ? 401 AR6 D H5D  1 
HETATM 12476 H H5DA . AR6 H 5 .   ? -3.666  147.049 30.404  1.00 70.07  ? 401 AR6 D H5DA 1 
HETATM 12477 H HD1  . AR6 H 5 .   ? -4.684  149.688 35.126  1.00 70.84  ? 401 AR6 D HD1  1 
HETATM 12478 O O    . HOH I 6 .   ? 12.958  62.541  62.912  1.00 9.91   ? 401 HOH A O    1 
HETATM 12479 O O    . HOH I 6 .   ? 34.355  42.518  11.735  1.00 0.82   ? 402 HOH A O    1 
HETATM 12480 O O    . HOH I 6 .   ? 19.724  64.278  38.695  1.00 5.62   ? 403 HOH A O    1 
HETATM 12481 O O    . HOH I 6 .   ? 20.162  56.478  40.206  1.00 8.54   ? 404 HOH A O    1 
HETATM 12482 O O    . HOH I 6 .   ? 19.970  73.476  48.482  1.00 5.72   ? 405 HOH A O    1 
HETATM 12483 O O    . HOH I 6 .   ? 1.140   61.730  55.832  1.00 4.29   ? 406 HOH A O    1 
HETATM 12484 O O    . HOH I 6 .   ? 15.919  46.117  43.431  1.00 0.82   ? 407 HOH A O    1 
HETATM 12485 O O    . HOH I 6 .   ? 29.090  39.833  17.694  1.00 9.31   ? 408 HOH A O    1 
HETATM 12486 O O    . HOH I 6 .   ? 40.503  73.536  30.820  1.00 27.69  ? 409 HOH A O    1 
HETATM 12487 O O    . HOH J 6 .   ? 23.608  105.421 -0.565  1.00 12.84  ? 401 HOH B O    1 
HETATM 12488 O O    . HOH J 6 .   ? 11.066  99.238  -7.144  1.00 10.91  ? 402 HOH B O    1 
HETATM 12489 O O    . HOH J 6 .   ? 8.088   91.786  5.230   1.00 17.64  ? 403 HOH B O    1 
HETATM 12490 O O    . HOH J 6 .   ? 6.568   94.678  36.945  1.00 2.72   ? 404 HOH B O    1 
HETATM 12491 O O    . HOH J 6 .   ? 13.071  98.185  18.913  1.00 11.23  ? 405 HOH B O    1 
HETATM 12492 O O    . HOH J 6 .   ? 18.747  100.606 12.266  1.00 3.71   ? 406 HOH B O    1 
HETATM 12493 O O    . HOH J 6 .   ? 4.453   91.536  10.442  1.00 14.70  ? 407 HOH B O    1 
HETATM 12494 O O    . HOH J 6 .   ? 8.335   102.435 16.253  1.00 0.82   ? 408 HOH B O    1 
HETATM 12495 O O    . HOH J 6 .   ? 0.688   127.954 38.535  1.00 3.84   ? 409 HOH B O    1 
HETATM 12496 O O    . HOH J 6 .   ? 4.220   84.543  -5.017  1.00 6.80   ? 410 HOH B O    1 
HETATM 12497 O O    . HOH K 6 .   ? 22.813  76.328  83.780  1.00 22.97  ? 501 HOH C O    1 
HETATM 12498 O O    . HOH K 6 .   ? 29.434  114.412 77.975  1.00 5.90   ? 502 HOH C O    1 
HETATM 12499 O O    . HOH K 6 .   ? 12.168  108.778 45.905  1.00 12.22  ? 503 HOH C O    1 
HETATM 12500 O O    . HOH K 6 .   ? 39.064  109.813 63.495  1.00 3.01   ? 504 HOH C O    1 
HETATM 12501 O O    . HOH K 6 .   ? 19.085  100.630 94.600  1.00 0.82   ? 505 HOH C O    1 
HETATM 12502 O O    . HOH L 6 .   ? -12.897 137.522 30.135  1.00 7.73   ? 501 HOH D O    1 
HETATM 12503 O O    . HOH L 6 .   ? -10.936 171.716 9.152   1.00 38.71  ? 502 HOH D O    1 
HETATM 12504 O O    . HOH L 6 .   ? -11.315 132.820 -4.596  1.00 15.81  ? 503 HOH D O    1 
HETATM 12505 O O    . HOH L 6 .   ? -17.963 145.752 -1.583  1.00 10.39  ? 504 HOH D O    1 
HETATM 12506 O O    . HOH L 6 .   ? 10.992  127.731 23.571  1.00 6.38   ? 505 HOH D O    1 
HETATM 12507 O O    . HOH L 6 .   ? -39.081 143.927 -13.858 1.00 22.79  ? 506 HOH D O    1 
HETATM 12508 O O    . HOH L 6 .   ? 22.485  163.214 6.371   1.00 11.10  ? 507 HOH D O    1 
HETATM 12509 O O    . HOH L 6 .   ? -31.914 152.552 0.254   1.00 21.20  ? 508 HOH D O    1 
HETATM 12510 O O    . HOH L 6 .   ? 25.403  159.412 11.228  1.00 11.26  ? 509 HOH D O    1 
HETATM 12511 O O    . HOH M 6 .   ? 29.178  106.816 34.587  1.00 6.41   ? 101 HOH F O    1 
HETATM 12512 O O    . HOH M 6 .   ? 48.441  106.359 55.857  1.00 23.35  ? 102 HOH F O    1 
# 
