data_8K6E
# 
_entry.id   8K6E 
# 
_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   8K6E         pdb_00008k6e 10.2210/pdb8k6e/pdb 
WWPDB D_1300039601 ?            ?                   
# 
_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       2025-02-05 
# 
_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                        8K6E 
_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         Ouyang 
_pdbx_contact_author.name_last          Songying 
_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 1  ? ? ? ? 
2 polymer     man 'Legionella effector LnaB' 40622.980 1  ? ? ? ? 
3 polymer     man Polyubiquitin-B 8519.778  1  ? ? ? ? 
4 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' 506.196   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    82 ? ? ? ? 
# 
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 ? 
2 'polypeptide(L)' no no 
;MSYQKIELSISLSLDSPKLDESDFILLSVKYLEKSLGKKKEFSGFFEDIEKLYFKQNYKEAIEKILDFCKKNESLLSEQV
VQRLAEVAPRLKSNPKDNESRRLYETLYADHLESVIKQESDLSVFNELRDSYNAVKPEYAVTHETEIKTLDEAKQFILSF
VMLNDNVELPLKAQSERYPKKDRSREELGNTPSANPGIMKPNSPNFTDNLVPVRDVPKIAINEKVAGGYSKTKPTTPFVA
SLSGTTYSLMVVLTDYIEKHKTDKDIEKKVNQIINLWISSYIKEGYHSYSEVVDVLTEPFLQSIFDKANIKLNYGVLDDT
HAEFRKAQDYVFGLTIQSAMHHELQERFKNKE
;
;MSYQKIELSISLSLDSPKLDESDFILLSVKYLEKSLGKKKEFSGFFEDIEKLYFKQNYKEAIEKILDFCKKNESLLSEQV
VQRLAEVAPRLKSNPKDNESRRLYETLYADHLESVIKQESDLSVFNELRDSYNAVKPEYAVTHETEIKTLDEAKQFILSF
VMLNDNVELPLKAQSERYPKKDRSREELGNTPSANPGIMKPNSPNFTDNLVPVRDVPKIAINEKVAGGYSKTKPTTPFVA
SLSGTTYSLMVVLTDYIEKHKTDKDIEKKVNQIINLWISSYIKEGYHSYSEVVDVLTEPFLQSIFDKANIKLNYGVLDDT
HAEFRKAQDYVFGLTIQSAMHHELQERFKNKE
;
B ? 
3 'polypeptide(L)' no no MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG 
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP 
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   MET n 
3 2   GLN n 
3 3   ILE n 
3 4   PHE n 
3 5   VAL n 
3 6   LYS n 
3 7   THR n 
3 8   LEU n 
3 9   THR n 
3 10  GLY n 
3 11  LYS n 
3 12  THR n 
3 13  ILE n 
3 14  THR n 
3 15  LEU n 
3 16  GLU n 
3 17  VAL n 
3 18  GLU n 
3 19  PRO n 
3 20  SER n 
3 21  ASP n 
3 22  THR n 
3 23  ILE n 
3 24  GLU n 
3 25  ASN n 
3 26  VAL n 
3 27  LYS n 
3 28  ALA n 
3 29  LYS n 
3 30  ILE n 
3 31  GLN n 
3 32  ASP n 
3 33  LYS n 
3 34  GLU n 
3 35  GLY n 
3 36  ILE n 
3 37  PRO n 
3 38  PRO n 
3 39  ASP n 
3 40  GLN n 
3 41  GLN n 
3 42  ARG n 
3 43  LEU n 
3 44  ILE n 
3 45  PHE n 
3 46  ALA n 
3 47  GLY n 
3 48  LYS n 
3 49  GLN n 
3 50  LEU n 
3 51  GLU n 
3 52  ASP n 
3 53  GLY n 
3 54  ARG n 
3 55  THR n 
3 56  LEU n 
3 57  SER n 
3 58  ASP n 
3 59  TYR n 
3 60  ASN n 
3 61  ILE n 
3 62  GLN n 
3 63  LYS n 
3 64  GLU n 
3 65  SER n 
3 66  THR n 
3 67  LEU n 
3 68  HIS n 
3 69  LEU n 
3 70  VAL n 
3 71  LEU n 
3 72  ARG n 
3 73  LEU n 
3 74  ARG n 
3 75  GLY n 
# 
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 75  human ? UBB ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           375 
_entity_src_nat.common_name                rabbit 
_entity_src_nat.pdbx_organism_scientific   'Oryctolagus cuniculus' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9986 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                           'C3 H7 N O2'        89.093  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ?                           'C10 H17 N6 O12 P3' 506.196 
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 
PRO 'L-peptide linking' y PROLINE ?                           'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?                           'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?                           'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                           'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?                           'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?                           'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   GLU 4   4   ?   ?   ?   A . n 
A 1 5   ILE 5   5   ?   ?   ?   A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  ASN 12  12  12  ASN ASN A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  MET 16  16  16  MET MET A . n 
A 1 17  CYS 17  17  17  CYS CYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  MET 44  44  44  MET MET A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  MET 47  47  47  MET MET A . n 
A 1 48  GLY 48  48  ?   ?   ?   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 2 1   MET 1   19  ?   ?   ?   B . n 
B 2 2   SER 2   20  ?   ?   ?   B . n 
B 2 3   TYR 3   21  ?   ?   ?   B . n 
B 2 4   GLN 4   22  ?   ?   ?   B . n 
B 2 5   LYS 5   23  23  LYS LYS B . n 
B 2 6   ILE 6   24  24  ILE ILE B . n 
B 2 7   GLU 7   25  25  GLU GLU B . n 
B 2 8   LEU 8   26  26  LEU LEU B . n 
B 2 9   SER 9   27  27  SER SER B . n 
B 2 10  ILE 10  28  28  ILE ILE B . n 
B 2 11  SER 11  29  29  SER SER B . n 
B 2 12  LEU 12  30  30  LEU LEU B . n 
B 2 13  SER 13  31  31  SER SER B . n 
B 2 14  LEU 14  32  32  LEU LEU B . n 
B 2 15  ASP 15  33  33  ASP ASP B . n 
B 2 16  SER 16  34  34  SER SER B . n 
B 2 17  PRO 17  35  35  PRO PRO B . n 
B 2 18  LYS 18  36  36  LYS LYS B . n 
B 2 19  LEU 19  37  37  LEU LEU B . n 
B 2 20  ASP 20  38  38  ASP ASP B . n 
B 2 21  GLU 21  39  39  GLU GLU B . n 
B 2 22  SER 22  40  40  SER SER B . n 
B 2 23  ASP 23  41  41  ASP ASP B . n 
B 2 24  PHE 24  42  42  PHE PHE B . n 
B 2 25  ILE 25  43  43  ILE ILE B . n 
B 2 26  LEU 26  44  44  LEU LEU B . n 
B 2 27  LEU 27  45  45  LEU LEU B . n 
B 2 28  SER 28  46  46  SER SER B . n 
B 2 29  VAL 29  47  47  VAL VAL B . n 
B 2 30  LYS 30  48  48  LYS LYS B . n 
B 2 31  TYR 31  49  49  TYR TYR B . n 
B 2 32  LEU 32  50  50  LEU LEU B . n 
B 2 33  GLU 33  51  51  GLU GLU B . n 
B 2 34  LYS 34  52  52  LYS LYS B . n 
B 2 35  SER 35  53  53  SER SER B . n 
B 2 36  LEU 36  54  54  LEU LEU B . n 
B 2 37  GLY 37  55  55  GLY GLY B . n 
B 2 38  LYS 38  56  56  LYS LYS B . n 
B 2 39  LYS 39  57  57  LYS LYS B . n 
B 2 40  LYS 40  58  58  LYS LYS B . n 
B 2 41  GLU 41  59  59  GLU GLU B . n 
B 2 42  PHE 42  60  60  PHE PHE B . n 
B 2 43  SER 43  61  61  SER SER B . n 
B 2 44  GLY 44  62  62  GLY GLY B . n 
B 2 45  PHE 45  63  63  PHE PHE B . n 
B 2 46  PHE 46  64  64  PHE PHE B . n 
B 2 47  GLU 47  65  65  GLU GLU B . n 
B 2 48  ASP 48  66  66  ASP ASP B . n 
B 2 49  ILE 49  67  67  ILE ILE B . n 
B 2 50  GLU 50  68  68  GLU GLU B . n 
B 2 51  LYS 51  69  69  LYS LYS B . n 
B 2 52  LEU 52  70  70  LEU LEU B . n 
B 2 53  TYR 53  71  71  TYR TYR B . n 
B 2 54  PHE 54  72  72  PHE PHE B . n 
B 2 55  LYS 55  73  73  LYS LYS B . n 
B 2 56  GLN 56  74  74  GLN GLN B . n 
B 2 57  ASN 57  75  75  ASN ASN B . n 
B 2 58  TYR 58  76  76  TYR TYR B . n 
B 2 59  LYS 59  77  77  LYS LYS B . n 
B 2 60  GLU 60  78  78  GLU GLU B . n 
B 2 61  ALA 61  79  79  ALA ALA B . n 
B 2 62  ILE 62  80  80  ILE ILE B . n 
B 2 63  GLU 63  81  81  GLU GLU B . n 
B 2 64  LYS 64  82  82  LYS LYS B . n 
B 2 65  ILE 65  83  83  ILE ILE B . n 
B 2 66  LEU 66  84  84  LEU LEU B . n 
B 2 67  ASP 67  85  85  ASP ASP B . n 
B 2 68  PHE 68  86  86  PHE PHE B . n 
B 2 69  CYS 69  87  87  CYS CYS B . n 
B 2 70  LYS 70  88  88  LYS LYS B . n 
B 2 71  LYS 71  89  89  LYS LYS B . n 
B 2 72  ASN 72  90  90  ASN ASN B . n 
B 2 73  GLU 73  91  91  GLU GLU B . n 
B 2 74  SER 74  92  92  SER SER B . n 
B 2 75  LEU 75  93  93  LEU LEU B . n 
B 2 76  LEU 76  94  94  LEU LEU B . n 
B 2 77  SER 77  95  95  SER SER B . n 
B 2 78  GLU 78  96  96  GLU GLU B . n 
B 2 79  GLN 79  97  97  GLN GLN B . n 
B 2 80  VAL 80  98  98  VAL VAL B . n 
B 2 81  VAL 81  99  99  VAL VAL B . n 
B 2 82  GLN 82  100 100 GLN GLN B . n 
B 2 83  ARG 83  101 101 ARG ARG B . n 
B 2 84  LEU 84  102 102 LEU LEU B . n 
B 2 85  ALA 85  103 103 ALA ALA B . n 
B 2 86  GLU 86  104 104 GLU GLU B . n 
B 2 87  VAL 87  105 105 VAL VAL B . n 
B 2 88  ALA 88  106 106 ALA ALA B . n 
B 2 89  PRO 89  107 107 PRO PRO B . n 
B 2 90  ARG 90  108 108 ARG ARG B . n 
B 2 91  LEU 91  109 109 LEU LEU B . n 
B 2 92  LYS 92  110 110 LYS LYS B . n 
B 2 93  SER 93  111 111 SER SER B . n 
B 2 94  ASN 94  112 112 ASN ASN B . n 
B 2 95  PRO 95  113 113 PRO PRO B . n 
B 2 96  LYS 96  114 114 LYS LYS B . n 
B 2 97  ASP 97  115 115 ASP ASP B . n 
B 2 98  ASN 98  116 116 ASN ASN B . n 
B 2 99  GLU 99  117 117 GLU GLU B . n 
B 2 100 SER 100 118 118 SER SER B . n 
B 2 101 ARG 101 119 119 ARG ARG B . n 
B 2 102 ARG 102 120 120 ARG ARG B . n 
B 2 103 LEU 103 121 121 LEU LEU B . n 
B 2 104 TYR 104 122 122 TYR TYR B . n 
B 2 105 GLU 105 123 123 GLU GLU B . n 
B 2 106 THR 106 124 124 THR THR B . n 
B 2 107 LEU 107 125 125 LEU LEU B . n 
B 2 108 TYR 108 126 126 TYR TYR B . n 
B 2 109 ALA 109 127 127 ALA ALA B . n 
B 2 110 ASP 110 128 128 ASP ASP B . n 
B 2 111 HIS 111 129 129 HIS HIS B . n 
B 2 112 LEU 112 130 130 LEU LEU B . n 
B 2 113 GLU 113 131 131 GLU GLU B . n 
B 2 114 SER 114 132 132 SER SER B . n 
B 2 115 VAL 115 133 133 VAL VAL B . n 
B 2 116 ILE 116 134 134 ILE ILE B . n 
B 2 117 LYS 117 135 135 LYS LYS B . n 
B 2 118 GLN 118 136 136 GLN GLN B . n 
B 2 119 GLU 119 137 137 GLU GLU B . n 
B 2 120 SER 120 138 138 SER SER B . n 
B 2 121 ASP 121 139 139 ASP ASP B . n 
B 2 122 LEU 122 140 140 LEU LEU B . n 
B 2 123 SER 123 141 141 SER SER B . n 
B 2 124 VAL 124 142 142 VAL VAL B . n 
B 2 125 PHE 125 143 143 PHE PHE B . n 
B 2 126 ASN 126 144 144 ASN ASN B . n 
B 2 127 GLU 127 145 145 GLU GLU B . n 
B 2 128 LEU 128 146 146 LEU LEU B . n 
B 2 129 ARG 129 147 147 ARG ARG B . n 
B 2 130 ASP 130 148 148 ASP ASP B . n 
B 2 131 SER 131 149 149 SER SER B . n 
B 2 132 TYR 132 150 150 TYR TYR B . n 
B 2 133 ASN 133 151 151 ASN ASN B . n 
B 2 134 ALA 134 152 152 ALA ALA B . n 
B 2 135 VAL 135 153 153 VAL VAL B . n 
B 2 136 LYS 136 154 154 LYS LYS B . n 
B 2 137 PRO 137 155 155 PRO PRO B . n 
B 2 138 GLU 138 156 156 GLU GLU B . n 
B 2 139 TYR 139 157 157 TYR TYR B . n 
B 2 140 ALA 140 158 158 ALA ALA B . n 
B 2 141 VAL 141 159 159 VAL VAL B . n 
B 2 142 THR 142 160 160 THR THR B . n 
B 2 143 HIS 143 161 161 HIS HIS B . n 
B 2 144 GLU 144 162 162 GLU GLU B . n 
B 2 145 THR 145 163 163 THR THR B . n 
B 2 146 GLU 146 164 164 GLU GLU B . n 
B 2 147 ILE 147 165 165 ILE ILE B . n 
B 2 148 LYS 148 166 166 LYS LYS B . n 
B 2 149 THR 149 167 167 THR THR B . n 
B 2 150 LEU 150 168 168 LEU LEU B . n 
B 2 151 ASP 151 169 169 ASP ASP B . n 
B 2 152 GLU 152 170 170 GLU GLU B . n 
B 2 153 ALA 153 171 171 ALA ALA B . n 
B 2 154 LYS 154 172 172 LYS LYS B . n 
B 2 155 GLN 155 173 173 GLN GLN B . n 
B 2 156 PHE 156 174 174 PHE PHE B . n 
B 2 157 ILE 157 175 175 ILE ILE B . n 
B 2 158 LEU 158 176 176 LEU LEU B . n 
B 2 159 SER 159 177 177 SER SER B . n 
B 2 160 PHE 160 178 178 PHE PHE B . n 
B 2 161 VAL 161 179 179 VAL VAL B . n 
B 2 162 MET 162 180 180 MET MET B . n 
B 2 163 LEU 163 181 181 LEU LEU B . n 
B 2 164 ASN 164 182 182 ASN ASN B . n 
B 2 165 ASP 165 183 183 ASP ASP B . n 
B 2 166 ASN 166 184 184 ASN ASN B . n 
B 2 167 VAL 167 185 185 VAL VAL B . n 
B 2 168 GLU 168 186 186 GLU GLU B . n 
B 2 169 LEU 169 187 187 LEU LEU B . n 
B 2 170 PRO 170 188 188 PRO PRO B . n 
B 2 171 LEU 171 189 189 LEU LEU B . n 
B 2 172 LYS 172 190 190 LYS LYS B . n 
B 2 173 ALA 173 191 191 ALA ALA B . n 
B 2 174 GLN 174 192 192 GLN GLN B . n 
B 2 175 SER 175 193 193 SER SER B . n 
B 2 176 GLU 176 194 194 GLU GLU B . n 
B 2 177 ARG 177 195 195 ARG ARG B . n 
B 2 178 TYR 178 196 196 TYR TYR B . n 
B 2 179 PRO 179 197 197 PRO PRO B . n 
B 2 180 LYS 180 198 198 LYS LYS B . n 
B 2 181 LYS 181 199 199 LYS LYS B . n 
B 2 182 ASP 182 200 200 ASP ASP B . n 
B 2 183 ARG 183 201 201 ARG ARG B . n 
B 2 184 SER 184 202 202 SER SER B . n 
B 2 185 ARG 185 203 203 ARG ARG B . n 
B 2 186 GLU 186 204 204 GLU GLU B . n 
B 2 187 GLU 187 205 205 GLU GLU B . n 
B 2 188 LEU 188 206 206 LEU LEU B . n 
B 2 189 GLY 189 207 207 GLY GLY B . n 
B 2 190 ASN 190 208 208 ASN ASN B . n 
B 2 191 THR 191 209 209 THR THR B . n 
B 2 192 PRO 192 210 210 PRO PRO B . n 
B 2 193 SER 193 211 211 SER SER B . n 
B 2 194 ALA 194 212 212 ALA ALA B . n 
B 2 195 ASN 195 213 213 ASN ASN B . n 
B 2 196 PRO 196 214 214 PRO PRO B . n 
B 2 197 GLY 197 215 215 GLY GLY B . n 
B 2 198 ILE 198 216 216 ILE ILE B . n 
B 2 199 MET 199 217 217 MET MET B . n 
B 2 200 LYS 200 218 218 LYS LYS B . n 
B 2 201 PRO 201 219 219 PRO PRO B . n 
B 2 202 ASN 202 220 220 ASN ASN B . n 
B 2 203 SER 203 221 221 SER SER B . n 
B 2 204 PRO 204 222 222 PRO PRO B . n 
B 2 205 ASN 205 223 223 ASN ASN B . n 
B 2 206 PHE 206 224 224 PHE PHE B . n 
B 2 207 THR 207 225 225 THR THR B . n 
B 2 208 ASP 208 226 226 ASP ASP B . n 
B 2 209 ASN 209 227 227 ASN ASN B . n 
B 2 210 LEU 210 228 228 LEU LEU B . n 
B 2 211 VAL 211 229 229 VAL VAL B . n 
B 2 212 PRO 212 230 230 PRO PRO B . n 
B 2 213 VAL 213 231 231 VAL VAL B . n 
B 2 214 ARG 214 232 232 ARG ARG B . n 
B 2 215 ASP 215 233 233 ASP ASP B . n 
B 2 216 VAL 216 234 234 VAL VAL B . n 
B 2 217 PRO 217 235 235 PRO PRO B . n 
B 2 218 LYS 218 236 236 LYS LYS B . n 
B 2 219 ILE 219 237 237 ILE ILE B . n 
B 2 220 ALA 220 238 238 ALA ALA B . n 
B 2 221 ILE 221 239 239 ILE ILE B . n 
B 2 222 ASN 222 240 240 ASN ASN B . n 
B 2 223 GLU 223 241 241 GLU GLU B . n 
B 2 224 LYS 224 242 242 LYS LYS B . n 
B 2 225 VAL 225 243 243 VAL VAL B . n 
B 2 226 ALA 226 244 244 ALA ALA B . n 
B 2 227 GLY 227 245 245 GLY GLY B . n 
B 2 228 GLY 228 246 246 GLY GLY B . n 
B 2 229 TYR 229 247 247 TYR TYR B . n 
B 2 230 SER 230 248 248 SER SER B . n 
B 2 231 LYS 231 249 249 LYS LYS B . n 
B 2 232 THR 232 250 250 THR THR B . n 
B 2 233 LYS 233 251 251 LYS LYS B . n 
B 2 234 PRO 234 252 252 PRO PRO B . n 
B 2 235 THR 235 253 253 THR THR B . n 
B 2 236 THR 236 254 254 THR THR B . n 
B 2 237 PRO 237 255 255 PRO PRO B . n 
B 2 238 PHE 238 256 256 PHE PHE B . n 
B 2 239 VAL 239 257 257 VAL VAL B . n 
B 2 240 ALA 240 258 258 ALA ALA B . n 
B 2 241 SER 241 259 259 SER SER B . n 
B 2 242 LEU 242 260 260 LEU LEU B . n 
B 2 243 SER 243 261 261 SER SER B . n 
B 2 244 GLY 244 262 262 GLY GLY B . n 
B 2 245 THR 245 263 263 THR THR B . n 
B 2 246 THR 246 264 264 THR THR B . n 
B 2 247 TYR 247 265 265 TYR TYR B . n 
B 2 248 SER 248 266 266 SER SER B . n 
B 2 249 LEU 249 267 267 LEU LEU B . n 
B 2 250 MET 250 268 268 MET MET B . n 
B 2 251 VAL 251 269 269 VAL VAL B . n 
B 2 252 VAL 252 270 270 VAL VAL B . n 
B 2 253 LEU 253 271 271 LEU LEU B . n 
B 2 254 THR 254 272 272 THR THR B . n 
B 2 255 ASP 255 273 273 ASP ASP B . n 
B 2 256 TYR 256 274 274 TYR TYR B . n 
B 2 257 ILE 257 275 275 ILE ILE B . n 
B 2 258 GLU 258 276 276 GLU GLU B . n 
B 2 259 LYS 259 277 277 LYS LYS B . n 
B 2 260 HIS 260 278 278 HIS HIS B . n 
B 2 261 LYS 261 279 279 LYS LYS B . n 
B 2 262 THR 262 280 280 THR THR B . n 
B 2 263 ASP 263 281 281 ASP ASP B . n 
B 2 264 LYS 264 282 282 LYS LYS B . n 
B 2 265 ASP 265 283 283 ASP ASP B . n 
B 2 266 ILE 266 284 284 ILE ILE B . n 
B 2 267 GLU 267 285 285 GLU GLU B . n 
B 2 268 LYS 268 286 286 LYS LYS B . n 
B 2 269 LYS 269 287 287 LYS LYS B . n 
B 2 270 VAL 270 288 288 VAL VAL B . n 
B 2 271 ASN 271 289 289 ASN ASN B . n 
B 2 272 GLN 272 290 290 GLN GLN B . n 
B 2 273 ILE 273 291 291 ILE ILE B . n 
B 2 274 ILE 274 292 292 ILE ILE B . n 
B 2 275 ASN 275 293 293 ASN ASN B . n 
B 2 276 LEU 276 294 294 LEU LEU B . n 
B 2 277 TRP 277 295 295 TRP TRP B . n 
B 2 278 ILE 278 296 296 ILE ILE B . n 
B 2 279 SER 279 297 297 SER SER B . n 
B 2 280 SER 280 298 298 SER SER B . n 
B 2 281 TYR 281 299 299 TYR TYR B . n 
B 2 282 ILE 282 300 300 ILE ILE B . n 
B 2 283 LYS 283 301 301 LYS LYS B . n 
B 2 284 GLU 284 302 302 GLU GLU B . n 
B 2 285 GLY 285 303 303 GLY GLY B . n 
B 2 286 TYR 286 304 304 TYR TYR B . n 
B 2 287 HIS 287 305 305 HIS HIS B . n 
B 2 288 SER 288 306 306 SER SER B . n 
B 2 289 TYR 289 307 307 TYR TYR B . n 
B 2 290 SER 290 308 308 SER SER B . n 
B 2 291 GLU 291 309 309 GLU GLU B . n 
B 2 292 VAL 292 310 310 VAL VAL B . n 
B 2 293 VAL 293 311 311 VAL VAL B . n 
B 2 294 ASP 294 312 312 ASP ASP B . n 
B 2 295 VAL 295 313 313 VAL VAL B . n 
B 2 296 LEU 296 314 314 LEU LEU B . n 
B 2 297 THR 297 315 315 THR THR B . n 
B 2 298 GLU 298 316 316 GLU GLU B . n 
B 2 299 PRO 299 317 317 PRO PRO B . n 
B 2 300 PHE 300 318 318 PHE PHE B . n 
B 2 301 LEU 301 319 319 LEU LEU B . n 
B 2 302 GLN 302 320 320 GLN GLN B . n 
B 2 303 SER 303 321 321 SER SER B . n 
B 2 304 ILE 304 322 322 ILE ILE B . n 
B 2 305 PHE 305 323 323 PHE PHE B . n 
B 2 306 ASP 306 324 324 ASP ASP B . n 
B 2 307 LYS 307 325 325 LYS LYS B . n 
B 2 308 ALA 308 326 326 ALA ALA B . n 
B 2 309 ASN 309 327 327 ASN ASN B . n 
B 2 310 ILE 310 328 328 ILE ILE B . n 
B 2 311 LYS 311 329 329 LYS LYS B . n 
B 2 312 LEU 312 330 330 LEU LEU B . n 
B 2 313 ASN 313 331 331 ASN ASN B . n 
B 2 314 TYR 314 332 332 TYR TYR B . n 
B 2 315 GLY 315 333 333 GLY GLY B . n 
B 2 316 VAL 316 334 334 VAL VAL B . n 
B 2 317 LEU 317 335 335 LEU LEU B . n 
B 2 318 ASP 318 336 336 ASP ASP B . n 
B 2 319 ASP 319 337 337 ASP ASP B . n 
B 2 320 THR 320 338 338 THR THR B . n 
B 2 321 HIS 321 339 339 HIS HIS B . n 
B 2 322 ALA 322 340 340 ALA ALA B . n 
B 2 323 GLU 323 341 341 GLU GLU B . n 
B 2 324 PHE 324 342 342 PHE PHE B . n 
B 2 325 ARG 325 343 343 ARG ARG B . n 
B 2 326 LYS 326 344 344 LYS LYS B . n 
B 2 327 ALA 327 345 345 ALA ALA B . n 
B 2 328 GLN 328 346 346 GLN GLN B . n 
B 2 329 ASP 329 347 347 ASP ASP B . n 
B 2 330 TYR 330 348 348 TYR TYR B . n 
B 2 331 VAL 331 349 349 VAL VAL B . n 
B 2 332 PHE 332 350 350 PHE PHE B . n 
B 2 333 GLY 333 351 351 GLY GLY B . n 
B 2 334 LEU 334 352 352 LEU LEU B . n 
B 2 335 THR 335 353 353 THR THR B . n 
B 2 336 ILE 336 354 354 ILE ILE B . n 
B 2 337 GLN 337 355 355 GLN GLN B . n 
B 2 338 SER 338 356 356 SER SER B . n 
B 2 339 ALA 339 357 357 ALA ALA B . n 
B 2 340 MET 340 358 358 MET MET B . n 
B 2 341 HIS 341 359 359 HIS HIS B . n 
B 2 342 HIS 342 360 360 HIS HIS B . n 
B 2 343 GLU 343 361 361 GLU GLU B . n 
B 2 344 LEU 344 362 362 LEU LEU B . n 
B 2 345 GLN 345 363 363 GLN GLN B . n 
B 2 346 GLU 346 364 364 GLU GLU B . n 
B 2 347 ARG 347 365 365 ARG ARG B . n 
B 2 348 PHE 348 366 366 PHE PHE B . n 
B 2 349 LYS 349 367 367 LYS LYS B . n 
B 2 350 ASN 350 368 368 ASN ASN B . n 
B 2 351 LYS 351 369 369 LYS LYS B . n 
B 2 352 GLU 352 370 ?   ?   ?   B . n 
C 3 1   MET 1   1   1   MET MET C . n 
C 3 2   GLN 2   2   2   GLN GLN C . n 
C 3 3   ILE 3   3   3   ILE ILE C . n 
C 3 4   PHE 4   4   4   PHE PHE C . n 
C 3 5   VAL 5   5   5   VAL VAL C . n 
C 3 6   LYS 6   6   6   LYS LYS C . n 
C 3 7   THR 7   7   7   THR THR C . n 
C 3 8   LEU 8   8   8   LEU LEU C . n 
C 3 9   THR 9   9   9   THR THR C . n 
C 3 10  GLY 10  10  10  GLY GLY C . n 
C 3 11  LYS 11  11  11  LYS LYS C . n 
C 3 12  THR 12  12  12  THR THR C . n 
C 3 13  ILE 13  13  13  ILE ILE C . n 
C 3 14  THR 14  14  14  THR THR C . n 
C 3 15  LEU 15  15  15  LEU LEU C . n 
C 3 16  GLU 16  16  16  GLU GLU C . n 
C 3 17  VAL 17  17  17  VAL VAL C . n 
C 3 18  GLU 18  18  18  GLU GLU C . n 
C 3 19  PRO 19  19  19  PRO PRO C . n 
C 3 20  SER 20  20  20  SER SER C . n 
C 3 21  ASP 21  21  21  ASP ASP C . n 
C 3 22  THR 22  22  22  THR THR C . n 
C 3 23  ILE 23  23  23  ILE ILE C . n 
C 3 24  GLU 24  24  24  GLU GLU C . n 
C 3 25  ASN 25  25  25  ASN ASN C . n 
C 3 26  VAL 26  26  26  VAL VAL C . n 
C 3 27  LYS 27  27  27  LYS LYS C . n 
C 3 28  ALA 28  28  28  ALA ALA C . n 
C 3 29  LYS 29  29  29  LYS LYS C . n 
C 3 30  ILE 30  30  30  ILE ILE C . n 
C 3 31  GLN 31  31  31  GLN GLN C . n 
C 3 32  ASP 32  32  32  ASP ASP C . n 
C 3 33  LYS 33  33  33  LYS LYS C . n 
C 3 34  GLU 34  34  34  GLU GLU C . n 
C 3 35  GLY 35  35  35  GLY GLY C . n 
C 3 36  ILE 36  36  36  ILE ILE C . n 
C 3 37  PRO 37  37  37  PRO PRO C . n 
C 3 38  PRO 38  38  38  PRO PRO C . n 
C 3 39  ASP 39  39  39  ASP ASP C . n 
C 3 40  GLN 40  40  40  GLN GLN C . n 
C 3 41  GLN 41  41  41  GLN GLN C . n 
C 3 42  ARG 42  42  42  ARG ARG C . n 
C 3 43  LEU 43  43  43  LEU LEU C . n 
C 3 44  ILE 44  44  44  ILE ILE C . n 
C 3 45  PHE 45  45  45  PHE PHE C . n 
C 3 46  ALA 46  46  46  ALA ALA C . n 
C 3 47  GLY 47  47  47  GLY GLY C . n 
C 3 48  LYS 48  48  48  LYS LYS C . n 
C 3 49  GLN 49  49  49  GLN GLN C . n 
C 3 50  LEU 50  50  50  LEU LEU C . n 
C 3 51  GLU 51  51  51  GLU GLU C . n 
C 3 52  ASP 52  52  52  ASP ASP C . n 
C 3 53  GLY 53  53  53  GLY GLY C . n 
C 3 54  ARG 54  54  54  ARG ARG C . n 
C 3 55  THR 55  55  55  THR THR C . n 
C 3 56  LEU 56  56  56  LEU LEU C . n 
C 3 57  SER 57  57  57  SER SER C . n 
C 3 58  ASP 58  58  58  ASP ASP C . n 
C 3 59  TYR 59  59  59  TYR TYR C . n 
C 3 60  ASN 60  60  60  ASN ASN C . n 
C 3 61  ILE 61  61  61  ILE ILE C . n 
C 3 62  GLN 62  62  62  GLN GLN C . n 
C 3 63  LYS 63  63  63  LYS LYS C . n 
C 3 64  GLU 64  64  64  GLU GLU C . n 
C 3 65  SER 65  65  65  SER SER C . n 
C 3 66  THR 66  66  66  THR THR C . n 
C 3 67  LEU 67  67  67  LEU LEU C . n 
C 3 68  HIS 68  68  68  HIS HIS C . n 
C 3 69  LEU 69  69  69  LEU LEU C . n 
C 3 70  VAL 70  70  70  VAL VAL C . n 
C 3 71  LEU 71  71  71  LEU LEU C . n 
C 3 72  ARG 72  72  72  ARG ARG C . n 
C 3 73  LEU 73  73  73  LEU LEU C . n 
C 3 74  ARG 74  74  74  ARG ARG C . n 
C 3 75  GLY 75  75  75  GLY GLY C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ANP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ANP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
D 4 ANP 1  401 401 ANP ANP A . 
E 5 AR6 1  101 101 AR6 AR6 C . 
F 6 HOH 1  501 29  HOH HOH A . 
F 6 HOH 2  502 11  HOH HOH A . 
F 6 HOH 3  503 25  HOH HOH A . 
F 6 HOH 4  504 68  HOH HOH A . 
F 6 HOH 5  505 17  HOH HOH A . 
F 6 HOH 6  506 27  HOH HOH A . 
F 6 HOH 7  507 21  HOH HOH A . 
F 6 HOH 8  508 75  HOH HOH A . 
F 6 HOH 9  509 51  HOH HOH A . 
F 6 HOH 10 510 34  HOH HOH A . 
F 6 HOH 11 511 31  HOH HOH A . 
F 6 HOH 12 512 82  HOH HOH A . 
F 6 HOH 13 513 23  HOH HOH A . 
F 6 HOH 14 514 59  HOH HOH A . 
F 6 HOH 15 515 73  HOH HOH A . 
F 6 HOH 16 516 61  HOH HOH A . 
F 6 HOH 17 517 49  HOH HOH A . 
F 6 HOH 18 518 53  HOH HOH A . 
F 6 HOH 19 519 74  HOH HOH A . 
F 6 HOH 20 520 52  HOH HOH A . 
F 6 HOH 21 521 13  HOH HOH A . 
F 6 HOH 22 522 46  HOH HOH A . 
F 6 HOH 23 523 93  HOH HOH A . 
F 6 HOH 24 524 58  HOH HOH A . 
F 6 HOH 25 525 55  HOH HOH A . 
F 6 HOH 26 526 54  HOH HOH A . 
F 6 HOH 27 527 78  HOH HOH A . 
F 6 HOH 28 528 43  HOH HOH A . 
F 6 HOH 29 529 94  HOH HOH A . 
F 6 HOH 30 530 77  HOH HOH A . 
F 6 HOH 31 531 64  HOH HOH A . 
F 6 HOH 32 532 87  HOH HOH A . 
F 6 HOH 33 533 19  HOH HOH A . 
F 6 HOH 34 534 88  HOH HOH A . 
F 6 HOH 35 535 38  HOH HOH A . 
F 6 HOH 36 536 95  HOH HOH A . 
F 6 HOH 37 537 98  HOH HOH A . 
F 6 HOH 38 538 72  HOH HOH A . 
F 6 HOH 39 539 99  HOH HOH A . 
G 6 HOH 1  401 26  HOH HOH B . 
G 6 HOH 2  402 89  HOH HOH B . 
G 6 HOH 3  403 20  HOH HOH B . 
G 6 HOH 4  404 83  HOH HOH B . 
G 6 HOH 5  405 67  HOH HOH B . 
G 6 HOH 6  406 14  HOH HOH B . 
G 6 HOH 7  407 37  HOH HOH B . 
G 6 HOH 8  408 69  HOH HOH B . 
G 6 HOH 9  409 47  HOH HOH B . 
G 6 HOH 10 410 36  HOH HOH B . 
G 6 HOH 11 411 15  HOH HOH B . 
G 6 HOH 12 412 33  HOH HOH B . 
G 6 HOH 13 413 84  HOH HOH B . 
G 6 HOH 14 414 12  HOH HOH B . 
G 6 HOH 15 415 39  HOH HOH B . 
G 6 HOH 16 416 8   HOH HOH B . 
G 6 HOH 17 417 80  HOH HOH B . 
G 6 HOH 18 418 70  HOH HOH B . 
G 6 HOH 19 419 48  HOH HOH B . 
G 6 HOH 20 420 85  HOH HOH B . 
G 6 HOH 21 421 92  HOH HOH B . 
G 6 HOH 22 422 60  HOH HOH B . 
G 6 HOH 23 423 91  HOH HOH B . 
G 6 HOH 24 424 16  HOH HOH B . 
G 6 HOH 25 425 62  HOH HOH B . 
G 6 HOH 26 426 35  HOH HOH B . 
G 6 HOH 27 427 44  HOH HOH B . 
G 6 HOH 28 428 30  HOH HOH B . 
G 6 HOH 29 429 86  HOH HOH B . 
G 6 HOH 30 430 42  HOH HOH B . 
G 6 HOH 31 431 65  HOH HOH B . 
G 6 HOH 32 432 57  HOH HOH B . 
G 6 HOH 33 433 97  HOH HOH B . 
G 6 HOH 34 434 81  HOH HOH B . 
G 6 HOH 35 435 41  HOH HOH B . 
G 6 HOH 36 436 56  HOH HOH B . 
G 6 HOH 37 437 40  HOH HOH B . 
H 6 HOH 1  201 100 HOH HOH C . 
H 6 HOH 2  202 66  HOH HOH C . 
H 6 HOH 3  203 101 HOH HOH C . 
H 6 HOH 4  204 9   HOH HOH C . 
H 6 HOH 5  205 32  HOH HOH C . 
H 6 HOH 6  206 102 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 N 1 C AR6 101 ? N1    ? E AR6 1 N1    
2  1 N 1 C AR6 101 ? C2    ? E AR6 1 C2    
3  1 N 1 C AR6 101 ? N3    ? E AR6 1 N3    
4  1 N 1 C AR6 101 ? C4    ? E AR6 1 C4    
5  1 N 1 C AR6 101 ? C5    ? E AR6 1 C5    
6  1 N 1 C AR6 101 ? C6    ? E AR6 1 C6    
7  1 N 1 C AR6 101 ? N6    ? E AR6 1 N6    
8  1 N 1 C AR6 101 ? N7    ? E AR6 1 N7    
9  1 N 1 C AR6 101 ? C8    ? E AR6 1 C8    
10 1 N 1 C AR6 101 ? N9    ? E AR6 1 N9    
11 1 N 1 C AR6 101 ? PA    ? E AR6 1 PA    
12 1 N 1 C AR6 101 ? "C1'" ? E AR6 1 "C1'" 
13 1 N 1 C AR6 101 ? O1A   ? E AR6 1 O1A   
14 1 N 1 C AR6 101 ? "C2'" ? E AR6 1 "C2'" 
15 1 N 1 C AR6 101 ? "O2'" ? E AR6 1 "O2'" 
16 1 N 1 C AR6 101 ? O2A   ? E AR6 1 O2A   
17 1 N 1 C AR6 101 ? "C3'" ? E AR6 1 "C3'" 
18 1 N 1 C AR6 101 ? "O3'" ? E AR6 1 "O3'" 
19 1 N 1 C AR6 101 ? "C4'" ? E AR6 1 "C4'" 
20 1 N 1 C AR6 101 ? "O4'" ? E AR6 1 "O4'" 
21 1 N 1 C AR6 101 ? "C5'" ? E AR6 1 "C5'" 
22 1 N 1 C AR6 101 ? "O5'" ? E 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   ? ? ? '(1.18_3845: ???)' 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                     8K6E 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     215.317 
_cell.length_a_esd                 ? 
_cell.length_b                     55.152 
_cell.length_b_esd                 ? 
_cell.length_c                     80.907 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8K6E 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   8K6E 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.64 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.39 
_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    'PEG 8000; Sodium chloride; Sodium HEPES' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-02 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979191 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979191 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8K6E 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.74 
_reflns.d_resolution_low                               107.7 
_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                                     26157 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           96 
_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                          10.97 
_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                                0.069 
_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                                   0.993 
_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                                    2.74 
_reflns_shell.d_res_low                                     2.83 
_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                             25220 
_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                                  0.831 
_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                                 8K6E 
_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                            2.74 
_refine.ls_d_res_low                             64.68 
_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                     25354 
_refine.ls_number_reflns_R_free                  1240 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.24 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1912 
_refine.ls_R_factor_R_free                       0.2455 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1883 
_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                          0.23 
_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                 24.72 
_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                            0.36 
_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                       2.74 
_refine_hist.d_res_low                        64.68 
_refine_hist.number_atoms_solvent             82 
_refine_hist.number_atoms_total               6404 
_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        6322 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.010 ? 6451 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.214 ? 8725 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 9.324 ? 856  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.060 ? 980  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007 ? 1112 ? 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' 2.74 2.84  . . 109 2548 93.00 . . . . 0.2456 . . . . . . . . . . . 0.3473 
'X-RAY DIFFRACTION' 2.84 2.97  . . 124 2587 94.00 . . . . 0.2357 . . . . . . . . . . . 0.3040 
'X-RAY DIFFRACTION' 2.97 3.13  . . 127 2613 96.00 . . . . 0.2352 . . . . . . . . . . . 0.2922 
'X-RAY DIFFRACTION' 3.13 3.33  . . 151 2634 97.00 . . . . 0.2233 . . . . . . . . . . . 0.3140 
'X-RAY DIFFRACTION' 3.33 3.58  . . 130 2686 97.00 . . . . 0.2024 . . . . . . . . . . . 0.2789 
'X-RAY DIFFRACTION' 3.58 3.94  . . 147 2629 95.00 . . . . 0.2023 . . . . . . . . . . . 0.3125 
'X-RAY DIFFRACTION' 3.94 4.52  . . 158 2730 99.00 . . . . 0.1505 . . . . . . . . . . . 0.1937 
'X-RAY DIFFRACTION' 4.52 5.69  . . 148 2778 99.00 . . . . 0.1503 . . . . . . . . . . . 0.1778 
'X-RAY DIFFRACTION' 5.69 64.68 . . 146 2909 98.00 . . . . 0.1764 . . . . . . . . . . . 0.2101 
# 
_struct.entry_id                     8K6E 
_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        8K6E 
_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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 6 ? 
H 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 8K6E             8K6E       ? 2 ? 1 
3 UNP J3QS39_HUMAN     J3QS39     ? 3 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRG 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 8K6E A 1 ? 375 ? A0A8C6VAB1 1  ? 375 ? 1  375 
2 2 8K6E B 1 ? 352 ? 8K6E       19 ? 370 ? 19 370 
3 3 8K6E C 1 ? 75  ? J3QS39     1  ? 75  ? 1  75  
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5630  ? 
1 MORE         -20   ? 
1 'SSA (A^2)'  33970 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 55  ? LYS A 61  ? GLY A 55  LYS A 61  1 ? 7  
HELX_P HELX_P2  AA2 ASN A 78  ? ASN A 92  ? ASN A 78  ASN A 92  1 ? 15 
HELX_P HELX_P3  AA3 ALA A 97  ? HIS A 101 ? ALA A 97  HIS A 101 5 ? 5  
HELX_P HELX_P4  AA4 PRO A 112 ? THR A 126 ? PRO A 112 THR A 126 1 ? 15 
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 ? GLY A 197 ? ALA A 181 GLY A 197 1 ? 17 
HELX_P HELX_P7  AA7 THR A 202 ? CYS A 217 ? THR A 202 CYS A 217 1 ? 16 
HELX_P HELX_P8  AA8 ASP A 222 ? SER A 233 ? ASP A 222 SER A 233 1 ? 12 
HELX_P HELX_P9  AA9 ASN A 252 ? CYS A 257 ? ASN A 252 CYS A 257 1 ? 6  
HELX_P HELX_P10 AB1 PRO A 258 ? PHE A 262 ? PRO A 258 PHE A 262 5 ? 5  
HELX_P HELX_P11 AB2 GLN A 263 ? GLY A 268 ? GLN A 263 GLY A 268 5 ? 6  
HELX_P HELX_P12 AB3 GLY A 273 ? LYS A 284 ? GLY A 273 LYS A 284 1 ? 12 
HELX_P HELX_P13 AB4 CYS A 285 ? ASP A 288 ? CYS A 285 ASP A 288 5 ? 4  
HELX_P HELX_P14 AB5 ILE A 289 ? ALA A 295 ? ILE A 289 ALA A 295 1 ? 7  
HELX_P HELX_P15 AB6 GLY A 301 ? TYR A 306 ? GLY A 301 TYR A 306 5 ? 6  
HELX_P HELX_P16 AB7 GLY A 308 ? ALA A 321 ? GLY A 308 ALA A 321 1 ? 14 
HELX_P HELX_P17 AB8 GLU A 334 ? LYS A 336 ? GLU A 334 LYS A 336 5 ? 3  
HELX_P HELX_P18 AB9 TYR A 337 ? LEU A 349 ? TYR A 337 LEU A 349 1 ? 13 
HELX_P HELX_P19 AC1 SER A 350 ? MET A 355 ? SER A 350 MET A 355 5 ? 6  
HELX_P HELX_P20 AC2 LYS A 359 ? GLY A 366 ? LYS A 359 GLY A 366 1 ? 8  
HELX_P HELX_P21 AC3 ILE A 369 ? CYS A 374 ? ILE A 369 CYS A 374 1 ? 6  
HELX_P HELX_P22 AC4 ILE B 6   ? ASP B 15  ? ILE B 24  ASP B 33  1 ? 10 
HELX_P HELX_P23 AC5 ASP B 20  ? LEU B 36  ? ASP B 38  LEU B 54  1 ? 17 
HELX_P HELX_P24 AC6 LYS B 39  ? GLU B 41  ? LYS B 57  GLU B 59  5 ? 3  
HELX_P HELX_P25 AC7 PHE B 42  ? LYS B 55  ? PHE B 60  LYS B 73  1 ? 14 
HELX_P HELX_P26 AC8 ASN B 57  ? LYS B 71  ? ASN B 75  LYS B 89  1 ? 15 
HELX_P HELX_P27 AC9 ASN B 72  ? LEU B 76  ? ASN B 90  LEU B 94  5 ? 5  
HELX_P HELX_P28 AD1 SER B 77  ? ALA B 88  ? SER B 95  ALA B 106 1 ? 12 
HELX_P HELX_P29 AD2 PRO B 89  ? LEU B 91  ? PRO B 107 LEU B 109 5 ? 3  
HELX_P HELX_P30 AD3 ASN B 98  ? SER B 120 ? ASN B 116 SER B 138 1 ? 23 
HELX_P HELX_P31 AD4 LEU B 122 ? LYS B 136 ? LEU B 140 LYS B 154 1 ? 15 
HELX_P HELX_P32 AD5 THR B 149 ? SER B 159 ? THR B 167 SER B 177 1 ? 11 
HELX_P HELX_P33 AD6 PHE B 160 ? ASN B 164 ? PHE B 178 ASN B 182 5 ? 5  
HELX_P HELX_P34 AD7 GLU B 168 ? ALA B 173 ? GLU B 186 ALA B 191 1 ? 6  
HELX_P HELX_P35 AD8 ARG B 177 ? LYS B 181 ? ARG B 195 LYS B 199 5 ? 5  
HELX_P HELX_P36 AD9 GLY B 228 ? LYS B 233 ? GLY B 246 LYS B 251 1 ? 6  
HELX_P HELX_P37 AE1 GLY B 244 ? LYS B 259 ? GLY B 262 LYS B 277 1 ? 16 
HELX_P HELX_P38 AE2 ASP B 265 ? GLU B 284 ? ASP B 283 GLU B 302 1 ? 20 
HELX_P HELX_P39 AE3 SER B 288 ? THR B 297 ? SER B 306 THR B 315 1 ? 10 
HELX_P HELX_P40 AE4 GLU B 298 ? LYS B 307 ? GLU B 316 LYS B 325 1 ? 10 
HELX_P HELX_P41 AE5 THR B 320 ? ASN B 350 ? THR B 338 ASN B 368 1 ? 31 
HELX_P HELX_P42 AE6 THR C 22  ? GLY C 35  ? THR C 22  GLY C 35  1 ? 14 
HELX_P HELX_P43 AE7 PRO C 37  ? ASP C 39  ? PRO C 37  ASP C 39  5 ? 3  
HELX_P HELX_P44 AE8 LEU C 56  ? ASN C 60  ? LEU C 56  ASN C 60  5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        none 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           C 
_struct_conn.ptnr1_label_comp_id           ARG 
_struct_conn.ptnr1_label_seq_id            42 
_struct_conn.ptnr1_label_atom_id           NH1 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           E 
_struct_conn.ptnr2_label_comp_id           AR6 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           O1D 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            C 
_struct_conn.ptnr1_auth_comp_id            ARG 
_struct_conn.ptnr1_auth_seq_id             42 
_struct_conn.ptnr2_auth_asym_id            C 
_struct_conn.ptnr2_auth_comp_id            AR6 
_struct_conn.ptnr2_auth_seq_id             101 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.302 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      AR6 
_pdbx_modification_feature.label_asym_id                      E 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     ARG 
_pdbx_modification_feature.modified_residue_label_asym_id     C 
_pdbx_modification_feature.modified_residue_label_seq_id      42 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       AR6 
_pdbx_modification_feature.auth_asym_id                       C 
_pdbx_modification_feature.auth_seq_id                        101 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      ARG 
_pdbx_modification_feature.modified_residue_auth_asym_id      C 
_pdbx_modification_feature.modified_residue_auth_seq_id       42 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               O1D 
_pdbx_modification_feature.modified_residue_id_linking_atom   NH1 
_pdbx_modification_feature.modified_residue_id                ARG 
_pdbx_modification_feature.ref_pcm_id                         14 
_pdbx_modification_feature.ref_comp_id                        AR6 
_pdbx_modification_feature.type                               ADP-ribosylation 
_pdbx_modification_feature.category                           ADP-ribose 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 29  ? PRO A 32  ? ALA A 29  PRO A 32  
AA1 2 MET A 16  ? PHE A 21  ? MET A 16  PHE A 21  
AA1 3 LEU A 8   ? ASN A 12  ? LEU A 8   ASN A 12  
AA1 4 VAL A 103 ? GLU A 107 ? VAL A 103 GLU A 107 
AA1 5 ALA A 131 ? ILE A 136 ? ALA A 131 ILE A 136 
AA1 6 ILE A 357 ? SER A 358 ? ILE A 357 SER A 358 
AA2 1 TYR A 53  ? VAL A 54  ? TYR A 53  VAL A 54  
AA2 2 VAL A 35  ? PRO A 38  ? VAL A 35  PRO A 38  
AA2 3 LEU A 65  ? LYS A 68  ? LEU A 65  LYS A 68  
AA3 1 TYR A 169 ? ALA A 170 ? TYR A 169 ALA A 170 
AA3 2 THR A 160 ? TYR A 166 ? THR A 160 TYR A 166 
AA3 3 LEU A 176 ? LEU A 178 ? LEU A 176 LEU A 178 
AA4 1 TYR A 169 ? ALA A 170 ? TYR A 169 ALA A 170 
AA4 2 THR A 160 ? TYR A 166 ? THR A 160 TYR A 166 
AA4 3 GLY A 150 ? SER A 155 ? GLY A 150 SER A 155 
AA4 4 THR A 297 ? SER A 300 ? THR A 297 SER A 300 
AA4 5 ILE A 329 ? ILE A 330 ? ILE A 329 ILE A 330 
AA5 1 LYS A 238 ? GLU A 241 ? LYS A 238 GLU A 241 
AA5 2 VAL A 247 ? ILE A 250 ? VAL A 247 ILE A 250 
AA6 1 ASN B 190 ? SER B 193 ? ASN B 208 SER B 211 
AA6 2 ARG B 214 ? PRO B 217 ? ARG B 232 PRO B 235 
AA7 1 THR C 12  ? GLU C 16  ? THR C 12  GLU C 16  
AA7 2 GLN C 2   ? THR C 7   ? GLN C 2   THR C 7   
AA7 3 THR C 66  ? LEU C 71  ? THR C 66  LEU C 71  
AA7 4 GLN C 41  ? PHE C 45  ? GLN C 41  PHE C 45  
AA7 5 LYS C 48  ? GLN C 49  ? LYS C 48  GLN C 49  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 29  ? O ALA A 29  N ALA A 19  ? N ALA A 19  
AA1 2 3 O LYS A 18  ? O LYS A 18  N ASP A 11  ? N ASP A 11  
AA1 3 4 N LEU A 8   ? N LEU A 8   O LEU A 104 ? O LEU A 104 
AA1 4 5 N LEU A 105 ? N LEU A 105 O TYR A 133 ? O TYR A 133 
AA1 5 6 N MET A 132 ? N MET A 132 O ILE A 357 ? O ILE A 357 
AA2 1 2 O TYR A 53  ? O TYR A 53  N GLY A 36  ? N GLY A 36  
AA2 2 3 N ARG A 37  ? N ARG A 37  O THR A 66  ? O THR A 66  
AA3 1 2 O TYR A 169 ? O TYR A 169 N TYR A 166 ? N TYR A 166 
AA3 2 3 N THR A 160 ? N THR A 160 O LEU A 178 ? O LEU A 178 
AA4 1 2 O TYR A 169 ? O TYR A 169 N TYR A 166 ? N TYR A 166 
AA4 2 3 O ILE A 165 ? O ILE A 165 N GLY A 150 ? N GLY A 150 
AA4 3 4 N MET A 153 ? N MET A 153 O VAL A 298 ? O VAL A 298 
AA4 4 5 N THR A 297 ? N THR A 297 O ILE A 330 ? O ILE A 330 
AA5 1 2 N TYR A 240 ? N TYR A 240 O ILE A 248 ? O ILE A 248 
AA6 1 2 N SER B 193 ? N SER B 211 O ARG B 214 ? O ARG B 232 
AA7 1 2 O ILE C 13  ? O ILE C 13  N VAL C 5   ? N VAL C 5   
AA7 2 3 N LYS C 6   ? N LYS C 6   O LEU C 69  ? O LEU C 69  
AA7 3 4 O HIS C 68  ? O HIS C 68  N ILE C 44  ? N ILE C 44  
AA7 4 5 N PHE C 45  ? N PHE C 45  O LYS C 48  ? O LYS C 48  
# 
_pdbx_entry_details.entry_id                   8K6E 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   CZ 
_pdbx_validate_close_contact.auth_asym_id_1   C 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    42 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O1D 
_pdbx_validate_close_contact.auth_asym_id_2   C 
_pdbx_validate_close_contact.auth_comp_id_2   AR6 
_pdbx_validate_close_contact.auth_seq_id_2    101 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.08 
# 
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 CB A PRO 112 ? ? CA A PRO 112 ? ? C   A PRO 112 ? ? 125.59 111.70 13.89 2.10 N 
2 1 CB A ASP 222 ? ? CG A ASP 222 ? ? OD2 A ASP 222 ? ? 111.74 118.30 -6.56 0.90 N 
3 1 CB B LYS 58  ? ? CA B LYS 58  ? ? C   B LYS 58  ? ? 133.03 110.40 22.63 2.00 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 ILE A 71  ? ? -142.09 41.48   
2  1 PRO A 112 ? ? -49.04  154.34  
3  1 GLU A 167 ? ? 39.41   56.92   
4  1 ASP A 179 ? ? -87.79  48.91   
5  1 GLU A 270 ? ? -91.67  39.02   
6  1 ASN A 296 ? ? -148.81 44.90   
7  1 ASN B 75  ? ? -99.97  58.76   
8  1 LEU B 94  ? ? -126.80 -167.87 
9  1 ASP B 115 ? ? -145.43 48.45   
10 1 ASN B 116 ? ? -109.55 64.07   
11 1 ASN B 184 ? ? -158.03 -81.20  
12 1 ASP B 200 ? ? -144.49 41.02   
13 1 GLU B 241 ? ? 71.37   -14.23  
14 1 ALA B 258 ? ? -156.32 20.51   
15 1 SER B 259 ? ? 78.27   -142.81 
16 1 ASN B 327 ? ? 71.58   37.93   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A GLU 2   ? A GLU 2   
3  1 Y 1 A GLU 3   ? A GLU 3   
4  1 Y 1 A GLU 4   ? A GLU 4   
5  1 Y 1 A ILE 5   ? A ILE 5   
6  1 Y 1 A GLY 48  ? A GLY 48  
7  1 Y 1 A GLN 49  ? A GLN 49  
8  1 Y 1 A LYS 50  ? A LYS 50  
9  1 Y 1 B MET 19  ? B MET 1   
10 1 Y 1 B SER 20  ? B SER 2   
11 1 Y 1 B TYR 21  ? B TYR 3   
12 1 Y 1 B GLN 22  ? B GLN 4   
13 1 Y 1 B GLU 370 ? B GLU 352 
# 
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  
ANP PG     P N N 14  
ANP O1G    O N N 15  
ANP O2G    O N N 16  
ANP O3G    O N N 17  
ANP PB     P N N 18  
ANP O1B    O N N 19  
ANP O2B    O N N 20  
ANP N3B    N N N 21  
ANP PA     P N N 22  
ANP O1A    O N N 23  
ANP O2A    O N N 24  
ANP O3A    O N N 25  
ANP "O5'"  O N N 26  
ANP "C5'"  C N N 27  
ANP "C4'"  C N R 28  
ANP "O4'"  O N N 29  
ANP "C3'"  C N S 30  
ANP "O3'"  O N N 31  
ANP "C2'"  C N R 32  
ANP "O2'"  O N N 33  
ANP "C1'"  C N R 34  
ANP N9     N Y N 35  
ANP C8     C Y N 36  
ANP N7     N Y N 37  
ANP C5     C Y N 38  
ANP C6     C Y N 39  
ANP N6     N N N 40  
ANP N1     N Y N 41  
ANP C2     C Y N 42  
ANP N3     N Y N 43  
ANP C4     C Y N 44  
ANP HOG2   H N N 45  
ANP HOG3   H N N 46  
ANP HOB2   H N N 47  
ANP HNB1   H N N 48  
ANP HOA2   H N N 49  
ANP "H5'1" H N N 50  
ANP "H5'2" H N N 51  
ANP "H4'"  H N N 52  
ANP "H3'"  H N N 53  
ANP "HO3'" H N N 54  
ANP "H2'"  H N N 55  
ANP "HO2'" H N N 56  
ANP "H1'"  H N N 57  
ANP H8     H N N 58  
ANP HN61   H N N 59  
ANP HN62   H N N 60  
ANP H2     H N N 61  
AR6 N1     N Y N 62  
AR6 C2     C Y N 63  
AR6 N3     N Y N 64  
AR6 C4     C Y N 65  
AR6 C5     C Y N 66  
AR6 C6     C Y N 67  
AR6 N6     N N N 68  
AR6 N7     N Y N 69  
AR6 C8     C Y N 70  
AR6 N9     N Y N 71  
AR6 PA     P N N 72  
AR6 PB     P N N 73  
AR6 "C1'"  C N R 74  
AR6 O1A    O N N 75  
AR6 O1B    O N N 76  
AR6 C1D    C N S 77  
AR6 O1D    O N N 78  
AR6 "C2'"  C N R 79  
AR6 "O2'"  O N N 80  
AR6 O2A    O N N 81  
AR6 O2B    O N N 82  
AR6 C2D    C N R 83  
AR6 O2D    O N N 84  
AR6 "C3'"  C N S 85  
AR6 "O3'"  O N N 86  
AR6 O3A    O N N 87  
AR6 C3D    C N S 88  
AR6 O3D    O N N 89  
AR6 "C4'"  C N R 90  
AR6 "O4'"  O N N 91  
AR6 C4D    C N R 92  
AR6 O4D    O N N 93  
AR6 "C5'"  C N N 94  
AR6 "O5'"  O N N 95  
AR6 C5D    C N N 96  
AR6 O5D    O N N 97  
AR6 H2     H N N 98  
AR6 HN6    H N N 99  
AR6 HN6A   H N N 100 
AR6 H8     H N N 101 
AR6 "H1'"  H N N 102 
AR6 H1D    H N N 103 
AR6 "H2'"  H N N 104 
AR6 "HO2'" H N N 105 
AR6 H2D    H N N 106 
AR6 HO2D   H N N 107 
AR6 "H3'"  H N N 108 
AR6 "HO3'" H N N 109 
AR6 H3D    H N N 110 
AR6 HO3D   H N N 111 
AR6 "H4'"  H N N 112 
AR6 H4D    H N N 113 
AR6 "H5'"  H N N 114 
AR6 "H5'A" H N N 115 
AR6 H5D    H N N 116 
AR6 H5DA   H N N 117 
AR6 H1A    H N N 118 
AR6 H1B    H N N 119 
AR6 HD1    H N N 120 
ARG N      N N N 121 
ARG CA     C N S 122 
ARG C      C N N 123 
ARG O      O N N 124 
ARG CB     C N N 125 
ARG CG     C N N 126 
ARG CD     C N N 127 
ARG NE     N N N 128 
ARG CZ     C N N 129 
ARG NH1    N N N 130 
ARG NH2    N N N 131 
ARG OXT    O N N 132 
ARG H      H N N 133 
ARG H2     H N N 134 
ARG HA     H N N 135 
ARG HB2    H N N 136 
ARG HB3    H N N 137 
ARG HG2    H N N 138 
ARG HG3    H N N 139 
ARG HD2    H N N 140 
ARG HD3    H N N 141 
ARG HE     H N N 142 
ARG HH11   H N N 143 
ARG HH12   H N N 144 
ARG HH21   H N N 145 
ARG HH22   H N N 146 
ARG HXT    H N N 147 
ASN N      N N N 148 
ASN CA     C N S 149 
ASN C      C N N 150 
ASN O      O N N 151 
ASN CB     C N N 152 
ASN CG     C N N 153 
ASN OD1    O N N 154 
ASN ND2    N N N 155 
ASN OXT    O N N 156 
ASN H      H N N 157 
ASN H2     H N N 158 
ASN HA     H N N 159 
ASN HB2    H N N 160 
ASN HB3    H N N 161 
ASN HD21   H N N 162 
ASN HD22   H N N 163 
ASN HXT    H N N 164 
ASP N      N N N 165 
ASP CA     C N S 166 
ASP C      C N N 167 
ASP O      O N N 168 
ASP CB     C N N 169 
ASP CG     C N N 170 
ASP OD1    O N N 171 
ASP OD2    O N N 172 
ASP OXT    O N N 173 
ASP H      H N N 174 
ASP H2     H N N 175 
ASP HA     H N N 176 
ASP HB2    H N N 177 
ASP HB3    H N N 178 
ASP HD2    H N N 179 
ASP HXT    H N N 180 
CYS N      N N N 181 
CYS CA     C N R 182 
CYS C      C N N 183 
CYS O      O N N 184 
CYS CB     C N N 185 
CYS SG     S N N 186 
CYS OXT    O N N 187 
CYS H      H N N 188 
CYS H2     H N N 189 
CYS HA     H N N 190 
CYS HB2    H N N 191 
CYS HB3    H N N 192 
CYS HG     H N N 193 
CYS HXT    H N N 194 
GLN N      N N N 195 
GLN CA     C N S 196 
GLN C      C N N 197 
GLN O      O N N 198 
GLN CB     C N N 199 
GLN CG     C N N 200 
GLN CD     C N N 201 
GLN OE1    O N N 202 
GLN NE2    N N N 203 
GLN OXT    O N N 204 
GLN H      H N N 205 
GLN H2     H N N 206 
GLN HA     H N N 207 
GLN HB2    H N N 208 
GLN HB3    H N N 209 
GLN HG2    H N N 210 
GLN HG3    H N N 211 
GLN HE21   H N N 212 
GLN HE22   H N N 213 
GLN HXT    H N N 214 
GLU N      N N N 215 
GLU CA     C N S 216 
GLU C      C N N 217 
GLU O      O N N 218 
GLU CB     C N N 219 
GLU CG     C N N 220 
GLU CD     C N N 221 
GLU OE1    O N N 222 
GLU OE2    O N N 223 
GLU OXT    O N N 224 
GLU H      H N N 225 
GLU H2     H N N 226 
GLU HA     H N N 227 
GLU HB2    H N N 228 
GLU HB3    H N N 229 
GLU HG2    H N N 230 
GLU HG3    H N N 231 
GLU HE2    H N N 232 
GLU HXT    H N N 233 
GLY N      N N N 234 
GLY CA     C N N 235 
GLY C      C N N 236 
GLY O      O N N 237 
GLY OXT    O N N 238 
GLY H      H N N 239 
GLY H2     H N N 240 
GLY HA2    H N N 241 
GLY HA3    H N N 242 
GLY HXT    H N N 243 
HIS N      N N N 244 
HIS CA     C N S 245 
HIS C      C N N 246 
HIS O      O N N 247 
HIS CB     C N N 248 
HIS CG     C Y N 249 
HIS ND1    N Y N 250 
HIS CD2    C Y N 251 
HIS CE1    C Y N 252 
HIS NE2    N Y N 253 
HIS OXT    O N N 254 
HIS H      H N N 255 
HIS H2     H N N 256 
HIS HA     H N N 257 
HIS HB2    H N N 258 
HIS HB3    H N N 259 
HIS HD1    H N N 260 
HIS HD2    H N N 261 
HIS HE1    H N N 262 
HIS HE2    H N N 263 
HIS HXT    H N N 264 
HOH O      O N N 265 
HOH H1     H N N 266 
HOH H2     H N N 267 
ILE N      N N N 268 
ILE CA     C N S 269 
ILE C      C N N 270 
ILE O      O N N 271 
ILE CB     C N S 272 
ILE CG1    C N N 273 
ILE CG2    C N N 274 
ILE CD1    C N N 275 
ILE OXT    O N N 276 
ILE H      H N N 277 
ILE H2     H N N 278 
ILE HA     H N N 279 
ILE HB     H N N 280 
ILE HG12   H N N 281 
ILE HG13   H N N 282 
ILE HG21   H N N 283 
ILE HG22   H N N 284 
ILE HG23   H N N 285 
ILE HD11   H N N 286 
ILE HD12   H N N 287 
ILE HD13   H N N 288 
ILE HXT    H N N 289 
LEU N      N N N 290 
LEU CA     C N S 291 
LEU C      C N N 292 
LEU O      O N N 293 
LEU CB     C N N 294 
LEU CG     C N N 295 
LEU CD1    C N N 296 
LEU CD2    C N N 297 
LEU OXT    O N N 298 
LEU H      H N N 299 
LEU H2     H N N 300 
LEU HA     H N N 301 
LEU HB2    H N N 302 
LEU HB3    H N N 303 
LEU HG     H N N 304 
LEU HD11   H N N 305 
LEU HD12   H N N 306 
LEU HD13   H N N 307 
LEU HD21   H N N 308 
LEU HD22   H N N 309 
LEU HD23   H N N 310 
LEU HXT    H N N 311 
LYS N      N N N 312 
LYS CA     C N S 313 
LYS C      C N N 314 
LYS O      O N N 315 
LYS CB     C N N 316 
LYS CG     C N N 317 
LYS CD     C N N 318 
LYS CE     C N N 319 
LYS NZ     N N N 320 
LYS OXT    O N N 321 
LYS H      H N N 322 
LYS H2     H N N 323 
LYS HA     H N N 324 
LYS HB2    H N N 325 
LYS HB3    H N N 326 
LYS HG2    H N N 327 
LYS HG3    H N N 328 
LYS HD2    H N N 329 
LYS HD3    H N N 330 
LYS HE2    H N N 331 
LYS HE3    H N N 332 
LYS HZ1    H N N 333 
LYS HZ2    H N N 334 
LYS HZ3    H N N 335 
LYS HXT    H N N 336 
MET N      N N N 337 
MET CA     C N S 338 
MET C      C N N 339 
MET O      O N N 340 
MET CB     C N N 341 
MET CG     C N N 342 
MET SD     S N N 343 
MET CE     C N N 344 
MET OXT    O N N 345 
MET H      H N N 346 
MET H2     H N N 347 
MET HA     H N N 348 
MET HB2    H N N 349 
MET HB3    H N N 350 
MET HG2    H N N 351 
MET HG3    H N N 352 
MET HE1    H N N 353 
MET HE2    H N N 354 
MET HE3    H N N 355 
MET HXT    H N N 356 
PHE N      N N N 357 
PHE CA     C N S 358 
PHE C      C N N 359 
PHE O      O N N 360 
PHE CB     C N N 361 
PHE CG     C Y N 362 
PHE CD1    C Y N 363 
PHE CD2    C Y N 364 
PHE CE1    C Y N 365 
PHE CE2    C Y N 366 
PHE CZ     C Y N 367 
PHE OXT    O N N 368 
PHE H      H N N 369 
PHE H2     H N N 370 
PHE HA     H N N 371 
PHE HB2    H N N 372 
PHE HB3    H N N 373 
PHE HD1    H N N 374 
PHE HD2    H N N 375 
PHE HE1    H N N 376 
PHE HE2    H N N 377 
PHE HZ     H N N 378 
PHE HXT    H N N 379 
PRO N      N N N 380 
PRO CA     C N S 381 
PRO C      C N N 382 
PRO O      O N N 383 
PRO CB     C N N 384 
PRO CG     C N N 385 
PRO CD     C N N 386 
PRO OXT    O N N 387 
PRO H      H N N 388 
PRO HA     H N N 389 
PRO HB2    H N N 390 
PRO HB3    H N N 391 
PRO HG2    H N N 392 
PRO HG3    H N N 393 
PRO HD2    H N N 394 
PRO HD3    H N N 395 
PRO HXT    H N N 396 
SER N      N N N 397 
SER CA     C N S 398 
SER C      C N N 399 
SER O      O N N 400 
SER CB     C N N 401 
SER OG     O N N 402 
SER OXT    O N N 403 
SER H      H N N 404 
SER H2     H N N 405 
SER HA     H N N 406 
SER HB2    H N N 407 
SER HB3    H N N 408 
SER HG     H N N 409 
SER HXT    H N N 410 
THR N      N N N 411 
THR CA     C N S 412 
THR C      C N N 413 
THR O      O N N 414 
THR CB     C N R 415 
THR OG1    O N N 416 
THR CG2    C N N 417 
THR OXT    O N N 418 
THR H      H N N 419 
THR H2     H N N 420 
THR HA     H N N 421 
THR HB     H N N 422 
THR HG1    H N N 423 
THR HG21   H N N 424 
THR HG22   H N N 425 
THR HG23   H N N 426 
THR HXT    H N N 427 
TRP N      N N N 428 
TRP CA     C N S 429 
TRP C      C N N 430 
TRP O      O N N 431 
TRP CB     C N N 432 
TRP CG     C Y N 433 
TRP CD1    C Y N 434 
TRP CD2    C Y N 435 
TRP NE1    N Y N 436 
TRP CE2    C Y N 437 
TRP CE3    C Y N 438 
TRP CZ2    C Y N 439 
TRP CZ3    C Y N 440 
TRP CH2    C Y N 441 
TRP OXT    O N N 442 
TRP H      H N N 443 
TRP H2     H N N 444 
TRP HA     H N N 445 
TRP HB2    H N N 446 
TRP HB3    H N N 447 
TRP HD1    H N N 448 
TRP HE1    H N N 449 
TRP HE3    H N N 450 
TRP HZ2    H N N 451 
TRP HZ3    H N N 452 
TRP HH2    H N N 453 
TRP HXT    H N N 454 
TYR N      N N N 455 
TYR CA     C N S 456 
TYR C      C N N 457 
TYR O      O N N 458 
TYR CB     C N N 459 
TYR CG     C Y N 460 
TYR CD1    C Y N 461 
TYR CD2    C Y N 462 
TYR CE1    C Y N 463 
TYR CE2    C Y N 464 
TYR CZ     C Y N 465 
TYR OH     O N N 466 
TYR OXT    O N N 467 
TYR H      H N N 468 
TYR H2     H N N 469 
TYR HA     H N N 470 
TYR HB2    H N N 471 
TYR HB3    H N N 472 
TYR HD1    H N N 473 
TYR HD2    H N N 474 
TYR HE1    H N N 475 
TYR HE2    H N N 476 
TYR HH     H N N 477 
TYR HXT    H N N 478 
VAL N      N N N 479 
VAL CA     C N S 480 
VAL C      C N N 481 
VAL O      O N N 482 
VAL CB     C N N 483 
VAL CG1    C N N 484 
VAL CG2    C N N 485 
VAL OXT    O N N 486 
VAL H      H N N 487 
VAL H2     H N N 488 
VAL HA     H N N 489 
VAL HB     H N N 490 
VAL HG11   H N N 491 
VAL HG12   H N N 492 
VAL HG13   H N N 493 
VAL HG21   H N N 494 
VAL HG22   H N N 495 
VAL HG23   H N N 496 
VAL HXT    H N N 497 
# 
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  
ANP PG    O1G    doub N N 13  
ANP PG    O2G    sing N N 14  
ANP PG    O3G    sing N N 15  
ANP PG    N3B    sing N N 16  
ANP O2G   HOG2   sing N N 17  
ANP O3G   HOG3   sing N N 18  
ANP PB    O1B    doub N N 19  
ANP PB    O2B    sing N N 20  
ANP PB    N3B    sing N N 21  
ANP PB    O3A    sing N N 22  
ANP O2B   HOB2   sing N N 23  
ANP N3B   HNB1   sing N N 24  
ANP PA    O1A    doub N N 25  
ANP PA    O2A    sing N N 26  
ANP PA    O3A    sing N N 27  
ANP PA    "O5'"  sing N N 28  
ANP O2A   HOA2   sing N N 29  
ANP "O5'" "C5'"  sing N N 30  
ANP "C5'" "C4'"  sing N N 31  
ANP "C5'" "H5'1" sing N N 32  
ANP "C5'" "H5'2" sing N N 33  
ANP "C4'" "O4'"  sing N N 34  
ANP "C4'" "C3'"  sing N N 35  
ANP "C4'" "H4'"  sing N N 36  
ANP "O4'" "C1'"  sing N N 37  
ANP "C3'" "O3'"  sing N N 38  
ANP "C3'" "C2'"  sing N N 39  
ANP "C3'" "H3'"  sing N N 40  
ANP "O3'" "HO3'" sing N N 41  
ANP "C2'" "O2'"  sing N N 42  
ANP "C2'" "C1'"  sing N N 43  
ANP "C2'" "H2'"  sing N N 44  
ANP "O2'" "HO2'" sing N N 45  
ANP "C1'" N9     sing N N 46  
ANP "C1'" "H1'"  sing N N 47  
ANP N9    C8     sing Y N 48  
ANP N9    C4     sing Y N 49  
ANP C8    N7     doub Y N 50  
ANP C8    H8     sing N N 51  
ANP N7    C5     sing Y N 52  
ANP C5    C6     sing Y N 53  
ANP C5    C4     doub Y N 54  
ANP C6    N6     sing N N 55  
ANP C6    N1     doub Y N 56  
ANP N6    HN61   sing N N 57  
ANP N6    HN62   sing N N 58  
ANP N1    C2     sing Y N 59  
ANP C2    N3     doub Y N 60  
ANP C2    H2     sing N N 61  
ANP N3    C4     sing Y N 62  
AR6 N1    C2     doub Y N 63  
AR6 N1    C6     sing Y N 64  
AR6 C2    N3     sing Y N 65  
AR6 N3    C4     doub Y N 66  
AR6 C4    C5     sing Y N 67  
AR6 C4    N9     sing Y N 68  
AR6 C5    C6     doub Y N 69  
AR6 C5    N7     sing Y N 70  
AR6 C6    N6     sing N N 71  
AR6 N7    C8     doub Y N 72  
AR6 C8    N9     sing Y N 73  
AR6 N9    "C1'"  sing N N 74  
AR6 PA    O1A    sing N N 75  
AR6 PA    O2A    doub N N 76  
AR6 PA    O3A    sing N N 77  
AR6 PA    "O5'"  sing N N 78  
AR6 PB    O1B    sing N N 79  
AR6 PB    O2B    doub N N 80  
AR6 PB    O3A    sing N N 81  
AR6 PB    O5D    sing N N 82  
AR6 "C1'" "C2'"  sing N N 83  
AR6 "C1'" "O4'"  sing N N 84  
AR6 C1D   O1D    sing N N 85  
AR6 C1D   C2D    sing N N 86  
AR6 C1D   O4D    sing N N 87  
AR6 "C2'" "O2'"  sing N N 88  
AR6 "C2'" "C3'"  sing N N 89  
AR6 C2D   O2D    sing N N 90  
AR6 C2D   C3D    sing N N 91  
AR6 "C3'" "O3'"  sing N N 92  
AR6 "C3'" "C4'"  sing N N 93  
AR6 C3D   O3D    sing N N 94  
AR6 C3D   C4D    sing N N 95  
AR6 "C4'" "O4'"  sing N N 96  
AR6 "C4'" "C5'"  sing N N 97  
AR6 C4D   O4D    sing N N 98  
AR6 C4D   C5D    sing N N 99  
AR6 "C5'" "O5'"  sing N N 100 
AR6 C5D   O5D    sing N N 101 
AR6 C2    H2     sing N N 102 
AR6 N6    HN6    sing N N 103 
AR6 N6    HN6A   sing N N 104 
AR6 C8    H8     sing N N 105 
AR6 "C1'" "H1'"  sing N N 106 
AR6 C1D   H1D    sing N N 107 
AR6 "C2'" "H2'"  sing N N 108 
AR6 "O2'" "HO2'" sing N N 109 
AR6 C2D   H2D    sing N N 110 
AR6 O2D   HO2D   sing N N 111 
AR6 "C3'" "H3'"  sing N N 112 
AR6 "O3'" "HO3'" sing N N 113 
AR6 C3D   H3D    sing N N 114 
AR6 O3D   HO3D   sing N N 115 
AR6 "C4'" "H4'"  sing N N 116 
AR6 C4D   H4D    sing N N 117 
AR6 "C5'" "H5'"  sing N N 118 
AR6 "C5'" "H5'A" sing N N 119 
AR6 C5D   H5D    sing N N 120 
AR6 C5D   H5DA   sing N N 121 
AR6 O1A   H1A    sing N N 122 
AR6 O1B   H1B    sing N N 123 
AR6 O1D   HD1    sing N N 124 
ARG N     CA     sing N N 125 
ARG N     H      sing N N 126 
ARG N     H2     sing N N 127 
ARG CA    C      sing N N 128 
ARG CA    CB     sing N N 129 
ARG CA    HA     sing N N 130 
ARG C     O      doub N N 131 
ARG C     OXT    sing N N 132 
ARG CB    CG     sing N N 133 
ARG CB    HB2    sing N N 134 
ARG CB    HB3    sing N N 135 
ARG CG    CD     sing N N 136 
ARG CG    HG2    sing N N 137 
ARG CG    HG3    sing N N 138 
ARG CD    NE     sing N N 139 
ARG CD    HD2    sing N N 140 
ARG CD    HD3    sing N N 141 
ARG NE    CZ     sing N N 142 
ARG NE    HE     sing N N 143 
ARG CZ    NH1    sing N N 144 
ARG CZ    NH2    doub N N 145 
ARG NH1   HH11   sing N N 146 
ARG NH1   HH12   sing N N 147 
ARG NH2   HH21   sing N N 148 
ARG NH2   HH22   sing N N 149 
ARG OXT   HXT    sing N N 150 
ASN N     CA     sing N N 151 
ASN N     H      sing N N 152 
ASN N     H2     sing N N 153 
ASN CA    C      sing N N 154 
ASN CA    CB     sing N N 155 
ASN CA    HA     sing N N 156 
ASN C     O      doub N N 157 
ASN C     OXT    sing N N 158 
ASN CB    CG     sing N N 159 
ASN CB    HB2    sing N N 160 
ASN CB    HB3    sing N N 161 
ASN CG    OD1    doub N N 162 
ASN CG    ND2    sing N N 163 
ASN ND2   HD21   sing N N 164 
ASN ND2   HD22   sing N N 165 
ASN OXT   HXT    sing N N 166 
ASP N     CA     sing N N 167 
ASP N     H      sing N N 168 
ASP N     H2     sing N N 169 
ASP CA    C      sing N N 170 
ASP CA    CB     sing N N 171 
ASP CA    HA     sing N N 172 
ASP C     O      doub N N 173 
ASP C     OXT    sing N N 174 
ASP CB    CG     sing N N 175 
ASP CB    HB2    sing N N 176 
ASP CB    HB3    sing N N 177 
ASP CG    OD1    doub N N 178 
ASP CG    OD2    sing N N 179 
ASP OD2   HD2    sing N N 180 
ASP OXT   HXT    sing N N 181 
CYS N     CA     sing N N 182 
CYS N     H      sing N N 183 
CYS N     H2     sing N N 184 
CYS CA    C      sing N N 185 
CYS CA    CB     sing N N 186 
CYS CA    HA     sing N N 187 
CYS C     O      doub N N 188 
CYS C     OXT    sing N N 189 
CYS CB    SG     sing N N 190 
CYS CB    HB2    sing N N 191 
CYS CB    HB3    sing N N 192 
CYS SG    HG     sing N N 193 
CYS OXT   HXT    sing N N 194 
GLN N     CA     sing N N 195 
GLN N     H      sing N N 196 
GLN N     H2     sing N N 197 
GLN CA    C      sing N N 198 
GLN CA    CB     sing N N 199 
GLN CA    HA     sing N N 200 
GLN C     O      doub N N 201 
GLN C     OXT    sing N N 202 
GLN CB    CG     sing N N 203 
GLN CB    HB2    sing N N 204 
GLN CB    HB3    sing N N 205 
GLN CG    CD     sing N N 206 
GLN CG    HG2    sing N N 207 
GLN CG    HG3    sing N N 208 
GLN CD    OE1    doub N N 209 
GLN CD    NE2    sing N N 210 
GLN NE2   HE21   sing N N 211 
GLN NE2   HE22   sing N N 212 
GLN OXT   HXT    sing N N 213 
GLU N     CA     sing N N 214 
GLU N     H      sing N N 215 
GLU N     H2     sing N N 216 
GLU CA    C      sing N N 217 
GLU CA    CB     sing N N 218 
GLU CA    HA     sing N N 219 
GLU C     O      doub N N 220 
GLU C     OXT    sing N N 221 
GLU CB    CG     sing N N 222 
GLU CB    HB2    sing N N 223 
GLU CB    HB3    sing N N 224 
GLU CG    CD     sing N N 225 
GLU CG    HG2    sing N N 226 
GLU CG    HG3    sing N N 227 
GLU CD    OE1    doub N N 228 
GLU CD    OE2    sing N N 229 
GLU OE2   HE2    sing N N 230 
GLU OXT   HXT    sing N N 231 
GLY N     CA     sing N N 232 
GLY N     H      sing N N 233 
GLY N     H2     sing N N 234 
GLY CA    C      sing N N 235 
GLY CA    HA2    sing N N 236 
GLY CA    HA3    sing N N 237 
GLY C     O      doub N N 238 
GLY C     OXT    sing N N 239 
GLY OXT   HXT    sing N N 240 
HIS N     CA     sing N N 241 
HIS N     H      sing N N 242 
HIS N     H2     sing N N 243 
HIS CA    C      sing N N 244 
HIS CA    CB     sing N N 245 
HIS CA    HA     sing N N 246 
HIS C     O      doub N N 247 
HIS C     OXT    sing N N 248 
HIS CB    CG     sing N N 249 
HIS CB    HB2    sing N N 250 
HIS CB    HB3    sing N N 251 
HIS CG    ND1    sing Y N 252 
HIS CG    CD2    doub Y N 253 
HIS ND1   CE1    doub Y N 254 
HIS ND1   HD1    sing N N 255 
HIS CD2   NE2    sing Y N 256 
HIS CD2   HD2    sing N N 257 
HIS CE1   NE2    sing Y N 258 
HIS CE1   HE1    sing N N 259 
HIS NE2   HE2    sing N N 260 
HIS OXT   HXT    sing N N 261 
HOH O     H1     sing N N 262 
HOH O     H2     sing N N 263 
ILE N     CA     sing N N 264 
ILE N     H      sing N N 265 
ILE N     H2     sing N N 266 
ILE CA    C      sing N N 267 
ILE CA    CB     sing N N 268 
ILE CA    HA     sing N N 269 
ILE C     O      doub N N 270 
ILE C     OXT    sing N N 271 
ILE CB    CG1    sing N N 272 
ILE CB    CG2    sing N N 273 
ILE CB    HB     sing N N 274 
ILE CG1   CD1    sing N N 275 
ILE CG1   HG12   sing N N 276 
ILE CG1   HG13   sing N N 277 
ILE CG2   HG21   sing N N 278 
ILE CG2   HG22   sing N N 279 
ILE CG2   HG23   sing N N 280 
ILE CD1   HD11   sing N N 281 
ILE CD1   HD12   sing N N 282 
ILE CD1   HD13   sing N N 283 
ILE OXT   HXT    sing N N 284 
LEU N     CA     sing N N 285 
LEU N     H      sing N N 286 
LEU N     H2     sing N N 287 
LEU CA    C      sing N N 288 
LEU CA    CB     sing N N 289 
LEU CA    HA     sing N N 290 
LEU C     O      doub N N 291 
LEU C     OXT    sing N N 292 
LEU CB    CG     sing N N 293 
LEU CB    HB2    sing N N 294 
LEU CB    HB3    sing N N 295 
LEU CG    CD1    sing N N 296 
LEU CG    CD2    sing N N 297 
LEU CG    HG     sing N N 298 
LEU CD1   HD11   sing N N 299 
LEU CD1   HD12   sing N N 300 
LEU CD1   HD13   sing N N 301 
LEU CD2   HD21   sing N N 302 
LEU CD2   HD22   sing N N 303 
LEU CD2   HD23   sing N N 304 
LEU OXT   HXT    sing N N 305 
LYS N     CA     sing N N 306 
LYS N     H      sing N N 307 
LYS N     H2     sing N N 308 
LYS CA    C      sing N N 309 
LYS CA    CB     sing N N 310 
LYS CA    HA     sing N N 311 
LYS C     O      doub N N 312 
LYS C     OXT    sing N N 313 
LYS CB    CG     sing N N 314 
LYS CB    HB2    sing N N 315 
LYS CB    HB3    sing N N 316 
LYS CG    CD     sing N N 317 
LYS CG    HG2    sing N N 318 
LYS CG    HG3    sing N N 319 
LYS CD    CE     sing N N 320 
LYS CD    HD2    sing N N 321 
LYS CD    HD3    sing N N 322 
LYS CE    NZ     sing N N 323 
LYS CE    HE2    sing N N 324 
LYS CE    HE3    sing N N 325 
LYS NZ    HZ1    sing N N 326 
LYS NZ    HZ2    sing N N 327 
LYS NZ    HZ3    sing N N 328 
LYS OXT   HXT    sing N N 329 
MET N     CA     sing N N 330 
MET N     H      sing N N 331 
MET N     H2     sing N N 332 
MET CA    C      sing N N 333 
MET CA    CB     sing N N 334 
MET CA    HA     sing N N 335 
MET C     O      doub N N 336 
MET C     OXT    sing N N 337 
MET CB    CG     sing N N 338 
MET CB    HB2    sing N N 339 
MET CB    HB3    sing N N 340 
MET CG    SD     sing N N 341 
MET CG    HG2    sing N N 342 
MET CG    HG3    sing N N 343 
MET SD    CE     sing N N 344 
MET CE    HE1    sing N N 345 
MET CE    HE2    sing N N 346 
MET CE    HE3    sing N N 347 
MET OXT   HXT    sing N N 348 
PHE N     CA     sing N N 349 
PHE N     H      sing N N 350 
PHE N     H2     sing N N 351 
PHE CA    C      sing N N 352 
PHE CA    CB     sing N N 353 
PHE CA    HA     sing N N 354 
PHE C     O      doub N N 355 
PHE C     OXT    sing N N 356 
PHE CB    CG     sing N N 357 
PHE CB    HB2    sing N N 358 
PHE CB    HB3    sing N N 359 
PHE CG    CD1    doub Y N 360 
PHE CG    CD2    sing Y N 361 
PHE CD1   CE1    sing Y N 362 
PHE CD1   HD1    sing N N 363 
PHE CD2   CE2    doub Y N 364 
PHE CD2   HD2    sing N N 365 
PHE CE1   CZ     doub Y N 366 
PHE CE1   HE1    sing N N 367 
PHE CE2   CZ     sing Y N 368 
PHE CE2   HE2    sing N N 369 
PHE CZ    HZ     sing N N 370 
PHE OXT   HXT    sing N N 371 
PRO N     CA     sing N N 372 
PRO N     CD     sing N N 373 
PRO N     H      sing N N 374 
PRO CA    C      sing N N 375 
PRO CA    CB     sing N N 376 
PRO CA    HA     sing N N 377 
PRO C     O      doub N N 378 
PRO C     OXT    sing N N 379 
PRO CB    CG     sing N N 380 
PRO CB    HB2    sing N N 381 
PRO CB    HB3    sing N N 382 
PRO CG    CD     sing N N 383 
PRO CG    HG2    sing N N 384 
PRO CG    HG3    sing N N 385 
PRO CD    HD2    sing N N 386 
PRO CD    HD3    sing N N 387 
PRO OXT   HXT    sing N N 388 
SER N     CA     sing N N 389 
SER N     H      sing N N 390 
SER N     H2     sing N N 391 
SER CA    C      sing N N 392 
SER CA    CB     sing N N 393 
SER CA    HA     sing N N 394 
SER C     O      doub N N 395 
SER C     OXT    sing N N 396 
SER CB    OG     sing N N 397 
SER CB    HB2    sing N N 398 
SER CB    HB3    sing N N 399 
SER OG    HG     sing N N 400 
SER OXT   HXT    sing N N 401 
THR N     CA     sing N N 402 
THR N     H      sing N N 403 
THR N     H2     sing N N 404 
THR CA    C      sing N N 405 
THR CA    CB     sing N N 406 
THR CA    HA     sing N N 407 
THR C     O      doub N N 408 
THR C     OXT    sing N N 409 
THR CB    OG1    sing N N 410 
THR CB    CG2    sing N N 411 
THR CB    HB     sing N N 412 
THR OG1   HG1    sing N N 413 
THR CG2   HG21   sing N N 414 
THR CG2   HG22   sing N N 415 
THR CG2   HG23   sing N N 416 
THR OXT   HXT    sing N N 417 
TRP N     CA     sing N N 418 
TRP N     H      sing N N 419 
TRP N     H2     sing N N 420 
TRP CA    C      sing N N 421 
TRP CA    CB     sing N N 422 
TRP CA    HA     sing N N 423 
TRP C     O      doub N N 424 
TRP C     OXT    sing N N 425 
TRP CB    CG     sing N N 426 
TRP CB    HB2    sing N N 427 
TRP CB    HB3    sing N N 428 
TRP CG    CD1    doub Y N 429 
TRP CG    CD2    sing Y N 430 
TRP CD1   NE1    sing Y N 431 
TRP CD1   HD1    sing N N 432 
TRP CD2   CE2    doub Y N 433 
TRP CD2   CE3    sing Y N 434 
TRP NE1   CE2    sing Y N 435 
TRP NE1   HE1    sing N N 436 
TRP CE2   CZ2    sing Y N 437 
TRP CE3   CZ3    doub Y N 438 
TRP CE3   HE3    sing N N 439 
TRP CZ2   CH2    doub Y N 440 
TRP CZ2   HZ2    sing N N 441 
TRP CZ3   CH2    sing Y N 442 
TRP CZ3   HZ3    sing N N 443 
TRP CH2   HH2    sing N N 444 
TRP OXT   HXT    sing N N 445 
TYR N     CA     sing N N 446 
TYR N     H      sing N N 447 
TYR N     H2     sing N N 448 
TYR CA    C      sing N N 449 
TYR CA    CB     sing N N 450 
TYR CA    HA     sing N N 451 
TYR C     O      doub N N 452 
TYR C     OXT    sing N N 453 
TYR CB    CG     sing N N 454 
TYR CB    HB2    sing N N 455 
TYR CB    HB3    sing N N 456 
TYR CG    CD1    doub Y N 457 
TYR CG    CD2    sing Y N 458 
TYR CD1   CE1    sing Y N 459 
TYR CD1   HD1    sing N N 460 
TYR CD2   CE2    doub Y N 461 
TYR CD2   HD2    sing N N 462 
TYR CE1   CZ     doub Y N 463 
TYR CE1   HE1    sing N N 464 
TYR CE2   CZ     sing Y N 465 
TYR CE2   HE2    sing N N 466 
TYR CZ    OH     sing N N 467 
TYR OH    HH     sing N N 468 
TYR OXT   HXT    sing N N 469 
VAL N     CA     sing N N 470 
VAL N     H      sing N N 471 
VAL N     H2     sing N N 472 
VAL CA    C      sing N N 473 
VAL CA    CB     sing N N 474 
VAL CA    HA     sing N N 475 
VAL C     O      doub N N 476 
VAL C     OXT    sing N N 477 
VAL CB    CG1    sing N N 478 
VAL CB    CG2    sing N N 479 
VAL CB    HB     sing N N 480 
VAL CG1   HG11   sing N N 481 
VAL CG1   HG12   sing N N 482 
VAL CG1   HG13   sing N N 483 
VAL CG2   HG21   sing N N 484 
VAL CG2   HG22   sing N N 485 
VAL CG2   HG23   sing N N 486 
VAL OXT   HXT    sing N N 487 
# 
_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                    8K6E 
_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]   0.004644 
_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]   0.018132 
_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]   0.012360 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . ALA A 1 6   ? 10.679 1.975   11.876 1.00 35.89  ?  6   ALA A N     1 
ATOM   2    C CA    . ALA A 1 6   ? 12.005 2.608   11.842 1.00 37.55  ?  6   ALA A CA    1 
ATOM   3    C C     . ALA A 1 6   ? 12.100 3.802   12.801 1.00 41.77  ?  6   ALA A C     1 
ATOM   4    O O     . ALA A 1 6   ? 11.322 4.761   12.645 1.00 40.99  ?  6   ALA A O     1 
ATOM   5    C CB    . ALA A 1 6   ? 12.334 3.055   10.441 1.00 33.10  ?  6   ALA A CB    1 
ATOM   6    N N     . ALA A 1 7   ? 13.063 3.758   13.747 1.00 36.97  ?  7   ALA A N     1 
ATOM   7    C CA    . ALA A 1 7   ? 13.199 4.754   14.818 1.00 27.87  ?  7   ALA A CA    1 
ATOM   8    C C     . ALA A 1 7   ? 13.943 6.022   14.393 1.00 30.24  ?  7   ALA A C     1 
ATOM   9    O O     . ALA A 1 7   ? 14.957 5.969   13.691 1.00 32.59  ?  7   ALA A O     1 
ATOM   10   C CB    . ALA A 1 7   ? 13.934 4.150   16.000 1.00 29.22  ?  7   ALA A CB    1 
ATOM   11   N N     . LEU A 1 8   ? 13.448 7.166   14.872 1.00 33.11  ?  8   LEU A N     1 
ATOM   12   C CA    . LEU A 1 8   ? 13.990 8.498   14.612 1.00 28.79  ?  8   LEU A CA    1 
ATOM   13   C C     . LEU A 1 8   ? 15.087 8.854   15.598 1.00 28.65  ?  8   LEU A C     1 
ATOM   14   O O     . LEU A 1 8   ? 15.073 8.416   16.751 1.00 30.34  ?  8   LEU A O     1 
ATOM   15   C CB    . LEU A 1 8   ? 12.893 9.554   14.720 1.00 29.58  ?  8   LEU A CB    1 
ATOM   16   C CG    . LEU A 1 8   ? 11.592 9.223   14.005 1.00 31.14  ?  8   LEU A CG    1 
ATOM   17   C CD1   . LEU A 1 8   ? 10.514 10.204  14.405 1.00 29.52  ?  8   LEU A CD1   1 
ATOM   18   C CD2   . LEU A 1 8   ? 11.845 9.259   12.516 1.00 27.88  ?  8   LEU A CD2   1 
ATOM   19   N N     . VAL A 1 9   ? 15.996 9.719   15.147 1.00 27.12  ?  9   VAL A N     1 
ATOM   20   C CA    . VAL A 1 9   ? 17.138 10.206  15.913 1.00 23.38  ?  9   VAL A CA    1 
ATOM   21   C C     . VAL A 1 9   ? 17.253 11.716  15.680 1.00 24.02  ?  9   VAL A C     1 
ATOM   22   O O     . VAL A 1 9   ? 17.657 12.142  14.599 1.00 27.93  ?  9   VAL A O     1 
ATOM   23   C CB    . VAL A 1 9   ? 18.423 9.494   15.472 1.00 23.95  ?  9   VAL A CB    1 
ATOM   24   C CG1   . VAL A 1 9   ? 19.692 10.190  15.994 1.00 24.58  ?  9   VAL A CG1   1 
ATOM   25   C CG2   . VAL A 1 9   ? 18.362 8.059   15.849 1.00 22.17  ?  9   VAL A CG2   1 
ATOM   26   N N     . ILE A 1 10  ? 16.972 12.511  16.701 1.00 23.72  ?  10  ILE A N     1 
ATOM   27   C CA    . ILE A 1 10  ? 17.132 13.986  16.572 1.00 26.53  ?  10  ILE A CA    1 
ATOM   28   C C     . ILE A 1 10  ? 18.197 14.531  17.526 1.00 28.94  ?  10  ILE A C     1 
ATOM   29   O O     . ILE A 1 10  ? 18.074 14.318  18.739 1.00 27.56  ?  10  ILE A O     1 
ATOM   30   C CB    . ILE A 1 10  ? 15.788 14.742  16.647 1.00 25.89  ?  10  ILE A CB    1 
ATOM   31   C CG1   . ILE A 1 10  ? 15.909 16.117  17.296 1.00 25.12  ?  10  ILE A CG1   1 
ATOM   32   C CG2   . ILE A 1 10  ? 14.702 13.890  17.277 1.00 30.75  ?  10  ILE A CG2   1 
ATOM   33   C CD1   . ILE A 1 10  ? 14.958 17.117  16.738 1.00 27.56  ?  10  ILE A CD1   1 
ATOM   34   N N     . ASP A 1 11  ? 19.220 15.179  16.967 1.00 26.82  ?  11  ASP A N     1 
ATOM   35   C CA    . ASP A 1 11  ? 20.265 15.853  17.771 1.00 28.79  ?  11  ASP A CA    1 
ATOM   36   C C     . ASP A 1 11  ? 19.785 17.282  17.999 1.00 29.57  ?  11  ASP A C     1 
ATOM   37   O O     . ASP A 1 11  ? 19.751 18.044  17.039 1.00 29.16  ?  11  ASP A O     1 
ATOM   38   C CB    . ASP A 1 11  ? 21.639 15.711  17.111 1.00 27.49  ?  11  ASP A CB    1 
ATOM   39   C CG    . ASP A 1 11  ? 22.790 16.412  17.808 1.00 34.03  ?  11  ASP A CG    1 
ATOM   40   O OD1   . ASP A 1 11  ? 22.656 16.749  18.991 1.00 30.40  ?  11  ASP A OD1   1 
ATOM   41   O OD2   . ASP A 1 11  ? 23.825 16.586  17.156 1.00 36.61  -1 11  ASP A OD2   1 
ATOM   42   N N     . ASN A 1 12  ? 19.426 17.604  19.235 1.00 29.27  ?  12  ASN A N     1 
ATOM   43   C CA    . ASN A 1 12  ? 18.923 18.952  19.595 1.00 30.64  ?  12  ASN A CA    1 
ATOM   44   C C     . ASN A 1 12  ? 20.114 19.881  19.780 1.00 29.35  ?  12  ASN A C     1 
ATOM   45   O O     . ASN A 1 12  ? 20.569 20.010  20.913 1.00 29.19  ?  12  ASN A O     1 
ATOM   46   C CB    . ASN A 1 12  ? 18.095 18.863  20.873 1.00 30.11  ?  12  ASN A CB    1 
ATOM   47   C CG    . ASN A 1 12  ? 16.947 17.894  20.759 1.00 31.58  ?  12  ASN A CG    1 
ATOM   48   O OD1   . ASN A 1 12  ? 16.163 17.994  19.832 1.00 34.97  ?  12  ASN A OD1   1 
ATOM   49   N ND2   . ASN A 1 12  ? 16.839 16.966  21.692 1.00 32.08  ?  12  ASN A ND2   1 
ATOM   50   N N     . GLY A 1 13  ? 20.565 20.527  18.712 1.00 29.49  ?  13  GLY A N     1 
ATOM   51   C CA    . GLY A 1 13  ? 21.798 21.320  18.788 1.00 30.96  ?  13  GLY A CA    1 
ATOM   52   C C     . GLY A 1 13  ? 21.644 22.793  19.060 1.00 31.99  ?  13  GLY A C     1 
ATOM   53   O O     . GLY A 1 13  ? 20.631 23.351  18.674 1.00 32.20  ?  13  GLY A O     1 
ATOM   54   N N     . SER A 1 14  ? 22.669 23.397  19.645 1.00 30.96  ?  14  SER A N     1 
ATOM   55   C CA    . SER A 1 14  ? 22.701 24.838  19.985 1.00 35.48  ?  14  SER A CA    1 
ATOM   56   C C     . SER A 1 14  ? 22.462 25.749  18.782 1.00 34.10  ?  14  SER A C     1 
ATOM   57   O O     . SER A 1 14  ? 21.896 26.829  18.971 1.00 38.42  ?  14  SER A O     1 
ATOM   58   C CB    . SER A 1 14  ? 24.004 25.146  20.649 1.00 34.70  ?  14  SER A CB    1 
ATOM   59   O OG    . SER A 1 14  ? 25.035 25.299  19.699 1.00 33.98  ?  14  SER A OG    1 
ATOM   60   N N     . GLY A 1 15  ? 22.880 25.331  17.597 1.00 32.05  ?  15  GLY A N     1 
ATOM   61   C CA    . GLY A 1 15  ? 22.617 26.133  16.396 1.00 34.08  ?  15  GLY A CA    1 
ATOM   62   C C     . GLY A 1 15  ? 22.068 25.308  15.264 1.00 30.85  ?  15  GLY A C     1 
ATOM   63   O O     . GLY A 1 15  ? 21.382 25.863  14.415 1.00 29.01  ?  15  GLY A O     1 
ATOM   64   N N     . MET A 1 16  ? 22.363 24.018  15.256 1.00 33.83  ?  16  MET A N     1 
ATOM   65   C CA    . MET A 1 16  ? 21.759 23.179  14.201 1.00 32.92  ?  16  MET A CA    1 
ATOM   66   C C     . MET A 1 16  ? 21.041 21.978  14.779 1.00 30.03  ?  16  MET A C     1 
ATOM   67   O O     . MET A 1 16  ? 21.575 21.345  15.662 1.00 37.33  ?  16  MET A O     1 
ATOM   68   C CB    . MET A 1 16  ? 22.781 22.687  13.170 1.00 38.30  ?  16  MET A CB    1 
ATOM   69   C CG    . MET A 1 16  ? 24.036 23.507  13.086 1.00 39.86  ?  16  MET A CG    1 
ATOM   70   S SD    . MET A 1 16  ? 24.204 24.205  11.441 1.00 50.65  ?  16  MET A SD    1 
ATOM   71   C CE    . MET A 1 16  ? 22.504 24.181  10.880 1.00 37.45  ?  16  MET A CE    1 
ATOM   72   N N     . CYS A 1 17  ? 19.856 21.704  14.267 1.00 32.32  ?  17  CYS A N     1 
ATOM   73   C CA    . CYS A 1 17  ? 19.167 20.463  14.655 1.00 32.61  ?  17  CYS A CA    1 
ATOM   74   C C     . CYS A 1 17  ? 19.502 19.436  13.574 1.00 31.47  ?  17  CYS A C     1 
ATOM   75   O O     . CYS A 1 17  ? 19.400 19.782  12.402 1.00 28.76  ?  17  CYS A O     1 
ATOM   76   C CB    . CYS A 1 17  ? 17.669 20.677  14.766 1.00 32.96  ?  17  CYS A CB    1 
ATOM   77   S SG    . CYS A 1 17  ? 16.737 19.147  14.536 1.00 54.90  ?  17  CYS A SG    1 
ATOM   78   N N     . LYS A 1 18  ? 19.970 18.259  13.973 1.00 25.99  ?  18  LYS A N     1 
ATOM   79   C CA    . LYS A 1 18  ? 20.326 17.193  13.013 1.00 26.46  ?  18  LYS A CA    1 
ATOM   80   C C     . LYS A 1 18  ? 19.362 16.027  13.199 1.00 29.09  ?  18  LYS A C     1 
ATOM   81   O O     . LYS A 1 18  ? 19.474 15.355  14.210 1.00 31.41  ?  18  LYS A O     1 
ATOM   82   C CB    . LYS A 1 18  ? 21.741 16.693  13.294 1.00 27.71  ?  18  LYS A CB    1 
ATOM   83   C CG    . LYS A 1 18  ? 22.862 17.511  12.687 1.00 25.75  ?  18  LYS A CG    1 
ATOM   84   C CD    . LYS A 1 18  ? 23.914 17.853  13.694 1.00 24.41  ?  18  LYS A CD    1 
ATOM   85   C CE    . LYS A 1 18  ? 23.707 19.235  14.257 1.00 23.12  ?  18  LYS A CE    1 
ATOM   86   N NZ    . LYS A 1 18  ? 23.668 19.218  15.733 1.00 26.33  ?  18  LYS A NZ    1 
ATOM   87   N N     . ALA A 1 19  ? 18.438 15.817  12.263 1.00 30.35  ?  19  ALA A N     1 
ATOM   88   C CA    . ALA A 1 19  ? 17.481 14.736  12.484 1.00 29.20  ?  19  ALA A CA    1 
ATOM   89   C C     . ALA A 1 19  ? 17.506 13.766  11.318 1.00 25.61  ?  19  ALA A C     1 
ATOM   90   O O     . ALA A 1 19  ? 17.894 14.115  10.208 1.00 25.06  ?  19  ALA A O     1 
ATOM   91   C CB    . ALA A 1 19  ? 16.046 15.251  12.706 1.00 24.44  ?  19  ALA A CB    1 
ATOM   92   N N     . GLY A 1 20  ? 17.081 12.544  11.604 1.00 25.22  ?  20  GLY A N     1 
ATOM   93   C CA    . GLY A 1 20  ? 17.041 11.502  10.599 1.00 25.39  ?  20  GLY A CA    1 
ATOM   94   C C     . GLY A 1 20  ? 16.579 10.191  11.193 1.00 25.58  ?  20  GLY A C     1 
ATOM   95   O O     . GLY A 1 20  ? 16.008 10.148  12.287 1.00 23.37  ?  20  GLY A O     1 
ATOM   96   N N     . PHE A 1 21  ? 16.869 9.114   10.468 1.00 27.24  ?  21  PHE A N     1 
ATOM   97   C CA    . PHE A 1 21  ? 16.339 7.784   10.747 1.00 26.60  ?  21  PHE A CA    1 
ATOM   98   C C     . PHE A 1 21  ? 17.475 6.830   11.094 1.00 27.68  ?  21  PHE A C     1 
ATOM   99   O O     . PHE A 1 21  ? 18.517 6.839   10.443 1.00 31.91  ?  21  PHE A O     1 
ATOM   100  C CB    . PHE A 1 21  ? 15.558 7.247   9.537  1.00 25.33  ?  21  PHE A CB    1 
ATOM   101  C CG    . PHE A 1 21  ? 14.583 8.237   8.924  1.00 27.51  ?  21  PHE A CG    1 
ATOM   102  C CD1   . PHE A 1 21  ? 13.246 8.257   9.310  1.00 29.93  ?  21  PHE A CD1   1 
ATOM   103  C CD2   . PHE A 1 21  ? 14.984 9.118   7.923  1.00 29.14  ?  21  PHE A CD2   1 
ATOM   104  C CE1   . PHE A 1 21  ? 12.346 9.164   8.745  1.00 25.76  ?  21  PHE A CE1   1 
ATOM   105  C CE2   . PHE A 1 21  ? 14.097 9.999   7.365  1.00 24.39  ?  21  PHE A CE2   1 
ATOM   106  C CZ    . PHE A 1 21  ? 12.773 10.023  7.779  1.00 24.84  ?  21  PHE A CZ    1 
ATOM   107  N N     . ALA A 1 22  ? 17.274 5.990   12.103 1.00 25.62  ?  22  ALA A N     1 
ATOM   108  C CA    . ALA A 1 22  ? 18.340 5.097   12.538 1.00 29.59  ?  22  ALA A CA    1 
ATOM   109  C C     . ALA A 1 22  ? 18.570 3.970   11.526 1.00 32.74  ?  22  ALA A C     1 
ATOM   110  O O     . ALA A 1 22  ? 17.625 3.378   10.999 1.00 35.60  ?  22  ALA A O     1 
ATOM   111  C CB    . ALA A 1 22  ? 18.001 4.534   13.914 1.00 30.28  ?  22  ALA A CB    1 
ATOM   112  N N     . GLY A 1 23  ? 19.833 3.657   11.267 1.00 29.81  ?  23  GLY A N     1 
ATOM   113  C CA    . GLY A 1 23  ? 20.154 2.829   10.123 1.00 33.26  ?  23  GLY A CA    1 
ATOM   114  C C     . GLY A 1 23  ? 20.880 3.584   9.019  1.00 38.14  ?  23  GLY A C     1 
ATOM   115  O O     . GLY A 1 23  ? 21.836 3.060   8.440  1.00 43.49  ?  23  GLY A O     1 
ATOM   116  N N     . ASP A 1 24  ? 20.419 4.799   8.703  1.00 36.19  ?  24  ASP A N     1 
ATOM   117  C CA    . ASP A 1 24  ? 21.181 5.745   7.892  1.00 36.64  ?  24  ASP A CA    1 
ATOM   118  C C     . ASP A 1 24  ? 22.431 6.200   8.645  1.00 42.44  ?  24  ASP A C     1 
ATOM   119  O O     . ASP A 1 24  ? 22.423 6.312   9.878  1.00 42.28  ?  24  ASP A O     1 
ATOM   120  C CB    . ASP A 1 24  ? 20.346 6.998   7.566  1.00 40.76  ?  24  ASP A CB    1 
ATOM   121  C CG    . ASP A 1 24  ? 19.066 6.716   6.766  1.00 41.47  ?  24  ASP A CG    1 
ATOM   122  O OD1   . ASP A 1 24  ? 18.180 7.610   6.744  1.00 39.31  ?  24  ASP A OD1   1 
ATOM   123  O OD2   . ASP A 1 24  ? 18.937 5.638   6.153  1.00 46.96  -1 24  ASP A OD2   1 
ATOM   124  N N     . ASP A 1 25  ? 23.511 6.509   7.900  1.00 45.28  ?  25  ASP A N     1 
ATOM   125  C CA    . ASP A 1 25  ? 24.723 7.055   8.525  1.00 44.53  ?  25  ASP A CA    1 
ATOM   126  C C     . ASP A 1 25  ? 24.931 8.547   8.237  1.00 43.96  ?  25  ASP A C     1 
ATOM   127  O O     . ASP A 1 25  ? 26.037 9.065   8.443  1.00 39.24  ?  25  ASP A O     1 
ATOM   128  C CB    . ASP A 1 25  ? 25.984 6.241   8.173  1.00 50.24  ?  25  ASP A CB    1 
ATOM   129  C CG    . ASP A 1 25  ? 26.397 6.319   6.697  1.00 51.63  ?  25  ASP A CG    1 
ATOM   130  O OD1   . ASP A 1 25  ? 27.017 7.320   6.270  1.00 52.58  ?  25  ASP A OD1   1 
ATOM   131  O OD2   . ASP A 1 25  ? 26.136 5.333   5.972  1.00 59.05  -1 25  ASP A OD2   1 
ATOM   132  N N     . ALA A 1 26  ? 23.880 9.258   7.802  1.00 40.96  ?  26  ALA A N     1 
ATOM   133  C CA    . ALA A 1 26  ? 23.828 10.705  7.932  1.00 33.78  ?  26  ALA A CA    1 
ATOM   134  C C     . ALA A 1 26  ? 22.425 11.173  8.284  1.00 36.60  ?  26  ALA A C     1 
ATOM   135  O O     . ALA A 1 26  ? 21.429 10.564  7.848  1.00 37.65  ?  26  ALA A O     1 
ATOM   136  C CB    . ALA A 1 26  ? 24.280 11.411  6.660  1.00 39.11  ?  26  ALA A CB    1 
ATOM   137  N N     . PRO A 1 27  ? 22.308 12.247  9.061  1.00 35.71  ?  27  PRO A N     1 
ATOM   138  C CA    . PRO A 1 27  ? 20.995 12.878  9.228  1.00 33.05  ?  27  PRO A CA    1 
ATOM   139  C C     . PRO A 1 27  ? 20.447 13.324  7.875  1.00 31.94  ?  27  PRO A C     1 
ATOM   140  O O     . PRO A 1 27  ? 21.198 13.763  6.999  1.00 33.10  ?  27  PRO A O     1 
ATOM   141  C CB    . PRO A 1 27  ? 21.286 14.072  10.143 1.00 28.88  ?  27  PRO A CB    1 
ATOM   142  C CG    . PRO A 1 27  ? 22.746 14.294  10.049 1.00 26.93  ?  27  PRO A CG    1 
ATOM   143  C CD    . PRO A 1 27  ? 23.376 12.976  9.765  1.00 29.53  ?  27  PRO A CD    1 
ATOM   144  N N     . ARG A 1 28  ? 19.127 13.205  7.712  1.00 26.02  ?  28  ARG A N     1 
ATOM   145  C CA    . ARG A 1 28  ? 18.481 13.683  6.498  1.00 29.56  ?  28  ARG A CA    1 
ATOM   146  C C     . ARG A 1 28  ? 18.261 15.172  6.524  1.00 33.60  ?  28  ARG A C     1 
ATOM   147  O O     . ARG A 1 28  ? 18.289 15.814  5.468  1.00 44.14  ?  28  ARG A O     1 
ATOM   148  C CB    . ARG A 1 28  ? 17.138 13.026  6.296  1.00 28.60  ?  28  ARG A CB    1 
ATOM   149  C CG    . ARG A 1 28  ? 17.256 11.761  5.621  1.00 38.56  ?  28  ARG A CG    1 
ATOM   150  C CD    . ARG A 1 28  ? 16.707 11.768  4.244  1.00 37.60  ?  28  ARG A CD    1 
ATOM   151  N NE    . ARG A 1 28  ? 16.123 10.438  4.076  1.00 43.24  ?  28  ARG A NE    1 
ATOM   152  C CZ    . ARG A 1 28  ? 16.836 9.327   4.219  1.00 45.01  ?  28  ARG A CZ    1 
ATOM   153  N NH1   . ARG A 1 28  ? 18.135 9.427   4.521  1.00 44.05  ?  28  ARG A NH1   1 
ATOM   154  N NH2   . ARG A 1 28  ? 16.254 8.136   4.087  1.00 46.02  ?  28  ARG A NH2   1 
ATOM   155  N N     . ALA A 1 29  ? 17.961 15.713  7.702  1.00 27.58  ?  29  ALA A N     1 
ATOM   156  C CA    . ALA A 1 29  ? 17.612 17.110  7.885  1.00 30.03  ?  29  ALA A CA    1 
ATOM   157  C C     . ALA A 1 29  ? 18.622 17.763  8.818  1.00 33.42  ?  29  ALA A C     1 
ATOM   158  O O     . ALA A 1 29  ? 18.900 17.256  9.916  1.00 33.88  ?  29  ALA A O     1 
ATOM   159  C CB    . ALA A 1 29  ? 16.199 17.258  8.441  1.00 31.59  ?  29  ALA A CB    1 
ATOM   160  N N     . VAL A 1 30  ? 19.187 18.871  8.358  1.00 31.44  ?  30  VAL A N     1 
ATOM   161  C CA    . VAL A 1 30  ? 20.098 19.693  9.130  1.00 29.25  ?  30  VAL A CA    1 
ATOM   162  C C     . VAL A 1 30  ? 19.665 21.119  8.823  1.00 32.08  ?  30  VAL A C     1 
ATOM   163  O O     . VAL A 1 30  ? 19.786 21.569  7.677  1.00 37.18  ?  30  VAL A O     1 
ATOM   164  C CB    . VAL A 1 30  ? 21.572 19.447  8.761  1.00 28.23  ?  30  VAL A CB    1 
ATOM   165  C CG1   . VAL A 1 30  ? 22.466 20.470  9.407  1.00 28.21  ?  30  VAL A CG1   1 
ATOM   166  C CG2   . VAL A 1 30  ? 21.993 18.041  9.175  1.00 26.29  ?  30  VAL A CG2   1 
ATOM   167  N N     . PHE A 1 31  ? 19.099 21.802  9.814  1.00 28.58  ?  31  PHE A N     1 
ATOM   168  C CA    . PHE A 1 31  ? 18.494 23.099  9.620  1.00 30.06  ?  31  PHE A CA    1 
ATOM   169  C C     . PHE A 1 31  ? 18.746 23.939  10.859 1.00 33.26  ?  31  PHE A C     1 
ATOM   170  O O     . PHE A 1 31  ? 18.914 23.399  11.965 1.00 31.59  ?  31  PHE A O     1 
ATOM   171  C CB    . PHE A 1 31  ? 16.997 22.958  9.320  1.00 35.97  ?  31  PHE A CB    1 
ATOM   172  C CG    . PHE A 1 31  ? 16.203 22.358  10.436 1.00 31.55  ?  31  PHE A CG    1 
ATOM   173  C CD1   . PHE A 1 31  ? 15.929 21.000  10.481 1.00 34.67  ?  31  PHE A CD1   1 
ATOM   174  C CD2   . PHE A 1 31  ? 15.681 23.168  11.411 1.00 31.43  ?  31  PHE A CD2   1 
ATOM   175  C CE1   . PHE A 1 31  ? 15.189 20.455  11.522 1.00 36.98  ?  31  PHE A CE1   1 
ATOM   176  C CE2   . PHE A 1 31  ? 14.943 22.640  12.443 1.00 38.10  ?  31  PHE A CE2   1 
ATOM   177  C CZ    . PHE A 1 31  ? 14.698 21.276  12.506 1.00 36.66  ?  31  PHE A CZ    1 
ATOM   178  N N     . PRO A 1 32  ? 18.871 25.257  10.693 1.00 35.09  ?  32  PRO A N     1 
ATOM   179  C CA    . PRO A 1 32  ? 19.067 26.142  11.842 1.00 34.28  ?  32  PRO A CA    1 
ATOM   180  C C     . PRO A 1 32  ? 18.033 25.882  12.917 1.00 35.46  ?  32  PRO A C     1 
ATOM   181  O O     . PRO A 1 32  ? 16.833 25.872  12.653 1.00 39.93  ?  32  PRO A O     1 
ATOM   182  C CB    . PRO A 1 32  ? 18.900 27.538  11.239 1.00 35.15  ?  32  PRO A CB    1 
ATOM   183  C CG    . PRO A 1 32  ? 19.302 27.374  9.861  1.00 34.54  ?  32  PRO A CG    1 
ATOM   184  C CD    . PRO A 1 32  ? 18.800 26.023  9.440  1.00 36.95  ?  32  PRO A CD    1 
ATOM   185  N N     . SER A 1 33  ? 18.505 25.708  14.148 1.00 35.51  ?  33  SER A N     1 
ATOM   186  C CA    . SER A 1 33  ? 17.619 25.478  15.286 1.00 36.66  ?  33  SER A CA    1 
ATOM   187  C C     . SER A 1 33  ? 17.226 26.829  15.912 1.00 40.28  ?  33  SER A C     1 
ATOM   188  O O     . SER A 1 33  ? 17.661 27.229  17.002 1.00 40.94  ?  33  SER A O     1 
ATOM   189  C CB    . SER A 1 33  ? 18.269 24.485  16.244 1.00 32.42  ?  33  SER A CB    1 
ATOM   190  O OG    . SER A 1 33  ? 19.216 25.086  17.089 1.00 36.02  ?  33  SER A OG    1 
ATOM   191  N N     . ILE A 1 34  ? 16.315 27.508  15.204 1.00 39.84  ?  34  ILE A N     1 
ATOM   192  C CA    . ILE A 1 34  ? 15.866 28.871  15.489 1.00 39.20  ?  34  ILE A CA    1 
ATOM   193  C C     . ILE A 1 34  ? 14.391 29.005  15.097 1.00 38.85  ?  34  ILE A C     1 
ATOM   194  O O     . ILE A 1 34  ? 13.948 28.442  14.093 1.00 43.59  ?  34  ILE A O     1 
ATOM   195  C CB    . ILE A 1 34  ? 16.736 29.888  14.730 1.00 39.25  ?  34  ILE A CB    1 
ATOM   196  C CG1   . ILE A 1 34  ? 16.459 29.787  13.233 1.00 40.47  ?  34  ILE A CG1   1 
ATOM   197  C CG2   . ILE A 1 34  ? 18.202 29.637  15.004 1.00 42.47  ?  34  ILE A CG2   1 
ATOM   198  C CD1   . ILE A 1 34  ? 15.486 30.840  12.742 1.00 42.59  ?  34  ILE A CD1   1 
ATOM   199  N N     . VAL A 1 35  ? 13.624 29.758  15.883 1.00 38.14  ?  35  VAL A N     1 
ATOM   200  C CA    . VAL A 1 35  ? 12.202 29.976  15.625 1.00 41.84  ?  35  VAL A CA    1 
ATOM   201  C C     . VAL A 1 35  ? 11.975 31.458  15.370 1.00 41.86  ?  35  VAL A C     1 
ATOM   202  O O     . VAL A 1 35  ? 12.432 32.303  16.151 1.00 38.37  ?  35  VAL A O     1 
ATOM   203  C CB    . VAL A 1 35  ? 11.312 29.505  16.792 1.00 39.08  ?  35  VAL A CB    1 
ATOM   204  C CG1   . VAL A 1 35  ? 9.869  29.795  16.480 1.00 40.77  ?  35  VAL A CG1   1 
ATOM   205  C CG2   . VAL A 1 35  ? 11.503 28.039  17.070 1.00 39.50  ?  35  VAL A CG2   1 
ATOM   206  N N     . GLY A 1 36  ? 11.250 31.770  14.296 1.00 41.81  ?  36  GLY A N     1 
ATOM   207  C CA    . GLY A 1 36  ? 10.929 33.159  14.011 1.00 50.70  ?  36  GLY A CA    1 
ATOM   208  C C     . GLY A 1 36  ? 9.452  33.519  14.047 1.00 52.82  ?  36  GLY A C     1 
ATOM   209  O O     . GLY A 1 36  ? 8.628  32.868  13.393 1.00 50.94  ?  36  GLY A O     1 
ATOM   210  N N     . ARG A 1 37  ? 9.097  34.550  14.806 1.00 55.09  ?  37  ARG A N     1 
ATOM   211  C CA    . ARG A 1 37  ? 7.735  35.077  14.802 1.00 57.81  ?  37  ARG A CA    1 
ATOM   212  C C     . ARG A 1 37  ? 7.717  36.476  14.190 1.00 56.92  ?  37  ARG A C     1 
ATOM   213  O O     . ARG A 1 37  ? 8.746  37.161  14.188 1.00 57.17  ?  37  ARG A O     1 
ATOM   214  C CB    . ARG A 1 37  ? 7.166  35.105  16.226 1.00 59.06  ?  37  ARG A CB    1 
ATOM   215  C CG    . ARG A 1 37  ? 6.148  34.006  16.496 1.00 61.45  ?  37  ARG A CG    1 
ATOM   216  C CD    . ARG A 1 37  ? 5.835  33.898  17.982 1.00 67.83  ?  37  ARG A CD    1 
ATOM   217  N NE    . ARG A 1 37  ? 5.868  32.510  18.426 1.00 67.32  ?  37  ARG A NE    1 
ATOM   218  C CZ    . ARG A 1 37  ? 6.981  31.891  18.793 1.00 65.63  ?  37  ARG A CZ    1 
ATOM   219  N NH1   . ARG A 1 37  ? 8.150  32.539  18.754 1.00 59.80  ?  37  ARG A NH1   1 
ATOM   220  N NH2   . ARG A 1 37  ? 6.925  30.628  19.193 1.00 64.37  ?  37  ARG A NH2   1 
ATOM   221  N N     . PRO A 1 38  ? 6.572  36.930  13.646 1.00 58.04  ?  38  PRO A N     1 
ATOM   222  C CA    . PRO A 1 38  ? 6.551  38.194  12.869 1.00 51.93  ?  38  PRO A CA    1 
ATOM   223  C C     . PRO A 1 38  ? 6.912  39.408  13.717 1.00 57.77  ?  38  PRO A C     1 
ATOM   224  O O     . PRO A 1 38  ? 6.558  39.505  14.895 1.00 64.31  ?  38  PRO A O     1 
ATOM   225  C CB    . PRO A 1 38  ? 5.105  38.290  12.372 1.00 50.91  ?  38  PRO A CB    1 
ATOM   226  C CG    . PRO A 1 38  ? 4.559  36.918  12.477 1.00 60.71  ?  38  PRO A CG    1 
ATOM   227  C CD    . PRO A 1 38  ? 5.251  36.284  13.670 1.00 56.96  ?  38  PRO A CD    1 
ATOM   228  N N     . ARG A 1 39  ? 7.604  40.357  13.107 1.00 53.48  ?  39  ARG A N     1 
ATOM   229  C CA    . ARG A 1 39  ? 8.064  41.490  13.897 1.00 55.96  ?  39  ARG A CA    1 
ATOM   230  C C     . ARG A 1 39  ? 6.929  42.485  14.143 1.00 52.56  ?  39  ARG A C     1 
ATOM   231  O O     . ARG A 1 39  ? 6.771  42.988  15.258 1.00 51.34  ?  39  ARG A O     1 
ATOM   232  C CB    . ARG A 1 39  ? 9.260  42.141  13.193 1.00 59.35  ?  39  ARG A CB    1 
ATOM   233  C CG    . ARG A 1 39  ? 10.152 42.988  14.068 1.00 55.37  ?  39  ARG A CG    1 
ATOM   234  C CD    . ARG A 1 39  ? 11.297 43.550  13.253 1.00 59.41  ?  39  ARG A CD    1 
ATOM   235  N NE    . ARG A 1 39  ? 12.499 42.719  13.267 1.00 58.49  ?  39  ARG A NE    1 
ATOM   236  C CZ    . ARG A 1 39  ? 13.374 42.656  12.261 1.00 62.18  ?  39  ARG A CZ    1 
ATOM   237  N NH1   . ARG A 1 39  ? 13.169 43.363  11.151 1.00 63.56  ?  39  ARG A NH1   1 
ATOM   238  N NH2   . ARG A 1 39  ? 14.459 41.888  12.361 1.00 58.70  ?  39  ARG A NH2   1 
ATOM   239  N N     . HIS A 1 40  ? 6.131  42.766  13.121 1.00 51.59  ?  40  HIS A N     1 
ATOM   240  C CA    . HIS A 1 40  ? 4.941  43.589  13.229 1.00 52.43  ?  40  HIS A CA    1 
ATOM   241  C C     . HIS A 1 40  ? 3.774  42.763  12.726 1.00 51.47  ?  40  HIS A C     1 
ATOM   242  O O     . HIS A 1 40  ? 3.914  42.028  11.748 1.00 52.92  ?  40  HIS A O     1 
ATOM   243  C CB    . HIS A 1 40  ? 5.045  44.883  12.396 1.00 51.52  ?  40  HIS A CB    1 
ATOM   244  C CG    . HIS A 1 40  ? 6.291  45.673  12.637 1.00 61.91  ?  40  HIS A CG    1 
ATOM   245  N ND1   . HIS A 1 40  ? 7.327  45.734  11.725 1.00 69.11  ?  40  HIS A ND1   1 
ATOM   246  C CD2   . HIS A 1 40  ? 6.665  46.450  13.682 1.00 68.26  ?  40  HIS A CD2   1 
ATOM   247  C CE1   . HIS A 1 40  ? 8.286  46.512  12.199 1.00 72.14  ?  40  HIS A CE1   1 
ATOM   248  N NE2   . HIS A 1 40  ? 7.911  46.958  13.386 1.00 77.15  ?  40  HIS A NE2   1 
ATOM   249  N N     . GLN A 1 41  ? 2.631  42.867  13.396 1.00 53.13  ?  41  GLN A N     1 
ATOM   250  C CA    . GLN A 1 41  ? 1.399  42.311  12.854 1.00 48.83  ?  41  GLN A CA    1 
ATOM   251  C C     . GLN A 1 41  ? 1.178  42.777  11.415 1.00 52.08  ?  41  GLN A C     1 
ATOM   252  O O     . GLN A 1 41  ? 1.653  43.838  10.987 1.00 59.98  ?  41  GLN A O     1 
ATOM   253  C CB    . GLN A 1 41  ? 0.220  42.744  13.716 1.00 48.93  ?  41  GLN A CB    1 
ATOM   254  C CG    . GLN A 1 41  ? 0.221  42.301  15.132 1.00 48.79  ?  41  GLN A CG    1 
ATOM   255  C CD    . GLN A 1 41  ? -1.089 42.658  15.817 1.00 47.93  ?  41  GLN A CD    1 
ATOM   256  O OE1   . GLN A 1 41  ? -1.858 43.478  15.325 1.00 52.31  ?  41  GLN A OE1   1 
ATOM   257  N NE2   . GLN A 1 41  ? -1.361 42.018  16.930 1.00 47.56  ?  41  GLN A NE2   1 
ATOM   258  N N     . GLY A 1 42  ? 0.439  41.991  10.650 1.00 46.55  ?  42  GLY A N     1 
ATOM   259  C CA    . GLY A 1 42  ? 0.099  42.408  9.321  1.00 51.14  ?  42  GLY A CA    1 
ATOM   260  C C     . GLY A 1 42  ? 0.974  41.823  8.240  1.00 53.49  ?  42  GLY A C     1 
ATOM   261  O O     . GLY A 1 42  ? 0.541  41.744  7.083  1.00 57.27  ?  42  GLY A O     1 
ATOM   262  N N     . VAL A 1 43  ? 2.186  41.399  8.583  1.00 51.75  ?  43  VAL A N     1 
ATOM   263  C CA    . VAL A 1 43  ? 2.834  40.394  7.753  1.00 57.05  ?  43  VAL A CA    1 
ATOM   264  C C     . VAL A 1 43  ? 2.100  39.074  7.979  1.00 57.73  ?  43  VAL A C     1 
ATOM   265  O O     . VAL A 1 43  ? 2.393  38.055  7.335  1.00 61.20  ?  43  VAL A O     1 
ATOM   266  C CB    . VAL A 1 43  ? 4.333  40.285  8.057  1.00 54.37  ?  43  VAL A CB    1 
ATOM   267  C CG1   . VAL A 1 43  ? 4.542  39.543  9.350  1.00 50.17  ?  43  VAL A CG1   1 
ATOM   268  C CG2   . VAL A 1 43  ? 5.047  39.584  6.898  1.00 52.36  ?  43  VAL A CG2   1 
ATOM   269  N N     . MET A 1 44  ? 1.133  39.098  8.907  1.00 57.96  ?  44  MET A N     1 
ATOM   270  C CA    . MET A 1 44  ? 0.284  37.962  9.240  1.00 54.13  ?  44  MET A CA    1 
ATOM   271  C C     . MET A 1 44  ? -1.079 37.994  8.562  1.00 54.26  ?  44  MET A C     1 
ATOM   272  O O     . MET A 1 44  ? -1.764 36.965  8.572  1.00 57.77  ?  44  MET A O     1 
ATOM   273  C CB    . MET A 1 44  ? 0.072  37.890  10.750 1.00 52.69  ?  44  MET A CB    1 
ATOM   274  C CG    . MET A 1 44  ? 0.787  36.757  11.443 1.00 58.12  ?  44  MET A CG    1 
ATOM   275  S SD    . MET A 1 44  ? 0.481  36.816  13.224 1.00 58.76  ?  44  MET A SD    1 
ATOM   276  C CE    . MET A 1 44  ? 0.839  38.538  13.572 1.00 47.94  ?  44  MET A CE    1 
ATOM   277  N N     . VAL A 1 45  ? -1.483 39.122  7.966  1.00 53.24  ?  45  VAL A N     1 
ATOM   278  C CA    . VAL A 1 45  ? -2.825 39.248  7.391  1.00 56.04  ?  45  VAL A CA    1 
ATOM   279  C C     . VAL A 1 45  ? -2.919 38.421  6.110  1.00 59.57  ?  45  VAL A C     1 
ATOM   280  O O     . VAL A 1 45  ? -2.252 38.720  5.112  1.00 64.04  ?  45  VAL A O     1 
ATOM   281  C CB    . VAL A 1 45  ? -3.192 40.723  7.136  1.00 53.36  ?  45  VAL A CB    1 
ATOM   282  C CG1   . VAL A 1 45  ? -2.809 41.591  8.302  1.00 50.77  ?  45  VAL A CG1   1 
ATOM   283  C CG2   . VAL A 1 45  ? -2.521 41.257  5.905  1.00 62.79  ?  45  VAL A CG2   1 
ATOM   284  N N     . GLY A 1 46  ? -3.758 37.380  6.133  1.00 57.98  ?  46  GLY A N     1 
ATOM   285  C CA    . GLY A 1 46  ? -3.998 36.538  4.974  1.00 61.42  ?  46  GLY A CA    1 
ATOM   286  C C     . GLY A 1 46  ? -3.418 35.135  5.036  1.00 65.66  ?  46  GLY A C     1 
ATOM   287  O O     . GLY A 1 46  ? -3.387 34.448  3.994  1.00 54.97  ?  46  GLY A O     1 
ATOM   288  N N     . MET A 1 47  ? -2.978 34.689  6.219  1.00 64.34  ?  47  MET A N     1 
ATOM   289  C CA    . MET A 1 47  ? -2.356 33.377  6.411  1.00 64.56  ?  47  MET A CA    1 
ATOM   290  C C     . MET A 1 47  ? -3.294 32.377  7.083  1.00 60.14  ?  47  MET A C     1 
ATOM   291  O O     . MET A 1 47  ? -2.858 31.539  7.878  1.00 62.61  ?  47  MET A O     1 
ATOM   292  C CB    . MET A 1 47  ? -1.084 33.517  7.249  1.00 67.93  ?  47  MET A CB    1 
ATOM   293  C CG    . MET A 1 47  ? -0.146 34.652  6.826  1.00 67.37  ?  47  MET A CG    1 
ATOM   294  S SD    . MET A 1 47  ? 1.519  34.059  6.387  1.00 95.67  ?  47  MET A SD    1 
ATOM   295  C CE    . MET A 1 47  ? 2.472  34.458  7.864  1.00 74.28  ?  47  MET A CE    1 
ATOM   296  N N     . ASP A 1 51  ? 1.943  32.594  10.909 1.00 66.79  ?  51  ASP A N     1 
ATOM   297  C CA    . ASP A 1 51  ? 1.814  32.340  12.345 1.00 62.58  ?  51  ASP A CA    1 
ATOM   298  C C     . ASP A 1 51  ? 3.187  32.346  13.053 1.00 64.17  ?  51  ASP A C     1 
ATOM   299  O O     . ASP A 1 51  ? 3.379  33.069  14.043 1.00 62.52  ?  51  ASP A O     1 
ATOM   300  C CB    . ASP A 1 51  ? 1.086  31.012  12.575 1.00 61.27  ?  51  ASP A CB    1 
ATOM   301  C CG    . ASP A 1 51  ? -0.123 30.836  11.645 1.00 74.15  ?  51  ASP A CG    1 
ATOM   302  O OD1   . ASP A 1 51  ? -1.216 30.415  12.122 1.00 72.36  ?  51  ASP A OD1   1 
ATOM   303  O OD2   . ASP A 1 51  ? 0.023  31.128  10.432 1.00 70.51  -1 51  ASP A OD2   1 
ATOM   304  N N     . SER A 1 52  ? 4.126  31.551  12.527 1.00 61.49  ?  52  SER A N     1 
ATOM   305  C CA    . SER A 1 52  ? 5.508  31.436  12.995 1.00 51.10  ?  52  SER A CA    1 
ATOM   306  C C     . SER A 1 52  ? 6.320  30.682  11.947 1.00 55.39  ?  52  SER A C     1 
ATOM   307  O O     . SER A 1 52  ? 5.760  29.985  11.095 1.00 62.00  ?  52  SER A O     1 
ATOM   308  C CB    . SER A 1 52  ? 5.582  30.715  14.330 1.00 55.27  ?  52  SER A CB    1 
ATOM   309  O OG    . SER A 1 52  ? 5.262  29.350  14.131 1.00 60.92  ?  52  SER A OG    1 
ATOM   310  N N     . TYR A 1 53  ? 7.651  30.816  12.028 1.00 52.54  ?  53  TYR A N     1 
ATOM   311  C CA    . TYR A 1 53  ? 8.575  30.183  11.084 1.00 54.18  ?  53  TYR A CA    1 
ATOM   312  C C     . TYR A 1 53  ? 9.725  29.481  11.816 1.00 50.10  ?  53  TYR A C     1 
ATOM   313  O O     . TYR A 1 53  ? 10.280 30.009  12.789 1.00 46.65  ?  53  TYR A O     1 
ATOM   314  C CB    . TYR A 1 53  ? 9.147  31.230  10.082 1.00 57.91  ?  53  TYR A CB    1 
ATOM   315  C CG    . TYR A 1 53  ? 8.165  31.726  9.022  1.00 61.63  ?  53  TYR A CG    1 
ATOM   316  C CD1   . TYR A 1 53  ? 7.496  32.945  9.172  1.00 54.22  ?  53  TYR A CD1   1 
ATOM   317  C CD2   . TYR A 1 53  ? 7.924  30.979  7.861  1.00 64.46  ?  53  TYR A CD2   1 
ATOM   318  C CE1   . TYR A 1 53  ? 6.606  33.395  8.204  1.00 58.52  ?  53  TYR A CE1   1 
ATOM   319  C CE2   . TYR A 1 53  ? 7.030  31.419  6.883  1.00 62.95  ?  53  TYR A CE2   1 
ATOM   320  C CZ    . TYR A 1 53  ? 6.371  32.628  7.056  1.00 65.21  ?  53  TYR A CZ    1 
ATOM   321  O OH    . TYR A 1 53  ? 5.481  33.066  6.083  1.00 64.45  ?  53  TYR A OH    1 
ATOM   322  N N     . VAL A 1 54  ? 10.101 28.301  11.335 1.00 47.78  ?  54  VAL A N     1 
ATOM   323  C CA    . VAL A 1 54  ? 11.190 27.542  11.936 1.00 48.18  ?  54  VAL A CA    1 
ATOM   324  C C     . VAL A 1 54  ? 12.297 27.328  10.901 1.00 53.54  ?  54  VAL A C     1 
ATOM   325  O O     . VAL A 1 54  ? 12.049 27.245  9.692  1.00 55.36  ?  54  VAL A O     1 
ATOM   326  C CB    . VAL A 1 54  ? 10.688 26.189  12.507 1.00 50.18  ?  54  VAL A CB    1 
ATOM   327  C CG1   . VAL A 1 54  ? 11.854 25.264  12.868 1.00 45.38  ?  54  VAL A CG1   1 
ATOM   328  C CG2   . VAL A 1 54  ? 9.809  26.414  13.740 1.00 47.48  ?  54  VAL A CG2   1 
ATOM   329  N N     . GLY A 1 55  ? 13.537 27.284  11.384 1.00 47.34  ?  55  GLY A N     1 
ATOM   330  C CA    . GLY A 1 55  ? 14.608 26.675  10.598 1.00 46.22  ?  55  GLY A CA    1 
ATOM   331  C C     . GLY A 1 55  ? 15.086 27.497  9.412  1.00 46.31  ?  55  GLY A C     1 
ATOM   332  O O     . GLY A 1 55  ? 15.459 28.668  9.526  1.00 46.02  ?  55  GLY A O     1 
ATOM   333  N N     . ASP A 1 56  ? 15.127 26.858  8.249  1.00 51.18  ?  56  ASP A N     1 
ATOM   334  C CA    . ASP A 1 56  ? 15.784 27.491  7.113  1.00 52.20  ?  56  ASP A CA    1 
ATOM   335  C C     . ASP A 1 56  ? 14.971 28.650  6.582  1.00 52.85  ?  56  ASP A C     1 
ATOM   336  O O     . ASP A 1 56  ? 15.534 29.639  6.100  1.00 49.50  ?  56  ASP A O     1 
ATOM   337  C CB    . ASP A 1 56  ? 16.036 26.452  6.033  1.00 51.94  ?  56  ASP A CB    1 
ATOM   338  C CG    . ASP A 1 56  ? 17.331 25.727  6.255  1.00 53.69  ?  56  ASP A CG    1 
ATOM   339  O OD1   . ASP A 1 56  ? 17.380 24.473  6.125  1.00 50.22  ?  56  ASP A OD1   1 
ATOM   340  O OD2   . ASP A 1 56  ? 18.304 26.449  6.589  1.00 53.31  -1 56  ASP A OD2   1 
ATOM   341  N N     . GLU A 1 57  ? 13.649 28.541  6.695  1.00 60.14  ?  57  GLU A N     1 
ATOM   342  C CA    . GLU A 1 57  ? 12.737 29.590  6.267  1.00 60.24  ?  57  GLU A CA    1 
ATOM   343  C C     . GLU A 1 57  ? 12.781 30.787  7.199  1.00 56.21  ?  57  GLU A C     1 
ATOM   344  O O     . GLU A 1 57  ? 12.627 31.925  6.748  1.00 58.68  ?  57  GLU A O     1 
ATOM   345  C CB    . GLU A 1 57  ? 11.337 29.001  6.190  1.00 65.20  ?  57  GLU A CB    1 
ATOM   346  C CG    . GLU A 1 57  ? 11.437 27.472  6.308  1.00 74.39  ?  57  GLU A CG    1 
ATOM   347  C CD    . GLU A 1 57  ? 10.123 26.785  6.641  1.00 86.72  ?  57  GLU A CD    1 
ATOM   348  O OE1   . GLU A 1 57  ? 9.217  27.456  7.219  1.00 83.23  ?  57  GLU A OE1   1 
ATOM   349  O OE2   . GLU A 1 57  ? 10.018 25.565  6.324  1.00 88.49  -1 57  GLU A OE2   1 
ATOM   350  N N     . ALA A 1 58  ? 13.002 30.563  8.491  1.00 50.46  ?  58  ALA A N     1 
ATOM   351  C CA    . ALA A 1 58  ? 13.040 31.691  9.406  1.00 48.55  ?  58  ALA A CA    1 
ATOM   352  C C     . ALA A 1 58  ? 14.311 32.505  9.254  1.00 49.82  ?  58  ALA A C     1 
ATOM   353  O O     . ALA A 1 58  ? 14.332 33.674  9.652  1.00 49.26  ?  58  ALA A O     1 
ATOM   354  C CB    . ALA A 1 58  ? 12.893 31.211  10.840 1.00 47.67  ?  58  ALA A CB    1 
ATOM   355  N N     . GLN A 1 59  ? 15.360 31.937  8.664  1.00 54.81  ?  59  GLN A N     1 
ATOM   356  C CA    . GLN A 1 59  ? 16.587 32.732  8.380  1.00 50.95  ?  59  GLN A CA    1 
ATOM   357  C C     . GLN A 1 59  ? 16.343 33.491  7.077  1.00 51.35  ?  59  GLN A C     1 
ATOM   358  O O     . GLN A 1 59  ? 16.782 34.633  6.962  1.00 53.02  ?  59  GLN A O     1 
ATOM   359  C CB    . GLN A 1 59  ? 17.821 31.827  8.360  1.00 50.51  ?  59  GLN A CB    1 
ATOM   360  C CG    . GLN A 1 59  ? 19.057 32.441  7.719  1.00 56.92  ?  59  GLN A CG    1 
ATOM   361  C CD    . GLN A 1 59  ? 19.859 33.306  8.660  1.00 62.68  ?  59  GLN A CD    1 
ATOM   362  O OE1   . GLN A 1 59  ? 19.572 33.402  9.850  1.00 63.62  ?  59  GLN A OE1   1 
ATOM   363  N NE2   . GLN A 1 59  ? 20.882 33.951  8.125  1.00 61.06  ?  59  GLN A NE2   1 
ATOM   364  N N     . SER A 1 60  ? 15.591 32.893  6.162  1.00 52.29  ?  60  SER A N     1 
ATOM   365  C CA    . SER A 1 60  ? 15.241 33.568  4.892  1.00 49.33  ?  60  SER A CA    1 
ATOM   366  C C     . SER A 1 60  ? 14.390 34.809  5.159  1.00 55.40  ?  60  SER A C     1 
ATOM   367  O O     . SER A 1 60  ? 14.502 35.768  4.378  1.00 55.71  ?  60  SER A O     1 
ATOM   368  C CB    . SER A 1 60  ? 14.515 32.621  4.004  1.00 52.13  ?  60  SER A CB    1 
ATOM   369  O OG    . SER A 1 60  ? 15.158 31.359  3.982  1.00 61.11  ?  60  SER A OG    1 
ATOM   370  N N     . LYS A 1 61  ? 13.571 34.795  6.210  1.00 53.55  ?  61  LYS A N     1 
ATOM   371  C CA    . LYS A 1 61  ? 12.647 35.923  6.482  1.00 48.44  ?  61  LYS A CA    1 
ATOM   372  C C     . LYS A 1 61  ? 13.107 36.678  7.723  1.00 50.13  ?  61  LYS A C     1 
ATOM   373  O O     . LYS A 1 61  ? 12.290 37.370  8.307  1.00 49.72  ?  61  LYS A O     1 
ATOM   374  C CB    . LYS A 1 61  ? 11.222 35.390  6.579  1.00 47.91  ?  61  LYS A CB    1 
ATOM   375  C CG    . LYS A 1 61  ? 10.662 34.822  5.284  1.00 55.54  ?  61  LYS A CG    1 
ATOM   376  C CD    . LYS A 1 61  ? 9.671  33.712  5.509  1.00 60.06  ?  61  LYS A CD    1 
ATOM   377  C CE    . LYS A 1 61  ? 9.542  32.783  4.324  1.00 59.71  ?  61  LYS A CE    1 
ATOM   378  N NZ    . LYS A 1 61  ? 8.188  32.847  3.727  1.00 60.34  ?  61  LYS A NZ    1 
ATOM   379  N N     . ARG A 1 62  ? 14.384 36.585  8.063  1.00 50.05  ?  62  ARG A N     1 
ATOM   380  C CA    . ARG A 1 62  ? 14.986 37.306  9.209  1.00 48.20  ?  62  ARG A CA    1 
ATOM   381  C C     . ARG A 1 62  ? 14.507 38.749  9.323  1.00 51.21  ?  62  ARG A C     1 
ATOM   382  O O     . ARG A 1 62  ? 14.437 39.231  10.456 1.00 57.47  ?  62  ARG A O     1 
ATOM   383  C CB    . ARG A 1 62  ? 16.467 37.467  8.871  1.00 52.62  ?  62  ARG A CB    1 
ATOM   384  C CG    . ARG A 1 62  ? 17.463 36.892  9.862  1.00 56.65  ?  62  ARG A CG    1 
ATOM   385  C CD    . ARG A 1 62  ? 18.834 36.932  9.217  1.00 55.71  ?  62  ARG A CD    1 
ATOM   386  N NE    . ARG A 1 62  ? 18.741 36.543  7.818  1.00 57.56  ?  62  ARG A NE    1 
ATOM   387  C CZ    . ARG A 1 62  ? 19.448 37.073  6.828  1.00 61.16  ?  62  ARG A CZ    1 
ATOM   388  N NH1   . ARG A 1 62  ? 19.278 36.641  5.590  1.00 59.95  ?  62  ARG A NH1   1 
ATOM   389  N NH2   . ARG A 1 62  ? 20.314 38.035  7.073  1.00 55.66  ?  62  ARG A NH2   1 
ATOM   390  N N     . GLY A 1 63  ? 14.256 39.439  8.211  1.00 50.10  ?  63  GLY A N     1 
ATOM   391  C CA    . GLY A 1 63  ? 13.933 40.878  8.263  1.00 50.49  ?  63  GLY A CA    1 
ATOM   392  C C     . GLY A 1 63  ? 12.492 41.173  8.604  1.00 53.64  ?  63  GLY A C     1 
ATOM   393  O O     . GLY A 1 63  ? 12.203 42.320  8.936  1.00 50.13  ?  63  GLY A O     1 
ATOM   394  N N     . ILE A 1 64  ? 11.609 40.191  8.461  1.00 54.33  ?  64  ILE A N     1 
ATOM   395  C CA    . ILE A 1 64  ? 10.186 40.374  8.853  1.00 51.54  ?  64  ILE A CA    1 
ATOM   396  C C     . ILE A 1 64  ? 9.964  39.569  10.127 1.00 52.33  ?  64  ILE A C     1 
ATOM   397  O O     . ILE A 1 64  ? 8.812  39.448  10.533 1.00 54.74  ?  64  ILE A O     1 
ATOM   398  C CB    . ILE A 1 64  ? 9.239  39.948  7.719  1.00 47.89  ?  64  ILE A CB    1 
ATOM   399  C CG1   . ILE A 1 64  ? 9.211  38.433  7.509  1.00 48.58  ?  64  ILE A CG1   1 
ATOM   400  C CG2   . ILE A 1 64  ? 9.574  40.686  6.436  1.00 45.71  ?  64  ILE A CG2   1 
ATOM   401  C CD1   . ILE A 1 64  ? 8.372  37.993  6.341  1.00 46.07  ?  64  ILE A CD1   1 
ATOM   402  N N     . LEU A 1 65  ? 11.041 39.090  10.752 1.00 52.58  ?  65  LEU A N     1 
ATOM   403  C CA    . LEU A 1 65  ? 10.884 38.201  11.928 1.00 51.02  ?  65  LEU A CA    1 
ATOM   404  C C     . LEU A 1 65  ? 11.794 38.560  13.104 1.00 53.04  ?  65  LEU A C     1 
ATOM   405  O O     . LEU A 1 65  ? 12.801 39.232  12.882 1.00 50.97  ?  65  LEU A O     1 
ATOM   406  C CB    . LEU A 1 65  ? 11.162 36.747  11.525 1.00 51.76  ?  65  LEU A CB    1 
ATOM   407  C CG    . LEU A 1 65  ? 10.277 36.081  10.475 1.00 50.57  ?  65  LEU A CG    1 
ATOM   408  C CD1   . LEU A 1 65  ? 10.771 34.674  10.209 1.00 52.42  ?  65  LEU A CD1   1 
ATOM   409  C CD2   . LEU A 1 65  ? 8.824  36.042  10.893 1.00 50.06  ?  65  LEU A CD2   1 
ATOM   410  N N     . THR A 1 66  ? 11.412 38.153  14.314 1.00 52.97  ?  66  THR A N     1 
ATOM   411  C CA    . THR A 1 66  ? 12.210 38.275  15.535 1.00 50.61  ?  66  THR A CA    1 
ATOM   412  C C     . THR A 1 66  ? 12.677 36.865  15.905 1.00 53.57  ?  66  THR A C     1 
ATOM   413  O O     . THR A 1 66  ? 11.904 36.060  16.441 1.00 51.81  ?  66  THR A O     1 
ATOM   414  C CB    . THR A 1 66  ? 11.415 38.922  16.667 1.00 49.87  ?  66  THR A CB    1 
ATOM   415  O OG1   . THR A 1 66  ? 11.311 40.326  16.436 1.00 57.85  ?  66  THR A OG1   1 
ATOM   416  C CG2   . THR A 1 66  ? 12.100 38.713  18.014 1.00 49.33  ?  66  THR A CG2   1 
ATOM   417  N N     . LEU A 1 67  ? 13.948 36.578  15.615 1.00 56.08  ?  67  LEU A N     1 
ATOM   418  C CA    . LEU A 1 67  ? 14.509 35.250  15.802 1.00 50.07  ?  67  LEU A CA    1 
ATOM   419  C C     . LEU A 1 67  ? 14.770 34.980  17.282 1.00 54.24  ?  67  LEU A C     1 
ATOM   420  O O     . LEU A 1 67  ? 15.064 35.888  18.065 1.00 52.22  ?  67  LEU A O     1 
ATOM   421  C CB    . LEU A 1 67  ? 15.796 35.099  14.994 1.00 49.02  ?  67  LEU A CB    1 
ATOM   422  C CG    . LEU A 1 67  ? 15.639 34.665  13.527 1.00 51.61  ?  67  LEU A CG    1 
ATOM   423  C CD1   . LEU A 1 67  ? 14.471 35.356  12.868 1.00 50.18  ?  67  LEU A CD1   1 
ATOM   424  C CD2   . LEU A 1 67  ? 16.908 34.916  12.715 1.00 50.27  ?  67  LEU A CD2   1 
ATOM   425  N N     . LYS A 1 68  ? 14.612 33.716  17.667 1.00 54.12  ?  68  LYS A N     1 
ATOM   426  C CA    . LYS A 1 68  ? 14.885 33.259  19.019 1.00 48.86  ?  68  LYS A CA    1 
ATOM   427  C C     . LYS A 1 68  ? 15.610 31.928  18.888 1.00 46.14  ?  68  LYS A C     1 
ATOM   428  O O     . LYS A 1 68  ? 15.222 31.096  18.068 1.00 44.25  ?  68  LYS A O     1 
ATOM   429  C CB    . LYS A 1 68  ? 13.595 33.123  19.839 1.00 48.63  ?  68  LYS A CB    1 
ATOM   430  C CG    . LYS A 1 68  ? 13.187 34.382  20.619 1.00 49.47  ?  68  LYS A CG    1 
ATOM   431  C CD    . LYS A 1 68  ? 11.920 34.156  21.472 1.00 46.97  ?  68  LYS A CD    1 
ATOM   432  C CE    . LYS A 1 68  ? 12.038 34.802  22.874 1.00 63.12  ?  68  LYS A CE    1 
ATOM   433  N NZ    . LYS A 1 68  ? 12.757 33.961  23.908 1.00 70.05  ?  68  LYS A NZ    1 
ATOM   434  N N     . TYR A 1 69  ? 16.704 31.759  19.630 1.00 49.24  ?  69  TYR A N     1 
ATOM   435  C CA    . TYR A 1 69  ? 17.446 30.508  19.666 1.00 48.21  ?  69  TYR A CA    1 
ATOM   436  C C     . TYR A 1 69  ? 16.991 29.761  20.910 1.00 47.78  ?  69  TYR A C     1 
ATOM   437  O O     . TYR A 1 69  ? 17.476 30.047  22.018 1.00 47.22  ?  69  TYR A O     1 
ATOM   438  C CB    . TYR A 1 69  ? 18.956 30.756  19.699 1.00 52.47  ?  69  TYR A CB    1 
ATOM   439  C CG    . TYR A 1 69  ? 19.508 31.333  18.404 1.00 61.19  ?  69  TYR A CG    1 
ATOM   440  C CD1   . TYR A 1 69  ? 20.675 30.811  17.822 1.00 61.66  ?  69  TYR A CD1   1 
ATOM   441  C CD2   . TYR A 1 69  ? 18.866 32.403  17.761 1.00 58.43  ?  69  TYR A CD2   1 
ATOM   442  C CE1   . TYR A 1 69  ? 21.183 31.328  16.628 1.00 68.50  ?  69  TYR A CE1   1 
ATOM   443  C CE2   . TYR A 1 69  ? 19.358 32.933  16.567 1.00 65.10  ?  69  TYR A CE2   1 
ATOM   444  C CZ    . TYR A 1 69  ? 20.518 32.396  15.999 1.00 81.84  ?  69  TYR A CZ    1 
ATOM   445  O OH    . TYR A 1 69  ? 21.000 32.934  14.809 1.00 90.31  ?  69  TYR A OH    1 
ATOM   446  N N     . PRO A 1 70  ? 16.033 28.842  20.806 1.00 43.23  ?  70  PRO A N     1 
ATOM   447  C CA    . PRO A 1 70  ? 15.478 28.251  22.021 1.00 42.03  ?  70  PRO A CA    1 
ATOM   448  C C     . PRO A 1 70  ? 16.477 27.376  22.750 1.00 46.22  ?  70  PRO A C     1 
ATOM   449  O O     . PRO A 1 70  ? 16.191 26.925  23.871 1.00 42.43  ?  70  PRO A O     1 
ATOM   450  C CB    . PRO A 1 70  ? 14.270 27.453  21.504 1.00 42.05  ?  70  PRO A CB    1 
ATOM   451  C CG    . PRO A 1 70  ? 14.597 27.127  20.084 1.00 40.89  ?  70  PRO A CG    1 
ATOM   452  C CD    . PRO A 1 70  ? 15.489 28.233  19.576 1.00 44.59  ?  70  PRO A CD    1 
ATOM   453  N N     . ILE A 1 71  ? 17.656 27.159  22.173 1.00 44.66  ?  71  ILE A N     1 
ATOM   454  C CA    . ILE A 1 71  ? 18.601 26.206  22.735 1.00 44.10  ?  71  ILE A CA    1 
ATOM   455  C C     . ILE A 1 71  ? 20.021 26.757  22.578 1.00 45.89  ?  71  ILE A C     1 
ATOM   456  O O     . ILE A 1 71  ? 20.977 26.021  22.302 1.00 43.40  ?  71  ILE A O     1 
ATOM   457  C CB    . ILE A 1 71  ? 18.374 24.848  22.056 1.00 44.70  ?  71  ILE A CB    1 
ATOM   458  C CG1   . ILE A 1 71  ? 19.341 23.798  22.561 1.00 42.79  ?  71  ILE A CG1   1 
ATOM   459  C CG2   . ILE A 1 71  ? 18.387 24.995  20.524 1.00 44.19  ?  71  ILE A CG2   1 
ATOM   460  C CD1   . ILE A 1 71  ? 18.799 22.418  22.313 1.00 43.69  ?  71  ILE A CD1   1 
ATOM   461  N N     . GLU A 1 72  ? 20.147 28.068  22.833 1.00 50.52  ?  72  GLU A N     1 
ATOM   462  C CA    . GLU A 1 72  ? 21.318 28.865  22.472 1.00 47.94  ?  72  GLU A CA    1 
ATOM   463  C C     . GLU A 1 72  ? 22.601 28.312  23.078 1.00 50.33  ?  72  GLU A C     1 
ATOM   464  O O     . GLU A 1 72  ? 23.633 28.238  22.399 1.00 53.99  ?  72  GLU A O     1 
ATOM   465  C CB    . GLU A 1 72  ? 21.084 30.308  22.928 1.00 50.76  ?  72  GLU A CB    1 
ATOM   466  C CG    . GLU A 1 72  ? 21.922 31.386  22.268 1.00 57.83  ?  72  GLU A CG    1 
ATOM   467  C CD    . GLU A 1 72  ? 22.167 32.591  23.191 1.00 64.09  ?  72  GLU A CD    1 
ATOM   468  O OE1   . GLU A 1 72  ? 21.258 32.967  23.962 1.00 62.37  ?  72  GLU A OE1   1 
ATOM   469  O OE2   . GLU A 1 72  ? 23.287 33.152  23.158 1.00 72.76  -1 72  GLU A OE2   1 
ATOM   470  N N     . HIS A 1 73  ? 22.569 27.938  24.354 1.00 46.23  ?  73  HIS A N     1 
ATOM   471  C CA    . HIS A 1 73  ? 23.758 27.475  25.054 1.00 46.58  ?  73  HIS A CA    1 
ATOM   472  C C     . HIS A 1 73  ? 23.717 25.976  25.333 1.00 50.49  ?  73  HIS A C     1 
ATOM   473  O O     . HIS A 1 73  ? 24.325 25.506  26.301 1.00 47.76  ?  73  HIS A O     1 
ATOM   474  C CB    . HIS A 1 73  ? 23.940 28.252  26.351 1.00 52.47  ?  73  HIS A CB    1 
ATOM   475  C CG    . HIS A 1 73  ? 24.117 29.722  26.144 1.00 58.01  ?  73  HIS A CG    1 
ATOM   476  N ND1   . HIS A 1 73  ? 25.250 30.262  25.567 1.00 59.88  ?  73  HIS A ND1   1 
ATOM   477  C CD2   . HIS A 1 73  ? 23.294 30.764  26.415 1.00 55.81  ?  73  HIS A CD2   1 
ATOM   478  C CE1   . HIS A 1 73  ? 25.120 31.576  25.499 1.00 62.53  ?  73  HIS A CE1   1 
ATOM   479  N NE2   . HIS A 1 73  ? 23.942 31.905  26.005 1.00 62.84  ?  73  HIS A NE2   1 
ATOM   480  N N     . GLY A 1 74  ? 23.010 25.214  24.485 1.00 46.28  ?  74  GLY A N     1 
ATOM   481  C CA    . GLY A 1 74  ? 22.997 23.776  24.547 1.00 36.92  ?  74  GLY A CA    1 
ATOM   482  C C     . GLY A 1 74  ? 21.901 23.186  25.403 1.00 41.98  ?  74  GLY A C     1 
ATOM   483  O O     . GLY A 1 74  ? 21.534 22.021  25.197 1.00 40.14  ?  74  GLY A O     1 
ATOM   484  N N     . ILE A 1 75  ? 21.362 23.957  26.347 1.00 41.61  ?  75  ILE A N     1 
ATOM   485  C CA    . ILE A 1 75  ? 20.266 23.527  27.212 1.00 41.47  ?  75  ILE A CA    1 
ATOM   486  C C     . ILE A 1 75  ? 19.001 24.219  26.729 1.00 41.91  ?  75  ILE A C     1 
ATOM   487  O O     . ILE A 1 75  ? 18.980 25.451  26.626 1.00 45.13  ?  75  ILE A O     1 
ATOM   488  C CB    . ILE A 1 75  ? 20.555 23.873  28.680 1.00 40.27  ?  75  ILE A CB    1 
ATOM   489  C CG1   . ILE A 1 75  ? 21.682 22.990  29.224 1.00 37.07  ?  75  ILE A CG1   1 
ATOM   490  C CG2   . ILE A 1 75  ? 19.307 23.728  29.511 1.00 34.15  ?  75  ILE A CG2   1 
ATOM   491  C CD1   . ILE A 1 75  ? 21.931 23.204  30.682 1.00 41.36  ?  75  ILE A CD1   1 
ATOM   492  N N     . VAL A 1 76  ? 17.948 23.456  26.407 1.00 42.50  ?  76  VAL A N     1 
ATOM   493  C CA    . VAL A 1 76  ? 16.758 24.113  25.870 1.00 43.03  ?  76  VAL A CA    1 
ATOM   494  C C     . VAL A 1 76  ? 16.136 24.956  26.971 1.00 43.54  ?  76  VAL A C     1 
ATOM   495  O O     . VAL A 1 76  ? 15.987 24.507  28.115 1.00 42.29  ?  76  VAL A O     1 
ATOM   496  C CB    . VAL A 1 76  ? 15.744 23.123  25.262 1.00 36.73  ?  76  VAL A CB    1 
ATOM   497  C CG1   . VAL A 1 76  ? 16.307 21.727  25.076 1.00 32.61  ?  76  VAL A CG1   1 
ATOM   498  C CG2   . VAL A 1 76  ? 14.472 23.127  26.061 1.00 40.17  ?  76  VAL A CG2   1 
ATOM   499  N N     . THR A 1 77  ? 15.808 26.202  26.633 1.00 47.46  ?  77  THR A N     1 
ATOM   500  C CA    . THR A 1 77  ? 15.382 27.219  27.587 1.00 47.62  ?  77  THR A CA    1 
ATOM   501  C C     . THR A 1 77  ? 13.947 27.690  27.383 1.00 51.82  ?  77  THR A C     1 
ATOM   502  O O     . THR A 1 77  ? 13.289 28.054  28.356 1.00 57.16  ?  77  THR A O     1 
ATOM   503  C CB    . THR A 1 77  ? 16.314 28.439  27.509 1.00 44.06  ?  77  THR A CB    1 
ATOM   504  O OG1   . THR A 1 77  ? 16.145 29.077  26.236 1.00 43.58  ?  77  THR A OG1   1 
ATOM   505  C CG2   . THR A 1 77  ? 17.779 28.023  27.683 1.00 42.37  ?  77  THR A CG2   1 
ATOM   506  N N     . ASN A 1 78  ? 13.440 27.678  26.150 1.00 52.32  ?  78  ASN A N     1 
ATOM   507  C CA    . ASN A 1 78  ? 12.083 28.118  25.836 1.00 56.01  ?  78  ASN A CA    1 
ATOM   508  C C     . ASN A 1 78  ? 11.268 26.944  25.294 1.00 50.84  ?  78  ASN A C     1 
ATOM   509  O O     . ASN A 1 78  ? 11.422 26.570  24.126 1.00 46.27  ?  78  ASN A O     1 
ATOM   510  C CB    . ASN A 1 78  ? 12.122 29.266  24.833 1.00 55.51  ?  78  ASN A CB    1 
ATOM   511  C CG    . ASN A 1 78  ? 10.748 29.761  24.476 1.00 56.63  ?  78  ASN A CG    1 
ATOM   512  O OD1   . ASN A 1 78  ? 9.752  29.066  24.682 1.00 54.02  ?  78  ASN A OD1   1 
ATOM   513  N ND2   . ASN A 1 78  ? 10.679 30.982  23.950 1.00 67.92  ?  78  ASN A ND2   1 
ATOM   514  N N     . TRP A 1 79  ? 10.362 26.395  26.123 1.00 47.91  ?  79  TRP A N     1 
ATOM   515  C CA    . TRP A 1 79  ? 9.683  25.152  25.759 1.00 42.79  ?  79  TRP A CA    1 
ATOM   516  C C     . TRP A 1 79  ? 8.587  25.329  24.721 1.00 43.34  ?  79  TRP A C     1 
ATOM   517  O O     . TRP A 1 79  ? 8.228  24.344  24.070 1.00 41.40  ?  79  TRP A O     1 
ATOM   518  C CB    . TRP A 1 79  ? 9.095  24.474  26.990 1.00 38.04  ?  79  TRP A CB    1 
ATOM   519  C CG    . TRP A 1 79  ? 10.141 23.883  27.824 1.00 39.90  ?  79  TRP A CG    1 
ATOM   520  C CD1   . TRP A 1 79  ? 10.538 24.310  29.052 1.00 41.42  ?  79  TRP A CD1   1 
ATOM   521  C CD2   . TRP A 1 79  ? 10.971 22.760  27.498 1.00 39.13  ?  79  TRP A CD2   1 
ATOM   522  N NE1   . TRP A 1 79  ? 11.559 23.518  29.523 1.00 42.38  ?  79  TRP A NE1   1 
ATOM   523  C CE2   . TRP A 1 79  ? 11.841 22.554  28.586 1.00 44.07  ?  79  TRP A CE2   1 
ATOM   524  C CE3   . TRP A 1 79  ? 11.056 21.906  26.406 1.00 34.93  ?  79  TRP A CE3   1 
ATOM   525  C CZ2   . TRP A 1 79  ? 12.796 21.528  28.601 1.00 38.24  ?  79  TRP A CZ2   1 
ATOM   526  C CZ3   . TRP A 1 79  ? 12.003 20.893  26.427 1.00 38.34  ?  79  TRP A CZ3   1 
ATOM   527  C CH2   . TRP A 1 79  ? 12.857 20.715  27.517 1.00 36.79  ?  79  TRP A CH2   1 
ATOM   528  N N     . ASP A 1 80  ? 8.053  26.546  24.546 1.00 49.28  ?  80  ASP A N     1 
ATOM   529  C CA    . ASP A 1 80  ? 7.059  26.772  23.497 1.00 50.56  ?  80  ASP A CA    1 
ATOM   530  C C     . ASP A 1 80  ? 7.712  26.727  22.119 1.00 50.01  ?  80  ASP A C     1 
ATOM   531  O O     . ASP A 1 80  ? 7.137  26.177  21.176 1.00 49.54  ?  80  ASP A O     1 
ATOM   532  C CB    . ASP A 1 80  ? 6.337  28.113  23.710 1.00 53.56  ?  80  ASP A CB    1 
ATOM   533  C CG    . ASP A 1 80  ? 5.157  28.022  24.700 1.00 64.23  ?  80  ASP A CG    1 
ATOM   534  O OD1   . ASP A 1 80  ? 4.876  29.032  25.401 1.00 66.48  ?  80  ASP A OD1   1 
ATOM   535  O OD2   . ASP A 1 80  ? 4.508  26.951  24.779 1.00 64.95  -1 80  ASP A OD2   1 
ATOM   536  N N     . ASP A 1 81  ? 8.926  27.284  21.997 1.00 49.38  ?  81  ASP A N     1 
ATOM   537  C CA    . ASP A 1 81  ? 9.686  27.240  20.747 1.00 47.87  ?  81  ASP A CA    1 
ATOM   538  C C     . ASP A 1 81  ? 10.282 25.857  20.474 1.00 43.92  ?  81  ASP A C     1 
ATOM   539  O O     . ASP A 1 81  ? 10.320 25.428  19.314 1.00 39.60  ?  81  ASP A O     1 
ATOM   540  C CB    . ASP A 1 81  ? 10.787 28.305  20.772 1.00 47.74  ?  81  ASP A CB    1 
ATOM   541  C CG    . ASP A 1 81  ? 10.234 29.727  21.007 1.00 57.66  ?  81  ASP A CG    1 
ATOM   542  O OD1   . ASP A 1 81  ? 8.990  29.916  20.949 1.00 60.15  ?  81  ASP A OD1   1 
ATOM   543  O OD2   . ASP A 1 81  ? 11.041 30.660  21.253 1.00 58.22  -1 81  ASP A OD2   1 
ATOM   544  N N     . MET A 1 82  ? 10.762 25.156  21.509 1.00 40.16  ?  82  MET A N     1 
ATOM   545  C CA    . MET A 1 82  ? 11.185 23.769  21.331 1.00 40.24  ?  82  MET A CA    1 
ATOM   546  C C     . MET A 1 82  ? 10.057 22.894  20.800 1.00 40.76  ?  82  MET A C     1 
ATOM   547  O O     . MET A 1 82  ? 10.284 22.039  19.935 1.00 38.05  ?  82  MET A O     1 
ATOM   548  C CB    . MET A 1 82  ? 11.700 23.195  22.646 1.00 40.72  ?  82  MET A CB    1 
ATOM   549  C CG    . MET A 1 82  ? 12.731 22.109  22.471 1.00 40.61  ?  82  MET A CG    1 
ATOM   550  S SD    . MET A 1 82  ? 14.012 22.555  21.253 1.00 43.20  ?  82  MET A SD    1 
ATOM   551  C CE    . MET A 1 82  ? 14.133 21.065  20.211 1.00 38.26  ?  82  MET A CE    1 
ATOM   552  N N     . GLU A 1 83  ? 8.843  23.061  21.336 1.00 42.55  ?  83  GLU A N     1 
ATOM   553  C CA    . GLU A 1 83  ? 7.686  22.337  20.811 1.00 42.00  ?  83  GLU A CA    1 
ATOM   554  C C     . GLU A 1 83  ? 7.555  22.540  19.309 1.00 35.19  ?  83  GLU A C     1 
ATOM   555  O O     . GLU A 1 83  ? 7.215  21.609  18.579 1.00 37.54  ?  83  GLU A O     1 
ATOM   556  C CB    . GLU A 1 83  ? 6.406  22.804  21.524 1.00 47.40  ?  83  GLU A CB    1 
ATOM   557  C CG    . GLU A 1 83  ? 5.481  21.732  22.125 1.00 49.81  ?  83  GLU A CG    1 
ATOM   558  C CD    . GLU A 1 83  ? 4.610  22.289  23.291 1.00 67.91  ?  83  GLU A CD    1 
ATOM   559  O OE1   . GLU A 1 83  ? 3.942  23.348  23.110 1.00 72.20  ?  83  GLU A OE1   1 
ATOM   560  O OE2   . GLU A 1 83  ? 4.593  21.671  24.392 1.00 66.96  -1 83  GLU A OE2   1 
ATOM   561  N N     . LYS A 1 84  ? 7.818  23.756  18.833 1.00 34.61  ?  84  LYS A N     1 
ATOM   562  C CA    . LYS A 1 84  ? 7.640  24.077  17.428 1.00 34.50  ?  84  LYS A CA    1 
ATOM   563  C C     . LYS A 1 84  ? 8.808  23.610  16.570 1.00 38.97  ?  84  LYS A C     1 
ATOM   564  O O     . LYS A 1 84  ? 8.602  23.230  15.415 1.00 38.51  ?  84  LYS A O     1 
ATOM   565  C CB    . LYS A 1 84  ? 7.443  25.576  17.273 1.00 41.09  ?  84  LYS A CB    1 
ATOM   566  C CG    . LYS A 1 84  ? 6.263  26.139  18.068 1.00 47.57  ?  84  LYS A CG    1 
ATOM   567  C CD    . LYS A 1 84  ? 6.460  27.621  18.382 1.00 53.74  ?  84  LYS A CD    1 
ATOM   568  C CE    . LYS A 1 84  ? 5.161  28.415  18.328 1.00 61.84  ?  84  LYS A CE    1 
ATOM   569  N NZ    . LYS A 1 84  ? 4.790  28.730  16.929 1.00 58.05  ?  84  LYS A NZ    1 
ATOM   570  N N     . ILE A 1 85  ? 10.035 23.645  17.097 1.00 39.39  ?  85  ILE A N     1 
ATOM   571  C CA    . ILE A 1 85  ? 11.156 23.034  16.394 1.00 34.65  ?  85  ILE A CA    1 
ATOM   572  C C     . ILE A 1 85  ? 10.870 21.560  16.152 1.00 36.12  ?  85  ILE A C     1 
ATOM   573  O O     . ILE A 1 85  ? 10.972 21.066  15.019 1.00 35.69  ?  85  ILE A O     1 
ATOM   574  C CB    . ILE A 1 85  ? 12.459 23.232  17.190 1.00 39.37  ?  85  ILE A CB    1 
ATOM   575  C CG1   . ILE A 1 85  ? 12.936 24.676  17.108 1.00 39.52  ?  85  ILE A CG1   1 
ATOM   576  C CG2   . ILE A 1 85  ? 13.559 22.329  16.667 1.00 32.62  ?  85  ILE A CG2   1 
ATOM   577  C CD1   . ILE A 1 85  ? 13.957 24.886  16.046 1.00 40.35  ?  85  ILE A CD1   1 
ATOM   578  N N     . TRP A 1 86  ? 10.492 20.836  17.219 1.00 32.59  ?  86  TRP A N     1 
ATOM   579  C CA    . TRP A 1 86  ? 10.298 19.394  17.108 1.00 31.49  ?  86  TRP A CA    1 
ATOM   580  C C     . TRP A 1 86  ? 9.166  19.072  16.184 1.00 30.69  ?  86  TRP A C     1 
ATOM   581  O O     . TRP A 1 86  ? 9.180  18.029  15.525 1.00 31.70  ?  86  TRP A O     1 
ATOM   582  C CB    . TRP A 1 86  ? 10.001 18.765  18.461 1.00 31.93  ?  86  TRP A CB    1 
ATOM   583  C CG    . TRP A 1 86  ? 11.205 18.441  19.206 1.00 34.32  ?  86  TRP A CG    1 
ATOM   584  C CD1   . TRP A 1 86  ? 12.403 18.032  18.694 1.00 34.72  ?  86  TRP A CD1   1 
ATOM   585  C CD2   . TRP A 1 86  ? 11.374 18.516  20.621 1.00 37.36  ?  86  TRP A CD2   1 
ATOM   586  N NE1   . TRP A 1 86  ? 13.311 17.850  19.711 1.00 37.15  ?  86  TRP A NE1   1 
ATOM   587  C CE2   . TRP A 1 86  ? 12.699 18.136  20.903 1.00 37.77  ?  86  TRP A CE2   1 
ATOM   588  C CE3   . TRP A 1 86  ? 10.531 18.875  21.679 1.00 38.00  ?  86  TRP A CE3   1 
ATOM   589  C CZ2   . TRP A 1 86  ? 13.196 18.087  22.199 1.00 41.57  ?  86  TRP A CZ2   1 
ATOM   590  C CZ3   . TRP A 1 86  ? 11.022 18.834  22.966 1.00 38.62  ?  86  TRP A CZ3   1 
ATOM   591  C CH2   . TRP A 1 86  ? 12.345 18.441  23.218 1.00 46.39  ?  86  TRP A CH2   1 
ATOM   592  N N     . HIS A 1 87  ? 8.153  19.927  16.172 1.00 31.58  ?  87  HIS A N     1 
ATOM   593  C CA    . HIS A 1 87  ? 7.033  19.737  15.274 1.00 31.33  ?  87  HIS A CA    1 
ATOM   594  C C     . HIS A 1 87  ? 7.479  19.911  13.835 1.00 33.50  ?  87  HIS A C     1 
ATOM   595  O O     . HIS A 1 87  ? 7.138  19.103  12.965 1.00 33.25  ?  87  HIS A O     1 
ATOM   596  C CB    . HIS A 1 87  ? 5.929  20.711  15.638 1.00 30.92  ?  87  HIS A CB    1 
ATOM   597  C CG    . HIS A 1 87  ? 4.687  20.536  14.831 1.00 35.66  ?  87  HIS A CG    1 
ATOM   598  N ND1   . HIS A 1 87  ? 4.548  21.054  13.563 1.00 33.26  ?  87  HIS A ND1   1 
ATOM   599  C CD2   . HIS A 1 87  ? 3.528  19.898  15.107 1.00 36.30  ?  87  HIS A CD2   1 
ATOM   600  C CE1   . HIS A 1 87  ? 3.361  20.736  13.086 1.00 34.30  ?  87  HIS A CE1   1 
ATOM   601  N NE2   . HIS A 1 87  ? 2.718  20.045  14.006 1.00 38.60  ?  87  HIS A NE2   1 
ATOM   602  N N     . HIS A 1 88  ? 8.291  20.932  13.584 1.00 35.85  ?  88  HIS A N     1 
ATOM   603  C CA    . HIS A 1 88  ? 8.840  21.145  12.252 1.00 37.30  ?  88  HIS A CA    1 
ATOM   604  C C     . HIS A 1 88  ? 9.747  19.999  11.837 1.00 36.18  ?  88  HIS A C     1 
ATOM   605  O O     . HIS A 1 88  ? 9.751  19.590  10.670 1.00 35.63  ?  88  HIS A O     1 
ATOM   606  C CB    . HIS A 1 88  ? 9.602  22.461  12.237 1.00 38.02  ?  88  HIS A CB    1 
ATOM   607  C CG    . HIS A 1 88  ? 10.207 22.779  10.917 1.00 40.47  ?  88  HIS A CG    1 
ATOM   608  N ND1   . HIS A 1 88  ? 9.454  23.170  9.833  1.00 42.05  ?  88  HIS A ND1   1 
ATOM   609  C CD2   . HIS A 1 88  ? 11.493 22.765  10.502 1.00 41.77  ?  88  HIS A CD2   1 
ATOM   610  C CE1   . HIS A 1 88  ? 10.252 23.397  8.808  1.00 47.98  ?  88  HIS A CE1   1 
ATOM   611  N NE2   . HIS A 1 88  ? 11.494 23.155  9.187  1.00 48.98  ?  88  HIS A NE2   1 
ATOM   612  N N     . THR A 1 89  ? 10.530 19.479  12.785 1.00 31.99  ?  89  THR A N     1 
ATOM   613  C CA    . THR A 1 89  ? 11.402 18.348  12.505 1.00 30.94  ?  89  THR A CA    1 
ATOM   614  C C     . THR A 1 89  ? 10.608 17.146  12.027 1.00 35.25  ?  89  THR A C     1 
ATOM   615  O O     . THR A 1 89  ? 10.901 16.577  10.970 1.00 39.28  ?  89  THR A O     1 
ATOM   616  C CB    . THR A 1 89  ? 12.200 18.003  13.757 1.00 33.61  ?  89  THR A CB    1 
ATOM   617  O OG1   . THR A 1 89  ? 12.945 19.154  14.156 1.00 35.02  ?  89  THR A OG1   1 
ATOM   618  C CG2   . THR A 1 89  ? 13.151 16.836  13.504 1.00 27.66  ?  89  THR A CG2   1 
ATOM   619  N N     . PHE A 1 90  ? 9.576  16.758  12.785 1.00 38.22  ?  90  PHE A N     1 
ATOM   620  C CA    . PHE A 1 90  ? 8.818  15.545  12.490 1.00 36.60  ?  90  PHE A CA    1 
ATOM   621  C C     . PHE A 1 90  ? 8.004  15.656  11.196 1.00 39.30  ?  90  PHE A C     1 
ATOM   622  O O     . PHE A 1 90  ? 7.926  14.696  10.419 1.00 34.81  ?  90  PHE A O     1 
ATOM   623  C CB    . PHE A 1 90  ? 7.897  15.251  13.661 1.00 35.98  ?  90  PHE A CB    1 
ATOM   624  C CG    . PHE A 1 90  ? 8.600  14.752  14.872 1.00 35.86  ?  90  PHE A CG    1 
ATOM   625  C CD1   . PHE A 1 90  ? 9.792  14.044  14.752 1.00 36.03  ?  90  PHE A CD1   1 
ATOM   626  C CD2   . PHE A 1 90  ? 8.065  14.973  16.137 1.00 34.67  ?  90  PHE A CD2   1 
ATOM   627  C CE1   . PHE A 1 90  ? 10.445 13.562  15.878 1.00 35.09  ?  90  PHE A CE1   1 
ATOM   628  C CE2   . PHE A 1 90  ? 8.695  14.499  17.274 1.00 35.04  ?  90  PHE A CE2   1 
ATOM   629  C CZ    . PHE A 1 90  ? 9.888  13.787  17.154 1.00 38.40  ?  90  PHE A CZ    1 
ATOM   630  N N     . TYR A 1 91  ? 7.387  16.816  10.952 1.00 39.49  ?  91  TYR A N     1 
ATOM   631  C CA    . TYR A 1 91  ? 6.316  16.953  9.973  1.00 42.07  ?  91  TYR A CA    1 
ATOM   632  C C     . TYR A 1 91  ? 6.742  17.608  8.663  1.00 45.13  ?  91  TYR A C     1 
ATOM   633  O O     . TYR A 1 91  ? 6.170  17.285  7.615  1.00 48.11  ?  91  TYR A O     1 
ATOM   634  C CB    . TYR A 1 91  ? 5.154  17.754  10.587 1.00 42.00  ?  91  TYR A CB    1 
ATOM   635  C CG    . TYR A 1 91  ? 4.334  16.994  11.624 1.00 41.71  ?  91  TYR A CG    1 
ATOM   636  C CD1   . TYR A 1 91  ? 3.595  15.871  11.265 1.00 41.61  ?  91  TYR A CD1   1 
ATOM   637  C CD2   . TYR A 1 91  ? 4.294  17.403  12.951 1.00 37.64  ?  91  TYR A CD2   1 
ATOM   638  C CE1   . TYR A 1 91  ? 2.851  15.187  12.191 1.00 41.34  ?  91  TYR A CE1   1 
ATOM   639  C CE2   . TYR A 1 91  ? 3.548  16.718  13.877 1.00 38.03  ?  91  TYR A CE2   1 
ATOM   640  C CZ    . TYR A 1 91  ? 2.829  15.612  13.489 1.00 40.03  ?  91  TYR A CZ    1 
ATOM   641  O OH    . TYR A 1 91  ? 2.087  14.920  14.411 1.00 39.76  ?  91  TYR A OH    1 
ATOM   642  N N     . ASN A 1 92  ? 7.703  18.531  8.686  1.00 43.37  ?  92  ASN A N     1 
ATOM   643  C CA    . ASN A 1 92  ? 8.189  19.104  7.437  1.00 42.66  ?  92  ASN A CA    1 
ATOM   644  C C     . ASN A 1 92  ? 9.446  18.401  6.947  1.00 46.05  ?  92  ASN A C     1 
ATOM   645  O O     . ASN A 1 92  ? 9.507  17.965  5.795  1.00 49.97  ?  92  ASN A O     1 
ATOM   646  C CB    . ASN A 1 92  ? 8.473  20.598  7.584  1.00 40.65  ?  92  ASN A CB    1 
ATOM   647  C CG    . ASN A 1 92  ? 7.248  21.385  7.965  1.00 50.53  ?  92  ASN A CG    1 
ATOM   648  O OD1   . ASN A 1 92  ? 6.273  20.828  8.494  1.00 49.47  ?  92  ASN A OD1   1 
ATOM   649  N ND2   . ASN A 1 92  ? 7.285  22.698  7.709  1.00 55.03  ?  92  ASN A ND2   1 
ATOM   650  N N     . GLU A 1 93  ? 10.452 18.273  7.807  1.00 44.73  ?  93  GLU A N     1 
ATOM   651  C CA    . GLU A 1 93  ? 11.736 17.765  7.363  1.00 38.12  ?  93  GLU A CA    1 
ATOM   652  C C     . GLU A 1 93  ? 11.679 16.267  7.114  1.00 40.28  ?  93  GLU A C     1 
ATOM   653  O O     . GLU A 1 93  ? 11.793 15.831  5.963  1.00 40.81  ?  93  GLU A O     1 
ATOM   654  C CB    . GLU A 1 93  ? 12.803 18.116  8.380  1.00 40.52  ?  93  GLU A CB    1 
ATOM   655  C CG    . GLU A 1 93  ? 12.865 19.619  8.692  1.00 42.95  ?  93  GLU A CG    1 
ATOM   656  C CD    . GLU A 1 93  ? 13.618 20.428  7.633  1.00 54.56  ?  93  GLU A CD    1 
ATOM   657  O OE1   . GLU A 1 93  ? 13.447 21.665  7.643  1.00 56.32  ?  93  GLU A OE1   1 
ATOM   658  O OE2   . GLU A 1 93  ? 14.376 19.852  6.797  1.00 57.38  -1 93  GLU A OE2   1 
ATOM   659  N N     . LEU A 1 94  ? 11.481 15.469  8.169  1.00 38.70  ?  94  LEU A N     1 
ATOM   660  C CA    . LEU A 1 94  ? 11.410 14.017  7.992  1.00 35.17  ?  94  LEU A CA    1 
ATOM   661  C C     . LEU A 1 94  ? 10.104 13.567  7.346  1.00 40.91  ?  94  LEU A C     1 
ATOM   662  O O     . LEU A 1 94  ? 10.057 12.480  6.763  1.00 42.89  ?  94  LEU A O     1 
ATOM   663  C CB    . LEU A 1 94  ? 11.575 13.287  9.328  1.00 35.45  ?  94  LEU A CB    1 
ATOM   664  C CG    . LEU A 1 94  ? 12.683 13.548  10.367 1.00 30.10  ?  94  LEU A CG    1 
ATOM   665  C CD1   . LEU A 1 94  ? 12.696 12.428  11.387 1.00 29.02  ?  94  LEU A CD1   1 
ATOM   666  C CD2   . LEU A 1 94  ? 14.056 13.659  9.779  1.00 29.45  ?  94  LEU A CD2   1 
ATOM   667  N N     . ARG A 1 95  ? 9.036  14.361  7.447  1.00 44.80  ?  95  ARG A N     1 
ATOM   668  C CA    . ARG A 1 95  ? 7.747  14.036  6.823  1.00 45.77  ?  95  ARG A CA    1 
ATOM   669  C C     . ARG A 1 95  ? 7.183  12.714  7.355  1.00 42.82  ?  95  ARG A C     1 
ATOM   670  O O     . ARG A 1 95  ? 6.819  11.816  6.593  1.00 47.18  ?  95  ARG A O     1 
ATOM   671  C CB    . ARG A 1 95  ? 7.869  14.014  5.290  1.00 45.29  ?  95  ARG A CB    1 
ATOM   672  C CG    . ARG A 1 95  ? 8.147  15.373  4.673  1.00 44.03  ?  95  ARG A CG    1 
ATOM   673  C CD    . ARG A 1 95  ? 7.938  15.374  3.171  1.00 54.08  ?  95  ARG A CD    1 
ATOM   674  N NE    . ARG A 1 95  ? 6.587  14.965  2.784  1.00 63.87  ?  95  ARG A NE    1 
ATOM   675  C CZ    . ARG A 1 95  ? 5.679  15.774  2.238  1.00 61.25  ?  95  ARG A CZ    1 
ATOM   676  N NH1   . ARG A 1 95  ? 5.963  17.053  2.010  1.00 51.09  ?  95  ARG A NH1   1 
ATOM   677  N NH2   . ARG A 1 95  ? 4.477  15.301  1.928  1.00 63.77  ?  95  ARG A NH2   1 
ATOM   678  N N     . VAL A 1 96  ? 7.077  12.613  8.685  1.00 41.68  ?  96  VAL A N     1 
ATOM   679  C CA    . VAL A 1 96  ? 6.576  11.412  9.347  1.00 42.00  ?  96  VAL A CA    1 
ATOM   680  C C     . VAL A 1 96  ? 5.637  11.790  10.483 1.00 41.14  ?  96  VAL A C     1 
ATOM   681  O O     . VAL A 1 96  ? 5.689  12.894  11.026 1.00 40.25  ?  96  VAL A O     1 
ATOM   682  C CB    . VAL A 1 96  ? 7.717  10.529  9.901  1.00 38.73  ?  96  VAL A CB    1 
ATOM   683  C CG1   . VAL A 1 96  ? 8.717  10.264  8.819  1.00 40.05  ?  96  VAL A CG1   1 
ATOM   684  C CG2   . VAL A 1 96  ? 8.389  11.201  11.074 1.00 37.75  ?  96  VAL A CG2   1 
ATOM   685  N N     . ALA A 1 97  ? 4.787  10.841  10.862 1.00 42.20  ?  97  ALA A N     1 
ATOM   686  C CA    . ALA A 1 97  ? 3.957  11.025  12.047 1.00 48.34  ?  97  ALA A CA    1 
ATOM   687  C C     . ALA A 1 97  ? 4.679  10.459  13.267 1.00 45.69  ?  97  ALA A C     1 
ATOM   688  O O     . ALA A 1 97  ? 5.007  9.265   13.280 1.00 42.62  ?  97  ALA A O     1 
ATOM   689  C CB    . ALA A 1 97  ? 2.607  10.349  11.874 1.00 47.76  ?  97  ALA A CB    1 
ATOM   690  N N     . PRO A 1 98  ? 4.972  11.261  14.288 1.00 42.45  ?  98  PRO A N     1 
ATOM   691  C CA    . PRO A 1 98  ? 5.752  10.725  15.412 1.00 40.96  ?  98  PRO A CA    1 
ATOM   692  C C     . PRO A 1 98  ? 5.086  9.573   16.164 1.00 41.50  ?  98  PRO A C     1 
ATOM   693  O O     . PRO A 1 98  ? 5.836  8.773   16.734 1.00 38.05  ?  98  PRO A O     1 
ATOM   694  C CB    . PRO A 1 98  ? 5.979  11.952  16.309 1.00 38.30  ?  98  PRO A CB    1 
ATOM   695  C CG    . PRO A 1 98  ? 4.999  12.970  15.844 1.00 40.92  ?  98  PRO A CG    1 
ATOM   696  C CD    . PRO A 1 98  ? 4.803  12.719  14.374 1.00 42.24  ?  98  PRO A CD    1 
ATOM   697  N N     . GLU A 1 99  ? 3.737  9.453   16.196 1.00 43.56  ?  99  GLU A N     1 
ATOM   698  C CA    . GLU A 1 99  ? 3.119  8.285   16.841 1.00 41.74  ?  99  GLU A CA    1 
ATOM   699  C C     . GLU A 1 99  ? 3.632  6.973   16.284 1.00 41.85  ?  99  GLU A C     1 
ATOM   700  O O     . GLU A 1 99  ? 3.361  5.912   16.863 1.00 36.33  ?  99  GLU A O     1 
ATOM   701  C CB    . GLU A 1 99  ? 1.612  8.186   16.666 1.00 41.45  ?  99  GLU A CB    1 
ATOM   702  C CG    . GLU A 1 99  ? 0.841  9.456   16.743 1.00 55.66  ?  99  GLU A CG    1 
ATOM   703  C CD    . GLU A 1 99  ? -0.505 9.373   16.026 1.00 64.86  ?  99  GLU A CD    1 
ATOM   704  O OE1   . GLU A 1 99  ? -0.592 8.631   15.013 1.00 63.93  ?  99  GLU A OE1   1 
ATOM   705  O OE2   . GLU A 1 99  ? -1.451 10.075  16.467 1.00 69.77  -1 99  GLU A OE2   1 
ATOM   706  N N     . GLU A 1 100 ? 4.330  7.008   15.159 1.00 41.93  ?  100 GLU A N     1 
ATOM   707  C CA    . GLU A 1 100 ? 4.611  5.807   14.398 1.00 41.97  ?  100 GLU A CA    1 
ATOM   708  C C     . GLU A 1 100 ? 6.075  5.379   14.442 1.00 42.19  ?  100 GLU A C     1 
ATOM   709  O O     . GLU A 1 100 ? 6.425  4.424   13.745 1.00 45.29  ?  100 GLU A O     1 
ATOM   710  C CB    . GLU A 1 100 ? 4.128  5.987   12.950 1.00 44.62  ?  100 GLU A CB    1 
ATOM   711  C CG    . GLU A 1 100 ? 2.659  5.466   12.737 1.00 58.10  ?  100 GLU A CG    1 
ATOM   712  C CD    . GLU A 1 100 ? 1.903  6.064   11.528 1.00 67.21  ?  100 GLU A CD    1 
ATOM   713  O OE1   . GLU A 1 100 ? 0.662  5.880   11.435 1.00 73.26  ?  100 GLU A OE1   1 
ATOM   714  O OE2   . GLU A 1 100 ? 2.538  6.689   10.650 1.00 68.38  -1 100 GLU A OE2   1 
ATOM   715  N N     . HIS A 1 101 ? 6.946  6.043   15.279 1.00 41.14  ?  101 HIS A N     1 
ATOM   716  C CA    . HIS A 1 101 ? 8.389  5.765   15.382 1.00 35.63  ?  101 HIS A CA    1 
ATOM   717  C C     . HIS A 1 101 ? 8.968  6.023   16.779 1.00 35.68  ?  101 HIS A C     1 
ATOM   718  O O     . HIS A 1 101 ? 8.882  7.152   17.281 1.00 33.79  ?  101 HIS A O     1 
ATOM   719  C CB    . HIS A 1 101 ? 9.197  6.616   14.392 1.00 35.63  ?  101 HIS A CB    1 
ATOM   720  C CG    . HIS A 1 101 ? 8.596  6.738   13.027 1.00 38.49  ?  101 HIS A CG    1 
ATOM   721  N ND1   . HIS A 1 101 ? 8.980  5.939   11.972 1.00 36.96  ?  101 HIS A ND1   1 
ATOM   722  C CD2   . HIS A 1 101 ? 7.670  7.595   12.533 1.00 39.68  ?  101 HIS A CD2   1 
ATOM   723  C CE1   . HIS A 1 101 ? 8.292  6.278   10.896 1.00 35.61  ?  101 HIS A CE1   1 
ATOM   724  N NE2   . HIS A 1 101 ? 7.492  7.280   11.209 1.00 40.13  ?  101 HIS A NE2   1 
ATOM   725  N N     . PRO A 1 102 ? 9.597  5.031   17.425 1.00 35.40  ?  102 PRO A N     1 
ATOM   726  C CA    . PRO A 1 102 ? 10.363 5.320   18.643 1.00 30.22  ?  102 PRO A CA    1 
ATOM   727  C C     . PRO A 1 102 ? 11.325 6.448   18.341 1.00 31.75  ?  102 PRO A C     1 
ATOM   728  O O     . PRO A 1 102 ? 11.790 6.572   17.212 1.00 34.81  ?  102 PRO A O     1 
ATOM   729  C CB    . PRO A 1 102 ? 11.117 4.017   18.916 1.00 30.97  ?  102 PRO A CB    1 
ATOM   730  C CG    . PRO A 1 102 ? 10.505 3.005   18.050 1.00 30.43  ?  102 PRO A CG    1 
ATOM   731  C CD    . PRO A 1 102 ? 9.855  3.677   16.915 1.00 30.81  ?  102 PRO A CD    1 
ATOM   732  N N     . VAL A 1 103 ? 11.640 7.272   19.343 1.00 31.73  ?  103 VAL A N     1 
ATOM   733  C CA    . VAL A 1 103 ? 12.390 8.495   19.065 1.00 30.33  ?  103 VAL A CA    1 
ATOM   734  C C     . VAL A 1 103 ? 13.508 8.697   20.083 1.00 31.69  ?  103 VAL A C     1 
ATOM   735  O O     . VAL A 1 103 ? 13.244 8.867   21.274 1.00 33.29  ?  103 VAL A O     1 
ATOM   736  C CB    . VAL A 1 103 ? 11.473 9.719   19.024 1.00 27.14  ?  103 VAL A CB    1 
ATOM   737  C CG1   . VAL A 1 103 ? 12.301 10.946  18.814 1.00 32.34  ?  103 VAL A CG1   1 
ATOM   738  C CG2   . VAL A 1 103 ? 10.501 9.562   17.901 1.00 26.99  ?  103 VAL A CG2   1 
ATOM   739  N N     . LEU A 1 104 ? 14.750 8.705   19.607 1.00 29.77  ?  104 LEU A N     1 
ATOM   740  C CA    . LEU A 1 104 ? 15.934 8.958   20.417 1.00 27.10  ?  104 LEU A CA    1 
ATOM   741  C C     . LEU A 1 104 ? 16.331 10.432  20.309 1.00 30.94  ?  104 LEU A C     1 
ATOM   742  O O     . LEU A 1 104 ? 16.635 10.915  19.205 1.00 27.90  ?  104 LEU A O     1 
ATOM   743  C CB    . LEU A 1 104 ? 17.075 8.051   19.955 1.00 26.18  ?  104 LEU A CB    1 
ATOM   744  C CG    . LEU A 1 104 ? 18.475 8.475   20.397 1.00 29.17  ?  104 LEU A CG    1 
ATOM   745  C CD1   . LEU A 1 104 ? 18.472 8.679   21.901 1.00 29.11  ?  104 LEU A CD1   1 
ATOM   746  C CD2   . LEU A 1 104 ? 19.522 7.452   19.996 1.00 25.59  ?  104 LEU A CD2   1 
ATOM   747  N N     . LEU A 1 105 ? 16.326 11.139  21.451 1.00 28.02  ?  105 LEU A N     1 
ATOM   748  C CA    . LEU A 1 105 ? 16.701 12.549  21.568 1.00 27.28  ?  105 LEU A CA    1 
ATOM   749  C C     . LEU A 1 105 ? 18.058 12.698  22.242 1.00 27.23  ?  105 LEU A C     1 
ATOM   750  O O     . LEU A 1 105 ? 18.417 11.927  23.132 1.00 29.01  ?  105 LEU A O     1 
ATOM   751  C CB    . LEU A 1 105 ? 15.704 13.341  22.411 1.00 31.18  ?  105 LEU A CB    1 
ATOM   752  C CG    . LEU A 1 105 ? 14.232 13.450  22.075 1.00 33.73  ?  105 LEU A CG    1 
ATOM   753  C CD1   . LEU A 1 105 ? 13.536 14.189  23.213 1.00 34.05  ?  105 LEU A CD1   1 
ATOM   754  C CD2   . LEU A 1 105 ? 14.100 14.205  20.764 1.00 33.59  ?  105 LEU A CD2   1 
ATOM   755  N N     . THR A 1 106 ? 18.801 13.716  21.856 1.00 25.46  ?  106 THR A N     1 
ATOM   756  C CA    . THR A 1 106 ? 20.056 13.962  22.547 1.00 24.95  ?  106 THR A CA    1 
ATOM   757  C C     . THR A 1 106 ? 19.855 15.088  23.544 1.00 25.90  ?  106 THR A C     1 
ATOM   758  O O     . THR A 1 106 ? 18.935 15.893  23.426 1.00 29.68  ?  106 THR A O     1 
ATOM   759  C CB    . THR A 1 106 ? 21.184 14.295  21.568 1.00 25.85  ?  106 THR A CB    1 
ATOM   760  O OG1   . THR A 1 106 ? 21.024 15.637  21.092 1.00 32.41  ?  106 THR A OG1   1 
ATOM   761  C CG2   . THR A 1 106 ? 21.153 13.347  20.365 1.00 22.61  ?  106 THR A CG2   1 
ATOM   762  N N     . GLU A 1 107 ? 20.700 15.114  24.560 1.00 28.59  ?  107 GLU A N     1 
ATOM   763  C CA    . GLU A 1 107 ? 20.684 16.186  25.536 1.00 30.29  ?  107 GLU A CA    1 
ATOM   764  C C     . GLU A 1 107 ? 22.112 16.628  25.776 1.00 31.53  ?  107 GLU A C     1 
ATOM   765  O O     . GLU A 1 107 ? 23.063 15.878  25.526 1.00 30.29  ?  107 GLU A O     1 
ATOM   766  C CB    . GLU A 1 107 ? 20.024 15.760  26.851 1.00 34.53  ?  107 GLU A CB    1 
ATOM   767  C CG    . GLU A 1 107 ? 20.731 14.598  27.538 1.00 36.12  ?  107 GLU A CG    1 
ATOM   768  C CD    . GLU A 1 107 ? 20.105 14.228  28.881 1.00 41.33  ?  107 GLU A CD    1 
ATOM   769  O OE1   . GLU A 1 107 ? 20.227 13.050  29.316 1.00 41.02  ?  107 GLU A OE1   1 
ATOM   770  O OE2   . GLU A 1 107 ? 19.481 15.125  29.503 1.00 46.52  -1 107 GLU A OE2   1 
ATOM   771  N N     . ALA A 1 108 ? 22.250 17.871  26.248 1.00 34.16  ?  108 ALA A N     1 
ATOM   772  C CA    . ALA A 1 108 ? 23.558 18.405  26.606 1.00 33.62  ?  108 ALA A CA    1 
ATOM   773  C C     . ALA A 1 108 ? 24.044 17.807  27.926 1.00 33.23  ?  108 ALA A C     1 
ATOM   774  O O     . ALA A 1 108 ? 23.246 17.327  28.742 1.00 28.71  ?  108 ALA A O     1 
ATOM   775  C CB    . ALA A 1 108 ? 23.512 19.929  26.718 1.00 31.50  ?  108 ALA A CB    1 
ATOM   776  N N     . PRO A 1 109 ? 25.359 17.832  28.153 1.00 34.84  ?  109 PRO A N     1 
ATOM   777  C CA    . PRO A 1 109 ? 25.903 17.441  29.462 1.00 34.71  ?  109 PRO A CA    1 
ATOM   778  C C     . PRO A 1 109 ? 25.470 18.386  30.571 1.00 33.95  ?  109 PRO A C     1 
ATOM   779  O O     . PRO A 1 109 ? 25.288 19.591  30.362 1.00 38.01  ?  109 PRO A O     1 
ATOM   780  C CB    . PRO A 1 109 ? 27.425 17.499  29.256 1.00 32.54  ?  109 PRO A CB    1 
ATOM   781  C CG    . PRO A 1 109 ? 27.622 18.355  28.054 1.00 33.92  ?  109 PRO A CG    1 
ATOM   782  C CD    . PRO A 1 109 ? 26.416 18.173  27.183 1.00 33.35  ?  109 PRO A CD    1 
ATOM   783  N N     . LEU A 1 110 ? 25.319 17.810  31.768 1.00 35.50  ?  110 LEU A N     1 
ATOM   784  C CA    . LEU A 1 110 ? 24.806 18.503  32.956 1.00 33.74  ?  110 LEU A CA    1 
ATOM   785  C C     . LEU A 1 110 ? 23.401 19.062  32.729 1.00 34.84  ?  110 LEU A C     1 
ATOM   786  O O     . LEU A 1 110 ? 23.054 20.123  33.251 1.00 38.69  ?  110 LEU A O     1 
ATOM   787  C CB    . LEU A 1 110 ? 25.759 19.611  33.410 1.00 29.40  ?  110 LEU A CB    1 
ATOM   788  C CG    . LEU A 1 110 ? 27.193 19.159  33.649 1.00 28.44  ?  110 LEU A CG    1 
ATOM   789  C CD1   . LEU A 1 110 ? 28.073 20.329  33.969 1.00 22.51  ?  110 LEU A CD1   1 
ATOM   790  C CD2   . LEU A 1 110 ? 27.260 18.120  34.748 1.00 21.97  ?  110 LEU A CD2   1 
ATOM   791  N N     . ASN A 1 111 ? 22.582 18.380  31.938 1.00 37.89  ?  111 ASN A N     1 
ATOM   792  C CA    . ASN A 1 111 ? 21.208 18.865  31.649 1.00 38.69  ?  111 ASN A CA    1 
ATOM   793  C C     . ASN A 1 111 ? 20.380 18.761  32.918 1.00 41.40  ?  111 ASN A C     1 
ATOM   794  O O     . ASN A 1 111 ? 20.331 17.672  33.493 1.00 44.96  ?  111 ASN A O     1 
ATOM   795  C CB    . ASN A 1 111 ? 20.536 18.082  30.527 1.00 37.95  ?  111 ASN A CB    1 
ATOM   796  C CG    . ASN A 1 111 ? 19.332 18.767  29.926 1.00 41.35  ?  111 ASN A CG    1 
ATOM   797  O OD1   . ASN A 1 111 ? 18.235 18.223  29.955 1.00 41.58  ?  111 ASN A OD1   1 
ATOM   798  N ND2   . ASN A 1 111 ? 19.532 19.943  29.358 1.00 40.35  ?  111 ASN A ND2   1 
ATOM   799  N N     . PRO A 1 112 ? 19.725 19.846  33.371 1.00 40.63  ?  112 PRO A N     1 
ATOM   800  C CA    . PRO A 1 112 ? 19.007 19.807  34.625 1.00 40.30  ?  112 PRO A CA    1 
ATOM   801  C C     . PRO A 1 112 ? 18.126 18.552  34.615 1.00 41.74  ?  112 PRO A C     1 
ATOM   802  O O     . PRO A 1 112 ? 17.798 18.108  33.552 1.00 42.24  ?  112 PRO A O     1 
ATOM   803  C CB    . PRO A 1 112 ? 18.506 21.244  34.762 1.00 32.88  ?  112 PRO A CB    1 
ATOM   804  C CG    . PRO A 1 112 ? 19.443 22.050  33.910 1.00 32.12  ?  112 PRO A CG    1 
ATOM   805  C CD    . PRO A 1 112 ? 19.680 21.150  32.724 1.00 32.86  ?  112 PRO A CD    1 
ATOM   806  N N     . LYS A 1 113 ? 17.788 18.019  35.788 1.00 36.67  ?  113 LYS A N     1 
ATOM   807  C CA    . LYS A 1 113 ? 16.747 16.982  36.008 1.00 40.13  ?  113 LYS A CA    1 
ATOM   808  C C     . LYS A 1 113 ? 15.439 17.344  35.304 1.00 42.59  ?  113 LYS A C     1 
ATOM   809  O O     . LYS A 1 113 ? 14.935 16.512  34.550 1.00 38.63  ?  113 LYS A O     1 
ATOM   810  C CB    . LYS A 1 113 ? 16.462 17.007  37.510 1.00 42.73  ?  113 LYS A CB    1 
ATOM   811  C CG    . LYS A 1 113 ? 16.420 15.683  38.245 1.00 42.08  ?  113 LYS A CG    1 
ATOM   812  C CD    . LYS A 1 113 ? 15.453 15.729  39.401 1.00 44.80  ?  113 LYS A CD    1 
ATOM   813  C CE    . LYS A 1 113 ? 15.451 17.063  40.114 1.00 48.00  ?  113 LYS A CE    1 
ATOM   814  N NZ    . LYS A 1 113 ? 16.268 17.027  41.349 1.00 46.80  ?  113 LYS A NZ    1 
ATOM   815  N N     . ALA A 1 114 ? 14.885 18.519  35.584 1.00 45.95  ?  114 ALA A N     1 
ATOM   816  C CA    . ALA A 1 114 ? 13.550 18.918  35.087 1.00 39.76  ?  114 ALA A CA    1 
ATOM   817  C C     . ALA A 1 114 ? 13.532 19.089  33.574 1.00 39.99  ?  114 ALA A C     1 
ATOM   818  O O     . ALA A 1 114 ? 12.501 18.802  32.973 1.00 37.38  ?  114 ALA A O     1 
ATOM   819  C CB    . ALA A 1 114 ? 13.177 20.199  35.764 1.00 34.80  ?  114 ALA A CB    1 
ATOM   820  N N     . ASN A 1 115 ? 14.630 19.561  32.997 1.00 37.99  ?  115 ASN A N     1 
ATOM   821  C CA    . ASN A 1 115 ? 14.727 19.713  31.527 1.00 40.17  ?  115 ASN A CA    1 
ATOM   822  C C     . ASN A 1 115 ? 14.534 18.328  30.913 1.00 38.68  ?  115 ASN A C     1 
ATOM   823  O O     . ASN A 1 115 ? 13.898 18.248  29.868 1.00 38.50  ?  115 ASN A O     1 
ATOM   824  C CB    . ASN A 1 115 ? 16.043 20.413  31.183 1.00 44.26  ?  115 ASN A CB    1 
ATOM   825  C CG    . ASN A 1 115 ? 16.031 21.239  29.920 1.00 44.53  ?  115 ASN A CG    1 
ATOM   826  O OD1   . ASN A 1 115 ? 16.337 20.740  28.841 1.00 47.78  ?  115 ASN A OD1   1 
ATOM   827  N ND2   . ASN A 1 115 ? 15.721 22.515  30.057 1.00 47.35  ?  115 ASN A ND2   1 
ATOM   828  N N     . ARG A 1 116 ? 15.044 17.286  31.570 1.00 40.71  ?  116 ARG A N     1 
ATOM   829  C CA    . ARG A 1 116 ? 14.913 15.883  31.101 1.00 39.81  ?  116 ARG A CA    1 
ATOM   830  C C     . ARG A 1 116 ? 13.468 15.409  31.243 1.00 36.21  ?  116 ARG A C     1 
ATOM   831  O O     . ARG A 1 116 ? 12.966 14.810  30.293 1.00 33.30  ?  116 ARG A O     1 
ATOM   832  C CB    . ARG A 1 116 ? 15.842 14.976  31.911 1.00 35.58  ?  116 ARG A CB    1 
ATOM   833  C CG    . ARG A 1 116 ? 17.234 15.521  32.175 1.00 38.01  ?  116 ARG A CG    1 
ATOM   834  C CD    . ARG A 1 116 ? 18.030 14.451  32.892 1.00 34.51  ?  116 ARG A CD    1 
ATOM   835  N NE    . ARG A 1 116 ? 18.458 13.420  31.962 1.00 35.03  ?  116 ARG A NE    1 
ATOM   836  C CZ    . ARG A 1 116 ? 18.170 12.130  32.067 1.00 37.32  ?  116 ARG A CZ    1 
ATOM   837  N NH1   . ARG A 1 116 ? 17.442 11.692  33.076 1.00 37.53  ?  116 ARG A NH1   1 
ATOM   838  N NH2   . ARG A 1 116 ? 18.610 11.282  31.159 1.00 37.20  ?  116 ARG A NH2   1 
ATOM   839  N N     . GLU A 1 117 ? 12.846 15.637  32.397 1.00 34.82  ?  117 GLU A N     1 
ATOM   840  C CA    . GLU A 1 117 ? 11.446 15.296  32.566 1.00 37.06  ?  117 GLU A CA    1 
ATOM   841  C C     . GLU A 1 117 ? 10.576 16.017  31.543 1.00 37.75  ?  117 GLU A C     1 
ATOM   842  O O     . GLU A 1 117 ? 9.629  15.427  31.001 1.00 36.39  ?  117 GLU A O     1 
ATOM   843  C CB    . GLU A 1 117 ? 11.000 15.623  33.991 1.00 38.29  ?  117 GLU A CB    1 
ATOM   844  C CG    . GLU A 1 117 ? 11.165 14.460  34.948 1.00 42.10  ?  117 GLU A CG    1 
ATOM   845  C CD    . GLU A 1 117 ? 11.492 14.901  36.361 1.00 47.83  ?  117 GLU A CD    1 
ATOM   846  O OE1   . GLU A 1 117 ? 10.954 14.303  37.331 1.00 50.27  ?  117 GLU A OE1   1 
ATOM   847  O OE2   . GLU A 1 117 ? 12.291 15.855  36.498 1.00 51.07  -1 117 GLU A OE2   1 
ATOM   848  N N     . LYS A 1 118 ? 10.878 17.291  31.254 1.00 34.02  ?  118 LYS A N     1 
ATOM   849  C CA    . LYS A 1 118 ? 9.993  18.043  30.373 1.00 36.05  ?  118 LYS A CA    1 
ATOM   850  C C     . LYS A 1 118 ? 10.118 17.561  28.931 1.00 38.83  ?  118 LYS A C     1 
ATOM   851  O O     . LYS A 1 118 ? 9.115  17.501  28.206 1.00 41.47  ?  118 LYS A O     1 
ATOM   852  C CB    . LYS A 1 118 ? 10.263 19.545  30.488 1.00 38.64  ?  118 LYS A CB    1 
ATOM   853  C CG    . LYS A 1 118 ? 9.342  20.385  29.586 1.00 39.73  ?  118 LYS A CG    1 
ATOM   854  C CD    . LYS A 1 118 ? 8.561  21.487  30.316 1.00 42.23  ?  118 LYS A CD    1 
ATOM   855  C CE    . LYS A 1 118 ? 7.263  21.900  29.547 1.00 44.15  ?  118 LYS A CE    1 
ATOM   856  N NZ    . LYS A 1 118 ? 6.208  20.826  29.306 1.00 40.84  ?  118 LYS A NZ    1 
ATOM   857  N N     . MET A 1 119 ? 11.337 17.199  28.506 1.00 35.35  ?  119 MET A N     1 
ATOM   858  C CA    . MET A 1 119 ? 11.549 16.515  27.231 1.00 36.21  ?  119 MET A CA    1 
ATOM   859  C C     . MET A 1 119 ? 10.657 15.281  27.070 1.00 38.42  ?  119 MET A C     1 
ATOM   860  O O     . MET A 1 119 ? 10.036 15.080  26.016 1.00 33.76  ?  119 MET A O     1 
ATOM   861  C CB    . MET A 1 119 ? 13.011 16.106  27.119 1.00 39.60  ?  119 MET A CB    1 
ATOM   862  C CG    . MET A 1 119 ? 13.842 16.923  26.166 1.00 52.65  ?  119 MET A CG    1 
ATOM   863  S SD    . MET A 1 119 ? 15.540 16.300  26.126 1.00 55.55  ?  119 MET A SD    1 
ATOM   864  C CE    . MET A 1 119 ? 16.065 17.119  27.638 1.00 43.70  ?  119 MET A CE    1 
ATOM   865  N N     . THR A 1 120 ? 10.637 14.411  28.095 1.00 37.93  ?  120 THR A N     1 
ATOM   866  C CA    . THR A 1 120 ? 9.836  13.187  28.062 1.00 36.23  ?  120 THR A CA    1 
ATOM   867  C C     . THR A 1 120 ? 8.348  13.505  28.006 1.00 36.77  ?  120 THR A C     1 
ATOM   868  O O     . THR A 1 120 ? 7.602  12.917  27.213 1.00 35.73  ?  120 THR A O     1 
ATOM   869  C CB    . THR A 1 120 ? 10.145 12.337  29.300 1.00 33.93  ?  120 THR A CB    1 
ATOM   870  O OG1   . THR A 1 120 ? 11.553 12.262  29.496 1.00 30.15  ?  120 THR A OG1   1 
ATOM   871  C CG2   . THR A 1 120 ? 9.596  10.934  29.153 1.00 32.71  ?  120 THR A CG2   1 
ATOM   872  N N     . GLN A 1 121 ? 7.904  14.422  28.876 1.00 40.25  ?  121 GLN A N     1 
ATOM   873  C CA    . GLN A 1 121 ? 6.521  14.898  28.899 1.00 38.28  ?  121 GLN A CA    1 
ATOM   874  C C     . GLN A 1 121 ? 6.052  15.335  27.522 1.00 38.18  ?  121 GLN A C     1 
ATOM   875  O O     . GLN A 1 121 ? 4.994  14.902  27.057 1.00 38.50  ?  121 GLN A O     1 
ATOM   876  C CB    . GLN A 1 121 ? 6.390  16.062  29.885 1.00 39.69  ?  121 GLN A CB    1 
ATOM   877  C CG    . GLN A 1 121 ? 5.030  16.133  30.560 1.00 42.24  ?  121 GLN A CG    1 
ATOM   878  C CD    . GLN A 1 121 ? 4.722  17.477  31.209 1.00 44.77  ?  121 GLN A CD    1 
ATOM   879  O OE1   . GLN A 1 121 ? 5.572  18.374  31.265 1.00 47.31  ?  121 GLN A OE1   1 
ATOM   880  N NE2   . GLN A 1 121 ? 3.492  17.619  31.714 1.00 48.30  ?  121 GLN A NE2   1 
ATOM   881  N N     . ILE A 1 122 ? 6.814  16.218  26.862 1.00 34.55  ?  122 ILE A N     1 
ATOM   882  C CA    . ILE A 1 122 ? 6.405  16.691  25.539 1.00 36.71  ?  122 ILE A CA    1 
ATOM   883  C C     . ILE A 1 122 ? 6.366  15.547  24.528 1.00 35.61  ?  122 ILE A C     1 
ATOM   884  O O     . ILE A 1 122 ? 5.434  15.449  23.724 1.00 35.92  ?  122 ILE A O     1 
ATOM   885  C CB    . ILE A 1 122 ? 7.323  17.824  25.055 1.00 36.33  ?  122 ILE A CB    1 
ATOM   886  C CG1   . ILE A 1 122 ? 7.072  19.098  25.850 1.00 34.17  ?  122 ILE A CG1   1 
ATOM   887  C CG2   . ILE A 1 122 ? 7.109  18.054  23.569 1.00 33.19  ?  122 ILE A CG2   1 
ATOM   888  C CD1   . ILE A 1 122 ? 8.066  20.165  25.575 1.00 32.18  ?  122 ILE A CD1   1 
ATOM   889  N N     . MET A 1 123 ? 7.376  14.677  24.528 1.00 35.95  ?  123 MET A N     1 
ATOM   890  C CA    . MET A 1 123 ? 7.411  13.637  23.497 1.00 40.56  ?  123 MET A CA    1 
ATOM   891  C C     . MET A 1 123 ? 6.254  12.656  23.637 1.00 41.27  ?  123 MET A C     1 
ATOM   892  O O     . MET A 1 123 ? 5.767  12.139  22.624 1.00 42.12  ?  123 MET A O     1 
ATOM   893  C CB    . MET A 1 123 ? 8.746  12.877  23.504 1.00 36.94  ?  123 MET A CB    1 
ATOM   894  C CG    . MET A 1 123 ? 9.946  13.740  23.134 1.00 38.66  ?  123 MET A CG    1 
ATOM   895  S SD    . MET A 1 123 ? 10.010 14.235  21.388 1.00 35.78  ?  123 MET A SD    1 
ATOM   896  C CE    . MET A 1 123 ? 9.390  12.725  20.625 1.00 35.16  ?  123 MET A CE    1 
ATOM   897  N N     . PHE A 1 124 ? 5.779  12.401  24.859 1.00 37.44  ?  124 PHE A N     1 
ATOM   898  C CA    . PHE A 1 124 ? 4.659  11.476  24.979 1.00 37.02  ?  124 PHE A CA    1 
ATOM   899  C C     . PHE A 1 124 ? 3.307  12.168  24.878 1.00 38.19  ?  124 PHE A C     1 
ATOM   900  O O     . PHE A 1 124 ? 2.407  11.655  24.210 1.00 39.46  ?  124 PHE A O     1 
ATOM   901  C CB    . PHE A 1 124 ? 4.763  10.699  26.283 1.00 35.58  ?  124 PHE A CB    1 
ATOM   902  C CG    . PHE A 1 124 ? 5.743  9.589   26.227 1.00 32.92  ?  124 PHE A CG    1 
ATOM   903  C CD1   . PHE A 1 124 ? 6.863  9.591   27.047 1.00 32.66  ?  124 PHE A CD1   1 
ATOM   904  C CD2   . PHE A 1 124 ? 5.567  8.547   25.332 1.00 36.74  ?  124 PHE A CD2   1 
ATOM   905  C CE1   . PHE A 1 124 ? 7.790  8.559   26.992 1.00 35.70  ?  124 PHE A CE1   1 
ATOM   906  C CE2   . PHE A 1 124 ? 6.489  7.499   25.271 1.00 36.84  ?  124 PHE A CE2   1 
ATOM   907  C CZ    . PHE A 1 124 ? 7.607  7.507   26.102 1.00 34.85  ?  124 PHE A CZ    1 
ATOM   908  N N     . GLU A 1 125 ? 3.157  13.341  25.489 1.00 37.88  ?  125 GLU A N     1 
ATOM   909  C CA    . GLU A 1 125 ? 1.874  14.028  25.556 1.00 37.27  ?  125 GLU A CA    1 
ATOM   910  C C     . GLU A 1 125 ? 1.616  15.012  24.421 1.00 41.44  ?  125 GLU A C     1 
ATOM   911  O O     . GLU A 1 125 ? 0.474  15.461  24.274 1.00 45.38  ?  125 GLU A O     1 
ATOM   912  C CB    . GLU A 1 125 ? 1.754  14.786  26.876 1.00 38.18  ?  125 GLU A CB    1 
ATOM   913  C CG    . GLU A 1 125 ? 1.820  13.886  28.092 1.00 40.23  ?  125 GLU A CG    1 
ATOM   914  C CD    . GLU A 1 125 ? 1.607  14.635  29.402 1.00 43.22  ?  125 GLU A CD    1 
ATOM   915  O OE1   . GLU A 1 125 ? 1.355  15.876  29.370 1.00 42.91  ?  125 GLU A OE1   1 
ATOM   916  O OE2   . GLU A 1 125 ? 1.701  13.970  30.464 1.00 43.28  -1 125 GLU A OE2   1 
ATOM   917  N N     . THR A 1 126 ? 2.628  15.404  23.647 1.00 40.76  ?  126 THR A N     1 
ATOM   918  C CA    . THR A 1 126 ? 2.408  16.309  22.518 1.00 40.97  ?  126 THR A CA    1 
ATOM   919  C C     . THR A 1 126 ? 2.649  15.653  21.173 1.00 39.16  ?  126 THR A C     1 
ATOM   920  O O     . THR A 1 126 ? 1.986  16.011  20.201 1.00 40.18  ?  126 THR A O     1 
ATOM   921  C CB    . THR A 1 126 ? 3.308  17.553  22.620 1.00 38.98  ?  126 THR A CB    1 
ATOM   922  O OG1   . THR A 1 126 ? 3.226  18.107  23.942 1.00 43.17  ?  126 THR A OG1   1 
ATOM   923  C CG2   . THR A 1 126 ? 2.919  18.613  21.584 1.00 29.69  ?  126 THR A CG2   1 
ATOM   924  N N     . PHE A 1 127 ? 3.575  14.701  21.093 1.00 37.90  ?  127 PHE A N     1 
ATOM   925  C CA    . PHE A 1 127 ? 3.838  14.006  19.847 1.00 40.96  ?  127 PHE A CA    1 
ATOM   926  C C     . PHE A 1 127 ? 3.434  12.541  19.894 1.00 41.99  ?  127 PHE A C     1 
ATOM   927  O O     . PHE A 1 127 ? 3.458  11.874  18.852 1.00 42.18  ?  127 PHE A O     1 
ATOM   928  C CB    . PHE A 1 127 ? 5.321  14.164  19.472 1.00 37.38  ?  127 PHE A CB    1 
ATOM   929  C CG    . PHE A 1 127 ? 5.698  15.597  19.189 1.00 39.90  ?  127 PHE A CG    1 
ATOM   930  C CD1   . PHE A 1 127 ? 5.155  16.268  18.099 1.00 35.51  ?  127 PHE A CD1   1 
ATOM   931  C CD2   . PHE A 1 127 ? 6.555  16.289  20.032 1.00 36.18  ?  127 PHE A CD2   1 
ATOM   932  C CE1   . PHE A 1 127 ? 5.478  17.579  17.851 1.00 33.97  ?  127 PHE A CE1   1 
ATOM   933  C CE2   . PHE A 1 127 ? 6.881  17.595  19.782 1.00 35.15  ?  127 PHE A CE2   1 
ATOM   934  C CZ    . PHE A 1 127 ? 6.337  18.248  18.690 1.00 34.40  ?  127 PHE A CZ    1 
ATOM   935  N N     . ASN A 1 128 ? 3.026  12.051  21.063 1.00 41.12  ?  128 ASN A N     1 
ATOM   936  C CA    . ASN A 1 128 ? 2.457  10.718  21.254 1.00 41.69  ?  128 ASN A CA    1 
ATOM   937  C C     . ASN A 1 128 ? 3.305  9.645   20.575 1.00 37.68  ?  128 ASN A C     1 
ATOM   938  O O     . ASN A 1 128 ? 2.828  8.836   19.775 1.00 39.82  ?  128 ASN A O     1 
ATOM   939  C CB    . ASN A 1 128 ? 1.004  10.665  20.771 1.00 40.74  ?  128 ASN A CB    1 
ATOM   940  C CG    . ASN A 1 128 ? 0.325  9.352   21.127 1.00 45.48  ?  128 ASN A CG    1 
ATOM   941  O OD1   . ASN A 1 128 ? -0.322 8.728   20.281 1.00 45.44  ?  128 ASN A OD1   1 
ATOM   942  N ND2   . ASN A 1 128 ? 0.475  8.922   22.383 1.00 45.47  ?  128 ASN A ND2   1 
ATOM   943  N N     . THR A 1 129 ? 4.565  9.654   20.915 1.00 35.06  ?  129 THR A N     1 
ATOM   944  C CA    . THR A 1 129 ? 5.499  8.657   20.436 1.00 35.66  ?  129 THR A CA    1 
ATOM   945  C C     . THR A 1 129 ? 5.274  7.343   21.178 1.00 30.75  ?  129 THR A C     1 
ATOM   946  O O     . THR A 1 129 ? 4.856  7.335   22.331 1.00 36.24  ?  129 THR A O     1 
ATOM   947  C CB    . THR A 1 129 ? 6.945  9.140   20.628 1.00 36.97  ?  129 THR A CB    1 
ATOM   948  O OG1   . THR A 1 129 ? 7.201  9.364   22.018 1.00 37.01  ?  129 THR A OG1   1 
ATOM   949  C CG2   . THR A 1 129 ? 7.182  10.452  19.905 1.00 30.78  ?  129 THR A CG2   1 
ATOM   950  N N     . PRO A 1 130 ? 5.509  6.213   20.527 1.00 32.87  ?  130 PRO A N     1 
ATOM   951  C CA    . PRO A 1 130 ? 5.388  4.923   21.234 1.00 29.64  ?  130 PRO A CA    1 
ATOM   952  C C     . PRO A 1 130 ? 6.497  4.665   22.229 1.00 32.33  ?  130 PRO A C     1 
ATOM   953  O O     . PRO A 1 130 ? 6.289  3.875   23.152 1.00 37.96  ?  130 PRO A O     1 
ATOM   954  C CB    . PRO A 1 130 ? 5.435  3.889   20.101 1.00 25.22  ?  130 PRO A CB    1 
ATOM   955  C CG    . PRO A 1 130 ? 6.134  4.605   18.956 1.00 29.72  ?  130 PRO A CG    1 
ATOM   956  C CD    . PRO A 1 130 ? 5.818  6.063   19.093 1.00 32.58  ?  130 PRO A CD    1 
ATOM   957  N N     . ALA A 1 131 ? 7.655  5.305   22.069 1.00 29.57  ?  131 ALA A N     1 
ATOM   958  C CA    . ALA A 1 131 ? 8.901  4.988   22.747 1.00 29.71  ?  131 ALA A CA    1 
ATOM   959  C C     . ALA A 1 131 ? 9.826  6.195   22.634 1.00 32.98  ?  131 ALA A C     1 
ATOM   960  O O     . ALA A 1 131 ? 9.724  6.973   21.684 1.00 36.49  ?  131 ALA A O     1 
ATOM   961  C CB    . ALA A 1 131 ? 9.569  3.752   22.137 1.00 27.01  ?  131 ALA A CB    1 
ATOM   962  N N     . MET A 1 132 ? 10.724 6.357   23.604 1.00 32.71  ?  132 MET A N     1 
ATOM   963  C CA    . MET A 1 132 ? 11.756 7.383   23.477 1.00 33.95  ?  132 MET A CA    1 
ATOM   964  C C     . MET A 1 132 ? 12.906 7.055   24.419 1.00 31.23  ?  132 MET A C     1 
ATOM   965  O O     . MET A 1 132 ? 12.799 6.167   25.271 1.00 26.73  ?  132 MET A O     1 
ATOM   966  C CB    . MET A 1 132 ? 11.200 8.786   23.752 1.00 32.32  ?  132 MET A CB    1 
ATOM   967  C CG    . MET A 1 132 ? 10.809 8.995   25.193 1.00 33.93  ?  132 MET A CG    1 
ATOM   968  S SD    . MET A 1 132 ? 11.384 10.550  25.826 1.00 43.71  ?  132 MET A SD    1 
ATOM   969  C CE    . MET A 1 132 ? 13.105 10.205  26.206 1.00 34.70  ?  132 MET A CE    1 
ATOM   970  N N     . TYR A 1 133 ? 14.018 7.779   24.230 1.00 27.77  ?  133 TYR A N     1 
ATOM   971  C CA    . TYR A 1 133 ? 15.241 7.661   25.027 1.00 34.07  ?  133 TYR A CA    1 
ATOM   972  C C     . TYR A 1 133 ? 16.005 8.982   24.929 1.00 30.76  ?  133 TYR A C     1 
ATOM   973  O O     . TYR A 1 133 ? 15.880 9.699   23.939 1.00 32.09  ?  133 TYR A O     1 
ATOM   974  C CB    . TYR A 1 133 ? 16.115 6.474   24.550 1.00 32.14  ?  133 TYR A CB    1 
ATOM   975  C CG    . TYR A 1 133 ? 17.167 6.016   25.539 1.00 30.25  ?  133 TYR A CG    1 
ATOM   976  C CD1   . TYR A 1 133 ? 16.867 5.065   26.504 1.00 34.09  ?  133 TYR A CD1   1 
ATOM   977  C CD2   . TYR A 1 133 ? 18.459 6.532   25.503 1.00 27.45  ?  133 TYR A CD2   1 
ATOM   978  C CE1   . TYR A 1 133 ? 17.824 4.640   27.416 1.00 34.01  ?  133 TYR A CE1   1 
ATOM   979  C CE2   . TYR A 1 133 ? 19.421 6.117   26.388 1.00 26.92  ?  133 TYR A CE2   1 
ATOM   980  C CZ    . TYR A 1 133 ? 19.105 5.165   27.353 1.00 34.89  ?  133 TYR A CZ    1 
ATOM   981  O OH    . TYR A 1 133 ? 20.055 4.740   28.275 1.00 39.22  ?  133 TYR A OH    1 
ATOM   982  N N     . VAL A 1 134 ? 16.792 9.307   25.956 1.00 29.28  ?  134 VAL A N     1 
ATOM   983  C CA    . VAL A 1 134 ? 17.623 10.510  25.931 1.00 31.06  ?  134 VAL A CA    1 
ATOM   984  C C     . VAL A 1 134 ? 19.050 10.147  26.315 1.00 30.70  ?  134 VAL A C     1 
ATOM   985  O O     . VAL A 1 134 ? 19.320 9.786   27.464 1.00 35.44  ?  134 VAL A O     1 
ATOM   986  C CB    . VAL A 1 134 ? 17.094 11.636  26.838 1.00 31.23  ?  134 VAL A CB    1 
ATOM   987  C CG1   . VAL A 1 134 ? 16.239 12.592  26.034 1.00 36.64  ?  134 VAL A CG1   1 
ATOM   988  C CG2   . VAL A 1 134 ? 16.333 11.094  27.986 1.00 28.91  ?  134 VAL A CG2   1 
ATOM   989  N N     . ALA A 1 135 ? 19.969 10.304  25.377 1.00 29.73  ?  135 ALA A N     1 
ATOM   990  C CA    . ALA A 1 135 ? 21.389 10.098  25.607 1.00 31.90  ?  135 ALA A CA    1 
ATOM   991  C C     . ALA A 1 135 ? 22.134 11.427  25.587 1.00 32.36  ?  135 ALA A C     1 
ATOM   992  O O     . ALA A 1 135 ? 21.752 12.371  24.887 1.00 32.46  ?  135 ALA A O     1 
ATOM   993  C CB    . ALA A 1 135 ? 21.988 9.175   24.541 1.00 31.07  ?  135 ALA A CB    1 
ATOM   994  N N     . ILE A 1 136 ? 23.225 11.483  26.343 1.00 30.88  ?  136 ILE A N     1 
ATOM   995  C CA    . ILE A 1 136 ? 24.086 12.655  26.305 1.00 29.41  ?  136 ILE A CA    1 
ATOM   996  C C     . ILE A 1 136 ? 24.837 12.691  24.984 1.00 30.53  ?  136 ILE A C     1 
ATOM   997  O O     . ILE A 1 136 ? 25.398 11.680  24.535 1.00 29.50  ?  136 ILE A O     1 
ATOM   998  C CB    . ILE A 1 136 ? 25.057 12.637  27.493 1.00 28.23  ?  136 ILE A CB    1 
ATOM   999  C CG1   . ILE A 1 136 ? 24.275 12.475  28.793 1.00 26.63  ?  136 ILE A CG1   1 
ATOM   1000 C CG2   . ILE A 1 136 ? 25.948 13.876  27.488 1.00 29.15  ?  136 ILE A CG2   1 
ATOM   1001 C CD1   . ILE A 1 136 ? 24.977 13.103  29.955 1.00 34.49  ?  136 ILE A CD1   1 
ATOM   1002 N N     . GLN A 1 137 ? 24.877 13.873  24.365 1.00 29.47  ?  137 GLN A N     1 
ATOM   1003 C CA    . GLN A 1 137 ? 25.559 14.012  23.088 1.00 28.09  ?  137 GLN A CA    1 
ATOM   1004 C C     . GLN A 1 137 ? 26.969 13.412  23.121 1.00 27.03  ?  137 GLN A C     1 
ATOM   1005 O O     . GLN A 1 137 ? 27.302 12.557  22.296 1.00 28.91  ?  137 GLN A O     1 
ATOM   1006 C CB    . GLN A 1 137 ? 25.561 15.483  22.690 1.00 29.13  ?  137 GLN A CB    1 
ATOM   1007 C CG    . GLN A 1 137 ? 24.203 15.936  22.199 1.00 23.88  ?  137 GLN A CG    1 
ATOM   1008 C CD    . GLN A 1 137 ? 23.855 17.333  22.638 1.00 28.08  ?  137 GLN A CD    1 
ATOM   1009 O OE1   . GLN A 1 137 ? 24.726 18.118  23.038 1.00 32.64  ?  137 GLN A OE1   1 
ATOM   1010 N NE2   . GLN A 1 137 ? 22.572 17.665  22.573 1.00 29.34  ?  137 GLN A NE2   1 
ATOM   1011 N N     . ALA A 1 138 ? 27.805 13.824  24.079 1.00 27.63  ?  138 ALA A N     1 
ATOM   1012 C CA    . ALA A 1 138 ? 29.190 13.357  24.094 1.00 25.74  ?  138 ALA A CA    1 
ATOM   1013 C C     . ALA A 1 138 ? 29.269 11.849  24.158 1.00 27.97  ?  138 ALA A C     1 
ATOM   1014 O O     . ALA A 1 138 ? 30.132 11.245  23.518 1.00 30.84  ?  138 ALA A O     1 
ATOM   1015 C CB    . ALA A 1 138 ? 29.961 13.941  25.271 1.00 24.09  ?  138 ALA A CB    1 
ATOM   1016 N N     . VAL A 1 139 ? 28.408 11.220  24.956 1.00 29.45  ?  139 VAL A N     1 
ATOM   1017 C CA    . VAL A 1 139 ? 28.450 9.767   25.079 1.00 26.65  ?  139 VAL A CA    1 
ATOM   1018 C C     . VAL A 1 139 ? 28.218 9.129   23.719 1.00 28.05  ?  139 VAL A C     1 
ATOM   1019 O O     . VAL A 1 139 ? 28.982 8.257   23.292 1.00 27.98  ?  139 VAL A O     1 
ATOM   1020 C CB    . VAL A 1 139 ? 27.430 9.275   26.127 1.00 29.88  ?  139 VAL A CB    1 
ATOM   1021 C CG1   . VAL A 1 139 ? 27.442 7.741   26.224 1.00 24.15  ?  139 VAL A CG1   1 
ATOM   1022 C CG2   . VAL A 1 139 ? 27.724 9.893   27.507 1.00 28.03  ?  139 VAL A CG2   1 
ATOM   1023 N N     . LEU A 1 140 ? 27.176 9.586   23.001 1.00 28.05  ?  140 LEU A N     1 
ATOM   1024 C CA    . LEU A 1 140 ? 26.907 9.122   21.636 1.00 25.90  ?  140 LEU A CA    1 
ATOM   1025 C C     . LEU A 1 140 ? 28.129 9.262   20.725 1.00 29.36  ?  140 LEU A C     1 
ATOM   1026 O O     . LEU A 1 140 ? 28.424 8.347   19.938 1.00 29.44  ?  140 LEU A O     1 
ATOM   1027 C CB    . LEU A 1 140 ? 25.725 9.883   21.047 1.00 24.03  ?  140 LEU A CB    1 
ATOM   1028 C CG    . LEU A 1 140 ? 24.325 9.515   21.548 1.00 27.10  ?  140 LEU A CG    1 
ATOM   1029 C CD1   . LEU A 1 140 ? 23.245 10.422  20.932 1.00 21.35  ?  140 LEU A CD1   1 
ATOM   1030 C CD2   . LEU A 1 140 ? 24.020 8.046   21.286 1.00 25.57  ?  140 LEU A CD2   1 
ATOM   1031 N N     . SER A 1 141 ? 28.856 10.396  20.821 1.00 25.92  ?  141 SER A N     1 
ATOM   1032 C CA    . SER A 1 141 ? 30.041 10.641  19.994 1.00 24.76  ?  141 SER A CA    1 
ATOM   1033 C C     . SER A 1 141 ? 31.161 9.661   20.309 1.00 28.12  ?  141 SER A C     1 
ATOM   1034 O O     . SER A 1 141 ? 31.872 9.207   19.403 1.00 27.74  ?  141 SER A O     1 
ATOM   1035 C CB    . SER A 1 141 ? 30.543 12.065  20.204 1.00 28.43  ?  141 SER A CB    1 
ATOM   1036 O OG    . SER A 1 141 ? 30.275 12.885  19.090 1.00 30.51  ?  141 SER A OG    1 
ATOM   1037 N N     . LEU A 1 142 ? 31.351 9.357   21.599 1.00 31.28  ?  142 LEU A N     1 
ATOM   1038 C CA    . LEU A 1 142 ? 32.283 8.314   22.023 1.00 29.21  ?  142 LEU A CA    1 
ATOM   1039 C C     . LEU A 1 142 ? 31.871 6.951   21.483 1.00 30.25  ?  142 LEU A C     1 
ATOM   1040 O O     . LEU A 1 142 ? 32.732 6.155   21.084 1.00 34.04  ?  142 LEU A O     1 
ATOM   1041 C CB    . LEU A 1 142 ? 32.372 8.274   23.555 1.00 25.83  ?  142 LEU A CB    1 
ATOM   1042 C CG    . LEU A 1 142 ? 33.557 7.524   24.174 1.00 23.80  ?  142 LEU A CG    1 
ATOM   1043 C CD1   . LEU A 1 142 ? 34.848 8.297   24.007 1.00 21.81  ?  142 LEU A CD1   1 
ATOM   1044 C CD2   . LEU A 1 142 ? 33.311 7.251   25.643 1.00 27.08  ?  142 LEU A CD2   1 
ATOM   1045 N N     . TYR A 1 143 ? 30.563 6.656   21.477 1.00 28.96  ?  143 TYR A N     1 
ATOM   1046 C CA    . TYR A 1 143 ? 30.074 5.351   21.025 1.00 27.64  ?  143 TYR A CA    1 
ATOM   1047 C C     . TYR A 1 143 ? 30.327 5.156   19.544 1.00 32.01  ?  143 TYR A C     1 
ATOM   1048 O O     . TYR A 1 143 ? 30.641 4.044   19.106 1.00 34.58  ?  143 TYR A O     1 
ATOM   1049 C CB    . TYR A 1 143 ? 28.582 5.204   21.289 1.00 26.03  ?  143 TYR A CB    1 
ATOM   1050 C CG    . TYR A 1 143 ? 28.166 4.900   22.720 1.00 27.83  ?  143 TYR A CG    1 
ATOM   1051 C CD1   . TYR A 1 143 ? 29.090 4.518   23.688 1.00 25.21  ?  143 TYR A CD1   1 
ATOM   1052 C CD2   . TYR A 1 143 ? 26.829 4.990   23.092 1.00 24.22  ?  143 TYR A CD2   1 
ATOM   1053 C CE1   . TYR A 1 143 ? 28.681 4.236   24.986 1.00 26.72  ?  143 TYR A CE1   1 
ATOM   1054 C CE2   . TYR A 1 143 ? 26.414 4.705   24.366 1.00 27.94  ?  143 TYR A CE2   1 
ATOM   1055 C CZ    . TYR A 1 143 ? 27.332 4.329   25.315 1.00 29.64  ?  143 TYR A CZ    1 
ATOM   1056 O OH    . TYR A 1 143 ? 26.875 4.056   26.587 1.00 31.58  ?  143 TYR A OH    1 
ATOM   1057 N N     . ALA A 1 144 ? 30.169 6.223   18.752 1.00 30.31  ?  144 ALA A N     1 
ATOM   1058 C CA    . ALA A 1 144 ? 30.381 6.155   17.311 1.00 29.64  ?  144 ALA A CA    1 
ATOM   1059 C C     . ALA A 1 144 ? 31.836 5.888   16.942 1.00 34.70  ?  144 ALA A C     1 
ATOM   1060 O O     . ALA A 1 144 ? 32.131 5.569   15.786 1.00 34.75  ?  144 ALA A O     1 
ATOM   1061 C CB    . ALA A 1 144 ? 29.912 7.461   16.678 1.00 27.16  ?  144 ALA A CB    1 
ATOM   1062 N N     . SER A 1 145 ? 32.755 6.061   17.883 1.00 33.46  ?  145 SER A N     1 
ATOM   1063 C CA    . SER A 1 145 ? 34.152 5.745   17.681 1.00 31.52  ?  145 SER A CA    1 
ATOM   1064 C C     . SER A 1 145 ? 34.539 4.467   18.419 1.00 39.31  ?  145 SER A C     1 
ATOM   1065 O O     . SER A 1 145 ? 35.729 4.218   18.645 1.00 40.67  ?  145 SER A O     1 
ATOM   1066 C CB    . SER A 1 145 ? 35.016 6.918   18.133 1.00 30.39  ?  145 SER A CB    1 
ATOM   1067 O OG    . SER A 1 145 ? 35.148 6.934   19.547 1.00 34.51  ?  145 SER A OG    1 
ATOM   1068 N N     . GLY A 1 146 ? 33.550 3.668   18.829 1.00 36.67  ?  146 GLY A N     1 
ATOM   1069 C CA    . GLY A 1 146 ? 33.776 2.335   19.340 1.00 37.18  ?  146 GLY A CA    1 
ATOM   1070 C C     . GLY A 1 146 ? 34.352 2.259   20.729 1.00 36.79  ?  146 GLY A C     1 
ATOM   1071 O O     . GLY A 1 146 ? 34.767 1.173   21.163 1.00 33.39  ?  146 GLY A O     1 
ATOM   1072 N N     . ARG A 1 147 ? 34.395 3.376   21.438 1.00 34.92  ?  147 ARG A N     1 
ATOM   1073 C CA    . ARG A 1 147 ? 34.880 3.424   22.802 1.00 32.92  ?  147 ARG A CA    1 
ATOM   1074 C C     . ARG A 1 147 ? 33.689 3.520   23.732 1.00 31.47  ?  147 ARG A C     1 
ATOM   1075 O O     . ARG A 1 147 ? 32.621 3.974   23.326 1.00 31.74  ?  147 ARG A O     1 
ATOM   1076 C CB    . ARG A 1 147 ? 35.802 4.628   22.995 1.00 31.81  ?  147 ARG A CB    1 
ATOM   1077 C CG    . ARG A 1 147 ? 37.141 4.407   22.408 1.00 31.68  ?  147 ARG A CG    1 
ATOM   1078 C CD    . ARG A 1 147 ? 37.785 5.679   21.992 1.00 32.11  ?  147 ARG A CD    1 
ATOM   1079 N NE    . ARG A 1 147 ? 39.087 5.429   21.371 1.00 34.11  ?  147 ARG A NE    1 
ATOM   1080 C CZ    . ARG A 1 147 ? 39.260 5.331   20.061 1.00 33.56  ?  147 ARG A CZ    1 
ATOM   1081 N NH1   . ARG A 1 147 ? 38.205 5.467   19.265 1.00 32.95  ?  147 ARG A NH1   1 
ATOM   1082 N NH2   . ARG A 1 147 ? 40.473 5.102   19.551 1.00 38.36  ?  147 ARG A NH2   1 
ATOM   1083 N N     . THR A 1 148 ? 33.870 3.074   24.980 1.00 29.82  ?  148 THR A N     1 
ATOM   1084 C CA    . THR A 1 148 ? 32.933 3.424   26.043 1.00 29.19  ?  148 THR A CA    1 
ATOM   1085 C C     . THR A 1 148 ? 33.627 4.174   27.166 1.00 28.91  ?  148 THR A C     1 
ATOM   1086 O O     . THR A 1 148 ? 32.989 4.498   28.171 1.00 29.97  ?  148 THR A O     1 
ATOM   1087 C CB    . THR A 1 148 ? 32.226 2.179   26.605 1.00 31.11  ?  148 THR A CB    1 
ATOM   1088 O OG1   . THR A 1 148 ? 33.078 1.511   27.544 1.00 33.98  ?  148 THR A OG1   1 
ATOM   1089 C CG2   . THR A 1 148 ? 31.914 1.207   25.482 1.00 32.75  ?  148 THR A CG2   1 
ATOM   1090 N N     . THR A 1 149 ? 34.916 4.462   27.013 1.00 28.63  ?  149 THR A N     1 
ATOM   1091 C CA    . THR A 1 149 ? 35.681 5.249   27.968 1.00 29.33  ?  149 THR A CA    1 
ATOM   1092 C C     . THR A 1 149 ? 36.588 6.194   27.192 1.00 27.98  ?  149 THR A C     1 
ATOM   1093 O O     . THR A 1 149 ? 37.371 5.751   26.345 1.00 27.53  ?  149 THR A O     1 
ATOM   1094 C CB    . THR A 1 149 ? 36.500 4.342   28.899 1.00 28.87  ?  149 THR A CB    1 
ATOM   1095 O OG1   . THR A 1 149 ? 35.602 3.489   29.618 1.00 34.85  ?  149 THR A OG1   1 
ATOM   1096 C CG2   . THR A 1 149 ? 37.356 5.166   29.894 1.00 24.30  ?  149 THR A CG2   1 
ATOM   1097 N N     . GLY A 1 150 ? 36.458 7.483   27.474 1.00 23.67  ?  150 GLY A N     1 
ATOM   1098 C CA    . GLY A 1 150 ? 37.437 8.470   27.071 1.00 23.61  ?  150 GLY A CA    1 
ATOM   1099 C C     . GLY A 1 150 ? 36.992 9.844   27.523 1.00 24.69  ?  150 GLY A C     1 
ATOM   1100 O O     . GLY A 1 150 ? 36.052 9.996   28.311 1.00 24.33  ?  150 GLY A O     1 
ATOM   1101 N N     . ILE A 1 151 ? 37.666 10.861  27.020 1.00 21.73  ?  151 ILE A N     1 
ATOM   1102 C CA    . ILE A 1 151 ? 37.195 12.215  27.234 1.00 24.71  ?  151 ILE A CA    1 
ATOM   1103 C C     . ILE A 1 151 ? 36.854 12.788  25.881 1.00 22.93  ?  151 ILE A C     1 
ATOM   1104 O O     . ILE A 1 151 ? 37.675 12.753  24.961 1.00 25.60  ?  151 ILE A O     1 
ATOM   1105 C CB    . ILE A 1 151 ? 38.207 13.088  27.978 1.00 25.29  ?  151 ILE A CB    1 
ATOM   1106 C CG1   . ILE A 1 151 ? 37.632 14.489  28.108 1.00 22.05  ?  151 ILE A CG1   1 
ATOM   1107 C CG2   . ILE A 1 151 ? 39.567 13.040  27.293 1.00 23.46  ?  151 ILE A CG2   1 
ATOM   1108 C CD1   . ILE A 1 151 ? 38.149 15.190  29.285 1.00 26.06  ?  151 ILE A CD1   1 
ATOM   1109 N N     . VAL A 1 152 ? 35.642 13.255  25.752 1.00 23.14  ?  152 VAL A N     1 
ATOM   1110 C CA    . VAL A 1 152 ? 35.117 13.793  24.516 1.00 22.88  ?  152 VAL A CA    1 
ATOM   1111 C C     . VAL A 1 152 ? 35.236 15.298  24.558 1.00 25.88  ?  152 VAL A C     1 
ATOM   1112 O O     . VAL A 1 152 ? 35.006 15.949  25.588 1.00 27.82  ?  152 VAL A O     1 
ATOM   1113 C CB    . VAL A 1 152 ? 33.657 13.375  24.295 1.00 26.52  ?  152 VAL A CB    1 
ATOM   1114 C CG1   . VAL A 1 152 ? 33.054 14.187  23.170 1.00 21.78  ?  152 VAL A CG1   1 
ATOM   1115 C CG2   . VAL A 1 152 ? 33.581 11.870  24.038 1.00 25.28  ?  152 VAL A CG2   1 
ATOM   1116 N N     . MET A 1 153 ? 35.600 15.838  23.446 1.00 26.47  ?  153 MET A N     1 
ATOM   1117 C CA    . MET A 1 153 ? 35.813 17.255  23.269 1.00 26.40  ?  153 MET A CA    1 
ATOM   1118 C C     . MET A 1 153 ? 34.730 17.680  22.289 1.00 31.23  ?  153 MET A C     1 
ATOM   1119 O O     . MET A 1 153 ? 34.860 17.439  21.083 1.00 32.87  ?  153 MET A O     1 
ATOM   1120 C CB    . MET A 1 153 ? 37.222 17.452  22.738 1.00 29.32  ?  153 MET A CB    1 
ATOM   1121 C CG    . MET A 1 153 ? 37.932 18.604  23.284 1.00 36.32  ?  153 MET A CG    1 
ATOM   1122 S SD    . MET A 1 153 ? 37.021 20.007  22.668 1.00 48.59  ?  153 MET A SD    1 
ATOM   1123 C CE    . MET A 1 153 ? 37.841 20.204  21.094 1.00 33.56  ?  153 MET A CE    1 
ATOM   1124 N N     . ASP A 1 154 ? 33.620 18.224  22.802 1.00 29.71  ?  154 ASP A N     1 
ATOM   1125 C CA    . ASP A 1 154 ? 32.450 18.544  21.973 1.00 31.20  ?  154 ASP A CA    1 
ATOM   1126 C C     . ASP A 1 154 ? 32.406 20.053  21.743 1.00 30.41  ?  154 ASP A C     1 
ATOM   1127 O O     . ASP A 1 154 ? 32.229 20.825  22.687 1.00 30.59  ?  154 ASP A O     1 
ATOM   1128 C CB    . ASP A 1 154 ? 31.161 18.060  22.636 1.00 34.01  ?  154 ASP A CB    1 
ATOM   1129 C CG    . ASP A 1 154 ? 30.002 17.859  21.634 1.00 45.50  ?  154 ASP A CG    1 
ATOM   1130 O OD1   . ASP A 1 154 ? 29.821 18.724  20.741 1.00 45.98  ?  154 ASP A OD1   1 
ATOM   1131 O OD2   . ASP A 1 154 ? 29.246 16.852  21.761 1.00 46.69  -1 154 ASP A OD2   1 
ATOM   1132 N N     . SER A 1 155 ? 32.580 20.484  20.498 1.00 29.27  ?  155 SER A N     1 
ATOM   1133 C CA    . SER A 1 155 ? 32.606 21.911  20.194 1.00 27.18  ?  155 SER A CA    1 
ATOM   1134 C C     . SER A 1 155 ? 31.660 22.153  19.042 1.00 25.38  ?  155 SER A C     1 
ATOM   1135 O O     . SER A 1 155 ? 31.972 21.784  17.911 1.00 24.89  ?  155 SER A O     1 
ATOM   1136 C CB    . SER A 1 155 ? 34.008 22.404  19.845 1.00 24.69  ?  155 SER A CB    1 
ATOM   1137 O OG    . SER A 1 155 ? 33.987 23.801  19.658 1.00 25.00  ?  155 SER A OG    1 
ATOM   1138 N N     . GLY A 1 156 ? 30.525 22.782  19.339 1.00 24.51  ?  156 GLY A N     1 
ATOM   1139 C CA    . GLY A 1 156 ? 29.480 23.038  18.375 1.00 26.76  ?  156 GLY A CA    1 
ATOM   1140 C C     . GLY A 1 156 ? 29.330 24.502  18.029 1.00 29.33  ?  156 GLY A C     1 
ATOM   1141 O O     . GLY A 1 156 ? 30.324 25.179  17.782 1.00 32.74  ?  156 GLY A O     1 
ATOM   1142 N N     . ASP A 1 157 ? 28.099 25.011  18.022 1.00 33.72  ?  157 ASP A N     1 
ATOM   1143 C CA    . ASP A 1 157 ? 27.820 26.378  17.586 1.00 35.85  ?  157 ASP A CA    1 
ATOM   1144 C C     . ASP A 1 157 ? 27.869 27.382  18.730 1.00 34.05  ?  157 ASP A C     1 
ATOM   1145 O O     . ASP A 1 157 ? 28.510 28.425  18.601 1.00 38.34  ?  157 ASP A O     1 
ATOM   1146 C CB    . ASP A 1 157 ? 26.451 26.445  16.885 1.00 35.66  ?  157 ASP A CB    1 
ATOM   1147 C CG    . ASP A 1 157 ? 26.132 27.832  16.321 1.00 42.13  ?  157 ASP A CG    1 
ATOM   1148 O OD1   . ASP A 1 157 ? 25.167 28.464  16.822 1.00 45.18  ?  157 ASP A OD1   1 
ATOM   1149 O OD2   . ASP A 1 157 ? 26.822 28.287  15.371 1.00 44.12  -1 157 ASP A OD2   1 
ATOM   1150 N N     . GLY A 1 158 ? 27.191 27.101  19.838 1.00 35.03  ?  158 GLY A N     1 
ATOM   1151 C CA    . GLY A 1 158 ? 27.124 28.053  20.930 1.00 33.64  ?  158 GLY A CA    1 
ATOM   1152 C C     . GLY A 1 158 ? 27.849 27.628  22.197 1.00 35.58  ?  158 GLY A C     1 
ATOM   1153 O O     . GLY A 1 158 ? 27.960 28.434  23.127 1.00 40.93  ?  158 GLY A O     1 
ATOM   1154 N N     . VAL A 1 159 ? 28.360 26.394  22.256 1.00 29.86  ?  159 VAL A N     1 
ATOM   1155 C CA    . VAL A 1 159 ? 28.893 25.838  23.500 1.00 32.15  ?  159 VAL A CA    1 
ATOM   1156 C C     . VAL A 1 159 ? 29.917 24.758  23.178 1.00 29.41  ?  159 VAL A C     1 
ATOM   1157 O O     . VAL A 1 159 ? 29.752 23.999  22.224 1.00 26.88  ?  159 VAL A O     1 
ATOM   1158 C CB    . VAL A 1 159 ? 27.767 25.269  24.401 1.00 31.79  ?  159 VAL A CB    1 
ATOM   1159 C CG1   . VAL A 1 159 ? 27.088 24.060  23.749 1.00 23.26  ?  159 VAL A CG1   1 
ATOM   1160 C CG2   . VAL A 1 159 ? 28.316 24.910  25.776 1.00 30.88  ?  159 VAL A CG2   1 
ATOM   1161 N N     . THR A 1 160 ? 30.971 24.679  23.994 1.00 27.76  ?  160 THR A N     1 
ATOM   1162 C CA    . THR A 1 160 ? 31.922 23.575  23.969 1.00 28.65  ?  160 THR A CA    1 
ATOM   1163 C C     . THR A 1 160 ? 31.908 22.893  25.330 1.00 26.59  ?  160 THR A C     1 
ATOM   1164 O O     . THR A 1 160 ? 31.737 23.559  26.347 1.00 30.19  ?  160 THR A O     1 
ATOM   1165 C CB    . THR A 1 160 ? 33.350 24.064  23.632 1.00 28.98  ?  160 THR A CB    1 
ATOM   1166 O OG1   . THR A 1 160 ? 33.368 24.715  22.361 1.00 27.21  ?  160 THR A OG1   1 
ATOM   1167 C CG2   . THR A 1 160 ? 34.328 22.922  23.586 1.00 26.44  ?  160 THR A CG2   1 
ATOM   1168 N N     . HIS A 1 161 ? 32.075 21.567  25.346 1.00 26.67  ?  161 HIS A N     1 
ATOM   1169 C CA    . HIS A 1 161 ? 32.146 20.761  26.565 1.00 26.35  ?  161 HIS A CA    1 
ATOM   1170 C C     . HIS A 1 161 ? 33.350 19.828  26.515 1.00 26.28  ?  161 HIS A C     1 
ATOM   1171 O O     . HIS A 1 161 ? 33.594 19.191  25.490 1.00 29.49  ?  161 HIS A O     1 
ATOM   1172 C CB    . HIS A 1 161 ? 30.900 19.896  26.739 1.00 24.11  ?  161 HIS A CB    1 
ATOM   1173 C CG    . HIS A 1 161 ? 29.668 20.649  27.128 1.00 29.84  ?  161 HIS A CG    1 
ATOM   1174 N ND1   . HIS A 1 161 ? 28.643 20.909  26.243 1.00 30.20  ?  161 HIS A ND1   1 
ATOM   1175 C CD2   . HIS A 1 161 ? 29.269 21.157  28.320 1.00 31.73  ?  161 HIS A CD2   1 
ATOM   1176 C CE1   . HIS A 1 161 ? 27.687 21.576  26.863 1.00 29.65  ?  161 HIS A CE1   1 
ATOM   1177 N NE2   . HIS A 1 161 ? 28.040 21.734  28.125 1.00 30.93  ?  161 HIS A NE2   1 
ATOM   1178 N N     . THR A 1 162 ? 34.093 19.713  27.614 1.00 26.44  ?  162 THR A N     1 
ATOM   1179 C CA    . THR A 1 162 ? 35.051 18.618  27.764 1.00 30.72  ?  162 THR A CA    1 
ATOM   1180 C C     . THR A 1 162 ? 34.433 17.651  28.782 1.00 30.44  ?  162 THR A C     1 
ATOM   1181 O O     . THR A 1 162 ? 34.097 18.060  29.896 1.00 30.60  ?  162 THR A O     1 
ATOM   1182 C CB    . THR A 1 162 ? 36.474 19.098  28.150 1.00 28.62  ?  162 THR A CB    1 
ATOM   1183 O OG1   . THR A 1 162 ? 36.488 20.477  28.485 1.00 30.26  ?  162 THR A OG1   1 
ATOM   1184 C CG2   . THR A 1 162 ? 37.419 18.997  26.974 1.00 26.27  ?  162 THR A CG2   1 
ATOM   1185 N N     . VAL A 1 163 ? 34.210 16.398  28.360 1.00 28.10  ?  163 VAL A N     1 
ATOM   1186 C CA    . VAL A 1 163 ? 33.302 15.431  28.994 1.00 25.75  ?  163 VAL A CA    1 
ATOM   1187 C C     . VAL A 1 163 ? 33.972 14.081  29.211 1.00 28.00  ?  163 VAL A C     1 
ATOM   1188 O O     . VAL A 1 163 ? 33.922 13.217  28.324 1.00 25.86  ?  163 VAL A O     1 
ATOM   1189 C CB    . VAL A 1 163 ? 32.048 15.187  28.136 1.00 24.63  ?  163 VAL A CB    1 
ATOM   1190 C CG1   . VAL A 1 163 ? 30.991 14.338  28.898 1.00 16.70  ?  163 VAL A CG1   1 
ATOM   1191 C CG2   . VAL A 1 163 ? 31.491 16.503  27.572 1.00 24.81  ?  163 VAL A CG2   1 
ATOM   1192 N N     . PRO A 1 164 ? 34.578 13.829  30.364 1.00 32.38  ?  164 PRO A N     1 
ATOM   1193 C CA    . PRO A 1 164 ? 35.115 12.480  30.614 1.00 28.80  ?  164 PRO A CA    1 
ATOM   1194 C C     . PRO A 1 164 ? 33.985 11.460  30.801 1.00 31.62  ?  164 PRO A C     1 
ATOM   1195 O O     . PRO A 1 164 ? 32.968 11.741  31.441 1.00 30.25  ?  164 PRO A O     1 
ATOM   1196 C CB    . PRO A 1 164 ? 35.955 12.661  31.887 1.00 25.57  ?  164 PRO A CB    1 
ATOM   1197 C CG    . PRO A 1 164 ? 35.540 14.008  32.465 1.00 26.13  ?  164 PRO A CG    1 
ATOM   1198 C CD    . PRO A 1 164 ? 35.004 14.827  31.368 1.00 26.43  ?  164 PRO A CD    1 
ATOM   1199 N N     . ILE A 1 165 ? 34.173 10.263  30.236 1.00 28.99  ?  165 ILE A N     1 
ATOM   1200 C CA    . ILE A 1 165 ? 33.152 9.217   30.221 1.00 27.96  ?  165 ILE A CA    1 
ATOM   1201 C C     . ILE A 1 165 ? 33.800 7.904   30.647 1.00 28.47  ?  165 ILE A C     1 
ATOM   1202 O O     . ILE A 1 165 ? 34.755 7.453   30.015 1.00 32.53  ?  165 ILE A O     1 
ATOM   1203 C CB    . ILE A 1 165 ? 32.522 9.090   28.821 1.00 30.05  ?  165 ILE A CB    1 
ATOM   1204 C CG1   . ILE A 1 165 ? 31.830 10.408  28.447 1.00 26.07  ?  165 ILE A CG1   1 
ATOM   1205 C CG2   . ILE A 1 165 ? 31.609 7.858   28.743 1.00 26.77  ?  165 ILE A CG2   1 
ATOM   1206 C CD1   . ILE A 1 165 ? 31.138 10.393  27.115 1.00 26.35  ?  165 ILE A CD1   1 
ATOM   1207 N N     . TYR A 1 166 ? 33.309 7.287   31.711 1.00 29.14  ?  166 TYR A N     1 
ATOM   1208 C CA    . TYR A 1 166 ? 33.915 6.045   32.190 1.00 30.13  ?  166 TYR A CA    1 
ATOM   1209 C C     . TYR A 1 166 ? 32.885 4.924   32.103 1.00 33.92  ?  166 TYR A C     1 
ATOM   1210 O O     . TYR A 1 166 ? 31.805 5.018   32.706 1.00 30.26  ?  166 TYR A O     1 
ATOM   1211 C CB    . TYR A 1 166 ? 34.453 6.198   33.615 1.00 28.55  ?  166 TYR A CB    1 
ATOM   1212 C CG    . TYR A 1 166 ? 35.087 4.932   34.155 1.00 36.60  ?  166 TYR A CG    1 
ATOM   1213 C CD1   . TYR A 1 166 ? 36.278 4.438   33.619 1.00 36.41  ?  166 TYR A CD1   1 
ATOM   1214 C CD2   . TYR A 1 166 ? 34.504 4.228   35.205 1.00 36.17  ?  166 TYR A CD2   1 
ATOM   1215 C CE1   . TYR A 1 166 ? 36.875 3.265   34.113 1.00 36.85  ?  166 TYR A CE1   1 
ATOM   1216 C CE2   . TYR A 1 166 ? 35.083 3.061   35.694 1.00 41.98  ?  166 TYR A CE2   1 
ATOM   1217 C CZ    . TYR A 1 166 ? 36.269 2.576   35.142 1.00 44.38  ?  166 TYR A CZ    1 
ATOM   1218 O OH    . TYR A 1 166 ? 36.842 1.407   35.634 1.00 48.46  ?  166 TYR A OH    1 
ATOM   1219 N N     . GLU A 1 167 ? 33.214 3.874   31.347 1.00 30.90  ?  167 GLU A N     1 
ATOM   1220 C CA    . GLU A 1 167 ? 32.288 2.770   31.048 1.00 33.90  ?  167 GLU A CA    1 
ATOM   1221 C C     . GLU A 1 167 ? 30.865 3.276   30.796 1.00 34.56  ?  167 GLU A C     1 
ATOM   1222 O O     . GLU A 1 167 ? 29.902 2.861   31.450 1.00 37.03  ?  167 GLU A O     1 
ATOM   1223 C CB    . GLU A 1 167 ? 32.265 1.693   32.149 1.00 33.80  ?  167 GLU A CB    1 
ATOM   1224 C CG    . GLU A 1 167 ? 33.542 1.506   32.950 1.00 39.91  ?  167 GLU A CG    1 
ATOM   1225 C CD    . GLU A 1 167 ? 33.618 0.140   33.589 1.00 52.49  ?  167 GLU A CD    1 
ATOM   1226 O OE1   . GLU A 1 167 ? 32.827 -0.120  34.532 1.00 63.25  ?  167 GLU A OE1   1 
ATOM   1227 O OE2   . GLU A 1 167 ? 34.490 -0.660  33.175 1.00 60.28  -1 167 GLU A OE2   1 
ATOM   1228 N N     . GLY A 1 168 ? 30.750 4.180   29.812 1.00 30.77  ?  168 GLY A N     1 
ATOM   1229 C CA    . GLY A 1 168 ? 29.471 4.666   29.328 1.00 28.71  ?  168 GLY A CA    1 
ATOM   1230 C C     . GLY A 1 168 ? 28.871 5.847   30.078 1.00 28.80  ?  168 GLY A C     1 
ATOM   1231 O O     . GLY A 1 168 ? 27.958 6.496   29.548 1.00 29.30  ?  168 GLY A O     1 
ATOM   1232 N N     . TYR A 1 169 ? 29.338 6.141   31.292 1.00 28.11  ?  169 TYR A N     1 
ATOM   1233 C CA    . TYR A 1 169 ? 28.734 7.151   32.154 1.00 24.99  ?  169 TYR A CA    1 
ATOM   1234 C C     . TYR A 1 169 ? 29.552 8.439   32.133 1.00 28.03  ?  169 TYR A C     1 
ATOM   1235 O O     . TYR A 1 169 ? 30.734 8.438   32.506 1.00 29.40  ?  169 TYR A O     1 
ATOM   1236 C CB    . TYR A 1 169 ? 28.638 6.607   33.565 1.00 26.01  ?  169 TYR A CB    1 
ATOM   1237 C CG    . TYR A 1 169 ? 28.050 7.520   34.576 1.00 25.61  ?  169 TYR A CG    1 
ATOM   1238 C CD1   . TYR A 1 169 ? 26.797 8.069   34.398 1.00 25.86  ?  169 TYR A CD1   1 
ATOM   1239 C CD2   . TYR A 1 169 ? 28.737 7.792   35.754 1.00 27.82  ?  169 TYR A CD2   1 
ATOM   1240 C CE1   . TYR A 1 169 ? 26.239 8.896   35.364 1.00 28.01  ?  169 TYR A CE1   1 
ATOM   1241 C CE2   . TYR A 1 169 ? 28.207 8.625   36.726 1.00 28.23  ?  169 TYR A CE2   1 
ATOM   1242 C CZ    . TYR A 1 169 ? 26.954 9.175   36.533 1.00 29.44  ?  169 TYR A CZ    1 
ATOM   1243 O OH    . TYR A 1 169 ? 26.437 10.001  37.505 1.00 25.54  ?  169 TYR A OH    1 
ATOM   1244 N N     . ALA A 1 170 ? 28.930 9.529   31.687 1.00 26.74  ?  170 ALA A N     1 
ATOM   1245 C CA    . ALA A 1 170 ? 29.559 10.840  31.797 1.00 28.76  ?  170 ALA A CA    1 
ATOM   1246 C C     . ALA A 1 170 ? 29.582 11.283  33.259 1.00 30.76  ?  170 ALA A C     1 
ATOM   1247 O O     . ALA A 1 170 ? 28.552 11.246  33.949 1.00 28.31  ?  170 ALA A O     1 
ATOM   1248 C CB    . ALA A 1 170 ? 28.831 11.872  30.943 1.00 25.85  ?  170 ALA A CB    1 
ATOM   1249 N N     . LEU A 1 171 ? 30.770 11.715  33.717 1.00 28.55  ?  171 LEU A N     1 
ATOM   1250 C CA    . LEU A 1 171 ? 31.085 12.022  35.104 1.00 28.64  ?  171 LEU A CA    1 
ATOM   1251 C C     . LEU A 1 171 ? 30.674 13.451  35.435 1.00 28.86  ?  171 LEU A C     1 
ATOM   1252 O O     . LEU A 1 171 ? 31.389 14.401  35.098 1.00 28.81  ?  171 LEU A O     1 
ATOM   1253 C CB    . LEU A 1 171 ? 32.575 11.802  35.376 1.00 27.02  ?  171 LEU A CB    1 
ATOM   1254 C CG    . LEU A 1 171 ? 33.086 10.387  35.050 1.00 32.07  ?  171 LEU A CG    1 
ATOM   1255 C CD1   . LEU A 1 171 ? 34.569 10.279  35.296 1.00 28.14  ?  171 LEU A CD1   1 
ATOM   1256 C CD2   . LEU A 1 171 ? 32.348 9.292   35.843 1.00 30.63  ?  171 LEU A CD2   1 
ATOM   1257 N N     . PRO A 1 172 ? 29.533 13.634  36.104 1.00 27.76  ?  172 PRO A N     1 
ATOM   1258 C CA    . PRO A 1 172 ? 29.072 14.993  36.407 1.00 26.78  ?  172 PRO A CA    1 
ATOM   1259 C C     . PRO A 1 172 ? 30.079 15.829  37.171 1.00 27.20  ?  172 PRO A C     1 
ATOM   1260 O O     . PRO A 1 172 ? 30.053 17.059  37.049 1.00 27.27  ?  172 PRO A O     1 
ATOM   1261 C CB    . PRO A 1 172 ? 27.802 14.751  37.238 1.00 29.57  ?  172 PRO A CB    1 
ATOM   1262 C CG    . PRO A 1 172 ? 27.722 13.292  37.485 1.00 27.24  ?  172 PRO A CG    1 
ATOM   1263 C CD    . PRO A 1 172 ? 28.555 12.609  36.498 1.00 24.77  ?  172 PRO A CD    1 
ATOM   1264 N N     . HIS A 1 173 ? 30.968 15.215  37.960 1.00 26.97  ?  173 HIS A N     1 
ATOM   1265 C CA    . HIS A 1 173 ? 31.857 16.021  38.787 1.00 27.58  ?  173 HIS A CA    1 
ATOM   1266 C C     . HIS A 1 173 ? 33.008 16.620  37.998 1.00 26.11  ?  173 HIS A C     1 
ATOM   1267 O O     . HIS A 1 173 ? 33.597 17.602  38.460 1.00 28.66  ?  173 HIS A O     1 
ATOM   1268 C CB    . HIS A 1 173 ? 32.412 15.211  39.961 1.00 27.34  ?  173 HIS A CB    1 
ATOM   1269 C CG    . HIS A 1 173 ? 33.088 13.938  39.554 1.00 29.72  ?  173 HIS A CG    1 
ATOM   1270 N ND1   . HIS A 1 173 ? 32.477 12.702  39.648 1.00 26.49  ?  173 HIS A ND1   1 
ATOM   1271 C CD2   . HIS A 1 173 ? 34.325 13.707  39.056 1.00 26.92  ?  173 HIS A CD2   1 
ATOM   1272 C CE1   . HIS A 1 173 ? 33.310 11.764  39.232 1.00 25.81  ?  173 HIS A CE1   1 
ATOM   1273 N NE2   . HIS A 1 173 ? 34.431 12.349  38.848 1.00 29.40  ?  173 HIS A NE2   1 
ATOM   1274 N N     . ALA A 1 174 ? 33.323 16.090  36.819 1.00 22.19  ?  174 ALA A N     1 
ATOM   1275 C CA    . ALA A 1 174 ? 34.464 16.589  36.062 1.00 28.05  ?  174 ALA A CA    1 
ATOM   1276 C C     . ALA A 1 174 ? 34.104 17.188  34.700 1.00 28.04  ?  174 ALA A C     1 
ATOM   1277 O O     . ALA A 1 174 ? 35.008 17.627  33.968 1.00 23.23  ?  174 ALA A O     1 
ATOM   1278 C CB    . ALA A 1 174 ? 35.517 15.476  35.895 1.00 24.98  ?  174 ALA A CB    1 
ATOM   1279 N N     . ILE A 1 175 ? 32.821 17.257  34.346 1.00 26.38  ?  175 ILE A N     1 
ATOM   1280 C CA    . ILE A 1 175 ? 32.442 17.860  33.074 1.00 31.15  ?  175 ILE A CA    1 
ATOM   1281 C C     . ILE A 1 175 ? 32.670 19.369  33.107 1.00 33.25  ?  175 ILE A C     1 
ATOM   1282 O O     . ILE A 1 175 ? 32.149 20.065  33.984 1.00 34.68  ?  175 ILE A O     1 
ATOM   1283 C CB    . ILE A 1 175 ? 30.982 17.540  32.752 1.00 27.88  ?  175 ILE A CB    1 
ATOM   1284 C CG1   . ILE A 1 175 ? 30.882 16.070  32.333 1.00 26.09  ?  175 ILE A CG1   1 
ATOM   1285 C CG2   . ILE A 1 175 ? 30.482 18.499  31.683 1.00 26.56  ?  175 ILE A CG2   1 
ATOM   1286 C CD1   . ILE A 1 175 ? 29.468 15.523  32.258 1.00 22.69  ?  175 ILE A CD1   1 
ATOM   1287 N N     . LEU A 1 176 ? 33.444 19.887  32.145 1.00 34.34  ?  176 LEU A N     1 
ATOM   1288 C CA    . LEU A 1 176 ? 33.695 21.324  32.021 1.00 35.94  ?  176 LEU A CA    1 
ATOM   1289 C C     . LEU A 1 176 ? 32.935 21.895  30.819 1.00 36.38  ?  176 LEU A C     1 
ATOM   1290 O O     . LEU A 1 176 ? 32.865 21.273  29.750 1.00 33.84  ?  176 LEU A O     1 
ATOM   1291 C CB    . LEU A 1 176 ? 35.209 21.624  31.921 1.00 31.75  ?  176 LEU A CB    1 
ATOM   1292 C CG    . LEU A 1 176 ? 35.887 21.396  33.289 1.00 34.48  ?  176 LEU A CG    1 
ATOM   1293 C CD1   . LEU A 1 176 ? 37.329 21.729  33.360 1.00 33.76  ?  176 LEU A CD1   1 
ATOM   1294 C CD2   . LEU A 1 176 ? 35.168 22.190  34.337 1.00 42.28  ?  176 LEU A CD2   1 
ATOM   1295 N N     . ARG A 1 177 ? 32.339 23.069  31.014 1.00 35.22  ?  177 ARG A N     1 
ATOM   1296 C CA    . ARG A 1 177 ? 31.587 23.760  29.978 1.00 37.84  ?  177 ARG A CA    1 
ATOM   1297 C C     . ARG A 1 177 ? 32.216 25.118  29.717 1.00 39.04  ?  177 ARG A C     1 
ATOM   1298 O O     . ARG A 1 177 ? 32.891 25.689  30.579 1.00 44.83  ?  177 ARG A O     1 
ATOM   1299 C CB    . ARG A 1 177 ? 30.124 23.924  30.372 1.00 40.51  ?  177 ARG A CB    1 
ATOM   1300 C CG    . ARG A 1 177 ? 29.419 25.084  29.721 1.00 41.65  ?  177 ARG A CG    1 
ATOM   1301 C CD    . ARG A 1 177 ? 27.976 25.155  30.189 1.00 47.60  ?  177 ARG A CD    1 
ATOM   1302 N NE    . ARG A 1 177 ? 27.268 26.314  29.652 1.00 57.82  ?  177 ARG A NE    1 
ATOM   1303 C CZ    . ARG A 1 177 ? 26.044 26.679  30.032 1.00 58.43  ?  177 ARG A CZ    1 
ATOM   1304 N NH1   . ARG A 1 177 ? 25.401 25.981  30.962 1.00 53.50  ?  177 ARG A NH1   1 
ATOM   1305 N NH2   . ARG A 1 177 ? 25.467 27.746  29.495 1.00 56.31  ?  177 ARG A NH2   1 
ATOM   1306 N N     . LEU A 1 178 ? 31.989 25.635  28.518 1.00 38.24  ?  178 LEU A N     1 
ATOM   1307 C CA    . LEU A 1 178 ? 32.786 26.748  28.013 1.00 40.52  ?  178 LEU A CA    1 
ATOM   1308 C C     . LEU A 1 178 ? 31.984 27.437  26.928 1.00 36.84  ?  178 LEU A C     1 
ATOM   1309 O O     . LEU A 1 178 ? 31.612 26.793  25.952 1.00 35.59  ?  178 LEU A O     1 
ATOM   1310 C CB    . LEU A 1 178 ? 34.109 26.226  27.471 1.00 38.91  ?  178 LEU A CB    1 
ATOM   1311 C CG    . LEU A 1 178 ? 34.870 27.224  26.632 1.00 41.54  ?  178 LEU A CG    1 
ATOM   1312 C CD1   . LEU A 1 178 ? 35.073 28.459  27.488 1.00 38.35  ?  178 LEU A CD1   1 
ATOM   1313 C CD2   . LEU A 1 178 ? 36.186 26.615  26.199 1.00 39.14  ?  178 LEU A CD2   1 
ATOM   1314 N N     . ASP A 1 179 ? 31.609 28.694  27.127 1.00 44.36  ?  179 ASP A N     1 
ATOM   1315 C CA    . ASP A 1 179 ? 30.689 29.353  26.163 1.00 52.82  ?  179 ASP A CA    1 
ATOM   1316 C C     . ASP A 1 179 ? 31.442 30.014  25.006 1.00 51.85  ?  179 ASP A C     1 
ATOM   1317 O O     . ASP A 1 179 ? 31.162 31.179  24.710 1.00 54.16  ?  179 ASP A O     1 
ATOM   1318 C CB    . ASP A 1 179 ? 29.625 30.175  26.893 1.00 55.26  ?  179 ASP A CB    1 
ATOM   1319 C CG    . ASP A 1 179 ? 28.481 29.308  27.387 1.00 72.10  ?  179 ASP A CG    1 
ATOM   1320 O OD1   . ASP A 1 179 ? 27.830 28.672  26.543 1.00 70.86  ?  179 ASP A OD1   1 
ATOM   1321 O OD2   . ASP A 1 179 ? 28.264 29.259  28.610 1.00 93.17  -1 179 ASP A OD2   1 
ATOM   1322 N N     . LEU A 1 180 ? 32.361 29.287  24.385 1.00 42.43  ?  180 LEU A N     1 
ATOM   1323 C CA    . LEU A 1 180 ? 33.057 29.785  23.177 1.00 42.55  ?  180 LEU A CA    1 
ATOM   1324 C C     . LEU A 1 180 ? 32.995 28.657  22.156 1.00 41.31  ?  180 LEU A C     1 
ATOM   1325 O O     . LEU A 1 180 ? 33.457 27.557  22.470 1.00 34.12  ?  180 LEU A O     1 
ATOM   1326 C CB    . LEU A 1 180 ? 34.500 30.172  23.507 1.00 41.09  ?  180 LEU A CB    1 
ATOM   1327 C CG    . LEU A 1 180 ? 35.438 30.403  22.326 1.00 37.49  ?  180 LEU A CG    1 
ATOM   1328 C CD1   . LEU A 1 180 ? 35.719 31.884  22.148 1.00 35.13  ?  180 LEU A CD1   1 
ATOM   1329 C CD2   . LEU A 1 180 ? 36.740 29.658  22.542 1.00 36.70  ?  180 LEU A CD2   1 
ATOM   1330 N N     . ALA A 1 181 ? 32.391 28.926  21.002 1.00 40.48  ?  181 ALA A N     1 
ATOM   1331 C CA    . ALA A 1 181 ? 32.350 27.923  19.927 1.00 31.32  ?  181 ALA A CA    1 
ATOM   1332 C C     . ALA A 1 181 ? 31.876 28.677  18.696 1.00 29.83  ?  181 ALA A C     1 
ATOM   1333 O O     . ALA A 1 181 ? 31.709 29.878  18.811 1.00 32.23  ?  181 ALA A O     1 
ATOM   1334 C CB    . ALA A 1 181 ? 31.222 26.979  20.157 1.00 30.00  ?  181 ALA A CB    1 
ATOM   1335 N N     . GLY A 1 182 ? 31.642 27.980  17.591 1.00 33.74  ?  182 GLY A N     1 
ATOM   1336 C CA    . GLY A 1 182 ? 31.605 28.477  16.203 1.00 33.64  ?  182 GLY A CA    1 
ATOM   1337 C C     . GLY A 1 182 ? 30.991 29.851  16.077 1.00 35.67  ?  182 GLY A C     1 
ATOM   1338 O O     . GLY A 1 182 ? 31.554 30.643  15.344 1.00 35.26  ?  182 GLY A O     1 
ATOM   1339 N N     . ARG A 1 183 ? 29.861 30.102  16.728 1.00 37.84  ?  183 ARG A N     1 
ATOM   1340 C CA    . ARG A 1 183 ? 29.200 31.423  16.629 1.00 38.43  ?  183 ARG A CA    1 
ATOM   1341 C C     . ARG A 1 183 ? 30.224 32.488  17.008 1.00 36.66  ?  183 ARG A C     1 
ATOM   1342 O O     . ARG A 1 183 ? 30.303 33.500  16.311 1.00 32.72  ?  183 ARG A O     1 
ATOM   1343 C CB    . ARG A 1 183 ? 27.951 31.485  17.511 1.00 38.22  ?  183 ARG A CB    1 
ATOM   1344 C CG    . ARG A 1 183 ? 26.647 31.532  16.732 1.00 42.40  ?  183 ARG A CG    1 
ATOM   1345 C CD    . ARG A 1 183 ? 25.391 31.655  17.568 1.00 48.28  ?  183 ARG A CD    1 
ATOM   1346 N NE    . ARG A 1 183 ? 25.600 31.725  19.004 1.00 53.78  ?  183 ARG A NE    1 
ATOM   1347 C CZ    . ARG A 1 183 ? 25.068 30.887  19.885 1.00 58.42  ?  183 ARG A CZ    1 
ATOM   1348 N NH1   . ARG A 1 183 ? 24.311 29.882  19.477 1.00 48.51  ?  183 ARG A NH1   1 
ATOM   1349 N NH2   . ARG A 1 183 ? 25.311 31.049  21.172 1.00 56.90  ?  183 ARG A NH2   1 
ATOM   1350 N N     . ASP A 1 184 ? 30.994 32.230  18.063 1.00 35.30  ?  184 ASP A N     1 
ATOM   1351 C CA    . ASP A 1 184 ? 32.001 33.198  18.462 1.00 34.66  ?  184 ASP A CA    1 
ATOM   1352 C C     . ASP A 1 184 ? 33.154 33.242  17.476 1.00 33.73  ?  184 ASP A C     1 
ATOM   1353 O O     . ASP A 1 184 ? 33.717 34.312  17.225 1.00 33.92  ?  184 ASP A O     1 
ATOM   1354 C CB    . ASP A 1 184 ? 32.503 32.863  19.864 1.00 37.87  ?  184 ASP A CB    1 
ATOM   1355 C CG    . ASP A 1 184 ? 31.370 32.691  20.869 1.00 43.03  ?  184 ASP A CG    1 
ATOM   1356 O OD1   . ASP A 1 184 ? 30.793 33.727  21.278 1.00 47.00  ?  184 ASP A OD1   1 
ATOM   1357 O OD2   . ASP A 1 184 ? 31.062 31.530  21.264 1.00 46.66  -1 184 ASP A OD2   1 
ATOM   1358 N N     . LEU A 1 185 ? 33.523 32.094  16.919 1.00 31.54  ?  185 LEU A N     1 
ATOM   1359 C CA    . LEU A 1 185 ? 34.561 32.074  15.900 1.00 32.85  ?  185 LEU A CA    1 
ATOM   1360 C C     . LEU A 1 185 ? 34.120 32.790  14.631 1.00 32.94  ?  185 LEU A C     1 
ATOM   1361 O O     . LEU A 1 185 ? 34.946 33.410  13.948 1.00 30.79  ?  185 LEU A O     1 
ATOM   1362 C CB    . LEU A 1 185 ? 34.948 30.639  15.574 1.00 30.97  ?  185 LEU A CB    1 
ATOM   1363 C CG    . LEU A 1 185 ? 35.651 29.880  16.681 1.00 28.47  ?  185 LEU A CG    1 
ATOM   1364 C CD1   . LEU A 1 185 ? 36.426 28.807  16.001 1.00 28.86  ?  185 LEU A CD1   1 
ATOM   1365 C CD2   . LEU A 1 185 ? 36.540 30.787  17.496 1.00 26.32  ?  185 LEU A CD2   1 
ATOM   1366 N N     . THR A 1 186 ? 32.838 32.669  14.269 1.00 31.59  ?  186 THR A N     1 
ATOM   1367 C CA    . THR A 1 186 ? 32.338 33.328  13.065 1.00 34.58  ?  186 THR A CA    1 
ATOM   1368 C C     . THR A 1 186 ? 32.322 34.847  13.218 1.00 36.90  ?  186 THR A C     1 
ATOM   1369 O O     . THR A 1 186 ? 32.564 35.569  12.244 1.00 35.45  ?  186 THR A O     1 
ATOM   1370 C CB    . THR A 1 186 ? 30.942 32.846  12.719 1.00 33.21  ?  186 THR A CB    1 
ATOM   1371 O OG1   . THR A 1 186 ? 31.033 31.724  11.851 1.00 33.05  ?  186 THR A OG1   1 
ATOM   1372 C CG2   . THR A 1 186 ? 30.208 33.939  11.995 1.00 34.06  ?  186 THR A CG2   1 
ATOM   1373 N N     . ASP A 1 187 ? 32.031 35.347  14.427 1.00 35.82  ?  187 ASP A N     1 
ATOM   1374 C CA    . ASP A 1 187 ? 32.022 36.789  14.664 1.00 37.92  ?  187 ASP A CA    1 
ATOM   1375 C C     . ASP A 1 187 ? 33.429 37.354  14.657 1.00 37.64  ?  187 ASP A C     1 
ATOM   1376 O O     . ASP A 1 187 ? 33.676 38.411  14.060 1.00 39.58  ?  187 ASP A O     1 
ATOM   1377 C CB    . ASP A 1 187 ? 31.342 37.113  15.997 1.00 39.99  ?  187 ASP A CB    1 
ATOM   1378 C CG    . ASP A 1 187 ? 29.837 36.848  15.978 1.00 49.95  ?  187 ASP A CG    1 
ATOM   1379 O OD1   . ASP A 1 187 ? 29.230 36.736  14.869 1.00 48.62  ?  187 ASP A OD1   1 
ATOM   1380 O OD2   . ASP A 1 187 ? 29.257 36.753  17.091 1.00 52.01  -1 187 ASP A OD2   1 
ATOM   1381 N N     . TYR A 1 188 ? 34.361 36.680  15.334 1.00 34.25  ?  188 TYR A N     1 
ATOM   1382 C CA    . TYR A 1 188 ? 35.757 37.088  15.251 1.00 34.02  ?  188 TYR A CA    1 
ATOM   1383 C C     . TYR A 1 188 ? 36.218 37.137  13.800 1.00 38.97  ?  188 TYR A C     1 
ATOM   1384 O O     . TYR A 1 188 ? 36.849 38.116  13.378 1.00 38.32  ?  188 TYR A O     1 
ATOM   1385 C CB    . TYR A 1 188 ? 36.649 36.149  16.056 1.00 32.89  ?  188 TYR A CB    1 
ATOM   1386 C CG    . TYR A 1 188 ? 38.035 36.702  16.313 1.00 34.52  ?  188 TYR A CG    1 
ATOM   1387 C CD1   . TYR A 1 188 ? 38.212 37.991  16.813 1.00 32.48  ?  188 TYR A CD1   1 
ATOM   1388 C CD2   . TYR A 1 188 ? 39.172 35.927  16.077 1.00 34.26  ?  188 TYR A CD2   1 
ATOM   1389 C CE1   . TYR A 1 188 ? 39.479 38.494  17.069 1.00 35.10  ?  188 TYR A CE1   1 
ATOM   1390 C CE2   . TYR A 1 188 ? 40.455 36.425  16.333 1.00 31.57  ?  188 TYR A CE2   1 
ATOM   1391 C CZ    . TYR A 1 188 ? 40.606 37.706  16.822 1.00 34.18  ?  188 TYR A CZ    1 
ATOM   1392 O OH    . TYR A 1 188 ? 41.873 38.206  17.073 1.00 28.20  ?  188 TYR A OH    1 
ATOM   1393 N N     . LEU A 1 189 ? 35.911 36.096  13.006 1.00 35.88  ?  189 LEU A N     1 
ATOM   1394 C CA    . LEU A 1 189 ? 36.323 36.164  11.614 1.00 31.22  ?  189 LEU A CA    1 
ATOM   1395 C C     . LEU A 1 189 ? 35.776 37.424  10.976 1.00 33.10  ?  189 LEU A C     1 
ATOM   1396 O O     . LEU A 1 189 ? 36.520 38.155  10.316 1.00 36.60  ?  189 LEU A O     1 
ATOM   1397 C CB    . LEU A 1 189 ? 35.904 34.922  10.832 1.00 34.35  ?  189 LEU A CB    1 
ATOM   1398 C CG    . LEU A 1 189 ? 36.587 34.861  9.452  1.00 29.20  ?  189 LEU A CG    1 
ATOM   1399 C CD1   . LEU A 1 189 ? 38.048 35.156  9.575  1.00 30.09  ?  189 LEU A CD1   1 
ATOM   1400 C CD2   . LEU A 1 189 ? 36.414 33.552  8.783  1.00 28.61  ?  189 LEU A CD2   1 
ATOM   1401 N N     . MET A 1 190 ? 34.496 37.732  11.213 1.00 33.25  ?  190 MET A N     1 
ATOM   1402 C CA    . MET A 1 190 ? 33.944 39.017  10.780 1.00 36.65  ?  190 MET A CA    1 
ATOM   1403 C C     . MET A 1 190 ? 34.835 40.179  11.204 1.00 36.91  ?  190 MET A C     1 
ATOM   1404 O O     . MET A 1 190 ? 35.266 40.992  10.376 1.00 32.87  ?  190 MET A O     1 
ATOM   1405 C CB    . MET A 1 190 ? 32.548 39.222  11.360 1.00 37.40  ?  190 MET A CB    1 
ATOM   1406 C CG    . MET A 1 190 ? 31.387 38.912  10.438 1.00 43.31  ?  190 MET A CG    1 
ATOM   1407 S SD    . MET A 1 190 ? 29.849 38.917  11.395 1.00 44.53  ?  190 MET A SD    1 
ATOM   1408 C CE    . MET A 1 190 ? 29.592 40.682  11.572 1.00 43.60  ?  190 MET A CE    1 
ATOM   1409 N N     . LYS A 1 191 ? 35.113 40.272  12.508 1.00 34.35  ?  191 LYS A N     1 
ATOM   1410 C CA    . LYS A 1 191 ? 35.830 41.428  13.024 1.00 38.39  ?  191 LYS A CA    1 
ATOM   1411 C C     . LYS A 1 191 ? 37.156 41.618  12.291 1.00 38.58  ?  191 LYS A C     1 
ATOM   1412 O O     . LYS A 1 191 ? 37.434 42.703  11.773 1.00 38.14  ?  191 LYS A O     1 
ATOM   1413 C CB    . LYS A 1 191 ? 36.037 41.291  14.539 1.00 42.59  ?  191 LYS A CB    1 
ATOM   1414 C CG    . LYS A 1 191 ? 36.384 42.608  15.261 1.00 51.44  ?  191 LYS A CG    1 
ATOM   1415 C CD    . LYS A 1 191 ? 37.379 42.416  16.422 1.00 55.20  ?  191 LYS A CD    1 
ATOM   1416 C CE    . LYS A 1 191 ? 37.687 43.731  17.194 1.00 70.49  ?  191 LYS A CE    1 
ATOM   1417 N NZ    . LYS A 1 191 ? 36.627 44.232  18.136 1.00 64.94  ?  191 LYS A NZ    1 
ATOM   1418 N N     . ILE A 1 192 ? 37.967 40.560  12.193 1.00 35.10  ?  192 ILE A N     1 
ATOM   1419 C CA    . ILE A 1 192 ? 39.332 40.744  11.703 1.00 36.34  ?  192 ILE A CA    1 
ATOM   1420 C C     . ILE A 1 192 ? 39.380 40.953  10.191 1.00 35.39  ?  192 ILE A C     1 
ATOM   1421 O O     . ILE A 1 192 ? 40.286 41.627  9.691  1.00 34.25  ?  192 ILE A O     1 
ATOM   1422 C CB    . ILE A 1 192 ? 40.254 39.586  12.136 1.00 33.38  ?  192 ILE A CB    1 
ATOM   1423 C CG1   . ILE A 1 192 ? 39.845 38.251  11.521 1.00 27.83  ?  192 ILE A CG1   1 
ATOM   1424 C CG2   . ILE A 1 192 ? 40.325 39.503  13.650 1.00 29.76  ?  192 ILE A CG2   1 
ATOM   1425 C CD1   . ILE A 1 192 ? 40.652 37.124  12.046 1.00 27.30  ?  192 ILE A CD1   1 
ATOM   1426 N N     . LEU A 1 193 ? 38.440 40.388  9.437  1.00 33.10  ?  193 LEU A N     1 
ATOM   1427 C CA    . LEU A 1 193 ? 38.369 40.719  8.019  1.00 34.23  ?  193 LEU A CA    1 
ATOM   1428 C C     . LEU A 1 193 ? 37.947 42.167  7.802  1.00 39.07  ?  193 LEU A C     1 
ATOM   1429 O O     . LEU A 1 193 ? 38.304 42.764  6.783  1.00 39.93  ?  193 LEU A O     1 
ATOM   1430 C CB    . LEU A 1 193 ? 37.402 39.784  7.313  1.00 32.96  ?  193 LEU A CB    1 
ATOM   1431 C CG    . LEU A 1 193 ? 37.898 38.365  7.165  1.00 30.25  ?  193 LEU A CG    1 
ATOM   1432 C CD1   . LEU A 1 193 ? 36.805 37.540  6.542  1.00 29.23  ?  193 LEU A CD1   1 
ATOM   1433 C CD2   . LEU A 1 193 ? 39.122 38.364  6.309  1.00 28.99  ?  193 LEU A CD2   1 
ATOM   1434 N N     . THR A 1 194 ? 37.163 42.730  8.730  1.00 41.07  ?  194 THR A N     1 
ATOM   1435 C CA    . THR A 1 194 ? 36.813 44.147  8.681  1.00 43.66  ?  194 THR A CA    1 
ATOM   1436 C C     . THR A 1 194 ? 38.033 45.020  8.926  1.00 41.16  ?  194 THR A C     1 
ATOM   1437 O O     . THR A 1 194 ? 38.221 46.029  8.249  1.00 44.47  ?  194 THR A O     1 
ATOM   1438 C CB    . THR A 1 194 ? 35.729 44.454  9.721  1.00 44.42  ?  194 THR A CB    1 
ATOM   1439 O OG1   . THR A 1 194 ? 34.450 44.037  9.235  1.00 41.91  ?  194 THR A OG1   1 
ATOM   1440 C CG2   . THR A 1 194 ? 35.683 45.930  10.061 1.00 44.85  ?  194 THR A CG2   1 
ATOM   1441 N N     . GLU A 1 195 ? 38.868 44.643  9.896  1.00 42.58  ?  195 GLU A N     1 
ATOM   1442 C CA    . GLU A 1 195 ? 40.059 45.413  10.241 1.00 46.63  ?  195 GLU A CA    1 
ATOM   1443 C C     . GLU A 1 195 ? 41.062 45.430  9.106  1.00 42.53  ?  195 GLU A C     1 
ATOM   1444 O O     . GLU A 1 195 ? 41.921 46.315  9.064  1.00 46.60  ?  195 GLU A O     1 
ATOM   1445 C CB    . GLU A 1 195 ? 40.743 44.848  11.499 1.00 42.85  ?  195 GLU A CB    1 
ATOM   1446 C CG    . GLU A 1 195 ? 39.895 44.783  12.788 1.00 52.02  ?  195 GLU A CG    1 
ATOM   1447 C CD    . GLU A 1 195 ? 38.677 45.761  12.832 1.00 74.71  ?  195 GLU A CD    1 
ATOM   1448 O OE1   . GLU A 1 195 ? 38.774 46.908  12.299 1.00 80.27  ?  195 GLU A OE1   1 
ATOM   1449 O OE2   . GLU A 1 195 ? 37.618 45.376  13.421 1.00 71.92  -1 195 GLU A OE2   1 
ATOM   1450 N N     . ARG A 1 196 ? 40.962 44.462  8.197  1.00 43.24  ?  196 ARG A N     1 
ATOM   1451 C CA    . ARG A 1 196 ? 41.820 44.322  7.028  1.00 41.38  ?  196 ARG A CA    1 
ATOM   1452 C C     . ARG A 1 196 ? 41.365 45.207  5.869  1.00 46.06  ?  196 ARG A C     1 
ATOM   1453 O O     . ARG A 1 196 ? 42.182 45.534  4.991  1.00 41.51  ?  196 ARG A O     1 
ATOM   1454 C CB    . ARG A 1 196 ? 41.848 42.839  6.632  1.00 39.55  ?  196 ARG A CB    1 
ATOM   1455 C CG    . ARG A 1 196 ? 42.303 42.509  5.239  1.00 39.26  ?  196 ARG A CG    1 
ATOM   1456 C CD    . ARG A 1 196 ? 43.796 42.500  5.157  1.00 37.01  ?  196 ARG A CD    1 
ATOM   1457 N NE    . ARG A 1 196 ? 44.401 41.556  6.089  1.00 45.22  ?  196 ARG A NE    1 
ATOM   1458 C CZ    . ARG A 1 196 ? 45.613 41.699  6.634  1.00 44.16  ?  196 ARG A CZ    1 
ATOM   1459 N NH1   . ARG A 1 196 ? 46.358 42.778  6.362  1.00 36.62  ?  196 ARG A NH1   1 
ATOM   1460 N NH2   . ARG A 1 196 ? 46.084 40.752  7.445  1.00 39.90  ?  196 ARG A NH2   1 
ATOM   1461 N N     . GLY A 1 197 ? 40.089 45.619  5.872  1.00 45.79  ?  197 GLY A N     1 
ATOM   1462 C CA    . GLY A 1 197 ? 39.523 46.507  4.874  1.00 43.04  ?  197 GLY A CA    1 
ATOM   1463 C C     . GLY A 1 197 ? 38.197 46.035  4.313  1.00 48.14  ?  197 GLY A C     1 
ATOM   1464 O O     . GLY A 1 197 ? 37.405 46.841  3.810  1.00 56.32  ?  197 GLY A O     1 
ATOM   1465 N N     . TYR A 1 198 ? 37.985 44.719  4.357  1.00 45.90  ?  198 TYR A N     1 
ATOM   1466 C CA    . TYR A 1 198 ? 36.766 44.100  3.777  1.00 49.57  ?  198 TYR A CA    1 
ATOM   1467 C C     . TYR A 1 198 ? 35.581 44.199  4.746  1.00 50.73  ?  198 TYR A C     1 
ATOM   1468 O O     . TYR A 1 198 ? 35.545 43.430  5.702  1.00 56.49  ?  198 TYR A O     1 
ATOM   1469 C CB    . TYR A 1 198 ? 37.039 42.616  3.526  1.00 41.43  ?  198 TYR A CB    1 
ATOM   1470 C CG    . TYR A 1 198 ? 38.232 42.259  2.679  1.00 43.25  ?  198 TYR A CG    1 
ATOM   1471 C CD1   . TYR A 1 198 ? 38.429 42.826  1.434  1.00 42.97  ?  198 TYR A CD1   1 
ATOM   1472 C CD2   . TYR A 1 198 ? 39.138 41.306  3.106  1.00 44.05  ?  198 TYR A CD2   1 
ATOM   1473 C CE1   . TYR A 1 198 ? 39.515 42.479  0.650  1.00 41.07  ?  198 TYR A CE1   1 
ATOM   1474 C CE2   . TYR A 1 198 ? 40.228 40.946  2.334  1.00 40.37  ?  198 TYR A CE2   1 
ATOM   1475 C CZ    . TYR A 1 198 ? 40.417 41.533  1.099  1.00 43.71  ?  198 TYR A CZ    1 
ATOM   1476 O OH    . TYR A 1 198 ? 41.486 41.184  0.329  1.00 47.40  ?  198 TYR A OH    1 
ATOM   1477 N N     . SER A 1 199 ? 34.596 45.045  4.458  1.00 45.14  ?  199 SER A N     1 
ATOM   1478 C CA    . SER A 1 199 ? 33.470 45.263  5.402  1.00 45.21  ?  199 SER A CA    1 
ATOM   1479 C C     . SER A 1 199 ? 32.480 44.100  5.470  1.00 46.37  ?  199 SER A C     1 
ATOM   1480 O O     . SER A 1 199 ? 31.828 43.817  4.457  1.00 45.37  ?  199 SER A O     1 
ATOM   1481 C CB    . SER A 1 199 ? 32.769 46.562  5.153  1.00 44.20  ?  199 SER A CB    1 
ATOM   1482 O OG    . SER A 1 199 ? 31.860 46.854  6.202  1.00 50.22  ?  199 SER A OG    1 
ATOM   1483 N N     . PHE A 1 200 ? 32.387 43.461  6.634  1.00 50.74  ?  200 PHE A N     1 
ATOM   1484 C CA    . PHE A 1 200 ? 31.394 42.391  6.887  1.00 53.56  ?  200 PHE A CA    1 
ATOM   1485 C C     . PHE A 1 200 ? 30.721 42.745  8.215  1.00 51.95  ?  200 PHE A C     1 
ATOM   1486 O O     . PHE A 1 200 ? 31.383 42.610  9.248  1.00 50.07  ?  200 PHE A O     1 
ATOM   1487 C CB    . PHE A 1 200 ? 32.080 41.030  6.989  1.00 48.74  ?  200 PHE A CB    1 
ATOM   1488 C CG    . PHE A 1 200 ? 32.653 40.493  5.705  1.00 50.15  ?  200 PHE A CG    1 
ATOM   1489 C CD1   . PHE A 1 200 ? 31.827 39.976  4.723  1.00 46.40  ?  200 PHE A CD1   1 
ATOM   1490 C CD2   . PHE A 1 200 ? 34.019 40.480  5.493  1.00 44.51  ?  200 PHE A CD2   1 
ATOM   1491 C CE1   . PHE A 1 200 ? 32.357 39.464  3.552  1.00 41.88  ?  200 PHE A CE1   1 
ATOM   1492 C CE2   . PHE A 1 200 ? 34.547 39.974  4.319  1.00 41.19  ?  200 PHE A CE2   1 
ATOM   1493 C CZ    . PHE A 1 200 ? 33.715 39.468  3.351  1.00 41.16  ?  200 PHE A CZ    1 
ATOM   1494 N N     . THR A 1 201 ? 29.482 43.239  8.180  1.00 48.82  ?  201 THR A N     1 
ATOM   1495 C CA    . THR A 1 201 ? 28.781 43.686  9.412  1.00 50.14  ?  201 THR A CA    1 
ATOM   1496 C C     . THR A 1 201 ? 27.316 43.255  9.375  1.00 49.56  ?  201 THR A C     1 
ATOM   1497 O O     . THR A 1 201 ? 26.740 43.062  10.448 1.00 48.62  ?  201 THR A O     1 
ATOM   1498 C CB    . THR A 1 201 ? 28.844 45.209  9.548  1.00 55.82  ?  201 THR A CB    1 
ATOM   1499 O OG1   . THR A 1 201 ? 29.730 45.726  8.555  1.00 58.82  ?  201 THR A OG1   1 
ATOM   1500 C CG2   . THR A 1 201 ? 29.293 45.660  10.920 1.00 57.15  ?  201 THR A CG2   1 
ATOM   1501 N N     . THR A 1 202 ? 26.753 43.091  8.181  1.00 52.97  ?  202 THR A N     1 
ATOM   1502 C CA    . THR A 1 202 ? 25.317 42.748  8.043  1.00 50.98  ?  202 THR A CA    1 
ATOM   1503 C C     . THR A 1 202 ? 25.097 41.271  8.345  1.00 52.89  ?  202 THR A C     1 
ATOM   1504 O O     . THR A 1 202 ? 26.048 40.505  8.246  1.00 49.93  ?  202 THR A O     1 
ATOM   1505 C CB    . THR A 1 202 ? 24.751 43.166  6.680  1.00 46.68  ?  202 THR A CB    1 
ATOM   1506 O OG1   . THR A 1 202 ? 24.990 42.143  5.716  1.00 47.48  ?  202 THR A OG1   1 
ATOM   1507 C CG2   . THR A 1 202 ? 25.294 44.489  6.193  1.00 46.29  ?  202 THR A CG2   1 
ATOM   1508 N N     . THR A 1 203 ? 23.872 40.913  8.715  1.00 54.56  ?  203 THR A N     1 
ATOM   1509 C CA    . THR A 1 203 ? 23.546 39.514  9.059  1.00 52.08  ?  203 THR A CA    1 
ATOM   1510 C C     . THR A 1 203 ? 23.709 38.681  7.794  1.00 49.73  ?  203 THR A C     1 
ATOM   1511 O O     . THR A 1 203 ? 23.938 37.469  7.913  1.00 54.47  ?  203 THR A O     1 
ATOM   1512 C CB    . THR A 1 203 ? 22.156 39.441  9.703  1.00 51.20  ?  203 THR A CB    1 
ATOM   1513 O OG1   . THR A 1 203 ? 21.245 40.150  8.866  1.00 54.57  ?  203 THR A OG1   1 
ATOM   1514 C CG2   . THR A 1 203 ? 22.118 40.024  11.097 1.00 39.82  ?  203 THR A CG2   1 
ATOM   1515 N N     . ALA A 1 204 ? 23.553 39.311  6.634  1.00 48.65  ?  204 ALA A N     1 
ATOM   1516 C CA    . ALA A 1 204 ? 23.757 38.604  5.379  1.00 45.90  ?  204 ALA A CA    1 
ATOM   1517 C C     . ALA A 1 204 ? 25.244 38.391  5.123  1.00 45.94  ?  204 ALA A C     1 
ATOM   1518 O O     . ALA A 1 204 ? 25.657 37.334  4.629  1.00 41.88  ?  204 ALA A O     1 
ATOM   1519 C CB    . ALA A 1 204 ? 23.100 39.382  4.246  1.00 43.94  ?  204 ALA A CB    1 
ATOM   1520 N N     . GLU A 1 205 ? 26.060 39.387  5.473  1.00 47.08  ?  205 GLU A N     1 
ATOM   1521 C CA    . GLU A 1 205 ? 27.503 39.233  5.395  1.00 44.62  ?  205 GLU A CA    1 
ATOM   1522 C C     . GLU A 1 205 ? 28.016 38.275  6.466  1.00 45.84  ?  205 GLU A C     1 
ATOM   1523 O O     . GLU A 1 205 ? 29.030 37.600  6.245  1.00 44.61  ?  205 GLU A O     1 
ATOM   1524 C CB    . GLU A 1 205 ? 28.186 40.604  5.503  1.00 44.68  ?  205 GLU A CB    1 
ATOM   1525 C CG    . GLU A 1 205 ? 27.976 41.489  4.277  1.00 49.33  ?  205 GLU A CG    1 
ATOM   1526 C CD    . GLU A 1 205 ? 28.191 42.987  4.541  1.00 55.40  ?  205 GLU A CD    1 
ATOM   1527 O OE1   . GLU A 1 205 ? 28.082 43.783  3.575  1.00 55.55  ?  205 GLU A OE1   1 
ATOM   1528 O OE2   . GLU A 1 205 ? 28.472 43.367  5.705  1.00 55.39  -1 205 GLU A OE2   1 
ATOM   1529 N N     . ARG A 1 206 ? 27.349 38.194  7.627  1.00 43.56  ?  206 ARG A N     1 
ATOM   1530 C CA    . ARG A 1 206 ? 27.749 37.191  8.610  1.00 39.77  ?  206 ARG A CA    1 
ATOM   1531 C C     . ARG A 1 206 ? 27.650 35.799  8.015  1.00 39.43  ?  206 ARG A C     1 
ATOM   1532 O O     . ARG A 1 206 ? 28.507 34.947  8.270  1.00 40.55  ?  206 ARG A O     1 
ATOM   1533 C CB    . ARG A 1 206 ? 26.900 37.296  9.883  1.00 43.08  ?  206 ARG A CB    1 
ATOM   1534 C CG    . ARG A 1 206 ? 27.241 36.240  10.954 1.00 38.39  ?  206 ARG A CG    1 
ATOM   1535 C CD    . ARG A 1 206 ? 26.647 36.561  12.343 1.00 43.08  ?  206 ARG A CD    1 
ATOM   1536 N NE    . ARG A 1 206 ? 27.160 35.688  13.414 1.00 47.53  ?  206 ARG A NE    1 
ATOM   1537 C CZ    . ARG A 1 206 ? 27.144 34.342  13.398 1.00 52.22  ?  206 ARG A CZ    1 
ATOM   1538 N NH1   . ARG A 1 206 ? 26.644 33.662  12.352 1.00 45.81  ?  206 ARG A NH1   1 
ATOM   1539 N NH2   . ARG A 1 206 ? 27.641 33.661  14.440 1.00 45.33  ?  206 ARG A NH2   1 
ATOM   1540 N N     . GLU A 1 207 ? 26.636 35.568  7.175  1.00 40.56  ?  207 GLU A N     1 
ATOM   1541 C CA    . GLU A 1 207 ? 26.443 34.265  6.548  1.00 41.43  ?  207 GLU A CA    1 
ATOM   1542 C C     . GLU A 1 207 ? 27.587 33.898  5.594  1.00 38.52  ?  207 GLU A C     1 
ATOM   1543 O O     . GLU A 1 207 ? 27.992 32.732  5.532  1.00 41.90  ?  207 GLU A O     1 
ATOM   1544 C CB    . GLU A 1 207 ? 25.098 34.247  5.819  1.00 45.36  ?  207 GLU A CB    1 
ATOM   1545 C CG    . GLU A 1 207 ? 24.295 32.963  5.995  1.00 52.11  ?  207 GLU A CG    1 
ATOM   1546 C CD    . GLU A 1 207 ? 24.279 32.456  7.444  1.00 62.99  ?  207 GLU A CD    1 
ATOM   1547 O OE1   . GLU A 1 207 ? 24.349 33.291  8.384  1.00 56.61  ?  207 GLU A OE1   1 
ATOM   1548 O OE2   . GLU A 1 207 ? 24.198 31.213  7.638  1.00 67.37  -1 207 GLU A OE2   1 
ATOM   1549 N N     . ILE A 1 208 ? 28.115 34.854  4.828  1.00 33.80  ?  208 ILE A N     1 
ATOM   1550 C CA    . ILE A 1 208 ? 29.226 34.508  3.946  1.00 36.25  ?  208 ILE A CA    1 
ATOM   1551 C C     . ILE A 1 208 ? 30.482 34.200  4.753  1.00 34.87  ?  208 ILE A C     1 
ATOM   1552 O O     . ILE A 1 208 ? 31.281 33.333  4.382  1.00 34.41  ?  208 ILE A O     1 
ATOM   1553 C CB    . ILE A 1 208 ? 29.491 35.624  2.927  1.00 35.54  ?  208 ILE A CB    1 
ATOM   1554 C CG1   . ILE A 1 208 ? 28.193 36.259  2.472  1.00 34.49  ?  208 ILE A CG1   1 
ATOM   1555 C CG2   . ILE A 1 208 ? 30.242 35.070  1.755  1.00 34.63  ?  208 ILE A CG2   1 
ATOM   1556 C CD1   . ILE A 1 208 ? 28.393 37.641  1.965  1.00 36.72  ?  208 ILE A CD1   1 
ATOM   1557 N N     . VAL A 1 209 ? 30.698 34.937  5.841  1.00 35.87  ?  209 VAL A N     1 
ATOM   1558 C CA    . VAL A 1 209 ? 31.886 34.761  6.661  1.00 34.20  ?  209 VAL A CA    1 
ATOM   1559 C C     . VAL A 1 209 ? 31.888 33.382  7.307  1.00 37.11  ?  209 VAL A C     1 
ATOM   1560 O O     . VAL A 1 209 ? 32.958 32.781  7.480  1.00 35.98  ?  209 VAL A O     1 
ATOM   1561 C CB    . VAL A 1 209 ? 31.972 35.901  7.700  1.00 38.28  ?  209 VAL A CB    1 
ATOM   1562 C CG1   . VAL A 1 209 ? 33.075 35.645  8.713  1.00 34.13  ?  209 VAL A CG1   1 
ATOM   1563 C CG2   . VAL A 1 209 ? 32.181 37.235  6.998  1.00 37.20  ?  209 VAL A CG2   1 
ATOM   1564 N N     . ARG A 1 210 ? 30.702 32.839  7.645  1.00 33.33  ?  210 ARG A N     1 
ATOM   1565 C CA    . ARG A 1 210 ? 30.628 31.443  8.080  1.00 34.94  ?  210 ARG A CA    1 
ATOM   1566 C C     . ARG A 1 210 ? 31.088 30.481  6.980  1.00 37.18  ?  210 ARG A C     1 
ATOM   1567 O O     . ARG A 1 210 ? 31.809 29.509  7.257  1.00 33.56  ?  210 ARG A O     1 
ATOM   1568 C CB    . ARG A 1 210 ? 29.214 31.086  8.524  1.00 41.02  ?  210 ARG A CB    1 
ATOM   1569 C CG    . ARG A 1 210 ? 29.104 29.688  9.160  1.00 36.23  ?  210 ARG A CG    1 
ATOM   1570 C CD    . ARG A 1 210 ? 27.662 29.307  9.464  1.00 42.75  ?  210 ARG A CD    1 
ATOM   1571 N NE    . ARG A 1 210 ? 26.758 29.603  8.352  1.00 49.98  ?  210 ARG A NE    1 
ATOM   1572 C CZ    . ARG A 1 210 ? 26.435 28.735  7.389  1.00 59.02  ?  210 ARG A CZ    1 
ATOM   1573 N NH1   . ARG A 1 210 ? 26.938 27.497  7.410  1.00 55.65  ?  210 ARG A NH1   1 
ATOM   1574 N NH2   . ARG A 1 210 ? 25.599 29.101  6.406  1.00 56.17  ?  210 ARG A NH2   1 
ATOM   1575 N N     . ASP A 1 211 ? 30.687 30.732  5.725  1.00 34.12  ?  211 ASP A N     1 
ATOM   1576 C CA    . ASP A 1 211 ? 31.205 29.943  4.608  1.00 31.14  ?  211 ASP A CA    1 
ATOM   1577 C C     . ASP A 1 211 ? 32.716 30.078  4.483  1.00 36.08  ?  211 ASP A C     1 
ATOM   1578 O O     . ASP A 1 211 ? 33.426 29.082  4.289  1.00 32.93  ?  211 ASP A O     1 
ATOM   1579 C CB    . ASP A 1 211 ? 30.549 30.358  3.301  1.00 30.91  ?  211 ASP A CB    1 
ATOM   1580 C CG    . ASP A 1 211 ? 30.829 29.381  2.186  1.00 37.30  ?  211 ASP A CG    1 
ATOM   1581 O OD1   . ASP A 1 211 ? 31.634 29.668  1.271  1.00 39.96  ?  211 ASP A OD1   1 
ATOM   1582 O OD2   . ASP A 1 211 ? 30.228 28.299  2.214  1.00 48.27  -1 211 ASP A OD2   1 
ATOM   1583 N N     . ILE A 1 212 ? 33.232 31.314  4.544  1.00 36.41  ?  212 ILE A N     1 
ATOM   1584 C CA    . ILE A 1 212 ? 34.678 31.490  4.465  1.00 36.59  ?  212 ILE A CA    1 
ATOM   1585 C C     . ILE A 1 212 ? 35.354 30.715  5.589  1.00 33.89  ?  212 ILE A C     1 
ATOM   1586 O O     . ILE A 1 212 ? 36.404 30.102  5.386  1.00 30.45  ?  212 ILE A O     1 
ATOM   1587 C CB    . ILE A 1 212 ? 35.060 32.984  4.487  1.00 37.52  ?  212 ILE A CB    1 
ATOM   1588 C CG1   . ILE A 1 212 ? 34.447 33.725  3.303  1.00 34.09  ?  212 ILE A CG1   1 
ATOM   1589 C CG2   . ILE A 1 212 ? 36.571 33.156  4.441  1.00 28.23  ?  212 ILE A CG2   1 
ATOM   1590 C CD1   . ILE A 1 212 ? 34.823 35.198  3.283  1.00 30.07  ?  212 ILE A CD1   1 
ATOM   1591 N N     . LYS A 1 213 ? 34.740 30.693  6.780  1.00 36.03  ?  213 LYS A N     1 
ATOM   1592 C CA    . LYS A 1 213 ? 35.342 29.984  7.910  1.00 35.04  ?  213 LYS A CA    1 
ATOM   1593 C C     . LYS A 1 213 ? 35.406 28.473  7.663  1.00 31.74  ?  213 LYS A C     1 
ATOM   1594 O O     . LYS A 1 213 ? 36.455 27.855  7.840  1.00 34.03  ?  213 LYS A O     1 
ATOM   1595 C CB    . LYS A 1 213 ? 34.587 30.285  9.207  1.00 31.51  ?  213 LYS A CB    1 
ATOM   1596 C CG    . LYS A 1 213 ? 35.109 29.454  10.401 1.00 33.16  ?  213 LYS A CG    1 
ATOM   1597 C CD    . LYS A 1 213 ? 34.512 29.853  11.743 1.00 27.48  ?  213 LYS A CD    1 
ATOM   1598 C CE    . LYS A 1 213 ? 32.993 29.821  11.694 1.00 29.49  ?  213 LYS A CE    1 
ATOM   1599 N NZ    . LYS A 1 213 ? 32.338 28.566  12.102 1.00 27.21  ?  213 LYS A NZ    1 
ATOM   1600 N N     . GLU A 1 214 ? 34.304 27.860  7.256  1.00 30.29  ?  214 GLU A N     1 
ATOM   1601 C CA    . GLU A 1 214 ? 34.305 26.413  7.113  1.00 32.24  ?  214 GLU A CA    1 
ATOM   1602 C C     . GLU A 1 214 ? 35.008 25.924  5.850  1.00 31.64  ?  214 GLU A C     1 
ATOM   1603 O O     . GLU A 1 214 ? 35.156 24.710  5.669  1.00 34.98  ?  214 GLU A O     1 
ATOM   1604 C CB    . GLU A 1 214 ? 32.861 25.884  7.129  1.00 36.08  ?  214 GLU A CB    1 
ATOM   1605 C CG    . GLU A 1 214 ? 31.959 26.545  8.149  1.00 36.92  ?  214 GLU A CG    1 
ATOM   1606 C CD    . GLU A 1 214 ? 30.481 26.158  8.008  1.00 45.05  ?  214 GLU A CD    1 
ATOM   1607 O OE1   . GLU A 1 214 ? 29.683 26.557  8.889  1.00 49.64  ?  214 GLU A OE1   1 
ATOM   1608 O OE2   . GLU A 1 214 ? 30.098 25.466  7.036  1.00 45.62  -1 214 GLU A OE2   1 
ATOM   1609 N N     . LYS A 1 215 ? 35.411 26.816  4.952  1.00 32.81  ?  215 LYS A N     1 
ATOM   1610 C CA    . LYS A 1 215 ? 36.061 26.400  3.715  1.00 29.89  ?  215 LYS A CA    1 
ATOM   1611 C C     . LYS A 1 215 ? 37.555 26.695  3.683  1.00 30.02  ?  215 LYS A C     1 
ATOM   1612 O O     . LYS A 1 215 ? 38.300 25.975  3.010  1.00 28.08  ?  215 LYS A O     1 
ATOM   1613 C CB    . LYS A 1 215 ? 35.399 27.076  2.503  1.00 32.83  ?  215 LYS A CB    1 
ATOM   1614 C CG    . LYS A 1 215 ? 34.270 26.284  1.822  1.00 36.60  ?  215 LYS A CG    1 
ATOM   1615 C CD    . LYS A 1 215 ? 33.147 27.203  1.278  1.00 37.41  ?  215 LYS A CD    1 
ATOM   1616 C CE    . LYS A 1 215 ? 31.981 26.396  0.697  1.00 42.69  ?  215 LYS A CE    1 
ATOM   1617 N NZ    . LYS A 1 215 ? 31.935 24.975  1.224  1.00 47.03  ?  215 LYS A NZ    1 
ATOM   1618 N N     . LEU A 1 216 ? 38.015 27.720  4.399  1.00 27.06  ?  216 LEU A N     1 
ATOM   1619 C CA    . LEU A 1 216 ? 39.402 28.139  4.315  1.00 28.45  ?  216 LEU A CA    1 
ATOM   1620 C C     . LEU A 1 216 ? 40.160 28.172  5.641  1.00 30.34  ?  216 LEU A C     1 
ATOM   1621 O O     . LEU A 1 216 ? 41.390 28.265  5.610  1.00 33.13  ?  216 LEU A O     1 
ATOM   1622 C CB    . LEU A 1 216 ? 39.503 29.529  3.670  1.00 26.51  ?  216 LEU A CB    1 
ATOM   1623 C CG    . LEU A 1 216 ? 39.378 29.730  2.166  1.00 29.41  ?  216 LEU A CG    1 
ATOM   1624 C CD1   . LEU A 1 216 ? 38.355 28.835  1.541  1.00 25.79  ?  216 LEU A CD1   1 
ATOM   1625 C CD2   . LEU A 1 216 ? 39.027 31.173  1.931  1.00 30.93  ?  216 LEU A CD2   1 
ATOM   1626 N N     . CYS A 1 217 ? 39.500 28.109  6.795  1.00 28.17  ?  217 CYS A N     1 
ATOM   1627 C CA    . CYS A 1 217 ? 40.271 28.259  8.022  1.00 26.48  ?  217 CYS A CA    1 
ATOM   1628 C C     . CYS A 1 217 ? 40.885 26.925  8.457  1.00 30.32  ?  217 CYS A C     1 
ATOM   1629 O O     . CYS A 1 217 ? 40.415 25.849  8.064  1.00 33.27  ?  217 CYS A O     1 
ATOM   1630 C CB    . CYS A 1 217 ? 39.382 28.833  9.115  1.00 31.35  ?  217 CYS A CB    1 
ATOM   1631 S SG    . CYS A 1 217 ? 39.063 30.613  8.911  1.00 34.93  ?  217 CYS A SG    1 
ATOM   1632 N N     . TYR A 1 218 ? 41.949 27.003  9.271  1.00 26.63  ?  218 TYR A N     1 
ATOM   1633 C CA    . TYR A 1 218 ? 42.670 25.826  9.777  1.00 28.16  ?  218 TYR A CA    1 
ATOM   1634 C C     . TYR A 1 218 ? 43.458 26.157  11.049 1.00 29.38  ?  218 TYR A C     1 
ATOM   1635 O O     . TYR A 1 218 ? 43.736 27.320  11.342 1.00 29.51  ?  218 TYR A O     1 
ATOM   1636 C CB    . TYR A 1 218 ? 43.633 25.281  8.732  1.00 26.07  ?  218 TYR A CB    1 
ATOM   1637 C CG    . TYR A 1 218 ? 44.800 26.201  8.441  1.00 26.23  ?  218 TYR A CG    1 
ATOM   1638 C CD1   . TYR A 1 218 ? 44.640 27.358  7.673  1.00 26.67  ?  218 TYR A CD1   1 
ATOM   1639 C CD2   . TYR A 1 218 ? 46.064 25.905  8.920  1.00 25.08  ?  218 TYR A CD2   1 
ATOM   1640 C CE1   . TYR A 1 218 ? 45.715 28.191  7.395  1.00 26.34  ?  218 TYR A CE1   1 
ATOM   1641 C CE2   . TYR A 1 218 ? 47.145 26.711  8.644  1.00 29.35  ?  218 TYR A CE2   1 
ATOM   1642 C CZ    . TYR A 1 218 ? 46.978 27.859  7.878  1.00 32.02  ?  218 TYR A CZ    1 
ATOM   1643 O OH    . TYR A 1 218 ? 48.087 28.658  7.619  1.00 30.59  ?  218 TYR A OH    1 
ATOM   1644 N N     . VAL A 1 219 ? 43.860 25.118  11.789 1.00 27.88  ?  219 VAL A N     1 
ATOM   1645 C CA    . VAL A 1 219 ? 44.648 25.329  13.004 1.00 32.23  ?  219 VAL A CA    1 
ATOM   1646 C C     . VAL A 1 219 ? 46.137 25.317  12.660 1.00 34.27  ?  219 VAL A C     1 
ATOM   1647 O O     . VAL A 1 219 ? 46.650 24.362  12.052 1.00 35.08  ?  219 VAL A O     1 
ATOM   1648 C CB    . VAL A 1 219 ? 44.311 24.292  14.100 1.00 29.49  ?  219 VAL A CB    1 
ATOM   1649 C CG1   . VAL A 1 219 ? 45.147 24.541  15.340 1.00 26.70  ?  219 VAL A CG1   1 
ATOM   1650 C CG2   . VAL A 1 219 ? 42.838 24.377  14.514 1.00 28.98  ?  219 VAL A CG2   1 
ATOM   1651 N N     . ALA A 1 220 ? 46.821 26.404  13.026 1.00 31.78  ?  220 ALA A N     1 
ATOM   1652 C CA    . ALA A 1 220 ? 48.280 26.450  13.033 1.00 34.39  ?  220 ALA A CA    1 
ATOM   1653 C C     . ALA A 1 220 ? 48.863 25.396  13.970 1.00 34.98  ?  220 ALA A C     1 
ATOM   1654 O O     . ALA A 1 220 ? 48.365 25.213  15.084 1.00 31.89  ?  220 ALA A O     1 
ATOM   1655 C CB    . ALA A 1 220 ? 48.742 27.833  13.502 1.00 31.77  ?  220 ALA A CB    1 
ATOM   1656 N N     . LEU A 1 221 ? 49.971 24.752  13.556 1.00 33.57  ?  221 LEU A N     1 
ATOM   1657 C CA    . LEU A 1 221 ? 50.622 23.797  14.462 1.00 31.38  ?  221 LEU A CA    1 
ATOM   1658 C C     . LEU A 1 221 ? 51.354 24.512  15.602 1.00 31.68  ?  221 LEU A C     1 
ATOM   1659 O O     . LEU A 1 221 ? 51.154 24.166  16.768 1.00 32.29  ?  221 LEU A O     1 
ATOM   1660 C CB    . LEU A 1 221 ? 51.585 22.862  13.724 1.00 29.93  ?  221 LEU A CB    1 
ATOM   1661 C CG    . LEU A 1 221 ? 52.144 21.779  14.682 1.00 25.12  ?  221 LEU A CG    1 
ATOM   1662 C CD1   . LEU A 1 221 ? 51.070 21.037  15.477 1.00 25.12  ?  221 LEU A CD1   1 
ATOM   1663 C CD2   . LEU A 1 221 ? 52.989 20.790  13.966 1.00 23.49  ?  221 LEU A CD2   1 
ATOM   1664 N N     . ASP A 1 222 ? 52.250 25.470  15.295 1.00 34.65  ?  222 ASP A N     1 
ATOM   1665 C CA    . ASP A 1 222 ? 52.520 26.575  16.210 1.00 41.76  ?  222 ASP A CA    1 
ATOM   1666 C C     . ASP A 1 222 ? 52.069 27.906  15.609 1.00 39.53  ?  222 ASP A C     1 
ATOM   1667 O O     . ASP A 1 222 ? 52.437 28.238  14.476 1.00 36.98  ?  222 ASP A O     1 
ATOM   1668 C CB    . ASP A 1 222 ? 53.964 26.679  16.612 1.00 37.50  ?  222 ASP A CB    1 
ATOM   1669 C CG    . ASP A 1 222 ? 54.171 27.868  17.433 1.00 49.06  ?  222 ASP A CG    1 
ATOM   1670 O OD1   . ASP A 1 222 ? 53.484 28.114  18.494 1.00 54.27  ?  222 ASP A OD1   1 
ATOM   1671 O OD2   . ASP A 1 222 ? 55.054 28.580  16.983 1.00 46.67  -1 222 ASP A OD2   1 
ATOM   1672 N N     . PHE A 1 223 ? 51.345 28.690  16.419 1.00 35.70  ?  223 PHE A N     1 
ATOM   1673 C CA    . PHE A 1 223 ? 50.843 29.978  15.982 1.00 35.83  ?  223 PHE A CA    1 
ATOM   1674 C C     . PHE A 1 223 ? 51.963 30.851  15.432 1.00 37.77  ?  223 PHE A C     1 
ATOM   1675 O O     . PHE A 1 223 ? 51.854 31.407  14.330 1.00 37.00  ?  223 PHE A O     1 
ATOM   1676 C CB    . PHE A 1 223 ? 50.144 30.650  17.151 1.00 29.06  ?  223 PHE A CB    1 
ATOM   1677 C CG    . PHE A 1 223 ? 49.389 31.872  16.768 1.00 31.44  ?  223 PHE A CG    1 
ATOM   1678 C CD1   . PHE A 1 223 ? 48.360 31.802  15.835 1.00 32.71  ?  223 PHE A CD1   1 
ATOM   1679 C CD2   . PHE A 1 223 ? 49.700 33.102  17.331 1.00 30.95  ?  223 PHE A CD2   1 
ATOM   1680 C CE1   . PHE A 1 223 ? 47.658 32.920  15.479 1.00 32.45  ?  223 PHE A CE1   1 
ATOM   1681 C CE2   . PHE A 1 223 ? 49.007 34.223  16.978 1.00 32.03  ?  223 PHE A CE2   1 
ATOM   1682 C CZ    . PHE A 1 223 ? 47.978 34.134  16.049 1.00 33.88  ?  223 PHE A CZ    1 
ATOM   1683 N N     . GLU A 1 224 ? 53.049 30.992  16.193 1.00 36.05  ?  224 GLU A N     1 
ATOM   1684 C CA    . GLU A 1 224 ? 54.089 31.928  15.793 1.00 37.04  ?  224 GLU A CA    1 
ATOM   1685 C C     . GLU A 1 224 ? 54.693 31.592  14.425 1.00 37.42  ?  224 GLU A C     1 
ATOM   1686 O O     . GLU A 1 224 ? 54.745 32.470  13.569 1.00 37.68  ?  224 GLU A O     1 
ATOM   1687 C CB    . GLU A 1 224 ? 55.136 32.062  16.895 1.00 40.15  ?  224 GLU A CB    1 
ATOM   1688 C CG    . GLU A 1 224 ? 54.662 33.038  17.970 1.00 37.46  ?  224 GLU A CG    1 
ATOM   1689 C CD    . GLU A 1 224 ? 55.692 33.329  19.041 1.00 44.37  ?  224 GLU A CD    1 
ATOM   1690 O OE1   . GLU A 1 224 ? 56.901 33.062  18.833 1.00 42.20  ?  224 GLU A OE1   1 
ATOM   1691 O OE2   . GLU A 1 224 ? 55.271 33.835  20.111 1.00 51.03  -1 224 GLU A OE2   1 
ATOM   1692 N N     . GLN A 1 225 ? 55.144 30.361  14.148 1.00 38.14  ?  225 GLN A N     1 
ATOM   1693 C CA    . GLN A 1 225 ? 55.769 30.243  12.817 1.00 47.86  ?  225 GLN A CA    1 
ATOM   1694 C C     . GLN A 1 225 ? 54.770 30.484  11.716 1.00 42.01  ?  225 GLN A C     1 
ATOM   1695 O O     . GLN A 1 225 ? 55.148 30.847  10.593 1.00 40.71  ?  225 GLN A O     1 
ATOM   1696 C CB    . GLN A 1 225 ? 56.375 28.885  12.503 1.00 51.69  ?  225 GLN A CB    1 
ATOM   1697 C CG    . GLN A 1 225 ? 57.507 28.477  13.327 1.00 59.30  ?  225 GLN A CG    1 
ATOM   1698 C CD    . GLN A 1 225 ? 57.118 28.007  14.647 1.00 62.14  ?  225 GLN A CD    1 
ATOM   1699 O OE1   . GLN A 1 225 ? 56.405 26.966  14.795 1.00 68.19  ?  225 GLN A OE1   1 
ATOM   1700 N NE2   . GLN A 1 225 ? 57.661 28.686  15.687 1.00 60.98  ?  225 GLN A NE2   1 
ATOM   1701 N N     . GLU A 1 226 ? 53.510 30.150  11.968 1.00 37.70  ?  226 GLU A N     1 
ATOM   1702 C CA    . GLU A 1 226 ? 52.534 30.421  10.937 1.00 34.87  ?  226 GLU A CA    1 
ATOM   1703 C C     . GLU A 1 226 ? 52.425 31.921  10.717 1.00 37.49  ?  226 GLU A C     1 
ATOM   1704 O O     . GLU A 1 226 ? 52.492 32.380  9.576  1.00 40.71  ?  226 GLU A O     1 
ATOM   1705 C CB    . GLU A 1 226 ? 51.188 29.784  11.272 1.00 36.11  ?  226 GLU A CB    1 
ATOM   1706 C CG    . GLU A 1 226 ? 50.424 29.211  10.047 1.00 35.34  ?  226 GLU A CG    1 
ATOM   1707 C CD    . GLU A 1 226 ? 50.925 27.836  9.562  1.00 42.23  ?  226 GLU A CD    1 
ATOM   1708 O OE1   . GLU A 1 226 ? 50.472 27.375  8.476  1.00 36.02  ?  226 GLU A OE1   1 
ATOM   1709 O OE2   . GLU A 1 226 ? 51.760 27.211  10.270 1.00 46.06  -1 226 GLU A OE2   1 
ATOM   1710 N N     . MET A 1 227 ? 52.303 32.715  11.791 1.00 36.63  ?  227 MET A N     1 
ATOM   1711 C CA    . MET A 1 227 ? 52.359 34.164  11.600 1.00 37.70  ?  227 MET A CA    1 
ATOM   1712 C C     . MET A 1 227 ? 53.631 34.559  10.861 1.00 34.96  ?  227 MET A C     1 
ATOM   1713 O O     . MET A 1 227 ? 53.578 35.335  9.905  1.00 32.60  ?  227 MET A O     1 
ATOM   1714 C CB    . MET A 1 227 ? 52.234 34.918  12.929 1.00 33.00  ?  227 MET A CB    1 
ATOM   1715 C CG    . MET A 1 227 ? 50.874 34.726  13.582 1.00 36.41  ?  227 MET A CG    1 
ATOM   1716 S SD    . MET A 1 227 ? 49.530 35.785  13.065 1.00 39.12  ?  227 MET A SD    1 
ATOM   1717 C CE    . MET A 1 227 ? 50.432 37.287  12.738 1.00 37.37  ?  227 MET A CE    1 
ATOM   1718 N N     . ALA A 1 228 ? 54.779 33.991  11.248 1.00 32.33  ?  228 ALA A N     1 
ATOM   1719 C CA    . ALA A 1 228 ? 56.023 34.349  10.573 1.00 34.86  ?  228 ALA A CA    1 
ATOM   1720 C C     . ALA A 1 228 ? 55.958 34.030  9.079  1.00 39.75  ?  228 ALA A C     1 
ATOM   1721 O O     . ALA A 1 228 ? 56.381 34.844  8.243  1.00 41.09  ?  228 ALA A O     1 
ATOM   1722 C CB    . ALA A 1 228 ? 57.208 33.648  11.232 1.00 33.01  ?  228 ALA A CB    1 
ATOM   1723 N N     . THR A 1 229 ? 55.397 32.862  8.728  1.00 37.74  ?  229 THR A N     1 
ATOM   1724 C CA    . THR A 1 229 ? 55.237 32.451  7.331  1.00 35.89  ?  229 THR A CA    1 
ATOM   1725 C C     . THR A 1 229 ? 54.253 33.337  6.579  1.00 40.27  ?  229 THR A C     1 
ATOM   1726 O O     . THR A 1 229 ? 54.473 33.658  5.405  1.00 41.08  ?  229 THR A O     1 
ATOM   1727 C CB    . THR A 1 229 ? 54.764 31.006  7.273  1.00 35.67  ?  229 THR A CB    1 
ATOM   1728 O OG1   . THR A 1 229 ? 55.817 30.153  7.718  1.00 41.95  ?  229 THR A OG1   1 
ATOM   1729 C CG2   . THR A 1 229 ? 54.366 30.626  5.877  1.00 33.74  ?  229 THR A CG2   1 
ATOM   1730 N N     . ALA A 1 230 ? 53.137 33.696  7.217  1.00 39.88  ?  230 ALA A N     1 
ATOM   1731 C CA    . ALA A 1 230 ? 52.235 34.684  6.640  1.00 37.33  ?  230 ALA A CA    1 
ATOM   1732 C C     . ALA A 1 230 ? 52.954 36.012  6.393  1.00 41.04  ?  230 ALA A C     1 
ATOM   1733 O O     . ALA A 1 230 ? 52.787 36.637  5.339  1.00 41.43  ?  230 ALA A O     1 
ATOM   1734 C CB    . ALA A 1 230 ? 51.024 34.873  7.554  1.00 35.47  ?  230 ALA A CB    1 
ATOM   1735 N N     . ALA A 1 231 ? 53.782 36.448  7.342  1.00 44.74  ?  231 ALA A N     1 
ATOM   1736 C CA    . ALA A 1 231 ? 54.445 37.743  7.229  1.00 42.06  ?  231 ALA A CA    1 
ATOM   1737 C C     . ALA A 1 231 ? 55.566 37.748  6.195  1.00 47.84  ?  231 ALA A C     1 
ATOM   1738 O O     . ALA A 1 231 ? 56.081 38.827  5.879  1.00 45.09  ?  231 ALA A O     1 
ATOM   1739 C CB    . ALA A 1 231 ? 54.995 38.166  8.597  1.00 32.86  ?  231 ALA A CB    1 
ATOM   1740 N N     . SER A 1 232 ? 55.935 36.578  5.642  1.00 49.65  ?  232 SER A N     1 
ATOM   1741 C CA    . SER A 1 232 ? 57.152 36.425  4.851  1.00 46.62  ?  232 SER A CA    1 
ATOM   1742 C C     . SER A 1 232 ? 56.966 35.625  3.548  1.00 48.13  ?  232 SER A C     1 
ATOM   1743 O O     . SER A 1 232 ? 57.962 35.251  2.909  1.00 46.92  ?  232 SER A O     1 
ATOM   1744 C CB    . SER A 1 232 ? 58.229 35.811  5.754  1.00 41.24  ?  232 SER A CB    1 
ATOM   1745 O OG    . SER A 1 232 ? 58.197 34.397  5.700  1.00 49.92  ?  232 SER A OG    1 
ATOM   1746 N N     . SER A 1 233 ? 55.728 35.388  3.111  1.00 49.13  ?  233 SER A N     1 
ATOM   1747 C CA    . SER A 1 233 ? 55.473 34.802  1.797  1.00 48.10  ?  233 SER A CA    1 
ATOM   1748 C C     . SER A 1 233 ? 53.964 34.724  1.562  1.00 50.24  ?  233 SER A C     1 
ATOM   1749 O O     . SER A 1 233 ? 53.155 34.817  2.493  1.00 46.74  ?  233 SER A O     1 
ATOM   1750 C CB    . SER A 1 233 ? 56.117 33.418  1.647  1.00 49.22  ?  233 SER A CB    1 
ATOM   1751 O OG    . SER A 1 233 ? 55.201 32.381  1.962  1.00 46.87  ?  233 SER A OG    1 
ATOM   1752 N N     . SER A 1 234 ? 53.605 34.564  0.291  1.00 52.29  ?  234 SER A N     1 
ATOM   1753 C CA    . SER A 1 234 ? 52.231 34.508  -0.174 1.00 45.32  ?  234 SER A CA    1 
ATOM   1754 C C     . SER A 1 234 ? 51.619 33.129  -0.035 1.00 49.49  ?  234 SER A C     1 
ATOM   1755 O O     . SER A 1 234 ? 50.462 32.941  -0.425 1.00 50.36  ?  234 SER A O     1 
ATOM   1756 C CB    . SER A 1 234 ? 52.180 34.916  -1.643 1.00 53.82  ?  234 SER A CB    1 
ATOM   1757 O OG    . SER A 1 234 ? 51.902 36.295  -1.799 1.00 65.03  ?  234 SER A OG    1 
ATOM   1758 N N     . SER A 1 235 ? 52.369 32.156  0.484  1.00 51.78  ?  235 SER A N     1 
ATOM   1759 C CA    . SER A 1 235 ? 51.964 30.762  0.346  1.00 51.98  ?  235 SER A CA    1 
ATOM   1760 C C     . SER A 1 235 ? 50.668 30.456  1.089  1.00 53.77  ?  235 SER A C     1 
ATOM   1761 O O     . SER A 1 235 ? 49.919 29.561  0.678  1.00 51.24  ?  235 SER A O     1 
ATOM   1762 C CB    . SER A 1 235 ? 53.090 29.847  0.819  1.00 49.73  ?  235 SER A CB    1 
ATOM   1763 O OG    . SER A 1 235 ? 53.723 30.384  1.963  1.00 47.76  ?  235 SER A OG    1 
ATOM   1764 N N     . LEU A 1 236 ? 50.365 31.188  2.161  1.00 51.01  ?  236 LEU A N     1 
ATOM   1765 C CA    . LEU A 1 236 ? 49.163 30.871  2.924  1.00 47.67  ?  236 LEU A CA    1 
ATOM   1766 C C     . LEU A 1 236 ? 47.897 31.540  2.391  1.00 47.24  ?  236 LEU A C     1 
ATOM   1767 O O     . LEU A 1 236 ? 46.792 31.105  2.740  1.00 45.20  ?  236 LEU A O     1 
ATOM   1768 C CB    . LEU A 1 236 ? 49.364 31.240  4.394  1.00 47.99  ?  236 LEU A CB    1 
ATOM   1769 C CG    . LEU A 1 236 ? 50.498 30.426  5.008  1.00 43.91  ?  236 LEU A CG    1 
ATOM   1770 C CD1   . LEU A 1 236 ? 50.587 30.619  6.503  1.00 38.67  ?  236 LEU A CD1   1 
ATOM   1771 C CD2   . LEU A 1 236 ? 50.298 28.969  4.635  1.00 44.15  ?  236 LEU A CD2   1 
ATOM   1772 N N     . GLU A 1 237 ? 48.012 32.563  1.546  1.00 51.85  ?  237 GLU A N     1 
ATOM   1773 C CA    . GLU A 1 237 ? 46.824 33.283  1.095  1.00 45.31  ?  237 GLU A CA    1 
ATOM   1774 C C     . GLU A 1 237 ? 45.992 32.419  0.149  1.00 45.82  ?  237 GLU A C     1 
ATOM   1775 O O     . GLU A 1 237 ? 46.505 31.536  -0.552 1.00 47.40  ?  237 GLU A O     1 
ATOM   1776 C CB    . GLU A 1 237 ? 47.220 34.603  0.441  1.00 36.45  ?  237 GLU A CB    1 
ATOM   1777 C CG    . GLU A 1 237 ? 48.412 35.229  1.129  1.00 43.30  ?  237 GLU A CG    1 
ATOM   1778 C CD    . GLU A 1 237 ? 48.635 36.691  0.808  1.00 54.51  ?  237 GLU A CD    1 
ATOM   1779 O OE1   . GLU A 1 237 ? 48.843 37.492  1.761  1.00 61.33  ?  237 GLU A OE1   1 
ATOM   1780 O OE2   . GLU A 1 237 ? 48.636 37.041  -0.395 1.00 64.78  -1 237 GLU A OE2   1 
ATOM   1781 N N     . LYS A 1 238 ? 44.680 32.653  0.184  1.00 42.80  ?  238 LYS A N     1 
ATOM   1782 C CA    . LYS A 1 238 ? 43.688 31.910  -0.578 1.00 38.79  ?  238 LYS A CA    1 
ATOM   1783 C C     . LYS A 1 238 ? 42.637 32.903  -1.028 1.00 41.60  ?  238 LYS A C     1 
ATOM   1784 O O     . LYS A 1 238 ? 42.226 33.775  -0.255 1.00 41.08  ?  238 LYS A O     1 
ATOM   1785 C CB    . LYS A 1 238 ? 43.029 30.797  0.248  1.00 34.82  ?  238 LYS A CB    1 
ATOM   1786 C CG    . LYS A 1 238 ? 43.921 29.597  0.489  1.00 38.97  ?  238 LYS A CG    1 
ATOM   1787 C CD    . LYS A 1 238 ? 43.703 28.527  -0.560 1.00 40.70  ?  238 LYS A CD    1 
ATOM   1788 C CE    . LYS A 1 238 ? 43.755 27.125  0.033  1.00 44.21  ?  238 LYS A CE    1 
ATOM   1789 N NZ    . LYS A 1 238 ? 45.157 26.621  0.247  1.00 49.97  ?  238 LYS A NZ    1 
ATOM   1790 N N     . SER A 1 239 ? 42.221 32.793  -2.280 1.00 41.53  ?  239 SER A N     1 
ATOM   1791 C CA    . SER A 1 239 ? 41.223 33.700  -2.804 1.00 38.73  ?  239 SER A CA    1 
ATOM   1792 C C     . SER A 1 239 ? 39.845 33.129  -2.506 1.00 38.34  ?  239 SER A C     1 
ATOM   1793 O O     . SER A 1 239 ? 39.656 31.913  -2.451 1.00 37.39  ?  239 SER A O     1 
ATOM   1794 C CB    . SER A 1 239 ? 41.432 33.937  -4.300 1.00 45.57  ?  239 SER A CB    1 
ATOM   1795 O OG    . SER A 1 239 ? 41.835 32.752  -4.977 1.00 49.02  ?  239 SER A OG    1 
ATOM   1796 N N     . TYR A 1 240 ? 38.901 34.016  -2.234 1.00 38.22  ?  240 TYR A N     1 
ATOM   1797 C CA    . TYR A 1 240 ? 37.528 33.631  -1.977 1.00 36.72  ?  240 TYR A CA    1 
ATOM   1798 C C     . TYR A 1 240 ? 36.644 34.554  -2.780 1.00 41.85  ?  240 TYR A C     1 
ATOM   1799 O O     . TYR A 1 240 ? 36.867 35.771  -2.812 1.00 41.53  ?  240 TYR A O     1 
ATOM   1800 C CB    . TYR A 1 240 ? 37.158 33.696  -0.489 1.00 39.79  ?  240 TYR A CB    1 
ATOM   1801 C CG    . TYR A 1 240 ? 35.736 33.238  -0.188 1.00 39.19  ?  240 TYR A CG    1 
ATOM   1802 C CD1   . TYR A 1 240 ? 34.710 34.158  -0.087 1.00 38.74  ?  240 TYR A CD1   1 
ATOM   1803 C CD2   . TYR A 1 240 ? 35.422 31.886  -0.012 1.00 36.96  ?  240 TYR A CD2   1 
ATOM   1804 C CE1   . TYR A 1 240 ? 33.419 33.768  0.175  1.00 38.60  ?  240 TYR A CE1   1 
ATOM   1805 C CE2   . TYR A 1 240 ? 34.125 31.492  0.257  1.00 37.93  ?  240 TYR A CE2   1 
ATOM   1806 C CZ    . TYR A 1 240 ? 33.127 32.449  0.345  1.00 38.58  ?  240 TYR A CZ    1 
ATOM   1807 O OH    . TYR A 1 240 ? 31.820 32.114  0.610  1.00 38.70  ?  240 TYR A OH    1 
ATOM   1808 N N     . GLU A 1 241 ? 35.657 33.955  -3.433 1.00 46.17  ?  241 GLU A N     1 
ATOM   1809 C CA    . GLU A 1 241 ? 34.752 34.632  -4.345 1.00 50.33  ?  241 GLU A CA    1 
ATOM   1810 C C     . GLU A 1 241 ? 33.421 34.846  -3.641 1.00 52.76  ?  241 GLU A C     1 
ATOM   1811 O O     . GLU A 1 241 ? 32.804 33.879  -3.169 1.00 53.63  ?  241 GLU A O     1 
ATOM   1812 C CB    . GLU A 1 241 ? 34.570 33.796  -5.609 1.00 52.72  ?  241 GLU A CB    1 
ATOM   1813 C CG    . GLU A 1 241 ? 34.075 34.575  -6.799 1.00 58.80  ?  241 GLU A CG    1 
ATOM   1814 C CD    . GLU A 1 241 ? 33.153 33.742  -7.661 1.00 71.75  ?  241 GLU A CD    1 
ATOM   1815 O OE1   . GLU A 1 241 ? 33.624 33.142  -8.663 1.00 77.10  ?  241 GLU A OE1   1 
ATOM   1816 O OE2   . GLU A 1 241 ? 31.950 33.671  -7.314 1.00 78.88  -1 241 GLU A OE2   1 
ATOM   1817 N N     . LEU A 1 242 ? 32.988 36.102  -3.571 1.00 49.17  ?  242 LEU A N     1 
ATOM   1818 C CA    . LEU A 1 242 ? 31.729 36.468  -2.934 1.00 46.85  ?  242 LEU A CA    1 
ATOM   1819 C C     . LEU A 1 242 ? 30.563 36.190  -3.877 1.00 50.84  ?  242 LEU A C     1 
ATOM   1820 O O     . LEU A 1 242 ? 30.739 35.787  -5.038 1.00 50.46  ?  242 LEU A O     1 
ATOM   1821 C CB    . LEU A 1 242 ? 31.777 37.929  -2.510 1.00 47.98  ?  242 LEU A CB    1 
ATOM   1822 C CG    . LEU A 1 242 ? 33.001 38.328  -1.686 1.00 49.19  ?  242 LEU A CG    1 
ATOM   1823 C CD1   . LEU A 1 242 ? 33.076 39.832  -1.478 1.00 48.59  ?  242 LEU A CD1   1 
ATOM   1824 C CD2   . LEU A 1 242 ? 32.948 37.608  -0.351 1.00 47.08  ?  242 LEU A CD2   1 
ATOM   1825 N N     . PRO A 1 243 ? 29.328 36.379  -3.402 1.00 47.24  ?  243 PRO A N     1 
ATOM   1826 C CA    . PRO A 1 243 ? 28.182 36.043  -4.256 1.00 48.56  ?  243 PRO A CA    1 
ATOM   1827 C C     . PRO A 1 243 ? 28.015 37.001  -5.407 1.00 53.16  ?  243 PRO A C     1 
ATOM   1828 O O     . PRO A 1 243 ? 27.612 36.574  -6.499 1.00 60.46  ?  243 PRO A O     1 
ATOM   1829 C CB    . PRO A 1 243 ? 26.989 36.083  -3.290 1.00 46.66  ?  243 PRO A CB    1 
ATOM   1830 C CG    . PRO A 1 243 ? 27.583 35.917  -1.931 1.00 45.65  ?  243 PRO A CG    1 
ATOM   1831 C CD    . PRO A 1 243 ? 28.924 36.606  -2.007 1.00 46.34  ?  243 PRO A CD    1 
ATOM   1832 N N     . ASP A 1 244 ? 28.327 38.285  -5.208 1.00 52.85  ?  244 ASP A N     1 
ATOM   1833 C CA    . ASP A 1 244 ? 28.191 39.268  -6.284 1.00 53.39  ?  244 ASP A CA    1 
ATOM   1834 C C     . ASP A 1 244 ? 29.386 39.297  -7.227 1.00 50.54  ?  244 ASP A C     1 
ATOM   1835 O O     . ASP A 1 244 ? 29.507 40.254  -7.992 1.00 51.54  ?  244 ASP A O     1 
ATOM   1836 C CB    . ASP A 1 244 ? 27.928 40.681  -5.723 1.00 57.11  ?  244 ASP A CB    1 
ATOM   1837 C CG    . ASP A 1 244 ? 29.168 41.325  -5.067 1.00 59.15  ?  244 ASP A CG    1 
ATOM   1838 O OD1   . ASP A 1 244 ? 30.302 40.863  -5.330 1.00 54.85  ?  244 ASP A OD1   1 
ATOM   1839 O OD2   . ASP A 1 244 ? 28.994 42.342  -4.323 1.00 57.98  -1 244 ASP A OD2   1 
ATOM   1840 N N     . GLY A 1 245 ? 30.264 38.290  -7.188 1.00 53.25  ?  245 GLY A N     1 
ATOM   1841 C CA    . GLY A 1 245 ? 31.362 38.150  -8.118 1.00 56.31  ?  245 GLY A CA    1 
ATOM   1842 C C     . GLY A 1 245 ? 32.714 38.644  -7.619 1.00 58.73  ?  245 GLY A C     1 
ATOM   1843 O O     . GLY A 1 245 ? 33.747 38.137  -8.079 1.00 61.21  ?  245 GLY A O     1 
ATOM   1844 N N     . GLN A 1 246 ? 32.734 39.627  -6.706 1.00 54.04  ?  246 GLN A N     1 
ATOM   1845 C CA    . GLN A 1 246 ? 33.986 40.175  -6.184 1.00 50.10  ?  246 GLN A CA    1 
ATOM   1846 C C     . GLN A 1 246 ? 34.833 39.088  -5.527 1.00 54.64  ?  246 GLN A C     1 
ATOM   1847 O O     . GLN A 1 246 ? 34.313 38.233  -4.802 1.00 58.29  ?  246 GLN A O     1 
ATOM   1848 C CB    . GLN A 1 246 ? 33.700 41.267  -5.157 1.00 46.91  ?  246 GLN A CB    1 
ATOM   1849 C CG    . GLN A 1 246 ? 32.947 42.496  -5.657 1.00 44.93  ?  246 GLN A CG    1 
ATOM   1850 C CD    . GLN A 1 246 ? 33.148 43.691  -4.722 1.00 46.16  ?  246 GLN A CD    1 
ATOM   1851 O OE1   . GLN A 1 246 ? 32.226 44.110  -4.003 1.00 44.31  ?  246 GLN A OE1   1 
ATOM   1852 N NE2   . GLN A 1 246 ? 34.375 44.229  -4.710 1.00 42.62  ?  246 GLN A NE2   1 
ATOM   1853 N N     . VAL A 1 247 ? 36.148 39.126  -5.763 1.00 50.94  ?  247 VAL A N     1 
ATOM   1854 C CA    . VAL A 1 247 ? 37.085 38.179  -5.159 1.00 50.02  ?  247 VAL A CA    1 
ATOM   1855 C C     . VAL A 1 247 ? 37.924 38.900  -4.108 1.00 52.16  ?  247 VAL A C     1 
ATOM   1856 O O     . VAL A 1 247 ? 38.437 40.001  -4.358 1.00 56.98  ?  247 VAL A O     1 
ATOM   1857 C CB    . VAL A 1 247 ? 37.988 37.514  -6.210 1.00 48.83  ?  247 VAL A CB    1 
ATOM   1858 C CG1   . VAL A 1 247 ? 39.021 36.653  -5.526 1.00 47.05  ?  247 VAL A CG1   1 
ATOM   1859 C CG2   . VAL A 1 247 ? 37.167 36.656  -7.122 1.00 53.79  ?  247 VAL A CG2   1 
ATOM   1860 N N     . ILE A 1 248 ? 38.053 38.282  -2.931 1.00 44.99  ?  248 ILE A N     1 
ATOM   1861 C CA    . ILE A 1 248 ? 38.883 38.783  -1.842 1.00 46.12  ?  248 ILE A CA    1 
ATOM   1862 C C     . ILE A 1 248 ? 39.852 37.666  -1.464 1.00 47.65  ?  248 ILE A C     1 
ATOM   1863 O O     . ILE A 1 248 ? 39.690 36.519  -1.879 1.00 51.51  ?  248 ILE A O     1 
ATOM   1864 C CB    . ILE A 1 248 ? 38.051 39.224  -0.626 1.00 43.56  ?  248 ILE A CB    1 
ATOM   1865 C CG1   . ILE A 1 248 ? 37.385 37.997  0.013  1.00 41.41  ?  248 ILE A CG1   1 
ATOM   1866 C CG2   . ILE A 1 248 ? 37.023 40.268  -1.051 1.00 42.68  ?  248 ILE A CG2   1 
ATOM   1867 C CD1   . ILE A 1 248 ? 36.955 38.168  1.457  1.00 39.02  ?  248 ILE A CD1   1 
ATOM   1868 N N     . THR A 1 249 ? 40.869 37.999  -0.671 1.00 42.61  ?  249 THR A N     1 
ATOM   1869 C CA    . THR A 1 249 ? 41.893 37.014  -0.343 1.00 43.96  ?  249 THR A CA    1 
ATOM   1870 C C     . THR A 1 249 ? 42.140 36.971  1.159  1.00 37.54  ?  249 THR A C     1 
ATOM   1871 O O     . THR A 1 249 ? 42.306 38.015  1.787  1.00 36.01  ?  249 THR A O     1 
ATOM   1872 C CB    . THR A 1 249 ? 43.191 37.309  -1.103 1.00 49.55  ?  249 THR A CB    1 
ATOM   1873 O OG1   . THR A 1 249 ? 43.678 38.606  -0.732 1.00 50.19  ?  249 THR A OG1   1 
ATOM   1874 C CG2   . THR A 1 249 ? 42.939 37.237  -2.626 1.00 44.10  ?  249 THR A CG2   1 
ATOM   1875 N N     . ILE A 1 250 ? 42.157 35.762  1.719  1.00 33.49  ?  250 ILE A N     1 
ATOM   1876 C CA    . ILE A 1 250 ? 42.300 35.525  3.152  1.00 35.78  ?  250 ILE A CA    1 
ATOM   1877 C C     . ILE A 1 250 ? 43.738 35.101  3.442  1.00 36.14  ?  250 ILE A C     1 
ATOM   1878 O O     . ILE A 1 250 ? 44.243 34.122  2.876  1.00 33.80  ?  250 ILE A O     1 
ATOM   1879 C CB    . ILE A 1 250 ? 41.312 34.453  3.655  1.00 36.09  ?  250 ILE A CB    1 
ATOM   1880 C CG1   . ILE A 1 250 ? 40.080 34.345  2.767  1.00 37.41  ?  250 ILE A CG1   1 
ATOM   1881 C CG2   . ILE A 1 250 ? 40.898 34.696  5.105  1.00 29.80  ?  250 ILE A CG2   1 
ATOM   1882 C CD1   . ILE A 1 250 ? 39.230 35.591  2.777  1.00 40.82  ?  250 ILE A CD1   1 
ATOM   1883 N N     . GLY A 1 251 ? 44.394 35.820  4.341  1.00 35.29  ?  251 GLY A N     1 
ATOM   1884 C CA    . GLY A 1 251 ? 45.749 35.486  4.734  1.00 37.93  ?  251 GLY A CA    1 
ATOM   1885 C C     . GLY A 1 251 ? 45.824 34.895  6.128  1.00 35.94  ?  251 GLY A C     1 
ATOM   1886 O O     . GLY A 1 251 ? 45.255 33.825  6.378  1.00 31.62  ?  251 GLY A O     1 
ATOM   1887 N N     . ASN A 1 252 ? 46.510 35.570  7.056  1.00 34.42  ?  252 ASN A N     1 
ATOM   1888 C CA    . ASN A 1 252 ? 46.685 34.945  8.361  1.00 33.54  ?  252 ASN A CA    1 
ATOM   1889 C C     . ASN A 1 252 ? 45.354 34.799  9.070  1.00 36.61  ?  252 ASN A C     1 
ATOM   1890 O O     . ASN A 1 252 ? 45.227 33.942  9.953  1.00 38.42  ?  252 ASN A O     1 
ATOM   1891 C CB    . ASN A 1 252 ? 47.703 35.705  9.228  1.00 37.26  ?  252 ASN A CB    1 
ATOM   1892 C CG    . ASN A 1 252 ? 47.398 37.201  9.372  1.00 39.97  ?  252 ASN A CG    1 
ATOM   1893 O OD1   . ASN A 1 252 ? 46.335 37.683  8.992  1.00 42.67  ?  252 ASN A OD1   1 
ATOM   1894 N ND2   . ASN A 1 252 ? 48.347 37.937  9.937  1.00 38.76  ?  252 ASN A ND2   1 
ATOM   1895 N N     . GLU A 1 253 ? 44.350 35.582  8.662  1.00 37.31  ?  253 GLU A N     1 
ATOM   1896 C CA    . GLU A 1 253 ? 42.973 35.426  9.115  1.00 34.90  ?  253 GLU A CA    1 
ATOM   1897 C C     . GLU A 1 253 ? 42.544 33.968  9.095  1.00 32.85  ?  253 GLU A C     1 
ATOM   1898 O O     . GLU A 1 253 ? 41.756 33.541  9.947  1.00 32.48  ?  253 GLU A O     1 
ATOM   1899 C CB    . GLU A 1 253 ? 42.017 36.242  8.242  1.00 33.46  ?  253 GLU A CB    1 
ATOM   1900 C CG    . GLU A 1 253 ? 42.058 37.710  8.518  1.00 36.53  ?  253 GLU A CG    1 
ATOM   1901 C CD    . GLU A 1 253 ? 43.064 38.469  7.655  1.00 42.89  ?  253 GLU A CD    1 
ATOM   1902 O OE1   . GLU A 1 253 ? 43.156 39.716  7.826  1.00 44.14  ?  253 GLU A OE1   1 
ATOM   1903 O OE2   . GLU A 1 253 ? 43.743 37.835  6.803  1.00 41.53  -1 253 GLU A OE2   1 
ATOM   1904 N N     . ARG A 1 254 ? 43.030 33.209  8.106  1.00 31.17  ?  254 ARG A N     1 
ATOM   1905 C CA    . ARG A 1 254 ? 42.652 31.808  8.000  1.00 29.70  ?  254 ARG A CA    1 
ATOM   1906 C C     . ARG A 1 254 ? 42.896 31.070  9.313  1.00 32.54  ?  254 ARG A C     1 
ATOM   1907 O O     . ARG A 1 254 ? 42.026 30.329  9.785  1.00 33.25  ?  254 ARG A O     1 
ATOM   1908 C CB    . ARG A 1 254 ? 43.415 31.138  6.868  1.00 31.47  ?  254 ARG A CB    1 
ATOM   1909 C CG    . ARG A 1 254 ? 43.058 31.583  5.491  1.00 29.04  ?  254 ARG A CG    1 
ATOM   1910 C CD    . ARG A 1 254 ? 43.957 30.872  4.493  1.00 30.37  ?  254 ARG A CD    1 
ATOM   1911 N NE    . ARG A 1 254 ? 43.610 29.464  4.355  1.00 31.04  ?  254 ARG A NE    1 
ATOM   1912 C CZ    . ARG A 1 254 ? 44.458 28.496  3.990  1.00 34.12  ?  254 ARG A CZ    1 
ATOM   1913 N NH1   . ARG A 1 254 ? 45.720 28.777  3.727  1.00 35.65  ?  254 ARG A NH1   1 
ATOM   1914 N NH2   . ARG A 1 254 ? 44.045 27.236  3.888  1.00 29.50  ?  254 ARG A NH2   1 
ATOM   1915 N N     . PHE A 1 255 ? 44.074 31.257  9.932  1.00 31.81  ?  255 PHE A N     1 
ATOM   1916 C CA    . PHE A 1 255 ? 44.359 30.578  11.197 1.00 30.24  ?  255 PHE A CA    1 
ATOM   1917 C C     . PHE A 1 255 ? 44.276 31.476  12.429 1.00 32.35  ?  255 PHE A C     1 
ATOM   1918 O O     . PHE A 1 255 ? 44.249 30.949  13.548 1.00 31.14  ?  255 PHE A O     1 
ATOM   1919 C CB    . PHE A 1 255 ? 45.746 29.907  11.171 1.00 27.44  ?  255 PHE A CB    1 
ATOM   1920 C CG    . PHE A 1 255 ? 46.888 30.871  10.963 1.00 32.26  ?  255 PHE A CG    1 
ATOM   1921 C CD1   . PHE A 1 255 ? 47.397 31.097  9.687  1.00 30.96  ?  255 PHE A CD1   1 
ATOM   1922 C CD2   . PHE A 1 255 ? 47.439 31.573  12.045 1.00 31.85  ?  255 PHE A CD2   1 
ATOM   1923 C CE1   . PHE A 1 255 ? 48.440 31.990  9.489  1.00 34.46  ?  255 PHE A CE1   1 
ATOM   1924 C CE2   . PHE A 1 255 ? 48.473 32.473  11.860 1.00 33.58  ?  255 PHE A CE2   1 
ATOM   1925 C CZ    . PHE A 1 255 ? 48.985 32.681  10.580 1.00 37.05  ?  255 PHE A CZ    1 
ATOM   1926 N N     . ARG A 1 256 ? 44.244 32.803  12.275 1.00 28.46  ?  256 ARG A N     1 
ATOM   1927 C CA    . ARG A 1 256 ? 44.055 33.624  13.463 1.00 30.49  ?  256 ARG A CA    1 
ATOM   1928 C C     . ARG A 1 256 ? 42.689 33.381  14.068 1.00 30.34  ?  256 ARG A C     1 
ATOM   1929 O O     . ARG A 1 256 ? 42.514 33.523  15.282 1.00 32.64  ?  256 ARG A O     1 
ATOM   1930 C CB    . ARG A 1 256 ? 44.219 35.112  13.163 1.00 29.15  ?  256 ARG A CB    1 
ATOM   1931 C CG    . ARG A 1 256 ? 45.639 35.503  12.904 1.00 32.08  ?  256 ARG A CG    1 
ATOM   1932 C CD    . ARG A 1 256 ? 45.709 36.837  12.230 1.00 32.63  ?  256 ARG A CD    1 
ATOM   1933 N NE    . ARG A 1 256 ? 45.132 37.878  13.077 1.00 35.32  ?  256 ARG A NE    1 
ATOM   1934 C CZ    . ARG A 1 256 ? 44.459 38.929  12.618 1.00 31.33  ?  256 ARG A CZ    1 
ATOM   1935 N NH1   . ARG A 1 256 ? 44.269 39.074  11.306 1.00 31.38  ?  256 ARG A NH1   1 
ATOM   1936 N NH2   . ARG A 1 256 ? 43.969 39.820  13.474 1.00 28.39  ?  256 ARG A NH2   1 
ATOM   1937 N N     . CYS A 1 257 ? 41.729 32.987  13.254 1.00 28.96  ?  257 CYS A N     1 
ATOM   1938 C CA    . CYS A 1 257 ? 40.351 32.897  13.701 1.00 31.18  ?  257 CYS A CA    1 
ATOM   1939 C C     . CYS A 1 257 ? 40.151 31.661  14.586 1.00 28.08  ?  257 CYS A C     1 
ATOM   1940 O O     . CYS A 1 257 ? 39.789 31.810  15.757 1.00 29.68  ?  257 CYS A O     1 
ATOM   1941 C CB    . CYS A 1 257 ? 39.428 32.935  12.465 1.00 32.69  ?  257 CYS A CB    1 
ATOM   1942 S SG    . CYS A 1 257 ? 37.852 32.021  12.567 1.00 39.44  ?  257 CYS A SG    1 
ATOM   1943 N N     . PRO A 1 258 ? 40.385 30.436  14.095 1.00 31.35  ?  258 PRO A N     1 
ATOM   1944 C CA    . PRO A 1 258 ? 40.245 29.263  14.983 1.00 33.09  ?  258 PRO A CA    1 
ATOM   1945 C C     . PRO A 1 258 ? 41.237 29.265  16.131 1.00 33.99  ?  258 PRO A C     1 
ATOM   1946 O O     . PRO A 1 258 ? 41.025 28.555  17.127 1.00 31.10  ?  258 PRO A O     1 
ATOM   1947 C CB    . PRO A 1 258 ? 40.487 28.075  14.047 1.00 31.83  ?  258 PRO A CB    1 
ATOM   1948 C CG    . PRO A 1 258 ? 41.358 28.647  12.960 1.00 30.73  ?  258 PRO A CG    1 
ATOM   1949 C CD    . PRO A 1 258 ? 40.859 30.044  12.750 1.00 32.51  ?  258 PRO A CD    1 
ATOM   1950 N N     . GLU A 1 259 ? 42.319 30.042  16.023 1.00 33.05  ?  259 GLU A N     1 
ATOM   1951 C CA    . GLU A 1 259 ? 43.235 30.193  17.145 1.00 32.31  ?  259 GLU A CA    1 
ATOM   1952 C C     . GLU A 1 259 ? 42.498 30.629  18.402 1.00 31.25  ?  259 GLU A C     1 
ATOM   1953 O O     . GLU A 1 259 ? 42.938 30.310  19.511 1.00 28.92  ?  259 GLU A O     1 
ATOM   1954 C CB    . GLU A 1 259 ? 44.343 31.191  16.793 1.00 30.29  ?  259 GLU A CB    1 
ATOM   1955 C CG    . GLU A 1 259 ? 45.414 31.355  17.874 1.00 32.28  ?  259 GLU A CG    1 
ATOM   1956 C CD    . GLU A 1 259 ? 46.214 30.049  18.185 1.00 36.49  ?  259 GLU A CD    1 
ATOM   1957 O OE1   . GLU A 1 259 ? 46.323 29.142  17.298 1.00 26.32  ?  259 GLU A OE1   1 
ATOM   1958 O OE2   . GLU A 1 259 ? 46.741 29.955  19.336 1.00 34.60  -1 259 GLU A OE2   1 
ATOM   1959 N N     . ALA A 1 260 ? 41.368 31.346  18.246 1.00 30.78  ?  260 ALA A N     1 
ATOM   1960 C CA    . ALA A 1 260 ? 40.579 31.795  19.389 1.00 29.87  ?  260 ALA A CA    1 
ATOM   1961 C C     . ALA A 1 260 ? 40.264 30.644  20.354 1.00 31.53  ?  260 ALA A C     1 
ATOM   1962 O O     . ALA A 1 260 ? 40.087 30.894  21.544 1.00 32.03  ?  260 ALA A O     1 
ATOM   1963 C CB    . ALA A 1 260 ? 39.301 32.502  18.894 1.00 23.59  ?  260 ALA A CB    1 
ATOM   1964 N N     . LEU A 1 261 ? 40.250 29.384  19.885 1.00 31.62  ?  261 LEU A N     1 
ATOM   1965 C CA    . LEU A 1 261 ? 39.880 28.251  20.741 1.00 30.16  ?  261 LEU A CA    1 
ATOM   1966 C C     . LEU A 1 261 ? 40.929 27.955  21.802 1.00 32.06  ?  261 LEU A C     1 
ATOM   1967 O O     . LEU A 1 261 ? 40.602 27.405  22.863 1.00 30.73  ?  261 LEU A O     1 
ATOM   1968 C CB    . LEU A 1 261 ? 39.667 26.990  19.910 1.00 27.36  ?  261 LEU A CB    1 
ATOM   1969 C CG    . LEU A 1 261 ? 38.402 26.920  19.074 1.00 27.72  ?  261 LEU A CG    1 
ATOM   1970 C CD1   . LEU A 1 261 ? 38.395 25.681  18.199 1.00 23.40  ?  261 LEU A CD1   1 
ATOM   1971 C CD2   . LEU A 1 261 ? 37.227 26.944  19.998 1.00 25.82  ?  261 LEU A CD2   1 
ATOM   1972 N N     . PHE A 1 262 ? 42.193 28.262  21.520 1.00 32.79  ?  262 PHE A N     1 
ATOM   1973 C CA    . PHE A 1 262 ? 43.289 28.060  22.453 1.00 29.24  ?  262 PHE A CA    1 
ATOM   1974 C C     . PHE A 1 262 ? 43.692 29.356  23.151 1.00 34.03  ?  262 PHE A C     1 
ATOM   1975 O O     . PHE A 1 262 ? 44.447 29.317  24.129 1.00 33.62  ?  262 PHE A O     1 
ATOM   1976 C CB    . PHE A 1 262 ? 44.495 27.454  21.715 1.00 29.57  ?  262 PHE A CB    1 
ATOM   1977 C CG    . PHE A 1 262 ? 44.169 26.200  20.904 1.00 32.47  ?  262 PHE A CG    1 
ATOM   1978 C CD1   . PHE A 1 262 ? 44.337 24.920  21.456 1.00 32.68  ?  262 PHE A CD1   1 
ATOM   1979 C CD2   . PHE A 1 262 ? 43.705 26.291  19.589 1.00 29.04  ?  262 PHE A CD2   1 
ATOM   1980 C CE1   . PHE A 1 262 ? 44.039 23.756  20.694 1.00 33.63  ?  262 PHE A CE1   1 
ATOM   1981 C CE2   . PHE A 1 262 ? 43.395 25.141  18.839 1.00 27.51  ?  262 PHE A CE2   1 
ATOM   1982 C CZ    . PHE A 1 262 ? 43.563 23.880  19.381 1.00 27.30  ?  262 PHE A CZ    1 
ATOM   1983 N N     . GLN A 1 263 ? 43.182 30.492  22.684 1.00 34.03  ?  263 GLN A N     1 
ATOM   1984 C CA    . GLN A 1 263 ? 43.493 31.803  23.251 1.00 36.16  ?  263 GLN A CA    1 
ATOM   1985 C C     . GLN A 1 263 ? 42.216 32.624  23.258 1.00 38.40  ?  263 GLN A C     1 
ATOM   1986 O O     . GLN A 1 263 ? 41.995 33.471  22.382 1.00 35.07  ?  263 GLN A O     1 
ATOM   1987 C CB    . GLN A 1 263 ? 44.593 32.506  22.453 1.00 31.82  ?  263 GLN A CB    1 
ATOM   1988 C CG    . GLN A 1 263 ? 45.851 31.676  22.276 1.00 29.44  ?  263 GLN A CG    1 
ATOM   1989 C CD    . GLN A 1 263 ? 47.054 32.518  21.869 1.00 32.51  ?  263 GLN A CD    1 
ATOM   1990 O OE1   . GLN A 1 263 ? 47.527 33.388  22.634 1.00 31.60  ?  263 GLN A OE1   1 
ATOM   1991 N NE2   . GLN A 1 263 ? 47.556 32.268  20.656 1.00 23.30  ?  263 GLN A NE2   1 
ATOM   1992 N N     . PRO A 1 264 ? 41.322 32.366  24.217 1.00 39.18  ?  264 PRO A N     1 
ATOM   1993 C CA    . PRO A 1 264 ? 40.087 33.157  24.294 1.00 39.56  ?  264 PRO A CA    1 
ATOM   1994 C C     . PRO A 1 264 ? 40.327 34.643  24.565 1.00 44.60  ?  264 PRO A C     1 
ATOM   1995 O O     . PRO A 1 264 ? 39.403 35.449  24.372 1.00 45.75  ?  264 PRO A O     1 
ATOM   1996 C CB    . PRO A 1 264 ? 39.304 32.490  25.434 1.00 42.68  ?  264 PRO A CB    1 
ATOM   1997 C CG    . PRO A 1 264 ? 40.198 31.437  26.003 1.00 42.60  ?  264 PRO A CG    1 
ATOM   1998 C CD    . PRO A 1 264 ? 41.262 31.143  25.029 1.00 37.56  ?  264 PRO A CD    1 
ATOM   1999 N N     . SER A 1 265 ? 41.530 35.037  24.991 1.00 43.53  ?  265 SER A N     1 
ATOM   2000 C CA    . SER A 1 265 ? 41.834 36.460  25.084 1.00 38.35  ?  265 SER A CA    1 
ATOM   2001 C C     . SER A 1 265 ? 41.567 37.171  23.768 1.00 38.75  ?  265 SER A C     1 
ATOM   2002 O O     . SER A 1 265 ? 41.267 38.366  23.765 1.00 43.16  ?  265 SER A O     1 
ATOM   2003 C CB    . SER A 1 265 ? 43.291 36.666  25.474 1.00 38.92  ?  265 SER A CB    1 
ATOM   2004 O OG    . SER A 1 265 ? 44.151 35.765  24.795 1.00 41.70  ?  265 SER A OG    1 
ATOM   2005 N N     . PHE A 1 266 ? 41.684 36.462  22.641 1.00 31.23  ?  266 PHE A N     1 
ATOM   2006 C CA    . PHE A 1 266 ? 41.410 37.074  21.344 1.00 37.38  ?  266 PHE A CA    1 
ATOM   2007 C C     . PHE A 1 266 ? 40.027 37.727  21.283 1.00 37.66  ?  266 PHE A C     1 
ATOM   2008 O O     . PHE A 1 266 ? 39.795 38.582  20.418 1.00 36.29  ?  266 PHE A O     1 
ATOM   2009 C CB    . PHE A 1 266 ? 41.534 36.033  20.209 1.00 32.33  ?  266 PHE A CB    1 
ATOM   2010 C CG    . PHE A 1 266 ? 42.961 35.713  19.797 1.00 28.98  ?  266 PHE A CG    1 
ATOM   2011 C CD1   . PHE A 1 266 ? 44.008 35.783  20.708 1.00 31.03  ?  266 PHE A CD1   1 
ATOM   2012 C CD2   . PHE A 1 266 ? 43.245 35.315  18.496 1.00 30.51  ?  266 PHE A CD2   1 
ATOM   2013 C CE1   . PHE A 1 266 ? 45.307 35.483  20.325 1.00 27.50  ?  266 PHE A CE1   1 
ATOM   2014 C CE2   . PHE A 1 266 ? 44.548 35.004  18.103 1.00 30.72  ?  266 PHE A CE2   1 
ATOM   2015 C CZ    . PHE A 1 266 ? 45.581 35.096  19.016 1.00 28.53  ?  266 PHE A CZ    1 
ATOM   2016 N N     . LEU A 1 267 ? 39.102 37.312  22.146 1.00 41.02  ?  267 LEU A N     1 
ATOM   2017 C CA    . LEU A 1 267 ? 37.698 37.796  22.062 1.00 39.80  ?  267 LEU A CA    1 
ATOM   2018 C C     . LEU A 1 267 ? 37.340 38.538  23.342 1.00 43.83  ?  267 LEU A C     1 
ATOM   2019 O O     . LEU A 1 267 ? 36.208 39.018  23.441 1.00 45.99  ?  267 LEU A O     1 
ATOM   2020 C CB    . LEU A 1 267 ? 36.786 36.579  21.881 1.00 38.84  ?  267 LEU A CB    1 
ATOM   2021 C CG    . LEU A 1 267 ? 36.301 36.309  20.462 1.00 36.84  ?  267 LEU A CG    1 
ATOM   2022 C CD1   . LEU A 1 267 ? 35.959 37.604  19.751 1.00 48.90  ?  267 LEU A CD1   1 
ATOM   2023 C CD2   . LEU A 1 267 ? 37.344 35.535  19.686 1.00 36.40  ?  267 LEU A CD2   1 
ATOM   2024 N N     . GLY A 1 268 ? 38.270 38.596  24.287 1.00 38.81  ?  268 GLY A N     1 
ATOM   2025 C CA    . GLY A 1 268 ? 38.039 39.311  25.550 1.00 41.52  ?  268 GLY A CA    1 
ATOM   2026 C C     . GLY A 1 268 ? 37.677 38.349  26.650 1.00 44.21  ?  268 GLY A C     1 
ATOM   2027 O O     . GLY A 1 268 ? 37.291 38.800  27.734 1.00 48.95  ?  268 GLY A O     1 
ATOM   2028 N N     . MET A 1 269 ? 37.798 37.060  26.372 1.00 42.19  ?  269 MET A N     1 
ATOM   2029 C CA    . MET A 1 269 ? 37.383 36.055  27.368 1.00 45.83  ?  269 MET A CA    1 
ATOM   2030 C C     . MET A 1 269 ? 38.595 35.664  28.200 1.00 52.14  ?  269 MET A C     1 
ATOM   2031 O O     . MET A 1 269 ? 39.621 35.313  27.624 1.00 53.17  ?  269 MET A O     1 
ATOM   2032 C CB    . MET A 1 269 ? 36.796 34.817  26.690 1.00 44.76  ?  269 MET A CB    1 
ATOM   2033 C CG    . MET A 1 269 ? 35.599 35.102  25.822 1.00 46.18  ?  269 MET A CG    1 
ATOM   2034 S SD    . MET A 1 269 ? 34.629 33.610  25.519 1.00 45.45  ?  269 MET A SD    1 
ATOM   2035 C CE    . MET A 1 269 ? 34.965 32.677  27.009 1.00 40.42  ?  269 MET A CE    1 
ATOM   2036 N N     . GLU A 1 270 ? 38.461 35.731  29.519 1.00 60.72  ?  270 GLU A N     1 
ATOM   2037 C CA    . GLU A 1 270 ? 39.554 35.314  30.425 1.00 64.30  ?  270 GLU A CA    1 
ATOM   2038 C C     . GLU A 1 270 ? 39.358 33.838  30.768 1.00 65.02  ?  270 GLU A C     1 
ATOM   2039 O O     . GLU A 1 270 ? 39.612 33.471  31.919 1.00 71.67  ?  270 GLU A O     1 
ATOM   2040 C CB    . GLU A 1 270 ? 39.566 36.202  31.666 1.00 66.08  ?  270 GLU A CB    1 
ATOM   2041 C CG    . GLU A 1 270 ? 38.379 37.140  31.746 1.00 72.46  ?  270 GLU A CG    1 
ATOM   2042 C CD    . GLU A 1 270 ? 37.154 36.531  32.404 1.00 91.27  ?  270 GLU A CD    1 
ATOM   2043 O OE1   . GLU A 1 270 ? 37.268 36.093  33.565 1.00 96.91  ?  270 GLU A OE1   1 
ATOM   2044 O OE2   . GLU A 1 270 ? 36.094 36.489  31.749 1.00 92.13  -1 270 GLU A OE2   1 
ATOM   2045 N N     . SER A 1 271 ? 38.939 33.029  29.794 1.00 60.41  ?  271 SER A N     1 
ATOM   2046 C CA    . SER A 1 271 ? 38.794 31.570  30.005 1.00 56.74  ?  271 SER A CA    1 
ATOM   2047 C C     . SER A 1 271 ? 40.123 30.872  29.747 1.00 55.36  ?  271 SER A C     1 
ATOM   2048 O O     . SER A 1 271 ? 41.143 31.562  29.632 1.00 60.11  ?  271 SER A O     1 
ATOM   2049 C CB    . SER A 1 271 ? 37.702 30.991  29.169 1.00 54.37  ?  271 SER A CB    1 
ATOM   2050 O OG    . SER A 1 271 ? 37.276 29.749  29.701 1.00 59.64  ?  271 SER A OG    1 
ATOM   2051 N N     . CYS A 1 272 ? 40.100 29.560  29.562 1.00 49.68  ?  272 CYS A N     1 
ATOM   2052 C CA    . CYS A 1 272 ? 41.377 28.819  29.499 1.00 46.68  ?  272 CYS A CA    1 
ATOM   2053 C C     . CYS A 1 272 ? 41.798 28.432  28.086 1.00 49.02  ?  272 CYS A C     1 
ATOM   2054 O O     . CYS A 1 272 ? 42.921 28.767  27.698 1.00 50.58  ?  272 CYS A O     1 
ATOM   2055 C CB    . CYS A 1 272 ? 41.254 27.589  30.380 1.00 50.77  ?  272 CYS A CB    1 
ATOM   2056 S SG    . CYS A 1 272 ? 40.175 27.861  31.809 1.00 81.95  ?  272 CYS A SG    1 
ATOM   2057 N N     . GLY A 1 273 ? 40.947 27.760  27.336 1.00 41.83  ?  273 GLY A N     1 
ATOM   2058 C CA    . GLY A 1 273 ? 41.400 27.276  26.024 1.00 39.28  ?  273 GLY A CA    1 
ATOM   2059 C C     . GLY A 1 273 ? 41.014 25.837  25.926 1.00 32.99  ?  273 GLY A C     1 
ATOM   2060 O O     . GLY A 1 273 ? 41.100 25.168  26.944 1.00 33.86  ?  273 GLY A O     1 
ATOM   2061 N N     . ILE A 1 274 ? 40.626 25.375  24.743 1.00 29.31  ?  274 ILE A N     1 
ATOM   2062 C CA    . ILE A 1 274 ? 40.100 24.019  24.785 1.00 32.87  ?  274 ILE A CA    1 
ATOM   2063 C C     . ILE A 1 274 ? 41.113 22.984  25.287 1.00 32.90  ?  274 ILE A C     1 
ATOM   2064 O O     . ILE A 1 274 ? 40.702 21.925  25.780 1.00 27.98  ?  274 ILE A O     1 
ATOM   2065 C CB    . ILE A 1 274 ? 39.527 23.644  23.404 1.00 27.12  ?  274 ILE A CB    1 
ATOM   2066 C CG1   . ILE A 1 274 ? 40.557 23.880  22.308 1.00 25.97  ?  274 ILE A CG1   1 
ATOM   2067 C CG2   . ILE A 1 274 ? 38.298 24.471  23.142 1.00 25.27  ?  274 ILE A CG2   1 
ATOM   2068 C CD1   . ILE A 1 274 ? 40.104 23.413  20.913 1.00 27.63  ?  274 ILE A CD1   1 
ATOM   2069 N N     . HIS A 1 275 ? 42.423 23.260  25.203 1.00 30.94  ?  275 HIS A N     1 
ATOM   2070 C CA    . HIS A 1 275 ? 43.401 22.309  25.722 1.00 28.04  ?  275 HIS A CA    1 
ATOM   2071 C C     . HIS A 1 275 ? 43.495 22.386  27.238 1.00 30.75  ?  275 HIS A C     1 
ATOM   2072 O O     . HIS A 1 275 ? 43.548 21.345  27.915 1.00 33.12  ?  275 HIS A O     1 
ATOM   2073 C CB    . HIS A 1 275 ? 44.774 22.537  25.101 1.00 30.09  ?  275 HIS A CB    1 
ATOM   2074 C CG    . HIS A 1 275 ? 45.360 23.881  25.403 1.00 34.98  ?  275 HIS A CG    1 
ATOM   2075 N ND1   . HIS A 1 275 ? 44.736 25.063  25.067 1.00 34.53  ?  275 HIS A ND1   1 
ATOM   2076 C CD2   . HIS A 1 275 ? 46.523 24.231  25.998 1.00 34.72  ?  275 HIS A CD2   1 
ATOM   2077 C CE1   . HIS A 1 275 ? 45.478 26.083  25.456 1.00 30.85  ?  275 HIS A CE1   1 
ATOM   2078 N NE2   . HIS A 1 275 ? 46.567 25.606  26.027 1.00 34.22  ?  275 HIS A NE2   1 
ATOM   2079 N N     . GLU A 1 276 ? 43.498 23.598  27.796 1.00 26.66  ?  276 GLU A N     1 
ATOM   2080 C CA    . GLU A 1 276 ? 43.564 23.702  29.246 1.00 30.99  ?  276 GLU A CA    1 
ATOM   2081 C C     . GLU A 1 276 ? 42.307 23.134  29.899 1.00 30.17  ?  276 GLU A C     1 
ATOM   2082 O O     . GLU A 1 276 ? 42.404 22.405  30.886 1.00 27.36  ?  276 GLU A O     1 
ATOM   2083 C CB    . GLU A 1 276 ? 43.814 25.144  29.674 1.00 33.24  ?  276 GLU A CB    1 
ATOM   2084 C CG    . GLU A 1 276 ? 45.282 25.449  29.739 1.00 37.60  ?  276 GLU A CG    1 
ATOM   2085 C CD    . GLU A 1 276 ? 45.602 26.940  29.807 1.00 52.91  ?  276 GLU A CD    1 
ATOM   2086 O OE1   . GLU A 1 276 ? 45.254 27.684  28.858 1.00 47.63  ?  276 GLU A OE1   1 
ATOM   2087 O OE2   . GLU A 1 276 ? 46.225 27.365  30.810 1.00 64.68  -1 276 GLU A OE2   1 
ATOM   2088 N N     . THR A 1 277 ? 41.119 23.413  29.352 1.00 30.29  ?  277 THR A N     1 
ATOM   2089 C CA    . THR A 1 277 ? 39.928 22.859  29.983 1.00 28.70  ?  277 THR A CA    1 
ATOM   2090 C C     . THR A 1 277 ? 39.950 21.337  29.903 1.00 28.79  ?  277 THR A C     1 
ATOM   2091 O O     . THR A 1 277 ? 39.572 20.660  30.863 1.00 31.65  ?  277 THR A O     1 
ATOM   2092 C CB    . THR A 1 277 ? 38.644 23.448  29.375 1.00 29.44  ?  277 THR A CB    1 
ATOM   2093 O OG1   . THR A 1 277 ? 38.432 22.954  28.047 1.00 36.83  ?  277 THR A OG1   1 
ATOM   2094 C CG2   . THR A 1 277 ? 38.736 24.960  29.308 1.00 29.79  ?  277 THR A CG2   1 
ATOM   2095 N N     . THR A 1 278 ? 40.456 20.781  28.795 1.00 28.25  ?  278 THR A N     1 
ATOM   2096 C CA    . THR A 1 278 ? 40.626 19.335  28.692 1.00 27.93  ?  278 THR A CA    1 
ATOM   2097 C C     . THR A 1 278 ? 41.468 18.795  29.852 1.00 30.28  ?  278 THR A C     1 
ATOM   2098 O O     . THR A 1 278 ? 41.052 17.852  30.528 1.00 27.44  ?  278 THR A O     1 
ATOM   2099 C CB    . THR A 1 278 ? 41.232 18.979  27.329 1.00 26.48  ?  278 THR A CB    1 
ATOM   2100 O OG1   . THR A 1 278 ? 40.240 19.181  26.328 1.00 29.30  ?  278 THR A OG1   1 
ATOM   2101 C CG2   . THR A 1 278 ? 41.642 17.518  27.245 1.00 23.81  ?  278 THR A CG2   1 
ATOM   2102 N N     . PHE A 1 279 ? 42.657 19.381  30.094 1.00 27.54  ?  279 PHE A N     1 
ATOM   2103 C CA    . PHE A 1 279 ? 43.501 18.971  31.219 1.00 25.92  ?  279 PHE A CA    1 
ATOM   2104 C C     . PHE A 1 279 ? 42.779 19.196  32.537 1.00 30.03  ?  279 PHE A C     1 
ATOM   2105 O O     . PHE A 1 279 ? 42.751 18.319  33.412 1.00 30.91  ?  279 PHE A O     1 
ATOM   2106 C CB    . PHE A 1 279 ? 44.833 19.748  31.182 1.00 28.50  ?  279 PHE A CB    1 
ATOM   2107 C CG    . PHE A 1 279 ? 45.761 19.559  32.411 1.00 29.07  ?  279 PHE A CG    1 
ATOM   2108 C CD1   . PHE A 1 279 ? 46.670 18.499  32.479 1.00 28.02  ?  279 PHE A CD1   1 
ATOM   2109 C CD2   . PHE A 1 279 ? 45.786 20.499  33.445 1.00 26.91  ?  279 PHE A CD2   1 
ATOM   2110 C CE1   . PHE A 1 279 ? 47.544 18.336  33.576 1.00 25.76  ?  279 PHE A CE1   1 
ATOM   2111 C CE2   . PHE A 1 279 ? 46.678 20.350  34.538 1.00 28.02  ?  279 PHE A CE2   1 
ATOM   2112 C CZ    . PHE A 1 279 ? 47.553 19.262  34.599 1.00 24.52  ?  279 PHE A CZ    1 
ATOM   2113 N N     . ASN A 1 280 ? 42.190 20.377  32.702 1.00 30.43  ?  280 ASN A N     1 
ATOM   2114 C CA    . ASN A 1 280 ? 41.458 20.655  33.927 1.00 26.56  ?  280 ASN A CA    1 
ATOM   2115 C C     . ASN A 1 280 ? 40.393 19.600  34.129 1.00 29.00  ?  280 ASN A C     1 
ATOM   2116 O O     . ASN A 1 280 ? 40.247 19.063  35.225 1.00 32.58  ?  280 ASN A O     1 
ATOM   2117 C CB    . ASN A 1 280 ? 40.862 22.066  33.877 1.00 24.24  ?  280 ASN A CB    1 
ATOM   2118 C CG    . ASN A 1 280 ? 41.949 23.175  33.965 1.00 26.55  ?  280 ASN A CG    1 
ATOM   2119 O OD1   . ASN A 1 280 ? 43.088 22.919  34.372 1.00 23.57  ?  280 ASN A OD1   1 
ATOM   2120 N ND2   . ASN A 1 280 ? 41.591 24.398  33.575 1.00 24.21  ?  280 ASN A ND2   1 
ATOM   2121 N N     . SER A 1 281 ? 39.675 19.254  33.062 1.00 29.76  ?  281 SER A N     1 
ATOM   2122 C CA    . SER A 1 281 ? 38.671 18.203  33.126 1.00 28.46  ?  281 SER A CA    1 
ATOM   2123 C C     . SER A 1 281 ? 39.261 16.903  33.657 1.00 30.22  ?  281 SER A C     1 
ATOM   2124 O O     . SER A 1 281 ? 38.789 16.348  34.658 1.00 29.79  ?  281 SER A O     1 
ATOM   2125 C CB    . SER A 1 281 ? 38.081 17.989  31.744 1.00 26.89  ?  281 SER A CB    1 
ATOM   2126 O OG    . SER A 1 281 ? 36.736 17.620  31.847 1.00 33.15  ?  281 SER A OG    1 
ATOM   2127 N N     . ILE A 1 282 ? 40.308 16.409  32.989 1.00 30.28  ?  282 ILE A N     1 
ATOM   2128 C CA    . ILE A 1 282 ? 40.968 15.161  33.371 1.00 27.64  ?  282 ILE A CA    1 
ATOM   2129 C C     . ILE A 1 282 ? 41.408 15.173  34.829 1.00 32.89  ?  282 ILE A C     1 
ATOM   2130 O O     . ILE A 1 282 ? 41.436 14.120  35.480 1.00 33.31  ?  282 ILE A O     1 
ATOM   2131 C CB    . ILE A 1 282 ? 42.170 14.885  32.456 1.00 27.70  ?  282 ILE A CB    1 
ATOM   2132 C CG1   . ILE A 1 282 ? 41.720 14.385  31.084 1.00 28.24  ?  282 ILE A CG1   1 
ATOM   2133 C CG2   . ILE A 1 282 ? 43.070 13.856  33.084 1.00 28.09  ?  282 ILE A CG2   1 
ATOM   2134 C CD1   . ILE A 1 282 ? 42.809 14.458  30.070 1.00 23.14  ?  282 ILE A CD1   1 
ATOM   2135 N N     . MET A 1 283 ? 41.778 16.344  35.362 1.00 33.09  ?  283 MET A N     1 
ATOM   2136 C CA    . MET A 1 283 ? 42.294 16.451  36.724 1.00 29.79  ?  283 MET A CA    1 
ATOM   2137 C C     . MET A 1 283 ? 41.209 16.577  37.788 1.00 33.09  ?  283 MET A C     1 
ATOM   2138 O O     . MET A 1 283 ? 41.537 16.546  38.980 1.00 37.65  ?  283 MET A O     1 
ATOM   2139 C CB    . MET A 1 283 ? 43.255 17.632  36.842 1.00 28.71  ?  283 MET A CB    1 
ATOM   2140 C CG    . MET A 1 283 ? 44.471 17.510  35.951 1.00 32.05  ?  283 MET A CG    1 
ATOM   2141 S SD    . MET A 1 283 ? 45.691 16.295  36.510 1.00 39.06  ?  283 MET A SD    1 
ATOM   2142 C CE    . MET A 1 283 ? 46.104 16.979  38.116 1.00 24.35  ?  283 MET A CE    1 
ATOM   2143 N N     . LYS A 1 284 ? 39.940 16.710  37.412 1.00 28.89  ?  284 LYS A N     1 
ATOM   2144 C CA    . LYS A 1 284 ? 38.873 16.504  38.377 1.00 30.39  ?  284 LYS A CA    1 
ATOM   2145 C C     . LYS A 1 284 ? 38.433 15.037  38.422 1.00 32.50  ?  284 LYS A C     1 
ATOM   2146 O O     . LYS A 1 284 ? 37.488 14.703  39.141 1.00 29.10  ?  284 LYS A O     1 
ATOM   2147 C CB    . LYS A 1 284 ? 37.690 17.431  38.070 1.00 29.19  ?  284 LYS A CB    1 
ATOM   2148 C CG    . LYS A 1 284 ? 38.031 18.899  38.244 1.00 34.16  ?  284 LYS A CG    1 
ATOM   2149 C CD    . LYS A 1 284 ? 36.814 19.817  38.317 1.00 37.75  ?  284 LYS A CD    1 
ATOM   2150 C CE    . LYS A 1 284 ? 36.672 20.437  39.728 1.00 48.17  ?  284 LYS A CE    1 
ATOM   2151 N NZ    . LYS A 1 284 ? 35.805 19.667  40.723 1.00 39.75  ?  284 LYS A NZ    1 
ATOM   2152 N N     . CYS A 1 285 ? 39.096 14.156  37.676 1.00 28.30  ?  285 CYS A N     1 
ATOM   2153 C CA    . CYS A 1 285 ? 38.842 12.734  37.756 1.00 26.62  ?  285 CYS A CA    1 
ATOM   2154 C C     . CYS A 1 285 ? 39.893 12.079  38.633 1.00 34.52  ?  285 CYS A C     1 
ATOM   2155 O O     . CYS A 1 285 ? 41.030 12.545  38.728 1.00 35.39  ?  285 CYS A O     1 
ATOM   2156 C CB    . CYS A 1 285 ? 38.850 12.072  36.383 1.00 26.53  ?  285 CYS A CB    1 
ATOM   2157 S SG    . CYS A 1 285 ? 37.633 12.680  35.209 1.00 32.34  ?  285 CYS A SG    1 
ATOM   2158 N N     . ASP A 1 286 ? 39.470 11.005  39.299 1.00 39.46  ?  286 ASP A N     1 
ATOM   2159 C CA    . ASP A 1 286 ? 40.331 10.105  40.048 1.00 36.71  ?  286 ASP A CA    1 
ATOM   2160 C C     . ASP A 1 286 ? 41.586 9.757   39.257 1.00 37.36  ?  286 ASP A C     1 
ATOM   2161 O O     . ASP A 1 286 ? 41.518 9.470   38.060 1.00 37.56  ?  286 ASP A O     1 
ATOM   2162 C CB    . ASP A 1 286 ? 39.515 8.844   40.356 1.00 39.69  ?  286 ASP A CB    1 
ATOM   2163 C CG    . ASP A 1 286 ? 40.298 7.780   41.102 1.00 49.15  ?  286 ASP A CG    1 
ATOM   2164 O OD1   . ASP A 1 286 ? 41.387 8.082   41.651 1.00 51.12  ?  286 ASP A OD1   1 
ATOM   2165 O OD2   . ASP A 1 286 ? 39.791 6.624   41.156 1.00 55.47  -1 286 ASP A OD2   1 
ATOM   2166 N N     . VAL A 1 287 ? 42.734 9.757   39.950 1.00 39.54  ?  287 VAL A N     1 
ATOM   2167 C CA    . VAL A 1 287 ? 44.028 9.466   39.324 1.00 37.91  ?  287 VAL A CA    1 
ATOM   2168 C C     . VAL A 1 287 ? 43.990 8.141   38.561 1.00 38.67  ?  287 VAL A C     1 
ATOM   2169 O O     . VAL A 1 287 ? 44.555 8.022   37.461 1.00 37.50  ?  287 VAL A O     1 
ATOM   2170 C CB    . VAL A 1 287 ? 45.137 9.475   40.398 1.00 37.42  ?  287 VAL A CB    1 
ATOM   2171 C CG1   . VAL A 1 287 ? 46.512 9.705   39.768 1.00 31.81  ?  287 VAL A CG1   1 
ATOM   2172 C CG2   . VAL A 1 287 ? 44.820 10.532  41.468 1.00 38.39  ?  287 VAL A CG2   1 
ATOM   2173 N N     . ASP A 1 288 ? 43.312 7.130   39.122 1.00 38.93  ?  288 ASP A N     1 
ATOM   2174 C CA    . ASP A 1 288 ? 43.325 5.781   38.545 1.00 40.95  ?  288 ASP A CA    1 
ATOM   2175 C C     . ASP A 1 288 ? 42.783 5.707   37.125 1.00 36.64  ?  288 ASP A C     1 
ATOM   2176 O O     . ASP A 1 288 ? 43.042 4.706   36.450 1.00 35.48  ?  288 ASP A O     1 
ATOM   2177 C CB    . ASP A 1 288 ? 42.501 4.790   39.379 1.00 42.01  ?  288 ASP A CB    1 
ATOM   2178 C CG    . ASP A 1 288 ? 43.059 4.567   40.766 1.00 45.57  ?  288 ASP A CG    1 
ATOM   2179 O OD1   . ASP A 1 288 ? 44.210 4.966   41.027 1.00 49.53  ?  288 ASP A OD1   1 
ATOM   2180 O OD2   . ASP A 1 288 ? 42.326 4.001   41.606 1.00 50.62  -1 288 ASP A OD2   1 
ATOM   2181 N N     . ILE A 1 289 ? 41.995 6.688   36.668 1.00 34.63  ?  289 ILE A N     1 
ATOM   2182 C CA    . ILE A 1 289 ? 41.408 6.618   35.331 1.00 36.84  ?  289 ILE A CA    1 
ATOM   2183 C C     . ILE A 1 289 ? 42.034 7.609   34.342 1.00 35.78  ?  289 ILE A C     1 
ATOM   2184 O O     . ILE A 1 289 ? 41.730 7.535   33.133 1.00 33.20  ?  289 ILE A O     1 
ATOM   2185 C CB    . ILE A 1 289 ? 39.863 6.761   35.346 1.00 29.94  ?  289 ILE A CB    1 
ATOM   2186 C CG1   . ILE A 1 289 ? 39.369 8.141   35.777 1.00 30.72  ?  289 ILE A CG1   1 
ATOM   2187 C CG2   . ILE A 1 289 ? 39.182 5.657   36.146 1.00 28.70  ?  289 ILE A CG2   1 
ATOM   2188 C CD1   . ILE A 1 289 ? 37.907 8.358   35.396 1.00 27.38  ?  289 ILE A CD1   1 
ATOM   2189 N N     . ARG A 1 290 ? 42.940 8.486   34.790 1.00 32.45  ?  290 ARG A N     1 
ATOM   2190 C CA    . ARG A 1 290 ? 43.489 9.487   33.879 1.00 30.53  ?  290 ARG A CA    1 
ATOM   2191 C C     . ARG A 1 290 ? 44.218 8.857   32.698 1.00 30.50  ?  290 ARG A C     1 
ATOM   2192 O O     . ARG A 1 290 ? 44.143 9.382   31.585 1.00 30.07  ?  290 ARG A O     1 
ATOM   2193 C CB    . ARG A 1 290 ? 44.407 10.440  34.633 1.00 28.52  ?  290 ARG A CB    1 
ATOM   2194 C CG    . ARG A 1 290 ? 43.674 11.210  35.699 1.00 29.77  ?  290 ARG A CG    1 
ATOM   2195 C CD    . ARG A 1 290 ? 44.481 12.347  36.224 1.00 27.52  ?  290 ARG A CD    1 
ATOM   2196 N NE    . ARG A 1 290 ? 43.900 12.841  37.457 1.00 28.51  ?  290 ARG A NE    1 
ATOM   2197 C CZ    . ARG A 1 290 ? 44.608 13.178  38.524 1.00 29.41  ?  290 ARG A CZ    1 
ATOM   2198 N NH1   . ARG A 1 290 ? 45.932 13.075  38.503 1.00 23.94  ?  290 ARG A NH1   1 
ATOM   2199 N NH2   . ARG A 1 290 ? 43.984 13.633  39.601 1.00 31.53  ?  290 ARG A NH2   1 
ATOM   2200 N N     . LYS A 1 291 ? 44.926 7.738   32.900 1.00 32.42  ?  291 LYS A N     1 
ATOM   2201 C CA    . LYS A 1 291 ? 45.658 7.150   31.775 1.00 36.55  ?  291 LYS A CA    1 
ATOM   2202 C C     . LYS A 1 291 ? 44.703 6.789   30.626 1.00 36.01  ?  291 LYS A C     1 
ATOM   2203 O O     . LYS A 1 291 ? 44.956 7.124   29.461 1.00 31.53  ?  291 LYS A O     1 
ATOM   2204 C CB    . LYS A 1 291 ? 46.478 5.943   32.235 1.00 30.84  ?  291 LYS A CB    1 
ATOM   2205 C CG    . LYS A 1 291 ? 47.546 6.284   33.244 1.00 41.65  ?  291 LYS A CG    1 
ATOM   2206 C CD    . LYS A 1 291 ? 48.810 5.409   33.121 1.00 49.40  ?  291 LYS A CD    1 
ATOM   2207 C CE    . LYS A 1 291 ? 48.556 3.928   33.438 1.00 54.48  ?  291 LYS A CE    1 
ATOM   2208 N NZ    . LYS A 1 291 ? 49.807 3.163   33.829 1.00 55.75  ?  291 LYS A NZ    1 
ATOM   2209 N N     . ASP A 1 292 ? 43.574 6.150   30.946 1.00 38.03  ?  292 ASP A N     1 
ATOM   2210 C CA    . ASP A 1 292 ? 42.572 5.822   29.928 1.00 39.68  ?  292 ASP A CA    1 
ATOM   2211 C C     . ASP A 1 292 ? 42.050 7.066   29.215 1.00 39.04  ?  292 ASP A C     1 
ATOM   2212 O O     . ASP A 1 292 ? 41.969 7.097   27.979 1.00 39.62  ?  292 ASP A O     1 
ATOM   2213 C CB    . ASP A 1 292 ? 41.406 5.082   30.571 1.00 41.60  ?  292 ASP A CB    1 
ATOM   2214 C CG    . ASP A 1 292 ? 41.736 3.662   30.873 1.00 49.57  ?  292 ASP A CG    1 
ATOM   2215 O OD1   . ASP A 1 292 ? 40.985 3.014   31.654 1.00 57.14  ?  292 ASP A OD1   1 
ATOM   2216 O OD2   . ASP A 1 292 ? 42.754 3.205   30.309 1.00 50.14  -1 292 ASP A OD2   1 
ATOM   2217 N N     . LEU A 1 293 ? 41.634 8.079   29.990 1.00 34.74  ?  293 LEU A N     1 
ATOM   2218 C CA    . LEU A 1 293 ? 41.205 9.363   29.439 1.00 30.07  ?  293 LEU A CA    1 
ATOM   2219 C C     . LEU A 1 293 ? 42.236 9.952   28.477 1.00 29.41  ?  293 LEU A C     1 
ATOM   2220 O O     . LEU A 1 293 ? 41.912 10.290  27.341 1.00 29.48  ?  293 LEU A O     1 
ATOM   2221 C CB    . LEU A 1 293 ? 40.946 10.333  30.588 1.00 28.57  ?  293 LEU A CB    1 
ATOM   2222 C CG    . LEU A 1 293 ? 39.533 10.476  31.123 1.00 25.49  ?  293 LEU A CG    1 
ATOM   2223 C CD1   . LEU A 1 293 ? 38.780 9.136   31.157 1.00 24.25  ?  293 LEU A CD1   1 
ATOM   2224 C CD2   . LEU A 1 293 ? 39.664 11.087  32.487 1.00 24.61  ?  293 LEU A CD2   1 
ATOM   2225 N N     . TYR A 1 294 ? 43.490 10.085  28.923 1.00 29.19  ?  294 TYR A N     1 
ATOM   2226 C CA    . TYR A 1 294 ? 44.526 10.707  28.105 1.00 28.08  ?  294 TYR A CA    1 
ATOM   2227 C C     . TYR A 1 294 ? 44.757 9.959   26.805 1.00 32.05  ?  294 TYR A C     1 
ATOM   2228 O O     . TYR A 1 294 ? 45.268 10.538  25.836 1.00 31.75  ?  294 TYR A O     1 
ATOM   2229 C CB    . TYR A 1 294 ? 45.839 10.745  28.844 1.00 29.70  ?  294 TYR A CB    1 
ATOM   2230 C CG    . TYR A 1 294 ? 46.101 11.898  29.750 1.00 30.25  ?  294 TYR A CG    1 
ATOM   2231 C CD1   . TYR A 1 294 ? 46.147 13.196  29.269 1.00 29.49  ?  294 TYR A CD1   1 
ATOM   2232 C CD2   . TYR A 1 294 ? 46.428 11.675  31.085 1.00 29.97  ?  294 TYR A CD2   1 
ATOM   2233 C CE1   . TYR A 1 294 ? 46.461 14.265  30.115 1.00 30.04  ?  294 TYR A CE1   1 
ATOM   2234 C CE2   . TYR A 1 294 ? 46.748 12.719  31.928 1.00 29.84  ?  294 TYR A CE2   1 
ATOM   2235 C CZ    . TYR A 1 294 ? 46.757 14.020  31.444 1.00 33.93  ?  294 TYR A CZ    1 
ATOM   2236 O OH    . TYR A 1 294 ? 47.058 15.076  32.291 1.00 33.09  ?  294 TYR A OH    1 
ATOM   2237 N N     . ALA A 1 295 ? 44.451 8.666   26.772 1.00 33.99  ?  295 ALA A N     1 
ATOM   2238 C CA    . ALA A 1 295 ? 44.644 7.876   25.563 1.00 33.81  ?  295 ALA A CA    1 
ATOM   2239 C C     . ALA A 1 295 ? 43.369 7.753   24.745 1.00 31.69  ?  295 ALA A C     1 
ATOM   2240 O O     . ALA A 1 295 ? 43.320 6.933   23.826 1.00 31.69  ?  295 ALA A O     1 
ATOM   2241 C CB    . ALA A 1 295 ? 45.180 6.485   25.905 1.00 30.90  ?  295 ALA A CB    1 
ATOM   2242 N N     . ASN A 1 296 ? 42.338 8.537   25.054 1.00 29.88  ?  296 ASN A N     1 
ATOM   2243 C CA    . ASN A 1 296 ? 41.106 8.480   24.277 1.00 29.18  ?  296 ASN A CA    1 
ATOM   2244 C C     . ASN A 1 296 ? 40.416 9.840   24.244 1.00 28.90  ?  296 ASN A C     1 
ATOM   2245 O O     . ASN A 1 296 ? 39.205 9.933   24.436 1.00 30.43  ?  296 ASN A O     1 
ATOM   2246 C CB    . ASN A 1 296 ? 40.154 7.418   24.828 1.00 27.08  ?  296 ASN A CB    1 
ATOM   2247 C CG    . ASN A 1 296 ? 40.683 5.989   24.667 1.00 32.11  ?  296 ASN A CG    1 
ATOM   2248 O OD1   . ASN A 1 296 ? 40.462 5.355   23.635 1.00 36.74  ?  296 ASN A OD1   1 
ATOM   2249 N ND2   . ASN A 1 296 ? 41.362 5.473   25.695 1.00 25.71  ?  296 ASN A ND2   1 
ATOM   2250 N N     . THR A 1 297 ? 41.175 10.926  24.011 1.00 27.96  ?  297 THR A N     1 
ATOM   2251 C CA    . THR A 1 297 ? 40.560 12.242  23.757 1.00 29.34  ?  297 THR A CA    1 
ATOM   2252 C C     . THR A 1 297 ? 39.860 12.183  22.409 1.00 27.58  ?  297 THR A C     1 
ATOM   2253 O O     . THR A 1 297 ? 40.519 12.036  21.379 1.00 29.77  ?  297 THR A O     1 
ATOM   2254 C CB    . THR A 1 297 ? 41.588 13.379  23.766 1.00 29.13  ?  297 THR A CB    1 
ATOM   2255 O OG1   . THR A 1 297 ? 42.652 13.059  24.658 1.00 32.72  ?  297 THR A OG1   1 
ATOM   2256 C CG2   . THR A 1 297 ? 40.969 14.705  24.217 1.00 23.85  ?  297 THR A CG2   1 
ATOM   2257 N N     . VAL A 1 298 ? 38.532 12.267  22.409 1.00 25.64  ?  298 VAL A N     1 
ATOM   2258 C CA    . VAL A 1 298 ? 37.733 12.170  21.191 1.00 27.21  ?  298 VAL A CA    1 
ATOM   2259 C C     . VAL A 1 298 ? 37.229 13.562  20.821 1.00 25.48  ?  298 VAL A C     1 
ATOM   2260 O O     . VAL A 1 298 ? 36.465 14.172  21.577 1.00 28.63  ?  298 VAL A O     1 
ATOM   2261 C CB    . VAL A 1 298 ? 36.573 11.179  21.360 1.00 23.38  ?  298 VAL A CB    1 
ATOM   2262 C CG1   . VAL A 1 298 ? 35.632 11.266  20.186 1.00 23.76  ?  298 VAL A CG1   1 
ATOM   2263 C CG2   . VAL A 1 298 ? 37.105 9.793   21.430 1.00 24.20  ?  298 VAL A CG2   1 
ATOM   2264 N N     . LEU A 1 299 ? 37.640 14.061  19.655 1.00 25.05  ?  299 LEU A N     1 
ATOM   2265 C CA    . LEU A 1 299 ? 37.133 15.337  19.144 1.00 27.98  ?  299 LEU A CA    1 
ATOM   2266 C C     . LEU A 1 299 ? 35.774 15.120  18.462 1.00 26.57  ?  299 LEU A C     1 
ATOM   2267 O O     . LEU A 1 299 ? 35.534 14.078  17.846 1.00 24.71  ?  299 LEU A O     1 
ATOM   2268 C CB    . LEU A 1 299 ? 38.151 15.985  18.176 1.00 25.27  ?  299 LEU A CB    1 
ATOM   2269 C CG    . LEU A 1 299 ? 39.508 16.565  18.645 1.00 20.92  ?  299 LEU A CG    1 
ATOM   2270 C CD1   . LEU A 1 299 ? 39.914 17.777  17.884 1.00 20.57  ?  299 LEU A CD1   1 
ATOM   2271 C CD2   . LEU A 1 299 ? 39.549 16.886  20.112 1.00 22.85  ?  299 LEU A CD2   1 
ATOM   2272 N N     . SER A 1 300 ? 34.872 16.096  18.592 1.00 27.30  ?  300 SER A N     1 
ATOM   2273 C CA    . SER A 1 300 ? 33.494 15.917  18.143 1.00 25.17  ?  300 SER A CA    1 
ATOM   2274 C C     . SER A 1 300 ? 32.826 17.269  17.856 1.00 27.69  ?  300 SER A C     1 
ATOM   2275 O O     . SER A 1 300 ? 33.002 18.244  18.600 1.00 24.78  ?  300 SER A O     1 
ATOM   2276 C CB    . SER A 1 300 ? 32.723 15.111  19.205 1.00 29.48  ?  300 SER A CB    1 
ATOM   2277 O OG    . SER A 1 300 ? 31.350 15.437  19.315 1.00 33.36  ?  300 SER A OG    1 
ATOM   2278 N N     . GLY A 1 301 ? 32.077 17.328  16.760 1.00 27.03  ?  301 GLY A N     1 
ATOM   2279 C CA    . GLY A 1 301 ? 31.231 18.467  16.474 1.00 25.42  ?  301 GLY A CA    1 
ATOM   2280 C C     . GLY A 1 301 ? 31.811 19.377  15.405 1.00 27.78  ?  301 GLY A C     1 
ATOM   2281 O O     . GLY A 1 301 ? 32.995 19.315  15.050 1.00 26.97  ?  301 GLY A O     1 
ATOM   2282 N N     . GLY A 1 302 ? 30.943 20.271  14.918 1.00 26.19  ?  302 GLY A N     1 
ATOM   2283 C CA    . GLY A 1 302 ? 31.293 21.079  13.761 1.00 28.65  ?  302 GLY A CA    1 
ATOM   2284 C C     . GLY A 1 302 ? 32.569 21.886  13.938 1.00 31.64  ?  302 GLY A C     1 
ATOM   2285 O O     . GLY A 1 302 ? 33.358 22.033  13.000 1.00 29.47  ?  302 GLY A O     1 
ATOM   2286 N N     . THR A 1 303 ? 32.787 22.434  15.138 1.00 29.19  ?  303 THR A N     1 
ATOM   2287 C CA    . THR A 1 303 ? 33.926 23.307  15.372 1.00 27.25  ?  303 THR A CA    1 
ATOM   2288 C C     . THR A 1 303 ? 35.239 22.551  15.595 1.00 28.86  ?  303 THR A C     1 
ATOM   2289 O O     . THR A 1 303 ? 36.296 23.180  15.534 1.00 30.36  ?  303 THR A O     1 
ATOM   2290 C CB    . THR A 1 303 ? 33.605 24.237  16.542 1.00 25.39  ?  303 THR A CB    1 
ATOM   2291 O OG1   . THR A 1 303 ? 32.529 25.075  16.147 1.00 30.28  ?  303 THR A OG1   1 
ATOM   2292 C CG2   . THR A 1 303 ? 34.801 25.113  16.956 1.00 21.30  ?  303 THR A CG2   1 
ATOM   2293 N N     . THR A 1 304 ? 35.222 21.233  15.823 1.00 25.37  ?  304 THR A N     1 
ATOM   2294 C CA    . THR A 1 304 ? 36.489 20.504  15.790 1.00 29.68  ?  304 THR A CA    1 
ATOM   2295 C C     . THR A 1 304 ? 36.934 20.167  14.366 1.00 31.26  ?  304 THR A C     1 
ATOM   2296 O O     . THR A 1 304 ? 38.006 19.577  14.188 1.00 35.32  ?  304 THR A O     1 
ATOM   2297 C CB    . THR A 1 304 ? 36.425 19.203  16.639 1.00 27.29  ?  304 THR A CB    1 
ATOM   2298 O OG1   . THR A 1 304 ? 35.659 18.193  15.974 1.00 25.66  ?  304 THR A OG1   1 
ATOM   2299 C CG2   . THR A 1 304 ? 35.813 19.451  18.005 1.00 26.30  ?  304 THR A CG2   1 
ATOM   2300 N N     . MET A 1 305 ? 36.154 20.548  13.358 1.00 26.95  ?  305 MET A N     1 
ATOM   2301 C CA    . MET A 1 305 ? 36.320 20.202  11.954 1.00 29.38  ?  305 MET A CA    1 
ATOM   2302 C C     . MET A 1 305 ? 37.454 20.963  11.236 1.00 34.35  ?  305 MET A C     1 
ATOM   2303 O O     . MET A 1 305 ? 37.620 20.777  10.024 1.00 39.10  ?  305 MET A O     1 
ATOM   2304 C CB    . MET A 1 305 ? 34.996 20.472  11.238 1.00 32.65  ?  305 MET A CB    1 
ATOM   2305 C CG    . MET A 1 305 ? 34.027 19.305  11.173 1.00 36.30  ?  305 MET A CG    1 
ATOM   2306 S SD    . MET A 1 305 ? 34.778 17.731  10.750 1.00 46.89  ?  305 MET A SD    1 
ATOM   2307 C CE    . MET A 1 305 ? 34.314 17.636  9.020  1.00 35.40  ?  305 MET A CE    1 
ATOM   2308 N N     . TYR A 1 306 ? 38.218 21.817  11.915 1.00 33.77  ?  306 TYR A N     1 
ATOM   2309 C CA    . TYR A 1 306 ? 39.283 22.591  11.274 1.00 34.05  ?  306 TYR A CA    1 
ATOM   2310 C C     . TYR A 1 306 ? 40.483 21.696  10.968 1.00 33.33  ?  306 TYR A C     1 
ATOM   2311 O O     . TYR A 1 306 ? 40.965 20.975  11.858 1.00 32.69  ?  306 TYR A O     1 
ATOM   2312 C CB    . TYR A 1 306 ? 39.751 23.754  12.169 1.00 31.55  ?  306 TYR A CB    1 
ATOM   2313 C CG    . TYR A 1 306 ? 38.717 24.808  12.428 1.00 30.63  ?  306 TYR A CG    1 
ATOM   2314 C CD1   . TYR A 1 306 ? 38.364 25.719  11.442 1.00 31.16  ?  306 TYR A CD1   1 
ATOM   2315 C CD2   . TYR A 1 306 ? 38.090 24.893  13.661 1.00 30.43  ?  306 TYR A CD2   1 
ATOM   2316 C CE1   . TYR A 1 306 ? 37.407 26.680  11.664 1.00 31.24  ?  306 TYR A CE1   1 
ATOM   2317 C CE2   . TYR A 1 306 ? 37.132 25.851  13.901 1.00 30.88  ?  306 TYR A CE2   1 
ATOM   2318 C CZ    . TYR A 1 306 ? 36.794 26.746  12.897 1.00 32.61  ?  306 TYR A CZ    1 
ATOM   2319 O OH    . TYR A 1 306 ? 35.829 27.699  13.130 1.00 35.78  ?  306 TYR A OH    1 
ATOM   2320 N N     . PRO A 1 307 ? 41.000 21.724  9.745  1.00 31.46  ?  307 PRO A N     1 
ATOM   2321 C CA    . PRO A 1 307 ? 42.282 21.068  9.486  1.00 24.74  ?  307 PRO A CA    1 
ATOM   2322 C C     . PRO A 1 307 ? 43.314 21.520  10.507 1.00 26.44  ?  307 PRO A C     1 
ATOM   2323 O O     . PRO A 1 307 ? 43.365 22.695  10.880 1.00 31.59  ?  307 PRO A O     1 
ATOM   2324 C CB    . PRO A 1 307 ? 42.635 21.535  8.073  1.00 20.83  ?  307 PRO A CB    1 
ATOM   2325 C CG    . PRO A 1 307 ? 41.361 21.913  7.456  1.00 24.15  ?  307 PRO A CG    1 
ATOM   2326 C CD    . PRO A 1 307 ? 40.452 22.383  8.546  1.00 28.14  ?  307 PRO A CD    1 
ATOM   2327 N N     . GLY A 1 308 ? 44.134 20.571  10.960 1.00 22.22  ?  308 GLY A N     1 
ATOM   2328 C CA    . GLY A 1 308 ? 45.224 20.806  11.870 1.00 22.07  ?  308 GLY A CA    1 
ATOM   2329 C C     . GLY A 1 308 ? 44.875 20.709  13.345 1.00 29.77  ?  308 GLY A C     1 
ATOM   2330 O O     . GLY A 1 308 ? 45.783 20.844  14.192 1.00 27.45  ?  308 GLY A O     1 
ATOM   2331 N N     . ILE A 1 309 ? 43.599 20.479  13.690 1.00 26.00  ?  309 ILE A N     1 
ATOM   2332 C CA    . ILE A 1 309 ? 43.222 20.626  15.089 1.00 27.87  ?  309 ILE A CA    1 
ATOM   2333 C C     . ILE A 1 309 ? 43.666 19.425  15.905 1.00 29.74  ?  309 ILE A C     1 
ATOM   2334 O O     . ILE A 1 309 ? 44.104 19.574  17.050 1.00 28.66  ?  309 ILE A O     1 
ATOM   2335 C CB    . ILE A 1 309 ? 41.722 20.861  15.244 1.00 28.98  ?  309 ILE A CB    1 
ATOM   2336 C CG1   . ILE A 1 309 ? 41.449 21.144  16.720 1.00 26.76  ?  309 ILE A CG1   1 
ATOM   2337 C CG2   . ILE A 1 309 ? 40.953 19.638  14.802 1.00 28.24  ?  309 ILE A CG2   1 
ATOM   2338 C CD1   . ILE A 1 309 ? 40.465 22.254  16.964 1.00 26.55  ?  309 ILE A CD1   1 
ATOM   2339 N N     . ALA A 1 310 ? 43.539 18.220  15.344 1.00 29.02  ?  310 ALA A N     1 
ATOM   2340 C CA    . ALA A 1 310 ? 44.048 17.029  16.015 1.00 27.90  ?  310 ALA A CA    1 
ATOM   2341 C C     . ALA A 1 310 ? 45.509 17.212  16.429 1.00 35.70  ?  310 ALA A C     1 
ATOM   2342 O O     . ALA A 1 310 ? 45.871 16.960  17.590 1.00 38.08  ?  310 ALA A O     1 
ATOM   2343 C CB    . ALA A 1 310 ? 43.891 15.811  15.107 1.00 19.83  ?  310 ALA A CB    1 
ATOM   2344 N N     . ASP A 1 311 ? 46.366 17.677  15.494 1.00 33.57  ?  311 ASP A N     1 
ATOM   2345 C CA    . ASP A 1 311 ? 47.810 17.711  15.741 1.00 27.93  ?  311 ASP A CA    1 
ATOM   2346 C C     . ASP A 1 311 ? 48.184 18.759  16.770 1.00 29.45  ?  311 ASP A C     1 
ATOM   2347 O O     . ASP A 1 311 ? 49.185 18.610  17.479 1.00 30.45  ?  311 ASP A O     1 
ATOM   2348 C CB    . ASP A 1 311 ? 48.578 17.984  14.450 1.00 30.10  ?  311 ASP A CB    1 
ATOM   2349 C CG    . ASP A 1 311 ? 48.770 16.724  13.558 1.00 43.45  ?  311 ASP A CG    1 
ATOM   2350 O OD1   . ASP A 1 311 ? 48.453 15.550  13.965 1.00 36.49  ?  311 ASP A OD1   1 
ATOM   2351 O OD2   . ASP A 1 311 ? 49.257 16.942  12.415 1.00 44.46  -1 311 ASP A OD2   1 
ATOM   2352 N N     . ARG A 1 312 ? 47.419 19.835  16.861 1.00 31.02  ?  312 ARG A N     1 
ATOM   2353 C CA    . ARG A 1 312 ? 47.782 20.824  17.851 1.00 26.25  ?  312 ARG A CA    1 
ATOM   2354 C C     . ARG A 1 312 ? 47.291 20.408  19.223 1.00 30.80  ?  312 ARG A C     1 
ATOM   2355 O O     . ARG A 1 312 ? 47.960 20.664  20.232 1.00 33.16  ?  312 ARG A O     1 
ATOM   2356 C CB    . ARG A 1 312 ? 47.229 22.182  17.466 1.00 24.99  ?  312 ARG A CB    1 
ATOM   2357 C CG    . ARG A 1 312 ? 48.158 23.299  17.914 1.00 28.54  ?  312 ARG A CG    1 
ATOM   2358 C CD    . ARG A 1 312 ? 47.352 24.240  18.736 1.00 30.43  ?  312 ARG A CD    1 
ATOM   2359 N NE    . ARG A 1 312 ? 48.076 25.396  19.259 1.00 31.83  ?  312 ARG A NE    1 
ATOM   2360 C CZ    . ARG A 1 312 ? 48.063 26.608  18.697 1.00 32.48  ?  312 ARG A CZ    1 
ATOM   2361 N NH1   . ARG A 1 312 ? 47.406 26.824  17.552 1.00 25.75  ?  312 ARG A NH1   1 
ATOM   2362 N NH2   . ARG A 1 312 ? 48.738 27.607  19.263 1.00 39.16  ?  312 ARG A NH2   1 
ATOM   2363 N N     . MET A 1 313 ? 46.121 19.772  19.279 1.00 28.38  ?  313 MET A N     1 
ATOM   2364 C CA    . MET A 1 313 ? 45.668 19.195  20.533 1.00 30.29  ?  313 MET A CA    1 
ATOM   2365 C C     . MET A 1 313 ? 46.691 18.207  21.072 1.00 36.24  ?  313 MET A C     1 
ATOM   2366 O O     . MET A 1 313 ? 47.011 18.226  22.271 1.00 36.12  ?  313 MET A O     1 
ATOM   2367 C CB    . MET A 1 313 ? 44.316 18.525  20.335 1.00 32.36  ?  313 MET A CB    1 
ATOM   2368 C CG    . MET A 1 313 ? 43.148 19.436  20.652 1.00 35.62  ?  313 MET A CG    1 
ATOM   2369 S SD    . MET A 1 313 ? 43.227 19.895  22.400 1.00 45.26  ?  313 MET A SD    1 
ATOM   2370 C CE    . MET A 1 313 ? 41.545 20.437  22.693 1.00 36.84  ?  313 MET A CE    1 
ATOM   2371 N N     . GLN A 1 314 ? 47.211 17.333  20.195 1.00 31.99  ?  314 GLN A N     1 
ATOM   2372 C CA    . GLN A 1 314 ? 48.317 16.449  20.553 1.00 34.88  ?  314 GLN A CA    1 
ATOM   2373 C C     . GLN A 1 314 ? 49.459 17.218  21.220 1.00 36.48  ?  314 GLN A C     1 
ATOM   2374 O O     . GLN A 1 314 ? 49.953 16.840  22.293 1.00 36.66  ?  314 GLN A O     1 
ATOM   2375 C CB    . GLN A 1 314 ? 48.821 15.733  19.295 1.00 35.93  ?  314 GLN A CB    1 
ATOM   2376 C CG    . GLN A 1 314 ? 50.087 14.924  19.490 1.00 34.47  ?  314 GLN A CG    1 
ATOM   2377 C CD    . GLN A 1 314 ? 49.795 13.668  20.265 1.00 39.72  ?  314 GLN A CD    1 
ATOM   2378 O OE1   . GLN A 1 314 ? 48.708 13.100  20.129 1.00 39.83  ?  314 GLN A OE1   1 
ATOM   2379 N NE2   . GLN A 1 314 ? 50.739 13.240  21.114 1.00 39.41  ?  314 GLN A NE2   1 
ATOM   2380 N N     . LYS A 1 315 ? 49.892 18.305  20.588 1.00 34.51  ?  315 LYS A N     1 
ATOM   2381 C CA    . LYS A 1 315 ? 51.055 19.038  21.067 1.00 33.29  ?  315 LYS A CA    1 
ATOM   2382 C C     . LYS A 1 315 ? 50.770 19.692  22.416 1.00 34.35  ?  315 LYS A C     1 
ATOM   2383 O O     . LYS A 1 315 ? 51.582 19.587  23.345 1.00 34.65  ?  315 LYS A O     1 
ATOM   2384 C CB    . LYS A 1 315 ? 51.472 20.063  20.001 1.00 33.09  ?  315 LYS A CB    1 
ATOM   2385 C CG    . LYS A 1 315 ? 52.661 20.952  20.326 1.00 31.34  ?  315 LYS A CG    1 
ATOM   2386 C CD    . LYS A 1 315 ? 52.533 22.343  19.676 1.00 33.33  ?  315 LYS A CD    1 
ATOM   2387 C CE    . LYS A 1 315 ? 53.670 22.635  18.715 1.00 33.90  ?  315 LYS A CE    1 
ATOM   2388 N NZ    . LYS A 1 315 ? 55.023 22.533  19.365 1.00 41.25  ?  315 LYS A NZ    1 
ATOM   2389 N N     . GLU A 1 316 ? 49.603 20.339  22.553 1.00 30.36  ?  316 GLU A N     1 
ATOM   2390 C CA    . GLU A 1 316 ? 49.354 21.195  23.710 1.00 28.67  ?  316 GLU A CA    1 
ATOM   2391 C C     . GLU A 1 316 ? 49.096 20.376  24.961 1.00 32.92  ?  316 GLU A C     1 
ATOM   2392 O O     . GLU A 1 316 ? 49.572 20.733  26.044 1.00 35.01  ?  316 GLU A O     1 
ATOM   2393 C CB    . GLU A 1 316 ? 48.165 22.124  23.450 1.00 35.32  ?  316 GLU A CB    1 
ATOM   2394 C CG    . GLU A 1 316 ? 48.319 23.100  22.286 1.00 35.00  ?  316 GLU A CG    1 
ATOM   2395 C CD    . GLU A 1 316 ? 49.383 24.187  22.538 1.00 44.98  ?  316 GLU A CD    1 
ATOM   2396 O OE1   . GLU A 1 316 ? 49.849 24.339  23.709 1.00 45.45  ?  316 GLU A OE1   1 
ATOM   2397 O OE2   . GLU A 1 316 ? 49.749 24.891  21.557 1.00 45.79  -1 316 GLU A OE2   1 
ATOM   2398 N N     . ILE A 1 317 ? 48.320 19.287  24.838 1.00 36.01  ?  317 ILE A N     1 
ATOM   2399 C CA    . ILE A 1 317 ? 48.106 18.373  25.960 1.00 32.13  ?  317 ILE A CA    1 
ATOM   2400 C C     . ILE A 1 317 ? 49.403 17.677  26.334 1.00 31.07  ?  317 ILE A C     1 
ATOM   2401 O O     . ILE A 1 317 ? 49.646 17.389  27.508 1.00 33.88  ?  317 ILE A O     1 
ATOM   2402 C CB    . ILE A 1 317 ? 47.008 17.334  25.644 1.00 34.63  ?  317 ILE A CB    1 
ATOM   2403 C CG1   . ILE A 1 317 ? 45.667 17.986  25.299 1.00 29.75  ?  317 ILE A CG1   1 
ATOM   2404 C CG2   . ILE A 1 317 ? 46.835 16.400  26.817 1.00 25.29  ?  317 ILE A CG2   1 
ATOM   2405 C CD1   . ILE A 1 317 ? 45.128 18.872  26.376 1.00 29.37  ?  317 ILE A CD1   1 
ATOM   2406 N N     . THR A 1 318 ? 50.241 17.348  25.347 1.00 32.41  ?  318 THR A N     1 
ATOM   2407 C CA    . THR A 1 318 ? 51.530 16.760  25.689 1.00 31.48  ?  318 THR A CA    1 
ATOM   2408 C C     . THR A 1 318 ? 52.351 17.718  26.547 1.00 30.16  ?  318 THR A C     1 
ATOM   2409 O O     . THR A 1 318 ? 53.110 17.279  27.420 1.00 27.39  ?  318 THR A O     1 
ATOM   2410 C CB    . THR A 1 318 ? 52.272 16.356  24.415 1.00 28.95  ?  318 THR A CB    1 
ATOM   2411 O OG1   . THR A 1 318 ? 51.765 15.098  23.965 1.00 31.51  ?  318 THR A OG1   1 
ATOM   2412 C CG2   . THR A 1 318 ? 53.773 16.226  24.667 1.00 21.02  ?  318 THR A CG2   1 
ATOM   2413 N N     . ALA A 1 319 ? 52.171 19.028  26.337 1.00 30.67  ?  319 ALA A N     1 
ATOM   2414 C CA    . ALA A 1 319 ? 52.850 20.056  27.126 1.00 35.23  ?  319 ALA A CA    1 
ATOM   2415 C C     . ALA A 1 319 ? 52.268 20.215  28.537 1.00 38.12  ?  319 ALA A C     1 
ATOM   2416 O O     . ALA A 1 319 ? 52.990 20.630  29.452 1.00 37.84  ?  319 ALA A O     1 
ATOM   2417 C CB    . ALA A 1 319 ? 52.790 21.394  26.397 1.00 28.74  ?  319 ALA A CB    1 
ATOM   2418 N N     . LEU A 1 320 ? 50.981 19.901  28.735 1.00 35.18  ?  320 LEU A N     1 
ATOM   2419 C CA    . LEU A 1 320 ? 50.337 20.008  30.039 1.00 32.16  ?  320 LEU A CA    1 
ATOM   2420 C C     . LEU A 1 320 ? 50.428 18.733  30.869 1.00 32.39  ?  320 LEU A C     1 
ATOM   2421 O O     . LEU A 1 320 ? 50.350 18.802  32.105 1.00 31.06  ?  320 LEU A O     1 
ATOM   2422 C CB    . LEU A 1 320 ? 48.862 20.382  29.863 1.00 30.25  ?  320 LEU A CB    1 
ATOM   2423 C CG    . LEU A 1 320 ? 48.566 21.659  29.074 1.00 30.55  ?  320 LEU A CG    1 
ATOM   2424 C CD1   . LEU A 1 320 ? 47.112 21.738  28.711 1.00 28.62  ?  320 LEU A CD1   1 
ATOM   2425 C CD2   . LEU A 1 320 ? 48.963 22.894  29.842 1.00 27.26  ?  320 LEU A CD2   1 
ATOM   2426 N N     . ALA A 1 321 ? 50.606 17.590  30.232 1.00 31.91  ?  321 ALA A N     1 
ATOM   2427 C CA    . ALA A 1 321 ? 50.538 16.322  30.935 1.00 37.24  ?  321 ALA A CA    1 
ATOM   2428 C C     . ALA A 1 321 ? 51.920 15.873  31.399 1.00 41.16  ?  321 ALA A C     1 
ATOM   2429 O O     . ALA A 1 321 ? 52.946 16.384  30.928 1.00 41.11  ?  321 ALA A O     1 
ATOM   2430 C CB    . ALA A 1 321 ? 49.909 15.256  30.034 1.00 34.36  ?  321 ALA A CB    1 
ATOM   2431 N N     . PRO A 1 322 ? 51.963 14.921  32.341 1.00 40.83  ?  322 PRO A N     1 
ATOM   2432 C CA    . PRO A 1 322 ? 53.244 14.342  32.782 1.00 39.15  ?  322 PRO A CA    1 
ATOM   2433 C C     . PRO A 1 322 ? 54.000 13.672  31.642 1.00 44.35  ?  322 PRO A C     1 
ATOM   2434 O O     . PRO A 1 322 ? 53.406 13.092  30.730 1.00 45.96  ?  322 PRO A O     1 
ATOM   2435 C CB    . PRO A 1 322 ? 52.832 13.313  33.836 1.00 39.36  ?  322 PRO A CB    1 
ATOM   2436 C CG    . PRO A 1 322 ? 51.436 13.666  34.224 1.00 36.93  ?  322 PRO A CG    1 
ATOM   2437 C CD    . PRO A 1 322 ? 50.807 14.435  33.112 1.00 34.93  ?  322 PRO A CD    1 
ATOM   2438 N N     . SER A 1 323 ? 55.335 13.701  31.752 1.00 46.94  ?  323 SER A N     1 
ATOM   2439 C CA    . SER A 1 323 ? 56.249 13.528  30.627 1.00 46.13  ?  323 SER A CA    1 
ATOM   2440 C C     . SER A 1 323 ? 56.250 12.123  30.046 1.00 43.92  ?  323 SER A C     1 
ATOM   2441 O O     . SER A 1 323 ? 56.858 11.917  28.989 1.00 45.66  ?  323 SER A O     1 
ATOM   2442 C CB    . SER A 1 323 ? 57.675 13.907  31.047 1.00 47.83  ?  323 SER A CB    1 
ATOM   2443 O OG    . SER A 1 323 ? 57.936 13.549  32.394 1.00 53.38  ?  323 SER A OG    1 
ATOM   2444 N N     . THR A 1 324 ? 55.603 11.165  30.701 1.00 43.88  ?  324 THR A N     1 
ATOM   2445 C CA    . THR A 1 324 ? 55.530 9.791   30.217 1.00 45.36  ?  324 THR A CA    1 
ATOM   2446 C C     . THR A 1 324 ? 54.144 9.400   29.723 1.00 44.90  ?  324 THR A C     1 
ATOM   2447 O O     . THR A 1 324 ? 53.964 8.269   29.256 1.00 46.40  ?  324 THR A O     1 
ATOM   2448 C CB    . THR A 1 324 ? 55.949 8.822   31.328 1.00 44.63  ?  324 THR A CB    1 
ATOM   2449 O OG1   . THR A 1 324 ? 56.012 9.525   32.578 1.00 47.93  ?  324 THR A OG1   1 
ATOM   2450 C CG2   . THR A 1 324 ? 57.291 8.223   31.026 1.00 46.04  ?  324 THR A CG2   1 
ATOM   2451 N N     . MET A 1 325 ? 53.161 10.288  29.842 1.00 41.37  ?  325 MET A N     1 
ATOM   2452 C CA    . MET A 1 325 ? 51.774 9.955   29.561 1.00 36.65  ?  325 MET A CA    1 
ATOM   2453 C C     . MET A 1 325 ? 51.586 9.681   28.082 1.00 34.42  ?  325 MET A C     1 
ATOM   2454 O O     . MET A 1 325 ? 51.841 10.553  27.253 1.00 32.13  ?  325 MET A O     1 
ATOM   2455 C CB    . MET A 1 325 ? 50.875 11.107  29.990 1.00 39.73  ?  325 MET A CB    1 
ATOM   2456 C CG    . MET A 1 325 ? 49.401 10.734  30.190 1.00 39.07  ?  325 MET A CG    1 
ATOM   2457 S SD    . MET A 1 325 ? 49.066 9.737   31.671 1.00 46.53  ?  325 MET A SD    1 
ATOM   2458 C CE    . MET A 1 325 ? 49.606 8.096   31.231 1.00 46.32  ?  325 MET A CE    1 
ATOM   2459 N N     . LYS A 1 326 ? 51.129 8.477   27.750 1.00 38.47  ?  326 LYS A N     1 
ATOM   2460 C CA    . LYS A 1 326 ? 50.753 8.148   26.380 1.00 31.45  ?  326 LYS A CA    1 
ATOM   2461 C C     . LYS A 1 326 ? 49.459 8.878   26.035 1.00 29.40  ?  326 LYS A C     1 
ATOM   2462 O O     . LYS A 1 326 ? 48.460 8.741   26.744 1.00 31.76  ?  326 LYS A O     1 
ATOM   2463 C CB    . LYS A 1 326 ? 50.605 6.633   26.242 1.00 34.06  ?  326 LYS A CB    1 
ATOM   2464 C CG    . LYS A 1 326 ? 50.049 6.134   24.904 1.00 46.25  ?  326 LYS A CG    1 
ATOM   2465 C CD    . LYS A 1 326 ? 50.006 4.588   24.832 1.00 55.74  ?  326 LYS A CD    1 
ATOM   2466 C CE    . LYS A 1 326 ? 49.178 4.067   23.649 1.00 61.34  ?  326 LYS A CE    1 
ATOM   2467 N NZ    . LYS A 1 326 ? 47.909 4.832   23.435 1.00 59.83  ?  326 LYS A NZ    1 
ATOM   2468 N N     . ILE A 1 327 ? 49.478 9.660   24.953 1.00 32.12  ?  327 ILE A N     1 
ATOM   2469 C CA    . ILE A 1 327 ? 48.401 10.587  24.594 1.00 33.49  ?  327 ILE A CA    1 
ATOM   2470 C C     . ILE A 1 327 ? 47.914 10.306  23.174 1.00 33.23  ?  327 ILE A C     1 
ATOM   2471 O O     . ILE A 1 327 ? 48.718 10.254  22.237 1.00 31.58  ?  327 ILE A O     1 
ATOM   2472 C CB    . ILE A 1 327 ? 48.864 12.050  24.697 1.00 27.81  ?  327 ILE A CB    1 
ATOM   2473 C CG1   . ILE A 1 327 ? 49.450 12.304  26.079 1.00 25.53  ?  327 ILE A CG1   1 
ATOM   2474 C CG2   . ILE A 1 327 ? 47.740 12.980  24.299 1.00 25.13  ?  327 ILE A CG2   1 
ATOM   2475 C CD1   . ILE A 1 327 ? 48.887 13.463  26.756 1.00 30.86  ?  327 ILE A CD1   1 
ATOM   2476 N N     . LYS A 1 328 ? 46.601 10.155  23.008 1.00 30.80  ?  328 LYS A N     1 
ATOM   2477 C CA    . LYS A 1 328 ? 46.013 9.956   21.689 1.00 34.47  ?  328 LYS A CA    1 
ATOM   2478 C C     . LYS A 1 328 ? 44.880 10.961  21.497 1.00 35.79  ?  328 LYS A C     1 
ATOM   2479 O O     . LYS A 1 328 ? 44.007 11.086  22.359 1.00 34.26  ?  328 LYS A O     1 
ATOM   2480 C CB    . LYS A 1 328 ? 45.505 8.508   21.531 1.00 36.60  ?  328 LYS A CB    1 
ATOM   2481 C CG    . LYS A 1 328 ? 45.516 7.921   20.112 1.00 43.09  ?  328 LYS A CG    1 
ATOM   2482 C CD    . LYS A 1 328 ? 44.812 6.528   20.072 1.00 46.21  ?  328 LYS A CD    1 
ATOM   2483 C CE    . LYS A 1 328 ? 45.472 5.535   19.108 1.00 45.11  ?  328 LYS A CE    1 
ATOM   2484 N NZ    . LYS A 1 328 ? 44.735 5.321   17.821 1.00 43.29  ?  328 LYS A NZ    1 
ATOM   2485 N N     . ILE A 1 329 ? 44.901 11.696  20.390 1.00 32.49  ?  329 ILE A N     1 
ATOM   2486 C CA    . ILE A 1 329 ? 43.759 12.503  19.982 1.00 30.54  ?  329 ILE A CA    1 
ATOM   2487 C C     . ILE A 1 329 ? 43.062 11.762  18.846 1.00 33.16  ?  329 ILE A C     1 
ATOM   2488 O O     . ILE A 1 329 ? 43.671 11.513  17.798 1.00 38.01  ?  329 ILE A O     1 
ATOM   2489 C CB    . ILE A 1 329 ? 44.189 13.907  19.541 1.00 30.91  ?  329 ILE A CB    1 
ATOM   2490 C CG1   . ILE A 1 329 ? 45.020 14.614  20.633 1.00 29.09  ?  329 ILE A CG1   1 
ATOM   2491 C CG2   . ILE A 1 329 ? 42.982 14.703  19.075 1.00 28.81  ?  329 ILE A CG2   1 
ATOM   2492 C CD1   . ILE A 1 329 ? 44.479 14.469  21.998 1.00 30.00  ?  329 ILE A CD1   1 
ATOM   2493 N N     . ILE A 1 330 ? 41.797 11.394  19.045 1.00 30.01  ?  330 ILE A N     1 
ATOM   2494 C CA    . ILE A 1 330 ? 41.007 10.683  18.039 1.00 30.70  ?  330 ILE A CA    1 
ATOM   2495 C C     . ILE A 1 330 ? 40.054 11.691  17.402 1.00 32.83  ?  330 ILE A C     1 
ATOM   2496 O O     . ILE A 1 330 ? 39.115 12.157  18.057 1.00 34.79  ?  330 ILE A O     1 
ATOM   2497 C CB    . ILE A 1 330 ? 40.224 9.508   18.649 1.00 29.33  ?  330 ILE A CB    1 
ATOM   2498 C CG1   . ILE A 1 330 ? 41.141 8.449   19.258 1.00 31.66  ?  330 ILE A CG1   1 
ATOM   2499 C CG2   . ILE A 1 330 ? 39.424 8.821   17.596 1.00 27.79  ?  330 ILE A CG2   1 
ATOM   2500 C CD1   . ILE A 1 330 ? 41.667 8.796   20.620 1.00 33.68  ?  330 ILE A CD1   1 
ATOM   2501 N N     . ALA A 1 331 ? 40.260 12.034  16.127 1.00 29.65  ?  331 ALA A N     1 
ATOM   2502 C CA    . ALA A 1 331 ? 39.374 12.971  15.422 1.00 31.77  ?  331 ALA A CA    1 
ATOM   2503 C C     . ALA A 1 331 ? 38.837 12.295  14.171 1.00 31.55  ?  331 ALA A C     1 
ATOM   2504 O O     . ALA A 1 331 ? 39.420 12.428  13.083 1.00 29.69  ?  331 ALA A O     1 
ATOM   2505 C CB    . ALA A 1 331 ? 40.073 14.287  15.064 1.00 28.23  ?  331 ALA A CB    1 
ATOM   2506 N N     . PRO A 1 332 ? 37.725 11.572  14.284 1.00 35.69  ?  332 PRO A N     1 
ATOM   2507 C CA    . PRO A 1 332 ? 37.119 10.904  13.121 1.00 33.41  ?  332 PRO A CA    1 
ATOM   2508 C C     . PRO A 1 332 ? 36.874 11.869  11.974 1.00 40.98  ?  332 PRO A C     1 
ATOM   2509 O O     . PRO A 1 332 ? 36.741 13.091  12.178 1.00 38.17  ?  332 PRO A O     1 
ATOM   2510 C CB    . PRO A 1 332 ? 35.799 10.371  13.688 1.00 30.51  ?  332 PRO A CB    1 
ATOM   2511 C CG    . PRO A 1 332 ? 36.102 10.141  15.107 1.00 29.14  ?  332 PRO A CG    1 
ATOM   2512 C CD    . PRO A 1 332 ? 37.034 11.221  15.538 1.00 29.34  ?  332 PRO A CD    1 
ATOM   2513 N N     . PRO A 1 333 ? 36.827 11.358  10.736 1.00 42.52  ?  333 PRO A N     1 
ATOM   2514 C CA    . PRO A 1 333 ? 36.406 12.204  9.611  1.00 41.06  ?  333 PRO A CA    1 
ATOM   2515 C C     . PRO A 1 333 ? 34.923 12.550  9.637  1.00 44.65  ?  333 PRO A C     1 
ATOM   2516 O O     . PRO A 1 333 ? 34.535 13.610  9.127  1.00 48.85  ?  333 PRO A O     1 
ATOM   2517 C CB    . PRO A 1 333 ? 36.775 11.357  8.384  1.00 43.67  ?  333 PRO A CB    1 
ATOM   2518 C CG    . PRO A 1 333 ? 36.819 9.948   8.895  1.00 45.66  ?  333 PRO A CG    1 
ATOM   2519 C CD    . PRO A 1 333 ? 37.327 10.044  10.291 1.00 44.19  ?  333 PRO A CD    1 
ATOM   2520 N N     . GLU A 1 334 ? 34.081 11.703  10.221 1.00 41.97  ?  334 GLU A N     1 
ATOM   2521 C CA    . GLU A 1 334 ? 32.649 11.937  10.253 1.00 44.37  ?  334 GLU A CA    1 
ATOM   2522 C C     . GLU A 1 334 ? 32.203 12.763  11.460 1.00 46.18  ?  334 GLU A C     1 
ATOM   2523 O O     . GLU A 1 334 ? 30.991 12.844  11.726 1.00 47.98  ?  334 GLU A O     1 
ATOM   2524 C CB    . GLU A 1 334 ? 31.905 10.599  10.230 1.00 51.73  ?  334 GLU A CB    1 
ATOM   2525 C CG    . GLU A 1 334 ? 32.197 9.699   11.432 1.00 60.47  ?  334 GLU A CG    1 
ATOM   2526 C CD    . GLU A 1 334 ? 31.807 8.227   11.201 1.00 76.47  ?  334 GLU A CD    1 
ATOM   2527 O OE1   . GLU A 1 334 ? 32.148 7.375   12.057 1.00 80.23  ?  334 GLU A OE1   1 
ATOM   2528 O OE2   . GLU A 1 334 ? 31.162 7.918   10.167 1.00 78.30  -1 334 GLU A OE2   1 
ATOM   2529 N N     . ARG A 1 335 ? 33.142 13.413  12.167 1.00 42.64  ?  335 ARG A N     1 
ATOM   2530 C CA    . ARG A 1 335 ? 32.869 13.969  13.498 1.00 39.18  ?  335 ARG A CA    1 
ATOM   2531 C C     . ARG A 1 335 ? 31.989 15.220  13.467 1.00 37.87  ?  335 ARG A C     1 
ATOM   2532 O O     . ARG A 1 335 ? 31.552 15.669  14.534 1.00 36.29  ?  335 ARG A O     1 
ATOM   2533 C CB    . ARG A 1 335 ? 34.194 14.252  14.238 1.00 33.66  ?  335 ARG A CB    1 
ATOM   2534 C CG    . ARG A 1 335 ? 34.995 15.444  13.727 1.00 34.32  ?  335 ARG A CG    1 
ATOM   2535 C CD    . ARG A 1 335 ? 36.440 15.425  14.184 1.00 29.70  ?  335 ARG A CD    1 
ATOM   2536 N NE    . ARG A 1 335 ? 37.191 16.579  13.685 1.00 30.28  ?  335 ARG A NE    1 
ATOM   2537 C CZ    . ARG A 1 335 ? 38.092 16.540  12.704 1.00 29.34  ?  335 ARG A CZ    1 
ATOM   2538 N NH1   . ARG A 1 335 ? 38.377 15.392  12.088 1.00 26.44  ?  335 ARG A NH1   1 
ATOM   2539 N NH2   . ARG A 1 335 ? 38.714 17.658  12.342 1.00 26.08  ?  335 ARG A NH2   1 
ATOM   2540 N N     . LYS A 1 336 ? 31.731 15.796  12.287 1.00 38.36  ?  336 LYS A N     1 
ATOM   2541 C CA    . LYS A 1 336 ? 30.722 16.847  12.171 1.00 35.65  ?  336 LYS A CA    1 
ATOM   2542 C C     . LYS A 1 336 ? 29.383 16.377  12.723 1.00 34.96  ?  336 LYS A C     1 
ATOM   2543 O O     . LYS A 1 336 ? 28.700 17.121  13.431 1.00 36.75  ?  336 LYS A O     1 
ATOM   2544 C CB    . LYS A 1 336 ? 30.590 17.265  10.702 1.00 38.15  ?  336 LYS A CB    1 
ATOM   2545 C CG    . LYS A 1 336 ? 29.664 18.429  10.391 1.00 36.41  ?  336 LYS A CG    1 
ATOM   2546 C CD    . LYS A 1 336 ? 30.171 19.162  9.143  1.00 42.38  ?  336 LYS A CD    1 
ATOM   2547 C CE    . LYS A 1 336 ? 29.063 19.891  8.400  1.00 50.41  ?  336 LYS A CE    1 
ATOM   2548 N NZ    . LYS A 1 336 ? 29.332 21.338  8.142  1.00 48.35  ?  336 LYS A NZ    1 
ATOM   2549 N N     . TYR A 1 337 ? 28.995 15.141  12.418 1.00 33.95  ?  337 TYR A N     1 
ATOM   2550 C CA    . TYR A 1 337 ? 27.724 14.588  12.863 1.00 36.37  ?  337 TYR A CA    1 
ATOM   2551 C C     . TYR A 1 337 ? 27.915 13.299  13.650 1.00 34.09  ?  337 TYR A C     1 
ATOM   2552 O O     . TYR A 1 337 ? 27.093 12.389  13.548 1.00 30.44  ?  337 TYR A O     1 
ATOM   2553 C CB    . TYR A 1 337 ? 26.782 14.302  11.689 1.00 39.36  ?  337 TYR A CB    1 
ATOM   2554 C CG    . TYR A 1 337 ? 26.578 15.427  10.710 1.00 40.96  ?  337 TYR A CG    1 
ATOM   2555 C CD1   . TYR A 1 337 ? 26.865 15.263  9.353  1.00 39.80  ?  337 TYR A CD1   1 
ATOM   2556 C CD2   . TYR A 1 337 ? 26.093 16.658  11.135 1.00 41.50  ?  337 TYR A CD2   1 
ATOM   2557 C CE1   . TYR A 1 337 ? 26.674 16.302  8.441  1.00 41.36  ?  337 TYR A CE1   1 
ATOM   2558 C CE2   . TYR A 1 337 ? 25.899 17.702  10.232 1.00 43.33  ?  337 TYR A CE2   1 
ATOM   2559 C CZ    . TYR A 1 337 ? 26.189 17.520  8.888  1.00 45.80  ?  337 TYR A CZ    1 
ATOM   2560 O OH    . TYR A 1 337 ? 25.989 18.571  8.008  1.00 51.59  ?  337 TYR A OH    1 
ATOM   2561 N N     . SER A 1 338 ? 28.989 13.175  14.419 1.00 32.66  ?  338 SER A N     1 
ATOM   2562 C CA    . SER A 1 338 ? 29.179 11.883  15.051 1.00 27.34  ?  338 SER A CA    1 
ATOM   2563 C C     . SER A 1 338 ? 28.244 11.700  16.237 1.00 30.32  ?  338 SER A C     1 
ATOM   2564 O O     . SER A 1 338 ? 27.911 10.562  16.568 1.00 31.08  ?  338 SER A O     1 
ATOM   2565 C CB    . SER A 1 338 ? 30.625 11.698  15.465 1.00 30.12  ?  338 SER A CB    1 
ATOM   2566 O OG    . SER A 1 338 ? 31.041 12.776  16.282 1.00 37.52  ?  338 SER A OG    1 
ATOM   2567 N N     . VAL A 1 339 ? 27.787 12.788  16.875 1.00 29.84  ?  339 VAL A N     1 
ATOM   2568 C CA    . VAL A 1 339 ? 26.706 12.672  17.858 1.00 26.22  ?  339 VAL A CA    1 
ATOM   2569 C C     . VAL A 1 339 ? 25.536 11.902  17.254 1.00 29.60  ?  339 VAL A C     1 
ATOM   2570 O O     . VAL A 1 339 ? 25.148 10.827  17.739 1.00 27.03  ?  339 VAL A O     1 
ATOM   2571 C CB    . VAL A 1 339 ? 26.260 14.060  18.346 1.00 27.50  ?  339 VAL A CB    1 
ATOM   2572 C CG1   . VAL A 1 339 ? 24.921 13.978  19.061 1.00 23.24  ?  339 VAL A CG1   1 
ATOM   2573 C CG2   . VAL A 1 339 ? 27.298 14.650  19.261 1.00 30.80  ?  339 VAL A CG2   1 
ATOM   2574 N N     . TRP A 1 340 ? 24.968 12.450  16.170 1.00 29.82  ?  340 TRP A N     1 
ATOM   2575 C CA    . TRP A 1 340 ? 23.852 11.815  15.481 1.00 24.55  ?  340 TRP A CA    1 
ATOM   2576 C C     . TRP A 1 340 ? 24.186 10.396  15.023 1.00 25.95  ?  340 TRP A C     1 
ATOM   2577 O O     . TRP A 1 340 ? 23.340 9.497   15.079 1.00 25.08  ?  340 TRP A O     1 
ATOM   2578 C CB    . TRP A 1 340 ? 23.430 12.674  14.291 1.00 29.66  ?  340 TRP A CB    1 
ATOM   2579 C CG    . TRP A 1 340 ? 22.162 12.191  13.659 1.00 30.99  ?  340 TRP A CG    1 
ATOM   2580 C CD1   . TRP A 1 340 ? 20.895 12.653  13.904 1.00 28.06  ?  340 TRP A CD1   1 
ATOM   2581 C CD2   . TRP A 1 340 ? 22.025 11.127  12.704 1.00 29.84  ?  340 TRP A CD2   1 
ATOM   2582 N NE1   . TRP A 1 340 ? 19.984 11.945  13.160 1.00 29.68  ?  340 TRP A NE1   1 
ATOM   2583 C CE2   . TRP A 1 340 ? 20.644 11.005  12.411 1.00 30.60  ?  340 TRP A CE2   1 
ATOM   2584 C CE3   . TRP A 1 340 ? 22.932 10.279  12.056 1.00 30.57  ?  340 TRP A CE3   1 
ATOM   2585 C CZ2   . TRP A 1 340 ? 20.146 10.058  11.508 1.00 31.30  ?  340 TRP A CZ2   1 
ATOM   2586 C CZ3   . TRP A 1 340 ? 22.428 9.314   11.158 1.00 35.13  ?  340 TRP A CZ3   1 
ATOM   2587 C CH2   . TRP A 1 340 ? 21.049 9.218   10.896 1.00 34.73  ?  340 TRP A CH2   1 
ATOM   2588 N N     . ILE A 1 341 ? 25.400 10.170  14.543 1.00 25.76  ?  341 ILE A N     1 
ATOM   2589 C CA    . ILE A 1 341 ? 25.710 8.848   14.015 1.00 28.11  ?  341 ILE A CA    1 
ATOM   2590 C C     . ILE A 1 341 ? 25.746 7.828   15.144 1.00 31.33  ?  341 ILE A C     1 
ATOM   2591 O O     . ILE A 1 341 ? 25.208 6.717   15.019 1.00 34.00  ?  341 ILE A O     1 
ATOM   2592 C CB    . ILE A 1 341 ? 27.030 8.872   13.225 1.00 31.19  ?  341 ILE A CB    1 
ATOM   2593 C CG1   . ILE A 1 341 ? 26.883 9.736   11.975 1.00 30.71  ?  341 ILE A CG1   1 
ATOM   2594 C CG2   . ILE A 1 341 ? 27.455 7.460   12.849 1.00 32.10  ?  341 ILE A CG2   1 
ATOM   2595 C CD1   . ILE A 1 341 ? 28.179 10.100  11.363 1.00 36.98  ?  341 ILE A CD1   1 
ATOM   2596 N N     . GLY A 1 342 ? 26.381 8.182   16.264 1.00 27.92  ?  342 GLY A N     1 
ATOM   2597 C CA    . GLY A 1 342 ? 26.275 7.355   17.450 1.00 26.43  ?  342 GLY A CA    1 
ATOM   2598 C C     . GLY A 1 342 ? 24.841 7.148   17.886 1.00 27.80  ?  342 GLY A C     1 
ATOM   2599 O O     . GLY A 1 342 ? 24.491 6.084   18.397 1.00 27.01  ?  342 GLY A O     1 
ATOM   2600 N N     . GLY A 1 343 ? 23.991 8.157   17.692 1.00 25.76  ?  343 GLY A N     1 
ATOM   2601 C CA    . GLY A 1 343 ? 22.575 7.956   17.942 1.00 26.80  ?  343 GLY A CA    1 
ATOM   2602 C C     . GLY A 1 343 ? 21.968 6.927   17.009 1.00 26.73  ?  343 GLY A C     1 
ATOM   2603 O O     . GLY A 1 343 ? 21.272 6.015   17.446 1.00 25.10  ?  343 GLY A O     1 
ATOM   2604 N N     . SER A 1 344 ? 22.204 7.085   15.698 1.00 29.82  ?  344 SER A N     1 
ATOM   2605 C CA    . SER A 1 344 ? 21.744 6.107   14.715 1.00 25.65  ?  344 SER A CA    1 
ATOM   2606 C C     . SER A 1 344 ? 22.243 4.709   15.045 1.00 27.60  ?  344 SER A C     1 
ATOM   2607 O O     . SER A 1 344 ? 21.490 3.731   14.941 1.00 25.62  ?  344 SER A O     1 
ATOM   2608 C CB    . SER A 1 344 ? 22.210 6.512   13.320 1.00 27.10  ?  344 SER A CB    1 
ATOM   2609 O OG    . SER A 1 344 ? 21.775 5.577   12.348 1.00 30.14  ?  344 SER A OG    1 
ATOM   2610 N N     . ILE A 1 345 ? 23.521 4.594   15.419 1.00 25.45  ?  345 ILE A N     1 
ATOM   2611 C CA    . ILE A 1 345 ? 24.078 3.293   15.760 1.00 26.09  ?  345 ILE A CA    1 
ATOM   2612 C C     . ILE A 1 345 ? 23.315 2.696   16.927 1.00 30.32  ?  345 ILE A C     1 
ATOM   2613 O O     . ILE A 1 345 ? 22.806 1.574   16.852 1.00 34.72  ?  345 ILE A O     1 
ATOM   2614 C CB    . ILE A 1 345 ? 25.575 3.414   16.081 1.00 29.15  ?  345 ILE A CB    1 
ATOM   2615 C CG1   . ILE A 1 345 ? 26.354 3.883   14.854 1.00 33.17  ?  345 ILE A CG1   1 
ATOM   2616 C CG2   . ILE A 1 345 ? 26.111 2.089   16.583 1.00 29.81  ?  345 ILE A CG2   1 
ATOM   2617 C CD1   . ILE A 1 345 ? 27.808 3.532   14.900 1.00 35.55  ?  345 ILE A CD1   1 
ATOM   2618 N N     . LEU A 1 346 ? 23.221 3.449   18.021 1.00 27.36  ?  346 LEU A N     1 
ATOM   2619 C CA    . LEU A 1 346 ? 22.546 2.988   19.224 1.00 28.32  ?  346 LEU A CA    1 
ATOM   2620 C C     . LEU A 1 346 ? 21.109 2.535   18.949 1.00 31.44  ?  346 LEU A C     1 
ATOM   2621 O O     . LEU A 1 346 ? 20.701 1.436   19.350 1.00 29.58  ?  346 LEU A O     1 
ATOM   2622 C CB    . LEU A 1 346 ? 22.576 4.118   20.251 1.00 27.75  ?  346 LEU A CB    1 
ATOM   2623 C CG    . LEU A 1 346 ? 22.054 3.794   21.630 1.00 27.09  ?  346 LEU A CG    1 
ATOM   2624 C CD1   . LEU A 1 346 ? 22.884 2.666   22.198 1.00 27.31  ?  346 LEU A CD1   1 
ATOM   2625 C CD2   . LEU A 1 346 ? 22.138 5.028   22.483 1.00 25.52  ?  346 LEU A CD2   1 
ATOM   2626 N N     . ALA A 1 347 ? 20.315 3.384   18.283 1.00 31.13  ?  347 ALA A N     1 
ATOM   2627 C CA    . ALA A 1 347 ? 18.908 3.061   18.072 1.00 29.99  ?  347 ALA A CA    1 
ATOM   2628 C C     . ALA A 1 347 ? 18.755 1.742   17.331 1.00 35.09  ?  347 ALA A C     1 
ATOM   2629 O O     . ALA A 1 347 ? 17.746 1.051   17.500 1.00 39.61  ?  347 ALA A O     1 
ATOM   2630 C CB    . ALA A 1 347 ? 18.205 4.195   17.322 1.00 22.94  ?  347 ALA A CB    1 
ATOM   2631 N N     . SER A 1 348 ? 19.776 1.349   16.562 1.00 37.88  ?  348 SER A N     1 
ATOM   2632 C CA    . SER A 1 348 ? 19.714 0.201   15.659 1.00 35.60  ?  348 SER A CA    1 
ATOM   2633 C C     . SER A 1 348 ? 20.053 -1.111  16.346 1.00 38.05  ?  348 SER A C     1 
ATOM   2634 O O     . SER A 1 348 ? 19.492 -2.149  15.981 1.00 39.23  ?  348 SER A O     1 
ATOM   2635 C CB    . SER A 1 348 ? 20.686 0.405   14.500 1.00 34.64  ?  348 SER A CB    1 
ATOM   2636 O OG    . SER A 1 348 ? 20.062 1.171   13.497 1.00 44.43  ?  348 SER A OG    1 
ATOM   2637 N N     . LEU A 1 349 ? 20.997 -1.089  17.294 1.00 38.04  ?  349 LEU A N     1 
ATOM   2638 C CA    . LEU A 1 349 ? 21.329 -2.259  18.089 1.00 33.84  ?  349 LEU A CA    1 
ATOM   2639 C C     . LEU A 1 349 ? 20.055 -2.947  18.541 1.00 37.65  ?  349 LEU A C     1 
ATOM   2640 O O     . LEU A 1 349 ? 19.087 -2.289  18.931 1.00 36.71  ?  349 LEU A O     1 
ATOM   2641 C CB    . LEU A 1 349 ? 22.142 -1.835  19.307 1.00 36.22  ?  349 LEU A CB    1 
ATOM   2642 C CG    . LEU A 1 349 ? 23.577 -1.360  19.093 1.00 37.01  ?  349 LEU A CG    1 
ATOM   2643 C CD1   . LEU A 1 349 ? 24.226 -1.070  20.436 1.00 33.80  ?  349 LEU A CD1   1 
ATOM   2644 C CD2   . LEU A 1 349 ? 24.374 -2.385  18.302 1.00 32.86  ?  349 LEU A CD2   1 
ATOM   2645 N N     . SER A 1 350 ? 20.035 -4.281  18.475 1.00 42.22  ?  350 SER A N     1 
ATOM   2646 C CA    . SER A 1 350 ? 18.827 -4.982  18.917 1.00 42.40  ?  350 SER A CA    1 
ATOM   2647 C C     . SER A 1 350 ? 18.674 -4.877  20.432 1.00 38.60  ?  350 SER A C     1 
ATOM   2648 O O     . SER A 1 350 ? 17.594 -4.536  20.936 1.00 36.13  ?  350 SER A O     1 
ATOM   2649 C CB    . SER A 1 350 ? 18.826 -6.446  18.440 1.00 38.11  ?  350 SER A CB    1 
ATOM   2650 O OG    . SER A 1 350 ? 19.975 -7.162  18.841 1.00 36.69  ?  350 SER A OG    1 
ATOM   2651 N N     . THR A 1 351 ? 19.765 -5.111  21.169 1.00 37.65  ?  351 THR A N     1 
ATOM   2652 C CA    . THR A 1 351 ? 19.740 -4.987  22.618 1.00 36.66  ?  351 THR A CA    1 
ATOM   2653 C C     . THR A 1 351 ? 19.165 -3.645  23.070 1.00 38.34  ?  351 THR A C     1 
ATOM   2654 O O     . THR A 1 351 ? 18.552 -3.555  24.142 1.00 37.02  ?  351 THR A O     1 
ATOM   2655 C CB    . THR A 1 351 ? 21.149 -5.201  23.154 1.00 35.56  ?  351 THR A CB    1 
ATOM   2656 O OG1   . THR A 1 351 ? 21.190 -4.878  24.545 1.00 37.94  ?  351 THR A OG1   1 
ATOM   2657 C CG2   . THR A 1 351 ? 22.104 -4.326  22.417 1.00 38.43  ?  351 THR A CG2   1 
ATOM   2658 N N     . PHE A 1 352 ? 19.316 -2.595  22.264 1.00 39.30  ?  352 PHE A N     1 
ATOM   2659 C CA    . PHE A 1 352 ? 18.668 -1.336  22.610 1.00 35.45  ?  352 PHE A CA    1 
ATOM   2660 C C     . PHE A 1 352 ? 17.147 -1.431  22.572 1.00 36.44  ?  352 PHE A C     1 
ATOM   2661 O O     . PHE A 1 352 ? 16.472 -0.509  23.036 1.00 36.11  ?  352 PHE A O     1 
ATOM   2662 C CB    . PHE A 1 352 ? 19.144 -0.228  21.678 1.00 32.05  ?  352 PHE A CB    1 
ATOM   2663 C CG    . PHE A 1 352 ? 18.760 1.152   22.127 1.00 35.03  ?  352 PHE A CG    1 
ATOM   2664 C CD1   . PHE A 1 352 ? 19.402 1.754   23.202 1.00 29.59  ?  352 PHE A CD1   1 
ATOM   2665 C CD2   . PHE A 1 352 ? 17.739 1.856   21.465 1.00 37.49  ?  352 PHE A CD2   1 
ATOM   2666 C CE1   . PHE A 1 352 ? 19.049 3.025   23.610 1.00 28.77  ?  352 PHE A CE1   1 
ATOM   2667 C CE2   . PHE A 1 352 ? 17.361 3.140   21.863 1.00 32.53  ?  352 PHE A CE2   1 
ATOM   2668 C CZ    . PHE A 1 352 ? 18.027 3.730   22.942 1.00 34.15  ?  352 PHE A CZ    1 
ATOM   2669 N N     . GLN A 1 353 ? 16.581 -2.501  22.026 1.00 35.01  ?  353 GLN A N     1 
ATOM   2670 C CA    . GLN A 1 353 ? 15.131 -2.579  22.023 1.00 36.73  ?  353 GLN A CA    1 
ATOM   2671 C C     . GLN A 1 353 ? 14.567 -2.862  23.413 1.00 43.82  ?  353 GLN A C     1 
ATOM   2672 O O     . GLN A 1 353 ? 13.363 -2.684  23.616 1.00 48.83  ?  353 GLN A O     1 
ATOM   2673 C CB    . GLN A 1 353 ? 14.678 -3.646  21.034 1.00 38.36  ?  353 GLN A CB    1 
ATOM   2674 C CG    . GLN A 1 353 ? 14.178 -3.133  19.677 1.00 40.23  ?  353 GLN A CG    1 
ATOM   2675 C CD    . GLN A 1 353 ? 14.951 -1.940  19.127 1.00 43.32  ?  353 GLN A CD    1 
ATOM   2676 O OE1   . GLN A 1 353 ? 16.186 -1.965  19.030 1.00 42.33  ?  353 GLN A OE1   1 
ATOM   2677 N NE2   . GLN A 1 353 ? 14.219 -0.903  18.706 1.00 45.77  ?  353 GLN A NE2   1 
ATOM   2678 N N     . GLN A 1 354 ? 15.404 -3.273  24.371 1.00 40.65  ?  354 GLN A N     1 
ATOM   2679 C CA    . GLN A 1 354 ? 15.001 -3.488  25.756 1.00 42.79  ?  354 GLN A CA    1 
ATOM   2680 C C     . GLN A 1 354 ? 15.141 -2.243  26.624 1.00 42.30  ?  354 GLN A C     1 
ATOM   2681 O O     . GLN A 1 354 ? 14.817 -2.307  27.817 1.00 43.93  ?  354 GLN A O     1 
ATOM   2682 C CB    . GLN A 1 354 ? 15.825 -4.626  26.387 1.00 45.51  ?  354 GLN A CB    1 
ATOM   2683 C CG    . GLN A 1 354 ? 15.551 -6.008  25.817 1.00 52.67  ?  354 GLN A CG    1 
ATOM   2684 C CD    . GLN A 1 354 ? 14.095 -6.190  25.373 1.00 62.05  ?  354 GLN A CD    1 
ATOM   2685 O OE1   . GLN A 1 354 ? 13.168 -6.153  26.202 1.00 62.36  ?  354 GLN A OE1   1 
ATOM   2686 N NE2   . GLN A 1 354 ? 13.887 -6.390  24.060 1.00 55.95  ?  354 GLN A NE2   1 
ATOM   2687 N N     . MET A 1 355 ? 15.608 -1.116  26.058 1.00 39.48  ?  355 MET A N     1 
ATOM   2688 C CA    . MET A 1 355 ? 15.924 0.080   26.825 1.00 35.09  ?  355 MET A CA    1 
ATOM   2689 C C     . MET A 1 355 ? 15.091 1.311   26.509 1.00 37.90  ?  355 MET A C     1 
ATOM   2690 O O     . MET A 1 355 ? 15.268 2.323   27.192 1.00 40.24  ?  355 MET A O     1 
ATOM   2691 C CB    . MET A 1 355 ? 17.391 0.462   26.637 1.00 33.22  ?  355 MET A CB    1 
ATOM   2692 C CG    . MET A 1 355 ? 18.263 -0.733  26.456 1.00 39.88  ?  355 MET A CG    1 
ATOM   2693 S SD    . MET A 1 355 ? 19.986 -0.270  26.355 1.00 49.71  ?  355 MET A SD    1 
ATOM   2694 C CE    . MET A 1 355 ? 20.617 -1.751  25.582 1.00 42.53  ?  355 MET A CE    1 
ATOM   2695 N N     . TRP A 1 356 ? 14.230 1.287   25.491 1.00 39.16  ?  356 TRP A N     1 
ATOM   2696 C CA    . TRP A 1 356 ? 13.312 2.402   25.279 1.00 35.39  ?  356 TRP A CA    1 
ATOM   2697 C C     . TRP A 1 356 ? 12.455 2.617   26.521 1.00 38.59  ?  356 TRP A C     1 
ATOM   2698 O O     . TRP A 1 356 ? 12.118 1.667   27.236 1.00 45.02  ?  356 TRP A O     1 
ATOM   2699 C CB    . TRP A 1 356 ? 12.392 2.133   24.089 1.00 35.21  ?  356 TRP A CB    1 
ATOM   2700 C CG    . TRP A 1 356 ? 13.045 2.091   22.749 1.00 35.39  ?  356 TRP A CG    1 
ATOM   2701 C CD1   . TRP A 1 356 ? 13.302 0.979   21.988 1.00 32.49  ?  356 TRP A CD1   1 
ATOM   2702 C CD2   . TRP A 1 356 ? 13.484 3.213   21.979 1.00 32.85  ?  356 TRP A CD2   1 
ATOM   2703 N NE1   . TRP A 1 356 ? 13.885 1.344   20.803 1.00 31.91  ?  356 TRP A NE1   1 
ATOM   2704 C CE2   . TRP A 1 356 ? 14.020 2.712   20.779 1.00 36.11  ?  356 TRP A CE2   1 
ATOM   2705 C CE3   . TRP A 1 356 ? 13.492 4.591   22.194 1.00 30.53  ?  356 TRP A CE3   1 
ATOM   2706 C CZ2   . TRP A 1 356 ? 14.563 3.551   19.802 1.00 33.63  ?  356 TRP A CZ2   1 
ATOM   2707 C CZ3   . TRP A 1 356 ? 14.029 5.414   21.223 1.00 29.73  ?  356 TRP A CZ3   1 
ATOM   2708 C CH2   . TRP A 1 356 ? 14.558 4.892   20.048 1.00 28.76  ?  356 TRP A CH2   1 
ATOM   2709 N N     . ILE A 1 357 ? 12.114 3.877   26.786 1.00 36.28  ?  357 ILE A N     1 
ATOM   2710 C CA    . ILE A 1 357 ? 10.977 4.196   27.646 1.00 39.17  ?  357 ILE A CA    1 
ATOM   2711 C C     . ILE A 1 357 ? 9.716  4.018   26.808 1.00 39.46  ?  357 ILE A C     1 
ATOM   2712 O O     . ILE A 1 357 ? 9.569  4.686   25.778 1.00 37.11  ?  357 ILE A O     1 
ATOM   2713 C CB    . ILE A 1 357 ? 11.059 5.636   28.177 1.00 37.36  ?  357 ILE A CB    1 
ATOM   2714 C CG1   . ILE A 1 357 ? 12.400 5.944   28.825 1.00 35.09  ?  357 ILE A CG1   1 
ATOM   2715 C CG2   . ILE A 1 357 ? 9.927  5.923   29.128 1.00 35.15  ?  357 ILE A CG2   1 
ATOM   2716 C CD1   . ILE A 1 357 ? 12.406 7.330   29.448 1.00 30.00  ?  357 ILE A CD1   1 
ATOM   2717 N N     . SER A 1 358 ? 8.792  3.153   27.266 1.00 45.54  ?  358 SER A N     1 
ATOM   2718 C CA    . SER A 1 358 ? 7.552  2.807   26.551 1.00 43.81  ?  358 SER A CA    1 
ATOM   2719 C C     . SER A 1 358 ? 6.389  3.722   26.934 1.00 47.77  ?  358 SER A C     1 
ATOM   2720 O O     . SER A 1 358 ? 6.311  4.219   28.058 1.00 46.00  ?  358 SER A O     1 
ATOM   2721 C CB    . SER A 1 358 ? 7.128  1.372   26.858 1.00 43.73  ?  358 SER A CB    1 
ATOM   2722 O OG    . SER A 1 358 ? 8.159  0.468   26.542 1.00 48.55  ?  358 SER A OG    1 
ATOM   2723 N N     . LYS A 1 359 ? 5.452  3.910   25.997 1.00 50.62  ?  359 LYS A N     1 
ATOM   2724 C CA    . LYS A 1 359 ? 4.200  4.581   26.346 1.00 48.56  ?  359 LYS A CA    1 
ATOM   2725 C C     . LYS A 1 359 ? 3.588  3.973   27.594 1.00 51.42  ?  359 LYS A C     1 
ATOM   2726 O O     . LYS A 1 359 ? 3.126  4.693   28.477 1.00 53.54  ?  359 LYS A O     1 
ATOM   2727 C CB    . LYS A 1 359 ? 3.202  4.511   25.197 1.00 46.25  ?  359 LYS A CB    1 
ATOM   2728 C CG    . LYS A 1 359 ? 1.966  5.391   25.386 1.00 57.39  ?  359 LYS A CG    1 
ATOM   2729 C CD    . LYS A 1 359 ? 2.293  6.899   25.329 1.00 57.64  ?  359 LYS A CD    1 
ATOM   2730 C CE    . LYS A 1 359 ? 1.070  7.798   25.665 1.00 59.92  ?  359 LYS A CE    1 
ATOM   2731 N NZ    . LYS A 1 359 ? 0.499  7.632   27.049 1.00 63.66  ?  359 LYS A NZ    1 
ATOM   2732 N N     . GLN A 1 360 ? 3.583  2.645   27.693 1.00 53.37  ?  360 GLN A N     1 
ATOM   2733 C CA    . GLN A 1 360 ? 3.076  2.016   28.906 1.00 59.43  ?  360 GLN A CA    1 
ATOM   2734 C C     . GLN A 1 360 ? 3.816  2.540   30.136 1.00 64.20  ?  360 GLN A C     1 
ATOM   2735 O O     . GLN A 1 360 ? 3.202  3.081   31.062 1.00 67.41  ?  360 GLN A O     1 
ATOM   2736 C CB    . GLN A 1 360 ? 3.187  0.489   28.801 1.00 69.93  ?  360 GLN A CB    1 
ATOM   2737 C CG    . GLN A 1 360 ? 2.138  -0.302  29.634 1.00 88.31  ?  360 GLN A CG    1 
ATOM   2738 C CD    . GLN A 1 360 ? 2.637  -0.716  31.032 1.00 97.34  ?  360 GLN A CD    1 
ATOM   2739 O OE1   . GLN A 1 360 ? 3.668  -1.400  31.169 1.00 97.53  ?  360 GLN A OE1   1 
ATOM   2740 N NE2   . GLN A 1 360 ? 1.894  -0.311  32.073 1.00 92.86  ?  360 GLN A NE2   1 
ATOM   2741 N N     . GLU A 1 361 ? 5.146  2.416   30.152 1.00 58.76  ?  361 GLU A N     1 
ATOM   2742 C CA    . GLU A 1 361 ? 5.896  2.782   31.347 1.00 55.56  ?  361 GLU A CA    1 
ATOM   2743 C C     . GLU A 1 361 ? 5.686  4.247   31.728 1.00 54.49  ?  361 GLU A C     1 
ATOM   2744 O O     . GLU A 1 361 ? 5.842  4.620   32.896 1.00 53.52  ?  361 GLU A O     1 
ATOM   2745 C CB    . GLU A 1 361 ? 7.378  2.495   31.126 1.00 55.87  ?  361 GLU A CB    1 
ATOM   2746 C CG    . GLU A 1 361 ? 7.877  1.126   31.621 1.00 62.91  ?  361 GLU A CG    1 
ATOM   2747 C CD    . GLU A 1 361 ? 9.242  0.740   31.008 1.00 70.68  ?  361 GLU A CD    1 
ATOM   2748 O OE1   . GLU A 1 361 ? 10.071 0.117   31.731 1.00 70.78  ?  361 GLU A OE1   1 
ATOM   2749 O OE2   . GLU A 1 361 ? 9.480  1.059   29.806 1.00 64.12  -1 361 GLU A OE2   1 
ATOM   2750 N N     . TYR A 1 362 ? 5.308  5.085   30.768 1.00 55.96  ?  362 TYR A N     1 
ATOM   2751 C CA    . TYR A 1 362 ? 5.265  6.520   31.012 1.00 50.59  ?  362 TYR A CA    1 
ATOM   2752 C C     . TYR A 1 362 ? 4.027  6.926   31.815 1.00 57.04  ?  362 TYR A C     1 
ATOM   2753 O O     . TYR A 1 362 ? 4.138  7.662   32.804 1.00 54.08  ?  362 TYR A O     1 
ATOM   2754 C CB    . TYR A 1 362 ? 5.327  7.276   29.687 1.00 40.25  ?  362 TYR A CB    1 
ATOM   2755 C CG    . TYR A 1 362 ? 5.058  8.723   29.875 1.00 38.75  ?  362 TYR A CG    1 
ATOM   2756 C CD1   . TYR A 1 362 ? 6.035  9.565   30.388 1.00 41.62  ?  362 TYR A CD1   1 
ATOM   2757 C CD2   . TYR A 1 362 ? 3.818  9.258   29.584 1.00 40.62  ?  362 TYR A CD2   1 
ATOM   2758 C CE1   . TYR A 1 362 ? 5.793  10.917  30.580 1.00 39.66  ?  362 TYR A CE1   1 
ATOM   2759 C CE2   . TYR A 1 362 ? 3.560  10.611  29.768 1.00 36.02  ?  362 TYR A CE2   1 
ATOM   2760 C CZ    . TYR A 1 362 ? 4.549  11.428  30.265 1.00 38.61  ?  362 TYR A CZ    1 
ATOM   2761 O OH    . TYR A 1 362 ? 4.296  12.758  30.459 1.00 40.62  ?  362 TYR A OH    1 
ATOM   2762 N N     . ASP A 1 363 ? 2.832  6.478   31.414 1.00 58.85  ?  363 ASP A N     1 
ATOM   2763 C CA    . ASP A 1 363 ? 1.672  6.859   32.214 1.00 62.27  ?  363 ASP A CA    1 
ATOM   2764 C C     . ASP A 1 363 ? 1.481  5.967   33.434 1.00 58.99  ?  363 ASP A C     1 
ATOM   2765 O O     . ASP A 1 363 ? 0.568  6.226   34.226 1.00 58.90  ?  363 ASP A O     1 
ATOM   2766 C CB    . ASP A 1 363 ? 0.394  6.904   31.360 1.00 73.02  ?  363 ASP A CB    1 
ATOM   2767 C CG    . ASP A 1 363 ? 0.438  5.966   30.179 1.00 73.31  ?  363 ASP A CG    1 
ATOM   2768 O OD1   . ASP A 1 363 ? 0.026  6.381   29.062 1.00 77.19  ?  363 ASP A OD1   1 
ATOM   2769 O OD2   . ASP A 1 363 ? 0.864  4.808   30.381 1.00 75.99  -1 363 ASP A OD2   1 
ATOM   2770 N N     . GLU A 1 364 ? 2.341  4.958   33.620 1.00 57.22  ?  364 GLU A N     1 
ATOM   2771 C CA    . GLU A 1 364 ? 2.460  4.295   34.914 1.00 58.10  ?  364 GLU A CA    1 
ATOM   2772 C C     . GLU A 1 364 ? 3.241  5.129   35.927 1.00 53.47  ?  364 GLU A C     1 
ATOM   2773 O O     . GLU A 1 364 ? 2.918  5.094   37.115 1.00 55.57  ?  364 GLU A O     1 
ATOM   2774 C CB    . GLU A 1 364 ? 3.111  2.922   34.747 1.00 61.73  ?  364 GLU A CB    1 
ATOM   2775 C CG    . GLU A 1 364 ? 3.717  2.311   36.017 1.00 64.37  ?  364 GLU A CG    1 
ATOM   2776 C CD    . GLU A 1 364 ? 4.443  0.971   35.741 1.00 82.88  ?  364 GLU A CD    1 
ATOM   2777 O OE1   . GLU A 1 364 ? 5.277  0.528   36.580 1.00 81.26  ?  364 GLU A OE1   1 
ATOM   2778 O OE2   . GLU A 1 364 ? 4.180  0.359   34.672 1.00 89.56  -1 364 GLU A OE2   1 
ATOM   2779 N N     . SER A 1 365 ? 4.247  5.900   35.497 1.00 54.14  ?  365 SER A N     1 
ATOM   2780 C CA    . SER A 1 365 ? 5.024  6.709   36.434 1.00 50.29  ?  365 SER A CA    1 
ATOM   2781 C C     . SER A 1 365 ? 5.284  8.153   36.010 1.00 47.35  ?  365 SER A C     1 
ATOM   2782 O O     . SER A 1 365 ? 5.849  8.909   36.808 1.00 49.85  ?  365 SER A O     1 
ATOM   2783 C CB    . SER A 1 365 ? 6.378  6.049   36.721 1.00 55.74  ?  365 SER A CB    1 
ATOM   2784 O OG    . SER A 1 365 ? 7.068  6.743   37.758 1.00 68.32  ?  365 SER A OG    1 
ATOM   2785 N N     . GLY A 1 366 ? 4.901  8.567   34.809 1.00 47.04  ?  366 GLY A N     1 
ATOM   2786 C CA    . GLY A 1 366 ? 5.052  9.948   34.415 1.00 42.50  ?  366 GLY A CA    1 
ATOM   2787 C C     . GLY A 1 366 ? 6.468  10.328  34.027 1.00 45.00  ?  366 GLY A C     1 
ATOM   2788 O O     . GLY A 1 366 ? 7.370  9.486   33.939 1.00 44.83  ?  366 GLY A O     1 
ATOM   2789 N N     . PRO A 1 367 ? 6.696  11.620  33.800 1.00 41.68  ?  367 PRO A N     1 
ATOM   2790 C CA    . PRO A 1 367 ? 7.990  12.041  33.238 1.00 38.09  ?  367 PRO A CA    1 
ATOM   2791 C C     . PRO A 1 367 ? 9.201  11.674  34.088 1.00 39.40  ?  367 PRO A C     1 
ATOM   2792 O O     . PRO A 1 367 ? 10.281 11.462  33.530 1.00 42.36  ?  367 PRO A O     1 
ATOM   2793 C CB    . PRO A 1 367 ? 7.830  13.565  33.092 1.00 40.77  ?  367 PRO A CB    1 
ATOM   2794 C CG    . PRO A 1 367 ? 6.668  13.932  33.925 1.00 40.52  ?  367 PRO A CG    1 
ATOM   2795 C CD    . PRO A 1 367 ? 5.769  12.742  33.983 1.00 37.50  ?  367 PRO A CD    1 
ATOM   2796 N N     . SER A 1 368 ? 9.076  11.588  35.413 1.00 43.03  ?  368 SER A N     1 
ATOM   2797 C CA    . SER A 1 368 ? 10.230 11.236  36.239 1.00 40.23  ?  368 SER A CA    1 
ATOM   2798 C C     . SER A 1 368 ? 10.850 9.889   35.868 1.00 42.55  ?  368 SER A C     1 
ATOM   2799 O O     . SER A 1 368 ? 11.924 9.559   36.384 1.00 40.23  ?  368 SER A O     1 
ATOM   2800 C CB    . SER A 1 368 ? 9.835  11.206  37.717 1.00 40.87  ?  368 SER A CB    1 
ATOM   2801 O OG    . SER A 1 368 ? 9.413  9.895   38.101 1.00 49.71  ?  368 SER A OG    1 
ATOM   2802 N N     . ILE A 1 369 ? 10.195 9.094   35.014 1.00 40.73  ?  369 ILE A N     1 
ATOM   2803 C CA    . ILE A 1 369 ? 10.715 7.776   34.671 1.00 40.85  ?  369 ILE A CA    1 
ATOM   2804 C C     . ILE A 1 369 ? 12.057 7.899   33.963 1.00 41.04  ?  369 ILE A C     1 
ATOM   2805 O O     . ILE A 1 369 ? 12.941 7.043   34.125 1.00 37.83  ?  369 ILE A O     1 
ATOM   2806 C CB    . ILE A 1 369 ? 9.695  7.009   33.811 1.00 42.27  ?  369 ILE A CB    1 
ATOM   2807 C CG1   . ILE A 1 369 ? 10.004 5.513   33.847 1.00 38.28  ?  369 ILE A CG1   1 
ATOM   2808 C CG2   . ILE A 1 369 ? 9.667  7.559   32.378 1.00 34.43  ?  369 ILE A CG2   1 
ATOM   2809 C CD1   . ILE A 1 369 ? 9.458  4.784   32.666 1.00 42.30  ?  369 ILE A CD1   1 
ATOM   2810 N N     . VAL A 1 370 ? 12.231 8.967   33.174 1.00 39.87  ?  370 VAL A N     1 
ATOM   2811 C CA    . VAL A 1 370 ? 13.484 9.214   32.464 1.00 37.23  ?  370 VAL A CA    1 
ATOM   2812 C C     . VAL A 1 370 ? 14.687 9.048   33.385 1.00 37.00  ?  370 VAL A C     1 
ATOM   2813 O O     . VAL A 1 370 ? 15.758 8.641   32.930 1.00 37.09  ?  370 VAL A O     1 
ATOM   2814 C CB    . VAL A 1 370 ? 13.451 10.618  31.792 1.00 34.08  ?  370 VAL A CB    1 
ATOM   2815 C CG1   . VAL A 1 370 ? 13.744 11.749  32.812 1.00 30.13  ?  370 VAL A CG1   1 
ATOM   2816 C CG2   . VAL A 1 370 ? 14.352 10.676  30.524 1.00 21.40  ?  370 VAL A CG2   1 
ATOM   2817 N N     . HIS A 1 371 ? 14.544 9.342   34.690 1.00 39.30  ?  371 HIS A N     1 
ATOM   2818 C CA    . HIS A 1 371 ? 15.715 9.252   35.572 1.00 39.44  ?  371 HIS A CA    1 
ATOM   2819 C C     . HIS A 1 371 ? 16.060 7.823   35.889 1.00 38.98  ?  371 HIS A C     1 
ATOM   2820 O O     . HIS A 1 371 ? 17.214 7.530   36.210 1.00 42.21  ?  371 HIS A O     1 
ATOM   2821 C CB    . HIS A 1 371 ? 15.530 9.988   36.891 1.00 35.65  ?  371 HIS A CB    1 
ATOM   2822 C CG    . HIS A 1 371 ? 15.032 11.375  36.726 1.00 35.10  ?  371 HIS A CG    1 
ATOM   2823 N ND1   . HIS A 1 371 ? 15.771 12.356  36.114 1.00 35.61  ?  371 HIS A ND1   1 
ATOM   2824 C CD2   . HIS A 1 371 ? 13.847 11.935  37.042 1.00 36.69  ?  371 HIS A CD2   1 
ATOM   2825 C CE1   . HIS A 1 371 ? 15.068 13.469  36.074 1.00 37.22  ?  371 HIS A CE1   1 
ATOM   2826 N NE2   . HIS A 1 371 ? 13.895 13.238  36.628 1.00 36.42  ?  371 HIS A NE2   1 
ATOM   2827 N N     . ARG A 1 372 ? 15.088 6.931   35.840 1.00 42.16  ?  372 ARG A N     1 
ATOM   2828 C CA    . ARG A 1 372 ? 15.395 5.565   36.208 1.00 45.56  ?  372 ARG A CA    1 
ATOM   2829 C C     . ARG A 1 372 ? 15.747 4.721   35.003 1.00 38.17  ?  372 ARG A C     1 
ATOM   2830 O O     . ARG A 1 372 ? 16.387 3.683   35.163 1.00 43.45  ?  372 ARG A O     1 
ATOM   2831 C CB    . ARG A 1 372 ? 14.233 4.960   37.011 1.00 51.43  ?  372 ARG A CB    1 
ATOM   2832 C CG    . ARG A 1 372 ? 14.224 5.466   38.480 1.00 56.74  ?  372 ARG A CG    1 
ATOM   2833 C CD    . ARG A 1 372 ? 12.887 5.247   39.205 1.00 68.60  ?  372 ARG A CD    1 
ATOM   2834 N NE    . ARG A 1 372 ? 11.978 4.360   38.472 1.00 69.82  ?  372 ARG A NE    1 
ATOM   2835 C CZ    . ARG A 1 372 ? 10.741 4.682   38.090 1.00 67.38  ?  372 ARG A CZ    1 
ATOM   2836 N NH1   . ARG A 1 372 ? 10.234 5.889   38.359 1.00 60.65  ?  372 ARG A NH1   1 
ATOM   2837 N NH2   . ARG A 1 372 ? 10.008 3.786   37.435 1.00 63.45  ?  372 ARG A NH2   1 
ATOM   2838 N N     . LYS A 1 373 ? 15.406 5.167   33.803 1.00 38.47  ?  373 LYS A N     1 
ATOM   2839 C CA    . LYS A 1 373 ? 15.720 4.403   32.603 1.00 37.92  ?  373 LYS A CA    1 
ATOM   2840 C C     . LYS A 1 373 ? 16.906 4.957   31.826 1.00 38.47  ?  373 LYS A C     1 
ATOM   2841 O O     . LYS A 1 373 ? 17.774 4.180   31.424 1.00 44.16  ?  373 LYS A O     1 
ATOM   2842 C CB    . LYS A 1 373 ? 14.486 4.312   31.694 1.00 42.68  ?  373 LYS A CB    1 
ATOM   2843 C CG    . LYS A 1 373 ? 13.423 3.329   32.208 1.00 37.10  ?  373 LYS A CG    1 
ATOM   2844 C CD    . LYS A 1 373 ? 12.882 2.450   31.086 1.00 44.79  ?  373 LYS A CD    1 
ATOM   2845 C CE    . LYS A 1 373 ? 13.864 1.364   30.638 1.00 49.60  ?  373 LYS A CE    1 
ATOM   2846 N NZ    . LYS A 1 373 ? 13.223 0.335   29.723 1.00 49.26  ?  373 LYS A NZ    1 
ATOM   2847 N N     . CYS A 1 374 ? 17.010 6.276   31.639 1.00 38.41  ?  374 CYS A N     1 
ATOM   2848 C CA    . CYS A 1 374 ? 18.105 6.870   30.850 1.00 40.84  ?  374 CYS A CA    1 
ATOM   2849 C C     . CYS A 1 374 ? 19.195 7.445   31.762 1.00 41.60  ?  374 CYS A C     1 
ATOM   2850 O O     . CYS A 1 374 ? 19.150 8.608   32.173 1.00 37.74  ?  374 CYS A O     1 
ATOM   2851 C CB    . CYS A 1 374 ? 17.571 7.935   29.893 1.00 35.00  ?  374 CYS A CB    1 
ATOM   2852 S SG    . CYS A 1 374 ? 16.247 7.343   28.833 1.00 35.23  ?  374 CYS A SG    1 
ATOM   2853 N N     . PHE A 1 375 ? 20.213 6.630   32.034 1.00 42.79  ?  375 PHE A N     1 
ATOM   2854 C CA    . PHE A 1 375 ? 21.405 7.075   32.753 1.00 43.46  ?  375 PHE A CA    1 
ATOM   2855 C C     . PHE A 1 375 ? 22.576 6.152   32.374 1.00 50.80  ?  375 PHE A C     1 
ATOM   2856 O O     . PHE A 1 375 ? 23.728 6.337   32.804 1.00 51.24  ?  375 PHE A O     1 
ATOM   2857 C CB    . PHE A 1 375 ? 21.168 7.074   34.272 1.00 42.26  ?  375 PHE A CB    1 
ATOM   2858 C CG    . PHE A 1 375 ? 20.971 5.696   34.851 1.00 39.12  ?  375 PHE A CG    1 
ATOM   2859 C CD1   . PHE A 1 375 ? 22.059 4.882   35.125 1.00 38.38  ?  375 PHE A CD1   1 
ATOM   2860 C CD2   . PHE A 1 375 ? 19.702 5.211   35.098 1.00 34.93  ?  375 PHE A CD2   1 
ATOM   2861 C CE1   . PHE A 1 375 ? 21.878 3.615   35.632 1.00 39.66  ?  375 PHE A CE1   1 
ATOM   2862 C CE2   . PHE A 1 375 ? 19.518 3.944   35.605 1.00 37.65  ?  375 PHE A CE2   1 
ATOM   2863 C CZ    . PHE A 1 375 ? 20.605 3.145   35.877 1.00 37.05  ?  375 PHE A CZ    1 
ATOM   2864 N N     . LYS B 2 5   ? 9.009  -9.584  26.379 1.00 76.46  ?  23  LYS B N     1 
ATOM   2865 C CA    . LYS B 2 5   ? 10.029 -8.601  26.735 1.00 80.52  ?  23  LYS B CA    1 
ATOM   2866 C C     . LYS B 2 5   ? 10.813 -8.995  28.008 1.00 82.44  ?  23  LYS B C     1 
ATOM   2867 O O     . LYS B 2 5   ? 12.034 -9.155  27.958 1.00 78.50  ?  23  LYS B O     1 
ATOM   2868 C CB    . LYS B 2 5   ? 9.396  -7.207  26.916 1.00 81.51  ?  23  LYS B CB    1 
ATOM   2869 C CG    . LYS B 2 5   ? 8.895  -6.557  25.626 1.00 72.43  ?  23  LYS B CG    1 
ATOM   2870 C CD    . LYS B 2 5   ? 9.876  -5.537  25.035 1.00 69.44  ?  23  LYS B CD    1 
ATOM   2871 C CE    . LYS B 2 5   ? 10.141 -5.822  23.550 1.00 65.85  ?  23  LYS B CE    1 
ATOM   2872 N NZ    . LYS B 2 5   ? 10.640 -4.643  22.786 1.00 60.25  ?  23  LYS B NZ    1 
ATOM   2873 N N     . ILE B 2 6   ? 10.120 -9.167  29.139 1.00 84.20  ?  24  ILE B N     1 
ATOM   2874 C CA    . ILE B 2 6   ? 10.819 -9.364  30.412 1.00 81.48  ?  24  ILE B CA    1 
ATOM   2875 C C     . ILE B 2 6   ? 11.667 -10.636 30.405 1.00 75.63  ?  24  ILE B C     1 
ATOM   2876 O O     . ILE B 2 6   ? 12.744 -10.670 31.011 1.00 68.00  ?  24  ILE B O     1 
ATOM   2877 C CB    . ILE B 2 6   ? 9.804  -9.355  31.575 1.00 84.35  ?  24  ILE B CB    1 
ATOM   2878 C CG1   . ILE B 2 6   ? 9.533  -7.910  32.059 1.00 89.29  ?  24  ILE B CG1   1 
ATOM   2879 C CG2   . ILE B 2 6   ? 10.248 -10.286 32.682 1.00 76.41  ?  24  ILE B CG2   1 
ATOM   2880 C CD1   . ILE B 2 6   ? 10.518 -7.360  33.099 1.00 85.15  ?  24  ILE B CD1   1 
ATOM   2881 N N     . GLU B 2 7   ? 11.207 -11.690 29.714 1.00 83.99  ?  25  GLU B N     1 
ATOM   2882 C CA    . GLU B 2 7   ? 11.978 -12.935 29.599 1.00 84.52  ?  25  GLU B CA    1 
ATOM   2883 C C     . GLU B 2 7   ? 13.311 -12.713 28.884 1.00 81.44  ?  25  GLU B C     1 
ATOM   2884 O O     . GLU B 2 7   ? 14.329 -13.330 29.234 1.00 78.47  ?  25  GLU B O     1 
ATOM   2885 C CB    . GLU B 2 7   ? 11.149 -14.008 28.870 1.00 88.64  ?  25  GLU B CB    1 
ATOM   2886 C CG    . GLU B 2 7   ? 10.863 -13.767 27.356 1.00 94.13  ?  25  GLU B CG    1 
ATOM   2887 C CD    . GLU B 2 7   ? 9.804  -12.669 27.067 1.00 101.03 ?  25  GLU B CD    1 
ATOM   2888 O OE1   . GLU B 2 7   ? 8.978  -12.355 27.973 1.00 99.35  ?  25  GLU B OE1   1 
ATOM   2889 O OE2   . GLU B 2 7   ? 9.819  -12.110 25.933 1.00 95.14  -1 25  GLU B OE2   1 
ATOM   2890 N N     . LEU B 2 8   ? 13.316 -11.842 27.871 1.00 79.32  ?  26  LEU B N     1 
ATOM   2891 C CA    . LEU B 2 8   ? 14.503 -11.580 27.067 1.00 73.42  ?  26  LEU B CA    1 
ATOM   2892 C C     . LEU B 2 8   ? 15.412 -10.548 27.720 1.00 65.66  ?  26  LEU B C     1 
ATOM   2893 O O     . LEU B 2 8   ? 16.629 -10.588 27.514 1.00 56.10  ?  26  LEU B O     1 
ATOM   2894 C CB    . LEU B 2 8   ? 14.071 -11.115 25.677 1.00 72.53  ?  26  LEU B CB    1 
ATOM   2895 C CG    . LEU B 2 8   ? 15.137 -10.942 24.602 1.00 73.15  ?  26  LEU B CG    1 
ATOM   2896 C CD1   . LEU B 2 8   ? 15.418 -12.266 23.918 1.00 70.70  ?  26  LEU B CD1   1 
ATOM   2897 C CD2   . LEU B 2 8   ? 14.702 -9.880  23.589 1.00 69.86  ?  26  LEU B CD2   1 
ATOM   2898 N N     . SER B 2 9   ? 14.826 -9.626  28.499 1.00 67.77  ?  27  SER B N     1 
ATOM   2899 C CA    . SER B 2 9   ? 15.591 -8.638  29.253 1.00 59.28  ?  27  SER B CA    1 
ATOM   2900 C C     . SER B 2 9   ? 16.419 -9.296  30.344 1.00 58.51  ?  27  SER B C     1 
ATOM   2901 O O     . SER B 2 9   ? 17.616 -9.014  30.488 1.00 57.60  ?  27  SER B O     1 
ATOM   2902 C CB    . SER B 2 9   ? 14.654 -7.614  29.884 1.00 58.43  ?  27  SER B CB    1 
ATOM   2903 O OG    . SER B 2 9   ? 14.128 -6.729  28.928 1.00 64.72  ?  27  SER B OG    1 
ATOM   2904 N N     . ILE B 2 10  ? 15.788 -10.139 31.159 1.00 53.41  ?  28  ILE B N     1 
ATOM   2905 C CA    . ILE B 2 10  ? 16.553 -10.787 32.212 1.00 56.45  ?  28  ILE B CA    1 
ATOM   2906 C C     . ILE B 2 10  ? 17.576 -11.731 31.595 1.00 55.30  ?  28  ILE B C     1 
ATOM   2907 O O     . ILE B 2 10  ? 18.640 -11.974 32.178 1.00 49.15  ?  28  ILE B O     1 
ATOM   2908 C CB    . ILE B 2 10  ? 15.614 -11.490 33.217 1.00 55.04  ?  28  ILE B CB    1 
ATOM   2909 C CG1   . ILE B 2 10  ? 15.097 -10.504 34.279 1.00 55.28  ?  28  ILE B CG1   1 
ATOM   2910 C CG2   . ILE B 2 10  ? 16.299 -12.641 33.889 1.00 48.38  ?  28  ILE B CG2   1 
ATOM   2911 C CD1   . ILE B 2 10  ? 14.077 -9.499  33.778 1.00 61.18  ?  28  ILE B CD1   1 
ATOM   2912 N N     . SER B 2 11  ? 17.292 -12.246 30.394 1.00 57.30  ?  29  SER B N     1 
ATOM   2913 C CA    . SER B 2 11  ? 18.267 -13.056 29.670 1.00 54.53  ?  29  SER B CA    1 
ATOM   2914 C C     . SER B 2 11  ? 19.530 -12.259 29.380 1.00 53.08  ?  29  SER B C     1 
ATOM   2915 O O     . SER B 2 11  ? 20.637 -12.673 29.744 1.00 51.09  ?  29  SER B O     1 
ATOM   2916 C CB    . SER B 2 11  ? 17.655 -13.562 28.366 1.00 64.41  ?  29  SER B CB    1 
ATOM   2917 O OG    . SER B 2 11  ? 17.086 -14.847 28.520 1.00 71.80  ?  29  SER B OG    1 
ATOM   2918 N N     . LEU B 2 12  ? 19.376 -11.127 28.681 1.00 55.83  ?  30  LEU B N     1 
ATOM   2919 C CA    . LEU B 2 12  ? 20.472 -10.186 28.467 1.00 51.59  ?  30  LEU B CA    1 
ATOM   2920 C C     . LEU B 2 12  ? 21.115 -9.796  29.778 1.00 51.19  ?  30  LEU B C     1 
ATOM   2921 O O     . LEU B 2 12  ? 22.334 -9.910  29.952 1.00 50.37  ?  30  LEU B O     1 
ATOM   2922 C CB    . LEU B 2 12  ? 19.954 -8.933  27.768 1.00 45.59  ?  30  LEU B CB    1 
ATOM   2923 C CG    . LEU B 2 12  ? 19.688 -9.206  26.302 1.00 45.16  ?  30  LEU B CG    1 
ATOM   2924 C CD1   . LEU B 2 12  ? 18.963 -8.066  25.604 1.00 41.25  ?  30  LEU B CD1   1 
ATOM   2925 C CD2   . LEU B 2 12  ? 21.019 -9.503  25.677 1.00 43.20  ?  30  LEU B CD2   1 
ATOM   2926 N N     . SER B 2 13  ? 20.294 -9.313  30.711 1.00 50.31  ?  31  SER B N     1 
ATOM   2927 C CA    . SER B 2 13  ? 20.796 -8.895  32.011 1.00 50.69  ?  31  SER B CA    1 
ATOM   2928 C C     . SER B 2 13  ? 21.696 -9.944  32.655 1.00 50.40  ?  31  SER B C     1 
ATOM   2929 O O     . SER B 2 13  ? 22.650 -9.594  33.350 1.00 49.91  ?  31  SER B O     1 
ATOM   2930 C CB    . SER B 2 13  ? 19.633 -8.570  32.934 1.00 52.60  ?  31  SER B CB    1 
ATOM   2931 O OG    . SER B 2 13  ? 20.148 -8.087  34.153 1.00 55.98  ?  31  SER B OG    1 
ATOM   2932 N N     . LEU B 2 14  ? 21.398 -11.230 32.466 1.00 50.50  ?  32  LEU B N     1 
ATOM   2933 C CA    . LEU B 2 14  ? 22.182 -12.264 33.132 1.00 51.64  ?  32  LEU B CA    1 
ATOM   2934 C C     . LEU B 2 14  ? 23.498 -12.543 32.430 1.00 53.12  ?  32  LEU B C     1 
ATOM   2935 O O     . LEU B 2 14  ? 24.404 -13.134 33.032 1.00 53.08  ?  32  LEU B O     1 
ATOM   2936 C CB    . LEU B 2 14  ? 21.366 -13.553 33.252 1.00 53.51  ?  32  LEU B CB    1 
ATOM   2937 C CG    . LEU B 2 14  ? 20.453 -13.496 34.478 1.00 48.26  ?  32  LEU B CG    1 
ATOM   2938 C CD1   . LEU B 2 14  ? 19.576 -14.724 34.603 1.00 45.52  ?  32  LEU B CD1   1 
ATOM   2939 C CD2   . LEU B 2 14  ? 21.304 -13.294 35.716 1.00 46.96  ?  32  LEU B CD2   1 
ATOM   2940 N N     . ASP B 2 15  ? 23.625 -12.113 31.179 1.00 56.07  ?  33  ASP B N     1 
ATOM   2941 C CA    . ASP B 2 15  ? 24.852 -12.298 30.425 1.00 57.45  ?  33  ASP B CA    1 
ATOM   2942 C C     . ASP B 2 15  ? 26.019 -11.477 30.963 1.00 56.27  ?  33  ASP B C     1 
ATOM   2943 O O     . ASP B 2 15  ? 27.151 -11.680 30.508 1.00 59.51  ?  33  ASP B O     1 
ATOM   2944 C CB    . ASP B 2 15  ? 24.593 -11.955 28.957 1.00 58.76  ?  33  ASP B CB    1 
ATOM   2945 C CG    . ASP B 2 15  ? 24.456 -13.188 28.098 1.00 66.51  ?  33  ASP B CG    1 
ATOM   2946 O OD1   . ASP B 2 15  ? 23.349 -13.418 27.560 1.00 67.82  ?  33  ASP B OD1   1 
ATOM   2947 O OD2   . ASP B 2 15  ? 25.465 -13.923 27.960 1.00 70.66  -1 33  ASP B OD2   1 
ATOM   2948 N N     . SER B 2 16  ? 25.791 -10.578 31.916 1.00 55.19  ?  34  SER B N     1 
ATOM   2949 C CA    . SER B 2 16  ? 26.830 -9.625  32.258 1.00 53.93  ?  34  SER B CA    1 
ATOM   2950 C C     . SER B 2 16  ? 28.008 -10.355 32.894 1.00 55.72  ?  34  SER B C     1 
ATOM   2951 O O     . SER B 2 16  ? 27.815 -11.344 33.608 1.00 51.59  ?  34  SER B O     1 
ATOM   2952 C CB    . SER B 2 16  ? 26.318 -8.550  33.205 1.00 48.99  ?  34  SER B CB    1 
ATOM   2953 O OG    . SER B 2 16  ? 27.400 -8.048  33.974 1.00 55.89  ?  34  SER B OG    1 
ATOM   2954 N N     . PRO B 2 17  ? 29.240 -9.914  32.622 1.00 58.73  ?  35  PRO B N     1 
ATOM   2955 C CA    . PRO B 2 17  ? 30.396 -10.558 33.250 1.00 56.06  ?  35  PRO B CA    1 
ATOM   2956 C C     . PRO B 2 17  ? 30.551 -10.197 34.711 1.00 57.67  ?  35  PRO B C     1 
ATOM   2957 O O     . PRO B 2 17  ? 30.992 -11.047 35.498 1.00 59.71  ?  35  PRO B O     1 
ATOM   2958 C CB    . PRO B 2 17  ? 31.585 -10.043 32.419 1.00 52.60  ?  35  PRO B CB    1 
ATOM   2959 C CG    . PRO B 2 17  ? 30.999 -9.398  31.223 1.00 52.89  ?  35  PRO B CG    1 
ATOM   2960 C CD    . PRO B 2 17  ? 29.651 -8.913  31.627 1.00 60.92  ?  35  PRO B CD    1 
ATOM   2961 N N     . LYS B 2 18  ? 30.188 -8.971  35.099 1.00 56.26  ?  36  LYS B N     1 
ATOM   2962 C CA    . LYS B 2 18  ? 30.514 -8.421  36.409 1.00 52.71  ?  36  LYS B CA    1 
ATOM   2963 C C     . LYS B 2 18  ? 29.399 -8.633  37.441 1.00 49.95  ?  36  LYS B C     1 
ATOM   2964 O O     . LYS B 2 18  ? 29.439 -8.024  38.520 1.00 47.13  ?  36  LYS B O     1 
ATOM   2965 C CB    . LYS B 2 18  ? 30.862 -6.931  36.259 1.00 51.27  ?  36  LYS B CB    1 
ATOM   2966 C CG    . LYS B 2 18  ? 32.211 -6.655  35.550 1.00 52.48  ?  36  LYS B CG    1 
ATOM   2967 C CD    . LYS B 2 18  ? 32.378 -5.175  35.156 1.00 55.41  ?  36  LYS B CD    1 
ATOM   2968 C CE    . LYS B 2 18  ? 33.858 -4.733  35.103 1.00 57.71  ?  36  LYS B CE    1 
ATOM   2969 N NZ    . LYS B 2 18  ? 34.112 -3.309  35.569 1.00 57.94  ?  36  LYS B NZ    1 
ATOM   2970 N N     . LEU B 2 19  ? 28.434 -9.505  37.138 1.00 48.76  ?  37  LEU B N     1 
ATOM   2971 C CA    . LEU B 2 19  ? 27.264 -9.730  37.986 1.00 48.38  ?  37  LEU B CA    1 
ATOM   2972 C C     . LEU B 2 19  ? 27.663 -10.315 39.331 1.00 44.22  ?  37  LEU B C     1 
ATOM   2973 O O     . LEU B 2 19  ? 28.307 -11.366 39.389 1.00 42.61  ?  37  LEU B O     1 
ATOM   2974 C CB    . LEU B 2 19  ? 26.300 -10.672 37.267 1.00 48.24  ?  37  LEU B CB    1 
ATOM   2975 C CG    . LEU B 2 19  ? 24.869 -10.876 37.756 1.00 45.02  ?  37  LEU B CG    1 
ATOM   2976 C CD1   . LEU B 2 19  ? 23.959 -9.924  37.039 1.00 45.66  ?  37  LEU B CD1   1 
ATOM   2977 C CD2   . LEU B 2 19  ? 24.430 -12.310 37.490 1.00 46.69  ?  37  LEU B CD2   1 
ATOM   2978 N N     . ASP B 2 20  ? 27.263 -9.655  40.416 1.00 47.12  ?  38  ASP B N     1 
ATOM   2979 C CA    . ASP B 2 20  ? 27.678 -10.071 41.751 1.00 44.18  ?  38  ASP B CA    1 
ATOM   2980 C C     . ASP B 2 20  ? 26.505 -10.707 42.501 1.00 40.81  ?  38  ASP B C     1 
ATOM   2981 O O     . ASP B 2 20  ? 25.375 -10.779 42.010 1.00 40.33  ?  38  ASP B O     1 
ATOM   2982 C CB    . ASP B 2 20  ? 28.327 -8.890  42.510 1.00 45.47  ?  38  ASP B CB    1 
ATOM   2983 C CG    . ASP B 2 20  ? 27.332 -7.980  43.227 1.00 46.96  ?  38  ASP B CG    1 
ATOM   2984 O OD1   . ASP B 2 20  ? 26.707 -7.131  42.558 1.00 48.25  ?  38  ASP B OD1   1 
ATOM   2985 O OD2   . ASP B 2 20  ? 27.246 -8.049  44.480 1.00 47.00  -1 38  ASP B OD2   1 
ATOM   2986 N N     . GLU B 2 21  ? 26.791 -11.226 43.695 1.00 43.36  ?  39  GLU B N     1 
ATOM   2987 C CA    . GLU B 2 21  ? 25.749 -11.900 44.470 1.00 41.88  ?  39  GLU B CA    1 
ATOM   2988 C C     . GLU B 2 21  ? 24.550 -10.993 44.710 1.00 39.03  ?  39  GLU B C     1 
ATOM   2989 O O     . GLU B 2 21  ? 23.407 -11.453 44.667 1.00 41.58  ?  39  GLU B O     1 
ATOM   2990 C CB    . GLU B 2 21  ? 26.306 -12.395 45.802 1.00 42.99  ?  39  GLU B CB    1 
ATOM   2991 C CG    . GLU B 2 21  ? 26.969 -13.752 45.749 1.00 47.23  ?  39  GLU B CG    1 
ATOM   2992 C CD    . GLU B 2 21  ? 27.547 -14.199 47.101 1.00 60.28  ?  39  GLU B CD    1 
ATOM   2993 O OE1   . GLU B 2 21  ? 27.971 -13.325 47.906 1.00 55.36  ?  39  GLU B OE1   1 
ATOM   2994 O OE2   . GLU B 2 21  ? 27.606 -15.437 47.345 1.00 70.24  -1 39  GLU B OE2   1 
ATOM   2995 N N     . SER B 2 22  ? 24.779 -9.704  44.972 1.00 37.39  ?  40  SER B N     1 
ATOM   2996 C CA    . SER B 2 22  ? 23.658 -8.823  45.274 1.00 35.99  ?  40  SER B CA    1 
ATOM   2997 C C     . SER B 2 22  ? 22.898 -8.431  44.011 1.00 42.38  ?  40  SER B C     1 
ATOM   2998 O O     . SER B 2 22  ? 21.670 -8.210  44.056 1.00 33.95  ?  40  SER B O     1 
ATOM   2999 C CB    . SER B 2 22  ? 24.156 -7.585  46.014 1.00 32.17  ?  40  SER B CB    1 
ATOM   3000 O OG    . SER B 2 22  ? 23.209 -6.537  45.958 1.00 31.05  ?  40  SER B OG    1 
ATOM   3001 N N     . ASP B 2 23  ? 23.616 -8.347  42.881 1.00 43.92  ?  41  ASP B N     1 
ATOM   3002 C CA    . ASP B 2 23  ? 22.978 -8.101  41.589 1.00 42.40  ?  41  ASP B CA    1 
ATOM   3003 C C     . ASP B 2 23  ? 22.005 -9.227  41.245 1.00 40.30  ?  41  ASP B C     1 
ATOM   3004 O O     . ASP B 2 23  ? 20.861 -8.982  40.840 1.00 35.43  ?  41  ASP B O     1 
ATOM   3005 C CB    . ASP B 2 23  ? 24.047 -7.960  40.493 1.00 42.79  ?  41  ASP B CB    1 
ATOM   3006 C CG    . ASP B 2 23  ? 24.719 -6.570  40.478 1.00 53.04  ?  41  ASP B CG    1 
ATOM   3007 O OD1   . ASP B 2 23  ? 24.249 -5.626  41.158 1.00 56.41  ?  41  ASP B OD1   1 
ATOM   3008 O OD2   . ASP B 2 23  ? 25.746 -6.423  39.767 1.00 61.42  -1 41  ASP B OD2   1 
ATOM   3009 N N     . PHE B 2 24  ? 22.461 -10.475 41.396 1.00 39.40  ?  42  PHE B N     1 
ATOM   3010 C CA    . PHE B 2 24  ? 21.642 -11.645 41.095 1.00 37.57  ?  42  PHE B CA    1 
ATOM   3011 C C     . PHE B 2 24  ? 20.368 -11.662 41.930 1.00 37.30  ?  42  PHE B C     1 
ATOM   3012 O O     . PHE B 2 24  ? 19.266 -11.819 41.395 1.00 37.98  ?  42  PHE B O     1 
ATOM   3013 C CB    . PHE B 2 24  ? 22.479 -12.898 41.335 1.00 42.09  ?  42  PHE B CB    1 
ATOM   3014 C CG    . PHE B 2 24  ? 21.737 -14.185 41.171 1.00 42.55  ?  42  PHE B CG    1 
ATOM   3015 C CD1   . PHE B 2 24  ? 21.357 -14.915 42.269 1.00 43.38  ?  42  PHE B CD1   1 
ATOM   3016 C CD2   . PHE B 2 24  ? 21.462 -14.690 39.914 1.00 49.06  ?  42  PHE B CD2   1 
ATOM   3017 C CE1   . PHE B 2 24  ? 20.696 -16.113 42.126 1.00 46.50  ?  42  PHE B CE1   1 
ATOM   3018 C CE2   . PHE B 2 24  ? 20.790 -15.883 39.768 1.00 47.92  ?  42  PHE B CE2   1 
ATOM   3019 C CZ    . PHE B 2 24  ? 20.408 -16.593 40.883 1.00 44.61  ?  42  PHE B CZ    1 
ATOM   3020 N N     . ILE B 2 25  ? 20.495 -11.480 43.246 1.00 36.81  ?  43  ILE B N     1 
ATOM   3021 C CA    . ILE B 2 25  ? 19.319 -11.496 44.113 1.00 34.19  ?  43  ILE B CA    1 
ATOM   3022 C C     . ILE B 2 25  ? 18.270 -10.502 43.627 1.00 34.61  ?  43  ILE B C     1 
ATOM   3023 O O     . ILE B 2 25  ? 17.085 -10.832 43.527 1.00 34.71  ?  43  ILE B O     1 
ATOM   3024 C CB    . ILE B 2 25  ? 19.726 -11.207 45.562 1.00 32.17  ?  43  ILE B CB    1 
ATOM   3025 C CG1   . ILE B 2 25  ? 20.584 -12.359 46.089 1.00 36.73  ?  43  ILE B CG1   1 
ATOM   3026 C CG2   . ILE B 2 25  ? 18.498 -10.941 46.369 1.00 26.33  ?  43  ILE B CG2   1 
ATOM   3027 C CD1   . ILE B 2 25  ? 20.932 -12.288 47.572 1.00 34.77  ?  43  ILE B CD1   1 
ATOM   3028 N N     . LEU B 2 26  ? 18.689 -9.256  43.342 1.00 35.29  ?  44  LEU B N     1 
ATOM   3029 C CA    . LEU B 2 26  ? 17.751 -8.211  42.927 1.00 33.47  ?  44  LEU B CA    1 
ATOM   3030 C C     . LEU B 2 26  ? 17.178 -8.502  41.549 1.00 36.53  ?  44  LEU B C     1 
ATOM   3031 O O     . LEU B 2 26  ? 16.005 -8.211  41.272 1.00 33.10  ?  44  LEU B O     1 
ATOM   3032 C CB    . LEU B 2 26  ? 18.445 -6.858  42.900 1.00 33.75  ?  44  LEU B CB    1 
ATOM   3033 C CG    . LEU B 2 26  ? 18.901 -6.168  44.172 1.00 33.63  ?  44  LEU B CG    1 
ATOM   3034 C CD1   . LEU B 2 26  ? 19.901 -5.120  43.796 1.00 29.64  ?  44  LEU B CD1   1 
ATOM   3035 C CD2   . LEU B 2 26  ? 17.723 -5.536  44.837 1.00 34.39  ?  44  LEU B CD2   1 
ATOM   3036 N N     . LEU B 2 27  ? 18.009 -9.047  40.663 1.00 37.45  ?  45  LEU B N     1 
ATOM   3037 C CA    . LEU B 2 27  ? 17.571 -9.328  39.306 1.00 37.03  ?  45  LEU B CA    1 
ATOM   3038 C C     . LEU B 2 27  ? 16.578 -10.470 39.302 1.00 39.59  ?  45  LEU B C     1 
ATOM   3039 O O     . LEU B 2 27  ? 15.545 -10.406 38.625 1.00 38.53  ?  45  LEU B O     1 
ATOM   3040 C CB    . LEU B 2 27  ? 18.782 -9.648  38.441 1.00 36.27  ?  45  LEU B CB    1 
ATOM   3041 C CG    . LEU B 2 27  ? 18.733 -9.312  36.955 1.00 47.10  ?  45  LEU B CG    1 
ATOM   3042 C CD1   . LEU B 2 27  ? 17.898 -8.080  36.675 1.00 47.34  ?  45  LEU B CD1   1 
ATOM   3043 C CD2   . LEU B 2 27  ? 20.146 -9.151  36.420 1.00 46.52  ?  45  LEU B CD2   1 
ATOM   3044 N N     . SER B 2 28  ? 16.866 -11.505 40.091 1.00 35.49  ?  46  SER B N     1 
ATOM   3045 C CA    . SER B 2 28  ? 15.966 -12.634 40.258 1.00 33.73  ?  46  SER B CA    1 
ATOM   3046 C C     . SER B 2 28  ? 14.587 -12.190 40.703 1.00 39.42  ?  46  SER B C     1 
ATOM   3047 O O     . SER B 2 28  ? 13.578 -12.476 40.054 1.00 44.50  ?  46  SER B O     1 
ATOM   3048 C CB    . SER B 2 28  ? 16.555 -13.579 41.287 1.00 35.70  ?  46  SER B CB    1 
ATOM   3049 O OG    . SER B 2 28  ? 17.578 -14.332 40.681 1.00 43.97  ?  46  SER B OG    1 
ATOM   3050 N N     . VAL B 2 29  ? 14.529 -11.506 41.838 1.00 42.00  ?  47  VAL B N     1 
ATOM   3051 C CA    . VAL B 2 29  ? 13.246 -11.140 42.418 1.00 43.63  ?  47  VAL B CA    1 
ATOM   3052 C C     . VAL B 2 29  ? 12.457 -10.247 41.462 1.00 48.16  ?  47  VAL B C     1 
ATOM   3053 O O     . VAL B 2 29  ? 11.245 -10.425 41.294 1.00 49.84  ?  47  VAL B O     1 
ATOM   3054 C CB    . VAL B 2 29  ? 13.471 -10.489 43.794 1.00 40.52  ?  47  VAL B CB    1 
ATOM   3055 C CG1   . VAL B 2 29  ? 12.320 -9.565  44.151 1.00 42.15  ?  47  VAL B CG1   1 
ATOM   3056 C CG2   . VAL B 2 29  ? 13.666 -11.568 44.835 1.00 36.33  ?  47  VAL B CG2   1 
ATOM   3057 N N     . LYS B 2 30  ? 13.124 -9.290  40.799 1.00 46.63  ?  48  LYS B N     1 
ATOM   3058 C CA    . LYS B 2 30  ? 12.403 -8.455  39.840 1.00 48.41  ?  48  LYS B CA    1 
ATOM   3059 C C     . LYS B 2 30  ? 11.680 -9.316  38.822 1.00 52.20  ?  48  LYS B C     1 
ATOM   3060 O O     . LYS B 2 30  ? 10.565 -8.990  38.405 1.00 54.84  ?  48  LYS B O     1 
ATOM   3061 C CB    . LYS B 2 30  ? 13.341 -7.490  39.118 1.00 48.16  ?  48  LYS B CB    1 
ATOM   3062 C CG    . LYS B 2 30  ? 12.699 -6.839  37.876 1.00 51.12  ?  48  LYS B CG    1 
ATOM   3063 C CD    . LYS B 2 30  ? 13.592 -5.755  37.250 1.00 58.90  ?  48  LYS B CD    1 
ATOM   3064 C CE    . LYS B 2 30  ? 12.814 -4.761  36.358 1.00 63.27  ?  48  LYS B CE    1 
ATOM   3065 N NZ    . LYS B 2 30  ? 13.113 -3.305  36.656 1.00 50.63  ?  48  LYS B NZ    1 
ATOM   3066 N N     . TYR B 2 31  ? 12.300 -10.430 38.421 1.00 51.35  ?  49  TYR B N     1 
ATOM   3067 C CA    . TYR B 2 31  ? 11.687 -11.343 37.459 1.00 52.48  ?  49  TYR B CA    1 
ATOM   3068 C C     . TYR B 2 31  ? 10.424 -11.992 38.027 1.00 56.72  ?  49  TYR B C     1 
ATOM   3069 O O     . TYR B 2 31  ? 9.386  -12.051 37.359 1.00 55.97  ?  49  TYR B O     1 
ATOM   3070 C CB    . TYR B 2 31  ? 12.701 -12.405 37.042 1.00 47.95  ?  49  TYR B CB    1 
ATOM   3071 C CG    . TYR B 2 31  ? 12.128 -13.453 36.119 1.00 58.24  ?  49  TYR B CG    1 
ATOM   3072 C CD1   . TYR B 2 31  ? 12.116 -14.797 36.476 1.00 54.65  ?  49  TYR B CD1   1 
ATOM   3073 C CD2   . TYR B 2 31  ? 11.594 -13.098 34.881 1.00 58.51  ?  49  TYR B CD2   1 
ATOM   3074 C CE1   . TYR B 2 31  ? 11.582 -15.753 35.628 1.00 58.19  ?  49  TYR B CE1   1 
ATOM   3075 C CE2   . TYR B 2 31  ? 11.065 -14.048 34.032 1.00 59.04  ?  49  TYR B CE2   1 
ATOM   3076 C CZ    . TYR B 2 31  ? 11.057 -15.372 34.409 1.00 57.98  ?  49  TYR B CZ    1 
ATOM   3077 O OH    . TYR B 2 31  ? 10.522 -16.310 33.555 1.00 62.09  ?  49  TYR B OH    1 
ATOM   3078 N N     . LEU B 2 32  ? 10.492 -12.475 39.269 1.00 56.61  ?  50  LEU B N     1 
ATOM   3079 C CA    . LEU B 2 32  ? 9.349  -13.128 39.901 1.00 60.80  ?  50  LEU B CA    1 
ATOM   3080 C C     . LEU B 2 32  ? 8.281  -12.153 40.408 1.00 62.92  ?  50  LEU B C     1 
ATOM   3081 O O     . LEU B 2 32  ? 7.146  -12.573 40.640 1.00 68.61  ?  50  LEU B O     1 
ATOM   3082 C CB    . LEU B 2 32  ? 9.831  -14.014 41.062 1.00 62.79  ?  50  LEU B CB    1 
ATOM   3083 C CG    . LEU B 2 32  ? 11.141 -14.786 40.845 1.00 58.78  ?  50  LEU B CG    1 
ATOM   3084 C CD1   . LEU B 2 32  ? 11.503 -15.591 42.070 1.00 54.92  ?  50  LEU B CD1   1 
ATOM   3085 C CD2   . LEU B 2 32  ? 11.075 -15.681 39.612 1.00 54.61  ?  50  LEU B CD2   1 
ATOM   3086 N N     . GLU B 2 33  ? 8.597  -10.876 40.609 1.00 62.62  ?  51  GLU B N     1 
ATOM   3087 C CA    . GLU B 2 33  ? 7.530  -9.919  40.872 1.00 65.01  ?  51  GLU B CA    1 
ATOM   3088 C C     . GLU B 2 33  ? 6.767  -9.547  39.610 1.00 67.87  ?  51  GLU B C     1 
ATOM   3089 O O     . GLU B 2 33  ? 5.612  -9.117  39.709 1.00 75.91  ?  51  GLU B O     1 
ATOM   3090 C CB    . GLU B 2 33  ? 8.084  -8.646  41.512 1.00 71.43  ?  51  GLU B CB    1 
ATOM   3091 C CG    . GLU B 2 33  ? 7.943  -8.597  43.032 1.00 77.46  ?  51  GLU B CG    1 
ATOM   3092 C CD    . GLU B 2 33  ? 8.801  -7.500  43.663 1.00 81.46  ?  51  GLU B CD    1 
ATOM   3093 O OE1   . GLU B 2 33  ? 9.789  -7.836  44.356 1.00 75.25  ?  51  GLU B OE1   1 
ATOM   3094 O OE2   . GLU B 2 33  ? 8.486  -6.302  43.465 1.00 84.73  -1 51  GLU B OE2   1 
ATOM   3095 N N     . LYS B 2 34  ? 7.385  -9.686  38.432 1.00 63.39  ?  52  LYS B N     1 
ATOM   3096 C CA    . LYS B 2 34  ? 6.694  -9.433  37.173 1.00 66.43  ?  52  LYS B CA    1 
ATOM   3097 C C     . LYS B 2 34  ? 6.028  -10.690 36.633 1.00 64.76  ?  52  LYS B C     1 
ATOM   3098 O O     . LYS B 2 34  ? 4.918  -10.624 36.096 1.00 62.53  ?  52  LYS B O     1 
ATOM   3099 C CB    . LYS B 2 34  ? 7.661  -8.867  36.126 1.00 62.85  ?  52  LYS B CB    1 
ATOM   3100 C CG    . LYS B 2 34  ? 7.261  -7.504  35.550 1.00 66.59  ?  52  LYS B CG    1 
ATOM   3101 C CD    . LYS B 2 34  ? 6.674  -6.554  36.610 1.00 68.16  ?  52  LYS B CD    1 
ATOM   3102 C CE    . LYS B 2 34  ? 6.106  -5.278  35.967 1.00 77.88  ?  52  LYS B CE    1 
ATOM   3103 N NZ    . LYS B 2 34  ? 6.117  -4.076  36.870 1.00 72.56  ?  52  LYS B NZ    1 
ATOM   3104 N N     . SER B 2 35  ? 6.676  -11.844 36.789 1.00 65.94  ?  53  SER B N     1 
ATOM   3105 C CA    . SER B 2 35  ? 6.137  -13.073 36.221 1.00 61.96  ?  53  SER B CA    1 
ATOM   3106 C C     . SER B 2 35  ? 4.901  -13.537 36.974 1.00 66.23  ?  53  SER B C     1 
ATOM   3107 O O     . SER B 2 35  ? 3.865  -13.827 36.366 1.00 71.84  ?  53  SER B O     1 
ATOM   3108 C CB    . SER B 2 35  ? 7.201  -14.161 36.218 1.00 56.97  ?  53  SER B CB    1 
ATOM   3109 O OG    . SER B 2 35  ? 7.975  -14.081 35.040 1.00 52.80  ?  53  SER B OG    1 
ATOM   3110 N N     . LEU B 2 36  ? 4.994  -13.628 38.296 1.00 65.34  ?  54  LEU B N     1 
ATOM   3111 C CA    . LEU B 2 36  ? 3.915  -14.139 39.125 1.00 66.76  ?  54  LEU B CA    1 
ATOM   3112 C C     . LEU B 2 36  ? 3.118  -13.024 39.786 1.00 75.26  ?  54  LEU B C     1 
ATOM   3113 O O     . LEU B 2 36  ? 2.343  -13.291 40.707 1.00 81.08  ?  54  LEU B O     1 
ATOM   3114 C CB    . LEU B 2 36  ? 4.469  -15.097 40.182 1.00 64.53  ?  54  LEU B CB    1 
ATOM   3115 C CG    . LEU B 2 36  ? 5.305  -16.298 39.709 1.00 61.93  ?  54  LEU B CG    1 
ATOM   3116 C CD1   . LEU B 2 36  ? 6.637  -15.866 39.132 1.00 64.63  ?  54  LEU B CD1   1 
ATOM   3117 C CD2   . LEU B 2 36  ? 5.533  -17.273 40.842 1.00 66.11  ?  54  LEU B CD2   1 
ATOM   3118 N N     . GLY B 2 37  ? 3.358  -11.794 39.344 1.00 77.19  ?  55  GLY B N     1 
ATOM   3119 C CA    . GLY B 2 37  ? 2.587  -10.638 39.836 1.00 81.83  ?  55  GLY B CA    1 
ATOM   3120 C C     . GLY B 2 37  ? 2.466  -10.550 41.341 1.00 85.91  ?  55  GLY B C     1 
ATOM   3121 O O     . GLY B 2 37  ? 3.458  -10.811 42.048 1.00 79.02  ?  55  GLY B O     1 
ATOM   3122 N N     . LYS B 2 38  ? 1.287  -10.142 41.803 1.00 85.62  ?  56  LYS B N     1 
ATOM   3123 C CA    . LYS B 2 38  ? 1.086  -9.961  43.255 1.00 87.21  ?  56  LYS B CA    1 
ATOM   3124 C C     . LYS B 2 38  ? 0.142  -11.044 43.750 1.00 90.76  ?  56  LYS B C     1 
ATOM   3125 O O     . LYS B 2 38  ? -0.681 -10.744 44.621 1.00 98.43  ?  56  LYS B O     1 
ATOM   3126 C CB    . LYS B 2 38  ? 0.533  -8.569  43.566 1.00 92.36  ?  56  LYS B CB    1 
ATOM   3127 C CG    . LYS B 2 38  ? 1.178  -7.874  44.758 1.00 98.03  ?  56  LYS B CG    1 
ATOM   3128 C CD    . LYS B 2 38  ? 0.921  -6.386  44.804 1.00 97.02  ?  56  LYS B CD    1 
ATOM   3129 C CE    . LYS B 2 38  ? 2.193  -5.567  44.744 1.00 95.07  ?  56  LYS B CE    1 
ATOM   3130 N NZ    . LYS B 2 38  ? 2.238  -4.709  43.536 1.00 89.31  ?  56  LYS B NZ    1 
ATOM   3131 N N     . LYS B 2 39  ? 0.223  -12.240 43.178 1.00 88.25  ?  57  LYS B N     1 
ATOM   3132 C CA    . LYS B 2 39  ? -0.565 -13.348 43.759 1.00 85.27  ?  57  LYS B CA    1 
ATOM   3133 C C     . LYS B 2 39  ? -0.120 -13.381 45.215 1.00 85.26  ?  57  LYS B C     1 
ATOM   3134 O O     . LYS B 2 39  ? 1.084  -13.566 45.445 1.00 88.79  ?  57  LYS B O     1 
ATOM   3135 C CB    . LYS B 2 39  ? -0.254 -14.650 43.022 1.00 77.78  ?  57  LYS B CB    1 
ATOM   3136 C CG    . LYS B 2 39  ? -0.840 -14.752 41.621 1.00 80.40  ?  57  LYS B CG    1 
ATOM   3137 C CD    . LYS B 2 39  ? -0.372 -15.969 40.856 1.00 81.86  ?  57  LYS B CD    1 
ATOM   3138 C CE    . LYS B 2 39  ? -1.502 -16.893 40.456 1.00 84.56  ?  57  LYS B CE    1 
ATOM   3139 N NZ    . LYS B 2 39  ? -1.390 -18.220 41.107 1.00 85.07  ?  57  LYS B NZ    1 
ATOM   3140 N N     . LYS B 2 40  ? -1.033 -13.181 46.162 1.00 85.34  ?  58  LYS B N     1 
ATOM   3141 C CA    . LYS B 2 40  ? -0.621 -13.072 47.586 1.00 83.76  ?  58  LYS B CA    1 
ATOM   3142 C C     . LYS B 2 40  ? 0.312  -14.211 47.978 1.00 75.84  ?  58  LYS B C     1 
ATOM   3143 O O     . LYS B 2 40  ? 1.168  -13.996 48.843 1.00 78.74  ?  58  LYS B O     1 
ATOM   3144 C CB    . LYS B 2 40  ? -1.619 -12.222 48.374 1.00 87.77  ?  58  LYS B CB    1 
ATOM   3145 C CG    . LYS B 2 40  ? -1.339 -10.726 48.345 1.00 89.34  ?  58  LYS B CG    1 
ATOM   3146 C CD    . LYS B 2 40  ? -2.568 -9.896  48.057 1.00 95.10  ?  58  LYS B CD    1 
ATOM   3147 C CE    . LYS B 2 40  ? -2.378 -8.924  46.913 1.00 94.64  ?  58  LYS B CE    1 
ATOM   3148 N NZ    . LYS B 2 40  ? -3.053 -9.395  45.681 1.00 93.97  ?  58  LYS B NZ    1 
ATOM   3149 N N     . GLU B 2 41  ? 0.126  -15.377 47.377 1.00 77.53  ?  59  GLU B N     1 
ATOM   3150 C CA    . GLU B 2 41  ? 0.492  -16.716 47.878 1.00 80.20  ?  59  GLU B CA    1 
ATOM   3151 C C     . GLU B 2 41  ? 2.001  -16.655 48.054 1.00 79.51  ?  59  GLU B C     1 
ATOM   3152 O O     . GLU B 2 41  ? 2.515  -17.255 49.008 1.00 77.07  ?  59  GLU B O     1 
ATOM   3153 C CB    . GLU B 2 41  ? 0.153  -17.750 46.806 1.00 75.55  ?  59  GLU B CB    1 
ATOM   3154 C CG    . GLU B 2 41  ? -0.729 -17.200 45.707 1.00 80.85  ?  59  GLU B CG    1 
ATOM   3155 C CD    . GLU B 2 41  ? -1.222 -18.242 44.723 1.00 94.26  ?  59  GLU B CD    1 
ATOM   3156 O OE1   . GLU B 2 41  ? -0.585 -19.307 44.630 1.00 98.06  ?  59  GLU B OE1   1 
ATOM   3157 O OE2   . GLU B 2 41  ? -2.244 -17.987 44.056 1.00 96.56  -1 59  GLU B OE2   1 
ATOM   3158 N N     . PHE B 2 42  ? 2.660  -15.898 47.180 1.00 78.73  ?  60  PHE B N     1 
ATOM   3159 C CA    . PHE B 2 42  ? 4.136  -15.809 47.211 1.00 74.63  ?  60  PHE B CA    1 
ATOM   3160 C C     . PHE B 2 42  ? 4.530  -14.487 47.860 1.00 72.11  ?  60  PHE B C     1 
ATOM   3161 O O     . PHE B 2 42  ? 5.720  -14.170 47.894 1.00 70.88  ?  60  PHE B O     1 
ATOM   3162 C CB    . PHE B 2 42  ? 4.676  -15.913 45.787 1.00 70.76  ?  60  PHE B CB    1 
ATOM   3163 C CG    . PHE B 2 42  ? 3.918  -16.847 44.880 1.00 74.82  ?  60  PHE B CG    1 
ATOM   3164 C CD1   . PHE B 2 42  ? 4.011  -18.219 45.039 1.00 69.76  ?  60  PHE B CD1   1 
ATOM   3165 C CD2   . PHE B 2 42  ? 3.126  -16.354 43.858 1.00 78.48  ?  60  PHE B CD2   1 
ATOM   3166 C CE1   . PHE B 2 42  ? 3.323  -19.078 44.200 1.00 69.70  ?  60  PHE B CE1   1 
ATOM   3167 C CE2   . PHE B 2 42  ? 2.436  -17.215 43.022 1.00 75.50  ?  60  PHE B CE2   1 
ATOM   3168 C CZ    . PHE B 2 42  ? 2.538  -18.574 43.192 1.00 71.94  ?  60  PHE B CZ    1 
ATOM   3169 N N     . SER B 2 43  ? 3.548  -13.758 48.370 1.00 75.49  ?  61  SER B N     1 
ATOM   3170 C CA    . SER B 2 43  ? 3.809  -12.443 49.002 1.00 73.47  ?  61  SER B CA    1 
ATOM   3171 C C     . SER B 2 43  ? 4.899  -12.554 50.068 1.00 71.53  ?  61  SER B C     1 
ATOM   3172 O O     . SER B 2 43  ? 5.682  -11.610 50.192 1.00 73.83  ?  61  SER B O     1 
ATOM   3173 C CB    . SER B 2 43  ? 2.541  -11.899 49.587 1.00 76.19  ?  61  SER B CB    1 
ATOM   3174 O OG    . SER B 2 43  ? 2.313  -10.572 49.143 1.00 81.06  ?  61  SER B OG    1 
ATOM   3175 N N     . GLY B 2 44  ? 4.944  -13.658 50.803 1.00 65.43  ?  62  GLY B N     1 
ATOM   3176 C CA    . GLY B 2 44  ? 5.912  -13.788 51.904 1.00 63.95  ?  62  GLY B CA    1 
ATOM   3177 C C     . GLY B 2 44  ? 7.281  -14.253 51.459 1.00 61.93  ?  62  GLY B C     1 
ATOM   3178 O O     . GLY B 2 44  ? 8.205  -14.133 52.262 1.00 61.26  ?  62  GLY B O     1 
ATOM   3179 N N     . PHE B 2 45  ? 7.412  -14.773 50.241 1.00 61.30  ?  63  PHE B N     1 
ATOM   3180 C CA    . PHE B 2 45  ? 8.750  -15.135 49.717 1.00 56.93  ?  63  PHE B CA    1 
ATOM   3181 C C     . PHE B 2 45  ? 9.449  -13.828 49.395 1.00 55.22  ?  63  PHE B C     1 
ATOM   3182 O O     . PHE B 2 45  ? 10.616 -13.653 49.725 1.00 47.55  ?  63  PHE B O     1 
ATOM   3183 C CB    . PHE B 2 45  ? 8.604  -15.966 48.444 1.00 59.64  ?  63  PHE B CB    1 
ATOM   3184 C CG    . PHE B 2 45  ? 9.854  -16.105 47.615 1.00 59.05  ?  63  PHE B CG    1 
ATOM   3185 C CD1   . PHE B 2 45  ? 9.981  -15.440 46.407 1.00 60.95  ?  63  PHE B CD1   1 
ATOM   3186 C CD2   . PHE B 2 45  ? 10.897 -16.911 48.037 1.00 55.64  ?  63  PHE B CD2   1 
ATOM   3187 C CE1   . PHE B 2 45  ? 11.130 -15.565 45.649 1.00 54.05  ?  63  PHE B CE1   1 
ATOM   3188 C CE2   . PHE B 2 45  ? 12.045 -17.037 47.273 1.00 55.28  ?  63  PHE B CE2   1 
ATOM   3189 C CZ    . PHE B 2 45  ? 12.156 -16.368 46.079 1.00 56.99  ?  63  PHE B CZ    1 
ATOM   3190 N N     . PHE B 2 46  ? 8.706  -12.931 48.770 1.00 60.91  ?  64  PHE B N     1 
ATOM   3191 C CA    . PHE B 2 46  ? 9.255  -11.605 48.430 1.00 57.47  ?  64  PHE B CA    1 
ATOM   3192 C C     . PHE B 2 46  ? 9.632  -10.900 49.722 1.00 54.90  ?  64  PHE B C     1 
ATOM   3193 O O     . PHE B 2 46  ? 10.723 -10.337 49.793 1.00 57.80  ?  64  PHE B O     1 
ATOM   3194 C CB    . PHE B 2 46  ? 8.210  -10.841 47.623 1.00 57.03  ?  64  PHE B CB    1 
ATOM   3195 C CG    . PHE B 2 46  ? 7.912  -11.481 46.295 1.00 64.61  ?  64  PHE B CG    1 
ATOM   3196 C CD1   . PHE B 2 46  ? 8.944  -11.885 45.464 1.00 55.30  ?  64  PHE B CD1   1 
ATOM   3197 C CD2   . PHE B 2 46  ? 6.608  -11.698 45.887 1.00 64.00  ?  64  PHE B CD2   1 
ATOM   3198 C CE1   . PHE B 2 46  ? 8.675  -12.486 44.248 1.00 54.48  ?  64  PHE B CE1   1 
ATOM   3199 C CE2   . PHE B 2 46  ? 6.342  -12.303 44.671 1.00 61.34  ?  64  PHE B CE2   1 
ATOM   3200 C CZ    . PHE B 2 46  ? 7.376  -12.696 43.859 1.00 61.19  ?  64  PHE B CZ    1 
ATOM   3201 N N     . GLU B 2 47  ? 8.763  -10.984 50.722 1.00 58.27  ?  65  GLU B N     1 
ATOM   3202 C CA    . GLU B 2 47  ? 9.010  -10.292 52.007 1.00 58.18  ?  65  GLU B CA    1 
ATOM   3203 C C     . GLU B 2 47  ? 10.244 -10.900 52.670 1.00 57.22  ?  65  GLU B C     1 
ATOM   3204 O O     . GLU B 2 47  ? 11.060 -10.137 53.199 1.00 56.11  ?  65  GLU B O     1 
ATOM   3205 C CB    . GLU B 2 47  ? 7.755  -10.356 52.873 1.00 57.08  ?  65  GLU B CB    1 
ATOM   3206 C CG    . GLU B 2 47  ? 7.019  -9.034  52.962 1.00 65.12  ?  65  GLU B CG    1 
ATOM   3207 C CD    . GLU B 2 47  ? 5.611  -9.039  52.393 1.00 77.91  ?  65  GLU B CD    1 
ATOM   3208 O OE1   . GLU B 2 47  ? 5.406  -8.434  51.327 1.00 83.40  ?  65  GLU B OE1   1 
ATOM   3209 O OE2   . GLU B 2 47  ? 4.722  -9.644  53.019 1.00 80.55  -1 65  GLU B OE2   1 
ATOM   3210 N N     . ASP B 2 48  ? 10.405 -12.215 52.577 1.00 53.43  ?  66  ASP B N     1 
ATOM   3211 C CA    . ASP B 2 48  ? 11.530 -12.881 53.272 1.00 52.71  ?  66  ASP B CA    1 
ATOM   3212 C C     . ASP B 2 48  ? 12.841 -12.588 52.554 1.00 50.07  ?  66  ASP B C     1 
ATOM   3213 O O     . ASP B 2 48  ? 13.844 -12.407 53.238 1.00 47.41  ?  66  ASP B O     1 
ATOM   3214 C CB    . ASP B 2 48  ? 11.290 -14.383 53.402 1.00 54.37  ?  66  ASP B CB    1 
ATOM   3215 C CG    . ASP B 2 48  ? 12.243 -15.057 54.372 1.00 67.41  ?  66  ASP B CG    1 
ATOM   3216 O OD1   . ASP B 2 48  ? 12.489 -14.484 55.451 1.00 70.72  ?  66  ASP B OD1   1 
ATOM   3217 O OD2   . ASP B 2 48  ? 12.735 -16.145 54.038 1.00 74.35  -1 66  ASP B OD2   1 
ATOM   3218 N N     . ILE B 2 49  ? 12.821 -12.547 51.227 1.00 52.18  ?  67  ILE B N     1 
ATOM   3219 C CA    . ILE B 2 49  ? 14.077 -12.351 50.459 1.00 46.21  ?  67  ILE B CA    1 
ATOM   3220 C C     . ILE B 2 49  ? 14.606 -10.959 50.778 1.00 49.45  ?  67  ILE B C     1 
ATOM   3221 O O     . ILE B 2 49  ? 15.808 -10.834 51.001 1.00 44.93  ?  67  ILE B O     1 
ATOM   3222 C CB    . ILE B 2 49  ? 13.842 -12.556 48.954 1.00 50.59  ?  67  ILE B CB    1 
ATOM   3223 C CG1   . ILE B 2 49  ? 13.755 -14.040 48.598 1.00 52.54  ?  67  ILE B CG1   1 
ATOM   3224 C CG2   . ILE B 2 49  ? 14.918 -11.862 48.137 1.00 50.25  ?  67  ILE B CG2   1 
ATOM   3225 C CD1   . ILE B 2 49  ? 14.667 -14.919 49.410 1.00 53.72  ?  67  ILE B CD1   1 
ATOM   3226 N N     . GLU B 2 50  ? 13.720 -9.971  50.861 1.00 48.80  ?  68  GLU B N     1 
ATOM   3227 C CA    . GLU B 2 50  ? 14.158 -8.582  51.114 1.00 41.77  ?  68  GLU B CA    1 
ATOM   3228 C C     . GLU B 2 50  ? 14.783 -8.502  52.504 1.00 38.28  ?  68  GLU B C     1 
ATOM   3229 O O     . GLU B 2 50  ? 15.756 -7.770  52.668 1.00 37.54  ?  68  GLU B O     1 
ATOM   3230 C CB    . GLU B 2 50  ? 12.958 -7.656  50.977 1.00 44.58  ?  68  GLU B CB    1 
ATOM   3231 C CG    . GLU B 2 50  ? 12.446 -7.527  49.564 1.00 49.35  ?  68  GLU B CG    1 
ATOM   3232 C CD    . GLU B 2 50  ? 11.475 -6.379  49.373 1.00 56.14  ?  68  GLU B CD    1 
ATOM   3233 O OE1   . GLU B 2 50  ? 11.497 -5.451  50.198 1.00 55.97  ?  68  GLU B OE1   1 
ATOM   3234 O OE2   . GLU B 2 50  ? 10.704 -6.420  48.400 1.00 57.17  -1 68  GLU B OE2   1 
ATOM   3235 N N     . LYS B 2 51  ? 14.224 -9.234  53.458 1.00 38.33  ?  69  LYS B N     1 
ATOM   3236 C CA    . LYS B 2 51  ? 14.732 -9.220  54.850 1.00 38.98  ?  69  LYS B CA    1 
ATOM   3237 C C     . LYS B 2 51  ? 16.073 -9.962  54.937 1.00 39.47  ?  69  LYS B C     1 
ATOM   3238 O O     . LYS B 2 51  ? 16.965 -9.478  55.629 1.00 36.08  ?  69  LYS B O     1 
ATOM   3239 C CB    . LYS B 2 51  ? 13.628 -9.716  55.787 1.00 37.45  ?  69  LYS B CB    1 
ATOM   3240 C CG    . LYS B 2 51  ? 12.680 -8.635  56.283 1.00 41.32  ?  69  LYS B CG    1 
ATOM   3241 C CD    . LYS B 2 51  ? 11.261 -9.109  56.476 1.00 47.94  ?  69  LYS B CD    1 
ATOM   3242 C CE    . LYS B 2 51  ? 10.233 -8.054  56.129 1.00 55.58  ?  69  LYS B CE    1 
ATOM   3243 N NZ    . LYS B 2 51  ? 10.479 -7.464  54.792 1.00 58.04  ?  69  LYS B NZ    1 
ATOM   3244 N N     . LEU B 2 52  ? 16.215 -11.080 54.242 1.00 37.91  ?  70  LEU B N     1 
ATOM   3245 C CA    . LEU B 2 52  ? 17.507 -11.796 54.191 1.00 39.06  ?  70  LEU B CA    1 
ATOM   3246 C C     . LEU B 2 52  ? 18.517 -10.945 53.415 1.00 42.92  ?  70  LEU B C     1 
ATOM   3247 O O     . LEU B 2 52  ? 19.687 -10.949 53.794 1.00 41.11  ?  70  LEU B O     1 
ATOM   3248 C CB    . LEU B 2 52  ? 17.281 -13.131 53.476 1.00 47.17  ?  70  LEU B CB    1 
ATOM   3249 C CG    . LEU B 2 52  ? 16.647 -14.246 54.300 1.00 46.10  ?  70  LEU B CG    1 
ATOM   3250 C CD1   . LEU B 2 52  ? 16.400 -15.466 53.433 1.00 49.55  ?  70  LEU B CD1   1 
ATOM   3251 C CD2   . LEU B 2 52  ? 17.524 -14.608 55.485 1.00 51.24  ?  70  LEU B CD2   1 
ATOM   3252 N N     . TYR B 2 53  ? 18.072 -10.250 52.363 1.00 42.90  ?  71  TYR B N     1 
ATOM   3253 C CA    . TYR B 2 53  ? 18.989 -9.418  51.586 1.00 36.86  ?  71  TYR B CA    1 
ATOM   3254 C C     . TYR B 2 53  ? 19.559 -8.299  52.442 1.00 37.30  ?  71  TYR B C     1 
ATOM   3255 O O     . TYR B 2 53  ? 20.767 -8.031  52.399 1.00 42.34  ?  71  TYR B O     1 
ATOM   3256 C CB    . TYR B 2 53  ? 18.284 -8.851  50.346 1.00 34.43  ?  71  TYR B CB    1 
ATOM   3257 C CG    . TYR B 2 53  ? 19.081 -7.809  49.572 1.00 34.69  ?  71  TYR B CG    1 
ATOM   3258 C CD1   . TYR B 2 53  ? 19.887 -8.179  48.499 1.00 33.63  ?  71  TYR B CD1   1 
ATOM   3259 C CD2   . TYR B 2 53  ? 19.023 -6.451  49.909 1.00 33.11  ?  71  TYR B CD2   1 
ATOM   3260 C CE1   . TYR B 2 53  ? 20.625 -7.243  47.795 1.00 31.51  ?  71  TYR B CE1   1 
ATOM   3261 C CE2   . TYR B 2 53  ? 19.758 -5.502  49.213 1.00 30.41  ?  71  TYR B CE2   1 
ATOM   3262 C CZ    . TYR B 2 53  ? 20.562 -5.905  48.151 1.00 33.95  ?  71  TYR B CZ    1 
ATOM   3263 O OH    . TYR B 2 53  ? 21.305 -4.984  47.433 1.00 30.69  ?  71  TYR B OH    1 
ATOM   3264 N N     . PHE B 2 54  ? 18.712 -7.640  53.233 1.00 34.67  ?  72  PHE B N     1 
ATOM   3265 C CA    . PHE B 2 54  ? 19.204 -6.583  54.111 1.00 37.68  ?  72  PHE B CA    1 
ATOM   3266 C C     . PHE B 2 54  ? 20.228 -7.117  55.099 1.00 39.14  ?  72  PHE B C     1 
ATOM   3267 O O     . PHE B 2 54  ? 21.233 -6.456  55.397 1.00 37.07  ?  72  PHE B O     1 
ATOM   3268 C CB    . PHE B 2 54  ? 18.055 -5.952  54.876 1.00 35.62  ?  72  PHE B CB    1 
ATOM   3269 C CG    . PHE B 2 54  ? 18.490 -4.860  55.799 1.00 36.27  ?  72  PHE B CG    1 
ATOM   3270 C CD1   . PHE B 2 54  ? 18.587 -3.547  55.340 1.00 33.37  ?  72  PHE B CD1   1 
ATOM   3271 C CD2   . PHE B 2 54  ? 18.818 -5.138  57.119 1.00 33.00  ?  72  PHE B CD2   1 
ATOM   3272 C CE1   . PHE B 2 54  ? 18.990 -2.518  56.186 1.00 31.50  ?  72  PHE B CE1   1 
ATOM   3273 C CE2   . PHE B 2 54  ? 19.211 -4.119  57.980 1.00 35.12  ?  72  PHE B CE2   1 
ATOM   3274 C CZ    . PHE B 2 54  ? 19.301 -2.803  57.512 1.00 37.96  ?  72  PHE B CZ    1 
ATOM   3275 N N     . LYS B 2 55  ? 19.968 -8.282  55.642 1.00 39.01  ?  73  LYS B N     1 
ATOM   3276 C CA    . LYS B 2 55  ? 20.868 -8.872  56.591 1.00 41.49  ?  73  LYS B CA    1 
ATOM   3277 C C     . LYS B 2 55  ? 22.111 -9.469  55.890 1.00 43.65  ?  73  LYS B C     1 
ATOM   3278 O O     . LYS B 2 55  ? 22.958 -10.134 56.500 1.00 44.16  ?  73  LYS B O     1 
ATOM   3279 C CB    . LYS B 2 55  ? 20.099 -9.901  57.439 1.00 43.53  ?  73  LYS B CB    1 
ATOM   3280 C CG    . LYS B 2 55  ? 19.349 -9.335  58.697 1.00 42.73  ?  73  LYS B CG    1 
ATOM   3281 C CD    . LYS B 2 55  ? 20.294 -8.626  59.690 1.00 51.06  ?  73  LYS B CD    1 
ATOM   3282 C CE    . LYS B 2 55  ? 21.555 -9.493  60.058 1.00 62.61  ?  73  LYS B CE    1 
ATOM   3283 N NZ    . LYS B 2 55  ? 22.858 -8.696  60.111 1.00 60.78  ?  73  LYS B NZ    1 
ATOM   3284 N N     . GLN B 2 56  ? 22.263 -9.168  54.595 1.00 41.43  ?  74  GLN B N     1 
ATOM   3285 C CA    . GLN B 2 56  ? 23.416 -9.617  53.822 1.00 41.26  ?  74  GLN B CA    1 
ATOM   3286 C C     . GLN B 2 56  ? 23.538 -11.129 53.863 1.00 46.99  ?  74  GLN B C     1 
ATOM   3287 O O     . GLN B 2 56  ? 24.643 -11.677 53.912 1.00 46.61  ?  74  GLN B O     1 
ATOM   3288 C CB    . GLN B 2 56  ? 24.700 -8.996  54.326 1.00 42.39  ?  74  GLN B CB    1 
ATOM   3289 C CG    . GLN B 2 56  ? 25.068 -7.718  53.668 1.00 43.14  ?  74  GLN B CG    1 
ATOM   3290 C CD    . GLN B 2 56  ? 26.243 -7.111  54.379 1.00 43.63  ?  74  GLN B CD    1 
ATOM   3291 O OE1   . GLN B 2 56  ? 26.086 -6.433  55.402 1.00 41.48  ?  74  GLN B OE1   1 
ATOM   3292 N NE2   . GLN B 2 56  ? 27.437 -7.390  53.877 1.00 41.56  ?  74  GLN B NE2   1 
ATOM   3293 N N     . ASN B 2 57  ? 22.391 -11.803 53.874 1.00 48.84  ?  75  ASN B N     1 
ATOM   3294 C CA    . ASN B 2 57  ? 22.346 -13.259 53.974 1.00 54.25  ?  75  ASN B CA    1 
ATOM   3295 C C     . ASN B 2 57  ? 22.126 -13.878 52.596 1.00 52.56  ?  75  ASN B C     1 
ATOM   3296 O O     . ASN B 2 57  ? 21.169 -14.607 52.348 1.00 51.87  ?  75  ASN B O     1 
ATOM   3297 C CB    . ASN B 2 57  ? 21.267 -13.682 54.965 1.00 53.96  ?  75  ASN B CB    1 
ATOM   3298 C CG    . ASN B 2 57  ? 21.787 -14.680 55.974 1.00 68.71  ?  75  ASN B CG    1 
ATOM   3299 O OD1   . ASN B 2 57  ? 22.114 -15.828 55.621 1.00 70.09  ?  75  ASN B OD1   1 
ATOM   3300 N ND2   . ASN B 2 57  ? 21.912 -14.241 57.235 1.00 68.88  ?  75  ASN B ND2   1 
ATOM   3301 N N     . TYR B 2 58  ? 23.061 -13.569 51.694 1.00 49.25  ?  76  TYR B N     1 
ATOM   3302 C CA    . TYR B 2 58  ? 22.880 -13.909 50.288 1.00 44.80  ?  76  TYR B CA    1 
ATOM   3303 C C     . TYR B 2 58  ? 22.837 -15.412 50.084 1.00 48.11  ?  76  TYR B C     1 
ATOM   3304 O O     . TYR B 2 58  ? 22.118 -15.904 49.205 1.00 47.89  ?  76  TYR B O     1 
ATOM   3305 C CB    . TYR B 2 58  ? 24.002 -13.302 49.449 1.00 43.91  ?  76  TYR B CB    1 
ATOM   3306 C CG    . TYR B 2 58  ? 24.123 -11.796 49.503 1.00 42.75  ?  76  TYR B CG    1 
ATOM   3307 C CD1   . TYR B 2 58  ? 23.111 -11.001 50.052 1.00 41.94  ?  76  TYR B CD1   1 
ATOM   3308 C CD2   . TYR B 2 58  ? 25.250 -11.162 48.994 1.00 38.18  ?  76  TYR B CD2   1 
ATOM   3309 C CE1   . TYR B 2 58  ? 23.223 -9.615  50.087 1.00 35.73  ?  76  TYR B CE1   1 
ATOM   3310 C CE2   . TYR B 2 58  ? 25.366 -9.783  49.023 1.00 38.45  ?  76  TYR B CE2   1 
ATOM   3311 C CZ    . TYR B 2 58  ? 24.352 -9.018  49.569 1.00 35.24  ?  76  TYR B CZ    1 
ATOM   3312 O OH    . TYR B 2 58  ? 24.494 -7.659  49.590 1.00 34.03  ?  76  TYR B OH    1 
ATOM   3313 N N     . LYS B 2 59  ? 23.617 -16.160 50.873 1.00 53.34  ?  77  LYS B N     1 
ATOM   3314 C CA    . LYS B 2 59  ? 23.664 -17.607 50.692 1.00 53.32  ?  77  LYS B CA    1 
ATOM   3315 C C     . LYS B 2 59  ? 22.292 -18.224 50.926 1.00 53.68  ?  77  LYS B C     1 
ATOM   3316 O O     . LYS B 2 59  ? 21.768 -18.933 50.062 1.00 56.16  ?  77  LYS B O     1 
ATOM   3317 C CB    . LYS B 2 59  ? 24.717 -18.230 51.611 1.00 59.33  ?  77  LYS B CB    1 
ATOM   3318 C CG    . LYS B 2 59  ? 25.374 -19.491 51.034 1.00 63.33  ?  77  LYS B CG    1 
ATOM   3319 C CD    . LYS B 2 59  ? 25.767 -20.504 52.119 1.00 60.04  ?  77  LYS B CD    1 
ATOM   3320 C CE    . LYS B 2 59  ? 24.629 -21.454 52.452 1.00 59.55  ?  77  LYS B CE    1 
ATOM   3321 N NZ    . LYS B 2 59  ? 25.139 -22.704 53.088 1.00 69.86  ?  77  LYS B NZ    1 
ATOM   3322 N N     . GLU B 2 60  ? 21.676 -17.936 52.082 1.00 55.94  ?  78  GLU B N     1 
ATOM   3323 C CA    . GLU B 2 60  ? 20.336 -18.459 52.353 1.00 57.20  ?  78  GLU B CA    1 
ATOM   3324 C C     . GLU B 2 60  ? 19.338 -18.001 51.294 1.00 55.51  ?  78  GLU B C     1 
ATOM   3325 O O     . GLU B 2 60  ? 18.520 -18.799 50.818 1.00 61.41  ?  78  GLU B O     1 
ATOM   3326 C CB    . GLU B 2 60  ? 19.859 -18.049 53.753 1.00 54.30  ?  78  GLU B CB    1 
ATOM   3327 C CG    . GLU B 2 60  ? 18.946 -19.101 54.399 1.00 58.79  ?  78  GLU B CG    1 
ATOM   3328 C CD    . GLU B 2 60  ? 18.239 -18.639 55.688 1.00 66.82  ?  78  GLU B CD    1 
ATOM   3329 O OE1   . GLU B 2 60  ? 16.997 -18.787 55.792 1.00 64.38  ?  78  GLU B OE1   1 
ATOM   3330 O OE2   . GLU B 2 60  ? 18.917 -18.151 56.618 1.00 74.73  -1 78  GLU B OE2   1 
ATOM   3331 N N     . ALA B 2 61  ? 19.408 -16.728 50.889 1.00 49.94  ?  79  ALA B N     1 
ATOM   3332 C CA    . ALA B 2 61  ? 18.394 -16.174 49.998 1.00 49.23  ?  79  ALA B CA    1 
ATOM   3333 C C     . ALA B 2 61  ? 18.572 -16.658 48.567 1.00 49.83  ?  79  ALA B C     1 
ATOM   3334 O O     . ALA B 2 61  ? 17.582 -16.883 47.866 1.00 48.11  ?  79  ALA B O     1 
ATOM   3335 C CB    . ALA B 2 61  ? 18.416 -14.649 50.047 1.00 49.18  ?  79  ALA B CB    1 
ATOM   3336 N N     . ILE B 2 62  ? 19.816 -16.809 48.103 1.00 48.80  ?  80  ILE B N     1 
ATOM   3337 C CA    . ILE B 2 62  ? 20.020 -17.442 46.802 1.00 52.00  ?  80  ILE B CA    1 
ATOM   3338 C C     . ILE B 2 62  ? 19.536 -18.886 46.847 1.00 57.57  ?  80  ILE B C     1 
ATOM   3339 O O     . ILE B 2 62  ? 18.951 -19.400 45.879 1.00 55.43  ?  80  ILE B O     1 
ATOM   3340 C CB    . ILE B 2 62  ? 21.494 -17.355 46.371 1.00 51.71  ?  80  ILE B CB    1 
ATOM   3341 C CG1   . ILE B 2 62  ? 21.803 -15.978 45.806 1.00 47.87  ?  80  ILE B CG1   1 
ATOM   3342 C CG2   . ILE B 2 62  ? 21.804 -18.385 45.299 1.00 47.35  ?  80  ILE B CG2   1 
ATOM   3343 C CD1   . ILE B 2 62  ? 23.244 -15.808 45.480 1.00 43.86  ?  80  ILE B CD1   1 
ATOM   3344 N N     . GLU B 2 63  ? 19.773 -19.562 47.976 1.00 54.80  ?  81  GLU B N     1 
ATOM   3345 C CA    . GLU B 2 63  ? 19.242 -20.904 48.171 1.00 57.73  ?  81  GLU B CA    1 
ATOM   3346 C C     . GLU B 2 63  ? 17.720 -20.900 48.068 1.00 59.82  ?  81  GLU B C     1 
ATOM   3347 O O     . GLU B 2 63  ? 17.131 -21.681 47.308 1.00 58.52  ?  81  GLU B O     1 
ATOM   3348 C CB    . GLU B 2 63  ? 19.714 -21.431 49.525 1.00 61.35  ?  81  GLU B CB    1 
ATOM   3349 C CG    . GLU B 2 63  ? 19.458 -22.896 49.791 1.00 70.95  ?  81  GLU B CG    1 
ATOM   3350 C CD    . GLU B 2 63  ? 19.179 -23.169 51.271 1.00 81.51  ?  81  GLU B CD    1 
ATOM   3351 O OE1   . GLU B 2 63  ? 19.435 -24.312 51.724 1.00 82.65  ?  81  GLU B OE1   1 
ATOM   3352 O OE2   . GLU B 2 63  ? 18.703 -22.239 51.979 1.00 76.82  -1 81  GLU B OE2   1 
ATOM   3353 N N     . LYS B 2 64  ? 17.070 -19.982 48.793 1.00 55.62  ?  82  LYS B N     1 
ATOM   3354 C CA    . LYS B 2 64  ? 15.615 -19.889 48.758 1.00 55.06  ?  82  LYS B CA    1 
ATOM   3355 C C     . LYS B 2 64  ? 15.085 -19.523 47.370 1.00 55.45  ?  82  LYS B C     1 
ATOM   3356 O O     . LYS B 2 64  ? 13.942 -19.862 47.047 1.00 56.67  ?  82  LYS B O     1 
ATOM   3357 C CB    . LYS B 2 64  ? 15.134 -18.882 49.810 1.00 47.86  ?  82  LYS B CB    1 
ATOM   3358 C CG    . LYS B 2 64  ? 15.012 -19.499 51.184 1.00 52.26  ?  82  LYS B CG    1 
ATOM   3359 C CD    . LYS B 2 64  ? 14.331 -18.623 52.213 1.00 49.88  ?  82  LYS B CD    1 
ATOM   3360 C CE    . LYS B 2 64  ? 14.623 -19.155 53.632 1.00 53.77  ?  82  LYS B CE    1 
ATOM   3361 N NZ    . LYS B 2 64  ? 13.643 -20.176 54.139 1.00 57.25  ?  82  LYS B NZ    1 
ATOM   3362 N N     . ILE B 2 65  ? 15.886 -18.849 46.536 1.00 53.64  ?  83  ILE B N     1 
ATOM   3363 C CA    . ILE B 2 65  ? 15.404 -18.388 45.229 1.00 57.42  ?  83  ILE B CA    1 
ATOM   3364 C C     . ILE B 2 65  ? 15.416 -19.524 44.202 1.00 59.04  ?  83  ILE B C     1 
ATOM   3365 O O     . ILE B 2 65  ? 14.432 -19.748 43.492 1.00 53.95  ?  83  ILE B O     1 
ATOM   3366 C CB    . ILE B 2 65  ? 16.228 -17.179 44.741 1.00 54.14  ?  83  ILE B CB    1 
ATOM   3367 C CG1   . ILE B 2 65  ? 15.964 -15.958 45.610 1.00 55.59  ?  83  ILE B CG1   1 
ATOM   3368 C CG2   . ILE B 2 65  ? 15.885 -16.817 43.299 1.00 45.31  ?  83  ILE B CG2   1 
ATOM   3369 C CD1   . ILE B 2 65  ? 16.899 -14.793 45.300 1.00 49.90  ?  83  ILE B CD1   1 
ATOM   3370 N N     . LEU B 2 66  ? 16.532 -20.245 44.083 1.00 58.36  ?  84  LEU B N     1 
ATOM   3371 C CA    . LEU B 2 66  ? 16.551 -21.411 43.207 1.00 60.11  ?  84  LEU B CA    1 
ATOM   3372 C C     . LEU B 2 66  ? 15.469 -22.413 43.603 1.00 66.44  ?  84  LEU B C     1 
ATOM   3373 O O     . LEU B 2 66  ? 14.733 -22.919 42.746 1.00 61.47  ?  84  LEU B O     1 
ATOM   3374 C CB    . LEU B 2 66  ? 17.935 -22.061 43.234 1.00 57.42  ?  84  LEU B CB    1 
ATOM   3375 C CG    . LEU B 2 66  ? 19.068 -21.087 42.943 1.00 52.65  ?  84  LEU B CG    1 
ATOM   3376 C CD1   . LEU B 2 66  ? 20.430 -21.709 43.157 1.00 44.15  ?  84  LEU B CD1   1 
ATOM   3377 C CD2   . LEU B 2 66  ? 18.915 -20.606 41.519 1.00 52.40  ?  84  LEU B CD2   1 
ATOM   3378 N N     . ASP B 2 67  ? 15.347 -22.697 44.909 1.00 66.49  ?  85  ASP B N     1 
ATOM   3379 C CA    . ASP B 2 67  ? 14.384 -23.694 45.370 1.00 68.48  ?  85  ASP B CA    1 
ATOM   3380 C C     . ASP B 2 67  ? 12.945 -23.249 45.113 1.00 67.04  ?  85  ASP B C     1 
ATOM   3381 O O     . ASP B 2 67  ? 12.130 -24.038 44.622 1.00 69.30  ?  85  ASP B O     1 
ATOM   3382 C CB    . ASP B 2 67  ? 14.623 -24.002 46.848 1.00 75.83  ?  85  ASP B CB    1 
ATOM   3383 C CG    . ASP B 2 67  ? 15.835 -24.928 47.066 1.00 89.15  ?  85  ASP B CG    1 
ATOM   3384 O OD1   . ASP B 2 67  ? 16.470 -25.328 46.054 1.00 87.63  ?  85  ASP B OD1   1 
ATOM   3385 O OD2   . ASP B 2 67  ? 16.142 -25.268 48.239 1.00 89.15  -1 85  ASP B OD2   1 
ATOM   3386 N N     . PHE B 2 68  ? 12.615 -21.990 45.412 1.00 65.09  ?  86  PHE B N     1 
ATOM   3387 C CA    . PHE B 2 68  ? 11.338 -21.427 44.958 1.00 65.19  ?  86  PHE B CA    1 
ATOM   3388 C C     . PHE B 2 68  ? 11.182 -21.528 43.445 1.00 64.92  ?  86  PHE B C     1 
ATOM   3389 O O     . PHE B 2 68  ? 10.071 -21.715 42.936 1.00 63.78  ?  86  PHE B O     1 
ATOM   3390 C CB    . PHE B 2 68  ? 11.227 -19.967 45.391 1.00 61.09  ?  86  PHE B CB    1 
ATOM   3391 C CG    . PHE B 2 68  ? 9.939  -19.285 44.982 1.00 60.39  ?  86  PHE B CG    1 
ATOM   3392 C CD1   . PHE B 2 68  ? 8.898  -19.130 45.890 1.00 60.53  ?  86  PHE B CD1   1 
ATOM   3393 C CD2   . PHE B 2 68  ? 9.788  -18.747 43.711 1.00 61.44  ?  86  PHE B CD2   1 
ATOM   3394 C CE1   . PHE B 2 68  ? 7.724  -18.481 45.526 1.00 62.03  ?  86  PHE B CE1   1 
ATOM   3395 C CE2   . PHE B 2 68  ? 8.611  -18.088 43.340 1.00 58.93  ?  86  PHE B CE2   1 
ATOM   3396 C CZ    . PHE B 2 68  ? 7.582  -17.957 44.246 1.00 61.55  ?  86  PHE B CZ    1 
ATOM   3397 N N     . CYS B 2 69  ? 12.285 -21.393 42.707 1.00 69.33  ?  87  CYS B N     1 
ATOM   3398 C CA    . CYS B 2 69  ? 12.234 -21.442 41.249 1.00 65.72  ?  87  CYS B CA    1 
ATOM   3399 C C     . CYS B 2 69  ? 12.017 -22.855 40.721 1.00 69.71  ?  87  CYS B C     1 
ATOM   3400 O O     . CYS B 2 69  ? 11.435 -23.018 39.644 1.00 69.82  ?  87  CYS B O     1 
ATOM   3401 C CB    . CYS B 2 69  ? 13.525 -20.876 40.669 1.00 70.31  ?  87  CYS B CB    1 
ATOM   3402 S SG    . CYS B 2 69  ? 13.444 -19.164 40.135 1.00 67.23  ?  87  CYS B SG    1 
ATOM   3403 N N     . LYS B 2 70  ? 12.522 -23.879 41.428 1.00 73.95  ?  88  LYS B N     1 
ATOM   3404 C CA    . LYS B 2 70  ? 12.210 -25.267 41.080 1.00 73.64  ?  88  LYS B CA    1 
ATOM   3405 C C     . LYS B 2 70  ? 10.733 -25.570 41.328 1.00 70.84  ?  88  LYS B C     1 
ATOM   3406 O O     . LYS B 2 70  ? 10.032 -26.062 40.436 1.00 68.06  ?  88  LYS B O     1 
ATOM   3407 C CB    . LYS B 2 70  ? 13.101 -26.239 41.878 1.00 73.41  ?  88  LYS B CB    1 
ATOM   3408 C CG    . LYS B 2 70  ? 14.395 -26.700 41.175 1.00 79.94  ?  88  LYS B CG    1 
ATOM   3409 C CD    . LYS B 2 70  ? 15.459 -27.266 42.162 1.00 87.49  ?  88  LYS B CD    1 
ATOM   3410 C CE    . LYS B 2 70  ? 16.826 -26.526 42.050 1.00 93.39  ?  88  LYS B CE    1 
ATOM   3411 N NZ    . LYS B 2 70  ? 17.864 -26.857 43.099 1.00 84.65  ?  88  LYS B NZ    1 
ATOM   3412 N N     . LYS B 2 71  ? 10.232 -25.260 42.541 1.00 68.35  ?  89  LYS B N     1 
ATOM   3413 C CA    . LYS B 2 71  ? 8.875  -25.621 42.976 1.00 67.76  ?  89  LYS B CA    1 
ATOM   3414 C C     . LYS B 2 71  ? 7.776  -24.762 42.331 1.00 63.84  ?  89  LYS B C     1 
ATOM   3415 O O     . LYS B 2 71  ? 6.613  -24.833 42.736 1.00 64.96  ?  89  LYS B O     1 
ATOM   3416 C CB    . LYS B 2 71  ? 8.787  -25.557 44.506 1.00 65.46  ?  89  LYS B CB    1 
ATOM   3417 C CG    . LYS B 2 71  ? 9.738  -26.545 45.215 1.00 69.37  ?  89  LYS B CG    1 
ATOM   3418 C CD    . LYS B 2 71  ? 10.485 -25.917 46.406 1.00 69.62  ?  89  LYS B CD    1 
ATOM   3419 C CE    . LYS B 2 71  ? 11.699 -26.751 46.878 1.00 73.44  ?  89  LYS B CE    1 
ATOM   3420 N NZ    . LYS B 2 71  ? 12.821 -26.907 45.882 1.00 76.44  ?  89  LYS B NZ    1 
ATOM   3421 N N     . ASN B 2 72  ? 8.119  -23.955 41.333 1.00 64.13  ?  90  ASN B N     1 
ATOM   3422 C CA    . ASN B 2 72  ? 7.148  -23.197 40.556 1.00 63.37  ?  90  ASN B CA    1 
ATOM   3423 C C     . ASN B 2 72  ? 7.521  -23.220 39.079 1.00 65.38  ?  90  ASN B C     1 
ATOM   3424 O O     . ASN B 2 72  ? 7.111  -22.336 38.319 1.00 65.05  ?  90  ASN B O     1 
ATOM   3425 C CB    . ASN B 2 72  ? 7.046  -21.754 41.055 1.00 61.53  ?  90  ASN B CB    1 
ATOM   3426 C CG    . ASN B 2 72  ? 6.232  -21.628 42.328 1.00 59.30  ?  90  ASN B CG    1 
ATOM   3427 O OD1   . ASN B 2 72  ? 5.006  -21.634 42.296 1.00 61.44  ?  90  ASN B OD1   1 
ATOM   3428 N ND2   . ASN B 2 72  ? 6.911  -21.490 43.451 1.00 58.21  ?  90  ASN B ND2   1 
ATOM   3429 N N     . GLU B 2 73  ? 8.275  -24.248 38.666 1.00 68.19  ?  91  GLU B N     1 
ATOM   3430 C CA    . GLU B 2 73  ? 8.929  -24.278 37.357 1.00 69.14  ?  91  GLU B CA    1 
ATOM   3431 C C     . GLU B 2 73  ? 7.941  -24.081 36.206 1.00 74.39  ?  91  GLU B C     1 
ATOM   3432 O O     . GLU B 2 73  ? 8.253  -23.389 35.225 1.00 73.32  ?  91  GLU B O     1 
ATOM   3433 C CB    . GLU B 2 73  ? 9.676  -25.605 37.205 1.00 74.29  ?  91  GLU B CB    1 
ATOM   3434 C CG    . GLU B 2 73  ? 10.817 -25.613 36.179 1.00 82.99  ?  91  GLU B CG    1 
ATOM   3435 C CD    . GLU B 2 73  ? 12.126 -26.230 36.718 1.00 88.13  ?  91  GLU B CD    1 
ATOM   3436 O OE1   . GLU B 2 73  ? 13.192 -25.994 36.095 1.00 86.74  ?  91  GLU B OE1   1 
ATOM   3437 O OE2   . GLU B 2 73  ? 12.096 -26.943 37.756 1.00 84.72  -1 91  GLU B OE2   1 
ATOM   3438 N N     . SER B 2 74  ? 6.757  -24.706 36.290 1.00 74.79  ?  92  SER B N     1 
ATOM   3439 C CA    . SER B 2 74  ? 5.760  -24.612 35.224 1.00 69.35  ?  92  SER B CA    1 
ATOM   3440 C C     . SER B 2 74  ? 5.200  -23.207 35.076 1.00 70.55  ?  92  SER B C     1 
ATOM   3441 O O     . SER B 2 74  ? 4.615  -22.893 34.037 1.00 69.71  ?  92  SER B O     1 
ATOM   3442 C CB    . SER B 2 74  ? 4.614  -25.578 35.493 1.00 72.10  ?  92  SER B CB    1 
ATOM   3443 O OG    . SER B 2 74  ? 3.912  -25.183 36.663 1.00 74.08  ?  92  SER B OG    1 
ATOM   3444 N N     . LEU B 2 75  ? 5.366  -22.364 36.094 1.00 70.14  ?  93  LEU B N     1 
ATOM   3445 C CA    . LEU B 2 75  ? 4.866  -20.997 36.090 1.00 69.70  ?  93  LEU B CA    1 
ATOM   3446 C C     . LEU B 2 75  ? 5.775  -20.018 35.358 1.00 70.31  ?  93  LEU B C     1 
ATOM   3447 O O     . LEU B 2 75  ? 5.366  -18.867 35.154 1.00 66.14  ?  93  LEU B O     1 
ATOM   3448 C CB    . LEU B 2 75  ? 4.685  -20.514 37.529 1.00 67.44  ?  93  LEU B CB    1 
ATOM   3449 C CG    . LEU B 2 75  ? 3.249  -20.412 38.004 1.00 64.06  ?  93  LEU B CG    1 
ATOM   3450 C CD1   . LEU B 2 75  ? 2.548  -19.270 37.282 1.00 62.83  ?  93  LEU B CD1   1 
ATOM   3451 C CD2   . LEU B 2 75  ? 2.579  -21.733 37.740 1.00 67.84  ?  93  LEU B CD2   1 
ATOM   3452 N N     . LEU B 2 76  ? 6.982  -20.447 34.964 1.00 70.06  ?  94  LEU B N     1 
ATOM   3453 C CA    . LEU B 2 76  ? 8.063  -19.552 34.558 1.00 67.10  ?  94  LEU B CA    1 
ATOM   3454 C C     . LEU B 2 76  ? 8.616  -19.921 33.184 1.00 72.62  ?  94  LEU B C     1 
ATOM   3455 O O     . LEU B 2 76  ? 8.023  -20.722 32.452 1.00 82.34  ?  94  LEU B O     1 
ATOM   3456 C CB    . LEU B 2 76  ? 9.210  -19.600 35.585 1.00 66.11  ?  94  LEU B CB    1 
ATOM   3457 C CG    . LEU B 2 76  ? 9.246  -18.844 36.914 1.00 57.40  ?  94  LEU B CG    1 
ATOM   3458 C CD1   . LEU B 2 76  ? 8.314  -17.637 36.934 1.00 57.18  ?  94  LEU B CD1   1 
ATOM   3459 C CD2   . LEU B 2 76  ? 8.989  -19.766 38.085 1.00 53.19  ?  94  LEU B CD2   1 
ATOM   3460 N N     . SER B 2 77  ? 9.755  -19.341 32.822 1.00 69.42  ?  95  SER B N     1 
ATOM   3461 C CA    . SER B 2 77  ? 10.494 -19.774 31.651 1.00 66.56  ?  95  SER B CA    1 
ATOM   3462 C C     . SER B 2 77  ? 11.540 -20.799 32.074 1.00 69.64  ?  95  SER B C     1 
ATOM   3463 O O     . SER B 2 77  ? 12.297 -20.570 33.021 1.00 67.61  ?  95  SER B O     1 
ATOM   3464 C CB    . SER B 2 77  ? 11.155 -18.580 30.965 1.00 69.40  ?  95  SER B CB    1 
ATOM   3465 O OG    . SER B 2 77  ? 12.269 -18.985 30.198 1.00 80.13  ?  95  SER B OG    1 
ATOM   3466 N N     . GLU B 2 78  ? 11.565 -21.938 31.386 1.00 76.21  ?  96  GLU B N     1 
ATOM   3467 C CA    . GLU B 2 78  ? 12.635 -22.900 31.619 1.00 75.34  ?  96  GLU B CA    1 
ATOM   3468 C C     . GLU B 2 78  ? 13.961 -22.356 31.120 1.00 70.31  ?  96  GLU B C     1 
ATOM   3469 O O     . GLU B 2 78  ? 15.027 -22.728 31.627 1.00 68.14  ?  96  GLU B O     1 
ATOM   3470 C CB    . GLU B 2 78  ? 12.320 -24.213 30.916 1.00 79.14  ?  96  GLU B CB    1 
ATOM   3471 C CG    . GLU B 2 78  ? 12.301 -24.060 29.408 1.00 83.29  ?  96  GLU B CG    1 
ATOM   3472 C CD    . GLU B 2 78  ? 11.056 -24.647 28.784 1.00 93.04  ?  96  GLU B CD    1 
ATOM   3473 O OE1   . GLU B 2 78  ? 10.666 -25.781 29.176 1.00 93.30  ?  96  GLU B OE1   1 
ATOM   3474 O OE2   . GLU B 2 78  ? 10.470 -23.966 27.903 1.00 97.93  -1 96  GLU B OE2   1 
ATOM   3475 N N     . GLN B 2 79  ? 13.909 -21.489 30.111 1.00 71.33  ?  97  GLN B N     1 
ATOM   3476 C CA    . GLN B 2 79  ? 15.117 -20.827 29.639 1.00 72.73  ?  97  GLN B CA    1 
ATOM   3477 C C     . GLN B 2 79  ? 15.709 -19.923 30.715 1.00 69.95  ?  97  GLN B C     1 
ATOM   3478 O O     . GLN B 2 79  ? 16.933 -19.888 30.897 1.00 67.47  ?  97  GLN B O     1 
ATOM   3479 C CB    . GLN B 2 79  ? 14.801 -20.035 28.371 1.00 73.87  ?  97  GLN B CB    1 
ATOM   3480 C CG    . GLN B 2 79  ? 16.021 -19.529 27.633 1.00 73.55  ?  97  GLN B CG    1 
ATOM   3481 C CD    . GLN B 2 79  ? 15.696 -18.384 26.690 1.00 79.18  ?  97  GLN B CD    1 
ATOM   3482 O OE1   . GLN B 2 79  ? 16.386 -17.357 26.673 1.00 79.59  ?  97  GLN B OE1   1 
ATOM   3483 N NE2   . GLN B 2 79  ? 14.648 -18.560 25.887 1.00 81.10  ?  97  GLN B NE2   1 
ATOM   3484 N N     . VAL B 2 80  ? 14.853 -19.201 31.452 1.00 69.91  ?  98  VAL B N     1 
ATOM   3485 C CA    . VAL B 2 80  ? 15.316 -18.232 32.445 1.00 62.75  ?  98  VAL B CA    1 
ATOM   3486 C C     . VAL B 2 80  ? 15.769 -18.915 33.729 1.00 62.67  ?  98  VAL B C     1 
ATOM   3487 O O     . VAL B 2 80  ? 16.763 -18.500 34.333 1.00 62.07  ?  98  VAL B O     1 
ATOM   3488 C CB    . VAL B 2 80  ? 14.230 -17.183 32.731 1.00 64.80  ?  98  VAL B CB    1 
ATOM   3489 C CG1   . VAL B 2 80  ? 14.640 -16.313 33.913 1.00 61.56  ?  98  VAL B CG1   1 
ATOM   3490 C CG2   . VAL B 2 80  ? 13.971 -16.326 31.497 1.00 69.36  ?  98  VAL B CG2   1 
ATOM   3491 N N     . VAL B 2 81  ? 15.059 -19.954 34.187 1.00 63.07  ?  99  VAL B N     1 
ATOM   3492 C CA    . VAL B 2 81  ? 15.533 -20.666 35.375 1.00 59.74  ?  99  VAL B CA    1 
ATOM   3493 C C     . VAL B 2 81  ? 16.833 -21.419 35.092 1.00 61.63  ?  99  VAL B C     1 
ATOM   3494 O O     . VAL B 2 81  ? 17.664 -21.569 35.994 1.00 62.11  ?  99  VAL B O     1 
ATOM   3495 C CB    . VAL B 2 81  ? 14.471 -21.625 35.948 1.00 58.60  ?  99  VAL B CB    1 
ATOM   3496 C CG1   . VAL B 2 81  ? 13.258 -20.865 36.452 1.00 55.54  ?  99  VAL B CG1   1 
ATOM   3497 C CG2   . VAL B 2 81  ? 14.104 -22.673 34.924 1.00 64.76  ?  99  VAL B CG2   1 
ATOM   3498 N N     . GLN B 2 82  ? 17.047 -21.916 33.869 1.00 61.11  ?  100 GLN B N     1 
ATOM   3499 C CA    . GLN B 2 82  ? 18.330 -22.563 33.600 1.00 64.63  ?  100 GLN B CA    1 
ATOM   3500 C C     . GLN B 2 82  ? 19.487 -21.582 33.781 1.00 64.59  ?  100 GLN B C     1 
ATOM   3501 O O     . GLN B 2 82  ? 20.478 -21.905 34.449 1.00 65.31  ?  100 GLN B O     1 
ATOM   3502 C CB    . GLN B 2 82  ? 18.357 -23.193 32.198 1.00 75.06  ?  100 GLN B CB    1 
ATOM   3503 C CG    . GLN B 2 82  ? 19.714 -23.870 31.780 1.00 78.50  ?  100 GLN B CG    1 
ATOM   3504 C CD    . GLN B 2 82  ? 20.490 -24.575 32.928 1.00 91.27  ?  100 GLN B CD    1 
ATOM   3505 O OE1   . GLN B 2 82  ? 19.987 -24.746 34.046 1.00 90.19  ?  100 GLN B OE1   1 
ATOM   3506 N NE2   . GLN B 2 82  ? 21.723 -24.995 32.632 1.00 88.17  ?  100 GLN B NE2   1 
ATOM   3507 N N     . ARG B 2 83  ? 19.378 -20.373 33.207 1.00 66.42  ?  101 ARG B N     1 
ATOM   3508 C CA    . ARG B 2 83  ? 20.430 -19.368 33.376 1.00 63.87  ?  101 ARG B CA    1 
ATOM   3509 C C     . ARG B 2 83  ? 20.586 -18.958 34.836 1.00 61.18  ?  101 ARG B C     1 
ATOM   3510 O O     . ARG B 2 83  ? 21.714 -18.791 35.314 1.00 61.61  ?  101 ARG B O     1 
ATOM   3511 C CB    . ARG B 2 83  ? 20.148 -18.135 32.518 1.00 62.89  ?  101 ARG B CB    1 
ATOM   3512 C CG    . ARG B 2 83  ? 20.105 -18.406 31.023 1.00 72.92  ?  101 ARG B CG    1 
ATOM   3513 C CD    . ARG B 2 83  ? 21.500 -18.482 30.405 1.00 75.02  ?  101 ARG B CD    1 
ATOM   3514 N NE    . ARG B 2 83  ? 22.521 -17.778 31.182 1.00 75.02  ?  101 ARG B NE    1 
ATOM   3515 C CZ    . ARG B 2 83  ? 22.869 -16.498 31.016 1.00 74.60  ?  101 ARG B CZ    1 
ATOM   3516 N NH1   . ARG B 2 83  ? 22.267 -15.728 30.096 1.00 66.29  ?  101 ARG B NH1   1 
ATOM   3517 N NH2   . ARG B 2 83  ? 23.830 -15.987 31.787 1.00 68.66  ?  101 ARG B NH2   1 
ATOM   3518 N N     . LEU B 2 84  ? 19.469 -18.793 35.561 1.00 54.99  ?  102 LEU B N     1 
ATOM   3519 C CA    . LEU B 2 84  ? 19.537 -18.488 36.993 1.00 51.81  ?  102 LEU B CA    1 
ATOM   3520 C C     . LEU B 2 84  ? 20.315 -19.548 37.756 1.00 53.80  ?  102 LEU B C     1 
ATOM   3521 O O     . LEU B 2 84  ? 21.249 -19.231 38.502 1.00 51.86  ?  102 LEU B O     1 
ATOM   3522 C CB    . LEU B 2 84  ? 18.141 -18.378 37.582 1.00 49.28  ?  102 LEU B CB    1 
ATOM   3523 C CG    . LEU B 2 84  ? 17.371 -17.153 37.132 1.00 51.85  ?  102 LEU B CG    1 
ATOM   3524 C CD1   . LEU B 2 84  ? 15.911 -17.290 37.537 1.00 47.33  ?  102 LEU B CD1   1 
ATOM   3525 C CD2   . LEU B 2 84  ? 18.022 -15.905 37.703 1.00 45.54  ?  102 LEU B CD2   1 
ATOM   3526 N N     . ALA B 2 85  ? 19.916 -20.814 37.607 1.00 53.58  ?  103 ALA B N     1 
ATOM   3527 C CA    . ALA B 2 85  ? 20.560 -21.887 38.343 1.00 48.64  ?  103 ALA B CA    1 
ATOM   3528 C C     . ALA B 2 85  ? 21.946 -22.196 37.811 1.00 51.28  ?  103 ALA B C     1 
ATOM   3529 O O     . ALA B 2 85  ? 22.783 -22.692 38.564 1.00 48.17  ?  103 ALA B O     1 
ATOM   3530 C CB    . ALA B 2 85  ? 19.697 -23.138 38.312 1.00 43.41  ?  103 ALA B CB    1 
ATOM   3531 N N     . GLU B 2 86  ? 22.220 -21.913 36.544 1.00 53.71  ?  104 GLU B N     1 
ATOM   3532 C CA    . GLU B 2 86  ? 23.562 -22.196 36.057 1.00 60.85  ?  104 GLU B CA    1 
ATOM   3533 C C     . GLU B 2 86  ? 24.559 -21.151 36.509 1.00 63.89  ?  104 GLU B C     1 
ATOM   3534 O O     . GLU B 2 86  ? 25.747 -21.459 36.677 1.00 66.50  ?  104 GLU B O     1 
ATOM   3535 C CB    . GLU B 2 86  ? 23.601 -22.265 34.538 1.00 66.31  ?  104 GLU B CB    1 
ATOM   3536 C CG    . GLU B 2 86  ? 25.018 -22.140 33.998 1.00 67.94  ?  104 GLU B CG    1 
ATOM   3537 C CD    . GLU B 2 86  ? 25.087 -21.269 32.764 1.00 87.99  ?  104 GLU B CD    1 
ATOM   3538 O OE1   . GLU B 2 86  ? 24.356 -21.569 31.780 1.00 95.47  ?  104 GLU B OE1   1 
ATOM   3539 O OE2   . GLU B 2 86  ? 25.863 -20.280 32.786 1.00 89.27  -1 104 GLU B OE2   1 
ATOM   3540 N N     . VAL B 2 87  ? 24.097 -19.915 36.686 1.00 62.09  ?  105 VAL B N     1 
ATOM   3541 C CA    . VAL B 2 87  ? 24.986 -18.817 37.024 1.00 59.61  ?  105 VAL B CA    1 
ATOM   3542 C C     . VAL B 2 87  ? 25.233 -18.728 38.528 1.00 57.26  ?  105 VAL B C     1 
ATOM   3543 O O     . VAL B 2 87  ? 26.302 -18.255 38.940 1.00 54.47  ?  105 VAL B O     1 
ATOM   3544 C CB    . VAL B 2 87  ? 24.395 -17.529 36.425 1.00 56.36  ?  105 VAL B CB    1 
ATOM   3545 C CG1   . VAL B 2 87  ? 24.059 -16.512 37.507 1.00 52.27  ?  105 VAL B CG1   1 
ATOM   3546 C CG2   . VAL B 2 87  ? 25.333 -16.973 35.367 1.00 58.29  ?  105 VAL B CG2   1 
ATOM   3547 N N     . ALA B 2 88  ? 24.318 -19.266 39.344 1.00 55.92  ?  106 ALA B N     1 
ATOM   3548 C CA    . ALA B 2 88  ? 24.367 -19.114 40.799 1.00 51.81  ?  106 ALA B CA    1 
ATOM   3549 C C     . ALA B 2 88  ? 25.622 -19.680 41.459 1.00 54.61  ?  106 ALA B C     1 
ATOM   3550 O O     . ALA B 2 88  ? 26.211 -18.985 42.306 1.00 55.86  ?  106 ALA B O     1 
ATOM   3551 C CB    . ALA B 2 88  ? 23.104 -19.738 41.400 1.00 48.41  ?  106 ALA B CB    1 
ATOM   3552 N N     . PRO B 2 89  ? 26.069 -20.905 41.168 1.00 54.04  ?  107 PRO B N     1 
ATOM   3553 C CA    . PRO B 2 89  ? 27.200 -21.468 41.926 1.00 54.09  ?  107 PRO B CA    1 
ATOM   3554 C C     . PRO B 2 89  ? 28.514 -20.722 41.727 1.00 56.64  ?  107 PRO B C     1 
ATOM   3555 O O     . PRO B 2 89  ? 29.451 -20.932 42.520 1.00 52.01  ?  107 PRO B O     1 
ATOM   3556 C CB    . PRO B 2 89  ? 27.291 -22.904 41.401 1.00 50.65  ?  107 PRO B CB    1 
ATOM   3557 C CG    . PRO B 2 89  ? 26.658 -22.853 40.049 1.00 52.04  ?  107 PRO B CG    1 
ATOM   3558 C CD    . PRO B 2 89  ? 25.555 -21.853 40.167 1.00 54.83  ?  107 PRO B CD    1 
ATOM   3559 N N     . ARG B 2 90  ? 28.609 -19.860 40.710 1.00 54.98  ?  108 ARG B N     1 
ATOM   3560 C CA    . ARG B 2 90  ? 29.828 -19.115 40.403 1.00 56.51  ?  108 ARG B CA    1 
ATOM   3561 C C     . ARG B 2 90  ? 29.772 -17.654 40.844 1.00 56.18  ?  108 ARG B C     1 
ATOM   3562 O O     . ARG B 2 90  ? 30.621 -16.863 40.416 1.00 50.91  ?  108 ARG B O     1 
ATOM   3563 C CB    . ARG B 2 90  ? 30.121 -19.155 38.901 1.00 61.47  ?  108 ARG B CB    1 
ATOM   3564 C CG    . ARG B 2 90  ? 30.415 -20.511 38.296 1.00 64.52  ?  108 ARG B CG    1 
ATOM   3565 C CD    . ARG B 2 90  ? 30.386 -20.363 36.790 1.00 73.67  ?  108 ARG B CD    1 
ATOM   3566 N NE    . ARG B 2 90  ? 29.521 -19.242 36.420 1.00 77.74  ?  108 ARG B NE    1 
ATOM   3567 C CZ    . ARG B 2 90  ? 29.756 -18.393 35.420 1.00 84.99  ?  108 ARG B CZ    1 
ATOM   3568 N NH1   . ARG B 2 90  ? 30.848 -18.528 34.665 1.00 85.82  ?  108 ARG B NH1   1 
ATOM   3569 N NH2   . ARG B 2 90  ? 28.891 -17.408 35.177 1.00 74.50  ?  108 ARG B NH2   1 
ATOM   3570 N N     . LEU B 2 91  ? 28.796 -17.277 41.679 1.00 54.88  ?  109 LEU B N     1 
ATOM   3571 C CA    . LEU B 2 91  ? 28.582 -15.884 42.066 1.00 52.06  ?  109 LEU B CA    1 
ATOM   3572 C C     . LEU B 2 91  ? 29.453 -15.493 43.261 1.00 51.70  ?  109 LEU B C     1 
ATOM   3573 O O     . LEU B 2 91  ? 29.438 -16.170 44.295 1.00 49.96  ?  109 LEU B O     1 
ATOM   3574 C CB    . LEU B 2 91  ? 27.107 -15.661 42.396 1.00 49.04  ?  109 LEU B CB    1 
ATOM   3575 C CG    . LEU B 2 91  ? 26.152 -15.413 41.228 1.00 47.65  ?  109 LEU B CG    1 
ATOM   3576 C CD1   . LEU B 2 91  ? 24.720 -15.490 41.706 1.00 47.90  ?  109 LEU B CD1   1 
ATOM   3577 C CD2   . LEU B 2 91  ? 26.410 -14.075 40.552 1.00 44.78  ?  109 LEU B CD2   1 
ATOM   3578 N N     . LYS B 2 92  ? 30.197 -14.395 43.125 1.00 50.05  ?  110 LYS B N     1 
ATOM   3579 C CA    . LYS B 2 92  ? 31.005 -13.878 44.227 1.00 52.57  ?  110 LYS B CA    1 
ATOM   3580 C C     . LYS B 2 92  ? 30.576 -12.453 44.587 1.00 48.80  ?  110 LYS B C     1 
ATOM   3581 O O     . LYS B 2 92  ? 29.715 -11.854 43.939 1.00 50.55  ?  110 LYS B O     1 
ATOM   3582 C CB    . LYS B 2 92  ? 32.500 -13.931 43.876 1.00 53.33  ?  110 LYS B CB    1 
ATOM   3583 C CG    . LYS B 2 92  ? 33.236 -15.210 44.319 1.00 61.36  ?  110 LYS B CG    1 
ATOM   3584 C CD    . LYS B 2 92  ? 33.002 -15.569 45.813 1.00 65.89  ?  110 LYS B CD    1 
ATOM   3585 C CE    . LYS B 2 92  ? 32.883 -14.331 46.732 1.00 72.17  ?  110 LYS B CE    1 
ATOM   3586 N NZ    . LYS B 2 92  ? 32.240 -14.637 48.053 1.00 67.56  ?  110 LYS B NZ    1 
ATOM   3587 N N     . SER B 2 93  ? 31.165 -11.917 45.654 1.00 47.57  ?  111 SER B N     1 
ATOM   3588 C CA    . SER B 2 93  ? 31.027 -10.513 46.031 1.00 45.44  ?  111 SER B CA    1 
ATOM   3589 C C     . SER B 2 93  ? 32.396 -9.845  46.075 1.00 46.64  ?  111 SER B C     1 
ATOM   3590 O O     . SER B 2 93  ? 33.388 -10.463 46.468 1.00 53.60  ?  111 SER B O     1 
ATOM   3591 C CB    . SER B 2 93  ? 30.354 -10.356 47.401 1.00 49.13  ?  111 SER B CB    1 
ATOM   3592 O OG    . SER B 2 93  ? 28.952 -10.135 47.295 1.00 52.99  ?  111 SER B OG    1 
ATOM   3593 N N     . ASN B 2 94  ? 32.455 -8.571  45.694 1.00 48.84  ?  112 ASN B N     1 
ATOM   3594 C CA    . ASN B 2 94  ? 33.724 -7.843  45.611 1.00 45.88  ?  112 ASN B CA    1 
ATOM   3595 C C     . ASN B 2 94  ? 33.637 -6.529  46.385 1.00 42.37  ?  112 ASN B C     1 
ATOM   3596 O O     . ASN B 2 94  ? 33.058 -5.550  45.884 1.00 40.48  ?  112 ASN B O     1 
ATOM   3597 C CB    . ASN B 2 94  ? 34.088 -7.616  44.144 1.00 49.25  ?  112 ASN B CB    1 
ATOM   3598 C CG    . ASN B 2 94  ? 35.446 -6.951  43.956 1.00 55.71  ?  112 ASN B CG    1 
ATOM   3599 O OD1   . ASN B 2 94  ? 36.202 -6.756  44.921 1.00 56.84  ?  112 ASN B OD1   1 
ATOM   3600 N ND2   . ASN B 2 94  ? 35.758 -6.580  42.702 1.00 58.19  ?  112 ASN B ND2   1 
ATOM   3601 N N     . PRO B 2 95  ? 34.215 -6.457  47.623 1.00 46.27  ?  113 PRO B N     1 
ATOM   3602 C CA    . PRO B 2 95  ? 34.065 -5.241  48.456 1.00 44.50  ?  113 PRO B CA    1 
ATOM   3603 C C     . PRO B 2 95  ? 34.480 -3.929  47.794 1.00 42.62  ?  113 PRO B C     1 
ATOM   3604 O O     . PRO B 2 95  ? 34.058 -2.859  48.243 1.00 40.87  ?  113 PRO B O     1 
ATOM   3605 C CB    . PRO B 2 95  ? 34.952 -5.516  49.685 1.00 37.82  ?  113 PRO B CB    1 
ATOM   3606 C CG    . PRO B 2 95  ? 35.377 -6.926  49.605 1.00 41.68  ?  113 PRO B CG    1 
ATOM   3607 C CD    . PRO B 2 95  ? 34.827 -7.571  48.359 1.00 44.28  ?  113 PRO B CD    1 
ATOM   3608 N N     . LYS B 2 96  ? 35.329 -3.979  46.769 1.00 43.94  ?  114 LYS B N     1 
ATOM   3609 C CA    . LYS B 2 96  ? 35.707 -2.775  46.046 1.00 40.60  ?  114 LYS B CA    1 
ATOM   3610 C C     . LYS B 2 96  ? 34.619 -2.320  45.089 1.00 41.59  ?  114 LYS B C     1 
ATOM   3611 O O     . LYS B 2 96  ? 34.635 -1.169  44.640 1.00 40.06  ?  114 LYS B O     1 
ATOM   3612 C CB    . LYS B 2 96  ? 37.005 -3.017  45.259 1.00 45.53  ?  114 LYS B CB    1 
ATOM   3613 C CG    . LYS B 2 96  ? 38.308 -2.983  46.066 1.00 42.55  ?  114 LYS B CG    1 
ATOM   3614 C CD    . LYS B 2 96  ? 39.500 -3.434  45.200 1.00 43.93  ?  114 LYS B CD    1 
ATOM   3615 C CE    . LYS B 2 96  ? 40.741 -3.799  46.039 1.00 55.68  ?  114 LYS B CE    1 
ATOM   3616 N NZ    . LYS B 2 96  ? 42.061 -3.206  45.603 1.00 54.13  ?  114 LYS B NZ    1 
ATOM   3617 N N     . ASP B 2 97  ? 33.659 -3.185  44.805 1.00 43.11  ?  115 ASP B N     1 
ATOM   3618 C CA    . ASP B 2 97  ? 32.866 -3.093  43.590 1.00 46.53  ?  115 ASP B CA    1 
ATOM   3619 C C     . ASP B 2 97  ? 31.444 -3.556  43.900 1.00 46.62  ?  115 ASP B C     1 
ATOM   3620 O O     . ASP B 2 97  ? 30.875 -4.400  43.205 1.00 57.05  ?  115 ASP B O     1 
ATOM   3621 C CB    . ASP B 2 97  ? 33.479 -3.970  42.488 1.00 49.95  ?  115 ASP B CB    1 
ATOM   3622 C CG    . ASP B 2 97  ? 34.282 -3.183  41.427 1.00 59.38  ?  115 ASP B CG    1 
ATOM   3623 O OD1   . ASP B 2 97  ? 34.773 -2.052  41.705 1.00 55.86  ?  115 ASP B OD1   1 
ATOM   3624 O OD2   . ASP B 2 97  ? 34.458 -3.731  40.302 1.00 62.67  -1 115 ASP B OD2   1 
ATOM   3625 N N     . ASN B 2 98  ? 30.839 -3.062  44.965 1.00 33.97  ?  116 ASN B N     1 
ATOM   3626 C CA    . ASN B 2 98  ? 29.535 -3.662  45.260 1.00 34.59  ?  116 ASN B CA    1 
ATOM   3627 C C     . ASN B 2 98  ? 28.424 -2.654  44.971 1.00 36.86  ?  116 ASN B C     1 
ATOM   3628 O O     . ASN B 2 98  ? 27.676 -2.243  45.869 1.00 36.43  ?  116 ASN B O     1 
ATOM   3629 C CB    . ASN B 2 98  ? 29.478 -4.180  46.706 1.00 36.10  ?  116 ASN B CB    1 
ATOM   3630 C CG    . ASN B 2 98  ? 29.905 -5.663  46.838 1.00 35.99  ?  116 ASN B CG    1 
ATOM   3631 O OD1   . ASN B 2 98  ? 29.664 -6.507  45.959 1.00 36.77  ?  116 ASN B OD1   1 
ATOM   3632 N ND2   . ASN B 2 98  ? 30.522 -5.974  47.957 1.00 35.62  ?  116 ASN B ND2   1 
ATOM   3633 N N     . GLU B 2 99  ? 28.293 -2.276  43.701 1.00 35.49  ?  117 GLU B N     1 
ATOM   3634 C CA    . GLU B 2 99  ? 27.616 -1.030  43.384 1.00 32.33  ?  117 GLU B CA    1 
ATOM   3635 C C     . GLU B 2 99  ? 26.120 -1.097  43.647 1.00 33.04  ?  117 GLU B C     1 
ATOM   3636 O O     . GLU B 2 99  ? 25.508 -0.090  44.008 1.00 33.95  ?  117 GLU B O     1 
ATOM   3637 C CB    . GLU B 2 99  ? 27.865 -0.657  41.936 1.00 35.96  ?  117 GLU B CB    1 
ATOM   3638 C CG    . GLU B 2 99  ? 29.162 0.029   41.730 1.00 40.94  ?  117 GLU B CG    1 
ATOM   3639 C CD    . GLU B 2 99  ? 29.855 -0.508  40.530 1.00 50.65  ?  117 GLU B CD    1 
ATOM   3640 O OE1   . GLU B 2 99  ? 30.184 0.288   39.617 1.00 54.13  ?  117 GLU B OE1   1 
ATOM   3641 O OE2   . GLU B 2 99  ? 30.047 -1.743  40.498 1.00 60.52  -1 117 GLU B OE2   1 
ATOM   3642 N N     . SER B 2 100 ? 25.487 -2.236  43.406 1.00 34.15  ?  118 SER B N     1 
ATOM   3643 C CA    . SER B 2 100 ? 24.063 -2.295  43.680 1.00 29.24  ?  118 SER B CA    1 
ATOM   3644 C C     . SER B 2 100 ? 23.814 -2.136  45.175 1.00 30.37  ?  118 SER B C     1 
ATOM   3645 O O     . SER B 2 100 ? 22.851 -1.480  45.593 1.00 27.11  ?  118 SER B O     1 
ATOM   3646 C CB    . SER B 2 100 ? 23.490 -3.605  43.148 1.00 32.02  ?  118 SER B CB    1 
ATOM   3647 O OG    . SER B 2 100 ? 24.265 -4.697  43.606 1.00 35.01  ?  118 SER B OG    1 
ATOM   3648 N N     . ARG B 2 101 ? 24.700 -2.694  45.999 1.00 28.60  ?  119 ARG B N     1 
ATOM   3649 C CA    . ARG B 2 101 ? 24.487 -2.631  47.434 1.00 26.04  ?  119 ARG B CA    1 
ATOM   3650 C C     . ARG B 2 101 ? 24.797 -1.232  47.966 1.00 29.07  ?  119 ARG B C     1 
ATOM   3651 O O     . ARG B 2 101 ? 24.101 -0.744  48.866 1.00 29.09  ?  119 ARG B O     1 
ATOM   3652 C CB    . ARG B 2 101 ? 25.317 -3.718  48.121 1.00 28.29  ?  119 ARG B CB    1 
ATOM   3653 C CG    . ARG B 2 101 ? 25.293 -3.709  49.663 1.00 29.68  ?  119 ARG B CG    1 
ATOM   3654 C CD    . ARG B 2 101 ? 24.002 -4.243  50.228 1.00 28.17  ?  119 ARG B CD    1 
ATOM   3655 N NE    . ARG B 2 101 ? 24.026 -4.245  51.685 1.00 33.08  ?  119 ARG B NE    1 
ATOM   3656 C CZ    . ARG B 2 101 ? 23.030 -4.698  52.446 1.00 36.28  ?  119 ARG B CZ    1 
ATOM   3657 N NH1   . ARG B 2 101 ? 21.939 -5.187  51.877 1.00 32.57  ?  119 ARG B NH1   1 
ATOM   3658 N NH2   . ARG B 2 101 ? 23.121 -4.671  53.771 1.00 33.17  ?  119 ARG B NH2   1 
ATOM   3659 N N     . ARG B 2 102 ? 25.805 -0.554  47.402 1.00 25.45  ?  120 ARG B N     1 
ATOM   3660 C CA    . ARG B 2 102 ? 26.083 0.817   47.808 1.00 23.74  ?  120 ARG B CA    1 
ATOM   3661 C C     . ARG B 2 102 ? 24.856 1.690   47.606 1.00 25.01  ?  120 ARG B C     1 
ATOM   3662 O O     . ARG B 2 102 ? 24.472 2.461   48.488 1.00 24.43  ?  120 ARG B O     1 
ATOM   3663 C CB    . ARG B 2 102 ? 27.281 1.379   47.037 1.00 27.34  ?  120 ARG B CB    1 
ATOM   3664 C CG    . ARG B 2 102 ? 28.599 0.747   47.400 1.00 25.17  ?  120 ARG B CG    1 
ATOM   3665 C CD    . ARG B 2 102 ? 29.719 1.015   46.394 1.00 29.25  ?  120 ARG B CD    1 
ATOM   3666 N NE    . ARG B 2 102 ? 30.947 0.282   46.748 1.00 34.02  ?  120 ARG B NE    1 
ATOM   3667 C CZ    . ARG B 2 102 ? 31.855 0.702   47.643 1.00 32.09  ?  120 ARG B CZ    1 
ATOM   3668 N NH1   . ARG B 2 102 ? 31.693 1.862   48.273 1.00 29.74  ?  120 ARG B NH1   1 
ATOM   3669 N NH2   . ARG B 2 102 ? 32.928 -0.036  47.923 1.00 29.02  ?  120 ARG B NH2   1 
ATOM   3670 N N     . LEU B 2 103 ? 24.210 1.575   46.451 1.00 26.85  ?  121 LEU B N     1 
ATOM   3671 C CA    . LEU B 2 103 ? 23.063 2.435   46.208 1.00 26.76  ?  121 LEU B CA    1 
ATOM   3672 C C     . LEU B 2 103 ? 21.915 2.071   47.140 1.00 29.55  ?  121 LEU B C     1 
ATOM   3673 O O     . LEU B 2 103 ? 21.273 2.957   47.719 1.00 31.34  ?  121 LEU B O     1 
ATOM   3674 C CB    . LEU B 2 103 ? 22.633 2.373   44.745 1.00 27.04  ?  121 LEU B CB    1 
ATOM   3675 C CG    . LEU B 2 103 ? 21.280 3.063   44.495 1.00 29.66  ?  121 LEU B CG    1 
ATOM   3676 C CD1   . LEU B 2 103 ? 21.383 4.337   43.682 1.00 24.50  ?  121 LEU B CD1   1 
ATOM   3677 C CD2   . LEU B 2 103 ? 20.280 2.102   43.852 1.00 31.02  ?  121 LEU B CD2   1 
ATOM   3678 N N     . TYR B 2 104 ? 21.663 0.775   47.333 1.00 28.21  ?  122 TYR B N     1 
ATOM   3679 C CA    . TYR B 2 104 ? 20.641 0.355   48.286 1.00 28.24  ?  122 TYR B CA    1 
ATOM   3680 C C     . TYR B 2 104 ? 20.894 0.963   49.664 1.00 29.90  ?  122 TYR B C     1 
ATOM   3681 O O     . TYR B 2 104 ? 20.042 1.674   50.209 1.00 25.80  ?  122 TYR B O     1 
ATOM   3682 C CB    . TYR B 2 104 ? 20.618 -1.165  48.344 1.00 29.29  ?  122 TYR B CB    1 
ATOM   3683 C CG    . TYR B 2 104 ? 19.711 -1.818  49.363 1.00 32.92  ?  122 TYR B CG    1 
ATOM   3684 C CD1   . TYR B 2 104 ? 20.231 -2.381  50.534 1.00 33.53  ?  122 TYR B CD1   1 
ATOM   3685 C CD2   . TYR B 2 104 ? 18.352 -1.942  49.130 1.00 33.91  ?  122 TYR B CD2   1 
ATOM   3686 C CE1   . TYR B 2 104 ? 19.406 -3.017  51.456 1.00 33.80  ?  122 TYR B CE1   1 
ATOM   3687 C CE2   . TYR B 2 104 ? 17.528 -2.583  50.035 1.00 36.86  ?  122 TYR B CE2   1 
ATOM   3688 C CZ    . TYR B 2 104 ? 18.056 -3.121  51.191 1.00 35.90  ?  122 TYR B CZ    1 
ATOM   3689 O OH    . TYR B 2 104 ? 17.216 -3.747  52.075 1.00 35.56  ?  122 TYR B OH    1 
ATOM   3690 N N     . GLU B 2 105 ? 22.082 0.712   50.234 1.00 27.64  ?  123 GLU B N     1 
ATOM   3691 C CA    . GLU B 2 105 ? 22.336 1.149   51.602 1.00 25.85  ?  123 GLU B CA    1 
ATOM   3692 C C     . GLU B 2 105 ? 22.186 2.651   51.739 1.00 28.17  ?  123 GLU B C     1 
ATOM   3693 O O     . GLU B 2 105 ? 21.750 3.132   52.795 1.00 27.06  ?  123 GLU B O     1 
ATOM   3694 C CB    . GLU B 2 105 ? 23.722 0.713   52.068 1.00 23.39  ?  123 GLU B CB    1 
ATOM   3695 C CG    . GLU B 2 105 ? 23.913 -0.784  52.074 1.00 29.60  ?  123 GLU B CG    1 
ATOM   3696 C CD    . GLU B 2 105 ? 24.964 -1.254  53.073 1.00 34.42  ?  123 GLU B CD    1 
ATOM   3697 O OE1   . GLU B 2 105 ? 25.174 -2.489  53.228 1.00 35.58  ?  123 GLU B OE1   1 
ATOM   3698 O OE2   . GLU B 2 105 ? 25.581 -0.383  53.716 1.00 35.60  -1 123 GLU B OE2   1 
ATOM   3699 N N     . THR B 2 106 ? 22.519 3.402   50.678 1.00 25.23  ?  124 THR B N     1 
ATOM   3700 C CA    . THR B 2 106 ? 22.467 4.863   50.724 1.00 23.38  ?  124 THR B CA    1 
ATOM   3701 C C     . THR B 2 106 ? 21.025 5.366   50.722 1.00 28.71  ?  124 THR B C     1 
ATOM   3702 O O     . THR B 2 106 ? 20.685 6.291   51.471 1.00 28.71  ?  124 THR B O     1 
ATOM   3703 C CB    . THR B 2 106 ? 23.262 5.446   49.538 1.00 27.19  ?  124 THR B CB    1 
ATOM   3704 O OG1   . THR B 2 106 ? 24.652 5.094   49.646 1.00 27.73  ?  124 THR B OG1   1 
ATOM   3705 C CG2   . THR B 2 106 ? 23.135 6.965   49.469 1.00 22.84  ?  124 THR B CG2   1 
ATOM   3706 N N     . LEU B 2 107 ? 20.165 4.781   49.869 1.00 28.76  ?  125 LEU B N     1 
ATOM   3707 C CA    . LEU B 2 107 ? 18.730 5.053   49.938 1.00 28.11  ?  125 LEU B CA    1 
ATOM   3708 C C     . LEU B 2 107 ? 18.147 4.620   51.278 1.00 32.81  ?  125 LEU B C     1 
ATOM   3709 O O     . LEU B 2 107 ? 17.241 5.271   51.810 1.00 32.16  ?  125 LEU B O     1 
ATOM   3710 C CB    . LEU B 2 107 ? 18.003 4.325   48.820 1.00 26.24  ?  125 LEU B CB    1 
ATOM   3711 C CG    . LEU B 2 107 ? 18.472 4.603   47.409 1.00 28.45  ?  125 LEU B CG    1 
ATOM   3712 C CD1   . LEU B 2 107 ? 17.718 3.687   46.442 1.00 28.10  ?  125 LEU B CD1   1 
ATOM   3713 C CD2   . LEU B 2 107 ? 18.286 6.066   47.067 1.00 24.79  ?  125 LEU B CD2   1 
ATOM   3714 N N     . TYR B 2 108 ? 18.638 3.495   51.818 1.00 32.70  ?  126 TYR B N     1 
ATOM   3715 C CA    . TYR B 2 108 ? 18.164 3.010   53.106 1.00 32.70  ?  126 TYR B CA    1 
ATOM   3716 C C     . TYR B 2 108 ? 18.509 3.989   54.226 1.00 33.67  ?  126 TYR B C     1 
ATOM   3717 O O     . TYR B 2 108 ? 17.683 4.234   55.113 1.00 34.04  ?  126 TYR B O     1 
ATOM   3718 C CB    . TYR B 2 108 ? 18.739 1.611   53.371 1.00 32.05  ?  126 TYR B CB    1 
ATOM   3719 C CG    . TYR B 2 108 ? 18.840 1.240   54.830 1.00 31.61  ?  126 TYR B CG    1 
ATOM   3720 C CD1   . TYR B 2 108 ? 17.708 0.859   55.558 1.00 34.19  ?  126 TYR B CD1   1 
ATOM   3721 C CD2   . TYR B 2 108 ? 20.074 1.261   55.481 1.00 29.19  ?  126 TYR B CD2   1 
ATOM   3722 C CE1   . TYR B 2 108 ? 17.805 0.515   56.904 1.00 33.98  ?  126 TYR B CE1   1 
ATOM   3723 C CE2   . TYR B 2 108 ? 20.189 0.935   56.819 1.00 32.69  ?  126 TYR B CE2   1 
ATOM   3724 C CZ    . TYR B 2 108 ? 19.051 0.558   57.532 1.00 35.27  ?  126 TYR B CZ    1 
ATOM   3725 O OH    . TYR B 2 108 ? 19.174 0.250   58.866 1.00 30.72  ?  126 TYR B OH    1 
ATOM   3726 N N     . ALA B 2 109 ? 19.708 4.584   54.184 1.00 28.84  ?  127 ALA B N     1 
ATOM   3727 C CA    . ALA B 2 109 ? 20.085 5.570   55.186 1.00 29.51  ?  127 ALA B CA    1 
ATOM   3728 C C     . ALA B 2 109 ? 19.090 6.722   55.256 1.00 34.86  ?  127 ALA B C     1 
ATOM   3729 O O     . ALA B 2 109 ? 18.917 7.328   56.320 1.00 35.91  ?  127 ALA B O     1 
ATOM   3730 C CB    . ALA B 2 109 ? 21.482 6.109   54.898 1.00 29.50  ?  127 ALA B CB    1 
ATOM   3731 N N     . ASP B 2 110 ? 18.433 7.047   54.141 1.00 37.47  ?  128 ASP B N     1 
ATOM   3732 C CA    . ASP B 2 110 ? 17.447 8.130   54.132 1.00 36.88  ?  128 ASP B CA    1 
ATOM   3733 C C     . ASP B 2 110 ? 16.126 7.668   54.704 1.00 35.49  ?  128 ASP B C     1 
ATOM   3734 O O     . ASP B 2 110 ? 15.474 8.399   55.453 1.00 36.11  ?  128 ASP B O     1 
ATOM   3735 C CB    . ASP B 2 110 ? 17.218 8.638   52.712 1.00 37.49  ?  128 ASP B CB    1 
ATOM   3736 C CG    . ASP B 2 110 ? 18.399 9.424   52.172 1.00 45.94  ?  128 ASP B CG    1 
ATOM   3737 O OD1   . ASP B 2 110 ? 19.006 10.205  52.943 1.00 45.23  ?  128 ASP B OD1   1 
ATOM   3738 O OD2   . ASP B 2 110 ? 18.734 9.234   50.971 1.00 54.80  -1 128 ASP B OD2   1 
ATOM   3739 N N     . HIS B 2 111 ? 15.709 6.466   54.327 1.00 34.72  ?  129 HIS B N     1 
ATOM   3740 C CA    . HIS B 2 111 ? 14.499 5.902   54.888 1.00 36.45  ?  129 HIS B CA    1 
ATOM   3741 C C     . HIS B 2 111 ? 14.623 5.797   56.403 1.00 38.88  ?  129 HIS B C     1 
ATOM   3742 O O     . HIS B 2 111 ? 13.737 6.236   57.137 1.00 40.50  ?  129 HIS B O     1 
ATOM   3743 C CB    . HIS B 2 111 ? 14.231 4.549   54.229 1.00 38.55  ?  129 HIS B CB    1 
ATOM   3744 C CG    . HIS B 2 111 ? 12.947 3.917   54.650 1.00 39.07  ?  129 HIS B CG    1 
ATOM   3745 N ND1   . HIS B 2 111 ? 12.728 2.561   54.574 1.00 41.03  ?  129 HIS B ND1   1 
ATOM   3746 C CD2   . HIS B 2 111 ? 11.825 4.451   55.182 1.00 41.54  ?  129 HIS B CD2   1 
ATOM   3747 C CE1   . HIS B 2 111 ? 11.520 2.283   55.024 1.00 41.77  ?  129 HIS B CE1   1 
ATOM   3748 N NE2   . HIS B 2 111 ? 10.951 3.413   55.400 1.00 50.45  ?  129 HIS B NE2   1 
ATOM   3749 N N     . LEU B 2 112 ? 15.745 5.253   56.885 1.00 37.18  ?  130 LEU B N     1 
ATOM   3750 C CA    . LEU B 2 112 ? 16.002 5.170   58.318 1.00 34.58  ?  130 LEU B CA    1 
ATOM   3751 C C     . LEU B 2 112 ? 15.956 6.548   58.966 1.00 38.41  ?  130 LEU B C     1 
ATOM   3752 O O     . LEU B 2 112 ? 15.299 6.745   59.997 1.00 40.96  ?  130 LEU B O     1 
ATOM   3753 C CB    . LEU B 2 112 ? 17.358 4.501   58.560 1.00 32.43  ?  130 LEU B CB    1 
ATOM   3754 C CG    . LEU B 2 112 ? 17.856 4.172   59.967 1.00 29.30  ?  130 LEU B CG    1 
ATOM   3755 C CD1   . LEU B 2 112 ? 16.768 3.526   60.779 1.00 30.42  ?  130 LEU B CD1   1 
ATOM   3756 C CD2   . LEU B 2 112 ? 19.054 3.257   59.897 1.00 28.41  ?  130 LEU B CD2   1 
ATOM   3757 N N     . GLU B 2 113 ? 16.648 7.521   58.383 1.00 34.65  ?  131 GLU B N     1 
ATOM   3758 C CA    . GLU B 2 113 ? 16.670 8.826   59.019 1.00 37.35  ?  131 GLU B CA    1 
ATOM   3759 C C     . GLU B 2 113 ? 15.278 9.429   59.105 1.00 42.05  ?  131 GLU B C     1 
ATOM   3760 O O     . GLU B 2 113 ? 14.976 10.163  60.050 1.00 45.63  ?  131 GLU B O     1 
ATOM   3761 C CB    . GLU B 2 113 ? 17.597 9.778   58.279 1.00 40.46  ?  131 GLU B CB    1 
ATOM   3762 C CG    . GLU B 2 113 ? 17.660 11.164  58.900 1.00 44.38  ?  131 GLU B CG    1 
ATOM   3763 C CD    . GLU B 2 113 ? 18.447 12.151  58.041 1.00 57.47  ?  131 GLU B CD    1 
ATOM   3764 O OE1   . GLU B 2 113 ? 19.263 12.927  58.614 1.00 56.98  ?  131 GLU B OE1   1 
ATOM   3765 O OE2   . GLU B 2 113 ? 18.256 12.139  56.792 1.00 57.86  -1 131 GLU B OE2   1 
ATOM   3766 N N     . SER B 2 114 ? 14.423 9.159   58.132 1.00 42.48  ?  132 SER B N     1 
ATOM   3767 C CA    . SER B 2 114 ? 13.122 9.804   58.154 1.00 42.91  ?  132 SER B CA    1 
ATOM   3768 C C     . SER B 2 114 ? 12.181 9.101   59.118 1.00 43.51  ?  132 SER B C     1 
ATOM   3769 O O     . SER B 2 114 ? 11.277 9.743   59.681 1.00 42.20  ?  132 SER B O     1 
ATOM   3770 C CB    . SER B 2 114 ? 12.538 9.846   56.748 1.00 41.20  ?  132 SER B CB    1 
ATOM   3771 O OG    . SER B 2 114 ? 11.437 8.969   56.656 1.00 48.54  ?  132 SER B OG    1 
ATOM   3772 N N     . VAL B 2 115 ? 12.403 7.797   59.333 1.00 40.84  ?  133 VAL B N     1 
ATOM   3773 C CA    . VAL B 2 115 ? 11.656 7.055   60.343 1.00 39.34  ?  133 VAL B CA    1 
ATOM   3774 C C     . VAL B 2 115 ? 11.979 7.595   61.732 1.00 45.84  ?  133 VAL B C     1 
ATOM   3775 O O     . VAL B 2 115 ? 11.093 7.738   62.586 1.00 45.25  ?  133 VAL B O     1 
ATOM   3776 C CB    . VAL B 2 115 ? 11.971 5.555   60.231 1.00 35.59  ?  133 VAL B CB    1 
ATOM   3777 C CG1   . VAL B 2 115 ? 11.323 4.784   61.383 1.00 37.01  ?  133 VAL B CG1   1 
ATOM   3778 C CG2   . VAL B 2 115 ? 11.544 5.020   58.868 1.00 35.64  ?  133 VAL B CG2   1 
ATOM   3779 N N     . ILE B 2 116 ? 13.256 7.918   61.974 1.00 43.42  ?  134 ILE B N     1 
ATOM   3780 C CA    . ILE B 2 116 ? 13.647 8.499   63.244 1.00 39.01  ?  134 ILE B CA    1 
ATOM   3781 C C     . ILE B 2 116 ? 13.066 9.894   63.381 1.00 42.18  ?  134 ILE B C     1 
ATOM   3782 O O     . ILE B 2 116 ? 12.651 10.289  64.475 1.00 46.21  ?  134 ILE B O     1 
ATOM   3783 C CB    . ILE B 2 116 ? 15.182 8.483   63.378 1.00 38.27  ?  134 ILE B CB    1 
ATOM   3784 C CG1   . ILE B 2 116 ? 15.704 7.082   63.083 1.00 38.57  ?  134 ILE B CG1   1 
ATOM   3785 C CG2   . ILE B 2 116 ? 15.608 8.767   64.801 1.00 34.86  ?  134 ILE B CG2   1 
ATOM   3786 C CD1   . ILE B 2 116 ? 17.182 6.936   63.260 1.00 32.61  ?  134 ILE B CD1   1 
ATOM   3787 N N     . LYS B 2 117 ? 12.969 10.645  62.281 1.00 43.61  ?  135 LYS B N     1 
ATOM   3788 C CA    . LYS B 2 117 ? 12.498 12.027  62.371 1.00 47.84  ?  135 LYS B CA    1 
ATOM   3789 C C     . LYS B 2 117 ? 11.065 12.122  62.885 1.00 50.84  ?  135 LYS B C     1 
ATOM   3790 O O     . LYS B 2 117 ? 10.733 13.097  63.568 1.00 61.57  ?  135 LYS B O     1 
ATOM   3791 C CB    . LYS B 2 117 ? 12.601 12.758  61.020 1.00 51.19  ?  135 LYS B CB    1 
ATOM   3792 C CG    . LYS B 2 117 ? 12.739 14.316  61.127 1.00 47.33  ?  135 LYS B CG    1 
ATOM   3793 C CD    . LYS B 2 117 ? 12.546 15.070  59.782 1.00 47.97  ?  135 LYS B CD    1 
ATOM   3794 C CE    . LYS B 2 117 ? 12.897 14.214  58.526 1.00 67.41  ?  135 LYS B CE    1 
ATOM   3795 N NZ    . LYS B 2 117 ? 14.381 14.104  58.159 1.00 66.71  ?  135 LYS B NZ    1 
ATOM   3796 N N     . GLN B 2 118 ? 10.187 11.166  62.561 1.00 47.81  ?  136 GLN B N     1 
ATOM   3797 C CA    . GLN B 2 118 ? 8.845  11.251  63.133 1.00 50.32  ?  136 GLN B CA    1 
ATOM   3798 C C     . GLN B 2 118 ? 8.687  10.441  64.412 1.00 48.17  ?  136 GLN B C     1 
ATOM   3799 O O     . GLN B 2 118 ? 7.698  10.631  65.125 1.00 50.14  ?  136 GLN B O     1 
ATOM   3800 C CB    . GLN B 2 118 ? 7.770  10.835  62.121 1.00 53.00  ?  136 GLN B CB    1 
ATOM   3801 C CG    . GLN B 2 118 ? 7.945  9.472   61.504 1.00 56.51  ?  136 GLN B CG    1 
ATOM   3802 C CD    . GLN B 2 118 ? 7.206  9.340   60.169 1.00 69.95  ?  136 GLN B CD    1 
ATOM   3803 O OE1   . GLN B 2 118 ? 7.746  8.779   59.195 1.00 59.81  ?  136 GLN B OE1   1 
ATOM   3804 N NE2   . GLN B 2 118 ? 5.960  9.856   60.117 1.00 72.45  ?  136 GLN B NE2   1 
ATOM   3805 N N     . GLU B 2 119 ? 9.646  9.573   64.730 1.00 50.57  ?  137 GLU B N     1 
ATOM   3806 C CA    . GLU B 2 119 ? 9.625  8.795   65.967 1.00 51.07  ?  137 GLU B CA    1 
ATOM   3807 C C     . GLU B 2 119 ? 10.117 9.635   67.153 1.00 51.88  ?  137 GLU B C     1 
ATOM   3808 O O     . GLU B 2 119 ? 9.395  9.825   68.139 1.00 47.91  ?  137 GLU B O     1 
ATOM   3809 C CB    . GLU B 2 119 ? 10.473 7.526   65.774 1.00 49.01  ?  137 GLU B CB    1 
ATOM   3810 C CG    . GLU B 2 119 ? 10.145 6.312   66.648 1.00 56.04  ?  137 GLU B CG    1 
ATOM   3811 C CD    . GLU B 2 119 ? 11.400 5.439   66.984 1.00 69.21  ?  137 GLU B CD    1 
ATOM   3812 O OE1   . GLU B 2 119 ? 12.144 5.029   66.036 1.00 67.70  ?  137 GLU B OE1   1 
ATOM   3813 O OE2   . GLU B 2 119 ? 11.641 5.182   68.208 1.00 62.31  -1 137 GLU B OE2   1 
ATOM   3814 N N     . SER B 2 120 ? 11.324 10.192  67.051 1.00 50.70  ?  138 SER B N     1 
ATOM   3815 C CA    . SER B 2 120 ? 11.989 10.778  68.209 1.00 50.05  ?  138 SER B CA    1 
ATOM   3816 C C     . SER B 2 120 ? 11.496 12.182  68.523 1.00 51.15  ?  138 SER B C     1 
ATOM   3817 O O     . SER B 2 120 ? 11.341 13.012  67.621 1.00 52.36  ?  138 SER B O     1 
ATOM   3818 C CB    . SER B 2 120 ? 13.496 10.829  67.986 1.00 46.87  ?  138 SER B CB    1 
ATOM   3819 O OG    . SER B 2 120 ? 14.138 10.978  69.231 1.00 46.13  ?  138 SER B OG    1 
ATOM   3820 N N     . ASP B 2 121 ? 11.282 12.453  69.820 1.00 51.18  ?  139 ASP B N     1 
ATOM   3821 C CA    . ASP B 2 121 ? 11.020 13.801  70.332 1.00 53.87  ?  139 ASP B CA    1 
ATOM   3822 C C     . ASP B 2 121 ? 12.302 14.564  70.654 1.00 51.29  ?  139 ASP B C     1 
ATOM   3823 O O     . ASP B 2 121 ? 12.239 15.667  71.207 1.00 47.03  ?  139 ASP B O     1 
ATOM   3824 C CB    . ASP B 2 121 ? 10.114 13.760  71.577 1.00 55.24  ?  139 ASP B CB    1 
ATOM   3825 C CG    . ASP B 2 121 ? 10.627 12.817  72.681 1.00 61.83  ?  139 ASP B CG    1 
ATOM   3826 O OD1   . ASP B 2 121 ? 10.189 12.975  73.859 1.00 63.20  ?  139 ASP B OD1   1 
ATOM   3827 O OD2   . ASP B 2 121 ? 11.444 11.910  72.374 1.00 60.38  -1 139 ASP B OD2   1 
ATOM   3828 N N     . LEU B 2 122 ? 13.453 13.998  70.313 1.00 49.86  ?  140 LEU B N     1 
ATOM   3829 C CA    . LEU B 2 122 ? 14.757 14.613  70.491 1.00 46.30  ?  140 LEU B CA    1 
ATOM   3830 C C     . LEU B 2 122 ? 15.109 14.829  71.957 1.00 50.49  ?  140 LEU B C     1 
ATOM   3831 O O     . LEU B 2 122 ? 16.067 15.549  72.253 1.00 49.55  ?  140 LEU B O     1 
ATOM   3832 C CB    . LEU B 2 122 ? 14.853 15.930  69.716 1.00 44.85  ?  140 LEU B CB    1 
ATOM   3833 C CG    . LEU B 2 122 ? 15.074 15.818  68.203 1.00 43.56  ?  140 LEU B CG    1 
ATOM   3834 C CD1   . LEU B 2 122 ? 14.383 14.607  67.640 1.00 45.20  ?  140 LEU B CD1   1 
ATOM   3835 C CD2   . LEU B 2 122 ? 14.600 17.049  67.486 1.00 41.79  ?  140 LEU B CD2   1 
ATOM   3836 N N     . SER B 2 123 ? 14.380 14.214  72.899 1.00 51.25  ?  141 SER B N     1 
ATOM   3837 C CA    . SER B 2 123 ? 14.804 14.355  74.287 1.00 47.21  ?  141 SER B CA    1 
ATOM   3838 C C     . SER B 2 123 ? 16.047 13.531  74.558 1.00 47.86  ?  141 SER B C     1 
ATOM   3839 O O     . SER B 2 123 ? 16.853 13.911  75.414 1.00 50.24  ?  141 SER B O     1 
ATOM   3840 C CB    . SER B 2 123 ? 13.712 13.948  75.274 1.00 45.02  ?  141 SER B CB    1 
ATOM   3841 O OG    . SER B 2 123 ? 13.079 12.749  74.900 1.00 50.44  ?  141 SER B OG    1 
ATOM   3842 N N     . VAL B 2 124 ? 16.221 12.403  73.852 1.00 46.13  ?  142 VAL B N     1 
ATOM   3843 C CA    . VAL B 2 124 ? 17.352 11.523  74.153 1.00 46.16  ?  142 VAL B CA    1 
ATOM   3844 C C     . VAL B 2 124 ? 18.655 12.242  73.882 1.00 42.27  ?  142 VAL B C     1 
ATOM   3845 O O     . VAL B 2 124 ? 19.625 12.094  74.629 1.00 43.65  ?  142 VAL B O     1 
ATOM   3846 C CB    . VAL B 2 124 ? 17.279 10.197  73.367 1.00 42.33  ?  142 VAL B CB    1 
ATOM   3847 C CG1   . VAL B 2 124 ? 17.596 10.431  71.904 1.00 41.11  ?  142 VAL B CG1   1 
ATOM   3848 C CG2   . VAL B 2 124 ? 18.269 9.183   73.955 1.00 33.71  ?  142 VAL B CG2   1 
ATOM   3849 N N     . PHE B 2 125 ? 18.698 13.043  72.825 1.00 39.55  ?  143 PHE B N     1 
ATOM   3850 C CA    . PHE B 2 125 ? 19.944 13.716  72.503 1.00 40.10  ?  143 PHE B CA    1 
ATOM   3851 C C     . PHE B 2 125 ? 20.195 14.876  73.446 1.00 41.39  ?  143 PHE B C     1 
ATOM   3852 O O     . PHE B 2 125 ? 21.353 15.203  73.721 1.00 41.27  ?  143 PHE B O     1 
ATOM   3853 C CB    . PHE B 2 125 ? 19.937 14.150  71.036 1.00 36.06  ?  143 PHE B CB    1 
ATOM   3854 C CG    . PHE B 2 125 ? 19.680 13.007  70.092 1.00 39.05  ?  143 PHE B CG    1 
ATOM   3855 C CD1   . PHE B 2 125 ? 20.665 12.061  69.835 1.00 35.58  ?  143 PHE B CD1   1 
ATOM   3856 C CD2   . PHE B 2 125 ? 18.435 12.835  69.507 1.00 37.90  ?  143 PHE B CD2   1 
ATOM   3857 C CE1   . PHE B 2 125 ? 20.419 10.984  68.985 1.00 32.30  ?  143 PHE B CE1   1 
ATOM   3858 C CE2   . PHE B 2 125 ? 18.193 11.761  68.656 1.00 31.36  ?  143 PHE B CE2   1 
ATOM   3859 C CZ    . PHE B 2 125 ? 19.182 10.845  68.393 1.00 30.49  ?  143 PHE B CZ    1 
ATOM   3860 N N     . ASN B 2 126 ? 19.136 15.475  73.993 1.00 44.95  ?  144 ASN B N     1 
ATOM   3861 C CA    . ASN B 2 126 ? 19.331 16.529  74.979 1.00 43.95  ?  144 ASN B CA    1 
ATOM   3862 C C     . ASN B 2 126 ? 19.805 15.945  76.297 1.00 43.88  ?  144 ASN B C     1 
ATOM   3863 O O     . ASN B 2 126 ? 20.671 16.521  76.968 1.00 49.23  ?  144 ASN B O     1 
ATOM   3864 C CB    . ASN B 2 126 ? 18.049 17.326  75.135 1.00 40.73  ?  144 ASN B CB    1 
ATOM   3865 C CG    . ASN B 2 126 ? 17.953 18.416  74.110 1.00 45.88  ?  144 ASN B CG    1 
ATOM   3866 O OD1   . ASN B 2 126 ? 18.714 19.372  74.158 1.00 51.25  ?  144 ASN B OD1   1 
ATOM   3867 N ND2   . ASN B 2 126 ? 17.060 18.261  73.145 1.00 46.68  ?  144 ASN B ND2   1 
ATOM   3868 N N     . GLU B 2 127 ? 19.285 14.773  76.651 1.00 41.30  ?  145 GLU B N     1 
ATOM   3869 C CA    . GLU B 2 127 ? 19.796 14.048  77.799 1.00 42.85  ?  145 GLU B CA    1 
ATOM   3870 C C     . GLU B 2 127 ? 21.243 13.593  77.592 1.00 42.48  ?  145 GLU B C     1 
ATOM   3871 O O     . GLU B 2 127 ? 22.019 13.538  78.555 1.00 41.15  ?  145 GLU B O     1 
ATOM   3872 C CB    . GLU B 2 127 ? 18.877 12.864  78.079 1.00 43.39  ?  145 GLU B CB    1 
ATOM   3873 C CG    . GLU B 2 127 ? 17.433 13.254  78.315 1.00 46.00  ?  145 GLU B CG    1 
ATOM   3874 C CD    . GLU B 2 127 ? 16.583 12.059  78.744 1.00 50.38  ?  145 GLU B CD    1 
ATOM   3875 O OE1   . GLU B 2 127 ? 17.188 11.003  79.026 1.00 48.93  ?  145 GLU B OE1   1 
ATOM   3876 O OE2   . GLU B 2 127 ? 15.327 12.170  78.802 1.00 47.37  -1 145 GLU B OE2   1 
ATOM   3877 N N     . LEU B 2 128 ? 21.622 13.265  76.351 1.00 40.41  ?  146 LEU B N     1 
ATOM   3878 C CA    . LEU B 2 128 ? 22.934 12.705  76.052 1.00 37.10  ?  146 LEU B CA    1 
ATOM   3879 C C     . LEU B 2 128 ? 24.053 13.742  76.065 1.00 42.17  ?  146 LEU B C     1 
ATOM   3880 O O     . LEU B 2 128 ? 25.220 13.370  76.263 1.00 38.43  ?  146 LEU B O     1 
ATOM   3881 C CB    . LEU B 2 128 ? 22.904 12.019  74.694 1.00 37.85  ?  146 LEU B CB    1 
ATOM   3882 C CG    . LEU B 2 128 ? 24.041 11.061  74.370 1.00 33.54  ?  146 LEU B CG    1 
ATOM   3883 C CD1   . LEU B 2 128 ? 24.040 9.894   75.331 1.00 28.33  ?  146 LEU B CD1   1 
ATOM   3884 C CD2   . LEU B 2 128 ? 23.854 10.594  72.970 1.00 28.15  ?  146 LEU B CD2   1 
ATOM   3885 N N     . ARG B 2 129 ? 23.726 15.026  75.856 1.00 44.39  ?  147 ARG B N     1 
ATOM   3886 C CA    . ARG B 2 129 ? 24.671 16.128  76.021 1.00 39.59  ?  147 ARG B CA    1 
ATOM   3887 C C     . ARG B 2 129 ? 25.509 15.939  77.273 1.00 40.95  ?  147 ARG B C     1 
ATOM   3888 O O     . ARG B 2 129 ? 26.719 16.177  77.259 1.00 40.77  ?  147 ARG B O     1 
ATOM   3889 C CB    . ARG B 2 129 ? 23.939 17.467  76.104 1.00 44.05  ?  147 ARG B CB    1 
ATOM   3890 C CG    . ARG B 2 129 ? 23.636 18.124  74.784 1.00 46.39  ?  147 ARG B CG    1 
ATOM   3891 C CD    . ARG B 2 129 ? 22.602 19.227  74.967 1.00 51.31  ?  147 ARG B CD    1 
ATOM   3892 N NE    . ARG B 2 129 ? 22.905 20.098  76.102 1.00 56.94  ?  147 ARG B NE    1 
ATOM   3893 C CZ    . ARG B 2 129 ? 21.972 20.691  76.847 1.00 66.58  ?  147 ARG B CZ    1 
ATOM   3894 N NH1   . ARG B 2 129 ? 20.683 20.499  76.556 1.00 60.77  ?  147 ARG B NH1   1 
ATOM   3895 N NH2   . ARG B 2 129 ? 22.314 21.469  77.878 1.00 66.96  ?  147 ARG B NH2   1 
ATOM   3896 N N     . ASP B 2 130 ? 24.879 15.508  78.368 1.00 41.32  ?  148 ASP B N     1 
ATOM   3897 C CA    . ASP B 2 130 ? 25.603 15.451  79.631 1.00 40.54  ?  148 ASP B CA    1 
ATOM   3898 C C     . ASP B 2 130 ? 26.591 14.315  79.670 1.00 37.23  ?  148 ASP B C     1 
ATOM   3899 O O     . ASP B 2 130 ? 27.646 14.460  80.288 1.00 37.59  ?  148 ASP B O     1 
ATOM   3900 C CB    . ASP B 2 130 ? 24.648 15.336  80.800 1.00 44.35  ?  148 ASP B CB    1 
ATOM   3901 C CG    . ASP B 2 130 ? 24.214 16.680  81.287 1.00 66.59  ?  148 ASP B CG    1 
ATOM   3902 O OD1   . ASP B 2 130 ? 25.131 17.505  81.555 1.00 68.52  ?  148 ASP B OD1   1 
ATOM   3903 O OD2   . ASP B 2 130 ? 22.975 16.922  81.345 1.00 74.57  -1 148 ASP B OD2   1 
ATOM   3904 N N     . SER B 2 131 ? 26.271 13.179  79.045 1.00 35.37  ?  149 SER B N     1 
ATOM   3905 C CA    . SER B 2 131 ? 27.220 12.070  79.029 1.00 34.49  ?  149 SER B CA    1 
ATOM   3906 C C     . SER B 2 131 ? 28.458 12.399  78.204 1.00 36.52  ?  149 SER B C     1 
ATOM   3907 O O     . SER B 2 131 ? 29.548 11.883  78.482 1.00 30.43  ?  149 SER B O     1 
ATOM   3908 C CB    . SER B 2 131 ? 26.545 10.823  78.490 1.00 34.25  ?  149 SER B CB    1 
ATOM   3909 O OG    . SER B 2 131 ? 25.615 10.316  79.419 1.00 38.10  ?  149 SER B OG    1 
ATOM   3910 N N     . TYR B 2 132 ? 28.305 13.251  77.187 1.00 35.94  ?  150 TYR B N     1 
ATOM   3911 C CA    . TYR B 2 132 ? 29.436 13.696  76.391 1.00 33.44  ?  150 TYR B CA    1 
ATOM   3912 C C     . TYR B 2 132 ? 30.234 14.756  77.120 1.00 36.86  ?  150 TYR B C     1 
ATOM   3913 O O     . TYR B 2 132 ? 31.466 14.731  77.095 1.00 37.87  ?  150 TYR B O     1 
ATOM   3914 C CB    . TYR B 2 132 ? 28.944 14.223  75.047 1.00 36.33  ?  150 TYR B CB    1 
ATOM   3915 C CG    . TYR B 2 132 ? 29.933 15.059  74.271 1.00 37.17  ?  150 TYR B CG    1 
ATOM   3916 C CD1   . TYR B 2 132 ? 30.929 14.456  73.504 1.00 32.68  ?  150 TYR B CD1   1 
ATOM   3917 C CD2   . TYR B 2 132 ? 29.842 16.462  74.264 1.00 37.46  ?  150 TYR B CD2   1 
ATOM   3918 C CE1   . TYR B 2 132 ? 31.834 15.221  72.782 1.00 34.34  ?  150 TYR B CE1   1 
ATOM   3919 C CE2   . TYR B 2 132 ? 30.747 17.244  73.539 1.00 38.09  ?  150 TYR B CE2   1 
ATOM   3920 C CZ    . TYR B 2 132 ? 31.739 16.613  72.803 1.00 36.34  ?  150 TYR B CZ    1 
ATOM   3921 O OH    . TYR B 2 132 ? 32.634 17.358  72.081 1.00 37.69  ?  150 TYR B OH    1 
ATOM   3922 N N     . ASN B 2 133 ? 29.553 15.695  77.773 1.00 37.87  ?  151 ASN B N     1 
ATOM   3923 C CA    . ASN B 2 133 ? 30.273 16.726  78.502 1.00 37.36  ?  151 ASN B CA    1 
ATOM   3924 C C     . ASN B 2 133 ? 31.077 16.138  79.652 1.00 39.05  ?  151 ASN B C     1 
ATOM   3925 O O     . ASN B 2 133 ? 31.978 16.810  80.164 1.00 48.34  ?  151 ASN B O     1 
ATOM   3926 C CB    . ASN B 2 133 ? 29.302 17.784  79.021 1.00 37.22  ?  151 ASN B CB    1 
ATOM   3927 C CG    . ASN B 2 133 ? 28.747 18.678  77.917 1.00 41.96  ?  151 ASN B CG    1 
ATOM   3928 O OD1   . ASN B 2 133 ? 29.401 18.917  76.894 1.00 39.12  ?  151 ASN B OD1   1 
ATOM   3929 N ND2   . ASN B 2 133 ? 27.532 19.198  78.136 1.00 43.87  ?  151 ASN B ND2   1 
ATOM   3930 N N     . ALA B 2 134 ? 30.785 14.899  80.052 1.00 34.90  ?  152 ALA B N     1 
ATOM   3931 C CA    . ALA B 2 134 ? 31.467 14.213  81.147 1.00 38.07  ?  152 ALA B CA    1 
ATOM   3932 C C     . ALA B 2 134 ? 32.671 13.406  80.665 1.00 41.75  ?  152 ALA B C     1 
ATOM   3933 O O     . ALA B 2 134 ? 33.748 13.484  81.267 1.00 48.57  ?  152 ALA B O     1 
ATOM   3934 C CB    . ALA B 2 134 ? 30.493 13.289  81.895 1.00 32.62  ?  152 ALA B CB    1 
ATOM   3935 N N     . VAL B 2 135 ? 32.513 12.634  79.582 1.00 36.88  ?  153 VAL B N     1 
ATOM   3936 C CA    . VAL B 2 135 ? 33.585 11.763  79.096 1.00 42.74  ?  153 VAL B CA    1 
ATOM   3937 C C     . VAL B 2 135 ? 34.450 12.381  77.982 1.00 41.27  ?  153 VAL B C     1 
ATOM   3938 O O     . VAL B 2 135 ? 35.463 11.772  77.605 1.00 38.97  ?  153 VAL B O     1 
ATOM   3939 C CB    . VAL B 2 135 ? 33.032 10.403  78.609 1.00 38.53  ?  153 VAL B CB    1 
ATOM   3940 C CG1   . VAL B 2 135 ? 32.162 9.768   79.680 1.00 33.97  ?  153 VAL B CG1   1 
ATOM   3941 C CG2   . VAL B 2 135 ? 32.298 10.542  77.262 1.00 36.81  ?  153 VAL B CG2   1 
ATOM   3942 N N     . LYS B 2 136 ? 34.091 13.548  77.444 1.00 38.49  ?  154 LYS B N     1 
ATOM   3943 C CA    . LYS B 2 136 ? 34.919 14.150  76.414 1.00 35.27  ?  154 LYS B CA    1 
ATOM   3944 C C     . LYS B 2 136 ? 36.313 14.400  76.968 1.00 38.84  ?  154 LYS B C     1 
ATOM   3945 O O     . LYS B 2 136 ? 36.482 14.591  78.173 1.00 43.43  ?  154 LYS B O     1 
ATOM   3946 C CB    . LYS B 2 136 ? 34.327 15.463  75.920 1.00 33.05  ?  154 LYS B CB    1 
ATOM   3947 C CG    . LYS B 2 136 ? 34.359 16.596  76.913 1.00 36.91  ?  154 LYS B CG    1 
ATOM   3948 C CD    . LYS B 2 136 ? 33.720 17.833  76.290 1.00 37.23  ?  154 LYS B CD    1 
ATOM   3949 C CE    . LYS B 2 136 ? 33.823 19.036  77.177 1.00 35.92  ?  154 LYS B CE    1 
ATOM   3950 N NZ    . LYS B 2 136 ? 35.210 19.279  77.628 1.00 40.07  ?  154 LYS B NZ    1 
ATOM   3951 N N     . PRO B 2 137 ? 37.333 14.372  76.123 1.00 38.29  ?  155 PRO B N     1 
ATOM   3952 C CA    . PRO B 2 137 ? 38.646 14.828  76.561 1.00 39.20  ?  155 PRO B CA    1 
ATOM   3953 C C     . PRO B 2 137 ? 38.593 16.327  76.810 1.00 44.60  ?  155 PRO B C     1 
ATOM   3954 O O     . PRO B 2 137 ? 37.610 17.001  76.491 1.00 43.70  ?  155 PRO B O     1 
ATOM   3955 C CB    . PRO B 2 137 ? 39.560 14.454  75.390 1.00 38.47  ?  155 PRO B CB    1 
ATOM   3956 C CG    . PRO B 2 137 ? 38.680 14.412  74.220 1.00 37.12  ?  155 PRO B CG    1 
ATOM   3957 C CD    . PRO B 2 137 ? 37.349 13.930  74.719 1.00 38.48  ?  155 PRO B CD    1 
ATOM   3958 N N     . GLU B 2 138 ? 39.669 16.856  77.401 1.00 49.33  ?  156 GLU B N     1 
ATOM   3959 C CA    . GLU B 2 138 ? 39.673 18.279  77.737 1.00 48.42  ?  156 GLU B CA    1 
ATOM   3960 C C     . GLU B 2 138 ? 39.691 19.167  76.497 1.00 47.54  ?  156 GLU B C     1 
ATOM   3961 O O     . GLU B 2 138 ? 39.149 20.279  76.530 1.00 50.35  ?  156 GLU B O     1 
ATOM   3962 C CB    . GLU B 2 138 ? 40.854 18.603  78.634 1.00 48.05  ?  156 GLU B CB    1 
ATOM   3963 C CG    . GLU B 2 138 ? 42.127 17.958  78.171 1.00 60.17  ?  156 GLU B CG    1 
ATOM   3964 C CD    . GLU B 2 138 ? 43.364 18.663  78.708 1.00 70.11  ?  156 GLU B CD    1 
ATOM   3965 O OE1   . GLU B 2 138 ? 43.813 19.649  78.067 1.00 67.29  ?  156 GLU B OE1   1 
ATOM   3966 O OE2   . GLU B 2 138 ? 43.884 18.223  79.767 1.00 72.38  -1 156 GLU B OE2   1 
ATOM   3967 N N     . TYR B 2 139 ? 40.299 18.706  75.401 1.00 45.69  ?  157 TYR B N     1 
ATOM   3968 C CA    . TYR B 2 139 ? 40.416 19.518  74.196 1.00 40.22  ?  157 TYR B CA    1 
ATOM   3969 C C     . TYR B 2 139 ? 39.139 19.530  73.367 1.00 43.16  ?  157 TYR B C     1 
ATOM   3970 O O     . TYR B 2 139 ? 39.079 20.233  72.356 1.00 42.72  ?  157 TYR B O     1 
ATOM   3971 C CB    . TYR B 2 139 ? 41.593 19.033  73.338 1.00 36.04  ?  157 TYR B CB    1 
ATOM   3972 C CG    . TYR B 2 139 ? 41.654 17.540  73.141 1.00 40.49  ?  157 TYR B CG    1 
ATOM   3973 C CD1   . TYR B 2 139 ? 40.863 16.908  72.172 1.00 43.67  ?  157 TYR B CD1   1 
ATOM   3974 C CD2   . TYR B 2 139 ? 42.496 16.751  73.910 1.00 41.00  ?  157 TYR B CD2   1 
ATOM   3975 C CE1   . TYR B 2 139 ? 40.910 15.536  71.982 1.00 38.93  ?  157 TYR B CE1   1 
ATOM   3976 C CE2   . TYR B 2 139 ? 42.555 15.367  73.717 1.00 39.33  ?  157 TYR B CE2   1 
ATOM   3977 C CZ    . TYR B 2 139 ? 41.761 14.777  72.758 1.00 38.08  ?  157 TYR B CZ    1 
ATOM   3978 O OH    . TYR B 2 139 ? 41.809 13.426  72.579 1.00 37.04  ?  157 TYR B OH    1 
ATOM   3979 N N     . ALA B 2 140 ? 38.122 18.770  73.753 1.00 43.03  ?  158 ALA B N     1 
ATOM   3980 C CA    . ALA B 2 140 ? 36.852 18.786  73.052 1.00 43.04  ?  158 ALA B CA    1 
ATOM   3981 C C     . ALA B 2 140 ? 35.925 19.809  73.705 1.00 42.96  ?  158 ALA B C     1 
ATOM   3982 O O     . ALA B 2 140 ? 35.870 19.907  74.933 1.00 41.94  ?  158 ALA B O     1 
ATOM   3983 C CB    . ALA B 2 140 ? 36.234 17.387  73.066 1.00 41.27  ?  158 ALA B CB    1 
ATOM   3984 N N     . VAL B 2 141 ? 35.219 20.593  72.873 1.00 42.78  ?  159 VAL B N     1 
ATOM   3985 C CA    . VAL B 2 141 ? 34.334 21.633  73.392 1.00 39.83  ?  159 VAL B CA    1 
ATOM   3986 C C     . VAL B 2 141 ? 33.133 20.980  74.048 1.00 43.18  ?  159 VAL B C     1 
ATOM   3987 O O     . VAL B 2 141 ? 32.625 19.946  73.584 1.00 45.34  ?  159 VAL B O     1 
ATOM   3988 C CB    . VAL B 2 141 ? 33.843 22.613  72.303 1.00 44.86  ?  159 VAL B CB    1 
ATOM   3989 C CG1   . VAL B 2 141 ? 33.508 23.966  72.919 1.00 48.48  ?  159 VAL B CG1   1 
ATOM   3990 C CG2   . VAL B 2 141 ? 34.820 22.769  71.183 1.00 41.39  ?  159 VAL B CG2   1 
ATOM   3991 N N     . THR B 2 142 ? 32.648 21.605  75.116 1.00 44.85  ?  160 THR B N     1 
ATOM   3992 C CA    . THR B 2 142 ? 31.376 21.197  75.686 1.00 45.37  ?  160 THR B CA    1 
ATOM   3993 C C     . THR B 2 142 ? 30.249 21.632  74.758 1.00 48.17  ?  160 THR B C     1 
ATOM   3994 O O     . THR B 2 142 ? 30.369 22.610  74.013 1.00 45.07  ?  160 THR B O     1 
ATOM   3995 C CB    . THR B 2 142 ? 31.183 21.794  77.085 1.00 44.15  ?  160 THR B CB    1 
ATOM   3996 O OG1   . THR B 2 142 ? 30.911 23.189  76.971 1.00 54.71  ?  160 THR B OG1   1 
ATOM   3997 C CG2   . THR B 2 142 ? 32.420 21.625  77.938 1.00 45.12  ?  160 THR B CG2   1 
ATOM   3998 N N     . HIS B 2 143 ? 29.158 20.872  74.790 1.00 51.24  ?  161 HIS B N     1 
ATOM   3999 C CA    . HIS B 2 143 ? 27.935 21.197  74.063 1.00 51.43  ?  161 HIS B CA    1 
ATOM   4000 C C     . HIS B 2 143 ? 26.942 21.828  75.035 1.00 57.72  ?  161 HIS B C     1 
ATOM   4001 O O     . HIS B 2 143 ? 26.526 21.174  76.002 1.00 62.28  ?  161 HIS B O     1 
ATOM   4002 C CB    . HIS B 2 143 ? 27.339 19.940  73.429 1.00 45.14  ?  161 HIS B CB    1 
ATOM   4003 C CG    . HIS B 2 143 ? 26.233 20.222  72.470 1.00 48.90  ?  161 HIS B CG    1 
ATOM   4004 N ND1   . HIS B 2 143 ? 26.378 20.080  71.106 1.00 48.60  ?  161 HIS B ND1   1 
ATOM   4005 C CD2   . HIS B 2 143 ? 24.968 20.660  72.672 1.00 51.16  ?  161 HIS B CD2   1 
ATOM   4006 C CE1   . HIS B 2 143 ? 25.249 20.414  70.507 1.00 49.23  ?  161 HIS B CE1   1 
ATOM   4007 N NE2   . HIS B 2 143 ? 24.379 20.773  71.435 1.00 54.52  ?  161 HIS B NE2   1 
ATOM   4008 N N     . GLU B 2 144 ? 26.562 23.095  74.792 1.00 60.34  ?  162 GLU B N     1 
ATOM   4009 C CA    . GLU B 2 144 ? 25.632 23.787  75.687 1.00 66.09  ?  162 GLU B CA    1 
ATOM   4010 C C     . GLU B 2 144 ? 24.378 24.323  75.012 1.00 61.15  ?  162 GLU B C     1 
ATOM   4011 O O     . GLU B 2 144 ? 23.511 24.869  75.707 1.00 60.01  ?  162 GLU B O     1 
ATOM   4012 C CB    . GLU B 2 144 ? 26.316 24.964  76.400 1.00 66.21  ?  162 GLU B CB    1 
ATOM   4013 C CG    . GLU B 2 144 ? 27.741 24.732  76.812 1.00 67.63  ?  162 GLU B CG    1 
ATOM   4014 C CD    . GLU B 2 144 ? 28.572 25.989  76.653 1.00 82.75  ?  162 GLU B CD    1 
ATOM   4015 O OE1   . GLU B 2 144 ? 28.863 26.353  75.485 1.00 83.65  ?  162 GLU B OE1   1 
ATOM   4016 O OE2   . GLU B 2 144 ? 28.919 26.618  77.684 1.00 89.02  -1 162 GLU B OE2   1 
ATOM   4017 N N     . THR B 2 145 ? 24.264 24.209  73.698 1.00 53.18  ?  163 THR B N     1 
ATOM   4018 C CA    . THR B 2 145 ? 23.029 24.541  73.012 1.00 57.99  ?  163 THR B CA    1 
ATOM   4019 C C     . THR B 2 145 ? 22.004 23.415  73.181 1.00 63.37  ?  163 THR B C     1 
ATOM   4020 O O     . THR B 2 145 ? 22.359 22.248  73.385 1.00 64.88  ?  163 THR B O     1 
ATOM   4021 C CB    . THR B 2 145 ? 23.319 24.786  71.534 1.00 58.73  ?  163 THR B CB    1 
ATOM   4022 O OG1   . THR B 2 145 ? 23.170 23.562  70.800 1.00 56.66  ?  163 THR B OG1   1 
ATOM   4023 C CG2   . THR B 2 145 ? 24.748 25.274  71.375 1.00 63.58  ?  163 THR B CG2   1 
ATOM   4024 N N     . GLU B 2 146 ? 20.722 23.765  73.111 1.00 58.84  ?  164 GLU B N     1 
ATOM   4025 C CA    . GLU B 2 146 ? 19.682 22.746  73.163 1.00 55.96  ?  164 GLU B CA    1 
ATOM   4026 C C     . GLU B 2 146 ? 19.473 22.153  71.776 1.00 55.52  ?  164 GLU B C     1 
ATOM   4027 O O     . GLU B 2 146 ? 19.442 22.878  70.779 1.00 57.84  ?  164 GLU B O     1 
ATOM   4028 C CB    . GLU B 2 146 ? 18.379 23.339  73.688 1.00 59.18  ?  164 GLU B CB    1 
ATOM   4029 C CG    . GLU B 2 146 ? 17.147 22.586  73.240 1.00 61.41  ?  164 GLU B CG    1 
ATOM   4030 C CD    . GLU B 2 146 ? 16.047 22.578  74.295 1.00 71.44  ?  164 GLU B CD    1 
ATOM   4031 O OE1   . GLU B 2 146 ? 15.167 21.673  74.259 1.00 69.48  ?  164 GLU B OE1   1 
ATOM   4032 O OE2   . GLU B 2 146 ? 16.069 23.484  75.160 1.00 74.74  -1 164 GLU B OE2   1 
ATOM   4033 N N     . ILE B 2 147 ? 19.350 20.827  71.712 1.00 51.92  ?  165 ILE B N     1 
ATOM   4034 C CA    . ILE B 2 147 ? 19.173 20.125  70.440 1.00 49.09  ?  165 ILE B CA    1 
ATOM   4035 C C     . ILE B 2 147 ? 17.698 20.201  70.064 1.00 49.31  ?  165 ILE B C     1 
ATOM   4036 O O     . ILE B 2 147 ? 16.897 19.388  70.522 1.00 47.88  ?  165 ILE B O     1 
ATOM   4037 C CB    . ILE B 2 147 ? 19.660 18.672  70.499 1.00 47.87  ?  165 ILE B CB    1 
ATOM   4038 C CG1   . ILE B 2 147 ? 21.174 18.574  70.774 1.00 45.22  ?  165 ILE B CG1   1 
ATOM   4039 C CG2   . ILE B 2 147 ? 19.284 17.927  69.212 1.00 43.23  ?  165 ILE B CG2   1 
ATOM   4040 C CD1   . ILE B 2 147 ? 21.568 18.274  72.196 1.00 46.86  ?  165 ILE B CD1   1 
ATOM   4041 N N     . LYS B 2 148 ? 17.342 21.148  69.189 1.00 54.56  ?  166 LYS B N     1 
ATOM   4042 C CA    . LYS B 2 148 ? 15.961 21.355  68.747 1.00 53.52  ?  166 LYS B CA    1 
ATOM   4043 C C     . LYS B 2 148 ? 15.604 20.618  67.458 1.00 51.68  ?  166 LYS B C     1 
ATOM   4044 O O     . LYS B 2 148 ? 14.453 20.210  67.300 1.00 50.43  ?  166 LYS B O     1 
ATOM   4045 C CB    . LYS B 2 148 ? 15.672 22.853  68.546 1.00 52.16  ?  166 LYS B CB    1 
ATOM   4046 C CG    . LYS B 2 148 ? 15.713 23.716  69.803 1.00 56.50  ?  166 LYS B CG    1 
ATOM   4047 C CD    . LYS B 2 148 ? 16.621 24.937  69.624 1.00 61.36  ?  166 LYS B CD    1 
ATOM   4048 C CE    . LYS B 2 148 ? 16.774 25.742  70.933 1.00 68.11  ?  166 LYS B CE    1 
ATOM   4049 N NZ    . LYS B 2 148 ? 18.038 26.561  71.003 1.00 71.58  ?  166 LYS B NZ    1 
ATOM   4050 N N     . THR B 2 149 ? 16.536 20.441  66.524 1.00 53.54  ?  167 THR B N     1 
ATOM   4051 C CA    . THR B 2 149 ? 16.232 19.799  65.250 1.00 55.15  ?  167 THR B CA    1 
ATOM   4052 C C     . THR B 2 149 ? 17.102 18.570  65.070 1.00 50.44  ?  167 THR B C     1 
ATOM   4053 O O     . THR B 2 149 ? 18.185 18.473  65.650 1.00 47.42  ?  167 THR B O     1 
ATOM   4054 C CB    . THR B 2 149 ? 16.456 20.743  64.062 1.00 52.17  ?  167 THR B CB    1 
ATOM   4055 O OG1   . THR B 2 149 ? 17.862 21.013  63.911 1.00 48.32  ?  167 THR B OG1   1 
ATOM   4056 C CG2   . THR B 2 149 ? 15.744 22.028  64.316 1.00 49.42  ?  167 THR B CG2   1 
ATOM   4057 N N     . LEU B 2 150 ? 16.640 17.653  64.212 1.00 49.66  ?  168 LEU B N     1 
ATOM   4058 C CA    . LEU B 2 150 ? 17.362 16.397  64.038 1.00 43.89  ?  168 LEU B CA    1 
ATOM   4059 C C     . LEU B 2 150 ? 18.749 16.600  63.439 1.00 45.59  ?  168 LEU B C     1 
ATOM   4060 O O     . LEU B 2 150 ? 19.648 15.809  63.735 1.00 44.09  ?  168 LEU B O     1 
ATOM   4061 C CB    . LEU B 2 150 ? 16.550 15.414  63.193 1.00 43.30  ?  168 LEU B CB    1 
ATOM   4062 C CG    . LEU B 2 150 ? 17.163 14.012  63.015 1.00 44.77  ?  168 LEU B CG    1 
ATOM   4063 C CD1   . LEU B 2 150 ? 16.888 13.104  64.210 1.00 35.57  ?  168 LEU B CD1   1 
ATOM   4064 C CD2   . LEU B 2 150 ? 16.717 13.344  61.711 1.00 43.85  ?  168 LEU B CD2   1 
ATOM   4065 N N     . ASP B 2 151 ? 18.959 17.631  62.598 1.00 51.54  ?  169 ASP B N     1 
ATOM   4066 C CA    . ASP B 2 151 ? 20.325 17.919  62.140 1.00 48.95  ?  169 ASP B CA    1 
ATOM   4067 C C     . ASP B 2 151 ? 21.187 18.385  63.289 1.00 48.68  ?  169 ASP B C     1 
ATOM   4068 O O     . ASP B 2 151 ? 22.403 18.177  63.282 1.00 50.63  ?  169 ASP B O     1 
ATOM   4069 C CB    . ASP B 2 151 ? 20.393 19.013  61.071 1.00 52.15  ?  169 ASP B CB    1 
ATOM   4070 C CG    . ASP B 2 151 ? 19.398 18.822  59.943 1.00 72.61  ?  169 ASP B CG    1 
ATOM   4071 O OD1   . ASP B 2 151 ? 18.230 18.440  60.224 1.00 79.00  ?  169 ASP B OD1   1 
ATOM   4072 O OD2   . ASP B 2 151 ? 19.770 19.100  58.774 1.00 73.37  -1 169 ASP B OD2   1 
ATOM   4073 N N     . GLU B 2 152 ? 20.595 19.125  64.226 1.00 50.29  ?  170 GLU B N     1 
ATOM   4074 C CA    . GLU B 2 152 ? 21.377 19.609  65.351 1.00 52.76  ?  170 GLU B CA    1 
ATOM   4075 C C     . GLU B 2 152 ? 21.858 18.439  66.196 1.00 47.15  ?  170 GLU B C     1 
ATOM   4076 O O     . GLU B 2 152 ? 22.947 18.503  66.772 1.00 47.25  ?  170 GLU B O     1 
ATOM   4077 C CB    . GLU B 2 152 ? 20.564 20.608  66.191 1.00 54.35  ?  170 GLU B CB    1 
ATOM   4078 C CG    . GLU B 2 152 ? 20.462 22.051  65.626 1.00 56.92  ?  170 GLU B CG    1 
ATOM   4079 C CD    . GLU B 2 152 ? 19.728 23.046  66.571 1.00 63.79  ?  170 GLU B CD    1 
ATOM   4080 O OE1   . GLU B 2 152 ? 19.980 24.280  66.499 1.00 67.08  ?  170 GLU B OE1   1 
ATOM   4081 O OE2   . GLU B 2 152 ? 18.894 22.595  67.387 1.00 62.05  -1 170 GLU B OE2   1 
ATOM   4082 N N     . ALA B 2 153 ? 21.072 17.359  66.258 1.00 41.56  ?  171 ALA B N     1 
ATOM   4083 C CA    . ALA B 2 153 ? 21.500 16.137  66.922 1.00 38.16  ?  171 ALA B CA    1 
ATOM   4084 C C     . ALA B 2 153 ? 22.410 15.314  66.024 1.00 43.00  ?  171 ALA B C     1 
ATOM   4085 O O     . ALA B 2 153 ? 23.331 14.646  66.515 1.00 41.49  ?  171 ALA B O     1 
ATOM   4086 C CB    . ALA B 2 153 ? 20.285 15.310  67.349 1.00 31.85  ?  171 ALA B CB    1 
ATOM   4087 N N     . LYS B 2 154 ? 22.171 15.353  64.713 1.00 43.22  ?  172 LYS B N     1 
ATOM   4088 C CA    . LYS B 2 154 ? 23.083 14.714  63.774 1.00 42.22  ?  172 LYS B CA    1 
ATOM   4089 C C     . LYS B 2 154 ? 24.501 15.261  63.916 1.00 43.97  ?  172 LYS B C     1 
ATOM   4090 O O     . LYS B 2 154 ? 25.468 14.494  63.931 1.00 44.51  ?  172 LYS B O     1 
ATOM   4091 C CB    . LYS B 2 154 ? 22.566 14.894  62.346 1.00 40.65  ?  172 LYS B CB    1 
ATOM   4092 C CG    . LYS B 2 154 ? 23.160 13.914  61.369 1.00 39.80  ?  172 LYS B CG    1 
ATOM   4093 C CD    . LYS B 2 154 ? 22.434 13.929  60.027 1.00 46.41  ?  172 LYS B CD    1 
ATOM   4094 C CE    . LYS B 2 154 ? 23.375 14.360  58.882 1.00 46.87  ?  172 LYS B CE    1 
ATOM   4095 N NZ    . LYS B 2 154 ? 23.990 13.225  58.129 1.00 40.48  ?  172 LYS B NZ    1 
ATOM   4096 N N     . GLN B 2 155 ? 24.656 16.582  64.027 1.00 45.64  ?  173 GLN B N     1 
ATOM   4097 C CA    . GLN B 2 155 ? 26.000 17.133  64.172 1.00 48.08  ?  173 GLN B CA    1 
ATOM   4098 C C     . GLN B 2 155 ? 26.578 16.836  65.550 1.00 44.66  ?  173 GLN B C     1 
ATOM   4099 O O     . GLN B 2 155 ? 27.798 16.677  65.697 1.00 42.69  ?  173 GLN B O     1 
ATOM   4100 C CB    . GLN B 2 155 ? 25.992 18.641  63.923 1.00 55.59  ?  173 GLN B CB    1 
ATOM   4101 C CG    . GLN B 2 155 ? 25.606 19.035  62.516 1.00 61.82  ?  173 GLN B CG    1 
ATOM   4102 C CD    . GLN B 2 155 ? 25.058 20.454  62.454 1.00 74.36  ?  173 GLN B CD    1 
ATOM   4103 O OE1   . GLN B 2 155 ? 25.549 21.352  63.158 1.00 78.56  ?  173 GLN B OE1   1 
ATOM   4104 N NE2   . GLN B 2 155 ? 24.037 20.667  61.608 1.00 71.23  ?  173 GLN B NE2   1 
ATOM   4105 N N     . PHE B 2 156 ? 25.723 16.765  66.565 1.00 42.28  ?  174 PHE B N     1 
ATOM   4106 C CA    . PHE B 2 156 ? 26.185 16.439  67.908 1.00 43.54  ?  174 PHE B CA    1 
ATOM   4107 C C     . PHE B 2 156 ? 26.719 15.017  67.958 1.00 40.19  ?  174 PHE B C     1 
ATOM   4108 O O     . PHE B 2 156 ? 27.857 14.775  68.367 1.00 38.21  ?  174 PHE B O     1 
ATOM   4109 C CB    . PHE B 2 156 ? 25.038 16.615  68.903 1.00 37.94  ?  174 PHE B CB    1 
ATOM   4110 C CG    . PHE B 2 156 ? 25.307 16.032  70.231 1.00 36.57  ?  174 PHE B CG    1 
ATOM   4111 C CD1   . PHE B 2 156 ? 26.366 16.491  70.993 1.00 38.06  ?  174 PHE B CD1   1 
ATOM   4112 C CD2   . PHE B 2 156 ? 24.507 15.017  70.733 1.00 36.29  ?  174 PHE B CD2   1 
ATOM   4113 C CE1   . PHE B 2 156 ? 26.621 15.968  72.259 1.00 38.43  ?  174 PHE B CE1   1 
ATOM   4114 C CE2   . PHE B 2 156 ? 24.753 14.473  71.994 1.00 37.56  ?  174 PHE B CE2   1 
ATOM   4115 C CZ    . PHE B 2 156 ? 25.819 14.953  72.764 1.00 37.90  ?  174 PHE B CZ    1 
ATOM   4116 N N     . ILE B 2 157 ? 25.889 14.062  67.552 1.00 39.49  ?  175 ILE B N     1 
ATOM   4117 C CA    . ILE B 2 157 ? 26.271 12.659  67.558 1.00 36.76  ?  175 ILE B CA    1 
ATOM   4118 C C     . ILE B 2 157 ? 27.600 12.480  66.825 1.00 39.42  ?  175 ILE B C     1 
ATOM   4119 O O     . ILE B 2 157 ? 28.534 11.854  67.346 1.00 39.07  ?  175 ILE B O     1 
ATOM   4120 C CB    . ILE B 2 157 ? 25.102 11.823  66.975 1.00 41.15  ?  175 ILE B CB    1 
ATOM   4121 C CG1   . ILE B 2 157 ? 24.168 11.402  68.099 1.00 44.53  ?  175 ILE B CG1   1 
ATOM   4122 C CG2   . ILE B 2 157 ? 25.512 10.592  66.224 1.00 40.26  ?  175 ILE B CG2   1 
ATOM   4123 C CD1   . ILE B 2 157 ? 24.878 11.208  69.432 1.00 43.02  ?  175 ILE B CD1   1 
ATOM   4124 N N     . LEU B 2 158 ? 27.744 13.108  65.652 1.00 37.81  ?  176 LEU B N     1 
ATOM   4125 C CA    . LEU B 2 158 ? 28.975 12.956  64.873 1.00 37.80  ?  176 LEU B CA    1 
ATOM   4126 C C     . LEU B 2 158 ? 30.204 13.497  65.601 1.00 37.61  ?  176 LEU B C     1 
ATOM   4127 O O     . LEU B 2 158 ? 31.315 13.001  65.386 1.00 41.39  ?  176 LEU B O     1 
ATOM   4128 C CB    . LEU B 2 158 ? 28.838 13.647  63.514 1.00 35.58  ?  176 LEU B CB    1 
ATOM   4129 C CG    . LEU B 2 158 ? 27.887 12.950  62.549 1.00 35.96  ?  176 LEU B CG    1 
ATOM   4130 C CD1   . LEU B 2 158 ? 28.009 13.488  61.168 1.00 33.01  ?  176 LEU B CD1   1 
ATOM   4131 C CD2   . LEU B 2 158 ? 28.165 11.462  62.567 1.00 37.57  ?  176 LEU B CD2   1 
ATOM   4132 N N     . SER B 2 159 ? 30.043 14.513  66.445 1.00 37.35  ?  177 SER B N     1 
ATOM   4133 C CA    . SER B 2 159 ? 31.210 15.123  67.073 1.00 37.63  ?  177 SER B CA    1 
ATOM   4134 C C     . SER B 2 159 ? 31.876 14.217  68.115 1.00 40.64  ?  177 SER B C     1 
ATOM   4135 O O     . SER B 2 159 ? 32.864 14.638  68.735 1.00 37.68  ?  177 SER B O     1 
ATOM   4136 C CB    . SER B 2 159 ? 30.821 16.482  67.681 1.00 37.45  ?  177 SER B CB    1 
ATOM   4137 O OG    . SER B 2 159 ? 30.276 16.379  68.986 1.00 33.02  ?  177 SER B OG    1 
ATOM   4138 N N     . PHE B 2 160 ? 31.380 12.984  68.304 1.00 44.01  ?  178 PHE B N     1 
ATOM   4139 C CA    . PHE B 2 160 ? 32.013 12.026  69.210 1.00 38.96  ?  178 PHE B CA    1 
ATOM   4140 C C     . PHE B 2 160 ? 33.359 11.558  68.690 1.00 40.56  ?  178 PHE B C     1 
ATOM   4141 O O     . PHE B 2 160 ? 34.136 10.969  69.459 1.00 39.71  ?  178 PHE B O     1 
ATOM   4142 C CB    . PHE B 2 160 ? 31.119 10.807  69.424 1.00 38.79  ?  178 PHE B CB    1 
ATOM   4143 C CG    . PHE B 2 160 ? 29.838 11.112  70.136 1.00 36.49  ?  178 PHE B CG    1 
ATOM   4144 C CD1   . PHE B 2 160 ? 29.570 12.391  70.595 1.00 36.75  ?  178 PHE B CD1   1 
ATOM   4145 C CD2   . PHE B 2 160 ? 28.907 10.120  70.351 1.00 32.49  ?  178 PHE B CD2   1 
ATOM   4146 C CE1   . PHE B 2 160 ? 28.407 12.669  71.253 1.00 34.56  ?  178 PHE B CE1   1 
ATOM   4147 C CE2   . PHE B 2 160 ? 27.734 10.390  70.997 1.00 32.68  ?  178 PHE B CE2   1 
ATOM   4148 C CZ    . PHE B 2 160 ? 27.484 11.666  71.455 1.00 37.69  ?  178 PHE B CZ    1 
ATOM   4149 N N     . VAL B 2 161 ? 33.637 11.792  67.403 1.00 37.04  ?  179 VAL B N     1 
ATOM   4150 C CA    . VAL B 2 161 ? 34.948 11.496  66.859 1.00 39.06  ?  179 VAL B CA    1 
ATOM   4151 C C     . VAL B 2 161 ? 36.033 12.245  67.622 1.00 42.52  ?  179 VAL B C     1 
ATOM   4152 O O     . VAL B 2 161 ? 37.205 11.850  67.568 1.00 43.55  ?  179 VAL B O     1 
ATOM   4153 C CB    . VAL B 2 161 ? 34.961 11.836  65.356 1.00 36.69  ?  179 VAL B CB    1 
ATOM   4154 C CG1   . VAL B 2 161 ? 35.024 13.321  65.179 1.00 37.65  ?  179 VAL B CG1   1 
ATOM   4155 C CG2   . VAL B 2 161 ? 36.109 11.150  64.660 1.00 34.10  ?  179 VAL B CG2   1 
ATOM   4156 N N     . MET B 2 162 ? 35.673 13.322  68.343 1.00 42.49  ?  180 MET B N     1 
ATOM   4157 C CA    . MET B 2 162 ? 36.649 14.033  69.170 1.00 44.25  ?  180 MET B CA    1 
ATOM   4158 C C     . MET B 2 162 ? 37.259 13.132  70.225 1.00 43.30  ?  180 MET B C     1 
ATOM   4159 O O     . MET B 2 162 ? 38.370 13.417  70.693 1.00 42.99  ?  180 MET B O     1 
ATOM   4160 C CB    . MET B 2 162 ? 36.026 15.248  69.872 1.00 45.68  ?  180 MET B CB    1 
ATOM   4161 C CG    . MET B 2 162 ? 36.143 16.572  69.104 1.00 48.84  ?  180 MET B CG    1 
ATOM   4162 S SD    . MET B 2 162 ? 37.800 17.001  68.501 1.00 59.56  ?  180 MET B SD    1 
ATOM   4163 C CE    . MET B 2 162 ? 37.514 16.917  66.744 1.00 48.13  ?  180 MET B CE    1 
ATOM   4164 N N     . LEU B 2 163 ? 36.551 12.063  70.618 1.00 39.11  ?  181 LEU B N     1 
ATOM   4165 C CA    . LEU B 2 163 ? 37.035 11.136  71.638 1.00 38.66  ?  181 LEU B CA    1 
ATOM   4166 C C     . LEU B 2 163 ? 38.074 10.156  71.104 1.00 39.59  ?  181 LEU B C     1 
ATOM   4167 O O     . LEU B 2 163 ? 38.728 9.480   71.913 1.00 38.47  ?  181 LEU B O     1 
ATOM   4168 C CB    . LEU B 2 163 ? 35.862 10.350  72.238 1.00 35.73  ?  181 LEU B CB    1 
ATOM   4169 C CG    . LEU B 2 163 ? 34.977 10.939  73.344 1.00 35.27  ?  181 LEU B CG    1 
ATOM   4170 C CD1   . LEU B 2 163 ? 34.798 12.422  73.182 1.00 32.34  ?  181 LEU B CD1   1 
ATOM   4171 C CD2   . LEU B 2 163 ? 33.632 10.251  73.299 1.00 30.48  ?  181 LEU B CD2   1 
ATOM   4172 N N     . ASN B 2 164 ? 38.255 10.095  69.778 1.00 38.04  ?  182 ASN B N     1 
ATOM   4173 C CA    . ASN B 2 164 ? 38.969 8.996   69.134 1.00 37.70  ?  182 ASN B CA    1 
ATOM   4174 C C     . ASN B 2 164 ? 40.454 8.983   69.469 1.00 38.49  ?  182 ASN B C     1 
ATOM   4175 O O     . ASN B 2 164 ? 41.111 10.024  69.537 1.00 38.88  ?  182 ASN B O     1 
ATOM   4176 C CB    . ASN B 2 164 ? 38.808 9.072   67.620 1.00 40.64  ?  182 ASN B CB    1 
ATOM   4177 C CG    . ASN B 2 164 ? 37.594 8.333   67.127 1.00 38.26  ?  182 ASN B CG    1 
ATOM   4178 O OD1   . ASN B 2 164 ? 36.740 7.925   67.914 1.00 36.30  ?  182 ASN B OD1   1 
ATOM   4179 N ND2   . ASN B 2 164 ? 37.505 8.156   65.815 1.00 36.15  ?  182 ASN B ND2   1 
ATOM   4180 N N     . ASP B 2 165 ? 40.982 7.776   69.649 1.00 41.19  ?  183 ASP B N     1 
ATOM   4181 C CA    . ASP B 2 165 ? 42.406 7.543   69.867 1.00 38.21  ?  183 ASP B CA    1 
ATOM   4182 C C     . ASP B 2 165 ? 42.848 8.125   71.205 1.00 34.93  ?  183 ASP B C     1 
ATOM   4183 O O     . ASP B 2 165 ? 43.970 8.590   71.359 1.00 36.22  ?  183 ASP B O     1 
ATOM   4184 C CB    . ASP B 2 165 ? 43.238 8.085   68.698 1.00 37.84  ?  183 ASP B CB    1 
ATOM   4185 C CG    . ASP B 2 165 ? 43.045 7.250   67.395 1.00 47.22  ?  183 ASP B CG    1 
ATOM   4186 O OD1   . ASP B 2 165 ? 43.425 7.731   66.297 1.00 47.03  ?  183 ASP B OD1   1 
ATOM   4187 O OD2   . ASP B 2 165 ? 42.496 6.112   67.450 1.00 48.68  -1 183 ASP B OD2   1 
ATOM   4188 N N     . ASN B 2 166 ? 41.954 8.077   72.185 1.00 36.84  ?  184 ASN B N     1 
ATOM   4189 C CA    . ASN B 2 166 ? 42.260 8.517   73.545 1.00 38.82  ?  184 ASN B CA    1 
ATOM   4190 C C     . ASN B 2 166 ? 41.300 7.874   74.552 1.00 36.52  ?  184 ASN B C     1 
ATOM   4191 O O     . ASN B 2 166 ? 41.644 6.860   75.171 1.00 35.87  ?  184 ASN B O     1 
ATOM   4192 C CB    . ASN B 2 166 ? 42.217 10.052  73.618 1.00 34.78  ?  184 ASN B CB    1 
ATOM   4193 C CG    . ASN B 2 166 ? 42.466 10.589  75.015 1.00 33.67  ?  184 ASN B CG    1 
ATOM   4194 O OD1   . ASN B 2 166 ? 42.820 9.834   75.927 1.00 36.58  ?  184 ASN B OD1   1 
ATOM   4195 N ND2   . ASN B 2 166 ? 42.269 11.903  75.198 1.00 31.25  ?  184 ASN B ND2   1 
ATOM   4196 N N     . VAL B 2 167 ? 40.091 8.440   74.689 1.00 35.69  ?  185 VAL B N     1 
ATOM   4197 C CA    . VAL B 2 167 ? 39.121 8.003   75.696 1.00 39.65  ?  185 VAL B CA    1 
ATOM   4198 C C     . VAL B 2 167 ? 38.641 6.573   75.441 1.00 40.53  ?  185 VAL B C     1 
ATOM   4199 O O     . VAL B 2 167 ? 38.386 5.814   76.384 1.00 42.10  ?  185 VAL B O     1 
ATOM   4200 C CB    . VAL B 2 167 ? 37.923 8.973   75.740 1.00 39.30  ?  185 VAL B CB    1 
ATOM   4201 C CG1   . VAL B 2 167 ? 36.902 8.484   76.758 1.00 33.92  ?  185 VAL B CG1   1 
ATOM   4202 C CG2   . VAL B 2 167 ? 38.373 10.394  76.028 1.00 32.83  ?  185 VAL B CG2   1 
ATOM   4203 N N     . GLU B 2 168 ? 38.435 6.205   74.184 1.00 39.71  ?  186 GLU B N     1 
ATOM   4204 C CA    . GLU B 2 168 ? 37.868 4.902   73.853 1.00 38.50  ?  186 GLU B CA    1 
ATOM   4205 C C     . GLU B 2 168 ? 38.917 3.817   73.715 1.00 37.19  ?  186 GLU B C     1 
ATOM   4206 O O     . GLU B 2 168 ? 38.611 2.768   73.148 1.00 38.33  ?  186 GLU B O     1 
ATOM   4207 C CB    . GLU B 2 168 ? 37.047 5.002   72.554 1.00 38.87  ?  186 GLU B CB    1 
ATOM   4208 C CG    . GLU B 2 168 ? 37.803 4.728   71.235 1.00 39.44  ?  186 GLU B CG    1 
ATOM   4209 C CD    . GLU B 2 168 ? 39.090 5.561   71.050 1.00 45.71  ?  186 GLU B CD    1 
ATOM   4210 O OE1   . GLU B 2 168 ? 39.865 5.272   70.101 1.00 48.95  ?  186 GLU B OE1   1 
ATOM   4211 O OE2   . GLU B 2 168 ? 39.343 6.498   71.847 1.00 46.00  -1 186 GLU B OE2   1 
ATOM   4212 N N     . LEU B 2 169 ? 40.146 4.044   74.187 1.00 38.10  ?  187 LEU B N     1 
ATOM   4213 C CA    . LEU B 2 169 ? 41.213 3.077   73.933 1.00 37.98  ?  187 LEU B CA    1 
ATOM   4214 C C     . LEU B 2 169 ? 41.090 1.877   74.865 1.00 38.45  ?  187 LEU B C     1 
ATOM   4215 O O     . LEU B 2 169 ? 41.313 0.739   74.435 1.00 33.74  ?  187 LEU B O     1 
ATOM   4216 C CB    . LEU B 2 169 ? 42.593 3.710   74.078 1.00 36.62  ?  187 LEU B CB    1 
ATOM   4217 C CG    . LEU B 2 169 ? 43.067 4.481   72.840 1.00 39.52  ?  187 LEU B CG    1 
ATOM   4218 C CD1   . LEU B 2 169 ? 44.497 4.914   73.046 1.00 39.85  ?  187 LEU B CD1   1 
ATOM   4219 C CD2   . LEU B 2 169 ? 42.910 3.713   71.517 1.00 41.93  ?  187 LEU B CD2   1 
ATOM   4220 N N     . PRO B 2 170 ? 40.744 2.080   76.140 1.00 37.45  ?  188 PRO B N     1 
ATOM   4221 C CA    . PRO B 2 170 ? 40.440 0.921   76.989 1.00 31.36  ?  188 PRO B CA    1 
ATOM   4222 C C     . PRO B 2 170 ? 39.508 -0.099  76.343 1.00 35.69  ?  188 PRO B C     1 
ATOM   4223 O O     . PRO B 2 170 ? 39.813 -1.296  76.404 1.00 41.45  ?  188 PRO B O     1 
ATOM   4224 C CB    . PRO B 2 170 ? 39.831 1.562   78.235 1.00 28.52  ?  188 PRO B CB    1 
ATOM   4225 C CG    . PRO B 2 170 ? 40.462 2.879   78.311 1.00 32.10  ?  188 PRO B CG    1 
ATOM   4226 C CD    . PRO B 2 170 ? 40.676 3.342   76.895 1.00 35.10  ?  188 PRO B CD    1 
ATOM   4227 N N     . LEU B 2 171 ? 38.376 0.288   75.748 1.00 34.04  ?  189 LEU B N     1 
ATOM   4228 C CA    . LEU B 2 171 ? 37.528 -0.804  75.282 1.00 36.01  ?  189 LEU B CA    1 
ATOM   4229 C C     . LEU B 2 171 ? 37.739 -1.140  73.826 1.00 38.21  ?  189 LEU B C     1 
ATOM   4230 O O     . LEU B 2 171 ? 37.365 -2.240  73.407 1.00 37.47  ?  189 LEU B O     1 
ATOM   4231 C CB    . LEU B 2 171 ? 36.028 -0.554  75.543 1.00 38.92  ?  189 LEU B CB    1 
ATOM   4232 C CG    . LEU B 2 171 ? 35.272 0.672   75.059 1.00 38.53  ?  189 LEU B CG    1 
ATOM   4233 C CD1   . LEU B 2 171 ? 33.793 0.550   75.313 1.00 30.08  ?  189 LEU B CD1   1 
ATOM   4234 C CD2   . LEU B 2 171 ? 35.853 1.874   75.796 1.00 42.67  ?  189 LEU B CD2   1 
ATOM   4235 N N     . LYS B 2 172 ? 38.345 -0.244  73.046 1.00 40.75  ?  190 LYS B N     1 
ATOM   4236 C CA    . LYS B 2 172 ? 38.851 -0.681  71.752 1.00 37.08  ?  190 LYS B CA    1 
ATOM   4237 C C     . LYS B 2 172 ? 39.698 -1.935  71.924 1.00 36.60  ?  190 LYS B C     1 
ATOM   4238 O O     . LYS B 2 172 ? 39.547 -2.908  71.179 1.00 42.03  ?  190 LYS B O     1 
ATOM   4239 C CB    . LYS B 2 172 ? 39.650 0.438   71.070 1.00 38.65  ?  190 LYS B CB    1 
ATOM   4240 C CG    . LYS B 2 172 ? 40.411 -0.023  69.799 1.00 44.17  ?  190 LYS B CG    1 
ATOM   4241 C CD    . LYS B 2 172 ? 40.678 1.127   68.814 1.00 49.72  ?  190 LYS B CD    1 
ATOM   4242 C CE    . LYS B 2 172 ? 42.041 0.992   68.112 1.00 55.42  ?  190 LYS B CE    1 
ATOM   4243 N NZ    . LYS B 2 172 ? 42.705 2.341   67.860 1.00 55.57  ?  190 LYS B NZ    1 
ATOM   4244 N N     . ALA B 2 173 ? 40.548 -1.957  72.941 1.00 32.77  ?  191 ALA B N     1 
ATOM   4245 C CA    . ALA B 2 173 ? 41.558 -2.996  73.045 1.00 34.90  ?  191 ALA B CA    1 
ATOM   4246 C C     . ALA B 2 173 ? 41.016 -4.343  73.524 1.00 35.71  ?  191 ALA B C     1 
ATOM   4247 O O     . ALA B 2 173 ? 41.785 -5.308  73.589 1.00 38.92  ?  191 ALA B O     1 
ATOM   4248 C CB    . ALA B 2 173 ? 42.685 -2.528  73.958 1.00 29.91  ?  191 ALA B CB    1 
ATOM   4249 N N     . GLN B 2 174 ? 39.730 -4.453  73.829 1.00 32.10  ?  192 GLN B N     1 
ATOM   4250 C CA    . GLN B 2 174 ? 39.142 -5.732  74.190 1.00 32.21  ?  192 GLN B CA    1 
ATOM   4251 C C     . GLN B 2 174 ? 38.585 -6.472  72.993 1.00 34.37  ?  192 GLN B C     1 
ATOM   4252 O O     . GLN B 2 174 ? 38.120 -7.608  73.154 1.00 39.07  ?  192 GLN B O     1 
ATOM   4253 C CB    . GLN B 2 174 ? 38.025 -5.544  75.225 1.00 34.62  ?  192 GLN B CB    1 
ATOM   4254 C CG    . GLN B 2 174 ? 38.466 -4.764  76.430 1.00 35.39  ?  192 GLN B CG    1 
ATOM   4255 C CD    . GLN B 2 174 ? 37.383 -4.600  77.462 1.00 36.55  ?  192 GLN B CD    1 
ATOM   4256 O OE1   . GLN B 2 174 ? 36.946 -3.466  77.731 1.00 29.39  ?  192 GLN B OE1   1 
ATOM   4257 N NE2   . GLN B 2 174 ? 36.958 -5.728  78.084 1.00 36.04  ?  192 GLN B NE2   1 
ATOM   4258 N N     . SER B 2 175 ? 38.608 -5.847  71.817 1.00 33.87  ?  193 SER B N     1 
ATOM   4259 C CA    . SER B 2 175 ? 38.089 -6.434  70.589 1.00 35.32  ?  193 SER B CA    1 
ATOM   4260 C C     . SER B 2 175 ? 39.057 -7.402  69.934 1.00 35.47  ?  193 SER B C     1 
ATOM   4261 O O     . SER B 2 175 ? 40.259 -7.126  69.822 1.00 38.19  ?  193 SER B O     1 
ATOM   4262 C CB    . SER B 2 175 ? 37.757 -5.337  69.581 1.00 35.67  ?  193 SER B CB    1 
ATOM   4263 O OG    . SER B 2 175 ? 37.104 -5.882  68.439 1.00 35.38  ?  193 SER B OG    1 
ATOM   4264 N N     . GLU B 2 176 ? 38.508 -8.523  69.461 1.00 35.43  ?  194 GLU B N     1 
ATOM   4265 C CA    . GLU B 2 176 ? 39.220 -9.440  68.582 1.00 38.86  ?  194 GLU B CA    1 
ATOM   4266 C C     . GLU B 2 176 ? 38.806 -9.298  67.129 1.00 37.63  ?  194 GLU B C     1 
ATOM   4267 O O     . GLU B 2 176 ? 39.471 -9.865  66.252 1.00 38.29  ?  194 GLU B O     1 
ATOM   4268 C CB    . GLU B 2 176 ? 39.009 -10.889 69.023 1.00 45.16  ?  194 GLU B CB    1 
ATOM   4269 C CG    . GLU B 2 176 ? 38.691 -11.036 70.504 1.00 52.99  ?  194 GLU B CG    1 
ATOM   4270 C CD    . GLU B 2 176 ? 38.768 -12.476 70.983 1.00 65.53  ?  194 GLU B CD    1 
ATOM   4271 O OE1   . GLU B 2 176 ? 39.815 -12.799 71.582 1.00 74.61  ?  194 GLU B OE1   1 
ATOM   4272 O OE2   . GLU B 2 176 ? 37.805 -13.270 70.777 1.00 66.69  -1 194 GLU B OE2   1 
ATOM   4273 N N     . ARG B 2 177 ? 37.725 -8.567  66.856 1.00 36.55  ?  195 ARG B N     1 
ATOM   4274 C CA    . ARG B 2 177 ? 37.358 -8.274  65.479 1.00 34.86  ?  195 ARG B CA    1 
ATOM   4275 C C     . ARG B 2 177 ? 38.164 -7.115  64.916 1.00 35.04  ?  195 ARG B C     1 
ATOM   4276 O O     . ARG B 2 177 ? 38.489 -7.122  63.722 1.00 33.13  ?  195 ARG B O     1 
ATOM   4277 C CB    . ARG B 2 177 ? 35.865 -7.960  65.379 1.00 32.19  ?  195 ARG B CB    1 
ATOM   4278 C CG    . ARG B 2 177 ? 34.949 -9.091  65.768 1.00 32.52  ?  195 ARG B CG    1 
ATOM   4279 C CD    . ARG B 2 177 ? 33.507 -8.703  65.578 1.00 32.81  ?  195 ARG B CD    1 
ATOM   4280 N NE    . ARG B 2 177 ? 32.599 -9.767  65.977 1.00 31.36  ?  195 ARG B NE    1 
ATOM   4281 C CZ    . ARG B 2 177 ? 31.276 -9.650  66.005 1.00 33.38  ?  195 ARG B CZ    1 
ATOM   4282 N NH1   . ARG B 2 177 ? 30.690 -8.507  65.667 1.00 33.36  ?  195 ARG B NH1   1 
ATOM   4283 N NH2   . ARG B 2 177 ? 30.530 -10.687 66.370 1.00 37.22  ?  195 ARG B NH2   1 
ATOM   4284 N N     . TYR B 2 178 ? 38.514 -6.132  65.756 1.00 32.07  ?  196 TYR B N     1 
ATOM   4285 C CA    . TYR B 2 178 ? 39.016 -4.855  65.268 1.00 31.74  ?  196 TYR B CA    1 
ATOM   4286 C C     . TYR B 2 178 ? 40.445 -4.921  64.750 1.00 35.68  ?  196 TYR B C     1 
ATOM   4287 O O     . TYR B 2 178 ? 40.791 -4.201  63.806 1.00 35.70  ?  196 TYR B O     1 
ATOM   4288 C CB    . TYR B 2 178 ? 38.940 -3.790  66.347 1.00 32.86  ?  196 TYR B CB    1 
ATOM   4289 C CG    . TYR B 2 178 ? 39.143 -2.416  65.779 1.00 35.26  ?  196 TYR B CG    1 
ATOM   4290 C CD1   . TYR B 2 178 ? 38.137 -1.776  65.065 1.00 31.15  ?  196 TYR B CD1   1 
ATOM   4291 C CD2   . TYR B 2 178 ? 40.355 -1.765  65.926 1.00 36.77  ?  196 TYR B CD2   1 
ATOM   4292 C CE1   . TYR B 2 178 ? 38.338 -0.519  64.545 1.00 31.70  ?  196 TYR B CE1   1 
ATOM   4293 C CE2   . TYR B 2 178 ? 40.565 -0.510  65.412 1.00 35.55  ?  196 TYR B CE2   1 
ATOM   4294 C CZ    . TYR B 2 178 ? 39.562 0.116   64.717 1.00 35.02  ?  196 TYR B CZ    1 
ATOM   4295 O OH    . TYR B 2 178 ? 39.800 1.388   64.206 1.00 41.02  ?  196 TYR B OH    1 
ATOM   4296 N N     . PRO B 2 179 ? 41.311 -5.739  65.348 1.00 38.22  ?  197 PRO B N     1 
ATOM   4297 C CA    . PRO B 2 179 ? 42.649 -5.932  64.767 1.00 34.43  ?  197 PRO B CA    1 
ATOM   4298 C C     . PRO B 2 179 ? 42.631 -6.482  63.351 1.00 31.30  ?  197 PRO B C     1 
ATOM   4299 O O     . PRO B 2 179 ? 43.623 -6.347  62.629 1.00 30.45  ?  197 PRO B O     1 
ATOM   4300 C CB    . PRO B 2 179 ? 43.306 -6.921  65.737 1.00 33.02  ?  197 PRO B CB    1 
ATOM   4301 C CG    . PRO B 2 179 ? 42.548 -6.777  67.007 1.00 31.89  ?  197 PRO B CG    1 
ATOM   4302 C CD    . PRO B 2 179 ? 41.155 -6.441  66.636 1.00 35.86  ?  197 PRO B CD    1 
ATOM   4303 N N     . LYS B 2 180 ? 41.556 -7.133  62.935 1.00 36.10  ?  198 LYS B N     1 
ATOM   4304 C CA    . LYS B 2 180 ? 41.446 -7.625  61.572 1.00 38.90  ?  198 LYS B CA    1 
ATOM   4305 C C     . LYS B 2 180 ? 40.897 -6.566  60.617 1.00 39.12  ?  198 LYS B C     1 
ATOM   4306 O O     . LYS B 2 180 ? 40.470 -6.924  59.511 1.00 37.81  ?  198 LYS B O     1 
ATOM   4307 C CB    . LYS B 2 180 ? 40.574 -8.890  61.536 1.00 40.95  ?  198 LYS B CB    1 
ATOM   4308 C CG    . LYS B 2 180 ? 41.362 -10.203 61.476 1.00 40.51  ?  198 LYS B CG    1 
ATOM   4309 C CD    . LYS B 2 180 ? 41.582 -10.788 62.858 1.00 48.02  ?  198 LYS B CD    1 
ATOM   4310 C CE    . LYS B 2 180 ? 42.525 -12.009 62.800 1.00 54.99  ?  198 LYS B CE    1 
ATOM   4311 N NZ    . LYS B 2 180 ? 43.546 -12.034 63.913 1.00 54.45  ?  198 LYS B NZ    1 
ATOM   4312 N N     . LYS B 2 181 ? 40.854 -5.291  61.046 1.00 32.95  ?  199 LYS B N     1 
ATOM   4313 C CA    . LYS B 2 181 ? 40.620 -4.159  60.155 1.00 31.68  ?  199 LYS B CA    1 
ATOM   4314 C C     . LYS B 2 181 ? 41.700 -4.115  59.078 1.00 38.07  ?  199 LYS B C     1 
ATOM   4315 O O     . LYS B 2 181 ? 42.831 -4.588  59.283 1.00 39.43  ?  199 LYS B O     1 
ATOM   4316 C CB    . LYS B 2 181 ? 40.621 -2.858  60.952 1.00 29.84  ?  199 LYS B CB    1 
ATOM   4317 C CG    . LYS B 2 181 ? 40.005 -1.644  60.266 1.00 27.88  ?  199 LYS B CG    1 
ATOM   4318 C CD    . LYS B 2 181 ? 40.247 -0.386  61.111 1.00 29.65  ?  199 LYS B CD    1 
ATOM   4319 C CE    . LYS B 2 181 ? 39.876 0.903   60.407 1.00 26.80  ?  199 LYS B CE    1 
ATOM   4320 N NZ    . LYS B 2 181 ? 39.556 1.972   61.399 1.00 28.54  ?  199 LYS B NZ    1 
ATOM   4321 N N     . ASP B 2 182 ? 41.351 -3.562  57.904 1.00 34.04  ?  200 ASP B N     1 
ATOM   4322 C CA    . ASP B 2 182 ? 42.306 -3.581  56.786 1.00 37.90  ?  200 ASP B CA    1 
ATOM   4323 C C     . ASP B 2 182 ? 42.211 -2.314  55.947 1.00 35.37  ?  200 ASP B C     1 
ATOM   4324 O O     . ASP B 2 182 ? 42.311 -2.356  54.719 1.00 35.18  ?  200 ASP B O     1 
ATOM   4325 C CB    . ASP B 2 182 ? 42.146 -4.846  55.927 1.00 40.59  ?  200 ASP B CB    1 
ATOM   4326 C CG    . ASP B 2 182 ? 40.743 -5.010  55.356 1.00 40.94  ?  200 ASP B CG    1 
ATOM   4327 O OD1   . ASP B 2 182 ? 39.946 -4.046  55.456 1.00 42.82  ?  200 ASP B OD1   1 
ATOM   4328 O OD2   . ASP B 2 182 ? 40.436 -6.123  54.847 1.00 39.73  -1 200 ASP B OD2   1 
ATOM   4329 N N     . ARG B 2 183 ? 42.062 -1.170  56.612 1.00 33.97  ?  201 ARG B N     1 
ATOM   4330 C CA    . ARG B 2 183 ? 42.192 0.124   55.961 1.00 33.41  ?  201 ARG B CA    1 
ATOM   4331 C C     . ARG B 2 183 ? 43.671 0.418   55.714 1.00 38.03  ?  201 ARG B C     1 
ATOM   4332 O O     . ARG B 2 183 ? 44.468 0.466   56.662 1.00 33.74  ?  201 ARG B O     1 
ATOM   4333 C CB    . ARG B 2 183 ? 41.558 1.210   56.820 1.00 28.85  ?  201 ARG B CB    1 
ATOM   4334 C CG    . ARG B 2 183 ? 41.810 2.592   56.300 1.00 29.13  ?  201 ARG B CG    1 
ATOM   4335 C CD    . ARG B 2 183 ? 41.080 3.633   57.110 1.00 28.20  ?  201 ARG B CD    1 
ATOM   4336 N NE    . ARG B 2 183 ? 41.246 4.934   56.491 1.00 32.35  ?  201 ARG B NE    1 
ATOM   4337 C CZ    . ARG B 2 183 ? 40.668 6.055   56.901 1.00 35.22  ?  201 ARG B CZ    1 
ATOM   4338 N NH1   . ARG B 2 183 ? 39.853 6.046   57.950 1.00 36.99  ?  201 ARG B NH1   1 
ATOM   4339 N NH2   . ARG B 2 183 ? 40.892 7.186   56.234 1.00 35.43  ?  201 ARG B NH2   1 
ATOM   4340 N N     . SER B 2 184 ? 44.040 0.618   54.445 1.00 39.38  ?  202 SER B N     1 
ATOM   4341 C CA    . SER B 2 184 ? 45.429 0.924   54.116 1.00 40.26  ?  202 SER B CA    1 
ATOM   4342 C C     . SER B 2 184 ? 45.834 2.283   54.680 1.00 41.11  ?  202 SER B C     1 
ATOM   4343 O O     . SER B 2 184 ? 45.043 3.233   54.691 1.00 41.33  ?  202 SER B O     1 
ATOM   4344 C CB    . SER B 2 184 ? 45.643 0.916   52.610 1.00 38.48  ?  202 SER B CB    1 
ATOM   4345 O OG    . SER B 2 184 ? 46.965 1.322   52.310 1.00 44.44  ?  202 SER B OG    1 
ATOM   4346 N N     . ARG B 2 185 ? 47.079 2.378   55.147 1.00 39.44  ?  203 ARG B N     1 
ATOM   4347 C CA    . ARG B 2 185 ? 47.561 3.618   55.736 1.00 37.62  ?  203 ARG B CA    1 
ATOM   4348 C C     . ARG B 2 185 ? 47.900 4.669   54.700 1.00 44.87  ?  203 ARG B C     1 
ATOM   4349 O O     . ARG B 2 185 ? 47.991 5.852   55.051 1.00 43.46  ?  203 ARG B O     1 
ATOM   4350 C CB    . ARG B 2 185 ? 48.817 3.383   56.557 1.00 35.71  ?  203 ARG B CB    1 
ATOM   4351 C CG    . ARG B 2 185 ? 48.627 2.664   57.824 1.00 36.81  ?  203 ARG B CG    1 
ATOM   4352 C CD    . ARG B 2 185 ? 49.979 2.273   58.381 1.00 40.94  ?  203 ARG B CD    1 
ATOM   4353 N NE    . ARG B 2 185 ? 49.843 1.757   59.739 1.00 46.04  ?  203 ARG B NE    1 
ATOM   4354 C CZ    . ARG B 2 185 ? 50.675 2.000   60.745 1.00 37.94  ?  203 ARG B CZ    1 
ATOM   4355 N NH1   . ARG B 2 185 ? 51.750 2.765   60.574 1.00 35.00  ?  203 ARG B NH1   1 
ATOM   4356 N NH2   . ARG B 2 185 ? 50.419 1.458   61.925 1.00 39.32  ?  203 ARG B NH2   1 
ATOM   4357 N N     . GLU B 2 186 ? 48.131 4.273   53.451 1.00 43.85  ?  204 GLU B N     1 
ATOM   4358 C CA    . GLU B 2 186 ? 48.713 5.209   52.504 1.00 49.27  ?  204 GLU B CA    1 
ATOM   4359 C C     . GLU B 2 186 ? 47.721 6.331   52.247 1.00 52.71  ?  204 GLU B C     1 
ATOM   4360 O O     . GLU B 2 186 ? 46.603 6.082   51.787 1.00 51.78  ?  204 GLU B O     1 
ATOM   4361 C CB    . GLU B 2 186 ? 49.113 4.501   51.214 1.00 49.62  ?  204 GLU B CB    1 
ATOM   4362 C CG    . GLU B 2 186 ? 47.973 3.960   50.409 1.00 54.68  ?  204 GLU B CG    1 
ATOM   4363 C CD    . GLU B 2 186 ? 48.412 3.460   49.034 1.00 59.92  ?  204 GLU B CD    1 
ATOM   4364 O OE1   . GLU B 2 186 ? 49.089 4.224   48.296 1.00 56.55  ?  204 GLU B OE1   1 
ATOM   4365 O OE2   . GLU B 2 186 ? 48.062 2.300   48.697 1.00 62.04  -1 204 GLU B OE2   1 
ATOM   4366 N N     . GLU B 2 187 ? 48.107 7.560   52.598 1.00 54.13  ?  205 GLU B N     1 
ATOM   4367 C CA    . GLU B 2 187 ? 47.203 8.685   52.415 1.00 52.49  ?  205 GLU B CA    1 
ATOM   4368 C C     . GLU B 2 187 ? 47.073 8.983   50.929 1.00 54.99  ?  205 GLU B C     1 
ATOM   4369 O O     . GLU B 2 187 ? 48.070 9.149   50.221 1.00 59.21  ?  205 GLU B O     1 
ATOM   4370 C CB    . GLU B 2 187 ? 47.682 9.907   53.192 1.00 48.39  ?  205 GLU B CB    1 
ATOM   4371 C CG    . GLU B 2 187 ? 48.104 9.605   54.632 1.00 56.35  ?  205 GLU B CG    1 
ATOM   4372 C CD    . GLU B 2 187 ? 46.979 9.065   55.548 1.00 63.89  ?  205 GLU B CD    1 
ATOM   4373 O OE1   . GLU B 2 187 ? 45.781 9.139   55.175 1.00 65.27  ?  205 GLU B OE1   1 
ATOM   4374 O OE2   . GLU B 2 187 ? 47.300 8.561   56.660 1.00 64.15  -1 205 GLU B OE2   1 
ATOM   4375 N N     . LEU B 2 188 ? 45.835 9.002   50.451 1.00 51.16  ?  206 LEU B N     1 
ATOM   4376 C CA    . LEU B 2 188 ? 45.562 9.064   49.032 1.00 48.75  ?  206 LEU B CA    1 
ATOM   4377 C C     . LEU B 2 188 ? 44.956 10.390  48.591 1.00 50.77  ?  206 LEU B C     1 
ATOM   4378 O O     . LEU B 2 188 ? 44.806 10.616  47.382 1.00 53.84  ?  206 LEU B O     1 
ATOM   4379 C CB    . LEU B 2 188 ? 44.619 7.916   48.642 1.00 50.12  ?  206 LEU B CB    1 
ATOM   4380 C CG    . LEU B 2 188 ? 45.237 6.558   48.342 1.00 46.40  ?  206 LEU B CG    1 
ATOM   4381 C CD1   . LEU B 2 188 ? 44.277 5.751   47.510 1.00 42.62  ?  206 LEU B CD1   1 
ATOM   4382 C CD2   . LEU B 2 188 ? 46.558 6.740   47.629 1.00 49.98  ?  206 LEU B CD2   1 
ATOM   4383 N N     . GLY B 2 189 ? 44.591 11.259  49.520 1.00 46.48  ?  207 GLY B N     1 
ATOM   4384 C CA    . GLY B 2 189 ? 44.013 12.522  49.129 1.00 44.50  ?  207 GLY B CA    1 
ATOM   4385 C C     . GLY B 2 189 ? 42.523 12.417  48.867 1.00 42.36  ?  207 GLY B C     1 
ATOM   4386 O O     . GLY B 2 189 ? 41.836 11.499  49.317 1.00 41.62  ?  207 GLY B O     1 
ATOM   4387 N N     . ASN B 2 190 ? 42.027 13.380  48.103 1.00 44.46  ?  208 ASN B N     1 
ATOM   4388 C CA    . ASN B 2 190 ? 40.601 13.602  47.937 1.00 39.22  ?  208 ASN B CA    1 
ATOM   4389 C C     . ASN B 2 190 ? 40.271 13.674  46.458 1.00 44.84  ?  208 ASN B C     1 
ATOM   4390 O O     . ASN B 2 190 ? 41.004 14.296  45.677 1.00 47.80  ?  208 ASN B O     1 
ATOM   4391 C CB    . ASN B 2 190 ? 40.190 14.891  48.618 1.00 40.60  ?  208 ASN B CB    1 
ATOM   4392 C CG    . ASN B 2 190 ? 39.996 14.716  50.090 1.00 42.64  ?  208 ASN B CG    1 
ATOM   4393 O OD1   . ASN B 2 190 ? 39.512 15.615  50.779 1.00 47.17  ?  208 ASN B OD1   1 
ATOM   4394 N ND2   . ASN B 2 190 ? 40.328 13.527  50.586 1.00 44.95  ?  208 ASN B ND2   1 
ATOM   4395 N N     . THR B 2 191 ? 39.170 13.020  46.085 1.00 40.73  ?  209 THR B N     1 
ATOM   4396 C CA    . THR B 2 191 ? 38.621 12.971  44.747 1.00 37.53  ?  209 THR B CA    1 
ATOM   4397 C C     . THR B 2 191 ? 37.223 13.593  44.742 1.00 34.30  ?  209 THR B C     1 
ATOM   4398 O O     . THR B 2 191 ? 36.474 13.422  45.709 1.00 30.64  ?  209 THR B O     1 
ATOM   4399 C CB    . THR B 2 191 ? 38.581 11.502  44.255 1.00 37.80  ?  209 THR B CB    1 
ATOM   4400 O OG1   . THR B 2 191 ? 38.127 11.429  42.894 1.00 42.09  ?  209 THR B OG1   1 
ATOM   4401 C CG2   . THR B 2 191 ? 37.685 10.656  45.140 1.00 35.46  ?  209 THR B CG2   1 
ATOM   4402 N N     . PRO B 2 192 ? 36.861 14.347  43.698 1.00 32.14  ?  210 PRO B N     1 
ATOM   4403 C CA    . PRO B 2 192 ? 35.530 14.966  43.639 1.00 32.88  ?  210 PRO B CA    1 
ATOM   4404 C C     . PRO B 2 192 ? 34.443 13.991  43.207 1.00 32.86  ?  210 PRO B C     1 
ATOM   4405 O O     . PRO B 2 192 ? 34.656 13.108  42.371 1.00 30.55  ?  210 PRO B O     1 
ATOM   4406 C CB    . PRO B 2 192 ? 35.695 16.073  42.591 1.00 30.18  ?  210 PRO B CB    1 
ATOM   4407 C CG    . PRO B 2 192 ? 37.109 16.057  42.188 1.00 32.96  ?  210 PRO B CG    1 
ATOM   4408 C CD    . PRO B 2 192 ? 37.680 14.733  42.547 1.00 31.87  ?  210 PRO B CD    1 
ATOM   4409 N N     . SER B 2 193 ? 33.252 14.178  43.778 1.00 28.99  ?  211 SER B N     1 
ATOM   4410 C CA    . SER B 2 193 ? 32.155 13.259  43.520 1.00 27.16  ?  211 SER B CA    1 
ATOM   4411 C C     . SER B 2 193 ? 30.807 13.983  43.590 1.00 32.20  ?  211 SER B C     1 
ATOM   4412 O O     . SER B 2 193 ? 30.640 14.968  44.322 1.00 34.58  ?  211 SER B O     1 
ATOM   4413 C CB    . SER B 2 193 ? 32.212 12.089  44.497 1.00 25.32  ?  211 SER B CB    1 
ATOM   4414 O OG    . SER B 2 193 ? 30.929 11.604  44.784 1.00 26.03  ?  211 SER B OG    1 
ATOM   4415 N N     . ALA B 2 194 ? 29.857 13.489  42.781 1.00 28.10  ?  212 ALA B N     1 
ATOM   4416 C CA    . ALA B 2 194 ? 28.465 13.908  42.774 1.00 25.61  ?  212 ALA B CA    1 
ATOM   4417 C C     . ALA B 2 194 ? 27.516 12.786  43.181 1.00 27.69  ?  212 ALA B C     1 
ATOM   4418 O O     . ALA B 2 194 ? 26.291 12.969  43.102 1.00 27.31  ?  212 ALA B O     1 
ATOM   4419 C CB    . ALA B 2 194 ? 28.064 14.428  41.380 1.00 23.30  ?  212 ALA B CB    1 
ATOM   4420 N N     . ASN B 2 195 ? 28.065 11.556  43.616 1.00 25.28  ?  213 ASN B N     1 
ATOM   4421 C CA    . ASN B 2 195 ? 27.130 10.568  44.159 1.00 29.26  ?  213 ASN B CA    1 
ATOM   4422 C C     . ASN B 2 195 ? 27.002 10.673  45.694 1.00 25.65  ?  213 ASN B C     1 
ATOM   4423 O O     . ASN B 2 195 ? 27.962 11.011  46.397 1.00 22.27  ?  213 ASN B O     1 
ATOM   4424 C CB    . ASN B 2 195 ? 27.561 9.145   43.775 1.00 27.65  ?  213 ASN B CB    1 
ATOM   4425 C CG    . ASN B 2 195 ? 27.444 8.878   42.303 1.00 23.46  ?  213 ASN B CG    1 
ATOM   4426 O OD1   . ASN B 2 195 ? 26.637 9.495   41.625 1.00 24.51  ?  213 ASN B OD1   1 
ATOM   4427 N ND2   . ASN B 2 195 ? 28.261 7.958   41.793 1.00 24.59  ?  213 ASN B ND2   1 
ATOM   4428 N N     . PRO B 2 196 ? 25.816 10.372  46.221 1.00 28.15  ?  214 PRO B N     1 
ATOM   4429 C CA    . PRO B 2 196 ? 25.575 10.460  47.667 1.00 27.38  ?  214 PRO B CA    1 
ATOM   4430 C C     . PRO B 2 196 ? 26.117 9.277   48.463 1.00 27.73  ?  214 PRO B C     1 
ATOM   4431 O O     . PRO B 2 196 ? 26.459 8.222   47.936 1.00 30.45  ?  214 PRO B O     1 
ATOM   4432 C CB    . PRO B 2 196 ? 24.049 10.488  47.751 1.00 24.63  ?  214 PRO B CB    1 
ATOM   4433 C CG    . PRO B 2 196 ? 23.597 9.769   46.577 1.00 25.98  ?  214 PRO B CG    1 
ATOM   4434 C CD    . PRO B 2 196 ? 24.565 10.152  45.480 1.00 29.45  ?  214 PRO B CD    1 
ATOM   4435 N N     . GLY B 2 197 ? 26.164 9.479   49.775 1.00 30.99  ?  215 GLY B N     1 
ATOM   4436 C CA    . GLY B 2 197 ? 26.343 8.401   50.733 1.00 27.91  ?  215 GLY B CA    1 
ATOM   4437 C C     . GLY B 2 197 ? 27.545 7.520   50.482 1.00 33.25  ?  215 GLY B C     1 
ATOM   4438 O O     . GLY B 2 197 ? 28.692 7.980   50.484 1.00 33.11  ?  215 GLY B O     1 
ATOM   4439 N N     . ILE B 2 198 ? 27.275 6.239   50.236 1.00 34.70  ?  216 ILE B N     1 
ATOM   4440 C CA    . ILE B 2 198 ? 28.299 5.214   50.174 1.00 29.71  ?  216 ILE B CA    1 
ATOM   4441 C C     . ILE B 2 198 ? 28.668 4.857   48.733 1.00 30.65  ?  216 ILE B C     1 
ATOM   4442 O O     . ILE B 2 198 ? 29.509 3.980   48.505 1.00 29.60  ?  216 ILE B O     1 
ATOM   4443 C CB    . ILE B 2 198 ? 27.811 4.022   51.001 1.00 31.79  ?  216 ILE B CB    1 
ATOM   4444 C CG1   . ILE B 2 198 ? 28.139 4.348   52.449 1.00 34.22  ?  216 ILE B CG1   1 
ATOM   4445 C CG2   . ILE B 2 198 ? 28.426 2.693   50.636 1.00 32.87  ?  216 ILE B CG2   1 
ATOM   4446 C CD1   . ILE B 2 198 ? 29.557 4.796   52.596 1.00 33.06  ?  216 ILE B CD1   1 
ATOM   4447 N N     . MET B 2 199 ? 28.110 5.576   47.754 1.00 32.08  ?  217 MET B N     1 
ATOM   4448 C CA    . MET B 2 199 ? 28.321 5.291   46.338 1.00 31.49  ?  217 MET B CA    1 
ATOM   4449 C C     . MET B 2 199 ? 29.747 5.646   45.921 1.00 30.83  ?  217 MET B C     1 
ATOM   4450 O O     . MET B 2 199 ? 30.449 6.407   46.595 1.00 36.17  ?  217 MET B O     1 
ATOM   4451 C CB    . MET B 2 199 ? 27.334 6.077   45.484 1.00 28.01  ?  217 MET B CB    1 
ATOM   4452 C CG    . MET B 2 199 ? 25.910 5.601   45.656 1.00 31.17  ?  217 MET B CG    1 
ATOM   4453 S SD    . MET B 2 199 ? 24.905 5.937   44.191 1.00 39.17  ?  217 MET B SD    1 
ATOM   4454 C CE    . MET B 2 199 ? 23.694 7.052   44.903 1.00 26.51  ?  217 MET B CE    1 
ATOM   4455 N N     . LYS B 2 200 ? 30.177 5.080   44.797 1.00 32.18  ?  218 LYS B N     1 
ATOM   4456 C CA    . LYS B 2 200 ? 31.523 5.390   44.303 1.00 30.85  ?  218 LYS B CA    1 
ATOM   4457 C C     . LYS B 2 200 ? 31.496 6.653   43.442 1.00 30.60  ?  218 LYS B C     1 
ATOM   4458 O O     . LYS B 2 200 ? 30.528 6.878   42.697 1.00 28.72  ?  218 LYS B O     1 
ATOM   4459 C CB    . LYS B 2 200 ? 32.085 4.223   43.493 1.00 27.32  ?  218 LYS B CB    1 
ATOM   4460 C CG    . LYS B 2 200 ? 32.875 3.232   44.330 1.00 26.85  ?  218 LYS B CG    1 
ATOM   4461 C CD    . LYS B 2 200 ? 32.944 1.853   43.701 1.00 30.38  ?  218 LYS B CD    1 
ATOM   4462 C CE    . LYS B 2 200 ? 34.273 1.575   43.017 1.00 30.63  ?  218 LYS B CE    1 
ATOM   4463 N NZ    . LYS B 2 200 ? 34.278 0.349   42.155 1.00 43.01  ?  218 LYS B NZ    1 
ATOM   4464 N N     . PRO B 2 201 ? 32.527 7.506   43.545 1.00 33.35  ?  219 PRO B N     1 
ATOM   4465 C CA    . PRO B 2 201 ? 32.543 8.717   42.707 1.00 29.01  ?  219 PRO B CA    1 
ATOM   4466 C C     . PRO B 2 201 ? 32.275 8.435   41.247 1.00 31.43  ?  219 PRO B C     1 
ATOM   4467 O O     . PRO B 2 201 ? 31.664 9.275   40.574 1.00 34.62  ?  219 PRO B O     1 
ATOM   4468 C CB    . PRO B 2 201 ? 33.946 9.281   42.929 1.00 29.17  ?  219 PRO B CB    1 
ATOM   4469 C CG    . PRO B 2 201 ? 34.342 8.786   44.269 1.00 24.88  ?  219 PRO B CG    1 
ATOM   4470 C CD    . PRO B 2 201 ? 33.674 7.461   44.475 1.00 27.00  ?  219 PRO B CD    1 
ATOM   4471 N N     . ASN B 2 202 ? 32.651 7.262   40.734 1.00 32.08  ?  220 ASN B N     1 
ATOM   4472 C CA    . ASN B 2 202 ? 32.602 7.032   39.294 1.00 28.39  ?  220 ASN B CA    1 
ATOM   4473 C C     . ASN B 2 202 ? 31.433 6.181   38.835 1.00 27.20  ?  220 ASN B C     1 
ATOM   4474 O O     . ASN B 2 202 ? 31.230 6.044   37.628 1.00 30.05  ?  220 ASN B O     1 
ATOM   4475 C CB    . ASN B 2 202 ? 33.909 6.393   38.826 1.00 31.16  ?  220 ASN B CB    1 
ATOM   4476 C CG    . ASN B 2 202 ? 35.020 7.396   38.732 1.00 32.90  ?  220 ASN B CG    1 
ATOM   4477 O OD1   . ASN B 2 202 ? 34.768 8.591   38.529 1.00 33.75  ?  220 ASN B OD1   1 
ATOM   4478 N ND2   . ASN B 2 202 ? 36.255 6.936   38.892 1.00 36.06  ?  220 ASN B ND2   1 
ATOM   4479 N N     . SER B 2 203 ? 30.648 5.626   39.742 1.00 28.90  ?  221 SER B N     1 
ATOM   4480 C CA    . SER B 2 203 ? 29.584 4.734   39.321 1.00 30.56  ?  221 SER B CA    1 
ATOM   4481 C C     . SER B 2 203 ? 28.413 5.516   38.710 1.00 33.75  ?  221 SER B C     1 
ATOM   4482 O O     . SER B 2 203 ? 28.142 6.666   39.094 1.00 28.69  ?  221 SER B O     1 
ATOM   4483 C CB    . SER B 2 203 ? 29.096 3.903   40.497 1.00 31.23  ?  221 SER B CB    1 
ATOM   4484 O OG    . SER B 2 203 ? 30.185 3.461   41.281 1.00 32.67  ?  221 SER B OG    1 
ATOM   4485 N N     . PRO B 2 204 ? 27.700 4.909   37.751 1.00 34.12  ?  222 PRO B N     1 
ATOM   4486 C CA    . PRO B 2 204 ? 26.475 5.525   37.235 1.00 26.65  ?  222 PRO B CA    1 
ATOM   4487 C C     . PRO B 2 204 ? 25.500 5.789   38.366 1.00 28.23  ?  222 PRO B C     1 
ATOM   4488 O O     . PRO B 2 204 ? 25.553 5.175   39.429 1.00 27.54  ?  222 PRO B O     1 
ATOM   4489 C CB    . PRO B 2 204 ? 25.934 4.473   36.268 1.00 30.61  ?  222 PRO B CB    1 
ATOM   4490 C CG    . PRO B 2 204 ? 27.125 3.686   35.870 1.00 29.84  ?  222 PRO B CG    1 
ATOM   4491 C CD    . PRO B 2 204 ? 27.998 3.630   37.079 1.00 29.46  ?  222 PRO B CD    1 
ATOM   4492 N N     . ASN B 2 205 ? 24.594 6.722   38.129 1.00 30.82  ?  223 ASN B N     1 
ATOM   4493 C CA    . ASN B 2 205 ? 23.622 7.059   39.157 1.00 31.61  ?  223 ASN B CA    1 
ATOM   4494 C C     . ASN B 2 205 ? 22.398 7.678   38.487 1.00 30.23  ?  223 ASN B C     1 
ATOM   4495 O O     . ASN B 2 205 ? 22.512 8.374   37.474 1.00 28.96  ?  223 ASN B O     1 
ATOM   4496 C CB    . ASN B 2 205 ? 24.247 8.004   40.212 1.00 30.61  ?  223 ASN B CB    1 
ATOM   4497 C CG    . ASN B 2 205 ? 23.342 8.223   41.436 1.00 28.46  ?  223 ASN B CG    1 
ATOM   4498 O OD1   . ASN B 2 205 ? 22.441 7.443   41.689 1.00 29.61  ?  223 ASN B OD1   1 
ATOM   4499 N ND2   . ASN B 2 205 ? 23.586 9.289   42.181 1.00 25.82  ?  223 ASN B ND2   1 
ATOM   4500 N N     . PHE B 2 206 ? 21.226 7.392   39.047 1.00 32.24  ?  224 PHE B N     1 
ATOM   4501 C CA    . PHE B 2 206 ? 20.006 8.055   38.600 1.00 33.87  ?  224 PHE B CA    1 
ATOM   4502 C C     . PHE B 2 206 ? 20.188 9.556   38.658 1.00 32.49  ?  224 PHE B C     1 
ATOM   4503 O O     . PHE B 2 206 ? 20.707 10.092  39.637 1.00 33.16  ?  224 PHE B O     1 
ATOM   4504 C CB    . PHE B 2 206 ? 18.833 7.660   39.484 1.00 33.15  ?  224 PHE B CB    1 
ATOM   4505 C CG    . PHE B 2 206 ? 18.592 6.194   39.540 1.00 35.44  ?  224 PHE B CG    1 
ATOM   4506 C CD1   . PHE B 2 206 ? 18.620 5.427   38.387 1.00 32.66  ?  224 PHE B CD1   1 
ATOM   4507 C CD2   . PHE B 2 206 ? 18.303 5.580   40.745 1.00 33.37  ?  224 PHE B CD2   1 
ATOM   4508 C CE1   . PHE B 2 206 ? 18.381 4.082   38.442 1.00 33.10  ?  224 PHE B CE1   1 
ATOM   4509 C CE2   . PHE B 2 206 ? 18.055 4.232   40.794 1.00 33.48  ?  224 PHE B CE2   1 
ATOM   4510 C CZ    . PHE B 2 206 ? 18.102 3.483   39.638 1.00 33.55  ?  224 PHE B CZ    1 
ATOM   4511 N N     . THR B 2 207 ? 19.725 10.244  37.629 1.00 35.23  ?  225 THR B N     1 
ATOM   4512 C CA    . THR B 2 207 ? 20.005 11.672  37.541 1.00 36.42  ?  225 THR B CA    1 
ATOM   4513 C C     . THR B 2 207 ? 19.124 12.528  38.438 1.00 37.13  ?  225 THR B C     1 
ATOM   4514 O O     . THR B 2 207 ? 19.227 13.753  38.359 1.00 46.02  ?  225 THR B O     1 
ATOM   4515 C CB    . THR B 2 207 ? 19.860 12.139  36.102 1.00 38.35  ?  225 THR B CB    1 
ATOM   4516 O OG1   . THR B 2 207 ? 18.633 11.618  35.567 1.00 43.75  ?  225 THR B OG1   1 
ATOM   4517 C CG2   . THR B 2 207 ? 21.028 11.615  35.262 1.00 38.98  ?  225 THR B CG2   1 
ATOM   4518 N N     . ASP B 2 208 ? 18.249 11.929  39.252 1.00 35.30  ?  226 ASP B N     1 
ATOM   4519 C CA    . ASP B 2 208 ? 17.527 12.626  40.314 1.00 40.17  ?  226 ASP B CA    1 
ATOM   4520 C C     . ASP B 2 208 ? 18.121 12.336  41.685 1.00 41.05  ?  226 ASP B C     1 
ATOM   4521 O O     . ASP B 2 208 ? 17.744 12.983  42.675 1.00 39.15  ?  226 ASP B O     1 
ATOM   4522 C CB    . ASP B 2 208 ? 16.031 12.253  40.295 1.00 38.26  ?  226 ASP B CB    1 
ATOM   4523 C CG    . ASP B 2 208 ? 15.764 10.803  40.692 1.00 44.00  ?  226 ASP B CG    1 
ATOM   4524 O OD1   . ASP B 2 208 ? 14.720 10.233  40.277 1.00 49.61  ?  226 ASP B OD1   1 
ATOM   4525 O OD2   . ASP B 2 208 ? 16.584 10.224  41.433 1.00 46.85  -1 226 ASP B OD2   1 
ATOM   4526 N N     . ASN B 2 209 ? 19.052 11.382  41.734 1.00 40.50  ?  227 ASN B N     1 
ATOM   4527 C CA    . ASN B 2 209 ? 19.782 10.936  42.909 1.00 33.20  ?  227 ASN B CA    1 
ATOM   4528 C C     . ASN B 2 209 ? 21.172 11.562  43.002 1.00 27.40  ?  227 ASN B C     1 
ATOM   4529 O O     . ASN B 2 209 ? 21.996 11.108  43.788 1.00 24.74  ?  227 ASN B O     1 
ATOM   4530 C CB    . ASN B 2 209 ? 19.890 9.412   42.874 1.00 28.68  ?  227 ASN B CB    1 
ATOM   4531 C CG    . ASN B 2 209 ? 20.155 8.824   44.224 1.00 29.86  ?  227 ASN B CG    1 
ATOM   4532 O OD1   . ASN B 2 209 ? 21.008 7.944   44.376 1.00 27.40  ?  227 ASN B OD1   1 
ATOM   4533 N ND2   . ASN B 2 209 ? 19.429 9.308   45.230 1.00 33.46  ?  227 ASN B ND2   1 
ATOM   4534 N N     . LEU B 2 210 ? 21.455 12.580  42.206 1.00 31.08  ?  228 LEU B N     1 
ATOM   4535 C CA    . LEU B 2 210 ? 22.717 13.272  42.358 1.00 29.60  ?  228 LEU B CA    1 
ATOM   4536 C C     . LEU B 2 210 ? 22.690 14.216  43.564 1.00 31.87  ?  228 LEU B C     1 
ATOM   4537 O O     . LEU B 2 210 ? 21.637 14.577  44.107 1.00 32.45  ?  228 LEU B O     1 
ATOM   4538 C CB    . LEU B 2 210 ? 23.051 14.052  41.095 1.00 31.26  ?  228 LEU B CB    1 
ATOM   4539 C CG    . LEU B 2 210 ? 23.370 13.240  39.843 1.00 32.02  ?  228 LEU B CG    1 
ATOM   4540 C CD1   . LEU B 2 210 ? 24.178 14.103  38.892 1.00 27.86  ?  228 LEU B CD1   1 
ATOM   4541 C CD2   . LEU B 2 210 ? 24.122 11.971  40.198 1.00 27.93  ?  228 LEU B CD2   1 
ATOM   4542 N N     . VAL B 2 211 ? 23.888 14.613  43.968 1.00 30.70  ?  229 VAL B N     1 
ATOM   4543 C CA    . VAL B 2 211 ? 24.135 15.534  45.071 1.00 34.58  ?  229 VAL B CA    1 
ATOM   4544 C C     . VAL B 2 211 ? 25.196 16.528  44.613 1.00 36.68  ?  229 VAL B C     1 
ATOM   4545 O O     . VAL B 2 211 ? 25.932 16.254  43.642 1.00 38.36  ?  229 VAL B O     1 
ATOM   4546 C CB    . VAL B 2 211 ? 24.575 14.754  46.336 1.00 32.07  ?  229 VAL B CB    1 
ATOM   4547 C CG1   . VAL B 2 211 ? 26.036 14.344  46.253 1.00 30.41  ?  229 VAL B CG1   1 
ATOM   4548 C CG2   . VAL B 2 211 ? 24.224 15.477  47.618 1.00 29.02  ?  229 VAL B CG2   1 
ATOM   4549 N N     . PRO B 2 212 ? 25.245 17.738  45.188 1.00 36.71  ?  230 PRO B N     1 
ATOM   4550 C CA    . PRO B 2 212 ? 26.178 18.765  44.671 1.00 31.68  ?  230 PRO B CA    1 
ATOM   4551 C C     . PRO B 2 212 ? 27.635 18.320  44.770 1.00 33.74  ?  230 PRO B C     1 
ATOM   4552 O O     . PRO B 2 212 ? 28.023 17.591  45.683 1.00 35.76  ?  230 PRO B O     1 
ATOM   4553 C CB    . PRO B 2 212 ? 25.910 19.985  45.555 1.00 26.73  ?  230 PRO B CB    1 
ATOM   4554 C CG    . PRO B 2 212 ? 25.092 19.473  46.718 1.00 31.14  ?  230 PRO B CG    1 
ATOM   4555 C CD    . PRO B 2 212 ? 24.360 18.267  46.246 1.00 30.81  ?  230 PRO B CD    1 
ATOM   4556 N N     . VAL B 2 213 ? 28.456 18.768  43.820 1.00 35.27  ?  231 VAL B N     1 
ATOM   4557 C CA    . VAL B 2 213 ? 29.810 18.223  43.691 1.00 34.52  ?  231 VAL B CA    1 
ATOM   4558 C C     . VAL B 2 213 ? 30.665 18.666  44.872 1.00 33.66  ?  231 VAL B C     1 
ATOM   4559 O O     . VAL B 2 213 ? 30.664 19.842  45.254 1.00 38.47  ?  231 VAL B O     1 
ATOM   4560 C CB    . VAL B 2 213 ? 30.437 18.646  42.347 1.00 35.81  ?  231 VAL B CB    1 
ATOM   4561 C CG1   . VAL B 2 213 ? 31.870 18.107  42.192 1.00 29.10  ?  231 VAL B CG1   1 
ATOM   4562 C CG2   . VAL B 2 213 ? 29.568 18.180  41.184 1.00 27.14  ?  231 VAL B CG2   1 
ATOM   4563 N N     . ARG B 2 214 ? 31.407 17.728  45.458 1.00 34.25  ?  232 ARG B N     1 
ATOM   4564 C CA    . ARG B 2 214 ? 32.353 18.061  46.526 1.00 36.91  ?  232 ARG B CA    1 
ATOM   4565 C C     . ARG B 2 214 ? 33.391 16.947  46.645 1.00 41.32  ?  232 ARG B C     1 
ATOM   4566 O O     . ARG B 2 214 ? 33.218 15.844  46.108 1.00 40.68  ?  232 ARG B O     1 
ATOM   4567 C CB    . ARG B 2 214 ? 31.647 18.272  47.863 1.00 33.41  ?  232 ARG B CB    1 
ATOM   4568 C CG    . ARG B 2 214 ? 31.298 16.979  48.588 1.00 30.99  ?  232 ARG B CG    1 
ATOM   4569 C CD    . ARG B 2 214 ? 30.366 16.104  47.764 1.00 30.41  ?  232 ARG B CD    1 
ATOM   4570 N NE    . ARG B 2 214 ? 29.845 14.957  48.519 1.00 31.71  ?  232 ARG B NE    1 
ATOM   4571 C CZ    . ARG B 2 214 ? 29.553 13.762  47.998 1.00 29.35  ?  232 ARG B CZ    1 
ATOM   4572 N NH1   . ARG B 2 214 ? 29.732 13.521  46.701 1.00 29.77  ?  232 ARG B NH1   1 
ATOM   4573 N NH2   . ARG B 2 214 ? 29.064 12.804  48.769 1.00 24.58  ?  232 ARG B NH2   1 
ATOM   4574 N N     . ASP B 2 215 ? 34.473 17.236  47.367 1.00 38.37  ?  233 ASP B N     1 
ATOM   4575 C CA    . ASP B 2 215 ? 35.541 16.254  47.517 1.00 36.73  ?  233 ASP B CA    1 
ATOM   4576 C C     . ASP B 2 215 ? 35.177 15.202  48.565 1.00 34.11  ?  233 ASP B C     1 
ATOM   4577 O O     . ASP B 2 215 ? 34.480 15.488  49.538 1.00 35.05  ?  233 ASP B O     1 
ATOM   4578 C CB    . ASP B 2 215 ? 36.850 16.950  47.895 1.00 40.10  ?  233 ASP B CB    1 
ATOM   4579 C CG    . ASP B 2 215 ? 37.288 17.952  46.851 1.00 47.71  ?  233 ASP B CG    1 
ATOM   4580 O OD1   . ASP B 2 215 ? 37.203 17.612  45.649 1.00 46.57  ?  233 ASP B OD1   1 
ATOM   4581 O OD2   . ASP B 2 215 ? 37.707 19.078  47.224 1.00 58.21  -1 233 ASP B OD2   1 
ATOM   4582 N N     . VAL B 2 216 ? 35.646 13.974  48.351 1.00 32.04  ?  234 VAL B N     1 
ATOM   4583 C CA    . VAL B 2 216 ? 35.470 12.885  49.314 1.00 29.70  ?  234 VAL B CA    1 
ATOM   4584 C C     . VAL B 2 216 ? 36.752 12.071  49.389 1.00 30.85  ?  234 VAL B C     1 
ATOM   4585 O O     . VAL B 2 216 ? 37.610 12.147  48.506 1.00 33.23  ?  234 VAL B O     1 
ATOM   4586 C CB    . VAL B 2 216 ? 34.287 11.970  48.956 1.00 27.63  ?  234 VAL B CB    1 
ATOM   4587 C CG1   . VAL B 2 216 ? 33.089 12.806  48.607 1.00 28.22  ?  234 VAL B CG1   1 
ATOM   4588 C CG2   . VAL B 2 216 ? 34.649 11.075  47.792 1.00 29.10  ?  234 VAL B CG2   1 
ATOM   4589 N N     . PRO B 2 217 ? 36.913 11.299  50.463 1.00 33.63  ?  235 PRO B N     1 
ATOM   4590 C CA    . PRO B 2 217 ? 38.164 10.547  50.650 1.00 30.42  ?  235 PRO B CA    1 
ATOM   4591 C C     . PRO B 2 217 ? 38.240 9.313   49.766 1.00 34.10  ?  235 PRO B C     1 
ATOM   4592 O O     . PRO B 2 217 ? 37.269 8.563   49.633 1.00 31.83  ?  235 PRO B O     1 
ATOM   4593 C CB    . PRO B 2 217 ? 38.119 10.140  52.131 1.00 26.00  ?  235 PRO B CB    1 
ATOM   4594 C CG    . PRO B 2 217 ? 37.032 10.975  52.755 1.00 25.90  ?  235 PRO B CG    1 
ATOM   4595 C CD    . PRO B 2 217 ? 36.054 11.261  51.657 1.00 28.44  ?  235 PRO B CD    1 
ATOM   4596 N N     . LYS B 2 218 ? 39.412 9.126   49.141 1.00 35.83  ?  236 LYS B N     1 
ATOM   4597 C CA    . LYS B 2 218 ? 39.832 7.824   48.640 1.00 32.93  ?  236 LYS B CA    1 
ATOM   4598 C C     . LYS B 2 218 ? 40.496 7.052   49.775 1.00 36.72  ?  236 LYS B C     1 
ATOM   4599 O O     . LYS B 2 218 ? 41.408 7.566   50.440 1.00 36.20  ?  236 LYS B O     1 
ATOM   4600 C CB    . LYS B 2 218 ? 40.834 7.961   47.487 1.00 42.09  ?  236 LYS B CB    1 
ATOM   4601 C CG    . LYS B 2 218 ? 40.458 8.887   46.349 1.00 46.59  ?  236 LYS B CG    1 
ATOM   4602 C CD    . LYS B 2 218 ? 41.316 8.587   45.122 1.00 51.35  ?  236 LYS B CD    1 
ATOM   4603 C CE    . LYS B 2 218 ? 41.389 7.083   44.888 1.00 50.20  ?  236 LYS B CE    1 
ATOM   4604 N NZ    . LYS B 2 218 ? 42.333 6.756   43.788 1.00 52.46  ?  236 LYS B NZ    1 
ATOM   4605 N N     . ILE B 2 219 ? 40.052 5.821   49.990 1.00 30.25  ?  237 ILE B N     1 
ATOM   4606 C CA    . ILE B 2 219 ? 40.676 4.925   50.948 1.00 30.36  ?  237 ILE B CA    1 
ATOM   4607 C C     . ILE B 2 219 ? 40.909 3.610   50.231 1.00 36.05  ?  237 ILE B C     1 
ATOM   4608 O O     . ILE B 2 219 ? 40.096 3.197   49.393 1.00 39.57  ?  237 ILE B O     1 
ATOM   4609 C CB    . ILE B 2 219 ? 39.807 4.744   52.214 1.00 33.22  ?  237 ILE B CB    1 
ATOM   4610 C CG1   . ILE B 2 219 ? 39.374 6.099   52.764 1.00 30.12  ?  237 ILE B CG1   1 
ATOM   4611 C CG2   . ILE B 2 219 ? 40.534 4.007   53.325 1.00 30.77  ?  237 ILE B CG2   1 
ATOM   4612 C CD1   . ILE B 2 219 ? 38.250 5.984   53.722 1.00 28.29  ?  237 ILE B CD1   1 
ATOM   4613 N N     . ALA B 2 220 ? 42.042 2.978   50.520 1.00 37.84  ?  238 ALA B N     1 
ATOM   4614 C CA    . ALA B 2 220 ? 42.427 1.711   49.917 1.00 32.33  ?  238 ALA B CA    1 
ATOM   4615 C C     . ALA B 2 220 ? 42.341 0.586   50.942 1.00 41.09  ?  238 ALA B C     1 
ATOM   4616 O O     . ALA B 2 220 ? 42.431 0.817   52.162 1.00 39.12  ?  238 ALA B O     1 
ATOM   4617 C CB    . ALA B 2 220 ? 43.843 1.780   49.359 1.00 35.98  ?  238 ALA B CB    1 
ATOM   4618 N N     . ILE B 2 221 ? 42.261 -0.651  50.439 1.00 37.06  ?  239 ILE B N     1 
ATOM   4619 C CA    . ILE B 2 221 ? 42.305 -1.851  51.325 1.00 40.28  ?  239 ILE B CA    1 
ATOM   4620 C C     . ILE B 2 221 ? 43.763 -2.319  51.340 1.00 40.96  ?  239 ILE B C     1 
ATOM   4621 O O     . ILE B 2 221 ? 44.410 -2.196  50.306 1.00 43.09  ?  239 ILE B O     1 
ATOM   4622 C CB    . ILE B 2 221 ? 41.365 -2.957  50.801 1.00 38.70  ?  239 ILE B CB    1 
ATOM   4623 C CG1   . ILE B 2 221 ? 40.107 -2.398  50.136 1.00 34.39  ?  239 ILE B CG1   1 
ATOM   4624 C CG2   . ILE B 2 221 ? 41.044 -3.982  51.870 1.00 31.70  ?  239 ILE B CG2   1 
ATOM   4625 C CD1   . ILE B 2 221 ? 39.123 -3.461  49.727 1.00 36.04  ?  239 ILE B CD1   1 
ATOM   4626 N N     . ASN B 2 222 ? 44.249 -2.827  52.472 1.00 43.03  ?  240 ASN B N     1 
ATOM   4627 C CA    . ASN B 2 222 ? 45.637 -3.348  52.561 1.00 43.04  ?  240 ASN B CA    1 
ATOM   4628 C C     . ASN B 2 222 ? 45.732 -4.665  51.796 1.00 46.04  ?  240 ASN B C     1 
ATOM   4629 O O     . ASN B 2 222 ? 46.772 -4.858  51.148 1.00 54.85  ?  240 ASN B O     1 
ATOM   4630 C CB    . ASN B 2 222 ? 46.157 -3.451  53.994 1.00 41.67  ?  240 ASN B CB    1 
ATOM   4631 C CG    . ASN B 2 222 ? 47.659 -3.611  54.054 1.00 45.28  ?  240 ASN B CG    1 
ATOM   4632 O OD1   . ASN B 2 222 ? 48.391 -2.866  53.410 1.00 52.68  ?  240 ASN B OD1   1 
ATOM   4633 N ND2   . ASN B 2 222 ? 48.126 -4.584  54.815 1.00 50.95  ?  240 ASN B ND2   1 
ATOM   4634 N N     . GLU B 2 223 ? 44.743 -5.550  51.919 1.00 44.44  ?  241 GLU B N     1 
ATOM   4635 C CA    . GLU B 2 223 ? 44.688 -6.816  51.127 1.00 46.61  ?  241 GLU B CA    1 
ATOM   4636 C C     . GLU B 2 223 ? 45.737 -7.834  51.573 1.00 41.70  ?  241 GLU B C     1 
ATOM   4637 O O     . GLU B 2 223 ? 45.623 -8.995  51.184 1.00 37.71  ?  241 GLU B O     1 
ATOM   4638 C CB    . GLU B 2 223 ? 44.755 -6.544  49.627 1.00 49.36  ?  241 GLU B CB    1 
ATOM   4639 C CG    . GLU B 2 223 ? 43.607 -7.163  48.859 1.00 59.81  ?  241 GLU B CG    1 
ATOM   4640 C CD    . GLU B 2 223 ? 42.522 -6.167  48.501 1.00 71.26  ?  241 GLU B CD    1 
ATOM   4641 O OE1   . GLU B 2 223 ? 41.375 -6.597  48.265 1.00 72.95  ?  241 GLU B OE1   1 
ATOM   4642 O OE2   . GLU B 2 223 ? 42.834 -4.963  48.461 1.00 64.90  -1 241 GLU B OE2   1 
ATOM   4643 N N     . LYS B 2 224 ? 46.715 -7.401  52.354 1.00 41.13  ?  242 LYS B N     1 
ATOM   4644 C CA    . LYS B 2 224 ? 47.773 -8.299  52.845 1.00 40.98  ?  242 LYS B CA    1 
ATOM   4645 C C     . LYS B 2 224 ? 47.476 -8.602  54.312 1.00 43.46  ?  242 LYS B C     1 
ATOM   4646 O O     . LYS B 2 224 ? 48.326 -9.201  54.972 1.00 44.05  ?  242 LYS B O     1 
ATOM   4647 C CB    . LYS B 2 224 ? 49.132 -7.633  52.636 1.00 41.13  ?  242 LYS B CB    1 
ATOM   4648 C CG    . LYS B 2 224 ? 49.524 -7.351  51.195 1.00 41.38  ?  242 LYS B CG    1 
ATOM   4649 C CD    . LYS B 2 224 ? 50.611 -6.309  51.093 1.00 45.36  ?  242 LYS B CD    1 
ATOM   4650 C CE    . LYS B 2 224 ? 50.941 -5.680  52.430 1.00 55.75  ?  242 LYS B CE    1 
ATOM   4651 N NZ    . LYS B 2 224 ? 51.084 -4.208  52.331 1.00 55.17  ?  242 LYS B NZ    1 
ATOM   4652 N N     . VAL B 2 225 ? 46.297 -8.201  54.790 1.00 41.42  ?  243 VAL B N     1 
ATOM   4653 C CA    . VAL B 2 225 ? 45.959 -8.435  56.219 1.00 39.13  ?  243 VAL B CA    1 
ATOM   4654 C C     . VAL B 2 225 ? 45.389 -9.842  56.330 1.00 43.28  ?  243 VAL B C     1 
ATOM   4655 O O     . VAL B 2 225 ? 44.430 -10.131 55.625 1.00 44.87  ?  243 VAL B O     1 
ATOM   4656 C CB    . VAL B 2 225 ? 45.018 -7.359  56.788 1.00 36.33  ?  243 VAL B CB    1 
ATOM   4657 C CG1   . VAL B 2 225 ? 44.524 -7.703  58.183 1.00 34.78  ?  243 VAL B CG1   1 
ATOM   4658 C CG2   . VAL B 2 225 ? 45.680 -5.995  56.791 1.00 32.80  ?  243 VAL B CG2   1 
ATOM   4659 N N     . ALA B 2 226 ? 45.981 -10.677 57.183 1.00 48.16  ?  244 ALA B N     1 
ATOM   4660 C CA    . ALA B 2 226 ? 45.522 -12.056 57.349 1.00 48.55  ?  244 ALA B CA    1 
ATOM   4661 C C     . ALA B 2 226 ? 44.232 -12.068 58.154 1.00 43.92  ?  244 ALA B C     1 
ATOM   4662 O O     . ALA B 2 226 ? 44.200 -11.575 59.285 1.00 42.75  ?  244 ALA B O     1 
ATOM   4663 C CB    . ALA B 2 226 ? 46.579 -12.913 58.033 1.00 45.56  ?  244 ALA B CB    1 
ATOM   4664 N N     . GLY B 2 227 ? 43.178 -12.645 57.578 1.00 38.40  ?  245 GLY B N     1 
ATOM   4665 C CA    . GLY B 2 227 ? 41.868 -12.595 58.191 1.00 39.93  ?  245 GLY B CA    1 
ATOM   4666 C C     . GLY B 2 227 ? 41.168 -11.258 58.083 1.00 43.13  ?  245 GLY B C     1 
ATOM   4667 O O     . GLY B 2 227 ? 40.155 -11.050 58.758 1.00 40.17  ?  245 GLY B O     1 
ATOM   4668 N N     . GLY B 2 228 ? 41.683 -10.347 57.255 1.00 42.54  ?  246 GLY B N     1 
ATOM   4669 C CA    . GLY B 2 228 ? 41.141 -9.010  57.121 1.00 39.89  ?  246 GLY B CA    1 
ATOM   4670 C C     . GLY B 2 228 ? 39.648 -8.990  56.887 1.00 41.46  ?  246 GLY B C     1 
ATOM   4671 O O     . GLY B 2 228 ? 39.091 -9.942  56.339 1.00 40.29  ?  246 GLY B O     1 
ATOM   4672 N N     . TYR B 2 229 ? 38.987 -7.901  57.286 1.00 41.21  ?  247 TYR B N     1 
ATOM   4673 C CA    . TYR B 2 229 ? 37.529 -7.879  57.288 1.00 37.75  ?  247 TYR B CA    1 
ATOM   4674 C C     . TYR B 2 229 ? 36.978 -7.982  55.871 1.00 40.37  ?  247 TYR B C     1 
ATOM   4675 O O     . TYR B 2 229 ? 35.996 -8.692  55.620 1.00 39.28  ?  247 TYR B O     1 
ATOM   4676 C CB    . TYR B 2 229 ? 37.050 -6.606  57.997 1.00 38.51  ?  247 TYR B CB    1 
ATOM   4677 C CG    . TYR B 2 229 ? 35.550 -6.484  58.111 1.00 38.91  ?  247 TYR B CG    1 
ATOM   4678 C CD1   . TYR B 2 229 ? 34.819 -7.339  58.928 1.00 34.17  ?  247 TYR B CD1   1 
ATOM   4679 C CD2   . TYR B 2 229 ? 34.860 -5.520  57.379 1.00 39.46  ?  247 TYR B CD2   1 
ATOM   4680 C CE1   . TYR B 2 229 ? 33.452 -7.244  59.014 1.00 34.71  ?  247 TYR B CE1   1 
ATOM   4681 C CE2   . TYR B 2 229 ? 33.482 -5.413  57.458 1.00 38.23  ?  247 TYR B CE2   1 
ATOM   4682 C CZ    . TYR B 2 229 ? 32.782 -6.280  58.279 1.00 37.95  ?  247 TYR B CZ    1 
ATOM   4683 O OH    . TYR B 2 229 ? 31.410 -6.183  58.360 1.00 37.24  ?  247 TYR B OH    1 
ATOM   4684 N N     . SER B 2 230 ? 37.619 -7.293  54.926 1.00 40.57  ?  248 SER B N     1 
ATOM   4685 C CA    . SER B 2 230 ? 37.237 -7.356  53.522 1.00 36.21  ?  248 SER B CA    1 
ATOM   4686 C C     . SER B 2 230 ? 37.183 -8.787  53.013 1.00 41.29  ?  248 SER B C     1 
ATOM   4687 O O     . SER B 2 230 ? 36.380 -9.109  52.125 1.00 41.73  ?  248 SER B O     1 
ATOM   4688 C CB    . SER B 2 230 ? 38.259 -6.582  52.707 1.00 41.01  ?  248 SER B CB    1 
ATOM   4689 O OG    . SER B 2 230 ? 38.021 -5.198  52.813 1.00 48.32  ?  248 SER B OG    1 
ATOM   4690 N N     . LYS B 2 231 ? 38.079 -9.640  53.523 1.00 39.82  ?  249 LYS B N     1 
ATOM   4691 C CA    . LYS B 2 231 ? 38.194 -11.021 53.080 1.00 37.05  ?  249 LYS B CA    1 
ATOM   4692 C C     . LYS B 2 231 ? 37.094 -11.892 53.674 1.00 39.53  ?  249 LYS B C     1 
ATOM   4693 O O     . LYS B 2 231 ? 36.548 -12.759 52.976 1.00 35.47  ?  249 LYS B O     1 
ATOM   4694 C CB    . LYS B 2 231 ? 39.560 -11.583 53.465 1.00 38.23  ?  249 LYS B CB    1 
ATOM   4695 C CG    . LYS B 2 231 ? 40.762 -10.924 52.835 1.00 38.28  ?  249 LYS B CG    1 
ATOM   4696 C CD    . LYS B 2 231 ? 42.019 -11.412 53.550 1.00 42.02  ?  249 LYS B CD    1 
ATOM   4697 C CE    . LYS B 2 231 ? 43.185 -11.549 52.595 1.00 42.45  ?  249 LYS B CE    1 
ATOM   4698 N NZ    . LYS B 2 231 ? 44.236 -10.572 52.940 1.00 43.68  ?  249 LYS B NZ    1 
ATOM   4699 N N     . THR B 2 232 ? 36.748 -11.663 54.956 1.00 34.83  ?  250 THR B N     1 
ATOM   4700 C CA    . THR B 2 232 ? 35.813 -12.524 55.667 1.00 34.75  ?  250 THR B CA    1 
ATOM   4701 C C     . THR B 2 232 ? 34.363 -12.143 55.455 1.00 38.76  ?  250 THR B C     1 
ATOM   4702 O O     . THR B 2 232 ? 33.480 -12.951 55.772 1.00 43.35  ?  250 THR B O     1 
ATOM   4703 C CB    . THR B 2 232 ? 36.065 -12.521 57.186 1.00 36.38  ?  250 THR B CB    1 
ATOM   4704 O OG1   . THR B 2 232 ? 35.729 -11.239 57.726 1.00 40.16  ?  250 THR B OG1   1 
ATOM   4705 C CG2   . THR B 2 232 ? 37.508 -12.893 57.542 1.00 29.14  ?  250 THR B CG2   1 
ATOM   4706 N N     . LYS B 2 233 ? 34.094 -10.930 54.973 1.00 37.65  ?  251 LYS B N     1 
ATOM   4707 C CA    . LYS B 2 233 ? 32.729 -10.445 54.767 1.00 38.22  ?  251 LYS B CA    1 
ATOM   4708 C C     . LYS B 2 233 ? 32.680 -9.654  53.469 1.00 38.65  ?  251 LYS B C     1 
ATOM   4709 O O     . LYS B 2 233 ? 32.398 -8.453  53.451 1.00 38.09  ?  251 LYS B O     1 
ATOM   4710 C CB    . LYS B 2 233 ? 32.247 -9.611  55.958 1.00 36.39  ?  251 LYS B CB    1 
ATOM   4711 C CG    . LYS B 2 233 ? 30.719 -9.490  55.999 1.00 36.51  ?  251 LYS B CG    1 
ATOM   4712 C CD    . LYS B 2 233 ? 30.193 -9.151  57.374 1.00 41.22  ?  251 LYS B CD    1 
ATOM   4713 C CE    . LYS B 2 233 ? 28.659 -8.985  57.394 1.00 42.03  ?  251 LYS B CE    1 
ATOM   4714 N NZ    . LYS B 2 233 ? 27.931 -10.250 57.038 1.00 52.54  ?  251 LYS B NZ    1 
ATOM   4715 N N     . PRO B 2 234 ? 32.967 -10.312 52.347 1.00 41.64  ?  252 PRO B N     1 
ATOM   4716 C CA    . PRO B 2 234 ? 32.991 -9.611  51.055 1.00 40.96  ?  252 PRO B CA    1 
ATOM   4717 C C     . PRO B 2 234 ? 31.637 -9.095  50.602 1.00 41.69  ?  252 PRO B C     1 
ATOM   4718 O O     . PRO B 2 234 ? 31.564 -8.439  49.558 1.00 39.66  ?  252 PRO B O     1 
ATOM   4719 C CB    . PRO B 2 234 ? 33.527 -10.682 50.092 1.00 44.55  ?  252 PRO B CB    1 
ATOM   4720 C CG    . PRO B 2 234 ? 33.246 -11.990 50.782 1.00 46.37  ?  252 PRO B CG    1 
ATOM   4721 C CD    . PRO B 2 234 ? 33.407 -11.712 52.238 1.00 42.50  ?  252 PRO B CD    1 
ATOM   4722 N N     . THR B 2 235 ? 30.566 -9.356  51.356 1.00 40.66  ?  253 THR B N     1 
ATOM   4723 C CA    . THR B 2 235 ? 29.245 -8.861  50.977 1.00 40.38  ?  253 THR B CA    1 
ATOM   4724 C C     . THR B 2 235 ? 29.098 -7.365  51.238 1.00 37.77  ?  253 THR B C     1 
ATOM   4725 O O     . THR B 2 235 ? 28.378 -6.671  50.505 1.00 34.64  ?  253 THR B O     1 
ATOM   4726 C CB    . THR B 2 235 ? 28.181 -9.629  51.743 1.00 38.23  ?  253 THR B CB    1 
ATOM   4727 O OG1   . THR B 2 235 ? 28.751 -10.075 52.976 1.00 45.26  ?  253 THR B OG1   1 
ATOM   4728 C CG2   . THR B 2 235 ? 27.724 -10.832 50.942 1.00 38.61  ?  253 THR B CG2   1 
ATOM   4729 N N     . THR B 2 236 ? 29.760 -6.865  52.264 1.00 35.15  ?  254 THR B N     1 
ATOM   4730 C CA    . THR B 2 236 ? 29.682 -5.462  52.634 1.00 35.15  ?  254 THR B CA    1 
ATOM   4731 C C     . THR B 2 236 ? 30.670 -4.657  51.793 1.00 34.25  ?  254 THR B C     1 
ATOM   4732 O O     . THR B 2 236 ? 31.843 -5.041  51.679 1.00 33.11  ?  254 THR B O     1 
ATOM   4733 C CB    . THR B 2 236 ? 29.951 -5.289  54.151 1.00 37.55  ?  254 THR B CB    1 
ATOM   4734 O OG1   . THR B 2 236 ? 30.632 -4.055  54.399 1.00 37.60  ?  254 THR B OG1   1 
ATOM   4735 C CG2   . THR B 2 236 ? 30.796 -6.437  54.715 1.00 33.40  ?  254 THR B CG2   1 
ATOM   4736 N N     . PRO B 2 237 ? 30.213 -3.527  51.204 1.00 32.44  ?  255 PRO B N     1 
ATOM   4737 C CA    . PRO B 2 237 ? 31.101 -2.642  50.465 1.00 30.67  ?  255 PRO B CA    1 
ATOM   4738 C C     . PRO B 2 237 ? 32.150 -1.960  51.348 1.00 31.10  ?  255 PRO B C     1 
ATOM   4739 O O     . PRO B 2 237 ? 31.834 -1.550  52.420 1.00 31.03  ?  255 PRO B O     1 
ATOM   4740 C CB    . PRO B 2 237 ? 30.144 -1.591  49.906 1.00 27.95  ?  255 PRO B CB    1 
ATOM   4741 C CG    . PRO B 2 237 ? 28.960 -1.605  50.822 1.00 29.32  ?  255 PRO B CG    1 
ATOM   4742 C CD    . PRO B 2 237 ? 28.818 -3.064  51.167 1.00 28.19  ?  255 PRO B CD    1 
ATOM   4743 N N     . PHE B 2 238 ? 33.377 -1.845  50.854 1.00 29.95  ?  256 PHE B N     1 
ATOM   4744 C CA    . PHE B 2 238 ? 34.452 -1.176  51.623 1.00 29.89  ?  256 PHE B CA    1 
ATOM   4745 C C     . PHE B 2 238 ? 34.330 0.338   51.491 1.00 31.93  ?  256 PHE B C     1 
ATOM   4746 O O     . PHE B 2 238 ? 34.309 0.852   50.379 1.00 31.61  ?  256 PHE B O     1 
ATOM   4747 C CB    . PHE B 2 238 ? 35.838 -1.646  51.174 1.00 30.50  ?  256 PHE B CB    1 
ATOM   4748 C CG    . PHE B 2 238 ? 37.012 -1.025  51.892 1.00 32.05  ?  256 PHE B CG    1 
ATOM   4749 C CD1   . PHE B 2 238 ? 37.603 -1.663  52.968 1.00 37.21  ?  256 PHE B CD1   1 
ATOM   4750 C CD2   . PHE B 2 238 ? 37.547 0.182   51.478 1.00 31.32  ?  256 PHE B CD2   1 
ATOM   4751 C CE1   . PHE B 2 238 ? 38.684 -1.099  53.626 1.00 36.48  ?  256 PHE B CE1   1 
ATOM   4752 C CE2   . PHE B 2 238 ? 38.622 0.750   52.139 1.00 33.13  ?  256 PHE B CE2   1 
ATOM   4753 C CZ    . PHE B 2 238 ? 39.190 0.108   53.212 1.00 35.14  ?  256 PHE B CZ    1 
ATOM   4754 N N     . VAL B 2 239 ? 34.242 1.026   52.613 1.00 27.68  ?  257 VAL B N     1 
ATOM   4755 C CA    . VAL B 2 239 ? 34.261 2.503   52.576 1.00 26.93  ?  257 VAL B CA    1 
ATOM   4756 C C     . VAL B 2 239 ? 35.505 2.912   53.362 1.00 26.71  ?  257 VAL B C     1 
ATOM   4757 O O     . VAL B 2 239 ? 36.304 3.673   52.823 1.00 25.55  ?  257 VAL B O     1 
ATOM   4758 C CB    . VAL B 2 239 ? 32.950 3.094   53.123 1.00 25.53  ?  257 VAL B CB    1 
ATOM   4759 C CG1   . VAL B 2 239 ? 32.900 4.598   52.950 1.00 20.11  ?  257 VAL B CG1   1 
ATOM   4760 C CG2   . VAL B 2 239 ? 31.745 2.431   52.481 1.00 23.78  ?  257 VAL B CG2   1 
ATOM   4761 N N     . ALA B 2 240 ? 35.676 2.358   54.560 1.00 28.09  ?  258 ALA B N     1 
ATOM   4762 C CA    . ALA B 2 240 ? 36.849 2.659   55.406 1.00 27.13  ?  258 ALA B CA    1 
ATOM   4763 C C     . ALA B 2 240 ? 37.106 1.519   56.394 1.00 28.28  ?  258 ALA B C     1 
ATOM   4764 O O     . ALA B 2 240 ? 37.777 1.755   57.375 1.00 26.45  ?  258 ALA B O     1 
ATOM   4765 C CB    . ALA B 2 240 ? 36.639 3.960   56.114 1.00 21.16  ?  258 ALA B CB    1 
ATOM   4766 N N     . SER B 2 241 ? 36.600 0.322   56.129 1.00 26.43  ?  259 SER B N     1 
ATOM   4767 C CA    . SER B 2 241 ? 36.752 -0.848  57.033 1.00 25.45  ?  259 SER B CA    1 
ATOM   4768 C C     . SER B 2 241 ? 35.851 -0.918  58.262 1.00 26.08  ?  259 SER B C     1 
ATOM   4769 O O     . SER B 2 241 ? 34.705 -0.549  58.172 1.00 26.24  ?  259 SER B O     1 
ATOM   4770 C CB    . SER B 2 241 ? 38.180 -1.281  57.210 1.00 26.86  ?  259 SER B CB    1 
ATOM   4771 O OG    . SER B 2 241 ? 38.273 -2.634  57.621 1.00 28.36  ?  259 SER B OG    1 
ATOM   4772 N N     . LEU B 2 242 ? 36.378 -1.401  59.373 1.00 27.43  ?  260 LEU B N     1 
ATOM   4773 C CA    . LEU B 2 242 ? 35.659 -1.329  60.661 1.00 26.95  ?  260 LEU B CA    1 
ATOM   4774 C C     . LEU B 2 242 ? 35.713 0.079   61.253 1.00 27.07  ?  260 LEU B C     1 
ATOM   4775 O O     . LEU B 2 242 ? 36.773 0.694   61.219 1.00 26.65  ?  260 LEU B O     1 
ATOM   4776 C CB    . LEU B 2 242 ? 36.209 -2.415  61.584 1.00 25.53  ?  260 LEU B CB    1 
ATOM   4777 C CG    . LEU B 2 242 ? 35.922 -3.844  61.133 1.00 28.17  ?  260 LEU B CG    1 
ATOM   4778 C CD1   . LEU B 2 242 ? 36.332 -4.842  62.200 1.00 26.57  ?  260 LEU B CD1   1 
ATOM   4779 C CD2   . LEU B 2 242 ? 34.454 -4.011  60.784 1.00 29.11  ?  260 LEU B CD2   1 
ATOM   4780 N N     . SER B 2 243 ? 34.579 0.556   61.772 1.00 28.89  ?  261 SER B N     1 
ATOM   4781 C CA    . SER B 2 243 ? 34.501 1.903   62.336 1.00 28.03  ?  261 SER B CA    1 
ATOM   4782 C C     . SER B 2 243 ? 35.035 1.898   63.760 1.00 32.16  ?  261 SER B C     1 
ATOM   4783 O O     . SER B 2 243 ? 34.397 1.354   64.675 1.00 30.34  ?  261 SER B O     1 
ATOM   4784 C CB    . SER B 2 243 ? 33.076 2.435   62.323 1.00 27.20  ?  261 SER B CB    1 
ATOM   4785 O OG    . SER B 2 243 ? 33.064 3.773   62.805 1.00 30.41  ?  261 SER B OG    1 
ATOM   4786 N N     . GLY B 2 244 ? 36.212 2.501   63.933 1.00 31.55  ?  262 GLY B N     1 
ATOM   4787 C CA    . GLY B 2 244 ? 36.771 2.664   65.254 1.00 22.96  ?  262 GLY B CA    1 
ATOM   4788 C C     . GLY B 2 244 ? 35.999 3.657   66.080 1.00 28.26  ?  262 GLY B C     1 
ATOM   4789 O O     . GLY B 2 244 ? 35.886 3.492   67.298 1.00 31.69  ?  262 GLY B O     1 
ATOM   4790 N N     . THR B 2 245 ? 35.435 4.693   65.440 1.00 31.37  ?  263 THR B N     1 
ATOM   4791 C CA    . THR B 2 245 ? 34.723 5.717   66.205 1.00 29.90  ?  263 THR B CA    1 
ATOM   4792 C C     . THR B 2 245 ? 33.595 5.122   67.031 1.00 31.83  ?  263 THR B C     1 
ATOM   4793 O O     . THR B 2 245 ? 33.178 5.734   68.019 1.00 33.50  ?  263 THR B O     1 
ATOM   4794 C CB    . THR B 2 245 ? 34.150 6.828   65.305 1.00 29.71  ?  263 THR B CB    1 
ATOM   4795 O OG1   . THR B 2 245 ? 35.188 7.374   64.500 1.00 39.96  ?  263 THR B OG1   1 
ATOM   4796 C CG2   . THR B 2 245 ? 33.590 7.964   66.125 1.00 27.04  ?  263 THR B CG2   1 
ATOM   4797 N N     . THR B 2 246 ? 33.086 3.946   66.676 1.00 29.31  ?  264 THR B N     1 
ATOM   4798 C CA    . THR B 2 246 ? 31.911 3.524   67.404 1.00 30.64  ?  264 THR B CA    1 
ATOM   4799 C C     . THR B 2 246 ? 32.256 3.001   68.791 1.00 32.35  ?  264 THR B C     1 
ATOM   4800 O O     . THR B 2 246 ? 31.362 2.922   69.639 1.00 33.51  ?  264 THR B O     1 
ATOM   4801 C CB    . THR B 2 246 ? 31.096 2.527   66.576 1.00 31.74  ?  264 THR B CB    1 
ATOM   4802 O OG1   . THR B 2 246 ? 31.251 1.202   67.086 1.00 35.48  ?  264 THR B OG1   1 
ATOM   4803 C CG2   . THR B 2 246 ? 31.522 2.570   65.142 1.00 31.14  ?  264 THR B CG2   1 
ATOM   4804 N N     . TYR B 2 247 ? 33.529 2.703   69.073 1.00 30.78  ?  265 TYR B N     1 
ATOM   4805 C CA    . TYR B 2 247 ? 33.939 2.582   70.471 1.00 31.02  ?  265 TYR B CA    1 
ATOM   4806 C C     . TYR B 2 247 ? 33.764 3.909   71.193 1.00 33.46  ?  265 TYR B C     1 
ATOM   4807 O O     . TYR B 2 247 ? 33.343 3.942   72.357 1.00 32.85  ?  265 TYR B O     1 
ATOM   4808 C CB    . TYR B 2 247 ? 35.388 2.093   70.571 1.00 31.91  ?  265 TYR B CB    1 
ATOM   4809 C CG    . TYR B 2 247 ? 35.555 0.740   69.918 1.00 35.09  ?  265 TYR B CG    1 
ATOM   4810 C CD1   . TYR B 2 247 ? 34.954 -0.395  70.464 1.00 34.58  ?  265 TYR B CD1   1 
ATOM   4811 C CD2   . TYR B 2 247 ? 36.270 0.599   68.736 1.00 31.73  ?  265 TYR B CD2   1 
ATOM   4812 C CE1   . TYR B 2 247 ? 35.078 -1.628  69.863 1.00 31.57  ?  265 TYR B CE1   1 
ATOM   4813 C CE2   . TYR B 2 247 ? 36.394 -0.628  68.124 1.00 30.90  ?  265 TYR B CE2   1 
ATOM   4814 C CZ    . TYR B 2 247 ? 35.789 -1.735  68.685 1.00 32.97  ?  265 TYR B CZ    1 
ATOM   4815 O OH    . TYR B 2 247 ? 35.910 -2.956  68.073 1.00 29.88  ?  265 TYR B OH    1 
ATOM   4816 N N     . SER B 2 248 ? 34.058 5.018   70.499 1.00 32.10  ?  266 SER B N     1 
ATOM   4817 C CA    . SER B 2 248 ? 33.834 6.346   71.059 1.00 30.20  ?  266 SER B CA    1 
ATOM   4818 C C     . SER B 2 248 ? 32.365 6.570   71.371 1.00 31.79  ?  266 SER B C     1 
ATOM   4819 O O     . SER B 2 248 ? 32.030 7.233   72.361 1.00 32.59  ?  266 SER B O     1 
ATOM   4820 C CB    . SER B 2 248 ? 34.333 7.414   70.098 1.00 31.68  ?  266 SER B CB    1 
ATOM   4821 O OG    . SER B 2 248 ? 35.745 7.444   70.070 1.00 33.66  ?  266 SER B OG    1 
ATOM   4822 N N     . LEU B 2 249 ? 31.468 6.031   70.539 1.00 29.38  ?  267 LEU B N     1 
ATOM   4823 C CA    . LEU B 2 249 ? 30.052 6.128   70.865 1.00 29.47  ?  267 LEU B CA    1 
ATOM   4824 C C     . LEU B 2 249 ? 29.702 5.225   72.042 1.00 34.87  ?  267 LEU B C     1 
ATOM   4825 O O     . LEU B 2 249 ? 28.780 5.525   72.816 1.00 33.06  ?  267 LEU B O     1 
ATOM   4826 C CB    . LEU B 2 249 ? 29.208 5.785   69.649 1.00 29.70  ?  267 LEU B CB    1 
ATOM   4827 C CG    . LEU B 2 249 ? 27.712 5.526   69.868 1.00 32.33  ?  267 LEU B CG    1 
ATOM   4828 C CD1   . LEU B 2 249 ? 27.007 6.754   70.371 1.00 26.15  ?  267 LEU B CD1   1 
ATOM   4829 C CD2   . LEU B 2 249 ? 27.061 5.018   68.578 1.00 27.84  ?  267 LEU B CD2   1 
ATOM   4830 N N     . MET B 2 250 ? 30.444 4.133   72.210 1.00 33.29  ?  268 MET B N     1 
ATOM   4831 C CA    . MET B 2 250 ? 30.141 3.218   73.290 1.00 32.45  ?  268 MET B CA    1 
ATOM   4832 C C     . MET B 2 250 ? 30.608 3.761   74.630 1.00 36.90  ?  268 MET B C     1 
ATOM   4833 O O     . MET B 2 250 ? 30.028 3.403   75.665 1.00 34.80  ?  268 MET B O     1 
ATOM   4834 C CB    . MET B 2 250 ? 30.770 1.861   72.994 1.00 33.23  ?  268 MET B CB    1 
ATOM   4835 C CG    . MET B 2 250 ? 30.053 1.124   71.864 1.00 33.99  ?  268 MET B CG    1 
ATOM   4836 S SD    . MET B 2 250 ? 28.349 0.670   72.283 1.00 38.30  ?  268 MET B SD    1 
ATOM   4837 C CE    . MET B 2 250 ? 28.538 0.248   74.033 1.00 32.36  ?  268 MET B CE    1 
ATOM   4838 N N     . VAL B 2 251 ? 31.630 4.632   74.634 1.00 31.42  ?  269 VAL B N     1 
ATOM   4839 C CA    . VAL B 2 251 ? 32.062 5.249   75.883 1.00 27.60  ?  269 VAL B CA    1 
ATOM   4840 C C     . VAL B 2 251 ? 31.027 6.251   76.355 1.00 33.88  ?  269 VAL B C     1 
ATOM   4841 O O     . VAL B 2 251 ? 30.768 6.378   77.562 1.00 37.39  ?  269 VAL B O     1 
ATOM   4842 C CB    . VAL B 2 251 ? 33.429 5.923   75.726 1.00 27.76  ?  269 VAL B CB    1 
ATOM   4843 C CG1   . VAL B 2 251 ? 33.743 6.707   76.954 1.00 23.84  ?  269 VAL B CG1   1 
ATOM   4844 C CG2   . VAL B 2 251 ? 34.493 4.902   75.468 1.00 32.10  ?  269 VAL B CG2   1 
ATOM   4845 N N     . VAL B 2 252 ? 30.435 6.999   75.418 1.00 31.37  ?  270 VAL B N     1 
ATOM   4846 C CA    . VAL B 2 252 ? 29.381 7.948   75.765 1.00 33.61  ?  270 VAL B CA    1 
ATOM   4847 C C     . VAL B 2 252 ? 28.118 7.215   76.227 1.00 33.90  ?  270 VAL B C     1 
ATOM   4848 O O     . VAL B 2 252 ? 27.505 7.592   77.230 1.00 30.53  ?  270 VAL B O     1 
ATOM   4849 C CB    . VAL B 2 252 ? 29.101 8.884   74.571 1.00 30.56  ?  270 VAL B CB    1 
ATOM   4850 C CG1   . VAL B 2 252 ? 28.095 9.957   74.949 1.00 27.53  ?  270 VAL B CG1   1 
ATOM   4851 C CG2   . VAL B 2 252 ? 30.377 9.501   74.080 1.00 26.62  ?  270 VAL B CG2   1 
ATOM   4852 N N     . LEU B 2 253 ? 27.719 6.150   75.505 1.00 37.73  ?  271 LEU B N     1 
ATOM   4853 C CA    . LEU B 2 253 ? 26.492 5.413   75.820 1.00 31.80  ?  271 LEU B CA    1 
ATOM   4854 C C     . LEU B 2 253 ? 26.597 4.697   77.160 1.00 33.71  ?  271 LEU B C     1 
ATOM   4855 O O     . LEU B 2 253 ? 25.653 4.715   77.954 1.00 36.68  ?  271 LEU B O     1 
ATOM   4856 C CB    . LEU B 2 253 ? 26.182 4.397   74.724 1.00 29.72  ?  271 LEU B CB    1 
ATOM   4857 C CG    . LEU B 2 253 ? 25.507 4.850   73.440 1.00 30.64  ?  271 LEU B CG    1 
ATOM   4858 C CD1   . LEU B 2 253 ? 25.078 3.675   72.568 1.00 24.22  ?  271 LEU B CD1   1 
ATOM   4859 C CD2   . LEU B 2 253 ? 24.347 5.741   73.778 1.00 31.57  ?  271 LEU B CD2   1 
ATOM   4860 N N     . THR B 2 254 ? 27.720 4.021   77.411 1.00 30.88  ?  272 THR B N     1 
ATOM   4861 C CA    . THR B 2 254 ? 27.949 3.421   78.722 1.00 33.13  ?  272 THR B CA    1 
ATOM   4862 C C     . THR B 2 254 ? 27.622 4.406   79.854 1.00 40.69  ?  272 THR B C     1 
ATOM   4863 O O     . THR B 2 254 ? 26.892 4.068   80.800 1.00 38.77  ?  272 THR B O     1 
ATOM   4864 C CB    . THR B 2 254 ? 29.397 2.937   78.827 1.00 36.50  ?  272 THR B CB    1 
ATOM   4865 O OG1   . THR B 2 254 ? 29.562 1.752   78.049 1.00 33.64  ?  272 THR B OG1   1 
ATOM   4866 C CG2   . THR B 2 254 ? 29.793 2.648   80.281 1.00 34.69  ?  272 THR B CG2   1 
ATOM   4867 N N     . ASP B 2 255 ? 28.169 5.630   79.776 1.00 37.95  ?  273 ASP B N     1 
ATOM   4868 C CA    . ASP B 2 255 ? 27.870 6.665   80.763 1.00 36.42  ?  273 ASP B CA    1 
ATOM   4869 C C     . ASP B 2 255 ? 26.375 6.967   80.804 1.00 38.08  ?  273 ASP B C     1 
ATOM   4870 O O     . ASP B 2 255 ? 25.782 7.059   81.888 1.00 37.96  ?  273 ASP B O     1 
ATOM   4871 C CB    . ASP B 2 255 ? 28.678 7.934   80.440 1.00 38.43  ?  273 ASP B CB    1 
ATOM   4872 C CG    . ASP B 2 255 ? 28.625 8.997   81.557 1.00 38.81  ?  273 ASP B CG    1 
ATOM   4873 O OD1   . ASP B 2 255 ? 27.743 9.904   81.496 1.00 35.07  ?  273 ASP B OD1   1 
ATOM   4874 O OD2   . ASP B 2 255 ? 29.490 8.941   82.468 1.00 38.24  -1 273 ASP B OD2   1 
ATOM   4875 N N     . TYR B 2 256 ? 25.746 7.100   79.628 1.00 32.75  ?  274 TYR B N     1 
ATOM   4876 C CA    . TYR B 2 256 ? 24.325 7.432   79.571 1.00 34.68  ?  274 TYR B CA    1 
ATOM   4877 C C     . TYR B 2 256 ? 23.481 6.348   80.228 1.00 35.45  ?  274 TYR B C     1 
ATOM   4878 O O     . TYR B 2 256 ? 22.579 6.641   81.024 1.00 33.66  ?  274 TYR B O     1 
ATOM   4879 C CB    . TYR B 2 256 ? 23.897 7.641   78.118 1.00 33.31  ?  274 TYR B CB    1 
ATOM   4880 C CG    . TYR B 2 256 ? 22.425 7.906   77.938 1.00 32.00  ?  274 TYR B CG    1 
ATOM   4881 C CD1   . TYR B 2 256 ? 21.596 6.972   77.300 1.00 31.92  ?  274 TYR B CD1   1 
ATOM   4882 C CD2   . TYR B 2 256 ? 21.859 9.083   78.398 1.00 33.74  ?  274 TYR B CD2   1 
ATOM   4883 C CE1   . TYR B 2 256 ? 20.252 7.204   77.131 1.00 28.25  ?  274 TYR B CE1   1 
ATOM   4884 C CE2   . TYR B 2 256 ? 20.516 9.332   78.231 1.00 35.72  ?  274 TYR B CE2   1 
ATOM   4885 C CZ    . TYR B 2 256 ? 19.717 8.386   77.602 1.00 36.48  ?  274 TYR B CZ    1 
ATOM   4886 O OH    . TYR B 2 256 ? 18.377 8.644   77.457 1.00 40.34  ?  274 TYR B OH    1 
ATOM   4887 N N     . ILE B 2 257 ? 23.756 5.086   79.885 1.00 34.75  ?  275 ILE B N     1 
ATOM   4888 C CA    . ILE B 2 257 ? 23.042 3.952   80.470 1.00 34.81  ?  275 ILE B CA    1 
ATOM   4889 C C     . ILE B 2 257 ? 23.226 3.926   81.982 1.00 36.93  ?  275 ILE B C     1 
ATOM   4890 O O     . ILE B 2 257 ? 22.286 3.655   82.738 1.00 37.47  ?  275 ILE B O     1 
ATOM   4891 C CB    . ILE B 2 257 ? 23.531 2.647   79.817 1.00 31.49  ?  275 ILE B CB    1 
ATOM   4892 C CG1   . ILE B 2 257 ? 22.980 2.510   78.416 1.00 30.95  ?  275 ILE B CG1   1 
ATOM   4893 C CG2   . ILE B 2 257 ? 23.157 1.439   80.610 1.00 28.99  ?  275 ILE B CG2   1 
ATOM   4894 C CD1   . ILE B 2 257 ? 23.634 1.382   77.676 1.00 35.55  ?  275 ILE B CD1   1 
ATOM   4895 N N     . GLU B 2 258 ? 24.438 4.213   82.451 1.00 38.89  ?  276 GLU B N     1 
ATOM   4896 C CA    . GLU B 2 258 ? 24.702 4.151   83.880 1.00 38.91  ?  276 GLU B CA    1 
ATOM   4897 C C     . GLU B 2 258 ? 23.809 5.116   84.646 1.00 43.34  ?  276 GLU B C     1 
ATOM   4898 O O     . GLU B 2 258 ? 23.320 4.796   85.740 1.00 44.71  ?  276 GLU B O     1 
ATOM   4899 C CB    . GLU B 2 258 ? 26.156 4.482   84.160 1.00 40.71  ?  276 GLU B CB    1 
ATOM   4900 C CG    . GLU B 2 258 ? 27.102 3.342   84.212 1.00 42.52  ?  276 GLU B CG    1 
ATOM   4901 C CD    . GLU B 2 258 ? 28.543 3.849   84.139 1.00 59.22  ?  276 GLU B CD    1 
ATOM   4902 O OE1   . GLU B 2 258 ? 28.891 4.793   84.919 1.00 57.09  ?  276 GLU B OE1   1 
ATOM   4903 O OE2   . GLU B 2 258 ? 29.326 3.306   83.315 1.00 65.24  -1 276 GLU B OE2   1 
ATOM   4904 N N     . LYS B 2 259 ? 23.617 6.317   84.113 1.00 40.03  ?  277 LYS B N     1 
ATOM   4905 C CA    . LYS B 2 259 ? 22.952 7.350   84.881 1.00 41.81  ?  277 LYS B CA    1 
ATOM   4906 C C     . LYS B 2 259 ? 21.514 7.543   84.438 1.00 41.20  ?  277 LYS B C     1 
ATOM   4907 O O     . LYS B 2 259 ? 20.870 8.524   84.834 1.00 44.23  ?  277 LYS B O     1 
ATOM   4908 C CB    . LYS B 2 259 ? 23.763 8.659   84.843 1.00 42.54  ?  277 LYS B CB    1 
ATOM   4909 C CG    . LYS B 2 259 ? 23.896 9.372   83.542 1.00 38.03  ?  277 LYS B CG    1 
ATOM   4910 C CD    . LYS B 2 259 ? 24.779 10.622  83.712 1.00 41.89  ?  277 LYS B CD    1 
ATOM   4911 C CE    . LYS B 2 259 ? 26.175 10.291  84.251 1.00 45.88  ?  277 LYS B CE    1 
ATOM   4912 N NZ    . LYS B 2 259 ? 27.175 11.401  84.010 1.00 43.81  ?  277 LYS B NZ    1 
ATOM   4913 N N     . HIS B 2 260 ? 20.990 6.587   83.666 1.00 40.83  ?  278 HIS B N     1 
ATOM   4914 C CA    . HIS B 2 260 ? 19.585 6.483   83.306 1.00 37.53  ?  278 HIS B CA    1 
ATOM   4915 C C     . HIS B 2 260 ? 19.139 5.028   83.392 1.00 43.31  ?  278 HIS B C     1 
ATOM   4916 O O     . HIS B 2 260 ? 18.243 4.601   82.656 1.00 48.95  ?  278 HIS B O     1 
ATOM   4917 C CB    . HIS B 2 260 ? 19.338 7.052   81.906 1.00 38.27  ?  278 HIS B CB    1 
ATOM   4918 C CG    . HIS B 2 260 ? 19.412 8.552   81.831 1.00 40.76  ?  278 HIS B CG    1 
ATOM   4919 N ND1   . HIS B 2 260 ? 18.289 9.357   81.809 1.00 40.79  ?  278 HIS B ND1   1 
ATOM   4920 C CD2   . HIS B 2 260 ? 20.473 9.391   81.767 1.00 36.17  ?  278 HIS B CD2   1 
ATOM   4921 C CE1   . HIS B 2 260 ? 18.656 10.622  81.725 1.00 39.63  ?  278 HIS B CE1   1 
ATOM   4922 N NE2   . HIS B 2 260 ? 19.976 10.671  81.708 1.00 38.74  ?  278 HIS B NE2   1 
ATOM   4923 N N     . LYS B 2 261 ? 19.760 4.248   84.283 1.00 42.03  ?  279 LYS B N     1 
ATOM   4924 C CA    . LYS B 2 261 ? 19.471 2.817   84.355 1.00 45.93  ?  279 LYS B CA    1 
ATOM   4925 C C     . LYS B 2 261 ? 18.008 2.555   84.722 1.00 48.70  ?  279 LYS B C     1 
ATOM   4926 O O     . LYS B 2 261 ? 17.363 1.675   84.140 1.00 49.48  ?  279 LYS B O     1 
ATOM   4927 C CB    . LYS B 2 261 ? 20.431 2.155   85.353 1.00 47.25  ?  279 LYS B CB    1 
ATOM   4928 C CG    . LYS B 2 261 ? 20.233 0.656   85.609 1.00 52.82  ?  279 LYS B CG    1 
ATOM   4929 C CD    . LYS B 2 261 ? 20.156 0.388   87.126 1.00 60.68  ?  279 LYS B CD    1 
ATOM   4930 C CE    . LYS B 2 261 ? 21.371 -0.369  87.688 1.00 68.53  ?  279 LYS B CE    1 
ATOM   4931 N NZ    . LYS B 2 261 ? 21.495 -0.278  89.192 1.00 59.05  ?  279 LYS B NZ    1 
ATOM   4932 N N     . THR B 2 262 ? 17.461 3.321   85.671 1.00 47.43  ?  280 THR B N     1 
ATOM   4933 C CA    . THR B 2 262 ? 16.080 3.161   86.116 1.00 42.48  ?  280 THR B CA    1 
ATOM   4934 C C     . THR B 2 262 ? 15.061 3.669   85.101 1.00 45.34  ?  280 THR B C     1 
ATOM   4935 O O     . THR B 2 262 ? 13.860 3.440   85.275 1.00 47.48  ?  280 THR B O     1 
ATOM   4936 C CB    . THR B 2 262 ? 15.898 3.895   87.440 1.00 42.93  ?  280 THR B CB    1 
ATOM   4937 O OG1   . THR B 2 262 ? 16.070 5.305   87.223 1.00 44.57  ?  280 THR B OG1   1 
ATOM   4938 C CG2   . THR B 2 262 ? 16.918 3.407   88.453 1.00 37.86  ?  280 THR B CG2   1 
ATOM   4939 N N     . ASP B 2 263 ? 15.510 4.358   84.059 1.00 49.24  ?  281 ASP B N     1 
ATOM   4940 C CA    . ASP B 2 263 ? 14.617 4.867   83.027 1.00 49.30  ?  281 ASP B CA    1 
ATOM   4941 C C     . ASP B 2 263 ? 13.810 3.725   82.405 1.00 53.21  ?  281 ASP B C     1 
ATOM   4942 O O     . ASP B 2 263 ? 14.361 2.692   82.003 1.00 51.00  ?  281 ASP B O     1 
ATOM   4943 C CB    . ASP B 2 263 ? 15.444 5.598   81.964 1.00 47.56  ?  281 ASP B CB    1 
ATOM   4944 C CG    . ASP B 2 263 ? 15.003 7.032   81.757 1.00 49.40  ?  281 ASP B CG    1 
ATOM   4945 O OD1   . ASP B 2 263 ? 15.862 7.931   81.758 1.00 59.11  ?  281 ASP B OD1   1 
ATOM   4946 O OD2   . ASP B 2 263 ? 13.796 7.267   81.567 1.00 62.01  -1 281 ASP B OD2   1 
ATOM   4947 N N     . LYS B 2 264 ? 12.489 3.907   82.337 1.00 58.16  ?  282 LYS B N     1 
ATOM   4948 C CA    . LYS B 2 264 ? 11.630 2.836   81.839 1.00 54.01  ?  282 LYS B CA    1 
ATOM   4949 C C     . LYS B 2 264 ? 11.699 2.719   80.318 1.00 50.72  ?  282 LYS B C     1 
ATOM   4950 O O     . LYS B 2 264 ? 11.650 1.606   79.780 1.00 52.20  ?  282 LYS B O     1 
ATOM   4951 C CB    . LYS B 2 264 ? 10.196 3.057   82.319 1.00 53.29  ?  282 LYS B CB    1 
ATOM   4952 C CG    . LYS B 2 264 ? 9.955  2.593   83.755 1.00 57.60  ?  282 LYS B CG    1 
ATOM   4953 C CD    . LYS B 2 264 ? 8.460  2.661   84.114 1.00 71.11  ?  282 LYS B CD    1 
ATOM   4954 C CE    . LYS B 2 264 ? 7.993  1.420   84.897 1.00 75.79  ?  282 LYS B CE    1 
ATOM   4955 N NZ    . LYS B 2 264 ? 6.759  0.745   84.334 1.00 73.65  ?  282 LYS B NZ    1 
ATOM   4956 N N     . ASP B 2 265 ? 11.842 3.847   79.611 1.00 50.84  ?  283 ASP B N     1 
ATOM   4957 C CA    . ASP B 2 265 ? 11.954 3.879   78.155 1.00 51.06  ?  283 ASP B CA    1 
ATOM   4958 C C     . ASP B 2 265 ? 13.400 3.839   77.675 1.00 51.38  ?  283 ASP B C     1 
ATOM   4959 O O     . ASP B 2 265 ? 13.677 4.237   76.535 1.00 45.72  ?  283 ASP B O     1 
ATOM   4960 C CB    . ASP B 2 265 ? 11.273 5.128   77.596 1.00 47.72  ?  283 ASP B CB    1 
ATOM   4961 C CG    . ASP B 2 265 ? 11.675 6.382   78.342 1.00 56.65  ?  283 ASP B CG    1 
ATOM   4962 O OD1   . ASP B 2 265 ? 11.531 7.500   77.787 1.00 61.67  ?  283 ASP B OD1   1 
ATOM   4963 O OD2   . ASP B 2 265 ? 12.138 6.245   79.498 1.00 55.62  -1 283 ASP B OD2   1 
ATOM   4964 N N     . ILE B 2 266 ? 14.320 3.364   78.521 1.00 48.84  ?  284 ILE B N     1 
ATOM   4965 C CA    . ILE B 2 266 ? 15.738 3.396   78.187 1.00 46.41  ?  284 ILE B CA    1 
ATOM   4966 C C     . ILE B 2 266 ? 15.988 2.683   76.857 1.00 47.51  ?  284 ILE B C     1 
ATOM   4967 O O     . ILE B 2 266 ? 16.670 3.213   75.968 1.00 44.32  ?  284 ILE B O     1 
ATOM   4968 C CB    . ILE B 2 266 ? 16.567 2.794   79.341 1.00 46.42  ?  284 ILE B CB    1 
ATOM   4969 C CG1   . ILE B 2 266 ? 18.072 2.869   79.042 1.00 40.18  ?  284 ILE B CG1   1 
ATOM   4970 C CG2   . ILE B 2 266 ? 16.137 1.377   79.641 1.00 43.15  ?  284 ILE B CG2   1 
ATOM   4971 C CD1   . ILE B 2 266 ? 18.531 4.268   78.691 1.00 37.08  ?  284 ILE B CD1   1 
ATOM   4972 N N     . GLU B 2 267 ? 15.416 1.480   76.690 1.00 44.34  ?  285 GLU B N     1 
ATOM   4973 C CA    . GLU B 2 267 ? 15.603 0.737   75.446 1.00 42.29  ?  285 GLU B CA    1 
ATOM   4974 C C     . GLU B 2 267 ? 15.116 1.524   74.229 1.00 43.31  ?  285 GLU B C     1 
ATOM   4975 O O     . GLU B 2 267 ? 15.783 1.532   73.188 1.00 41.77  ?  285 GLU B O     1 
ATOM   4976 C CB    . GLU B 2 267 ? 14.885 -0.600  75.520 1.00 41.24  ?  285 GLU B CB    1 
ATOM   4977 C CG    . GLU B 2 267 ? 15.180 -1.497  74.352 1.00 43.31  ?  285 GLU B CG    1 
ATOM   4978 C CD    . GLU B 2 267 ? 14.301 -2.730  74.350 1.00 49.70  ?  285 GLU B CD    1 
ATOM   4979 O OE1   . GLU B 2 267 ? 14.840 -3.863  74.497 1.00 52.37  ?  285 GLU B OE1   1 
ATOM   4980 O OE2   . GLU B 2 267 ? 13.065 -2.557  74.208 1.00 52.39  -1 285 GLU B OE2   1 
ATOM   4981 N N     . LYS B 2 268 ? 13.949 2.173   74.328 1.00 40.07  ?  286 LYS B N     1 
ATOM   4982 C CA    . LYS B 2 268 ? 13.467 2.982   73.214 1.00 36.68  ?  286 LYS B CA    1 
ATOM   4983 C C     . LYS B 2 268 ? 14.516 3.992   72.798 1.00 38.72  ?  286 LYS B C     1 
ATOM   4984 O O     . LYS B 2 268 ? 14.852 4.101   71.612 1.00 37.46  ?  286 LYS B O     1 
ATOM   4985 C CB    . LYS B 2 268 ? 12.177 3.708   73.593 1.00 36.90  ?  286 LYS B CB    1 
ATOM   4986 C CG    . LYS B 2 268 ? 11.196 3.822   72.473 1.00 35.46  ?  286 LYS B CG    1 
ATOM   4987 C CD    . LYS B 2 268 ? 10.321 5.051   72.610 1.00 45.55  ?  286 LYS B CD    1 
ATOM   4988 C CE    . LYS B 2 268 ? 9.554  5.341   71.306 1.00 47.79  ?  286 LYS B CE    1 
ATOM   4989 N NZ    . LYS B 2 268 ? 8.649  6.523   71.425 1.00 42.01  ?  286 LYS B NZ    1 
ATOM   4990 N N     . LYS B 2 269 ? 15.060 4.726   73.785 1.00 38.26  ?  287 LYS B N     1 
ATOM   4991 C CA    . LYS B 2 269 ? 15.894 5.899   73.541 1.00 35.65  ?  287 LYS B CA    1 
ATOM   4992 C C     . LYS B 2 269 ? 17.311 5.532   73.141 1.00 33.91  ?  287 LYS B C     1 
ATOM   4993 O O     . LYS B 2 269 ? 17.963 6.305   72.437 1.00 34.92  ?  287 LYS B O     1 
ATOM   4994 C CB    . LYS B 2 269 ? 15.937 6.799   74.781 1.00 35.65  ?  287 LYS B CB    1 
ATOM   4995 C CG    . LYS B 2 269 ? 14.611 7.419   75.149 1.00 36.67  ?  287 LYS B CG    1 
ATOM   4996 C CD    . LYS B 2 269 ? 14.789 8.600   76.092 1.00 43.09  ?  287 LYS B CD    1 
ATOM   4997 C CE    . LYS B 2 269 ? 14.509 8.210   77.528 1.00 48.50  ?  287 LYS B CE    1 
ATOM   4998 N NZ    . LYS B 2 269 ? 15.615 8.566   78.452 1.00 44.79  ?  287 LYS B NZ    1 
ATOM   4999 N N     . VAL B 2 270 ? 17.825 4.385   73.578 1.00 31.23  ?  288 VAL B N     1 
ATOM   5000 C CA    . VAL B 2 270 ? 19.151 4.024   73.102 1.00 30.94  ?  288 VAL B CA    1 
ATOM   5001 C C     . VAL B 2 270 ? 19.084 3.609   71.641 1.00 30.91  ?  288 VAL B C     1 
ATOM   5002 O O     . VAL B 2 270 ? 20.025 3.853   70.879 1.00 31.34  ?  288 VAL B O     1 
ATOM   5003 C CB    . VAL B 2 270 ? 19.779 2.940   73.995 1.00 29.89  ?  288 VAL B CB    1 
ATOM   5004 C CG1   . VAL B 2 270 ? 21.006 2.338   73.346 1.00 28.98  ?  288 VAL B CG1   1 
ATOM   5005 C CG2   . VAL B 2 270 ? 20.157 3.542   75.296 1.00 28.03  ?  288 VAL B CG2   1 
ATOM   5006 N N     . ASN B 2 271 ? 17.972 3.012   71.207 1.00 31.20  ?  289 ASN B N     1 
ATOM   5007 C CA    . ASN B 2 271 ? 17.861 2.646   69.796 1.00 30.37  ?  289 ASN B CA    1 
ATOM   5008 C C     . ASN B 2 271 ? 17.767 3.891   68.902 1.00 32.64  ?  289 ASN B C     1 
ATOM   5009 O O     . ASN B 2 271 ? 18.247 3.870   67.764 1.00 32.65  ?  289 ASN B O     1 
ATOM   5010 C CB    . ASN B 2 271 ? 16.671 1.696   69.585 1.00 29.26  ?  289 ASN B CB    1 
ATOM   5011 C CG    . ASN B 2 271 ? 17.033 0.196   69.810 1.00 33.68  ?  289 ASN B CG    1 
ATOM   5012 O OD1   . ASN B 2 271 ? 17.830 -0.394  69.081 1.00 37.18  ?  289 ASN B OD1   1 
ATOM   5013 N ND2   . ASN B 2 271 ? 16.414 -0.413  70.803 1.00 35.07  ?  289 ASN B ND2   1 
ATOM   5014 N N     . GLN B 2 272 ? 17.205 5.001   69.391 1.00 29.76  ?  290 GLN B N     1 
ATOM   5015 C CA    . GLN B 2 272 ? 17.208 6.201   68.560 1.00 30.98  ?  290 GLN B CA    1 
ATOM   5016 C C     . GLN B 2 272 ? 18.628 6.689   68.294 1.00 34.96  ?  290 GLN B C     1 
ATOM   5017 O O     . GLN B 2 272 ? 18.925 7.161   67.192 1.00 35.58  ?  290 GLN B O     1 
ATOM   5018 C CB    . GLN B 2 272 ? 16.388 7.307   69.200 1.00 34.71  ?  290 GLN B CB    1 
ATOM   5019 C CG    . GLN B 2 272 ? 15.105 6.845   69.784 1.00 35.50  ?  290 GLN B CG    1 
ATOM   5020 C CD    . GLN B 2 272 ? 14.167 7.993   70.049 1.00 39.68  ?  290 GLN B CD    1 
ATOM   5021 O OE1   . GLN B 2 272 ? 13.079 8.064   69.474 1.00 45.89  ?  290 GLN B OE1   1 
ATOM   5022 N NE2   . GLN B 2 272 ? 14.569 8.896   70.936 1.00 35.44  ?  290 GLN B NE2   1 
ATOM   5023 N N     . ILE B 2 273 ? 19.519 6.606   69.290 1.00 36.06  ?  291 ILE B N     1 
ATOM   5024 C CA    . ILE B 2 273 ? 20.916 6.972   69.056 1.00 32.62  ?  291 ILE B CA    1 
ATOM   5025 C C     . ILE B 2 273 ? 21.580 5.961   68.139 1.00 32.05  ?  291 ILE B C     1 
ATOM   5026 O O     . ILE B 2 273 ? 22.078 6.316   67.066 1.00 32.61  ?  291 ILE B O     1 
ATOM   5027 C CB    . ILE B 2 273 ? 21.704 7.108   70.369 1.00 31.43  ?  291 ILE B CB    1 
ATOM   5028 C CG1   . ILE B 2 273 ? 20.876 7.773   71.465 1.00 31.75  ?  291 ILE B CG1   1 
ATOM   5029 C CG2   . ILE B 2 273 ? 22.945 7.920   70.110 1.00 28.19  ?  291 ILE B CG2   1 
ATOM   5030 C CD1   . ILE B 2 273 ? 21.597 7.824   72.795 1.00 29.18  ?  291 ILE B CD1   1 
ATOM   5031 N N     . ILE B 2 274 ? 21.610 4.687   68.548 1.00 31.01  ?  292 ILE B N     1 
ATOM   5032 C CA    . ILE B 2 274 ? 22.306 3.699   67.722 1.00 31.92  ?  292 ILE B CA    1 
ATOM   5033 C C     . ILE B 2 274 ? 21.844 3.820   66.283 1.00 31.66  ?  292 ILE B C     1 
ATOM   5034 O O     . ILE B 2 274 ? 22.645 3.742   65.351 1.00 34.15  ?  292 ILE B O     1 
ATOM   5035 C CB    . ILE B 2 274 ? 22.107 2.264   68.251 1.00 34.13  ?  292 ILE B CB    1 
ATOM   5036 C CG1   . ILE B 2 274 ? 22.687 2.084   69.660 1.00 30.28  ?  292 ILE B CG1   1 
ATOM   5037 C CG2   . ILE B 2 274 ? 22.748 1.270   67.301 1.00 26.95  ?  292 ILE B CG2   1 
ATOM   5038 C CD1   . ILE B 2 274 ? 24.118 2.412   69.769 1.00 24.52  ?  292 ILE B CD1   1 
ATOM   5039 N N     . ASN B 2 275 ? 20.555 4.074   66.077 1.00 31.53  ?  293 ASN B N     1 
ATOM   5040 C CA    . ASN B 2 275 ? 20.048 4.083   64.711 1.00 35.22  ?  293 ASN B CA    1 
ATOM   5041 C C     . ASN B 2 275 ? 20.354 5.390   63.996 1.00 33.63  ?  293 ASN B C     1 
ATOM   5042 O O     . ASN B 2 275 ? 20.731 5.367   62.822 1.00 35.01  ?  293 ASN B O     1 
ATOM   5043 C CB    . ASN B 2 275 ? 18.552 3.774   64.703 1.00 33.82  ?  293 ASN B CB    1 
ATOM   5044 C CG    . ASN B 2 275 ? 18.277 2.359   65.161 1.00 38.77  ?  293 ASN B CG    1 
ATOM   5045 O OD1   . ASN B 2 275 ? 19.188 1.666   65.666 1.00 39.73  ?  293 ASN B OD1   1 
ATOM   5046 N ND2   . ASN B 2 275 ? 17.043 1.909   64.997 1.00 37.35  ?  293 ASN B ND2   1 
ATOM   5047 N N     . LEU B 2 276 ? 20.213 6.535   64.674 1.00 33.36  ?  294 LEU B N     1 
ATOM   5048 C CA    . LEU B 2 276 ? 20.574 7.799   64.042 1.00 30.62  ?  294 LEU B CA    1 
ATOM   5049 C C     . LEU B 2 276 ? 22.051 7.816   63.694 1.00 31.98  ?  294 LEU B C     1 
ATOM   5050 O O     . LEU B 2 276 ? 22.446 8.310   62.632 1.00 31.85  ?  294 LEU B O     1 
ATOM   5051 C CB    . LEU B 2 276 ? 20.249 8.975   64.955 1.00 31.83  ?  294 LEU B CB    1 
ATOM   5052 C CG    . LEU B 2 276 ? 20.643 10.324  64.331 1.00 28.40  ?  294 LEU B CG    1 
ATOM   5053 C CD1   . LEU B 2 276 ? 20.037 10.462  62.924 1.00 27.77  ?  294 LEU B CD1   1 
ATOM   5054 C CD2   . LEU B 2 276 ? 20.260 11.479  65.209 1.00 25.91  ?  294 LEU B CD2   1 
ATOM   5055 N N     . TRP B 2 277 ? 22.878 7.298   64.596 1.00 30.15  ?  295 TRP B N     1 
ATOM   5056 C CA    . TRP B 2 277 ? 24.284 7.069   64.309 1.00 28.38  ?  295 TRP B CA    1 
ATOM   5057 C C     . TRP B 2 277 ? 24.472 6.283   63.016 1.00 30.59  ?  295 TRP B C     1 
ATOM   5058 O O     . TRP B 2 277 ? 25.234 6.704   62.137 1.00 32.75  ?  295 TRP B O     1 
ATOM   5059 C CB    . TRP B 2 277 ? 24.913 6.334   65.486 1.00 29.90  ?  295 TRP B CB    1 
ATOM   5060 C CG    . TRP B 2 277 ? 26.355 6.024   65.335 1.00 30.31  ?  295 TRP B CG    1 
ATOM   5061 C CD1   . TRP B 2 277 ? 26.895 4.928   64.745 1.00 27.85  ?  295 TRP B CD1   1 
ATOM   5062 C CD2   . TRP B 2 277 ? 27.453 6.812   65.807 1.00 30.93  ?  295 TRP B CD2   1 
ATOM   5063 N NE1   . TRP B 2 277 ? 28.265 4.979   64.816 1.00 32.58  ?  295 TRP B NE1   1 
ATOM   5064 C CE2   . TRP B 2 277 ? 28.634 6.128   65.460 1.00 30.39  ?  295 TRP B CE2   1 
ATOM   5065 C CE3   . TRP B 2 277 ? 27.552 8.032   66.487 1.00 30.80  ?  295 TRP B CE3   1 
ATOM   5066 C CZ2   . TRP B 2 277 ? 29.901 6.624   65.758 1.00 31.12  ?  295 TRP B CZ2   1 
ATOM   5067 C CZ3   . TRP B 2 277 ? 28.813 8.528   66.786 1.00 32.43  ?  295 TRP B CZ3   1 
ATOM   5068 C CH2   . TRP B 2 277 ? 29.970 7.828   66.419 1.00 34.36  ?  295 TRP B CH2   1 
ATOM   5069 N N     . ILE B 2 278 ? 23.780 5.141   62.879 1.00 29.44  ?  296 ILE B N     1 
ATOM   5070 C CA    . ILE B 2 278 ? 23.937 4.297   61.687 1.00 32.22  ?  296 ILE B CA    1 
ATOM   5071 C C     . ILE B 2 278 ? 23.528 5.055   60.421 1.00 32.01  ?  296 ILE B C     1 
ATOM   5072 O O     . ILE B 2 278 ? 24.248 5.065   59.412 1.00 29.29  ?  296 ILE B O     1 
ATOM   5073 C CB    . ILE B 2 278 ? 23.127 2.997   61.832 1.00 31.17  ?  296 ILE B CB    1 
ATOM   5074 C CG1   . ILE B 2 278 ? 23.766 2.058   62.846 1.00 25.58  ?  296 ILE B CG1   1 
ATOM   5075 C CG2   . ILE B 2 278 ? 22.978 2.297   60.477 1.00 23.63  ?  296 ILE B CG2   1 
ATOM   5076 C CD1   . ILE B 2 278 ? 22.856 0.900   63.154 1.00 28.30  ?  296 ILE B CD1   1 
ATOM   5077 N N     . SER B 2 279 ? 22.357 5.683   60.446 1.00 28.74  ?  297 SER B N     1 
ATOM   5078 C CA    . SER B 2 279 ? 21.912 6.426   59.278 1.00 31.28  ?  297 SER B CA    1 
ATOM   5079 C C     . SER B 2 279 ? 22.909 7.514   58.892 1.00 34.03  ?  297 SER B C     1 
ATOM   5080 O O     . SER B 2 279 ? 23.189 7.713   57.703 1.00 33.95  ?  297 SER B O     1 
ATOM   5081 C CB    . SER B 2 279 ? 20.545 7.036   59.542 1.00 30.70  ?  297 SER B CB    1 
ATOM   5082 O OG    . SER B 2 279 ? 20.735 8.325   60.082 1.00 36.44  ?  297 SER B OG    1 
ATOM   5083 N N     . SER B 2 280 ? 23.441 8.251   59.870 1.00 33.52  ?  298 SER B N     1 
ATOM   5084 C CA    . SER B 2 280 ? 24.332 9.341   59.502 1.00 31.41  ?  298 SER B CA    1 
ATOM   5085 C C     . SER B 2 280 ? 25.656 8.838   58.993 1.00 31.78  ?  298 SER B C     1 
ATOM   5086 O O     . SER B 2 280 ? 26.255 9.496   58.141 1.00 33.29  ?  298 SER B O     1 
ATOM   5087 C CB    . SER B 2 280 ? 24.546 10.294  60.658 1.00 28.60  ?  298 SER B CB    1 
ATOM   5088 O OG    . SER B 2 280 ? 23.288 10.608  61.187 1.00 34.64  ?  298 SER B OG    1 
ATOM   5089 N N     . TYR B 2 281 ? 26.137 7.689   59.486 1.00 32.34  ?  299 TYR B N     1 
ATOM   5090 C CA    . TYR B 2 281 ? 27.456 7.226   59.048 1.00 30.27  ?  299 TYR B CA    1 
ATOM   5091 C C     . TYR B 2 281 ? 27.438 6.746   57.606 1.00 31.57  ?  299 TYR B C     1 
ATOM   5092 O O     . TYR B 2 281 ? 28.428 6.929   56.883 1.00 29.82  ?  299 TYR B O     1 
ATOM   5093 C CB    . TYR B 2 281 ? 27.991 6.145   59.966 1.00 26.74  ?  299 TYR B CB    1 
ATOM   5094 C CG    . TYR B 2 281 ? 29.005 6.693   60.919 1.00 32.75  ?  299 TYR B CG    1 
ATOM   5095 C CD1   . TYR B 2 281 ? 28.660 7.689   61.839 1.00 34.12  ?  299 TYR B CD1   1 
ATOM   5096 C CD2   . TYR B 2 281 ? 30.318 6.247   60.899 1.00 33.84  ?  299 TYR B CD2   1 
ATOM   5097 C CE1   . TYR B 2 281 ? 29.605 8.218   62.725 1.00 33.31  ?  299 TYR B CE1   1 
ATOM   5098 C CE2   . TYR B 2 281 ? 31.264 6.763   61.782 1.00 35.68  ?  299 TYR B CE2   1 
ATOM   5099 C CZ    . TYR B 2 281 ? 30.900 7.749   62.683 1.00 34.37  ?  299 TYR B CZ    1 
ATOM   5100 O OH    . TYR B 2 281 ? 31.834 8.263   63.539 1.00 40.37  ?  299 TYR B OH    1 
ATOM   5101 N N     . ILE B 2 282 ? 26.318 6.162   57.165 1.00 32.73  ?  300 ILE B N     1 
ATOM   5102 C CA    . ILE B 2 282 ? 26.137 5.826   55.753 1.00 31.59  ?  300 ILE B CA    1 
ATOM   5103 C C     . ILE B 2 282 ? 25.897 7.088   54.921 1.00 29.25  ?  300 ILE B C     1 
ATOM   5104 O O     . ILE B 2 282 ? 26.594 7.339   53.938 1.00 28.61  ?  300 ILE B O     1 
ATOM   5105 C CB    . ILE B 2 282 ? 24.981 4.822   55.611 1.00 33.31  ?  300 ILE B CB    1 
ATOM   5106 C CG1   . ILE B 2 282 ? 25.302 3.547   56.385 1.00 26.56  ?  300 ILE B CG1   1 
ATOM   5107 C CG2   . ILE B 2 282 ? 24.663 4.552   54.139 1.00 28.59  ?  300 ILE B CG2   1 
ATOM   5108 C CD1   . ILE B 2 282 ? 24.165 2.573   56.407 1.00 24.07  ?  300 ILE B CD1   1 
ATOM   5109 N N     . LYS B 2 283 ? 24.914 7.906   55.315 1.00 29.61  ?  301 LYS B N     1 
ATOM   5110 C CA    . LYS B 2 283 ? 24.543 9.100   54.552 1.00 30.88  ?  301 LYS B CA    1 
ATOM   5111 C C     . LYS B 2 283 ? 25.724 10.035  54.300 1.00 33.94  ?  301 LYS B C     1 
ATOM   5112 O O     . LYS B 2 283 ? 25.749 10.742  53.285 1.00 35.60  ?  301 LYS B O     1 
ATOM   5113 C CB    . LYS B 2 283 ? 23.438 9.856   55.285 1.00 30.54  ?  301 LYS B CB    1 
ATOM   5114 C CG    . LYS B 2 283 ? 22.320 10.377  54.408 1.00 34.37  ?  301 LYS B CG    1 
ATOM   5115 C CD    . LYS B 2 283 ? 21.358 11.285  55.187 1.00 37.95  ?  301 LYS B CD    1 
ATOM   5116 C CE    . LYS B 2 283 ? 20.834 12.436  54.331 1.00 39.85  ?  301 LYS B CE    1 
ATOM   5117 N NZ    . LYS B 2 283 ? 19.402 12.751  54.647 1.00 45.40  ?  301 LYS B NZ    1 
ATOM   5118 N N     . GLU B 2 284 ? 26.681 10.092  55.224 1.00 33.24  ?  302 GLU B N     1 
ATOM   5119 C CA    . GLU B 2 284 ? 27.847 10.959  55.118 1.00 33.38  ?  302 GLU B CA    1 
ATOM   5120 C C     . GLU B 2 284 ? 29.054 10.245  54.530 1.00 31.67  ?  302 GLU B C     1 
ATOM   5121 O O     . GLU B 2 284 ? 30.123 10.850  54.425 1.00 31.89  ?  302 GLU B O     1 
ATOM   5122 C CB    . GLU B 2 284 ? 28.223 11.531  56.497 1.00 39.50  ?  302 GLU B CB    1 
ATOM   5123 C CG    . GLU B 2 284 ? 27.234 12.539  57.115 1.00 43.74  ?  302 GLU B CG    1 
ATOM   5124 C CD    . GLU B 2 284 ? 26.807 13.629  56.141 1.00 53.97  ?  302 GLU B CD    1 
ATOM   5125 O OE1   . GLU B 2 284 ? 25.663 13.573  55.607 1.00 51.71  ?  302 GLU B OE1   1 
ATOM   5126 O OE2   . GLU B 2 284 ? 27.629 14.539  55.903 1.00 58.92  -1 302 GLU B OE2   1 
ATOM   5127 N N     . GLY B 2 285 ? 28.925 8.969   54.183 1.00 30.04  ?  303 GLY B N     1 
ATOM   5128 C CA    . GLY B 2 285 ? 29.993 8.251   53.512 1.00 29.14  ?  303 GLY B CA    1 
ATOM   5129 C C     . GLY B 2 285 ? 31.157 7.817   54.368 1.00 29.61  ?  303 GLY B C     1 
ATOM   5130 O O     . GLY B 2 285 ? 32.207 7.485   53.823 1.00 34.57  ?  303 GLY B O     1 
ATOM   5131 N N     . TYR B 2 286 ? 31.008 7.805   55.694 1.00 31.47  ?  304 TYR B N     1 
ATOM   5132 C CA    . TYR B 2 286 ? 32.109 7.413   56.563 1.00 27.05  ?  304 TYR B CA    1 
ATOM   5133 C C     . TYR B 2 286 ? 32.335 5.911   56.512 1.00 29.70  ?  304 TYR B C     1 
ATOM   5134 O O     . TYR B 2 286 ? 33.478 5.452   56.525 1.00 30.83  ?  304 TYR B O     1 
ATOM   5135 C CB    . TYR B 2 286 ? 31.828 7.854   57.997 1.00 30.67  ?  304 TYR B CB    1 
ATOM   5136 C CG    . TYR B 2 286 ? 31.659 9.357   58.177 1.00 38.04  ?  304 TYR B CG    1 
ATOM   5137 C CD1   . TYR B 2 286 ? 32.043 10.246  57.181 1.00 36.09  ?  304 TYR B CD1   1 
ATOM   5138 C CD2   . TYR B 2 286 ? 31.118 9.892   59.355 1.00 39.42  ?  304 TYR B CD2   1 
ATOM   5139 C CE1   . TYR B 2 286 ? 31.892 11.621  57.349 1.00 37.42  ?  304 TYR B CE1   1 
ATOM   5140 C CE2   . TYR B 2 286 ? 30.971 11.279  59.530 1.00 36.70  ?  304 TYR B CE2   1 
ATOM   5141 C CZ    . TYR B 2 286 ? 31.357 12.131  58.520 1.00 38.43  ?  304 TYR B CZ    1 
ATOM   5142 O OH    . TYR B 2 286 ? 31.224 13.499  58.666 1.00 44.23  ?  304 TYR B OH    1 
ATOM   5143 N N     . HIS B 2 287 ? 31.256 5.139   56.418 1.00 30.18  ?  305 HIS B N     1 
ATOM   5144 C CA    . HIS B 2 287 ? 31.248 3.698   56.616 1.00 29.88  ?  305 HIS B CA    1 
ATOM   5145 C C     . HIS B 2 287 ? 29.941 3.162   56.057 1.00 30.05  ?  305 HIS B C     1 
ATOM   5146 O O     . HIS B 2 287 ? 28.908 3.832   56.144 1.00 28.24  ?  305 HIS B O     1 
ATOM   5147 C CB    . HIS B 2 287 ? 31.341 3.316   58.103 1.00 29.27  ?  305 HIS B CB    1 
ATOM   5148 C CG    . HIS B 2 287 ? 32.694 3.518   58.698 1.00 31.16  ?  305 HIS B CG    1 
ATOM   5149 N ND1   . HIS B 2 287 ? 33.770 2.714   58.389 1.00 28.90  ?  305 HIS B ND1   1 
ATOM   5150 C CD2   . HIS B 2 287 ? 33.151 4.437   59.578 1.00 29.91  ?  305 HIS B CD2   1 
ATOM   5151 C CE1   . HIS B 2 287 ? 34.827 3.119   59.065 1.00 23.73  ?  305 HIS B CE1   1 
ATOM   5152 N NE2   . HIS B 2 287 ? 34.479 4.165   59.788 1.00 28.23  ?  305 HIS B NE2   1 
ATOM   5153 N N     . SER B 2 288 ? 29.989 1.942   55.514 1.00 25.81  ?  306 SER B N     1 
ATOM   5154 C CA    . SER B 2 288 ? 28.780 1.219   55.160 1.00 28.56  ?  306 SER B CA    1 
ATOM   5155 C C     . SER B 2 288 ? 28.179 0.567   56.410 1.00 30.46  ?  306 SER B C     1 
ATOM   5156 O O     . SER B 2 288 ? 28.778 0.575   57.483 1.00 34.23  ?  306 SER B O     1 
ATOM   5157 C CB    . SER B 2 288 ? 29.080 0.174   54.083 1.00 31.63  ?  306 SER B CB    1 
ATOM   5158 O OG    . SER B 2 288 ? 30.141 -0.687  54.476 1.00 31.02  ?  306 SER B OG    1 
ATOM   5159 N N     . TYR B 2 289 ? 26.996 -0.036  56.254 1.00 29.60  ?  307 TYR B N     1 
ATOM   5160 C CA    . TYR B 2 289 ? 26.232 -0.545  57.392 1.00 31.58  ?  307 TYR B CA    1 
ATOM   5161 C C     . TYR B 2 289 ? 27.030 -1.532  58.243 1.00 33.34  ?  307 TYR B C     1 
ATOM   5162 O O     . TYR B 2 289 ? 27.213 -1.328  59.447 1.00 30.61  ?  307 TYR B O     1 
ATOM   5163 C CB    . TYR B 2 289 ? 24.960 -1.200  56.883 1.00 32.61  ?  307 TYR B CB    1 
ATOM   5164 C CG    . TYR B 2 289 ? 24.084 -1.823  57.942 1.00 34.76  ?  307 TYR B CG    1 
ATOM   5165 C CD1   . TYR B 2 289 ? 23.103 -1.083  58.584 1.00 32.30  ?  307 TYR B CD1   1 
ATOM   5166 C CD2   . TYR B 2 289 ? 24.198 -3.169  58.261 1.00 34.29  ?  307 TYR B CD2   1 
ATOM   5167 C CE1   . TYR B 2 289 ? 22.273 -1.671  59.535 1.00 35.80  ?  307 TYR B CE1   1 
ATOM   5168 C CE2   . TYR B 2 289 ? 23.374 -3.755  59.211 1.00 32.07  ?  307 TYR B CE2   1 
ATOM   5169 C CZ    . TYR B 2 289 ? 22.414 -3.010  59.845 1.00 33.37  ?  307 TYR B CZ    1 
ATOM   5170 O OH    . TYR B 2 289 ? 21.590 -3.606  60.788 1.00 35.78  ?  307 TYR B OH    1 
ATOM   5171 N N     . SER B 2 290 ? 27.484 -2.629  57.639 1.00 33.65  ?  308 SER B N     1 
ATOM   5172 C CA    . SER B 2 290 ? 28.204 -3.648  58.393 1.00 31.18  ?  308 SER B CA    1 
ATOM   5173 C C     . SER B 2 290 ? 29.523 -3.140  58.966 1.00 31.63  ?  308 SER B C     1 
ATOM   5174 O O     . SER B 2 290 ? 30.006 -3.684  59.954 1.00 28.40  ?  308 SER B O     1 
ATOM   5175 C CB    . SER B 2 290 ? 28.460 -4.835  57.493 1.00 32.06  ?  308 SER B CB    1 
ATOM   5176 O OG    . SER B 2 290 ? 27.222 -5.388  57.135 1.00 40.65  ?  308 SER B OG    1 
ATOM   5177 N N     . GLU B 2 291 ? 30.134 -2.119  58.377 1.00 34.17  ?  309 GLU B N     1 
ATOM   5178 C CA    . GLU B 2 291 ? 31.383 -1.665  58.962 1.00 33.45  ?  309 GLU B CA    1 
ATOM   5179 C C     . GLU B 2 291 ? 31.150 -1.064  60.334 1.00 33.55  ?  309 GLU B C     1 
ATOM   5180 O O     . GLU B 2 291 ? 32.100 -0.947  61.119 1.00 32.69  ?  309 GLU B O     1 
ATOM   5181 C CB    . GLU B 2 291 ? 32.081 -0.657  58.058 1.00 30.07  ?  309 GLU B CB    1 
ATOM   5182 C CG    . GLU B 2 291 ? 32.496 -1.215  56.727 1.00 27.07  ?  309 GLU B CG    1 
ATOM   5183 C CD    . GLU B 2 291 ? 33.346 -0.228  55.940 1.00 30.34  ?  309 GLU B CD    1 
ATOM   5184 O OE1   . GLU B 2 291 ? 33.269 1.004   56.204 1.00 28.27  ?  309 GLU B OE1   1 
ATOM   5185 O OE2   . GLU B 2 291 ? 34.102 -0.690  55.052 1.00 31.93  -1 309 GLU B OE2   1 
ATOM   5186 N N     . VAL B 2 292 ? 29.914 -0.692  60.638 1.00 30.58  ?  310 VAL B N     1 
ATOM   5187 C CA    . VAL B 2 292 ? 29.541 -0.181  61.952 1.00 31.65  ?  310 VAL B CA    1 
ATOM   5188 C C     . VAL B 2 292 ? 28.928 -1.270  62.828 1.00 34.66  ?  310 VAL B C     1 
ATOM   5189 O O     . VAL B 2 292 ? 29.276 -1.405  64.004 1.00 38.35  ?  310 VAL B O     1 
ATOM   5190 C CB    . VAL B 2 292 ? 28.557 0.988   61.778 1.00 27.64  ?  310 VAL B CB    1 
ATOM   5191 C CG1   . VAL B 2 292 ? 27.938 1.356   63.103 1.00 21.89  ?  310 VAL B CG1   1 
ATOM   5192 C CG2   . VAL B 2 292 ? 29.221 2.118   61.048 1.00 29.89  ?  310 VAL B CG2   1 
ATOM   5193 N N     . VAL B 2 293 ? 27.994 -2.044  62.264 1.00 29.95  ?  311 VAL B N     1 
ATOM   5194 C CA    . VAL B 2 293 ? 27.167 -2.932  63.057 1.00 31.57  ?  311 VAL B CA    1 
ATOM   5195 C C     . VAL B 2 293 ? 27.973 -4.118  63.540 1.00 34.26  ?  311 VAL B C     1 
ATOM   5196 O O     . VAL B 2 293 ? 27.687 -4.676  64.605 1.00 31.73  ?  311 VAL B O     1 
ATOM   5197 C CB    . VAL B 2 293 ? 25.943 -3.388  62.250 1.00 33.91  ?  311 VAL B CB    1 
ATOM   5198 C CG1   . VAL B 2 293 ? 25.248 -4.523  62.980 1.00 31.88  ?  311 VAL B CG1   1 
ATOM   5199 C CG2   . VAL B 2 293 ? 24.981 -2.222  62.021 1.00 30.80  ?  311 VAL B CG2   1 
ATOM   5200 N N     . ASP B 2 294 ? 28.991 -4.519  62.781 1.00 30.77  ?  312 ASP B N     1 
ATOM   5201 C CA    . ASP B 2 294 ? 29.816 -5.650  63.173 1.00 31.78  ?  312 ASP B CA    1 
ATOM   5202 C C     . ASP B 2 294 ? 30.868 -5.304  64.214 1.00 32.68  ?  312 ASP B C     1 
ATOM   5203 O O     . ASP B 2 294 ? 31.487 -6.220  64.751 1.00 36.03  ?  312 ASP B O     1 
ATOM   5204 C CB    . ASP B 2 294 ? 30.487 -6.278  61.951 1.00 30.36  ?  312 ASP B CB    1 
ATOM   5205 C CG    . ASP B 2 294 ? 29.503 -7.074  61.090 1.00 34.73  ?  312 ASP B CG    1 
ATOM   5206 O OD1   . ASP B 2 294 ? 28.388 -7.395  61.580 1.00 38.36  ?  312 ASP B OD1   1 
ATOM   5207 O OD2   . ASP B 2 294 ? 29.826 -7.361  59.912 1.00 35.00  -1 312 ASP B OD2   1 
ATOM   5208 N N     . VAL B 2 295 ? 31.092 -4.035  64.538 1.00 32.88  ?  313 VAL B N     1 
ATOM   5209 C CA    . VAL B 2 295 ? 31.808 -3.776  65.782 1.00 36.32  ?  313 VAL B CA    1 
ATOM   5210 C C     . VAL B 2 295 ? 30.821 -3.653  66.942 1.00 34.08  ?  313 VAL B C     1 
ATOM   5211 O O     . VAL B 2 295 ? 31.132 -4.054  68.068 1.00 33.81  ?  313 VAL B O     1 
ATOM   5212 C CB    . VAL B 2 295 ? 32.755 -2.551  65.681 1.00 34.55  ?  313 VAL B CB    1 
ATOM   5213 C CG1   . VAL B 2 295 ? 33.097 -2.232  64.226 1.00 29.63  ?  313 VAL B CG1   1 
ATOM   5214 C CG2   . VAL B 2 295 ? 32.207 -1.352  66.393 1.00 35.08  ?  313 VAL B CG2   1 
ATOM   5215 N N     . LEU B 2 296 ? 29.606 -3.186  66.675 1.00 35.06  ?  314 LEU B N     1 
ATOM   5216 C CA    . LEU B 2 296 ? 28.610 -3.092  67.735 1.00 33.58  ?  314 LEU B CA    1 
ATOM   5217 C C     . LEU B 2 296 ? 28.189 -4.469  68.256 1.00 35.43  ?  314 LEU B C     1 
ATOM   5218 O O     . LEU B 2 296 ? 27.892 -4.621  69.441 1.00 40.40  ?  314 LEU B O     1 
ATOM   5219 C CB    . LEU B 2 296 ? 27.402 -2.333  67.215 1.00 33.38  ?  314 LEU B CB    1 
ATOM   5220 C CG    . LEU B 2 296 ? 27.238 -0.897  67.676 1.00 34.05  ?  314 LEU B CG    1 
ATOM   5221 C CD1   . LEU B 2 296 ? 26.012 -0.352  66.996 1.00 32.66  ?  314 LEU B CD1   1 
ATOM   5222 C CD2   . LEU B 2 296 ? 27.083 -0.849  69.165 1.00 31.31  ?  314 LEU B CD2   1 
ATOM   5223 N N     . THR B 2 297 ? 28.123 -5.478  67.399 1.00 34.71  ?  315 THR B N     1 
ATOM   5224 C CA    . THR B 2 297 ? 27.558 -6.754  67.822 1.00 36.02  ?  315 THR B CA    1 
ATOM   5225 C C     . THR B 2 297 ? 28.577 -7.661  68.497 1.00 40.84  ?  315 THR B C     1 
ATOM   5226 O O     . THR B 2 297 ? 28.223 -8.792  68.857 1.00 41.45  ?  315 THR B O     1 
ATOM   5227 C CB    . THR B 2 297 ? 26.951 -7.522  66.638 1.00 33.49  ?  315 THR B CB    1 
ATOM   5228 O OG1   . THR B 2 297 ? 27.933 -7.652  65.594 1.00 38.23  ?  315 THR B OG1   1 
ATOM   5229 C CG2   . THR B 2 297 ? 25.717 -6.823  66.093 1.00 31.38  ?  315 THR B CG2   1 
ATOM   5230 N N     . GLU B 2 298 ? 29.824 -7.230  68.654 1.00 35.57  ?  316 GLU B N     1 
ATOM   5231 C CA    . GLU B 2 298 ? 30.789 -8.106  69.286 1.00 35.01  ?  316 GLU B CA    1 
ATOM   5232 C C     . GLU B 2 298 ? 30.365 -8.359  70.729 1.00 33.30  ?  316 GLU B C     1 
ATOM   5233 O O     . GLU B 2 298 ? 29.942 -7.427  71.420 1.00 32.45  ?  316 GLU B O     1 
ATOM   5234 C CB    . GLU B 2 298 ? 32.199 -7.512  69.235 1.00 38.06  ?  316 GLU B CB    1 
ATOM   5235 C CG    . GLU B 2 298 ? 33.326 -8.551  69.163 1.00 37.55  ?  316 GLU B CG    1 
ATOM   5236 C CD    . GLU B 2 298 ? 34.717 -7.924  69.105 1.00 40.39  ?  316 GLU B CD    1 
ATOM   5237 O OE1   . GLU B 2 298 ? 34.830 -6.717  68.804 1.00 43.52  ?  316 GLU B OE1   1 
ATOM   5238 O OE2   . GLU B 2 298 ? 35.719 -8.635  69.350 1.00 44.29  -1 316 GLU B OE2   1 
ATOM   5239 N N     . PRO B 2 299 ? 30.506 -9.594  71.220 1.00 31.95  ?  317 PRO B N     1 
ATOM   5240 C CA    . PRO B 2 299 ? 29.817 -9.989  72.456 1.00 32.18  ?  317 PRO B CA    1 
ATOM   5241 C C     . PRO B 2 299 ? 30.269 -9.245  73.706 1.00 36.94  ?  317 PRO B C     1 
ATOM   5242 O O     . PRO B 2 299 ? 29.498 -9.198  74.669 1.00 39.64  ?  317 PRO B O     1 
ATOM   5243 C CB    . PRO B 2 299 ? 30.121 -11.489 72.556 1.00 34.55  ?  317 PRO B CB    1 
ATOM   5244 C CG    . PRO B 2 299 ? 30.558 -11.880 71.194 1.00 30.37  ?  317 PRO B CG    1 
ATOM   5245 C CD    . PRO B 2 299 ? 31.242 -10.717 70.618 1.00 30.30  ?  317 PRO B CD    1 
ATOM   5246 N N     . PHE B 2 300 ? 31.476 -8.665  73.729 1.00 34.89  ?  318 PHE B N     1 
ATOM   5247 C CA    . PHE B 2 300 ? 31.900 -7.879  74.878 1.00 32.08  ?  318 PHE B CA    1 
ATOM   5248 C C     . PHE B 2 300 ? 31.233 -6.509  74.917 1.00 38.01  ?  318 PHE B C     1 
ATOM   5249 O O     . PHE B 2 300 ? 31.004 -5.975  76.011 1.00 39.92  ?  318 PHE B O     1 
ATOM   5250 C CB    . PHE B 2 300 ? 33.422 -7.754  74.904 1.00 31.16  ?  318 PHE B CB    1 
ATOM   5251 C CG    . PHE B 2 300 ? 33.970 -6.615  74.090 1.00 36.92  ?  318 PHE B CG    1 
ATOM   5252 C CD1   . PHE B 2 300 ? 34.117 -6.730  72.713 1.00 38.60  ?  318 PHE B CD1   1 
ATOM   5253 C CD2   . PHE B 2 300 ? 34.384 -5.446  74.699 1.00 35.43  ?  318 PHE B CD2   1 
ATOM   5254 C CE1   . PHE B 2 300 ? 34.652 -5.697  71.972 1.00 36.19  ?  318 PHE B CE1   1 
ATOM   5255 C CE2   . PHE B 2 300 ? 34.907 -4.411  73.956 1.00 34.67  ?  318 PHE B CE2   1 
ATOM   5256 C CZ    . PHE B 2 300 ? 35.036 -4.534  72.596 1.00 35.25  ?  318 PHE B CZ    1 
ATOM   5257 N N     . LEU B 2 301 ? 30.906 -5.927  73.756 1.00 37.19  ?  319 LEU B N     1 
ATOM   5258 C CA    . LEU B 2 301 ? 30.022 -4.765  73.736 1.00 39.17  ?  319 LEU B CA    1 
ATOM   5259 C C     . LEU B 2 301 ? 28.571 -5.156  73.986 1.00 41.99  ?  319 LEU B C     1 
ATOM   5260 O O     . LEU B 2 301 ? 27.813 -4.369  74.571 1.00 38.48  ?  319 LEU B O     1 
ATOM   5261 C CB    . LEU B 2 301 ? 30.124 -4.030  72.399 1.00 38.35  ?  319 LEU B CB    1 
ATOM   5262 C CG    . LEU B 2 301 ? 31.337 -3.130  72.273 1.00 37.84  ?  319 LEU B CG    1 
ATOM   5263 C CD1   . LEU B 2 301 ? 31.517 -2.739  70.822 1.00 34.36  ?  319 LEU B CD1   1 
ATOM   5264 C CD2   . LEU B 2 301 ? 31.109 -1.928  73.145 1.00 34.96  ?  319 LEU B CD2   1 
ATOM   5265 N N     . GLN B 2 302 ? 28.167 -6.355  73.552 1.00 37.40  ?  320 GLN B N     1 
ATOM   5266 C CA    . GLN B 2 302 ? 26.782 -6.764  73.739 1.00 42.09  ?  320 GLN B CA    1 
ATOM   5267 C C     . GLN B 2 302 ? 26.444 -6.938  75.216 1.00 44.24  ?  320 GLN B C     1 
ATOM   5268 O O     . GLN B 2 302 ? 25.315 -6.647  75.626 1.00 43.16  ?  320 GLN B O     1 
ATOM   5269 C CB    . GLN B 2 302 ? 26.498 -8.049  72.957 1.00 41.73  ?  320 GLN B CB    1 
ATOM   5270 C CG    . GLN B 2 302 ? 25.015 -8.309  72.670 1.00 47.79  ?  320 GLN B CG    1 
ATOM   5271 C CD    . GLN B 2 302 ? 24.313 -7.134  71.997 1.00 54.93  ?  320 GLN B CD    1 
ATOM   5272 O OE1   . GLN B 2 302 ? 24.969 -6.246  71.409 1.00 50.38  ?  320 GLN B OE1   1 
ATOM   5273 N NE2   . GLN B 2 302 ? 22.968 -7.112  72.088 1.00 50.29  ?  320 GLN B NE2   1 
ATOM   5274 N N     . SER B 2 303 ? 27.400 -7.392  76.033 1.00 43.67  ?  321 SER B N     1 
ATOM   5275 C CA    . SER B 2 303 ? 27.172 -7.425  77.474 1.00 43.70  ?  321 SER B CA    1 
ATOM   5276 C C     . SER B 2 303 ? 26.632 -6.094  77.953 1.00 44.71  ?  321 SER B C     1 
ATOM   5277 O O     . SER B 2 303 ? 25.633 -6.034  78.681 1.00 46.76  ?  321 SER B O     1 
ATOM   5278 C CB    . SER B 2 303 ? 28.457 -7.750  78.235 1.00 37.45  ?  321 SER B CB    1 
ATOM   5279 O OG    . SER B 2 303 ? 29.075 -8.909  77.739 1.00 40.09  ?  321 SER B OG    1 
ATOM   5280 N N     . ILE B 2 304 ? 27.295 -5.013  77.554 1.00 39.25  ?  322 ILE B N     1 
ATOM   5281 C CA    . ILE B 2 304 ? 26.988 -3.714  78.129 1.00 39.35  ?  322 ILE B CA    1 
ATOM   5282 C C     . ILE B 2 304 ? 25.493 -3.472  78.081 1.00 41.67  ?  322 ILE B C     1 
ATOM   5283 O O     . ILE B 2 304 ? 24.892 -3.061  79.081 1.00 45.39  ?  322 ILE B O     1 
ATOM   5284 C CB    . ILE B 2 304 ? 27.791 -2.618  77.407 1.00 37.71  ?  322 ILE B CB    1 
ATOM   5285 C CG1   . ILE B 2 304 ? 29.277 -2.992  77.376 1.00 35.11  ?  322 ILE B CG1   1 
ATOM   5286 C CG2   . ILE B 2 304 ? 27.579 -1.296  78.059 1.00 34.50  ?  322 ILE B CG2   1 
ATOM   5287 C CD1   . ILE B 2 304 ? 30.186 -1.896  76.904 1.00 33.07  ?  322 ILE B CD1   1 
ATOM   5288 N N     . PHE B 2 305 ? 24.861 -3.812  76.941 1.00 42.72  ?  323 PHE B N     1 
ATOM   5289 C CA    . PHE B 2 305 ? 23.423 -3.654  76.708 1.00 43.15  ?  323 PHE B CA    1 
ATOM   5290 C C     . PHE B 2 305 ? 22.613 -4.737  77.410 1.00 45.16  ?  323 PHE B C     1 
ATOM   5291 O O     . PHE B 2 305 ? 21.588 -4.455  78.043 1.00 43.90  ?  323 PHE B O     1 
ATOM   5292 C CB    . PHE B 2 305 ? 23.118 -3.696  75.201 1.00 43.55  ?  323 PHE B CB    1 
ATOM   5293 C CG    . PHE B 2 305 ? 23.689 -2.550  74.443 1.00 42.19  ?  323 PHE B CG    1 
ATOM   5294 C CD1   . PHE B 2 305 ? 24.663 -2.759  73.484 1.00 42.25  ?  323 PHE B CD1   1 
ATOM   5295 C CD2   . PHE B 2 305 ? 23.276 -1.245  74.715 1.00 45.96  ?  323 PHE B CD2   1 
ATOM   5296 C CE1   . PHE B 2 305 ? 25.223 -1.686  72.800 1.00 44.68  ?  323 PHE B CE1   1 
ATOM   5297 C CE2   . PHE B 2 305 ? 23.820 -0.161  74.030 1.00 39.99  ?  323 PHE B CE2   1 
ATOM   5298 C CZ    . PHE B 2 305 ? 24.801 -0.387  73.070 1.00 41.45  ?  323 PHE B CZ    1 
ATOM   5299 N N     . ASP B 2 306 ? 23.044 -5.988  77.274 1.00 44.79  ?  324 ASP B N     1 
ATOM   5300 C CA    . ASP B 2 306 ? 22.276 -7.095  77.819 1.00 44.96  ?  324 ASP B CA    1 
ATOM   5301 C C     . ASP B 2 306 ? 22.115 -6.948  79.324 1.00 49.92  ?  324 ASP B C     1 
ATOM   5302 O O     . ASP B 2 306 ? 20.994 -7.023  79.850 1.00 52.39  ?  324 ASP B O     1 
ATOM   5303 C CB    . ASP B 2 306 ? 22.957 -8.403  77.429 1.00 44.47  ?  324 ASP B CB    1 
ATOM   5304 C CG    . ASP B 2 306 ? 22.708 -8.754  75.949 1.00 58.23  ?  324 ASP B CG    1 
ATOM   5305 O OD1   . ASP B 2 306 ? 21.869 -8.048  75.300 1.00 62.76  ?  324 ASP B OD1   1 
ATOM   5306 O OD2   . ASP B 2 306 ? 23.355 -9.699  75.422 1.00 60.39  -1 324 ASP B OD2   1 
ATOM   5307 N N     . LYS B 2 307 ? 23.221 -6.679  80.028 1.00 47.70  ?  325 LYS B N     1 
ATOM   5308 C CA    . LYS B 2 307 ? 23.177 -6.455  81.472 1.00 46.84  ?  325 LYS B CA    1 
ATOM   5309 C C     . LYS B 2 307 ? 22.318 -5.262  81.867 1.00 43.17  ?  325 LYS B C     1 
ATOM   5310 O O     . LYS B 2 307 ? 21.994 -5.132  83.051 1.00 45.55  ?  325 LYS B O     1 
ATOM   5311 C CB    . LYS B 2 307 ? 24.602 -6.270  82.029 1.00 52.45  ?  325 LYS B CB    1 
ATOM   5312 C CG    . LYS B 2 307 ? 25.383 -7.587  82.208 1.00 56.49  ?  325 LYS B CG    1 
ATOM   5313 C CD    . LYS B 2 307 ? 26.909 -7.396  82.272 1.00 59.55  ?  325 LYS B CD    1 
ATOM   5314 C CE    . LYS B 2 307 ? 27.407 -6.258  81.354 1.00 62.07  ?  325 LYS B CE    1 
ATOM   5315 N NZ    . LYS B 2 307 ? 28.861 -6.371  80.922 1.00 56.63  ?  325 LYS B NZ    1 
ATOM   5316 N N     . ALA B 2 308 ? 21.957 -4.383  80.930 1.00 42.19  ?  326 ALA B N     1 
ATOM   5317 C CA    . ALA B 2 308 ? 21.060 -3.267  81.215 1.00 36.69  ?  326 ALA B CA    1 
ATOM   5318 C C     . ALA B 2 308 ? 19.686 -3.448  80.593 1.00 40.18  ?  326 ALA B C     1 
ATOM   5319 O O     . ALA B 2 308 ? 18.879 -2.517  80.626 1.00 36.41  ?  326 ALA B O     1 
ATOM   5320 C CB    . ALA B 2 308 ? 21.668 -1.952  80.742 1.00 31.43  ?  326 ALA B CB    1 
ATOM   5321 N N     . ASN B 2 309 ? 19.410 -4.621  80.008 1.00 46.19  ?  327 ASN B N     1 
ATOM   5322 C CA    . ASN B 2 309 ? 18.083 -4.978  79.474 1.00 47.30  ?  327 ASN B CA    1 
ATOM   5323 C C     . ASN B 2 309 ? 17.743 -4.210  78.203 1.00 44.91  ?  327 ASN B C     1 
ATOM   5324 O O     . ASN B 2 309 ? 16.592 -3.819  77.988 1.00 44.36  ?  327 ASN B O     1 
ATOM   5325 C CB    . ASN B 2 309 ? 16.985 -4.776  80.514 1.00 47.84  ?  327 ASN B CB    1 
ATOM   5326 C CG    . ASN B 2 309 ? 16.933 -5.898  81.515 1.00 60.12  ?  327 ASN B CG    1 
ATOM   5327 O OD1   . ASN B 2 309 ? 16.901 -5.655  82.733 1.00 60.75  ?  327 ASN B OD1   1 
ATOM   5328 N ND2   . ASN B 2 309 ? 16.945 -7.151  81.015 1.00 60.64  ?  327 ASN B ND2   1 
ATOM   5329 N N     . ILE B 2 310 ? 18.738 -3.999  77.351 1.00 41.04  ?  328 ILE B N     1 
ATOM   5330 C CA    . ILE B 2 310 ? 18.552 -3.275  76.106 1.00 41.70  ?  328 ILE B CA    1 
ATOM   5331 C C     . ILE B 2 310 ? 18.725 -4.242  74.947 1.00 40.16  ?  328 ILE B C     1 
ATOM   5332 O O     . ILE B 2 310 ? 19.728 -4.971  74.870 1.00 40.38  ?  328 ILE B O     1 
ATOM   5333 C CB    . ILE B 2 310 ? 19.517 -2.086  76.001 1.00 41.81  ?  328 ILE B CB    1 
ATOM   5334 C CG1   . ILE B 2 310 ? 19.442 -1.265  77.297 1.00 35.36  ?  328 ILE B CG1   1 
ATOM   5335 C CG2   . ILE B 2 310 ? 19.184 -1.260  74.745 1.00 37.45  ?  328 ILE B CG2   1 
ATOM   5336 C CD1   . ILE B 2 310 ? 19.833 0.190   77.144 1.00 34.38  ?  328 ILE B CD1   1 
ATOM   5337 N N     . LYS B 2 311 ? 17.731 -4.277  74.065 1.00 36.25  ?  329 LYS B N     1 
ATOM   5338 C CA    . LYS B 2 311 ? 17.819 -5.076  72.857 1.00 39.09  ?  329 LYS B CA    1 
ATOM   5339 C C     . LYS B 2 311 ? 17.856 -4.116  71.686 1.00 36.75  ?  329 LYS B C     1 
ATOM   5340 O O     . LYS B 2 311 ? 16.937 -3.303  71.528 1.00 35.55  ?  329 LYS B O     1 
ATOM   5341 C CB    . LYS B 2 311 ? 16.663 -6.067  72.733 1.00 41.35  ?  329 LYS B CB    1 
ATOM   5342 C CG    . LYS B 2 311 ? 17.057 -7.278  71.880 1.00 42.61  ?  329 LYS B CG    1 
ATOM   5343 C CD    . LYS B 2 311 ? 15.850 -8.060  71.371 1.00 49.86  ?  329 LYS B CD    1 
ATOM   5344 C CE    . LYS B 2 311 ? 16.137 -8.816  70.057 1.00 49.53  ?  329 LYS B CE    1 
ATOM   5345 N NZ    . LYS B 2 311 ? 15.866 -8.018  68.827 1.00 52.37  ?  329 LYS B NZ    1 
ATOM   5346 N N     . LEU B 2 312 ? 18.934 -4.186  70.900 1.00 32.43  ?  330 LEU B N     1 
ATOM   5347 C CA    . LEU B 2 312 ? 19.152 -3.266  69.784 1.00 36.21  ?  330 LEU B CA    1 
ATOM   5348 C C     . LEU B 2 312 ? 18.479 -3.800  68.524 1.00 35.22  ?  330 LEU B C     1 
ATOM   5349 O O     . LEU B 2 312 ? 18.631 -4.979  68.191 1.00 37.51  ?  330 LEU B O     1 
ATOM   5350 C CB    . LEU B 2 312 ? 20.649 -3.064  69.533 1.00 33.61  ?  330 LEU B CB    1 
ATOM   5351 C CG    . LEU B 2 312 ? 21.306 -1.861  70.212 1.00 34.04  ?  330 LEU B CG    1 
ATOM   5352 C CD1   . LEU B 2 312 ? 20.436 -1.386  71.359 1.00 34.51  ?  330 LEU B CD1   1 
ATOM   5353 C CD2   . LEU B 2 312 ? 22.708 -2.168  70.695 1.00 29.52  ?  330 LEU B CD2   1 
ATOM   5354 N N     . ASN B 2 313 ? 17.712 -2.948  67.837 1.00 35.38  ?  331 ASN B N     1 
ATOM   5355 C CA    . ASN B 2 313 ? 17.137 -3.399  66.578 1.00 32.95  ?  331 ASN B CA    1 
ATOM   5356 C C     . ASN B 2 313 ? 18.079 -3.171  65.405 1.00 33.70  ?  331 ASN B C     1 
ATOM   5357 O O     . ASN B 2 313 ? 17.876 -3.779  64.351 1.00 34.77  ?  331 ASN B O     1 
ATOM   5358 C CB    . ASN B 2 313 ? 15.762 -2.753  66.304 1.00 29.73  ?  331 ASN B CB    1 
ATOM   5359 C CG    . ASN B 2 313 ? 15.752 -1.233  66.445 1.00 35.94  ?  331 ASN B CG    1 
ATOM   5360 O OD1   . ASN B 2 313 ? 16.387 -0.506  65.670 1.00 37.03  ?  331 ASN B OD1   1 
ATOM   5361 N ND2   . ASN B 2 313 ? 14.987 -0.742  67.420 1.00 38.22  ?  331 ASN B ND2   1 
ATOM   5362 N N     . TYR B 2 314 ? 19.120 -2.350  65.575 1.00 32.85  ?  332 TYR B N     1 
ATOM   5363 C CA    . TYR B 2 314 ? 20.162 -2.182  64.570 1.00 33.83  ?  332 TYR B CA    1 
ATOM   5364 C C     . TYR B 2 314 ? 19.623 -1.499  63.323 1.00 32.57  ?  332 TYR B C     1 
ATOM   5365 O O     . TYR B 2 314 ? 20.127 -1.700  62.214 1.00 26.02  ?  332 TYR B O     1 
ATOM   5366 C CB    . TYR B 2 314 ? 20.816 -3.531  64.220 1.00 35.64  ?  332 TYR B CB    1 
ATOM   5367 C CG    . TYR B 2 314 ? 21.527 -4.135  65.413 1.00 35.80  ?  332 TYR B CG    1 
ATOM   5368 C CD1   . TYR B 2 314 ? 21.227 -5.414  65.875 1.00 35.06  ?  332 TYR B CD1   1 
ATOM   5369 C CD2   . TYR B 2 314 ? 22.467 -3.392  66.113 1.00 33.71  ?  332 TYR B CD2   1 
ATOM   5370 C CE1   . TYR B 2 314 ? 21.876 -5.936  66.989 1.00 35.46  ?  332 TYR B CE1   1 
ATOM   5371 C CE2   . TYR B 2 314 ? 23.117 -3.902  67.216 1.00 34.58  ?  332 TYR B CE2   1 
ATOM   5372 C CZ    . TYR B 2 314 ? 22.824 -5.167  67.656 1.00 38.39  ?  332 TYR B CZ    1 
ATOM   5373 O OH    . TYR B 2 314 ? 23.500 -5.629  68.770 1.00 43.98  ?  332 TYR B OH    1 
ATOM   5374 N N     . GLY B 2 315 ? 18.588 -0.690  63.505 1.00 33.02  ?  333 GLY B N     1 
ATOM   5375 C CA    . GLY B 2 315 ? 17.973 -0.053  62.374 1.00 32.70  ?  333 GLY B CA    1 
ATOM   5376 C C     . GLY B 2 315 ? 17.296 -1.007  61.418 1.00 38.53  ?  333 GLY B C     1 
ATOM   5377 O O     . GLY B 2 315 ? 17.016 -0.619  60.283 1.00 40.56  ?  333 GLY B O     1 
ATOM   5378 N N     . VAL B 2 316 ? 17.008 -2.245  61.832 1.00 34.43  ?  334 VAL B N     1 
ATOM   5379 C CA    . VAL B 2 316 ? 16.188 -3.119  61.000 1.00 37.02  ?  334 VAL B CA    1 
ATOM   5380 C C     . VAL B 2 316 ? 14.763 -2.572  60.946 1.00 41.67  ?  334 VAL B C     1 
ATOM   5381 O O     . VAL B 2 316 ? 14.143 -2.270  61.979 1.00 38.35  ?  334 VAL B O     1 
ATOM   5382 C CB    . VAL B 2 316 ? 16.218 -4.561  61.520 1.00 34.51  ?  334 VAL B CB    1 
ATOM   5383 C CG1   . VAL B 2 316 ? 15.380 -5.434  60.640 1.00 33.53  ?  334 VAL B CG1   1 
ATOM   5384 C CG2   . VAL B 2 316 ? 17.620 -5.075  61.555 1.00 33.18  ?  334 VAL B CG2   1 
ATOM   5385 N N     . LEU B 2 317 ? 14.246 -2.420  59.735 1.00 45.84  ?  335 LEU B N     1 
ATOM   5386 C CA    . LEU B 2 317 ? 12.996 -1.721  59.485 1.00 48.74  ?  335 LEU B CA    1 
ATOM   5387 C C     . LEU B 2 317 ? 11.898 -2.694  59.081 1.00 54.92  ?  335 LEU B C     1 
ATOM   5388 O O     . LEU B 2 317 ? 12.149 -3.835  58.669 1.00 58.43  ?  335 LEU B O     1 
ATOM   5389 C CB    . LEU B 2 317 ? 13.167 -0.665  58.388 1.00 48.43  ?  335 LEU B CB    1 
ATOM   5390 C CG    . LEU B 2 317 ? 14.044 0.535   58.724 1.00 42.91  ?  335 LEU B CG    1 
ATOM   5391 C CD1   . LEU B 2 317 ? 14.108 1.469   57.526 1.00 43.58  ?  335 LEU B CD1   1 
ATOM   5392 C CD2   . LEU B 2 317 ? 13.521 1.259   59.944 1.00 37.89  ?  335 LEU B CD2   1 
ATOM   5393 N N     . ASP B 2 318 ? 10.667 -2.216  59.207 1.00 58.81  ?  336 ASP B N     1 
ATOM   5394 C CA    . ASP B 2 318 ? 9.492  -2.980  58.818 1.00 60.40  ?  336 ASP B CA    1 
ATOM   5395 C C     . ASP B 2 318 ? 9.657  -3.504  57.400 1.00 60.42  ?  336 ASP B C     1 
ATOM   5396 O O     . ASP B 2 318 ? 9.766  -4.718  57.200 1.00 61.17  ?  336 ASP B O     1 
ATOM   5397 C CB    . ASP B 2 318 ? 8.271  -2.091  58.972 1.00 60.55  ?  336 ASP B CB    1 
ATOM   5398 C CG    . ASP B 2 318 ? 8.566  -0.895  59.861 1.00 71.46  ?  336 ASP B CG    1 
ATOM   5399 O OD1   . ASP B 2 318 ? 8.130  -0.928  61.042 1.00 78.17  ?  336 ASP B OD1   1 
ATOM   5400 O OD2   . ASP B 2 318 ? 9.276  0.044   59.393 1.00 60.68  -1 336 ASP B OD2   1 
ATOM   5401 N N     . ASP B 2 319 ? 9.724  -2.606  56.415 1.00 56.64  ?  337 ASP B N     1 
ATOM   5402 C CA    . ASP B 2 319 ? 9.926  -3.012  55.033 1.00 56.11  ?  337 ASP B CA    1 
ATOM   5403 C C     . ASP B 2 319 ? 10.977 -2.136  54.378 1.00 53.48  ?  337 ASP B C     1 
ATOM   5404 O O     . ASP B 2 319 ? 11.161 -0.977  54.747 1.00 53.57  ?  337 ASP B O     1 
ATOM   5405 C CB    . ASP B 2 319 ? 8.634  -2.935  54.233 1.00 59.35  ?  337 ASP B CB    1 
ATOM   5406 C CG    . ASP B 2 319 ? 8.201  -1.516  53.983 1.00 56.11  ?  337 ASP B CG    1 
ATOM   5407 O OD1   . ASP B 2 319 ? 8.733  -0.870  53.046 1.00 55.49  ?  337 ASP B OD1   1 
ATOM   5408 O OD2   . ASP B 2 319 ? 7.348  -1.045  54.764 1.00 52.09  -1 337 ASP B OD2   1 
ATOM   5409 N N     . THR B 2 320 ? 11.657 -2.709  53.388 1.00 54.52  ?  338 THR B N     1 
ATOM   5410 C CA    . THR B 2 320 ? 12.635 -1.992  52.580 1.00 55.98  ?  338 THR B CA    1 
ATOM   5411 C C     . THR B 2 320 ? 12.187 -1.865  51.130 1.00 54.35  ?  338 THR B C     1 
ATOM   5412 O O     . THR B 2 320 ? 13.032 -1.735  50.239 1.00 52.36  ?  338 THR B O     1 
ATOM   5413 C CB    . THR B 2 320 ? 14.003 -2.686  52.612 1.00 52.59  ?  338 THR B CB    1 
ATOM   5414 O OG1   . THR B 2 320 ? 13.833 -4.117  52.695 1.00 56.23  ?  338 THR B OG1   1 
ATOM   5415 C CG2   . THR B 2 320 ? 14.855 -2.172  53.754 1.00 46.08  ?  338 THR B CG2   1 
ATOM   5416 N N     . HIS B 2 321 ? 10.876 -1.917  50.866 1.00 53.35  ?  339 HIS B N     1 
ATOM   5417 C CA    . HIS B 2 321 ? 10.440 -2.209  49.504 1.00 51.05  ?  339 HIS B CA    1 
ATOM   5418 C C     . HIS B 2 321 ? 10.880 -1.129  48.518 1.00 45.85  ?  339 HIS B C     1 
ATOM   5419 O O     . HIS B 2 321 ? 11.463 -1.439  47.477 1.00 42.04  ?  339 HIS B O     1 
ATOM   5420 C CB    . HIS B 2 321 ? 8.934  -2.416  49.432 1.00 55.05  ?  339 HIS B CB    1 
ATOM   5421 C CG    . HIS B 2 321 ? 8.493  -2.972  48.109 1.00 68.93  ?  339 HIS B CG    1 
ATOM   5422 N ND1   . HIS B 2 321 ? 8.567  -4.317  47.804 1.00 69.95  ?  339 HIS B ND1   1 
ATOM   5423 C CD2   . HIS B 2 321 ? 8.031  -2.359  46.990 1.00 67.22  ?  339 HIS B CD2   1 
ATOM   5424 C CE1   . HIS B 2 321 ? 8.137  -4.511  46.570 1.00 72.30  ?  339 HIS B CE1   1 
ATOM   5425 N NE2   . HIS B 2 321 ? 7.811  -3.339  46.051 1.00 72.50  ?  339 HIS B NE2   1 
ATOM   5426 N N     . ALA B 2 322 ? 10.611 0.143   48.825 1.00 45.98  ?  340 ALA B N     1 
ATOM   5427 C CA    . ALA B 2 322 ? 11.002 1.231   47.928 1.00 37.71  ?  340 ALA B CA    1 
ATOM   5428 C C     . ALA B 2 322 ? 12.477 1.159   47.568 1.00 43.13  ?  340 ALA B C     1 
ATOM   5429 O O     . ALA B 2 322 ? 12.852 1.257   46.391 1.00 44.11  ?  340 ALA B O     1 
ATOM   5430 C CB    . ALA B 2 322 ? 10.701 2.582   48.571 1.00 32.03  ?  340 ALA B CB    1 
ATOM   5431 N N     . GLU B 2 323 ? 13.337 1.033   48.583 1.00 41.49  ?  341 GLU B N     1 
ATOM   5432 C CA    . GLU B 2 323 ? 14.771 1.068   48.348 1.00 40.51  ?  341 GLU B CA    1 
ATOM   5433 C C     . GLU B 2 323 ? 15.242 -0.195  47.650 1.00 40.54  ?  341 GLU B C     1 
ATOM   5434 O O     . GLU B 2 323 ? 16.234 -0.160  46.917 1.00 40.24  ?  341 GLU B O     1 
ATOM   5435 C CB    . GLU B 2 323 ? 15.515 1.264   49.671 1.00 41.65  ?  341 GLU B CB    1 
ATOM   5436 C CG    . GLU B 2 323 ? 14.807 2.183   50.672 1.00 45.54  ?  341 GLU B CG    1 
ATOM   5437 C CD    . GLU B 2 323 ? 13.971 1.418   51.704 1.00 53.91  ?  341 GLU B CD    1 
ATOM   5438 O OE1   . GLU B 2 323 ? 12.715 1.520   51.660 1.00 55.45  ?  341 GLU B OE1   1 
ATOM   5439 O OE2   . GLU B 2 323 ? 14.566 0.714   52.556 1.00 52.74  -1 341 GLU B OE2   1 
ATOM   5440 N N     . PHE B 2 324 ? 14.544 -1.310  47.870 1.00 39.59  ?  342 PHE B N     1 
ATOM   5441 C CA    . PHE B 2 324 ? 14.842 -2.556  47.175 1.00 38.27  ?  342 PHE B CA    1 
ATOM   5442 C C     . PHE B 2 324 ? 14.423 -2.480  45.711 1.00 37.30  ?  342 PHE B C     1 
ATOM   5443 O O     . PHE B 2 324 ? 15.202 -2.807  44.813 1.00 36.03  ?  342 PHE B O     1 
ATOM   5444 C CB    . PHE B 2 324 ? 14.125 -3.696  47.887 1.00 40.47  ?  342 PHE B CB    1 
ATOM   5445 C CG    . PHE B 2 324 ? 14.562 -5.054  47.463 1.00 38.25  ?  342 PHE B CG    1 
ATOM   5446 C CD1   . PHE B 2 324 ? 13.766 -5.818  46.643 1.00 38.54  ?  342 PHE B CD1   1 
ATOM   5447 C CD2   . PHE B 2 324 ? 15.760 -5.579  47.909 1.00 37.05  ?  342 PHE B CD2   1 
ATOM   5448 C CE1   . PHE B 2 324 ? 14.157 -7.073  46.267 1.00 41.41  ?  342 PHE B CE1   1 
ATOM   5449 C CE2   . PHE B 2 324 ? 16.165 -6.837  47.545 1.00 34.55  ?  342 PHE B CE2   1 
ATOM   5450 C CZ    . PHE B 2 324 ? 15.364 -7.587  46.716 1.00 41.06  ?  342 PHE B CZ    1 
ATOM   5451 N N     . ARG B 2 325 ? 13.188 -2.045  45.459 1.00 40.76  ?  343 ARG B N     1 
ATOM   5452 C CA    . ARG B 2 325 ? 12.723 -1.749  44.106 1.00 42.91  ?  343 ARG B CA    1 
ATOM   5453 C C     . ARG B 2 325 ? 13.701 -0.847  43.360 1.00 45.90  ?  343 ARG B C     1 
ATOM   5454 O O     . ARG B 2 325 ? 14.138 -1.172  42.247 1.00 43.50  ?  343 ARG B O     1 
ATOM   5455 C CB    . ARG B 2 325 ? 11.338 -1.096  44.169 1.00 47.45  ?  343 ARG B CB    1 
ATOM   5456 C CG    . ARG B 2 325 ? 10.586 -0.985  42.834 1.00 65.82  ?  343 ARG B CG    1 
ATOM   5457 C CD    . ARG B 2 325 ? 9.907  0.401   42.657 1.00 71.51  ?  343 ARG B CD    1 
ATOM   5458 N NE    . ARG B 2 325 ? 10.630 1.282   41.733 1.00 72.74  ?  343 ARG B NE    1 
ATOM   5459 C CZ    . ARG B 2 325 ? 10.856 2.581   41.941 1.00 76.51  ?  343 ARG B CZ    1 
ATOM   5460 N NH1   . ARG B 2 325 ? 10.413 3.174   43.048 1.00 82.44  ?  343 ARG B NH1   1 
ATOM   5461 N NH2   . ARG B 2 325 ? 11.535 3.290   41.043 1.00 75.06  ?  343 ARG B NH2   1 
ATOM   5462 N N     . LYS B 2 326 ? 14.024 0.320   43.944 1.00 45.07  ?  344 LYS B N     1 
ATOM   5463 C CA    . LYS B 2 326 ? 14.932 1.259   43.290 1.00 39.11  ?  344 LYS B CA    1 
ATOM   5464 C C     . LYS B 2 326 ? 16.223 0.559   42.893 1.00 40.01  ?  344 LYS B C     1 
ATOM   5465 O O     . LYS B 2 326 ? 16.752 0.793   41.797 1.00 41.48  ?  344 LYS B O     1 
ATOM   5466 C CB    . LYS B 2 326 ? 15.231 2.462   44.205 1.00 44.85  ?  344 LYS B CB    1 
ATOM   5467 C CG    . LYS B 2 326 ? 14.213 3.630   44.204 1.00 47.61  ?  344 LYS B CG    1 
ATOM   5468 C CD    . LYS B 2 326 ? 14.818 4.891   43.578 1.00 49.77  ?  344 LYS B CD    1 
ATOM   5469 C CE    . LYS B 2 326 ? 14.102 6.218   43.951 1.00 57.76  ?  344 LYS B CE    1 
ATOM   5470 N NZ    . LYS B 2 326 ? 14.511 7.395   43.044 1.00 59.18  ?  344 LYS B NZ    1 
ATOM   5471 N N     . ALA B 2 327 ? 16.728 -0.342  43.753 1.00 36.91  ?  345 ALA B N     1 
ATOM   5472 C CA    . ALA B 2 327 ? 17.994 -1.007  43.457 1.00 30.61  ?  345 ALA B CA    1 
ATOM   5473 C C     . ALA B 2 327 ? 17.860 -1.972  42.291 1.00 33.33  ?  345 ALA B C     1 
ATOM   5474 O O     . ALA B 2 327 ? 18.763 -2.058  41.462 1.00 34.98  ?  345 ALA B O     1 
ATOM   5475 C CB    . ALA B 2 327 ? 18.511 -1.728  44.685 1.00 31.63  ?  345 ALA B CB    1 
ATOM   5476 N N     . GLN B 2 328 ? 16.749 -2.712  42.211 1.00 37.50  ?  346 GLN B N     1 
ATOM   5477 C CA    . GLN B 2 328 ? 16.459 -3.544  41.040 1.00 37.09  ?  346 GLN B CA    1 
ATOM   5478 C C     . GLN B 2 328 ? 16.610 -2.761  39.739 1.00 39.47  ?  346 GLN B C     1 
ATOM   5479 O O     . GLN B 2 328 ? 17.321 -3.175  38.817 1.00 42.07  ?  346 GLN B O     1 
ATOM   5480 C CB    . GLN B 2 328 ? 15.036 -4.097  41.116 1.00 36.91  ?  346 GLN B CB    1 
ATOM   5481 C CG    . GLN B 2 328 ? 14.855 -5.280  41.990 1.00 41.68  ?  346 GLN B CG    1 
ATOM   5482 C CD    . GLN B 2 328 ? 13.417 -5.437  42.366 1.00 41.96  ?  346 GLN B CD    1 
ATOM   5483 O OE1   . GLN B 2 328 ? 12.550 -4.840  41.734 1.00 48.63  ?  346 GLN B OE1   1 
ATOM   5484 N NE2   . GLN B 2 328 ? 13.144 -6.237  43.395 1.00 40.15  ?  346 GLN B NE2   1 
ATOM   5485 N N     . ASP B 2 329 ? 15.890 -1.649  39.634 1.00 37.67  ?  347 ASP B N     1 
ATOM   5486 C CA    . ASP B 2 329 ? 16.016 -0.777  38.479 1.00 39.58  ?  347 ASP B CA    1 
ATOM   5487 C C     . ASP B 2 329 ? 17.471 -0.486  38.161 1.00 39.19  ?  347 ASP B C     1 
ATOM   5488 O O     . ASP B 2 329 ? 17.902 -0.599  37.010 1.00 36.91  ?  347 ASP B O     1 
ATOM   5489 C CB    . ASP B 2 329 ? 15.254 0.508   38.764 1.00 44.87  ?  347 ASP B CB    1 
ATOM   5490 C CG    . ASP B 2 329 ? 13.830 0.235   39.136 1.00 48.54  ?  347 ASP B CG    1 
ATOM   5491 O OD1   . ASP B 2 329 ? 13.239 1.006   39.915 1.00 52.29  ?  347 ASP B OD1   1 
ATOM   5492 O OD2   . ASP B 2 329 ? 13.306 -0.775  38.628 1.00 52.16  -1 347 ASP B OD2   1 
ATOM   5493 N N     . TYR B 2 330 ? 18.242 -0.107  39.188 1.00 38.71  ?  348 TYR B N     1 
ATOM   5494 C CA    . TYR B 2 330 ? 19.659 0.194   39.025 1.00 31.24  ?  348 TYR B CA    1 
ATOM   5495 C C     . TYR B 2 330 ? 20.409 -0.956  38.383 1.00 32.66  ?  348 TYR B C     1 
ATOM   5496 O O     . TYR B 2 330 ? 21.116 -0.769  37.392 1.00 35.10  ?  348 TYR B O     1 
ATOM   5497 C CB    . TYR B 2 330 ? 20.267 0.527   40.383 1.00 30.97  ?  348 TYR B CB    1 
ATOM   5498 C CG    . TYR B 2 330 ? 21.661 1.091   40.324 1.00 31.13  ?  348 TYR B CG    1 
ATOM   5499 C CD1   . TYR B 2 330 ? 22.743 0.365   40.813 1.00 34.19  ?  348 TYR B CD1   1 
ATOM   5500 C CD2   . TYR B 2 330 ? 21.904 2.350   39.797 1.00 28.84  ?  348 TYR B CD2   1 
ATOM   5501 C CE1   . TYR B 2 330 ? 24.032 0.871   40.771 1.00 32.38  ?  348 TYR B CE1   1 
ATOM   5502 C CE2   . TYR B 2 330 ? 23.182 2.866   39.752 1.00 29.42  ?  348 TYR B CE2   1 
ATOM   5503 C CZ    . TYR B 2 330 ? 24.244 2.122   40.249 1.00 31.88  ?  348 TYR B CZ    1 
ATOM   5504 O OH    . TYR B 2 330 ? 25.522 2.624   40.214 1.00 31.54  ?  348 TYR B OH    1 
ATOM   5505 N N     . VAL B 2 331 ? 20.306 -2.158  38.951 1.00 37.49  ?  349 VAL B N     1 
ATOM   5506 C CA    . VAL B 2 331 ? 21.111 -3.232  38.382 1.00 39.50  ?  349 VAL B CA    1 
ATOM   5507 C C     . VAL B 2 331 ? 20.531 -3.645  37.049 1.00 37.30  ?  349 VAL B C     1 
ATOM   5508 O O     . VAL B 2 331 ? 21.267 -4.060  36.147 1.00 35.70  ?  349 VAL B O     1 
ATOM   5509 C CB    . VAL B 2 331 ? 21.261 -4.423  39.351 1.00 36.23  ?  349 VAL B CB    1 
ATOM   5510 C CG1   . VAL B 2 331 ? 20.331 -4.275  40.522 1.00 31.25  ?  349 VAL B CG1   1 
ATOM   5511 C CG2   . VAL B 2 331 ? 21.092 -5.755  38.601 1.00 37.16  ?  349 VAL B CG2   1 
ATOM   5512 N N     . PHE B 2 332 ? 19.215 -3.495  36.884 1.00 37.85  ?  350 PHE B N     1 
ATOM   5513 C CA    . PHE B 2 332 ? 18.608 -3.697  35.570 1.00 42.69  ?  350 PHE B CA    1 
ATOM   5514 C C     . PHE B 2 332 ? 19.205 -2.756  34.528 1.00 40.86  ?  350 PHE B C     1 
ATOM   5515 O O     . PHE B 2 332 ? 19.633 -3.196  33.455 1.00 40.02  ?  350 PHE B O     1 
ATOM   5516 C CB    . PHE B 2 332 ? 17.097 -3.516  35.648 1.00 47.09  ?  350 PHE B CB    1 
ATOM   5517 C CG    . PHE B 2 332 ? 16.364 -4.147  34.508 1.00 53.64  ?  350 PHE B CG    1 
ATOM   5518 C CD1   . PHE B 2 332 ? 15.909 -3.377  33.452 1.00 54.97  ?  350 PHE B CD1   1 
ATOM   5519 C CD2   . PHE B 2 332 ? 16.156 -5.517  34.475 1.00 55.02  ?  350 PHE B CD2   1 
ATOM   5520 C CE1   . PHE B 2 332 ? 15.236 -3.960  32.388 1.00 60.06  ?  350 PHE B CE1   1 
ATOM   5521 C CE2   . PHE B 2 332 ? 15.488 -6.106  33.419 1.00 60.45  ?  350 PHE B CE2   1 
ATOM   5522 C CZ    . PHE B 2 332 ? 15.025 -5.325  32.374 1.00 66.00  ?  350 PHE B CZ    1 
ATOM   5523 N N     . GLY B 2 333 ? 19.254 -1.457  34.833 1.00 36.83  ?  351 GLY B N     1 
ATOM   5524 C CA    . GLY B 2 333 ? 19.903 -0.513  33.933 1.00 37.43  ?  351 GLY B CA    1 
ATOM   5525 C C     . GLY B 2 333 ? 21.343 -0.880  33.617 1.00 38.06  ?  351 GLY B C     1 
ATOM   5526 O O     . GLY B 2 333 ? 21.728 -0.981  32.453 1.00 41.04  ?  351 GLY B O     1 
ATOM   5527 N N     . LEU B 2 334 ? 22.151 -1.102  34.654 1.00 37.57  ?  352 LEU B N     1 
ATOM   5528 C CA    . LEU B 2 334 ? 23.586 -1.320  34.481 1.00 38.18  ?  352 LEU B CA    1 
ATOM   5529 C C     . LEU B 2 334 ? 23.891 -2.559  33.655 1.00 37.54  ?  352 LEU B C     1 
ATOM   5530 O O     . LEU B 2 334 ? 24.820 -2.546  32.839 1.00 34.82  ?  352 LEU B O     1 
ATOM   5531 C CB    . LEU B 2 334 ? 24.254 -1.450  35.849 1.00 37.38  ?  352 LEU B CB    1 
ATOM   5532 C CG    . LEU B 2 334 ? 24.189 -0.157  36.625 1.00 37.90  ?  352 LEU B CG    1 
ATOM   5533 C CD1   . LEU B 2 334 ? 25.302 -0.107  37.631 1.00 41.36  ?  352 LEU B CD1   1 
ATOM   5534 C CD2   . LEU B 2 334 ? 24.280 0.985   35.605 1.00 41.41  ?  352 LEU B CD2   1 
ATOM   5535 N N     . THR B 2 335 ? 23.167 -3.663  33.903 1.00 39.22  ?  353 THR B N     1 
ATOM   5536 C CA    . THR B 2 335 ? 23.464 -4.925  33.229 1.00 40.96  ?  353 THR B CA    1 
ATOM   5537 C C     . THR B 2 335 ? 22.924 -4.962  31.800 1.00 42.26  ?  353 THR B C     1 
ATOM   5538 O O     . THR B 2 335 ? 23.453 -5.698  30.953 1.00 44.23  ?  353 THR B O     1 
ATOM   5539 C CB    . THR B 2 335 ? 22.905 -6.123  34.008 1.00 40.01  ?  353 THR B CB    1 
ATOM   5540 O OG1   . THR B 2 335 ? 21.478 -6.111  33.949 1.00 39.14  ?  353 THR B OG1   1 
ATOM   5541 C CG2   . THR B 2 335 ? 23.351 -6.103  35.447 1.00 41.58  ?  353 THR B CG2   1 
ATOM   5542 N N     . ILE B 2 336 ? 21.880 -4.201  31.497 1.00 39.47  ?  354 ILE B N     1 
ATOM   5543 C CA    . ILE B 2 336 ? 21.488 -4.135  30.097 1.00 39.15  ?  354 ILE B CA    1 
ATOM   5544 C C     . ILE B 2 336 ? 22.430 -3.213  29.318 1.00 41.20  ?  354 ILE B C     1 
ATOM   5545 O O     . ILE B 2 336 ? 22.770 -3.507  28.168 1.00 39.61  ?  354 ILE B O     1 
ATOM   5546 C CB    . ILE B 2 336 ? 20.013 -3.721  29.980 1.00 40.52  ?  354 ILE B CB    1 
ATOM   5547 C CG1   . ILE B 2 336 ? 19.179 -4.928  29.572 1.00 38.61  ?  354 ILE B CG1   1 
ATOM   5548 C CG2   . ILE B 2 336 ? 19.824 -2.552  29.013 1.00 40.69  ?  354 ILE B CG2   1 
ATOM   5549 C CD1   . ILE B 2 336 ? 17.862 -4.552  28.966 1.00 49.20  ?  354 ILE B CD1   1 
ATOM   5550 N N     . GLN B 2 337 ? 22.902 -2.116  29.941 1.00 37.49  ?  355 GLN B N     1 
ATOM   5551 C CA    . GLN B 2 337 ? 23.947 -1.296  29.329 1.00 37.46  ?  355 GLN B CA    1 
ATOM   5552 C C     . GLN B 2 337 ? 25.189 -2.119  29.019 1.00 39.76  ?  355 GLN B C     1 
ATOM   5553 O O     . GLN B 2 337 ? 25.776 -1.973  27.941 1.00 37.93  ?  355 GLN B O     1 
ATOM   5554 C CB    . GLN B 2 337 ? 24.322 -0.139  30.240 1.00 40.75  ?  355 GLN B CB    1 
ATOM   5555 C CG    . GLN B 2 337 ? 24.522 1.192   29.554 1.00 44.36  ?  355 GLN B CG    1 
ATOM   5556 C CD    . GLN B 2 337 ? 24.598 2.320   30.578 1.00 61.25  ?  355 GLN B CD    1 
ATOM   5557 O OE1   . GLN B 2 337 ? 23.562 2.716   31.169 1.00 60.54  ?  355 GLN B OE1   1 
ATOM   5558 N NE2   . GLN B 2 337 ? 25.828 2.834   30.822 1.00 52.31  ?  355 GLN B NE2   1 
ATOM   5559 N N     . SER B 2 338 ? 25.618 -2.964  29.972 1.00 41.39  ?  356 SER B N     1 
ATOM   5560 C CA    . SER B 2 338 ? 26.692 -3.934  29.743 1.00 38.42  ?  356 SER B CA    1 
ATOM   5561 C C     . SER B 2 338 ? 26.438 -4.765  28.499 1.00 35.60  ?  356 SER B C     1 
ATOM   5562 O O     . SER B 2 338 ? 27.335 -4.971  27.680 1.00 33.43  ?  356 SER B O     1 
ATOM   5563 C CB    . SER B 2 338 ? 26.836 -4.858  30.956 1.00 40.40  ?  356 SER B CB    1 
ATOM   5564 O OG    . SER B 2 338 ? 27.994 -5.674  30.843 1.00 44.48  ?  356 SER B OG    1 
ATOM   5565 N N     . ALA B 2 339 ? 25.216 -5.273  28.365 1.00 36.79  ?  357 ALA B N     1 
ATOM   5566 C CA    . ALA B 2 339 ? 24.841 -6.021  27.175 1.00 36.91  ?  357 ALA B CA    1 
ATOM   5567 C C     . ALA B 2 339 ? 24.948 -5.151  25.931 1.00 36.81  ?  357 ALA B C     1 
ATOM   5568 O O     . ALA B 2 339 ? 25.544 -5.553  24.927 1.00 38.35  ?  357 ALA B O     1 
ATOM   5569 C CB    . ALA B 2 339 ? 23.420 -6.569  27.341 1.00 35.43  ?  357 ALA B CB    1 
ATOM   5570 N N     . MET B 2 340 ? 24.374 -3.946  25.987 1.00 36.22  ?  358 MET B N     1 
ATOM   5571 C CA    . MET B 2 340 ? 24.424 -3.017  24.867 1.00 35.96  ?  358 MET B CA    1 
ATOM   5572 C C     . MET B 2 340 ? 25.864 -2.662  24.481 1.00 38.83  ?  358 MET B C     1 
ATOM   5573 O O     . MET B 2 340 ? 26.204 -2.628  23.290 1.00 38.51  ?  358 MET B O     1 
ATOM   5574 C CB    . MET B 2 340 ? 23.630 -1.767  25.224 1.00 35.85  ?  358 MET B CB    1 
ATOM   5575 C CG    . MET B 2 340 ? 23.442 -0.794  24.085 1.00 36.69  ?  358 MET B CG    1 
ATOM   5576 S SD    . MET B 2 340 ? 24.858 0.300   23.921 1.00 37.10  ?  358 MET B SD    1 
ATOM   5577 C CE    . MET B 2 340 ? 24.722 1.381   25.340 1.00 31.01  ?  358 MET B CE    1 
ATOM   5578 N N     . HIS B 2 341 ? 26.724 -2.384  25.465 1.00 36.06  ?  359 HIS B N     1 
ATOM   5579 C CA    . HIS B 2 341 ? 28.123 -2.123  25.141 1.00 36.56  ?  359 HIS B CA    1 
ATOM   5580 C C     . HIS B 2 341 ? 28.780 -3.308  24.473 1.00 39.81  ?  359 HIS B C     1 
ATOM   5581 O O     . HIS B 2 341 ? 29.671 -3.125  23.640 1.00 39.67  ?  359 HIS B O     1 
ATOM   5582 C CB    . HIS B 2 341 ? 28.927 -1.762  26.381 1.00 32.66  ?  359 HIS B CB    1 
ATOM   5583 C CG    . HIS B 2 341 ? 28.564 -0.440  26.945 1.00 34.05  ?  359 HIS B CG    1 
ATOM   5584 N ND1   . HIS B 2 341 ? 28.785 -0.106  28.262 1.00 40.02  ?  359 HIS B ND1   1 
ATOM   5585 C CD2   . HIS B 2 341 ? 27.951 0.623   26.381 1.00 34.70  ?  359 HIS B CD2   1 
ATOM   5586 C CE1   . HIS B 2 341 ? 28.330 1.114   28.486 1.00 40.04  ?  359 HIS B CE1   1 
ATOM   5587 N NE2   . HIS B 2 341 ? 27.822 1.579   27.358 1.00 42.91  ?  359 HIS B NE2   1 
ATOM   5588 N N     . HIS B 2 342 ? 28.397 -4.529  24.843 1.00 40.62  ?  360 HIS B N     1 
ATOM   5589 C CA    . HIS B 2 342 ? 29.037 -5.662  24.192 1.00 46.67  ?  360 HIS B CA    1 
ATOM   5590 C C     . HIS B 2 342 ? 28.565 -5.807  22.752 1.00 44.84  ?  360 HIS B C     1 
ATOM   5591 O O     . HIS B 2 342 ? 29.361 -6.158  21.872 1.00 47.26  ?  360 HIS B O     1 
ATOM   5592 C CB    . HIS B 2 342 ? 28.809 -6.967  24.941 1.00 47.29  ?  360 HIS B CB    1 
ATOM   5593 C CG    . HIS B 2 342 ? 29.390 -8.142  24.221 1.00 56.82  ?  360 HIS B CG    1 
ATOM   5594 N ND1   . HIS B 2 342 ? 28.620 -9.169  23.717 1.00 59.22  ?  360 HIS B ND1   1 
ATOM   5595 C CD2   . HIS B 2 342 ? 30.668 -8.415  23.858 1.00 58.99  ?  360 HIS B CD2   1 
ATOM   5596 C CE1   . HIS B 2 342 ? 29.401 -10.039 23.101 1.00 65.69  ?  360 HIS B CE1   1 
ATOM   5597 N NE2   . HIS B 2 342 ? 30.648 -9.603  23.168 1.00 68.35  ?  360 HIS B NE2   1 
ATOM   5598 N N     . GLU B 2 343 ? 27.285 -5.537  22.482 1.00 40.96  ?  361 GLU B N     1 
ATOM   5599 C CA    . GLU B 2 343 ? 26.861 -5.540  21.090 1.00 40.85  ?  361 GLU B CA    1 
ATOM   5600 C C     . GLU B 2 343 ? 27.559 -4.438  20.311 1.00 41.94  ?  361 GLU B C     1 
ATOM   5601 O O     . GLU B 2 343 ? 27.970 -4.653  19.165 1.00 40.93  ?  361 GLU B O     1 
ATOM   5602 C CB    . GLU B 2 343 ? 25.345 -5.405  20.944 1.00 37.88  ?  361 GLU B CB    1 
ATOM   5603 C CG    . GLU B 2 343 ? 24.982 -5.566  19.448 1.00 38.09  ?  361 GLU B CG    1 
ATOM   5604 C CD    . GLU B 2 343 ? 23.502 -5.497  19.082 1.00 39.85  ?  361 GLU B CD    1 
ATOM   5605 O OE1   . GLU B 2 343 ? 23.184 -5.743  17.891 1.00 44.25  ?  361 GLU B OE1   1 
ATOM   5606 O OE2   . GLU B 2 343 ? 22.657 -5.199  19.950 1.00 42.35  -1 361 GLU B OE2   1 
ATOM   5607 N N     . LEU B 2 344 ? 27.713 -3.257  20.928 1.00 40.24  ?  362 LEU B N     1 
ATOM   5608 C CA    . LEU B 2 344 ? 28.356 -2.119  20.266 1.00 41.09  ?  362 LEU B CA    1 
ATOM   5609 C C     . LEU B 2 344 ? 29.775 -2.458  19.805 1.00 45.71  ?  362 LEU B C     1 
ATOM   5610 O O     . LEU B 2 344 ? 30.122 -2.275  18.632 1.00 47.20  ?  362 LEU B O     1 
ATOM   5611 C CB    . LEU B 2 344 ? 28.377 -0.915  21.211 1.00 37.05  ?  362 LEU B CB    1 
ATOM   5612 C CG    . LEU B 2 344 ? 28.317 0.539   20.724 1.00 29.33  ?  362 LEU B CG    1 
ATOM   5613 C CD1   . LEU B 2 344 ? 29.528 1.267   21.157 1.00 30.28  ?  362 LEU B CD1   1 
ATOM   5614 C CD2   . LEU B 2 344 ? 28.158 0.660   19.239 1.00 35.60  ?  362 LEU B CD2   1 
ATOM   5615 N N     . GLN B 2 345 ? 30.615 -2.949  20.717 1.00 44.32  ?  363 GLN B N     1 
ATOM   5616 C CA    . GLN B 2 345 ? 32.022 -3.144  20.381 1.00 49.62  ?  363 GLN B CA    1 
ATOM   5617 C C     . GLN B 2 345 ? 32.227 -4.336  19.457 1.00 53.66  ?  363 GLN B C     1 
ATOM   5618 O O     . GLN B 2 345 ? 33.202 -4.373  18.696 1.00 53.60  ?  363 GLN B O     1 
ATOM   5619 C CB    . GLN B 2 345 ? 32.829 -3.274  21.667 1.00 45.70  ?  363 GLN B CB    1 
ATOM   5620 C CG    . GLN B 2 345 ? 32.387 -2.207  22.672 1.00 51.53  ?  363 GLN B CG    1 
ATOM   5621 C CD    . GLN B 2 345 ? 33.444 -1.818  23.687 1.00 58.72  ?  363 GLN B CD    1 
ATOM   5622 O OE1   . GLN B 2 345 ? 34.389 -1.074  23.374 1.00 57.06  ?  363 GLN B OE1   1 
ATOM   5623 N NE2   . GLN B 2 345 ? 33.276 -2.295  24.930 1.00 55.40  ?  363 GLN B NE2   1 
ATOM   5624 N N     . GLU B 2 346 ? 31.321 -5.305  19.486 1.00 55.46  ?  364 GLU B N     1 
ATOM   5625 C CA    . GLU B 2 346 ? 31.400 -6.383  18.520 1.00 59.60  ?  364 GLU B CA    1 
ATOM   5626 C C     . GLU B 2 346 ? 30.813 -6.005  17.165 1.00 64.01  ?  364 GLU B C     1 
ATOM   5627 O O     . GLU B 2 346 ? 30.917 -6.797  16.227 1.00 75.17  ?  364 GLU B O     1 
ATOM   5628 C CB    . GLU B 2 346 ? 30.718 -7.632  19.071 1.00 60.90  ?  364 GLU B CB    1 
ATOM   5629 C CG    . GLU B 2 346 ? 31.421 -8.918  18.651 1.00 73.79  ?  364 GLU B CG    1 
ATOM   5630 C CD    . GLU B 2 346 ? 30.535 -10.152 18.778 1.00 86.69  ?  364 GLU B CD    1 
ATOM   5631 O OE1   . GLU B 2 346 ? 29.983 -10.383 19.885 1.00 81.98  ?  364 GLU B OE1   1 
ATOM   5632 O OE2   . GLU B 2 346 ? 30.387 -10.882 17.763 1.00 87.64  -1 364 GLU B OE2   1 
ATOM   5633 N N     . ARG B 2 347 ? 30.216 -4.821  17.031 1.00 60.58  ?  365 ARG B N     1 
ATOM   5634 C CA    . ARG B 2 347 ? 29.839 -4.288  15.725 1.00 59.45  ?  365 ARG B CA    1 
ATOM   5635 C C     . ARG B 2 347 ? 30.938 -3.455  15.084 1.00 66.09  ?  365 ARG B C     1 
ATOM   5636 O O     . ARG B 2 347 ? 30.921 -3.264  13.864 1.00 66.91  ?  365 ARG B O     1 
ATOM   5637 C CB    . ARG B 2 347 ? 28.585 -3.427  15.838 1.00 53.53  ?  365 ARG B CB    1 
ATOM   5638 C CG    . ARG B 2 347 ? 28.008 -3.068  14.496 1.00 59.26  ?  365 ARG B CG    1 
ATOM   5639 C CD    . ARG B 2 347 ? 26.813 -2.140  14.592 1.00 52.45  ?  365 ARG B CD    1 
ATOM   5640 N NE    . ARG B 2 347 ? 27.056 -0.858  13.930 1.00 55.53  ?  365 ARG B NE    1 
ATOM   5641 C CZ    . ARG B 2 347 ? 26.816 -0.614  12.639 1.00 63.80  ?  365 ARG B CZ    1 
ATOM   5642 N NH1   . ARG B 2 347 ? 26.314 -1.579  11.849 1.00 63.33  ?  365 ARG B NH1   1 
ATOM   5643 N NH2   . ARG B 2 347 ? 27.081 0.596   12.134 1.00 58.07  ?  365 ARG B NH2   1 
ATOM   5644 N N     . PHE B 2 348 ? 31.882 -2.950  15.884 1.00 69.48  ?  366 PHE B N     1 
ATOM   5645 C CA    . PHE B 2 348 ? 33.033 -2.221  15.368 1.00 66.09  ?  366 PHE B CA    1 
ATOM   5646 C C     . PHE B 2 348 ? 34.122 -3.159  14.882 1.00 73.37  ?  366 PHE B C     1 
ATOM   5647 O O     . PHE B 2 348 ? 34.753 -2.894  13.854 1.00 78.19  ?  366 PHE B O     1 
ATOM   5648 C CB    . PHE B 2 348 ? 33.582 -1.293  16.442 1.00 66.49  ?  366 PHE B CB    1 
ATOM   5649 C CG    . PHE B 2 348 ? 33.085 0.087   16.305 1.00 71.61  ?  366 PHE B CG    1 
ATOM   5650 C CD1   . PHE B 2 348 ? 33.865 1.061   15.699 1.00 67.61  ?  366 PHE B CD1   1 
ATOM   5651 C CD2   . PHE B 2 348 ? 31.797 0.404   16.716 1.00 72.08  ?  366 PHE B CD2   1 
ATOM   5652 C CE1   . PHE B 2 348 ? 33.379 2.342   15.530 1.00 67.03  ?  366 PHE B CE1   1 
ATOM   5653 C CE2   . PHE B 2 348 ? 31.300 1.683   16.555 1.00 74.84  ?  366 PHE B CE2   1 
ATOM   5654 C CZ    . PHE B 2 348 ? 32.092 2.656   15.960 1.00 74.85  ?  366 PHE B CZ    1 
ATOM   5655 N N     . LYS B 2 349 ? 34.369 -4.244  15.623 1.00 75.50  ?  367 LYS B N     1 
ATOM   5656 C CA    . LYS B 2 349 ? 35.255 -5.297  15.138 1.00 80.48  ?  367 LYS B CA    1 
ATOM   5657 C C     . LYS B 2 349 ? 34.929 -5.656  13.689 1.00 83.27  ?  367 LYS B C     1 
ATOM   5658 O O     . LYS B 2 349 ? 35.823 -5.721  12.836 1.00 86.14  ?  367 LYS B O     1 
ATOM   5659 C CB    . LYS B 2 349 ? 35.146 -6.536  16.042 1.00 82.05  ?  367 LYS B CB    1 
ATOM   5660 C CG    . LYS B 2 349 ? 35.601 -6.341  17.488 1.00 76.88  ?  367 LYS B CG    1 
ATOM   5661 C CD    . LYS B 2 349 ? 37.098 -6.066  17.590 1.00 80.36  ?  367 LYS B CD    1 
ATOM   5662 C CE    . LYS B 2 349 ? 37.932 -7.232  17.070 1.00 87.56  ?  367 LYS B CE    1 
ATOM   5663 N NZ    . LYS B 2 349 ? 39.022 -6.775  16.153 1.00 91.71  ?  367 LYS B NZ    1 
ATOM   5664 N N     . ASN B 2 350 ? 33.635 -5.853  13.391 1.00 80.99  ?  368 ASN B N     1 
ATOM   5665 C CA    . ASN B 2 350 ? 33.160 -6.388  12.117 1.00 83.06  ?  368 ASN B CA    1 
ATOM   5666 C C     . ASN B 2 350 ? 33.179 -5.375  10.977 1.00 82.37  ?  368 ASN B C     1 
ATOM   5667 O O     . ASN B 2 350 ? 33.017 -5.777  9.819  1.00 85.44  ?  368 ASN B O     1 
ATOM   5668 C CB    . ASN B 2 350 ? 31.740 -6.951  12.285 1.00 84.09  ?  368 ASN B CB    1 
ATOM   5669 C CG    . ASN B 2 350 ? 31.678 -8.114  13.300 1.00 96.27  ?  368 ASN B CG    1 
ATOM   5670 O OD1   . ASN B 2 350 ? 32.713 -8.680  13.691 1.00 98.47  ?  368 ASN B OD1   1 
ATOM   5671 N ND2   . ASN B 2 350 ? 30.458 -8.472  13.725 1.00 92.17  ?  368 ASN B ND2   1 
ATOM   5672 N N     . LYS B 2 351 ? 33.384 -4.091  11.265 1.00 82.50  ?  369 LYS B N     1 
ATOM   5673 C CA    . LYS B 2 351 ? 33.375 -3.046  10.243 1.00 82.19  ?  369 LYS B CA    1 
ATOM   5674 C C     . LYS B 2 351 ? 34.545 -3.205  9.270  1.00 85.75  ?  369 LYS B C     1 
ATOM   5675 O O     . LYS B 2 351 ? 34.450 -2.841  8.091  1.00 91.04  ?  369 LYS B O     1 
ATOM   5676 C CB    . LYS B 2 351 ? 33.412 -1.652  10.897 1.00 83.02  ?  369 LYS B CB    1 
ATOM   5677 C CG    . LYS B 2 351 ? 32.175 -1.300  11.742 1.00 78.17  ?  369 LYS B CG    1 
ATOM   5678 C CD    . LYS B 2 351 ? 31.697 0.148   11.512 1.00 77.01  ?  369 LYS B CD    1 
ATOM   5679 C CE    . LYS B 2 351 ? 30.788 0.651   12.650 1.00 70.68  ?  369 LYS B CE    1 
ATOM   5680 N NZ    . LYS B 2 351 ? 29.613 1.461   12.195 1.00 66.42  ?  369 LYS B NZ    1 
ATOM   5681 N N     . MET C 3 1   ? 57.419 33.792  66.314 1.00 62.31  ?  1   MET C N     1 
ATOM   5682 C CA    . MET C 3 1   ? 56.521 33.548  67.501 1.00 66.04  ?  1   MET C CA    1 
ATOM   5683 C C     . MET C 3 1   ? 56.517 32.093  68.012 1.00 62.22  ?  1   MET C C     1 
ATOM   5684 O O     . MET C 3 1   ? 56.918 31.159  67.315 1.00 62.07  ?  1   MET C O     1 
ATOM   5685 C CB    . MET C 3 1   ? 55.078 33.990  67.155 1.00 64.57  ?  1   MET C CB    1 
ATOM   5686 C CG    . MET C 3 1   ? 53.993 32.895  67.207 1.00 58.72  ?  1   MET C CG    1 
ATOM   5687 S SD    . MET C 3 1   ? 52.362 33.365  66.542 1.00 60.31  ?  1   MET C SD    1 
ATOM   5688 C CE    . MET C 3 1   ? 52.394 32.546  64.943 1.00 57.27  ?  1   MET C CE    1 
ATOM   5689 H H1    . MET C 3 1   ? 57.380 34.651  66.084 1.00 74.77  ?  1   MET C H1    1 
ATOM   5690 H H2    . MET C 3 1   ? 58.257 33.579  66.527 1.00 74.77  ?  1   MET C H2    1 
ATOM   5691 H H3    . MET C 3 1   ? 57.150 33.289  65.631 1.00 74.77  ?  1   MET C H3    1 
ATOM   5692 H HA    . MET C 3 1   ? 56.866 34.087  68.230 1.00 79.25  ?  1   MET C HA    1 
ATOM   5693 H HB2   . MET C 3 1   ? 54.815 34.680  67.784 1.00 77.48  ?  1   MET C HB2   1 
ATOM   5694 H HB3   . MET C 3 1   ? 55.079 34.346  66.253 1.00 77.48  ?  1   MET C HB3   1 
ATOM   5695 H HG2   . MET C 3 1   ? 54.304 32.133  66.693 1.00 70.47  ?  1   MET C HG2   1 
ATOM   5696 H HG3   . MET C 3 1   ? 53.863 32.639  68.134 1.00 70.47  ?  1   MET C HG3   1 
ATOM   5697 H HE1   . MET C 3 1   ? 51.592 32.783  64.451 1.00 68.72  ?  1   MET C HE1   1 
ATOM   5698 H HE2   . MET C 3 1   ? 53.179 32.836  64.455 1.00 68.72  ?  1   MET C HE2   1 
ATOM   5699 H HE3   . MET C 3 1   ? 52.426 31.586  65.081 1.00 68.72  ?  1   MET C HE3   1 
ATOM   5700 N N     . GLN C 3 2   ? 56.021 31.923  69.236 1.00 58.25  ?  2   GLN C N     1 
ATOM   5701 C CA    . GLN C 3 2   ? 56.118 30.690  70.005 1.00 51.12  ?  2   GLN C CA    1 
ATOM   5702 C C     . GLN C 3 2   ? 54.726 30.138  70.287 1.00 53.00  ?  2   GLN C C     1 
ATOM   5703 O O     . GLN C 3 2   ? 53.792 30.897  70.566 1.00 51.58  ?  2   GLN C O     1 
ATOM   5704 C CB    . GLN C 3 2   ? 56.856 30.993  71.304 1.00 51.89  ?  2   GLN C CB    1 
ATOM   5705 C CG    . GLN C 3 2   ? 57.227 29.845  72.182 1.00 54.46  ?  2   GLN C CG    1 
ATOM   5706 C CD    . GLN C 3 2   ? 58.643 29.994  72.732 1.00 57.98  ?  2   GLN C CD    1 
ATOM   5707 O OE1   . GLN C 3 2   ? 59.611 30.022  71.964 1.00 62.93  ?  2   GLN C OE1   1 
ATOM   5708 N NE2   . GLN C 3 2   ? 58.771 30.113  74.063 1.00 49.12  ?  2   GLN C NE2   1 
ATOM   5709 H H     . GLN C 3 2   ? 55.602 32.542  69.662 1.00 69.91  ?  2   GLN C H     1 
ATOM   5710 H HA    . GLN C 3 2   ? 56.592 30.001  69.514 1.00 61.34  ?  2   GLN C HA    1 
ATOM   5711 H HB2   . GLN C 3 2   ? 57.682 31.446  71.075 1.00 62.27  ?  2   GLN C HB2   1 
ATOM   5712 H HB3   . GLN C 3 2   ? 56.292 31.578  71.834 1.00 62.27  ?  2   GLN C HB3   1 
ATOM   5713 H HG2   . GLN C 3 2   ? 56.612 29.802  72.931 1.00 65.35  ?  2   GLN C HG2   1 
ATOM   5714 H HG3   . GLN C 3 2   ? 57.183 29.022  71.671 1.00 65.35  ?  2   GLN C HG3   1 
ATOM   5715 H HE21  . GLN C 3 2   ? 58.072 30.103  74.565 1.00 58.94  ?  2   GLN C HE21  1 
ATOM   5716 H HE22  . GLN C 3 2   ? 59.551 30.200  74.415 1.00 58.94  ?  2   GLN C HE22  1 
ATOM   5717 N N     . ILE C 3 3   ? 54.580 28.811  70.201 1.00 56.34  ?  3   ILE C N     1 
ATOM   5718 C CA    . ILE C 3 3   ? 53.349 28.117  70.587 1.00 55.25  ?  3   ILE C CA    1 
ATOM   5719 C C     . ILE C 3 3   ? 53.712 26.831  71.326 1.00 53.46  ?  3   ILE C C     1 
ATOM   5720 O O     . ILE C 3 3   ? 54.860 26.381  71.327 1.00 48.47  ?  3   ILE C O     1 
ATOM   5721 C CB    . ILE C 3 3   ? 52.422 27.789  69.391 1.00 48.85  ?  3   ILE C CB    1 
ATOM   5722 C CG1   . ILE C 3 3   ? 53.097 26.817  68.424 1.00 45.62  ?  3   ILE C CG1   1 
ATOM   5723 C CG2   . ILE C 3 3   ? 51.974 29.057  68.693 1.00 52.17  ?  3   ILE C CG2   1 
ATOM   5724 C CD1   . ILE C 3 3   ? 52.209 26.391  67.289 1.00 45.50  ?  3   ILE C CD1   1 
ATOM   5725 H H     . ILE C 3 3   ? 55.194 28.281  69.915 1.00 67.61  ?  3   ILE C H     1 
ATOM   5726 H HA    . ILE C 3 3   ? 52.862 28.698  71.192 1.00 66.30  ?  3   ILE C HA    1 
ATOM   5727 H HB    . ILE C 3 3   ? 51.629 27.349  69.735 1.00 58.62  ?  3   ILE C HB    1 
ATOM   5728 H HG12  . ILE C 3 3   ? 53.880 27.246  68.044 1.00 54.75  ?  3   ILE C HG12  1 
ATOM   5729 H HG13  . ILE C 3 3   ? 53.359 26.021  68.912 1.00 54.75  ?  3   ILE C HG13  1 
ATOM   5730 H HG21  . ILE C 3 3   ? 51.383 28.822  67.960 1.00 62.60  ?  3   ILE C HG21  1 
ATOM   5731 H HG22  . ILE C 3 3   ? 51.505 29.619  69.329 1.00 62.60  ?  3   ILE C HG22  1 
ATOM   5732 H HG23  . ILE C 3 3   ? 52.754 29.522  68.352 1.00 62.60  ?  3   ILE C HG23  1 
ATOM   5733 H HD11  . ILE C 3 3   ? 52.687 25.754  66.735 1.00 54.60  ?  3   ILE C HD11  1 
ATOM   5734 H HD12  . ILE C 3 3   ? 51.409 25.979  67.652 1.00 54.60  ?  3   ILE C HD12  1 
ATOM   5735 H HD13  . ILE C 3 3   ? 51.970 27.171  66.764 1.00 54.60  ?  3   ILE C HD13  1 
ATOM   5736 N N     . PHE C 3 4   ? 52.697 26.229  71.941 1.00 52.29  ?  4   PHE C N     1 
ATOM   5737 C CA    . PHE C 3 4   ? 52.867 25.071  72.805 1.00 52.87  ?  4   PHE C CA    1 
ATOM   5738 C C     . PHE C 3 4   ? 51.894 23.988  72.365 1.00 51.52  ?  4   PHE C C     1 
ATOM   5739 O O     . PHE C 3 4   ? 50.693 24.245  72.253 1.00 54.16  ?  4   PHE C O     1 
ATOM   5740 C CB    . PHE C 3 4   ? 52.624 25.431  74.275 1.00 51.12  ?  4   PHE C CB    1 
ATOM   5741 C CG    . PHE C 3 4   ? 53.492 26.553  74.790 1.00 54.91  ?  4   PHE C CG    1 
ATOM   5742 C CD1   . PHE C 3 4   ? 54.817 26.329  75.113 1.00 56.33  ?  4   PHE C CD1   1 
ATOM   5743 C CD2   . PHE C 3 4   ? 52.976 27.832  74.966 1.00 57.42  ?  4   PHE C CD2   1 
ATOM   5744 C CE1   . PHE C 3 4   ? 55.622 27.353  75.603 1.00 56.66  ?  4   PHE C CE1   1 
ATOM   5745 C CE2   . PHE C 3 4   ? 53.777 28.861  75.447 1.00 58.43  ?  4   PHE C CE2   1 
ATOM   5746 C CZ    . PHE C 3 4   ? 55.102 28.615  75.773 1.00 56.80  ?  4   PHE C CZ    1 
ATOM   5747 H H     . PHE C 3 4   ? 51.878 26.483  71.869 1.00 62.75  ?  4   PHE C H     1 
ATOM   5748 H HA    . PHE C 3 4   ? 53.772 24.732  72.721 1.00 63.45  ?  4   PHE C HA    1 
ATOM   5749 H HB2   . PHE C 3 4   ? 51.699 25.703  74.378 1.00 61.35  ?  4   PHE C HB2   1 
ATOM   5750 H HB3   . PHE C 3 4   ? 52.802 24.648  74.819 1.00 61.35  ?  4   PHE C HB3   1 
ATOM   5751 H HD1   . PHE C 3 4   ? 55.177 25.478  75.002 1.00 67.59  ?  4   PHE C HD1   1 
ATOM   5752 H HD2   . PHE C 3 4   ? 52.085 28.001  74.760 1.00 68.90  ?  4   PHE C HD2   1 
ATOM   5753 H HE1   . PHE C 3 4   ? 56.512 27.184  75.815 1.00 67.99  ?  4   PHE C HE1   1 
ATOM   5754 H HE2   . PHE C 3 4   ? 53.423 29.715  75.552 1.00 70.11  ?  4   PHE C HE2   1 
ATOM   5755 H HZ    . PHE C 3 4   ? 55.637 29.300  76.104 1.00 68.16  ?  4   PHE C HZ    1 
ATOM   5756 N N     . VAL C 3 5   ? 52.414 22.785  72.116 1.00 50.99  ?  5   VAL C N     1 
ATOM   5757 C CA    . VAL C 3 5   ? 51.624 21.622  71.719 1.00 46.98  ?  5   VAL C CA    1 
ATOM   5758 C C     . VAL C 3 5   ? 51.606 20.645  72.881 1.00 44.86  ?  5   VAL C C     1 
ATOM   5759 O O     . VAL C 3 5   ? 52.664 20.197  73.336 1.00 46.54  ?  5   VAL C O     1 
ATOM   5760 C CB    . VAL C 3 5   ? 52.191 20.951  70.462 1.00 46.76  ?  5   VAL C CB    1 
ATOM   5761 C CG1   . VAL C 3 5   ? 51.203 19.951  69.924 1.00 45.70  ?  5   VAL C CG1   1 
ATOM   5762 C CG2   . VAL C 3 5   ? 52.520 21.985  69.413 1.00 48.83  ?  5   VAL C CG2   1 
ATOM   5763 H H     . VAL C 3 5   ? 53.255 22.613  72.174 1.00 61.19  ?  5   VAL C H     1 
ATOM   5764 H HA    . VAL C 3 5   ? 50.715 21.907  71.537 1.00 56.38  ?  5   VAL C HA    1 
ATOM   5765 H HB    . VAL C 3 5   ? 53.010 20.485  70.691 1.00 56.11  ?  5   VAL C HB    1 
ATOM   5766 H HG11  . VAL C 3 5   ? 51.575 19.536  69.130 1.00 54.84  ?  5   VAL C HG11  1 
ATOM   5767 H HG12  . VAL C 3 5   ? 51.035 19.278  70.601 1.00 54.84  ?  5   VAL C HG12  1 
ATOM   5768 H HG13  . VAL C 3 5   ? 50.378 20.411  69.702 1.00 54.84  ?  5   VAL C HG13  1 
ATOM   5769 H HG21  . VAL C 3 5   ? 52.859 21.537  68.622 1.00 58.60  ?  5   VAL C HG21  1 
ATOM   5770 H HG22  . VAL C 3 5   ? 51.715 22.479  69.193 1.00 58.60  ?  5   VAL C HG22  1 
ATOM   5771 H HG23  . VAL C 3 5   ? 53.193 22.589  69.764 1.00 58.60  ?  5   VAL C HG23  1 
ATOM   5772 N N     . LYS C 3 6   ? 50.410 20.311  73.358 1.00 47.03  ?  6   LYS C N     1 
ATOM   5773 C CA    . LYS C 3 6   ? 50.235 19.475  74.541 1.00 51.70  ?  6   LYS C CA    1 
ATOM   5774 C C     . LYS C 3 6   ? 49.725 18.091  74.144 1.00 51.00  ?  6   LYS C C     1 
ATOM   5775 O O     . LYS C 3 6   ? 48.744 17.964  73.393 1.00 48.26  ?  6   LYS C O     1 
ATOM   5776 C CB    . LYS C 3 6   ? 49.274 20.137  75.538 1.00 52.25  ?  6   LYS C CB    1 
ATOM   5777 C CG    . LYS C 3 6   ? 49.452 19.690  77.010 1.00 55.12  ?  6   LYS C CG    1 
ATOM   5778 C CD    . LYS C 3 6   ? 48.140 19.882  77.818 1.00 61.61  ?  6   LYS C CD    1 
ATOM   5779 C CE    . LYS C 3 6   ? 47.742 18.650  78.707 1.00 65.66  ?  6   LYS C CE    1 
ATOM   5780 N NZ    . LYS C 3 6   ? 47.257 17.341  78.068 1.00 59.75  ?  6   LYS C NZ    1 
ATOM   5781 H H     . LYS C 3 6   ? 49.668 20.563  73.005 1.00 56.43  ?  6   LYS C H     1 
ATOM   5782 H HA    . LYS C 3 6   ? 51.094 19.354  74.974 1.00 62.04  ?  6   LYS C HA    1 
ATOM   5783 H HB2   . LYS C 3 6   ? 49.412 21.096  75.507 1.00 62.69  ?  6   LYS C HB2   1 
ATOM   5784 H HB3   . LYS C 3 6   ? 48.365 19.923  75.277 1.00 62.69  ?  6   LYS C HB3   1 
ATOM   5785 H HG2   . LYS C 3 6   ? 49.691 18.751  77.035 1.00 66.14  ?  6   LYS C HG2   1 
ATOM   5786 H HG3   . LYS C 3 6   ? 50.148 20.221  77.426 1.00 66.14  ?  6   LYS C HG3   1 
ATOM   5787 H HD2   . LYS C 3 6   ? 48.247 20.646  78.406 1.00 73.93  ?  6   LYS C HD2   1 
ATOM   5788 H HD3   . LYS C 3 6   ? 47.413 20.042  77.196 1.00 73.93  ?  6   LYS C HD3   1 
ATOM   5789 H HE2   . LYS C 3 6   ? 48.523 18.414  79.232 1.00 78.79  ?  6   LYS C HE2   1 
ATOM   5790 H HE3   . LYS C 3 6   ? 47.025 18.941  79.292 1.00 78.79  ?  6   LYS C HE3   1 
ATOM   5791 H HZ1   . LYS C 3 6   ? 47.092 16.737  78.699 1.00 71.70  ?  6   LYS C HZ1   1 
ATOM   5792 H HZ2   . LYS C 3 6   ? 46.510 17.487  77.606 1.00 71.70  ?  6   LYS C HZ2   1 
ATOM   5793 H HZ3   . LYS C 3 6   ? 47.879 17.022  77.517 1.00 71.70  ?  6   LYS C HZ3   1 
ATOM   5794 N N     . THR C 3 7   ? 50.389 17.064  74.676 1.00 52.27  ?  7   THR C N     1 
ATOM   5795 C CA    . THR C 3 7   ? 50.100 15.661  74.411 1.00 52.59  ?  7   THR C CA    1 
ATOM   5796 C C     . THR C 3 7   ? 49.332 15.037  75.569 1.00 50.46  ?  7   THR C C     1 
ATOM   5797 O O     . THR C 3 7   ? 49.284 15.569  76.679 1.00 52.52  ?  7   THR C O     1 
ATOM   5798 C CB    . THR C 3 7   ? 51.393 14.869  74.201 1.00 51.68  ?  7   THR C CB    1 
ATOM   5799 O OG1   . THR C 3 7   ? 51.980 14.587  75.485 1.00 49.68  ?  7   THR C OG1   1 
ATOM   5800 C CG2   . THR C 3 7   ? 52.367 15.654  73.336 1.00 46.93  ?  7   THR C CG2   1 
ATOM   5801 H H     . THR C 3 7   ? 51.045 17.163  75.223 1.00 62.72  ?  7   THR C H     1 
ATOM   5802 H HA    . THR C 3 7   ? 49.560 15.613  73.606 1.00 63.11  ?  7   THR C HA    1 
ATOM   5803 H HB    . THR C 3 7   ? 51.206 14.035  73.743 1.00 62.02  ?  7   THR C HB    1 
ATOM   5804 H HG1   . THR C 3 7   ? 52.680 14.134  75.388 1.00 59.62  ?  7   THR C HG1   1 
ATOM   5805 H HG21  . THR C 3 7   ? 53.180 15.142  73.205 1.00 56.31  ?  7   THR C HG21  1 
ATOM   5806 H HG22  . THR C 3 7   ? 51.968 15.839  72.472 1.00 56.31  ?  7   THR C HG22  1 
ATOM   5807 H HG23  . THR C 3 7   ? 52.589 16.494  73.767 1.00 56.31  ?  7   THR C HG23  1 
ATOM   5808 N N     . LEU C 3 8   ? 48.780 13.853  75.306 1.00 48.20  ?  8   LEU C N     1 
ATOM   5809 C CA    . LEU C 3 8   ? 47.885 13.220  76.267 1.00 49.11  ?  8   LEU C CA    1 
ATOM   5810 C C     . LEU C 3 8   ? 48.497 13.127  77.662 1.00 49.12  ?  8   LEU C C     1 
ATOM   5811 O O     . LEU C 3 8   ? 47.786 13.286  78.659 1.00 48.87  ?  8   LEU C O     1 
ATOM   5812 C CB    . LEU C 3 8   ? 47.500 11.835  75.757 1.00 48.49  ?  8   LEU C CB    1 
ATOM   5813 C CG    . LEU C 3 8   ? 46.667 11.772  74.475 1.00 38.42  ?  8   LEU C CG    1 
ATOM   5814 C CD1   . LEU C 3 8   ? 45.875 10.498  74.389 1.00 34.46  ?  8   LEU C CD1   1 
ATOM   5815 C CD2   . LEU C 3 8   ? 45.723 12.922  74.387 1.00 42.35  ?  8   LEU C CD2   1 
ATOM   5816 H H     . LEU C 3 8   ? 48.907 13.401  74.585 1.00 57.84  ?  8   LEU C H     1 
ATOM   5817 H HA    . LEU C 3 8   ? 47.080 13.756  76.347 1.00 58.93  ?  8   LEU C HA    1 
ATOM   5818 H HB2   . LEU C 3 8   ? 48.318 11.342  75.588 1.00 58.19  ?  8   LEU C HB2   1 
ATOM   5819 H HB3   . LEU C 3 8   ? 46.985 11.394  76.451 1.00 58.19  ?  8   LEU C HB3   1 
ATOM   5820 H HG    . LEU C 3 8   ? 47.289 11.807  73.731 1.00 46.10  ?  8   LEU C HG    1 
ATOM   5821 H HD11  . LEU C 3 8   ? 45.358 10.503  73.569 1.00 41.35  ?  8   LEU C HD11  1 
ATOM   5822 H HD12  . LEU C 3 8   ? 46.487 9.745   74.390 1.00 41.35  ?  8   LEU C HD12  1 
ATOM   5823 H HD13  . LEU C 3 8   ? 45.282 10.443  75.154 1.00 41.35  ?  8   LEU C HD13  1 
ATOM   5824 H HD21  . LEU C 3 8   ? 45.165 12.814  73.601 1.00 50.81  ?  8   LEU C HD21  1 
ATOM   5825 H HD22  . LEU C 3 8   ? 45.171 12.939  75.185 1.00 50.81  ?  8   LEU C HD22  1 
ATOM   5826 H HD23  . LEU C 3 8   ? 46.233 13.745  74.320 1.00 50.81  ?  8   LEU C HD23  1 
ATOM   5827 N N     . THR C 3 9   ? 49.804 12.888  77.759 1.00 53.68  ?  9   THR C N     1 
ATOM   5828 C CA    . THR C 3 9   ? 50.464 12.803  79.060 1.00 55.02  ?  9   THR C CA    1 
ATOM   5829 C C     . THR C 3 9   ? 50.626 14.158  79.729 1.00 53.78  ?  9   THR C C     1 
ATOM   5830 O O     . THR C 3 9   ? 51.112 14.218  80.870 1.00 54.02  ?  9   THR C O     1 
ATOM   5831 C CB    . THR C 3 9   ? 51.863 12.172  78.953 1.00 56.28  ?  9   THR C CB    1 
ATOM   5832 O OG1   . THR C 3 9   ? 52.569 12.726  77.832 1.00 55.45  ?  9   THR C OG1   1 
ATOM   5833 C CG2   . THR C 3 9   ? 51.779 10.643  78.828 1.00 52.30  ?  9   THR C CG2   1 
ATOM   5834 H H     . THR C 3 9   ? 50.328 12.772  77.088 1.00 64.42  ?  9   THR C H     1 
ATOM   5835 H HA    . THR C 3 9   ? 49.914 12.226  79.612 1.00 66.02  ?  9   THR C HA    1 
ATOM   5836 H HB    . THR C 3 9   ? 52.361 12.367  79.762 1.00 67.54  ?  9   THR C HB    1 
ATOM   5837 H HG1   . THR C 3 9   ? 53.338 12.392  77.782 1.00 66.54  ?  9   THR C HG1   1 
ATOM   5838 H HG21  . THR C 3 9   ? 52.670 10.265  78.762 1.00 62.76  ?  9   THR C HG21  1 
ATOM   5839 H HG22  . THR C 3 9   ? 51.336 10.270  79.607 1.00 62.76  ?  9   THR C HG22  1 
ATOM   5840 H HG23  . THR C 3 9   ? 51.276 10.402  78.034 1.00 62.76  ?  9   THR C HG23  1 
ATOM   5841 N N     . GLY C 3 10  ? 50.256 15.239  79.049 1.00 54.37  ?  10  GLY C N     1 
ATOM   5842 C CA    . GLY C 3 10  ? 50.397 16.562  79.607 1.00 54.58  ?  10  GLY C CA    1 
ATOM   5843 C C     . GLY C 3 10  ? 51.793 17.129  79.541 1.00 54.76  ?  10  GLY C C     1 
ATOM   5844 O O     . GLY C 3 10  ? 52.015 18.238  80.050 1.00 56.43  ?  10  GLY C O     1 
ATOM   5845 H H     . GLY C 3 10  ? 49.919 15.224  78.258 1.00 65.24  ?  10  GLY C H     1 
ATOM   5846 H HA2   . GLY C 3 10  ? 49.809 17.166  79.127 1.00 65.50  ?  10  GLY C HA2   1 
ATOM   5847 H HA3   . GLY C 3 10  ? 50.132 16.536  80.539 1.00 65.50  ?  10  GLY C HA3   1 
ATOM   5848 N N     . LYS C 3 11  ? 52.747 16.384  78.981 1.00 55.81  ?  11  LYS C N     1 
ATOM   5849 C CA    . LYS C 3 11  ? 54.000 16.971  78.537 1.00 53.34  ?  11  LYS C CA    1 
ATOM   5850 C C     . LYS C 3 11  ? 53.703 17.943  77.405 1.00 50.34  ?  11  LYS C C     1 
ATOM   5851 O O     . LYS C 3 11  ? 52.680 17.847  76.722 1.00 52.36  ?  11  LYS C O     1 
ATOM   5852 C CB    . LYS C 3 11  ? 54.984 15.897  78.085 1.00 53.83  ?  11  LYS C CB    1 
ATOM   5853 C CG    . LYS C 3 11  ? 55.571 15.078  79.233 1.00 57.79  ?  11  LYS C CG    1 
ATOM   5854 C CD    . LYS C 3 11  ? 56.978 15.501  79.621 1.00 60.19  ?  11  LYS C CD    1 
ATOM   5855 C CE    . LYS C 3 11  ? 57.805 14.271  80.011 1.00 66.38  ?  11  LYS C CE    1 
ATOM   5856 N NZ    . LYS C 3 11  ? 58.615 13.679  78.872 1.00 75.00  ?  11  LYS C NZ    1 
ATOM   5857 H H     . LYS C 3 11  ? 52.689 15.536  78.849 1.00 66.98  ?  11  LYS C H     1 
ATOM   5858 H HA    . LYS C 3 11  ? 54.429 17.447  79.265 1.00 64.00  ?  11  LYS C HA    1 
ATOM   5859 H HB2   . LYS C 3 11  ? 54.525 15.284  77.489 1.00 64.59  ?  11  LYS C HB2   1 
ATOM   5860 H HB3   . LYS C 3 11  ? 55.720 16.324  77.620 1.00 64.59  ?  11  LYS C HB3   1 
ATOM   5861 H HG2   . LYS C 3 11  ? 55.004 15.181  80.014 1.00 69.35  ?  11  LYS C HG2   1 
ATOM   5862 H HG3   . LYS C 3 11  ? 55.604 14.145  78.969 1.00 69.35  ?  11  LYS C HG3   1 
ATOM   5863 H HD2   . LYS C 3 11  ? 57.406 15.938  78.869 1.00 72.23  ?  11  LYS C HD2   1 
ATOM   5864 H HD3   . LYS C 3 11  ? 56.941 16.105  80.379 1.00 72.23  ?  11  LYS C HD3   1 
ATOM   5865 H HE2   . LYS C 3 11  ? 58.426 14.524  80.712 1.00 79.65  ?  11  LYS C HE2   1 
ATOM   5866 H HE3   . LYS C 3 11  ? 57.204 13.582  80.334 1.00 79.65  ?  11  LYS C HE3   1 
ATOM   5867 H HZ1   . LYS C 3 11  ? 59.068 12.969  79.158 1.00 90.01  ?  11  LYS C HZ1   1 
ATOM   5868 H HZ2   . LYS C 3 11  ? 58.073 13.430  78.211 1.00 90.01  ?  11  LYS C HZ2   1 
ATOM   5869 H HZ3   . LYS C 3 11  ? 59.190 14.283  78.562 1.00 90.01  ?  11  LYS C HZ3   1 
ATOM   5870 N N     . THR C 3 12  ? 54.601 18.902  77.219 1.00 51.39  ?  12  THR C N     1 
ATOM   5871 C CA    . THR C 3 12  ? 54.332 20.034  76.346 1.00 51.35  ?  12  THR C CA    1 
ATOM   5872 C C     . THR C 3 12  ? 55.558 20.311  75.505 1.00 45.31  ?  12  THR C C     1 
ATOM   5873 O O     . THR C 3 12  ? 56.634 20.562  76.046 1.00 51.67  ?  12  THR C O     1 
ATOM   5874 C CB    . THR C 3 12  ? 53.962 21.279  77.158 1.00 56.79  ?  12  THR C CB    1 
ATOM   5875 O OG1   . THR C 3 12  ? 54.127 22.445  76.337 1.00 57.68  ?  12  THR C OG1   1 
ATOM   5876 C CG2   . THR C 3 12  ? 54.840 21.381  78.398 1.00 59.16  ?  12  THR C CG2   1 
ATOM   5877 H H     . THR C 3 12  ? 55.377 18.919  77.589 1.00 61.67  ?  12  THR C H     1 
ATOM   5878 H HA    . THR C 3 12  ? 53.596 19.811  75.755 1.00 61.62  ?  12  THR C HA    1 
ATOM   5879 H HB    . THR C 3 12  ? 53.038 21.226  77.450 1.00 68.15  ?  12  THR C HB    1 
ATOM   5880 H HG1   . THR C 3 12  ? 53.879 23.129  76.756 1.00 69.22  ?  12  THR C HG1   1 
ATOM   5881 H HG21  . THR C 3 12  ? 54.570 22.143  78.934 1.00 70.99  ?  12  THR C HG21  1 
ATOM   5882 H HG22  . THR C 3 12  ? 54.755 20.575  78.932 1.00 70.99  ?  12  THR C HG22  1 
ATOM   5883 H HG23  . THR C 3 12  ? 55.768 21.491  78.140 1.00 70.99  ?  12  THR C HG23  1 
ATOM   5884 N N     . ILE C 3 13  ? 55.394 20.303  74.196 1.00 42.95  ?  13  ILE C N     1 
ATOM   5885 C CA    . ILE C 3 13  ? 56.477 20.624  73.277 1.00 46.95  ?  13  ILE C CA    1 
ATOM   5886 C C     . ILE C 3 13  ? 56.292 22.055  72.772 1.00 50.63  ?  13  ILE C C     1 
ATOM   5887 O O     . ILE C 3 13  ? 55.227 22.418  72.253 1.00 48.28  ?  13  ILE C O     1 
ATOM   5888 C CB    . ILE C 3 13  ? 56.549 19.596  72.131 1.00 42.18  ?  13  ILE C CB    1 
ATOM   5889 C CG1   . ILE C 3 13  ? 56.695 20.236  70.750 1.00 52.16  ?  13  ILE C CG1   1 
ATOM   5890 C CG2   . ILE C 3 13  ? 55.342 18.703  72.108 1.00 42.52  ?  13  ILE C CG2   1 
ATOM   5891 C CD1   . ILE C 3 13  ? 57.300 19.258  69.705 1.00 53.35  ?  13  ILE C CD1   1 
ATOM   5892 H H     . ILE C 3 13  ? 54.652 20.111  73.806 1.00 51.54  ?  13  ILE C H     1 
ATOM   5893 H HA    . ILE C 3 13  ? 57.326 20.601  73.746 1.00 56.34  ?  13  ILE C HA    1 
ATOM   5894 H HB    . ILE C 3 13  ? 57.349 19.079  72.318 1.00 50.61  ?  13  ILE C HB    1 
ATOM   5895 H HG12  . ILE C 3 13  ? 55.820 20.512  70.434 1.00 62.60  ?  13  ILE C HG12  1 
ATOM   5896 H HG13  . ILE C 3 13  ? 57.281 21.006  70.817 1.00 62.60  ?  13  ILE C HG13  1 
ATOM   5897 H HG21  . ILE C 3 13  ? 55.417 18.091  71.359 1.00 51.02  ?  13  ILE C HG21  1 
ATOM   5898 H HG22  . ILE C 3 13  ? 55.302 18.205  72.940 1.00 51.02  ?  13  ILE C HG22  1 
ATOM   5899 H HG23  . ILE C 3 13  ? 54.547 19.249  72.011 1.00 51.02  ?  13  ILE C HG23  1 
ATOM   5900 H HD11  . ILE C 3 13  ? 57.370 19.712  68.851 1.00 64.01  ?  13  ILE C HD11  1 
ATOM   5901 H HD12  . ILE C 3 13  ? 58.179 18.979  70.005 1.00 64.01  ?  13  ILE C HD12  1 
ATOM   5902 H HD13  . ILE C 3 13  ? 56.718 18.486  69.622 1.00 64.01  ?  13  ILE C HD13  1 
ATOM   5903 N N     . THR C 3 14  ? 57.334 22.871  72.928 1.00 46.98  ?  14  THR C N     1 
ATOM   5904 C CA    . THR C 3 14  ? 57.285 24.275  72.551 1.00 47.29  ?  14  THR C CA    1 
ATOM   5905 C C     . THR C 3 14  ? 57.997 24.456  71.211 1.00 44.40  ?  14  THR C C     1 
ATOM   5906 O O     . THR C 3 14  ? 59.025 23.829  70.952 1.00 41.97  ?  14  THR C O     1 
ATOM   5907 C CB    . THR C 3 14  ? 57.876 25.151  73.670 1.00 42.22  ?  14  THR C CB    1 
ATOM   5908 O OG1   . THR C 3 14  ? 58.945 25.951  73.170 1.00 49.54  ?  14  THR C OG1   1 
ATOM   5909 C CG2   . THR C 3 14  ? 58.348 24.302  74.860 1.00 45.40  ?  14  THR C CG2   1 
ATOM   5910 H H     . THR C 3 14  ? 58.091 22.627  73.256 1.00 56.38  ?  14  THR C H     1 
ATOM   5911 H HA    . THR C 3 14  ? 56.373 24.579  72.425 1.00 56.75  ?  14  THR C HA    1 
ATOM   5912 H HB    . THR C 3 14  ? 57.181 25.743  73.997 1.00 50.66  ?  14  THR C HB    1 
ATOM   5913 H HG1   . THR C 3 14  ? 59.329 26.347  73.804 1.00 59.44  ?  14  THR C HG1   1 
ATOM   5914 H HG21  . THR C 3 14  ? 58.713 24.875  75.553 1.00 54.48  ?  14  THR C HG21  1 
ATOM   5915 H HG22  . THR C 3 14  ? 57.603 23.800  75.226 1.00 54.48  ?  14  THR C HG22  1 
ATOM   5916 H HG23  . THR C 3 14  ? 59.035 23.680  74.572 1.00 54.48  ?  14  THR C HG23  1 
ATOM   5917 N N     . LEU C 3 15  ? 57.408 25.283  70.346 1.00 44.97  ?  15  LEU C N     1 
ATOM   5918 C CA    . LEU C 3 15  ? 57.819 25.401  68.954 1.00 48.03  ?  15  LEU C CA    1 
ATOM   5919 C C     . LEU C 3 15  ? 57.887 26.853  68.501 1.00 50.61  ?  15  LEU C C     1 
ATOM   5920 O O     . LEU C 3 15  ? 56.946 27.614  68.726 1.00 54.73  ?  15  LEU C O     1 
ATOM   5921 C CB    . LEU C 3 15  ? 56.825 24.674  68.054 1.00 45.37  ?  15  LEU C CB    1 
ATOM   5922 C CG    . LEU C 3 15  ? 56.626 23.178  68.190 1.00 48.47  ?  15  LEU C CG    1 
ATOM   5923 C CD1   . LEU C 3 15  ? 55.786 22.726  67.015 1.00 45.67  ?  15  LEU C CD1   1 
ATOM   5924 C CD2   . LEU C 3 15  ? 57.924 22.450  68.229 1.00 48.99  ?  15  LEU C CD2   1 
ATOM   5925 H H     . LEU C 3 15  ? 56.750 25.798  70.550 1.00 53.96  ?  15  LEU C H     1 
ATOM   5926 H HA    . LEU C 3 15  ? 58.712 25.029  68.876 1.00 57.64  ?  15  LEU C HA    1 
ATOM   5927 H HB2   . LEU C 3 15  ? 55.955 25.076  68.207 1.00 54.45  ?  15  LEU C HB2   1 
ATOM   5928 H HB3   . LEU C 3 15  ? 57.104 24.826  67.138 1.00 54.45  ?  15  LEU C HB3   1 
ATOM   5929 H HG    . LEU C 3 15  ? 56.179 22.970  69.025 1.00 58.16  ?  15  LEU C HG    1 
ATOM   5930 H HD11  . LEU C 3 15  ? 55.667 21.765  67.064 1.00 54.81  ?  15  LEU C HD11  1 
ATOM   5931 H HD12  . LEU C 3 15  ? 54.924 23.169  67.054 1.00 54.81  ?  15  LEU C HD12  1 
ATOM   5932 H HD13  . LEU C 3 15  ? 56.243 22.962  66.192 1.00 54.81  ?  15  LEU C HD13  1 
ATOM   5933 H HD21  . LEU C 3 15  ? 57.750 21.498  68.305 1.00 58.79  ?  15  LEU C HD21  1 
ATOM   5934 H HD22  . LEU C 3 15  ? 58.413 22.632  67.412 1.00 58.79  ?  15  LEU C HD22  1 
ATOM   5935 H HD23  . LEU C 3 15  ? 58.434 22.754  68.996 1.00 58.79  ?  15  LEU C HD23  1 
ATOM   5936 N N     . GLU C 3 16  ? 58.961 27.234  67.818 1.00 49.38  ?  16  GLU C N     1 
ATOM   5937 C CA    . GLU C 3 16  ? 59.033 28.573  67.243 1.00 57.26  ?  16  GLU C CA    1 
ATOM   5938 C C     . GLU C 3 16  ? 58.427 28.538  65.847 1.00 52.90  ?  16  GLU C C     1 
ATOM   5939 O O     . GLU C 3 16  ? 58.826 27.717  65.015 1.00 50.29  ?  16  GLU C O     1 
ATOM   5940 C CB    . GLU C 3 16  ? 60.470 29.096  67.183 1.00 63.90  ?  16  GLU C CB    1 
ATOM   5941 C CG    . GLU C 3 16  ? 60.966 29.681  68.492 1.00 74.19  ?  16  GLU C CG    1 
ATOM   5942 C CD    . GLU C 3 16  ? 61.659 28.628  69.337 1.00 81.57  ?  16  GLU C CD    1 
ATOM   5943 O OE1   . GLU C 3 16  ? 61.355 28.550  70.567 1.00 82.67  ?  16  GLU C OE1   1 
ATOM   5944 O OE2   . GLU C 3 16  ? 62.495 27.883  68.751 1.00 78.35  -1 16  GLU C OE2   1 
ATOM   5945 H H     . GLU C 3 16  ? 59.651 26.742  67.676 1.00 59.26  ?  16  GLU C H     1 
ATOM   5946 H HA    . GLU C 3 16  ? 58.532 29.187  67.802 1.00 68.71  ?  16  GLU C HA    1 
ATOM   5947 H HB2   . GLU C 3 16  ? 61.059 28.363  66.944 1.00 76.68  ?  16  GLU C HB2   1 
ATOM   5948 H HB3   . GLU C 3 16  ? 60.519 29.794  66.510 1.00 76.68  ?  16  GLU C HB3   1 
ATOM   5949 H HG2   . GLU C 3 16  ? 61.600 30.391  68.308 1.00 89.02  ?  16  GLU C HG2   1 
ATOM   5950 H HG3   . GLU C 3 16  ? 60.213 30.030  68.995 1.00 89.02  ?  16  GLU C HG3   1 
ATOM   5951 N N     . VAL C 3 17  ? 57.450 29.413  65.597 1.00 55.70  ?  17  VAL C N     1 
ATOM   5952 C CA    . VAL C 3 17  ? 56.739 29.419  64.326 1.00 57.89  ?  17  VAL C CA    1 
ATOM   5953 C C     . VAL C 3 17  ? 56.443 30.836  63.856 1.00 58.19  ?  17  VAL C C     1 
ATOM   5954 O O     . VAL C 3 17  ? 56.422 31.792  64.633 1.00 57.39  ?  17  VAL C O     1 
ATOM   5955 C CB    . VAL C 3 17  ? 55.409 28.625  64.399 1.00 56.39  ?  17  VAL C CB    1 
ATOM   5956 C CG1   . VAL C 3 17  ? 55.651 27.184  64.802 1.00 52.34  ?  17  VAL C CG1   1 
ATOM   5957 C CG2   . VAL C 3 17  ? 54.426 29.284  65.352 1.00 57.51  ?  17  VAL C CG2   1 
ATOM   5958 H H     . VAL C 3 17  ? 57.183 30.013  66.153 1.00 66.85  ?  17  VAL C H     1 
ATOM   5959 H HA    . VAL C 3 17  ? 57.332 29.020  63.670 1.00 69.47  ?  17  VAL C HA    1 
ATOM   5960 H HB    . VAL C 3 17  ? 55.015 28.627  63.512 1.00 67.67  ?  17  VAL C HB    1 
ATOM   5961 H HG11  . VAL C 3 17  ? 54.802 26.714  64.817 1.00 62.81  ?  17  VAL C HG11  1 
ATOM   5962 H HG12  . VAL C 3 17  ? 56.246 26.771  64.157 1.00 62.81  ?  17  VAL C HG12  1 
ATOM   5963 H HG13  . VAL C 3 17  ? 56.055 27.166  65.683 1.00 62.81  ?  17  VAL C HG13  1 
ATOM   5964 H HG21  . VAL C 3 17  ? 53.608 28.763  65.372 1.00 69.01  ?  17  VAL C HG21  1 
ATOM   5965 H HG22  . VAL C 3 17  ? 54.819 29.318  66.238 1.00 69.01  ?  17  VAL C HG22  1 
ATOM   5966 H HG23  . VAL C 3 17  ? 54.238 30.183  65.039 1.00 69.01  ?  17  VAL C HG23  1 
ATOM   5967 N N     . GLU C 3 18  ? 56.185 30.943  62.543 1.00 63.39  ?  18  GLU C N     1 
ATOM   5968 C CA    . GLU C 3 18  ? 55.731 32.153  61.854 1.00 65.02  ?  18  GLU C CA    1 
ATOM   5969 C C     . GLU C 3 18  ? 54.233 32.045  61.569 1.00 62.30  ?  18  GLU C C     1 
ATOM   5970 O O     . GLU C 3 18  ? 53.773 30.990  61.096 1.00 59.08  ?  18  GLU C O     1 
ATOM   5971 C CB    . GLU C 3 18  ? 56.496 32.344  60.539 1.00 64.51  ?  18  GLU C CB    1 
ATOM   5972 C CG    . GLU C 3 18  ? 57.884 33.054  60.615 1.00 66.70  ?  18  GLU C CG    1 
ATOM   5973 C CD    . GLU C 3 18  ? 58.767 32.591  61.775 1.00 71.52  ?  18  GLU C CD    1 
ATOM   5974 O OE1   . GLU C 3 18  ? 58.939 33.382  62.748 1.00 70.27  ?  18  GLU C OE1   1 
ATOM   5975 O OE2   . GLU C 3 18  ? 59.279 31.436  61.711 1.00 71.63  -1 18  GLU C OE2   1 
ATOM   5976 H H     . GLU C 3 18  ? 56.272 30.285  61.998 1.00 76.07  ?  18  GLU C H     1 
ATOM   5977 H HA    . GLU C 3 18  ? 55.893 32.930  62.412 1.00 78.02  ?  18  GLU C HA    1 
ATOM   5978 H HB2   . GLU C 3 18  ? 56.650 31.467  60.154 1.00 77.42  ?  18  GLU C HB2   1 
ATOM   5979 H HB3   . GLU C 3 18  ? 55.941 32.874  59.946 1.00 77.42  ?  18  GLU C HB3   1 
ATOM   5980 H HG2   . GLU C 3 18  ? 58.366 32.881  59.792 1.00 80.04  ?  18  GLU C HG2   1 
ATOM   5981 H HG3   . GLU C 3 18  ? 57.739 34.008  60.720 1.00 80.04  ?  18  GLU C HG3   1 
ATOM   5982 N N     . PRO C 3 19  ? 53.431 33.090  61.815 1.00 62.35  ?  19  PRO C N     1 
ATOM   5983 C CA    . PRO C 3 19  ? 51.975 32.969  61.599 1.00 58.76  ?  19  PRO C CA    1 
ATOM   5984 C C     . PRO C 3 19  ? 51.594 32.569  60.182 1.00 53.81  ?  19  PRO C C     1 
ATOM   5985 O O     . PRO C 3 19  ? 50.450 32.184  59.926 1.00 48.48  ?  19  PRO C O     1 
ATOM   5986 C CB    . PRO C 3 19  ? 51.445 34.371  61.937 1.00 60.53  ?  19  PRO C CB    1 
ATOM   5987 C CG    . PRO C 3 19  ? 52.483 34.963  62.850 1.00 63.70  ?  19  PRO C CG    1 
ATOM   5988 C CD    . PRO C 3 19  ? 53.807 34.383  62.415 1.00 62.61  ?  19  PRO C CD    1 
ATOM   5989 H HA    . PRO C 3 19  ? 51.615 32.315  62.219 1.00 70.52  ?  19  PRO C HA    1 
ATOM   5990 H HB2   . PRO C 3 19  ? 51.356 34.895  61.126 1.00 72.64  ?  19  PRO C HB2   1 
ATOM   5991 H HB3   . PRO C 3 19  ? 50.587 34.302  62.384 1.00 72.64  ?  19  PRO C HB3   1 
ATOM   5992 H HG2   . PRO C 3 19  ? 52.485 35.928  62.758 1.00 76.45  ?  19  PRO C HG2   1 
ATOM   5993 H HG3   . PRO C 3 19  ? 52.287 34.717  63.768 1.00 76.45  ?  19  PRO C HG3   1 
ATOM   5994 H HD2   . PRO C 3 19  ? 54.235 34.956  61.760 1.00 75.14  ?  19  PRO C HD2   1 
ATOM   5995 H HD3   . PRO C 3 19  ? 54.393 34.253  63.176 1.00 75.14  ?  19  PRO C HD3   1 
ATOM   5996 N N     . SER C 3 20  ? 52.550 32.675  59.257 1.00 57.33  ?  20  SER C N     1 
ATOM   5997 C CA    . SER C 3 20  ? 52.344 32.267  57.873 1.00 55.22  ?  20  SER C CA    1 
ATOM   5998 C C     . SER C 3 20  ? 52.435 30.755  57.692 1.00 56.12  ?  20  SER C C     1 
ATOM   5999 O O     . SER C 3 20  ? 51.976 30.237  56.664 1.00 50.31  ?  20  SER C O     1 
ATOM   6000 C CB    . SER C 3 20  ? 53.385 32.951  56.979 1.00 54.14  ?  20  SER C CB    1 
ATOM   6001 O OG    . SER C 3 20  ? 54.409 33.569  57.748 1.00 51.94  ?  20  SER C OG    1 
ATOM   6002 H H     . SER C 3 20  ? 53.338 32.985  59.411 1.00 68.80  ?  20  SER C H     1 
ATOM   6003 H HA    . SER C 3 20  ? 51.462 32.550  57.587 1.00 66.27  ?  20  SER C HA    1 
ATOM   6004 H HB2   . SER C 3 20  ? 53.787 32.284  56.401 1.00 64.96  ?  20  SER C HB2   1 
ATOM   6005 H HB3   . SER C 3 20  ? 52.941 33.629  56.446 1.00 64.96  ?  20  SER C HB3   1 
ATOM   6006 H HG    . SER C 3 20  ? 54.991 33.898  57.240 1.00 62.33  ?  20  SER C HG    1 
ATOM   6007 N N     . ASP C 3 21  ? 52.998 30.048  58.676 1.00 57.56  ?  21  ASP C N     1 
ATOM   6008 C CA    . ASP C 3 21  ? 53.288 28.627  58.540 1.00 56.84  ?  21  ASP C CA    1 
ATOM   6009 C C     . ASP C 3 21  ? 52.015 27.799  58.501 1.00 53.45  ?  21  ASP C C     1 
ATOM   6010 O O     . ASP C 3 21  ? 51.094 27.995  59.301 1.00 52.91  ?  21  ASP C O     1 
ATOM   6011 C CB    . ASP C 3 21  ? 54.163 28.142  59.700 1.00 57.68  ?  21  ASP C CB    1 
ATOM   6012 C CG    . ASP C 3 21  ? 55.617 28.593  59.580 1.00 65.66  ?  21  ASP C CG    1 
ATOM   6013 O OD1   . ASP C 3 21  ? 56.091 28.868  58.439 1.00 64.44  ?  21  ASP C OD1   1 
ATOM   6014 O OD2   . ASP C 3 21  ? 56.287 28.665  60.643 1.00 63.24  -1 21  ASP C OD2   1 
ATOM   6015 H H     . ASP C 3 21  ? 53.223 30.375  59.439 1.00 69.08  ?  21  ASP C H     1 
ATOM   6016 H HA    . ASP C 3 21  ? 53.766 28.494  57.706 1.00 68.21  ?  21  ASP C HA    1 
ATOM   6017 H HB2   . ASP C 3 21  ? 53.808 28.495  60.531 1.00 69.22  ?  21  ASP C HB2   1 
ATOM   6018 H HB3   . ASP C 3 21  ? 54.151 27.172  59.719 1.00 69.22  ?  21  ASP C HB3   1 
ATOM   6019 N N     . THR C 3 22  ? 51.980 26.850  57.579 1.00 52.70  ?  22  THR C N     1 
ATOM   6020 C CA    . THR C 3 22  ? 50.810 26.009  57.437 1.00 55.92  ?  22  THR C CA    1 
ATOM   6021 C C     . THR C 3 22  ? 50.805 24.933  58.514 1.00 53.85  ?  22  THR C C     1 
ATOM   6022 O O     . THR C 3 22  ? 51.661 24.883  59.404 1.00 49.16  ?  22  THR C O     1 
ATOM   6023 C CB    . THR C 3 22  ? 50.765 25.355  56.059 1.00 56.89  ?  22  THR C CB    1 
ATOM   6024 O OG1   . THR C 3 22  ? 51.715 24.285  56.009 1.00 55.08  ?  22  THR C OG1   1 
ATOM   6025 C CG2   . THR C 3 22  ? 51.073 26.373  54.991 1.00 59.49  ?  22  THR C CG2   1 
ATOM   6026 H H     . THR C 3 22  ? 52.617 26.677  57.028 1.00 63.24  ?  22  THR C H     1 
ATOM   6027 H HA    . THR C 3 22  ? 50.029 26.575  57.537 1.00 67.11  ?  22  THR C HA    1 
ATOM   6028 H HB    . THR C 3 22  ? 49.880 24.997  55.888 1.00 68.27  ?  22  THR C HB    1 
ATOM   6029 H HG1   . THR C 3 22  ? 51.735 23.954  55.237 1.00 66.10  ?  22  THR C HG1   1 
ATOM   6030 H HG21  . THR C 3 22  ? 51.046 25.955  54.116 1.00 71.39  ?  22  THR C HG21  1 
ATOM   6031 H HG22  . THR C 3 22  ? 50.419 27.089  55.017 1.00 71.39  ?  22  THR C HG22  1 
ATOM   6032 H HG23  . THR C 3 22  ? 51.956 26.748  55.134 1.00 71.39  ?  22  THR C HG23  1 
ATOM   6033 N N     . ILE C 3 23  ? 49.820 24.046  58.423 1.00 54.63  ?  23  ILE C N     1 
ATOM   6034 C CA    . ILE C 3 23  ? 49.758 22.959  59.384 1.00 54.28  ?  23  ILE C CA    1 
ATOM   6035 C C     . ILE C 3 23  ? 50.684 21.835  58.957 1.00 53.08  ?  23  ILE C C     1 
ATOM   6036 O O     . ILE C 3 23  ? 51.361 21.233  59.793 1.00 51.25  ?  23  ILE C O     1 
ATOM   6037 C CB    . ILE C 3 23  ? 48.308 22.484  59.569 1.00 57.42  ?  23  ILE C CB    1 
ATOM   6038 C CG1   . ILE C 3 23  ? 47.435 23.656  60.028 1.00 55.29  ?  23  ILE C CG1   1 
ATOM   6039 C CG2   . ILE C 3 23  ? 48.242 21.343  60.600 1.00 54.44  ?  23  ILE C CG2   1 
ATOM   6040 C CD1   . ILE C 3 23  ? 47.726 24.118  61.436 1.00 52.13  ?  23  ILE C CD1   1 
ATOM   6041 H H     . ILE C 3 23  ? 49.195 24.054  57.833 1.00 65.55  ?  23  ILE C H     1 
ATOM   6042 H HA    . ILE C 3 23  ? 50.060 23.283  60.246 1.00 65.14  ?  23  ILE C HA    1 
ATOM   6043 H HB    . ILE C 3 23  ? 47.980 22.152  58.719 1.00 68.90  ?  23  ILE C HB    1 
ATOM   6044 H HG12  . ILE C 3 23  ? 47.584 24.407  59.433 1.00 66.35  ?  23  ILE C HG12  1 
ATOM   6045 H HG13  . ILE C 3 23  ? 46.505 23.384  59.992 1.00 66.35  ?  23  ILE C HG13  1 
ATOM   6046 H HG21  . ILE C 3 23  ? 47.314 21.101  60.744 1.00 65.33  ?  23  ILE C HG21  1 
ATOM   6047 H HG22  . ILE C 3 23  ? 48.734 20.580  60.258 1.00 65.33  ?  23  ILE C HG22  1 
ATOM   6048 H HG23  . ILE C 3 23  ? 48.638 21.646  61.432 1.00 65.33  ?  23  ILE C HG23  1 
ATOM   6049 H HD11  . ILE C 3 23  ? 47.175 24.891  61.635 1.00 62.55  ?  23  ILE C HD11  1 
ATOM   6050 H HD12  . ILE C 3 23  ? 47.522 23.399  62.053 1.00 62.55  ?  23  ILE C HD12  1 
ATOM   6051 H HD13  . ILE C 3 23  ? 48.664 24.355  61.503 1.00 62.55  ?  23  ILE C HD13  1 
ATOM   6052 N N     . GLU C 3 24  ? 50.752 21.549  57.655 1.00 58.11  ?  24  GLU C N     1 
ATOM   6053 C CA    . GLU C 3 24  ? 51.794 20.676  57.124 1.00 54.98  ?  24  GLU C CA    1 
ATOM   6054 C C     . GLU C 3 24  ? 53.135 21.043  57.751 1.00 52.81  ?  24  GLU C C     1 
ATOM   6055 O O     . GLU C 3 24  ? 53.929 20.162  58.107 1.00 54.76  ?  24  GLU C O     1 
ATOM   6056 C CB    . GLU C 3 24  ? 51.892 20.798  55.602 1.00 66.02  ?  24  GLU C CB    1 
ATOM   6057 C CG    . GLU C 3 24  ? 51.090 19.784  54.756 1.00 74.69  ?  24  GLU C CG    1 
ATOM   6058 C CD    . GLU C 3 24  ? 50.258 20.452  53.651 1.00 86.38  ?  24  GLU C CD    1 
ATOM   6059 O OE1   . GLU C 3 24  ? 49.212 19.878  53.254 1.00 86.85  ?  24  GLU C OE1   1 
ATOM   6060 O OE2   . GLU C 3 24  ? 50.647 21.558  53.190 1.00 82.76  -1 24  GLU C OE2   1 
ATOM   6061 H H     . GLU C 3 24  ? 50.206 21.848  57.062 1.00 69.73  ?  24  GLU C H     1 
ATOM   6062 H HA    . GLU C 3 24  ? 51.573 19.755  57.334 1.00 65.98  ?  24  GLU C HA    1 
ATOM   6063 H HB2   . GLU C 3 24  ? 51.579 21.681  55.353 1.00 79.23  ?  24  GLU C HB2   1 
ATOM   6064 H HB3   . GLU C 3 24  ? 52.824 20.695  55.355 1.00 79.23  ?  24  GLU C HB3   1 
ATOM   6065 H HG2   . GLU C 3 24  ? 51.708 19.167  54.333 1.00 89.63  ?  24  GLU C HG2   1 
ATOM   6066 H HG3   . GLU C 3 24  ? 50.483 19.299  55.336 1.00 89.63  ?  24  GLU C HG3   1 
ATOM   6067 N N     . ASN C 3 25  ? 53.381 22.348  57.906 1.00 51.53  ?  25  ASN C N     1 
ATOM   6068 C CA    . ASN C 3 25  ? 54.649 22.810  58.456 1.00 50.98  ?  25  ASN C CA    1 
ATOM   6069 C C     . ASN C 3 25  ? 54.782 22.477  59.938 1.00 48.95  ?  25  ASN C C     1 
ATOM   6070 O O     . ASN C 3 25  ? 55.821 21.969  60.376 1.00 47.76  ?  25  ASN C O     1 
ATOM   6071 C CB    . ASN C 3 25  ? 54.794 24.316  58.265 1.00 56.10  ?  25  ASN C CB    1 
ATOM   6072 C CG    . ASN C 3 25  ? 55.044 24.706  56.836 1.00 62.20  ?  25  ASN C CG    1 
ATOM   6073 O OD1   . ASN C 3 25  ? 55.129 23.853  55.944 1.00 67.55  ?  25  ASN C OD1   1 
ATOM   6074 N ND2   . ASN C 3 25  ? 55.177 26.012  56.601 1.00 63.53  ?  25  ASN C ND2   1 
ATOM   6075 H H     . ASN C 3 25  ? 52.833 22.979  57.701 1.00 61.84  ?  25  ASN C H     1 
ATOM   6076 H HA    . ASN C 3 25  ? 55.358 22.358  57.972 1.00 61.17  ?  25  ASN C HA    1 
ATOM   6077 H HB2   . ASN C 3 25  ? 53.977 24.751  58.555 1.00 67.32  ?  25  ASN C HB2   1 
ATOM   6078 H HB3   . ASN C 3 25  ? 55.543 24.630  58.796 1.00 67.32  ?  25  ASN C HB3   1 
ATOM   6079 H HD21  . ASN C 3 25  ? 55.118 26.574  57.249 1.00 76.23  ?  25  ASN C HD21  1 
ATOM   6080 H HD22  . ASN C 3 25  ? 55.321 26.293  55.801 1.00 76.23  ?  25  ASN C HD22  1 
ATOM   6081 N N     . VAL C 3 26  ? 53.773 22.814  60.742 1.00 44.11  ?  26  VAL C N     1 
ATOM   6082 C CA    . VAL C 3 26  ? 53.885 22.552  62.175 1.00 47.90  ?  26  VAL C CA    1 
ATOM   6083 C C     . VAL C 3 26  ? 54.017 21.050  62.442 1.00 47.06  ?  26  VAL C C     1 
ATOM   6084 O O     . VAL C 3 26  ? 54.791 20.628  63.311 1.00 41.59  ?  26  VAL C O     1 
ATOM   6085 C CB    . VAL C 3 26  ? 52.695 23.172  62.936 1.00 46.27  ?  26  VAL C CB    1 
ATOM   6086 C CG1   . VAL C 3 26  ? 51.416 22.433  62.655 1.00 46.14  ?  26  VAL C CG1   1 
ATOM   6087 C CG2   . VAL C 3 26  ? 52.977 23.183  64.433 1.00 41.43  ?  26  VAL C CG2   1 
ATOM   6088 H H     . VAL C 3 26  ? 53.038 23.183  60.491 1.00 52.93  ?  26  VAL C H     1 
ATOM   6089 H HA    . VAL C 3 26  ? 54.693 22.980  62.499 1.00 57.48  ?  26  VAL C HA    1 
ATOM   6090 H HB    . VAL C 3 26  ? 52.581 24.085  62.629 1.00 55.52  ?  26  VAL C HB    1 
ATOM   6091 H HG11  . VAL C 3 26  ? 50.687 22.877  63.116 1.00 55.36  ?  26  VAL C HG11  1 
ATOM   6092 H HG12  . VAL C 3 26  ? 51.254 22.436  61.699 1.00 55.36  ?  26  VAL C HG12  1 
ATOM   6093 H HG13  . VAL C 3 26  ? 51.502 21.521  62.973 1.00 55.36  ?  26  VAL C HG13  1 
ATOM   6094 H HG21  . VAL C 3 26  ? 52.236 23.610  64.890 1.00 49.72  ?  26  VAL C HG21  1 
ATOM   6095 H HG22  . VAL C 3 26  ? 53.075 22.269  64.743 1.00 49.72  ?  26  VAL C HG22  1 
ATOM   6096 H HG23  . VAL C 3 26  ? 53.795 23.678  64.596 1.00 49.72  ?  26  VAL C HG23  1 
ATOM   6097 N N     . LYS C 3 27  ? 53.281 20.219  61.689 1.00 48.00  ?  27  LYS C N     1 
ATOM   6098 C CA    . LYS C 3 27  ? 53.382 18.773  61.866 1.00 38.45  ?  27  LYS C CA    1 
ATOM   6099 C C     . LYS C 3 27  ? 54.779 18.285  61.521 1.00 40.92  ?  27  LYS C C     1 
ATOM   6100 O O     . LYS C 3 27  ? 55.341 17.441  62.222 1.00 43.18  ?  27  LYS C O     1 
ATOM   6101 C CB    . LYS C 3 27  ? 52.350 18.063  61.004 1.00 37.46  ?  27  LYS C CB    1 
ATOM   6102 C CG    . LYS C 3 27  ? 50.930 18.118  61.522 1.00 38.29  ?  27  LYS C CG    1 
ATOM   6103 C CD    . LYS C 3 27  ? 49.936 17.586  60.489 1.00 40.81  ?  27  LYS C CD    1 
ATOM   6104 C CE    . LYS C 3 27  ? 48.503 17.473  61.039 1.00 45.09  ?  27  LYS C CE    1 
ATOM   6105 N NZ    . LYS C 3 27  ? 47.777 16.213  60.627 1.00 47.35  ?  27  LYS C NZ    1 
ATOM   6106 H H     . LYS C 3 27  ? 52.725 20.467  61.081 1.00 57.60  ?  27  LYS C H     1 
ATOM   6107 H HA    . LYS C 3 27  ? 53.197 18.558  62.793 1.00 46.14  ?  27  LYS C HA    1 
ATOM   6108 H HB2   . LYS C 3 27  ? 52.354 18.470  60.124 1.00 44.95  ?  27  LYS C HB2   1 
ATOM   6109 H HB3   . LYS C 3 27  ? 52.599 17.128  60.938 1.00 44.95  ?  27  LYS C HB3   1 
ATOM   6110 H HG2   . LYS C 3 27  ? 50.858 17.575  62.323 1.00 45.95  ?  27  LYS C HG2   1 
ATOM   6111 H HG3   . LYS C 3 27  ? 50.697 19.038  61.724 1.00 45.95  ?  27  LYS C HG3   1 
ATOM   6112 H HD2   . LYS C 3 27  ? 49.918 18.188  59.729 1.00 48.98  ?  27  LYS C HD2   1 
ATOM   6113 H HD3   . LYS C 3 27  ? 50.218 16.702  60.206 1.00 48.98  ?  27  LYS C HD3   1 
ATOM   6114 H HE2   . LYS C 3 27  ? 48.540 17.487  62.009 1.00 54.11  ?  27  LYS C HE2   1 
ATOM   6115 H HE3   . LYS C 3 27  ? 47.986 18.228  60.717 1.00 54.11  ?  27  LYS C HE3   1 
ATOM   6116 H HZ1   . LYS C 3 27  ? 46.947 16.222  60.948 1.00 56.82  ?  27  LYS C HZ1   1 
ATOM   6117 H HZ2   . LYS C 3 27  ? 47.744 16.158  59.740 1.00 56.82  ?  27  LYS C HZ2   1 
ATOM   6118 H HZ3   . LYS C 3 27  ? 48.203 15.499  60.945 1.00 56.82  ?  27  LYS C HZ3   1 
ATOM   6119 N N     . ALA C 3 28  ? 55.373 18.827  60.458 1.00 47.21  ?  28  ALA C N     1 
ATOM   6120 C CA    . ALA C 3 28  ? 56.756 18.490  60.130 1.00 41.67  ?  28  ALA C CA    1 
ATOM   6121 C C     . ALA C 3 28  ? 57.718 18.941  61.218 1.00 43.90  ?  28  ALA C C     1 
ATOM   6122 O O     . ALA C 3 28  ? 58.683 18.238  61.527 1.00 46.02  ?  28  ALA C O     1 
ATOM   6123 C CB    . ALA C 3 28  ? 57.150 19.121  58.803 1.00 41.00  ?  28  ALA C CB    1 
ATOM   6124 H H     . ALA C 3 28  ? 55.002 19.384  59.918 1.00 56.65  ?  28  ALA C H     1 
ATOM   6125 H HA    . ALA C 3 28  ? 56.819 17.525  60.046 1.00 50.00  ?  28  ALA C HA    1 
ATOM   6126 H HB1   . ALA C 3 28  ? 58.070 18.889  58.604 1.00 49.20  ?  28  ALA C HB1   1 
ATOM   6127 H HB2   . ALA C 3 28  ? 56.565 18.783  58.107 1.00 49.20  ?  28  ALA C HB2   1 
ATOM   6128 H HB3   . ALA C 3 28  ? 57.059 20.085  58.873 1.00 49.20  ?  28  ALA C HB3   1 
ATOM   6129 N N     . LYS C 3 29  ? 57.491 20.123  61.797 1.00 47.56  ?  29  LYS C N     1 
ATOM   6130 C CA    . LYS C 3 29  ? 58.354 20.585  62.883 1.00 47.54  ?  29  LYS C CA    1 
ATOM   6131 C C     . LYS C 3 29  ? 58.268 19.647  64.077 1.00 44.62  ?  29  LYS C C     1 
ATOM   6132 O O     . LYS C 3 29  ? 59.245 19.478  64.818 1.00 44.27  ?  29  LYS C O     1 
ATOM   6133 C CB    . LYS C 3 29  ? 57.974 22.006  63.312 1.00 46.99  ?  29  LYS C CB    1 
ATOM   6134 C CG    . LYS C 3 29  ? 58.628 23.128  62.518 1.00 49.65  ?  29  LYS C CG    1 
ATOM   6135 C CD    . LYS C 3 29  ? 58.046 24.513  62.910 1.00 53.94  ?  29  LYS C CD    1 
ATOM   6136 C CE    . LYS C 3 29  ? 57.954 25.530  61.746 1.00 51.49  ?  29  LYS C CE    1 
ATOM   6137 N NZ    . LYS C 3 29  ? 59.000 26.612  61.785 1.00 55.54  ?  29  LYS C NZ    1 
ATOM   6138 H H     . LYS C 3 29  ? 56.858 20.664  61.584 1.00 57.08  ?  29  LYS C H     1 
ATOM   6139 H HA    . LYS C 3 29  ? 59.268 20.604  62.558 1.00 57.05  ?  29  LYS C HA    1 
ATOM   6140 H HB2   . LYS C 3 29  ? 57.014 22.107  63.217 1.00 56.39  ?  29  LYS C HB2   1 
ATOM   6141 H HB3   . LYS C 3 29  ? 58.229 22.123  64.240 1.00 56.39  ?  29  LYS C HB3   1 
ATOM   6142 H HG2   . LYS C 3 29  ? 59.581 23.136  62.697 1.00 59.57  ?  29  LYS C HG2   1 
ATOM   6143 H HG3   . LYS C 3 29  ? 58.469 22.987  61.571 1.00 59.57  ?  29  LYS C HG3   1 
ATOM   6144 H HD2   . LYS C 3 29  ? 57.148 24.384  63.255 1.00 64.73  ?  29  LYS C HD2   1 
ATOM   6145 H HD3   . LYS C 3 29  ? 58.611 24.903  63.594 1.00 64.73  ?  29  LYS C HD3   1 
ATOM   6146 H HE2   . LYS C 3 29  ? 58.057 25.053  60.908 1.00 61.79  ?  29  LYS C HE2   1 
ATOM   6147 H HE3   . LYS C 3 29  ? 57.086 25.961  61.778 1.00 61.79  ?  29  LYS C HE3   1 
ATOM   6148 H HZ1   . LYS C 3 29  ? 58.890 27.167  61.098 1.00 66.65  ?  29  LYS C HZ1   1 
ATOM   6149 H HZ2   . LYS C 3 29  ? 58.933 27.074  62.543 1.00 66.65  ?  29  LYS C HZ2   1 
ATOM   6150 H HZ3   . LYS C 3 29  ? 59.813 26.252  61.737 1.00 66.65  ?  29  LYS C HZ3   1 
ATOM   6151 N N     . ILE C 3 30  ? 57.089 19.063  64.301 1.00 43.69  ?  30  ILE C N     1 
ATOM   6152 C CA    . ILE C 3 30  ? 56.910 18.124  65.405 1.00 47.09  ?  30  ILE C CA    1 
ATOM   6153 C C     . ILE C 3 30  ? 57.667 16.828  65.125 1.00 43.45  ?  30  ILE C C     1 
ATOM   6154 O O     . ILE C 3 30  ? 58.326 16.263  66.005 1.00 40.06  ?  30  ILE C O     1 
ATOM   6155 C CB    . ILE C 3 30  ? 55.405 17.876  65.644 1.00 44.08  ?  30  ILE C CB    1 
ATOM   6156 C CG1   . ILE C 3 30  ? 54.753 19.140  66.216 1.00 42.37  ?  30  ILE C CG1   1 
ATOM   6157 C CG2   . ILE C 3 30  ? 55.173 16.684  66.568 1.00 41.41  ?  30  ILE C CG2   1 
ATOM   6158 C CD1   . ILE C 3 30  ? 53.201 19.090  66.291 1.00 43.33  ?  30  ILE C CD1   1 
ATOM   6159 H H     . ILE C 3 30  ? 56.381 19.193  63.831 1.00 52.43  ?  30  ILE C H     1 
ATOM   6160 H HA    . ILE C 3 30  ? 57.280 18.509  66.215 1.00 56.50  ?  30  ILE C HA    1 
ATOM   6161 H HB    . ILE C 3 30  ? 54.997 17.666  64.789 1.00 52.90  ?  30  ILE C HB    1 
ATOM   6162 H HG12  . ILE C 3 30  ? 55.084 19.278  67.117 1.00 50.84  ?  30  ILE C HG12  1 
ATOM   6163 H HG13  . ILE C 3 30  ? 54.994 19.894  65.655 1.00 50.84  ?  30  ILE C HG13  1 
ATOM   6164 H HG21  . ILE C 3 30  ? 54.218 16.539  66.663 1.00 49.69  ?  30  ILE C HG21  1 
ATOM   6165 H HG22  . ILE C 3 30  ? 55.590 15.898  66.181 1.00 49.69  ?  30  ILE C HG22  1 
ATOM   6166 H HG23  . ILE C 3 30  ? 55.566 16.874  67.434 1.00 49.69  ?  30  ILE C HG23  1 
ATOM   6167 H HD11  . ILE C 3 30  ? 52.874 19.935  66.639 1.00 51.99  ?  30  ILE C HD11  1 
ATOM   6168 H HD12  . ILE C 3 30  ? 52.847 18.940  65.401 1.00 51.99  ?  30  ILE C HD12  1 
ATOM   6169 H HD13  . ILE C 3 30  ? 52.936 18.366  66.879 1.00 51.99  ?  30  ILE C HD13  1 
ATOM   6170 N N     . GLN C 3 31  ? 57.567 16.333  63.895 1.00 43.07  ?  31  GLN C N     1 
ATOM   6171 C CA    . GLN C 3 31  ? 58.364 15.188  63.481 1.00 41.07  ?  31  GLN C CA    1 
ATOM   6172 C C     . GLN C 3 31  ? 59.847 15.431  63.712 1.00 40.73  ?  31  GLN C C     1 
ATOM   6173 O O     . GLN C 3 31  ? 60.569 14.563  64.207 1.00 38.67  ?  31  GLN C O     1 
ATOM   6174 C CB    . GLN C 3 31  ? 58.086 14.921  62.013 1.00 39.20  ?  31  GLN C CB    1 
ATOM   6175 C CG    . GLN C 3 31  ? 59.106 14.089  61.340 1.00 38.99  ?  31  GLN C CG    1 
ATOM   6176 C CD    . GLN C 3 31  ? 58.575 13.522  60.055 1.00 36.83  ?  31  GLN C CD    1 
ATOM   6177 O OE1   . GLN C 3 31  ? 58.416 12.303  59.920 1.00 34.56  ?  31  GLN C OE1   1 
ATOM   6178 N NE2   . GLN C 3 31  ? 58.280 14.406  59.094 1.00 40.27  ?  31  GLN C NE2   1 
ATOM   6179 H H     . GLN C 3 31  ? 57.046 16.642  63.284 1.00 51.69  ?  31  GLN C H     1 
ATOM   6180 H HA    . GLN C 3 31  ? 58.115 14.409  64.002 1.00 49.28  ?  31  GLN C HA    1 
ATOM   6181 H HB2   . GLN C 3 31  ? 57.235 14.460  61.939 1.00 47.04  ?  31  GLN C HB2   1 
ATOM   6182 H HB3   . GLN C 3 31  ? 58.045 15.770  61.547 1.00 47.04  ?  31  GLN C HB3   1 
ATOM   6183 H HG2   . GLN C 3 31  ? 59.884 14.632  61.138 1.00 46.79  ?  31  GLN C HG2   1 
ATOM   6184 H HG3   . GLN C 3 31  ? 59.356 13.353  61.920 1.00 46.79  ?  31  GLN C HG3   1 
ATOM   6185 H HE21  . GLN C 3 31  ? 58.398 15.247  59.232 1.00 48.33  ?  31  GLN C HE21  1 
ATOM   6186 H HE22  . GLN C 3 31  ? 57.972 14.134  58.339 1.00 48.33  ?  31  GLN C HE22  1 
ATOM   6187 N N     . ASP C 3 32  ? 60.323 16.615  63.362 1.00 43.70  ?  32  ASP C N     1 
ATOM   6188 C CA    . ASP C 3 32  ? 61.750 16.863  63.493 1.00 48.24  ?  32  ASP C CA    1 
ATOM   6189 C C     . ASP C 3 32  ? 62.160 16.885  64.963 1.00 47.96  ?  32  ASP C C     1 
ATOM   6190 O O     . ASP C 3 32  ? 63.219 16.352  65.327 1.00 53.63  ?  32  ASP C O     1 
ATOM   6191 C CB    . ASP C 3 32  ? 62.117 18.157  62.755 1.00 48.30  ?  32  ASP C CB    1 
ATOM   6192 C CG    . ASP C 3 32  ? 61.886 18.056  61.210 1.00 55.80  ?  32  ASP C CG    1 
ATOM   6193 O OD1   . ASP C 3 32  ? 61.051 17.224  60.748 1.00 56.73  ?  32  ASP C OD1   1 
ATOM   6194 O OD2   . ASP C 3 32  ? 62.530 18.815  60.443 1.00 59.76  -1 32  ASP C OD2   1 
ATOM   6195 H H     . ASP C 3 32  ? 59.858 17.271  63.056 1.00 52.44  ?  32  ASP C H     1 
ATOM   6196 H HA    . ASP C 3 32  ? 62.256 16.151  63.071 1.00 57.88  ?  32  ASP C HA    1 
ATOM   6197 H HB2   . ASP C 3 32  ? 61.569 18.881  63.094 1.00 57.96  ?  32  ASP C HB2   1 
ATOM   6198 H HB3   . ASP C 3 32  ? 63.055 18.352  62.906 1.00 57.96  ?  32  ASP C HB3   1 
ATOM   6199 N N     . LYS C 3 33  ? 61.306 17.428  65.833 1.00 45.80  ?  33  LYS C N     1 
ATOM   6200 C CA    . LYS C 3 33  ? 61.658 17.572  67.242 1.00 45.94  ?  33  LYS C CA    1 
ATOM   6201 C C     . LYS C 3 33  ? 61.434 16.293  68.038 1.00 46.37  ?  33  LYS C C     1 
ATOM   6202 O O     . LYS C 3 33  ? 62.147 16.052  69.021 1.00 52.70  ?  33  LYS C O     1 
ATOM   6203 C CB    . LYS C 3 33  ? 60.834 18.693  67.887 1.00 52.56  ?  33  LYS C CB    1 
ATOM   6204 C CG    . LYS C 3 33  ? 61.453 20.085  67.830 1.00 58.22  ?  33  LYS C CG    1 
ATOM   6205 C CD    . LYS C 3 33  ? 61.111 20.879  69.091 1.00 56.32  ?  33  LYS C CD    1 
ATOM   6206 C CE    . LYS C 3 33  ? 61.950 20.423  70.277 1.00 69.02  ?  33  LYS C CE    1 
ATOM   6207 N NZ    . LYS C 3 33  ? 62.619 21.565  71.009 1.00 75.42  ?  33  LYS C NZ    1 
ATOM   6208 H H     . LYS C 3 33  ? 60.522 17.720  65.632 1.00 54.96  ?  33  LYS C H     1 
ATOM   6209 H HA    . LYS C 3 33  ? 62.599 17.804  67.285 1.00 55.13  ?  33  LYS C HA    1 
ATOM   6210 H HB2   . LYS C 3 33  ? 59.978 18.740  67.435 1.00 63.07  ?  33  LYS C HB2   1 
ATOM   6211 H HB3   . LYS C 3 33  ? 60.704 18.475  68.823 1.00 63.07  ?  33  LYS C HB3   1 
ATOM   6212 H HG2   . LYS C 3 33  ? 62.418 20.010  67.765 1.00 69.86  ?  33  LYS C HG2   1 
ATOM   6213 H HG3   . LYS C 3 33  ? 61.106 20.564  67.061 1.00 69.86  ?  33  LYS C HG3   1 
ATOM   6214 H HD2   . LYS C 3 33  ? 61.287 21.820  68.937 1.00 67.58  ?  33  LYS C HD2   1 
ATOM   6215 H HD3   . LYS C 3 33  ? 60.175 20.747  69.310 1.00 67.58  ?  33  LYS C HD3   1 
ATOM   6216 H HE2   . LYS C 3 33  ? 61.376 19.960  70.907 1.00 82.82  ?  33  LYS C HE2   1 
ATOM   6217 H HE3   . LYS C 3 33  ? 62.644 19.825  69.959 1.00 82.82  ?  33  LYS C HE3   1 
ATOM   6218 H HZ1   . LYS C 3 33  ? 63.093 21.251  71.694 1.00 90.50  ?  33  LYS C HZ1   1 
ATOM   6219 H HZ2   . LYS C 3 33  ? 63.163 22.003  70.458 1.00 90.50  ?  33  LYS C HZ2   1 
ATOM   6220 H HZ3   . LYS C 3 33  ? 62.005 22.129  71.319 1.00 90.50  ?  33  LYS C HZ3   1 
ATOM   6221 N N     . GLU C 3 34  ? 60.440 15.486  67.655 1.00 42.83  ?  34  GLU C N     1 
ATOM   6222 C CA    . GLU C 3 34  ? 59.991 14.353  68.459 1.00 41.14  ?  34  GLU C CA    1 
ATOM   6223 C C     . GLU C 3 34  ? 59.933 13.021  67.719 1.00 39.42  ?  34  GLU C C     1 
ATOM   6224 O O     . GLU C 3 34  ? 59.853 11.976  68.389 1.00 35.07  ?  34  GLU C O     1 
ATOM   6225 C CB    . GLU C 3 34  ? 58.592 14.636  69.044 1.00 43.36  ?  34  GLU C CB    1 
ATOM   6226 C CG    . GLU C 3 34  ? 58.594 15.321  70.416 1.00 43.59  ?  34  GLU C CG    1 
ATOM   6227 C CD    . GLU C 3 34  ? 58.784 14.354  71.569 1.00 47.54  ?  34  GLU C CD    1 
ATOM   6228 O OE1   . GLU C 3 34  ? 57.783 13.924  72.181 1.00 57.64  ?  34  GLU C OE1   1 
ATOM   6229 O OE2   . GLU C 3 34  ? 59.942 14.011  71.869 1.00 52.04  -1 34  GLU C OE2   1 
ATOM   6230 H H     . GLU C 3 34  ? 60.004 15.579  66.920 1.00 51.39  ?  34  GLU C H     1 
ATOM   6231 H HA    . GLU C 3 34  ? 60.616 14.245  69.192 1.00 49.37  ?  34  GLU C HA    1 
ATOM   6232 H HB2   . GLU C 3 34  ? 58.113 15.215  68.430 1.00 52.04  ?  34  GLU C HB2   1 
ATOM   6233 H HB3   . GLU C 3 34  ? 58.122 13.793  69.140 1.00 52.04  ?  34  GLU C HB3   1 
ATOM   6234 H HG2   . GLU C 3 34  ? 59.320 15.964  70.444 1.00 52.31  ?  34  GLU C HG2   1 
ATOM   6235 H HG3   . GLU C 3 34  ? 57.746 15.773  70.543 1.00 52.31  ?  34  GLU C HG3   1 
ATOM   6236 N N     . GLY C 3 35  ? 59.941 13.013  66.374 1.00 38.47  ?  35  GLY C N     1 
ATOM   6237 C CA    . GLY C 3 35  ? 59.960 11.797  65.587 1.00 33.53  ?  35  GLY C CA    1 
ATOM   6238 C C     . GLY C 3 35  ? 58.619 11.376  65.043 1.00 36.80  ?  35  GLY C C     1 
ATOM   6239 O O     . GLY C 3 35  ? 58.569 10.496  64.178 1.00 39.96  ?  35  GLY C O     1 
ATOM   6240 H H     . GLY C 3 35  ? 59.936 13.727  65.894 1.00 46.17  ?  35  GLY C H     1 
ATOM   6241 H HA2   . GLY C 3 35  ? 60.558 11.923  64.834 1.00 40.23  ?  35  GLY C HA2   1 
ATOM   6242 H HA3   . GLY C 3 35  ? 60.296 11.074  66.140 1.00 40.23  ?  35  GLY C HA3   1 
ATOM   6243 N N     . ILE C 3 36  ? 57.543 11.988  65.510 1.00 37.72  ?  36  ILE C N     1 
ATOM   6244 C CA    . ILE C 3 36  ? 56.186 11.574  65.151 1.00 35.99  ?  36  ILE C CA    1 
ATOM   6245 C C     . ILE C 3 36  ? 55.964 11.814  63.664 1.00 34.57  ?  36  ILE C C     1 
ATOM   6246 O O     . ILE C 3 36  ? 56.122 12.947  63.191 1.00 36.11  ?  36  ILE C O     1 
ATOM   6247 C CB    . ILE C 3 36  ? 55.169 12.342  65.997 1.00 34.43  ?  36  ILE C CB    1 
ATOM   6248 C CG1   . ILE C 3 36  ? 55.605 12.254  67.461 1.00 32.22  ?  36  ILE C CG1   1 
ATOM   6249 C CG2   . ILE C 3 36  ? 53.753 11.819  65.784 1.00 34.17  ?  36  ILE C CG2   1 
ATOM   6250 C CD1   . ILE C 3 36  ? 54.687 12.918  68.385 1.00 29.87  ?  36  ILE C CD1   1 
ATOM   6251 H H     . ILE C 3 36  ? 57.564 12.660  66.047 1.00 45.27  ?  36  ILE C H     1 
ATOM   6252 H HA    . ILE C 3 36  ? 56.076 10.625  65.321 1.00 43.19  ?  36  ILE C HA    1 
ATOM   6253 H HB    . ILE C 3 36  ? 55.150 13.273  65.724 1.00 41.31  ?  36  ILE C HB    1 
ATOM   6254 H HG12  . ILE C 3 36  ? 55.659 11.320  67.715 1.00 38.67  ?  36  ILE C HG12  1 
ATOM   6255 H HG13  . ILE C 3 36  ? 56.475 12.674  67.554 1.00 38.67  ?  36  ILE C HG13  1 
ATOM   6256 H HG21  . ILE C 3 36  ? 53.137 12.354  66.308 1.00 41.00  ?  36  ILE C HG21  1 
ATOM   6257 H HG22  . ILE C 3 36  ? 53.530 11.886  64.842 1.00 41.00  ?  36  ILE C HG22  1 
ATOM   6258 H HG23  . ILE C 3 36  ? 53.712 10.893  66.069 1.00 41.00  ?  36  ILE C HG23  1 
ATOM   6259 H HD11  . ILE C 3 36  ? 55.054 12.873  69.282 1.00 35.84  ?  36  ILE C HD11  1 
ATOM   6260 H HD12  . ILE C 3 36  ? 54.583 13.844  68.117 1.00 35.84  ?  36  ILE C HD12  1 
ATOM   6261 H HD13  . ILE C 3 36  ? 53.829 12.467  68.356 1.00 35.84  ?  36  ILE C HD13  1 
ATOM   6262 N N     . PRO C 3 37  ? 55.627 10.795  62.893 1.00 33.70  ?  37  PRO C N     1 
ATOM   6263 C CA    . PRO C 3 37  ? 55.262 11.010  61.480 1.00 36.66  ?  37  PRO C CA    1 
ATOM   6264 C C     . PRO C 3 37  ? 53.970 11.800  61.335 1.00 35.22  ?  37  PRO C C     1 
ATOM   6265 O O     . PRO C 3 37  ? 52.978 11.538  62.029 1.00 33.46  ?  37  PRO C O     1 
ATOM   6266 C CB    . PRO C 3 37  ? 55.116 9.579   60.938 1.00 35.08  ?  37  PRO C CB    1 
ATOM   6267 C CG    . PRO C 3 37  ? 55.005 8.716   62.130 1.00 33.41  ?  37  PRO C CG    1 
ATOM   6268 C CD    . PRO C 3 37  ? 55.781 9.371   63.219 1.00 32.87  ?  37  PRO C CD    1 
ATOM   6269 H HA    . PRO C 3 37  ? 55.971 11.476  61.010 1.00 43.99  ?  37  PRO C HA    1 
ATOM   6270 H HB2   . PRO C 3 37  ? 54.318 9.515   60.391 1.00 42.10  ?  37  PRO C HB2   1 
ATOM   6271 H HB3   . PRO C 3 37  ? 55.898 9.345   60.414 1.00 42.10  ?  37  PRO C HB3   1 
ATOM   6272 H HG2   . PRO C 3 37  ? 54.072 8.633   62.382 1.00 40.09  ?  37  PRO C HG2   1 
ATOM   6273 H HG3   . PRO C 3 37  ? 55.373 7.842   61.929 1.00 40.09  ?  37  PRO C HG3   1 
ATOM   6274 H HD2   . PRO C 3 37  ? 55.403 9.169   64.089 1.00 39.44  ?  37  PRO C HD2   1 
ATOM   6275 H HD3   . PRO C 3 37  ? 56.714 9.105   63.192 1.00 39.44  ?  37  PRO C HD3   1 
ATOM   6276 N N     . PRO C 3 38  ? 53.947 12.793  60.447 1.00 37.57  ?  38  PRO C N     1 
ATOM   6277 C CA    . PRO C 3 38  ? 52.768 13.677  60.368 1.00 40.01  ?  38  PRO C CA    1 
ATOM   6278 C C     . PRO C 3 38  ? 51.455 13.022  59.934 1.00 38.56  ?  38  PRO C C     1 
ATOM   6279 O O     . PRO C 3 38  ? 50.386 13.563  60.246 1.00 39.38  ?  38  PRO C O     1 
ATOM   6280 C CB    . PRO C 3 38  ? 53.201 14.746  59.352 1.00 39.62  ?  38  PRO C CB    1 
ATOM   6281 C CG    . PRO C 3 38  ? 54.627 14.485  59.030 1.00 36.65  ?  38  PRO C CG    1 
ATOM   6282 C CD    . PRO C 3 38  ? 55.156 13.473  59.966 1.00 35.07  ?  38  PRO C CD    1 
ATOM   6283 H HA    . PRO C 3 38  ? 52.634 14.064  61.247 1.00 48.02  ?  38  PRO C HA    1 
ATOM   6284 H HB2   . PRO C 3 38  ? 52.653 14.673  58.554 1.00 47.54  ?  38  PRO C HB2   1 
ATOM   6285 H HB3   . PRO C 3 38  ? 53.097 15.626  59.746 1.00 47.54  ?  38  PRO C HB3   1 
ATOM   6286 H HG2   . PRO C 3 38  ? 54.688 14.159  58.118 1.00 43.98  ?  38  PRO C HG2   1 
ATOM   6287 H HG3   . PRO C 3 38  ? 55.126 15.312  59.120 1.00 43.98  ?  38  PRO C HG3   1 
ATOM   6288 H HD2   . PRO C 3 38  ? 55.742 12.851  59.506 1.00 42.09  ?  38  PRO C HD2   1 
ATOM   6289 H HD3   . PRO C 3 38  ? 55.630 13.895  60.699 1.00 42.09  ?  38  PRO C HD3   1 
ATOM   6290 N N     . ASP C 3 39  ? 51.476 11.903  59.207 1.00 44.05  ?  39  ASP C N     1 
ATOM   6291 C CA    . ASP C 3 39  ? 50.214 11.262  58.817 1.00 48.94  ?  39  ASP C CA    1 
ATOM   6292 C C     . ASP C 3 39  ? 49.498 10.649  60.017 1.00 42.96  ?  39  ASP C C     1 
ATOM   6293 O O     . ASP C 3 39  ? 48.338 10.248  59.901 1.00 45.42  ?  39  ASP C O     1 
ATOM   6294 C CB    . ASP C 3 39  ? 50.448 10.195  57.726 1.00 54.08  ?  39  ASP C CB    1 
ATOM   6295 C CG    . ASP C 3 39  ? 50.911 10.794  56.374 1.00 57.66  ?  39  ASP C CG    1 
ATOM   6296 O OD1   . ASP C 3 39  ? 50.791 10.088  55.345 1.00 61.01  ?  39  ASP C OD1   1 
ATOM   6297 O OD2   . ASP C 3 39  ? 51.403 11.948  56.336 1.00 54.33  -1 39  ASP C OD2   1 
ATOM   6298 H H     . ASP C 3 39  ? 52.188 11.504  58.934 1.00 52.86  ?  39  ASP C H     1 
ATOM   6299 H HA    . ASP C 3 39  ? 49.632 11.931  58.423 1.00 58.72  ?  39  ASP C HA    1 
ATOM   6300 H HB2   . ASP C 3 39  ? 51.134 9.580   58.030 1.00 64.89  ?  39  ASP C HB2   1 
ATOM   6301 H HB3   . ASP C 3 39  ? 49.619 9.716   57.571 1.00 64.89  ?  39  ASP C HB3   1 
ATOM   6302 N N     . GLN C 3 40  ? 50.174 10.586  61.156 1.00 41.44  ?  40  GLN C N     1 
ATOM   6303 C CA    . GLN C 3 40  ? 49.638 10.149  62.431 1.00 39.69  ?  40  GLN C CA    1 
ATOM   6304 C C     . GLN C 3 40  ? 49.195 11.321  63.286 1.00 39.37  ?  40  GLN C C     1 
ATOM   6305 O O     . GLN C 3 40  ? 48.492 11.129  64.283 1.00 38.65  ?  40  GLN C O     1 
ATOM   6306 C CB    . GLN C 3 40  ? 50.728 9.342   63.161 1.00 40.93  ?  40  GLN C CB    1 
ATOM   6307 C CG    . GLN C 3 40  ? 50.305 8.464   64.327 1.00 42.68  ?  40  GLN C CG    1 
ATOM   6308 C CD    . GLN C 3 40  ? 51.504 7.961   65.138 1.00 38.85  ?  40  GLN C CD    1 
ATOM   6309 O OE1   . GLN C 3 40  ? 52.649 8.324   64.867 1.00 38.59  ?  40  GLN C OE1   1 
ATOM   6310 N NE2   . GLN C 3 40  ? 51.237 7.139   66.141 1.00 33.88  ?  40  GLN C NE2   1 
ATOM   6311 H H     . GLN C 3 40  ? 51.003 10.807  61.218 1.00 49.73  ?  40  GLN C H     1 
ATOM   6312 H HA    . GLN C 3 40  ? 48.869 9.570   62.311 1.00 47.63  ?  40  GLN C HA    1 
ATOM   6313 H HB2   . GLN C 3 40  ? 51.148 8.757   62.511 1.00 49.11  ?  40  GLN C HB2   1 
ATOM   6314 H HB3   . GLN C 3 40  ? 51.379 9.971   63.510 1.00 49.11  ?  40  GLN C HB3   1 
ATOM   6315 H HG2   . GLN C 3 40  ? 49.732 8.976   64.920 1.00 51.21  ?  40  GLN C HG2   1 
ATOM   6316 H HG3   . GLN C 3 40  ? 49.824 7.693   63.987 1.00 51.21  ?  40  GLN C HG3   1 
ATOM   6317 H HE21  . GLN C 3 40  ? 50.424 6.915   66.309 1.00 40.66  ?  40  GLN C HE21  1 
ATOM   6318 H HE22  . GLN C 3 40  ? 51.877 6.830   66.626 1.00 40.66  ?  40  GLN C HE22  1 
ATOM   6319 N N     . GLN C 3 41  ? 49.587 12.529  62.919 1.00 42.73  ?  41  GLN C N     1 
ATOM   6320 C CA    . GLN C 3 41  ? 49.322 13.675  63.770 1.00 42.18  ?  41  GLN C CA    1 
ATOM   6321 C C     . GLN C 3 41  ? 47.918 14.205  63.547 1.00 37.24  ?  41  GLN C C     1 
ATOM   6322 O O     . GLN C 3 41  ? 47.389 14.183  62.433 1.00 39.12  ?  41  GLN C O     1 
ATOM   6323 C CB    . GLN C 3 41  ? 50.359 14.770  63.536 1.00 37.47  ?  41  GLN C CB    1 
ATOM   6324 C CG    . GLN C 3 41  ? 51.671 14.432  64.207 1.00 35.83  ?  41  GLN C CG    1 
ATOM   6325 C CD    . GLN C 3 41  ? 52.677 15.521  64.067 1.00 39.00  ?  41  GLN C CD    1 
ATOM   6326 O OE1   . GLN C 3 41  ? 52.360 16.696  64.240 1.00 43.06  ?  41  GLN C OE1   1 
ATOM   6327 N NE2   . GLN C 3 41  ? 53.901 15.152  63.726 1.00 38.82  ?  41  GLN C NE2   1 
ATOM   6328 H H     . GLN C 3 41  ? 50.005 12.710  62.189 1.00 51.27  ?  41  GLN C H     1 
ATOM   6329 H HA    . GLN C 3 41  ? 49.385 13.403  64.699 1.00 50.61  ?  41  GLN C HA    1 
ATOM   6330 H HB2   . GLN C 3 41  ? 50.517 14.866  62.584 1.00 44.96  ?  41  GLN C HB2   1 
ATOM   6331 H HB3   . GLN C 3 41  ? 50.033 15.606  63.905 1.00 44.96  ?  41  GLN C HB3   1 
ATOM   6332 H HG2   . GLN C 3 41  ? 51.515 14.286  65.153 1.00 43.00  ?  41  GLN C HG2   1 
ATOM   6333 H HG3   . GLN C 3 41  ? 52.036 13.630  63.803 1.00 43.00  ?  41  GLN C HG3   1 
ATOM   6334 H HE21  . GLN C 3 41  ? 54.080 14.321  63.598 1.00 46.58  ?  41  GLN C HE21  1 
ATOM   6335 H HE22  . GLN C 3 41  ? 54.518 15.744  63.632 1.00 46.58  ?  41  GLN C HE22  1 
ATOM   6336 N N     . ARG C 3 42  ? 47.309 14.615  64.649 1.00 37.10  ?  42  ARG C N     1 
ATOM   6337 C CA    . ARG C 3 42  ? 46.009 15.264  64.689 1.00 42.09  ?  42  ARG C CA    1 
ATOM   6338 C C     . ARG C 3 42  ? 46.184 16.462  65.600 1.00 40.59  ?  42  ARG C C     1 
ATOM   6339 O O     . ARG C 3 42  ? 46.341 16.292  66.814 1.00 34.28  ?  42  ARG C O     1 
ATOM   6340 C CB    . ARG C 3 42  ? 44.926 14.349  65.252 1.00 44.82  ?  42  ARG C CB    1 
ATOM   6341 C CG    . ARG C 3 42  ? 44.256 13.451  64.254 1.00 52.15  ?  42  ARG C CG    1 
ATOM   6342 C CD    . ARG C 3 42  ? 42.852 13.168  64.721 1.00 58.00  ?  42  ARG C CD    1 
ATOM   6343 N NE    . ARG C 3 42  ? 42.708 11.892  65.421 1.00 57.38  ?  42  ARG C NE    1 
ATOM   6344 C CZ    . ARG C 3 42  ? 42.162 10.802  64.881 1.00 59.48  ?  42  ARG C CZ    1 
ATOM   6345 N NH1   . ARG C 3 42  ? 41.713 10.820  63.618 1.00 62.11  ?  42  ARG C NH1   1 
ATOM   6346 N NH2   . ARG C 3 42  ? 42.064 9.682   65.600 1.00 52.36  ?  42  ARG C NH2   1 
ATOM   6347 H H     . ARG C 3 42  ? 47.650 14.523  65.433 1.00 44.52  ?  42  ARG C H     1 
ATOM   6348 H HA    . ARG C 3 42  ? 45.739 15.529  63.796 1.00 50.51  ?  42  ARG C HA    1 
ATOM   6349 H HB2   . ARG C 3 42  ? 45.327 13.782  65.929 1.00 53.79  ?  42  ARG C HB2   1 
ATOM   6350 H HB3   . ARG C 3 42  ? 44.236 14.903  65.651 1.00 53.79  ?  42  ARG C HB3   1 
ATOM   6351 H HG2   . ARG C 3 42  ? 44.221 13.886  63.388 1.00 62.57  ?  42  ARG C HG2   1 
ATOM   6352 H HG3   . ARG C 3 42  ? 44.741 12.613  64.185 1.00 62.57  ?  42  ARG C HG3   1 
ATOM   6353 H HD2   . ARG C 3 42  ? 42.577 13.872  65.330 1.00 69.60  ?  42  ARG C HD2   1 
ATOM   6354 H HD3   . ARG C 3 42  ? 42.264 13.150  63.949 1.00 69.60  ?  42  ARG C HD3   1 
ATOM   6355 H HE    . ARG C 3 42  ? 42.993 11.842  66.231 1.00 68.86  ?  42  ARG C HE    1 
ATOM   6356 H HH11  . ARG C 3 42  ? 41.772 11.537  63.142 1.00 74.54  ?  42  ARG C HH11  1 
ATOM   6357 H HH21  . ARG C 3 42  ? 42.352 9.665   66.411 1.00 62.83  ?  42  ARG C HH21  1 
ATOM   6358 H HH22  . ARG C 3 42  ? 41.713 8.978   65.254 1.00 62.83  ?  42  ARG C HH22  1 
ATOM   6359 N N     . LEU C 3 43  ? 46.166 17.662  65.028 1.00 43.22  ?  43  LEU C N     1 
ATOM   6360 C CA    . LEU C 3 43  ? 46.289 18.884  65.810 1.00 41.67  ?  43  LEU C CA    1 
ATOM   6361 C C     . LEU C 3 43  ? 44.910 19.463  66.082 1.00 39.13  ?  43  LEU C C     1 
ATOM   6362 O O     . LEU C 3 43  ? 44.078 19.549  65.170 1.00 38.39  ?  43  LEU C O     1 
ATOM   6363 C CB    . LEU C 3 43  ? 47.180 19.887  65.088 1.00 39.41  ?  43  LEU C CB    1 
ATOM   6364 C CG    . LEU C 3 43  ? 48.617 19.386  64.965 1.00 36.22  ?  43  LEU C CG    1 
ATOM   6365 C CD1   . LEU C 3 43  ? 49.322 20.051  63.797 1.00 38.06  ?  43  LEU C CD1   1 
ATOM   6366 C CD2   . LEU C 3 43  ? 49.385 19.583  66.259 1.00 34.46  ?  43  LEU C CD2   1 
ATOM   6367 H H     . LEU C 3 43  ? 46.083 17.793  64.182 1.00 51.86  ?  43  LEU C H     1 
ATOM   6368 H HA    . LEU C 3 43  ? 46.694 18.689  66.670 1.00 50.00  ?  43  LEU C HA    1 
ATOM   6369 H HB2   . LEU C 3 43  ? 46.832 20.037  64.194 1.00 47.30  ?  43  LEU C HB2   1 
ATOM   6370 H HB3   . LEU C 3 43  ? 47.189 20.721  65.584 1.00 47.30  ?  43  LEU C HB3   1 
ATOM   6371 H HG    . LEU C 3 43  ? 48.597 18.432  64.791 1.00 43.46  ?  43  LEU C HG    1 
ATOM   6372 H HD11  . LEU C 3 43  ? 50.233 19.719  63.748 1.00 45.68  ?  43  LEU C HD11  1 
ATOM   6373 H HD12  . LEU C 3 43  ? 48.848 19.837  62.979 1.00 45.68  ?  43  LEU C HD12  1 
ATOM   6374 H HD13  . LEU C 3 43  ? 49.327 21.011  63.936 1.00 45.68  ?  43  LEU C HD13  1 
ATOM   6375 H HD21  . LEU C 3 43  ? 50.294 19.269  66.138 1.00 41.36  ?  43  LEU C HD21  1 
ATOM   6376 H HD22  . LEU C 3 43  ? 49.388 20.527  66.483 1.00 41.36  ?  43  LEU C HD22  1 
ATOM   6377 H HD23  . LEU C 3 43  ? 48.951 19.078  66.964 1.00 41.36  ?  43  LEU C HD23  1 
ATOM   6378 N N     . ILE C 3 44  ? 44.679 19.848  67.342 1.00 40.69  ?  44  ILE C N     1 
ATOM   6379 C CA    . ILE C 3 44  ? 43.379 20.318  67.823 1.00 43.94  ?  44  ILE C CA    1 
ATOM   6380 C C     . ILE C 3 44  ? 43.535 21.686  68.479 1.00 43.28  ?  44  ILE C C     1 
ATOM   6381 O O     . ILE C 3 44  ? 44.355 21.851  69.395 1.00 41.52  ?  44  ILE C O     1 
ATOM   6382 C CB    . ILE C 3 44  ? 42.744 19.350  68.841 1.00 45.20  ?  44  ILE C CB    1 
ATOM   6383 C CG1   . ILE C 3 44  ? 42.999 17.879  68.501 1.00 42.56  ?  44  ILE C CG1   1 
ATOM   6384 C CG2   . ILE C 3 44  ? 41.250 19.626  68.947 1.00 48.51  ?  44  ILE C CG2   1 
ATOM   6385 C CD1   . ILE C 3 44  ? 42.113 17.346  67.379 1.00 48.19  ?  44  ILE C CD1   1 
ATOM   6386 H H     . ILE C 3 44  ? 45.281 19.845  67.955 1.00 48.83  ?  44  ILE C H     1 
ATOM   6387 H HA    . ILE C 3 44  ? 42.803 20.402  67.048 1.00 52.72  ?  44  ILE C HA    1 
ATOM   6388 H HB    . ILE C 3 44  ? 43.171 19.512  69.697 1.00 54.24  ?  44  ILE C HB    1 
ATOM   6389 H HG12  . ILE C 3 44  ? 43.923 17.779  68.222 1.00 51.07  ?  44  ILE C HG12  1 
ATOM   6390 H HG13  . ILE C 3 44  ? 42.831 17.343  69.292 1.00 51.07  ?  44  ILE C HG13  1 
ATOM   6391 H HG21  . ILE C 3 44  ? 40.858 19.001  69.577 1.00 58.21  ?  44  ILE C HG21  1 
ATOM   6392 H HG22  . ILE C 3 44  ? 41.118 20.535  69.257 1.00 58.21  ?  44  ILE C HG22  1 
ATOM   6393 H HG23  . ILE C 3 44  ? 40.845 19.511  68.073 1.00 58.21  ?  44  ILE C HG23  1 
ATOM   6394 H HD11  . ILE C 3 44  ? 42.364 16.428  67.188 1.00 57.83  ?  44  ILE C HD11  1 
ATOM   6395 H HD12  . ILE C 3 44  ? 41.186 17.383  67.664 1.00 57.83  ?  44  ILE C HD12  1 
ATOM   6396 H HD13  . ILE C 3 44  ? 42.239 17.895  66.589 1.00 57.83  ?  44  ILE C HD13  1 
ATOM   6397 N N     . PHE C 3 45  ? 42.711 22.645  68.047 1.00 44.99  ?  45  PHE C N     1 
ATOM   6398 C CA    . PHE C 3 45  ? 42.693 23.985  68.627 1.00 45.73  ?  45  PHE C CA    1 
ATOM   6399 C C     . PHE C 3 45  ? 41.272 24.532  68.570 1.00 46.29  ?  45  PHE C C     1 
ATOM   6400 O O     . PHE C 3 45  ? 40.620 24.482  67.523 1.00 45.62  ?  45  PHE C O     1 
ATOM   6401 C CB    . PHE C 3 45  ? 43.650 24.943  67.901 1.00 43.61  ?  45  PHE C CB    1 
ATOM   6402 C CG    . PHE C 3 45  ? 43.709 26.300  68.526 1.00 45.89  ?  45  PHE C CG    1 
ATOM   6403 C CD1   . PHE C 3 45  ? 43.063 27.361  67.946 1.00 47.10  ?  45  PHE C CD1   1 
ATOM   6404 C CD2   . PHE C 3 45  ? 44.378 26.506  69.717 1.00 46.50  ?  45  PHE C CD2   1 
ATOM   6405 C CE1   . PHE C 3 45  ? 43.097 28.598  68.526 1.00 47.41  ?  45  PHE C CE1   1 
ATOM   6406 C CE2   . PHE C 3 45  ? 44.410 27.748  70.295 1.00 43.98  ?  45  PHE C CE2   1 
ATOM   6407 C CZ    . PHE C 3 45  ? 43.764 28.790  69.702 1.00 41.73  ?  45  PHE C CZ    1 
ATOM   6408 H H     . PHE C 3 45  ? 42.145 22.540  67.408 1.00 53.99  ?  45  PHE C H     1 
ATOM   6409 H HA    . PHE C 3 45  ? 42.971 23.925  69.554 1.00 54.87  ?  45  PHE C HA    1 
ATOM   6410 H HB2   . PHE C 3 45  ? 44.544 24.567  67.918 1.00 52.33  ?  45  PHE C HB2   1 
ATOM   6411 H HB3   . PHE C 3 45  ? 43.353 25.050  66.983 1.00 52.33  ?  45  PHE C HB3   1 
ATOM   6412 H HD1   . PHE C 3 45  ? 42.598 27.239  67.150 1.00 56.51  ?  45  PHE C HD1   1 
ATOM   6413 H HD2   . PHE C 3 45  ? 44.812 25.795  70.130 1.00 55.81  ?  45  PHE C HD2   1 
ATOM   6414 H HE1   . PHE C 3 45  ? 42.664 29.313  68.119 1.00 56.90  ?  45  PHE C HE1   1 
ATOM   6415 H HE2   . PHE C 3 45  ? 44.871 27.879  71.092 1.00 52.77  ?  45  PHE C HE2   1 
ATOM   6416 H HZ    . PHE C 3 45  ? 43.778 29.632  70.097 1.00 50.08  ?  45  PHE C HZ    1 
ATOM   6417 N N     . ALA C 3 46  ? 40.797 25.062  69.693 1.00 49.06  ?  46  ALA C N     1 
ATOM   6418 C CA    . ALA C 3 46  ? 39.423 25.548  69.794 1.00 49.13  ?  46  ALA C CA    1 
ATOM   6419 C C     . ALA C 3 46  ? 38.412 24.446  69.476 1.00 49.83  ?  46  ALA C C     1 
ATOM   6420 O O     . ALA C 3 46  ? 37.337 24.710  68.933 1.00 52.03  ?  46  ALA C O     1 
ATOM   6421 C CB    . ALA C 3 46  ? 39.195 26.752  68.880 1.00 48.79  ?  46  ALA C CB    1 
ATOM   6422 H H     . ALA C 3 46  ? 41.254 25.153  70.416 1.00 58.87  ?  46  ALA C H     1 
ATOM   6423 H HA    . ALA C 3 46  ? 39.273 25.825  70.712 1.00 58.96  ?  46  ALA C HA    1 
ATOM   6424 H HB1   . ALA C 3 46  ? 38.271 27.039  68.960 1.00 58.55  ?  46  ALA C HB1   1 
ATOM   6425 H HB2   . ALA C 3 46  ? 39.788 27.470  69.150 1.00 58.55  ?  46  ALA C HB2   1 
ATOM   6426 H HB3   . ALA C 3 46  ? 39.383 26.494  67.965 1.00 58.55  ?  46  ALA C HB3   1 
ATOM   6427 N N     . GLY C 3 47  ? 38.760 23.201  69.809 1.00 49.25  ?  47  GLY C N     1 
ATOM   6428 C CA    . GLY C 3 47  ? 37.855 22.085  69.620 1.00 48.84  ?  47  GLY C CA    1 
ATOM   6429 C C     . GLY C 3 47  ? 37.702 21.558  68.207 1.00 46.74  ?  47  GLY C C     1 
ATOM   6430 O O     . GLY C 3 47  ? 36.846 20.690  67.976 1.00 46.14  ?  47  GLY C O     1 
ATOM   6431 H H     . GLY C 3 47  ? 39.520 22.983  70.147 1.00 59.10  ?  47  GLY C H     1 
ATOM   6432 H HA2   . GLY C 3 47  ? 38.165 21.348  70.169 1.00 58.61  ?  47  GLY C HA2   1 
ATOM   6433 H HA3   . GLY C 3 47  ? 36.974 22.355  69.923 1.00 58.61  ?  47  GLY C HA3   1 
ATOM   6434 N N     . LYS C 3 48  ? 38.495 22.039  67.257 1.00 46.80  ?  48  LYS C N     1 
ATOM   6435 C CA    . LYS C 3 48  ? 38.456 21.557  65.882 1.00 54.01  ?  48  LYS C CA    1 
ATOM   6436 C C     . LYS C 3 48  ? 39.751 20.824  65.525 1.00 46.66  ?  48  LYS C C     1 
ATOM   6437 O O     . LYS C 3 48  ? 40.840 21.236  65.931 1.00 43.45  ?  48  LYS C O     1 
ATOM   6438 C CB    . LYS C 3 48  ? 38.229 22.725  64.907 1.00 56.23  ?  48  LYS C CB    1 
ATOM   6439 C CG    . LYS C 3 48  ? 36.760 23.125  64.664 1.00 61.02  ?  48  LYS C CG    1 
ATOM   6440 C CD    . LYS C 3 48  ? 36.636 24.405  63.792 1.00 73.86  ?  48  LYS C CD    1 
ATOM   6441 C CE    . LYS C 3 48  ? 37.313 25.662  64.441 1.00 77.43  ?  48  LYS C CE    1 
ATOM   6442 N NZ    . LYS C 3 48  ? 36.389 26.627  65.171 1.00 77.02  ?  48  LYS C NZ    1 
ATOM   6443 H H     . LYS C 3 48  ? 39.076 22.659  67.388 1.00 56.15  ?  48  LYS C H     1 
ATOM   6444 H HA    . LYS C 3 48  ? 37.729 20.922  65.788 1.00 64.81  ?  48  LYS C HA    1 
ATOM   6445 H HB2   . LYS C 3 48  ? 38.685 23.506  65.258 1.00 67.48  ?  48  LYS C HB2   1 
ATOM   6446 H HB3   . LYS C 3 48  ? 38.605 22.479  64.048 1.00 67.48  ?  48  LYS C HB3   1 
ATOM   6447 H HG2   . LYS C 3 48  ? 36.304 22.402  64.206 1.00 73.23  ?  48  LYS C HG2   1 
ATOM   6448 H HG3   . LYS C 3 48  ? 36.332 23.299  65.517 1.00 73.23  ?  48  LYS C HG3   1 
ATOM   6449 H HD2   . LYS C 3 48  ? 37.064 24.245  62.937 1.00 88.64  ?  48  LYS C HD2   1 
ATOM   6450 H HD3   . LYS C 3 48  ? 35.697 24.607  63.661 1.00 88.64  ?  48  LYS C HD3   1 
ATOM   6451 H HE2   . LYS C 3 48  ? 37.969 25.354  65.086 1.00 92.92  ?  48  LYS C HE2   1 
ATOM   6452 H HE3   . LYS C 3 48  ? 37.752 26.166  63.738 1.00 92.92  ?  48  LYS C HE3   1 
ATOM   6453 H HZ1   . LYS C 3 48  ? 36.859 27.302  65.510 1.00 92.43  ?  48  LYS C HZ1   1 
ATOM   6454 H HZ2   . LYS C 3 48  ? 35.782 26.952  64.607 1.00 92.43  ?  48  LYS C HZ2   1 
ATOM   6455 H HZ3   . LYS C 3 48  ? 35.970 26.205  65.834 1.00 92.43  ?  48  LYS C HZ3   1 
ATOM   6456 N N     . GLN C 3 49  ? 39.622 19.726  64.778 1.00 50.13  ?  49  GLN C N     1 
ATOM   6457 C CA    . GLN C 3 49  ? 40.775 19.150  64.093 1.00 54.21  ?  49  GLN C CA    1 
ATOM   6458 C C     . GLN C 3 49  ? 41.274 20.121  63.034 1.00 51.79  ?  49  GLN C C     1 
ATOM   6459 O O     . GLN C 3 49  ? 40.501 20.589  62.190 1.00 49.28  ?  49  GLN C O     1 
ATOM   6460 C CB    . GLN C 3 49  ? 40.421 17.831  63.416 1.00 51.94  ?  49  GLN C CB    1 
ATOM   6461 C CG    . GLN C 3 49  ? 39.718 16.826  64.265 1.00 57.42  ?  49  GLN C CG    1 
ATOM   6462 C CD    . GLN C 3 49  ? 40.385 15.472  64.184 1.00 65.20  ?  49  GLN C CD    1 
ATOM   6463 O OE1   . GLN C 3 49  ? 41.531 15.352  63.715 1.00 55.04  ?  49  GLN C OE1   1 
ATOM   6464 N NE2   . GLN C 3 49  ? 39.644 14.423  64.579 1.00 67.39  ?  49  GLN C NE2   1 
ATOM   6465 H H     . GLN C 3 49  ? 38.884 19.301  64.654 1.00 60.15  ?  49  GLN C H     1 
ATOM   6466 H HA    . GLN C 3 49  ? 41.467 18.976  64.750 1.00 65.06  ?  49  GLN C HA    1 
ATOM   6467 H HB2   . GLN C 3 49  ? 39.843 18.023  62.662 1.00 62.33  ?  49  GLN C HB2   1 
ATOM   6468 H HB3   . GLN C 3 49  ? 41.243 17.419  63.107 1.00 62.33  ?  49  GLN C HB3   1 
ATOM   6469 H HG2   . GLN C 3 49  ? 39.733 17.120  65.190 1.00 68.91  ?  49  GLN C HG2   1 
ATOM   6470 H HG3   . GLN C 3 49  ? 38.801 16.734  63.962 1.00 68.91  ?  49  GLN C HG3   1 
ATOM   6471 H HE21  . GLN C 3 49  ? 38.839 14.546  64.858 1.00 80.86  ?  49  GLN C HE21  1 
ATOM   6472 H HE22  . GLN C 3 49  ? 39.974 13.629  64.554 1.00 80.86  ?  49  GLN C HE22  1 
ATOM   6473 N N     . LEU C 3 50  ? 42.573 20.390  63.052 1.00 51.34  ?  50  LEU C N     1 
ATOM   6474 C CA    . LEU C 3 50  ? 43.163 21.378  62.161 1.00 53.80  ?  50  LEU C CA    1 
ATOM   6475 C C     . LEU C 3 50  ? 43.563 20.744  60.838 1.00 52.39  ?  50  LEU C C     1 
ATOM   6476 O O     . LEU C 3 50  ? 44.204 19.687  60.817 1.00 50.19  ?  50  LEU C O     1 
ATOM   6477 C CB    . LEU C 3 50  ? 44.366 22.025  62.836 1.00 51.50  ?  50  LEU C CB    1 
ATOM   6478 C CG    . LEU C 3 50  ? 43.982 22.682  64.166 1.00 51.13  ?  50  LEU C CG    1 
ATOM   6479 C CD1   . LEU C 3 50  ? 45.174 23.388  64.769 1.00 49.02  ?  50  LEU C CD1   1 
ATOM   6480 C CD2   . LEU C 3 50  ? 42.827 23.653  63.976 1.00 54.31  ?  50  LEU C CD2   1 
ATOM   6481 H H     . LEU C 3 50  ? 43.139 20.009  63.577 1.00 61.61  ?  50  LEU C H     1 
ATOM   6482 H HA    . LEU C 3 50  ? 42.509 22.064  61.960 1.00 64.56  ?  50  LEU C HA    1 
ATOM   6483 H HB2   . LEU C 3 50  ? 45.037 21.347  63.013 1.00 61.80  ?  50  LEU C HB2   1 
ATOM   6484 H HB3   . LEU C 3 50  ? 44.731 22.708  62.252 1.00 61.80  ?  50  LEU C HB3   1 
ATOM   6485 H HG    . LEU C 3 50  ? 43.691 21.992  64.784 1.00 61.36  ?  50  LEU C HG    1 
ATOM   6486 H HD11  . LEU C 3 50  ? 44.901 23.824  65.591 1.00 58.83  ?  50  LEU C HD11  1 
ATOM   6487 H HD12  . LEU C 3 50  ? 45.867 22.735  64.955 1.00 58.83  ?  50  LEU C HD12  1 
ATOM   6488 H HD13  . LEU C 3 50  ? 45.502 24.048  64.138 1.00 58.83  ?  50  LEU C HD13  1 
ATOM   6489 H HD21  . LEU C 3 50  ? 42.649 24.101  64.818 1.00 65.17  ?  50  LEU C HD21  1 
ATOM   6490 H HD22  . LEU C 3 50  ? 43.071 24.305  63.300 1.00 65.17  ?  50  LEU C HD22  1 
ATOM   6491 H HD23  . LEU C 3 50  ? 42.042 23.159  63.691 1.00 65.17  ?  50  LEU C HD23  1 
ATOM   6492 N N     . GLU C 3 51  ? 43.188 21.407  59.740 1.00 54.66  ?  51  GLU C N     1 
ATOM   6493 C CA    . GLU C 3 51  ? 43.405 20.897  58.392 1.00 63.32  ?  51  GLU C CA    1 
ATOM   6494 C C     . GLU C 3 51  ? 44.716 21.414  57.820 1.00 62.67  ?  51  GLU C C     1 
ATOM   6495 O O     . GLU C 3 51  ? 45.056 22.590  57.988 1.00 58.65  ?  51  GLU C O     1 
ATOM   6496 C CB    . GLU C 3 51  ? 42.253 21.274  57.455 1.00 67.69  ?  51  GLU C CB    1 
ATOM   6497 C CG    . GLU C 3 51  ? 40.961 20.501  57.740 1.00 77.85  ?  51  GLU C CG    1 
ATOM   6498 C CD    . GLU C 3 51  ? 40.446 19.669  56.558 1.00 88.47  ?  51  GLU C CD    1 
ATOM   6499 O OE1   . GLU C 3 51  ? 39.430 18.941  56.747 1.00 92.16  ?  51  GLU C OE1   1 
ATOM   6500 O OE2   . GLU C 3 51  ? 41.042 19.736  55.455 1.00 90.32  -1 51  GLU C OE2   1 
ATOM   6501 H H     . GLU C 3 51  ? 42.796 22.173  59.755 1.00 65.59  ?  51  GLU C H     1 
ATOM   6502 H HA    . GLU C 3 51  ? 43.455 19.929  58.439 1.00 75.98  ?  51  GLU C HA    1 
ATOM   6503 H HB2   . GLU C 3 51  ? 42.063 22.220  57.557 1.00 81.23  ?  51  GLU C HB2   1 
ATOM   6504 H HB3   . GLU C 3 51  ? 42.518 21.085  56.541 1.00 81.23  ?  51  GLU C HB3   1 
ATOM   6505 H HG2   . GLU C 3 51  ? 41.121 19.893  58.479 1.00 93.42  ?  51  GLU C HG2   1 
ATOM   6506 H HG3   . GLU C 3 51  ? 40.267 21.135  57.977 1.00 93.42  ?  51  GLU C HG3   1 
ATOM   6507 N N     . ASP C 3 52  ? 45.427 20.537  57.090 1.00 65.63  ?  52  ASP C N     1 
ATOM   6508 C CA    . ASP C 3 52  ? 46.815 20.763  56.608 1.00 66.93  ?  52  ASP C CA    1 
ATOM   6509 C C     . ASP C 3 52  ? 47.031 22.033  55.783 1.00 66.01  ?  52  ASP C C     1 
ATOM   6510 O O     . ASP C 3 52  ? 47.961 22.760  56.101 1.00 63.65  ?  52  ASP C O     1 
ATOM   6511 C CB    . ASP C 3 52  ? 47.322 19.519  55.881 1.00 70.63  ?  52  ASP C CB    1 
ATOM   6512 C CG    . ASP C 3 52  ? 47.413 18.268  56.739 1.00 71.96  ?  52  ASP C CG    1 
ATOM   6513 O OD1   . ASP C 3 52  ? 47.070 17.186  56.230 1.00 73.88  ?  52  ASP C OD1   1 
ATOM   6514 O OD2   . ASP C 3 52  ? 47.833 18.381  57.902 1.00 69.16  -1 52  ASP C OD2   1 
ATOM   6515 H H     . ASP C 3 52  ? 45.078 19.753  56.772 1.00 78.75  ?  52  ASP C H     1 
ATOM   6516 H HA    . ASP C 3 52  ? 47.359 20.812  57.362 1.00 80.32  ?  52  ASP C HA    1 
ATOM   6517 H HB2   . ASP C 3 52  ? 46.766 19.337  55.097 1.00 84.76  ?  52  ASP C HB2   1 
ATOM   6518 H HB3   . ASP C 3 52  ? 48.218 19.721  55.579 1.00 84.76  ?  52  ASP C HB3   1 
ATOM   6519 N N     . GLY C 3 53  ? 46.248 22.277  54.741 1.00 66.51  ?  53  GLY C N     1 
ATOM   6520 C CA    . GLY C 3 53  ? 46.480 23.412  53.828 1.00 65.45  ?  53  GLY C CA    1 
ATOM   6521 C C     . GLY C 3 53  ? 46.422 24.754  54.515 1.00 66.34  ?  53  GLY C C     1 
ATOM   6522 O O     . GLY C 3 53  ? 47.260 25.607  54.187 1.00 64.29  ?  53  GLY C O     1 
ATOM   6523 H H     . GLY C 3 53  ? 45.520 21.767  54.544 1.00 79.81  ?  53  GLY C H     1 
ATOM   6524 H HA2   . GLY C 3 53  ? 47.368 23.303  53.403 1.00 78.54  ?  53  GLY C HA2   1 
ATOM   6525 H HA3   . GLY C 3 53  ? 45.798 23.386  53.113 1.00 78.54  ?  53  GLY C HA3   1 
ATOM   6526 N N     . ARG C 3 54  ? 45.471 24.943  55.422 1.00 67.73  ?  54  ARG C N     1 
ATOM   6527 C CA    . ARG C 3 54  ? 45.265 26.234  56.120 1.00 66.43  ?  54  ARG C CA    1 
ATOM   6528 C C     . ARG C 3 54  ? 46.491 26.599  56.939 1.00 61.61  ?  54  ARG C C     1 
ATOM   6529 O O     . ARG C 3 54  ? 47.271 25.700  57.215 1.00 62.06  ?  54  ARG C O     1 
ATOM   6530 C CB    . ARG C 3 54  ? 44.045 26.171  57.043 1.00 71.15  ?  54  ARG C CB    1 
ATOM   6531 C CG    . ARG C 3 54  ? 42.708 26.368  56.345 1.00 76.67  ?  54  ARG C CG    1 
ATOM   6532 C CD    . ARG C 3 54  ? 41.582 26.759  57.285 1.00 82.22  ?  54  ARG C CD    1 
ATOM   6533 N NE    . ARG C 3 54  ? 40.634 27.644  56.616 1.00 96.65  ?  54  ARG C NE    1 
ATOM   6534 C CZ    . ARG C 3 54  ? 39.694 27.295  55.723 1.00 100.27 ?  54  ARG C CZ    1 
ATOM   6535 N NH1   . ARG C 3 54  ? 39.512 26.036  55.342 1.00 93.82  ?  54  ARG C NH1   1 
ATOM   6536 N NH2   . ARG C 3 54  ? 38.916 28.236  55.205 1.00 86.32  ?  54  ARG C NH2   1 
ATOM   6537 H H     . ARG C 3 54  ? 44.882 24.284  55.654 1.00 81.28  ?  54  ARG C H     1 
ATOM   6538 H HA    . ARG C 3 54  ? 45.121 26.937  55.440 1.00 79.71  ?  54  ARG C HA    1 
ATOM   6539 H HB2   . ARG C 3 54  ? 44.036 25.296  57.503 1.00 85.38  ?  54  ARG C HB2   1 
ATOM   6540 H HB3   . ARG C 3 54  ? 44.150 26.867  57.736 1.00 85.38  ?  54  ARG C HB3   1 
ATOM   6541 H HG2   . ARG C 3 54  ? 42.799 27.072  55.657 1.00 92.00  ?  54  ARG C HG2   1 
ATOM   6542 H HG3   . ARG C 3 54  ? 42.463 25.527  55.885 1.00 92.00  ?  54  ARG C HG3   1 
ATOM   6543 H HD2   . ARG C 3 54  ? 41.120 25.947  57.610 1.00 98.66  ?  54  ARG C HD2   1 
ATOM   6544 H HD3   . ARG C 3 54  ? 41.951 27.227  58.074 1.00 98.66  ?  54  ARG C HD3   1 
ATOM   6545 H HE    . ARG C 3 54  ? 40.698 28.517  56.820 1.00 115.98 ?  54  ARG C HE    1 
ATOM   6546 H HH11  . ARG C 3 54  ? 40.014 25.366  55.665 1.00 112.58 ?  54  ARG C HH11  1 
ATOM   6547 H HH12  . ARG C 3 54  ? 38.871 25.839  54.744 1.00 112.58 ?  54  ARG C HH12  1 
ATOM   6548 H HH21  . ARG C 3 54  ? 39.017 29.096  55.446 1.00 103.58 ?  54  ARG C HH21  1 
ATOM   6549 H HH22  . ARG C 3 54  ? 38.279 28.021  54.609 1.00 103.58 ?  54  ARG C HH22  1 
ATOM   6550 N N     . THR C 3 55  ? 46.606 27.858  57.352 1.00 64.47  ?  55  THR C N     1 
ATOM   6551 C CA    . THR C 3 55  ? 47.748 28.384  58.134 1.00 64.09  ?  55  THR C CA    1 
ATOM   6552 C C     . THR C 3 55  ? 47.285 28.783  59.526 1.00 60.11  ?  55  THR C C     1 
ATOM   6553 O O     . THR C 3 55  ? 46.088 28.686  59.773 1.00 56.89  ?  55  THR C O     1 
ATOM   6554 C CB    . THR C 3 55  ? 48.479 29.520  57.404 1.00 62.70  ?  55  THR C CB    1 
ATOM   6555 O OG1   . THR C 3 55  ? 48.002 30.777  57.878 1.00 64.51  ?  55  THR C OG1   1 
ATOM   6556 C CG2   . THR C 3 55  ? 48.355 29.457  55.898 1.00 62.60  ?  55  THR C CG2   1 
ATOM   6557 H H     . THR C 3 55  ? 45.963 28.488  57.209 1.00 77.37  ?  55  THR C H     1 
ATOM   6558 H HA    . THR C 3 55  ? 48.390 27.646  58.266 1.00 76.90  ?  55  THR C HA    1 
ATOM   6559 H HB    . THR C 3 55  ? 49.439 29.451  57.633 1.00 75.24  ?  55  THR C HB    1 
ATOM   6560 H HG1   . THR C 3 55  ? 48.647 31.234  58.158 1.00 77.41  ?  55  THR C HG1   1 
ATOM   6561 H HG21  . THR C 3 55  ? 49.051 30.027  55.489 1.00 75.12  ?  55  THR C HG21  1 
ATOM   6562 H HG22  . THR C 3 55  ? 48.477 28.525  55.592 1.00 75.12  ?  55  THR C HG22  1 
ATOM   6563 H HG23  . THR C 3 55  ? 47.462 29.782  55.623 1.00 75.12  ?  55  THR C HG23  1 
ATOM   6564 N N     . LEU C 3 56  ? 48.218 29.170  60.400 1.00 61.94  ?  56  LEU C N     1 
ATOM   6565 C CA    . LEU C 3 56  ? 47.908 29.522  61.784 1.00 56.36  ?  56  LEU C CA    1 
ATOM   6566 C C     . LEU C 3 56  ? 47.031 30.760  61.862 1.00 59.37  ?  56  LEU C C     1 
ATOM   6567 O O     . LEU C 3 56  ? 46.099 30.817  62.674 1.00 57.90  ?  56  LEU C O     1 
ATOM   6568 C CB    . LEU C 3 56  ? 49.191 29.750  62.575 1.00 54.37  ?  56  LEU C CB    1 
ATOM   6569 C CG    . LEU C 3 56  ? 50.241 28.649  62.519 1.00 53.37  ?  56  LEU C CG    1 
ATOM   6570 C CD1   . LEU C 3 56  ? 51.416 28.948  63.429 1.00 56.25  ?  56  LEU C CD1   1 
ATOM   6571 C CD2   . LEU C 3 56  ? 49.570 27.350  62.920 1.00 54.09  ?  56  LEU C CD2   1 
ATOM   6572 H H     . LEU C 3 56  ? 49.042 29.289  60.183 1.00 74.33  ?  56  LEU C H     1 
ATOM   6573 H HA    . LEU C 3 56  ? 47.428 28.780  62.183 1.00 67.63  ?  56  LEU C HA    1 
ATOM   6574 H HB2   . LEU C 3 56  ? 49.610 30.558  62.239 1.00 65.25  ?  56  LEU C HB2   1 
ATOM   6575 H HB3   . LEU C 3 56  ? 48.951 29.865  63.508 1.00 65.25  ?  56  LEU C HB3   1 
ATOM   6576 H HG    . LEU C 3 56  ? 50.602 28.577  61.621 1.00 64.04  ?  56  LEU C HG    1 
ATOM   6577 H HD11  . LEU C 3 56  ? 52.089 28.258  63.314 1.00 67.49  ?  56  LEU C HD11  1 
ATOM   6578 H HD12  . LEU C 3 56  ? 51.786 29.813  63.192 1.00 67.49  ?  56  LEU C HD12  1 
ATOM   6579 H HD13  . LEU C 3 56  ? 51.109 28.960  64.349 1.00 67.49  ?  56  LEU C HD13  1 
ATOM   6580 H HD21  . LEU C 3 56  ? 50.216 26.629  62.858 1.00 64.91  ?  56  LEU C HD21  1 
ATOM   6581 H HD22  . LEU C 3 56  ? 49.249 27.429  63.832 1.00 64.91  ?  56  LEU C HD22  1 
ATOM   6582 H HD23  . LEU C 3 56  ? 48.826 27.181  62.321 1.00 64.91  ?  56  LEU C HD23  1 
ATOM   6583 N N     . SER C 3 57  ? 47.327 31.767  61.038 1.00 62.21  ?  57  SER C N     1 
ATOM   6584 C CA    . SER C 3 57  ? 46.441 32.917  60.921 1.00 60.75  ?  57  SER C CA    1 
ATOM   6585 C C     . SER C 3 57  ? 45.004 32.477  60.677 1.00 63.29  ?  57  SER C C     1 
ATOM   6586 O O     . SER C 3 57  ? 44.090 32.902  61.394 1.00 62.67  ?  57  SER C O     1 
ATOM   6587 C CB    . SER C 3 57  ? 46.909 33.823  59.786 1.00 64.93  ?  57  SER C CB    1 
ATOM   6588 O OG    . SER C 3 57  ? 48.221 34.291  60.023 1.00 70.52  ?  57  SER C OG    1 
ATOM   6589 H H     . SER C 3 57  ? 48.028 31.805  60.541 1.00 74.65  ?  57  SER C H     1 
ATOM   6590 H HA    . SER C 3 57  ? 46.474 33.420  61.749 1.00 72.91  ?  57  SER C HA    1 
ATOM   6591 H HB2   . SER C 3 57  ? 46.898 33.321  58.957 1.00 77.92  ?  57  SER C HB2   1 
ATOM   6592 H HB3   . SER C 3 57  ? 46.310 34.583  59.722 1.00 77.92  ?  57  SER C HB3   1 
ATOM   6593 H HG    . SER C 3 57  ? 48.495 34.726  59.359 1.00 84.62  ?  57  SER C HG    1 
ATOM   6594 N N     . ASP C 3 58  ? 44.788 31.610  59.665 1.00 64.70  ?  58  ASP C N     1 
ATOM   6595 C CA    . ASP C 3 58  ? 43.433 31.206  59.284 1.00 61.17  ?  58  ASP C CA    1 
ATOM   6596 C C     . ASP C 3 58  ? 42.667 30.569  60.438 1.00 60.02  ?  58  ASP C C     1 
ATOM   6597 O O     . ASP C 3 58  ? 41.447 30.367  60.327 1.00 58.79  ?  58  ASP C O     1 
ATOM   6598 C CB    . ASP C 3 58  ? 43.416 30.179  58.137 1.00 63.51  ?  58  ASP C CB    1 
ATOM   6599 C CG    . ASP C 3 58  ? 44.362 30.522  57.004 1.00 69.70  ?  58  ASP C CG    1 
ATOM   6600 O OD1   . ASP C 3 58  ? 45.335 31.263  57.249 1.00 68.76  ?  58  ASP C OD1   1 
ATOM   6601 O OD2   . ASP C 3 58  ? 44.140 30.021  55.872 1.00 66.34  -1 58  ASP C OD2   1 
ATOM   6602 H H     . ASP C 3 58  ? 45.409 31.248  59.192 1.00 77.64  ?  58  ASP C H     1 
ATOM   6603 H HA    . ASP C 3 58  ? 42.998 32.018  58.982 1.00 73.41  ?  58  ASP C HA    1 
ATOM   6604 H HB2   . ASP C 3 58  ? 43.676 29.313  58.487 1.00 76.21  ?  58  ASP C HB2   1 
ATOM   6605 H HB3   . ASP C 3 58  ? 42.519 30.134  57.770 1.00 76.21  ?  58  ASP C HB3   1 
ATOM   6606 N N     . TYR C 3 59  ? 43.369 30.192  61.515 1.00 60.87  ?  59  TYR C N     1 
ATOM   6607 C CA    . TYR C 3 59  ? 42.768 29.656  62.733 1.00 62.67  ?  59  TYR C CA    1 
ATOM   6608 C C     . TYR C 3 59  ? 42.909 30.603  63.926 1.00 62.27  ?  59  TYR C C     1 
ATOM   6609 O O     . TYR C 3 59  ? 42.576 30.215  65.052 1.00 61.49  ?  59  TYR C O     1 
ATOM   6610 C CB    . TYR C 3 59  ? 43.390 28.299  63.113 1.00 60.57  ?  59  TYR C CB    1 
ATOM   6611 C CG    . TYR C 3 59  ? 43.050 27.141  62.200 1.00 58.63  ?  59  TYR C CG    1 
ATOM   6612 C CD1   . TYR C 3 59  ? 44.005 26.596  61.354 1.00 59.06  ?  59  TYR C CD1   1 
ATOM   6613 C CD2   . TYR C 3 59  ? 41.780 26.591  62.185 1.00 56.08  ?  59  TYR C CD2   1 
ATOM   6614 C CE1   . TYR C 3 59  ? 43.697 25.538  60.508 1.00 61.80  ?  59  TYR C CE1   1 
ATOM   6615 C CE2   . TYR C 3 59  ? 41.460 25.541  61.344 1.00 58.78  ?  59  TYR C CE2   1 
ATOM   6616 C CZ    . TYR C 3 59  ? 42.420 25.015  60.506 1.00 62.08  ?  59  TYR C CZ    1 
ATOM   6617 O OH    . TYR C 3 59  ? 42.105 23.960  59.673 1.00 63.55  ?  59  TYR C OH    1 
ATOM   6618 H H     . TYR C 3 59  ? 44.227 30.242  61.561 1.00 73.05  ?  59  TYR C H     1 
ATOM   6619 H HA    . TYR C 3 59  ? 41.826 29.519  62.548 1.00 75.20  ?  59  TYR C HA    1 
ATOM   6620 H HB2   . TYR C 3 59  ? 44.355 28.395  63.107 1.00 72.69  ?  59  TYR C HB2   1 
ATOM   6621 H HB3   . TYR C 3 59  ? 43.085 28.063  64.003 1.00 72.69  ?  59  TYR C HB3   1 
ATOM   6622 H HD1   . TYR C 3 59  ? 44.867 26.945  61.353 1.00 70.87  ?  59  TYR C HD1   1 
ATOM   6623 H HD2   . TYR C 3 59  ? 41.128 26.935  62.752 1.00 67.30  ?  59  TYR C HD2   1 
ATOM   6624 H HE1   . TYR C 3 59  ? 44.347 25.184  59.945 1.00 74.16  ?  59  TYR C HE1   1 
ATOM   6625 H HE2   . TYR C 3 59  ? 40.599 25.190  61.344 1.00 70.54  ?  59  TYR C HE2   1 
ATOM   6626 H HH    . TYR C 3 59  ? 41.317 23.707  59.814 1.00 76.26  ?  59  TYR C HH    1 
ATOM   6627 N N     . ASN C 3 60  ? 43.433 31.812  63.723 1.00 58.61  ?  60  ASN C N     1 
ATOM   6628 C CA    . ASN C 3 60  ? 43.525 32.803  64.793 1.00 60.59  ?  60  ASN C CA    1 
ATOM   6629 C C     . ASN C 3 60  ? 44.357 32.254  65.952 1.00 58.68  ?  60  ASN C C     1 
ATOM   6630 O O     . ASN C 3 60  ? 43.985 32.330  67.124 1.00 56.41  ?  60  ASN C O     1 
ATOM   6631 C CB    . ASN C 3 60  ? 42.124 33.234  65.250 1.00 66.98  ?  60  ASN C CB    1 
ATOM   6632 C CG    . ASN C 3 60  ? 42.152 34.317  66.331 1.00 71.75  ?  60  ASN C CG    1 
ATOM   6633 O OD1   . ASN C 3 60  ? 41.589 34.146  67.420 1.00 73.26  ?  60  ASN C OD1   1 
ATOM   6634 N ND2   . ASN C 3 60  ? 42.814 35.438  66.032 1.00 72.70  ?  60  ASN C ND2   1 
ATOM   6635 H H     . ASN C 3 60  ? 43.745 32.083  62.969 1.00 70.33  ?  60  ASN C H     1 
ATOM   6636 H HA    . ASN C 3 60  ? 43.977 33.595  64.464 1.00 72.71  ?  60  ASN C HA    1 
ATOM   6637 H HB2   . ASN C 3 60  ? 41.639 33.586  64.488 1.00 80.38  ?  60  ASN C HB2   1 
ATOM   6638 H HB3   . ASN C 3 60  ? 41.660 32.463  65.612 1.00 80.38  ?  60  ASN C HB3   1 
ATOM   6639 H HD21  . ASN C 3 60  ? 43.195 35.520  65.266 1.00 87.24  ?  60  ASN C HD21  1 
ATOM   6640 H HD22  . ASN C 3 60  ? 42.859 36.077  66.606 1.00 87.24  ?  60  ASN C HD22  1 
ATOM   6641 N N     . ILE C 3 61  ? 45.505 31.688  65.610 1.00 58.21  ?  61  ILE C N     1 
ATOM   6642 C CA    . ILE C 3 61  ? 46.437 31.159  66.593 1.00 55.17  ?  61  ILE C CA    1 
ATOM   6643 C C     . ILE C 3 61  ? 47.523 32.212  66.755 1.00 53.72  ?  61  ILE C C     1 
ATOM   6644 O O     . ILE C 3 61  ? 48.436 32.326  65.940 1.00 59.43  ?  61  ILE C O     1 
ATOM   6645 C CB    . ILE C 3 61  ? 46.987 29.792  66.179 1.00 56.68  ?  61  ILE C CB    1 
ATOM   6646 C CG1   . ILE C 3 61  ? 45.828 28.784  66.169 1.00 53.74  ?  61  ILE C CG1   1 
ATOM   6647 C CG2   . ILE C 3 61  ? 48.081 29.321  67.135 1.00 56.25  ?  61  ILE C CG2   1 
ATOM   6648 C CD1   . ILE C 3 61  ? 46.194 27.412  65.690 1.00 53.59  ?  61  ILE C CD1   1 
ATOM   6649 H H     . ILE C 3 61  ? 45.772 31.598  64.797 1.00 69.85  ?  61  ILE C H     1 
ATOM   6650 H HA    . ILE C 3 61  ? 45.993 31.044  67.448 1.00 66.20  ?  61  ILE C HA    1 
ATOM   6651 H HB    . ILE C 3 61  ? 47.380 29.865  65.295 1.00 68.02  ?  61  ILE C HB    1 
ATOM   6652 H HG12  . ILE C 3 61  ? 45.489 28.696  67.073 1.00 64.49  ?  61  ILE C HG12  1 
ATOM   6653 H HG13  . ILE C 3 61  ? 45.132 29.121  65.584 1.00 64.49  ?  61  ILE C HG13  1 
ATOM   6654 H HG21  . ILE C 3 61  ? 48.432 28.474  66.820 1.00 67.49  ?  61  ILE C HG21  1 
ATOM   6655 H HG22  . ILE C 3 61  ? 48.789 29.985  67.156 1.00 67.49  ?  61  ILE C HG22  1 
ATOM   6656 H HG23  . ILE C 3 61  ? 47.702 29.214  68.021 1.00 67.49  ?  61  ILE C HG23  1 
ATOM   6657 H HD11  . ILE C 3 61  ? 45.395 26.865  65.659 1.00 64.31  ?  61  ILE C HD11  1 
ATOM   6658 H HD12  . ILE C 3 61  ? 46.583 27.481  64.803 1.00 64.31  ?  61  ILE C HD12  1 
ATOM   6659 H HD13  . ILE C 3 61  ? 46.838 27.025  66.304 1.00 64.31  ?  61  ILE C HD13  1 
ATOM   6660 N N     . GLN C 3 62  ? 47.403 32.995  67.812 1.00 55.23  ?  62  GLN C N     1 
ATOM   6661 C CA    . GLN C 3 62  ? 48.352 34.035  68.130 1.00 57.44  ?  62  GLN C CA    1 
ATOM   6662 C C     . GLN C 3 62  ? 49.523 33.432  68.891 1.00 57.40  ?  62  GLN C C     1 
ATOM   6663 O O     . GLN C 3 62  ? 49.611 32.221  69.088 1.00 54.86  ?  62  GLN C O     1 
ATOM   6664 C CB    . GLN C 3 62  ? 47.678 35.129  68.956 1.00 64.25  ?  62  GLN C CB    1 
ATOM   6665 C CG    . GLN C 3 62  ? 46.257 35.494  68.476 1.00 68.10  ?  62  GLN C CG    1 
ATOM   6666 C CD    . GLN C 3 62  ? 45.266 35.679  69.631 1.00 74.68  ?  62  GLN C CD    1 
ATOM   6667 O OE1   . GLN C 3 62  ? 45.625 35.523  70.808 1.00 75.73  ?  62  GLN C OE1   1 
ATOM   6668 N NE2   . GLN C 3 62  ? 44.010 36.011  69.293 1.00 74.55  ?  62  GLN C NE2   1 
ATOM   6669 H H     . GLN C 3 62  ? 46.759 32.939  68.378 1.00 66.27  ?  62  GLN C H     1 
ATOM   6670 H HA    . GLN C 3 62  ? 48.678 34.433  67.307 1.00 68.93  ?  62  GLN C HA    1 
ATOM   6671 H HB2   . GLN C 3 62  ? 47.610 34.827  69.875 1.00 77.10  ?  62  GLN C HB2   1 
ATOM   6672 H HB3   . GLN C 3 62  ? 48.220 35.932  68.910 1.00 77.10  ?  62  GLN C HB3   1 
ATOM   6673 H HG2   . GLN C 3 62  ? 46.296 36.326  67.979 1.00 81.72  ?  62  GLN C HG2   1 
ATOM   6674 H HG3   . GLN C 3 62  ? 45.924 34.782  67.907 1.00 81.72  ?  62  GLN C HG3   1 
ATOM   6675 H HE21  . GLN C 3 62  ? 43.799 36.109  68.465 1.00 89.46  ?  62  GLN C HE21  1 
ATOM   6676 H HE22  . GLN C 3 62  ? 43.417 36.127  69.905 1.00 89.46  ?  62  GLN C HE22  1 
ATOM   6677 N N     . LYS C 3 63  ? 50.418 34.295  69.354 1.00 58.58  ?  63  LYS C N     1 
ATOM   6678 C CA    . LYS C 3 63  ? 51.505 33.856  70.217 1.00 59.14  ?  63  LYS C CA    1 
ATOM   6679 C C     . LYS C 3 63  ? 50.966 33.207  71.498 1.00 58.37  ?  63  LYS C C     1 
ATOM   6680 O O     . LYS C 3 63  ? 49.871 33.532  71.980 1.00 54.20  ?  63  LYS C O     1 
ATOM   6681 C CB    . LYS C 3 63  ? 52.413 35.048  70.547 1.00 62.74  ?  63  LYS C CB    1 
ATOM   6682 C CG    . LYS C 3 63  ? 51.665 36.358  70.942 1.00 66.59  ?  63  LYS C CG    1 
ATOM   6683 C CD    . LYS C 3 63  ? 52.478 37.281  71.868 1.00 60.93  ?  63  LYS C CD    1 
ATOM   6684 C CE    . LYS C 3 63  ? 52.780 36.631  73.222 1.00 69.38  ?  63  LYS C CE    1 
ATOM   6685 N NZ    . LYS C 3 63  ? 54.248 36.334  73.427 1.00 74.35  ?  63  LYS C NZ    1 
ATOM   6686 H H     . LYS C 3 63  ? 50.418 35.138  69.184 1.00 70.30  ?  63  LYS C H     1 
ATOM   6687 H HA    . LYS C 3 63  ? 52.037 33.185  69.761 1.00 70.96  ?  63  LYS C HA    1 
ATOM   6688 H HB2   . LYS C 3 63  ? 52.983 34.803  71.293 1.00 75.29  ?  63  LYS C HB2   1 
ATOM   6689 H HB3   . LYS C 3 63  ? 52.955 35.247  69.767 1.00 75.29  ?  63  LYS C HB3   1 
ATOM   6690 H HG2   . LYS C 3 63  ? 51.459 36.856  70.135 1.00 79.91  ?  63  LYS C HG2   1 
ATOM   6691 H HG3   . LYS C 3 63  ? 50.845 36.122  71.405 1.00 79.91  ?  63  LYS C HG3   1 
ATOM   6692 H HD2   . LYS C 3 63  ? 53.322 37.496  71.442 1.00 73.12  ?  63  LYS C HD2   1 
ATOM   6693 H HD3   . LYS C 3 63  ? 51.973 38.093  72.031 1.00 73.12  ?  63  LYS C HD3   1 
ATOM   6694 H HE2   . LYS C 3 63  ? 52.496 37.231  73.930 1.00 83.25  ?  63  LYS C HE2   1 
ATOM   6695 H HE3   . LYS C 3 63  ? 52.295 35.793  73.284 1.00 83.25  ?  63  LYS C HE3   1 
ATOM   6696 H HZ1   . LYS C 3 63  ? 54.375 35.961  74.225 1.00 89.21  ?  63  LYS C HZ1   1 
ATOM   6697 H HZ2   . LYS C 3 63  ? 54.536 35.774  72.798 1.00 89.21  ?  63  LYS C HZ2   1 
ATOM   6698 H HZ3   . LYS C 3 63  ? 54.720 37.087  73.382 1.00 89.21  ?  63  LYS C HZ3   1 
ATOM   6699 N N     . GLU C 3 64  ? 51.747 32.247  72.017 1.00 58.58  ?  64  GLU C N     1 
ATOM   6700 C CA    . GLU C 3 64  ? 51.499 31.477  73.237 1.00 56.75  ?  64  GLU C CA    1 
ATOM   6701 C C     . GLU C 3 64  ? 50.218 30.637  73.183 1.00 52.77  ?  64  GLU C C     1 
ATOM   6702 O O     . GLU C 3 64  ? 49.853 30.002  74.188 1.00 47.50  ?  64  GLU C O     1 
ATOM   6703 C CB    . GLU C 3 64  ? 51.483 32.387  74.470 1.00 61.40  ?  64  GLU C CB    1 
ATOM   6704 C CG    . GLU C 3 64  ? 52.872 32.829  74.961 1.00 67.48  ?  64  GLU C CG    1 
ATOM   6705 C CD    . GLU C 3 64  ? 52.845 34.134  75.773 1.00 79.70  ?  64  GLU C CD    1 
ATOM   6706 O OE1   . GLU C 3 64  ? 51.782 34.487  76.361 1.00 78.14  ?  64  GLU C OE1   1 
ATOM   6707 O OE2   . GLU C 3 64  ? 53.899 34.813  75.811 1.00 84.61  -1 64  GLU C OE2   1 
ATOM   6708 H H     . GLU C 3 64  ? 52.485 32.009  71.646 1.00 70.29  ?  64  GLU C H     1 
ATOM   6709 H HA    . GLU C 3 64  ? 52.229 30.846  73.336 1.00 68.10  ?  64  GLU C HA    1 
ATOM   6710 H HB2   . GLU C 3 64  ? 50.981 33.189  74.255 1.00 73.68  ?  64  GLU C HB2   1 
ATOM   6711 H HB3   . GLU C 3 64  ? 51.054 31.912  75.198 1.00 73.68  ?  64  GLU C HB3   1 
ATOM   6712 H HG2   . GLU C 3 64  ? 53.240 32.134  75.529 1.00 80.98  ?  64  GLU C HG2   1 
ATOM   6713 H HG3   . GLU C 3 64  ? 53.447 32.969  74.193 1.00 80.98  ?  64  GLU C HG3   1 
ATOM   6714 N N     . SER C 3 65  ? 49.527 30.615  72.043 1.00 50.22  ?  65  SER C N     1 
ATOM   6715 C CA    . SER C 3 65  ? 48.427 29.687  71.850 1.00 54.43  ?  65  SER C CA    1 
ATOM   6716 C C     . SER C 3 65  ? 48.897 28.270  72.105 1.00 55.65  ?  65  SER C C     1 
ATOM   6717 O O     . SER C 3 65  ? 50.048 27.913  71.838 1.00 53.97  ?  65  SER C O     1 
ATOM   6718 C CB    . SER C 3 65  ? 47.864 29.773  70.428 1.00 53.29  ?  65  SER C CB    1 
ATOM   6719 O OG    . SER C 3 65  ? 47.421 31.088  70.131 1.00 59.96  ?  65  SER C OG    1 
ATOM   6720 H H     . SER C 3 65  ? 49.679 31.127  71.370 1.00 60.26  ?  65  SER C H     1 
ATOM   6721 H HA    . SER C 3 65  ? 47.715 29.917  72.468 1.00 65.31  ?  65  SER C HA    1 
ATOM   6722 H HB2   . SER C 3 65  ? 48.560 29.526  69.799 1.00 63.95  ?  65  SER C HB2   1 
ATOM   6723 H HB3   . SER C 3 65  ? 47.114 29.163  70.349 1.00 63.95  ?  65  SER C HB3   1 
ATOM   6724 H HG    . SER C 3 65  ? 47.285 31.166  69.305 1.00 71.95  ?  65  SER C HG    1 
ATOM   6725 N N     . THR C 3 66  ? 47.990 27.458  72.626 1.00 54.02  ?  66  THR C N     1 
ATOM   6726 C CA    . THR C 3 66  ? 48.257 26.053  72.873 1.00 52.17  ?  66  THR C CA    1 
ATOM   6727 C C     . THR C 3 66  ? 47.491 25.203  71.861 1.00 54.05  ?  66  THR C C     1 
ATOM   6728 O O     . THR C 3 66  ? 46.279 25.376  71.686 1.00 54.93  ?  66  THR C O     1 
ATOM   6729 C CB    . THR C 3 66  ? 47.862 25.661  74.301 1.00 50.34  ?  66  THR C CB    1 
ATOM   6730 O OG1   . THR C 3 66  ? 48.774 26.238  75.243 1.00 49.33  ?  66  THR C OG1   1 
ATOM   6731 C CG2   . THR C 3 66  ? 47.878 24.144  74.435 1.00 48.78  ?  66  THR C CG2   1 
ATOM   6732 H H     . THR C 3 66  ? 47.197 27.704  72.849 1.00 64.83  ?  66  THR C H     1 
ATOM   6733 H HA    . THR C 3 66  ? 49.205 25.880  72.761 1.00 62.60  ?  66  THR C HA    1 
ATOM   6734 H HB    . THR C 3 66  ? 46.970 25.987  74.497 1.00 60.41  ?  66  THR C HB    1 
ATOM   6735 H HG1   . THR C 3 66  ? 48.533 26.055  76.026 1.00 59.19  ?  66  THR C HG1   1 
ATOM   6736 H HG21  . THR C 3 66  ? 47.687 23.890  75.352 1.00 58.54  ?  66  THR C HG21  1 
ATOM   6737 H HG22  . THR C 3 66  ? 47.206 23.752  73.854 1.00 58.54  ?  66  THR C HG22  1 
ATOM   6738 H HG23  . THR C 3 66  ? 48.749 23.797  74.187 1.00 58.54  ?  66  THR C HG23  1 
ATOM   6739 N N     . LEU C 3 67  ? 48.203 24.298  71.198 1.00 48.38  ?  67  LEU C N     1 
ATOM   6740 C CA    . LEU C 3 67  ? 47.615 23.217  70.428 1.00 46.40  ?  67  LEU C CA    1 
ATOM   6741 C C     . LEU C 3 67  ? 47.549 21.955  71.296 1.00 43.74  ?  67  LEU C C     1 
ATOM   6742 O O     . LEU C 3 67  ? 48.247 21.839  72.297 1.00 44.29  ?  67  LEU C O     1 
ATOM   6743 C CB    . LEU C 3 67  ? 48.456 22.978  69.183 1.00 51.31  ?  67  LEU C CB    1 
ATOM   6744 C CG    . LEU C 3 67  ? 48.224 23.815  67.920 1.00 52.45  ?  67  LEU C CG    1 
ATOM   6745 C CD1   . LEU C 3 67  ? 46.854 23.546  67.354 1.00 51.73  ?  67  LEU C CD1   1 
ATOM   6746 C CD2   . LEU C 3 67  ? 48.384 25.300  68.200 1.00 52.31  ?  67  LEU C CD2   1 
ATOM   6747 H H     . LEU C 3 67  ? 49.063 24.292  71.179 1.00 58.05  ?  67  LEU C H     1 
ATOM   6748 H HA    . LEU C 3 67  ? 46.713 23.434  70.146 1.00 55.68  ?  67  LEU C HA    1 
ATOM   6749 H HB2   . LEU C 3 67  ? 49.382 23.121  69.432 1.00 61.57  ?  67  LEU C HB2   1 
ATOM   6750 H HB3   . LEU C 3 67  ? 48.321 22.054  68.920 1.00 61.57  ?  67  LEU C HB3   1 
ATOM   6751 H HG    . LEU C 3 67  ? 48.891 23.562  67.263 1.00 62.93  ?  67  LEU C HG    1 
ATOM   6752 H HD11  . LEU C 3 67  ? 46.713 24.117  66.582 1.00 62.08  ?  67  LEU C HD11  1 
ATOM   6753 H HD12  . LEU C 3 67  ? 46.798 22.614  67.092 1.00 62.08  ?  67  LEU C HD12  1 
ATOM   6754 H HD13  . LEU C 3 67  ? 46.188 23.739  68.033 1.00 62.08  ?  67  LEU C HD13  1 
ATOM   6755 H HD21  . LEU C 3 67  ? 48.210 25.796  67.385 1.00 62.78  ?  67  LEU C HD21  1 
ATOM   6756 H HD22  . LEU C 3 67  ? 47.752 25.562  68.888 1.00 62.78  ?  67  LEU C HD22  1 
ATOM   6757 H HD23  . LEU C 3 67  ? 49.291 25.468  68.502 1.00 62.78  ?  67  LEU C HD23  1 
ATOM   6758 N N     . HIS C 3 68  ? 46.676 21.019  70.921 1.00 44.96  ?  68  HIS C N     1 
ATOM   6759 C CA    . HIS C 3 68  ? 46.636 19.687  71.531 1.00 43.62  ?  68  HIS C CA    1 
ATOM   6760 C C     . HIS C 3 68  ? 46.958 18.627  70.486 1.00 41.01  ?  68  HIS C C     1 
ATOM   6761 O O     . HIS C 3 68  ? 46.523 18.731  69.329 1.00 39.45  ?  68  HIS C O     1 
ATOM   6762 C CB    . HIS C 3 68  ? 45.274 19.386  72.147 1.00 39.17  ?  68  HIS C CB    1 
ATOM   6763 C CG    . HIS C 3 68  ? 45.161 19.839  73.559 1.00 40.98  ?  68  HIS C CG    1 
ATOM   6764 N ND1   . HIS C 3 68  ? 44.666 21.079  73.903 1.00 39.51  ?  68  HIS C ND1   1 
ATOM   6765 C CD2   . HIS C 3 68  ? 45.536 19.246  74.713 1.00 44.04  ?  68  HIS C CD2   1 
ATOM   6766 C CE1   . HIS C 3 68  ? 44.717 21.214  75.215 1.00 45.59  ?  68  HIS C CE1   1 
ATOM   6767 N NE2   . HIS C 3 68  ? 45.241 20.116  75.730 1.00 47.95  ?  68  HIS C NE2   1 
ATOM   6768 H H     . HIS C 3 68  ? 46.086 21.133  70.306 1.00 53.96  ?  68  HIS C H     1 
ATOM   6769 H HA    . HIS C 3 68  ? 47.304 19.648  72.233 1.00 52.34  ?  68  HIS C HA    1 
ATOM   6770 H HB2   . HIS C 3 68  ? 44.588 19.839  71.631 1.00 47.01  ?  68  HIS C HB2   1 
ATOM   6771 H HB3   . HIS C 3 68  ? 45.125 18.428  72.128 1.00 47.01  ?  68  HIS C HB3   1 
ATOM   6772 H HD1   . HIS C 3 68  ? 44.371 21.669  73.351 1.00 47.41  ?  68  HIS C HD1   1 
ATOM   6773 H HD2   . HIS C 3 68  ? 45.922 18.404  74.801 1.00 52.85  ?  68  HIS C HD2   1 
ATOM   6774 H HE1   . HIS C 3 68  ? 44.431 21.957  75.696 1.00 54.71  ?  68  HIS C HE1   1 
ATOM   6775 N N     . LEU C 3 69  ? 47.710 17.599  70.876 1.00 36.19  ?  69  LEU C N     1 
ATOM   6776 C CA    . LEU C 3 69  ? 48.166 16.605  69.910 1.00 37.33  ?  69  LEU C CA    1 
ATOM   6777 C C     . LEU C 3 69  ? 47.681 15.204  70.266 1.00 33.59  ?  69  LEU C C     1 
ATOM   6778 O O     . LEU C 3 69  ? 47.932 14.700  71.368 1.00 36.16  ?  69  LEU C O     1 
ATOM   6779 C CB    . LEU C 3 69  ? 49.689 16.626  69.788 1.00 37.10  ?  69  LEU C CB    1 
ATOM   6780 C CG    . LEU C 3 69  ? 50.257 15.609  68.802 1.00 36.11  ?  69  LEU C CG    1 
ATOM   6781 C CD1   . LEU C 3 69  ? 50.183 16.003  67.336 1.00 34.35  ?  69  LEU C CD1   1 
ATOM   6782 C CD2   . LEU C 3 69  ? 51.677 15.366  69.239 1.00 33.70  ?  69  LEU C CD2   1 
ATOM   6783 H H     . LEU C 3 69  ? 47.964 17.459  71.686 1.00 43.43  ?  69  LEU C H     1 
ATOM   6784 H HA    . LEU C 3 69  ? 47.765 16.824  69.055 1.00 44.80  ?  69  LEU C HA    1 
ATOM   6785 H HB2   . LEU C 3 69  ? 49.963 17.508  69.491 1.00 44.52  ?  69  LEU C HB2   1 
ATOM   6786 H HB3   . LEU C 3 69  ? 50.072 16.436  70.659 1.00 44.52  ?  69  LEU C HB3   1 
ATOM   6787 H HG    . LEU C 3 69  ? 49.717 14.804  68.825 1.00 43.34  ?  69  LEU C HG    1 
ATOM   6788 H HD11  . LEU C 3 69  ? 50.550 15.286  66.796 1.00 41.21  ?  69  LEU C HD11  1 
ATOM   6789 H HD12  . LEU C 3 69  ? 49.255 16.155  67.096 1.00 41.21  ?  69  LEU C HD12  1 
ATOM   6790 H HD13  . LEU C 3 69  ? 50.696 16.815  67.200 1.00 41.21  ?  69  LEU C HD13  1 
ATOM   6791 H HD21  . LEU C 3 69  ? 52.085 14.719  68.643 1.00 40.44  ?  69  LEU C HD21  1 
ATOM   6792 H HD22  . LEU C 3 69  ? 52.166 16.203  69.203 1.00 40.44  ?  69  LEU C HD22  1 
ATOM   6793 H HD23  . LEU C 3 69  ? 51.674 15.023  70.147 1.00 40.44  ?  69  LEU C HD23  1 
ATOM   6794 N N     . VAL C 3 70  ? 47.020 14.575  69.306 1.00 28.13  ?  70  VAL C N     1 
ATOM   6795 C CA    . VAL C 3 70  ? 46.517 13.218  69.424 1.00 31.95  ?  70  VAL C CA    1 
ATOM   6796 C C     . VAL C 3 70  ? 47.131 12.391  68.305 1.00 28.76  ?  70  VAL C C     1 
ATOM   6797 O O     . VAL C 3 70  ? 47.110 12.800  67.138 1.00 31.34  ?  70  VAL C O     1 
ATOM   6798 C CB    . VAL C 3 70  ? 44.979 13.178  69.361 1.00 31.52  ?  70  VAL C CB    1 
ATOM   6799 C CG1   . VAL C 3 70  ? 44.469 11.989  70.106 1.00 34.35  ?  70  VAL C CG1   1 
ATOM   6800 C CG2   . VAL C 3 70  ? 44.398 14.437  69.939 1.00 33.81  ?  70  VAL C CG2   1 
ATOM   6801 H H     . VAL C 3 70  ? 46.843 14.931  68.543 1.00 33.76  ?  70  VAL C H     1 
ATOM   6802 H HA    . VAL C 3 70  ? 46.794 12.839  70.273 1.00 38.34  ?  70  VAL C HA    1 
ATOM   6803 H HB    . VAL C 3 70  ? 44.702 13.110  68.434 1.00 37.83  ?  70  VAL C HB    1 
ATOM   6804 H HG11  . VAL C 3 70  ? 43.501 11.973  70.050 1.00 41.22  ?  70  VAL C HG11  1 
ATOM   6805 H HG12  . VAL C 3 70  ? 44.837 11.185  69.707 1.00 41.22  ?  70  VAL C HG12  1 
ATOM   6806 H HG13  . VAL C 3 70  ? 44.746 12.055  71.033 1.00 41.22  ?  70  VAL C HG13  1 
ATOM   6807 H HG21  . VAL C 3 70  ? 43.430 14.380  69.911 1.00 40.57  ?  70  VAL C HG21  1 
ATOM   6808 H HG22  . VAL C 3 70  ? 44.697 14.530  70.857 1.00 40.57  ?  70  VAL C HG22  1 
ATOM   6809 H HG23  . VAL C 3 70  ? 44.700 15.195  69.414 1.00 40.57  ?  70  VAL C HG23  1 
ATOM   6810 N N     . LEU C 3 71  ? 47.689 11.245  68.658 1.00 26.65  ?  71  LEU C N     1 
ATOM   6811 C CA    . LEU C 3 71  ? 48.326 10.376  67.682 1.00 31.73  ?  71  LEU C CA    1 
ATOM   6812 C C     . LEU C 3 71  ? 47.372 9.255   67.295 1.00 32.20  ?  71  LEU C C     1 
ATOM   6813 O O     . LEU C 3 71  ? 46.782 8.595   68.163 1.00 32.53  ?  71  LEU C O     1 
ATOM   6814 C CB    . LEU C 3 71  ? 49.639 9.818   68.227 1.00 33.36  ?  71  LEU C CB    1 
ATOM   6815 C CG    . LEU C 3 71  ? 50.851 10.732  68.038 1.00 34.54  ?  71  LEU C CG    1 
ATOM   6816 C CD1   . LEU C 3 71  ? 50.474 12.157  68.404 1.00 31.34  ?  71  LEU C CD1   1 
ATOM   6817 C CD2   . LEU C 3 71  ? 52.032 10.252  68.867 1.00 32.92  ?  71  LEU C CD2   1 
ATOM   6818 H H     . LEU C 3 71  ? 47.711 10.945  69.464 1.00 31.98  ?  71  LEU C H     1 
ATOM   6819 H HA    . LEU C 3 71  ? 48.529 10.881  66.879 1.00 38.07  ?  71  LEU C HA    1 
ATOM   6820 H HB2   . LEU C 3 71  ? 49.535 9.663   69.179 1.00 40.04  ?  71  LEU C HB2   1 
ATOM   6821 H HB3   . LEU C 3 71  ? 49.829 8.982   67.774 1.00 40.04  ?  71  LEU C HB3   1 
ATOM   6822 H HG    . LEU C 3 71  ? 51.129 10.713  67.109 1.00 41.45  ?  71  LEU C HG    1 
ATOM   6823 H HD11  . LEU C 3 71  ? 51.269 12.711  68.375 1.00 37.60  ?  71  LEU C HD11  1 
ATOM   6824 H HD12  . LEU C 3 71  ? 49.820 12.484  67.767 1.00 37.60  ?  71  LEU C HD12  1 
ATOM   6825 H HD13  . LEU C 3 71  ? 50.098 12.164  69.298 1.00 37.60  ?  71  LEU C HD13  1 
ATOM   6826 H HD21  . LEU C 3 71  ? 52.807 10.797  68.658 1.00 39.50  ?  71  LEU C HD21  1 
ATOM   6827 H HD22  . LEU C 3 71  ? 51.812 10.336  69.808 1.00 39.50  ?  71  LEU C HD22  1 
ATOM   6828 H HD23  . LEU C 3 71  ? 52.213 9.324   68.650 1.00 39.50  ?  71  LEU C HD23  1 
ATOM   6829 N N     . ARG C 3 72  ? 47.212 9.068   65.989 1.00 33.81  ?  72  ARG C N     1 
ATOM   6830 C CA    . ARG C 3 72  ? 46.357 8.018   65.455 1.00 39.46  ?  72  ARG C CA    1 
ATOM   6831 C C     . ARG C 3 72  ? 46.941 6.654   65.806 1.00 38.34  ?  72  ARG C C     1 
ATOM   6832 O O     . ARG C 3 72  ? 48.157 6.494   65.906 1.00 36.82  ?  72  ARG C O     1 
ATOM   6833 C CB    . ARG C 3 72  ? 46.207 8.195   63.933 1.00 40.70  ?  72  ARG C CB    1 
ATOM   6834 C CG    . ARG C 3 72  ? 45.565 9.564   63.515 1.00 42.63  ?  72  ARG C CG    1 
ATOM   6835 C CD    . ARG C 3 72  ? 45.491 9.770   61.999 1.00 47.58  ?  72  ARG C CD    1 
ATOM   6836 N NE    . ARG C 3 72  ? 44.798 8.650   61.360 1.00 55.41  ?  72  ARG C NE    1 
ATOM   6837 C CZ    . ARG C 3 72  ? 44.612 8.499   60.048 1.00 57.97  ?  72  ARG C CZ    1 
ATOM   6838 N NH1   . ARG C 3 72  ? 45.072 9.411   59.181 1.00 58.80  ?  72  ARG C NH1   1 
ATOM   6839 N NH2   . ARG C 3 72  ? 43.966 7.415   59.605 1.00 52.98  ?  72  ARG C NH2   1 
ATOM   6840 H H     . ARG C 3 72  ? 47.594 9.544   65.383 1.00 40.57  ?  72  ARG C H     1 
ATOM   6841 H HA    . ARG C 3 72  ? 45.468 8.065   65.839 1.00 47.35  ?  72  ARG C HA    1 
ATOM   6842 H HB2   . ARG C 3 72  ? 47.086 8.143   63.525 1.00 48.84  ?  72  ARG C HB2   1 
ATOM   6843 H HB3   . ARG C 3 72  ? 45.641 7.485   63.591 1.00 48.84  ?  72  ARG C HB3   1 
ATOM   6844 H HG2   . ARG C 3 72  ? 44.660 9.605   63.863 1.00 51.15  ?  72  ARG C HG2   1 
ATOM   6845 H HG3   . ARG C 3 72  ? 46.096 10.286  63.885 1.00 51.15  ?  72  ARG C HG3   1 
ATOM   6846 H HD2   . ARG C 3 72  ? 45.003 10.586  61.806 1.00 57.09  ?  72  ARG C HD2   1 
ATOM   6847 H HD3   . ARG C 3 72  ? 46.388 9.826   61.635 1.00 57.09  ?  72  ARG C HD3   1 
ATOM   6848 H HE    . ARG C 3 72  ? 44.483 8.037   61.874 1.00 66.50  ?  72  ARG C HE    1 
ATOM   6849 H HH11  . ARG C 3 72  ? 45.493 10.104  59.468 1.00 70.56  ?  72  ARG C HH11  1 
ATOM   6850 H HH12  . ARG C 3 72  ? 44.947 9.304   58.337 1.00 70.56  ?  72  ARG C HH12  1 
ATOM   6851 H HH21  . ARG C 3 72  ? 43.677 6.828   60.164 1.00 63.57  ?  72  ARG C HH21  1 
ATOM   6852 H HH22  . ARG C 3 72  ? 43.839 7.304   58.761 1.00 63.57  ?  72  ARG C HH22  1 
ATOM   6853 N N     . LEU C 3 73  ? 46.076 5.659   66.030 1.00 43.25  ?  73  LEU C N     1 
ATOM   6854 C CA    . LEU C 3 73  ? 46.471 4.257   66.308 1.00 43.02  ?  73  LEU C CA    1 
ATOM   6855 C C     . LEU C 3 73  ? 45.822 3.418   65.214 1.00 43.99  ?  73  LEU C C     1 
ATOM   6856 O O     . LEU C 3 73  ? 44.593 3.409   65.170 1.00 50.58  ?  73  LEU C O     1 
ATOM   6857 C CB    . LEU C 3 73  ? 46.014 3.858   67.708 1.00 44.13  ?  73  LEU C CB    1 
ATOM   6858 C CG    . LEU C 3 73  ? 46.756 4.519   68.868 1.00 45.28  ?  73  LEU C CG    1 
ATOM   6859 C CD1   . LEU C 3 73  ? 45.894 5.574   69.540 1.00 39.30  ?  73  LEU C CD1   1 
ATOM   6860 C CD2   . LEU C 3 73  ? 47.216 3.483   69.880 1.00 42.68  ?  73  LEU C CD2   1 
ATOM   6861 H H     . LEU C 3 73  ? 45.167 5.757   66.004 1.00 51.90  ?  73  LEU C H     1 
ATOM   6862 H HA    . LEU C 3 73  ? 47.444 4.166   66.244 1.00 51.62  ?  73  LEU C HA    1 
ATOM   6863 H HB2   . LEU C 3 73  ? 45.063 4.062   67.793 1.00 52.95  ?  73  LEU C HB2   1 
ATOM   6864 H HB3   . LEU C 3 73  ? 46.108 2.889   67.789 1.00 52.95  ?  73  LEU C HB3   1 
ATOM   6865 H HG    . LEU C 3 73  ? 47.559 4.969   68.506 1.00 54.33  ?  73  LEU C HG    1 
ATOM   6866 H HD11  . LEU C 3 73  ? 46.414 6.034   70.222 1.00 47.16  ?  73  LEU C HD11  1 
ATOM   6867 H HD12  . LEU C 3 73  ? 45.597 6.218   68.877 1.00 47.16  ?  73  LEU C HD12  1 
ATOM   6868 H HD13  . LEU C 3 73  ? 45.121 5.154   69.953 1.00 47.16  ?  73  LEU C HD13  1 
ATOM   6869 H HD21  . LEU C 3 73  ? 47.657 3.929   70.623 1.00 51.21  ?  73  LEU C HD21  1 
ATOM   6870 H HD22  . LEU C 3 73  ? 46.447 2.988   70.212 1.00 51.21  ?  73  LEU C HD22  1 
ATOM   6871 H HD23  . LEU C 3 73  ? 47.841 2.869   69.457 1.00 51.21  ?  73  LEU C HD23  1 
ATOM   6872 N N     . ARG C 3 74  ? 46.608 2.764   64.360 1.00 46.34  ?  74  ARG C N     1 
ATOM   6873 C CA    . ARG C 3 74  ? 46.100 2.036   63.174 1.00 52.74  ?  74  ARG C CA    1 
ATOM   6874 C C     . ARG C 3 74  ? 46.989 0.818   62.904 1.00 54.75  ?  74  ARG C C     1 
ATOM   6875 O O     . ARG C 3 74  ? 47.742 0.468   63.816 1.00 53.33  ?  74  ARG C O     1 
ATOM   6876 C CB    . ARG C 3 74  ? 45.989 3.060   62.037 1.00 49.72  ?  74  ARG C CB    1 
ATOM   6877 C CG    . ARG C 3 74  ? 47.274 3.768   61.623 1.00 49.40  ?  74  ARG C CG    1 
ATOM   6878 C CD    . ARG C 3 74  ? 47.248 5.272   61.866 1.00 47.26  ?  74  ARG C CD    1 
ATOM   6879 N NE    . ARG C 3 74  ? 48.226 6.008   61.068 1.00 48.17  ?  74  ARG C NE    1 
ATOM   6880 C CZ    . ARG C 3 74  ? 48.112 6.372   59.782 1.00 47.67  ?  74  ARG C CZ    1 
ATOM   6881 N NH1   . ARG C 3 74  ? 47.045 6.069   59.052 1.00 52.85  ?  74  ARG C NH1   1 
ATOM   6882 N NH2   . ARG C 3 74  ? 49.099 7.047   59.213 1.00 46.65  ?  74  ARG C NH2   1 
ATOM   6883 H H     . ARG C 3 74  ? 47.514 2.705   64.462 1.00 55.61  ?  74  ARG C H     1 
ATOM   6884 H HA    . ARG C 3 74  ? 45.192 1.702   63.377 1.00 63.28  ?  74  ARG C HA    1 
ATOM   6885 H HB2   . ARG C 3 74  ? 45.609 2.610   61.244 1.00 59.67  ?  74  ARG C HB2   1 
ATOM   6886 H HB3   . ARG C 3 74  ? 45.331 3.742   62.320 1.00 59.67  ?  74  ARG C HB3   1 
ATOM   6887 H HG2   . ARG C 3 74  ? 48.039 3.382   62.115 1.00 59.29  ?  74  ARG C HG2   1 
ATOM   6888 H HG3   . ARG C 3 74  ? 47.431 3.604   60.660 1.00 59.29  ?  74  ARG C HG3   1 
ATOM   6889 H HD2   . ARG C 3 74  ? 46.346 5.632   61.681 1.00 56.72  ?  74  ARG C HD2   1 
ATOM   6890 H HD3   . ARG C 3 74  ? 47.436 5.436   62.822 1.00 56.72  ?  74  ARG C HD3   1 
ATOM   6891 H HE    . ARG C 3 74  ? 48.977 6.256   61.496 1.00 57.80  ?  74  ARG C HE    1 
ATOM   6892 H HH11  . ARG C 3 74  ? 46.353 5.610   59.394 1.00 63.42  ?  74  ARG C HH11  1 
ATOM   6893 H HH12  . ARG C 3 74  ? 47.004 6.325   58.192 1.00 63.42  ?  74  ARG C HH12  1 
ATOM   6894 H HH21  . ARG C 3 74  ? 49.833 7.270   59.683 1.00 55.98  ?  74  ARG C HH21  1 
ATOM   6895 H HH22  . ARG C 3 74  ? 49.041 7.298   58.352 1.00 55.98  ?  74  ARG C HH22  1 
ATOM   6896 N N     . GLY C 3 75  ? 46.874 0.176   61.735 1.00 66.53  ?  75  GLY C N     1 
ATOM   6897 C CA    . GLY C 3 75  ? 47.684 -0.997  61.363 1.00 84.82  ?  75  GLY C CA    1 
ATOM   6898 C C     . GLY C 3 75  ? 47.946 -1.079  59.879 1.00 89.70  ?  75  GLY C C     1 
ATOM   6899 O O     . GLY C 3 75  ? 47.594 -0.123  59.205 1.00 80.90  ?  75  GLY C O     1 
ATOM   6900 H H     . GLY C 3 75  ? 46.261 0.404   61.106 1.00 79.84  ?  75  GLY C H     1 
ATOM   6901 H HA2   . GLY C 3 75  ? 48.552 -0.958  61.836 1.00 101.78 ?  75  GLY C HA2   1 
ATOM   6902 H HA3   . GLY C 3 75  ? 47.213 -1.816  61.657 1.00 101.78 ?  75  GLY C HA3   1 
HETATM 6903 P PG    . ANP D 4 .   ? 26.229 19.597  18.901 1.00 53.87  ?  401 ANP A PG    1 
HETATM 6904 O O1G   . ANP D 4 .   ? 27.678 19.705  18.366 1.00 38.49  ?  401 ANP A O1G   1 
HETATM 6905 O O2G   . ANP D 4 .   ? 25.782 18.159  18.825 1.00 41.81  ?  401 ANP A O2G   1 
HETATM 6906 O O3G   . ANP D 4 .   ? 26.158 20.139  20.341 1.00 41.37  ?  401 ANP A O3G   1 
HETATM 6907 P PB    . ANP D 4 .   ? 25.524 22.189  17.606 1.00 31.93  ?  401 ANP A PB    1 
HETATM 6908 O O1B   . ANP D 4 .   ? 24.485 22.848  16.768 1.00 30.82  ?  401 ANP A O1B   1 
HETATM 6909 O O2B   . ANP D 4 .   ? 25.843 22.931  18.900 1.00 29.60  ?  401 ANP A O2B   1 
HETATM 6910 N N3B   . ANP D 4 .   ? 25.174 20.542  17.924 1.00 35.28  ?  401 ANP A N3B   1 
HETATM 6911 P PA    . ANP D 4 .   ? 27.390 21.687  15.408 1.00 30.37  ?  401 ANP A PA    1 
HETATM 6912 O O1A   . ANP D 4 .   ? 26.200 21.083  14.714 1.00 28.14  -1 401 ANP A O1A   1 
HETATM 6913 O O2A   . ANP D 4 .   ? 28.562 20.780  15.603 1.00 29.04  ?  401 ANP A O2A   1 
HETATM 6914 O O3A   . ANP D 4 .   ? 26.931 22.301  16.831 1.00 34.55  ?  401 ANP A O3A   1 
HETATM 6915 O "O5'" . ANP D 4 .   ? 27.842 23.181  14.876 1.00 37.80  ?  401 ANP A "O5'" 1 
HETATM 6916 C "C5'" . ANP D 4 .   ? 28.510 23.351  13.668 1.00 36.36  ?  401 ANP A "C5'" 1 
HETATM 6917 C "C4'" . ANP D 4 .   ? 29.304 24.449  13.858 1.00 35.51  ?  401 ANP A "C4'" 1 
HETATM 6918 O "O4'" . ANP D 4 .   ? 30.619 24.067  13.266 1.00 38.01  ?  401 ANP A "O4'" 1 
HETATM 6919 C "C3'" . ANP D 4 .   ? 28.799 25.649  12.959 1.00 36.30  ?  401 ANP A "C3'" 1 
HETATM 6920 O "O3'" . ANP D 4 .   ? 29.103 26.892  13.723 1.00 36.40  ?  401 ANP A "O3'" 1 
HETATM 6921 C "C2'" . ANP D 4 .   ? 29.507 25.573  11.923 1.00 37.79  ?  401 ANP A "C2'" 1 
HETATM 6922 O "O2'" . ANP D 4 .   ? 29.718 26.882  11.278 1.00 35.75  ?  401 ANP A "O2'" 1 
HETATM 6923 C "C1'" . ANP D 4 .   ? 30.951 25.084  12.520 1.00 39.10  ?  401 ANP A "C1'" 1 
HETATM 6924 N N9    . ANP D 4 .   ? 31.855 24.597  11.522 1.00 39.57  ?  401 ANP A N9    1 
HETATM 6925 C C8    . ANP D 4 .   ? 32.939 25.365  11.857 1.00 39.97  ?  401 ANP A C8    1 
HETATM 6926 N N7    . ANP D 4 .   ? 33.982 25.065  11.040 1.00 31.77  ?  401 ANP A N7    1 
HETATM 6927 C C5    . ANP D 4 .   ? 33.528 24.098  10.236 1.00 34.97  ?  401 ANP A C5    1 
HETATM 6928 C C6    . ANP D 4 .   ? 34.147 23.416  9.230  1.00 37.01  ?  401 ANP A C6    1 
HETATM 6929 N N6    . ANP D 4 .   ? 35.532 23.571  8.739  1.00 47.18  ?  401 ANP A N6    1 
HETATM 6930 N N1    . ANP D 4 .   ? 33.465 22.513  8.579  1.00 42.93  ?  401 ANP A N1    1 
HETATM 6931 C C2    . ANP D 4 .   ? 32.144 22.263  8.917  1.00 49.38  ?  401 ANP A C2    1 
HETATM 6932 N N3    . ANP D 4 .   ? 31.508 22.918  9.920  1.00 35.89  ?  401 ANP A N3    1 
HETATM 6933 C C4    . ANP D 4 .   ? 32.231 23.820  10.544 1.00 35.61  ?  401 ANP A C4    1 
HETATM 6934 P PB    . AR6 E 5 .   ? 36.877 5.348   62.014 1.00 32.42  ?  101 AR6 C PB    1 
HETATM 6935 O O1B   . AR6 E 5 .   ? 35.492 5.327   62.530 1.00 39.31  ?  101 AR6 C O1B   1 
HETATM 6936 C C1D   . AR6 E 5 .   ? 40.828 8.590   62.836 1.00 57.02  ?  101 AR6 C C1D   1 
HETATM 6937 O O1D   . AR6 E 5 .   ? 41.266 9.612   63.427 1.00 66.44  ?  101 AR6 C O1D   1 
HETATM 6938 O O2B   . AR6 E 5 .   ? 36.720 5.367   60.511 1.00 44.76  ?  101 AR6 C O2B   1 
HETATM 6939 C C2D   . AR6 E 5 .   ? 41.282 8.757   61.363 1.00 59.89  ?  101 AR6 C C2D   1 
HETATM 6940 O O2D   . AR6 E 5 .   ? 41.639 10.163  60.896 1.00 64.80  ?  101 AR6 C O2D   1 
HETATM 6941 O O3A   . AR6 E 5 .   ? 37.854 4.051   62.368 1.00 39.66  ?  101 AR6 C O3A   1 
HETATM 6942 C C3D   . AR6 E 5 .   ? 40.238 8.341   60.662 1.00 59.04  ?  101 AR6 C C3D   1 
HETATM 6943 O O3D   . AR6 E 5 .   ? 39.973 8.982   59.376 1.00 60.50  ?  101 AR6 C O3D   1 
HETATM 6944 C C4D   . AR6 E 5 .   ? 38.888 8.565   61.592 1.00 49.14  ?  101 AR6 C C4D   1 
HETATM 6945 O O4D   . AR6 E 5 .   ? 39.238 8.460   62.809 1.00 54.49  ?  101 AR6 C O4D   1 
HETATM 6946 C C5D   . AR6 E 5 .   ? 38.127 7.338   61.085 1.00 51.61  ?  101 AR6 C C5D   1 
HETATM 6947 O O5D   . AR6 E 5 .   ? 37.595 6.793   62.241 1.00 45.72  ?  101 AR6 C O5D   1 
HETATM 6948 H H1D   . AR6 E 5 .   ? 41.184 7.638   63.345 1.00 68.43  ?  101 AR6 C H1D   1 
HETATM 6949 H H2D   . AR6 E 5 .   ? 42.198 8.141   61.259 1.00 71.86  ?  101 AR6 C H2D   1 
HETATM 6950 H HO2D  . AR6 E 5 .   ? 41.937 10.106  59.959 1.00 77.76  ?  101 AR6 C HO2D  1 
HETATM 6951 H H3D   . AR6 E 5 .   ? 40.489 7.289   60.478 1.00 70.85  ?  101 AR6 C H3D   1 
HETATM 6952 H HO3D  . AR6 E 5 .   ? 39.190 8.599   58.992 1.00 72.60  ?  101 AR6 C HO3D  1 
HETATM 6953 H H4D   . AR6 E 5 .   ? 38.382 9.524   61.555 1.00 58.97  ?  101 AR6 C H4D   1 
HETATM 6954 H H5D   . AR6 E 5 .   ? 37.332 7.628   60.388 1.00 61.93  ?  101 AR6 C H5D   1 
HETATM 6955 H H5DA  . AR6 E 5 .   ? 38.805 6.629   60.594 1.00 61.93  ?  101 AR6 C H5DA  1 
HETATM 6956 O O     . HOH F 6 .   ? 52.958 30.322  19.347 1.00 35.60  ?  501 HOH A O     1 
HETATM 6957 O O     . HOH F 6 .   ? 32.473 15.077  10.028 1.00 48.03  ?  502 HOH A O     1 
HETATM 6958 O O     . HOH F 6 .   ? 30.301 11.722  40.521 1.00 21.48  ?  503 HOH A O     1 
HETATM 6959 O O     . HOH F 6 .   ? 39.623 4.341   42.372 1.00 46.22  ?  504 HOH A O     1 
HETATM 6960 O O     . HOH F 6 .   ? 27.714 10.960  39.620 1.00 22.79  ?  505 HOH A O     1 
HETATM 6961 O O     . HOH F 6 .   ? 20.520 4.019   30.795 1.00 45.17  ?  506 HOH A O     1 
HETATM 6962 O O     . HOH F 6 .   ? 50.368 24.234  10.964 1.00 41.84  ?  507 HOH A O     1 
HETATM 6963 O O     . HOH F 6 .   ? 50.938 25.024  7.264  1.00 48.94  ?  508 HOH A O     1 
HETATM 6964 O O     . HOH F 6 .   ? 55.406 11.420  34.415 1.00 50.01  ?  509 HOH A O     1 
HETATM 6965 O O     . HOH F 6 .   ? 30.780 3.909   34.956 1.00 34.22  ?  510 HOH A O     1 
HETATM 6966 O O     . HOH F 6 .   ? 54.269 19.895  23.085 1.00 20.38  ?  511 HOH A O     1 
HETATM 6967 O O     . HOH F 6 .   ? 2.104  16.315  16.746 1.00 38.56  ?  512 HOH A O     1 
HETATM 6968 O O     . HOH F 6 .   ? 45.739 28.486  14.495 1.00 31.87  ?  513 HOH A O     1 
HETATM 6969 O O     . HOH F 6 .   ? 16.965 20.200  5.723  1.00 56.33  ?  514 HOH A O     1 
HETATM 6970 O O     . HOH F 6 .   ? 41.655 10.116  14.533 1.00 33.78  ?  515 HOH A O     1 
HETATM 6971 O O     . HOH F 6 .   ? 38.380 3.283   25.279 1.00 37.45  ?  516 HOH A O     1 
HETATM 6972 O O     . HOH F 6 .   ? 24.248 11.494  36.380 1.00 37.75  ?  517 HOH A O     1 
HETATM 6973 O O     . HOH F 6 .   ? 44.506 37.577  16.079 1.00 28.29  ?  518 HOH A O     1 
HETATM 6974 O O     . HOH F 6 .   ? 44.923 3.072   28.365 1.00 28.71  ?  519 HOH A O     1 
HETATM 6975 O O     . HOH F 6 .   ? 47.594 37.927  5.616  1.00 39.79  ?  520 HOH A O     1 
HETATM 6976 O O     . HOH F 6 .   ? 3.945  21.243  27.375 1.00 40.71  ?  521 HOH A O     1 
HETATM 6977 O O     . HOH F 6 .   ? 35.335 -0.278  37.630 1.00 47.97  ?  522 HOH A O     1 
HETATM 6978 O O     . HOH F 6 .   ? 12.647 23.238  32.338 1.00 27.69  ?  523 HOH A O     1 
HETATM 6979 O O     . HOH F 6 .   ? 29.891 31.861  -5.976 1.00 42.01  ?  524 HOH A O     1 
HETATM 6980 O O     . HOH F 6 .   ? 12.260 -2.600  29.537 1.00 56.59  ?  525 HOH A O     1 
HETATM 6981 O O     . HOH F 6 .   ? 50.353 6.338   29.882 1.00 31.56  ?  526 HOH A O     1 
HETATM 6982 O O     . HOH F 6 .   ? 12.348 8.182   39.152 1.00 53.19  ?  527 HOH A O     1 
HETATM 6983 O O     . HOH F 6 .   ? 54.520 27.487  8.750  1.00 43.34  ?  528 HOH A O     1 
HETATM 6984 O O     . HOH F 6 .   ? 27.817 28.324  4.309  1.00 44.85  ?  529 HOH A O     1 
HETATM 6985 O O     . HOH F 6 .   ? 49.337 35.340  20.932 1.00 24.99  ?  530 HOH A O     1 
HETATM 6986 O O     . HOH F 6 .   ? 15.595 20.517  37.949 1.00 41.29  ?  531 HOH A O     1 
HETATM 6987 O O     . HOH F 6 .   ? 22.525 26.846  32.001 1.00 40.27  ?  532 HOH A O     1 
HETATM 6988 O O     . HOH F 6 .   ? 28.326 30.538  13.187 1.00 41.78  ?  533 HOH A O     1 
HETATM 6989 O O     . HOH F 6 .   ? 19.894 1.909   29.955 1.00 35.59  ?  534 HOH A O     1 
HETATM 6990 O O     . HOH F 6 .   ? 40.668 13.783  41.832 1.00 35.48  ?  535 HOH A O     1 
HETATM 6991 O O     . HOH F 6 .   ? 47.279 4.088   27.012 1.00 34.75  ?  536 HOH A O     1 
HETATM 6992 O O     . HOH F 6 .   ? 44.909 4.141   14.159 1.00 48.73  ?  537 HOH A O     1 
HETATM 6993 O O     . HOH F 6 .   ? -1.106 31.141  2.633  1.00 39.38  ?  538 HOH A O     1 
HETATM 6994 O O     . HOH F 6 .   ? 43.070 5.565   13.124 1.00 38.84  ?  539 HOH A O     1 
HETATM 6995 O O     . HOH G 6 .   ? 21.176 13.647  57.656 1.00 48.25  ?  401 HOH B O     1 
HETATM 6996 O O     . HOH G 6 .   ? 29.257 6.970   85.437 1.00 39.94  ?  402 HOH B O     1 
HETATM 6997 O O     . HOH G 6 .   ? 36.578 10.568  79.332 1.00 33.84  ?  403 HOH B O     1 
HETATM 6998 O O     . HOH G 6 .   ? 29.362 -17.080 47.933 1.00 52.91  ?  404 HOH B O     1 
HETATM 6999 O O     . HOH G 6 .   ? 40.783 12.324  70.402 1.00 29.07  ?  405 HOH B O     1 
HETATM 7000 O O     . HOH G 6 .   ? 33.771 -4.499  68.479 1.00 32.89  ?  406 HOH B O     1 
HETATM 7001 O O     . HOH G 6 .   ? 38.536 5.958   78.858 1.00 34.87  ?  407 HOH B O     1 
HETATM 7002 O O     . HOH G 6 .   ? 35.805 -14.653 71.364 1.00 44.62  ?  408 HOH B O     1 
HETATM 7003 O O     . HOH G 6 .   ? 24.227 20.605  67.236 1.00 41.09  ?  409 HOH B O     1 
HETATM 7004 O O     . HOH G 6 .   ? 11.962 8.823   80.748 1.00 35.98  ?  410 HOH B O     1 
HETATM 7005 O O     . HOH G 6 .   ? 38.559 3.546   59.137 1.00 25.85  ?  411 HOH B O     1 
HETATM 7006 O O     . HOH G 6 .   ? 34.775 -3.118  54.262 1.00 26.83  ?  412 HOH B O     1 
HETATM 7007 O O     . HOH G 6 .   ? 12.523 13.825  65.375 1.00 43.57  ?  413 HOH B O     1 
HETATM 7008 O O     . HOH G 6 .   ? 27.057 17.545  48.150 1.00 26.81  ?  414 HOH B O     1 
HETATM 7009 O O     . HOH G 6 .   ? 15.988 -7.586  57.251 1.00 35.81  ?  415 HOH B O     1 
HETATM 7010 O O     . HOH G 6 .   ? 29.102 2.761   43.638 1.00 22.20  ?  416 HOH B O     1 
HETATM 7011 O O     . HOH G 6 .   ? 25.884 2.385   43.013 1.00 31.01  ?  417 HOH B O     1 
HETATM 7012 O O     . HOH G 6 .   ? 8.822  8.230   56.779 1.00 42.73  ?  418 HOH B O     1 
HETATM 7013 O O     . HOH G 6 .   ? 27.180 -3.277  54.898 1.00 34.27  ?  419 HOH B O     1 
HETATM 7014 O O     . HOH G 6 .   ? 14.237 11.159  72.423 1.00 49.55  ?  420 HOH B O     1 
HETATM 7015 O O     . HOH G 6 .   ? 32.484 6.229   48.409 1.00 41.72  ?  421 HOH B O     1 
HETATM 7016 O O     . HOH G 6 .   ? 23.285 -25.402 30.403 1.00 56.36  ?  422 HOH B O     1 
HETATM 7017 O O     . HOH G 6 .   ? 30.265 -13.534 49.633 1.00 57.88  ?  423 HOH B O     1 
HETATM 7018 O O     . HOH G 6 .   ? 45.618 1.931   58.758 1.00 42.00  ?  424 HOH B O     1 
HETATM 7019 O O     . HOH G 6 .   ? 44.113 4.252   52.241 1.00 36.88  ?  425 HOH B O     1 
HETATM 7020 O O     . HOH G 6 .   ? 24.327 -0.870  14.672 1.00 44.20  ?  426 HOH B O     1 
HETATM 7021 O O     . HOH G 6 .   ? 50.708 -10.673 54.536 1.00 31.01  ?  427 HOH B O     1 
HETATM 7022 O O     . HOH G 6 .   ? 36.831 -4.024  55.579 1.00 31.20  ?  428 HOH B O     1 
HETATM 7023 O O     . HOH G 6 .   ? 11.343 -0.370  73.434 1.00 38.47  ?  429 HOH B O     1 
HETATM 7024 O O     . HOH G 6 .   ? 10.713 6.170   82.899 1.00 47.37  ?  430 HOH B O     1 
HETATM 7025 O O     . HOH G 6 .   ? 1.299  -8.681  51.165 1.00 53.21  ?  431 HOH B O     1 
HETATM 7026 O O     . HOH G 6 .   ? 24.896 -8.443  29.943 1.00 34.98  ?  432 HOH B O     1 
HETATM 7027 O O     . HOH G 6 .   ? 40.218 -9.607  73.990 1.00 46.71  ?  433 HOH B O     1 
HETATM 7028 O O     . HOH G 6 .   ? 34.987 19.119  44.030 1.00 36.12  ?  434 HOH B O     1 
HETATM 7029 O O     . HOH G 6 .   ? 37.015 8.340   42.517 1.00 36.96  ?  435 HOH B O     1 
HETATM 7030 O O     . HOH G 6 .   ? 2.534  -16.923 34.745 1.00 38.79  ?  436 HOH B O     1 
HETATM 7031 O O     . HOH G 6 .   ? 37.172 -0.097  8.189  1.00 47.35  ?  437 HOH B O     1 
HETATM 7032 O O     . HOH H 6 .   ? 59.284 34.391  64.849 1.00 47.82  ?  201 HOH C O     1 
HETATM 7033 O O     . HOH H 6 .   ? 59.119 10.133  61.218 1.00 32.98  ?  202 HOH C O     1 
HETATM 7034 O O     . HOH H 6 .   ? 60.102 33.412  66.994 1.00 48.56  ?  203 HOH C O     1 
HETATM 7035 O O     . HOH H 6 .   ? 49.265 4.025   64.473 1.00 31.63  ?  204 HOH C O     1 
HETATM 7036 O O     . HOH H 6 .   ? 44.993 28.714  73.453 1.00 35.65  ?  205 HOH C O     1 
HETATM 7037 O O     . HOH H 6 .   ? 39.591 22.926  56.846 1.00 30.00  ?  206 HOH C O     1 
# 
