data_8K6R
# 
_entry.id   8K6R 
# 
_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   8K6R         pdb_00008k6r 10.2210/pdb8k6r/pdb 
WWPDB D_1300039663 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8K6R 
_pdbx_database_status.recvd_initial_deposition_date   2023-07-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ouyangsy@fjnu.edu.cn 
_pdbx_contact_author.name_first         Songying 
_pdbx_contact_author.name_last          Ouyang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1120-1524 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chen, T.T.'   1 ? 
'Ouyang, S.Y.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Complex structure of Legionella effector LnaB with host Actin and PR-Ub' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, T.T.' 1 ? 
primary 'Ouyang, S.' 2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man LnaB 40622.980 1   ? ? ? ? 
2 polymer     man Ubiquitin 8576.831  1   ? ? ? ? 
3 polymer     nat 'Actin gamma 1' 41838.766 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    134 ? ? ? ? 
# 
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 
;MSYQKIELSISLSLDSPKLDESDFILLSVKYLEKSLGKKKEFSGFFEDIEKLYFKQNYKEAIEKILDFCKKNESLLSEQV
VQRLAEVAPRLKSNPKDNESRRLYETLYADHLESVIKQESDLSVFNELRDSYNAVKPEYAVTHETEIKTLDEAKQFILSF
VMLNDNVELPLKAQSERYPKKDRSREELGNTPSANPGIMKPNSPNFTDNLVPVRDVPKIAINEKVAGGYSKTKPTTPFVA
SLSGTTYSLMVVLTDYIEKHKTDKDIEKKVNQIINLWISSYIKEGYHSYSEVVDVLTEPFLQSIFDKANIKLNYGVLDDT
HAEFRKAQDYVFGLTIQSAMHHELQERFKNKE
;
;MSYQKIELSISLSLDSPKLDESDFILLSVKYLEKSLGKKKEFSGFFEDIEKLYFKQNYKEAIEKILDFCKKNESLLSEQV
VQRLAEVAPRLKSNPKDNESRRLYETLYADHLESVIKQESDLSVFNELRDSYNAVKPEYAVTHETEIKTLDEAKQFILSF
VMLNDNVELPLKAQSERYPKKDRSREELGNTPSANPGIMKPNSPNFTDNLVPVRDVPKIAINEKVAGGYSKTKPTTPFVA
SLSGTTYSLMVVLTDYIEKHKTDKDIEKKVNQIINLWISSYIKEGYHSYSEVVDVLTEPFLQSIFDKANIKLNYGVLDDT
HAEFRKAQDYVFGLTIQSAMHHELQERFKNKE
;
A ? 
2 'polypeptide(L)' no no MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG C ? 
3 'polypeptide(L)' no no 
;MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD
DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT
HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL
APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
;
;MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD
DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT
HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL
APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
;
B ? 
# 
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   SER n 
1 3   TYR n 
1 4   GLN n 
1 5   LYS n 
1 6   ILE n 
1 7   GLU n 
1 8   LEU n 
1 9   SER n 
1 10  ILE n 
1 11  SER n 
1 12  LEU n 
1 13  SER n 
1 14  LEU n 
1 15  ASP n 
1 16  SER n 
1 17  PRO n 
1 18  LYS n 
1 19  LEU n 
1 20  ASP n 
1 21  GLU n 
1 22  SER n 
1 23  ASP n 
1 24  PHE n 
1 25  ILE n 
1 26  LEU n 
1 27  LEU n 
1 28  SER n 
1 29  VAL n 
1 30  LYS n 
1 31  TYR n 
1 32  LEU n 
1 33  GLU n 
1 34  LYS n 
1 35  SER n 
1 36  LEU n 
1 37  GLY n 
1 38  LYS n 
1 39  LYS n 
1 40  LYS n 
1 41  GLU n 
1 42  PHE n 
1 43  SER n 
1 44  GLY n 
1 45  PHE n 
1 46  PHE n 
1 47  GLU n 
1 48  ASP n 
1 49  ILE n 
1 50  GLU n 
1 51  LYS n 
1 52  LEU n 
1 53  TYR n 
1 54  PHE n 
1 55  LYS n 
1 56  GLN n 
1 57  ASN n 
1 58  TYR n 
1 59  LYS n 
1 60  GLU n 
1 61  ALA n 
1 62  ILE n 
1 63  GLU n 
1 64  LYS n 
1 65  ILE n 
1 66  LEU n 
1 67  ASP n 
1 68  PHE n 
1 69  CYS n 
1 70  LYS n 
1 71  LYS n 
1 72  ASN n 
1 73  GLU n 
1 74  SER n 
1 75  LEU n 
1 76  LEU n 
1 77  SER n 
1 78  GLU n 
1 79  GLN n 
1 80  VAL n 
1 81  VAL n 
1 82  GLN n 
1 83  ARG n 
1 84  LEU n 
1 85  ALA n 
1 86  GLU n 
1 87  VAL n 
1 88  ALA n 
1 89  PRO n 
1 90  ARG n 
1 91  LEU n 
1 92  LYS n 
1 93  SER n 
1 94  ASN n 
1 95  PRO n 
1 96  LYS n 
1 97  ASP n 
1 98  ASN n 
1 99  GLU n 
1 100 SER n 
1 101 ARG n 
1 102 ARG n 
1 103 LEU n 
1 104 TYR n 
1 105 GLU n 
1 106 THR n 
1 107 LEU n 
1 108 TYR n 
1 109 ALA n 
1 110 ASP n 
1 111 HIS n 
1 112 LEU n 
1 113 GLU n 
1 114 SER n 
1 115 VAL n 
1 116 ILE n 
1 117 LYS n 
1 118 GLN n 
1 119 GLU n 
1 120 SER n 
1 121 ASP n 
1 122 LEU n 
1 123 SER n 
1 124 VAL n 
1 125 PHE n 
1 126 ASN n 
1 127 GLU n 
1 128 LEU n 
1 129 ARG n 
1 130 ASP n 
1 131 SER n 
1 132 TYR n 
1 133 ASN n 
1 134 ALA n 
1 135 VAL n 
1 136 LYS n 
1 137 PRO n 
1 138 GLU n 
1 139 TYR n 
1 140 ALA n 
1 141 VAL n 
1 142 THR n 
1 143 HIS n 
1 144 GLU n 
1 145 THR n 
1 146 GLU n 
1 147 ILE n 
1 148 LYS n 
1 149 THR n 
1 150 LEU n 
1 151 ASP n 
1 152 GLU n 
1 153 ALA n 
1 154 LYS n 
1 155 GLN n 
1 156 PHE n 
1 157 ILE n 
1 158 LEU n 
1 159 SER n 
1 160 PHE n 
1 161 VAL n 
1 162 MET n 
1 163 LEU n 
1 164 ASN n 
1 165 ASP n 
1 166 ASN n 
1 167 VAL n 
1 168 GLU n 
1 169 LEU n 
1 170 PRO n 
1 171 LEU n 
1 172 LYS n 
1 173 ALA n 
1 174 GLN n 
1 175 SER n 
1 176 GLU n 
1 177 ARG n 
1 178 TYR n 
1 179 PRO n 
1 180 LYS n 
1 181 LYS n 
1 182 ASP n 
1 183 ARG n 
1 184 SER n 
1 185 ARG n 
1 186 GLU n 
1 187 GLU n 
1 188 LEU n 
1 189 GLY n 
1 190 ASN n 
1 191 THR n 
1 192 PRO n 
1 193 SER n 
1 194 ALA n 
1 195 ASN n 
1 196 PRO n 
1 197 GLY n 
1 198 ILE n 
1 199 MET n 
1 200 LYS n 
1 201 PRO n 
1 202 ASN n 
1 203 SER n 
1 204 PRO n 
1 205 ASN n 
1 206 PHE n 
1 207 THR n 
1 208 ASP n 
1 209 ASN n 
1 210 LEU n 
1 211 VAL n 
1 212 PRO n 
1 213 VAL n 
1 214 ARG n 
1 215 ASP n 
1 216 VAL n 
1 217 PRO n 
1 218 LYS n 
1 219 ILE n 
1 220 ALA n 
1 221 ILE n 
1 222 ASN n 
1 223 GLU n 
1 224 LYS n 
1 225 VAL n 
1 226 ALA n 
1 227 GLY n 
1 228 GLY n 
1 229 TYR n 
1 230 SER n 
1 231 LYS n 
1 232 THR n 
1 233 LYS n 
1 234 PRO n 
1 235 THR n 
1 236 THR n 
1 237 PRO n 
1 238 PHE n 
1 239 VAL n 
1 240 ALA n 
1 241 SER n 
1 242 LEU n 
1 243 SER n 
1 244 GLY n 
1 245 THR n 
1 246 THR n 
1 247 TYR n 
1 248 SER n 
1 249 LEU n 
1 250 MET n 
1 251 VAL n 
1 252 VAL n 
1 253 LEU n 
1 254 THR n 
1 255 ASP n 
1 256 TYR n 
1 257 ILE n 
1 258 GLU n 
1 259 LYS n 
1 260 HIS n 
1 261 LYS n 
1 262 THR n 
1 263 ASP n 
1 264 LYS n 
1 265 ASP n 
1 266 ILE n 
1 267 GLU n 
1 268 LYS n 
1 269 LYS n 
1 270 VAL n 
1 271 ASN n 
1 272 GLN n 
1 273 ILE n 
1 274 ILE n 
1 275 ASN n 
1 276 LEU n 
1 277 TRP n 
1 278 ILE n 
1 279 SER n 
1 280 SER n 
1 281 TYR n 
1 282 ILE n 
1 283 LYS n 
1 284 GLU n 
1 285 GLY n 
1 286 TYR n 
1 287 HIS n 
1 288 SER n 
1 289 TYR n 
1 290 SER n 
1 291 GLU n 
1 292 VAL n 
1 293 VAL n 
1 294 ASP n 
1 295 VAL n 
1 296 LEU n 
1 297 THR n 
1 298 GLU n 
1 299 PRO n 
1 300 PHE n 
1 301 LEU n 
1 302 GLN n 
1 303 SER n 
1 304 ILE n 
1 305 PHE n 
1 306 ASP n 
1 307 LYS n 
1 308 ALA n 
1 309 ASN n 
1 310 ILE n 
1 311 LYS n 
1 312 LEU n 
1 313 ASN n 
1 314 TYR n 
1 315 GLY n 
1 316 VAL n 
1 317 LEU n 
1 318 ASP n 
1 319 ASP n 
1 320 THR n 
1 321 HIS n 
1 322 ALA n 
1 323 GLU n 
1 324 PHE n 
1 325 ARG n 
1 326 LYS n 
1 327 ALA n 
1 328 GLN n 
1 329 ASP n 
1 330 TYR n 
1 331 VAL n 
1 332 PHE n 
1 333 GLY n 
1 334 LEU n 
1 335 THR n 
1 336 ILE n 
1 337 GLN n 
1 338 SER n 
1 339 ALA n 
1 340 MET n 
1 341 HIS n 
1 342 HIS n 
1 343 GLU n 
1 344 LEU n 
1 345 GLN n 
1 346 GLU n 
1 347 ARG n 
1 348 PHE n 
1 349 LYS n 
1 350 ASN n 
1 351 LYS n 
1 352 GLU n 
2 1   MET n 
2 2   GLN n 
2 3   ILE n 
2 4   PHE n 
2 5   VAL n 
2 6   LYS n 
2 7   THR n 
2 8   LEU n 
2 9   THR n 
2 10  GLY n 
2 11  LYS n 
2 12  THR n 
2 13  ILE n 
2 14  THR n 
2 15  LEU n 
2 16  GLU n 
2 17  VAL n 
2 18  GLU n 
2 19  PRO n 
2 20  SER n 
2 21  ASP n 
2 22  THR n 
2 23  ILE n 
2 24  GLU n 
2 25  ASN n 
2 26  VAL n 
2 27  LYS n 
2 28  ALA n 
2 29  LYS n 
2 30  ILE n 
2 31  GLN n 
2 32  ASP n 
2 33  LYS n 
2 34  GLU n 
2 35  GLY n 
2 36  ILE n 
2 37  PRO n 
2 38  PRO n 
2 39  ASP n 
2 40  GLN n 
2 41  GLN n 
2 42  ARG n 
2 43  LEU n 
2 44  ILE n 
2 45  PHE n 
2 46  ALA n 
2 47  GLY n 
2 48  LYS n 
2 49  GLN n 
2 50  LEU n 
2 51  GLU n 
2 52  ASP n 
2 53  GLY n 
2 54  ARG n 
2 55  THR n 
2 56  LEU n 
2 57  SER n 
2 58  ASP n 
2 59  TYR n 
2 60  ASN n 
2 61  ILE n 
2 62  GLN n 
2 63  LYS n 
2 64  GLU n 
2 65  SER n 
2 66  THR n 
2 67  LEU n 
2 68  HIS n 
2 69  LEU n 
2 70  VAL n 
2 71  LEU n 
2 72  ARG n 
2 73  LEU n 
2 74  ARG n 
2 75  GLY n 
2 76  GLY n 
3 1   MET n 
3 2   GLU n 
3 3   GLU n 
3 4   GLU n 
3 5   ILE n 
3 6   ALA n 
3 7   ALA n 
3 8   LEU n 
3 9   VAL n 
3 10  ILE n 
3 11  ASP n 
3 12  ASN n 
3 13  GLY n 
3 14  SER n 
3 15  GLY n 
3 16  MET n 
3 17  CYS n 
3 18  LYS n 
3 19  ALA n 
3 20  GLY n 
3 21  PHE n 
3 22  ALA n 
3 23  GLY n 
3 24  ASP n 
3 25  ASP n 
3 26  ALA n 
3 27  PRO n 
3 28  ARG n 
3 29  ALA n 
3 30  VAL n 
3 31  PHE n 
3 32  PRO n 
3 33  SER n 
3 34  ILE n 
3 35  VAL n 
3 36  GLY n 
3 37  ARG n 
3 38  PRO n 
3 39  ARG n 
3 40  HIS n 
3 41  GLN n 
3 42  GLY n 
3 43  VAL n 
3 44  MET n 
3 45  VAL n 
3 46  GLY n 
3 47  MET n 
3 48  GLY n 
3 49  GLN n 
3 50  LYS n 
3 51  ASP n 
3 52  SER n 
3 53  TYR n 
3 54  VAL n 
3 55  GLY n 
3 56  ASP n 
3 57  GLU n 
3 58  ALA n 
3 59  GLN n 
3 60  SER n 
3 61  LYS n 
3 62  ARG n 
3 63  GLY n 
3 64  ILE n 
3 65  LEU n 
3 66  THR n 
3 67  LEU n 
3 68  LYS n 
3 69  TYR n 
3 70  PRO n 
3 71  ILE n 
3 72  GLU n 
3 73  HIS n 
3 74  GLY n 
3 75  ILE n 
3 76  VAL n 
3 77  THR n 
3 78  ASN n 
3 79  TRP n 
3 80  ASP n 
3 81  ASP n 
3 82  MET n 
3 83  GLU n 
3 84  LYS n 
3 85  ILE n 
3 86  TRP n 
3 87  HIS n 
3 88  HIS n 
3 89  THR n 
3 90  PHE n 
3 91  TYR n 
3 92  ASN n 
3 93  GLU n 
3 94  LEU n 
3 95  ARG n 
3 96  VAL n 
3 97  ALA n 
3 98  PRO n 
3 99  GLU n 
3 100 GLU n 
3 101 HIS n 
3 102 PRO n 
3 103 VAL n 
3 104 LEU n 
3 105 LEU n 
3 106 THR n 
3 107 GLU n 
3 108 ALA n 
3 109 PRO n 
3 110 LEU n 
3 111 ASN n 
3 112 PRO n 
3 113 LYS n 
3 114 ALA n 
3 115 ASN n 
3 116 ARG n 
3 117 GLU n 
3 118 LYS n 
3 119 MET n 
3 120 THR n 
3 121 GLN n 
3 122 ILE n 
3 123 MET n 
3 124 PHE n 
3 125 GLU n 
3 126 THR n 
3 127 PHE n 
3 128 ASN n 
3 129 THR n 
3 130 PRO n 
3 131 ALA n 
3 132 MET n 
3 133 TYR n 
3 134 VAL n 
3 135 ALA n 
3 136 ILE n 
3 137 GLN n 
3 138 ALA n 
3 139 VAL n 
3 140 LEU n 
3 141 SER n 
3 142 LEU n 
3 143 TYR n 
3 144 ALA n 
3 145 SER n 
3 146 GLY n 
3 147 ARG n 
3 148 THR n 
3 149 THR n 
3 150 GLY n 
3 151 ILE n 
3 152 VAL n 
3 153 MET n 
3 154 ASP n 
3 155 SER n 
3 156 GLY n 
3 157 ASP n 
3 158 GLY n 
3 159 VAL n 
3 160 THR n 
3 161 HIS n 
3 162 THR n 
3 163 VAL n 
3 164 PRO n 
3 165 ILE n 
3 166 TYR n 
3 167 GLU n 
3 168 GLY n 
3 169 TYR n 
3 170 ALA n 
3 171 LEU n 
3 172 PRO n 
3 173 HIS n 
3 174 ALA n 
3 175 ILE n 
3 176 LEU n 
3 177 ARG n 
3 178 LEU n 
3 179 ASP n 
3 180 LEU n 
3 181 ALA n 
3 182 GLY n 
3 183 ARG n 
3 184 ASP n 
3 185 LEU n 
3 186 THR n 
3 187 ASP n 
3 188 TYR n 
3 189 LEU n 
3 190 MET n 
3 191 LYS n 
3 192 ILE n 
3 193 LEU n 
3 194 THR n 
3 195 GLU n 
3 196 ARG n 
3 197 GLY n 
3 198 TYR n 
3 199 SER n 
3 200 PHE n 
3 201 THR n 
3 202 THR n 
3 203 THR n 
3 204 ALA n 
3 205 GLU n 
3 206 ARG n 
3 207 GLU n 
3 208 ILE n 
3 209 VAL n 
3 210 ARG n 
3 211 ASP n 
3 212 ILE n 
3 213 LYS n 
3 214 GLU n 
3 215 LYS n 
3 216 LEU n 
3 217 CYS n 
3 218 TYR n 
3 219 VAL n 
3 220 ALA n 
3 221 LEU n 
3 222 ASP n 
3 223 PHE n 
3 224 GLU n 
3 225 GLN n 
3 226 GLU n 
3 227 MET n 
3 228 ALA n 
3 229 THR n 
3 230 ALA n 
3 231 ALA n 
3 232 SER n 
3 233 SER n 
3 234 SER n 
3 235 SER n 
3 236 LEU n 
3 237 GLU n 
3 238 LYS n 
3 239 SER n 
3 240 TYR n 
3 241 GLU n 
3 242 LEU n 
3 243 PRO n 
3 244 ASP n 
3 245 GLY n 
3 246 GLN n 
3 247 VAL n 
3 248 ILE n 
3 249 THR n 
3 250 ILE n 
3 251 GLY n 
3 252 ASN n 
3 253 GLU n 
3 254 ARG n 
3 255 PHE n 
3 256 ARG n 
3 257 CYS n 
3 258 PRO n 
3 259 GLU n 
3 260 ALA n 
3 261 LEU n 
3 262 PHE n 
3 263 GLN n 
3 264 PRO n 
3 265 SER n 
3 266 PHE n 
3 267 LEU n 
3 268 GLY n 
3 269 MET n 
3 270 GLU n 
3 271 SER n 
3 272 CYS n 
3 273 GLY n 
3 274 ILE n 
3 275 HIS n 
3 276 GLU n 
3 277 THR n 
3 278 THR n 
3 279 PHE n 
3 280 ASN n 
3 281 SER n 
3 282 ILE n 
3 283 MET n 
3 284 LYS n 
3 285 CYS n 
3 286 ASP n 
3 287 VAL n 
3 288 ASP n 
3 289 ILE n 
3 290 ARG n 
3 291 LYS n 
3 292 ASP n 
3 293 LEU n 
3 294 TYR n 
3 295 ALA n 
3 296 ASN n 
3 297 THR n 
3 298 VAL n 
3 299 LEU n 
3 300 SER n 
3 301 GLY n 
3 302 GLY n 
3 303 THR n 
3 304 THR n 
3 305 MET n 
3 306 TYR n 
3 307 PRO n 
3 308 GLY n 
3 309 ILE n 
3 310 ALA n 
3 311 ASP n 
3 312 ARG n 
3 313 MET n 
3 314 GLN n 
3 315 LYS n 
3 316 GLU n 
3 317 ILE n 
3 318 THR n 
3 319 ALA n 
3 320 LEU n 
3 321 ALA n 
3 322 PRO n 
3 323 SER n 
3 324 THR n 
3 325 MET n 
3 326 LYS n 
3 327 ILE n 
3 328 LYS n 
3 329 ILE n 
3 330 ILE n 
3 331 ALA n 
3 332 PRO n 
3 333 PRO n 
3 334 GLU n 
3 335 ARG n 
3 336 LYS n 
3 337 TYR n 
3 338 SER n 
3 339 VAL n 
3 340 TRP n 
3 341 ILE n 
3 342 GLY n 
3 343 GLY n 
3 344 SER n 
3 345 ILE n 
3 346 LEU n 
3 347 ALA n 
3 348 SER n 
3 349 LEU n 
3 350 SER n 
3 351 THR n 
3 352 PHE n 
3 353 GLN n 
3 354 GLN n 
3 355 MET n 
3 356 TRP n 
3 357 ILE n 
3 358 SER n 
3 359 LYS n 
3 360 GLN n 
3 361 GLU n 
3 362 TYR n 
3 363 ASP n 
3 364 GLU n 
3 365 SER n 
3 366 GLY n 
3 367 PRO n 
3 368 SER n 
3 369 ILE n 
3 370 VAL n 
3 371 HIS n 
3 372 ARG n 
3 373 LYS n 
3 374 CYS n 
3 375 PHE n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 352 ?     ? ?   ? ? ? ? ? ? Legionella     445  ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 76  human ? UBB ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_entity_src_nat.entity_id                  3 
_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   19  ?   ?   ?   A . n 
A 1 2   SER 2   20  ?   ?   ?   A . n 
A 1 3   TYR 3   21  ?   ?   ?   A . n 
A 1 4   GLN 4   22  ?   ?   ?   A . n 
A 1 5   LYS 5   23  ?   ?   ?   A . n 
A 1 6   ILE 6   24  ?   ?   ?   A . n 
A 1 7   GLU 7   25  25  GLU GLU A . n 
A 1 8   LEU 8   26  26  LEU LEU A . n 
A 1 9   SER 9   27  27  SER SER A . n 
A 1 10  ILE 10  28  28  ILE ILE A . n 
A 1 11  SER 11  29  29  SER SER A . n 
A 1 12  LEU 12  30  30  LEU LEU A . n 
A 1 13  SER 13  31  31  SER SER A . n 
A 1 14  LEU 14  32  32  LEU LEU A . n 
A 1 15  ASP 15  33  33  ASP ASP A . n 
A 1 16  SER 16  34  34  SER SER A . n 
A 1 17  PRO 17  35  35  PRO PRO A . n 
A 1 18  LYS 18  36  36  LYS LYS A . n 
A 1 19  LEU 19  37  37  LEU LEU A . n 
A 1 20  ASP 20  38  38  ASP ASP A . n 
A 1 21  GLU 21  39  39  GLU GLU A . n 
A 1 22  SER 22  40  40  SER SER A . n 
A 1 23  ASP 23  41  41  ASP ASP A . n 
A 1 24  PHE 24  42  42  PHE PHE A . n 
A 1 25  ILE 25  43  43  ILE ILE A . n 
A 1 26  LEU 26  44  44  LEU LEU A . n 
A 1 27  LEU 27  45  45  LEU LEU A . n 
A 1 28  SER 28  46  46  SER SER A . n 
A 1 29  VAL 29  47  47  VAL VAL A . n 
A 1 30  LYS 30  48  48  LYS LYS A . n 
A 1 31  TYR 31  49  49  TYR TYR A . n 
A 1 32  LEU 32  50  50  LEU LEU A . n 
A 1 33  GLU 33  51  51  GLU GLU A . n 
A 1 34  LYS 34  52  52  LYS LYS A . n 
A 1 35  SER 35  53  53  SER SER A . n 
A 1 36  LEU 36  54  54  LEU LEU A . n 
A 1 37  GLY 37  55  55  GLY GLY A . n 
A 1 38  LYS 38  56  56  LYS LYS A . n 
A 1 39  LYS 39  57  57  LYS LYS A . n 
A 1 40  LYS 40  58  58  LYS LYS A . n 
A 1 41  GLU 41  59  59  GLU GLU A . n 
A 1 42  PHE 42  60  60  PHE PHE A . n 
A 1 43  SER 43  61  61  SER SER A . n 
A 1 44  GLY 44  62  62  GLY GLY A . n 
A 1 45  PHE 45  63  63  PHE PHE A . n 
A 1 46  PHE 46  64  64  PHE PHE A . n 
A 1 47  GLU 47  65  65  GLU GLU A . n 
A 1 48  ASP 48  66  66  ASP ASP A . n 
A 1 49  ILE 49  67  67  ILE ILE A . n 
A 1 50  GLU 50  68  68  GLU GLU A . n 
A 1 51  LYS 51  69  69  LYS LYS A . n 
A 1 52  LEU 52  70  70  LEU LEU A . n 
A 1 53  TYR 53  71  71  TYR TYR A . n 
A 1 54  PHE 54  72  72  PHE PHE A . n 
A 1 55  LYS 55  73  73  LYS LYS A . n 
A 1 56  GLN 56  74  74  GLN GLN A . n 
A 1 57  ASN 57  75  75  ASN ASN A . n 
A 1 58  TYR 58  76  76  TYR TYR A . n 
A 1 59  LYS 59  77  77  LYS LYS A . n 
A 1 60  GLU 60  78  78  GLU GLU A . n 
A 1 61  ALA 61  79  79  ALA ALA A . n 
A 1 62  ILE 62  80  80  ILE ILE A . n 
A 1 63  GLU 63  81  81  GLU GLU A . n 
A 1 64  LYS 64  82  82  LYS LYS A . n 
A 1 65  ILE 65  83  83  ILE ILE A . n 
A 1 66  LEU 66  84  84  LEU LEU A . n 
A 1 67  ASP 67  85  85  ASP ASP A . n 
A 1 68  PHE 68  86  86  PHE PHE A . n 
A 1 69  CYS 69  87  87  CYS CYS A . n 
A 1 70  LYS 70  88  88  LYS LYS A . n 
A 1 71  LYS 71  89  89  LYS LYS A . n 
A 1 72  ASN 72  90  90  ASN ASN A . n 
A 1 73  GLU 73  91  91  GLU GLU A . n 
A 1 74  SER 74  92  92  SER SER A . n 
A 1 75  LEU 75  93  93  LEU LEU A . n 
A 1 76  LEU 76  94  94  LEU LEU A . n 
A 1 77  SER 77  95  95  SER SER A . n 
A 1 78  GLU 78  96  96  GLU GLU A . n 
A 1 79  GLN 79  97  97  GLN GLN A . n 
A 1 80  VAL 80  98  98  VAL VAL A . n 
A 1 81  VAL 81  99  99  VAL VAL A . n 
A 1 82  GLN 82  100 100 GLN GLN A . n 
A 1 83  ARG 83  101 101 ARG ARG A . n 
A 1 84  LEU 84  102 102 LEU LEU A . n 
A 1 85  ALA 85  103 103 ALA ALA A . n 
A 1 86  GLU 86  104 104 GLU GLU A . n 
A 1 87  VAL 87  105 105 VAL VAL A . n 
A 1 88  ALA 88  106 106 ALA ALA A . n 
A 1 89  PRO 89  107 107 PRO PRO A . n 
A 1 90  ARG 90  108 108 ARG ARG A . n 
A 1 91  LEU 91  109 109 LEU LEU A . n 
A 1 92  LYS 92  110 110 LYS LYS A . n 
A 1 93  SER 93  111 111 SER SER A . n 
A 1 94  ASN 94  112 112 ASN ASN A . n 
A 1 95  PRO 95  113 113 PRO PRO A . n 
A 1 96  LYS 96  114 114 LYS LYS A . n 
A 1 97  ASP 97  115 115 ASP ASP A . n 
A 1 98  ASN 98  116 116 ASN ASN A . n 
A 1 99  GLU 99  117 117 GLU GLU A . n 
A 1 100 SER 100 118 118 SER SER A . n 
A 1 101 ARG 101 119 119 ARG ARG A . n 
A 1 102 ARG 102 120 120 ARG ARG A . n 
A 1 103 LEU 103 121 121 LEU LEU A . n 
A 1 104 TYR 104 122 122 TYR TYR A . n 
A 1 105 GLU 105 123 123 GLU GLU A . n 
A 1 106 THR 106 124 124 THR THR A . n 
A 1 107 LEU 107 125 125 LEU LEU A . n 
A 1 108 TYR 108 126 126 TYR TYR A . n 
A 1 109 ALA 109 127 127 ALA ALA A . n 
A 1 110 ASP 110 128 128 ASP ASP A . n 
A 1 111 HIS 111 129 129 HIS HIS A . n 
A 1 112 LEU 112 130 130 LEU LEU A . n 
A 1 113 GLU 113 131 131 GLU GLU A . n 
A 1 114 SER 114 132 132 SER SER A . n 
A 1 115 VAL 115 133 133 VAL VAL A . n 
A 1 116 ILE 116 134 134 ILE ILE A . n 
A 1 117 LYS 117 135 135 LYS LYS A . n 
A 1 118 GLN 118 136 136 GLN GLN A . n 
A 1 119 GLU 119 137 137 GLU GLU A . n 
A 1 120 SER 120 138 138 SER SER A . n 
A 1 121 ASP 121 139 139 ASP ASP A . n 
A 1 122 LEU 122 140 140 LEU LEU A . n 
A 1 123 SER 123 141 141 SER SER A . n 
A 1 124 VAL 124 142 142 VAL VAL A . n 
A 1 125 PHE 125 143 143 PHE PHE A . n 
A 1 126 ASN 126 144 144 ASN ASN A . n 
A 1 127 GLU 127 145 145 GLU GLU A . n 
A 1 128 LEU 128 146 146 LEU LEU A . n 
A 1 129 ARG 129 147 147 ARG ARG A . n 
A 1 130 ASP 130 148 148 ASP ASP A . n 
A 1 131 SER 131 149 149 SER SER A . n 
A 1 132 TYR 132 150 150 TYR TYR A . n 
A 1 133 ASN 133 151 151 ASN ASN A . n 
A 1 134 ALA 134 152 152 ALA ALA A . n 
A 1 135 VAL 135 153 153 VAL VAL A . n 
A 1 136 LYS 136 154 154 LYS LYS A . n 
A 1 137 PRO 137 155 155 PRO PRO A . n 
A 1 138 GLU 138 156 156 GLU GLU A . n 
A 1 139 TYR 139 157 157 TYR TYR A . n 
A 1 140 ALA 140 158 158 ALA ALA A . n 
A 1 141 VAL 141 159 159 VAL VAL A . n 
A 1 142 THR 142 160 160 THR THR A . n 
A 1 143 HIS 143 161 161 HIS HIS A . n 
A 1 144 GLU 144 162 162 GLU GLU A . n 
A 1 145 THR 145 163 163 THR THR A . n 
A 1 146 GLU 146 164 164 GLU GLU A . n 
A 1 147 ILE 147 165 165 ILE ILE A . n 
A 1 148 LYS 148 166 166 LYS LYS A . n 
A 1 149 THR 149 167 167 THR THR A . n 
A 1 150 LEU 150 168 168 LEU LEU A . n 
A 1 151 ASP 151 169 169 ASP ASP A . n 
A 1 152 GLU 152 170 170 GLU GLU A . n 
A 1 153 ALA 153 171 171 ALA ALA A . n 
A 1 154 LYS 154 172 172 LYS LYS A . n 
A 1 155 GLN 155 173 173 GLN GLN A . n 
A 1 156 PHE 156 174 174 PHE PHE A . n 
A 1 157 ILE 157 175 175 ILE ILE A . n 
A 1 158 LEU 158 176 176 LEU LEU A . n 
A 1 159 SER 159 177 177 SER SER A . n 
A 1 160 PHE 160 178 178 PHE PHE A . n 
A 1 161 VAL 161 179 179 VAL VAL A . n 
A 1 162 MET 162 180 180 MET MET A . n 
A 1 163 LEU 163 181 181 LEU LEU A . n 
A 1 164 ASN 164 182 182 ASN ASN A . n 
A 1 165 ASP 165 183 183 ASP ASP A . n 
A 1 166 ASN 166 184 184 ASN ASN A . n 
A 1 167 VAL 167 185 185 VAL VAL A . n 
A 1 168 GLU 168 186 186 GLU GLU A . n 
A 1 169 LEU 169 187 187 LEU LEU A . n 
A 1 170 PRO 170 188 188 PRO PRO A . n 
A 1 171 LEU 171 189 189 LEU LEU A . n 
A 1 172 LYS 172 190 190 LYS LYS A . n 
A 1 173 ALA 173 191 191 ALA ALA A . n 
A 1 174 GLN 174 192 192 GLN GLN A . n 
A 1 175 SER 175 193 193 SER SER A . n 
A 1 176 GLU 176 194 194 GLU GLU A . n 
A 1 177 ARG 177 195 195 ARG ARG A . n 
A 1 178 TYR 178 196 196 TYR TYR A . n 
A 1 179 PRO 179 197 197 PRO PRO A . n 
A 1 180 LYS 180 198 198 LYS LYS A . n 
A 1 181 LYS 181 199 199 LYS LYS A . n 
A 1 182 ASP 182 200 200 ASP ASP A . n 
A 1 183 ARG 183 201 201 ARG ARG A . n 
A 1 184 SER 184 202 202 SER SER A . n 
A 1 185 ARG 185 203 203 ARG ARG A . n 
A 1 186 GLU 186 204 204 GLU GLU A . n 
A 1 187 GLU 187 205 205 GLU GLU A . n 
A 1 188 LEU 188 206 206 LEU LEU A . n 
A 1 189 GLY 189 207 207 GLY GLY A . n 
A 1 190 ASN 190 208 208 ASN ASN A . n 
A 1 191 THR 191 209 209 THR THR A . n 
A 1 192 PRO 192 210 210 PRO PRO A . n 
A 1 193 SER 193 211 211 SER SER A . n 
A 1 194 ALA 194 212 212 ALA ALA A . n 
A 1 195 ASN 195 213 213 ASN ASN A . n 
A 1 196 PRO 196 214 214 PRO PRO A . n 
A 1 197 GLY 197 215 215 GLY GLY A . n 
A 1 198 ILE 198 216 216 ILE ILE A . n 
A 1 199 MET 199 217 217 MET MET A . n 
A 1 200 LYS 200 218 218 LYS LYS A . n 
A 1 201 PRO 201 219 219 PRO PRO A . n 
A 1 202 ASN 202 220 220 ASN ASN A . n 
A 1 203 SER 203 221 221 SER SER A . n 
A 1 204 PRO 204 222 222 PRO PRO A . n 
A 1 205 ASN 205 223 223 ASN ASN A . n 
A 1 206 PHE 206 224 224 PHE PHE A . n 
A 1 207 THR 207 225 225 THR THR A . n 
A 1 208 ASP 208 226 226 ASP ASP A . n 
A 1 209 ASN 209 227 227 ASN ASN A . n 
A 1 210 LEU 210 228 228 LEU LEU A . n 
A 1 211 VAL 211 229 229 VAL VAL A . n 
A 1 212 PRO 212 230 230 PRO PRO A . n 
A 1 213 VAL 213 231 231 VAL VAL A . n 
A 1 214 ARG 214 232 232 ARG ARG A . n 
A 1 215 ASP 215 233 233 ASP ASP A . n 
A 1 216 VAL 216 234 234 VAL VAL A . n 
A 1 217 PRO 217 235 235 PRO PRO A . n 
A 1 218 LYS 218 236 236 LYS LYS A . n 
A 1 219 ILE 219 237 237 ILE ILE A . n 
A 1 220 ALA 220 238 238 ALA ALA A . n 
A 1 221 ILE 221 239 239 ILE ILE A . n 
A 1 222 ASN 222 240 240 ASN ASN A . n 
A 1 223 GLU 223 241 241 GLU GLU A . n 
A 1 224 LYS 224 242 242 LYS LYS A . n 
A 1 225 VAL 225 243 243 VAL VAL A . n 
A 1 226 ALA 226 244 244 ALA ALA A . n 
A 1 227 GLY 227 245 245 GLY GLY A . n 
A 1 228 GLY 228 246 246 GLY GLY A . n 
A 1 229 TYR 229 247 247 TYR TYR A . n 
A 1 230 SER 230 248 248 SER SER A . n 
A 1 231 LYS 231 249 249 LYS LYS A . n 
A 1 232 THR 232 250 250 THR THR A . n 
A 1 233 LYS 233 251 251 LYS LYS A . n 
A 1 234 PRO 234 252 252 PRO PRO A . n 
A 1 235 THR 235 253 253 THR THR A . n 
A 1 236 THR 236 254 254 THR THR A . n 
A 1 237 PRO 237 255 255 PRO PRO A . n 
A 1 238 PHE 238 256 256 PHE PHE A . n 
A 1 239 VAL 239 257 257 VAL VAL A . n 
A 1 240 ALA 240 258 258 ALA ALA A . n 
A 1 241 SER 241 259 259 SER SER A . n 
A 1 242 LEU 242 260 260 LEU LEU A . n 
A 1 243 SER 243 261 261 SER SER A . n 
A 1 244 GLY 244 262 262 GLY GLY A . n 
A 1 245 THR 245 263 263 THR THR A . n 
A 1 246 THR 246 264 264 THR THR A . n 
A 1 247 TYR 247 265 265 TYR TYR A . n 
A 1 248 SER 248 266 266 SER SER A . n 
A 1 249 LEU 249 267 267 LEU LEU A . n 
A 1 250 MET 250 268 268 MET MET A . n 
A 1 251 VAL 251 269 269 VAL VAL A . n 
A 1 252 VAL 252 270 270 VAL VAL A . n 
A 1 253 LEU 253 271 271 LEU LEU A . n 
A 1 254 THR 254 272 272 THR THR A . n 
A 1 255 ASP 255 273 273 ASP ASP A . n 
A 1 256 TYR 256 274 274 TYR TYR A . n 
A 1 257 ILE 257 275 275 ILE ILE A . n 
A 1 258 GLU 258 276 276 GLU GLU A . n 
A 1 259 LYS 259 277 277 LYS LYS A . n 
A 1 260 HIS 260 278 278 HIS HIS A . n 
A 1 261 LYS 261 279 279 LYS LYS A . n 
A 1 262 THR 262 280 280 THR THR A . n 
A 1 263 ASP 263 281 281 ASP ASP A . n 
A 1 264 LYS 264 282 282 LYS LYS A . n 
A 1 265 ASP 265 283 283 ASP ASP A . n 
A 1 266 ILE 266 284 284 ILE ILE A . n 
A 1 267 GLU 267 285 285 GLU GLU A . n 
A 1 268 LYS 268 286 286 LYS LYS A . n 
A 1 269 LYS 269 287 287 LYS LYS A . n 
A 1 270 VAL 270 288 288 VAL VAL A . n 
A 1 271 ASN 271 289 289 ASN ASN A . n 
A 1 272 GLN 272 290 290 GLN GLN A . n 
A 1 273 ILE 273 291 291 ILE ILE A . n 
A 1 274 ILE 274 292 292 ILE ILE A . n 
A 1 275 ASN 275 293 293 ASN ASN A . n 
A 1 276 LEU 276 294 294 LEU LEU A . n 
A 1 277 TRP 277 295 295 TRP TRP A . n 
A 1 278 ILE 278 296 296 ILE ILE A . n 
A 1 279 SER 279 297 297 SER SER A . n 
A 1 280 SER 280 298 298 SER SER A . n 
A 1 281 TYR 281 299 299 TYR TYR A . n 
A 1 282 ILE 282 300 300 ILE ILE A . n 
A 1 283 LYS 283 301 301 LYS LYS A . n 
A 1 284 GLU 284 302 302 GLU GLU A . n 
A 1 285 GLY 285 303 303 GLY GLY A . n 
A 1 286 TYR 286 304 304 TYR TYR A . n 
A 1 287 HIS 287 305 305 HIS HIS A . n 
A 1 288 SER 288 306 306 SER SER A . n 
A 1 289 TYR 289 307 307 TYR TYR A . n 
A 1 290 SER 290 308 308 SER SER A . n 
A 1 291 GLU 291 309 309 GLU GLU A . n 
A 1 292 VAL 292 310 310 VAL VAL A . n 
A 1 293 VAL 293 311 311 VAL VAL A . n 
A 1 294 ASP 294 312 312 ASP ASP A . n 
A 1 295 VAL 295 313 313 VAL VAL A . n 
A 1 296 LEU 296 314 314 LEU LEU A . n 
A 1 297 THR 297 315 315 THR THR A . n 
A 1 298 GLU 298 316 316 GLU GLU A . n 
A 1 299 PRO 299 317 317 PRO PRO A . n 
A 1 300 PHE 300 318 318 PHE PHE A . n 
A 1 301 LEU 301 319 319 LEU LEU A . n 
A 1 302 GLN 302 320 320 GLN GLN A . n 
A 1 303 SER 303 321 321 SER SER A . n 
A 1 304 ILE 304 322 322 ILE ILE A . n 
A 1 305 PHE 305 323 323 PHE PHE A . n 
A 1 306 ASP 306 324 324 ASP ASP A . n 
A 1 307 LYS 307 325 325 LYS LYS A . n 
A 1 308 ALA 308 326 326 ALA ALA A . n 
A 1 309 ASN 309 327 327 ASN ASN A . n 
A 1 310 ILE 310 328 328 ILE ILE A . n 
A 1 311 LYS 311 329 329 LYS LYS A . n 
A 1 312 LEU 312 330 330 LEU LEU A . n 
A 1 313 ASN 313 331 331 ASN ASN A . n 
A 1 314 TYR 314 332 332 TYR TYR A . n 
A 1 315 GLY 315 333 333 GLY GLY A . n 
A 1 316 VAL 316 334 334 VAL VAL A . n 
A 1 317 LEU 317 335 335 LEU LEU A . n 
A 1 318 ASP 318 336 336 ASP ASP A . n 
A 1 319 ASP 319 337 337 ASP ASP A . n 
A 1 320 THR 320 338 338 THR THR A . n 
A 1 321 HIS 321 339 339 HIS HIS A . n 
A 1 322 ALA 322 340 340 ALA ALA A . n 
A 1 323 GLU 323 341 341 GLU GLU A . n 
A 1 324 PHE 324 342 342 PHE PHE A . n 
A 1 325 ARG 325 343 343 ARG ARG A . n 
A 1 326 LYS 326 344 344 LYS LYS A . n 
A 1 327 ALA 327 345 345 ALA ALA A . n 
A 1 328 GLN 328 346 346 GLN GLN A . n 
A 1 329 ASP 329 347 347 ASP ASP A . n 
A 1 330 TYR 330 348 348 TYR TYR A . n 
A 1 331 VAL 331 349 349 VAL VAL A . n 
A 1 332 PHE 332 350 350 PHE PHE A . n 
A 1 333 GLY 333 351 351 GLY GLY A . n 
A 1 334 LEU 334 352 352 LEU LEU A . n 
A 1 335 THR 335 353 353 THR THR A . n 
A 1 336 ILE 336 354 354 ILE ILE A . n 
A 1 337 GLN 337 355 355 GLN GLN A . n 
A 1 338 SER 338 356 356 SER SER A . n 
A 1 339 ALA 339 357 357 ALA ALA A . n 
A 1 340 MET 340 358 358 MET MET A . n 
A 1 341 HIS 341 359 359 HIS HIS A . n 
A 1 342 HIS 342 360 360 HIS HIS A . n 
A 1 343 GLU 343 361 361 GLU GLU A . n 
A 1 344 LEU 344 362 362 LEU LEU A . n 
A 1 345 GLN 345 363 363 GLN GLN A . n 
A 1 346 GLU 346 364 364 GLU GLU A . n 
A 1 347 ARG 347 365 365 ARG ARG A . n 
A 1 348 PHE 348 366 366 PHE PHE A . n 
A 1 349 LYS 349 367 367 LYS LYS A . n 
A 1 350 ASN 350 368 368 ASN ASN A . n 
A 1 351 LYS 351 369 369 LYS LYS A . n 
A 1 352 GLU 352 370 370 GLU GLU A . n 
B 2 1   MET 1   1   1   MET MET C . n 
B 2 2   GLN 2   2   2   GLN GLN C . n 
B 2 3   ILE 3   3   3   ILE ILE C . n 
B 2 4   PHE 4   4   4   PHE PHE C . n 
B 2 5   VAL 5   5   5   VAL VAL C . n 
B 2 6   LYS 6   6   6   LYS LYS C . n 
B 2 7   THR 7   7   7   THR THR C . n 
B 2 8   LEU 8   8   8   LEU LEU C . n 
B 2 9   THR 9   9   9   THR THR C . n 
B 2 10  GLY 10  10  10  GLY GLY C . n 
B 2 11  LYS 11  11  11  LYS LYS C . n 
B 2 12  THR 12  12  12  THR THR C . n 
B 2 13  ILE 13  13  13  ILE ILE C . n 
B 2 14  THR 14  14  14  THR THR C . n 
B 2 15  LEU 15  15  15  LEU LEU C . n 
B 2 16  GLU 16  16  16  GLU GLU C . n 
B 2 17  VAL 17  17  17  VAL VAL C . n 
B 2 18  GLU 18  18  18  GLU GLU C . n 
B 2 19  PRO 19  19  19  PRO PRO C . n 
B 2 20  SER 20  20  20  SER SER C . n 
B 2 21  ASP 21  21  21  ASP ASP C . n 
B 2 22  THR 22  22  22  THR THR C . n 
B 2 23  ILE 23  23  23  ILE ILE C . n 
B 2 24  GLU 24  24  24  GLU GLU C . n 
B 2 25  ASN 25  25  25  ASN ASN C . n 
B 2 26  VAL 26  26  26  VAL VAL C . n 
B 2 27  LYS 27  27  27  LYS LYS C . n 
B 2 28  ALA 28  28  28  ALA ALA C . n 
B 2 29  LYS 29  29  29  LYS LYS C . n 
B 2 30  ILE 30  30  30  ILE ILE C . n 
B 2 31  GLN 31  31  31  GLN GLN C . n 
B 2 32  ASP 32  32  32  ASP ASP C . n 
B 2 33  LYS 33  33  33  LYS LYS C . n 
B 2 34  GLU 34  34  34  GLU GLU C . n 
B 2 35  GLY 35  35  35  GLY GLY C . n 
B 2 36  ILE 36  36  36  ILE ILE C . n 
B 2 37  PRO 37  37  37  PRO PRO C . n 
B 2 38  PRO 38  38  38  PRO PRO C . n 
B 2 39  ASP 39  39  39  ASP ASP C . n 
B 2 40  GLN 40  40  40  GLN GLN C . n 
B 2 41  GLN 41  41  41  GLN GLN C . n 
B 2 42  ARG 42  42  42  ARG ARG C . n 
B 2 43  LEU 43  43  43  LEU LEU C . n 
B 2 44  ILE 44  44  44  ILE ILE C . n 
B 2 45  PHE 45  45  45  PHE PHE C . n 
B 2 46  ALA 46  46  46  ALA ALA C . n 
B 2 47  GLY 47  47  47  GLY GLY C . n 
B 2 48  LYS 48  48  48  LYS LYS C . n 
B 2 49  GLN 49  49  49  GLN GLN C . n 
B 2 50  LEU 50  50  50  LEU LEU C . n 
B 2 51  GLU 51  51  51  GLU GLU C . n 
B 2 52  ASP 52  52  52  ASP ASP C . n 
B 2 53  GLY 53  53  53  GLY GLY C . n 
B 2 54  ARG 54  54  54  ARG ARG C . n 
B 2 55  THR 55  55  55  THR THR C . n 
B 2 56  LEU 56  56  56  LEU LEU C . n 
B 2 57  SER 57  57  57  SER SER C . n 
B 2 58  ASP 58  58  58  ASP ASP C . n 
B 2 59  TYR 59  59  59  TYR TYR C . n 
B 2 60  ASN 60  60  60  ASN ASN C . n 
B 2 61  ILE 61  61  61  ILE ILE C . n 
B 2 62  GLN 62  62  62  GLN GLN C . n 
B 2 63  LYS 63  63  63  LYS LYS C . n 
B 2 64  GLU 64  64  64  GLU GLU C . n 
B 2 65  SER 65  65  65  SER SER C . n 
B 2 66  THR 66  66  66  THR THR C . n 
B 2 67  LEU 67  67  67  LEU LEU C . n 
B 2 68  HIS 68  68  68  HIS HIS C . n 
B 2 69  LEU 69  69  69  LEU LEU C . n 
B 2 70  VAL 70  70  70  VAL VAL C . n 
B 2 71  LEU 71  71  71  LEU LEU C . n 
B 2 72  ARG 72  72  72  ARG ARG C . n 
B 2 73  LEU 73  73  73  LEU LEU C . n 
B 2 74  ARG 74  74  74  ARG ARG C . n 
B 2 75  GLY 75  75  75  GLY GLY C . n 
B 2 76  GLY 76  76  ?   ?   ?   C . n 
C 3 1   MET 1   1   ?   ?   ?   B . n 
C 3 2   GLU 2   2   ?   ?   ?   B . n 
C 3 3   GLU 3   3   ?   ?   ?   B . n 
C 3 4   GLU 4   4   ?   ?   ?   B . n 
C 3 5   ILE 5   5   5   ILE ILE B . n 
C 3 6   ALA 6   6   6   ALA ALA B . n 
C 3 7   ALA 7   7   7   ALA ALA B . n 
C 3 8   LEU 8   8   8   LEU LEU B . n 
C 3 9   VAL 9   9   9   VAL VAL B . n 
C 3 10  ILE 10  10  10  ILE ILE B . n 
C 3 11  ASP 11  11  11  ASP ASP B . n 
C 3 12  ASN 12  12  12  ASN ASN B . n 
C 3 13  GLY 13  13  13  GLY GLY B . n 
C 3 14  SER 14  14  14  SER SER B . n 
C 3 15  GLY 15  15  15  GLY GLY B . n 
C 3 16  MET 16  16  16  MET MET B . n 
C 3 17  CYS 17  17  17  CYS CYS B . n 
C 3 18  LYS 18  18  18  LYS LYS B . n 
C 3 19  ALA 19  19  19  ALA ALA B . n 
C 3 20  GLY 20  20  20  GLY GLY B . n 
C 3 21  PHE 21  21  21  PHE PHE B . n 
C 3 22  ALA 22  22  22  ALA ALA B . n 
C 3 23  GLY 23  23  23  GLY GLY B . n 
C 3 24  ASP 24  24  24  ASP ASP B . n 
C 3 25  ASP 25  25  25  ASP ASP B . n 
C 3 26  ALA 26  26  26  ALA ALA B . n 
C 3 27  PRO 27  27  27  PRO PRO B . n 
C 3 28  ARG 28  28  28  ARG ARG B . n 
C 3 29  ALA 29  29  29  ALA ALA B . n 
C 3 30  VAL 30  30  30  VAL VAL B . n 
C 3 31  PHE 31  31  31  PHE PHE B . n 
C 3 32  PRO 32  32  32  PRO PRO B . n 
C 3 33  SER 33  33  33  SER SER B . n 
C 3 34  ILE 34  34  34  ILE ILE B . n 
C 3 35  VAL 35  35  35  VAL VAL B . n 
C 3 36  GLY 36  36  36  GLY GLY B . n 
C 3 37  ARG 37  37  37  ARG ARG B . n 
C 3 38  PRO 38  38  38  PRO PRO B . n 
C 3 39  ARG 39  39  39  ARG ARG B . n 
C 3 40  HIS 40  40  40  HIS HIS B . n 
C 3 41  GLN 41  41  41  GLN GLN B . n 
C 3 42  GLY 42  42  42  GLY GLY B . n 
C 3 43  VAL 43  43  43  VAL VAL B . n 
C 3 44  MET 44  44  44  MET MET B . n 
C 3 45  VAL 45  45  45  VAL VAL B . n 
C 3 46  GLY 46  46  46  GLY GLY B . n 
C 3 47  MET 47  47  47  MET MET B . n 
C 3 48  GLY 48  48  48  GLY GLY B . n 
C 3 49  GLN 49  49  49  GLN GLN B . n 
C 3 50  LYS 50  50  50  LYS LYS B . n 
C 3 51  ASP 51  51  51  ASP ASP B . n 
C 3 52  SER 52  52  52  SER SER B . n 
C 3 53  TYR 53  53  53  TYR TYR B . n 
C 3 54  VAL 54  54  54  VAL VAL B . n 
C 3 55  GLY 55  55  55  GLY GLY B . n 
C 3 56  ASP 56  56  56  ASP ASP B . n 
C 3 57  GLU 57  57  57  GLU GLU B . n 
C 3 58  ALA 58  58  58  ALA ALA B . n 
C 3 59  GLN 59  59  59  GLN GLN B . n 
C 3 60  SER 60  60  60  SER SER B . n 
C 3 61  LYS 61  61  61  LYS LYS B . n 
C 3 62  ARG 62  62  62  ARG ARG B . n 
C 3 63  GLY 63  63  63  GLY GLY B . n 
C 3 64  ILE 64  64  64  ILE ILE B . n 
C 3 65  LEU 65  65  65  LEU LEU B . n 
C 3 66  THR 66  66  66  THR THR B . n 
C 3 67  LEU 67  67  67  LEU LEU B . n 
C 3 68  LYS 68  68  68  LYS LYS B . n 
C 3 69  TYR 69  69  69  TYR TYR B . n 
C 3 70  PRO 70  70  70  PRO PRO B . n 
C 3 71  ILE 71  71  71  ILE ILE B . n 
C 3 72  GLU 72  72  72  GLU GLU B . n 
C 3 73  HIS 73  73  73  HIS HIS B . n 
C 3 74  GLY 74  74  74  GLY GLY B . n 
C 3 75  ILE 75  75  75  ILE ILE B . n 
C 3 76  VAL 76  76  76  VAL VAL B . n 
C 3 77  THR 77  77  77  THR THR B . n 
C 3 78  ASN 78  78  78  ASN ASN B . n 
C 3 79  TRP 79  79  79  TRP TRP B . n 
C 3 80  ASP 80  80  80  ASP ASP B . n 
C 3 81  ASP 81  81  81  ASP ASP B . n 
C 3 82  MET 82  82  82  MET MET B . n 
C 3 83  GLU 83  83  83  GLU GLU B . n 
C 3 84  LYS 84  84  84  LYS LYS B . n 
C 3 85  ILE 85  85  85  ILE ILE B . n 
C 3 86  TRP 86  86  86  TRP TRP B . n 
C 3 87  HIS 87  87  87  HIS HIS B . n 
C 3 88  HIS 88  88  88  HIS HIS B . n 
C 3 89  THR 89  89  89  THR THR B . n 
C 3 90  PHE 90  90  90  PHE PHE B . n 
C 3 91  TYR 91  91  91  TYR TYR B . n 
C 3 92  ASN 92  92  92  ASN ASN B . n 
C 3 93  GLU 93  93  93  GLU GLU B . n 
C 3 94  LEU 94  94  94  LEU LEU B . n 
C 3 95  ARG 95  95  95  ARG ARG B . n 
C 3 96  VAL 96  96  96  VAL VAL B . n 
C 3 97  ALA 97  97  97  ALA ALA B . n 
C 3 98  PRO 98  98  98  PRO PRO B . n 
C 3 99  GLU 99  99  99  GLU GLU B . n 
C 3 100 GLU 100 100 100 GLU GLU B . n 
C 3 101 HIS 101 101 101 HIS HIS B . n 
C 3 102 PRO 102 102 102 PRO PRO B . n 
C 3 103 VAL 103 103 103 VAL VAL B . n 
C 3 104 LEU 104 104 104 LEU LEU B . n 
C 3 105 LEU 105 105 105 LEU LEU B . n 
C 3 106 THR 106 106 106 THR THR B . n 
C 3 107 GLU 107 107 107 GLU GLU B . n 
C 3 108 ALA 108 108 108 ALA ALA B . n 
C 3 109 PRO 109 109 109 PRO PRO B . n 
C 3 110 LEU 110 110 110 LEU LEU B . n 
C 3 111 ASN 111 111 111 ASN ASN B . n 
C 3 112 PRO 112 112 112 PRO PRO B . n 
C 3 113 LYS 113 113 113 LYS LYS B . n 
C 3 114 ALA 114 114 114 ALA ALA B . n 
C 3 115 ASN 115 115 115 ASN ASN B . n 
C 3 116 ARG 116 116 116 ARG ARG B . n 
C 3 117 GLU 117 117 117 GLU GLU B . n 
C 3 118 LYS 118 118 118 LYS LYS B . n 
C 3 119 MET 119 119 119 MET MET B . n 
C 3 120 THR 120 120 120 THR THR B . n 
C 3 121 GLN 121 121 121 GLN GLN B . n 
C 3 122 ILE 122 122 122 ILE ILE B . n 
C 3 123 MET 123 123 123 MET MET B . n 
C 3 124 PHE 124 124 124 PHE PHE B . n 
C 3 125 GLU 125 125 125 GLU GLU B . n 
C 3 126 THR 126 126 126 THR THR B . n 
C 3 127 PHE 127 127 127 PHE PHE B . n 
C 3 128 ASN 128 128 128 ASN ASN B . n 
C 3 129 THR 129 129 129 THR THR B . n 
C 3 130 PRO 130 130 130 PRO PRO B . n 
C 3 131 ALA 131 131 131 ALA ALA B . n 
C 3 132 MET 132 132 132 MET MET B . n 
C 3 133 TYR 133 133 133 TYR TYR B . n 
C 3 134 VAL 134 134 134 VAL VAL B . n 
C 3 135 ALA 135 135 135 ALA ALA B . n 
C 3 136 ILE 136 136 136 ILE ILE B . n 
C 3 137 GLN 137 137 137 GLN GLN B . n 
C 3 138 ALA 138 138 138 ALA ALA B . n 
C 3 139 VAL 139 139 139 VAL VAL B . n 
C 3 140 LEU 140 140 140 LEU LEU B . n 
C 3 141 SER 141 141 141 SER SER B . n 
C 3 142 LEU 142 142 142 LEU LEU B . n 
C 3 143 TYR 143 143 143 TYR TYR B . n 
C 3 144 ALA 144 144 144 ALA ALA B . n 
C 3 145 SER 145 145 145 SER SER B . n 
C 3 146 GLY 146 146 146 GLY GLY B . n 
C 3 147 ARG 147 147 147 ARG ARG B . n 
C 3 148 THR 148 148 148 THR THR B . n 
C 3 149 THR 149 149 149 THR THR B . n 
C 3 150 GLY 150 150 150 GLY GLY B . n 
C 3 151 ILE 151 151 151 ILE ILE B . n 
C 3 152 VAL 152 152 152 VAL VAL B . n 
C 3 153 MET 153 153 153 MET MET B . n 
C 3 154 ASP 154 154 154 ASP ASP B . n 
C 3 155 SER 155 155 155 SER SER B . n 
C 3 156 GLY 156 156 156 GLY GLY B . n 
C 3 157 ASP 157 157 157 ASP ASP B . n 
C 3 158 GLY 158 158 158 GLY GLY B . n 
C 3 159 VAL 159 159 159 VAL VAL B . n 
C 3 160 THR 160 160 160 THR THR B . n 
C 3 161 HIS 161 161 161 HIS HIS B . n 
C 3 162 THR 162 162 162 THR THR B . n 
C 3 163 VAL 163 163 163 VAL VAL B . n 
C 3 164 PRO 164 164 164 PRO PRO B . n 
C 3 165 ILE 165 165 165 ILE ILE B . n 
C 3 166 TYR 166 166 166 TYR TYR B . n 
C 3 167 GLU 167 167 167 GLU GLU B . n 
C 3 168 GLY 168 168 168 GLY GLY B . n 
C 3 169 TYR 169 169 169 TYR TYR B . n 
C 3 170 ALA 170 170 170 ALA ALA B . n 
C 3 171 LEU 171 171 171 LEU LEU B . n 
C 3 172 PRO 172 172 172 PRO PRO B . n 
C 3 173 HIS 173 173 173 HIS HIS B . n 
C 3 174 ALA 174 174 174 ALA ALA B . n 
C 3 175 ILE 175 175 175 ILE ILE B . n 
C 3 176 LEU 176 176 176 LEU LEU B . n 
C 3 177 ARG 177 177 177 ARG ARG B . n 
C 3 178 LEU 178 178 178 LEU LEU B . n 
C 3 179 ASP 179 179 179 ASP ASP B . n 
C 3 180 LEU 180 180 180 LEU LEU B . n 
C 3 181 ALA 181 181 181 ALA ALA B . n 
C 3 182 GLY 182 182 182 GLY GLY B . n 
C 3 183 ARG 183 183 183 ARG ARG B . n 
C 3 184 ASP 184 184 184 ASP ASP B . n 
C 3 185 LEU 185 185 185 LEU LEU B . n 
C 3 186 THR 186 186 186 THR THR B . n 
C 3 187 ASP 187 187 187 ASP ASP B . n 
C 3 188 TYR 188 188 188 TYR TYR B . n 
C 3 189 LEU 189 189 189 LEU LEU B . n 
C 3 190 MET 190 190 190 MET MET B . n 
C 3 191 LYS 191 191 191 LYS LYS B . n 
C 3 192 ILE 192 192 192 ILE ILE B . n 
C 3 193 LEU 193 193 193 LEU LEU B . n 
C 3 194 THR 194 194 194 THR THR B . n 
C 3 195 GLU 195 195 195 GLU GLU B . n 
C 3 196 ARG 196 196 196 ARG ARG B . n 
C 3 197 GLY 197 197 197 GLY GLY B . n 
C 3 198 TYR 198 198 198 TYR TYR B . n 
C 3 199 SER 199 199 199 SER SER B . n 
C 3 200 PHE 200 200 200 PHE PHE B . n 
C 3 201 THR 201 201 201 THR THR B . n 
C 3 202 THR 202 202 202 THR THR B . n 
C 3 203 THR 203 203 203 THR THR B . n 
C 3 204 ALA 204 204 204 ALA ALA B . n 
C 3 205 GLU 205 205 205 GLU GLU B . n 
C 3 206 ARG 206 206 206 ARG ARG B . n 
C 3 207 GLU 207 207 207 GLU GLU B . n 
C 3 208 ILE 208 208 208 ILE ILE B . n 
C 3 209 VAL 209 209 209 VAL VAL B . n 
C 3 210 ARG 210 210 210 ARG ARG B . n 
C 3 211 ASP 211 211 211 ASP ASP B . n 
C 3 212 ILE 212 212 212 ILE ILE B . n 
C 3 213 LYS 213 213 213 LYS LYS B . n 
C 3 214 GLU 214 214 214 GLU GLU B . n 
C 3 215 LYS 215 215 215 LYS LYS B . n 
C 3 216 LEU 216 216 216 LEU LEU B . n 
C 3 217 CYS 217 217 217 CYS CYS B . n 
C 3 218 TYR 218 218 218 TYR TYR B . n 
C 3 219 VAL 219 219 219 VAL VAL B . n 
C 3 220 ALA 220 220 220 ALA ALA B . n 
C 3 221 LEU 221 221 221 LEU LEU B . n 
C 3 222 ASP 222 222 222 ASP ASP B . n 
C 3 223 PHE 223 223 223 PHE PHE B . n 
C 3 224 GLU 224 224 224 GLU GLU B . n 
C 3 225 GLN 225 225 225 GLN GLN B . n 
C 3 226 GLU 226 226 226 GLU GLU B . n 
C 3 227 MET 227 227 227 MET MET B . n 
C 3 228 ALA 228 228 228 ALA ALA B . n 
C 3 229 THR 229 229 229 THR THR B . n 
C 3 230 ALA 230 230 230 ALA ALA B . n 
C 3 231 ALA 231 231 231 ALA ALA B . n 
C 3 232 SER 232 232 232 SER SER B . n 
C 3 233 SER 233 233 233 SER SER B . n 
C 3 234 SER 234 234 234 SER SER B . n 
C 3 235 SER 235 235 235 SER SER B . n 
C 3 236 LEU 236 236 236 LEU LEU B . n 
C 3 237 GLU 237 237 237 GLU GLU B . n 
C 3 238 LYS 238 238 238 LYS LYS B . n 
C 3 239 SER 239 239 239 SER SER B . n 
C 3 240 TYR 240 240 240 TYR TYR B . n 
C 3 241 GLU 241 241 241 GLU GLU B . n 
C 3 242 LEU 242 242 242 LEU LEU B . n 
C 3 243 PRO 243 243 243 PRO PRO B . n 
C 3 244 ASP 244 244 244 ASP ASP B . n 
C 3 245 GLY 245 245 245 GLY GLY B . n 
C 3 246 GLN 246 246 246 GLN GLN B . n 
C 3 247 VAL 247 247 247 VAL VAL B . n 
C 3 248 ILE 248 248 248 ILE ILE B . n 
C 3 249 THR 249 249 249 THR THR B . n 
C 3 250 ILE 250 250 250 ILE ILE B . n 
C 3 251 GLY 251 251 251 GLY GLY B . n 
C 3 252 ASN 252 252 252 ASN ASN B . n 
C 3 253 GLU 253 253 253 GLU GLU B . n 
C 3 254 ARG 254 254 254 ARG ARG B . n 
C 3 255 PHE 255 255 255 PHE PHE B . n 
C 3 256 ARG 256 256 256 ARG ARG B . n 
C 3 257 CYS 257 257 257 CYS CYS B . n 
C 3 258 PRO 258 258 258 PRO PRO B . n 
C 3 259 GLU 259 259 259 GLU GLU B . n 
C 3 260 ALA 260 260 260 ALA ALA B . n 
C 3 261 LEU 261 261 261 LEU LEU B . n 
C 3 262 PHE 262 262 262 PHE PHE B . n 
C 3 263 GLN 263 263 263 GLN GLN B . n 
C 3 264 PRO 264 264 264 PRO PRO B . n 
C 3 265 SER 265 265 265 SER SER B . n 
C 3 266 PHE 266 266 266 PHE PHE B . n 
C 3 267 LEU 267 267 267 LEU LEU B . n 
C 3 268 GLY 268 268 268 GLY GLY B . n 
C 3 269 MET 269 269 269 MET MET B . n 
C 3 270 GLU 270 270 270 GLU GLU B . n 
C 3 271 SER 271 271 271 SER SER B . n 
C 3 272 CYS 272 272 272 CYS CYS B . n 
C 3 273 GLY 273 273 273 GLY GLY B . n 
C 3 274 ILE 274 274 274 ILE ILE B . n 
C 3 275 HIS 275 275 275 HIS HIS B . n 
C 3 276 GLU 276 276 276 GLU GLU B . n 
C 3 277 THR 277 277 277 THR THR B . n 
C 3 278 THR 278 278 278 THR THR B . n 
C 3 279 PHE 279 279 279 PHE PHE B . n 
C 3 280 ASN 280 280 280 ASN ASN B . n 
C 3 281 SER 281 281 281 SER SER B . n 
C 3 282 ILE 282 282 282 ILE ILE B . n 
C 3 283 MET 283 283 283 MET MET B . n 
C 3 284 LYS 284 284 284 LYS LYS B . n 
C 3 285 CYS 285 285 285 CYS CYS B . n 
C 3 286 ASP 286 286 286 ASP ASP B . n 
C 3 287 VAL 287 287 287 VAL VAL B . n 
C 3 288 ASP 288 288 288 ASP ASP B . n 
C 3 289 ILE 289 289 289 ILE ILE B . n 
C 3 290 ARG 290 290 290 ARG ARG B . n 
C 3 291 LYS 291 291 291 LYS LYS B . n 
C 3 292 ASP 292 292 292 ASP ASP B . n 
C 3 293 LEU 293 293 293 LEU LEU B . n 
C 3 294 TYR 294 294 294 TYR TYR B . n 
C 3 295 ALA 295 295 295 ALA ALA B . n 
C 3 296 ASN 296 296 296 ASN ASN B . n 
C 3 297 THR 297 297 297 THR THR B . n 
C 3 298 VAL 298 298 298 VAL VAL B . n 
C 3 299 LEU 299 299 299 LEU LEU B . n 
C 3 300 SER 300 300 300 SER SER B . n 
C 3 301 GLY 301 301 301 GLY GLY B . n 
C 3 302 GLY 302 302 302 GLY GLY B . n 
C 3 303 THR 303 303 303 THR THR B . n 
C 3 304 THR 304 304 304 THR THR B . n 
C 3 305 MET 305 305 305 MET MET B . n 
C 3 306 TYR 306 306 306 TYR TYR B . n 
C 3 307 PRO 307 307 307 PRO PRO B . n 
C 3 308 GLY 308 308 308 GLY GLY B . n 
C 3 309 ILE 309 309 309 ILE ILE B . n 
C 3 310 ALA 310 310 310 ALA ALA B . n 
C 3 311 ASP 311 311 311 ASP ASP B . n 
C 3 312 ARG 312 312 312 ARG ARG B . n 
C 3 313 MET 313 313 313 MET MET B . n 
C 3 314 GLN 314 314 314 GLN GLN B . n 
C 3 315 LYS 315 315 315 LYS LYS B . n 
C 3 316 GLU 316 316 316 GLU GLU B . n 
C 3 317 ILE 317 317 317 ILE ILE B . n 
C 3 318 THR 318 318 318 THR THR B . n 
C 3 319 ALA 319 319 319 ALA ALA B . n 
C 3 320 LEU 320 320 320 LEU LEU B . n 
C 3 321 ALA 321 321 321 ALA ALA B . n 
C 3 322 PRO 322 322 322 PRO PRO B . n 
C 3 323 SER 323 323 323 SER SER B . n 
C 3 324 THR 324 324 324 THR THR B . n 
C 3 325 MET 325 325 325 MET MET B . n 
C 3 326 LYS 326 326 326 LYS LYS B . n 
C 3 327 ILE 327 327 327 ILE ILE B . n 
C 3 328 LYS 328 328 328 LYS LYS B . n 
C 3 329 ILE 329 329 329 ILE ILE B . n 
C 3 330 ILE 330 330 330 ILE ILE B . n 
C 3 331 ALA 331 331 331 ALA ALA B . n 
C 3 332 PRO 332 332 332 PRO PRO B . n 
C 3 333 PRO 333 333 333 PRO PRO B . n 
C 3 334 GLU 334 334 334 GLU GLU B . n 
C 3 335 ARG 335 335 335 ARG ARG B . n 
C 3 336 LYS 336 336 336 LYS LYS B . n 
C 3 337 TYR 337 337 337 TYR TYR B . n 
C 3 338 SER 338 338 338 SER SER B . n 
C 3 339 VAL 339 339 339 VAL VAL B . n 
C 3 340 TRP 340 340 340 TRP TRP B . n 
C 3 341 ILE 341 341 341 ILE ILE B . n 
C 3 342 GLY 342 342 342 GLY GLY B . n 
C 3 343 GLY 343 343 343 GLY GLY B . n 
C 3 344 SER 344 344 344 SER SER B . n 
C 3 345 ILE 345 345 345 ILE ILE B . n 
C 3 346 LEU 346 346 346 LEU LEU B . n 
C 3 347 ALA 347 347 347 ALA ALA B . n 
C 3 348 SER 348 348 348 SER SER B . n 
C 3 349 LEU 349 349 349 LEU LEU B . n 
C 3 350 SER 350 350 350 SER SER B . n 
C 3 351 THR 351 351 351 THR THR B . n 
C 3 352 PHE 352 352 352 PHE PHE B . n 
C 3 353 GLN 353 353 353 GLN GLN B . n 
C 3 354 GLN 354 354 354 GLN GLN B . n 
C 3 355 MET 355 355 355 MET MET B . n 
C 3 356 TRP 356 356 356 TRP TRP B . n 
C 3 357 ILE 357 357 357 ILE ILE B . n 
C 3 358 SER 358 358 358 SER SER B . n 
C 3 359 LYS 359 359 359 LYS LYS B . n 
C 3 360 GLN 360 360 360 GLN GLN B . n 
C 3 361 GLU 361 361 361 GLU GLU B . n 
C 3 362 TYR 362 362 362 TYR TYR B . n 
C 3 363 ASP 363 363 363 ASP ASP B . n 
C 3 364 GLU 364 364 364 GLU GLU B . n 
C 3 365 SER 365 365 365 SER SER B . n 
C 3 366 GLY 366 366 366 GLY GLY B . n 
C 3 367 PRO 367 367 367 PRO PRO B . n 
C 3 368 SER 368 368 368 SER SER B . n 
C 3 369 ILE 369 369 369 ILE ILE B . n 
C 3 370 VAL 370 370 370 VAL VAL B . n 
C 3 371 HIS 371 371 371 HIS HIS B . n 
C 3 372 ARG 372 372 372 ARG ARG B . n 
C 3 373 LYS 373 373 373 LYS LYS B . n 
C 3 374 CYS 374 374 374 CYS CYS B . n 
C 3 375 PHE 375 375 375 PHE PHE B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 AR6 ? ? AR6 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ANP ? ? ANP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 ANP 1  401 401 ANP ANP A . 
E 5 AR6 1  402 402 AR6 AR6 A . 
F 6 HOH 1  501 84  HOH HOH A . 
F 6 HOH 2  502 96  HOH HOH A . 
F 6 HOH 3  503 108 HOH HOH A . 
F 6 HOH 4  504 134 HOH HOH A . 
F 6 HOH 5  505 33  HOH HOH A . 
F 6 HOH 6  506 83  HOH HOH A . 
F 6 HOH 7  507 88  HOH HOH A . 
F 6 HOH 8  508 2   HOH HOH A . 
F 6 HOH 9  509 17  HOH HOH A . 
F 6 HOH 10 510 50  HOH HOH A . 
F 6 HOH 11 511 22  HOH HOH A . 
F 6 HOH 12 512 20  HOH HOH A . 
F 6 HOH 13 513 42  HOH HOH A . 
F 6 HOH 14 514 10  HOH HOH A . 
F 6 HOH 15 515 34  HOH HOH A . 
F 6 HOH 16 516 14  HOH HOH A . 
F 6 HOH 17 517 16  HOH HOH A . 
F 6 HOH 18 518 7   HOH HOH A . 
F 6 HOH 19 519 135 HOH HOH A . 
F 6 HOH 20 520 116 HOH HOH A . 
F 6 HOH 21 521 1   HOH HOH A . 
F 6 HOH 22 522 47  HOH HOH A . 
F 6 HOH 23 523 68  HOH HOH A . 
F 6 HOH 24 524 89  HOH HOH A . 
F 6 HOH 25 525 13  HOH HOH A . 
F 6 HOH 26 526 85  HOH HOH A . 
F 6 HOH 27 527 56  HOH HOH A . 
F 6 HOH 28 528 80  HOH HOH A . 
F 6 HOH 29 529 18  HOH HOH A . 
F 6 HOH 30 530 93  HOH HOH A . 
F 6 HOH 31 531 8   HOH HOH A . 
F 6 HOH 32 532 63  HOH HOH A . 
F 6 HOH 33 533 66  HOH HOH A . 
F 6 HOH 34 534 112 HOH HOH A . 
F 6 HOH 35 535 133 HOH HOH A . 
F 6 HOH 36 536 12  HOH HOH A . 
F 6 HOH 37 537 23  HOH HOH A . 
F 6 HOH 38 538 15  HOH HOH A . 
F 6 HOH 39 539 121 HOH HOH A . 
F 6 HOH 40 540 11  HOH HOH A . 
F 6 HOH 41 541 41  HOH HOH A . 
F 6 HOH 42 542 102 HOH HOH A . 
F 6 HOH 43 543 78  HOH HOH A . 
F 6 HOH 44 544 64  HOH HOH A . 
F 6 HOH 45 545 60  HOH HOH A . 
F 6 HOH 46 546 91  HOH HOH A . 
F 6 HOH 47 547 131 HOH HOH A . 
F 6 HOH 48 548 120 HOH HOH A . 
F 6 HOH 49 549 65  HOH HOH A . 
F 6 HOH 50 550 39  HOH HOH A . 
F 6 HOH 51 551 19  HOH HOH A . 
F 6 HOH 52 552 77  HOH HOH A . 
F 6 HOH 53 553 114 HOH HOH A . 
F 6 HOH 54 554 4   HOH HOH A . 
F 6 HOH 55 555 105 HOH HOH A . 
G 6 HOH 1  101 25  HOH HOH C . 
G 6 HOH 2  102 76  HOH HOH C . 
G 6 HOH 3  103 52  HOH HOH C . 
G 6 HOH 4  104 72  HOH HOH C . 
G 6 HOH 5  105 53  HOH HOH C . 
G 6 HOH 6  106 44  HOH HOH C . 
G 6 HOH 7  107 95  HOH HOH C . 
G 6 HOH 8  108 132 HOH HOH C . 
H 6 HOH 1  401 82  HOH HOH B . 
H 6 HOH 2  402 28  HOH HOH B . 
H 6 HOH 3  403 73  HOH HOH B . 
H 6 HOH 4  404 70  HOH HOH B . 
H 6 HOH 5  405 128 HOH HOH B . 
H 6 HOH 6  406 130 HOH HOH B . 
H 6 HOH 7  407 75  HOH HOH B . 
H 6 HOH 8  408 5   HOH HOH B . 
H 6 HOH 9  409 123 HOH HOH B . 
H 6 HOH 10 410 37  HOH HOH B . 
H 6 HOH 11 411 104 HOH HOH B . 
H 6 HOH 12 412 55  HOH HOH B . 
H 6 HOH 13 413 30  HOH HOH B . 
H 6 HOH 14 414 29  HOH HOH B . 
H 6 HOH 15 415 6   HOH HOH B . 
H 6 HOH 16 416 31  HOH HOH B . 
H 6 HOH 17 417 67  HOH HOH B . 
H 6 HOH 18 418 27  HOH HOH B . 
H 6 HOH 19 419 43  HOH HOH B . 
H 6 HOH 20 420 32  HOH HOH B . 
H 6 HOH 21 421 51  HOH HOH B . 
H 6 HOH 22 422 113 HOH HOH B . 
H 6 HOH 23 423 69  HOH HOH B . 
H 6 HOH 24 424 3   HOH HOH B . 
H 6 HOH 25 425 49  HOH HOH B . 
H 6 HOH 26 426 98  HOH HOH B . 
H 6 HOH 27 427 99  HOH HOH B . 
H 6 HOH 28 428 36  HOH HOH B . 
H 6 HOH 29 429 71  HOH HOH B . 
H 6 HOH 30 430 109 HOH HOH B . 
H 6 HOH 31 431 24  HOH HOH B . 
H 6 HOH 32 432 35  HOH HOH B . 
H 6 HOH 33 433 115 HOH HOH B . 
H 6 HOH 34 434 62  HOH HOH B . 
H 6 HOH 35 435 87  HOH HOH B . 
H 6 HOH 36 436 74  HOH HOH B . 
H 6 HOH 37 437 54  HOH HOH B . 
H 6 HOH 38 438 46  HOH HOH B . 
H 6 HOH 39 439 119 HOH HOH B . 
H 6 HOH 40 440 118 HOH HOH B . 
H 6 HOH 41 441 79  HOH HOH B . 
H 6 HOH 42 442 106 HOH HOH B . 
H 6 HOH 43 443 26  HOH HOH B . 
H 6 HOH 44 444 94  HOH HOH B . 
H 6 HOH 45 445 21  HOH HOH B . 
H 6 HOH 46 446 90  HOH HOH B . 
H 6 HOH 47 447 127 HOH HOH B . 
H 6 HOH 48 448 45  HOH HOH B . 
H 6 HOH 49 449 81  HOH HOH B . 
H 6 HOH 50 450 48  HOH HOH B . 
H 6 HOH 51 451 58  HOH HOH B . 
H 6 HOH 52 452 126 HOH HOH B . 
H 6 HOH 53 453 86  HOH HOH B . 
H 6 HOH 54 454 38  HOH HOH B . 
H 6 HOH 55 455 40  HOH HOH B . 
H 6 HOH 56 456 122 HOH HOH B . 
H 6 HOH 57 457 103 HOH HOH B . 
H 6 HOH 58 458 107 HOH HOH B . 
H 6 HOH 59 459 111 HOH HOH B . 
H 6 HOH 60 460 117 HOH HOH B . 
H 6 HOH 61 461 57  HOH HOH B . 
H 6 HOH 62 462 9   HOH HOH B . 
H 6 HOH 63 463 101 HOH HOH B . 
H 6 HOH 64 464 97  HOH HOH B . 
H 6 HOH 65 465 61  HOH HOH B . 
H 6 HOH 66 466 110 HOH HOH B . 
H 6 HOH 67 467 125 HOH HOH B . 
H 6 HOH 68 468 92  HOH HOH B . 
H 6 HOH 69 469 100 HOH HOH B . 
H 6 HOH 70 470 124 HOH HOH B . 
H 6 HOH 71 471 129 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 N 1 A AR6 402 ? N1    ? E AR6 1 N1    
2  1 N 1 A AR6 402 ? C2    ? E AR6 1 C2    
3  1 N 1 A AR6 402 ? N3    ? E AR6 1 N3    
4  1 N 1 A AR6 402 ? C4    ? E AR6 1 C4    
5  1 N 1 A AR6 402 ? C5    ? E AR6 1 C5    
6  1 N 1 A AR6 402 ? C6    ? E AR6 1 C6    
7  1 N 1 A AR6 402 ? N6    ? E AR6 1 N6    
8  1 N 1 A AR6 402 ? N7    ? E AR6 1 N7    
9  1 N 1 A AR6 402 ? C8    ? E AR6 1 C8    
10 1 N 1 A AR6 402 ? N9    ? E AR6 1 N9    
11 1 N 1 A AR6 402 ? PA    ? E AR6 1 PA    
12 1 N 1 A AR6 402 ? "C1'" ? E AR6 1 "C1'" 
13 1 N 1 A AR6 402 ? O1A   ? E AR6 1 O1A   
14 1 N 1 A AR6 402 ? "C2'" ? E AR6 1 "C2'" 
15 1 N 1 A AR6 402 ? "O2'" ? E AR6 1 "O2'" 
16 1 N 1 A AR6 402 ? O2A   ? E AR6 1 O2A   
17 1 N 1 A AR6 402 ? "C3'" ? E AR6 1 "C3'" 
18 1 N 1 A AR6 402 ? "O3'" ? E AR6 1 "O3'" 
19 1 N 1 A AR6 402 ? "C4'" ? E AR6 1 "C4'" 
20 1 N 1 A AR6 402 ? "O4'" ? E AR6 1 "O4'" 
21 1 N 1 A AR6 402 ? "C5'" ? E AR6 1 "C5'" 
22 1 N 1 A AR6 402 ? "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   ? ? ? '(1.19.2_4158: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8K6R 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     217.970 
_cell.length_a_esd                 ? 
_cell.length_b                     55.903 
_cell.length_b_esd                 ? 
_cell.length_c                     80.458 
_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                         8K6R 
_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                   8K6R 
_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             2.69 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.32 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'Sodium Chloride, Sodium HEPES, PEG8000' 
_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                                       8K6R 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.76 
_reflns.d_resolution_low                               75.48 
_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                                     26085 
_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                           98 
_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                          13.73 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.036 
_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                                    2.76 
_reflns_shell.d_res_low                                     2.86 
_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                             25650 
_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                                  0.769 
_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                                 8K6R 
_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                            2.76 
_refine.ls_d_res_low                             75.48 
_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                     25650 
_refine.ls_number_reflns_R_free                  1966 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.18 
_refine.ls_percent_reflns_R_free                 7.66 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2091 
_refine.ls_R_factor_R_free                       0.2612 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2048 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_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                 24.84 
_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                            0.34 
_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                       2.76 
_refine_hist.d_res_low                        75.48 
_refine_hist.number_atoms_solvent             134 
_refine_hist.number_atoms_total               6479 
_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        6314 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_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' ? 0.012  ? 6470 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.545  ? 8753 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.129 ? 2461 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.089  ? 982  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 1118 ? 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' 2.76 2.83  . . 131 1598 95.00  . . . . 0.2734 . . . . . . . . . . . 0.3514 
'X-RAY DIFFRACTION' 2.83 2.91  . . 130 1627 96.00  . . . . 0.2513 . . . . . . . . . . . 0.3260 
'X-RAY DIFFRACTION' 2.91 2.99  . . 139 1623 96.00  . . . . 0.2388 . . . . . . . . . . . 0.3039 
'X-RAY DIFFRACTION' 2.99 3.09  . . 139 1652 98.00  . . . . 0.2408 . . . . . . . . . . . 0.3065 
'X-RAY DIFFRACTION' 3.09 3.20  . . 137 1635 98.00  . . . . 0.2274 . . . . . . . . . . . 0.3049 
'X-RAY DIFFRACTION' 3.20 3.33  . . 142 1692 99.00  . . . . 0.2199 . . . . . . . . . . . 0.3228 
'X-RAY DIFFRACTION' 3.33 3.48  . . 139 1687 99.00  . . . . 0.2121 . . . . . . . . . . . 0.2600 
'X-RAY DIFFRACTION' 3.48 3.66  . . 139 1696 99.00  . . . . 0.2018 . . . . . . . . . . . 0.2518 
'X-RAY DIFFRACTION' 3.66 3.89  . . 140 1694 99.00  . . . . 0.2013 . . . . . . . . . . . 0.2693 
'X-RAY DIFFRACTION' 3.89 4.19  . . 141 1703 99.00  . . . . 0.1810 . . . . . . . . . . . 0.2148 
'X-RAY DIFFRACTION' 4.19 4.61  . . 145 1726 100.00 . . . . 0.1623 . . . . . . . . . . . 0.2448 
'X-RAY DIFFRACTION' 4.61 5.28  . . 143 1738 100.00 . . . . 0.1726 . . . . . . . . . . . 0.2094 
'X-RAY DIFFRACTION' 5.28 6.65  . . 147 1771 100.00 . . . . 0.2109 . . . . . . . . . . . 0.2509 
'X-RAY DIFFRACTION' 6.65 75.48 . . 154 1842 98.00  . . . . 0.1925 . . . . . . . . . . . 0.2209 
# 
_struct.entry_id                     8K6R 
_struct.title                        'LnaB-Actin-PRUb ternary complex in the presence of AMPPNP' 
_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        8K6R 
_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 PDB 8K6R             8K6R       ? 1 ? 1 
2 UNP UBB_HUMAN        P0CG47     ? 2 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 1 
3 UNP A0A8C6VAB1_NAJNA A0A8C6VAB1 ? 3 
;MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD
DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT
HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL
APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
;
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 8K6R A 1 ? 352 ? 8K6R       19 ? 370 ? 19 370 
2 2 8K6R C 1 ? 76  ? P0CG47     1  ? 76  ? 1  76  
3 3 8K6R B 1 ? 375 ? A0A8C6VAB1 1  ? 375 ? 1  375 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 7   ? LEU A 14  ? GLU A 25  LEU A 32  1 ? 8  
HELX_P HELX_P2  AA2 ASP A 20  ? GLY A 37  ? ASP A 38  GLY A 55  1 ? 18 
HELX_P HELX_P3  AA3 LYS A 39  ? GLU A 41  ? LYS A 57  GLU A 59  5 ? 3  
HELX_P HELX_P4  AA4 PHE A 42  ? LYS A 55  ? PHE A 60  LYS A 73  1 ? 14 
HELX_P HELX_P5  AA5 ASN A 57  ? LYS A 70  ? ASN A 75  LYS A 88  1 ? 14 
HELX_P HELX_P6  AA6 ASN A 72  ? LEU A 76  ? ASN A 90  LEU A 94  5 ? 5  
HELX_P HELX_P7  AA7 SER A 77  ? ALA A 88  ? SER A 95  ALA A 106 1 ? 12 
HELX_P HELX_P8  AA8 PRO A 89  ? LEU A 91  ? PRO A 107 LEU A 109 5 ? 3  
HELX_P HELX_P9  AA9 ASN A 98  ? SER A 120 ? ASN A 116 SER A 138 1 ? 23 
HELX_P HELX_P10 AB1 LEU A 122 ? LYS A 136 ? LEU A 140 LYS A 154 1 ? 15 
HELX_P HELX_P11 AB2 THR A 149 ? LEU A 158 ? THR A 167 LEU A 176 1 ? 10 
HELX_P HELX_P12 AB3 SER A 159 ? ASN A 164 ? SER A 177 ASN A 182 5 ? 6  
HELX_P HELX_P13 AB4 GLU A 168 ? ALA A 173 ? GLU A 186 ALA A 191 1 ? 6  
HELX_P HELX_P14 AB5 ARG A 177 ? LYS A 181 ? ARG A 195 LYS A 199 5 ? 5  
HELX_P HELX_P15 AB6 PHE A 206 ? LEU A 210 ? PHE A 224 LEU A 228 5 ? 5  
HELX_P HELX_P16 AB7 GLY A 228 ? LYS A 233 ? GLY A 246 LYS A 251 1 ? 6  
HELX_P HELX_P17 AB8 THR A 245 ? HIS A 260 ? THR A 263 HIS A 278 1 ? 16 
HELX_P HELX_P18 AB9 ASP A 265 ? GLU A 284 ? ASP A 283 GLU A 302 1 ? 20 
HELX_P HELX_P19 AC1 SER A 288 ? THR A 297 ? SER A 306 THR A 315 1 ? 10 
HELX_P HELX_P20 AC2 GLU A 298 ? ALA A 308 ? GLU A 316 ALA A 326 1 ? 11 
HELX_P HELX_P21 AC3 THR A 320 ? LYS A 349 ? THR A 338 LYS A 367 1 ? 30 
HELX_P HELX_P22 AC4 THR B 22  ? GLU B 34  ? THR C 22  GLU C 34  1 ? 13 
HELX_P HELX_P23 AC5 PRO B 37  ? ASP B 39  ? PRO C 37  ASP C 39  5 ? 3  
HELX_P HELX_P24 AC6 LEU B 56  ? ASN B 60  ? LEU C 56  ASN C 60  5 ? 5  
HELX_P HELX_P25 AC7 HIS C 40  ? MET C 44  ? HIS B 40  MET B 44  5 ? 5  
HELX_P HELX_P26 AC8 GLY C 55  ? LYS C 61  ? GLY B 55  LYS B 61  1 ? 7  
HELX_P HELX_P27 AC9 ASN C 78  ? ASN C 92  ? ASN B 78  ASN B 92  1 ? 15 
HELX_P HELX_P28 AD1 ALA C 97  ? HIS C 101 ? ALA B 97  HIS B 101 5 ? 5  
HELX_P HELX_P29 AD2 PRO C 112 ? THR C 126 ? PRO B 112 THR B 126 1 ? 15 
HELX_P HELX_P30 AD3 GLN C 137 ? SER C 145 ? GLN B 137 SER B 145 1 ? 9  
HELX_P HELX_P31 AD4 ALA C 181 ? GLY C 197 ? ALA B 181 GLY B 197 1 ? 17 
HELX_P HELX_P32 AD5 THR C 202 ? CYS C 217 ? THR B 202 CYS B 217 1 ? 16 
HELX_P HELX_P33 AD6 ASP C 222 ? SER C 233 ? ASP B 222 SER B 233 1 ? 12 
HELX_P HELX_P34 AD7 ASN C 252 ? CYS C 257 ? ASN B 252 CYS B 257 1 ? 6  
HELX_P HELX_P35 AD8 PRO C 258 ? PHE C 262 ? PRO B 258 PHE B 262 5 ? 5  
HELX_P HELX_P36 AD9 GLN C 263 ? GLY C 268 ? GLN B 263 GLY B 268 5 ? 6  
HELX_P HELX_P37 AE1 GLY C 273 ? LYS C 284 ? GLY B 273 LYS B 284 1 ? 12 
HELX_P HELX_P38 AE2 ASP C 286 ? ALA C 295 ? ASP B 286 ALA B 295 1 ? 10 
HELX_P HELX_P39 AE3 GLY C 308 ? ALA C 321 ? GLY B 308 ALA B 321 1 ? 14 
HELX_P HELX_P40 AE4 GLU C 334 ? LYS C 336 ? GLU B 334 LYS B 336 5 ? 3  
HELX_P HELX_P41 AE5 TYR C 337 ? SER C 348 ? TYR B 337 SER B 348 1 ? 12 
HELX_P HELX_P42 AE6 LEU C 349 ? TRP C 356 ? LEU B 349 TRP B 356 5 ? 8  
HELX_P HELX_P43 AE7 LYS C 359 ? GLY C 366 ? LYS B 359 GLY B 366 1 ? 8  
HELX_P HELX_P44 AE8 SER C 368 ? CYS C 374 ? SER B 368 CYS B 374 1 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
AA4 ? 3 ? 
AA5 ? 3 ? 
AA6 ? 5 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA7 1 2 ? anti-parallel 
# 
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 ASN A 190 ? SER A 193 ? ASN A 208 SER A 211 
AA1 2 ARG A 214 ? PRO A 217 ? ARG A 232 PRO A 235 
AA2 1 THR B 12  ? GLU B 16  ? THR C 12  GLU C 16  
AA2 2 GLN B 2   ? THR B 7   ? GLN C 2   THR C 7   
AA2 3 THR B 66  ? LEU B 71  ? THR C 66  LEU C 71  
AA2 4 GLN B 41  ? PHE B 45  ? GLN C 41  PHE C 45  
AA2 5 LYS B 48  ? GLN B 49  ? LYS C 48  GLN C 49  
AA3 1 ALA C 29  ? PRO C 32  ? ALA B 29  PRO B 32  
AA3 2 MET C 16  ? PHE C 21  ? MET B 16  PHE B 21  
AA3 3 LEU C 8   ? ASP C 11  ? LEU B 8   ASP B 11  
AA3 4 VAL C 103 ? GLU C 107 ? VAL B 103 GLU B 107 
AA3 5 ALA C 131 ? ILE C 136 ? ALA B 131 ILE B 136 
AA3 6 ILE C 357 ? SER C 358 ? ILE B 357 SER B 358 
AA4 1 TYR C 53  ? VAL C 54  ? TYR B 53  VAL B 54  
AA4 2 VAL C 35  ? PRO C 38  ? VAL B 35  PRO B 38  
AA4 3 LEU C 65  ? LYS C 68  ? LEU B 65  LYS B 68  
AA5 1 TYR C 169 ? ALA C 170 ? TYR B 169 ALA B 170 
AA5 2 THR C 160 ? TYR C 166 ? THR B 160 TYR B 166 
AA5 3 LEU C 176 ? LEU C 178 ? LEU B 176 LEU B 178 
AA6 1 TYR C 169 ? ALA C 170 ? TYR B 169 ALA B 170 
AA6 2 THR C 160 ? TYR C 166 ? THR B 160 TYR B 166 
AA6 3 GLY C 150 ? SER C 155 ? GLY B 150 SER B 155 
AA6 4 THR C 297 ? SER C 300 ? THR B 297 SER B 300 
AA6 5 ILE C 329 ? ILE C 330 ? ILE B 329 ILE B 330 
AA7 1 LYS C 238 ? GLU C 241 ? LYS B 238 GLU B 241 
AA7 2 VAL C 247 ? ILE C 250 ? VAL B 247 ILE B 250 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N THR A 191 ? N THR A 209 O VAL A 216 ? O VAL A 234 
AA2 1 2 O ILE B 13  ? O ILE C 13  N VAL B 5   ? N VAL C 5   
AA2 2 3 N PHE B 4   ? N PHE C 4   O LEU B 67  ? O LEU C 67  
AA2 3 4 O HIS B 68  ? O HIS C 68  N ILE B 44  ? N ILE C 44  
AA2 4 5 N PHE B 45  ? N PHE C 45  O LYS B 48  ? O LYS C 48  
AA3 1 2 O ALA C 29  ? O ALA B 29  N ALA C 19  ? N ALA B 19  
AA3 2 3 O LYS C 18  ? O LYS B 18  N ASP C 11  ? N ASP B 11  
AA3 3 4 N LEU C 8   ? N LEU B 8   O LEU C 104 ? O LEU B 104 
AA3 4 5 N LEU C 105 ? N LEU B 105 O TYR C 133 ? O TYR B 133 
AA3 5 6 N MET C 132 ? N MET B 132 O ILE C 357 ? O ILE B 357 
AA4 1 2 O TYR C 53  ? O TYR B 53  N GLY C 36  ? N GLY B 36  
AA4 2 3 N VAL C 35  ? N VAL B 35  O LYS C 68  ? O LYS B 68  
AA5 1 2 O TYR C 169 ? O TYR B 169 N TYR C 166 ? N TYR B 166 
AA5 2 3 N THR C 160 ? N THR B 160 O LEU C 178 ? O LEU B 178 
AA6 1 2 O TYR C 169 ? O TYR B 169 N TYR C 166 ? N TYR B 166 
AA6 2 3 O ILE C 165 ? O ILE B 165 N GLY C 150 ? N GLY B 150 
AA6 3 4 N MET C 153 ? N MET B 153 O VAL C 298 ? O VAL B 298 
AA6 4 5 N THR C 297 ? N THR B 297 O ILE C 330 ? O ILE B 330 
AA7 1 2 N LYS C 238 ? N LYS B 238 O ILE C 250 ? O ILE B 250 
# 
_pdbx_entry_details.entry_id                   8K6R 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              139 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              139 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              139 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                87.39 
_pdbx_validate_rmsd_angle.angle_target_value         111.00 
_pdbx_validate_rmsd_angle.angle_deviation            -23.61 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.70 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 56  ? ? -96.26  55.70   
2  1 ASN A 90  ? ? -142.67 15.92   
3  1 PRO A 113 ? ? -47.99  -19.50  
4  1 ASN A 116 ? ? -108.79 59.22   
5  1 LEU A 140 ? ? -88.23  37.69   
6  1 VAL A 185 ? ? 71.26   -50.49  
7  1 PRO A 197 ? ? -56.87  -9.57   
8  1 GLU A 241 ? ? -69.81  1.86    
9  1 ALA A 258 ? ? -140.69 22.34   
10 1 SER A 259 ? ? 64.48   -155.75 
11 1 THR A 338 ? ? -88.69  37.08   
12 1 SER B 14  ? ? 56.81   -141.91 
13 1 GLN B 49  ? ? 55.30   8.11    
14 1 ASP B 179 ? ? -95.88  54.09   
15 1 ALA B 181 ? ? -145.26 -158.52 
16 1 THR B 201 ? ? -144.71 -22.02  
17 1 ASN B 296 ? ? -151.28 58.77   
18 1 MET B 305 ? ? -90.32  52.15   
# 
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 19 ? A MET 1  
2  1 Y 1 A SER 20 ? A SER 2  
3  1 Y 1 A TYR 21 ? A TYR 3  
4  1 Y 1 A GLN 22 ? A GLN 4  
5  1 Y 1 A LYS 23 ? A LYS 5  
6  1 Y 1 A ILE 24 ? A ILE 6  
7  1 Y 1 C GLY 76 ? B GLY 76 
8  1 Y 1 B MET 1  ? C MET 1  
9  1 Y 1 B GLU 2  ? C GLU 2  
10 1 Y 1 B GLU 3  ? C GLU 3  
11 1 Y 1 B GLU 4  ? C GLU 4  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
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                    8K6R 
_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]   0.004588 
_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]   0.017888 
_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]   0.012429 
_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      . GLU A 1 7   ? 12.461 -9.214  -10.126 1.00 29.92 ? 25  GLU A N      1 
ATOM   2    C CA     . GLU A 1 7   ? 12.846 -10.625 -10.091 1.00 32.61 ? 25  GLU A CA     1 
ATOM   3    C C      . GLU A 1 7   ? 14.084 -10.887 -10.941 1.00 35.36 ? 25  GLU A C      1 
ATOM   4    O O      . GLU A 1 7   ? 15.029 -11.542 -10.501 1.00 29.65 ? 25  GLU A O      1 
ATOM   5    C CB     . GLU A 1 7   ? 11.688 -11.508 -10.555 1.00 43.47 ? 25  GLU A CB     1 
ATOM   6    C CG     . GLU A 1 7   ? 11.972 -13.005 -10.505 1.00 49.26 ? 25  GLU A CG     1 
ATOM   7    C CD     . GLU A 1 7   ? 12.354 -13.566 -11.862 1.00 58.87 ? 25  GLU A CD     1 
ATOM   8    O OE1    . GLU A 1 7   ? 12.381 -12.770 -12.833 1.00 58.28 ? 25  GLU A OE1    1 
ATOM   9    O OE2    . GLU A 1 7   ? 12.615 -14.795 -11.959 1.00 55.23 ? 25  GLU A OE2    1 
ATOM   10   N N      . LEU A 1 8   ? 14.078 -10.379 -12.174 1.00 44.79 ? 26  LEU A N      1 
ATOM   11   C CA     . LEU A 1 8   ? 15.320 -10.352 -12.943 1.00 40.42 ? 26  LEU A CA     1 
ATOM   12   C C      . LEU A 1 8   ? 16.338 -9.412  -12.302 1.00 37.88 ? 26  LEU A C      1 
ATOM   13   O O      . LEU A 1 8   ? 17.528 -9.746  -12.212 1.00 36.36 ? 26  LEU A O      1 
ATOM   14   C CB     . LEU A 1 8   ? 15.036 -9.949  -14.389 1.00 32.86 ? 26  LEU A CB     1 
ATOM   15   C CG     . LEU A 1 8   ? 16.248 -9.623  -15.262 1.00 42.88 ? 26  LEU A CG     1 
ATOM   16   C CD1    . LEU A 1 8   ? 17.252 -10.790 -15.357 1.00 38.45 ? 26  LEU A CD1    1 
ATOM   17   C CD2    . LEU A 1 8   ? 15.791 -9.168  -16.647 1.00 35.66 ? 26  LEU A CD2    1 
ATOM   18   N N      . SER A 1 9   ? 15.882 -8.247  -11.822 1.00 32.26 ? 27  SER A N      1 
ATOM   19   C CA     . SER A 1 9   ? 16.776 -7.294  -11.164 1.00 33.27 ? 27  SER A CA     1 
ATOM   20   C C      . SER A 1 9   ? 17.569 -7.944  -10.038 1.00 31.55 ? 27  SER A C      1 
ATOM   21   O O      . SER A 1 9   ? 18.776 -7.705  -9.892  1.00 27.32 ? 27  SER A O      1 
ATOM   22   C CB     . SER A 1 9   ? 15.977 -6.113  -10.615 1.00 30.04 ? 27  SER A CB     1 
ATOM   23   O OG     . SER A 1 9   ? 14.978 -6.571  -9.728  1.00 39.88 ? 27  SER A OG     1 
ATOM   24   N N      . ILE A 1 10  ? 16.905 -8.752  -9.214  1.00 32.66 ? 28  ILE A N      1 
ATOM   25   C CA     . ILE A 1 10  ? 17.600 -9.353  -8.084  1.00 31.29 ? 28  ILE A CA     1 
ATOM   26   C C      . ILE A 1 10  ? 18.655 -10.334 -8.576  1.00 30.00 ? 28  ILE A C      1 
ATOM   27   O O      . ILE A 1 10  ? 19.778 -10.363 -8.059  1.00 33.26 ? 28  ILE A O      1 
ATOM   28   C CB     . ILE A 1 10  ? 16.596 -10.006 -7.113  1.00 25.58 ? 28  ILE A CB     1 
ATOM   29   C CG1    . ILE A 1 10  ? 17.164 -10.015 -5.707  1.00 27.85 ? 28  ILE A CG1    1 
ATOM   30   C CG2    . ILE A 1 10  ? 16.293 -11.418 -7.514  1.00 26.75 ? 28  ILE A CG2    1 
ATOM   31   C CD1    . ILE A 1 10  ? 16.480 -11.026 -4.814  1.00 36.26 ? 28  ILE A CD1    1 
ATOM   32   N N      . SER A 1 11  ? 18.431 -11.053 -9.654  1.00 25.49 ? 29  SER A N      1 
ATOM   33   C CA     . SER A 1 11  ? 19.429 -11.965 -10.118 1.00 30.96 ? 29  SER A CA     1 
ATOM   34   C C      . SER A 1 11  ? 20.640 -11.202 -10.566 1.00 26.41 ? 29  SER A C      1 
ATOM   35   O O      . SER A 1 11  ? 21.753 -11.662 -10.425 1.00 25.93 ? 29  SER A O      1 
ATOM   36   C CB     . SER A 1 11  ? 18.859 -12.811 -11.227 1.00 35.71 ? 29  SER A CB     1 
ATOM   37   O OG     . SER A 1 11  ? 17.447 -12.783 -11.203 1.00 46.11 ? 29  SER A OG     1 
ATOM   38   N N      . LEU A 1 12  ? 20.422 -10.005 -11.056 1.00 26.63 ? 30  LEU A N      1 
ATOM   39   C CA     . LEU A 1 12  ? 21.508 -9.159  -11.522 1.00 28.92 ? 30  LEU A CA     1 
ATOM   40   C C      . LEU A 1 12  ? 22.244 -8.500  -10.387 1.00 32.17 ? 30  LEU A C      1 
ATOM   41   O O      . LEU A 1 12  ? 23.351 -8.031  -10.551 1.00 32.11 ? 30  LEU A O      1 
ATOM   42   C CB     . LEU A 1 12  ? 20.952 -8.088  -12.438 1.00 19.46 ? 30  LEU A CB     1 
ATOM   43   C CG     . LEU A 1 12  ? 20.465 -8.400  -13.838 1.00 31.02 ? 30  LEU A CG     1 
ATOM   44   C CD1    . LEU A 1 12  ? 19.692 -7.196  -14.341 1.00 30.39 ? 30  LEU A CD1    1 
ATOM   45   C CD2    . LEU A 1 12  ? 21.657 -8.674  -14.730 1.00 27.35 ? 30  LEU A CD2    1 
ATOM   46   N N      . SER A 1 13  ? 21.651 -8.505  -9.217  1.00 26.18 ? 31  SER A N      1 
ATOM   47   C CA     . SER A 1 13  ? 22.231 -7.884  -8.086  1.00 20.06 ? 31  SER A CA     1 
ATOM   48   C C      . SER A 1 13  ? 23.009 -8.901  -7.343  1.00 25.33 ? 31  SER A C      1 
ATOM   49   O O      . SER A 1 13  ? 23.946 -8.579  -6.657  1.00 29.68 ? 31  SER A O      1 
ATOM   50   C CB     . SER A 1 13  ? 21.079 -7.392  -7.243  1.00 25.35 ? 31  SER A CB     1 
ATOM   51   O OG     . SER A 1 13  ? 20.451 -6.252  -7.785  1.00 23.73 ? 31  SER A OG     1 
ATOM   52   N N      . LEU A 1 14  ? 22.645 -10.157 -7.501  1.00 34.82 ? 32  LEU A N      1 
ATOM   53   C CA     . LEU A 1 14  ? 23.324 -11.262 -6.837  1.00 28.24 ? 32  LEU A CA     1 
ATOM   54   C C      . LEU A 1 14  ? 24.536 -11.641 -7.614  1.00 23.64 ? 32  LEU A C      1 
ATOM   55   O O      . LEU A 1 14  ? 25.259 -12.542 -7.238  1.00 25.06 ? 32  LEU A O      1 
ATOM   56   C CB     . LEU A 1 14  ? 22.367 -12.438 -6.729  1.00 30.61 ? 32  LEU A CB     1 
ATOM   57   C CG     . LEU A 1 14  ? 21.211 -12.256 -5.767  1.00 29.99 ? 32  LEU A CG     1 
ATOM   58   C CD1    . LEU A 1 14  ? 20.215 -13.379 -5.973  1.00 25.90 ? 32  LEU A CD1    1 
ATOM   59   C CD2    . LEU A 1 14  ? 21.741 -12.227 -4.349  1.00 26.97 ? 32  LEU A CD2    1 
ATOM   60   N N      . ASP A 1 15  ? 24.762 -10.949 -8.705  1.00 23.50 ? 33  ASP A N      1 
ATOM   61   C CA     . ASP A 1 15  ? 25.914 -11.157 -9.507  1.00 28.96 ? 33  ASP A CA     1 
ATOM   62   C C      . ASP A 1 15  ? 27.071 -10.302 -9.012  1.00 27.53 ? 33  ASP A C      1 
ATOM   63   O O      . ASP A 1 15  ? 28.135 -10.359 -9.571  1.00 26.47 ? 33  ASP A O      1 
ATOM   64   C CB     . ASP A 1 15  ? 25.570 -10.725 -10.924 1.00 26.00 ? 33  ASP A CB     1 
ATOM   65   C CG     . ASP A 1 15  ? 25.061 -11.858 -11.787 1.00 38.40 ? 33  ASP A CG     1 
ATOM   66   O OD1    . ASP A 1 15  ? 25.498 -13.008 -11.593 1.00 41.31 ? 33  ASP A OD1    1 
ATOM   67   O OD2    . ASP A 1 15  ? 24.232 -11.591 -12.680 1.00 32.11 ? 33  ASP A OD2    1 
ATOM   68   N N      . SER A 1 16  ? 26.885 -9.531  -7.960  1.00 21.14 ? 34  SER A N      1 
ATOM   69   C CA     . SER A 1 16  ? 27.908 -8.619  -7.487  1.00 25.41 ? 34  SER A CA     1 
ATOM   70   C C      . SER A 1 16  ? 29.021 -9.294  -6.779  1.00 27.72 ? 34  SER A C      1 
ATOM   71   O O      . SER A 1 16  ? 28.806 -10.168 -5.958  1.00 26.76 ? 34  SER A O      1 
ATOM   72   C CB     . SER A 1 16  ? 27.331 -7.503  -6.617  1.00 24.47 ? 34  SER A CB     1 
ATOM   73   O OG     . SER A 1 16  ? 28.330 -6.701  -6.029  1.00 22.71 ? 34  SER A OG     1 
ATOM   74   N N      . PRO A 1 17  ? 30.237 -8.899  -7.130  1.00 24.65 ? 35  PRO A N      1 
ATOM   75   C CA     . PRO A 1 17  ? 31.391 -9.504  -6.520  1.00 22.34 ? 35  PRO A CA     1 
ATOM   76   C C      . PRO A 1 17  ? 31.579 -9.018  -5.112  1.00 24.40 ? 35  PRO A C      1 
ATOM   77   O O      . PRO A 1 17  ? 32.061 -9.760  -4.272  1.00 23.84 ? 35  PRO A O      1 
ATOM   78   C CB     . PRO A 1 17  ? 32.520 -9.035  -7.421  1.00 24.44 ? 35  PRO A CB     1 
ATOM   79   C CG     . PRO A 1 17  ? 32.000 -7.905  -8.220  1.00 20.92 ? 35  PRO A CG     1 
ATOM   80   C CD     . PRO A 1 17  ? 30.563 -8.207  -8.384  1.00 23.78 ? 35  PRO A CD     1 
ATOM   81   N N      . LYS A 1 18  ? 31.163 -7.804  -4.842  1.00 23.26 ? 36  LYS A N      1 
ATOM   82   C CA     . LYS A 1 18  ? 31.331 -7.188  -3.534  1.00 17.19 ? 36  LYS A CA     1 
ATOM   83   C C      . LYS A 1 18  ? 30.228 -7.552  -2.543  1.00 20.99 ? 36  LYS A C      1 
ATOM   84   O O      . LYS A 1 18  ? 30.213 -6.999  -1.436  1.00 19.71 ? 36  LYS A O      1 
ATOM   85   C CB     . LYS A 1 18  ? 31.403 -5.669  -3.691  1.00 22.37 ? 36  LYS A CB     1 
ATOM   86   C CG     . LYS A 1 18  ? 32.778 -5.164  -4.105  1.00 37.79 ? 36  LYS A CG     1 
ATOM   87   C CD     . LYS A 1 18  ? 32.882 -3.637  -3.981  1.00 41.51 ? 36  LYS A CD     1 
ATOM   88   C CE     . LYS A 1 18  ? 34.308 -3.168  -4.278  1.00 44.81 ? 36  LYS A CE     1 
ATOM   89   N NZ     . LYS A 1 18  ? 34.420 -1.693  -4.421  1.00 45.76 ? 36  LYS A NZ     1 
ATOM   90   N N      . LEU A 1 19  ? 29.347 -8.491  -2.886  1.00 17.62 ? 37  LEU A N      1 
ATOM   91   C CA     . LEU A 1 19  ? 28.163 -8.740  -2.078  1.00 17.97 ? 37  LEU A CA     1 
ATOM   92   C C      . LEU A 1 19  ? 28.551 -9.292  -0.715  1.00 20.15 ? 37  LEU A C      1 
ATOM   93   O O      . LEU A 1 19  ? 29.324 -10.248 -0.625  1.00 25.11 ? 37  LEU A O      1 
ATOM   94   C CB     . LEU A 1 19  ? 27.237 -9.710  -2.803  1.00 22.73 ? 37  LEU A CB     1 
ATOM   95   C CG     . LEU A 1 19  ? 25.760 -9.715  -2.388  1.00 33.73 ? 37  LEU A CG     1 
ATOM   96   C CD1    . LEU A 1 19  ? 25.004 -8.645  -3.169  1.00 29.75 ? 37  LEU A CD1    1 
ATOM   97   C CD2    . LEU A 1 19  ? 25.083 -11.090 -2.550  1.00 22.11 ? 37  LEU A CD2    1 
ATOM   98   N N      . ASP A 1 20  ? 28.018 -8.682  0.348   1.00 18.29 ? 38  ASP A N      1 
ATOM   99   C CA     . ASP A 1 20  ? 28.281 -9.080  1.729   1.00 16.84 ? 38  ASP A CA     1 
ATOM   100  C C      . ASP A 1 20  ? 27.056 -9.740  2.362   1.00 21.21 ? 38  ASP A C      1 
ATOM   101  O O      . ASP A 1 20  ? 25.952 -9.774  1.805   1.00 21.86 ? 38  ASP A O      1 
ATOM   102  C CB     . ASP A 1 20  ? 28.722 -7.880  2.585   1.00 19.92 ? 38  ASP A CB     1 
ATOM   103  C CG     . ASP A 1 20  ? 27.652 -6.758  2.662   1.00 27.93 ? 38  ASP A CG     1 
ATOM   104  O OD1    . ASP A 1 20  ? 26.440 -7.065  2.811   1.00 23.13 ? 38  ASP A OD1    1 
ATOM   105  O OD2    . ASP A 1 20  ? 28.027 -5.555  2.609   1.00 24.66 ? 38  ASP A OD2    1 
ATOM   106  N N      . GLU A 1 21  ? 27.265 -10.260 3.569   1.00 18.78 ? 39  GLU A N      1 
ATOM   107  C CA     . GLU A 1 21  ? 26.169 -10.887 4.300   1.00 17.33 ? 39  GLU A CA     1 
ATOM   108  C C      . GLU A 1 21  ? 25.014 -9.917  4.507   1.00 18.20 ? 39  GLU A C      1 
ATOM   109  O O      . GLU A 1 21  ? 23.841 -10.312 4.457   1.00 19.23 ? 39  GLU A O      1 
ATOM   110  C CB     . GLU A 1 21  ? 26.668 -11.421 5.641   1.00 17.17 ? 39  GLU A CB     1 
ATOM   111  C CG     . GLU A 1 21  ? 27.935 -12.235 5.512   1.00 19.04 ? 39  GLU A CG     1 
ATOM   112  C CD     . GLU A 1 21  ? 28.322 -12.895 6.805   1.00 25.00 ? 39  GLU A CD     1 
ATOM   113  O OE1    . GLU A 1 21  ? 28.665 -12.191 7.770   1.00 18.83 ? 39  GLU A OE1    1 
ATOM   114  O OE2    . GLU A 1 21  ? 28.267 -14.140 6.867   1.00 45.42 ? 39  GLU A OE2    1 
ATOM   115  N N      . SER A 1 22  ? 25.325 -8.643  4.755   1.00 21.37 ? 40  SER A N      1 
ATOM   116  C CA     . SER A 1 22  ? 24.275 -7.649  4.944   1.00 15.33 ? 40  SER A CA     1 
ATOM   117  C C      . SER A 1 22  ? 23.418 -7.512  3.694   1.00 13.56 ? 40  SER A C      1 
ATOM   118  O O      . SER A 1 22  ? 22.183 -7.553  3.762   1.00 13.03 ? 40  SER A O      1 
ATOM   119  C CB     . SER A 1 22  ? 24.897 -6.307  5.319   1.00 17.16 ? 40  SER A CB     1 
ATOM   120  O OG     . SER A 1 22  ? 23.890 -5.374  5.644   1.00 14.12 ? 40  SER A OG     1 
ATOM   121  N N      . ASP A 1 23  ? 24.063 -7.343  2.538   1.00 15.22 ? 41  ASP A N      1 
ATOM   122  C CA     . ASP A 1 23  ? 23.315 -7.135  1.302   1.00 18.53 ? 41  ASP A CA     1 
ATOM   123  C C      . ASP A 1 23  ? 22.367 -8.289  1.028   1.00 17.61 ? 41  ASP A C      1 
ATOM   124  O O      . ASP A 1 23  ? 21.225 -8.080  0.599   1.00 15.61 ? 41  ASP A O      1 
ATOM   125  C CB     . ASP A 1 23  ? 24.255 -6.997  0.104   1.00 20.27 ? 41  ASP A CB     1 
ATOM   126  C CG     . ASP A 1 23  ? 25.397 -6.060  0.346   1.00 28.41 ? 41  ASP A CG     1 
ATOM   127  O OD1    . ASP A 1 23  ? 25.203 -4.959  0.931   1.00 27.89 ? 41  ASP A OD1    1 
ATOM   128  O OD2    . ASP A 1 23  ? 26.506 -6.437  -0.098  1.00 35.08 ? 41  ASP A OD2    1 
ATOM   129  N N      . PHE A 1 24  ? 22.857 -9.517  1.206   1.00 15.17 ? 42  PHE A N      1 
ATOM   130  C CA     . PHE A 1 24  ? 22.054 -10.693 0.917   1.00 12.17 ? 42  PHE A CA     1 
ATOM   131  C C      . PHE A 1 24  ? 20.781 -10.679 1.746   1.00 16.02 ? 42  PHE A C      1 
ATOM   132  O O      . PHE A 1 24  ? 19.675 -10.826 1.218   1.00 19.14 ? 42  PHE A O      1 
ATOM   133  C CB     . PHE A 1 24  ? 22.887 -11.945 1.178   1.00 14.82 ? 42  PHE A CB     1 
ATOM   134  C CG     . PHE A 1 24  ? 22.174 -13.217 0.889   1.00 13.82 ? 42  PHE A CG     1 
ATOM   135  C CD1    . PHE A 1 24  ? 22.184 -13.756 -0.377  1.00 17.13 ? 42  PHE A CD1    1 
ATOM   136  C CD2    . PHE A 1 24  ? 21.509 -13.891 1.886   1.00 16.34 ? 42  PHE A CD2    1 
ATOM   137  C CE1    . PHE A 1 24  ? 21.522 -14.946 -0.651  1.00 22.12 ? 42  PHE A CE1    1 
ATOM   138  C CE2    . PHE A 1 24  ? 20.855 -15.076 1.622   1.00 22.98 ? 42  PHE A CE2    1 
ATOM   139  C CZ     . PHE A 1 24  ? 20.865 -15.605 0.350   1.00 23.14 ? 42  PHE A CZ     1 
ATOM   140  N N      . ILE A 1 25  ? 20.920 -10.457 3.049   1.00 13.60 ? 43  ILE A N      1 
ATOM   141  C CA     . ILE A 1 25  ? 19.746 -10.373 3.907   1.00 15.85 ? 43  ILE A CA     1 
ATOM   142  C C      . ILE A 1 25  ? 18.773 -9.309  3.404   1.00 17.74 ? 43  ILE A C      1 
ATOM   143  O O      . ILE A 1 25  ? 17.557 -9.525  3.375   1.00 19.78 ? 43  ILE A O      1 
ATOM   144  C CB     . ILE A 1 25  ? 20.181 -10.102 5.353   1.00 14.51 ? 43  ILE A CB     1 
ATOM   145  C CG1    . ILE A 1 25  ? 21.064 -11.248 5.856   1.00 15.26 ? 43  ILE A CG1    1 
ATOM   146  C CG2    . ILE A 1 25  ? 18.970 -9.863  6.198   1.00 12.83 ? 43  ILE A CG2    1 
ATOM   147  C CD1    . ILE A 1 25  ? 21.534 -11.090 7.282   1.00 15.01 ? 43  ILE A CD1    1 
ATOM   148  N N      . LEU A 1 26  ? 19.287 -8.138  3.020   1.00 17.59 ? 44  LEU A N      1 
ATOM   149  C CA     . LEU A 1 26  ? 18.415 -7.044  2.612   1.00 16.65 ? 44  LEU A CA     1 
ATOM   150  C C      . LEU A 1 26  ? 17.740 -7.351  1.286   1.00 17.63 ? 44  LEU A C      1 
ATOM   151  O O      . LEU A 1 26  ? 16.515 -7.254  1.162   1.00 16.24 ? 44  LEU A O      1 
ATOM   152  C CB     . LEU A 1 26  ? 19.219 -5.746  2.536   1.00 16.76 ? 44  LEU A CB     1 
ATOM   153  C CG     . LEU A 1 26  ? 19.501 -5.099  3.899   1.00 14.03 ? 44  LEU A CG     1 
ATOM   154  C CD1    . LEU A 1 26  ? 20.465 -3.913  3.813   1.00 8.04  ? 44  LEU A CD1    1 
ATOM   155  C CD2    . LEU A 1 26  ? 18.193 -4.697  4.543   1.00 13.13 ? 44  LEU A CD2    1 
ATOM   156  N N      . LEU A 1 27  ? 18.532 -7.734  0.289   1.00 17.89 ? 45  LEU A N      1 
ATOM   157  C CA     . LEU A 1 27  ? 18.002 -8.110  -1.015  1.00 17.16 ? 45  LEU A CA     1 
ATOM   158  C C      . LEU A 1 27  ? 17.029 -9.275  -0.913  1.00 18.79 ? 45  LEU A C      1 
ATOM   159  O O      . LEU A 1 27  ? 15.940 -9.251  -1.497  1.00 17.75 ? 45  LEU A O      1 
ATOM   160  C CB     . LEU A 1 27  ? 19.157 -8.482  -1.943  1.00 17.04 ? 45  LEU A CB     1 
ATOM   161  C CG     . LEU A 1 27  ? 19.708 -7.409  -2.871  1.00 18.74 ? 45  LEU A CG     1 
ATOM   162  C CD1    . LEU A 1 27  ? 20.951 -7.934  -3.537  1.00 25.94 ? 45  LEU A CD1    1 
ATOM   163  C CD2    . LEU A 1 27  ? 18.690 -7.057  -3.906  1.00 22.27 ? 45  LEU A CD2    1 
ATOM   164  N N      . SER A 1 28  ? 17.419 -10.325 -0.200  1.00 17.17 ? 46  SER A N      1 
ATOM   165  C CA     . SER A 1 28  ? 16.612 -11.534 -0.221  1.00 17.05 ? 46  SER A CA     1 
ATOM   166  C C      . SER A 1 28  ? 15.257 -11.299 0.425   1.00 25.51 ? 46  SER A C      1 
ATOM   167  O O      . SER A 1 28  ? 14.232 -11.777 -0.076  1.00 26.63 ? 46  SER A O      1 
ATOM   168  C CB     . SER A 1 28  ? 17.348 -12.670 0.471   1.00 19.64 ? 46  SER A CB     1 
ATOM   169  O OG     . SER A 1 28  ? 17.344 -12.446 1.865   1.00 30.01 ? 46  SER A OG     1 
ATOM   170  N N      . VAL A 1 29  ? 15.226 -10.548 1.529   1.00 20.55 ? 47  VAL A N      1 
ATOM   171  C CA     . VAL A 1 29  ? 13.954 -10.234 2.172   1.00 21.33 ? 47  VAL A CA     1 
ATOM   172  C C      . VAL A 1 29  ? 13.122 -9.300  1.303   1.00 29.76 ? 47  VAL A C      1 
ATOM   173  O O      . VAL A 1 29  ? 11.886 -9.381  1.294   1.00 35.62 ? 47  VAL A O      1 
ATOM   174  C CB     . VAL A 1 29  ? 14.180 -9.639  3.569   1.00 25.50 ? 47  VAL A CB     1 
ATOM   175  C CG1    . VAL A 1 29  ? 13.015 -8.723  3.924   1.00 25.29 ? 47  VAL A CG1    1 
ATOM   176  C CG2    . VAL A 1 29  ? 14.320 -10.747 4.589   1.00 21.86 ? 47  VAL A CG2    1 
ATOM   177  N N      . LYS A 1 30  ? 13.779 -8.388  0.577   1.00 27.62 ? 48  LYS A N      1 
ATOM   178  C CA     . LYS A 1 30  ? 13.076 -7.562  -0.404  1.00 23.27 ? 48  LYS A CA     1 
ATOM   179  C C      . LYS A 1 30  ? 12.344 -8.428  -1.424  1.00 27.10 ? 48  LYS A C      1 
ATOM   180  O O      . LYS A 1 30  ? 11.172 -8.186  -1.741  1.00 32.17 ? 48  LYS A O      1 
ATOM   181  C CB     . LYS A 1 30  ? 14.067 -6.630  -1.100  1.00 24.59 ? 48  LYS A CB     1 
ATOM   182  C CG     . LYS A 1 30  ? 13.499 -5.787  -2.229  1.00 25.61 ? 48  LYS A CG     1 
ATOM   183  C CD     . LYS A 1 30  ? 14.647 -4.988  -2.895  1.00 29.80 ? 48  LYS A CD     1 
ATOM   184  C CE     . LYS A 1 30  ? 14.155 -3.861  -3.804  1.00 34.25 ? 48  LYS A CE     1 
ATOM   185  N NZ     . LYS A 1 30  ? 13.473 -4.395  -5.016  1.00 38.81 ? 48  LYS A NZ     1 
ATOM   186  N N      . TYR A 1 31  ? 13.016 -9.451  -1.950  1.00 29.63 ? 49  TYR A N      1 
ATOM   187  C CA     . TYR A 1 31  ? 12.362 -10.313 -2.928  1.00 30.19 ? 49  TYR A CA     1 
ATOM   188  C C      . TYR A 1 31  ? 11.277 -11.170 -2.284  1.00 34.14 ? 49  TYR A C      1 
ATOM   189  O O      . TYR A 1 31  ? 10.232 -11.419 -2.901  1.00 31.64 ? 49  TYR A O      1 
ATOM   190  C CB     . TYR A 1 31  ? 13.384 -11.203 -3.632  1.00 27.71 ? 49  TYR A CB     1 
ATOM   191  C CG     . TYR A 1 31  ? 12.749 -12.367 -4.370  1.00 30.52 ? 49  TYR A CG     1 
ATOM   192  C CD1    . TYR A 1 31  ? 12.187 -12.191 -5.626  1.00 30.46 ? 49  TYR A CD1    1 
ATOM   193  C CD2    . TYR A 1 31  ? 12.712 -13.635 -3.812  1.00 29.94 ? 49  TYR A CD2    1 
ATOM   194  C CE1    . TYR A 1 31  ? 11.613 -13.234 -6.312  1.00 36.56 ? 49  TYR A CE1    1 
ATOM   195  C CE2    . TYR A 1 31  ? 12.128 -14.699 -4.488  1.00 37.41 ? 49  TYR A CE2    1 
ATOM   196  C CZ     . TYR A 1 31  ? 11.578 -14.493 -5.745  1.00 44.87 ? 49  TYR A CZ     1 
ATOM   197  O OH     . TYR A 1 31  ? 10.997 -15.538 -6.450  1.00 52.89 ? 49  TYR A OH     1 
ATOM   198  N N      . LEU A 1 32  ? 11.514 -11.664 -1.062  1.00 33.31 ? 50  LEU A N      1 
ATOM   199  C CA     . LEU A 1 32  ? 10.466 -12.412 -0.378  1.00 29.72 ? 50  LEU A CA     1 
ATOM   200  C C      . LEU A 1 32  ? 9.272  -11.536 -0.046  1.00 27.25 ? 50  LEU A C      1 
ATOM   201  O O      . LEU A 1 32  ? 8.155  -12.042 0.055   1.00 28.84 ? 50  LEU A O      1 
ATOM   202  C CB     . LEU A 1 32  ? 10.993 -13.049 0.903   1.00 24.54 ? 50  LEU A CB     1 
ATOM   203  C CG     . LEU A 1 32  ? 11.927 -14.220 0.675   1.00 27.68 ? 50  LEU A CG     1 
ATOM   204  C CD1    . LEU A 1 32  ? 12.141 -14.976 1.962   1.00 27.66 ? 50  LEU A CD1    1 
ATOM   205  C CD2    . LEU A 1 32  ? 11.350 -15.116 -0.412  1.00 33.30 ? 50  LEU A CD2    1 
ATOM   206  N N      . GLU A 1 33  ? 9.481  -10.233 0.144   1.00 28.55 ? 51  GLU A N      1 
ATOM   207  C CA     . GLU A 1 33  ? 8.372  -9.382  0.557   1.00 37.84 ? 51  GLU A CA     1 
ATOM   208  C C      . GLU A 1 33  ? 7.529  -8.935  -0.628  1.00 37.25 ? 51  GLU A C      1 
ATOM   209  O O      . GLU A 1 33  ? 6.317  -8.739  -0.482  1.00 47.33 ? 51  GLU A O      1 
ATOM   210  C CB     . GLU A 1 33  ? 8.886  -8.166  1.332   1.00 39.26 ? 51  GLU A CB     1 
ATOM   211  C CG     . GLU A 1 33  ? 7.776  -7.209  1.789   1.00 47.28 ? 51  GLU A CG     1 
ATOM   212  C CD     . GLU A 1 33  ? 8.304  -5.892  2.335   1.00 59.09 ? 51  GLU A CD     1 
ATOM   213  O OE1    . GLU A 1 33  ? 9.488  -5.567  2.091   1.00 56.28 ? 51  GLU A OE1    1 
ATOM   214  O OE2    . GLU A 1 33  ? 7.531  -5.183  3.017   1.00 61.28 ? 51  GLU A OE2    1 
ATOM   215  N N      . LYS A 1 34  ? 8.144  -8.762  -1.794  1.00 32.10 ? 52  LYS A N      1 
ATOM   216  C CA     . LYS A 1 34  ? 7.375  -8.428  -2.985  1.00 35.57 ? 52  LYS A CA     1 
ATOM   217  C C      . LYS A 1 34  ? 6.556  -9.628  -3.432  1.00 38.64 ? 52  LYS A C      1 
ATOM   218  O O      . LYS A 1 34  ? 5.325  -9.561  -3.546  1.00 46.83 ? 52  LYS A O      1 
ATOM   219  C CB     . LYS A 1 34  ? 8.324  -7.964  -4.099  1.00 33.14 ? 52  LYS A CB     1 
ATOM   220  C CG     . LYS A 1 34  ? 7.705  -7.095  -5.197  1.00 42.81 ? 52  LYS A CG     1 
ATOM   221  C CD     . LYS A 1 34  ? 7.280  -5.737  -4.668  1.00 54.25 ? 52  LYS A CD     1 
ATOM   222  C CE     . LYS A 1 34  ? 6.533  -4.929  -5.719  1.00 51.81 ? 52  LYS A CE     1 
ATOM   223  N NZ     . LYS A 1 34  ? 6.037  -3.672  -5.105  1.00 60.12 ? 52  LYS A NZ     1 
ATOM   224  N N      . SER A 1 35  ? 7.230  -10.746 -3.666  1.00 42.48 ? 53  SER A N      1 
ATOM   225  C CA     . SER A 1 35  ? 6.575  -11.876 -4.306  1.00 48.60 ? 53  SER A CA     1 
ATOM   226  C C      . SER A 1 35  ? 5.484  -12.460 -3.408  1.00 52.89 ? 53  SER A C      1 
ATOM   227  O O      . SER A 1 35  ? 4.334  -12.616 -3.839  1.00 53.99 ? 53  SER A O      1 
ATOM   228  C CB     . SER A 1 35  ? 7.625  -12.920 -4.686  1.00 40.16 ? 53  SER A CB     1 
ATOM   229  O OG     . SER A 1 35  ? 8.334  -13.309 -3.531  1.00 42.15 ? 53  SER A OG     1 
ATOM   230  N N      . LEU A 1 36  ? 5.816  -12.764 -2.148  1.00 48.58 ? 54  LEU A N      1 
ATOM   231  C CA     . LEU A 1 36  ? 4.809  -13.319 -1.242  1.00 53.93 ? 54  LEU A CA     1 
ATOM   232  C C      . LEU A 1 36  ? 3.680  -12.332 -0.977  1.00 64.72 ? 54  LEU A C      1 
ATOM   233  O O      . LEU A 1 36  ? 2.547  -12.745 -0.696  1.00 68.43 ? 54  LEU A O      1 
ATOM   234  C CB     . LEU A 1 36  ? 5.435  -13.738 0.094   1.00 47.94 ? 54  LEU A CB     1 
ATOM   235  C CG     . LEU A 1 36  ? 6.415  -14.910 0.045   1.00 48.06 ? 54  LEU A CG     1 
ATOM   236  C CD1    . LEU A 1 36  ? 6.802  -15.395 1.441   1.00 42.72 ? 54  LEU A CD1    1 
ATOM   237  C CD2    . LEU A 1 36  ? 5.810  -16.035 -0.779  1.00 52.85 ? 54  LEU A CD2    1 
ATOM   238  N N      . GLY A 1 37  ? 3.958  -11.037 -1.071  1.00 60.92 ? 55  GLY A N      1 
ATOM   239  C CA     . GLY A 1 37  ? 3.016  -10.064 -0.568  1.00 65.38 ? 55  GLY A CA     1 
ATOM   240  C C      . GLY A 1 37  ? 2.892  -10.141 0.951   1.00 63.40 ? 55  GLY A C      1 
ATOM   241  O O      . GLY A 1 37  ? 3.662  -10.821 1.655   1.00 51.32 ? 55  GLY A O      1 
ATOM   242  N N      . LYS A 1 38  ? 1.882  -9.428  1.446   1.00 64.18 ? 56  LYS A N      1 
ATOM   243  C CA     . LYS A 1 38  ? 1.649  -9.288  2.883   1.00 65.80 ? 56  LYS A CA     1 
ATOM   244  C C      . LYS A 1 38  ? 0.616  -10.290 3.394   1.00 63.19 ? 56  LYS A C      1 
ATOM   245  O O      . LYS A 1 38  ? -0.351 -9.927  4.059   1.00 65.34 ? 56  LYS A O      1 
ATOM   246  C CB     . LYS A 1 38  ? 1.234  -7.854  3.205   1.00 65.64 ? 56  LYS A CB     1 
ATOM   247  C CG     . LYS A 1 38  ? 2.395  -6.843  3.233   1.00 69.07 ? 56  LYS A CG     1 
ATOM   248  C CD     . LYS A 1 38  ? 1.887  -5.401  3.152   1.00 53.75 ? 56  LYS A CD     1 
ATOM   249  C CE     . LYS A 1 38  ? 3.032  -4.411  3.222   1.00 46.05 ? 56  LYS A CE     1 
ATOM   250  N NZ     . LYS A 1 38  ? 4.183  -4.940  2.442   1.00 58.99 ? 56  LYS A NZ     1 
ATOM   251  N N      . LYS A 1 39  ? 0.884  -11.556 3.142   1.00 50.17 ? 57  LYS A N      1 
ATOM   252  C CA     . LYS A 1 39  ? 0.055  -12.569 3.716   1.00 51.32 ? 57  LYS A CA     1 
ATOM   253  C C      . LYS A 1 39  ? 0.515  -12.579 5.156   1.00 49.37 ? 57  LYS A C      1 
ATOM   254  O O      . LYS A 1 39  ? 1.690  -12.720 5.426   1.00 52.28 ? 57  LYS A O      1 
ATOM   255  C CB     . LYS A 1 39  ? 0.343  -13.880 3.017   1.00 57.11 ? 57  LYS A CB     1 
ATOM   256  C CG     . LYS A 1 39  ? 0.401  -13.754 1.508   1.00 60.76 ? 57  LYS A CG     1 
ATOM   257  C CD     . LYS A 1 39  ? 0.405  -15.096 0.795   1.00 55.93 ? 57  LYS A CD     1 
ATOM   258  C CE     . LYS A 1 39  ? -1.008 -15.622 0.602   1.00 56.81 ? 57  LYS A CE     1 
ATOM   259  N NZ     . LYS A 1 39  ? -1.101 -16.618 -0.503  1.00 47.10 ? 57  LYS A NZ     1 
ATOM   260  N N      . LYS A 1 40  ? -0.399 -12.460 6.092   1.00 51.39 ? 58  LYS A N      1 
ATOM   261  C CA     . LYS A 1 40  ? -0.057 -12.356 7.504   1.00 55.01 ? 58  LYS A CA     1 
ATOM   262  C C      . LYS A 1 40  ? 0.545  -13.560 8.173   1.00 49.97 ? 58  LYS A C      1 
ATOM   263  O O      . LYS A 1 40  ? 1.006  -13.473 9.291   1.00 48.78 ? 58  LYS A O      1 
ATOM   264  C CB     . LYS A 1 40  ? -1.280 -11.885 8.281   1.00 59.98 ? 58  LYS A CB     1 
ATOM   265  C CG     . LYS A 1 40  ? -1.685 -10.442 8.032   1.00 61.31 ? 58  LYS A CG     1 
ATOM   266  C CD     . LYS A 1 40  ? -0.778 -9.461  8.760   1.00 57.51 ? 58  LYS A CD     1 
ATOM   267  C CE     . LYS A 1 40  ? 0.212  -8.806  7.814   1.00 63.43 ? 58  LYS A CE     1 
ATOM   268  N NZ     . LYS A 1 40  ? -0.485 -8.239  6.631   1.00 55.79 ? 58  LYS A NZ     1 
ATOM   269  N N      . GLU A 1 41  ? 0.461  -14.701 7.536   1.00 49.43 ? 59  GLU A N      1 
ATOM   270  C CA     . GLU A 1 41  ? 1.081  -15.874 8.066   1.00 47.43 ? 59  GLU A CA     1 
ATOM   271  C C      . GLU A 1 41  ? 2.563  -15.639 8.169   1.00 45.23 ? 59  GLU A C      1 
ATOM   272  O O      . GLU A 1 41  ? 3.191  -16.023 9.140   1.00 47.77 ? 59  GLU A O      1 
ATOM   273  C CB     . GLU A 1 41  ? 0.779  -17.036 7.137   1.00 49.35 ? 59  GLU A CB     1 
ATOM   274  C CG     . GLU A 1 41  ? 0.874  -16.747 5.651   1.00 50.16 ? 59  GLU A CG     1 
ATOM   275  C CD     . GLU A 1 41  ? -0.473 -16.607 4.980   1.00 58.36 ? 59  GLU A CD     1 
ATOM   276  O OE1    . GLU A 1 41  ? -1.402 -16.056 5.596   1.00 66.21 ? 59  GLU A OE1    1 
ATOM   277  O OE2    . GLU A 1 41  ? -0.594 -17.032 3.818   1.00 58.93 ? 59  GLU A OE2    1 
ATOM   278  N N      . PHE A 1 42  ? 3.125  -15.005 7.166   1.00 44.33 ? 60  PHE A N      1 
ATOM   279  C CA     . PHE A 1 42  ? 4.544  -14.702 7.140   1.00 39.58 ? 60  PHE A CA     1 
ATOM   280  C C      . PHE A 1 42  ? 4.883  -13.412 7.879   1.00 36.34 ? 60  PHE A C      1 
ATOM   281  O O      . PHE A 1 42  ? 6.018  -12.943 7.805   1.00 36.03 ? 60  PHE A O      1 
ATOM   282  C CB     . PHE A 1 42  ? 5.005  -14.635 5.687   1.00 36.59 ? 60  PHE A CB     1 
ATOM   283  C CG     . PHE A 1 42  ? 4.530  -15.800 4.852   1.00 44.98 ? 60  PHE A CG     1 
ATOM   284  C CD1    . PHE A 1 42  ? 4.751  -17.108 5.271   1.00 42.96 ? 60  PHE A CD1    1 
ATOM   285  C CD2    . PHE A 1 42  ? 3.847  -15.590 3.658   1.00 44.95 ? 60  PHE A CD2    1 
ATOM   286  C CE1    . PHE A 1 42  ? 4.314  -18.189 4.506   1.00 43.39 ? 60  PHE A CE1    1 
ATOM   287  C CE2    . PHE A 1 42  ? 3.403  -16.662 2.895   1.00 48.47 ? 60  PHE A CE2    1 
ATOM   288  C CZ     . PHE A 1 42  ? 3.640  -17.964 3.318   1.00 45.36 ? 60  PHE A CZ     1 
ATOM   289  N N      . SER A 1 43  ? 3.971  -12.799 8.571   1.00 42.55 ? 61  SER A N      1 
ATOM   290  C CA     . SER A 1 43  ? 4.269  -11.581 9.258   1.00 44.10 ? 61  SER A CA     1 
ATOM   291  C C      . SER A 1 43  ? 5.430  -11.756 10.180  1.00 41.96 ? 61  SER A C      1 
ATOM   292  O O      . SER A 1 43  ? 6.277  -10.888 10.297  1.00 42.05 ? 61  SER A O      1 
ATOM   293  C CB     . SER A 1 43  ? 3.053  -11.134 10.064  1.00 48.03 ? 61  SER A CB     1 
ATOM   294  O OG     . SER A 1 43  ? 3.354  -10.023 10.882  1.00 49.69 ? 61  SER A OG     1 
ATOM   295  N N      . GLY A 1 44  ? 5.472  -12.881 10.853  1.00 43.96 ? 62  GLY A N      1 
ATOM   296  C CA     . GLY A 1 44  ? 6.513  -13.091 11.833  1.00 49.65 ? 62  GLY A CA     1 
ATOM   297  C C      . GLY A 1 44  ? 7.888  -13.336 11.294  1.00 43.46 ? 62  GLY A C      1 
ATOM   298  O O      . GLY A 1 44  ? 8.843  -12.920 11.905  1.00 42.35 ? 62  GLY A O      1 
ATOM   299  N N      . PHE A 1 45  ? 7.994  -14.052 10.193  1.00 36.23 ? 63  PHE A N      1 
ATOM   300  C CA     . PHE A 1 45  ? 9.294  -14.236 9.561   1.00 33.91 ? 63  PHE A CA     1 
ATOM   301  C C      . PHE A 1 45  ? 9.932  -12.890 9.259   1.00 35.50 ? 63  PHE A C      1 
ATOM   302  O O      . PHE A 1 45  ? 11.137 -12.699 9.457   1.00 31.99 ? 63  PHE A O      1 
ATOM   303  C CB     . PHE A 1 45  ? 9.146  -15.063 8.289   1.00 30.44 ? 63  PHE A CB     1 
ATOM   304  C CG     . PHE A 1 45  ? 10.399 -15.155 7.469   1.00 34.57 ? 63  PHE A CG     1 
ATOM   305  C CD1    . PHE A 1 45  ? 11.371 -16.096 7.768   1.00 32.78 ? 63  PHE A CD1    1 
ATOM   306  C CD2    . PHE A 1 45  ? 10.588 -14.320 6.371   1.00 35.45 ? 63  PHE A CD2    1 
ATOM   307  C CE1    . PHE A 1 45  ? 12.520 -16.193 7.000   1.00 32.39 ? 63  PHE A CE1    1 
ATOM   308  C CE2    . PHE A 1 45  ? 11.732 -14.413 5.595   1.00 30.73 ? 63  PHE A CE2    1 
ATOM   309  C CZ     . PHE A 1 45  ? 12.700 -15.356 5.912   1.00 31.70 ? 63  PHE A CZ     1 
ATOM   310  N N      . PHE A 1 46  ? 9.130  -11.935 8.805   1.00 37.05 ? 64  PHE A N      1 
ATOM   311  C CA     . PHE A 1 46  ? 9.696  -10.651 8.430   1.00 33.72 ? 64  PHE A CA     1 
ATOM   312  C C      . PHE A 1 46  ? 10.102 -9.857  9.654   1.00 29.17 ? 64  PHE A C      1 
ATOM   313  O O      . PHE A 1 46  ? 11.185 -9.271  9.680   1.00 33.10 ? 64  PHE A O      1 
ATOM   314  C CB     . PHE A 1 46  ? 8.703  -9.879  7.575   1.00 35.26 ? 64  PHE A CB     1 
ATOM   315  C CG     . PHE A 1 46  ? 8.568  -10.419 6.205   1.00 23.18 ? 64  PHE A CG     1 
ATOM   316  C CD1    . PHE A 1 46  ? 9.688  -10.719 5.459   1.00 31.95 ? 64  PHE A CD1    1 
ATOM   317  C CD2    . PHE A 1 46  ? 7.334  -10.636 5.665   1.00 25.05 ? 64  PHE A CD2    1 
ATOM   318  C CE1    . PHE A 1 46  ? 9.571  -11.216 4.183   1.00 37.41 ? 64  PHE A CE1    1 
ATOM   319  C CE2    . PHE A 1 46  ? 7.208  -11.137 4.396   1.00 32.64 ? 64  PHE A CE2    1 
ATOM   320  C CZ     . PHE A 1 46  ? 8.322  -11.430 3.654   1.00 32.93 ? 64  PHE A CZ     1 
ATOM   321  N N      . GLU A 1 47  ? 9.260  -9.842  10.683  1.00 34.63 ? 65  GLU A N      1 
ATOM   322  C CA     . GLU A 1 47  ? 9.631  -9.153  11.911  1.00 30.48 ? 65  GLU A CA     1 
ATOM   323  C C      . GLU A 1 47  ? 10.894 -9.767  12.515  1.00 37.74 ? 65  GLU A C      1 
ATOM   324  O O      . GLU A 1 47  ? 11.791 -9.047  12.978  1.00 34.99 ? 65  GLU A O      1 
ATOM   325  C CB     . GLU A 1 47  ? 8.462  -9.195  12.897  1.00 33.65 ? 65  GLU A CB     1 
ATOM   326  C CG     . GLU A 1 47  ? 8.562  -8.179  14.033  1.00 54.05 ? 65  GLU A CG     1 
ATOM   327  C CD     . GLU A 1 47  ? 7.605  -8.467  15.192  1.00 57.14 ? 65  GLU A CD     1 
ATOM   328  O OE1    . GLU A 1 47  ? 6.963  -9.538  15.196  1.00 65.82 ? 65  GLU A OE1    1 
ATOM   329  O OE2    . GLU A 1 47  ? 7.501  -7.621  16.107  1.00 55.47 ? 65  GLU A OE2    1 
ATOM   330  N N      . ASP A 1 48  ? 10.999 -11.102 12.475  1.00 37.45 ? 66  ASP A N      1 
ATOM   331  C CA     . ASP A 1 48  ? 12.109 -11.802 13.115  1.00 26.27 ? 66  ASP A CA     1 
ATOM   332  C C      . ASP A 1 48  ? 13.421 -11.555 12.375  1.00 32.07 ? 66  ASP A C      1 
ATOM   333  O O      . ASP A 1 48  ? 14.457 -11.296 13.001  1.00 29.03 ? 66  ASP A O      1 
ATOM   334  C CB     . ASP A 1 48  ? 11.794 -13.298 13.190  1.00 32.08 ? 66  ASP A CB     1 
ATOM   335  C CG     . ASP A 1 48  ? 12.724 -14.064 14.128  1.00 46.23 ? 66  ASP A CG     1 
ATOM   336  O OD1    . ASP A 1 48  ? 13.183 -13.510 15.158  1.00 54.49 ? 66  ASP A OD1    1 
ATOM   337  O OD2    . ASP A 1 48  ? 12.984 -15.248 13.833  1.00 40.33 ? 66  ASP A OD2    1 
ATOM   338  N N      . ILE A 1 49  ? 13.402 -11.631 11.041  1.00 33.89 ? 67  ILE A N      1 
ATOM   339  C CA     . ILE A 1 49  ? 14.620 -11.391 10.272  1.00 26.06 ? 67  ILE A CA     1 
ATOM   340  C C      . ILE A 1 49  ? 15.186 -10.011 10.585  1.00 28.13 ? 67  ILE A C      1 
ATOM   341  O O      . ILE A 1 49  ? 16.408 -9.829  10.699  1.00 24.37 ? 67  ILE A O      1 
ATOM   342  C CB     . ILE A 1 49  ? 14.352 -11.550 8.768   1.00 21.57 ? 67  ILE A CB     1 
ATOM   343  C CG1    . ILE A 1 49  ? 14.218 -13.026 8.401   1.00 28.42 ? 67  ILE A CG1    1 
ATOM   344  C CG2    . ILE A 1 49  ? 15.491 -10.925 7.994   1.00 19.37 ? 67  ILE A CG2    1 
ATOM   345  C CD1    . ILE A 1 49  ? 15.534 -13.812 8.408   1.00 30.51 ? 67  ILE A CD1    1 
ATOM   346  N N      . GLU A 1 50  ? 14.313 -9.017  10.725  1.00 23.16 ? 68  GLU A N      1 
ATOM   347  C CA     . GLU A 1 50  ? 14.797 -7.662  10.946  1.00 26.55 ? 68  GLU A CA     1 
ATOM   348  C C      . GLU A 1 50  ? 15.441 -7.533  12.320  1.00 26.25 ? 68  GLU A C      1 
ATOM   349  O O      . GLU A 1 50  ? 16.437 -6.818  12.489  1.00 24.10 ? 68  GLU A O      1 
ATOM   350  C CB     . GLU A 1 50  ? 13.645 -6.672  10.767  1.00 27.89 ? 68  GLU A CB     1 
ATOM   351  C CG     . GLU A 1 50  ? 13.073 -6.700  9.362   1.00 24.27 ? 68  GLU A CG     1 
ATOM   352  C CD     . GLU A 1 50  ? 12.072 -5.584  9.102   1.00 37.08 ? 68  GLU A CD     1 
ATOM   353  O OE1    . GLU A 1 50  ? 12.228 -4.474  9.685   1.00 37.97 ? 68  GLU A OE1    1 
ATOM   354  O OE2    . GLU A 1 50  ? 11.136 -5.816  8.297   1.00 37.13 ? 68  GLU A OE2    1 
ATOM   355  N N      . LYS A 1 51  ? 14.879 -8.217  13.316  1.00 27.17 ? 69  LYS A N      1 
ATOM   356  C CA     . LYS A 1 51  ? 15.512 -8.241  14.629  1.00 24.96 ? 69  LYS A CA     1 
ATOM   357  C C      . LYS A 1 51  ? 16.870 -8.933  14.573  1.00 21.76 ? 69  LYS A C      1 
ATOM   358  O O      . LYS A 1 51  ? 17.855 -8.423  15.121  1.00 22.79 ? 69  LYS A O      1 
ATOM   359  C CB     . LYS A 1 51  ? 14.582 -8.909  15.652  1.00 29.55 ? 69  LYS A CB     1 
ATOM   360  C CG     . LYS A 1 51  ? 13.724 -7.911  16.450  1.00 30.84 ? 69  LYS A CG     1 
ATOM   361  C CD     . LYS A 1 51  ? 12.247 -8.274  16.454  1.00 29.40 ? 69  LYS A CD     1 
ATOM   362  C CE     . LYS A 1 51  ? 11.998 -9.594  17.160  1.00 45.29 ? 69  LYS A CE     1 
ATOM   363  N NZ     . LYS A 1 51  ? 10.602 -10.103 16.931  1.00 61.04 ? 69  LYS A NZ     1 
ATOM   364  N N      . LEU A 1 52  ? 16.950 -10.088 13.908  1.00 20.29 ? 70  LEU A N      1 
ATOM   365  C CA     . LEU A 1 52  ? 18.234 -10.766 13.784  1.00 13.90 ? 70  LEU A CA     1 
ATOM   366  C C      . LEU A 1 52  ? 19.248 -9.884  13.075  1.00 16.81 ? 70  LEU A C      1 
ATOM   367  O O      . LEU A 1 52  ? 20.427 -9.864  13.442  1.00 20.18 ? 70  LEU A O      1 
ATOM   368  C CB     . LEU A 1 52  ? 18.075 -12.087 13.034  1.00 17.98 ? 70  LEU A CB     1 
ATOM   369  C CG     . LEU A 1 52  ? 17.334 -13.273 13.663  1.00 22.13 ? 70  LEU A CG     1 
ATOM   370  C CD1    . LEU A 1 52  ? 17.332 -14.445 12.685  1.00 20.49 ? 70  LEU A CD1    1 
ATOM   371  C CD2    . LEU A 1 52  ? 17.915 -13.682 15.019  1.00 19.32 ? 70  LEU A CD2    1 
ATOM   372  N N      . TYR A 1 53  ? 18.808 -9.140  12.059  1.00 19.58 ? 71  TYR A N      1 
ATOM   373  C CA     . TYR A 1 53  ? 19.715 -8.266  11.320  1.00 15.90 ? 71  TYR A CA     1 
ATOM   374  C C      . TYR A 1 53  ? 20.321 -7.211  12.233  1.00 16.10 ? 71  TYR A C      1 
ATOM   375  O O      . TYR A 1 53  ? 21.545 -7.066  12.313  1.00 16.27 ? 71  TYR A O      1 
ATOM   376  C CB     . TYR A 1 53  ? 18.979 -7.614  10.148  1.00 19.03 ? 71  TYR A CB     1 
ATOM   377  C CG     . TYR A 1 53  ? 19.842 -6.689  9.319   1.00 18.35 ? 71  TYR A CG     1 
ATOM   378  C CD1    . TYR A 1 53  ? 20.706 -7.204  8.364   1.00 15.15 ? 71  TYR A CD1    1 
ATOM   379  C CD2    . TYR A 1 53  ? 19.786 -5.300  9.483   1.00 16.24 ? 71  TYR A CD2    1 
ATOM   380  C CE1    . TYR A 1 53  ? 21.488 -6.383  7.603   1.00 13.52 ? 71  TYR A CE1    1 
ATOM   381  C CE2    . TYR A 1 53  ? 20.579 -4.469  8.727   1.00 13.64 ? 71  TYR A CE2    1 
ATOM   382  C CZ     . TYR A 1 53  ? 21.431 -5.023  7.787   1.00 12.92 ? 71  TYR A CZ     1 
ATOM   383  O OH     . TYR A 1 53  ? 22.248 -4.235  7.015   1.00 12.99 ? 71  TYR A OH     1 
ATOM   384  N N      . PHE A 1 54  ? 19.472 -6.463  12.938  1.00 16.32 ? 72  PHE A N      1 
ATOM   385  C CA     . PHE A 1 54  ? 19.983 -5.459  13.858  1.00 14.37 ? 72  PHE A CA     1 
ATOM   386  C C      . PHE A 1 54  ? 21.058 -6.028  14.772  1.00 17.29 ? 72  PHE A C      1 
ATOM   387  O O      . PHE A 1 54  ? 22.081 -5.374  15.020  1.00 21.07 ? 72  PHE A O      1 
ATOM   388  C CB     . PHE A 1 54  ? 18.856 -4.880  14.693  1.00 14.45 ? 72  PHE A CB     1 
ATOM   389  C CG     . PHE A 1 54  ? 19.301 -3.789  15.608  1.00 13.47 ? 72  PHE A CG     1 
ATOM   390  C CD1    . PHE A 1 54  ? 19.557 -2.520  15.127  1.00 12.65 ? 72  PHE A CD1    1 
ATOM   391  C CD2    . PHE A 1 54  ? 19.466 -4.038  16.951  1.00 9.53  ? 72  PHE A CD2    1 
ATOM   392  C CE1    . PHE A 1 54  ? 19.950 -1.520  15.985  1.00 14.16 ? 72  PHE A CE1    1 
ATOM   393  C CE2    . PHE A 1 54  ? 19.855 -3.059  17.815  1.00 7.97  ? 72  PHE A CE2    1 
ATOM   394  C CZ     . PHE A 1 54  ? 20.098 -1.796  17.347  1.00 15.69 ? 72  PHE A CZ     1 
ATOM   395  N N      . LYS A 1 55  ? 20.857 -7.243  15.284  1.00 14.38 ? 73  LYS A N      1 
ATOM   396  C CA     . LYS A 1 55  ? 21.818 -7.795  16.229  1.00 18.28 ? 73  LYS A CA     1 
ATOM   397  C C      . LYS A 1 55  ? 22.977 -8.505  15.546  1.00 18.70 ? 73  LYS A C      1 
ATOM   398  O O      . LYS A 1 55  ? 23.812 -9.117  16.218  1.00 18.80 ? 73  LYS A O      1 
ATOM   399  C CB     . LYS A 1 55  ? 21.111 -8.709  17.233  1.00 17.23 ? 73  LYS A CB     1 
ATOM   400  C CG     . LYS A 1 55  ? 20.186 -7.900  18.170  1.00 16.59 ? 73  LYS A CG     1 
ATOM   401  C CD     . LYS A 1 55  ? 19.703 -8.675  19.384  1.00 13.44 ? 73  LYS A CD     1 
ATOM   402  C CE     . LYS A 1 55  ? 18.856 -7.754  20.239  1.00 17.59 ? 73  LYS A CE     1 
ATOM   403  N NZ     . LYS A 1 55  ? 18.414 -8.306  21.552  1.00 23.65 ? 73  LYS A NZ     1 
ATOM   404  N N      . GLN A 1 56  ? 23.093 -8.380  14.236  1.00 18.39 ? 74  GLN A N      1 
ATOM   405  C CA     . GLN A 1 56  ? 24.273 -8.892  13.563  1.00 19.80 ? 74  GLN A CA     1 
ATOM   406  C C      . GLN A 1 56  ? 24.379 -10.404 13.693  1.00 20.90 ? 74  GLN A C      1 
ATOM   407  O O      . GLN A 1 56  ? 25.474 -10.964 13.637  1.00 25.95 ? 74  GLN A O      1 
ATOM   408  C CB     . GLN A 1 56  ? 25.537 -8.230  14.102  1.00 17.41 ? 74  GLN A CB     1 
ATOM   409  C CG     . GLN A 1 56  ? 25.854 -6.901  13.431  1.00 20.52 ? 74  GLN A CG     1 
ATOM   410  C CD     . GLN A 1 56  ? 26.776 -6.042  14.283  1.00 21.13 ? 74  GLN A CD     1 
ATOM   411  O OE1    . GLN A 1 56  ? 27.971 -5.911  14.010  1.00 17.61 ? 74  GLN A OE1    1 
ATOM   412  N NE2    . GLN A 1 56  ? 26.220 -5.476  15.347  1.00 27.69 ? 74  GLN A NE2    1 
ATOM   413  N N      . ASN A 1 57  ? 23.242 -11.069 13.878  1.00 16.19 ? 75  ASN A N      1 
ATOM   414  C CA     . ASN A 1 57  ? 23.189 -12.525 13.821  1.00 21.88 ? 75  ASN A CA     1 
ATOM   415  C C      . ASN A 1 57  ? 22.848 -12.944 12.390  1.00 21.17 ? 75  ASN A C      1 
ATOM   416  O O      . ASN A 1 57  ? 21.768 -13.452 12.080  1.00 21.36 ? 75  ASN A O      1 
ATOM   417  C CB     . ASN A 1 57  ? 22.197 -13.061 14.850  1.00 22.06 ? 75  ASN A CB     1 
ATOM   418  C CG     . ASN A 1 57  ? 22.650 -12.788 16.280  1.00 24.86 ? 75  ASN A CG     1 
ATOM   419  O OD1    . ASN A 1 57  ? 23.850 -12.828 16.573  1.00 28.52 ? 75  ASN A OD1    1 
ATOM   420  N ND2    . ASN A 1 57  ? 21.702 -12.497 17.171  1.00 22.35 ? 75  ASN A ND2    1 
ATOM   421  N N      . TYR A 1 58  ? 23.810 -12.694 11.498  1.00 19.92 ? 76  TYR A N      1 
ATOM   422  C CA     . TYR A 1 58  ? 23.571 -12.961 10.084  1.00 17.42 ? 76  TYR A CA     1 
ATOM   423  C C      . TYR A 1 58  ? 23.458 -14.453 9.808   1.00 19.33 ? 76  TYR A C      1 
ATOM   424  O O      . TYR A 1 58  ? 22.646 -14.874 8.974   1.00 25.50 ? 76  TYR A O      1 
ATOM   425  C CB     . TYR A 1 58  ? 24.677 -12.360 9.225   1.00 16.09 ? 76  TYR A CB     1 
ATOM   426  C CG     . TYR A 1 58  ? 24.802 -10.855 9.294   1.00 23.15 ? 76  TYR A CG     1 
ATOM   427  C CD1    . TYR A 1 58  ? 23.819 -10.070 9.892   1.00 21.56 ? 76  TYR A CD1    1 
ATOM   428  C CD2    . TYR A 1 58  ? 25.905 -10.210 8.735   1.00 18.59 ? 76  TYR A CD2    1 
ATOM   429  C CE1    . TYR A 1 58  ? 23.938 -8.689  9.934   1.00 16.19 ? 76  TYR A CE1    1 
ATOM   430  C CE2    . TYR A 1 58  ? 26.029 -8.831  8.783   1.00 18.21 ? 76  TYR A CE2    1 
ATOM   431  C CZ     . TYR A 1 58  ? 25.043 -8.079  9.381   1.00 18.42 ? 76  TYR A CZ     1 
ATOM   432  O OH     . TYR A 1 58  ? 25.167 -6.706  9.424   1.00 18.28 ? 76  TYR A OH     1 
ATOM   433  N N      . LYS A 1 59  ? 24.275 -15.263 10.483  1.00 16.92 ? 77  LYS A N      1 
ATOM   434  C CA     . LYS A 1 59  ? 24.263 -16.702 10.237  1.00 24.03 ? 77  LYS A CA     1 
ATOM   435  C C      . LYS A 1 59  ? 22.884 -17.301 10.501  1.00 24.21 ? 77  LYS A C      1 
ATOM   436  O O      . LYS A 1 59  ? 22.389 -18.106 9.703   1.00 23.79 ? 77  LYS A O      1 
ATOM   437  C CB     . LYS A 1 59  ? 25.343 -17.382 11.082  1.00 26.29 ? 77  LYS A CB     1 
ATOM   438  C CG     . LYS A 1 59  ? 26.495 -17.976 10.248  1.00 37.19 ? 77  LYS A CG     1 
ATOM   439  C CD     . LYS A 1 59  ? 26.209 -19.412 9.751   1.00 45.61 ? 77  LYS A CD     1 
ATOM   440  C CE     . LYS A 1 59  ? 26.724 -20.506 10.716  1.00 37.30 ? 77  LYS A CE     1 
ATOM   441  N NZ     . LYS A 1 59  ? 26.095 -20.434 12.073  1.00 28.40 ? 77  LYS A NZ     1 
ATOM   442  N N      . GLU A 1 60  ? 22.235 -16.892 11.596  1.00 20.99 ? 78  GLU A N      1 
ATOM   443  C CA     . GLU A 1 60  ? 20.879 -17.348 11.879  1.00 17.98 ? 78  GLU A CA     1 
ATOM   444  C C      . GLU A 1 60  ? 19.877 -16.852 10.847  1.00 26.53 ? 78  GLU A C      1 
ATOM   445  O O      . GLU A 1 60  ? 18.930 -17.574 10.507  1.00 30.44 ? 78  GLU A O      1 
ATOM   446  C CB     . GLU A 1 60  ? 20.452 -16.889 13.267  1.00 23.45 ? 78  GLU A CB     1 
ATOM   447  C CG     . GLU A 1 60  ? 19.237 -17.606 13.797  1.00 23.50 ? 78  GLU A CG     1 
ATOM   448  C CD     . GLU A 1 60  ? 18.959 -17.296 15.256  1.00 36.07 ? 78  GLU A CD     1 
ATOM   449  O OE1    . GLU A 1 60  ? 19.891 -16.892 15.996  1.00 38.05 ? 78  GLU A OE1    1 
ATOM   450  O OE2    . GLU A 1 60  ? 17.792 -17.471 15.663  1.00 31.95 ? 78  GLU A OE2    1 
ATOM   451  N N      . ALA A 1 61  ? 20.058 -15.635 10.336  1.00 26.92 ? 79  ALA A N      1 
ATOM   452  C CA     . ALA A 1 61  ? 19.089 -15.099 9.386   1.00 27.11 ? 79  ALA A CA     1 
ATOM   453  C C      . ALA A 1 61  ? 19.240 -15.725 8.001   1.00 25.32 ? 79  ALA A C      1 
ATOM   454  O O      . ALA A 1 61  ? 18.241 -16.063 7.358   1.00 24.67 ? 79  ALA A O      1 
ATOM   455  C CB     . ALA A 1 61  ? 19.215 -13.581 9.312   1.00 23.28 ? 79  ALA A CB     1 
ATOM   456  N N      . ILE A 1 62  ? 20.473 -15.867 7.507   1.00 20.92 ? 80  ILE A N      1 
ATOM   457  C CA     . ILE A 1 62  ? 20.657 -16.512 6.209   1.00 26.21 ? 80  ILE A CA     1 
ATOM   458  C C      . ILE A 1 62  ? 20.090 -17.920 6.235   1.00 28.04 ? 80  ILE A C      1 
ATOM   459  O O      . ILE A 1 62  ? 19.466 -18.387 5.272   1.00 25.85 ? 80  ILE A O      1 
ATOM   460  C CB     . ILE A 1 62  ? 22.140 -16.534 5.817   1.00 25.16 ? 80  ILE A CB     1 
ATOM   461  C CG1    . ILE A 1 62  ? 22.688 -15.124 5.702   1.00 24.67 ? 80  ILE A CG1    1 
ATOM   462  C CG2    . ILE A 1 62  ? 22.314 -17.310 4.520   1.00 20.16 ? 80  ILE A CG2    1 
ATOM   463  C CD1    . ILE A 1 62  ? 24.177 -15.132 5.506   1.00 20.80 ? 80  ILE A CD1    1 
ATOM   464  N N      . GLU A 1 63  ? 20.323 -18.627 7.330   1.00 23.72 ? 81  GLU A N      1 
ATOM   465  C CA     . GLU A 1 63  ? 19.765 -19.954 7.484   1.00 26.42 ? 81  GLU A CA     1 
ATOM   466  C C      . GLU A 1 63  ? 18.238 -19.899 7.519   1.00 27.54 ? 81  GLU A C      1 
ATOM   467  O O      . GLU A 1 63  ? 17.560 -20.579 6.737   1.00 32.14 ? 81  GLU A O      1 
ATOM   468  C CB     . GLU A 1 63  ? 20.371 -20.574 8.737   1.00 30.71 ? 81  GLU A CB     1 
ATOM   469  C CG     . GLU A 1 63  ? 19.722 -21.807 9.272   1.00 34.65 ? 81  GLU A CG     1 
ATOM   470  C CD     . GLU A 1 63  ? 20.369 -22.181 10.581  1.00 48.63 ? 81  GLU A CD     1 
ATOM   471  O OE1    . GLU A 1 63  ? 21.544 -21.789 10.767  1.00 48.60 ? 81  GLU A OE1    1 
ATOM   472  O OE2    . GLU A 1 63  ? 19.719 -22.834 11.428  1.00 63.68 ? 81  GLU A OE2    1 
ATOM   473  N N      . LYS A 1 64  ? 17.663 -19.078 8.366   1.00 22.96 ? 82  LYS A N      1 
ATOM   474  C CA     . LYS A 1 64  ? 16.221 -18.923 8.392   1.00 24.36 ? 82  LYS A CA     1 
ATOM   475  C C      . LYS A 1 64  ? 15.656 -18.527 7.040   1.00 29.87 ? 82  LYS A C      1 
ATOM   476  O O      . LYS A 1 64  ? 14.645 -19.049 6.633   1.00 29.87 ? 82  LYS A O      1 
ATOM   477  C CB     . LYS A 1 64  ? 15.832 -17.911 9.453   1.00 23.27 ? 82  LYS A CB     1 
ATOM   478  C CG     . LYS A 1 64  ? 15.829 -18.381 10.887  1.00 25.72 ? 82  LYS A CG     1 
ATOM   479  C CD     . LYS A 1 64  ? 14.948 -17.440 11.681  1.00 30.26 ? 82  LYS A CD     1 
ATOM   480  C CE     . LYS A 1 64  ? 13.611 -17.290 10.971  1.00 39.99 ? 82  LYS A CE     1 
ATOM   481  N NZ     . LYS A 1 64  ? 12.962 -15.966 11.151  1.00 30.95 ? 82  LYS A NZ     1 
ATOM   482  N N      . ILE A 1 65  ? 16.271 -17.579 6.359   1.00 31.53 ? 83  ILE A N      1 
ATOM   483  C CA     . ILE A 1 65  ? 15.878 -17.196 4.996   1.00 32.06 ? 83  ILE A CA     1 
ATOM   484  C C      . ILE A 1 65  ? 15.899 -18.401 4.058   1.00 32.22 ? 83  ILE A C      1 
ATOM   485  O O      . ILE A 1 65  ? 14.965 -18.619 3.275   1.00 30.57 ? 83  ILE A O      1 
ATOM   486  C CB     . ILE A 1 65  ? 16.802 -16.082 4.459   1.00 28.67 ? 83  ILE A CB     1 
ATOM   487  C CG1    . ILE A 1 65  ? 16.666 -14.793 5.263   1.00 30.31 ? 83  ILE A CG1    1 
ATOM   488  C CG2    . ILE A 1 65  ? 16.529 -15.823 2.981   1.00 22.30 ? 83  ILE A CG2    1 
ATOM   489  C CD1    . ILE A 1 65  ? 17.551 -13.667 4.706   1.00 21.72 ? 83  ILE A CD1    1 
ATOM   490  N N      . LEU A 1 66  ? 16.961 -19.168 4.045   1.00 25.87 ? 84  LEU A N      1 
ATOM   491  C CA     . LEU A 1 66  ? 17.016 -20.297 3.158   1.00 30.36 ? 84  LEU A CA     1 
ATOM   492  C C      . LEU A 1 66  ? 16.022 -21.392 3.587   1.00 38.99 ? 84  LEU A C      1 
ATOM   493  O O      . LEU A 1 66  ? 15.467 -22.052 2.732   1.00 35.21 ? 84  LEU A O      1 
ATOM   494  C CB     . LEU A 1 66  ? 18.462 -20.766 3.026   1.00 26.35 ? 84  LEU A CB     1 
ATOM   495  C CG     . LEU A 1 66  ? 19.437 -19.828 2.324   1.00 19.88 ? 84  LEU A CG     1 
ATOM   496  C CD1    . LEU A 1 66  ? 20.829 -20.411 2.395   1.00 17.34 ? 84  LEU A CD1    1 
ATOM   497  C CD2    . LEU A 1 66  ? 19.031 -19.557 0.890   1.00 20.94 ? 84  LEU A CD2    1 
ATOM   498  N N      . ASP A 1 67  ? 15.784 -21.578 4.889   1.00 38.19 ? 85  ASP A N      1 
ATOM   499  C CA     . ASP A 1 67  ? 14.760 -22.503 5.380   1.00 40.90 ? 85  ASP A CA     1 
ATOM   500  C C      . ASP A 1 67  ? 13.356 -21.925 5.323   1.00 35.56 ? 85  ASP A C      1 
ATOM   501  O O      . ASP A 1 67  ? 12.436 -22.409 5.990   1.00 50.07 ? 85  ASP A O      1 
ATOM   502  C CB     . ASP A 1 67  ? 15.079 -22.947 6.809   1.00 43.68 ? 85  ASP A CB     1 
ATOM   503  C CG     . ASP A 1 67  ? 16.190 -23.992 6.847   1.00 55.79 ? 85  ASP A CG     1 
ATOM   504  O OD1    . ASP A 1 67  ? 16.287 -24.775 5.868   1.00 60.00 ? 85  ASP A OD1    1 
ATOM   505  O OD2    . ASP A 1 67  ? 16.972 -24.023 7.833   1.00 55.99 ? 85  ASP A OD2    1 
ATOM   506  N N      . PHE A 1 68  ? 13.177 -20.877 4.567   1.00 32.51 ? 86  PHE A N      1 
ATOM   507  C CA     . PHE A 1 68  ? 11.882 -20.302 4.275   1.00 31.26 ? 86  PHE A CA     1 
ATOM   508  C C      . PHE A 1 68  ? 11.620 -20.295 2.794   1.00 37.53 ? 86  PHE A C      1 
ATOM   509  O O      . PHE A 1 68  ? 10.479 -20.504 2.378   1.00 36.71 ? 86  PHE A O      1 
ATOM   510  C CB     . PHE A 1 68  ? 11.838 -18.876 4.835   1.00 30.56 ? 86  PHE A CB     1 
ATOM   511  C CG     . PHE A 1 68  ? 10.564 -18.129 4.595   1.00 27.78 ? 86  PHE A CG     1 
ATOM   512  C CD1    . PHE A 1 68  ? 10.332 -17.493 3.392   1.00 25.84 ? 86  PHE A CD1    1 
ATOM   513  C CD2    . PHE A 1 68  ? 9.631  -17.987 5.611   1.00 32.58 ? 86  PHE A CD2    1 
ATOM   514  C CE1    . PHE A 1 68  ? 9.170  -16.766 3.185   1.00 28.97 ? 86  PHE A CE1    1 
ATOM   515  C CE2    . PHE A 1 68  ? 8.457  -17.252 5.410   1.00 33.10 ? 86  PHE A CE2    1 
ATOM   516  C CZ     . PHE A 1 68  ? 8.232  -16.642 4.199   1.00 30.78 ? 86  PHE A CZ     1 
ATOM   517  N N      . CYS A 1 69  ? 12.678 -20.119 1.994   1.00 41.11 ? 87  CYS A N      1 
ATOM   518  C CA     . CYS A 1 69  ? 12.589 -20.182 0.542   1.00 41.83 ? 87  CYS A CA     1 
ATOM   519  C C      . CYS A 1 69  ? 12.354 -21.593 0.035   1.00 44.26 ? 87  CYS A C      1 
ATOM   520  O O      . CYS A 1 69  ? 11.818 -21.770 -1.065  1.00 48.41 ? 87  CYS A O      1 
ATOM   521  C CB     . CYS A 1 69  ? 13.867 -19.645 -0.080  1.00 37.70 ? 87  CYS A CB     1 
ATOM   522  S SG     . CYS A 1 69  ? 14.044 -17.932 0.158   1.00 46.36 ? 87  CYS A SG     1 
ATOM   523  N N      . LYS A 1 70  ? 12.720 -22.598 0.799   1.00 39.56 ? 88  LYS A N      1 
ATOM   524  C CA     . LYS A 1 70  ? 12.468 -23.936 0.358   1.00 45.26 ? 88  LYS A CA     1 
ATOM   525  C C      . LYS A 1 70  ? 11.107 -24.373 0.807   1.00 47.14 ? 88  LYS A C      1 
ATOM   526  O O      . LYS A 1 70  ? 10.446 -25.145 0.140   1.00 51.81 ? 88  LYS A O      1 
ATOM   527  C CB     . LYS A 1 70  ? 13.543 -24.884 0.851   1.00 47.23 ? 88  LYS A CB     1 
ATOM   528  C CG     . LYS A 1 70  ? 14.963 -24.440 0.566   1.00 50.56 ? 88  LYS A CG     1 
ATOM   529  C CD     . LYS A 1 70  ? 15.432 -24.857 -0.812  1.00 56.65 ? 88  LYS A CD     1 
ATOM   530  C CE     . LYS A 1 70  ? 16.817 -24.303 -1.103  1.00 67.66 ? 88  LYS A CE     1 
ATOM   531  N NZ     . LYS A 1 70  ? 17.124 -24.258 -2.559  1.00 45.21 ? 88  LYS A NZ     1 
ATOM   532  N N      . LYS A 1 71  ? 10.676 -23.866 1.938   1.00 44.73 ? 89  LYS A N      1 
ATOM   533  C CA     . LYS A 1 71  ? 9.379  -24.232 2.474   1.00 41.30 ? 89  LYS A CA     1 
ATOM   534  C C      . LYS A 1 71  ? 8.254  -23.418 1.860   1.00 39.00 ? 89  LYS A C      1 
ATOM   535  O O      . LYS A 1 71  ? 7.114  -23.524 2.313   1.00 49.27 ? 89  LYS A O      1 
ATOM   536  C CB     . LYS A 1 71  ? 9.377  -24.089 3.999   1.00 34.78 ? 89  LYS A CB     1 
ATOM   537  C CG     . LYS A 1 71  ? 10.309 -25.086 4.661   1.00 46.25 ? 89  LYS A CG     1 
ATOM   538  C CD     . LYS A 1 71  ? 10.537 -24.784 6.134   1.00 57.73 ? 89  LYS A CD     1 
ATOM   539  C CE     . LYS A 1 71  ? 11.507 -25.789 6.796   1.00 59.21 ? 89  LYS A CE     1 
ATOM   540  N NZ     . LYS A 1 71  ? 12.901 -25.777 6.212   1.00 37.21 ? 89  LYS A NZ     1 
ATOM   541  N N      . ASN A 1 72  ? 8.539  -22.619 0.838   1.00 33.10 ? 90  ASN A N      1 
ATOM   542  C CA     . ASN A 1 72  ? 7.475  -21.918 0.132   1.00 38.77 ? 90  ASN A CA     1 
ATOM   543  C C      . ASN A 1 72  ? 7.747  -21.841 -1.373  1.00 42.85 ? 90  ASN A C      1 
ATOM   544  O O      . ASN A 1 72  ? 7.083  -21.054 -2.074  1.00 30.97 ? 90  ASN A O      1 
ATOM   545  C CB     . ASN A 1 72  ? 7.268  -20.515 0.740   1.00 34.13 ? 90  ASN A CB     1 
ATOM   546  C CG     . ASN A 1 72  ? 6.651  -20.548 2.144   1.00 39.87 ? 90  ASN A CG     1 
ATOM   547  O OD1    . ASN A 1 72  ? 7.194  -19.970 3.088   1.00 36.54 ? 90  ASN A OD1    1 
ATOM   548  N ND2    . ASN A 1 72  ? 5.494  -21.198 2.274   1.00 41.09 ? 90  ASN A ND2    1 
ATOM   549  N N      . GLU A 1 73  ? 8.679  -22.658 -1.889  1.00 38.73 ? 91  GLU A N      1 
ATOM   550  C CA     . GLU A 1 73  ? 9.045  -22.617 -3.304  1.00 41.66 ? 91  GLU A CA     1 
ATOM   551  C C      . GLU A 1 73  ? 7.824  -22.616 -4.221  1.00 53.24 ? 91  GLU A C      1 
ATOM   552  O O      . GLU A 1 73  ? 7.871  -22.061 -5.332  1.00 47.89 ? 91  GLU A O      1 
ATOM   553  C CB     . GLU A 1 73  ? 9.947  -23.809 -3.645  1.00 39.68 ? 91  GLU A CB     1 
ATOM   554  C CG     . GLU A 1 73  ? 11.450 -23.522 -3.561  1.00 57.86 ? 91  GLU A CG     1 
ATOM   555  C CD     . GLU A 1 73  ? 12.310 -24.755 -3.241  1.00 66.50 ? 91  GLU A CD     1 
ATOM   556  O OE1    . GLU A 1 73  ? 11.843 -25.631 -2.473  1.00 61.48 ? 91  GLU A OE1    1 
ATOM   557  O OE2    . GLU A 1 73  ? 13.462 -24.834 -3.748  1.00 62.36 ? 91  GLU A OE2    1 
ATOM   558  N N      . SER A 1 74  ? 6.732  -23.260 -3.796  1.00 53.06 ? 92  SER A N      1 
ATOM   559  C CA     . SER A 1 74  ? 5.524  -23.265 -4.613  1.00 50.71 ? 92  SER A CA     1 
ATOM   560  C C      . SER A 1 74  ? 5.071  -21.844 -4.918  1.00 49.68 ? 92  SER A C      1 
ATOM   561  O O      . SER A 1 74  ? 4.640  -21.544 -6.038  1.00 46.98 ? 92  SER A O      1 
ATOM   562  C CB     . SER A 1 74  ? 4.417  -24.037 -3.898  1.00 52.34 ? 92  SER A CB     1 
ATOM   563  O OG     . SER A 1 74  ? 4.977  -25.025 -3.067  1.00 60.95 ? 92  SER A OG     1 
ATOM   564  N N      . LEU A 1 75  ? 5.174  -20.930 -3.949  1.00 52.61 ? 93  LEU A N      1 
ATOM   565  C CA     . LEU A 1 75  ? 4.768  -19.520 -4.137  1.00 54.27 ? 93  LEU A CA     1 
ATOM   566  C C      . LEU A 1 75  ? 5.939  -18.615 -4.491  1.00 47.32 ? 93  LEU A C      1 
ATOM   567  O O      . LEU A 1 75  ? 5.805  -17.403 -4.494  1.00 38.78 ? 93  LEU A O      1 
ATOM   568  C CB     . LEU A 1 75  ? 4.039  -18.990 -2.897  1.00 41.22 ? 93  LEU A CB     1 
ATOM   569  C CG     . LEU A 1 75  ? 2.610  -19.420 -2.620  1.00 38.86 ? 93  LEU A CG     1 
ATOM   570  C CD1    . LEU A 1 75  ? 2.167  -18.785 -1.319  1.00 35.48 ? 93  LEU A CD1    1 
ATOM   571  C CD2    . LEU A 1 75  ? 1.708  -18.980 -3.759  1.00 41.39 ? 93  LEU A CD2    1 
ATOM   572  N N      . LEU A 1 76  ? 7.079  -19.208 -4.802  1.00 45.25 ? 94  LEU A N      1 
ATOM   573  C CA     . LEU A 1 76  ? 8.290  -18.466 -5.142  1.00 39.08 ? 94  LEU A CA     1 
ATOM   574  C C      . LEU A 1 76  ? 8.826  -18.945 -6.479  1.00 39.50 ? 94  LEU A C      1 
ATOM   575  O O      . LEU A 1 76  ? 8.436  -19.996 -6.987  1.00 53.83 ? 94  LEU A O      1 
ATOM   576  C CB     . LEU A 1 76  ? 9.393  -18.654 -4.091  1.00 41.18 ? 94  LEU A CB     1 
ATOM   577  C CG     . LEU A 1 76  ? 9.161  -18.135 -2.679  1.00 41.62 ? 94  LEU A CG     1 
ATOM   578  C CD1    . LEU A 1 76  ? 10.304 -18.528 -1.752  1.00 27.61 ? 94  LEU A CD1    1 
ATOM   579  C CD2    . LEU A 1 76  ? 8.984  -16.617 -2.733  1.00 47.81 ? 94  LEU A CD2    1 
ATOM   580  N N      . SER A 1 77  ? 9.758  -18.182 -7.035  1.00 39.97 ? 95  SER A N      1 
ATOM   581  C CA     . SER A 1 77  ? 10.533 -18.649 -8.178  1.00 37.10 ? 95  SER A CA     1 
ATOM   582  C C      . SER A 1 77  ? 11.673 -19.525 -7.680  1.00 44.33 ? 95  SER A C      1 
ATOM   583  O O      . SER A 1 77  ? 12.574 -19.035 -6.989  1.00 46.79 ? 95  SER A O      1 
ATOM   584  C CB     . SER A 1 77  ? 11.104 -17.485 -8.978  1.00 39.45 ? 95  SER A CB     1 
ATOM   585  O OG     . SER A 1 77  ? 12.292 -17.927 -9.628  1.00 34.39 ? 95  SER A OG     1 
ATOM   586  N N      . GLU A 1 78  ? 11.653 -20.815 -8.041  1.00 52.57 ? 96  GLU A N      1 
ATOM   587  C CA     . GLU A 1 78  ? 12.772 -21.691 -7.697  1.00 50.70 ? 96  GLU A CA     1 
ATOM   588  C C      . GLU A 1 78  ? 14.037 -21.349 -8.481  1.00 45.10 ? 96  GLU A C      1 
ATOM   589  O O      . GLU A 1 78  ? 15.138 -21.749 -8.071  1.00 49.59 ? 96  GLU A O      1 
ATOM   590  C CB     . GLU A 1 78  ? 12.387 -23.161 -7.907  1.00 49.22 ? 96  GLU A CB     1 
ATOM   591  C CG     . GLU A 1 78  ? 11.903 -23.526 -9.325  1.00 64.15 ? 96  GLU A CG     1 
ATOM   592  C CD     . GLU A 1 78  ? 10.883 -24.683 -9.333  1.00 72.94 ? 96  GLU A CD     1 
ATOM   593  O OE1    . GLU A 1 78  ? 9.709  -24.446 -8.954  1.00 65.80 ? 96  GLU A OE1    1 
ATOM   594  O OE2    . GLU A 1 78  ? 11.256 -25.823 -9.717  1.00 58.46 ? 96  GLU A OE2    1 
ATOM   595  N N      . GLN A 1 79  ? 13.907 -20.614 -9.592  1.00 35.78 ? 97  GLN A N      1 
ATOM   596  C CA     . GLN A 1 79  ? 15.094 -20.146 -10.302 1.00 41.56 ? 97  GLN A CA     1 
ATOM   597  C C      . GLN A 1 79  ? 15.909 -19.193 -9.430  1.00 47.10 ? 97  GLN A C      1 
ATOM   598  O O      . GLN A 1 79  ? 17.145 -19.283 -9.366  1.00 37.78 ? 97  GLN A O      1 
ATOM   599  C CB     . GLN A 1 79  ? 14.668 -19.477 -11.609 1.00 46.35 ? 97  GLN A CB     1 
ATOM   600  C CG     . GLN A 1 79  ? 15.766 -19.294 -12.647 1.00 46.76 ? 97  GLN A CG     1 
ATOM   601  C CD     . GLN A 1 79  ? 16.607 -18.052 -12.414 1.00 49.37 ? 97  GLN A CD     1 
ATOM   602  O OE1    . GLN A 1 79  ? 17.826 -18.135 -12.205 1.00 49.87 ? 97  GLN A OE1    1 
ATOM   603  N NE2    . GLN A 1 79  ? 15.962 -16.889 -12.455 1.00 42.39 ? 97  GLN A NE2    1 
ATOM   604  N N      . VAL A 1 80  ? 15.218 -18.294 -8.724  1.00 47.81 ? 98  VAL A N      1 
ATOM   605  C CA     . VAL A 1 80  ? 15.858 -17.303 -7.865  1.00 42.20 ? 98  VAL A CA     1 
ATOM   606  C C      . VAL A 1 80  ? 16.362 -17.923 -6.564  1.00 37.55 ? 98  VAL A C      1 
ATOM   607  O O      . VAL A 1 80  ? 17.472 -17.615 -6.115  1.00 33.15 ? 98  VAL A O      1 
ATOM   608  C CB     . VAL A 1 80  ? 14.877 -16.147 -7.605  1.00 44.74 ? 98  VAL A CB     1 
ATOM   609  C CG1    . VAL A 1 80  ? 15.284 -15.373 -6.361  1.00 39.02 ? 98  VAL A CG1    1 
ATOM   610  C CG2    . VAL A 1 80  ? 14.807 -15.237 -8.827  1.00 37.95 ? 98  VAL A CG2    1 
ATOM   611  N N      . VAL A 1 81  ? 15.589 -18.807 -5.968  1.00 39.06 ? 99  VAL A N      1 
ATOM   612  C CA     . VAL A 1 81  ? 16.038 -19.510 -4.765  1.00 40.40 ? 99  VAL A CA     1 
ATOM   613  C C      . VAL A 1 81  ? 17.370 -20.195 -5.036  1.00 42.00 ? 99  VAL A C      1 
ATOM   614  O O      . VAL A 1 81  ? 18.241 -20.228 -4.185  1.00 38.47 ? 99  VAL A O      1 
ATOM   615  C CB     . VAL A 1 81  ? 14.963 -20.479 -4.264  1.00 33.61 ? 99  VAL A CB     1 
ATOM   616  C CG1    . VAL A 1 81  ? 15.416 -21.234 -3.033  1.00 37.35 ? 99  VAL A CG1    1 
ATOM   617  C CG2    . VAL A 1 81  ? 13.685 -19.727 -3.961  1.00 41.11 ? 99  VAL A CG2    1 
ATOM   618  N N      . GLN A 1 82  ? 17.554 -20.701 -6.240  1.00 36.92 ? 100 GLN A N      1 
ATOM   619  C CA     . GLN A 1 82  ? 18.814 -21.303 -6.593  1.00 39.38 ? 100 GLN A CA     1 
ATOM   620  C C      . GLN A 1 82  ? 20.031 -20.403 -6.422  1.00 36.21 ? 100 GLN A C      1 
ATOM   621  O O      . GLN A 1 82  ? 20.977 -20.770 -5.762  1.00 32.98 ? 100 GLN A O      1 
ATOM   622  C CB     . GLN A 1 82  ? 18.708 -21.826 -8.013  1.00 44.18 ? 100 GLN A CB     1 
ATOM   623  C CG     . GLN A 1 82  ? 19.967 -22.434 -8.596  1.00 45.66 ? 100 GLN A CG     1 
ATOM   624  C CD     . GLN A 1 82  ? 20.291 -23.791 -8.015  1.00 48.47 ? 100 GLN A CD     1 
ATOM   625  O OE1    . GLN A 1 82  ? 19.405 -24.529 -7.596  1.00 49.27 ? 100 GLN A OE1    1 
ATOM   626  N NE2    . GLN A 1 82  ? 21.568 -24.130 -7.994  1.00 46.74 ? 100 GLN A NE2    1 
ATOM   627  N N      . ARG A 1 83  ? 20.003 -19.226 -6.994  1.00 36.50 ? 101 ARG A N      1 
ATOM   628  C CA     . ARG A 1 83  ? 21.098 -18.298 -6.873  1.00 32.47 ? 101 ARG A CA     1 
ATOM   629  C C      . ARG A 1 83  ? 21.340 -17.858 -5.468  1.00 33.40 ? 101 ARG A C      1 
ATOM   630  O O      . ARG A 1 83  ? 22.454 -17.574 -5.111  1.00 26.51 ? 101 ARG A O      1 
ATOM   631  C CB     . ARG A 1 83  ? 20.792 -17.088 -7.722  1.00 28.57 ? 101 ARG A CB     1 
ATOM   632  C CG     . ARG A 1 83  ? 20.413 -17.388 -9.152  1.00 42.49 ? 101 ARG A CG     1 
ATOM   633  C CD     . ARG A 1 83  ? 21.340 -16.641 -10.086 1.00 38.92 ? 101 ARG A CD     1 
ATOM   634  N NE     . ARG A 1 83  ? 22.637 -16.408 -9.460  1.00 39.94 ? 101 ARG A NE     1 
ATOM   635  C CZ     . ARG A 1 83  ? 23.337 -15.291 -9.591  1.00 43.01 ? 101 ARG A CZ     1 
ATOM   636  N NH1    . ARG A 1 83  ? 22.865 -14.303 -10.328 1.00 38.01 ? 101 ARG A NH1    1 
ATOM   637  N NH2    . ARG A 1 83  ? 24.504 -15.167 -8.984  1.00 36.58 ? 101 ARG A NH2    1 
ATOM   638  N N      . LEU A 1 84  ? 20.297 -17.824 -4.660  1.00 33.78 ? 102 LEU A N      1 
ATOM   639  C CA     . LEU A 1 84  ? 20.402 -17.392 -3.299  1.00 26.52 ? 102 LEU A CA     1 
ATOM   640  C C      . LEU A 1 84  ? 21.126 -18.409 -2.505  1.00 27.76 ? 102 LEU A C      1 
ATOM   641  O O      . LEU A 1 84  ? 21.869 -18.095 -1.606  1.00 24.66 ? 102 LEU A O      1 
ATOM   642  C CB     . LEU A 1 84  ? 19.000 -17.179 -2.733  1.00 27.83 ? 102 LEU A CB     1 
ATOM   643  C CG     . LEU A 1 84  ? 18.117 -16.012 -3.175  1.00 29.26 ? 102 LEU A CG     1 
ATOM   644  C CD1    . LEU A 1 84  ? 16.717 -16.146 -2.611  1.00 13.47 ? 102 LEU A CD1    1 
ATOM   645  C CD2    . LEU A 1 84  ? 18.697 -14.669 -2.798  1.00 19.76 ? 102 LEU A CD2    1 
ATOM   646  N N      . ALA A 1 85  ? 20.952 -19.651 -2.878  1.00 31.49 ? 103 ALA A N      1 
ATOM   647  C CA     . ALA A 1 85  ? 21.574 -20.721 -2.171  1.00 28.07 ? 103 ALA A CA     1 
ATOM   648  C C      . ALA A 1 85  ? 22.965 -21.031 -2.631  1.00 26.28 ? 103 ALA A C      1 
ATOM   649  O O      . ALA A 1 85  ? 23.694 -21.694 -1.948  1.00 31.71 ? 103 ALA A O      1 
ATOM   650  C CB     . ALA A 1 85  ? 20.695 -21.929 -2.266  1.00 26.42 ? 103 ALA A CB     1 
ATOM   651  N N      . GLU A 1 86  ? 23.336 -20.562 -3.792  1.00 29.38 ? 104 GLU A N      1 
ATOM   652  C CA     . GLU A 1 86  ? 24.642 -20.816 -4.302  1.00 28.62 ? 104 GLU A CA     1 
ATOM   653  C C      . GLU A 1 86  ? 25.514 -19.756 -3.805  1.00 28.76 ? 104 GLU A C      1 
ATOM   654  O O      . GLU A 1 86  ? 26.682 -19.977 -3.570  1.00 39.45 ? 104 GLU A O      1 
ATOM   655  C CB     . GLU A 1 86  ? 24.655 -20.649 -5.804  1.00 36.72 ? 104 GLU A CB     1 
ATOM   656  C CG     . GLU A 1 86  ? 23.957 -21.698 -6.641  1.00 45.85 ? 104 GLU A CG     1 
ATOM   657  C CD     . GLU A 1 86  ? 23.702 -21.199 -8.054  1.00 49.31 ? 104 GLU A CD     1 
ATOM   658  O OE1    . GLU A 1 86  ? 23.868 -19.991 -8.297  1.00 46.46 ? 104 GLU A OE1    1 
ATOM   659  O OE2    . GLU A 1 86  ? 23.350 -22.007 -8.930  1.00 54.17 ? 104 GLU A OE2    1 
ATOM   660  N N      . VAL A 1 87  ? 24.968 -18.564 -3.690  1.00 31.14 ? 105 VAL A N      1 
ATOM   661  C CA     . VAL A 1 87  ? 25.753 -17.436 -3.285  1.00 30.41 ? 105 VAL A CA     1 
ATOM   662  C C      . VAL A 1 87  ? 26.008 -17.501 -1.801  1.00 32.23 ? 105 VAL A C      1 
ATOM   663  O O      . VAL A 1 87  ? 27.109 -17.239 -1.353  1.00 29.10 ? 105 VAL A O      1 
ATOM   664  C CB     . VAL A 1 87  ? 25.055 -16.128 -3.736  1.00 26.96 ? 105 VAL A CB     1 
ATOM   665  C CG1    . VAL A 1 87  ? 25.451 -14.933 -2.892  1.00 26.39 ? 105 VAL A CG1    1 
ATOM   666  C CG2    . VAL A 1 87  ? 25.334 -15.863 -5.202  1.00 24.51 ? 105 VAL A CG2    1 
ATOM   667  N N      . ALA A 1 88  ? 25.025 -17.928 -1.043  1.00 24.60 ? 106 ALA A N      1 
ATOM   668  C CA     . ALA A 1 88  ? 25.156 -17.933 0.390   1.00 24.74 ? 106 ALA A CA     1 
ATOM   669  C C      . ALA A 1 88  ? 26.388 -18.527 1.081   1.00 30.94 ? 106 ALA A C      1 
ATOM   670  O O      . ALA A 1 88  ? 26.919 -17.907 1.982   1.00 33.86 ? 106 ALA A O      1 
ATOM   671  C CB     . ALA A 1 88  ? 23.879 -18.458 1.002   1.00 24.57 ? 106 ALA A CB     1 
ATOM   672  N N      . PRO A 1 89  ? 26.816 -19.747 0.724   1.00 34.49 ? 107 PRO A N      1 
ATOM   673  C CA     . PRO A 1 89  ? 27.962 -20.275 1.450   1.00 26.10 ? 107 PRO A CA     1 
ATOM   674  C C      . PRO A 1 89  ? 29.228 -19.477 1.246   1.00 26.32 ? 107 PRO A C      1 
ATOM   675  O O      . PRO A 1 89  ? 30.178 -19.653 1.986   1.00 26.24 ? 107 PRO A O      1 
ATOM   676  C CB     . PRO A 1 89  ? 28.126 -21.644 0.814   1.00 27.06 ? 107 PRO A CB     1 
ATOM   677  C CG     . PRO A 1 89  ? 27.417 -21.597 -0.482  1.00 30.97 ? 107 PRO A CG     1 
ATOM   678  C CD     . PRO A 1 89  ? 26.238 -20.778 -0.148  1.00 27.68 ? 107 PRO A CD     1 
ATOM   679  N N      . ARG A 1 90  ? 29.231 -18.599 0.265   1.00 31.60 ? 108 ARG A N      1 
ATOM   680  C CA     . ARG A 1 90  ? 30.408 -17.818 -0.092  1.00 29.15 ? 108 ARG A CA     1 
ATOM   681  C C      . ARG A 1 90  ? 30.380 -16.402 0.475   1.00 31.76 ? 108 ARG A C      1 
ATOM   682  O O      . ARG A 1 90  ? 31.340 -15.656 0.280   1.00 43.85 ? 108 ARG A O      1 
ATOM   683  C CB     . ARG A 1 90  ? 30.550 -17.769 -1.623  1.00 32.21 ? 108 ARG A CB     1 
ATOM   684  C CG     . ARG A 1 90  ? 31.792 -17.041 -2.154  1.00 50.44 ? 108 ARG A CG     1 
ATOM   685  C CD     . ARG A 1 90  ? 33.111 -17.667 -1.664  1.00 61.69 ? 108 ARG A CD     1 
ATOM   686  N NE     . ARG A 1 90  ? 34.295 -16.943 -2.124  1.00 65.49 ? 108 ARG A NE     1 
ATOM   687  C CZ     . ARG A 1 90  ? 34.944 -16.018 -1.422  1.00 72.41 ? 108 ARG A CZ     1 
ATOM   688  N NH1    . ARG A 1 90  ? 34.549 -15.665 -0.206  1.00 62.34 ? 108 ARG A NH1    1 
ATOM   689  N NH2    . ARG A 1 90  ? 36.015 -15.430 -1.956  1.00 75.05 ? 108 ARG A NH2    1 
ATOM   690  N N      . LEU A 1 91  ? 29.329 -16.024 1.195   1.00 26.38 ? 109 LEU A N      1 
ATOM   691  C CA     . LEU A 1 91  ? 29.192 -14.664 1.694   1.00 24.02 ? 109 LEU A CA     1 
ATOM   692  C C      . LEU A 1 91  ? 30.147 -14.395 2.852   1.00 30.55 ? 109 LEU A C      1 
ATOM   693  O O      . LEU A 1 91  ? 30.275 -15.208 3.777   1.00 23.15 ? 109 LEU A O      1 
ATOM   694  C CB     . LEU A 1 91  ? 27.757 -14.405 2.158   1.00 24.46 ? 109 LEU A CB     1 
ATOM   695  C CG     . LEU A 1 91  ? 26.655 -14.159 1.129   1.00 18.75 ? 109 LEU A CG     1 
ATOM   696  C CD1    . LEU A 1 91  ? 25.332 -13.942 1.825   1.00 17.02 ? 109 LEU A CD1    1 
ATOM   697  C CD2    . LEU A 1 91  ? 27.025 -12.956 0.298   1.00 22.03 ? 109 LEU A CD2    1 
ATOM   698  N N      . LYS A 1 92  ? 30.805 -13.231 2.793   1.00 27.30 ? 110 LYS A N      1 
ATOM   699  C CA     . LYS A 1 92  ? 31.615 -12.670 3.864   1.00 27.83 ? 110 LYS A CA     1 
ATOM   700  C C      . LYS A 1 92  ? 31.073 -11.287 4.206   1.00 23.53 ? 110 LYS A C      1 
ATOM   701  O O      . LYS A 1 92  ? 30.095 -10.820 3.613   1.00 22.35 ? 110 LYS A O      1 
ATOM   702  C CB     . LYS A 1 92  ? 33.092 -12.597 3.464   1.00 25.21 ? 110 LYS A CB     1 
ATOM   703  C CG     . LYS A 1 92  ? 33.826 -13.910 3.630   1.00 31.34 ? 110 LYS A CG     1 
ATOM   704  C CD     . LYS A 1 92  ? 35.314 -13.683 3.932   1.00 45.51 ? 110 LYS A CD     1 
ATOM   705  C CE     . LYS A 1 92  ? 35.901 -14.873 4.690   1.00 42.69 ? 110 LYS A CE     1 
ATOM   706  N NZ     . LYS A 1 92  ? 37.294 -14.665 5.165   1.00 32.70 ? 110 LYS A NZ     1 
ATOM   707  N N      . SER A 1 93  ? 31.787 -10.621 5.125   1.00 18.02 ? 111 SER A N      1 
ATOM   708  C CA     . SER A 1 93  ? 31.492 -9.253  5.520   1.00 20.45 ? 111 SER A CA     1 
ATOM   709  C C      . SER A 1 93  ? 32.879 -8.586  5.613   1.00 16.57 ? 111 SER A C      1 
ATOM   710  O O      . SER A 1 93  ? 33.790 -9.216  6.075   1.00 18.65 ? 111 SER A O      1 
ATOM   711  C CB     . SER A 1 93  ? 30.655 -9.209  6.776   1.00 13.12 ? 111 SER A CB     1 
ATOM   712  O OG     . SER A 1 93  ? 30.781 -10.412 7.485   1.00 39.72 ? 111 SER A OG     1 
ATOM   713  N N      . ASN A 1 94  ? 33.061 -7.345  5.145   1.00 16.18 ? 112 ASN A N      1 
ATOM   714  C CA     . ASN A 1 94  ? 34.373 -6.699  5.068   1.00 17.55 ? 112 ASN A CA     1 
ATOM   715  C C      . ASN A 1 94  ? 34.326 -5.425  5.894   1.00 19.48 ? 112 ASN A C      1 
ATOM   716  O O      . ASN A 1 94  ? 33.742 -4.422  5.450   1.00 18.82 ? 112 ASN A O      1 
ATOM   717  C CB     . ASN A 1 94  ? 34.740 -6.396  3.609   1.00 13.55 ? 112 ASN A CB     1 
ATOM   718  C CG     . ASN A 1 94  ? 36.155 -5.853  3.450   1.00 22.09 ? 112 ASN A CG     1 
ATOM   719  O OD1    . ASN A 1 94  ? 36.415 -5.015  2.581   1.00 23.42 ? 112 ASN A OD1    1 
ATOM   720  N ND2    . ASN A 1 94  ? 37.078 -6.326  4.289   1.00 25.93 ? 112 ASN A ND2    1 
ATOM   721  N N      . PRO A 1 95  ? 34.868 -5.477  7.105   1.00 18.77 ? 113 PRO A N      1 
ATOM   722  C CA     . PRO A 1 95  ? 34.800 -4.335  7.999   1.00 18.49 ? 113 PRO A CA     1 
ATOM   723  C C      . PRO A 1 95  ? 35.180 -2.977  7.424   1.00 20.89 ? 113 PRO A C      1 
ATOM   724  O O      . PRO A 1 95  ? 34.799 -1.982  7.986   1.00 20.40 ? 113 PRO A O      1 
ATOM   725  C CB     . PRO A 1 95  ? 35.695 -4.775  9.169   1.00 15.70 ? 113 PRO A CB     1 
ATOM   726  C CG     . PRO A 1 95  ? 36.370 -6.019  8.761   1.00 21.86 ? 113 PRO A CG     1 
ATOM   727  C CD     . PRO A 1 95  ? 35.454 -6.644  7.780   1.00 18.49 ? 113 PRO A CD     1 
ATOM   728  N N      . LYS A 1 96  ? 35.901 -2.942  6.324   1.00 15.97 ? 114 LYS A N      1 
ATOM   729  C CA     . LYS A 1 96  ? 36.285 -1.711  5.684   1.00 23.61 ? 114 LYS A CA     1 
ATOM   730  C C      . LYS A 1 96  ? 35.305 -1.373  4.601   1.00 26.03 ? 114 LYS A C      1 
ATOM   731  O O      . LYS A 1 96  ? 35.384 -0.300  4.046   1.00 18.92 ? 114 LYS A O      1 
ATOM   732  C CB     . LYS A 1 96  ? 37.634 -1.965  5.020   1.00 24.52 ? 114 LYS A CB     1 
ATOM   733  C CG     . LYS A 1 96  ? 38.802 -2.223  5.937   1.00 30.78 ? 114 LYS A CG     1 
ATOM   734  C CD     . LYS A 1 96  ? 40.072 -2.344  5.117   1.00 23.65 ? 114 LYS A CD     1 
ATOM   735  C CE     . LYS A 1 96  ? 41.300 -2.469  6.000   1.00 26.25 ? 114 LYS A CE     1 
ATOM   736  N NZ     . LYS A 1 96  ? 42.551 -2.310  5.217   1.00 21.32 ? 114 LYS A NZ     1 
ATOM   737  N N      . ASP A 1 97  ? 34.340 -2.210  4.335   1.00 24.34 ? 115 ASP A N      1 
ATOM   738  C CA     . ASP A 1 97  ? 33.411 -1.990  3.266   1.00 22.64 ? 115 ASP A CA     1 
ATOM   739  C C      . ASP A 1 97  ? 32.099 -2.625  3.657   1.00 23.88 ? 115 ASP A C      1 
ATOM   740  O O      . ASP A 1 97  ? 31.652 -3.527  2.976   1.00 34.32 ? 115 ASP A O      1 
ATOM   741  C CB     . ASP A 1 97  ? 33.918 -2.676  1.986   1.00 17.98 ? 115 ASP A CB     1 
ATOM   742  C CG     . ASP A 1 97  ? 34.696 -1.772  1.082   1.00 31.74 ? 115 ASP A CG     1 
ATOM   743  O OD1    . ASP A 1 97  ? 35.875 -1.512  1.358   1.00 44.29 ? 115 ASP A OD1    1 
ATOM   744  O OD2    . ASP A 1 97  ? 34.139 -1.351  0.058   1.00 52.43 ? 115 ASP A OD2    1 
ATOM   745  N N      . ASN A 1 98  ? 31.468 -2.192  4.733   1.00 15.79 ? 116 ASN A N      1 
ATOM   746  C CA     . ASN A 1 98  ? 30.175 -2.773  5.055   1.00 11.59 ? 116 ASN A CA     1 
ATOM   747  C C      . ASN A 1 98  ? 29.149 -1.698  4.771   1.00 15.72 ? 116 ASN A C      1 
ATOM   748  O O      . ASN A 1 98  ? 28.409 -1.278  5.661   1.00 20.73 ? 116 ASN A O      1 
ATOM   749  C CB     . ASN A 1 98  ? 30.131 -3.281  6.501   1.00 17.59 ? 116 ASN A CB     1 
ATOM   750  C CG     . ASN A 1 98  ? 30.696 -4.712  6.663   1.00 18.06 ? 116 ASN A CG     1 
ATOM   751  O OD1    . ASN A 1 98  ? 30.960 -5.422  5.683   1.00 18.94 ? 116 ASN A OD1    1 
ATOM   752  N ND2    . ASN A 1 98  ? 30.874 -5.127  7.914   1.00 10.14 ? 116 ASN A ND2    1 
ATOM   753  N N      . GLU A 1 99  ? 29.106 -1.237  3.522   1.00 18.25 ? 117 GLU A N      1 
ATOM   754  C CA     . GLU A 1 99  ? 28.459 0.037   3.227   1.00 12.34 ? 117 GLU A CA     1 
ATOM   755  C C      . GLU A 1 99  ? 26.962 0.003   3.480   1.00 7.50  ? 117 GLU A C      1 
ATOM   756  O O      . GLU A 1 99  ? 26.405 0.984   3.963   1.00 12.00 ? 117 GLU A O      1 
ATOM   757  C CB     . GLU A 1 99  ? 28.754 0.450   1.789   1.00 12.60 ? 117 GLU A CB     1 
ATOM   758  C CG     . GLU A 1 99  ? 30.202 0.599   1.551   1.00 18.56 ? 117 GLU A CG     1 
ATOM   759  C CD     . GLU A 1 99  ? 30.522 1.023   0.145   1.00 33.30 ? 117 GLU A CD     1 
ATOM   760  O OE1    . GLU A 1 99  ? 29.577 1.354   -0.601  1.00 31.15 ? 117 GLU A OE1    1 
ATOM   761  O OE2    . GLU A 1 99  ? 31.722 1.021   -0.222  1.00 51.31 ? 117 GLU A OE2    1 
ATOM   762  N N      . SER A 1 100 ? 26.273 -1.072  3.122   1.00 7.62  ? 118 SER A N      1 
ATOM   763  C CA     . SER A 1 100 ? 24.831 -1.080  3.382   1.00 11.31 ? 118 SER A CA     1 
ATOM   764  C C      . SER A 1 100 ? 24.555 -0.929  4.871   1.00 14.23 ? 118 SER A C      1 
ATOM   765  O O      . SER A 1 100 ? 23.690 -0.133  5.274   1.00 10.59 ? 118 SER A O      1 
ATOM   766  C CB     . SER A 1 100 ? 24.172 -2.352  2.854   1.00 12.44 ? 118 SER A CB     1 
ATOM   767  O OG     . SER A 1 100 ? 24.927 -3.483  3.251   1.00 17.64 ? 118 SER A OG     1 
ATOM   768  N N      . ARG A 1 101 ? 25.329 -1.635  5.712   1.00 10.87 ? 119 ARG A N      1 
ATOM   769  C CA     . ARG A 1 101 ? 25.110 -1.515  7.141   1.00 7.94  ? 119 ARG A CA     1 
ATOM   770  C C      . ARG A 1 101 ? 25.498 -0.138  7.652   1.00 8.49  ? 119 ARG A C      1 
ATOM   771  O O      . ARG A 1 101 ? 24.878 0.363   8.596   1.00 7.02  ? 119 ARG A O      1 
ATOM   772  C CB     . ARG A 1 101 ? 25.855 -2.598  7.922   1.00 11.54 ? 119 ARG A CB     1 
ATOM   773  C CG     . ARG A 1 101 ? 25.073 -2.903  9.190   1.00 10.89 ? 119 ARG A CG     1 
ATOM   774  C CD     . ARG A 1 101 ? 25.790 -3.655  10.220  1.00 10.19 ? 119 ARG A CD     1 
ATOM   775  N NE     . ARG A 1 101 ? 25.272 -3.306  11.540  1.00 21.64 ? 119 ARG A NE     1 
ATOM   776  C CZ     . ARG A 1 101 ? 24.139 -3.751  12.067  1.00 15.79 ? 119 ARG A CZ     1 
ATOM   777  N NH1    . ARG A 1 101 ? 23.288 -4.492  11.370  1.00 10.66 ? 119 ARG A NH1    1 
ATOM   778  N NH2    . ARG A 1 101 ? 23.860 -3.456  13.333  1.00 12.02 ? 119 ARG A NH2    1 
ATOM   779  N N      . ARG A 1 102 ? 26.470 0.499   7.060   1.00 10.13 ? 120 ARG A N      1 
ATOM   780  C CA     . ARG A 1 102 ? 26.853 1.836   7.442   1.00 10.31 ? 120 ARG A CA     1 
ATOM   781  C C      . ARG A 1 102 ? 25.723 2.809   7.242   1.00 7.97  ? 120 ARG A C      1 
ATOM   782  O O      . ARG A 1 102 ? 25.586 3.733   7.997   1.00 5.04  ? 120 ARG A O      1 
ATOM   783  C CB     . ARG A 1 102 ? 28.134 2.215   6.710   1.00 8.05  ? 120 ARG A CB     1 
ATOM   784  C CG     . ARG A 1 102 ? 29.374 1.493   7.145   1.00 8.98  ? 120 ARG A CG     1 
ATOM   785  C CD     . ARG A 1 102 ? 30.519 1.862   6.237   1.00 9.19  ? 120 ARG A CD     1 
ATOM   786  N NE     . ARG A 1 102 ? 31.713 1.115   6.583   1.00 18.87 ? 120 ARG A NE     1 
ATOM   787  C CZ     . ARG A 1 102 ? 32.715 1.602   7.297   1.00 16.65 ? 120 ARG A CZ     1 
ATOM   788  N NH1    . ARG A 1 102 ? 32.680 2.844   7.734   1.00 14.00 ? 120 ARG A NH1    1 
ATOM   789  N NH2    . ARG A 1 102 ? 33.755 0.845   7.564   1.00 15.09 ? 120 ARG A NH2    1 
ATOM   790  N N      . LEU A 1 103 ? 24.890 2.566   6.244   1.00 7.49  ? 121 LEU A N      1 
ATOM   791  C CA     . LEU A 1 103 ? 23.733 3.409   6.017   1.00 7.89  ? 121 LEU A CA     1 
ATOM   792  C C      . LEU A 1 103 ? 22.616 3.058   6.989   1.00 8.95  ? 121 LEU A C      1 
ATOM   793  O O      . LEU A 1 103 ? 21.982 3.948   7.567   1.00 9.51  ? 121 LEU A O      1 
ATOM   794  C CB     . LEU A 1 103 ? 23.288 3.270   4.570   1.00 6.97  ? 121 LEU A CB     1 
ATOM   795  C CG     . LEU A 1 103 ? 22.047 4.058   4.208   1.00 8.16  ? 121 LEU A CG     1 
ATOM   796  C CD1    . LEU A 1 103 ? 22.381 4.949   3.049   1.00 9.08  ? 121 LEU A CD1    1 
ATOM   797  C CD2    . LEU A 1 103 ? 20.882 3.138   3.874   1.00 7.24  ? 121 LEU A CD2    1 
ATOM   798  N N      . TYR A 1 104 ? 22.382 1.763   7.201   1.00 8.71  ? 122 TYR A N      1 
ATOM   799  C CA     . TYR A 1 104 ? 21.339 1.341   8.124   1.00 7.81  ? 122 TYR A CA     1 
ATOM   800  C C      . TYR A 1 104 ? 21.557 1.940   9.513   1.00 10.56 ? 122 TYR A C      1 
ATOM   801  O O      . TYR A 1 104 ? 20.677 2.625   10.055  1.00 10.21 ? 122 TYR A O      1 
ATOM   802  C CB     . TYR A 1 104 ? 21.311 -0.178  8.157   1.00 8.06  ? 122 TYR A CB     1 
ATOM   803  C CG     . TYR A 1 104 ? 20.423 -0.801  9.191   1.00 9.90  ? 122 TYR A CG     1 
ATOM   804  C CD1    . TYR A 1 104 ? 19.063 -0.940  8.975   1.00 10.41 ? 122 TYR A CD1    1 
ATOM   805  C CD2    . TYR A 1 104 ? 20.959 -1.305  10.371  1.00 13.12 ? 122 TYR A CD2    1 
ATOM   806  C CE1    . TYR A 1 104 ? 18.255 -1.545  9.911   1.00 12.68 ? 122 TYR A CE1    1 
ATOM   807  C CE2    . TYR A 1 104 ? 20.161 -1.912  11.309  1.00 15.90 ? 122 TYR A CE2    1 
ATOM   808  C CZ     . TYR A 1 104 ? 18.806 -2.030  11.070  1.00 13.90 ? 122 TYR A CZ     1 
ATOM   809  O OH     . TYR A 1 104 ? 18.005 -2.621  12.013  1.00 14.53 ? 122 TYR A OH     1 
ATOM   810  N N      . GLU A 1 105 ? 22.736 1.713   10.102  1.00 10.22 ? 123 GLU A N      1 
ATOM   811  C CA     . GLU A 1 105 ? 22.998 2.228   11.439  1.00 6.89  ? 123 GLU A CA     1 
ATOM   812  C C      . GLU A 1 105 ? 22.904 3.745   11.474  1.00 8.93  ? 123 GLU A C      1 
ATOM   813  O O      . GLU A 1 105 ? 22.423 4.317   12.456  1.00 12.55 ? 123 GLU A O      1 
ATOM   814  C CB     . GLU A 1 105 ? 24.366 1.773   11.932  1.00 7.83  ? 123 GLU A CB     1 
ATOM   815  C CG     . GLU A 1 105 ? 24.537 0.281   12.026  1.00 12.45 ? 123 GLU A CG     1 
ATOM   816  C CD     . GLU A 1 105 ? 25.808 -0.130  12.759  1.00 17.20 ? 123 GLU A CD     1 
ATOM   817  O OE1    . GLU A 1 105 ? 26.494 0.756   13.327  1.00 16.93 ? 123 GLU A OE1    1 
ATOM   818  O OE2    . GLU A 1 105 ? 26.107 -1.343  12.773  1.00 11.95 ? 123 GLU A OE2    1 
ATOM   819  N N      . THR A 1 106 ? 23.335 4.442   10.455  1.00 7.21  ? 124 THR A N      1 
ATOM   820  C CA     . THR A 1 106 ? 23.234 5.873   10.475  1.00 7.61  ? 124 THR A CA     1 
ATOM   821  C C      . THR A 1 106 ? 21.777 6.318   10.509  1.00 9.73  ? 124 THR A C      1 
ATOM   822  O O      . THR A 1 106 ? 21.404 7.220   11.237  1.00 11.42 ? 124 THR A O      1 
ATOM   823  C CB     . THR A 1 106 ? 24.114 6.500   9.373   1.00 6.66  ? 124 THR A CB     1 
ATOM   824  O OG1    . THR A 1 106 ? 25.480 6.241   9.667   1.00 10.77 ? 124 THR A OG1    1 
ATOM   825  C CG2    . THR A 1 106 ? 23.881 7.960   9.248   1.00 5.74  ? 124 THR A CG2    1 
ATOM   826  N N      . LEU A 1 107 ? 20.933 5.642   9.773   1.00 7.56  ? 125 LEU A N      1 
ATOM   827  C CA     . LEU A 1 107 ? 19.536 5.949   9.800   1.00 9.00  ? 125 LEU A CA     1 
ATOM   828  C C      . LEU A 1 107 ? 18.880 5.568   11.132  1.00 16.04 ? 125 LEU A C      1 
ATOM   829  O O      . LEU A 1 107 ? 18.018 6.285   11.603  1.00 13.75 ? 125 LEU A O      1 
ATOM   830  C CB     . LEU A 1 107 ? 18.870 5.270   8.625   1.00 6.69  ? 125 LEU A CB     1 
ATOM   831  C CG     . LEU A 1 107 ? 19.136 5.599   7.172   1.00 9.01  ? 125 LEU A CG     1 
ATOM   832  C CD1    . LEU A 1 107 ? 18.454 4.528   6.348   1.00 9.58  ? 125 LEU A CD1    1 
ATOM   833  C CD2    . LEU A 1 107 ? 18.631 6.977   6.803   1.00 7.33  ? 125 LEU A CD2    1 
ATOM   834  N N      . TYR A 1 108 ? 19.294 4.471   11.748  1.00 13.42 ? 126 TYR A N      1 
ATOM   835  C CA     . TYR A 1 108 ? 18.777 4.022   13.018  1.00 11.56 ? 126 TYR A CA     1 
ATOM   836  C C      . TYR A 1 108 ? 19.122 4.935   14.141  1.00 11.19 ? 126 TYR A C      1 
ATOM   837  O O      . TYR A 1 108 ? 18.377 5.076   15.073  1.00 15.19 ? 126 TYR A O      1 
ATOM   838  C CB     . TYR A 1 108 ? 19.262 2.577   13.296  1.00 12.90 ? 126 TYR A CB     1 
ATOM   839  C CG     . TYR A 1 108 ? 19.512 2.237   14.744  1.00 13.48 ? 126 TYR A CG     1 
ATOM   840  C CD1    . TYR A 1 108 ? 18.462 1.934   15.595  1.00 15.73 ? 126 TYR A CD1    1 
ATOM   841  C CD2    . TYR A 1 108 ? 20.795 2.217   15.259  1.00 13.08 ? 126 TYR A CD2    1 
ATOM   842  C CE1    . TYR A 1 108 ? 18.679 1.651   16.917  1.00 13.23 ? 126 TYR A CE1    1 
ATOM   843  C CE2    . TYR A 1 108 ? 21.015 1.934   16.582  1.00 16.04 ? 126 TYR A CE2    1 
ATOM   844  C CZ     . TYR A 1 108 ? 19.950 1.648   17.401  1.00 14.22 ? 126 TYR A CZ     1 
ATOM   845  O OH     . TYR A 1 108 ? 20.165 1.341   18.708  1.00 11.51 ? 126 TYR A OH     1 
ATOM   846  N N      . ALA A 1 109 ? 20.254 5.569   14.063  1.00 10.35 ? 127 ALA A N      1 
ATOM   847  C CA     . ALA A 1 109 ? 20.670 6.442   15.099  1.00 10.25 ? 127 ALA A CA     1 
ATOM   848  C C      . ALA A 1 109 ? 19.823 7.661   15.162  1.00 13.14 ? 127 ALA A C      1 
ATOM   849  O O      . ALA A 1 109 ? 19.615 8.221   16.219  1.00 19.03 ? 127 ALA A O      1 
ATOM   850  C CB     . ALA A 1 109 ? 22.104 6.820   14.878  1.00 8.66  ? 127 ALA A CB     1 
ATOM   851  N N      . ASP A 1 110 ? 19.320 8.084   14.031  1.00 15.15 ? 128 ASP A N      1 
ATOM   852  C CA     . ASP A 1 110 ? 18.490 9.240   13.980  1.00 14.84 ? 128 ASP A CA     1 
ATOM   853  C C      . ASP A 1 110 ? 17.142 8.871   14.479  1.00 16.71 ? 128 ASP A C      1 
ATOM   854  O O      . ASP A 1 110 ? 16.457 9.689   15.045  1.00 17.87 ? 128 ASP A O      1 
ATOM   855  C CB     . ASP A 1 110 ? 18.457 9.749   12.560  1.00 21.98 ? 128 ASP A CB     1 
ATOM   856  C CG     . ASP A 1 110 ? 19.536 10.757  12.276  1.00 32.59 ? 128 ASP A CG     1 
ATOM   857  O OD1    . ASP A 1 110 ? 19.359 11.929  12.640  1.00 37.75 ? 128 ASP A OD1    1 
ATOM   858  O OD2    . ASP A 1 110 ? 20.559 10.389  11.675  1.00 31.13 ? 128 ASP A OD2    1 
ATOM   859  N N      . HIS A 1 111 ? 16.757 7.627   14.293  1.00 15.45 ? 129 HIS A N      1 
ATOM   860  C CA     . HIS A 1 111 ? 15.524 7.140   14.845  1.00 13.61 ? 129 HIS A CA     1 
ATOM   861  C C      . HIS A 1 111 ? 15.603 6.985   16.350  1.00 16.95 ? 129 HIS A C      1 
ATOM   862  O O      . HIS A 1 111 ? 14.721 7.391   17.033  1.00 17.16 ? 129 HIS A O      1 
ATOM   863  C CB     . HIS A 1 111 ? 15.178 5.826   14.184  1.00 13.42 ? 129 HIS A CB     1 
ATOM   864  C CG     . HIS A 1 111 ? 13.827 5.294   14.534  1.00 14.56 ? 129 HIS A CG     1 
ATOM   865  N ND1    . HIS A 1 111 ? 13.531 3.954   14.502  1.00 16.10 ? 129 HIS A ND1    1 
ATOM   866  C CD2    . HIS A 1 111 ? 12.690 5.918   14.910  1.00 16.88 ? 129 HIS A CD2    1 
ATOM   867  C CE1    . HIS A 1 111 ? 12.275 3.771   14.853  1.00 20.83 ? 129 HIS A CE1    1 
ATOM   868  N NE2    . HIS A 1 111 ? 11.742 4.948   15.107  1.00 24.26 ? 129 HIS A NE2    1 
ATOM   869  N N      . LEU A 1 112 ? 16.660 6.403   16.873  1.00 14.90 ? 130 LEU A N      1 
ATOM   870  C CA     . LEU A 1 112 ? 16.833 6.290   18.296  1.00 15.24 ? 130 LEU A CA     1 
ATOM   871  C C      . LEU A 1 112 ? 16.794 7.626   18.996  1.00 18.54 ? 130 LEU A C      1 
ATOM   872  O O      . LEU A 1 112 ? 16.233 7.715   20.060  1.00 25.18 ? 130 LEU A O      1 
ATOM   873  C CB     . LEU A 1 112 ? 18.095 5.481   18.655  1.00 12.37 ? 130 LEU A CB     1 
ATOM   874  C CG     . LEU A 1 112 ? 18.464 5.159   20.098  1.00 9.27  ? 130 LEU A CG     1 
ATOM   875  C CD1    . LEU A 1 112 ? 17.449 4.244   20.746  1.00 6.90  ? 130 LEU A CD1    1 
ATOM   876  C CD2    . LEU A 1 112 ? 19.834 4.528   20.129  1.00 9.97  ? 130 LEU A CD2    1 
ATOM   877  N N      . GLU A 1 113 ? 17.350 8.666   18.415  1.00 15.03 ? 131 GLU A N      1 
ATOM   878  C CA     . GLU A 1 113 ? 17.256 9.983   19.006  1.00 18.43 ? 131 GLU A CA     1 
ATOM   879  C C      . GLU A 1 113 ? 15.870 10.562  18.977  1.00 19.86 ? 131 GLU A C      1 
ATOM   880  O O      . GLU A 1 113 ? 15.461 11.204  19.911  1.00 20.41 ? 131 GLU A O      1 
ATOM   881  C CB     . GLU A 1 113 ? 18.197 10.944  18.327  1.00 23.23 ? 131 GLU A CB     1 
ATOM   882  C CG     . GLU A 1 113 ? 19.247 11.528  19.233  1.00 26.77 ? 131 GLU A CG     1 
ATOM   883  C CD     . GLU A 1 113 ? 20.265 12.341  18.473  1.00 41.62 ? 131 GLU A CD     1 
ATOM   884  O OE1    . GLU A 1 113 ? 21.479 12.047  18.595  1.00 44.44 ? 131 GLU A OE1    1 
ATOM   885  O OE2    . GLU A 1 113 ? 19.843 13.270  17.755  1.00 36.82 ? 131 GLU A OE2    1 
ATOM   886  N N      . SER A 1 114 ? 15.156 10.367  17.897  1.00 16.38 ? 132 SER A N      1 
ATOM   887  C CA     . SER A 1 114 ? 13.820 10.857  17.786  1.00 18.66 ? 132 SER A CA     1 
ATOM   888  C C      . SER A 1 114 ? 12.994 10.235  18.842  1.00 21.38 ? 132 SER A C      1 
ATOM   889  O O      . SER A 1 114 ? 12.088 10.853  19.372  1.00 23.70 ? 132 SER A O      1 
ATOM   890  C CB     . SER A 1 114 ? 13.240 10.514  16.420  1.00 16.78 ? 132 SER A CB     1 
ATOM   891  O OG     . SER A 1 114 ? 12.252 9.511   16.485  1.00 19.04 ? 132 SER A OG     1 
ATOM   892  N N      . VAL A 1 115 ? 13.306 8.992   19.152  1.00 21.90 ? 133 VAL A N      1 
ATOM   893  C CA     . VAL A 1 115 ? 12.517 8.271   20.138  1.00 18.89 ? 133 VAL A CA     1 
ATOM   894  C C      . VAL A 1 115 ? 12.765 8.840   21.522  1.00 19.99 ? 133 VAL A C      1 
ATOM   895  O O      . VAL A 1 115 ? 11.824 9.231   22.218  1.00 21.70 ? 133 VAL A O      1 
ATOM   896  C CB     . VAL A 1 115 ? 12.803 6.762   20.080  1.00 18.19 ? 133 VAL A CB     1 
ATOM   897  C CG1    . VAL A 1 115 ? 12.086 6.050   21.215  1.00 18.36 ? 133 VAL A CG1    1 
ATOM   898  C CG2    . VAL A 1 115 ? 12.339 6.211   18.750  1.00 16.86 ? 133 VAL A CG2    1 
ATOM   899  N N      . ILE A 1 116 ? 14.029 8.925   21.938  1.00 18.64 ? 134 ILE A N      1 
ATOM   900  C CA     . ILE A 1 116 ? 14.281 9.405   23.291  1.00 18.91 ? 134 ILE A CA     1 
ATOM   901  C C      . ILE A 1 116 ? 13.923 10.878  23.424  1.00 18.39 ? 134 ILE A C      1 
ATOM   902  O O      . ILE A 1 116 ? 13.608 11.346  24.522  1.00 16.24 ? 134 ILE A O      1 
ATOM   903  C CB     . ILE A 1 116 ? 15.731 9.124   23.710  1.00 15.60 ? 134 ILE A CB     1 
ATOM   904  C CG1    . ILE A 1 116 ? 16.706 9.848   22.795  1.00 16.06 ? 134 ILE A CG1    1 
ATOM   905  C CG2    . ILE A 1 116 ? 16.006 7.632   23.676  1.00 25.05 ? 134 ILE A CG2    1 
ATOM   906  C CD1    . ILE A 1 116 ? 18.036 9.068   22.599  1.00 19.42 ? 134 ILE A CD1    1 
ATOM   907  N N      . LYS A 1 117 ? 13.925 11.630  22.323  1.00 16.79 ? 135 LYS A N      1 
ATOM   908  C CA     . LYS A 1 117 ? 13.424 12.999  22.404  1.00 24.25 ? 135 LYS A CA     1 
ATOM   909  C C      . LYS A 1 117 ? 11.934 13.026  22.734  1.00 26.86 ? 135 LYS A C      1 
ATOM   910  O O      . LYS A 1 117 ? 11.445 14.009  23.298  1.00 37.32 ? 135 LYS A O      1 
ATOM   911  C CB     . LYS A 1 117 ? 13.706 13.766  21.101  1.00 25.77 ? 135 LYS A CB     1 
ATOM   912  C CG     . LYS A 1 117 ? 13.544 15.293  21.217  1.00 22.11 ? 135 LYS A CG     1 
ATOM   913  C CD     . LYS A 1 117 ? 13.899 16.070  19.927  1.00 22.59 ? 135 LYS A CD     1 
ATOM   914  C CE     . LYS A 1 117 ? 13.493 17.570  19.990  1.00 16.70 ? 135 LYS A CE     1 
ATOM   915  N NZ     . LYS A 1 117 ? 14.046 18.332  21.178  1.00 24.01 ? 135 LYS A NZ     1 
ATOM   916  N N      . GLN A 1 118 ? 11.204 11.954  22.432  1.00 25.36 ? 136 GLN A N      1 
ATOM   917  C CA     . GLN A 1 118 ? 9.776  11.893  22.708  1.00 24.63 ? 136 GLN A CA     1 
ATOM   918  C C      . GLN A 1 118 ? 9.435  11.177  24.007  1.00 23.46 ? 136 GLN A C      1 
ATOM   919  O O      . GLN A 1 118 ? 8.270  11.189  24.414  1.00 27.58 ? 136 GLN A O      1 
ATOM   920  C CB     . GLN A 1 118 ? 9.043  11.219  21.540  1.00 31.99 ? 136 GLN A CB     1 
ATOM   921  C CG     . GLN A 1 118 ? 9.028  12.063  20.248  1.00 40.75 ? 136 GLN A CG     1 
ATOM   922  C CD     . GLN A 1 118 ? 8.065  11.527  19.184  1.00 55.52 ? 136 GLN A CD     1 
ATOM   923  O OE1    . GLN A 1 118 ? 8.460  11.276  18.037  1.00 59.96 ? 136 GLN A OE1    1 
ATOM   924  N NE2    . GLN A 1 118 ? 6.790  11.365  19.559  1.00 53.43 ? 136 GLN A NE2    1 
ATOM   925  N N      . GLU A 1 119 ? 10.448 10.729  24.726  1.00 26.12 ? 137 GLU A N      1 
ATOM   926  C CA     . GLU A 1 119 ? 10.249 9.994   25.951  1.00 26.80 ? 137 GLU A CA     1 
ATOM   927  C C      . GLU A 1 119 ? 11.067 10.498  27.095  1.00 28.66 ? 137 GLU A C      1 
ATOM   928  O O      . GLU A 1 119 ? 11.168 9.828   28.097  1.00 34.79 ? 137 GLU A O      1 
ATOM   929  C CB     . GLU A 1 119 ? 10.675 8.549   25.732  1.00 21.74 ? 137 GLU A CB     1 
ATOM   930  C CG     . GLU A 1 119 ? 9.769  7.698   24.869  1.00 32.59 ? 137 GLU A CG     1 
ATOM   931  C CD     . GLU A 1 119 ? 10.353 6.326   24.616  1.00 41.83 ? 137 GLU A CD     1 
ATOM   932  O OE1    . GLU A 1 119 ? 11.399 6.005   25.209  1.00 41.94 ? 137 GLU A OE1    1 
ATOM   933  O OE2    . GLU A 1 119 ? 9.765  5.565   23.827  1.00 41.65 ? 137 GLU A OE2    1 
ATOM   934  N N      . SER A 1 120 ? 11.675 11.653  26.959  1.00 27.58 ? 138 SER A N      1 
ATOM   935  C CA     . SER A 1 120 ? 12.585 12.088  27.998  1.00 28.78 ? 138 SER A CA     1 
ATOM   936  C C      . SER A 1 120 ? 12.426 13.408  28.613  1.00 31.42 ? 138 SER A C      1 
ATOM   937  O O      . SER A 1 120 ? 12.404 14.414  27.953  1.00 32.10 ? 138 SER A O      1 
ATOM   938  C CB     . SER A 1 120 ? 14.058 11.929  27.581  1.00 30.04 ? 138 SER A CB     1 
ATOM   939  O OG     . SER A 1 120 ? 14.947 11.973  28.673  1.00 30.58 ? 138 SER A OG     1 
ATOM   940  N N      . ASP A 1 121 ? 12.305 13.395  29.916  1.00 38.36 ? 139 ASP A N      1 
ATOM   941  C CA     . ASP A 1 121 ? 12.307 14.595  30.639  1.00 35.34 ? 139 ASP A CA     1 
ATOM   942  C C      . ASP A 1 121 ? 13.769 14.476  30.703  1.00 39.27 ? 139 ASP A C      1 
ATOM   943  O O      . ASP A 1 121 ? 14.294 13.405  30.966  1.00 48.41 ? 139 ASP A O      1 
ATOM   944  C CB     . ASP A 1 121 ? 11.767 14.362  32.049  1.00 31.40 ? 139 ASP A CB     1 
ATOM   945  C CG     . ASP A 1 121 ? 11.820 12.906  32.485  1.00 40.68 ? 139 ASP A CG     1 
ATOM   946  O OD1    . ASP A 1 121 ? 11.060 12.077  31.951  1.00 41.98 ? 139 ASP A OD1    1 
ATOM   947  O OD2    . ASP A 1 121 ? 12.625 12.589  33.376  1.00 40.66 ? 139 ASP A OD2    1 
ATOM   948  N N      . LEU A 1 122 ? 14.496 15.534  30.500  1.00 32.93 ? 140 LEU A N      1 
ATOM   949  C CA     . LEU A 1 122 ? 15.905 15.371  30.479  1.00 29.18 ? 140 LEU A CA     1 
ATOM   950  C C      . LEU A 1 122 ? 16.390 15.514  31.891  1.00 25.82 ? 140 LEU A C      1 
ATOM   951  O O      . LEU A 1 122 ? 17.448 16.050  32.135  1.00 34.07 ? 140 LEU A O      1 
ATOM   952  C CB     . LEU A 1 122 ? 16.459 16.374  29.491  1.00 33.45 ? 140 LEU A CB     1 
ATOM   953  C CG     . LEU A 1 122 ? 15.711 16.327  28.168  1.00 34.41 ? 140 LEU A CG     1 
ATOM   954  C CD1    . LEU A 1 122 ? 15.923 17.604  27.405  1.00 33.02 ? 140 LEU A CD1    1 
ATOM   955  C CD2    . LEU A 1 122 ? 16.163 15.150  27.337  1.00 32.83 ? 140 LEU A CD2    1 
ATOM   956  N N      . SER A 1 123 ? 15.627 15.003  32.828  1.00 26.92 ? 141 SER A N      1 
ATOM   957  C CA     . SER A 1 123 ? 15.924 15.116  34.225  1.00 33.27 ? 141 SER A CA     1 
ATOM   958  C C      . SER A 1 123 ? 17.090 14.275  34.630  1.00 32.37 ? 141 SER A C      1 
ATOM   959  O O      . SER A 1 123 ? 17.779 14.604  35.568  1.00 27.86 ? 141 SER A O      1 
ATOM   960  C CB     . SER A 1 123 ? 14.677 14.695  34.984  1.00 25.01 ? 141 SER A CB     1 
ATOM   961  O OG     . SER A 1 123 ? 15.010 13.923  36.118  1.00 52.82 ? 141 SER A OG     1 
ATOM   962  N N      . VAL A 1 124 ? 17.317 13.193  33.906  1.00 27.95 ? 142 VAL A N      1 
ATOM   963  C CA     . VAL A 1 124 ? 18.455 12.357  34.181  1.00 29.82 ? 142 VAL A CA     1 
ATOM   964  C C      . VAL A 1 124 ? 19.728 13.081  33.851  1.00 24.14 ? 142 VAL A C      1 
ATOM   965  O O      . VAL A 1 124 ? 20.701 12.994  34.566  1.00 22.71 ? 142 VAL A O      1 
ATOM   966  C CB     . VAL A 1 124 ? 18.333 11.015  33.417  1.00 22.66 ? 142 VAL A CB     1 
ATOM   967  C CG1    . VAL A 1 124 ? 18.031 11.198  31.943  1.00 23.60 ? 142 VAL A CG1    1 
ATOM   968  C CG2    . VAL A 1 124 ? 19.521 10.130  33.667  1.00 15.12 ? 142 VAL A CG2    1 
ATOM   969  N N      . PHE A 1 125 ? 19.705 13.853  32.798  1.00 19.01 ? 143 PHE A N      1 
ATOM   970  C CA     . PHE A 1 125 ? 20.911 14.464  32.390  1.00 22.10 ? 143 PHE A CA     1 
ATOM   971  C C      . PHE A 1 125 ? 21.271 15.601  33.305  1.00 25.46 ? 143 PHE A C      1 
ATOM   972  O O      . PHE A 1 125 ? 22.439 15.836  33.525  1.00 27.81 ? 143 PHE A O      1 
ATOM   973  C CB     . PHE A 1 125 ? 20.841 14.864  30.920  1.00 24.50 ? 143 PHE A CB     1 
ATOM   974  C CG     . PHE A 1 125 ? 20.572 13.739  29.984  1.00 20.90 ? 143 PHE A CG     1 
ATOM   975  C CD1    . PHE A 1 125 ? 21.509 12.752  29.788  1.00 17.47 ? 143 PHE A CD1    1 
ATOM   976  C CD2    . PHE A 1 125 ? 19.388 13.687  29.276  1.00 22.16 ? 143 PHE A CD2    1 
ATOM   977  C CE1    . PHE A 1 125 ? 21.265 11.722  28.914  1.00 16.73 ? 143 PHE A CE1    1 
ATOM   978  C CE2    . PHE A 1 125 ? 19.136 12.655  28.401  1.00 21.09 ? 143 PHE A CE2    1 
ATOM   979  C CZ     . PHE A 1 125 ? 20.076 11.668  28.224  1.00 19.76 ? 143 PHE A CZ     1 
ATOM   980  N N      . ASN A 1 126 ? 20.284 16.275  33.880  1.00 29.27 ? 144 ASN A N      1 
ATOM   981  C CA     . ASN A 1 126 ? 20.554 17.342  34.844  1.00 27.18 ? 144 ASN A CA     1 
ATOM   982  C C      . ASN A 1 126 ? 21.095 16.792  36.120  1.00 17.33 ? 144 ASN A C      1 
ATOM   983  O O      . ASN A 1 126 ? 21.886 17.430  36.780  1.00 20.67 ? 144 ASN A O      1 
ATOM   984  C CB     . ASN A 1 126 ? 19.306 18.195  35.046  1.00 24.35 ? 144 ASN A CB     1 
ATOM   985  C CG     . ASN A 1 126 ? 19.214 19.327  34.069  1.00 27.87 ? 144 ASN A CG     1 
ATOM   986  O OD1    . ASN A 1 126 ? 20.029 20.235  34.088  1.00 28.40 ? 144 ASN A OD1    1 
ATOM   987  N ND2    . ASN A 1 126 ? 18.213 19.285  33.214  1.00 30.27 ? 144 ASN A ND2    1 
ATOM   988  N N      . GLU A 1 127 ? 20.653 15.622  36.490  1.00 20.01 ? 145 GLU A N      1 
ATOM   989  C CA     . GLU A 1 127 ? 21.194 14.929  37.631  1.00 24.92 ? 145 GLU A CA     1 
ATOM   990  C C      . GLU A 1 127 ? 22.607 14.383  37.448  1.00 23.78 ? 145 GLU A C      1 
ATOM   991  O O      . GLU A 1 127 ? 23.353 14.304  38.409  1.00 26.28 ? 145 GLU A O      1 
ATOM   992  C CB     . GLU A 1 127 ? 20.227 13.845  38.026  1.00 28.10 ? 145 GLU A CB     1 
ATOM   993  C CG     . GLU A 1 127 ? 18.915 14.346  38.591  1.00 28.56 ? 145 GLU A CG     1 
ATOM   994  C CD     . GLU A 1 127 ? 17.902 13.238  38.748  1.00 35.44 ? 145 GLU A CD     1 
ATOM   995  O OE1    . GLU A 1 127 ? 18.193 12.111  38.314  1.00 29.51 ? 145 GLU A OE1    1 
ATOM   996  O OE2    . GLU A 1 127 ? 16.816 13.496  39.298  1.00 33.02 ? 145 GLU A OE2    1 
ATOM   997  N N      . LEU A 1 128 ? 22.958 13.949  36.242  1.00 22.07 ? 146 LEU A N      1 
ATOM   998  C CA     . LEU A 1 128 ? 24.289 13.444  35.940  1.00 20.85 ? 146 LEU A CA     1 
ATOM   999  C C      . LEU A 1 128 ? 25.335 14.495  36.070  1.00 21.66 ? 146 LEU A C      1 
ATOM   1000 O O      . LEU A 1 128 ? 26.482 14.198  36.307  1.00 27.66 ? 146 LEU A O      1 
ATOM   1001 C CB     . LEU A 1 128 ? 24.365 12.900  34.534  1.00 22.22 ? 146 LEU A CB     1 
ATOM   1002 C CG     . LEU A 1 128 ? 24.379 11.443  34.131  1.00 22.78 ? 146 LEU A CG     1 
ATOM   1003 C CD1    . LEU A 1 128 ? 24.663 11.446  32.644  1.00 19.46 ? 146 LEU A CD1    1 
ATOM   1004 C CD2    . LEU A 1 128 ? 25.473 10.701  34.869  1.00 19.87 ? 146 LEU A CD2    1 
ATOM   1005 N N      . ARG A 1 129 ? 24.958 15.733  35.921  1.00 20.81 ? 147 ARG A N      1 
ATOM   1006 C CA     . ARG A 1 129 ? 25.925 16.781  35.955  1.00 21.81 ? 147 ARG A CA     1 
ATOM   1007 C C      . ARG A 1 129 ? 26.676 16.752  37.253  1.00 24.18 ? 147 ARG A C      1 
ATOM   1008 O O      . ARG A 1 129 ? 27.865 17.002  37.276  1.00 28.42 ? 147 ARG A O      1 
ATOM   1009 C CB     . ARG A 1 129 ? 25.239 18.118  35.757  1.00 19.42 ? 147 ARG A CB     1 
ATOM   1010 C CG     . ARG A 1 129 ? 24.481 18.244  34.458  1.00 24.65 ? 147 ARG A CG     1 
ATOM   1011 C CD     . ARG A 1 129 ? 24.046 19.671  34.192  1.00 32.70 ? 147 ARG A CD     1 
ATOM   1012 N NE     . ARG A 1 129 ? 22.932 20.125  35.014  1.00 44.01 ? 147 ARG A NE     1 
ATOM   1013 C CZ     . ARG A 1 129 ? 23.023 21.058  35.953  1.00 41.50 ? 147 ARG A CZ     1 
ATOM   1014 N NH1    . ARG A 1 129 ? 24.180 21.650  36.198  1.00 33.78 ? 147 ARG A NH1    1 
ATOM   1015 N NH2    . ARG A 1 129 ? 21.949 21.408  36.638  1.00 33.92 ? 147 ARG A NH2    1 
ATOM   1016 N N      . ASP A 1 130 ? 26.004 16.459  38.338  1.00 22.56 ? 148 ASP A N      1 
ATOM   1017 C CA     . ASP A 1 130 ? 26.642 16.361  39.623  1.00 30.84 ? 148 ASP A CA     1 
ATOM   1018 C C      . ASP A 1 130 ? 27.632 15.233  39.684  1.00 24.94 ? 148 ASP A C      1 
ATOM   1019 O O      . ASP A 1 130 ? 28.679 15.349  40.281  1.00 20.10 ? 148 ASP A O      1 
ATOM   1020 C CB     . ASP A 1 130 ? 25.560 16.203  40.668  1.00 31.94 ? 148 ASP A CB     1 
ATOM   1021 C CG     . ASP A 1 130 ? 25.877 16.931  41.949  1.00 55.59 ? 148 ASP A CG     1 
ATOM   1022 O OD1    . ASP A 1 130 ? 26.885 17.666  41.993  1.00 52.40 ? 148 ASP A OD1    1 
ATOM   1023 O OD2    . ASP A 1 130 ? 25.112 16.771  42.916  1.00 63.91 ? 148 ASP A OD2    1 
ATOM   1024 N N      . SER A 1 131 ? 27.319 14.149  39.028  1.00 29.42 ? 149 SER A N      1 
ATOM   1025 C CA     . SER A 1 131 ? 28.196 12.999  38.999  1.00 26.05 ? 149 SER A CA     1 
ATOM   1026 C C      . SER A 1 131 ? 29.429 13.255  38.132  1.00 23.94 ? 149 SER A C      1 
ATOM   1027 O O      . SER A 1 131 ? 30.508 12.794  38.439  1.00 18.65 ? 149 SER A O      1 
ATOM   1028 C CB     . SER A 1 131 ? 27.371 11.804  38.557  1.00 17.35 ? 149 SER A CB     1 
ATOM   1029 O OG     . SER A 1 131 ? 26.308 11.595  39.454  1.00 23.38 ? 149 SER A OG     1 
ATOM   1030 N N      . TYR A 1 132 ? 29.270 13.984  37.049  1.00 18.10 ? 150 TYR A N      1 
ATOM   1031 C CA     . TYR A 1 132 ? 30.394 14.352  36.227  1.00 20.72 ? 150 TYR A CA     1 
ATOM   1032 C C      . TYR A 1 132 ? 31.349 15.274  36.922  1.00 24.44 ? 150 TYR A C      1 
ATOM   1033 O O      . TYR A 1 132 ? 32.535 15.067  36.890  1.00 23.88 ? 150 TYR A O      1 
ATOM   1034 C CB     . TYR A 1 132 ? 29.856 15.005  34.966  1.00 23.14 ? 150 TYR A CB     1 
ATOM   1035 C CG     . TYR A 1 132 ? 30.848 15.821  34.171  1.00 27.69 ? 150 TYR A CG     1 
ATOM   1036 C CD1    . TYR A 1 132 ? 31.831 15.214  33.412  1.00 22.19 ? 150 TYR A CD1    1 
ATOM   1037 C CD2    . TYR A 1 132 ? 30.779 17.200  34.154  1.00 25.52 ? 150 TYR A CD2    1 
ATOM   1038 C CE1    . TYR A 1 132 ? 32.724 15.960  32.681  1.00 19.98 ? 150 TYR A CE1    1 
ATOM   1039 C CE2    . TYR A 1 132 ? 31.671 17.950  33.432  1.00 22.51 ? 150 TYR A CE2    1 
ATOM   1040 C CZ     . TYR A 1 132 ? 32.640 17.323  32.696  1.00 23.85 ? 150 TYR A CZ     1 
ATOM   1041 O OH     . TYR A 1 132 ? 33.526 18.071  31.972  1.00 28.74 ? 150 TYR A OH     1 
ATOM   1042 N N      . ASN A 1 133 ? 30.829 16.274  37.591  1.00 20.64 ? 151 ASN A N      1 
ATOM   1043 C CA     . ASN A 1 133 ? 31.667 17.246  38.269  1.00 21.24 ? 151 ASN A CA     1 
ATOM   1044 C C      . ASN A 1 133 ? 32.469 16.590  39.364  1.00 23.23 ? 151 ASN A C      1 
ATOM   1045 O O      . ASN A 1 133 ? 33.573 17.010  39.648  1.00 23.64 ? 151 ASN A O      1 
ATOM   1046 C CB     . ASN A 1 133 ? 30.847 18.447  38.717  1.00 19.65 ? 151 ASN A CB     1 
ATOM   1047 C CG     . ASN A 1 133 ? 30.175 19.142  37.574  1.00 24.75 ? 151 ASN A CG     1 
ATOM   1048 O OD1    . ASN A 1 133 ? 30.699 19.180  36.475  1.00 33.44 ? 151 ASN A OD1    1 
ATOM   1049 N ND2    . ASN A 1 133 ? 29.014 19.717  37.831  1.00 24.05 ? 151 ASN A ND2    1 
ATOM   1050 N N      . ALA A 1 134 ? 31.900 15.606  40.021  1.00 18.09 ? 152 ALA A N      1 
ATOM   1051 C CA     . ALA A 1 134 ? 32.621 14.832  40.991  1.00 13.86 ? 152 ALA A CA     1 
ATOM   1052 C C      . ALA A 1 134 ? 33.795 14.043  40.462  1.00 21.78 ? 152 ALA A C      1 
ATOM   1053 O O      . ALA A 1 134 ? 34.852 14.036  41.070  1.00 24.13 ? 152 ALA A O      1 
ATOM   1054 C CB     . ALA A 1 134 ? 31.649 13.849  41.546  1.00 10.14 ? 152 ALA A CB     1 
ATOM   1055 N N      . VAL A 1 135 ? 33.625 13.369  39.342  1.00 22.76 ? 153 VAL A N      1 
ATOM   1056 C CA     . VAL A 1 135 ? 34.656 12.514  38.803  1.00 22.37 ? 153 VAL A CA     1 
ATOM   1057 C C      . VAL A 1 135 ? 35.466 13.099  37.674  1.00 23.81 ? 153 VAL A C      1 
ATOM   1058 O O      . VAL A 1 135 ? 36.354 12.455  37.168  1.00 27.77 ? 153 VAL A O      1 
ATOM   1059 C CB     . VAL A 1 135 ? 34.031 11.201  38.347  1.00 29.25 ? 153 VAL A CB     1 
ATOM   1060 C CG1    . VAL A 1 135 ? 33.171 10.598  39.443  1.00 19.11 ? 153 VAL A CG1    1 
ATOM   1061 C CG2    . VAL A 1 135 ? 33.227 11.393  37.072  1.00 22.26 ? 153 VAL A CG2    1 
ATOM   1062 N N      . LYS A 1 136 ? 35.191 14.334  37.308  1.00 26.36 ? 154 LYS A N      1 
ATOM   1063 C CA     . LYS A 1 136 ? 35.892 14.986  36.242  1.00 22.64 ? 154 LYS A CA     1 
ATOM   1064 C C      . LYS A 1 136 ? 37.291 15.260  36.690  1.00 27.36 ? 154 LYS A C      1 
ATOM   1065 O O      . LYS A 1 136 ? 37.562 15.291  37.882  1.00 22.07 ? 154 LYS A O      1 
ATOM   1066 C CB     . LYS A 1 136 ? 35.190 16.276  35.820  1.00 16.38 ? 154 LYS A CB     1 
ATOM   1067 C CG     . LYS A 1 136 ? 35.309 17.417  36.791  1.00 22.36 ? 154 LYS A CG     1 
ATOM   1068 C CD     . LYS A 1 136 ? 34.738 18.684  36.207  1.00 24.71 ? 154 LYS A CD     1 
ATOM   1069 C CE     . LYS A 1 136 ? 35.102 19.847  37.096  1.00 26.02 ? 154 LYS A CE     1 
ATOM   1070 N NZ     . LYS A 1 136 ? 36.567 19.886  37.318  1.00 23.82 ? 154 LYS A NZ     1 
ATOM   1071 N N      . PRO A 1 137 ? 38.210 15.416  35.712  1.00 23.30 ? 155 PRO A N      1 
ATOM   1072 C CA     . PRO A 1 137 ? 39.569 15.742  36.072  1.00 18.24 ? 155 PRO A CA     1 
ATOM   1073 C C      . PRO A 1 137 ? 39.647 17.183  36.509  1.00 24.01 ? 155 PRO A C      1 
ATOM   1074 O O      . PRO A 1 137 ? 38.721 17.926  36.247  1.00 22.82 ? 155 PRO A O      1 
ATOM   1075 C CB     . PRO A 1 137 ? 40.313 15.504  34.780  1.00 15.88 ? 155 PRO A CB     1 
ATOM   1076 C CG     . PRO A 1 137 ? 39.459 14.622  33.962  1.00 21.32 ? 155 PRO A CG     1 
ATOM   1077 C CD     . PRO A 1 137 ? 38.112 15.144  34.266  1.00 20.32 ? 155 PRO A CD     1 
ATOM   1078 N N      . GLU A 1 138 ? 40.724 17.584  37.177  1.00 25.97 ? 156 GLU A N      1 
ATOM   1079 C CA     . GLU A 1 138 ? 40.849 18.995  37.529  1.00 27.16 ? 156 GLU A CA     1 
ATOM   1080 C C      . GLU A 1 138 ? 40.761 19.897  36.296  1.00 28.53 ? 156 GLU A C      1 
ATOM   1081 O O      . GLU A 1 138 ? 40.252 21.021  36.384  1.00 28.70 ? 156 GLU A O      1 
ATOM   1082 C CB     . GLU A 1 138 ? 42.143 19.229  38.288  1.00 24.41 ? 156 GLU A CB     1 
ATOM   1083 C CG     . GLU A 1 138 ? 42.616 20.647  38.212  1.00 36.23 ? 156 GLU A CG     1 
ATOM   1084 C CD     . GLU A 1 138 ? 44.132 20.748  38.281  1.00 57.97 ? 156 GLU A CD     1 
ATOM   1085 O OE1    . GLU A 1 138 ? 44.803 19.685  38.389  1.00 46.96 ? 156 GLU A OE1    1 
ATOM   1086 O OE2    . GLU A 1 138 ? 44.645 21.895  38.225  1.00 54.27 ? 156 GLU A OE2    1 
ATOM   1087 N N      . TYR A 1 139 ? 41.185 19.408  35.130  1.00 26.68 ? 157 TYR A N      1 
ATOM   1088 C CA     . TYR A 1 139 ? 41.227 20.199  33.896  1.00 21.44 ? 157 TYR A CA     1 
ATOM   1089 C C      . TYR A 1 139 ? 39.992 20.220  33.048  1.00 22.52 ? 157 TYR A C      1 
ATOM   1090 O O      . TYR A 1 139 ? 39.943 20.875  32.033  1.00 21.09 ? 157 TYR A O      1 
ATOM   1091 C CB     . TYR A 1 139 ? 42.409 19.758  33.056  1.00 21.62 ? 157 TYR A CB     1 
ATOM   1092 C CG     . TYR A 1 139 ? 42.578 18.286  32.857  1.00 20.03 ? 157 TYR A CG     1 
ATOM   1093 C CD1    . TYR A 1 139 ? 41.854 17.612  31.894  1.00 21.64 ? 157 TYR A CD1    1 
ATOM   1094 C CD2    . TYR A 1 139 ? 43.498 17.576  33.602  1.00 18.16 ? 157 TYR A CD2    1 
ATOM   1095 C CE1    . TYR A 1 139 ? 42.022 16.268  31.699  1.00 20.01 ? 157 TYR A CE1    1 
ATOM   1096 C CE2    . TYR A 1 139 ? 43.674 16.228  33.411  1.00 18.67 ? 157 TYR A CE2    1 
ATOM   1097 C CZ     . TYR A 1 139 ? 42.932 15.582  32.456  1.00 20.82 ? 157 TYR A CZ     1 
ATOM   1098 O OH     . TYR A 1 139 ? 43.100 14.240  32.264  1.00 29.61 ? 157 TYR A OH     1 
ATOM   1099 N N      . ALA A 1 140 ? 38.981 19.499  33.463  1.00 20.81 ? 158 ALA A N      1 
ATOM   1100 C CA     . ALA A 1 140 ? 37.756 19.541  32.743  1.00 24.61 ? 158 ALA A CA     1 
ATOM   1101 C C      . ALA A 1 140 ? 36.920 20.665  33.308  1.00 30.03 ? 158 ALA A C      1 
ATOM   1102 O O      . ALA A 1 140 ? 37.052 21.022  34.459  1.00 31.15 ? 158 ALA A O      1 
ATOM   1103 C CB     . ALA A 1 140 ? 37.046 18.234  32.873  1.00 22.59 ? 158 ALA A CB     1 
ATOM   1104 N N      . VAL A 1 141 ? 36.061 21.230  32.477  1.00 26.72 ? 159 VAL A N      1 
ATOM   1105 C CA     . VAL A 1 141 ? 35.219 22.321  32.958  1.00 24.35 ? 159 VAL A CA     1 
ATOM   1106 C C      . VAL A 1 141 ? 34.024 21.756  33.715  1.00 30.53 ? 159 VAL A C      1 
ATOM   1107 O O      . VAL A 1 141 ? 33.395 20.785  33.280  1.00 33.41 ? 159 VAL A O      1 
ATOM   1108 C CB     . VAL A 1 141 ? 34.768 23.218  31.791  1.00 21.00 ? 159 VAL A CB     1 
ATOM   1109 C CG1    . VAL A 1 141 ? 33.608 24.098  32.221  1.00 19.80 ? 159 VAL A CG1    1 
ATOM   1110 C CG2    . VAL A 1 141 ? 35.923 24.078  31.283  1.00 26.49 ? 159 VAL A CG2    1 
ATOM   1111 N N      . THR A 1 142 ? 33.702 22.368  34.855  1.00 32.47 ? 160 THR A N      1 
ATOM   1112 C CA     . THR A 1 142 ? 32.428 22.106  35.515  1.00 30.90 ? 160 THR A CA     1 
ATOM   1113 C C      . THR A 1 142 ? 31.273 22.493  34.602  1.00 26.27 ? 160 THR A C      1 
ATOM   1114 O O      . THR A 1 142 ? 31.283 23.570  34.004  1.00 36.22 ? 160 THR A O      1 
ATOM   1115 C CB     . THR A 1 142 ? 32.341 22.903  36.815  1.00 30.35 ? 160 THR A CB     1 
ATOM   1116 O OG1    . THR A 1 142 ? 33.598 22.832  37.487  1.00 34.07 ? 160 THR A OG1    1 
ATOM   1117 C CG2    . THR A 1 142 ? 31.276 22.333  37.727  1.00 29.04 ? 160 THR A CG2    1 
ATOM   1118 N N      . HIS A 1 143 ? 30.265 21.627  34.512  1.00 26.10 ? 161 HIS A N      1 
ATOM   1119 C CA     . HIS A 1 143 ? 29.035 21.933  33.781  1.00 30.15 ? 161 HIS A CA     1 
ATOM   1120 C C      . HIS A 1 143 ? 28.056 22.618  34.741  1.00 39.16 ? 161 HIS A C      1 
ATOM   1121 O O      . HIS A 1 143 ? 27.535 21.986  35.666  1.00 35.54 ? 161 HIS A O      1 
ATOM   1122 C CB     . HIS A 1 143 ? 28.441 20.664  33.179  1.00 20.18 ? 161 HIS A CB     1 
ATOM   1123 C CG     . HIS A 1 143 ? 27.390 20.915  32.150  1.00 23.77 ? 161 HIS A CG     1 
ATOM   1124 N ND1    . HIS A 1 143 ? 26.141 21.402  32.463  1.00 30.96 ? 161 HIS A ND1    1 
ATOM   1125 C CD2    . HIS A 1 143 ? 27.396 20.731  30.811  1.00 31.77 ? 161 HIS A CD2    1 
ATOM   1126 C CE1    . HIS A 1 143 ? 25.423 21.509  31.359  1.00 32.31 ? 161 HIS A CE1    1 
ATOM   1127 N NE2    . HIS A 1 143 ? 26.161 21.107  30.342  1.00 30.88 ? 161 HIS A NE2    1 
ATOM   1128 N N      . GLU A 1 144 ? 27.816 23.916  34.525  1.00 45.48 ? 162 GLU A N      1 
ATOM   1129 C CA     . GLU A 1 144 ? 27.017 24.748  35.423  1.00 46.18 ? 162 GLU A CA     1 
ATOM   1130 C C      . GLU A 1 144 ? 25.607 25.037  34.915  1.00 47.57 ? 162 GLU A C      1 
ATOM   1131 O O      . GLU A 1 144 ? 24.675 25.078  35.720  1.00 47.59 ? 162 GLU A O      1 
ATOM   1132 C CB     . GLU A 1 144 ? 27.735 26.085  35.672  1.00 44.89 ? 162 GLU A CB     1 
ATOM   1133 C CG     . GLU A 1 144 ? 29.175 26.001  36.202  1.00 45.61 ? 162 GLU A CG     1 
ATOM   1134 C CD     . GLU A 1 144 ? 29.270 25.944  37.727  1.00 56.26 ? 162 GLU A CD     1 
ATOM   1135 O OE1    . GLU A 1 144 ? 28.673 25.019  38.326  1.00 64.64 ? 162 GLU A OE1    1 
ATOM   1136 O OE2    . GLU A 1 144 ? 29.948 26.817  38.323  1.00 42.45 ? 162 GLU A OE2    1 
ATOM   1137 N N      . THR A 1 145 ? 25.430 25.249  33.611  1.00 38.47 ? 163 THR A N      1 
ATOM   1138 C CA     . THR A 1 145 ? 24.124 25.536  33.040  1.00 35.28 ? 163 THR A CA     1 
ATOM   1139 C C      . THR A 1 145 ? 23.158 24.368  33.253  1.00 40.80 ? 163 THR A C      1 
ATOM   1140 O O      . THR A 1 145 ? 23.543 23.258  33.628  1.00 39.91 ? 163 THR A O      1 
ATOM   1141 C CB     . THR A 1 145 ? 24.250 25.829  31.547  1.00 40.93 ? 163 THR A CB     1 
ATOM   1142 O OG1    . THR A 1 145 ? 24.325 24.594  30.818  1.00 39.27 ? 163 THR A OG1    1 
ATOM   1143 C CG2    . THR A 1 145 ? 25.505 26.643  31.286  1.00 43.52 ? 163 THR A CG2    1 
ATOM   1144 N N      . GLU A 1 146 ? 21.882 24.630  32.989  1.00 35.14 ? 164 GLU A N      1 
ATOM   1145 C CA     . GLU A 1 146 ? 20.843 23.611  33.052  1.00 35.87 ? 164 GLU A CA     1 
ATOM   1146 C C      . GLU A 1 146 ? 20.568 23.087  31.650  1.00 39.05 ? 164 GLU A C      1 
ATOM   1147 O O      . GLU A 1 146 ? 20.609 23.840  30.674  1.00 38.55 ? 164 GLU A O      1 
ATOM   1148 C CB     . GLU A 1 146 ? 19.553 24.169  33.664  1.00 31.71 ? 164 GLU A CB     1 
ATOM   1149 C CG     . GLU A 1 146 ? 18.522 23.124  34.023  1.00 33.92 ? 164 GLU A CG     1 
ATOM   1150 C CD     . GLU A 1 146 ? 17.190 23.345  33.315  1.00 51.55 ? 164 GLU A CD     1 
ATOM   1151 O OE1    . GLU A 1 146 ? 17.040 24.397  32.649  1.00 54.76 ? 164 GLU A OE1    1 
ATOM   1152 O OE2    . GLU A 1 146 ? 16.292 22.469  33.421  1.00 45.17 ? 164 GLU A OE2    1 
ATOM   1153 N N      . ILE A 1 147 ? 20.283 21.798  31.553  1.00 36.36 ? 165 ILE A N      1 
ATOM   1154 C CA     . ILE A 1 147 ? 20.020 21.158  30.273  1.00 29.38 ? 165 ILE A CA     1 
ATOM   1155 C C      . ILE A 1 147 ? 18.534 21.275  29.959  1.00 34.60 ? 165 ILE A C      1 
ATOM   1156 O O      . ILE A 1 147 ? 17.694 20.683  30.648  1.00 38.10 ? 165 ILE A O      1 
ATOM   1157 C CB     . ILE A 1 147 ? 20.456 19.688  30.298  1.00 30.22 ? 165 ILE A CB     1 
ATOM   1158 C CG1    . ILE A 1 147 ? 21.939 19.578  30.660  1.00 27.19 ? 165 ILE A CG1    1 
ATOM   1159 C CG2    . ILE A 1 147 ? 20.132 19.024  28.966  1.00 31.39 ? 165 ILE A CG2    1 
ATOM   1160 C CD1    . ILE A 1 147 ? 22.364 18.180  30.973  1.00 22.32 ? 165 ILE A CD1    1 
ATOM   1161 N N      . LYS A 1 148 ? 18.201 22.016  28.905  1.00 33.42 ? 166 LYS A N      1 
ATOM   1162 C CA     . LYS A 1 148 ? 16.819 22.094  28.446  1.00 34.97 ? 166 LYS A CA     1 
ATOM   1163 C C      . LYS A 1 148 ? 16.578 21.368  27.129  1.00 31.58 ? 166 LYS A C      1 
ATOM   1164 O O      . LYS A 1 148 ? 15.519 20.767  26.952  1.00 33.30 ? 166 LYS A O      1 
ATOM   1165 C CB     . LYS A 1 148 ? 16.400 23.565  28.317  1.00 41.35 ? 166 LYS A CB     1 
ATOM   1166 C CG     . LYS A 1 148 ? 16.867 24.428  29.505  1.00 39.68 ? 166 LYS A CG     1 
ATOM   1167 C CD     . LYS A 1 148 ? 16.660 25.919  29.271  1.00 46.30 ? 166 LYS A CD     1 
ATOM   1168 C CE     . LYS A 1 148 ? 15.186 26.300  29.389  1.00 63.24 ? 166 LYS A CE     1 
ATOM   1169 N NZ     . LYS A 1 148 ? 14.907 27.710  28.954  1.00 46.48 ? 166 LYS A NZ     1 
ATOM   1170 N N      . THR A 1 149 ? 17.543 21.395  26.215  1.00 37.16 ? 167 THR A N      1 
ATOM   1171 C CA     . THR A 1 149 ? 17.461 20.760  24.907  1.00 36.10 ? 167 THR A CA     1 
ATOM   1172 C C      . THR A 1 149 ? 18.094 19.379  24.937  1.00 35.70 ? 167 THR A C      1 
ATOM   1173 O O      . THR A 1 149 ? 19.012 19.115  25.721  1.00 35.24 ? 167 THR A O      1 
ATOM   1174 C CB     . THR A 1 149 ? 18.191 21.583  23.844  1.00 42.14 ? 167 THR A CB     1 
ATOM   1175 O OG1    . THR A 1 149 ? 17.750 22.942  23.902  1.00 42.97 ? 167 THR A OG1    1 
ATOM   1176 C CG2    . THR A 1 149 ? 17.910 20.999  22.441  1.00 43.12 ? 167 THR A CG2    1 
ATOM   1177 N N      . LEU A 1 150 ? 17.733 18.451  24.051  1.00 29.10 ? 168 LEU A N      1 
ATOM   1178 C CA     . LEU A 1 150 ? 18.419 17.163  23.946  1.00 23.55 ? 168 LEU A CA     1 
ATOM   1179 C C      . LEU A 1 150 ? 19.807 17.347  23.359  1.00 25.08 ? 168 LEU A C      1 
ATOM   1180 O O      . LEU A 1 150 ? 20.674 16.541  23.564  1.00 21.59 ? 168 LEU A O      1 
ATOM   1181 C CB     . LEU A 1 150 ? 17.613 16.202  23.090  1.00 21.48 ? 168 LEU A CB     1 
ATOM   1182 C CG     . LEU A 1 150 ? 18.028 14.738  22.956  1.00 21.27 ? 168 LEU A CG     1 
ATOM   1183 C CD1    . LEU A 1 150 ? 17.601 13.909  24.148  1.00 19.29 ? 168 LEU A CD1    1 
ATOM   1184 C CD2    . LEU A 1 150 ? 17.498 14.134  21.674  1.00 20.17 ? 168 LEU A CD2    1 
ATOM   1185 N N      . ASP A 1 151 ? 20.034 18.434  22.668  1.00 31.68 ? 169 ASP A N      1 
ATOM   1186 C CA     . ASP A 1 151 ? 21.312 18.723  22.063  1.00 28.80 ? 169 ASP A CA     1 
ATOM   1187 C C      . ASP A 1 151 ? 22.299 19.180  23.062  1.00 26.20 ? 169 ASP A C      1 
ATOM   1188 O O      . ASP A 1 151 ? 23.484 19.029  22.863  1.00 25.43 ? 169 ASP A O      1 
ATOM   1189 C CB     . ASP A 1 151 ? 21.151 19.828  21.040  1.00 23.20 ? 169 ASP A CB     1 
ATOM   1190 C CG     . ASP A 1 151 ? 20.353 19.409  19.829  1.00 42.03 ? 169 ASP A CG     1 
ATOM   1191 O OD1    . ASP A 1 151 ? 19.168 19.056  19.980  1.00 46.48 ? 169 ASP A OD1    1 
ATOM   1192 O OD2    . ASP A 1 151 ? 20.905 19.458  18.713  1.00 32.98 ? 169 ASP A OD2    1 
ATOM   1193 N N      . GLU A 1 152 ? 21.819 19.749  24.142  1.00 27.92 ? 170 GLU A N      1 
ATOM   1194 C CA     . GLU A 1 152 ? 22.672 20.201  25.194  1.00 29.09 ? 170 GLU A CA     1 
ATOM   1195 C C      . GLU A 1 152 ? 22.991 18.994  26.024  1.00 25.49 ? 170 GLU A C      1 
ATOM   1196 O O      . GLU A 1 152 ? 24.031 18.913  26.639  1.00 21.82 ? 170 GLU A O      1 
ATOM   1197 C CB     . GLU A 1 152 ? 21.914 21.225  26.022  1.00 30.41 ? 170 GLU A CB     1 
ATOM   1198 C CG     . GLU A 1 152 ? 21.956 22.660  25.566  1.00 32.52 ? 170 GLU A CG     1 
ATOM   1199 C CD     . GLU A 1 152 ? 21.075 23.526  26.441  1.00 41.61 ? 170 GLU A CD     1 
ATOM   1200 O OE1    . GLU A 1 152 ? 20.122 22.989  27.022  1.00 39.09 ? 170 GLU A OE1    1 
ATOM   1201 O OE2    . GLU A 1 152 ? 21.330 24.737  26.560  1.00 47.28 ? 170 GLU A OE2    1 
ATOM   1202 N N      . ALA A 1 153 ? 22.091 18.042  26.038  1.00 22.18 ? 171 ALA A N      1 
ATOM   1203 C CA     . ALA A 1 153 ? 22.330 16.818  26.731  1.00 23.35 ? 171 ALA A CA     1 
ATOM   1204 C C      . ALA A 1 153 ? 23.375 16.027  25.975  1.00 24.31 ? 171 ALA A C      1 
ATOM   1205 O O      . ALA A 1 153 ? 24.157 15.323  26.584  1.00 15.48 ? 171 ALA A O      1 
ATOM   1206 C CB     . ALA A 1 153 ? 21.043 16.061  26.814  1.00 21.24 ? 171 ALA A CB     1 
ATOM   1207 N N      . LYS A 1 154 ? 23.411 16.177  24.658  1.00 22.12 ? 172 LYS A N      1 
ATOM   1208 C CA     . LYS A 1 154 ? 24.397 15.519  23.831  1.00 18.44 ? 172 LYS A CA     1 
ATOM   1209 C C      . LYS A 1 154 ? 25.740 16.110  24.005  1.00 20.48 ? 172 LYS A C      1 
ATOM   1210 O O      . LYS A 1 154 ? 26.702 15.406  24.112  1.00 18.89 ? 172 LYS A O      1 
ATOM   1211 C CB     . LYS A 1 154 ? 24.018 15.662  22.374  1.00 23.31 ? 172 LYS A CB     1 
ATOM   1212 C CG     . LYS A 1 154 ? 22.932 14.736  21.891  1.00 26.47 ? 172 LYS A CG     1 
ATOM   1213 C CD     . LYS A 1 154 ? 22.696 14.968  20.416  1.00 29.40 ? 172 LYS A CD     1 
ATOM   1214 C CE     . LYS A 1 154 ? 24.014 15.280  19.730  1.00 42.07 ? 172 LYS A CE     1 
ATOM   1215 N NZ     . LYS A 1 154 ? 24.075 14.797  18.322  1.00 42.69 ? 172 LYS A NZ     1 
ATOM   1216 N N      . GLN A 1 155 ? 25.810 17.417  24.062  1.00 26.75 ? 173 GLN A N      1 
ATOM   1217 C CA     . GLN A 1 155 ? 27.056 18.116  24.232  1.00 20.48 ? 173 GLN A CA     1 
ATOM   1218 C C      . GLN A 1 155 ? 27.670 17.917  25.569  1.00 20.29 ? 173 GLN A C      1 
ATOM   1219 O O      . GLN A 1 155 ? 28.848 18.134  25.737  1.00 25.42 ? 173 GLN A O      1 
ATOM   1220 C CB     . GLN A 1 155 ? 26.795 19.594  23.983  1.00 29.00 ? 173 GLN A CB     1 
ATOM   1221 C CG     . GLN A 1 155 ? 26.963 20.017  22.538  1.00 31.06 ? 173 GLN A CG     1 
ATOM   1222 C CD     . GLN A 1 155 ? 28.325 19.651  21.984  1.00 50.87 ? 173 GLN A CD     1 
ATOM   1223 O OE1    . GLN A 1 155 ? 28.444 18.775  21.134  1.00 56.21 ? 173 GLN A OE1    1 
ATOM   1224 N NE2    . GLN A 1 155 ? 29.362 20.327  22.463  1.00 48.78 ? 173 GLN A NE2    1 
ATOM   1225 N N      . PHE A 1 156 ? 26.883 17.495  26.526  1.00 24.05 ? 174 PHE A N      1 
ATOM   1226 C CA     . PHE A 1 156 ? 27.350 17.226  27.860  1.00 25.55 ? 174 PHE A CA     1 
ATOM   1227 C C      . PHE A 1 156 ? 27.921 15.844  27.961  1.00 18.53 ? 174 PHE A C      1 
ATOM   1228 O O      . PHE A 1 156 ? 29.000 15.664  28.448  1.00 19.14 ? 174 PHE A O      1 
ATOM   1229 C CB     . PHE A 1 156 ? 26.167 17.400  28.817  1.00 24.07 ? 174 PHE A CB     1 
ATOM   1230 C CG     . PHE A 1 156 ? 26.378 16.833  30.184  1.00 24.50 ? 174 PHE A CG     1 
ATOM   1231 C CD1    . PHE A 1 156 ? 27.396 17.292  30.996  1.00 25.74 ? 174 PHE A CD1    1 
ATOM   1232 C CD2    . PHE A 1 156 ? 25.532 15.856  30.663  1.00 19.74 ? 174 PHE A CD2    1 
ATOM   1233 C CE1    . PHE A 1 156 ? 27.581 16.768  32.249  1.00 24.87 ? 174 PHE A CE1    1 
ATOM   1234 C CE2    . PHE A 1 156 ? 25.711 15.330  31.912  1.00 18.86 ? 174 PHE A CE2    1 
ATOM   1235 C CZ     . PHE A 1 156 ? 26.740 15.783  32.702  1.00 26.21 ? 174 PHE A CZ     1 
ATOM   1236 N N      . ILE A 1 157 ? 27.193 14.863  27.486  1.00 19.10 ? 175 ILE A N      1 
ATOM   1237 C CA     . ILE A 1 157 ? 27.632 13.498  27.592  1.00 20.19 ? 175 ILE A CA     1 
ATOM   1238 C C      . ILE A 1 157 ? 28.784 13.213  26.681  1.00 20.63 ? 175 ILE A C      1 
ATOM   1239 O O      . ILE A 1 157 ? 29.569 12.349  26.937  1.00 21.43 ? 175 ILE A O      1 
ATOM   1240 C CB     . ILE A 1 157 ? 26.490 12.500  27.386  1.00 18.32 ? 175 ILE A CB     1 
ATOM   1241 C CG1    . ILE A 1 157 ? 25.896 12.596  25.992  1.00 13.78 ? 175 ILE A CG1    1 
ATOM   1242 C CG2    . ILE A 1 157 ? 25.439 12.664  28.470  1.00 17.53 ? 175 ILE A CG2    1 
ATOM   1243 C CD1    . ILE A 1 157 ? 25.175 11.349  25.580  1.00 11.23 ? 175 ILE A CD1    1 
ATOM   1244 N N      . LEU A 1 158 ? 28.941 14.011  25.655  1.00 15.92 ? 176 LEU A N      1 
ATOM   1245 C CA     . LEU A 1 158 ? 30.008 13.811  24.747  1.00 14.20 ? 176 LEU A CA     1 
ATOM   1246 C C      . LEU A 1 158 ? 31.207 14.565  25.185  1.00 17.02 ? 176 LEU A C      1 
ATOM   1247 O O      . LEU A 1 158 ? 32.101 14.743  24.421  1.00 31.95 ? 176 LEU A O      1 
ATOM   1248 C CB     . LEU A 1 158 ? 29.574 14.193  23.334  1.00 15.34 ? 176 LEU A CB     1 
ATOM   1249 C CG     . LEU A 1 158 ? 29.193 13.184  22.260  1.00 12.62 ? 176 LEU A CG     1 
ATOM   1250 C CD1    . LEU A 1 158 ? 28.192 12.164  22.761  1.00 12.90 ? 176 LEU A CD1    1 
ATOM   1251 C CD2    . LEU A 1 158 ? 28.616 13.949  21.087  1.00 17.44 ? 176 LEU A CD2    1 
ATOM   1252 N N      . SER A 1 159 ? 31.273 14.959  26.429  1.00 18.99 ? 177 SER A N      1 
ATOM   1253 C CA     . SER A 1 159 ? 32.372 15.746  26.946  1.00 20.37 ? 177 SER A CA     1 
ATOM   1254 C C      . SER A 1 159 ? 33.033 14.952  27.980  1.00 20.26 ? 177 SER A C      1 
ATOM   1255 O O      . SER A 1 159 ? 33.956 15.397  28.628  1.00 20.36 ? 177 SER A O      1 
ATOM   1256 C CB     . SER A 1 159 ? 31.825 17.001  27.583  1.00 22.77 ? 177 SER A CB     1 
ATOM   1257 O OG     . SER A 1 159 ? 31.391 16.772  28.904  1.00 26.71 ? 177 SER A OG     1 
ATOM   1258 N N      . PHE A 1 160 ? 32.551 13.742  28.132  1.00 21.36 ? 178 PHE A N      1 
ATOM   1259 C CA     . PHE A 1 160 ? 33.074 12.881  29.127  1.00 19.32 ? 178 PHE A CA     1 
ATOM   1260 C C      . PHE A 1 160 ? 34.375 12.361  28.590  1.00 26.76 ? 178 PHE A C      1 
ATOM   1261 O O      . PHE A 1 160 ? 35.042 11.613  29.260  1.00 26.68 ? 178 PHE A O      1 
ATOM   1262 C CB     . PHE A 1 160 ? 32.109 11.737  29.326  1.00 22.32 ? 178 PHE A CB     1 
ATOM   1263 C CG     . PHE A 1 160 ? 30.819 12.104  30.015  1.00 23.03 ? 178 PHE A CG     1 
ATOM   1264 C CD1    . PHE A 1 160 ? 30.603 13.355  30.551  1.00 22.37 ? 178 PHE A CD1    1 
ATOM   1265 C CD2    . PHE A 1 160 ? 29.816 11.161  30.133  1.00 23.21 ? 178 PHE A CD2    1 
ATOM   1266 C CE1    . PHE A 1 160 ? 29.414 13.661  31.173  1.00 29.52 ? 178 PHE A CE1    1 
ATOM   1267 C CE2    . PHE A 1 160 ? 28.623 11.463  30.755  1.00 23.41 ? 178 PHE A CE2    1 
ATOM   1268 C CZ     . PHE A 1 160 ? 28.424 12.715  31.280  1.00 24.56 ? 178 PHE A CZ     1 
ATOM   1269 N N      . VAL A 1 161 ? 34.730 12.739  27.372  1.00 25.03 ? 179 VAL A N      1 
ATOM   1270 C CA     . VAL A 1 161 ? 35.980 12.350  26.785  1.00 17.21 ? 179 VAL A CA     1 
ATOM   1271 C C      . VAL A 1 161 ? 37.157 13.097  27.394  1.00 20.00 ? 179 VAL A C      1 
ATOM   1272 O O      . VAL A 1 161 ? 38.302 12.808  27.101  1.00 24.14 ? 179 VAL A O      1 
ATOM   1273 C CB     . VAL A 1 161 ? 35.881 12.644  25.288  1.00 17.53 ? 179 VAL A CB     1 
ATOM   1274 C CG1    . VAL A 1 161 ? 35.948 14.131  25.007  1.00 18.49 ? 179 VAL A CG1    1 
ATOM   1275 C CG2    . VAL A 1 161 ? 36.891 11.843  24.488  1.00 20.17 ? 179 VAL A CG2    1 
ATOM   1276 N N      . MET A 1 162 ? 36.895 14.054  28.261  1.00 20.75 ? 180 MET A N      1 
ATOM   1277 C CA     . MET A 1 162 ? 37.964 14.769  28.918  1.00 24.29 ? 180 MET A CA     1 
ATOM   1278 C C      . MET A 1 162 ? 38.431 13.984  30.084  1.00 21.94 ? 180 MET A C      1 
ATOM   1279 O O      . MET A 1 162 ? 39.410 14.283  30.697  1.00 28.27 ? 180 MET A O      1 
ATOM   1280 C CB     . MET A 1 162 ? 37.529 16.162  29.314  1.00 24.65 ? 180 MET A CB     1 
ATOM   1281 C CG     . MET A 1 162 ? 38.608 17.211  29.149  1.00 27.12 ? 180 MET A CG     1 
ATOM   1282 S SD     . MET A 1 162 ? 38.712 17.706  27.432  1.00 43.62 ? 180 MET A SD     1 
ATOM   1283 C CE     . MET A 1 162 ? 37.002 17.549  26.950  1.00 23.24 ? 180 MET A CE     1 
ATOM   1284 N N      . LEU A 1 163 ? 37.717 12.939  30.377  1.00 20.48 ? 181 LEU A N      1 
ATOM   1285 C CA     . LEU A 1 163 ? 38.092 12.107  31.443  1.00 20.29 ? 181 LEU A CA     1 
ATOM   1286 C C      . LEU A 1 163 ? 39.021 11.028  30.893  1.00 26.65 ? 181 LEU A C      1 
ATOM   1287 O O      . LEU A 1 163 ? 39.684 10.418  31.641  1.00 25.27 ? 181 LEU A O      1 
ATOM   1288 C CB     . LEU A 1 163 ? 36.847 11.575  32.112  1.00 18.26 ? 181 LEU A CB     1 
ATOM   1289 C CG     . LEU A 1 163 ? 35.991 12.375  33.083  1.00 19.94 ? 181 LEU A CG     1 
ATOM   1290 C CD1    . LEU A 1 163 ? 35.417 13.617  32.428  1.00 23.95 ? 181 LEU A CD1    1 
ATOM   1291 C CD2    . LEU A 1 163 ? 34.866 11.480  33.559  1.00 18.80 ? 181 LEU A CD2    1 
ATOM   1292 N N      . ASN A 1 164 ? 39.166 10.900  29.587  1.00 24.39 ? 182 ASN A N      1 
ATOM   1293 C CA     . ASN A 1 164 ? 40.019 9.899   28.956  1.00 20.21 ? 182 ASN A CA     1 
ATOM   1294 C C      . ASN A 1 164 ? 41.506 9.911   29.233  1.00 23.10 ? 182 ASN A C      1 
ATOM   1295 O O      . ASN A 1 164 ? 42.094 10.956  29.374  1.00 23.37 ? 182 ASN A O      1 
ATOM   1296 C CB     . ASN A 1 164 ? 39.819 9.931   27.442  1.00 26.75 ? 182 ASN A CB     1 
ATOM   1297 C CG     . ASN A 1 164 ? 38.702 9.041   26.960  1.00 26.87 ? 182 ASN A CG     1 
ATOM   1298 O OD1    . ASN A 1 164 ? 37.622 9.032   27.513  1.00 22.19 ? 182 ASN A OD1    1 
ATOM   1299 N ND2    . ASN A 1 164 ? 38.957 8.313   25.891  1.00 22.33 ? 182 ASN A ND2    1 
ATOM   1300 N N      . ASP A 1 165 ? 42.119 8.740   29.268  1.00 23.75 ? 183 ASP A N      1 
ATOM   1301 C CA     . ASP A 1 165 ? 43.546 8.583   29.586  1.00 19.94 ? 183 ASP A CA     1 
ATOM   1302 C C      . ASP A 1 165 ? 43.940 8.921   31.020  1.00 16.30 ? 183 ASP A C      1 
ATOM   1303 O O      . ASP A 1 165 ? 45.082 9.235   31.268  1.00 19.24 ? 183 ASP A O      1 
ATOM   1304 C CB     . ASP A 1 165 ? 44.443 9.168   28.496  1.00 16.90 ? 183 ASP A CB     1 
ATOM   1305 C CG     . ASP A 1 165 ? 44.221 8.529   27.146  1.00 25.00 ? 183 ASP A CG     1 
ATOM   1306 O OD1    . ASP A 1 165 ? 44.153 7.291   27.056  1.00 29.83 ? 183 ASP A OD1    1 
ATOM   1307 O OD2    . ASP A 1 165 ? 44.126 9.270   26.159  1.00 30.29 ? 183 ASP A OD2    1 
ATOM   1308 N N      . ASN A 1 166 ? 43.016 8.773   31.960  1.00 16.57 ? 184 ASN A N      1 
ATOM   1309 C CA     . ASN A 1 166 ? 43.214 9.105   33.360  1.00 20.57 ? 184 ASN A CA     1 
ATOM   1310 C C      . ASN A 1 166 ? 41.876 8.728   33.858  1.00 25.08 ? 184 ASN A C      1 
ATOM   1311 O O      . ASN A 1 166 ? 41.045 8.665   33.023  1.00 37.28 ? 184 ASN A O      1 
ATOM   1312 C CB     . ASN A 1 166 ? 43.297 10.639  33.476  1.00 16.59 ? 184 ASN A CB     1 
ATOM   1313 C CG     . ASN A 1 166 ? 43.463 11.137  34.885  1.00 21.23 ? 184 ASN A CG     1 
ATOM   1314 O OD1    . ASN A 1 166 ? 43.859 10.409  35.783  1.00 29.67 ? 184 ASN A OD1    1 
ATOM   1315 N ND2    . ASN A 1 166 ? 43.175 12.409  35.078  1.00 21.47 ? 184 ASN A ND2    1 
ATOM   1316 N N      . VAL A 1 167 ? 41.623 8.502   35.140  1.00 22.52 ? 185 VAL A N      1 
ATOM   1317 C CA     . VAL A 1 167 ? 40.232 8.308   35.675  1.00 30.43 ? 185 VAL A CA     1 
ATOM   1318 C C      . VAL A 1 167 ? 39.611 6.971   35.260  1.00 26.69 ? 185 VAL A C      1 
ATOM   1319 O O      . VAL A 1 167 ? 39.125 6.259   36.147  1.00 29.28 ? 185 VAL A O      1 
ATOM   1320 C CB     . VAL A 1 167 ? 39.295 9.508   35.405  1.00 22.66 ? 185 VAL A CB     1 
ATOM   1321 C CG1    . VAL A 1 167 ? 37.892 9.296   35.939  1.00 18.67 ? 185 VAL A CG1    1 
ATOM   1322 C CG2    . VAL A 1 167 ? 39.863 10.821  35.916  1.00 19.27 ? 185 VAL A CG2    1 
ATOM   1323 N N      . GLU A 1 168 ? 39.636 6.636   33.976  1.00 25.71 ? 186 GLU A N      1 
ATOM   1324 C CA     . GLU A 1 168 ? 38.991 5.394   33.488  1.00 21.76 ? 186 GLU A CA     1 
ATOM   1325 C C      . GLU A 1 168 ? 40.024 4.289   33.366  1.00 20.41 ? 186 GLU A C      1 
ATOM   1326 O O      . GLU A 1 168 ? 39.626 3.185   33.089  1.00 22.70 ? 186 GLU A O      1 
ATOM   1327 C CB     . GLU A 1 168 ? 38.339 5.630   32.132  1.00 23.50 ? 186 GLU A CB     1 
ATOM   1328 C CG     . GLU A 1 168 ? 38.999 6.717   31.317  1.00 34.93 ? 186 GLU A CG     1 
ATOM   1329 C CD     . GLU A 1 168 ? 40.090 6.214   30.396  1.00 50.72 ? 186 GLU A CD     1 
ATOM   1330 O OE1    . GLU A 1 168 ? 41.247 6.527   30.659  1.00 47.18 ? 186 GLU A OE1    1 
ATOM   1331 O OE2    . GLU A 1 168 ? 39.776 5.494   29.434  1.00 49.15 ? 186 GLU A OE2    1 
ATOM   1332 N N      . LEU A 1 169 ? 41.295 4.609   33.527  1.00 18.48 ? 187 LEU A N      1 
ATOM   1333 C CA     . LEU A 1 169 ? 42.392 3.609   33.457  1.00 22.67 ? 187 LEU A CA     1 
ATOM   1334 C C      . LEU A 1 169 ? 42.164 2.430   34.450  1.00 17.11 ? 187 LEU A C      1 
ATOM   1335 O O      . LEU A 1 169 ? 42.248 1.310   33.958  1.00 13.36 ? 187 LEU A O      1 
ATOM   1336 C CB     . LEU A 1 169 ? 43.708 4.374   33.649  1.00 19.17 ? 187 LEU A CB     1 
ATOM   1337 C CG     . LEU A 1 169 ? 44.107 5.305   32.515  1.00 14.72 ? 187 LEU A CG     1 
ATOM   1338 C CD1    . LEU A 1 169 ? 45.532 5.784   32.708  1.00 14.14 ? 187 LEU A CD1    1 
ATOM   1339 C CD2    . LEU A 1 169 ? 43.957 4.608   31.179  1.00 15.93 ? 187 LEU A CD2    1 
ATOM   1340 N N      . PRO A 1 170 ? 41.872 2.577   35.784  1.00 14.45 ? 188 PRO A N      1 
ATOM   1341 C CA     . PRO A 1 170 ? 41.515 1.415   36.628  1.00 17.70 ? 188 PRO A CA     1 
ATOM   1342 C C      . PRO A 1 170 ? 40.365 0.593   36.065  1.00 20.31 ? 188 PRO A C      1 
ATOM   1343 O O      . PRO A 1 170 ? 40.262 -0.611  36.350  1.00 17.43 ? 188 PRO A O      1 
ATOM   1344 C CB     . PRO A 1 170 ? 41.127 2.049   37.974  1.00 10.28 ? 188 PRO A CB     1 
ATOM   1345 C CG     . PRO A 1 170 ? 41.532 3.507   37.865  1.00 12.41 ? 188 PRO A CG     1 
ATOM   1346 C CD     . PRO A 1 170 ? 41.528 3.854   36.423  1.00 14.48 ? 188 PRO A CD     1 
ATOM   1347 N N      . LEU A 1 171 ? 39.479 1.213   35.284  1.00 17.30 ? 189 LEU A N      1 
ATOM   1348 C CA     . LEU A 1 171 ? 38.367 0.470   34.719  1.00 13.24 ? 189 LEU A CA     1 
ATOM   1349 C C      . LEU A 1 171 ? 38.785 -0.233  33.423  1.00 17.47 ? 189 LEU A C      1 
ATOM   1350 O O      . LEU A 1 171 ? 38.616 -1.451  33.270  1.00 16.26 ? 189 LEU A O      1 
ATOM   1351 C CB     . LEU A 1 171 ? 37.192 1.429   34.506  1.00 11.18 ? 189 LEU A CB     1 
ATOM   1352 C CG     . LEU A 1 171 ? 35.768 0.902   34.719  1.00 15.48 ? 189 LEU A CG     1 
ATOM   1353 C CD1    . LEU A 1 171 ? 35.681 0.002   35.955  1.00 14.47 ? 189 LEU A CD1    1 
ATOM   1354 C CD2    . LEU A 1 171 ? 34.769 2.063   34.809  1.00 14.16 ? 189 LEU A CD2    1 
ATOM   1355 N N      . LYS A 1 172 ? 39.363 0.520   32.486  1.00 22.04 ? 190 LYS A N      1 
ATOM   1356 C CA     . LYS A 1 172 ? 39.817 -0.058  31.223  1.00 15.61 ? 190 LYS A CA     1 
ATOM   1357 C C      . LYS A 1 172 ? 40.766 -1.224  31.455  1.00 14.78 ? 190 LYS A C      1 
ATOM   1358 O O      . LYS A 1 172 ? 40.836 -2.153  30.637  1.00 13.02 ? 190 LYS A O      1 
ATOM   1359 C CB     . LYS A 1 172 ? 40.496 1.032   30.382  1.00 15.84 ? 190 LYS A CB     1 
ATOM   1360 C CG     . LYS A 1 172 ? 41.492 0.549   29.338  1.00 12.99 ? 190 LYS A CG     1 
ATOM   1361 C CD     . LYS A 1 172 ? 41.827 1.657   28.349  1.00 16.17 ? 190 LYS A CD     1 
ATOM   1362 C CE     . LYS A 1 172 ? 43.270 2.181   28.469  1.00 21.94 ? 190 LYS A CE     1 
ATOM   1363 N NZ     . LYS A 1 172 ? 43.626 3.267   27.455  1.00 24.69 ? 190 LYS A NZ     1 
ATOM   1364 N N      . ALA A 1 173 ? 41.492 -1.206  32.572  1.00 15.72 ? 191 ALA A N      1 
ATOM   1365 C CA     . ALA A 1 173 ? 42.549 -2.185  32.773  1.00 14.56 ? 191 ALA A CA     1 
ATOM   1366 C C      . ALA A 1 173 ? 42.018 -3.547  33.181  1.00 13.06 ? 191 ALA A C      1 
ATOM   1367 O O      . ALA A 1 173 ? 42.780 -4.521  33.173  1.00 13.83 ? 191 ALA A O      1 
ATOM   1368 C CB     . ALA A 1 173 ? 43.551 -1.679  33.811  1.00 15.23 ? 191 ALA A CB     1 
ATOM   1369 N N      . GLN A 1 174 ? 40.725 -3.636  33.415  1.00 12.48 ? 192 GLN A N      1 
ATOM   1370 C CA     . GLN A 1 174 ? 40.103 -4.892  33.748  1.00 15.04 ? 192 GLN A CA     1 
ATOM   1371 C C      . GLN A 1 174 ? 39.426 -5.537  32.575  1.00 13.94 ? 192 GLN A C      1 
ATOM   1372 O O      . GLN A 1 174 ? 38.663 -6.459  32.741  1.00 24.08 ? 192 GLN A O      1 
ATOM   1373 C CB     . GLN A 1 174 ? 39.083 -4.686  34.842  1.00 17.55 ? 192 GLN A CB     1 
ATOM   1374 C CG     . GLN A 1 174 ? 39.422 -3.738  35.958  1.00 15.57 ? 192 GLN A CG     1 
ATOM   1375 C CD     . GLN A 1 174 ? 38.259 -3.594  36.912  1.00 24.78 ? 192 GLN A CD     1 
ATOM   1376 O OE1    . GLN A 1 174 ? 37.535 -4.552  37.158  1.00 19.92 ? 192 GLN A OE1    1 
ATOM   1377 N NE2    . GLN A 1 174 ? 38.065 -2.399  37.444  1.00 20.71 ? 192 GLN A NE2    1 
ATOM   1378 N N      . SER A 1 175 ? 39.702 -5.060  31.385  1.00 15.47 ? 193 SER A N      1 
ATOM   1379 C CA     . SER A 1 175 ? 39.157 -5.656  30.183  1.00 17.08 ? 193 SER A CA     1 
ATOM   1380 C C      . SER A 1 175 ? 40.055 -6.607  29.493  1.00 13.82 ? 193 SER A C      1 
ATOM   1381 O O      . SER A 1 175 ? 41.248 -6.447  29.532  1.00 12.03 ? 193 SER A O      1 
ATOM   1382 C CB     . SER A 1 175 ? 38.693 -4.599  29.186  1.00 17.39 ? 193 SER A CB     1 
ATOM   1383 O OG     . SER A 1 175 ? 38.243 -5.157  27.982  1.00 14.35 ? 193 SER A OG     1 
ATOM   1384 N N      . GLU A 1 176 ? 39.465 -7.614  28.877  1.00 16.86 ? 194 GLU A N      1 
ATOM   1385 C CA     . GLU A 1 176 ? 40.194 -8.591  28.115  1.00 18.13 ? 194 GLU A CA     1 
ATOM   1386 C C      . GLU A 1 176 ? 39.814 -8.397  26.676  1.00 23.44 ? 194 GLU A C      1 
ATOM   1387 O O      . GLU A 1 176 ? 40.483 -8.881  25.789  1.00 23.84 ? 194 GLU A O      1 
ATOM   1388 C CB     . GLU A 1 176 ? 39.763 -9.960  28.582  1.00 26.38 ? 194 GLU A CB     1 
ATOM   1389 C CG     . GLU A 1 176 ? 40.747 -11.087 28.331  1.00 42.91 ? 194 GLU A CG     1 
ATOM   1390 C CD     . GLU A 1 176 ? 40.262 -12.046 27.263  1.00 58.05 ? 194 GLU A CD     1 
ATOM   1391 O OE1    . GLU A 1 176 ? 39.053 -12.034 26.952  1.00 54.50 ? 194 GLU A OE1    1 
ATOM   1392 O OE2    . GLU A 1 176 ? 41.092 -12.806 26.726  1.00 55.35 ? 194 GLU A OE2    1 
ATOM   1393 N N      . ARG A 1 177 ? 38.751 -7.659  26.438  1.00 22.17 ? 195 ARG A N      1 
ATOM   1394 C CA     . ARG A 1 177 ? 38.287 -7.377  25.110  1.00 14.64 ? 195 ARG A CA     1 
ATOM   1395 C C      . ARG A 1 177 ? 39.003 -6.207  24.468  1.00 18.56 ? 195 ARG A C      1 
ATOM   1396 O O      . ARG A 1 177 ? 39.479 -6.322  23.362  1.00 20.73 ? 195 ARG A O      1 
ATOM   1397 C CB     . ARG A 1 177 ? 36.809 -7.083  25.191  1.00 14.34 ? 195 ARG A CB     1 
ATOM   1398 C CG     . ARG A 1 177 ? 35.919 -8.292  25.339  1.00 19.86 ? 195 ARG A CG     1 
ATOM   1399 C CD     . ARG A 1 177 ? 34.466 -7.901  25.169  1.00 13.77 ? 195 ARG A CD     1 
ATOM   1400 N NE     . ARG A 1 177 ? 33.562 -8.933  25.651  1.00 13.88 ? 195 ARG A NE     1 
ATOM   1401 C CZ     . ARG A 1 177 ? 32.248 -8.798  25.716  1.00 15.37 ? 195 ARG A CZ     1 
ATOM   1402 N NH1    . ARG A 1 177 ? 31.678 -7.672  25.329  1.00 19.31 ? 195 ARG A NH1    1 
ATOM   1403 N NH2    . ARG A 1 177 ? 31.507 -9.788  26.168  1.00 15.93 ? 195 ARG A NH2    1 
ATOM   1404 N N      . TYR A 1 178 ? 39.075 -5.082  25.155  1.00 17.02 ? 196 TYR A N      1 
ATOM   1405 C CA     . TYR A 1 178 ? 39.758 -3.890  24.641  1.00 16.53 ? 196 TYR A CA     1 
ATOM   1406 C C      . TYR A 1 178 ? 41.188 -4.095  24.270  1.00 18.23 ? 196 TYR A C      1 
ATOM   1407 O O      . TYR A 1 178 ? 41.683 -3.459  23.361  1.00 22.89 ? 196 TYR A O      1 
ATOM   1408 C CB     . TYR A 1 178 ? 39.692 -2.762  25.661  1.00 16.72 ? 196 TYR A CB     1 
ATOM   1409 C CG     . TYR A 1 178 ? 39.809 -1.381  25.115  1.00 19.37 ? 196 TYR A CG     1 
ATOM   1410 C CD1    . TYR A 1 178 ? 38.751 -0.791  24.455  1.00 19.76 ? 196 TYR A CD1    1 
ATOM   1411 C CD2    . TYR A 1 178 ? 40.967 -0.653  25.280  1.00 12.68 ? 196 TYR A CD2    1 
ATOM   1412 C CE1    . TYR A 1 178 ? 38.853 0.480   23.958  1.00 19.59 ? 196 TYR A CE1    1 
ATOM   1413 C CE2    . TYR A 1 178 ? 41.077 0.620   24.783  1.00 16.49 ? 196 TYR A CE2    1 
ATOM   1414 C CZ     . TYR A 1 178 ? 40.013 1.178   24.128  1.00 19.76 ? 196 TYR A CZ     1 
ATOM   1415 O OH     . TYR A 1 178 ? 40.114 2.450   23.637  1.00 27.57 ? 196 TYR A OH     1 
ATOM   1416 N N      . PRO A 1 179 ? 41.893 -4.931  25.010  1.00 20.35 ? 197 PRO A N      1 
ATOM   1417 C CA     . PRO A 1 179 ? 43.242 -5.211  24.551  1.00 17.78 ? 197 PRO A CA     1 
ATOM   1418 C C      . PRO A 1 179 ? 43.372 -5.775  23.108  1.00 19.22 ? 197 PRO A C      1 
ATOM   1419 O O      . PRO A 1 179 ? 44.471 -5.854  22.609  1.00 17.84 ? 197 PRO A O      1 
ATOM   1420 C CB     . PRO A 1 179 ? 43.727 -6.166  25.616  1.00 11.05 ? 197 PRO A CB     1 
ATOM   1421 C CG     . PRO A 1 179 ? 43.098 -5.674  26.846  1.00 13.52 ? 197 PRO A CG     1 
ATOM   1422 C CD     . PRO A 1 179 ? 41.724 -5.288  26.426  1.00 17.16 ? 197 PRO A CD     1 
ATOM   1423 N N      . LYS A 1 180 ? 42.285 -6.150  22.449  1.00 20.01 ? 198 LYS A N      1 
ATOM   1424 C CA     . LYS A 1 180 ? 42.306 -6.621  21.068  1.00 20.45 ? 198 LYS A CA     1 
ATOM   1425 C C      . LYS A 1 180 ? 41.733 -5.584  20.128  1.00 19.70 ? 198 LYS A C      1 
ATOM   1426 O O      . LYS A 1 180 ? 41.145 -5.931  19.141  1.00 15.27 ? 198 LYS A O      1 
ATOM   1427 C CB     . LYS A 1 180 ? 41.558 -7.937  20.941  1.00 15.67 ? 198 LYS A CB     1 
ATOM   1428 C CG     . LYS A 1 180 ? 41.901 -8.961  21.995  1.00 20.76 ? 198 LYS A CG     1 
ATOM   1429 C CD     . LYS A 1 180 ? 42.951 -9.926  21.485  1.00 30.68 ? 198 LYS A CD     1 
ATOM   1430 C CE     . LYS A 1 180 ? 42.583 -11.358 21.816  1.00 29.49 ? 198 LYS A CE     1 
ATOM   1431 N NZ     . LYS A 1 180 ? 41.353 -11.412 22.646  1.00 34.55 ? 198 LYS A NZ     1 
ATOM   1432 N N      . LYS A 1 181 ? 41.911 -4.313  20.441  1.00 18.28 ? 199 LYS A N      1 
ATOM   1433 C CA     . LYS A 1 181 ? 41.488 -3.234  19.593  1.00 13.63 ? 199 LYS A CA     1 
ATOM   1434 C C      . LYS A 1 181 ? 42.412 -3.202  18.436  1.00 16.88 ? 199 LYS A C      1 
ATOM   1435 O O      . LYS A 1 181 ? 43.567 -3.491  18.598  1.00 17.43 ? 199 LYS A O      1 
ATOM   1436 C CB     . LYS A 1 181 ? 41.505 -1.936  20.360  1.00 9.83  ? 199 LYS A CB     1 
ATOM   1437 C CG     . LYS A 1 181 ? 40.770 -0.794  19.705  1.00 16.42 ? 199 LYS A CG     1 
ATOM   1438 C CD     . LYS A 1 181 ? 40.851 0.451   20.556  1.00 13.26 ? 199 LYS A CD     1 
ATOM   1439 C CE     . LYS A 1 181 ? 40.472 1.678   19.757  1.00 12.75 ? 199 LYS A CE     1 
ATOM   1440 N NZ     . LYS A 1 181 ? 40.458 2.887   20.615  1.00 12.05 ? 199 LYS A NZ     1 
ATOM   1441 N N      . ASP A 1 182 ? 41.910 -2.876  17.253  1.00 21.04 ? 200 ASP A N      1 
ATOM   1442 C CA     . ASP A 1 182 ? 42.668 -2.915  16.016  1.00 12.07 ? 200 ASP A CA     1 
ATOM   1443 C C      . ASP A 1 182 ? 42.935 -1.578  15.316  1.00 14.08 ? 200 ASP A C      1 
ATOM   1444 O O      . ASP A 1 182 ? 43.198 -1.547  14.142  1.00 17.02 ? 200 ASP A O      1 
ATOM   1445 C CB     . ASP A 1 182 ? 41.993 -3.924  15.077  1.00 11.74 ? 200 ASP A CB     1 
ATOM   1446 C CG     . ASP A 1 182 ? 40.529 -3.677  14.891  1.00 24.51 ? 200 ASP A CG     1 
ATOM   1447 O OD1    . ASP A 1 182 ? 39.746 -4.007  15.786  1.00 39.41 ? 200 ASP A OD1    1 
ATOM   1448 O OD2    . ASP A 1 182 ? 40.140 -3.190  13.823  1.00 31.52 ? 200 ASP A OD2    1 
ATOM   1449 N N      . ARG A 1 183 ? 42.820 -0.475  16.017  1.00 8.10  ? 201 ARG A N      1 
ATOM   1450 C CA     . ARG A 1 183 ? 43.117 0.804   15.414  1.00 10.78 ? 201 ARG A CA     1 
ATOM   1451 C C      . ARG A 1 183 ? 44.583 1.131   15.223  1.00 11.75 ? 201 ARG A C      1 
ATOM   1452 O O      . ARG A 1 183 ? 45.353 1.076   16.139  1.00 11.10 ? 201 ARG A O      1 
ATOM   1453 C CB     . ARG A 1 183 ? 42.358 1.950   16.085  1.00 10.23 ? 201 ARG A CB     1 
ATOM   1454 C CG     . ARG A 1 183 ? 42.815 3.334   15.688  1.00 8.86  ? 201 ARG A CG     1 
ATOM   1455 C CD     . ARG A 1 183 ? 41.907 4.399   16.256  1.00 10.09 ? 201 ARG A CD     1 
ATOM   1456 N NE     . ARG A 1 183 ? 42.429 5.733   16.009  1.00 10.62 ? 201 ARG A NE     1 
ATOM   1457 C CZ     . ARG A 1 183 ? 41.746 6.856   16.182  1.00 13.73 ? 201 ARG A CZ     1 
ATOM   1458 N NH1    . ARG A 1 183 ? 40.499 6.822   16.586  1.00 17.20 ? 201 ARG A NH1    1 
ATOM   1459 N NH2    . ARG A 1 183 ? 42.313 8.017   15.929  1.00 13.44 ? 201 ARG A NH2    1 
ATOM   1460 N N      . SER A 1 184 ? 44.973 1.421   14.006  1.00 10.18 ? 202 SER A N      1 
ATOM   1461 C CA     . SER A 1 184 ? 46.323 1.806   13.712  1.00 9.88  ? 202 SER A CA     1 
ATOM   1462 C C      . SER A 1 184 ? 46.679 3.158   14.181  1.00 12.31 ? 202 SER A C      1 
ATOM   1463 O O      . SER A 1 184 ? 45.914 4.101   14.114  1.00 12.24 ? 202 SER A O      1 
ATOM   1464 C CB     . SER A 1 184 ? 46.655 1.701   12.229  1.00 9.45  ? 202 SER A CB     1 
ATOM   1465 O OG     . SER A 1 184 ? 47.970 2.084   11.921  1.00 13.75 ? 202 SER A OG     1 
ATOM   1466 N N      . ARG A 1 185 ? 47.877 3.224   14.676  1.00 14.23 ? 203 ARG A N      1 
ATOM   1467 C CA     . ARG A 1 185 ? 48.397 4.491   15.156  1.00 14.63 ? 203 ARG A CA     1 
ATOM   1468 C C      . ARG A 1 185 ? 48.682 5.472   14.032  1.00 16.98 ? 203 ARG A C      1 
ATOM   1469 O O      . ARG A 1 185 ? 48.742 6.684   14.284  1.00 17.69 ? 203 ARG A O      1 
ATOM   1470 C CB     . ARG A 1 185 ? 49.671 4.261   15.963  1.00 12.00 ? 203 ARG A CB     1 
ATOM   1471 C CG     . ARG A 1 185 ? 49.454 3.637   17.320  1.00 12.48 ? 203 ARG A CG     1 
ATOM   1472 C CD     . ARG A 1 185 ? 50.759 3.567   18.077  1.00 14.86 ? 203 ARG A CD     1 
ATOM   1473 N NE     . ARG A 1 185 ? 50.599 2.951   19.383  1.00 18.82 ? 203 ARG A NE     1 
ATOM   1474 C CZ     . ARG A 1 185 ? 51.564 2.868   20.282  1.00 14.94 ? 203 ARG A CZ     1 
ATOM   1475 N NH1    . ARG A 1 185 ? 52.764 3.367   20.046  1.00 11.62 ? 203 ARG A NH1    1 
ATOM   1476 N NH2    . ARG A 1 185 ? 51.317 2.273   21.447  1.00 18.50 ? 203 ARG A NH2    1 
ATOM   1477 N N      . GLU A 1 186 ? 48.858 4.975   12.812  1.00 12.81 ? 204 GLU A N      1 
ATOM   1478 C CA     . GLU A 1 186 ? 49.195 5.832   11.692  1.00 15.05 ? 204 GLU A CA     1 
ATOM   1479 C C      . GLU A 1 186 ? 48.286 7.054   11.677  1.00 19.26 ? 204 GLU A C      1 
ATOM   1480 O O      . GLU A 1 186 ? 47.071 6.944   11.869  1.00 22.31 ? 204 GLU A O      1 
ATOM   1481 C CB     . GLU A 1 186 ? 49.072 5.043   10.390  1.00 21.50 ? 204 GLU A CB     1 
ATOM   1482 C CG     . GLU A 1 186 ? 49.969 5.516   9.249   1.00 26.77 ? 204 GLU A CG     1 
ATOM   1483 C CD     . GLU A 1 186 ? 49.748 4.708   7.984   1.00 39.84 ? 204 GLU A CD     1 
ATOM   1484 O OE1    . GLU A 1 186 ? 49.145 3.613   8.083   1.00 48.27 ? 204 GLU A OE1    1 
ATOM   1485 O OE2    . GLU A 1 186 ? 50.166 5.169   6.897   1.00 39.93 ? 204 GLU A OE2    1 
ATOM   1486 N N      . GLU A 1 187 ? 48.888 8.229   11.492  1.00 21.47 ? 205 GLU A N      1 
ATOM   1487 C CA     . GLU A 1 187 ? 48.143 9.479   11.380  1.00 22.31 ? 205 GLU A CA     1 
ATOM   1488 C C      . GLU A 1 187 ? 47.859 9.737   9.904   1.00 24.91 ? 205 GLU A C      1 
ATOM   1489 O O      . GLU A 1 187 ? 48.770 10.048  9.134   1.00 25.34 ? 205 GLU A O      1 
ATOM   1490 C CB     . GLU A 1 187 ? 48.916 10.632  12.009  1.00 14.96 ? 205 GLU A CB     1 
ATOM   1491 C CG     . GLU A 1 187 ? 49.068 10.514  13.518  1.00 25.61 ? 205 GLU A CG     1 
ATOM   1492 C CD     . GLU A 1 187 ? 47.730 10.525  14.270  1.00 39.46 ? 205 GLU A CD     1 
ATOM   1493 O OE1    . GLU A 1 187 ? 46.812 11.254  13.828  1.00 46.36 ? 205 GLU A OE1    1 
ATOM   1494 O OE2    . GLU A 1 187 ? 47.593 9.806   15.301  1.00 35.95 ? 205 GLU A OE2    1 
ATOM   1495 N N      . LEU A 1 188 ? 46.600 9.591   9.498   1.00 22.64 ? 206 LEU A N      1 
ATOM   1496 C CA     . LEU A 1 188 ? 46.219 9.819   8.113   1.00 18.30 ? 206 LEU A CA     1 
ATOM   1497 C C      . LEU A 1 188 ? 45.513 11.159  7.907   1.00 17.49 ? 206 LEU A C      1 
ATOM   1498 O O      . LEU A 1 188 ? 45.151 11.491  6.774   1.00 20.60 ? 206 LEU A O      1 
ATOM   1499 C CB     . LEU A 1 188 ? 45.336 8.662   7.635   1.00 19.86 ? 206 LEU A CB     1 
ATOM   1500 C CG     . LEU A 1 188 ? 45.968 7.280   7.845   1.00 19.41 ? 206 LEU A CG     1 
ATOM   1501 C CD1    . LEU A 1 188 ? 45.040 6.144   7.385   1.00 20.22 ? 206 LEU A CD1    1 
ATOM   1502 C CD2    . LEU A 1 188 ? 47.254 7.245   7.093   1.00 17.88 ? 206 LEU A CD2    1 
ATOM   1503 N N      . GLY A 1 189 ? 45.323 11.936  8.970   1.00 15.53 ? 207 GLY A N      1 
ATOM   1504 C CA     . GLY A 1 189 ? 44.644 13.211  8.876   1.00 15.78 ? 207 GLY A CA     1 
ATOM   1505 C C      . GLY A 1 189 ? 43.136 13.077  8.704   1.00 14.47 ? 207 GLY A C      1 
ATOM   1506 O O      . GLY A 1 189 ? 42.524 12.039  8.971   1.00 12.78 ? 207 GLY A O      1 
ATOM   1507 N N      . ASN A 1 190 ? 42.574 14.128  8.129   1.00 16.21 ? 208 ASN A N      1 
ATOM   1508 C CA     . ASN A 1 190 ? 41.168 14.199  7.876   1.00 15.22 ? 208 ASN A CA     1 
ATOM   1509 C C      . ASN A 1 190 ? 40.867 14.306  6.393   1.00 16.92 ? 208 ASN A C      1 
ATOM   1510 O O      . ASN A 1 190 ? 41.705 14.716  5.622   1.00 21.64 ? 208 ASN A O      1 
ATOM   1511 C CB     . ASN A 1 190 ? 40.650 15.445  8.557   1.00 16.11 ? 208 ASN A CB     1 
ATOM   1512 C CG     . ASN A 1 190 ? 40.398 15.259  10.038  1.00 23.53 ? 208 ASN A CG     1 
ATOM   1513 O OD1    . ASN A 1 190 ? 41.150 14.595  10.732  1.00 25.38 ? 208 ASN A OD1    1 
ATOM   1514 N ND2    . ASN A 1 190 ? 39.335 15.870  10.530  1.00 33.50 ? 208 ASN A ND2    1 
ATOM   1515 N N      . THR A 1 191 ? 39.673 13.911  5.990   1.00 14.35 ? 209 THR A N      1 
ATOM   1516 C CA     . THR A 1 191 ? 39.250 13.998  4.605   1.00 16.00 ? 209 THR A CA     1 
ATOM   1517 C C      . THR A 1 191 ? 37.895 14.676  4.525   1.00 15.20 ? 209 THR A C      1 
ATOM   1518 O O      . THR A 1 191 ? 37.123 14.578  5.412   1.00 12.38 ? 209 THR A O      1 
ATOM   1519 C CB     . THR A 1 191 ? 39.124 12.606  3.931   1.00 14.08 ? 209 THR A CB     1 
ATOM   1520 O OG1    . THR A 1 191 ? 39.032 11.591  4.928   1.00 18.58 ? 209 THR A OG1    1 
ATOM   1521 C CG2    . THR A 1 191 ? 40.284 12.350  3.033   1.00 11.12 ? 209 THR A CG2    1 
ATOM   1522 N N      . PRO A 1 192 ? 37.605 15.353  3.423   1.00 11.12 ? 210 PRO A N      1 
ATOM   1523 C CA     . PRO A 1 192 ? 36.278 15.921  3.266   1.00 14.34 ? 210 PRO A CA     1 
ATOM   1524 C C      . PRO A 1 192 ? 35.109 14.937  3.041   1.00 9.93  ? 210 PRO A C      1 
ATOM   1525 O O      . PRO A 1 192 ? 35.276 13.947  2.368   1.00 9.27  ? 210 PRO A O      1 
ATOM   1526 C CB     . PRO A 1 192 ? 36.467 16.864  2.099   1.00 10.66 ? 210 PRO A CB     1 
ATOM   1527 C CG     . PRO A 1 192 ? 37.912 17.130  2.016   1.00 11.12 ? 210 PRO A CG     1 
ATOM   1528 C CD     . PRO A 1 192 ? 38.529 15.841  2.392   1.00 8.75  ? 210 PRO A CD     1 
ATOM   1529 N N      . SER A 1 193 ? 33.943 15.224  3.612   1.00 8.91  ? 211 SER A N      1 
ATOM   1530 C CA     . SER A 1 193 ? 32.802 14.368  3.390   1.00 10.07 ? 211 SER A CA     1 
ATOM   1531 C C      . SER A 1 193 ? 31.490 15.068  3.525   1.00 11.52 ? 211 SER A C      1 
ATOM   1532 O O      . SER A 1 193 ? 31.334 15.965  4.324   1.00 12.69 ? 211 SER A O      1 
ATOM   1533 C CB     . SER A 1 193 ? 32.757 13.177  4.370   1.00 8.28  ? 211 SER A CB     1 
ATOM   1534 O OG     . SER A 1 193 ? 31.688 12.302  4.126   1.00 10.66 ? 211 SER A OG     1 
ATOM   1535 N N      . ALA A 1 194 ? 30.551 14.673  2.710   1.00 10.06 ? 212 ALA A N      1 
ATOM   1536 C CA     . ALA A 1 194 ? 29.177 15.118  2.851   1.00 9.18  ? 212 ALA A CA     1 
ATOM   1537 C C      . ALA A 1 194 ? 28.260 13.979  3.261   1.00 11.53 ? 212 ALA A C      1 
ATOM   1538 O O      . ALA A 1 194 ? 27.040 14.087  3.118   1.00 10.32 ? 212 ALA A O      1 
ATOM   1539 C CB     . ALA A 1 194 ? 28.697 15.756  1.551   1.00 7.71  ? 212 ALA A CB     1 
ATOM   1540 N N      . ASN A 1 195 ? 28.817 12.910  3.751   1.00 10.48 ? 213 ASN A N      1 
ATOM   1541 C CA     . ASN A 1 195 ? 28.023 11.763  4.109   1.00 9.42  ? 213 ASN A CA     1 
ATOM   1542 C C      . ASN A 1 195 ? 27.816 11.649  5.593   1.00 9.25  ? 213 ASN A C      1 
ATOM   1543 O O      . ASN A 1 195 ? 28.732 11.844  6.344   1.00 10.55 ? 213 ASN A O      1 
ATOM   1544 C CB     . ASN A 1 195 ? 28.605 10.472  3.527   1.00 13.72 ? 213 ASN A CB     1 
ATOM   1545 C CG     . ASN A 1 195 ? 28.114 10.172  2.138   1.00 13.81 ? 213 ASN A CG     1 
ATOM   1546 O OD1    . ASN A 1 195 ? 27.056 10.611  1.733   1.00 10.76 ? 213 ASN A OD1    1 
ATOM   1547 N ND2    . ASN A 1 195 ? 28.891 9.409   1.404   1.00 8.04  ? 213 ASN A ND2    1 
ATOM   1548 N N      . PRO A 1 196 ? 26.597 11.294  6.017   1.00 12.85 ? 214 PRO A N      1 
ATOM   1549 C CA     . PRO A 1 196 ? 26.308 11.274  7.455   1.00 9.82  ? 214 PRO A CA     1 
ATOM   1550 C C      . PRO A 1 196 ? 26.801 10.016  8.163   1.00 9.21  ? 214 PRO A C      1 
ATOM   1551 O O      . PRO A 1 196 ? 27.008 8.968   7.561   1.00 8.68  ? 214 PRO A O      1 
ATOM   1552 C CB     . PRO A 1 196 ? 24.778 11.347  7.494   1.00 9.77  ? 214 PRO A CB     1 
ATOM   1553 C CG     . PRO A 1 196 ? 24.352 10.679  6.231   1.00 7.38  ? 214 PRO A CG     1 
ATOM   1554 C CD     . PRO A 1 196 ? 25.386 11.095  5.204   1.00 11.46 ? 214 PRO A CD     1 
ATOM   1555 N N      . GLY A 1 197 ? 26.968 10.103  9.461   1.00 9.65  ? 215 GLY A N      1 
ATOM   1556 C CA     . GLY A 1 197 ? 27.342 8.960   10.254  1.00 9.40  ? 215 GLY A CA     1 
ATOM   1557 C C      . GLY A 1 197 ? 28.557 8.119   10.067  1.00 11.31 ? 215 GLY A C      1 
ATOM   1558 O O      . GLY A 1 197 ? 29.664 8.602   10.035  1.00 17.03 ? 215 GLY A O      1 
ATOM   1559 N N      . ILE A 1 198 ? 28.337 6.824   9.990   1.00 9.53  ? 216 ILE A N      1 
ATOM   1560 C CA     . ILE A 1 198 ? 29.426 5.896   9.876   1.00 15.74 ? 216 ILE A CA     1 
ATOM   1561 C C      . ILE A 1 198 ? 29.559 5.524   8.434   1.00 12.31 ? 216 ILE A C      1 
ATOM   1562 O O      . ILE A 1 198 ? 30.331 4.666   8.092   1.00 15.84 ? 216 ILE A O      1 
ATOM   1563 C CB     . ILE A 1 198 ? 29.298 4.747   10.909  1.00 8.01  ? 216 ILE A CB     1 
ATOM   1564 C CG1    . ILE A 1 198 ? 28.001 3.971   10.723  1.00 10.01 ? 216 ILE A CG1    1 
ATOM   1565 C CG2    . ILE A 1 198 ? 29.412 5.314   12.308  1.00 8.80  ? 216 ILE A CG2    1 
ATOM   1566 C CD1    . ILE A 1 198 ? 28.199 2.479   10.733  1.00 11.63 ? 216 ILE A CD1    1 
ATOM   1567 N N      . MET A 1 199 ? 28.819 6.201   7.590   1.00 9.45  ? 217 MET A N      1 
ATOM   1568 C CA     . MET A 1 199 ? 28.965 6.025   6.178   1.00 12.42 ? 217 MET A CA     1 
ATOM   1569 C C      . MET A 1 199 ? 30.300 6.559   5.765   1.00 13.38 ? 217 MET A C      1 
ATOM   1570 O O      . MET A 1 199 ? 30.737 7.563   6.285   1.00 15.67 ? 217 MET A O      1 
ATOM   1571 C CB     . MET A 1 199 ? 27.888 6.797   5.434   1.00 11.83 ? 217 MET A CB     1 
ATOM   1572 C CG     . MET A 1 199 ? 26.469 6.281   5.569   1.00 11.18 ? 217 MET A CG     1 
ATOM   1573 S SD     . MET A 1 199 ? 25.338 7.199   4.510   1.00 14.21 ? 217 MET A SD     1 
ATOM   1574 C CE     . MET A 1 199 ? 25.912 6.743   2.885   1.00 8.40  ? 217 MET A CE     1 
ATOM   1575 N N      . LYS A 1 200 ? 30.947 5.892   4.824   1.00 14.62 ? 218 LYS A N      1 
ATOM   1576 C CA     . LYS A 1 200 ? 32.237 6.314   4.317   1.00 12.78 ? 218 LYS A CA     1 
ATOM   1577 C C      . LYS A 1 200 ? 32.138 7.481   3.367   1.00 10.05 ? 218 LYS A C      1 
ATOM   1578 O O      . LYS A 1 200 ? 31.132 7.655   2.719   1.00 11.54 ? 218 LYS A O      1 
ATOM   1579 C CB     . LYS A 1 200 ? 32.947 5.131   3.677   1.00 18.15 ? 218 LYS A CB     1 
ATOM   1580 C CG     . LYS A 1 200 ? 33.125 3.922   4.559   1.00 20.23 ? 218 LYS A CG     1 
ATOM   1581 C CD     . LYS A 1 200 ? 33.401 2.695   3.715   1.00 27.04 ? 218 LYS A CD     1 
ATOM   1582 C CE     . LYS A 1 200 ? 34.638 2.870   2.860   1.00 27.47 ? 218 LYS A CE     1 
ATOM   1583 N NZ     . LYS A 1 200 ? 34.841 1.714   1.951   1.00 24.92 ? 218 LYS A NZ     1 
ATOM   1584 N N      . PRO A 1 201 ? 33.190 8.292   3.273   1.00 11.17 ? 219 PRO A N      1 
ATOM   1585 C CA     . PRO A 1 201 ? 33.149 9.512   2.445   1.00 10.30 ? 219 PRO A CA     1 
ATOM   1586 C C      . PRO A 1 201 ? 32.900 9.350   0.934   1.00 8.34  ? 219 PRO A C      1 
ATOM   1587 O O      . PRO A 1 201 ? 32.108 10.085  0.383   1.00 6.93  ? 219 PRO A O      1 
ATOM   1588 C CB     . PRO A 1 201 ? 34.485 10.167  2.766   1.00 7.91  ? 219 PRO A CB     1 
ATOM   1589 C CG     . PRO A 1 201 ? 34.943 9.552   4.030   1.00 13.26 ? 219 PRO A CG     1 
ATOM   1590 C CD     . PRO A 1 201 ? 34.479 8.143   3.952   1.00 13.02 ? 219 PRO A CD     1 
ATOM   1591 N N      . ASN A 1 202 ? 33.520 8.372   0.293   1.00 10.28 ? 220 ASN A N      1 
ATOM   1592 C CA     . ASN A 1 202 ? 33.434 8.153   -1.144  1.00 10.02 ? 220 ASN A CA     1 
ATOM   1593 C C      . ASN A 1 202 ? 32.356 7.207   -1.541  1.00 10.49 ? 220 ASN A C      1 
ATOM   1594 O O      . ASN A 1 202 ? 32.264 6.814   -2.675  1.00 9.28  ? 220 ASN A O      1 
ATOM   1595 C CB     . ASN A 1 202 ? 34.769 7.630   -1.636  1.00 7.00  ? 220 ASN A CB     1 
ATOM   1596 C CG     . ASN A 1 202 ? 35.760 8.699   -1.869  1.00 8.75  ? 220 ASN A CG     1 
ATOM   1597 O OD1    . ASN A 1 202 ? 35.418 9.736   -2.384  1.00 10.43 ? 220 ASN A OD1    1 
ATOM   1598 N ND2    . ASN A 1 202 ? 37.002 8.447   -1.517  1.00 11.98 ? 220 ASN A ND2    1 
ATOM   1599 N N      . SER A 1 203 ? 31.502 6.893   -0.606  1.00 8.64  ? 221 SER A N      1 
ATOM   1600 C CA     . SER A 1 203 ? 30.402 6.016   -0.868  1.00 10.34 ? 221 SER A CA     1 
ATOM   1601 C C      . SER A 1 203 ? 29.175 6.692   -1.446  1.00 10.30 ? 221 SER A C      1 
ATOM   1602 O O      . SER A 1 203 ? 28.896 7.827   -1.150  1.00 11.00 ? 221 SER A O      1 
ATOM   1603 C CB     . SER A 1 203 ? 30.064 5.197   0.392   1.00 12.85 ? 221 SER A CB     1 
ATOM   1604 O OG     . SER A 1 203 ? 31.078 4.277   0.715   1.00 15.89 ? 221 SER A OG     1 
ATOM   1605 N N      . PRO A 1 204 ? 28.448 5.982   -2.301  1.00 12.14 ? 222 PRO A N      1 
ATOM   1606 C CA     . PRO A 1 204 ? 27.222 6.483   -2.907  1.00 9.29  ? 222 PRO A CA     1 
ATOM   1607 C C      . PRO A 1 204 ? 26.039 6.703   -1.957  1.00 11.47 ? 222 PRO A C      1 
ATOM   1608 O O      . PRO A 1 204 ? 25.812 5.934   -1.073  1.00 9.71  ? 222 PRO A O      1 
ATOM   1609 C CB     . PRO A 1 204 ? 26.938 5.442   -3.964  1.00 8.72  ? 222 PRO A CB     1 
ATOM   1610 C CG     . PRO A 1 204 ? 27.688 4.235   -3.589  1.00 9.07  ? 222 PRO A CG     1 
ATOM   1611 C CD     . PRO A 1 204 ? 28.907 4.734   -2.917  1.00 11.87 ? 222 PRO A CD     1 
ATOM   1612 N N      . ASN A 1 205 ? 25.303 7.774   -2.137  1.00 12.87 ? 223 ASN A N      1 
ATOM   1613 C CA     . ASN A 1 205 ? 24.229 8.090   -1.233  1.00 11.53 ? 223 ASN A CA     1 
ATOM   1614 C C      . ASN A 1 205 ? 22.982 8.660   -1.857  1.00 11.12 ? 223 ASN A C      1 
ATOM   1615 O O      . ASN A 1 205 ? 23.022 9.187   -2.950  1.00 11.55 ? 223 ASN A O      1 
ATOM   1616 C CB     . ASN A 1 205 ? 24.765 9.047   -0.164  1.00 12.07 ? 223 ASN A CB     1 
ATOM   1617 C CG     . ASN A 1 205 ? 23.932 9.083   1.113   1.00 9.37  ? 223 ASN A CG     1 
ATOM   1618 O OD1    . ASN A 1 205 ? 23.138 8.204   1.392   1.00 8.32  ? 223 ASN A OD1    1 
ATOM   1619 N ND2    . ASN A 1 205 ? 24.138 10.109  1.897   1.00 8.52  ? 223 ASN A ND2    1 
ATOM   1620 N N      . PHE A 1 206 ? 21.868 8.543   -1.135  1.00 11.10 ? 224 PHE A N      1 
ATOM   1621 C CA     . PHE A 1 206 ? 20.667 9.165   -1.604  1.00 10.51 ? 224 PHE A CA     1 
ATOM   1622 C C      . PHE A 1 206 ? 20.853 10.646  -1.497  1.00 12.93 ? 224 PHE A C      1 
ATOM   1623 O O      . PHE A 1 206 ? 21.521 11.104  -0.619  1.00 12.47 ? 224 PHE A O      1 
ATOM   1624 C CB     . PHE A 1 206 ? 19.526 8.803   -0.691  1.00 12.37 ? 224 PHE A CB     1 
ATOM   1625 C CG     . PHE A 1 206 ? 19.308 7.349   -0.483  1.00 10.69 ? 224 PHE A CG     1 
ATOM   1626 C CD1    . PHE A 1 206 ? 18.973 6.529   -1.524  1.00 12.09 ? 224 PHE A CD1    1 
ATOM   1627 C CD2    . PHE A 1 206 ? 19.347 6.825   0.789   1.00 9.73  ? 224 PHE A CD2    1 
ATOM   1628 C CE1    . PHE A 1 206 ? 18.735 5.194   -1.317  1.00 12.07 ? 224 PHE A CE1    1 
ATOM   1629 C CE2    . PHE A 1 206 ? 19.108 5.493   1.006   1.00 13.25 ? 224 PHE A CE2    1 
ATOM   1630 C CZ     . PHE A 1 206 ? 18.800 4.679   -0.051  1.00 13.33 ? 224 PHE A CZ     1 
ATOM   1631 N N      . THR A 1 207 ? 20.173 11.414  -2.322  1.00 17.01 ? 225 THR A N      1 
ATOM   1632 C CA     . THR A 1 207 ? 20.363 12.848  -2.413  1.00 16.24 ? 225 THR A CA     1 
ATOM   1633 C C      . THR A 1 207 ? 19.690 13.579  -1.252  1.00 16.60 ? 225 THR A C      1 
ATOM   1634 O O      . THR A 1 207 ? 20.130 14.646  -0.860  1.00 18.77 ? 225 THR A O      1 
ATOM   1635 C CB     . THR A 1 207 ? 19.902 13.311  -3.790  1.00 16.20 ? 225 THR A CB     1 
ATOM   1636 O OG1    . THR A 1 207 ? 20.149 12.277  -4.741  1.00 17.78 ? 225 THR A OG1    1 
ATOM   1637 C CG2    . THR A 1 207 ? 20.632 14.566  -4.203  1.00 21.63 ? 225 THR A CG2    1 
ATOM   1638 N N      . ASP A 1 208 ? 18.636 13.010  -0.688  1.00 13.98 ? 226 ASP A N      1 
ATOM   1639 C CA     . ASP A 1 208 ? 18.038 13.576  0.509   1.00 14.10 ? 226 ASP A CA     1 
ATOM   1640 C C      . ASP A 1 208 ? 18.641 12.995  1.774   1.00 13.05 ? 226 ASP A C      1 
ATOM   1641 O O      . ASP A 1 208 ? 17.989 12.993  2.820   1.00 15.34 ? 226 ASP A O      1 
ATOM   1642 C CB     . ASP A 1 208 ? 16.535 13.360  0.496   1.00 13.51 ? 226 ASP A CB     1 
ATOM   1643 C CG     . ASP A 1 208 ? 16.174 11.931  0.278   1.00 20.22 ? 226 ASP A CG     1 
ATOM   1644 O OD1    . ASP A 1 208 ? 17.084 11.073  0.286   1.00 20.29 ? 226 ASP A OD1    1 
ATOM   1645 O OD2    . ASP A 1 208 ? 14.974 11.656  0.092   1.00 21.80 ? 226 ASP A OD2    1 
ATOM   1646 N N      . ASN A 1 209 ? 19.874 12.495  1.694   1.00 12.04 ? 227 ASN A N      1 
ATOM   1647 C CA     . ASN A 1 209 ? 20.582 11.980  2.854   1.00 9.91  ? 227 ASN A CA     1 
ATOM   1648 C C      . ASN A 1 209 ? 21.984 12.560  3.002   1.00 8.31  ? 227 ASN A C      1 
ATOM   1649 O O      . ASN A 1 209 ? 22.781 12.013  3.770   1.00 5.08  ? 227 ASN A O      1 
ATOM   1650 C CB     . ASN A 1 209 ? 20.658 10.450  2.810   1.00 11.49 ? 227 ASN A CB     1 
ATOM   1651 C CG     . ASN A 1 209 ? 20.928 9.855   4.172   1.00 7.29  ? 227 ASN A CG     1 
ATOM   1652 O OD1    . ASN A 1 209 ? 20.403 10.326  5.162   1.00 2.18  ? 227 ASN A OD1    1 
ATOM   1653 N ND2    . ASN A 1 209 ? 21.772 8.836   4.227   1.00 10.29 ? 227 ASN A ND2    1 
ATOM   1654 N N      . LEU A 1 210 ? 22.296 13.659  2.312   1.00 11.77 ? 228 LEU A N      1 
ATOM   1655 C CA     . LEU A 1 210 ? 23.576 14.340  2.454   1.00 8.84  ? 228 LEU A CA     1 
ATOM   1656 C C      . LEU A 1 210 ? 23.586 15.255  3.678   1.00 7.55  ? 228 LEU A C      1 
ATOM   1657 O O      . LEU A 1 210 ? 22.546 15.616  4.231   1.00 13.38 ? 228 LEU A O      1 
ATOM   1658 C CB     . LEU A 1 210 ? 23.875 15.145  1.196   1.00 10.35 ? 228 LEU A CB     1 
ATOM   1659 C CG     . LEU A 1 210 ? 24.532 14.453  0.021   1.00 8.20  ? 228 LEU A CG     1 
ATOM   1660 C CD1    . LEU A 1 210 ? 24.011 13.041  -0.075  1.00 8.60  ? 228 LEU A CD1    1 
ATOM   1661 C CD2    . LEU A 1 210 ? 24.163 15.232  -1.190  1.00 6.76  ? 228 LEU A CD2    1 
ATOM   1662 N N      . VAL A 1 211 ? 24.786 15.617  4.111   1.00 9.98  ? 229 VAL A N      1 
ATOM   1663 C CA     . VAL A 1 211 ? 24.974 16.592  5.191   1.00 13.99 ? 229 VAL A CA     1 
ATOM   1664 C C      . VAL A 1 211 ? 25.998 17.591  4.678   1.00 11.28 ? 229 VAL A C      1 
ATOM   1665 O O      . VAL A 1 211 ? 26.841 17.231  3.853   1.00 12.54 ? 229 VAL A O      1 
ATOM   1666 C CB     . VAL A 1 211 ? 25.485 15.970  6.505   1.00 11.74 ? 229 VAL A CB     1 
ATOM   1667 C CG1    . VAL A 1 211 ? 24.573 14.841  6.999   1.00 5.88  ? 229 VAL A CG1    1 
ATOM   1668 C CG2    . VAL A 1 211 ? 26.928 15.485  6.323   1.00 9.67  ? 229 VAL A CG2    1 
ATOM   1669 N N      . PRO A 1 212 ? 25.999 18.821  5.160   1.00 13.86 ? 230 PRO A N      1 
ATOM   1670 C CA     . PRO A 1 212 ? 26.972 19.800  4.650   1.00 15.41 ? 230 PRO A CA     1 
ATOM   1671 C C      . PRO A 1 212 ? 28.403 19.261  4.751   1.00 14.56 ? 230 PRO A C      1 
ATOM   1672 O O      . PRO A 1 212 ? 28.735 18.496  5.654   1.00 14.87 ? 230 PRO A O      1 
ATOM   1673 C CB     . PRO A 1 212 ? 26.740 21.027  5.545   1.00 7.90  ? 230 PRO A CB     1 
ATOM   1674 C CG     . PRO A 1 212 ? 26.045 20.522  6.753   1.00 9.71  ? 230 PRO A CG     1 
ATOM   1675 C CD     . PRO A 1 212 ? 25.270 19.296  6.346   1.00 9.42  ? 230 PRO A CD     1 
ATOM   1676 N N      . VAL A 1 213 ? 29.258 19.652  3.806   1.00 10.65 ? 231 VAL A N      1 
ATOM   1677 C CA     . VAL A 1 213 ? 30.594 19.068  3.749   1.00 14.23 ? 231 VAL A CA     1 
ATOM   1678 C C      . VAL A 1 213 ? 31.421 19.547  4.931   1.00 11.03 ? 231 VAL A C      1 
ATOM   1679 O O      . VAL A 1 213 ? 31.530 20.752  5.184   1.00 18.81 ? 231 VAL A O      1 
ATOM   1680 C CB     . VAL A 1 213 ? 31.288 19.405  2.420   1.00 13.04 ? 231 VAL A CB     1 
ATOM   1681 C CG1    . VAL A 1 213 ? 32.650 18.792  2.413   1.00 11.06 ? 231 VAL A CG1    1 
ATOM   1682 C CG2    . VAL A 1 213 ? 30.488 18.899  1.243   1.00 8.45  ? 231 VAL A CG2    1 
ATOM   1683 N N      . ARG A 1 214 ? 32.075 18.609  5.598   1.00 10.66 ? 232 ARG A N      1 
ATOM   1684 C CA     . ARG A 1 214 ? 32.972 18.890  6.705   1.00 14.00 ? 232 ARG A CA     1 
ATOM   1685 C C      . ARG A 1 214 ? 34.142 17.905  6.580   1.00 16.14 ? 232 ARG A C      1 
ATOM   1686 O O      . ARG A 1 214 ? 34.037 16.934  5.881   1.00 15.67 ? 232 ARG A O      1 
ATOM   1687 C CB     . ARG A 1 214 ? 32.284 18.631  8.036   1.00 11.41 ? 232 ARG A CB     1 
ATOM   1688 C CG     . ARG A 1 214 ? 31.131 17.652  7.992   1.00 11.23 ? 232 ARG A CG     1 
ATOM   1689 C CD     . ARG A 1 214 ? 31.646 16.238  8.034   1.00 10.39 ? 232 ARG A CD     1 
ATOM   1690 N NE     . ARG A 1 214 ? 30.600 15.252  7.855   1.00 14.40 ? 232 ARG A NE     1 
ATOM   1691 C CZ     . ARG A 1 214 ? 30.298 14.362  8.781   1.00 14.40 ? 232 ARG A CZ     1 
ATOM   1692 N NH1    . ARG A 1 214 ? 29.341 13.488  8.580   1.00 21.54 ? 232 ARG A NH1    1 
ATOM   1693 N NH2    . ARG A 1 214 ? 30.958 14.358  9.925   1.00 21.54 ? 232 ARG A NH2    1 
ATOM   1694 N N      . ASP A 1 215 ? 35.238 18.126  7.285   1.00 16.51 ? 233 ASP A N      1 
ATOM   1695 C CA     . ASP A 1 215 ? 36.337 17.165  7.272   1.00 16.58 ? 233 ASP A CA     1 
ATOM   1696 C C      . ASP A 1 215 ? 36.172 16.132  8.382   1.00 18.79 ? 233 ASP A C      1 
ATOM   1697 O O      . ASP A 1 215 ? 35.616 16.416  9.450   1.00 16.44 ? 233 ASP A O      1 
ATOM   1698 C CB     . ASP A 1 215 ? 37.677 17.884  7.388   1.00 12.56 ? 233 ASP A CB     1 
ATOM   1699 C CG     . ASP A 1 215 ? 38.076 18.558  6.081   1.00 19.70 ? 233 ASP A CG     1 
ATOM   1700 O OD1    . ASP A 1 215 ? 37.205 19.171  5.415   1.00 25.21 ? 233 ASP A OD1    1 
ATOM   1701 O OD2    . ASP A 1 215 ? 39.256 18.468  5.689   1.00 27.62 ? 233 ASP A OD2    1 
ATOM   1702 N N      . VAL A 1 216 ? 36.555 14.915  8.055   1.00 21.63 ? 234 VAL A N      1 
ATOM   1703 C CA     . VAL A 1 216 ? 36.319 13.805  8.927   1.00 18.55 ? 234 VAL A CA     1 
ATOM   1704 C C      . VAL A 1 216 ? 37.553 12.961  9.055   1.00 17.86 ? 234 VAL A C      1 
ATOM   1705 O O      . VAL A 1 216 ? 38.370 12.905  8.168   1.00 15.27 ? 234 VAL A O      1 
ATOM   1706 C CB     . VAL A 1 216 ? 35.172 12.983  8.329   1.00 16.98 ? 234 VAL A CB     1 
ATOM   1707 C CG1    . VAL A 1 216 ? 33.929 13.832  8.165   1.00 17.48 ? 234 VAL A CG1    1 
ATOM   1708 C CG2    . VAL A 1 216 ? 35.571 12.366  7.007   1.00 18.02 ? 234 VAL A CG2    1 
ATOM   1709 N N      . PRO A 1 217 ? 37.694 12.306  10.185  1.00 22.93 ? 235 PRO A N      1 
ATOM   1710 C CA     . PRO A 1 217 ? 38.884 11.498  10.457  1.00 21.03 ? 235 PRO A CA     1 
ATOM   1711 C C      . PRO A 1 217 ? 39.171 10.233  9.643   1.00 19.40 ? 235 PRO A C      1 
ATOM   1712 O O      . PRO A 1 217 ? 38.320 9.382   9.534   1.00 21.33 ? 235 PRO A O      1 
ATOM   1713 C CB     . PRO A 1 217 ? 38.689 11.136  11.921  1.00 17.67 ? 235 PRO A CB     1 
ATOM   1714 C CG     . PRO A 1 217 ? 37.800 12.179  12.474  1.00 25.34 ? 235 PRO A CG     1 
ATOM   1715 C CD     . PRO A 1 217 ? 36.847 12.462  11.371  1.00 22.92 ? 235 PRO A CD     1 
ATOM   1716 N N      . LYS A 1 218 ? 40.359 10.105  9.108   1.00 17.34 ? 236 LYS A N      1 
ATOM   1717 C CA     . LYS A 1 218 ? 40.748 8.910   8.401   1.00 15.30 ? 236 LYS A CA     1 
ATOM   1718 C C      . LYS A 1 218 ? 41.475 7.968   9.366   1.00 10.96 ? 236 LYS A C      1 
ATOM   1719 O O      . LYS A 1 218 ? 42.518 8.292   9.891   1.00 9.22  ? 236 LYS A O      1 
ATOM   1720 C CB     . LYS A 1 218 ? 41.567 9.275   7.173   1.00 12.63 ? 236 LYS A CB     1 
ATOM   1721 C CG     . LYS A 1 218 ? 41.616 8.181   6.125   1.00 28.12 ? 236 LYS A CG     1 
ATOM   1722 C CD     . LYS A 1 218 ? 41.529 8.749   4.720   1.00 37.27 ? 236 LYS A CD     1 
ATOM   1723 C CE     . LYS A 1 218 ? 42.811 9.447   4.322   1.00 33.99 ? 236 LYS A CE     1 
ATOM   1724 N NZ     . LYS A 1 218 ? 43.926 8.480   4.149   1.00 30.75 ? 236 LYS A NZ     1 
ATOM   1725 N N      . ILE A 1 219 ? 40.859 6.823   9.650   1.00 13.78 ? 237 ILE A N      1 
ATOM   1726 C CA     . ILE A 1 219 ? 41.423 5.823   10.561  1.00 10.61 ? 237 ILE A CA     1 
ATOM   1727 C C      . ILE A 1 219 ? 41.674 4.509   9.856   1.00 9.92  ? 237 ILE A C      1 
ATOM   1728 O O      . ILE A 1 219 ? 40.850 4.054   9.106   1.00 12.06 ? 237 ILE A O      1 
ATOM   1729 C CB     . ILE A 1 219 ? 40.565 5.634   11.836  1.00 8.96  ? 237 ILE A CB     1 
ATOM   1730 C CG1    . ILE A 1 219 ? 40.215 6.985   12.436  1.00 14.39 ? 237 ILE A CG1    1 
ATOM   1731 C CG2    . ILE A 1 219 ? 41.268 4.767   12.850  1.00 10.66 ? 237 ILE A CG2    1 
ATOM   1732 C CD1    . ILE A 1 219 ? 39.079 6.921   13.407  1.00 14.77 ? 237 ILE A CD1    1 
ATOM   1733 N N      . ALA A 1 220 ? 42.814 3.901   10.121  1.00 13.23 ? 238 ALA A N      1 
ATOM   1734 C CA     . ALA A 1 220 ? 43.223 2.675   9.444   1.00 16.55 ? 238 ALA A CA     1 
ATOM   1735 C C      . ALA A 1 220 ? 43.254 1.508   10.415  1.00 11.05 ? 238 ALA A C      1 
ATOM   1736 O O      . ALA A 1 220 ? 43.605 1.675   11.582  1.00 9.52  ? 238 ALA A O      1 
ATOM   1737 C CB     . ALA A 1 220 ? 44.611 2.825   8.806   1.00 21.26 ? 238 ALA A CB     1 
ATOM   1738 N N      . ILE A 1 221 ? 42.949 0.331   9.921   1.00 12.32 ? 239 ILE A N      1 
ATOM   1739 C CA     . ILE A 1 221 ? 43.018 -0.865  10.728  1.00 15.57 ? 239 ILE A CA     1 
ATOM   1740 C C      . ILE A 1 221 ? 44.402 -1.487  10.772  1.00 16.04 ? 239 ILE A C      1 
ATOM   1741 O O      . ILE A 1 221 ? 45.074 -1.549  9.762   1.00 17.16 ? 239 ILE A O      1 
ATOM   1742 C CB     . ILE A 1 221 ? 42.011 -1.932  10.220  1.00 13.09 ? 239 ILE A CB     1 
ATOM   1743 C CG1    . ILE A 1 221 ? 40.644 -1.323  9.969   1.00 10.93 ? 239 ILE A CG1    1 
ATOM   1744 C CG2    . ILE A 1 221 ? 41.946 -3.120  11.160  1.00 12.43 ? 239 ILE A CG2    1 
ATOM   1745 C CD1    . ILE A 1 221 ? 39.633 -2.327  9.478   1.00 15.24 ? 239 ILE A CD1    1 
ATOM   1746 N N      . ASN A 1 222 ? 44.852 -1.884  11.944  1.00 12.95 ? 240 ASN A N      1 
ATOM   1747 C CA     . ASN A 1 222 ? 46.099 -2.637  12.086  1.00 13.69 ? 240 ASN A CA     1 
ATOM   1748 C C      . ASN A 1 222 ? 45.748 -4.115  11.960  1.00 16.78 ? 240 ASN A C      1 
ATOM   1749 O O      . ASN A 1 222 ? 45.280 -4.747  12.914  1.00 14.36 ? 240 ASN A O      1 
ATOM   1750 C CB     . ASN A 1 222 ? 46.800 -2.320  13.405  1.00 10.71 ? 240 ASN A CB     1 
ATOM   1751 C CG     . ASN A 1 222 ? 48.001 -3.235  13.675  1.00 14.53 ? 240 ASN A CG     1 
ATOM   1752 O OD1    . ASN A 1 222 ? 48.629 -3.772  12.755  1.00 18.66 ? 240 ASN A OD1    1 
ATOM   1753 N ND2    . ASN A 1 222 ? 48.302 -3.434  14.944  1.00 15.76 ? 240 ASN A ND2    1 
ATOM   1754 N N      . GLU A 1 223 ? 45.959 -4.668  10.767  1.00 15.26 ? 241 GLU A N      1 
ATOM   1755 C CA     . GLU A 1 223 ? 45.668 -6.077  10.494  1.00 15.93 ? 241 GLU A CA     1 
ATOM   1756 C C      . GLU A 1 223 ? 46.613 -7.048  11.199  1.00 12.76 ? 241 GLU A C      1 
ATOM   1757 O O      . GLU A 1 223 ? 46.468 -8.261  11.028  1.00 9.53  ? 241 GLU A O      1 
ATOM   1758 C CB     . GLU A 1 223 ? 45.677 -6.315  8.983   1.00 13.61 ? 241 GLU A CB     1 
ATOM   1759 C CG     . GLU A 1 223 ? 44.473 -5.720  8.289   1.00 23.61 ? 241 GLU A CG     1 
ATOM   1760 C CD     . GLU A 1 223 ? 44.686 -5.512  6.797   1.00 46.31 ? 241 GLU A CD     1 
ATOM   1761 O OE1    . GLU A 1 223 ? 45.641 -6.103  6.229   1.00 42.81 ? 241 GLU A OE1    1 
ATOM   1762 O OE2    . GLU A 1 223 ? 43.892 -4.748  6.196   1.00 53.99 ? 241 GLU A OE2    1 
ATOM   1763 N N      . LYS A 1 224 ? 47.561 -6.562  12.002  1.00 20.02 ? 242 LYS A N      1 
ATOM   1764 C CA     . LYS A 1 224 ? 48.481 -7.459  12.687  1.00 19.87 ? 242 LYS A CA     1 
ATOM   1765 C C      . LYS A 1 224 ? 48.022 -7.826  14.091  1.00 16.07 ? 242 LYS A C      1 
ATOM   1766 O O      . LYS A 1 224 ? 48.458 -8.849  14.619  1.00 14.55 ? 242 LYS A O      1 
ATOM   1767 C CB     . LYS A 1 224 ? 49.881 -6.833  12.718  1.00 19.40 ? 242 LYS A CB     1 
ATOM   1768 C CG     . LYS A 1 224 ? 50.483 -6.636  11.322  1.00 17.34 ? 242 LYS A CG     1 
ATOM   1769 C CD     . LYS A 1 224 ? 51.736 -5.768  11.307  1.00 17.68 ? 242 LYS A CD     1 
ATOM   1770 C CE     . LYS A 1 224 ? 51.577 -4.618  12.292  1.00 26.51 ? 242 LYS A CE     1 
ATOM   1771 N NZ     . LYS A 1 224 ? 52.259 -3.332  11.937  1.00 21.24 ? 242 LYS A NZ     1 
ATOM   1772 N N      . VAL A 1 225 ? 47.133 -7.050  14.689  1.00 13.88 ? 243 VAL A N      1 
ATOM   1773 C CA     . VAL A 1 225 ? 46.603 -7.416  15.994  1.00 16.72 ? 243 VAL A CA     1 
ATOM   1774 C C      . VAL A 1 225 ? 46.071 -8.848  15.959  1.00 18.51 ? 243 VAL A C      1 
ATOM   1775 O O      . VAL A 1 225 ? 45.102 -9.152  15.253  1.00 18.24 ? 243 VAL A O      1 
ATOM   1776 C CB     . VAL A 1 225 ? 45.519 -6.414  16.422  1.00 15.67 ? 243 VAL A CB     1 
ATOM   1777 C CG1    . VAL A 1 225 ? 44.911 -6.836  17.724  1.00 12.80 ? 243 VAL A CG1    1 
ATOM   1778 C CG2    . VAL A 1 225 ? 46.124 -5.029  16.505  1.00 12.74 ? 243 VAL A CG2    1 
ATOM   1779 N N      . ALA A 1 226 ? 46.715 -9.743  16.701  1.00 19.06 ? 244 ALA A N      1 
ATOM   1780 C CA     . ALA A 1 226 ? 46.248 -11.121 16.793  1.00 12.98 ? 244 ALA A CA     1 
ATOM   1781 C C      . ALA A 1 226 ? 44.981 -11.169 17.630  1.00 14.50 ? 244 ALA A C      1 
ATOM   1782 O O      . ALA A 1 226 ? 44.961 -10.697 18.770  1.00 21.26 ? 244 ALA A O      1 
ATOM   1783 C CB     . ALA A 1 226 ? 47.328 -12.003 17.397  1.00 16.06 ? 244 ALA A CB     1 
ATOM   1784 N N      . GLY A 1 227 ? 43.921 -11.729 17.057  1.00 15.42 ? 245 GLY A N      1 
ATOM   1785 C CA     . GLY A 1 227 ? 42.611 -11.688 17.675  1.00 18.49 ? 245 GLY A CA     1 
ATOM   1786 C C      . GLY A 1 227 ? 41.897 -10.364 17.583  1.00 21.96 ? 245 GLY A C      1 
ATOM   1787 O O      . GLY A 1 227 ? 40.917 -10.160 18.310  1.00 24.84 ? 245 GLY A O      1 
ATOM   1788 N N      . GLY A 1 228 ? 42.358 -9.457  16.720  1.00 17.56 ? 246 GLY A N      1 
ATOM   1789 C CA     . GLY A 1 228 ? 41.773 -8.134  16.579  1.00 18.45 ? 246 GLY A CA     1 
ATOM   1790 C C      . GLY A 1 228 ? 40.265 -8.106  16.437  1.00 16.08 ? 246 GLY A C      1 
ATOM   1791 O O      . GLY A 1 228 ? 39.660 -9.024  15.859  1.00 15.24 ? 246 GLY A O      1 
ATOM   1792 N N      . TYR A 1 229 ? 39.628 -7.060  16.947  1.00 14.05 ? 247 TYR A N      1 
ATOM   1793 C CA     . TYR A 1 229 ? 38.172 -7.002  16.950  1.00 16.09 ? 247 TYR A CA     1 
ATOM   1794 C C      . TYR A 1 229 ? 37.548 -7.108  15.590  1.00 14.34 ? 247 TYR A C      1 
ATOM   1795 O O      . TYR A 1 229 ? 36.470 -7.643  15.447  1.00 16.44 ? 247 TYR A O      1 
ATOM   1796 C CB     . TYR A 1 229 ? 37.640 -5.775  17.722  1.00 12.79 ? 247 TYR A CB     1 
ATOM   1797 C CG     . TYR A 1 229 ? 36.142 -5.654  17.759  1.00 14.29 ? 247 TYR A CG     1 
ATOM   1798 C CD1    . TYR A 1 229 ? 35.399 -6.326  18.707  1.00 9.39  ? 247 TYR A CD1    1 
ATOM   1799 C CD2    . TYR A 1 229 ? 35.474 -4.872  16.842  1.00 14.80 ? 247 TYR A CD2    1 
ATOM   1800 C CE1    . TYR A 1 229 ? 34.030 -6.221  18.737  1.00 10.44 ? 247 TYR A CE1    1 
ATOM   1801 C CE2    . TYR A 1 229 ? 34.106 -4.764  16.863  1.00 15.96 ? 247 TYR A CE2    1 
ATOM   1802 C CZ     . TYR A 1 229 ? 33.392 -5.438  17.814  1.00 18.51 ? 247 TYR A CZ     1 
ATOM   1803 O OH     . TYR A 1 229 ? 32.031 -5.320  17.829  1.00 19.27 ? 247 TYR A OH     1 
ATOM   1804 N N      . SER A 1 230 ? 38.240 -6.614  14.589  1.00 12.48 ? 248 SER A N      1 
ATOM   1805 C CA     . SER A 1 230 ? 37.622 -6.632  13.268  1.00 11.74 ? 248 SER A CA     1 
ATOM   1806 C C      . SER A 1 230 ? 37.767 -7.987  12.589  1.00 12.65 ? 248 SER A C      1 
ATOM   1807 O O      . SER A 1 230 ? 36.970 -8.323  11.707  1.00 17.01 ? 248 SER A O      1 
ATOM   1808 C CB     . SER A 1 230 ? 38.199 -5.528  12.389  1.00 12.08 ? 248 SER A CB     1 
ATOM   1809 O OG     . SER A 1 230 ? 39.537 -5.805  12.082  1.00 18.73 ? 248 SER A OG     1 
ATOM   1810 N N      . LYS A 1 231 ? 38.755 -8.785  12.973  1.00 15.27 ? 249 LYS A N      1 
ATOM   1811 C CA     . LYS A 1 231 ? 38.762 -10.171 12.521  1.00 15.62 ? 249 LYS A CA     1 
ATOM   1812 C C      . LYS A 1 231 ? 37.713 -10.991 13.252  1.00 12.90 ? 249 LYS A C      1 
ATOM   1813 O O      . LYS A 1 231 ? 37.178 -11.951 12.695  1.00 13.63 ? 249 LYS A O      1 
ATOM   1814 C CB     . LYS A 1 231 ? 40.144 -10.787 12.722  1.00 13.57 ? 249 LYS A CB     1 
ATOM   1815 C CG     . LYS A 1 231 ? 41.290 -10.038 12.037  1.00 12.25 ? 249 LYS A CG     1 
ATOM   1816 C CD     . LYS A 1 231 ? 42.595 -10.385 12.736  1.00 12.68 ? 249 LYS A CD     1 
ATOM   1817 C CE     . LYS A 1 231 ? 43.791 -9.934  11.944  1.00 11.90 ? 249 LYS A CE     1 
ATOM   1818 N NZ     . LYS A 1 231 ? 45.052 -10.179 12.690  1.00 11.18 ? 249 LYS A NZ     1 
ATOM   1819 N N      . THR A 1 232 ? 37.387 -10.591 14.480  1.00 16.08 ? 250 THR A N      1 
ATOM   1820 C CA     . THR A 1 232 ? 36.420 -11.298 15.313  1.00 16.00 ? 250 THR A CA     1 
ATOM   1821 C C      . THR A 1 232 ? 34.968 -10.970 14.962  1.00 17.26 ? 250 THR A C      1 
ATOM   1822 O O      . THR A 1 232 ? 34.081 -11.815 15.141  1.00 18.98 ? 250 THR A O      1 
ATOM   1823 C CB     . THR A 1 232 ? 36.685 -10.951 16.777  1.00 17.02 ? 250 THR A CB     1 
ATOM   1824 O OG1    . THR A 1 232 ? 37.793 -11.723 17.251  1.00 16.67 ? 250 THR A OG1    1 
ATOM   1825 C CG2    . THR A 1 232 ? 35.440 -11.207 17.623  1.00 15.70 ? 250 THR A CG2    1 
ATOM   1826 N N      . LYS A 1 233 ? 34.688 -9.691  14.689  1.00 14.22 ? 251 LYS A N      1 
ATOM   1827 C CA     . LYS A 1 233 ? 33.335 -9.218  14.351  1.00 15.51 ? 251 LYS A CA     1 
ATOM   1828 C C      . LYS A 1 233 ? 33.374 -8.554  12.931  1.00 15.20 ? 251 LYS A C      1 
ATOM   1829 O O      . LYS A 1 233 ? 33.233 -7.361  12.844  1.00 13.80 ? 251 LYS A O      1 
ATOM   1830 C CB     . LYS A 1 233 ? 32.749 -8.311  15.437  1.00 14.63 ? 251 LYS A CB     1 
ATOM   1831 C CG     . LYS A 1 233 ? 31.946 -9.013  16.500  1.00 14.63 ? 251 LYS A CG     1 
ATOM   1832 C CD     . LYS A 1 233 ? 30.495 -9.098  16.087  1.00 18.61 ? 251 LYS A CD     1 
ATOM   1833 C CE     . LYS A 1 233 ? 29.692 -7.969  16.687  1.00 18.45 ? 251 LYS A CE     1 
ATOM   1834 N NZ     . LYS A 1 233 ? 28.515 -8.470  17.433  1.00 25.46 ? 251 LYS A NZ     1 
ATOM   1835 N N      . PRO A 1 234 ? 33.616 -9.319  11.824  1.00 19.32 ? 252 PRO A N      1 
ATOM   1836 C CA     . PRO A 1 234 ? 33.682 -8.676  10.504  1.00 19.49 ? 252 PRO A CA     1 
ATOM   1837 C C      . PRO A 1 234 ? 32.381 -8.015  10.102  1.00 18.27 ? 252 PRO A C      1 
ATOM   1838 O O      . PRO A 1 234 ? 32.381 -7.239  9.139   1.00 18.80 ? 252 PRO A O      1 
ATOM   1839 C CB     . PRO A 1 234 ? 34.059 -9.828  9.555   1.00 17.48 ? 252 PRO A CB     1 
ATOM   1840 C CG     . PRO A 1 234 ? 33.943 -11.087 10.364  1.00 16.27 ? 252 PRO A CG     1 
ATOM   1841 C CD     . PRO A 1 234 ? 34.090 -10.715 11.796  1.00 15.81 ? 252 PRO A CD     1 
ATOM   1842 N N      . THR A 1 235 ? 31.274 -8.278  10.799  1.00 17.30 ? 253 THR A N      1 
ATOM   1843 C CA     . THR A 1 235 ? 30.020 -7.656  10.393  1.00 14.42 ? 253 THR A CA     1 
ATOM   1844 C C      . THR A 1 235 ? 29.885 -6.239  10.930  1.00 14.31 ? 253 THR A C      1 
ATOM   1845 O O      . THR A 1 235 ? 29.080 -5.461  10.416  1.00 17.08 ? 253 THR A O      1 
ATOM   1846 C CB     . THR A 1 235 ? 28.828 -8.498  10.844  1.00 17.47 ? 253 THR A CB     1 
ATOM   1847 O OG1    . THR A 1 235 ? 28.881 -8.686  12.265  1.00 17.35 ? 253 THR A OG1    1 
ATOM   1848 C CG2    . THR A 1 235 ? 28.843 -9.849  10.148  1.00 15.07 ? 253 THR A CG2    1 
ATOM   1849 N N      . THR A 1 236 ? 30.655 -5.890  11.937  1.00 12.15 ? 254 THR A N      1 
ATOM   1850 C CA     . THR A 1 236 ? 30.715 -4.524  12.422  1.00 12.35 ? 254 THR A CA     1 
ATOM   1851 C C      . THR A 1 236 ? 31.501 -3.681  11.433  1.00 17.26 ? 254 THR A C      1 
ATOM   1852 O O      . THR A 1 236 ? 32.676 -3.988  11.180  1.00 14.51 ? 254 THR A O      1 
ATOM   1853 C CB     . THR A 1 236 ? 31.407 -4.468  13.782  1.00 14.45 ? 254 THR A CB     1 
ATOM   1854 O OG1    . THR A 1 236 ? 30.818 -5.428  14.672  1.00 22.34 ? 254 THR A OG1    1 
ATOM   1855 C CG2    . THR A 1 236 ? 31.351 -3.075  14.376  1.00 8.98  ? 254 THR A CG2    1 
ATOM   1856 N N      . PRO A 1 237 ? 30.909 -2.530  11.030  1.00 13.62 ? 255 PRO A N      1 
ATOM   1857 C CA     . PRO A 1 237 ? 31.701 -1.608  10.229  1.00 11.17 ? 255 PRO A CA     1 
ATOM   1858 C C      . PRO A 1 237 ? 32.781 -0.923  11.053  1.00 8.97  ? 255 PRO A C      1 
ATOM   1859 O O      . PRO A 1 237 ? 32.530 -0.525  12.150  1.00 12.10 ? 255 PRO A O      1 
ATOM   1860 C CB     . PRO A 1 237 ? 30.668 -0.612  9.759   1.00 10.96 ? 255 PRO A CB     1 
ATOM   1861 C CG     . PRO A 1 237 ? 29.370 -1.326  9.819   1.00 14.60 ? 255 PRO A CG     1 
ATOM   1862 C CD     . PRO A 1 237 ? 29.498 -2.112  11.072  1.00 10.61 ? 255 PRO A CD     1 
ATOM   1863 N N      . PHE A 1 238 ? 33.977 -0.834  10.528  1.00 9.35  ? 256 PHE A N      1 
ATOM   1864 C CA     . PHE A 1 238 ? 35.064 -0.180  11.212  1.00 11.47 ? 256 PHE A CA     1 
ATOM   1865 C C      . PHE A 1 238 ? 35.031 1.299   11.075  1.00 12.98 ? 256 PHE A C      1 
ATOM   1866 O O      . PHE A 1 238 ? 35.121 1.832   9.992   1.00 17.79 ? 256 PHE A O      1 
ATOM   1867 C CB     . PHE A 1 238 ? 36.416 -0.718  10.743  1.00 8.70  ? 256 PHE A CB     1 
ATOM   1868 C CG     . PHE A 1 238 ? 37.613 -0.075  11.392  1.00 12.32 ? 256 PHE A CG     1 
ATOM   1869 C CD1    . PHE A 1 238 ? 38.184 1.066   10.861  1.00 12.83 ? 256 PHE A CD1    1 
ATOM   1870 C CD2    . PHE A 1 238 ? 38.205 -0.648  12.497  1.00 14.62 ? 256 PHE A CD2    1 
ATOM   1871 C CE1    . PHE A 1 238 ? 39.287 1.644   11.444  1.00 12.35 ? 256 PHE A CE1    1 
ATOM   1872 C CE2    . PHE A 1 238 ? 39.315 -0.077  13.082  1.00 9.95  ? 256 PHE A CE2    1 
ATOM   1873 C CZ     . PHE A 1 238 ? 39.855 1.072   12.556  1.00 11.36 ? 256 PHE A CZ     1 
ATOM   1874 N N      . VAL A 1 239 ? 34.876 1.970   12.186  1.00 10.67 ? 257 VAL A N      1 
ATOM   1875 C CA     . VAL A 1 239 ? 34.938 3.378   12.175  1.00 12.63 ? 257 VAL A CA     1 
ATOM   1876 C C      . VAL A 1 239 ? 36.215 3.744   12.916  1.00 12.98 ? 257 VAL A C      1 
ATOM   1877 O O      . VAL A 1 239 ? 37.116 4.286   12.327  1.00 13.09 ? 257 VAL A O      1 
ATOM   1878 C CB     . VAL A 1 239 ? 33.631 3.959   12.733  1.00 13.96 ? 257 VAL A CB     1 
ATOM   1879 C CG1    . VAL A 1 239 ? 33.595 5.457   12.580  1.00 12.43 ? 257 VAL A CG1    1 
ATOM   1880 C CG2    . VAL A 1 239 ? 32.441 3.317   12.042  1.00 8.19  ? 257 VAL A CG2    1 
ATOM   1881 N N      . ALA A 1 240 ? 36.313 3.418   14.186  1.00 10.65 ? 258 ALA A N      1 
ATOM   1882 C CA     . ALA A 1 240 ? 37.527 3.649   14.957  1.00 10.19 ? 258 ALA A CA     1 
ATOM   1883 C C      . ALA A 1 240 ? 37.871 2.526   15.929  1.00 19.11 ? 258 ALA A C      1 
ATOM   1884 O O      . ALA A 1 240 ? 38.595 2.764   16.873  1.00 40.04 ? 258 ALA A O      1 
ATOM   1885 C CB     . ALA A 1 240 ? 37.413 4.958   15.679  1.00 8.94  ? 258 ALA A CB     1 
ATOM   1886 N N      . SER A 1 241 ? 37.383 1.320   15.708  1.00 16.05 ? 259 SER A N      1 
ATOM   1887 C CA     . SER A 1 241 ? 37.516 0.179   16.635  1.00 11.88 ? 259 SER A CA     1 
ATOM   1888 C C      . SER A 1 241 ? 36.803 0.433   17.913  1.00 11.49 ? 259 SER A C      1 
ATOM   1889 O O      . SER A 1 241 ? 35.911 1.211   17.968  1.00 22.60 ? 259 SER A O      1 
ATOM   1890 C CB     . SER A 1 241 ? 38.904 -0.400  16.812  1.00 14.10 ? 259 SER A CB     1 
ATOM   1891 O OG     . SER A 1 241 ? 38.853 -1.749  17.203  1.00 16.76 ? 259 SER A OG     1 
ATOM   1892 N N      . LEU A 1 242 ? 37.203 -0.208  18.954  1.00 16.75 ? 260 LEU A N      1 
ATOM   1893 C CA     . LEU A 1 242 ? 36.572 -0.052  20.226  1.00 13.50 ? 260 LEU A CA     1 
ATOM   1894 C C      . LEU A 1 242 ? 36.682 1.276   20.929  1.00 17.68 ? 260 LEU A C      1 
ATOM   1895 O O      . LEU A 1 242 ? 37.662 1.955   20.814  1.00 20.54 ? 260 LEU A O      1 
ATOM   1896 C CB     . LEU A 1 242 ? 37.063 -1.168  21.116  1.00 12.60 ? 260 LEU A CB     1 
ATOM   1897 C CG     . LEU A 1 242 ? 36.800 -2.587  20.618  1.00 16.30 ? 260 LEU A CG     1 
ATOM   1898 C CD1    . LEU A 1 242 ? 37.309 -3.600  21.621  1.00 9.93  ? 260 LEU A CD1    1 
ATOM   1899 C CD2    . LEU A 1 242 ? 35.324 -2.802  20.332  1.00 13.18 ? 260 LEU A CD2    1 
ATOM   1900 N N      . SER A 1 243 ? 35.650 1.643   21.672  1.00 16.34 ? 261 SER A N      1 
ATOM   1901 C CA     . SER A 1 243 ? 35.627 2.882   22.402  1.00 11.64 ? 261 SER A CA     1 
ATOM   1902 C C      . SER A 1 243 ? 36.039 2.780   23.834  1.00 16.56 ? 261 SER A C      1 
ATOM   1903 O O      . SER A 1 243 ? 35.520 1.974   24.573  1.00 15.64 ? 261 SER A O      1 
ATOM   1904 C CB     . SER A 1 243 ? 34.249 3.508   22.304  1.00 12.77 ? 261 SER A CB     1 
ATOM   1905 O OG     . SER A 1 243 ? 34.162 4.772   22.922  1.00 16.01 ? 261 SER A OG     1 
ATOM   1906 N N      . GLY A 1 244 ? 36.991 3.602   24.228  1.00 16.90 ? 262 GLY A N      1 
ATOM   1907 C CA     . GLY A 1 244 ? 37.412 3.663   25.592  1.00 16.80 ? 262 GLY A CA     1 
ATOM   1908 C C      . GLY A 1 244 ? 36.861 4.836   26.289  1.00 13.98 ? 262 GLY A C      1 
ATOM   1909 O O      . GLY A 1 244 ? 37.246 5.118   27.391  1.00 20.92 ? 262 GLY A O      1 
ATOM   1910 N N      . THR A 1 245 ? 36.000 5.559   25.620  1.00 13.45 ? 263 THR A N      1 
ATOM   1911 C CA     . THR A 1 245 ? 35.335 6.639   26.235  1.00 15.54 ? 263 THR A CA     1 
ATOM   1912 C C      . THR A 1 245 ? 34.129 6.004   26.847  1.00 15.57 ? 263 THR A C      1 
ATOM   1913 O O      . THR A 1 245 ? 33.452 6.595   27.655  1.00 13.49 ? 263 THR A O      1 
ATOM   1914 C CB     . THR A 1 245 ? 35.055 7.734   25.226  1.00 13.29 ? 263 THR A CB     1 
ATOM   1915 O OG1    . THR A 1 245 ? 36.233 7.983   24.468  1.00 22.34 ? 263 THR A OG1    1 
ATOM   1916 C CG2    . THR A 1 245 ? 34.638 9.005   25.928  1.00 13.25 ? 263 THR A CG2    1 
ATOM   1917 N N      . THR A 1 246 ? 33.866 4.776   26.465  1.00 13.83 ? 264 THR A N      1 
ATOM   1918 C CA     . THR A 1 246 ? 32.787 4.018   27.042  1.00 14.25 ? 264 THR A CA     1 
ATOM   1919 C C      . THR A 1 246 ? 33.098 3.765   28.504  1.00 12.92 ? 264 THR A C      1 
ATOM   1920 O O      . THR A 1 246 ? 32.209 3.774   29.322  1.00 12.36 ? 264 THR A O      1 
ATOM   1921 C CB     . THR A 1 246 ? 32.522 2.767   26.193  1.00 13.57 ? 264 THR A CB     1 
ATOM   1922 O OG1    . THR A 1 246 ? 32.298 3.151   24.840  1.00 16.15 ? 264 THR A OG1    1 
ATOM   1923 C CG2    . THR A 1 246 ? 31.312 2.018   26.708  1.00 11.99 ? 264 THR A CG2    1 
ATOM   1924 N N      . TYR A 1 247 ? 34.351 3.521   28.825  1.00 12.77 ? 265 TYR A N      1 
ATOM   1925 C CA     . TYR A 1 247 ? 34.787 3.382   30.184  1.00 11.72 ? 265 TYR A CA     1 
ATOM   1926 C C      . TYR A 1 247 ? 34.596 4.679   30.936  1.00 16.24 ? 265 TYR A C      1 
ATOM   1927 O O      . TYR A 1 247 ? 34.316 4.675   32.112  1.00 14.90 ? 265 TYR A O      1 
ATOM   1928 C CB     . TYR A 1 247 ? 36.225 2.904   30.219  1.00 12.04 ? 265 TYR A CB     1 
ATOM   1929 C CG     . TYR A 1 247 ? 36.455 1.577   29.565  1.00 12.89 ? 265 TYR A CG     1 
ATOM   1930 C CD1    . TYR A 1 247 ? 35.876 0.427   30.065  1.00 13.13 ? 265 TYR A CD1    1 
ATOM   1931 C CD2    . TYR A 1 247 ? 37.264 1.471   28.451  1.00 13.87 ? 265 TYR A CD2    1 
ATOM   1932 C CE1    . TYR A 1 247 ? 36.087 -0.792  29.459  1.00 15.40 ? 265 TYR A CE1    1 
ATOM   1933 C CE2    . TYR A 1 247 ? 37.480 0.259   27.844  1.00 15.03 ? 265 TYR A CE2    1 
ATOM   1934 C CZ     . TYR A 1 247 ? 36.887 -0.866  28.354  1.00 16.07 ? 265 TYR A CZ     1 
ATOM   1935 O OH     . TYR A 1 247 ? 37.102 -2.066  27.750  1.00 16.33 ? 265 TYR A OH     1 
ATOM   1936 N N      . SER A 1 248 ? 34.790 5.795   30.283  1.00 15.19 ? 266 SER A N      1 
ATOM   1937 C CA     . SER A 1 248 ? 34.518 7.072   30.884  1.00 15.92 ? 266 SER A CA     1 
ATOM   1938 C C      . SER A 1 248 ? 33.067 7.337   31.246  1.00 14.81 ? 266 SER A C      1 
ATOM   1939 O O      . SER A 1 248 ? 32.810 7.907   32.282  1.00 18.66 ? 266 SER A O      1 
ATOM   1940 C CB     . SER A 1 248 ? 35.174 8.174   30.065  1.00 19.72 ? 266 SER A CB     1 
ATOM   1941 O OG     . SER A 1 248 ? 36.423 7.763   29.584  1.00 19.42 ? 266 SER A OG     1 
ATOM   1942 N N      . LEU A 1 249 ? 32.122 6.936   30.418  1.00 11.34 ? 267 LEU A N      1 
ATOM   1943 C CA     . LEU A 1 249 ? 30.719 7.030   30.752  1.00 10.37 ? 267 LEU A CA     1 
ATOM   1944 C C      . LEU A 1 249 ? 30.480 6.160   31.939  1.00 13.91 ? 267 LEU A C      1 
ATOM   1945 O O      . LEU A 1 249 ? 29.674 6.469   32.774  1.00 16.26 ? 267 LEU A O      1 
ATOM   1946 C CB     . LEU A 1 249 ? 29.825 6.610   29.583  1.00 9.99  ? 267 LEU A CB     1 
ATOM   1947 C CG     . LEU A 1 249 ? 28.334 6.445   29.781  1.00 8.29  ? 267 LEU A CG     1 
ATOM   1948 C CD1    . LEU A 1 249 ? 27.708 7.795   30.046  1.00 8.17  ? 267 LEU A CD1    1 
ATOM   1949 C CD2    . LEU A 1 249 ? 27.754 5.815   28.535  1.00 7.68  ? 267 LEU A CD2    1 
ATOM   1950 N N      . MET A 1 250 ? 31.162 5.049   32.009  1.00 12.00 ? 268 MET A N      1 
ATOM   1951 C CA     . MET A 1 250 ? 31.046 4.159   33.130  1.00 11.74 ? 268 MET A CA     1 
ATOM   1952 C C      . MET A 1 250 ? 31.460 4.707   34.465  1.00 15.84 ? 268 MET A C      1 
ATOM   1953 O O      . MET A 1 250 ? 30.823 4.401   35.437  1.00 20.97 ? 268 MET A O      1 
ATOM   1954 C CB     . MET A 1 250 ? 31.794 2.872   32.835  1.00 11.10 ? 268 MET A CB     1 
ATOM   1955 C CG     . MET A 1 250 ? 31.079 1.954   31.862  1.00 16.49 ? 268 MET A CG     1 
ATOM   1956 S SD     . MET A 1 250 ? 29.356 1.653   32.284  1.00 13.53 ? 268 MET A SD     1 
ATOM   1957 C CE     . MET A 1 250 ? 29.518 0.784   33.831  1.00 16.79 ? 268 MET A CE     1 
ATOM   1958 N N      . VAL A 1 251 ? 32.529 5.473   34.546  1.00 14.17 ? 269 VAL A N      1 
ATOM   1959 C CA     . VAL A 1 251 ? 32.929 6.097   35.772  1.00 13.03 ? 269 VAL A CA     1 
ATOM   1960 C C      . VAL A 1 251 ? 31.895 7.069   36.236  1.00 15.95 ? 269 VAL A C      1 
ATOM   1961 O O      . VAL A 1 251 ? 31.567 7.115   37.401  1.00 22.01 ? 269 VAL A O      1 
ATOM   1962 C CB     . VAL A 1 251 ? 34.289 6.804   35.606  1.00 15.00 ? 269 VAL A CB     1 
ATOM   1963 C CG1    . VAL A 1 251 ? 34.651 7.622   36.832  1.00 17.13 ? 269 VAL A CG1    1 
ATOM   1964 C CG2    . VAL A 1 251 ? 35.379 5.796   35.303  1.00 22.36 ? 269 VAL A CG2    1 
ATOM   1965 N N      . VAL A 1 252 ? 31.377 7.861   35.338  1.00 13.98 ? 270 VAL A N      1 
ATOM   1966 C CA     . VAL A 1 252 ? 30.319 8.765   35.696  1.00 17.97 ? 270 VAL A CA     1 
ATOM   1967 C C      . VAL A 1 252 ? 29.022 8.044   36.052  1.00 16.00 ? 270 VAL A C      1 
ATOM   1968 O O      . VAL A 1 252 ? 28.356 8.407   37.001  1.00 17.54 ? 270 VAL A O      1 
ATOM   1969 C CB     . VAL A 1 252 ? 30.193 9.931   34.673  1.00 16.45 ? 270 VAL A CB     1 
ATOM   1970 C CG1    . VAL A 1 252 ? 30.245 9.432   33.251  1.00 17.57 ? 270 VAL A CG1    1 
ATOM   1971 C CG2    . VAL A 1 252 ? 28.959 10.770  34.930  1.00 16.82 ? 270 VAL A CG2    1 
ATOM   1972 N N      . LEU A 1 253 ? 28.677 7.023   35.305  1.00 15.29 ? 271 LEU A N      1 
ATOM   1973 C CA     . LEU A 1 253 ? 27.481 6.249   35.563  1.00 17.22 ? 271 LEU A CA     1 
ATOM   1974 C C      . LEU A 1 253 ? 27.510 5.495   36.877  1.00 15.55 ? 271 LEU A C      1 
ATOM   1975 O O      . LEU A 1 253 ? 26.502 5.363   37.520  1.00 14.45 ? 271 LEU A O      1 
ATOM   1976 C CB     . LEU A 1 253 ? 27.178 5.339   34.375  1.00 9.83  ? 271 LEU A CB     1 
ATOM   1977 C CG     . LEU A 1 253 ? 26.376 5.897   33.217  1.00 9.94  ? 271 LEU A CG     1 
ATOM   1978 C CD1    . LEU A 1 253 ? 26.118 4.779   32.229  1.00 8.30  ? 271 LEU A CD1    1 
ATOM   1979 C CD2    . LEU A 1 253 ? 25.071 6.453   33.747  1.00 14.56 ? 271 LEU A CD2    1 
ATOM   1980 N N      . THR A 1 254 ? 28.663 4.978   37.254  1.00 12.99 ? 272 THR A N      1 
ATOM   1981 C CA     . THR A 1 254 ? 28.807 4.305   38.523  1.00 17.46 ? 272 THR A CA     1 
ATOM   1982 C C      . THR A 1 254 ? 28.528 5.254   39.657  1.00 22.84 ? 272 THR A C      1 
ATOM   1983 O O      . THR A 1 254 ? 27.801 4.903   40.559  1.00 22.37 ? 272 THR A O      1 
ATOM   1984 C CB     . THR A 1 254 ? 30.193 3.643   38.685  1.00 18.33 ? 272 THR A CB     1 
ATOM   1985 O OG1    . THR A 1 254 ? 30.390 2.672   37.656  1.00 22.41 ? 272 THR A OG1    1 
ATOM   1986 C CG2    . THR A 1 254 ? 30.296 2.952   40.015  1.00 10.07 ? 272 THR A CG2    1 
ATOM   1987 N N      . ASP A 1 255 ? 29.022 6.477   39.585  1.00 22.58 ? 273 ASP A N      1 
ATOM   1988 C CA     . ASP A 1 255 ? 28.749 7.477   40.593  1.00 16.47 ? 273 ASP A CA     1 
ATOM   1989 C C      . ASP A 1 255 ? 27.288 7.800   40.694  1.00 19.26 ? 273 ASP A C      1 
ATOM   1990 O O      . ASP A 1 255 ? 26.787 7.972   41.784  1.00 18.97 ? 273 ASP A O      1 
ATOM   1991 C CB     . ASP A 1 255 ? 29.507 8.749   40.231  1.00 21.31 ? 273 ASP A CB     1 
ATOM   1992 C CG     . ASP A 1 255 ? 29.482 9.789   41.314  1.00 23.18 ? 273 ASP A CG     1 
ATOM   1993 O OD1    . ASP A 1 255 ? 28.720 10.755  41.172  1.00 21.65 ? 273 ASP A OD1    1 
ATOM   1994 O OD2    . ASP A 1 255 ? 30.243 9.663   42.288  1.00 20.20 ? 273 ASP A OD2    1 
ATOM   1995 N N      . TYR A 1 256 ? 26.614 7.922   39.565  1.00 20.46 ? 274 TYR A N      1 
ATOM   1996 C CA     . TYR A 1 256 ? 25.197 8.216   39.529  1.00 20.43 ? 274 TYR A CA     1 
ATOM   1997 C C      . TYR A 1 256 ? 24.335 7.122   40.113  1.00 21.20 ? 274 TYR A C      1 
ATOM   1998 O O      . TYR A 1 256 ? 23.399 7.389   40.839  1.00 19.66 ? 274 TYR A O      1 
ATOM   1999 C CB     . TYR A 1 256 ? 24.798 8.500   38.075  1.00 16.95 ? 274 TYR A CB     1 
ATOM   2000 C CG     . TYR A 1 256 ? 23.365 8.863   37.843  1.00 13.50 ? 274 TYR A CG     1 
ATOM   2001 C CD1    . TYR A 1 256 ? 22.911 10.140  38.093  1.00 19.05 ? 274 TYR A CD1    1 
ATOM   2002 C CD2    . TYR A 1 256 ? 22.474 7.936   37.345  1.00 14.68 ? 274 TYR A CD2    1 
ATOM   2003 C CE1    . TYR A 1 256 ? 21.601 10.481  37.876  1.00 20.82 ? 274 TYR A CE1    1 
ATOM   2004 C CE2    . TYR A 1 256 ? 21.160 8.267   37.126  1.00 17.21 ? 274 TYR A CE2    1 
ATOM   2005 C CZ     . TYR A 1 256 ? 20.734 9.543   37.392  1.00 21.79 ? 274 TYR A CZ     1 
ATOM   2006 O OH     . TYR A 1 256 ? 19.432 9.880   37.171  1.00 21.78 ? 274 TYR A OH     1 
ATOM   2007 N N      . ILE A 1 257 ? 24.642 5.891   39.779  1.00 17.58 ? 275 ILE A N      1 
ATOM   2008 C CA     . ILE A 1 257 ? 23.892 4.788   40.273  1.00 18.63 ? 275 ILE A CA     1 
ATOM   2009 C C      . ILE A 1 257 ? 24.084 4.703   41.757  1.00 22.81 ? 275 ILE A C      1 
ATOM   2010 O O      . ILE A 1 257 ? 23.171 4.376   42.481  1.00 22.65 ? 275 ILE A O      1 
ATOM   2011 C CB     . ILE A 1 257 ? 24.243 3.491   39.536  1.00 16.02 ? 275 ILE A CB     1 
ATOM   2012 C CG1    . ILE A 1 257 ? 23.954 3.639   38.049  1.00 16.35 ? 275 ILE A CG1    1 
ATOM   2013 C CG2    . ILE A 1 257 ? 23.456 2.335   40.107  1.00 19.35 ? 275 ILE A CG2    1 
ATOM   2014 C CD1    . ILE A 1 257 ? 24.348 2.437   37.229  1.00 15.84 ? 275 ILE A CD1    1 
ATOM   2015 N N      . GLU A 1 258 ? 25.278 4.980   42.217  1.00 19.68 ? 276 GLU A N      1 
ATOM   2016 C CA     . GLU A 1 258 ? 25.546 4.945   43.614  1.00 18.51 ? 276 GLU A CA     1 
ATOM   2017 C C      . GLU A 1 258 ? 24.756 5.980   44.366  1.00 24.54 ? 276 GLU A C      1 
ATOM   2018 O O      . GLU A 1 258 ? 24.281 5.722   45.465  1.00 21.69 ? 276 GLU A O      1 
ATOM   2019 C CB     . GLU A 1 258 ? 27.028 5.072   43.866  1.00 19.31 ? 276 GLU A CB     1 
ATOM   2020 C CG     . GLU A 1 258 ? 27.880 3.952   43.297  1.00 31.84 ? 276 GLU A CG     1 
ATOM   2021 C CD     . GLU A 1 258 ? 27.383 2.560   43.640  1.00 51.05 ? 276 GLU A CD     1 
ATOM   2022 O OE1    . GLU A 1 258 ? 27.112 2.288   44.826  1.00 45.31 ? 276 GLU A OE1    1 
ATOM   2023 O OE2    . GLU A 1 258 ? 27.288 1.725   42.715  1.00 44.14 ? 276 GLU A OE2    1 
ATOM   2024 N N      . LYS A 1 259 ? 24.560 7.138   43.770  1.00 18.63 ? 277 LYS A N      1 
ATOM   2025 C CA     . LYS A 1 259 ? 23.871 8.212   44.451  1.00 22.78 ? 277 LYS A CA     1 
ATOM   2026 C C      . LYS A 1 259 ? 22.384 8.289   44.185  1.00 24.11 ? 277 LYS A C      1 
ATOM   2027 O O      . LYS A 1 259 ? 21.709 9.090   44.793  1.00 25.46 ? 277 LYS A O      1 
ATOM   2028 C CB     . LYS A 1 259 ? 24.588 9.533   44.214  1.00 23.28 ? 277 LYS A CB     1 
ATOM   2029 C CG     . LYS A 1 259 ? 24.630 10.073  42.807  1.00 23.37 ? 277 LYS A CG     1 
ATOM   2030 C CD     . LYS A 1 259 ? 25.562 11.265  42.794  1.00 27.57 ? 277 LYS A CD     1 
ATOM   2031 C CE     . LYS A 1 259 ? 26.687 11.058  43.797  1.00 25.88 ? 277 LYS A CE     1 
ATOM   2032 N NZ     . LYS A 1 259 ? 27.706 12.138  43.757  1.00 17.67 ? 277 LYS A NZ     1 
ATOM   2033 N N      . HIS A 1 260 ? 21.883 7.484   43.269  1.00 24.27 ? 278 HIS A N      1 
ATOM   2034 C CA     . HIS A 1 260 ? 20.466 7.409   42.978  1.00 20.31 ? 278 HIS A CA     1 
ATOM   2035 C C      . HIS A 1 260 ? 19.951 5.961   43.079  1.00 23.50 ? 278 HIS A C      1 
ATOM   2036 O O      . HIS A 1 260 ? 18.982 5.617   42.435  1.00 25.47 ? 278 HIS A O      1 
ATOM   2037 C CB     . HIS A 1 260 ? 20.193 7.996   41.603  1.00 17.80 ? 278 HIS A CB     1 
ATOM   2038 C CG     . HIS A 1 260 ? 20.223 9.485   41.559  1.00 18.57 ? 278 HIS A CG     1 
ATOM   2039 N ND1    . HIS A 1 260 ? 21.395 10.203  41.517  1.00 19.84 ? 278 HIS A ND1    1 
ATOM   2040 C CD2    . HIS A 1 260 ? 19.223 10.393  41.533  1.00 20.55 ? 278 HIS A CD2    1 
ATOM   2041 C CE1    . HIS A 1 260 ? 21.116 11.491  41.480  1.00 23.92 ? 278 HIS A CE1    1 
ATOM   2042 N NE2    . HIS A 1 260 ? 19.805 11.633  41.488  1.00 23.50 ? 278 HIS A NE2    1 
ATOM   2043 N N      . LYS A 1 261 ? 20.579 5.116   43.883  1.00 23.61 ? 279 LYS A N      1 
ATOM   2044 C CA     . LYS A 1 261 ? 20.202 3.697   44.017  1.00 21.38 ? 279 LYS A CA     1 
ATOM   2045 C C      . LYS A 1 261 ? 18.822 3.524   44.532  1.00 25.90 ? 279 LYS A C      1 
ATOM   2046 O O      . LYS A 1 261 ? 18.120 2.606   44.139  1.00 31.74 ? 279 LYS A O      1 
ATOM   2047 C CB     . LYS A 1 261 ? 21.164 2.999   44.967  1.00 21.56 ? 279 LYS A CB     1 
ATOM   2048 C CG     . LYS A 1 261 ? 21.880 1.800   44.386  1.00 24.97 ? 279 LYS A CG     1 
ATOM   2049 C CD     . LYS A 1 261 ? 23.339 1.806   44.796  1.00 32.31 ? 279 LYS A CD     1 
ATOM   2050 C CE     . LYS A 1 261 ? 23.481 2.043   46.286  1.00 36.21 ? 279 LYS A CE     1 
ATOM   2051 N NZ     . LYS A 1 261 ? 24.888 2.323   46.682  1.00 39.19 ? 279 LYS A NZ     1 
ATOM   2052 N N      . THR A 1 262 ? 18.438 4.376   45.449  1.00 27.23 ? 280 THR A N      1 
ATOM   2053 C CA     . THR A 1 262 ? 17.112 4.362   46.003  1.00 25.20 ? 280 THR A CA     1 
ATOM   2054 C C      . THR A 1 262 ? 16.058 4.672   44.946  1.00 30.32 ? 280 THR A C      1 
ATOM   2055 O O      . THR A 1 262 ? 14.950 4.169   45.031  1.00 40.27 ? 280 THR A O      1 
ATOM   2056 C CB     . THR A 1 262 ? 17.084 5.313   47.208  1.00 24.50 ? 280 THR A CB     1 
ATOM   2057 O OG1    . THR A 1 262 ? 18.019 4.852   48.184  1.00 26.33 ? 280 THR A OG1    1 
ATOM   2058 C CG2    . THR A 1 262 ? 15.722 5.367   47.841  1.00 22.92 ? 280 THR A CG2    1 
ATOM   2059 N N      . ASP A 1 263 ? 16.405 5.439   43.923  1.00 28.25 ? 281 ASP A N      1 
ATOM   2060 C CA     . ASP A 1 263 ? 15.464 5.806   42.882  1.00 27.80 ? 281 ASP A CA     1 
ATOM   2061 C C      . ASP A 1 263 ? 14.853 4.617   42.206  1.00 29.79 ? 281 ASP A C      1 
ATOM   2062 O O      . ASP A 1 263 ? 15.527 3.658   41.895  1.00 36.45 ? 281 ASP A O      1 
ATOM   2063 C CB     . ASP A 1 263 ? 16.129 6.730   41.852  1.00 22.66 ? 281 ASP A CB     1 
ATOM   2064 C CG     . ASP A 1 263 ? 15.428 8.034   41.701  1.00 27.97 ? 281 ASP A CG     1 
ATOM   2065 O OD1    . ASP A 1 263 ? 14.189 8.055   41.808  1.00 40.21 ? 281 ASP A OD1    1 
ATOM   2066 O OD2    . ASP A 1 263 ? 16.116 9.041   41.461  1.00 22.94 ? 281 ASP A OD2    1 
ATOM   2067 N N      . LYS A 1 264 ? 13.564 4.682   41.949  1.00 30.38 ? 282 LYS A N      1 
ATOM   2068 C CA     . LYS A 1 264 ? 12.845 3.552   41.393  1.00 32.43 ? 282 LYS A CA     1 
ATOM   2069 C C      . LYS A 1 264 ? 12.831 3.508   39.900  1.00 30.32 ? 282 LYS A C      1 
ATOM   2070 O O      . LYS A 1 264 ? 12.603 2.464   39.324  1.00 28.45 ? 282 LYS A O      1 
ATOM   2071 C CB     . LYS A 1 264 ? 11.416 3.669   41.862  1.00 34.93 ? 282 LYS A CB     1 
ATOM   2072 C CG     . LYS A 1 264 ? 11.250 3.904   43.351  1.00 34.52 ? 282 LYS A CG     1 
ATOM   2073 C CD     . LYS A 1 264 ? 11.313 2.604   44.130  1.00 49.01 ? 282 LYS A CD     1 
ATOM   2074 C CE     . LYS A 1 264 ? 10.952 2.824   45.589  1.00 46.86 ? 282 LYS A CE     1 
ATOM   2075 N NZ     . LYS A 1 264 ? 9.595  3.413   45.756  1.00 41.62 ? 282 LYS A NZ     1 
ATOM   2076 N N      . ASP A 1 265 ? 13.073 4.641   39.273  1.00 31.79 ? 283 ASP A N      1 
ATOM   2077 C CA     . ASP A 1 265 ? 13.091 4.744   37.817  1.00 27.97 ? 283 ASP A CA     1 
ATOM   2078 C C      . ASP A 1 265 ? 14.486 4.762   37.211  1.00 21.50 ? 283 ASP A C      1 
ATOM   2079 O O      . ASP A 1 265 ? 14.644 5.171   36.090  1.00 16.22 ? 283 ASP A O      1 
ATOM   2080 C CB     . ASP A 1 265 ? 12.216 5.930   37.373  1.00 24.52 ? 283 ASP A CB     1 
ATOM   2081 C CG     . ASP A 1 265 ? 12.622 7.261   38.000  1.00 34.79 ? 283 ASP A CG     1 
ATOM   2082 O OD1    . ASP A 1 265 ? 12.977 7.321   39.188  1.00 35.99 ? 283 ASP A OD1    1 
ATOM   2083 O OD2    . ASP A 1 265 ? 12.543 8.281   37.292  1.00 38.26 ? 283 ASP A OD2    1 
ATOM   2084 N N      . ILE A 1 266 ? 15.477 4.283   37.941  1.00 21.69 ? 284 ILE A N      1 
ATOM   2085 C CA     . ILE A 1 266 ? 16.878 4.278   37.506  1.00 20.10 ? 284 ILE A CA     1 
ATOM   2086 C C      . ILE A 1 266 ? 17.190 3.502   36.225  1.00 19.47 ? 284 ILE A C      1 
ATOM   2087 O O      . ILE A 1 266 ? 18.042 3.896   35.468  1.00 15.28 ? 284 ILE A O      1 
ATOM   2088 C CB     . ILE A 1 266 ? 17.793 3.830   38.687  1.00 18.39 ? 284 ILE A CB     1 
ATOM   2089 C CG1    . ILE A 1 266 ? 19.252 4.194   38.423  1.00 13.70 ? 284 ILE A CG1    1 
ATOM   2090 C CG2    . ILE A 1 266 ? 17.614 2.358   39.005  1.00 13.17 ? 284 ILE A CG2    1 
ATOM   2091 C CD1    . ILE A 1 266 ? 20.181 3.765   39.530  1.00 19.40 ? 284 ILE A CD1    1 
ATOM   2092 N N      . GLU A 1 267 ? 16.530 2.387   36.001  1.00 16.38 ? 285 GLU A N      1 
ATOM   2093 C CA     . GLU A 1 267 ? 16.722 1.651   34.788  1.00 16.82 ? 285 GLU A CA     1 
ATOM   2094 C C      . GLU A 1 267 ? 16.308 2.475   33.611  1.00 21.51 ? 285 GLU A C      1 
ATOM   2095 O O      . GLU A 1 267 ? 17.002 2.506   32.614  1.00 18.12 ? 285 GLU A O      1 
ATOM   2096 C CB     . GLU A 1 267 ? 15.861 0.415   34.839  1.00 17.92 ? 285 GLU A CB     1 
ATOM   2097 C CG     . GLU A 1 267 ? 16.483 -0.839  34.281  1.00 21.74 ? 285 GLU A CG     1 
ATOM   2098 C CD     . GLU A 1 267 ? 15.484 -1.962  34.254  1.00 24.27 ? 285 GLU A CD     1 
ATOM   2099 O OE1    . GLU A 1 267 ? 14.321 -1.689  33.916  1.00 31.90 ? 285 GLU A OE1    1 
ATOM   2100 O OE2    . GLU A 1 267 ? 15.847 -3.102  34.574  1.00 22.07 ? 285 GLU A OE2    1 
ATOM   2101 N N      . LYS A 1 268 ? 15.191 3.165   33.725  1.00 17.04 ? 286 LYS A N      1 
ATOM   2102 C CA     . LYS A 1 268 ? 14.726 4.012   32.672  1.00 13.99 ? 286 LYS A CA     1 
ATOM   2103 C C      . LYS A 1 268 ? 15.680 5.127   32.398  1.00 15.58 ? 286 LYS A C      1 
ATOM   2104 O O      . LYS A 1 268 ? 15.966 5.431   31.257  1.00 19.99 ? 286 LYS A O      1 
ATOM   2105 C CB     . LYS A 1 268 ? 13.358 4.556   33.076  1.00 14.57 ? 286 LYS A CB     1 
ATOM   2106 C CG     . LYS A 1 268 ? 12.603 5.373   32.049  1.00 11.74 ? 286 LYS A CG     1 
ATOM   2107 C CD     . LYS A 1 268 ? 11.248 5.749   32.619  1.00 15.13 ? 286 LYS A CD     1 
ATOM   2108 C CE     . LYS A 1 268 ? 10.279 6.203   31.543  1.00 23.98 ? 286 LYS A CE     1 
ATOM   2109 N NZ     . LYS A 1 268 ? 10.077 7.675   31.523  1.00 21.76 ? 286 LYS A NZ     1 
ATOM   2110 N N      . LYS A 1 269 ? 16.173 5.743   33.436  1.00 14.42 ? 287 LYS A N      1 
ATOM   2111 C CA     . LYS A 1 269 ? 17.124 6.814   33.302  1.00 17.34 ? 287 LYS A CA     1 
ATOM   2112 C C      . LYS A 1 269 ? 18.511 6.473   32.764  1.00 13.83 ? 287 LYS A C      1 
ATOM   2113 O O      . LYS A 1 269 ? 19.016 7.161   31.918  1.00 14.27 ? 287 LYS A O      1 
ATOM   2114 C CB     . LYS A 1 269 ? 17.188 7.525   34.656  1.00 20.83 ? 287 LYS A CB     1 
ATOM   2115 C CG     . LYS A 1 269 ? 15.874 8.135   35.100  1.00 18.69 ? 287 LYS A CG     1 
ATOM   2116 C CD     . LYS A 1 269 ? 15.838 8.317   36.604  1.00 23.89 ? 287 LYS A CD     1 
ATOM   2117 C CE     . LYS A 1 269 ? 16.161 9.738   37.006  1.00 26.49 ? 287 LYS A CE     1 
ATOM   2118 N NZ     . LYS A 1 269 ? 16.269 9.861   38.481  1.00 18.11 ? 287 LYS A NZ     1 
ATOM   2119 N N      . VAL A 1 270 ? 19.111 5.409   33.235  1.00 13.56 ? 288 VAL A N      1 
ATOM   2120 C CA     . VAL A 1 270 ? 20.402 4.949   32.743  1.00 12.42 ? 288 VAL A CA     1 
ATOM   2121 C C      . VAL A 1 270 ? 20.308 4.515   31.297  1.00 13.68 ? 288 VAL A C      1 
ATOM   2122 O O      . VAL A 1 270 ? 21.227 4.726   30.536  1.00 12.31 ? 288 VAL A O      1 
ATOM   2123 C CB     . VAL A 1 270 ? 20.999 3.882   33.668  1.00 13.28 ? 288 VAL A CB     1 
ATOM   2124 C CG1    . VAL A 1 270 ? 22.267 3.294   33.082  1.00 13.36 ? 288 VAL A CG1    1 
ATOM   2125 C CG2    . VAL A 1 270 ? 21.267 4.466   35.040  1.00 13.66 ? 288 VAL A CG2    1 
ATOM   2126 N N      . ASN A 1 271 ? 19.210 3.901   30.916  1.00 14.20 ? 289 ASN A N      1 
ATOM   2127 C CA     . ASN A 1 271 ? 18.987 3.559   29.523  1.00 14.02 ? 289 ASN A CA     1 
ATOM   2128 C C      . ASN A 1 271 ? 18.870 4.768   28.630  1.00 17.82 ? 289 ASN A C      1 
ATOM   2129 O O      . ASN A 1 271 ? 19.336 4.751   27.530  1.00 19.98 ? 289 ASN A O      1 
ATOM   2130 C CB     . ASN A 1 271 ? 17.784 2.636   29.367  1.00 15.46 ? 289 ASN A CB     1 
ATOM   2131 C CG     . ASN A 1 271 ? 18.152 1.177   29.414  1.00 14.86 ? 289 ASN A CG     1 
ATOM   2132 O OD1    . ASN A 1 271 ? 18.932 0.710   28.611  1.00 11.22 ? 289 ASN A OD1    1 
ATOM   2133 N ND2    . ASN A 1 271 ? 17.570 0.451   30.345  1.00 17.23 ? 289 ASN A ND2    1 
ATOM   2134 N N      . GLN A 1 272 ? 18.242 5.823   29.091  1.00 15.43 ? 290 GLN A N      1 
ATOM   2135 C CA     . GLN A 1 272 ? 18.169 7.032   28.330  1.00 14.53 ? 290 GLN A CA     1 
ATOM   2136 C C      . GLN A 1 272 ? 19.545 7.588   28.056  1.00 15.41 ? 290 GLN A C      1 
ATOM   2137 O O      . GLN A 1 272 ? 19.798 8.041   26.960  1.00 14.02 ? 290 GLN A O      1 
ATOM   2138 C CB     . GLN A 1 272 ? 17.377 8.032   29.149  1.00 15.26 ? 290 GLN A CB     1 
ATOM   2139 C CG     . GLN A 1 272 ? 16.049 8.445   28.563  1.00 23.41 ? 290 GLN A CG     1 
ATOM   2140 C CD     . GLN A 1 272 ? 15.009 8.713   29.621  1.00 21.21 ? 290 GLN A CD     1 
ATOM   2141 O OE1    . GLN A 1 272 ? 15.236 9.458   30.560  1.00 31.94 ? 290 GLN A OE1    1 
ATOM   2142 N NE2    . GLN A 1 272 ? 13.854 8.097   29.467  1.00 26.83 ? 290 GLN A NE2    1 
ATOM   2143 N N      . ILE A 1 273 ? 20.429 7.596   29.035  1.00 14.69 ? 291 ILE A N      1 
ATOM   2144 C CA     . ILE A 1 273 ? 21.811 7.998   28.809  1.00 15.16 ? 291 ILE A CA     1 
ATOM   2145 C C      . ILE A 1 273 ? 22.607 7.073   27.891  1.00 17.37 ? 291 ILE A C      1 
ATOM   2146 O O      . ILE A 1 273 ? 23.342 7.532   27.050  1.00 16.31 ? 291 ILE A O      1 
ATOM   2147 C CB     . ILE A 1 273 ? 22.577 8.113   30.144  1.00 17.92 ? 291 ILE A CB     1 
ATOM   2148 C CG1    . ILE A 1 273 ? 21.713 8.697   31.251  1.00 17.07 ? 291 ILE A CG1    1 
ATOM   2149 C CG2    . ILE A 1 273 ? 23.861 8.906   29.966  1.00 13.97 ? 291 ILE A CG2    1 
ATOM   2150 C CD1    . ILE A 1 273 ? 22.325 8.528   32.625  1.00 13.50 ? 291 ILE A CD1    1 
ATOM   2151 N N      . ILE A 1 274 ? 22.471 5.773   28.065  1.00 13.45 ? 292 ILE A N      1 
ATOM   2152 C CA     . ILE A 1 274 ? 23.168 4.818   27.251  1.00 12.40 ? 292 ILE A CA     1 
ATOM   2153 C C      . ILE A 1 274 ? 22.683 4.898   25.860  1.00 14.44 ? 292 ILE A C      1 
ATOM   2154 O O      . ILE A 1 274 ? 23.443 4.778   24.930  1.00 17.71 ? 292 ILE A O      1 
ATOM   2155 C CB     . ILE A 1 274 ? 23.025 3.386   27.797  1.00 15.88 ? 292 ILE A CB     1 
ATOM   2156 C CG1    . ILE A 1 274 ? 23.531 3.292   29.229  1.00 12.98 ? 292 ILE A CG1    1 
ATOM   2157 C CG2    . ILE A 1 274 ? 23.799 2.404   26.933  1.00 7.23  ? 292 ILE A CG2    1 
ATOM   2158 C CD1    . ILE A 1 274 ? 25.029 3.353   29.350  1.00 13.47 ? 292 ILE A CD1    1 
ATOM   2159 N N      . ASN A 1 275 ? 21.398 5.059   25.708  1.00 12.66 ? 293 ASN A N      1 
ATOM   2160 C CA     . ASN A 1 275 ? 20.813 5.190   24.403  1.00 12.65 ? 293 ASN A CA     1 
ATOM   2161 C C      . ASN A 1 275 ? 21.181 6.455   23.643  1.00 14.71 ? 293 ASN A C      1 
ATOM   2162 O O      . ASN A 1 275 ? 21.433 6.380   22.466  1.00 14.86 ? 293 ASN A O      1 
ATOM   2163 C CB     . ASN A 1 275 ? 19.319 4.963   24.518  1.00 10.55 ? 293 ASN A CB     1 
ATOM   2164 C CG     . ASN A 1 275 ? 18.972 3.532   24.788  1.00 12.84 ? 293 ASN A CG     1 
ATOM   2165 O OD1    . ASN A 1 275 ? 19.792 2.655   24.617  1.00 13.45 ? 293 ASN A OD1    1 
ATOM   2166 N ND2    . ASN A 1 275 ? 17.752 3.292   25.212  1.00 15.08 ? 293 ASN A ND2    1 
ATOM   2167 N N      . LEU A 1 276 ? 21.213 7.606   24.290  1.00 14.76 ? 294 LEU A N      1 
ATOM   2168 C CA     . LEU A 1 276 ? 21.658 8.866   23.663  1.00 18.84 ? 294 LEU A CA     1 
ATOM   2169 C C      . LEU A 1 276 ? 23.111 8.836   23.336  1.00 14.46 ? 294 LEU A C      1 
ATOM   2170 O O      . LEU A 1 276 ? 23.518 9.424   22.369  1.00 12.34 ? 294 LEU A O      1 
ATOM   2171 C CB     . LEU A 1 276 ? 21.268 10.116  24.471  1.00 18.27 ? 294 LEU A CB     1 
ATOM   2172 C CG     . LEU A 1 276 ? 21.555 11.472  23.839  1.00 15.92 ? 294 LEU A CG     1 
ATOM   2173 C CD1    . LEU A 1 276 ? 20.465 11.841  22.855  1.00 16.98 ? 294 LEU A CD1    1 
ATOM   2174 C CD2    . LEU A 1 276 ? 21.709 12.540  24.899  1.00 18.65 ? 294 LEU A CD2    1 
ATOM   2175 N N      . TRP A 1 277 ? 23.906 8.198   24.171  1.00 14.98 ? 295 TRP A N      1 
ATOM   2176 C CA     . TRP A 1 277 ? 25.303 8.008   23.901  1.00 10.58 ? 295 TRP A CA     1 
ATOM   2177 C C      . TRP A 1 277 ? 25.518 7.171   22.676  1.00 13.23 ? 295 TRP A C      1 
ATOM   2178 O O      . TRP A 1 277 ? 26.350 7.493   21.863  1.00 13.59 ? 295 TRP A O      1 
ATOM   2179 C CB     . TRP A 1 277 ? 25.912 7.308   25.111  1.00 8.56  ? 295 TRP A CB     1 
ATOM   2180 C CG     . TRP A 1 277 ? 27.352 6.927   24.985  1.00 11.75 ? 295 TRP A CG     1 
ATOM   2181 C CD1    . TRP A 1 277 ? 27.853 5.801   24.414  1.00 10.57 ? 295 TRP A CD1    1 
ATOM   2182 C CD2    . TRP A 1 277 ? 28.475 7.660   25.467  1.00 12.92 ? 295 TRP A CD2    1 
ATOM   2183 N NE1    . TRP A 1 277 ? 29.212 5.792   24.496  1.00 11.72 ? 295 TRP A NE1    1 
ATOM   2184 C CE2    . TRP A 1 277 ? 29.621 6.923   25.145  1.00 11.78 ? 295 TRP A CE2    1 
ATOM   2185 C CE3    . TRP A 1 277 ? 28.622 8.870   26.143  1.00 14.04 ? 295 TRP A CE3    1 
ATOM   2186 C CZ2    . TRP A 1 277 ? 30.894 7.356   25.468  1.00 13.26 ? 295 TRP A CZ2    1 
ATOM   2187 C CZ3    . TRP A 1 277 ? 29.884 9.292   26.463  1.00 12.10 ? 295 TRP A CZ3    1 
ATOM   2188 C CH2    . TRP A 1 277 ? 31.002 8.543   26.126  1.00 12.36 ? 295 TRP A CH2    1 
ATOM   2189 N N      . ILE A 1 278 ? 24.773 6.096   22.543  1.00 12.05 ? 296 ILE A N      1 
ATOM   2190 C CA     . ILE A 1 278 ? 24.880 5.217   21.397  1.00 12.47 ? 296 ILE A CA     1 
ATOM   2191 C C      . ILE A 1 278 ? 24.452 5.876   20.092  1.00 12.13 ? 296 ILE A C      1 
ATOM   2192 O O      . ILE A 1 278 ? 25.099 5.712   19.078  1.00 9.45  ? 296 ILE A O      1 
ATOM   2193 C CB     . ILE A 1 278 ? 24.146 3.868   21.649  1.00 10.47 ? 296 ILE A CB     1 
ATOM   2194 C CG1    . ILE A 1 278 ? 24.891 3.014   22.655  1.00 10.24 ? 296 ILE A CG1    1 
ATOM   2195 C CG2    . ILE A 1 278 ? 23.958 3.088   20.361  1.00 9.83  ? 296 ILE A CG2    1 
ATOM   2196 C CD1    . ILE A 1 278 ? 24.118 1.778   23.051  1.00 15.74 ? 296 ILE A CD1    1 
ATOM   2197 N N      . SER A 1 279 ? 23.372 6.629   20.125  1.00 10.39 ? 297 SER A N      1 
ATOM   2198 C CA     . SER A 1 279 ? 22.918 7.344   18.950  1.00 12.30 ? 297 SER A CA     1 
ATOM   2199 C C      . SER A 1 279 ? 23.884 8.380   18.540  1.00 9.45  ? 297 SER A C      1 
ATOM   2200 O O      . SER A 1 279 ? 24.167 8.539   17.379  1.00 8.66  ? 297 SER A O      1 
ATOM   2201 C CB     . SER A 1 279 ? 21.552 7.990   19.226  1.00 11.65 ? 297 SER A CB     1 
ATOM   2202 O OG     . SER A 1 279 ? 21.597 9.035   20.163  1.00 20.95 ? 297 SER A OG     1 
ATOM   2203 N N      . SER A 1 280 ? 24.393 9.090   19.505  1.00 14.17 ? 298 SER A N      1 
ATOM   2204 C CA     . SER A 1 280 ? 25.271 10.167  19.254  1.00 23.01 ? 298 SER A CA     1 
ATOM   2205 C C      . SER A 1 280 ? 26.576 9.761   18.702  1.00 19.06 ? 298 SER A C      1 
ATOM   2206 O O      . SER A 1 280 ? 27.153 10.451  17.884  1.00 23.73 ? 298 SER A O      1 
ATOM   2207 C CB     . SER A 1 280 ? 25.384 11.027  20.506  1.00 11.43 ? 298 SER A CB     1 
ATOM   2208 O OG     . SER A 1 280 ? 24.176 11.692  20.788  1.00 26.38 ? 298 SER A OG     1 
ATOM   2209 N N      . TYR A 1 281 ? 27.085 8.657   19.172  1.00 17.11 ? 299 TYR A N      1 
ATOM   2210 C CA     . TYR A 1 281 ? 28.314 8.157   18.632  1.00 10.79 ? 299 TYR A CA     1 
ATOM   2211 C C      . TYR A 1 281 ? 28.243 7.756   17.174  1.00 12.53 ? 299 TYR A C      1 
ATOM   2212 O O      . TYR A 1 281 ? 29.166 8.029   16.446  1.00 13.19 ? 299 TYR A O      1 
ATOM   2213 C CB     . TYR A 1 281 ? 28.890 7.094   19.548  1.00 11.37 ? 299 TYR A CB     1 
ATOM   2214 C CG     . TYR A 1 281 ? 29.894 7.631   20.521  1.00 12.56 ? 299 TYR A CG     1 
ATOM   2215 C CD1    . TYR A 1 281 ? 29.568 8.656   21.389  1.00 10.90 ? 299 TYR A CD1    1 
ATOM   2216 C CD2    . TYR A 1 281 ? 31.171 7.118   20.567  1.00 16.80 ? 299 TYR A CD2    1 
ATOM   2217 C CE1    . TYR A 1 281 ? 30.491 9.156   22.273  1.00 11.76 ? 299 TYR A CE1    1 
ATOM   2218 C CE2    . TYR A 1 281 ? 32.101 7.613   21.451  1.00 17.94 ? 299 TYR A CE2    1 
ATOM   2219 C CZ     . TYR A 1 281 ? 31.753 8.629   22.299  1.00 8.86  ? 299 TYR A CZ     1 
ATOM   2220 O OH     . TYR A 1 281 ? 32.680 9.115   23.170  1.00 12.20 ? 299 TYR A OH     1 
ATOM   2221 N N      . ILE A 1 282 ? 27.176 7.104   16.737  1.00 9.97  ? 300 ILE A N      1 
ATOM   2222 C CA     . ILE A 1 282 ? 26.996 6.794   15.327  1.00 10.04 ? 300 ILE A CA     1 
ATOM   2223 C C      . ILE A 1 282 ? 26.778 7.995   14.454  1.00 8.88  ? 300 ILE A C      1 
ATOM   2224 O O      . ILE A 1 282 ? 27.391 8.119   13.426  1.00 9.89  ? 300 ILE A O      1 
ATOM   2225 C CB     . ILE A 1 282 ? 25.842 5.791   15.113  1.00 12.76 ? 300 ILE A CB     1 
ATOM   2226 C CG1    . ILE A 1 282 ? 26.041 4.544   15.965  1.00 9.98  ? 300 ILE A CG1    1 
ATOM   2227 C CG2    . ILE A 1 282 ? 25.708 5.428   13.642  1.00 8.45  ? 300 ILE A CG2    1 
ATOM   2228 C CD1    . ILE A 1 282 ? 24.901 3.562   15.859  1.00 10.55 ? 300 ILE A CD1    1 
ATOM   2229 N N      . LYS A 1 283 ? 25.940 8.907   14.889  1.00 13.04 ? 301 LYS A N      1 
ATOM   2230 C CA     . LYS A 1 283 ? 25.641 10.111  14.149  1.00 14.01 ? 301 LYS A CA     1 
ATOM   2231 C C      . LYS A 1 283 ? 26.807 11.014  14.006  1.00 14.05 ? 301 LYS A C      1 
ATOM   2232 O O      . LYS A 1 283 ? 26.945 11.722  13.023  1.00 12.68 ? 301 LYS A O      1 
ATOM   2233 C CB     . LYS A 1 283 ? 24.497 10.856  14.804  1.00 11.19 ? 301 LYS A CB     1 
ATOM   2234 C CG     . LYS A 1 283 ? 23.155 10.617  14.155  1.00 20.86 ? 301 LYS A CG     1 
ATOM   2235 C CD     . LYS A 1 283 ? 22.101 11.529  14.754  1.00 21.27 ? 301 LYS A CD     1 
ATOM   2236 C CE     . LYS A 1 283 ? 22.482 12.986  14.586  1.00 29.36 ? 301 LYS A CE     1 
ATOM   2237 N NZ     . LYS A 1 283 ? 21.329 13.877  14.871  1.00 41.27 ? 301 LYS A NZ     1 
ATOM   2238 N N      . GLU A 1 284 ? 27.613 11.054  15.026  1.00 11.89 ? 302 GLU A N      1 
ATOM   2239 C CA     . GLU A 1 284 ? 28.739 11.912  15.017  1.00 13.18 ? 302 GLU A CA     1 
ATOM   2240 C C      . GLU A 1 284 ? 29.895 11.282  14.291  1.00 14.87 ? 302 GLU A C      1 
ATOM   2241 O O      . GLU A 1 284 ? 30.911 11.916  14.082  1.00 14.12 ? 302 GLU A O      1 
ATOM   2242 C CB     . GLU A 1 284 ? 29.026 12.293  16.453  1.00 16.43 ? 302 GLU A CB     1 
ATOM   2243 C CG     . GLU A 1 284 ? 29.164 13.783  16.701  1.00 18.96 ? 302 GLU A CG     1 
ATOM   2244 C CD     . GLU A 1 284 ? 27.897 14.556  16.425  1.00 31.38 ? 302 GLU A CD     1 
ATOM   2245 O OE1    . GLU A 1 284 ? 26.803 13.969  16.481  1.00 24.55 ? 302 GLU A OE1    1 
ATOM   2246 O OE2    . GLU A 1 284 ? 27.997 15.768  16.167  1.00 35.24 ? 302 GLU A OE2    1 
ATOM   2247 N N      . GLY A 1 285 ? 29.745 10.031  13.912  1.00 14.97 ? 303 GLY A N      1 
ATOM   2248 C CA     . GLY A 1 285 ? 30.765 9.316   13.180  1.00 17.08 ? 303 GLY A CA     1 
ATOM   2249 C C      . GLY A 1 285 ? 31.848 8.740   14.018  1.00 17.61 ? 303 GLY A C      1 
ATOM   2250 O O      . GLY A 1 285 ? 32.720 8.132   13.517  1.00 22.35 ? 303 GLY A O      1 
ATOM   2251 N N      . TYR A 1 286 ? 31.771 8.908   15.309  1.00 14.91 ? 304 TYR A N      1 
ATOM   2252 C CA     . TYR A 1 286 ? 32.819 8.464   16.179  1.00 17.10 ? 304 TYR A CA     1 
ATOM   2253 C C      . TYR A 1 286 ? 33.024 6.975   16.204  1.00 12.45 ? 304 TYR A C      1 
ATOM   2254 O O      . TYR A 1 286 ? 34.132 6.501   16.085  1.00 12.88 ? 304 TYR A O      1 
ATOM   2255 C CB     . TYR A 1 286 ? 32.481 8.928   17.590  1.00 14.28 ? 304 TYR A CB     1 
ATOM   2256 C CG     . TYR A 1 286 ? 32.342 10.395  17.839  1.00 18.01 ? 304 TYR A CG     1 
ATOM   2257 C CD1    . TYR A 1 286 ? 33.069 11.323  17.123  1.00 20.04 ? 304 TYR A CD1    1 
ATOM   2258 C CD2    . TYR A 1 286 ? 31.510 10.850  18.839  1.00 15.43 ? 304 TYR A CD2    1 
ATOM   2259 C CE1    . TYR A 1 286 ? 32.945 12.672  17.379  1.00 21.61 ? 304 TYR A CE1    1 
ATOM   2260 C CE2    . TYR A 1 286 ? 31.385 12.190  19.107  1.00 19.25 ? 304 TYR A CE2    1 
ATOM   2261 C CZ     . TYR A 1 286 ? 32.104 13.096  18.374  1.00 23.08 ? 304 TYR A CZ     1 
ATOM   2262 O OH     . TYR A 1 286 ? 31.969 14.428  18.643  1.00 22.38 ? 304 TYR A OH     1 
ATOM   2263 N N      . HIS A 1 287 ? 31.947 6.239   16.349  1.00 9.47  ? 305 HIS A N      1 
ATOM   2264 C CA     . HIS A 1 287 ? 32.016 4.818   16.359  1.00 11.12 ? 305 HIS A CA     1 
ATOM   2265 C C      . HIS A 1 287 ? 30.846 4.104   15.737  1.00 9.60  ? 305 HIS A C      1 
ATOM   2266 O O      . HIS A 1 287 ? 29.844 4.716   15.453  1.00 10.00 ? 305 HIS A O      1 
ATOM   2267 C CB     . HIS A 1 287 ? 32.159 4.325   17.800  1.00 11.17 ? 305 HIS A CB     1 
ATOM   2268 C CG     . HIS A 1 287 ? 33.509 4.543   18.387  1.00 15.48 ? 305 HIS A CG     1 
ATOM   2269 N ND1    . HIS A 1 287 ? 34.553 3.674   18.184  1.00 15.74 ? 305 HIS A ND1    1 
ATOM   2270 C CD2    . HIS A 1 287 ? 33.991 5.535   19.166  1.00 18.04 ? 305 HIS A CD2    1 
ATOM   2271 C CE1    . HIS A 1 287 ? 35.622 4.122   18.809  1.00 13.64 ? 305 HIS A CE1    1 
ATOM   2272 N NE2    . HIS A 1 287 ? 35.308 5.251   19.410  1.00 16.17 ? 305 HIS A NE2    1 
ATOM   2273 N N      . SER A 1 288 ? 30.989 2.811   15.491  1.00 8.42  ? 306 SER A N      1 
ATOM   2274 C CA     . SER A 1 288 ? 29.880 1.975   15.066  1.00 12.52 ? 306 SER A CA     1 
ATOM   2275 C C      . SER A 1 288 ? 29.194 1.428   16.309  1.00 10.06 ? 306 SER A C      1 
ATOM   2276 O O      . SER A 1 288 ? 29.744 1.517   17.371  1.00 7.77  ? 306 SER A O      1 
ATOM   2277 C CB     . SER A 1 288 ? 30.323 0.833   14.134  1.00 12.18 ? 306 SER A CB     1 
ATOM   2278 O OG     . SER A 1 288 ? 31.056 -0.152  14.803  1.00 10.03 ? 306 SER A OG     1 
ATOM   2279 N N      . TYR A 1 289 ? 28.014 0.842   16.178  1.00 13.82 ? 307 TYR A N      1 
ATOM   2280 C CA     . TYR A 1 289 ? 27.233 0.338   17.314  1.00 12.38 ? 307 TYR A CA     1 
ATOM   2281 C C      . TYR A 1 289 ? 27.894 -0.722  18.140  1.00 10.61 ? 307 TYR A C      1 
ATOM   2282 O O      . TYR A 1 289 ? 27.870 -0.644  19.338  1.00 10.79 ? 307 TYR A O      1 
ATOM   2283 C CB     . TYR A 1 289 ? 25.868 -0.145  16.803  1.00 9.53  ? 307 TYR A CB     1 
ATOM   2284 C CG     . TYR A 1 289 ? 24.978 -0.840  17.785  1.00 11.97 ? 307 TYR A CG     1 
ATOM   2285 C CD1    . TYR A 1 289 ? 24.057 -0.133  18.539  1.00 10.79 ? 307 TYR A CD1    1 
ATOM   2286 C CD2    . TYR A 1 289 ? 25.027 -2.214  17.931  1.00 14.72 ? 307 TYR A CD2    1 
ATOM   2287 C CE1    . TYR A 1 289 ? 23.232 -0.777  19.434  1.00 10.15 ? 307 TYR A CE1    1 
ATOM   2288 C CE2    . TYR A 1 289 ? 24.209 -2.861  18.822  1.00 12.06 ? 307 TYR A CE2    1 
ATOM   2289 C CZ     . TYR A 1 289 ? 23.314 -2.140  19.566  1.00 10.40 ? 307 TYR A CZ     1 
ATOM   2290 O OH     . TYR A 1 289 ? 22.508 -2.805  20.445  1.00 13.83 ? 307 TYR A OH     1 
ATOM   2291 N N      . SER A 1 290 ? 28.534 -1.680  17.505  1.00 12.30 ? 308 SER A N      1 
ATOM   2292 C CA     . SER A 1 290 ? 29.164 -2.759  18.207  1.00 12.23 ? 308 SER A CA     1 
ATOM   2293 C C      . SER A 1 290 ? 30.496 -2.348  18.716  1.00 11.86 ? 308 SER A C      1 
ATOM   2294 O O      . SER A 1 290 ? 31.081 -3.009  19.529  1.00 13.93 ? 308 SER A O      1 
ATOM   2295 C CB     . SER A 1 290 ? 29.154 -4.028  17.378  1.00 15.12 ? 308 SER A CB     1 
ATOM   2296 O OG     . SER A 1 290 ? 27.914 -4.675  17.469  1.00 18.14 ? 308 SER A OG     1 
ATOM   2297 N N      . GLU A 1 291 ? 30.953 -1.204  18.284  1.00 11.72 ? 309 GLU A N      1 
ATOM   2298 C CA     . GLU A 1 291 ? 32.183 -0.686  18.788  1.00 10.66 ? 309 GLU A CA     1 
ATOM   2299 C C      . GLU A 1 291 ? 31.944 -0.083  20.146  1.00 13.33 ? 309 GLU A C      1 
ATOM   2300 O O      . GLU A 1 291 ? 32.870 0.048   20.925  1.00 10.46 ? 309 GLU A O      1 
ATOM   2301 C CB     . GLU A 1 291 ? 32.803 0.267   17.803  1.00 9.85  ? 309 GLU A CB     1 
ATOM   2302 C CG     . GLU A 1 291 ? 33.495 -0.417  16.642  1.00 10.66 ? 309 GLU A CG     1 
ATOM   2303 C CD     . GLU A 1 291 ? 34.054 0.552   15.620  1.00 14.52 ? 309 GLU A CD     1 
ATOM   2304 O OE1    . GLU A 1 291 ? 33.863 1.768   15.769  1.00 15.46 ? 309 GLU A OE1    1 
ATOM   2305 O OE2    . GLU A 1 291 ? 34.699 0.087   14.668  1.00 10.22 ? 309 GLU A OE2    1 
ATOM   2306 N N      . VAL A 1 292 ? 30.704 0.280   20.435  1.00 11.69 ? 310 VAL A N      1 
ATOM   2307 C CA     . VAL A 1 292 ? 30.348 0.748   21.767  1.00 14.23 ? 310 VAL A CA     1 
ATOM   2308 C C      . VAL A 1 292 ? 29.666 -0.343  22.573  1.00 13.67 ? 310 VAL A C      1 
ATOM   2309 O O      . VAL A 1 292 ? 30.029 -0.591  23.723  1.00 9.84  ? 310 VAL A O      1 
ATOM   2310 C CB     . VAL A 1 292 ? 29.465 2.010   21.691  1.00 11.60 ? 310 VAL A CB     1 
ATOM   2311 C CG1    . VAL A 1 292 ? 28.549 2.065   22.878  1.00 10.36 ? 310 VAL A CG1    1 
ATOM   2312 C CG2    . VAL A 1 292 ? 30.348 3.241   21.666  1.00 18.21 ? 310 VAL A CG2    1 
ATOM   2313 N N      . VAL A 1 293 ? 28.736 -1.087  22.023  1.00 13.01 ? 311 VAL A N      1 
ATOM   2314 C CA     . VAL A 1 293 ? 27.997 -2.088  22.775  1.00 12.72 ? 311 VAL A CA     1 
ATOM   2315 C C      . VAL A 1 293 ? 28.883 -3.244  23.185  1.00 12.92 ? 311 VAL A C      1 
ATOM   2316 O O      . VAL A 1 293 ? 28.715 -3.829  24.226  1.00 11.02 ? 311 VAL A O      1 
ATOM   2317 C CB     . VAL A 1 293 ? 26.710 -2.485  22.030  1.00 12.43 ? 311 VAL A CB     1 
ATOM   2318 C CG1    . VAL A 1 293 ? 25.949 -3.586  22.741  1.00 13.79 ? 311 VAL A CG1    1 
ATOM   2319 C CG2    . VAL A 1 293 ? 25.819 -1.276  21.914  1.00 9.24  ? 311 VAL A CG2    1 
ATOM   2320 N N      . ASP A 1 294 ? 29.906 -3.513  22.411  1.00 12.74 ? 312 ASP A N      1 
ATOM   2321 C CA     . ASP A 1 294 ? 30.759 -4.634  22.724  1.00 17.20 ? 312 ASP A CA     1 
ATOM   2322 C C      . ASP A 1 294 ? 31.814 -4.310  23.731  1.00 12.53 ? 312 ASP A C      1 
ATOM   2323 O O      . ASP A 1 294 ? 32.700 -5.089  23.946  1.00 17.25 ? 312 ASP A O      1 
ATOM   2324 C CB     . ASP A 1 294 ? 31.276 -5.341  21.474  1.00 15.19 ? 312 ASP A CB     1 
ATOM   2325 C CG     . ASP A 1 294 ? 30.282 -6.264  20.880  1.00 12.72 ? 312 ASP A CG     1 
ATOM   2326 O OD1    . ASP A 1 294 ? 29.198 -6.406  21.461  1.00 16.65 ? 312 ASP A OD1    1 
ATOM   2327 O OD2    . ASP A 1 294 ? 30.594 -6.853  19.837  1.00 9.90  ? 312 ASP A OD2    1 
ATOM   2328 N N      . VAL A 1 295 ? 31.698 -3.173  24.374  1.00 13.43 ? 313 VAL A N      1 
ATOM   2329 C CA     . VAL A 1 295 ? 32.585 -2.796  25.451  1.00 11.29 ? 313 VAL A CA     1 
ATOM   2330 C C      . VAL A 1 295 ? 31.708 -2.822  26.679  1.00 12.98 ? 313 VAL A C      1 
ATOM   2331 O O      . VAL A 1 295 ? 32.078 -3.356  27.694  1.00 18.74 ? 313 VAL A O      1 
ATOM   2332 C CB     . VAL A 1 295 ? 33.194 -1.404  25.187  1.00 11.00 ? 313 VAL A CB     1 
ATOM   2333 C CG1    . VAL A 1 295 ? 33.804 -0.799  26.433  1.00 12.97 ? 313 VAL A CG1    1 
ATOM   2334 C CG2    . VAL A 1 295 ? 34.205 -1.455  24.059  1.00 10.11 ? 313 VAL A CG2    1 
ATOM   2335 N N      . LEU A 1 296 ? 30.507 -2.319  26.561  1.00 10.45 ? 314 LEU A N      1 
ATOM   2336 C CA     . LEU A 1 296 ? 29.567 -2.294  27.647  1.00 11.41 ? 314 LEU A CA     1 
ATOM   2337 C C      . LEU A 1 296 ? 29.033 -3.650  28.091  1.00 16.59 ? 314 LEU A C      1 
ATOM   2338 O O      . LEU A 1 296 ? 28.706 -3.836  29.246  1.00 18.06 ? 314 LEU A O      1 
ATOM   2339 C CB     . LEU A 1 296 ? 28.399 -1.443  27.205  1.00 10.46 ? 314 LEU A CB     1 
ATOM   2340 C CG     . LEU A 1 296 ? 28.301 0.040   27.453  1.00 12.16 ? 314 LEU A CG     1 
ATOM   2341 C CD1    . LEU A 1 296 ? 27.254 0.583   26.504  1.00 15.09 ? 314 LEU A CD1    1 
ATOM   2342 C CD2    . LEU A 1 296 ? 27.903 0.280   28.887  1.00 12.78 ? 314 LEU A CD2    1 
ATOM   2343 N N      . THR A 1 297 ? 28.942 -4.592  27.178  1.00 14.59 ? 315 THR A N      1 
ATOM   2344 C CA     . THR A 1 297 ? 28.451 -5.906  27.489  1.00 14.08 ? 315 THR A CA     1 
ATOM   2345 C C      . THR A 1 297 ? 29.452 -6.806  28.186  1.00 18.79 ? 315 THR A C      1 
ATOM   2346 O O      . THR A 1 297 ? 29.101 -7.883  28.630  1.00 20.94 ? 315 THR A O      1 
ATOM   2347 C CB     . THR A 1 297 ? 27.945 -6.603  26.226  1.00 16.93 ? 315 THR A CB     1 
ATOM   2348 O OG1    . THR A 1 297 ? 28.892 -6.438  25.171  1.00 25.70 ? 315 THR A OG1    1 
ATOM   2349 C CG2    . THR A 1 297 ? 26.608 -6.073  25.808  1.00 14.32 ? 315 THR A CG2    1 
ATOM   2350 N N      . GLU A 1 298 ? 30.687 -6.361  28.299  1.00 17.41 ? 316 GLU A N      1 
ATOM   2351 C CA     . GLU A 1 298 ? 31.655 -7.143  28.987  1.00 18.08 ? 316 GLU A CA     1 
ATOM   2352 C C      . GLU A 1 298 ? 31.200 -7.363  30.367  1.00 24.49 ? 316 GLU A C      1 
ATOM   2353 O O      . GLU A 1 298 ? 30.835 -6.430  31.052  1.00 22.68 ? 316 GLU A O      1 
ATOM   2354 C CB     . GLU A 1 298 ? 33.042 -6.551  28.958  1.00 17.49 ? 316 GLU A CB     1 
ATOM   2355 C CG     . GLU A 1 298 ? 34.130 -7.583  29.206  1.00 19.47 ? 316 GLU A CG     1 
ATOM   2356 C CD     . GLU A 1 298 ? 35.519 -7.101  28.901  1.00 16.10 ? 316 GLU A CD     1 
ATOM   2357 O OE1    . GLU A 1 298 ? 35.655 -6.069  28.251  1.00 21.21 ? 316 GLU A OE1    1 
ATOM   2358 O OE2    . GLU A 1 298 ? 36.479 -7.766  29.304  1.00 19.50 ? 316 GLU A OE2    1 
ATOM   2359 N N      . PRO A 1 299 ? 31.237 -8.625  30.803  1.00 25.89 ? 317 PRO A N      1 
ATOM   2360 C CA     . PRO A 1 299 ? 30.749 -8.974  32.124  1.00 26.02 ? 317 PRO A CA     1 
ATOM   2361 C C      . PRO A 1 299 ? 31.169 -8.142  33.348  1.00 23.04 ? 317 PRO A C      1 
ATOM   2362 O O      . PRO A 1 299 ? 30.376 -7.990  34.241  1.00 22.00 ? 317 PRO A O      1 
ATOM   2363 C CB     . PRO A 1 299 ? 31.186 -10.415 32.218  1.00 31.06 ? 317 PRO A CB     1 
ATOM   2364 C CG     . PRO A 1 299 ? 31.018 -10.927 30.847  1.00 21.69 ? 317 PRO A CG     1 
ATOM   2365 C CD     . PRO A 1 299 ? 31.556 -9.824  30.011  1.00 17.12 ? 317 PRO A CD     1 
ATOM   2366 N N      . PHE A 1 300 ? 32.375 -7.622  33.389  1.00 21.59 ? 318 PHE A N      1 
ATOM   2367 C CA     . PHE A 1 300 ? 32.819 -6.809  34.500  1.00 20.75 ? 318 PHE A CA     1 
ATOM   2368 C C      . PHE A 1 300 ? 32.115 -5.472  34.615  1.00 24.44 ? 318 PHE A C      1 
ATOM   2369 O O      . PHE A 1 300 ? 31.964 -4.938  35.696  1.00 23.67 ? 318 PHE A O      1 
ATOM   2370 C CB     . PHE A 1 300 ? 34.347 -6.698  34.488  1.00 12.03 ? 318 PHE A CB     1 
ATOM   2371 C CG     . PHE A 1 300 ? 34.911 -5.544  33.703  1.00 15.88 ? 318 PHE A CG     1 
ATOM   2372 C CD1    . PHE A 1 300 ? 35.089 -5.637  32.343  1.00 19.81 ? 318 PHE A CD1    1 
ATOM   2373 C CD2    . PHE A 1 300 ? 35.344 -4.400  34.344  1.00 21.18 ? 318 PHE A CD2    1 
ATOM   2374 C CE1    . PHE A 1 300 ? 35.629 -4.595  31.630  1.00 15.97 ? 318 PHE A CE1    1 
ATOM   2375 C CE2    . PHE A 1 300 ? 35.883 -3.358  33.638  1.00 14.97 ? 318 PHE A CE2    1 
ATOM   2376 C CZ     . PHE A 1 300 ? 36.034 -3.458  32.279  1.00 14.67 ? 318 PHE A CZ     1 
ATOM   2377 N N      . LEU A 1 301 ? 31.665 -4.942  33.501  1.00 25.15 ? 319 LEU A N      1 
ATOM   2378 C CA     . LEU A 1 301 ? 30.995 -3.688  33.495  1.00 21.30 ? 319 LEU A CA     1 
ATOM   2379 C C      . LEU A 1 301 ? 29.530 -3.907  33.594  1.00 21.05 ? 319 LEU A C      1 
ATOM   2380 O O      . LEU A 1 301 ? 28.797 -3.021  33.956  1.00 22.22 ? 319 LEU A O      1 
ATOM   2381 C CB     . LEU A 1 301 ? 31.336 -2.968  32.197  1.00 22.18 ? 319 LEU A CB     1 
ATOM   2382 C CG     . LEU A 1 301 ? 32.607 -2.176  32.002  1.00 20.65 ? 319 LEU A CG     1 
ATOM   2383 C CD1    . LEU A 1 301 ? 32.482 -1.396  30.712  1.00 17.21 ? 319 LEU A CD1    1 
ATOM   2384 C CD2    . LEU A 1 301 ? 32.817 -1.257  33.179  1.00 19.27 ? 319 LEU A CD2    1 
ATOM   2385 N N      . GLN A 1 302 ? 29.091 -5.088  33.243  1.00 27.40 ? 320 GLN A N      1 
ATOM   2386 C CA     . GLN A 1 302 ? 27.711 -5.423  33.363  1.00 23.22 ? 320 GLN A CA     1 
ATOM   2387 C C      . GLN A 1 302 ? 27.465 -5.796  34.793  1.00 23.88 ? 320 GLN A C      1 
ATOM   2388 O O      . GLN A 1 302 ? 26.373 -5.649  35.287  1.00 25.32 ? 320 GLN A O      1 
ATOM   2389 C CB     . GLN A 1 302 ? 27.354 -6.504  32.368  1.00 22.98 ? 320 GLN A CB     1 
ATOM   2390 C CG     . GLN A 1 302 ? 25.885 -6.871  32.295  1.00 29.83 ? 320 GLN A CG     1 
ATOM   2391 C CD     . GLN A 1 302 ? 25.018 -5.720  31.849  1.00 43.98 ? 320 GLN A CD     1 
ATOM   2392 O OE1    . GLN A 1 302 ? 25.457 -4.851  31.095  1.00 42.59 ? 320 GLN A OE1    1 
ATOM   2393 N NE2    . GLN A 1 302 ? 23.774 -5.709  32.304  1.00 38.59 ? 320 GLN A NE2    1 
ATOM   2394 N N      . SER A 1 303 ? 28.496 -6.245  35.479  1.00 25.21 ? 321 SER A N      1 
ATOM   2395 C CA     . SER A 1 303 ? 28.323 -6.479  36.906  1.00 24.00 ? 321 SER A CA     1 
ATOM   2396 C C      . SER A 1 303 ? 27.861 -5.218  37.623  1.00 25.98 ? 321 SER A C      1 
ATOM   2397 O O      . SER A 1 303 ? 27.126 -5.297  38.613  1.00 30.87 ? 321 SER A O      1 
ATOM   2398 C CB     . SER A 1 303 ? 29.628 -6.977  37.512  1.00 24.44 ? 321 SER A CB     1 
ATOM   2399 O OG     . SER A 1 303 ? 29.410 -7.382  38.841  1.00 40.06 ? 321 SER A OG     1 
ATOM   2400 N N      . ILE A 1 304 ? 28.277 -4.046  37.135  1.00 24.18 ? 322 ILE A N      1 
ATOM   2401 C CA     . ILE A 1 304 ? 27.933 -2.790  37.792  1.00 18.08 ? 322 ILE A CA     1 
ATOM   2402 C C      . ILE A 1 304 ? 26.436 -2.531  37.707  1.00 24.17 ? 322 ILE A C      1 
ATOM   2403 O O      . ILE A 1 304 ? 25.832 -1.989  38.641  1.00 27.64 ? 322 ILE A O      1 
ATOM   2404 C CB     . ILE A 1 304 ? 28.759 -1.649  37.179  1.00 18.15 ? 322 ILE A CB     1 
ATOM   2405 C CG1    . ILE A 1 304 ? 30.245 -1.924  37.403  1.00 16.39 ? 322 ILE A CG1    1 
ATOM   2406 C CG2    . ILE A 1 304 ? 28.324 -0.306  37.726  1.00 19.50 ? 322 ILE A CG2    1 
ATOM   2407 C CD1    . ILE A 1 304 ? 31.172 -0.845  36.864  1.00 19.75 ? 322 ILE A CD1    1 
ATOM   2408 N N      . PHE A 1 305 ? 25.812 -2.929  36.588  1.00 25.56 ? 323 PHE A N      1 
ATOM   2409 C CA     . PHE A 1 305 ? 24.372 -2.769  36.378  1.00 21.18 ? 323 PHE A CA     1 
ATOM   2410 C C      . PHE A 1 305 ? 23.558 -3.852  37.097  1.00 21.01 ? 323 PHE A C      1 
ATOM   2411 O O      . PHE A 1 305 ? 22.474 -3.573  37.624  1.00 19.82 ? 323 PHE A O      1 
ATOM   2412 C CB     . PHE A 1 305 ? 24.051 -2.785  34.872  1.00 18.18 ? 323 PHE A CB     1 
ATOM   2413 C CG     . PHE A 1 305 ? 24.687 -1.663  34.082  1.00 20.04 ? 323 PHE A CG     1 
ATOM   2414 C CD1    . PHE A 1 305 ? 24.349 -0.338  34.319  1.00 22.68 ? 323 PHE A CD1    1 
ATOM   2415 C CD2    . PHE A 1 305 ? 25.611 -1.929  33.078  1.00 22.33 ? 323 PHE A CD2    1 
ATOM   2416 C CE1    . PHE A 1 305 ? 24.947 0.702   33.583  1.00 17.81 ? 323 PHE A CE1    1 
ATOM   2417 C CE2    . PHE A 1 305 ? 26.200 -0.887  32.346  1.00 17.29 ? 323 PHE A CE2    1 
ATOM   2418 C CZ     . PHE A 1 305 ? 25.872 0.410   32.598  1.00 13.37 ? 323 PHE A CZ     1 
ATOM   2419 N N      . ASP A 1 306 ? 24.052 -5.095  37.121  1.00 28.35 ? 324 ASP A N      1 
ATOM   2420 C CA     . ASP A 1 306 ? 23.289 -6.181  37.740  1.00 26.43 ? 324 ASP A CA     1 
ATOM   2421 C C      . ASP A 1 306 ? 23.106 -5.941  39.234  1.00 26.30 ? 324 ASP A C      1 
ATOM   2422 O O      . ASP A 1 306 ? 22.037 -6.210  39.793  1.00 29.57 ? 324 ASP A O      1 
ATOM   2423 C CB     . ASP A 1 306 ? 23.975 -7.532  37.481  1.00 19.49 ? 324 ASP A CB     1 
ATOM   2424 C CG     . ASP A 1 306 ? 23.935 -7.938  36.000  1.00 36.08 ? 324 ASP A CG     1 
ATOM   2425 O OD1    . ASP A 1 306 ? 23.240 -7.240  35.205  1.00 41.02 ? 324 ASP A OD1    1 
ATOM   2426 O OD2    . ASP A 1 306 ? 24.605 -8.937  35.622  1.00 33.19 ? 324 ASP A OD2    1 
ATOM   2427 N N      . LYS A 1 307 ? 24.140 -5.431  39.898  1.00 27.80 ? 325 LYS A N      1 
ATOM   2428 C CA     . LYS A 1 307 ? 24.046 -5.156  41.324  1.00 22.32 ? 325 LYS A CA     1 
ATOM   2429 C C      . LYS A 1 307 ? 23.094 -4.007  41.625  1.00 19.64 ? 325 LYS A C      1 
ATOM   2430 O O      . LYS A 1 307 ? 22.523 -3.965  42.719  1.00 29.85 ? 325 LYS A O      1 
ATOM   2431 C CB     . LYS A 1 307 ? 25.435 -4.855  41.887  1.00 24.58 ? 325 LYS A CB     1 
ATOM   2432 C CG     . LYS A 1 307 ? 26.449 -5.950  41.622  1.00 26.74 ? 325 LYS A CG     1 
ATOM   2433 C CD     . LYS A 1 307 ? 27.794 -5.625  42.262  1.00 26.11 ? 325 LYS A CD     1 
ATOM   2434 C CE     . LYS A 1 307 ? 28.549 -6.909  42.575  1.00 39.18 ? 325 LYS A CE     1 
ATOM   2435 N NZ     . LYS A 1 307 ? 28.533 -7.878  41.442  1.00 30.18 ? 325 LYS A NZ     1 
ATOM   2436 N N      . ALA A 1 308 ? 22.923 -3.068  40.696  1.00 18.51 ? 326 ALA A N      1 
ATOM   2437 C CA     . ALA A 1 308 ? 21.923 -2.022  40.842  1.00 24.81 ? 326 ALA A CA     1 
ATOM   2438 C C      . ALA A 1 308 ? 20.576 -2.435  40.274  1.00 23.05 ? 326 ALA A C      1 
ATOM   2439 O O      . ALA A 1 308 ? 19.624 -1.649  40.317  1.00 25.33 ? 326 ALA A O      1 
ATOM   2440 C CB     . ALA A 1 308 ? 22.391 -0.717  40.173  1.00 15.86 ? 326 ALA A CB     1 
ATOM   2441 N N      . ASN A 1 309 ? 20.471 -3.647  39.748  1.00 20.63 ? 327 ASN A N      1 
ATOM   2442 C CA     . ASN A 1 309 ? 19.232 -4.114  39.146  1.00 24.60 ? 327 ASN A CA     1 
ATOM   2443 C C      . ASN A 1 309 ? 18.800 -3.179  38.011  1.00 24.31 ? 327 ASN A C      1 
ATOM   2444 O O      . ASN A 1 309 ? 17.687 -2.650  37.993  1.00 32.43 ? 327 ASN A O      1 
ATOM   2445 C CB     . ASN A 1 309 ? 18.133 -4.262  40.209  1.00 27.73 ? 327 ASN A CB     1 
ATOM   2446 C CG     . ASN A 1 309 ? 17.196 -5.414  39.907  1.00 45.46 ? 327 ASN A CG     1 
ATOM   2447 O OD1    . ASN A 1 309 ? 17.618 -6.430  39.343  1.00 48.86 ? 327 ASN A OD1    1 
ATOM   2448 N ND2    . ASN A 1 309 ? 15.912 -5.258  40.257  1.00 40.86 ? 327 ASN A ND2    1 
ATOM   2449 N N      . ILE A 1 310 ? 19.718 -2.966  37.066  1.00 20.97 ? 328 ILE A N      1 
ATOM   2450 C CA     . ILE A 1 310 ? 19.442 -2.216  35.844  1.00 19.17 ? 328 ILE A CA     1 
ATOM   2451 C C      . ILE A 1 310 ? 19.662 -3.142  34.660  1.00 15.14 ? 328 ILE A C      1 
ATOM   2452 O O      . ILE A 1 310 ? 20.780 -3.623  34.451  1.00 15.36 ? 328 ILE A O      1 
ATOM   2453 C CB     . ILE A 1 310 ? 20.327 -0.975  35.698  1.00 17.60 ? 328 ILE A CB     1 
ATOM   2454 C CG1    . ILE A 1 310 ? 19.994 0.092   36.745  1.00 18.75 ? 328 ILE A CG1    1 
ATOM   2455 C CG2    . ILE A 1 310 ? 20.158 -0.403  34.307  1.00 15.10 ? 328 ILE A CG2    1 
ATOM   2456 C CD1    . ILE A 1 310 ? 21.091 1.149   36.882  1.00 17.17 ? 328 ILE A CD1    1 
ATOM   2457 N N      . LYS A 1 311 ? 18.603 -3.373  33.879  1.00 15.46 ? 329 LYS A N      1 
ATOM   2458 C CA     . LYS A 1 311 ? 18.658 -4.195  32.675  1.00 14.22 ? 329 LYS A CA     1 
ATOM   2459 C C      . LYS A 1 311 ? 18.659 -3.267  31.460  1.00 16.66 ? 329 LYS A C      1 
ATOM   2460 O O      . LYS A 1 311 ? 17.634 -2.661  31.127  1.00 13.94 ? 329 LYS A O      1 
ATOM   2461 C CB     . LYS A 1 311 ? 17.492 -5.182  32.643  1.00 12.83 ? 329 LYS A CB     1 
ATOM   2462 C CG     . LYS A 1 311 ? 17.300 -5.910  31.319  1.00 22.00 ? 329 LYS A CG     1 
ATOM   2463 C CD     . LYS A 1 311 ? 18.336 -7.025  31.073  1.00 27.67 ? 329 LYS A CD     1 
ATOM   2464 C CE     . LYS A 1 311 ? 17.991 -7.860  29.820  1.00 29.36 ? 329 LYS A CE     1 
ATOM   2465 N NZ     . LYS A 1 311 ? 18.606 -9.224  29.825  1.00 31.07 ? 329 LYS A NZ     1 
ATOM   2466 N N      . LEU A 1 312 ? 19.813 -3.152  30.810  1.00 13.38 ? 330 LEU A N      1 
ATOM   2467 C CA     . LEU A 1 312 ? 19.940 -2.300  29.641  1.00 11.89 ? 330 LEU A CA     1 
ATOM   2468 C C      . LEU A 1 312 ? 19.248 -2.919  28.433  1.00 12.20 ? 330 LEU A C      1 
ATOM   2469 O O      . LEU A 1 312 ? 19.269 -4.136  28.235  1.00 11.28 ? 330 LEU A O      1 
ATOM   2470 C CB     . LEU A 1 312 ? 21.410 -2.054  29.325  1.00 10.99 ? 330 LEU A CB     1 
ATOM   2471 C CG     . LEU A 1 312 ? 22.016 -1.192  30.415  1.00 10.39 ? 330 LEU A CG     1 
ATOM   2472 C CD1    . LEU A 1 312 ? 23.453 -0.787  30.094  1.00 9.63  ? 330 LEU A CD1    1 
ATOM   2473 C CD2    . LEU A 1 312 ? 21.096 0.001   30.632  1.00 10.59 ? 330 LEU A CD2    1 
ATOM   2474 N N      . ASN A 1 313 ? 18.621 -2.057  27.626  1.00 10.40 ? 331 ASN A N      1 
ATOM   2475 C CA     . ASN A 1 313 ? 18.041 -2.457  26.354  1.00 8.77  ? 331 ASN A CA     1 
ATOM   2476 C C      . ASN A 1 313 ? 18.987 -2.234  25.179  1.00 13.30 ? 331 ASN A C      1 
ATOM   2477 O O      . ASN A 1 313 ? 18.696 -2.706  24.068  1.00 10.67 ? 331 ASN A O      1 
ATOM   2478 C CB     . ASN A 1 313 ? 16.714 -1.719  26.107  1.00 5.15  ? 331 ASN A CB     1 
ATOM   2479 C CG     . ASN A 1 313 ? 16.879 -0.213  25.998  1.00 12.18 ? 331 ASN A CG     1 
ATOM   2480 O OD1    . ASN A 1 313 ? 17.776 0.291   25.323  1.00 14.90 ? 331 ASN A OD1    1 
ATOM   2481 N ND2    . ASN A 1 313 ? 15.998 0.517   26.664  1.00 14.79 ? 331 ASN A ND2    1 
ATOM   2482 N N      . TYR A 1 314 ? 20.101 -1.525  25.395  1.00 10.14 ? 332 TYR A N      1 
ATOM   2483 C CA     . TYR A 1 314 ? 21.146 -1.383  24.385  1.00 12.62 ? 332 TYR A CA     1 
ATOM   2484 C C      . TYR A 1 314 ? 20.620 -0.732  23.118  1.00 12.63 ? 332 TYR A C      1 
ATOM   2485 O O      . TYR A 1 314 ? 21.103 -0.996  22.013  1.00 11.35 ? 332 TYR A O      1 
ATOM   2486 C CB     . TYR A 1 314 ? 21.798 -2.730  24.058  1.00 11.17 ? 332 TYR A CB     1 
ATOM   2487 C CG     . TYR A 1 314 ? 22.517 -3.287  25.231  1.00 11.33 ? 332 TYR A CG     1 
ATOM   2488 C CD1    . TYR A 1 314 ? 23.672 -2.673  25.713  1.00 15.71 ? 332 TYR A CD1    1 
ATOM   2489 C CD2    . TYR A 1 314 ? 22.030 -4.398  25.898  1.00 8.32  ? 332 TYR A CD2    1 
ATOM   2490 C CE1    . TYR A 1 314 ? 24.341 -3.179  26.836  1.00 11.88 ? 332 TYR A CE1    1 
ATOM   2491 C CE2    . TYR A 1 314 ? 22.670 -4.896  27.013  1.00 11.01 ? 332 TYR A CE2    1 
ATOM   2492 C CZ     . TYR A 1 314 ? 23.829 -4.294  27.481  1.00 11.27 ? 332 TYR A CZ     1 
ATOM   2493 O OH     . TYR A 1 314 ? 24.469 -4.811  28.598  1.00 24.20 ? 332 TYR A OH     1 
ATOM   2494 N N      . GLY A 1 315 ? 19.640 0.134   23.270  1.00 11.90 ? 333 GLY A N      1 
ATOM   2495 C CA     . GLY A 1 315 ? 19.174 0.866   22.125  1.00 11.31 ? 333 GLY A CA     1 
ATOM   2496 C C      . GLY A 1 315 ? 18.276 0.084   21.205  1.00 9.75  ? 333 GLY A C      1 
ATOM   2497 O O      . GLY A 1 315 ? 17.939 0.583   20.138  1.00 12.23 ? 333 GLY A O      1 
ATOM   2498 N N      . VAL A 1 316 ? 17.867 -1.122  21.575  1.00 12.90 ? 334 VAL A N      1 
ATOM   2499 C CA     . VAL A 1 316 ? 16.968 -1.892  20.718  1.00 15.28 ? 334 VAL A CA     1 
ATOM   2500 C C      . VAL A 1 316 ? 15.576 -1.266  20.748  1.00 18.21 ? 334 VAL A C      1 
ATOM   2501 O O      . VAL A 1 316 ? 15.020 -1.002  21.825  1.00 17.91 ? 334 VAL A O      1 
ATOM   2502 C CB     . VAL A 1 316 ? 16.945 -3.365  21.154  1.00 7.92  ? 334 VAL A CB     1 
ATOM   2503 C CG1    . VAL A 1 316 ? 15.873 -4.076  20.463  1.00 5.71  ? 334 VAL A CG1    1 
ATOM   2504 C CG2    . VAL A 1 316 ? 18.272 -4.019  20.851  1.00 6.43  ? 334 VAL A CG2    1 
ATOM   2505 N N      . LEU A 1 317 ? 15.019 -1.010  19.557  1.00 19.98 ? 335 LEU A N      1 
ATOM   2506 C CA     . LEU A 1 317 ? 13.694 -0.441  19.339  1.00 13.82 ? 335 LEU A CA     1 
ATOM   2507 C C      . LEU A 1 317 ? 12.706 -1.533  18.903  1.00 20.94 ? 335 LEU A C      1 
ATOM   2508 O O      . LEU A 1 317 ? 13.064 -2.705  18.745  1.00 20.81 ? 335 LEU A O      1 
ATOM   2509 C CB     . LEU A 1 317 ? 13.771 0.662   18.283  1.00 16.40 ? 335 LEU A CB     1 
ATOM   2510 C CG     . LEU A 1 317 ? 14.704 1.869   18.451  1.00 14.73 ? 335 LEU A CG     1 
ATOM   2511 C CD1    . LEU A 1 317 ? 15.014 2.470   17.095  1.00 12.17 ? 335 LEU A CD1    1 
ATOM   2512 C CD2    . LEU A 1 317 ? 14.068 2.932   19.339  1.00 11.22 ? 335 LEU A CD2    1 
ATOM   2513 N N      . ASP A 1 318 ? 11.443 -1.141  18.671  1.00 28.57 ? 336 ASP A N      1 
ATOM   2514 C CA     . ASP A 1 318 ? 10.419 -2.116  18.290  1.00 25.13 ? 336 ASP A CA     1 
ATOM   2515 C C      . ASP A 1 318 ? 10.257 -2.262  16.788  1.00 30.74 ? 336 ASP A C      1 
ATOM   2516 O O      . ASP A 1 318 ? 9.859  -3.331  16.317  1.00 36.18 ? 336 ASP A O      1 
ATOM   2517 C CB     . ASP A 1 318 ? 9.063  -1.754  18.910  1.00 30.37 ? 336 ASP A CB     1 
ATOM   2518 C CG     . ASP A 1 318 ? 8.941  -2.216  20.357  1.00 54.03 ? 336 ASP A CG     1 
ATOM   2519 O OD1    . ASP A 1 318 ? 9.422  -3.334  20.674  1.00 58.29 ? 336 ASP A OD1    1 
ATOM   2520 O OD2    . ASP A 1 318 ? 8.374  -1.458  21.176  1.00 50.80 ? 336 ASP A OD2    1 
ATOM   2521 N N      . ASP A 1 319 ? 10.557 -1.219  16.027  1.00 38.76 ? 337 ASP A N      1 
ATOM   2522 C CA     . ASP A 1 319 ? 10.432 -1.230  14.573  1.00 33.49 ? 337 ASP A CA     1 
ATOM   2523 C C      . ASP A 1 319 ? 11.714 -0.636  14.001  1.00 27.47 ? 337 ASP A C      1 
ATOM   2524 O O      . ASP A 1 319 ? 11.874 0.586   13.971  1.00 36.59 ? 337 ASP A O      1 
ATOM   2525 C CB     . ASP A 1 319 ? 9.212  -0.428  14.128  1.00 25.30 ? 337 ASP A CB     1 
ATOM   2526 C CG     . ASP A 1 319 ? 9.264  1.019   14.615  1.00 46.17 ? 337 ASP A CG     1 
ATOM   2527 O OD1    . ASP A 1 319 ? 9.792  1.243   15.727  1.00 49.38 ? 337 ASP A OD1    1 
ATOM   2528 O OD2    . ASP A 1 319 ? 8.798  1.935   13.892  1.00 55.11 ? 337 ASP A OD2    1 
ATOM   2529 N N      . THR A 1 320 ? 12.644 -1.473  13.561  1.00 22.02 ? 338 THR A N      1 
ATOM   2530 C CA     . THR A 1 320 ? 13.653 -0.926  12.657  1.00 25.16 ? 338 THR A CA     1 
ATOM   2531 C C      . THR A 1 320 ? 13.187 -1.024  11.222  1.00 23.17 ? 338 THR A C      1 
ATOM   2532 O O      . THR A 1 320 ? 13.997 -1.256  10.321  1.00 32.13 ? 338 THR A O      1 
ATOM   2533 C CB     . THR A 1 320 ? 15.022 -1.596  12.834  1.00 29.39 ? 338 THR A CB     1 
ATOM   2534 O OG1    . THR A 1 320 ? 14.958 -3.001  12.523  1.00 29.71 ? 338 THR A OG1    1 
ATOM   2535 C CG2    . THR A 1 320 ? 15.532 -1.399  14.262  1.00 23.62 ? 338 THR A CG2    1 
ATOM   2536 N N      . HIS A 1 321 ? 11.889 -0.820  10.973  1.00 23.35 ? 339 HIS A N      1 
ATOM   2537 C CA     . HIS A 1 321 ? 11.342 -1.160  9.669   1.00 27.82 ? 339 HIS A CA     1 
ATOM   2538 C C      . HIS A 1 321 ? 11.700 -0.111  8.620   1.00 24.12 ? 339 HIS A C      1 
ATOM   2539 O O      . HIS A 1 321 ? 12.205 -0.453  7.548   1.00 25.32 ? 339 HIS A O      1 
ATOM   2540 C CB     . HIS A 1 321 ? 9.832  -1.363  9.764   1.00 30.16 ? 339 HIS A CB     1 
ATOM   2541 C CG     . HIS A 1 321 ? 9.282  -2.225  8.672   1.00 44.19 ? 339 HIS A CG     1 
ATOM   2542 N ND1    . HIS A 1 321 ? 9.978  -2.495  7.512   1.00 49.68 ? 339 HIS A ND1    1 
ATOM   2543 C CD2    . HIS A 1 321 ? 8.106  -2.884  8.565   1.00 57.61 ? 339 HIS A CD2    1 
ATOM   2544 C CE1    . HIS A 1 321 ? 9.250  -3.274  6.733   1.00 50.93 ? 339 HIS A CE1    1 
ATOM   2545 N NE2    . HIS A 1 321 ? 8.110  -3.527  7.349   1.00 59.10 ? 339 HIS A NE2    1 
ATOM   2546 N N      . ALA A 1 322 ? 11.485 1.172   8.919   1.00 23.78 ? 340 ALA A N      1 
ATOM   2547 C CA     . ALA A 1 322 ? 11.817 2.217   7.953   1.00 20.62 ? 340 ALA A CA     1 
ATOM   2548 C C      . ALA A 1 322 ? 13.283 2.141   7.555   1.00 16.06 ? 340 ALA A C      1 
ATOM   2549 O O      . ALA A 1 322 ? 13.624 2.232   6.373   1.00 17.72 ? 340 ALA A O      1 
ATOM   2550 C CB     . ALA A 1 322 ? 11.493 3.600   8.519   1.00 20.26 ? 340 ALA A CB     1 
ATOM   2551 N N      . GLU A 1 323 ? 14.168 1.965   8.527   1.00 14.55 ? 341 GLU A N      1 
ATOM   2552 C CA     . GLU A 1 323 ? 15.585 1.915   8.205   1.00 15.91 ? 341 GLU A CA     1 
ATOM   2553 C C      . GLU A 1 323 ? 15.901 0.672   7.389   1.00 18.45 ? 341 GLU A C      1 
ATOM   2554 O O      . GLU A 1 323 ? 16.624 0.740   6.386   1.00 14.27 ? 341 GLU A O      1 
ATOM   2555 C CB     . GLU A 1 323 ? 16.430 1.957   9.487   1.00 15.91 ? 341 GLU A CB     1 
ATOM   2556 C CG     . GLU A 1 323 ? 16.052 3.028   10.501  1.00 17.74 ? 341 GLU A CG     1 
ATOM   2557 C CD     . GLU A 1 323 ? 15.019 2.551   11.527  1.00 24.46 ? 341 GLU A CD     1 
ATOM   2558 O OE1    . GLU A 1 323 ? 13.998 1.961   11.119  1.00 25.49 ? 341 GLU A OE1    1 
ATOM   2559 O OE2    . GLU A 1 323 ? 15.225 2.764   12.744  1.00 24.92 ? 341 GLU A OE2    1 
ATOM   2560 N N      . PHE A 1 324 ? 15.370 -0.480  7.811   1.00 15.74 ? 342 PHE A N      1 
ATOM   2561 C CA     . PHE A 1 324 ? 15.616 -1.710  7.067   1.00 15.00 ? 342 PHE A CA     1 
ATOM   2562 C C      . PHE A 1 324 ? 15.215 -1.531  5.613   1.00 13.41 ? 342 PHE A C      1 
ATOM   2563 O O      . PHE A 1 324 ? 15.970 -1.873  4.700   1.00 16.58 ? 342 PHE A O      1 
ATOM   2564 C CB     . PHE A 1 324 ? 14.855 -2.874  7.705   1.00 20.66 ? 342 PHE A CB     1 
ATOM   2565 C CG     . PHE A 1 324 ? 15.247 -4.243  7.190   1.00 14.65 ? 342 PHE A CG     1 
ATOM   2566 C CD1    . PHE A 1 324 ? 16.298 -4.940  7.767   1.00 17.87 ? 342 PHE A CD1    1 
ATOM   2567 C CD2    . PHE A 1 324 ? 14.522 -4.858  6.181   1.00 16.73 ? 342 PHE A CD2    1 
ATOM   2568 C CE1    . PHE A 1 324 ? 16.649 -6.211  7.334   1.00 18.05 ? 342 PHE A CE1    1 
ATOM   2569 C CE2    . PHE A 1 324 ? 14.868 -6.129  5.733   1.00 22.12 ? 342 PHE A CE2    1 
ATOM   2570 C CZ     . PHE A 1 324 ? 15.940 -6.808  6.319   1.00 17.45 ? 342 PHE A CZ     1 
ATOM   2571 N N      . ARG A 1 325 ? 14.077 -0.953  5.345   1.00 13.50 ? 343 ARG A N      1 
ATOM   2572 C CA     . ARG A 1 325 ? 13.604 -0.735  3.994   1.00 17.14 ? 343 ARG A CA     1 
ATOM   2573 C C      . ARG A 1 325 ? 14.356 0.227   3.136   1.00 14.38 ? 343 ARG A C      1 
ATOM   2574 O O      . ARG A 1 325 ? 14.394 0.073   1.943   1.00 15.55 ? 343 ARG A O      1 
ATOM   2575 C CB     . ARG A 1 325 ? 12.169 -0.284  4.052   1.00 18.27 ? 343 ARG A CB     1 
ATOM   2576 C CG     . ARG A 1 325 ? 11.167 -1.411  3.956   1.00 38.22 ? 343 ARG A CG     1 
ATOM   2577 C CD     . ARG A 1 325 ? 9.754  -0.868  3.992   1.00 54.53 ? 343 ARG A CD     1 
ATOM   2578 N NE     . ARG A 1 325 ? 9.602  0.219   4.955   1.00 64.64 ? 343 ARG A NE     1 
ATOM   2579 C CZ     . ARG A 1 325 ? 8.518  0.402   5.702   1.00 61.52 ? 343 ARG A CZ     1 
ATOM   2580 N NH1    . ARG A 1 325 ? 7.493  -0.433  5.595   1.00 61.02 ? 343 ARG A NH1    1 
ATOM   2581 N NH2    . ARG A 1 325 ? 8.456  1.415   6.551   1.00 47.99 ? 343 ARG A NH2    1 
ATOM   2582 N N      . LYS A 1 326 ? 14.953 1.225   3.741   1.00 14.80 ? 344 LYS A N      1 
ATOM   2583 C CA     . LYS A 1 326 ? 15.706 2.200   3.024   1.00 10.09 ? 344 LYS A CA     1 
ATOM   2584 C C      . LYS A 1 326 ? 17.046 1.677   2.666   1.00 11.29 ? 344 LYS A C      1 
ATOM   2585 O O      . LYS A 1 326 ? 17.648 2.147   1.740   1.00 15.93 ? 344 LYS A O      1 
ATOM   2586 C CB     . LYS A 1 326 ? 15.843 3.421   3.891   1.00 13.54 ? 344 LYS A CB     1 
ATOM   2587 C CG     . LYS A 1 326 ? 15.036 4.613   3.441   1.00 17.15 ? 344 LYS A CG     1 
ATOM   2588 C CD     . LYS A 1 326 ? 15.148 5.739   4.446   1.00 14.01 ? 344 LYS A CD     1 
ATOM   2589 C CE     . LYS A 1 326 ? 14.047 5.659   5.483   1.00 18.08 ? 344 LYS A CE     1 
ATOM   2590 N NZ     . LYS A 1 326 ? 14.583 5.801   6.861   1.00 29.24 ? 344 LYS A NZ     1 
ATOM   2591 N N      . ALA A 1 327 ? 17.504 0.675   3.367   1.00 10.19 ? 345 ALA A N      1 
ATOM   2592 C CA     . ALA A 1 327 ? 18.747 0.050   3.061   1.00 7.83  ? 345 ALA A CA     1 
ATOM   2593 C C      . ALA A 1 327 ? 18.601 -0.996  1.996   1.00 10.25 ? 345 ALA A C      1 
ATOM   2594 O O      . ALA A 1 327 ? 19.561 -1.401  1.407   1.00 9.60  ? 345 ALA A O      1 
ATOM   2595 C CB     . ALA A 1 327 ? 19.296 -0.527  4.310   1.00 7.22  ? 345 ALA A CB     1 
ATOM   2596 N N      . GLN A 1 328 ? 17.387 -1.406  1.721   1.00 16.37 ? 346 GLN A N      1 
ATOM   2597 C CA     . GLN A 1 328 ? 17.113 -2.353  0.683   1.00 17.08 ? 346 GLN A CA     1 
ATOM   2598 C C      . GLN A 1 328 ? 17.112 -1.577  -0.576  1.00 13.39 ? 346 GLN A C      1 
ATOM   2599 O O      . GLN A 1 328 ? 17.596 -2.024  -1.587  1.00 13.07 ? 346 GLN A O      1 
ATOM   2600 C CB     . GLN A 1 328 ? 15.737 -2.954  0.887   1.00 14.61 ? 346 GLN A CB     1 
ATOM   2601 C CG     . GLN A 1 328 ? 15.572 -3.904  2.041   1.00 16.84 ? 346 GLN A CG     1 
ATOM   2602 C CD     . GLN A 1 328 ? 14.138 -4.352  2.195   1.00 21.51 ? 346 GLN A CD     1 
ATOM   2603 O OE1    . GLN A 1 328 ? 13.215 -3.612  1.905   1.00 25.68 ? 346 GLN A OE1    1 
ATOM   2604 N NE2    . GLN A 1 328 ? 13.951 -5.572  2.636   1.00 27.31 ? 346 GLN A NE2    1 
ATOM   2605 N N      . ASP A 1 329 ? 16.568 -0.396  -0.519  1.00 10.34 ? 347 ASP A N      1 
ATOM   2606 C CA     . ASP A 1 329 ? 16.588 0.463   -1.648  1.00 13.45 ? 347 ASP A CA     1 
ATOM   2607 C C      . ASP A 1 329 ? 18.031 0.825   -1.974  1.00 16.40 ? 347 ASP A C      1 
ATOM   2608 O O      . ASP A 1 329 ? 18.390 0.931   -3.131  1.00 14.32 ? 347 ASP A O      1 
ATOM   2609 C CB     . ASP A 1 329 ? 15.721 1.680   -1.350  1.00 15.19 ? 347 ASP A CB     1 
ATOM   2610 C CG     . ASP A 1 329 ? 14.274 1.354   -1.252  1.00 15.32 ? 347 ASP A CG     1 
ATOM   2611 O OD1    . ASP A 1 329 ? 13.860 0.323   -1.810  1.00 26.41 ? 347 ASP A OD1    1 
ATOM   2612 O OD2    . ASP A 1 329 ? 13.547 2.136   -0.618  1.00 14.64 ? 347 ASP A OD2    1 
ATOM   2613 N N      . TYR A 1 330 ? 18.869 0.973   -0.965  1.00 14.70 ? 348 TYR A N      1 
ATOM   2614 C CA     . TYR A 1 330 ? 20.263 1.282   -1.136  1.00 9.72  ? 348 TYR A CA     1 
ATOM   2615 C C      . TYR A 1 330 ? 21.095 0.168   -1.696  1.00 9.00  ? 348 TYR A C      1 
ATOM   2616 O O      . TYR A 1 330 ? 22.026 0.394   -2.407  1.00 11.32 ? 348 TYR A O      1 
ATOM   2617 C CB     . TYR A 1 330 ? 20.777 1.668   0.221   1.00 8.52  ? 348 TYR A CB     1 
ATOM   2618 C CG     . TYR A 1 330 ? 22.174 2.180   0.265   1.00 8.80  ? 348 TYR A CG     1 
ATOM   2619 C CD1    . TYR A 1 330 ? 22.509 3.361   -0.346  1.00 7.78  ? 348 TYR A CD1    1 
ATOM   2620 C CD2    . TYR A 1 330 ? 23.156 1.484   0.934   1.00 8.93  ? 348 TYR A CD2    1 
ATOM   2621 C CE1    . TYR A 1 330 ? 23.787 3.828   -0.299  1.00 6.05  ? 348 TYR A CE1    1 
ATOM   2622 C CE2    . TYR A 1 330 ? 24.436 1.949   0.987   1.00 9.45  ? 348 TYR A CE2    1 
ATOM   2623 C CZ     . TYR A 1 330 ? 24.748 3.121   0.366   1.00 8.00  ? 348 TYR A CZ     1 
ATOM   2624 O OH     . TYR A 1 330 ? 26.036 3.578   0.413   1.00 8.73  ? 348 TYR A OH     1 
ATOM   2625 N N      . VAL A 1 331 ? 20.746 -1.048  -1.380  1.00 13.06 ? 349 VAL A N      1 
ATOM   2626 C CA     . VAL A 1 331 ? 21.514 -2.174  -1.839  1.00 15.32 ? 349 VAL A CA     1 
ATOM   2627 C C      . VAL A 1 331 ? 21.097 -2.575  -3.219  1.00 16.36 ? 349 VAL A C      1 
ATOM   2628 O O      . VAL A 1 331 ? 21.915 -2.939  -4.001  1.00 14.33 ? 349 VAL A O      1 
ATOM   2629 C CB     . VAL A 1 331 ? 21.584 -3.330  -0.823  1.00 9.61  ? 349 VAL A CB     1 
ATOM   2630 C CG1    . VAL A 1 331 ? 20.281 -4.089  -0.721  1.00 18.62 ? 349 VAL A CG1    1 
ATOM   2631 C CG2    . VAL A 1 331 ? 22.694 -4.250  -1.211  1.00 14.89 ? 349 VAL A CG2    1 
ATOM   2632 N N      . PHE A 1 332 ? 19.836 -2.416  -3.561  1.00 14.70 ? 350 PHE A N      1 
ATOM   2633 C CA     . PHE A 1 332 ? 19.436 -2.672  -4.912  1.00 16.49 ? 350 PHE A CA     1 
ATOM   2634 C C      . PHE A 1 332 ? 20.142 -1.643  -5.733  1.00 16.79 ? 350 PHE A C      1 
ATOM   2635 O O      . PHE A 1 332 ? 20.723 -1.976  -6.712  1.00 18.37 ? 350 PHE A O      1 
ATOM   2636 C CB     . PHE A 1 332 ? 17.924 -2.577  -5.087  1.00 19.96 ? 350 PHE A CB     1 
ATOM   2637 C CG     . PHE A 1 332 ? 17.479 -2.339  -6.506  1.00 24.37 ? 350 PHE A CG     1 
ATOM   2638 C CD1    . PHE A 1 332 ? 17.383 -3.388  -7.396  1.00 28.41 ? 350 PHE A CD1    1 
ATOM   2639 C CD2    . PHE A 1 332 ? 17.138 -1.067  -6.943  1.00 25.48 ? 350 PHE A CD2    1 
ATOM   2640 C CE1    . PHE A 1 332 ? 16.975 -3.171  -8.694  1.00 27.11 ? 350 PHE A CE1    1 
ATOM   2641 C CE2    . PHE A 1 332 ? 16.739 -0.843  -8.240  1.00 23.29 ? 350 PHE A CE2    1 
ATOM   2642 C CZ     . PHE A 1 332 ? 16.648 -1.900  -9.117  1.00 28.20 ? 350 PHE A CZ     1 
ATOM   2643 N N      . GLY A 1 333 ? 20.144 -0.405  -5.292  1.00 13.79 ? 351 GLY A N      1 
ATOM   2644 C CA     . GLY A 1 333 ? 20.762 0.651   -6.033  1.00 13.36 ? 351 GLY A CA     1 
ATOM   2645 C C      . GLY A 1 333 ? 22.204 0.429   -6.265  1.00 14.32 ? 351 GLY A C      1 
ATOM   2646 O O      . GLY A 1 333 ? 22.638 0.500   -7.380  1.00 15.84 ? 351 GLY A O      1 
ATOM   2647 N N      . LEU A 1 334 ? 22.955 0.197   -5.216  1.00 13.52 ? 352 LEU A N      1 
ATOM   2648 C CA     . LEU A 1 334 ? 24.366 -0.134  -5.354  1.00 11.15 ? 352 LEU A CA     1 
ATOM   2649 C C      . LEU A 1 334 ? 24.589 -1.306  -6.304  1.00 17.11 ? 352 LEU A C      1 
ATOM   2650 O O      . LEU A 1 334 ? 25.473 -1.238  -7.167  1.00 19.29 ? 352 LEU A O      1 
ATOM   2651 C CB     . LEU A 1 334 ? 24.973 -0.431  -3.983  1.00 12.66 ? 352 LEU A CB     1 
ATOM   2652 C CG     . LEU A 1 334 ? 25.699 0.725   -3.284  1.00 16.13 ? 352 LEU A CG     1 
ATOM   2653 C CD1    . LEU A 1 334 ? 24.994 2.081   -3.511  1.00 14.24 ? 352 LEU A CD1    1 
ATOM   2654 C CD2    . LEU A 1 334 ? 25.890 0.440   -1.798  1.00 14.43 ? 352 LEU A CD2    1 
ATOM   2655 N N      . THR A 1 335 ? 23.789 -2.382  -6.186  1.00 13.69 ? 353 THR A N      1 
ATOM   2656 C CA     . THR A 1 335 ? 24.147 -3.603  -6.901  1.00 15.44 ? 353 THR A CA     1 
ATOM   2657 C C      . THR A 1 335 ? 23.710 -3.620  -8.364  1.00 16.78 ? 353 THR A C      1 
ATOM   2658 O O      . THR A 1 335 ? 24.435 -4.191  -9.183  1.00 17.36 ? 353 THR A O      1 
ATOM   2659 C CB     . THR A 1 335 ? 23.615 -4.841  -6.182  1.00 15.56 ? 353 THR A CB     1 
ATOM   2660 O OG1    . THR A 1 335 ? 22.194 -4.805  -6.117  1.00 16.95 ? 353 THR A OG1    1 
ATOM   2661 C CG2    . THR A 1 335 ? 24.180 -4.932  -4.792  1.00 14.43 ? 353 THR A CG2    1 
ATOM   2662 N N      . ILE A 1 336 ? 22.569 -3.031  -8.746  1.00 15.45 ? 354 ILE A N      1 
ATOM   2663 C CA     . ILE A 1 336 ? 22.347 -2.943  -10.196 1.00 19.90 ? 354 ILE A CA     1 
ATOM   2664 C C      . ILE A 1 336 ? 23.309 -1.946  -10.801 1.00 16.26 ? 354 ILE A C      1 
ATOM   2665 O O      . ILE A 1 336 ? 23.731 -2.102  -11.952 1.00 13.70 ? 354 ILE A O      1 
ATOM   2666 C CB     . ILE A 1 336 ? 20.906 -2.572  -10.591 1.00 20.22 ? 354 ILE A CB     1 
ATOM   2667 C CG1    . ILE A 1 336 ? 20.328 -1.577  -9.599  1.00 23.30 ? 354 ILE A CG1    1 
ATOM   2668 C CG2    . ILE A 1 336 ? 20.022 -3.804  -10.755 1.00 18.84 ? 354 ILE A CG2    1 
ATOM   2669 C CD1    . ILE A 1 336 ? 20.627 -0.163  -9.936  1.00 19.80 ? 354 ILE A CD1    1 
ATOM   2670 N N      . GLN A 1 337 ? 23.664 -0.907  -10.044 1.00 14.88 ? 355 GLN A N      1 
ATOM   2671 C CA     . GLN A 1 337 ? 24.726 -0.007  -10.468 1.00 14.90 ? 355 GLN A CA     1 
ATOM   2672 C C      . GLN A 1 337 ? 25.967 -0.787  -10.878 1.00 18.23 ? 355 GLN A C      1 
ATOM   2673 O O      . GLN A 1 337 ? 26.538 -0.561  -11.952 1.00 16.84 ? 355 GLN A O      1 
ATOM   2674 C CB     . GLN A 1 337 ? 25.073 0.948   -9.334  1.00 13.70 ? 355 GLN A CB     1 
ATOM   2675 C CG     . GLN A 1 337 ? 26.193 1.875   -9.707  1.00 14.86 ? 355 GLN A CG     1 
ATOM   2676 C CD     . GLN A 1 337 ? 25.670 3.062   -10.445 1.00 20.95 ? 355 GLN A CD     1 
ATOM   2677 O OE1    . GLN A 1 337 ? 24.702 2.950   -11.209 1.00 17.69 ? 355 GLN A OE1    1 
ATOM   2678 N NE2    . GLN A 1 337 ? 26.273 4.227   -10.201 1.00 19.90 ? 355 GLN A NE2    1 
ATOM   2679 N N      . SER A 1 338 ? 26.418 -1.694  -9.999  1.00 20.38 ? 356 SER A N      1 
ATOM   2680 C CA     . SER A 1 338 ? 27.584 -2.521  -10.281 1.00 14.27 ? 356 SER A CA     1 
ATOM   2681 C C      . SER A 1 338 ? 27.334 -3.402  -11.500 1.00 14.99 ? 356 SER A C      1 
ATOM   2682 O O      . SER A 1 338 ? 28.178 -3.500  -12.398 1.00 10.67 ? 356 SER A O      1 
ATOM   2683 C CB     . SER A 1 338 ? 27.918 -3.349  -9.037  1.00 14.78 ? 356 SER A CB     1 
ATOM   2684 O OG     . SER A 1 338 ? 28.776 -4.449  -9.307  1.00 20.18 ? 356 SER A OG     1 
ATOM   2685 N N      . ALA A 1 339 ? 26.150 -4.022  -11.563 1.00 18.44 ? 357 ALA A N      1 
ATOM   2686 C CA     . ALA A 1 339 ? 25.774 -4.812  -12.737 1.00 19.58 ? 357 ALA A CA     1 
ATOM   2687 C C      . ALA A 1 339 ? 25.866 -3.970  -14.000 1.00 16.61 ? 357 ALA A C      1 
ATOM   2688 O O      . ALA A 1 339 ? 26.552 -4.331  -14.965 1.00 16.86 ? 357 ALA A O      1 
ATOM   2689 C CB     . ALA A 1 339 ? 24.353 -5.370  -12.572 1.00 13.93 ? 357 ALA A CB     1 
ATOM   2690 N N      . MET A 1 340 ? 25.181 -2.829  -13.994 1.00 18.54 ? 358 MET A N      1 
ATOM   2691 C CA     . MET A 1 340 ? 25.204 -1.924  -15.129 1.00 13.26 ? 358 MET A CA     1 
ATOM   2692 C C      . MET A 1 340 ? 26.635 -1.544  -15.494 1.00 12.07 ? 358 MET A C      1 
ATOM   2693 O O      . MET A 1 340 ? 27.013 -1.574  -16.670 1.00 11.30 ? 358 MET A O      1 
ATOM   2694 C CB     . MET A 1 340 ? 24.347 -0.704  -14.800 1.00 12.40 ? 358 MET A CB     1 
ATOM   2695 C CG     . MET A 1 340 ? 24.176 0.282   -15.920 1.00 15.76 ? 358 MET A CG     1 
ATOM   2696 S SD     . MET A 1 340 ? 25.557 1.431   -16.126 1.00 6.32  ? 358 MET A SD     1 
ATOM   2697 C CE     . MET A 1 340 ? 25.294 2.522   -14.737 1.00 13.07 ? 358 MET A CE     1 
ATOM   2698 N N      . HIS A 1 341 ? 27.470 -1.232  -14.505 1.00 11.94 ? 359 HIS A N      1 
ATOM   2699 C CA     . HIS A 1 341 ? 28.857 -0.906  -14.843 1.00 16.04 ? 359 HIS A CA     1 
ATOM   2700 C C      . HIS A 1 341 ? 29.559 -2.078  -15.524 1.00 12.60 ? 359 HIS A C      1 
ATOM   2701 O O      . HIS A 1 341 ? 30.406 -1.872  -16.401 1.00 13.30 ? 359 HIS A O      1 
ATOM   2702 C CB     . HIS A 1 341 ? 29.642 -0.459  -13.609 1.00 12.03 ? 359 HIS A CB     1 
ATOM   2703 C CG     . HIS A 1 341 ? 29.231 0.874   -13.086 1.00 11.71 ? 359 HIS A CG     1 
ATOM   2704 N ND1    . HIS A 1 341 ? 29.656 1.357   -11.866 1.00 16.05 ? 359 HIS A ND1    1 
ATOM   2705 C CD2    . HIS A 1 341 ? 28.420 1.822   -13.608 1.00 13.71 ? 359 HIS A CD2    1 
ATOM   2706 C CE1    . HIS A 1 341 ? 29.125 2.547   -11.661 1.00 15.53 ? 359 HIS A CE1    1 
ATOM   2707 N NE2    . HIS A 1 341 ? 28.375 2.855   -12.706 1.00 17.27 ? 359 HIS A NE2    1 
ATOM   2708 N N      . HIS A 1 342 ? 29.216 -3.312  -15.150 1.00 15.14 ? 360 HIS A N      1 
ATOM   2709 C CA     . HIS A 1 342 ? 29.846 -4.458  -15.799 1.00 21.32 ? 360 HIS A CA     1 
ATOM   2710 C C      . HIS A 1 342 ? 29.410 -4.578  -17.258 1.00 28.69 ? 360 HIS A C      1 
ATOM   2711 O O      . HIS A 1 342 ? 30.218 -4.936  -18.130 1.00 26.72 ? 360 HIS A O      1 
ATOM   2712 C CB     . HIS A 1 342 ? 29.538 -5.751  -15.044 1.00 20.87 ? 360 HIS A CB     1 
ATOM   2713 C CG     . HIS A 1 342 ? 30.228 -6.942  -15.622 1.00 36.01 ? 360 HIS A CG     1 
ATOM   2714 N ND1    . HIS A 1 342 ? 29.566 -7.911  -16.348 1.00 41.72 ? 360 HIS A ND1    1 
ATOM   2715 C CD2    . HIS A 1 342 ? 31.535 -7.297  -15.624 1.00 43.26 ? 360 HIS A CD2    1 
ATOM   2716 C CE1    . HIS A 1 342 ? 30.432 -8.824  -16.750 1.00 42.93 ? 360 HIS A CE1    1 
ATOM   2717 N NE2    . HIS A 1 342 ? 31.634 -8.475  -16.326 1.00 44.87 ? 360 HIS A NE2    1 
ATOM   2718 N N      . GLU A 1 343 ? 28.193 -4.215  -17.614 1.00 24.02 ? 361 GLU A N      1 
ATOM   2719 C CA     . GLU A 1 343 ? 27.788 -4.281  -18.990 1.00 16.00 ? 361 GLU A CA     1 
ATOM   2720 C C      . GLU A 1 343 ? 28.416 -3.246  -19.856 1.00 20.50 ? 361 GLU A C      1 
ATOM   2721 O O      . GLU A 1 343 ? 28.746 -3.512  -20.987 1.00 28.98 ? 361 GLU A O      1 
ATOM   2722 C CB     . GLU A 1 343 ? 26.286 -4.204  -19.091 1.00 18.08 ? 361 GLU A CB     1 
ATOM   2723 C CG     . GLU A 1 343 ? 25.688 -5.090  -20.163 1.00 16.31 ? 361 GLU A CG     1 
ATOM   2724 C CD     . GLU A 1 343 ? 24.503 -4.454  -20.840 1.00 21.31 ? 361 GLU A CD     1 
ATOM   2725 O OE1    . GLU A 1 343 ? 23.587 -4.040  -20.131 1.00 21.55 ? 361 GLU A OE1    1 
ATOM   2726 O OE2    . GLU A 1 343 ? 24.482 -4.367  -22.078 1.00 34.00 ? 361 GLU A OE2    1 
ATOM   2727 N N      . LEU A 1 344 ? 28.598 -2.057  -19.335 1.00 21.94 ? 362 LEU A N      1 
ATOM   2728 C CA     . LEU A 1 344 ? 29.147 -0.973  -20.104 1.00 22.28 ? 362 LEU A CA     1 
ATOM   2729 C C      . LEU A 1 344 ? 30.574 -1.239  -20.414 1.00 19.12 ? 362 LEU A C      1 
ATOM   2730 O O      . LEU A 1 344 ? 31.012 -1.052  -21.522 1.00 27.98 ? 362 LEU A O      1 
ATOM   2731 C CB     . LEU A 1 344 ? 28.972 0.334   -19.347 1.00 16.10 ? 362 LEU A CB     1 
ATOM   2732 C CG     . LEU A 1 344 ? 29.694 1.614   -19.757 1.00 15.64 ? 362 LEU A CG     1 
ATOM   2733 C CD1    . LEU A 1 344 ? 28.688 2.613   -20.272 1.00 19.03 ? 362 LEU A CD1    1 
ATOM   2734 C CD2    . LEU A 1 344 ? 30.448 2.204   -18.583 1.00 14.59 ? 362 LEU A CD2    1 
ATOM   2735 N N      . GLN A 1 345 ? 31.309 -1.684  -19.435 1.00 20.63 ? 363 GLN A N      1 
ATOM   2736 C CA     . GLN A 1 345 ? 32.699 -1.962  -19.636 1.00 30.88 ? 363 GLN A CA     1 
ATOM   2737 C C      . GLN A 1 345 ? 32.904 -3.016  -20.694 1.00 31.15 ? 363 GLN A C      1 
ATOM   2738 O O      . GLN A 1 345 ? 33.758 -2.870  -21.552 1.00 32.34 ? 363 GLN A O      1 
ATOM   2739 C CB     . GLN A 1 345 ? 33.342 -2.321  -18.304 1.00 22.78 ? 363 GLN A CB     1 
ATOM   2740 C CG     . GLN A 1 345 ? 33.856 -1.107  -17.549 1.00 25.91 ? 363 GLN A CG     1 
ATOM   2741 C CD     . GLN A 1 345 ? 33.927 -1.319  -16.050 1.00 45.74 ? 363 GLN A CD     1 
ATOM   2742 O OE1    . GLN A 1 345 ? 33.704 -2.421  -15.553 1.00 53.31 ? 363 GLN A OE1    1 
ATOM   2743 N NE2    . GLN A 1 345 ? 34.239 -0.260  -15.320 1.00 28.37 ? 363 GLN A NE2    1 
ATOM   2744 N N      . GLU A 1 346 ? 32.110 -4.058  -20.658 1.00 29.56 ? 364 GLU A N      1 
ATOM   2745 C CA     . GLU A 1 346 ? 32.161 -5.077  -21.660 1.00 35.85 ? 364 GLU A CA     1 
ATOM   2746 C C      . GLU A 1 346 ? 31.858 -4.581  -23.044 1.00 33.58 ? 364 GLU A C      1 
ATOM   2747 O O      . GLU A 1 346 ? 32.499 -5.000  -23.974 1.00 40.05 ? 364 GLU A O      1 
ATOM   2748 C CB     . GLU A 1 346 ? 31.195 -6.167  -21.257 1.00 37.37 ? 364 GLU A CB     1 
ATOM   2749 C CG     . GLU A 1 346 ? 31.790 -7.157  -20.278 1.00 43.56 ? 364 GLU A CG     1 
ATOM   2750 C CD     . GLU A 1 346 ? 32.364 -8.376  -20.965 1.00 57.86 ? 364 GLU A CD     1 
ATOM   2751 O OE1    . GLU A 1 346 ? 33.429 -8.265  -21.601 1.00 51.15 ? 364 GLU A OE1    1 
ATOM   2752 O OE2    . GLU A 1 346 ? 31.746 -9.452  -20.873 1.00 64.74 ? 364 GLU A OE2    1 
ATOM   2753 N N      . ARG A 1 347 ? 30.905 -3.688  -23.194 1.00 32.00 ? 365 ARG A N      1 
ATOM   2754 C CA     . ARG A 1 347 ? 30.577 -3.083  -24.466 1.00 27.10 ? 365 ARG A CA     1 
ATOM   2755 C C      . ARG A 1 347 ? 31.674 -2.226  -25.061 1.00 31.56 ? 365 ARG A C      1 
ATOM   2756 O O      . ARG A 1 347 ? 31.800 -2.099  -26.260 1.00 39.14 ? 365 ARG A O      1 
ATOM   2757 C CB     . ARG A 1 347 ? 29.327 -2.260  -24.237 1.00 28.99 ? 365 ARG A CB     1 
ATOM   2758 C CG     . ARG A 1 347 ? 28.766 -1.488  -25.412 1.00 42.35 ? 365 ARG A CG     1 
ATOM   2759 C CD     . ARG A 1 347 ? 28.716 -0.012  -25.072 1.00 38.61 ? 365 ARG A CD     1 
ATOM   2760 N NE     . ARG A 1 347 ? 28.285 0.804   -26.199 1.00 48.27 ? 365 ARG A NE     1 
ATOM   2761 C CZ     . ARG A 1 347 ? 29.091 1.590   -26.902 1.00 53.38 ? 365 ARG A CZ     1 
ATOM   2762 N NH1    . ARG A 1 347 ? 30.375 1.658   -26.605 1.00 68.13 ? 365 ARG A NH1    1 
ATOM   2763 N NH2    . ARG A 1 347 ? 28.612 2.303   -27.907 1.00 68.13 ? 365 ARG A NH2    1 
ATOM   2764 N N      . PHE A 1 348 ? 32.496 -1.650  -24.231 1.00 32.74 ? 366 PHE A N      1 
ATOM   2765 C CA     . PHE A 1 348 ? 33.530 -0.785  -24.715 1.00 38.70 ? 366 PHE A CA     1 
ATOM   2766 C C      . PHE A 1 348 ? 34.745 -1.576  -25.030 1.00 43.67 ? 366 PHE A C      1 
ATOM   2767 O O      . PHE A 1 348 ? 35.611 -1.127  -25.741 1.00 44.24 ? 366 PHE A O      1 
ATOM   2768 C CB     . PHE A 1 348 ? 33.846 0.267   -23.673 1.00 39.95 ? 366 PHE A CB     1 
ATOM   2769 C CG     . PHE A 1 348 ? 33.062 1.519   -23.840 1.00 38.96 ? 366 PHE A CG     1 
ATOM   2770 C CD1    . PHE A 1 348 ? 31.852 1.678   -23.204 1.00 28.28 ? 366 PHE A CD1    1 
ATOM   2771 C CD2    . PHE A 1 348 ? 33.532 2.530   -24.649 1.00 42.59 ? 366 PHE A CD2    1 
ATOM   2772 C CE1    . PHE A 1 348 ? 31.121 2.826   -23.368 1.00 33.02 ? 366 PHE A CE1    1 
ATOM   2773 C CE2    . PHE A 1 348 ? 32.812 3.683   -24.815 1.00 32.47 ? 366 PHE A CE2    1 
ATOM   2774 C CZ     . PHE A 1 348 ? 31.603 3.829   -24.176 1.00 48.13 ? 366 PHE A CZ     1 
ATOM   2775 N N      . LYS A 1 349 ? 34.803 -2.783  -24.508 1.00 45.77 ? 367 LYS A N      1 
ATOM   2776 C CA     . LYS A 1 349 ? 35.922 -3.647  -24.762 1.00 44.90 ? 367 LYS A CA     1 
ATOM   2777 C C      . LYS A 1 349 ? 35.679 -4.416  -26.022 1.00 50.34 ? 367 LYS A C      1 
ATOM   2778 O O      . LYS A 1 349 ? 36.548 -5.114  -26.501 1.00 56.16 ? 367 LYS A O      1 
ATOM   2779 C CB     . LYS A 1 349 ? 36.088 -4.614  -23.616 1.00 44.36 ? 367 LYS A CB     1 
ATOM   2780 C CG     . LYS A 1 349 ? 37.011 -4.093  -22.533 1.00 56.63 ? 367 LYS A CG     1 
ATOM   2781 C CD     . LYS A 1 349 ? 36.680 -4.689  -21.179 1.00 57.67 ? 367 LYS A CD     1 
ATOM   2782 C CE     . LYS A 1 349 ? 36.013 -6.040  -21.333 1.00 57.23 ? 367 LYS A CE     1 
ATOM   2783 N NZ     . LYS A 1 349 ? 35.459 -6.526  -20.041 1.00 58.35 ? 367 LYS A NZ     1 
ATOM   2784 N N      . ASN A 1 350 ? 34.488 -4.305  -26.563 1.00 41.47 ? 368 ASN A N      1 
ATOM   2785 C CA     . ASN A 1 350 ? 34.206 -4.977  -27.778 1.00 52.47 ? 368 ASN A CA     1 
ATOM   2786 C C      . ASN A 1 350 ? 34.097 -3.977  -28.920 1.00 60.44 ? 368 ASN A C      1 
ATOM   2787 O O      . ASN A 1 350 ? 33.752 -4.339  -30.038 1.00 60.22 ? 368 ASN A O      1 
ATOM   2788 C CB     . ASN A 1 350 ? 33.050 -5.996  -27.643 1.00 41.09 ? 368 ASN A CB     1 
ATOM   2789 C CG     . ASN A 1 350 ? 31.703 -5.382  -27.349 1.00 41.44 ? 368 ASN A CG     1 
ATOM   2790 O OD1    . ASN A 1 350 ? 31.263 -4.437  -27.994 1.00 50.78 ? 368 ASN A OD1    1 
ATOM   2791 N ND2    . ASN A 1 350 ? 30.997 -5.985  -26.406 1.00 39.18 ? 368 ASN A ND2    1 
ATOM   2792 N N      . LYS A 1 351 ? 34.442 -2.735  -28.655 1.00 51.56 ? 369 LYS A N      1 
ATOM   2793 C CA     . LYS A 1 351 ? 34.356 -1.703  -29.649 1.00 51.00 ? 369 LYS A CA     1 
ATOM   2794 C C      . LYS A 1 351 ? 35.689 -1.012  -29.665 1.00 71.68 ? 369 LYS A C      1 
ATOM   2795 O O      . LYS A 1 351 ? 35.994 -0.263  -30.592 1.00 73.31 ? 369 LYS A O      1 
ATOM   2796 C CB     . LYS A 1 351 ? 33.338 -0.690  -29.190 1.00 54.03 ? 369 LYS A CB     1 
ATOM   2797 C CG     . LYS A 1 351 ? 31.929 -0.931  -29.693 1.00 69.68 ? 369 LYS A CG     1 
ATOM   2798 C CD     . LYS A 1 351 ? 31.244 0.387   -30.005 1.00 66.14 ? 369 LYS A CD     1 
ATOM   2799 C CE     . LYS A 1 351 ? 32.215 1.549   -29.867 1.00 61.22 ? 369 LYS A CE     1 
ATOM   2800 N NZ     . LYS A 1 351 ? 32.016 2.582   -30.920 1.00 66.24 ? 369 LYS A NZ     1 
ATOM   2801 N N      . GLU A 1 352 ? 36.499 -1.252  -28.644 1.00 73.19 ? 370 GLU A N      1 
ATOM   2802 C CA     . GLU A 1 352 ? 37.804 -0.587  -28.511 1.00 74.09 ? 370 GLU A CA     1 
ATOM   2803 C C      . GLU A 1 352 ? 38.691 -0.698  -29.756 1.00 75.18 ? 370 GLU A C      1 
ATOM   2804 O O      . GLU A 1 352 ? 39.276 0.295   -30.212 1.00 70.15 ? 370 GLU A O      1 
ATOM   2805 C CB     . GLU A 1 352 ? 38.553 -1.150  -27.286 1.00 76.74 ? 370 GLU A CB     1 
ATOM   2806 C CG     . GLU A 1 352 ? 39.799 -0.370  -26.853 1.00 82.63 ? 370 GLU A CG     1 
ATOM   2807 C CD     . GLU A 1 352 ? 39.495 1.057   -26.423 1.00 83.80 ? 370 GLU A CD     1 
ATOM   2808 O OE1    . GLU A 1 352 ? 38.328 1.356   -26.099 1.00 80.79 ? 370 GLU A OE1    1 
ATOM   2809 O OE2    . GLU A 1 352 ? 40.428 1.886   -26.404 1.00 84.81 ? 370 GLU A OE2    1 
ATOM   2810 N N      . MET B 2 1   ? 57.425 34.299  25.695  1.00 51.09 ? 1   MET C N      1 
ATOM   2811 C CA     . MET B 2 1   ? 56.610 33.842  26.804  1.00 54.27 ? 1   MET C CA     1 
ATOM   2812 C C      . MET B 2 1   ? 57.176 32.652  27.528  1.00 55.37 ? 1   MET C C      1 
ATOM   2813 O O      . MET B 2 1   ? 58.135 32.051  27.076  1.00 60.88 ? 1   MET C O      1 
ATOM   2814 C CB     . MET B 2 1   ? 55.194 33.521  26.350  1.00 48.37 ? 1   MET C CB     1 
ATOM   2815 C CG     . MET B 2 1   ? 54.653 34.403  25.264  1.00 51.91 ? 1   MET C CG     1 
ATOM   2816 S SD     . MET B 2 1   ? 52.869 34.330  25.366  1.00 69.41 ? 1   MET C SD     1 
ATOM   2817 C CE     . MET B 2 1   ? 52.538 32.739  24.628  1.00 57.89 ? 1   MET C CE     1 
ATOM   2818 N N      . GLN B 2 2   ? 56.577 32.315  28.657  1.00 61.76 ? 2   GLN C N      1 
ATOM   2819 C CA     . GLN B 2 2   ? 57.017 31.176  29.414  1.00 53.46 ? 2   GLN C CA     1 
ATOM   2820 C C      . GLN B 2 2   ? 55.756 30.527  29.901  1.00 56.23 ? 2   GLN C C      1 
ATOM   2821 O O      . GLN B 2 2   ? 55.141 31.022  30.827  1.00 53.56 ? 2   GLN C O      1 
ATOM   2822 C CB     . GLN B 2 2   ? 57.931 31.602  30.547  1.00 45.61 ? 2   GLN C CB     1 
ATOM   2823 C CG     . GLN B 2 2   ? 58.334 30.502  31.492  1.00 52.28 ? 2   GLN C CG     1 
ATOM   2824 C CD     . GLN B 2 2   ? 59.608 30.818  32.248  1.00 63.68 ? 2   GLN C CD     1 
ATOM   2825 O OE1    . GLN B 2 2   ? 59.625 30.835  33.478  1.00 61.11 ? 2   GLN C OE1    1 
ATOM   2826 N NE2    . GLN B 2 2   ? 60.684 31.064  31.515  1.00 51.41 ? 2   GLN C NE2    1 
ATOM   2827 N N      . ILE B 2 3   ? 55.341 29.438  29.252  1.00 56.67 ? 3   ILE C N      1 
ATOM   2828 C CA     . ILE B 2 3   ? 54.162 28.711  29.665  1.00 40.64 ? 3   ILE C CA     1 
ATOM   2829 C C      . ILE B 2 3   ? 54.540 27.527  30.502  1.00 40.49 ? 3   ILE C C      1 
ATOM   2830 O O      . ILE B 2 3   ? 55.700 27.188  30.610  1.00 41.29 ? 3   ILE C O      1 
ATOM   2831 C CB     . ILE B 2 3   ? 53.283 28.299  28.489  1.00 39.54 ? 3   ILE C CB     1 
ATOM   2832 C CG1    . ILE B 2 3   ? 53.983 27.285  27.594  1.00 39.29 ? 3   ILE C CG1    1 
ATOM   2833 C CG2    . ILE B 2 3   ? 52.866 29.523  27.695  1.00 40.68 ? 3   ILE C CG2    1 
ATOM   2834 C CD1    . ILE B 2 3   ? 53.059 26.679  26.568  1.00 30.09 ? 3   ILE C CD1    1 
ATOM   2835 N N      . PHE B 2 4   ? 53.561 26.937  31.155  1.00 43.90 ? 4   PHE C N      1 
ATOM   2836 C CA     . PHE B 2 4   ? 53.812 25.815  32.034  1.00 41.74 ? 4   PHE C CA     1 
ATOM   2837 C C      . PHE B 2 4   ? 52.900 24.681  31.632  1.00 36.69 ? 4   PHE C C      1 
ATOM   2838 O O      . PHE B 2 4   ? 51.793 24.928  31.266  1.00 33.29 ? 4   PHE C O      1 
ATOM   2839 C CB     . PHE B 2 4   ? 53.600 26.209  33.489  1.00 40.16 ? 4   PHE C CB     1 
ATOM   2840 C CG     . PHE B 2 4   ? 54.384 27.407  33.919  1.00 43.36 ? 4   PHE C CG     1 
ATOM   2841 C CD1    . PHE B 2 4   ? 53.859 28.682  33.795  1.00 41.31 ? 4   PHE C CD1    1 
ATOM   2842 C CD2    . PHE B 2 4   ? 55.642 27.257  34.457  1.00 40.23 ? 4   PHE C CD2    1 
ATOM   2843 C CE1    . PHE B 2 4   ? 54.587 29.781  34.178  1.00 48.18 ? 4   PHE C CE1    1 
ATOM   2844 C CE2    . PHE B 2 4   ? 56.373 28.354  34.854  1.00 47.60 ? 4   PHE C CE2    1 
ATOM   2845 C CZ     . PHE B 2 4   ? 55.847 29.617  34.712  1.00 50.73 ? 4   PHE C CZ     1 
ATOM   2846 N N      . VAL B 2 5   ? 53.378 23.447  31.656  1.00 37.73 ? 5   VAL C N      1 
ATOM   2847 C CA     . VAL B 2 5   ? 52.625 22.277  31.212  1.00 30.83 ? 5   VAL C CA     1 
ATOM   2848 C C      . VAL B 2 5   ? 52.677 21.244  32.323  1.00 32.13 ? 5   VAL C C      1 
ATOM   2849 O O      . VAL B 2 5   ? 53.754 20.956  32.858  1.00 34.20 ? 5   VAL C O      1 
ATOM   2850 C CB     . VAL B 2 5   ? 53.186 21.708  29.901  1.00 28.03 ? 5   VAL C CB     1 
ATOM   2851 C CG1    . VAL B 2 5   ? 52.565 20.356  29.608  1.00 32.49 ? 5   VAL C CG1    1 
ATOM   2852 C CG2    . VAL B 2 5   ? 52.920 22.680  28.773  1.00 24.95 ? 5   VAL C CG2    1 
ATOM   2853 N N      . LYS B 2 6   ? 51.519 20.698  32.682  1.00 28.78 ? 6   LYS C N      1 
ATOM   2854 C CA     . LYS B 2 6   ? 51.383 19.944  33.920  1.00 27.82 ? 6   LYS C CA     1 
ATOM   2855 C C      . LYS B 2 6   ? 50.977 18.511  33.621  1.00 25.52 ? 6   LYS C C      1 
ATOM   2856 O O      . LYS B 2 6   ? 49.960 18.267  32.963  1.00 30.34 ? 6   LYS C O      1 
ATOM   2857 C CB     . LYS B 2 6   ? 50.378 20.623  34.847  1.00 32.74 ? 6   LYS C CB     1 
ATOM   2858 C CG     . LYS B 2 6   ? 50.506 20.178  36.277  1.00 38.34 ? 6   LYS C CG     1 
ATOM   2859 C CD     . LYS B 2 6   ? 50.272 21.315  37.253  1.00 46.11 ? 6   LYS C CD     1 
ATOM   2860 C CE     . LYS B 2 6   ? 49.720 20.770  38.568  1.00 49.71 ? 6   LYS C CE     1 
ATOM   2861 N NZ     . LYS B 2 6   ? 48.354 20.183  38.367  1.00 38.21 ? 6   LYS C NZ     1 
ATOM   2862 N N      . THR B 2 7   ? 51.768 17.572  34.102  1.00 23.92 ? 7   THR C N      1 
ATOM   2863 C CA     . THR B 2 7   ? 51.450 16.175  33.874  1.00 30.24 ? 7   THR C CA     1 
ATOM   2864 C C      . THR B 2 7   ? 50.562 15.666  35.000  1.00 30.19 ? 7   THR C C      1 
ATOM   2865 O O      . THR B 2 7   ? 50.582 16.185  36.119  1.00 26.86 ? 7   THR C O      1 
ATOM   2866 C CB     . THR B 2 7   ? 52.718 15.313  33.780  1.00 30.55 ? 7   THR C CB     1 
ATOM   2867 O OG1    . THR B 2 7   ? 53.300 15.152  35.082  1.00 28.87 ? 7   THR C OG1    1 
ATOM   2868 C CG2    . THR B 2 7   ? 53.713 15.955  32.854  1.00 23.66 ? 7   THR C CG2    1 
ATOM   2869 N N      . LEU B 2 8   ? 49.794 14.617  34.692  1.00 23.70 ? 8   LEU C N      1 
ATOM   2870 C CA     . LEU B 2 8   ? 48.935 14.003  35.696  1.00 18.57 ? 8   LEU C CA     1 
ATOM   2871 C C      . LEU B 2 8   ? 49.656 13.749  37.014  1.00 28.10 ? 8   LEU C C      1 
ATOM   2872 O O      . LEU B 2 8   ? 48.993 13.638  38.060  1.00 31.54 ? 8   LEU C O      1 
ATOM   2873 C CB     . LEU B 2 8   ? 48.369 12.697  35.157  1.00 23.01 ? 8   LEU C CB     1 
ATOM   2874 C CG     . LEU B 2 8   ? 47.104 12.776  34.322  1.00 19.56 ? 8   LEU C CG     1 
ATOM   2875 C CD1    . LEU B 2 8   ? 47.206 13.894  33.320  1.00 22.65 ? 8   LEU C CD1    1 
ATOM   2876 C CD2    . LEU B 2 8   ? 46.984 11.463  33.636  1.00 16.78 ? 8   LEU C CD2    1 
ATOM   2877 N N      . THR B 2 9   ? 50.994 13.621  36.981  1.00 29.80 ? 9   THR C N      1 
ATOM   2878 C CA     . THR B 2 9   ? 51.762 13.504  38.215  1.00 23.64 ? 9   THR C CA     1 
ATOM   2879 C C      . THR B 2 9   ? 51.705 14.782  39.038  1.00 21.00 ? 9   THR C C      1 
ATOM   2880 O O      . THR B 2 9   ? 51.771 14.734  40.270  1.00 17.75 ? 9   THR C O      1 
ATOM   2881 C CB     . THR B 2 9   ? 53.214 13.181  37.901  1.00 25.77 ? 9   THR C CB     1 
ATOM   2882 O OG1    . THR B 2 9   ? 53.336 11.787  37.621  1.00 32.28 ? 9   THR C OG1    1 
ATOM   2883 C CG2    . THR B 2 9   ? 54.082 13.533  39.068  1.00 32.82 ? 9   THR C CG2    1 
ATOM   2884 N N      . GLY B 2 10  ? 51.565 15.924  38.378  1.00 26.12 ? 10  GLY C N      1 
ATOM   2885 C CA     . GLY B 2 10  ? 51.721 17.223  38.993  1.00 28.97 ? 10  GLY C CA     1 
ATOM   2886 C C      . GLY B 2 10  ? 53.012 17.925  38.615  1.00 33.61 ? 10  GLY C C      1 
ATOM   2887 O O      . GLY B 2 10  ? 53.124 19.143  38.815  1.00 36.34 ? 10  GLY C O      1 
ATOM   2888 N N      . LYS B 2 11  ? 53.914 17.209  37.971  1.00 27.53 ? 11  LYS C N      1 
ATOM   2889 C CA     . LYS B 2 11  ? 55.159 17.775  37.558  1.00 27.01 ? 11  LYS C CA     1 
ATOM   2890 C C      . LYS B 2 11  ? 54.972 18.864  36.535  1.00 36.04 ? 11  LYS C C      1 
ATOM   2891 O O      . LYS B 2 11  ? 54.025 18.844  35.768  1.00 28.59 ? 11  LYS C O      1 
ATOM   2892 C CB     . LYS B 2 11  ? 56.139 16.694  37.170  1.00 30.56 ? 11  LYS C CB     1 
ATOM   2893 C CG     . LYS B 2 11  ? 56.913 16.167  38.361  1.00 31.10 ? 11  LYS C CG     1 
ATOM   2894 C CD     . LYS B 2 11  ? 57.399 14.749  38.151  1.00 47.40 ? 11  LYS C CD     1 
ATOM   2895 C CE     . LYS B 2 11  ? 57.738 14.105  39.484  1.00 50.13 ? 11  LYS C CE     1 
ATOM   2896 N NZ     . LYS B 2 11  ? 57.458 12.645  39.488  1.00 47.74 ? 11  LYS C NZ     1 
ATOM   2897 N N      . THR B 2 12  ? 55.901 19.808  36.497  1.00 38.48 ? 12  THR C N      1 
ATOM   2898 C CA     . THR B 2 12  ? 55.686 20.987  35.668  1.00 32.36 ? 12  THR C CA     1 
ATOM   2899 C C      . THR B 2 12  ? 56.837 21.176  34.690  1.00 37.05 ? 12  THR C C      1 
ATOM   2900 O O      . THR B 2 12  ? 57.979 21.410  35.097  1.00 45.22 ? 12  THR C O      1 
ATOM   2901 C CB     . THR B 2 12  ? 55.520 22.230  36.533  1.00 28.31 ? 12  THR C CB     1 
ATOM   2902 O OG1    . THR B 2 12  ? 54.479 21.988  37.485  1.00 38.29 ? 12  THR C OG1    1 
ATOM   2903 C CG2    . THR B 2 12  ? 55.150 23.437  35.666  1.00 29.59 ? 12  THR C CG2    1 
ATOM   2904 N N      . ILE B 2 13  ? 56.515 21.108  33.407  1.00 39.73 ? 13  ILE C N      1 
ATOM   2905 C CA     . ILE B 2 13  ? 57.431 21.460  32.332  1.00 34.63 ? 13  ILE C CA     1 
ATOM   2906 C C      . ILE B 2 13  ? 57.280 22.950  32.050  1.00 36.39 ? 13  ILE C C      1 
ATOM   2907 O O      . ILE B 2 13  ? 56.182 23.421  31.731  1.00 36.65 ? 13  ILE C O      1 
ATOM   2908 C CB     . ILE B 2 13  ? 57.132 20.641  31.072  1.00 29.94 ? 13  ILE C CB     1 
ATOM   2909 C CG1    . ILE B 2 13  ? 57.023 19.159  31.429  1.00 36.95 ? 13  ILE C CG1    1 
ATOM   2910 C CG2    . ILE B 2 13  ? 58.191 20.888  30.027  1.00 31.19 ? 13  ILE C CG2    1 
ATOM   2911 C CD1    . ILE B 2 13  ? 56.300 18.321  30.382  1.00 41.17 ? 13  ILE C CD1    1 
ATOM   2912 N N      . THR B 2 14  ? 58.369 23.684  32.143  1.00 35.76 ? 14  THR C N      1 
ATOM   2913 C CA     . THR B 2 14  ? 58.342 25.083  31.822  1.00 40.40 ? 14  THR C CA     1 
ATOM   2914 C C      . THR B 2 14  ? 58.935 25.250  30.433  1.00 37.93 ? 14  THR C C      1 
ATOM   2915 O O      . THR B 2 14  ? 59.989 24.733  30.150  1.00 39.57 ? 14  THR C O      1 
ATOM   2916 C CB     . THR B 2 14  ? 59.153 25.841  32.871  1.00 40.81 ? 14  THR C CB     1 
ATOM   2917 O OG1    . THR B 2 14  ? 58.565 25.653  34.159  1.00 45.52 ? 14  THR C OG1    1 
ATOM   2918 C CG2    . THR B 2 14  ? 59.207 27.296  32.552  1.00 44.89 ? 14  THR C CG2    1 
ATOM   2919 N N      . LEU B 2 15  ? 58.264 25.972  29.565  1.00 35.73 ? 15  LEU C N      1 
ATOM   2920 C CA     . LEU B 2 15  ? 58.723 26.141  28.211  1.00 36.77 ? 15  LEU C CA     1 
ATOM   2921 C C      . LEU B 2 15  ? 58.898 27.586  27.822  1.00 52.35 ? 15  LEU C C      1 
ATOM   2922 O O      . LEU B 2 15  ? 58.312 28.459  28.419  1.00 56.01 ? 15  LEU C O      1 
ATOM   2923 C CB     . LEU B 2 15  ? 57.687 25.582  27.264  1.00 44.07 ? 15  LEU C CB     1 
ATOM   2924 C CG     . LEU B 2 15  ? 57.828 24.273  26.481  1.00 48.13 ? 15  LEU C CG     1 
ATOM   2925 C CD1    . LEU B 2 15  ? 58.345 23.129  27.321  1.00 30.72 ? 15  LEU C CD1    1 
ATOM   2926 C CD2    . LEU B 2 15  ? 56.509 23.901  25.831  1.00 26.12 ? 15  LEU C CD2    1 
ATOM   2927 N N      . GLU B 2 16  ? 59.715 27.847  26.812  1.00 60.47 ? 16  GLU C N      1 
ATOM   2928 C CA     . GLU B 2 16  ? 59.907 29.196  26.298  1.00 52.86 ? 16  GLU C CA     1 
ATOM   2929 C C      . GLU B 2 16  ? 59.150 29.182  25.018  1.00 50.59 ? 16  GLU C C      1 
ATOM   2930 O O      . GLU B 2 16  ? 59.313 28.271  24.236  1.00 50.66 ? 16  GLU C O      1 
ATOM   2931 C CB     . GLU B 2 16  ? 61.372 29.429  26.039  1.00 54.96 ? 16  GLU C CB     1 
ATOM   2932 C CG     . GLU B 2 16  ? 62.298 28.918  27.138  1.00 57.40 ? 16  GLU C CG     1 
ATOM   2933 C CD     . GLU B 2 16  ? 62.269 29.770  28.392  1.00 59.30 ? 16  GLU C CD     1 
ATOM   2934 O OE1    . GLU B 2 16  ? 61.752 30.902  28.338  1.00 64.28 ? 16  GLU C OE1    1 
ATOM   2935 O OE2    . GLU B 2 16  ? 62.778 29.312  29.434  1.00 50.12 ? 16  GLU C OE2    1 
ATOM   2936 N N      . VAL B 2 17  ? 58.323 30.177  24.778  1.00 50.54 ? 17  VAL C N      1 
ATOM   2937 C CA     . VAL B 2 17  ? 57.444 30.115  23.634  1.00 51.61 ? 17  VAL C CA     1 
ATOM   2938 C C      . VAL B 2 17  ? 57.030 31.466  23.101  1.00 51.72 ? 17  VAL C C      1 
ATOM   2939 O O      . VAL B 2 17  ? 57.341 32.484  23.692  1.00 47.56 ? 17  VAL C O      1 
ATOM   2940 C CB     . VAL B 2 17  ? 56.194 29.279  24.021  1.00 58.42 ? 17  VAL C CB     1 
ATOM   2941 C CG1    . VAL B 2 17  ? 55.169 30.107  24.764  1.00 58.30 ? 17  VAL C CG1    1 
ATOM   2942 C CG2    . VAL B 2 17  ? 55.595 28.539  22.837  1.00 52.37 ? 17  VAL C CG2    1 
ATOM   2943 N N      . GLU B 2 18  ? 56.372 31.475  21.953  1.00 47.45 ? 18  GLU C N      1 
ATOM   2944 C CA     . GLU B 2 18  ? 55.916 32.700  21.349  1.00 47.90 ? 18  GLU C CA     1 
ATOM   2945 C C      . GLU B 2 18  ? 54.467 32.539  20.955  1.00 46.87 ? 18  GLU C C      1 
ATOM   2946 O O      . GLU B 2 18  ? 54.041 31.442  20.660  1.00 50.86 ? 18  GLU C O      1 
ATOM   2947 C CB     . GLU B 2 18  ? 56.748 33.000  20.094  1.00 51.98 ? 18  GLU C CB     1 
ATOM   2948 C CG     . GLU B 2 18  ? 58.257 33.031  20.276  1.00 38.55 ? 18  GLU C CG     1 
ATOM   2949 C CD     . GLU B 2 18  ? 58.734 34.257  21.020  1.00 48.96 ? 18  GLU C CD     1 
ATOM   2950 O OE1    . GLU B 2 18  ? 57.946 35.205  21.170  1.00 57.12 ? 18  GLU C OE1    1 
ATOM   2951 O OE2    . GLU B 2 18  ? 59.901 34.278  21.453  1.00 48.16 ? 18  GLU C OE2    1 
ATOM   2952 N N      . PRO B 2 19  ? 53.695 33.630  20.972  1.00 51.95 ? 19  PRO C N      1 
ATOM   2953 C CA     . PRO B 2 19  ? 52.287 33.587  20.591  1.00 45.67 ? 19  PRO C CA     1 
ATOM   2954 C C      . PRO B 2 19  ? 52.208 33.189  19.177  1.00 48.32 ? 19  PRO C C      1 
ATOM   2955 O O      . PRO B 2 19  ? 51.158 32.760  18.758  1.00 48.61 ? 19  PRO C O      1 
ATOM   2956 C CB     . PRO B 2 19  ? 51.849 35.017  20.736  1.00 50.88 ? 19  PRO C CB     1 
ATOM   2957 C CG     . PRO B 2 19  ? 52.772 35.615  21.733  1.00 55.02 ? 19  PRO C CG     1 
ATOM   2958 C CD     . PRO B 2 19  ? 54.088 34.952  21.486  1.00 57.94 ? 19  PRO C CD     1 
ATOM   2959 N N      . SER B 2 20  ? 53.277 33.378  18.426  1.00 56.52 ? 20  SER C N      1 
ATOM   2960 C CA     . SER B 2 20  ? 53.352 32.892  17.055  1.00 55.21 ? 20  SER C CA     1 
ATOM   2961 C C      . SER B 2 20  ? 53.189 31.375  16.993  1.00 48.70 ? 20  SER C C      1 
ATOM   2962 O O      . SER B 2 20  ? 52.499 30.858  16.103  1.00 47.31 ? 20  SER C O      1 
ATOM   2963 C CB     . SER B 2 20  ? 54.692 33.328  16.449  1.00 47.45 ? 20  SER C CB     1 
ATOM   2964 O OG     . SER B 2 20  ? 54.898 32.781  15.159  1.00 59.21 ? 20  SER C OG     1 
ATOM   2965 N N      . ASP B 2 21  ? 53.793 30.654  17.946  1.00 45.02 ? 21  ASP C N      1 
ATOM   2966 C CA     . ASP B 2 21  ? 54.013 29.217  17.795  1.00 41.15 ? 21  ASP C CA     1 
ATOM   2967 C C      . ASP B 2 21  ? 52.706 28.428  17.821  1.00 41.21 ? 21  ASP C C      1 
ATOM   2968 O O      . ASP B 2 21  ? 51.811 28.693  18.623  1.00 48.61 ? 21  ASP C O      1 
ATOM   2969 C CB     . ASP B 2 21  ? 54.952 28.700  18.886  1.00 44.89 ? 21  ASP C CB     1 
ATOM   2970 C CG     . ASP B 2 21  ? 56.361 29.266  18.772  1.00 52.93 ? 21  ASP C CG     1 
ATOM   2971 O OD1    . ASP B 2 21  ? 56.748 29.688  17.651  1.00 47.29 ? 21  ASP C OD1    1 
ATOM   2972 O OD2    . ASP B 2 21  ? 57.082 29.282  19.807  1.00 44.62 ? 21  ASP C OD2    1 
ATOM   2973 N N      . THR B 2 22  ? 52.607 27.442  16.937  1.00 42.74 ? 22  THR C N      1 
ATOM   2974 C CA     . THR B 2 22  ? 51.434 26.593  16.797  1.00 41.68 ? 22  THR C CA     1 
ATOM   2975 C C      . THR B 2 22  ? 51.411 25.529  17.906  1.00 41.72 ? 22  THR C C      1 
ATOM   2976 O O      . THR B 2 22  ? 52.349 25.400  18.699  1.00 33.97 ? 22  THR C O      1 
ATOM   2977 C CB     . THR B 2 22  ? 51.430 25.959  15.397  1.00 41.44 ? 22  THR C CB     1 
ATOM   2978 O OG1    . THR B 2 22  ? 50.220 25.219  15.195  1.00 51.54 ? 22  THR C OG1    1 
ATOM   2979 C CG2    . THR B 2 22  ? 52.640 25.033  15.203  1.00 41.19 ? 22  THR C CG2    1 
ATOM   2980 N N      . ILE B 2 23  ? 50.316 24.758  17.973  1.00 43.11 ? 23  ILE C N      1 
ATOM   2981 C CA     . ILE B 2 23  ? 50.271 23.655  18.936  1.00 44.56 ? 23  ILE C CA     1 
ATOM   2982 C C      . ILE B 2 23  ? 51.251 22.563  18.533  1.00 34.12 ? 23  ILE C C      1 
ATOM   2983 O O      . ILE B 2 23  ? 51.966 22.018  19.380  1.00 28.33 ? 23  ILE C O      1 
ATOM   2984 C CB     . ILE B 2 23  ? 48.843 23.102  19.098  1.00 43.16 ? 23  ILE C CB     1 
ATOM   2985 C CG1    . ILE B 2 23  ? 48.062 23.941  20.108  1.00 42.69 ? 23  ILE C CG1    1 
ATOM   2986 C CG2    . ILE B 2 23  ? 48.890 21.672  19.613  1.00 41.39 ? 23  ILE C CG2    1 
ATOM   2987 C CD1    . ILE B 2 23  ? 47.818 25.365  19.686  1.00 42.26 ? 23  ILE C CD1    1 
ATOM   2988 N N      . GLU B 2 24  ? 51.305 22.235  17.234  1.00 36.49 ? 24  GLU C N      1 
ATOM   2989 C CA     . GLU B 2 24  ? 52.335 21.331  16.725  1.00 37.01 ? 24  GLU C CA     1 
ATOM   2990 C C      . GLU B 2 24  ? 53.716 21.755  17.207  1.00 33.12 ? 24  GLU C C      1 
ATOM   2991 O O      . GLU B 2 24  ? 54.519 20.931  17.662  1.00 30.74 ? 24  GLU C O      1 
ATOM   2992 C CB     . GLU B 2 24  ? 52.290 21.284  15.194  1.00 34.37 ? 24  GLU C CB     1 
ATOM   2993 C CG     . GLU B 2 24  ? 51.137 20.446  14.630  1.00 45.43 ? 24  GLU C CG     1 
ATOM   2994 C CD     . GLU B 2 24  ? 50.385 21.130  13.483  1.00 64.69 ? 24  GLU C CD     1 
ATOM   2995 O OE1    . GLU B 2 24  ? 50.550 22.357  13.290  1.00 63.41 ? 24  GLU C OE1    1 
ATOM   2996 O OE2    . GLU B 2 24  ? 49.618 20.440  12.771  1.00 63.68 ? 24  GLU C OE2    1 
ATOM   2997 N N      . ASN B 2 25  ? 54.006 23.049  17.116  1.00 34.73 ? 25  ASN C N      1 
ATOM   2998 C CA     . ASN B 2 25  ? 55.286 23.535  17.599  1.00 36.05 ? 25  ASN C CA     1 
ATOM   2999 C C      . ASN B 2 25  ? 55.470 23.211  19.077  1.00 33.67 ? 25  ASN C C      1 
ATOM   3000 O O      . ASN B 2 25  ? 56.559 22.805  19.498  1.00 33.99 ? 25  ASN C O      1 
ATOM   3001 C CB     . ASN B 2 25  ? 55.391 25.042  17.346  1.00 42.18 ? 25  ASN C CB     1 
ATOM   3002 C CG     . ASN B 2 25  ? 56.586 25.415  16.497  1.00 43.19 ? 25  ASN C CG     1 
ATOM   3003 O OD1    . ASN B 2 25  ? 57.672 24.830  16.630  1.00 51.93 ? 25  ASN C OD1    1 
ATOM   3004 N ND2    . ASN B 2 25  ? 56.405 26.407  15.630  1.00 49.60 ? 25  ASN C ND2    1 
ATOM   3005 N N      . VAL B 2 26  ? 54.412 23.385  19.880  1.00 32.56 ? 26  VAL C N      1 
ATOM   3006 C CA     . VAL B 2 26  ? 54.523 23.215  21.328  1.00 24.35 ? 26  VAL C CA     1 
ATOM   3007 C C      . VAL B 2 26  ? 54.854 21.772  21.675  1.00 26.99 ? 26  VAL C C      1 
ATOM   3008 O O      . VAL B 2 26  ? 55.756 21.503  22.477  1.00 25.77 ? 26  VAL C O      1 
ATOM   3009 C CB     . VAL B 2 26  ? 53.224 23.658  22.028  1.00 30.25 ? 26  VAL C CB     1 
ATOM   3010 C CG1    . VAL B 2 26  ? 53.390 23.608  23.544  1.00 27.62 ? 26  VAL C CG1    1 
ATOM   3011 C CG2    . VAL B 2 26  ? 52.818 25.034  21.569  1.00 33.64 ? 26  VAL C CG2    1 
ATOM   3012 N N      . LYS B 2 27  ? 54.109 20.825  21.090  1.00 26.40 ? 27  LYS C N      1 
ATOM   3013 C CA     . LYS B 2 27  ? 54.351 19.408  21.341  1.00 21.83 ? 27  LYS C CA     1 
ATOM   3014 C C      . LYS B 2 27  ? 55.773 19.028  20.958  1.00 24.13 ? 27  LYS C C      1 
ATOM   3015 O O      . LYS B 2 27  ? 56.460 18.311  21.697  1.00 24.05 ? 27  LYS C O      1 
ATOM   3016 C CB     . LYS B 2 27  ? 53.339 18.555  20.570  1.00 20.23 ? 27  LYS C CB     1 
ATOM   3017 C CG     . LYS B 2 27  ? 51.887 18.880  20.878  1.00 20.39 ? 27  LYS C CG     1 
ATOM   3018 C CD     . LYS B 2 27  ? 50.957 18.198  19.924  1.00 18.94 ? 27  LYS C CD     1 
ATOM   3019 C CE     . LYS B 2 27  ? 49.577 18.078  20.526  1.00 22.52 ? 27  LYS C CE     1 
ATOM   3020 N NZ     . LYS B 2 27  ? 48.751 17.138  19.710  1.00 20.46 ? 27  LYS C NZ     1 
ATOM   3021 N N      . ALA B 2 28  ? 56.299 19.541  19.871  1.00 30.63 ? 28  ALA C N      1 
ATOM   3022 C CA     . ALA B 2 28  ? 57.704 19.309  19.528  1.00 23.86 ? 28  ALA C CA     1 
ATOM   3023 C C      . ALA B 2 28  ? 58.662 19.726  20.610  1.00 23.19 ? 28  ALA C C      1 
ATOM   3024 O O      . ALA B 2 28  ? 59.659 19.068  20.832  1.00 25.73 ? 28  ALA C O      1 
ATOM   3025 C CB     . ALA B 2 28  ? 58.049 20.015  18.261  1.00 17.09 ? 28  ALA C CB     1 
ATOM   3026 N N      . LYS B 2 29  ? 58.354 20.803  21.306  1.00 24.34 ? 29  LYS C N      1 
ATOM   3027 C CA     . LYS B 2 29  ? 59.228 21.298  22.348  1.00 30.95 ? 29  LYS C CA     1 
ATOM   3028 C C      . LYS B 2 29  ? 59.100 20.440  23.565  1.00 31.94 ? 29  LYS C C      1 
ATOM   3029 O O      . LYS B 2 29  ? 59.985 20.407  24.397  1.00 31.88 ? 29  LYS C O      1 
ATOM   3030 C CB     . LYS B 2 29  ? 58.929 22.753  22.658  1.00 26.36 ? 29  LYS C CB     1 
ATOM   3031 C CG     . LYS B 2 29  ? 59.266 23.727  21.556  1.00 44.27 ? 29  LYS C CG     1 
ATOM   3032 C CD     . LYS B 2 29  ? 59.055 25.155  22.027  1.00 56.69 ? 29  LYS C CD     1 
ATOM   3033 C CE     . LYS B 2 29  ? 57.920 25.823  21.270  1.00 49.48 ? 29  LYS C CE     1 
ATOM   3034 N NZ     . LYS B 2 29  ? 58.312 26.188  19.883  1.00 52.46 ? 29  LYS C NZ     1 
ATOM   3035 N N      . ILE B 2 30  ? 58.013 19.700  23.649  1.00 28.18 ? 30  ILE C N      1 
ATOM   3036 C CA     . ILE B 2 30  ? 57.836 18.773  24.730  1.00 25.07 ? 30  ILE C CA     1 
ATOM   3037 C C      . ILE B 2 30  ? 58.627 17.519  24.416  1.00 24.85 ? 30  ILE C C      1 
ATOM   3038 O O      . ILE B 2 30  ? 59.177 16.908  25.301  1.00 25.66 ? 30  ILE C O      1 
ATOM   3039 C CB     . ILE B 2 30  ? 56.333 18.542  24.998  1.00 27.03 ? 30  ILE C CB     1 
ATOM   3040 C CG1    . ILE B 2 30  ? 55.688 19.861  25.416  1.00 24.08 ? 30  ILE C CG1    1 
ATOM   3041 C CG2    . ILE B 2 30  ? 56.103 17.507  26.085  1.00 21.19 ? 30  ILE C CG2    1 
ATOM   3042 C CD1    . ILE B 2 30  ? 54.197 19.787  25.632  1.00 28.56 ? 30  ILE C CD1    1 
ATOM   3043 N N      . GLN B 2 31  ? 58.737 17.170  23.148  1.00 20.01 ? 31  GLN C N      1 
ATOM   3044 C CA     . GLN B 2 31  ? 59.482 15.988  22.777  1.00 23.86 ? 31  GLN C CA     1 
ATOM   3045 C C      . GLN B 2 31  ? 60.944 16.222  22.927  1.00 24.35 ? 31  GLN C C      1 
ATOM   3046 O O      . GLN B 2 31  ? 61.705 15.311  23.158  1.00 24.87 ? 31  GLN C O      1 
ATOM   3047 C CB     . GLN B 2 31  ? 59.163 15.545  21.364  1.00 25.39 ? 31  GLN C CB     1 
ATOM   3048 C CG     . GLN B 2 31  ? 59.708 14.188  20.984  1.00 24.15 ? 31  GLN C CG     1 
ATOM   3049 C CD     . GLN B 2 31  ? 59.717 13.968  19.497  1.00 26.72 ? 31  GLN C CD     1 
ATOM   3050 O OE1    . GLN B 2 31  ? 59.579 14.906  18.725  1.00 24.51 ? 31  GLN C OE1    1 
ATOM   3051 N NE2    . GLN B 2 31  ? 59.852 12.720  19.084  1.00 25.53 ? 31  GLN C NE2    1 
ATOM   3052 N N      . ASP B 2 32  ? 61.348 17.466  22.816  1.00 24.08 ? 32  ASP C N      1 
ATOM   3053 C CA     . ASP B 2 32  ? 62.730 17.787  22.927  1.00 26.78 ? 32  ASP C CA     1 
ATOM   3054 C C      . ASP B 2 32  ? 63.155 17.762  24.356  1.00 27.67 ? 32  ASP C C      1 
ATOM   3055 O O      . ASP B 2 32  ? 64.232 17.295  24.670  1.00 28.90 ? 32  ASP C O      1 
ATOM   3056 C CB     . ASP B 2 32  ? 62.931 19.169  22.354  1.00 28.59 ? 32  ASP C CB     1 
ATOM   3057 C CG     . ASP B 2 32  ? 62.830 19.210  20.857  1.00 33.72 ? 32  ASP C CG     1 
ATOM   3058 O OD1    . ASP B 2 32  ? 62.916 18.144  20.227  1.00 43.60 ? 32  ASP C OD1    1 
ATOM   3059 O OD2    . ASP B 2 32  ? 62.664 20.314  20.306  1.00 34.00 ? 32  ASP C OD2    1 
ATOM   3060 N N      . LYS B 2 33  ? 62.302 18.240  25.244  1.00 32.41 ? 33  LYS C N      1 
ATOM   3061 C CA     . LYS B 2 33  ? 62.611 18.308  26.663  1.00 31.22 ? 33  LYS C CA     1 
ATOM   3062 C C      . LYS B 2 33  ? 62.291 17.068  27.458  1.00 29.92 ? 33  LYS C C      1 
ATOM   3063 O O      . LYS B 2 33  ? 62.970 16.766  28.417  1.00 30.89 ? 33  LYS C O      1 
ATOM   3064 C CB     . LYS B 2 33  ? 61.863 19.492  27.249  1.00 26.70 ? 33  LYS C CB     1 
ATOM   3065 C CG     . LYS B 2 33  ? 62.363 20.007  28.579  1.00 30.58 ? 33  LYS C CG     1 
ATOM   3066 C CD     . LYS B 2 33  ? 62.059 21.486  28.723  1.00 39.05 ? 33  LYS C CD     1 
ATOM   3067 C CE     . LYS B 2 33  ? 62.566 22.013  30.052  1.00 40.12 ? 33  LYS C CE     1 
ATOM   3068 N NZ     . LYS B 2 33  ? 62.820 23.476  30.015  1.00 47.73 ? 33  LYS C NZ     1 
ATOM   3069 N N      . GLU B 2 34  ? 61.261 16.333  27.076  1.00 35.34 ? 34  GLU C N      1 
ATOM   3070 C CA     . GLU B 2 34  ? 60.833 15.174  27.859  1.00 33.04 ? 34  GLU C CA     1 
ATOM   3071 C C      . GLU B 2 34  ? 60.778 13.902  27.069  1.00 27.19 ? 34  GLU C C      1 
ATOM   3072 O O      . GLU B 2 34  ? 60.700 12.840  27.641  1.00 31.84 ? 34  GLU C O      1 
ATOM   3073 C CB     . GLU B 2 34  ? 59.491 15.459  28.553  1.00 27.92 ? 34  GLU C CB     1 
ATOM   3074 C CG     . GLU B 2 34  ? 59.591 16.340  29.778  1.00 24.11 ? 34  GLU C CG     1 
ATOM   3075 C CD     . GLU B 2 34  ? 60.021 15.571  31.006  1.00 41.53 ? 34  GLU C CD     1 
ATOM   3076 O OE1    . GLU B 2 34  ? 59.619 14.403  31.148  1.00 38.38 ? 34  GLU C OE1    1 
ATOM   3077 O OE2    . GLU B 2 34  ? 60.751 16.139  31.838  1.00 41.96 ? 34  GLU C OE2    1 
ATOM   3078 N N      . GLY B 2 35  ? 60.815 14.001  25.755  1.00 26.65 ? 35  GLY C N      1 
ATOM   3079 C CA     . GLY B 2 35  ? 60.851 12.819  24.920  1.00 23.24 ? 35  GLY C CA     1 
ATOM   3080 C C      . GLY B 2 35  ? 59.545 12.210  24.590  1.00 26.02 ? 35  GLY C C      1 
ATOM   3081 O O      . GLY B 2 35  ? 59.497 11.113  24.087  1.00 25.43 ? 35  GLY C O      1 
ATOM   3082 N N      . ILE B 2 36  ? 58.478 12.937  24.840  1.00 26.96 ? 36  ILE C N      1 
ATOM   3083 C CA     . ILE B 2 36  ? 57.171 12.382  24.663  1.00 22.67 ? 36  ILE C CA     1 
ATOM   3084 C C      . ILE B 2 36  ? 56.780 12.580  23.256  1.00 20.32 ? 36  ILE C C      1 
ATOM   3085 O O      . ILE B 2 36  ? 56.755 13.696  22.792  1.00 21.07 ? 36  ILE C O      1 
ATOM   3086 C CB     . ILE B 2 36  ? 56.150 13.058  25.601  1.00 21.83 ? 36  ILE C CB     1 
ATOM   3087 C CG1    . ILE B 2 36  ? 56.528 12.840  27.057  1.00 16.70 ? 36  ILE C CG1    1 
ATOM   3088 C CG2    . ILE B 2 36  ? 54.752 12.561  25.308  1.00 18.36 ? 36  ILE C CG2    1 
ATOM   3089 C CD1    . ILE B 2 36  ? 56.036 13.936  27.964  1.00 16.27 ? 36  ILE C CD1    1 
ATOM   3090 N N      . PRO B 2 37  ? 56.467 11.485  22.574  1.00 17.99 ? 37  PRO C N      1 
ATOM   3091 C CA     . PRO B 2 37  ? 56.040 11.564  21.193  1.00 19.95 ? 37  PRO C CA     1 
ATOM   3092 C C      . PRO B 2 37  ? 54.897 12.605  20.862  1.00 13.62 ? 37  PRO C C      1 
ATOM   3093 O O      . PRO B 2 37  ? 53.920 12.558  21.559  1.00 14.17 ? 37  PRO C O      1 
ATOM   3094 C CB     . PRO B 2 37  ? 55.689 10.115  20.880  1.00 12.59 ? 37  PRO C CB     1 
ATOM   3095 C CG     . PRO B 2 37  ? 56.519 9.317   21.781  1.00 10.78 ? 37  PRO C CG     1 
ATOM   3096 C CD     . PRO B 2 37  ? 56.551 10.098  23.044  1.00 15.80 ? 37  PRO C CD     1 
ATOM   3097 N N      . PRO B 2 38  ? 55.049 13.540  19.850  1.00 19.29 ? 38  PRO C N      1 
ATOM   3098 C CA     . PRO B 2 38  ? 53.905 14.430  19.549  1.00 21.32 ? 38  PRO C CA     1 
ATOM   3099 C C      . PRO B 2 38  ? 52.570 13.710  19.372  1.00 20.12 ? 38  PRO C C      1 
ATOM   3100 O O      . PRO B 2 38  ? 51.547 14.167  19.901  1.00 21.02 ? 38  PRO C O      1 
ATOM   3101 C CB     . PRO B 2 38  ? 54.360 15.133  18.266  1.00 10.84 ? 38  PRO C CB     1 
ATOM   3102 C CG     . PRO B 2 38  ? 55.878 15.218  18.468  1.00 16.20 ? 38  PRO C CG     1 
ATOM   3103 C CD     . PRO B 2 38  ? 56.277 13.940  19.142  1.00 15.26 ? 38  PRO C CD     1 
ATOM   3104 N N      . ASP B 2 39  ? 52.545 12.591  18.645  1.00 22.75 ? 39  ASP C N      1 
ATOM   3105 C CA     . ASP B 2 39  ? 51.304 11.856  18.439  1.00 19.16 ? 39  ASP C CA     1 
ATOM   3106 C C      . ASP B 2 39  ? 50.750 11.262  19.730  1.00 18.51 ? 39  ASP C C      1 
ATOM   3107 O O      . ASP B 2 39  ? 49.568 10.910  19.790  1.00 19.47 ? 39  ASP C O      1 
ATOM   3108 C CB     . ASP B 2 39  ? 51.525 10.755  17.398  1.00 23.51 ? 39  ASP C CB     1 
ATOM   3109 C CG     . ASP B 2 39  ? 51.821 11.315  16.002  1.00 32.27 ? 39  ASP C CG     1 
ATOM   3110 O OD1    . ASP B 2 39  ? 51.463 12.486  15.756  1.00 35.11 ? 39  ASP C OD1    1 
ATOM   3111 O OD2    . ASP B 2 39  ? 52.384 10.588  15.145  1.00 25.35 ? 39  ASP C OD2    1 
ATOM   3112 N N      . GLN B 2 40  ? 51.561 11.125  20.758  1.00 21.24 ? 40  GLN C N      1 
ATOM   3113 C CA     . GLN B 2 40  ? 51.007 10.661  22.016  1.00 21.89 ? 40  GLN C CA     1 
ATOM   3114 C C      . GLN B 2 40  ? 50.361 11.780  22.821  1.00 19.30 ? 40  GLN C C      1 
ATOM   3115 O O      . GLN B 2 40  ? 49.826 11.512  23.897  1.00 17.11 ? 40  GLN C O      1 
ATOM   3116 C CB     . GLN B 2 40  ? 52.097 9.972   22.840  1.00 16.11 ? 40  GLN C CB     1 
ATOM   3117 C CG     . GLN B 2 40  ? 51.568 9.187   24.027  1.00 19.64 ? 40  GLN C CG     1 
ATOM   3118 C CD     . GLN B 2 40  ? 52.673 8.648   24.920  1.00 20.89 ? 40  GLN C CD     1 
ATOM   3119 O OE1    . GLN B 2 40  ? 53.873 8.865   24.681  1.00 16.81 ? 40  GLN C OE1    1 
ATOM   3120 N NE2    . GLN B 2 40  ? 52.273 7.937   25.954  1.00 18.91 ? 40  GLN C NE2    1 
ATOM   3121 N N      . GLN B 2 41  ? 50.486 13.012  22.354  1.00 19.02 ? 41  GLN C N      1 
ATOM   3122 C CA     . GLN B 2 41  ? 50.117 14.169  23.202  1.00 19.57 ? 41  GLN C CA     1 
ATOM   3123 C C      . GLN B 2 41  ? 48.707 14.711  23.001  1.00 20.05 ? 41  GLN C C      1 
ATOM   3124 O O      . GLN B 2 41  ? 48.189 14.649  21.888  1.00 22.45 ? 41  GLN C O      1 
ATOM   3125 C CB     . GLN B 2 41  ? 51.189 15.244  23.077  1.00 15.40 ? 41  GLN C CB     1 
ATOM   3126 C CG     . GLN B 2 41  ? 52.550 14.836  23.599  1.00 16.84 ? 41  GLN C CG     1 
ATOM   3127 C CD     . GLN B 2 41  ? 53.508 15.992  23.494  1.00 19.57 ? 41  GLN C CD     1 
ATOM   3128 O OE1    . GLN B 2 41  ? 53.170 17.119  23.830  1.00 25.21 ? 41  GLN C OE1    1 
ATOM   3129 N NE2    . GLN B 2 41  ? 54.706 15.724  23.011  1.00 13.38 ? 41  GLN C NE2    1 
ATOM   3130 N N      . ARG B 2 42  ? 48.120 15.179  24.089  1.00 16.05 ? 42  ARG C N      1 
ATOM   3131 C CA     . ARG B 2 42  ? 46.778 15.787  24.061  1.00 22.71 ? 42  ARG C CA     1 
ATOM   3132 C C      . ARG B 2 42  ? 46.867 16.953  25.042  1.00 21.11 ? 42  ARG C C      1 
ATOM   3133 O O      . ARG B 2 42  ? 46.890 16.700  26.239  1.00 21.75 ? 42  ARG C O      1 
ATOM   3134 C CB     . ARG B 2 42  ? 45.700 14.790  24.497  1.00 23.99 ? 42  ARG C CB     1 
ATOM   3135 C CG     . ARG B 2 42  ? 45.187 13.841  23.425  1.00 30.41 ? 42  ARG C CG     1 
ATOM   3136 C CD     . ARG B 2 42  ? 43.734 13.492  23.682  1.00 30.75 ? 42  ARG C CD     1 
ATOM   3137 N NE     . ARG B 2 42  ? 43.323 12.110  23.480  1.00 56.85 ? 42  ARG C NE     1 
ATOM   3138 C CZ     . ARG B 2 42  ? 42.773 11.636  22.367  1.00 62.81 ? 42  ARG C CZ     1 
ATOM   3139 N NH1    . ARG B 2 42  ? 42.589 12.430  21.328  1.00 48.25 ? 42  ARG C NH1    1 
ATOM   3140 N NH2    . ARG B 2 42  ? 42.416 10.368  22.291  1.00 50.08 ? 42  ARG C NH2    1 
ATOM   3141 N N      . LEU B 2 43  ? 46.963 18.178  24.532  1.00 17.30 ? 43  LEU C N      1 
ATOM   3142 C CA     . LEU B 2 43  ? 47.134 19.358  25.410  1.00 19.99 ? 43  LEU C CA     1 
ATOM   3143 C C      . LEU B 2 43  ? 45.768 19.996  25.700  1.00 22.23 ? 43  LEU C C      1 
ATOM   3144 O O      . LEU B 2 43  ? 44.892 19.902  24.833  1.00 21.13 ? 43  LEU C O      1 
ATOM   3145 C CB     . LEU B 2 43  ? 48.131 20.306  24.742  1.00 19.13 ? 43  LEU C CB     1 
ATOM   3146 C CG     . LEU B 2 43  ? 49.608 20.000  24.972  1.00 18.67 ? 43  LEU C CG     1 
ATOM   3147 C CD1    . LEU B 2 43  ? 50.468 20.738  23.963  1.00 13.92 ? 43  LEU C CD1    1 
ATOM   3148 C CD2    . LEU B 2 43  ? 50.020 20.363  26.386  1.00 13.32 ? 43  LEU C CD2    1 
ATOM   3149 N N      . ILE B 2 44  ? 45.576 20.554  26.902  1.00 21.38 ? 44  ILE C N      1 
ATOM   3150 C CA     . ILE B 2 44  ? 44.260 21.070  27.270  1.00 23.29 ? 44  ILE C CA     1 
ATOM   3151 C C      . ILE B 2 44  ? 44.419 22.417  27.954  1.00 22.10 ? 44  ILE C C      1 
ATOM   3152 O O      . ILE B 2 44  ? 45.259 22.570  28.847  1.00 24.69 ? 44  ILE C O      1 
ATOM   3153 C CB     . ILE B 2 44  ? 43.487 20.104  28.190  1.00 23.83 ? 44  ILE C CB     1 
ATOM   3154 C CG1    . ILE B 2 44  ? 43.227 18.770  27.496  1.00 22.19 ? 44  ILE C CG1    1 
ATOM   3155 C CG2    . ILE B 2 44  ? 42.172 20.730  28.639  1.00 21.97 ? 44  ILE C CG2    1 
ATOM   3156 C CD1    . ILE B 2 44  ? 43.528 17.590  28.392  1.00 22.85 ? 44  ILE C CD1    1 
ATOM   3157 N N      . PHE B 2 45  ? 43.582 23.376  27.559  1.00 25.98 ? 45  PHE C N      1 
ATOM   3158 C CA     . PHE B 2 45  ? 43.543 24.717  28.130  1.00 20.93 ? 45  PHE C CA     1 
ATOM   3159 C C      . PHE B 2 45  ? 42.110 25.199  28.047  1.00 24.06 ? 45  PHE C C      1 
ATOM   3160 O O      . PHE B 2 45  ? 41.450 25.022  27.013  1.00 21.59 ? 45  PHE C O      1 
ATOM   3161 C CB     . PHE B 2 45  ? 44.457 25.689  27.386  1.00 21.39 ? 45  PHE C CB     1 
ATOM   3162 C CG     . PHE B 2 45  ? 44.586 27.034  28.038  1.00 23.71 ? 45  PHE C CG     1 
ATOM   3163 C CD1    . PHE B 2 45  ? 45.447 27.217  29.123  1.00 26.85 ? 45  PHE C CD1    1 
ATOM   3164 C CD2    . PHE B 2 45  ? 43.887 28.133  27.543  1.00 26.37 ? 45  PHE C CD2    1 
ATOM   3165 C CE1    . PHE B 2 45  ? 45.589 28.474  29.722  1.00 25.97 ? 45  PHE C CE1    1 
ATOM   3166 C CE2    . PHE B 2 45  ? 44.020 29.391  28.140  1.00 26.78 ? 45  PHE C CE2    1 
ATOM   3167 C CZ     . PHE B 2 45  ? 44.873 29.564  29.225  1.00 26.35 ? 45  PHE C CZ     1 
ATOM   3168 N N      . ALA B 2 46  ? 41.631 25.804  29.134  1.00 25.24 ? 46  ALA C N      1 
ATOM   3169 C CA     . ALA B 2 46  ? 40.259 26.275  29.161  1.00 24.59 ? 46  ALA C CA     1 
ATOM   3170 C C      . ALA B 2 46  ? 39.274 25.117  29.013  1.00 27.67 ? 46  ALA C C      1 
ATOM   3171 O O      . ALA B 2 46  ? 38.191 25.285  28.443  1.00 27.17 ? 46  ALA C O      1 
ATOM   3172 C CB     . ALA B 2 46  ? 40.019 27.305  28.052  1.00 26.35 ? 46  ALA C CB     1 
ATOM   3173 N N      . GLY B 2 47  ? 39.640 23.911  29.406  1.00 26.68 ? 47  GLY C N      1 
ATOM   3174 C CA     . GLY B 2 47  ? 38.768 22.760  29.295  1.00 22.40 ? 47  GLY C CA     1 
ATOM   3175 C C      . GLY B 2 47  ? 38.598 22.253  27.916  1.00 19.63 ? 47  GLY C C      1 
ATOM   3176 O O      . GLY B 2 47  ? 37.826 21.344  27.686  1.00 20.35 ? 47  GLY C O      1 
ATOM   3177 N N      . LYS B 2 48  ? 39.359 22.791  26.998  1.00 27.90 ? 48  LYS C N      1 
ATOM   3178 C CA     . LYS B 2 48  ? 39.168 22.480  25.588  1.00 32.21 ? 48  LYS C CA     1 
ATOM   3179 C C      . LYS B 2 48  ? 40.392 21.747  25.045  1.00 27.87 ? 48  LYS C C      1 
ATOM   3180 O O      . LYS B 2 48  ? 41.527 22.183  25.265  1.00 21.70 ? 48  LYS C O      1 
ATOM   3181 C CB     . LYS B 2 48  ? 38.884 23.774  24.809  1.00 26.02 ? 48  LYS C CB     1 
ATOM   3182 C CG     . LYS B 2 48  ? 38.377 23.591  23.382  1.00 40.44 ? 48  LYS C CG     1 
ATOM   3183 C CD     . LYS B 2 48  ? 37.385 22.427  23.233  1.00 46.44 ? 48  LYS C CD     1 
ATOM   3184 C CE     . LYS B 2 48  ? 37.090 22.154  21.742  1.00 48.17 ? 48  LYS C CE     1 
ATOM   3185 N NZ     . LYS B 2 48  ? 35.966 21.199  21.493  1.00 36.54 ? 48  LYS C NZ     1 
ATOM   3186 N N      . GLN B 2 49  ? 40.163 20.658  24.325  1.00 25.36 ? 49  GLN C N      1 
ATOM   3187 C CA     . GLN B 2 49  ? 41.241 19.974  23.641  1.00 27.55 ? 49  GLN C CA     1 
ATOM   3188 C C      . GLN B 2 49  ? 41.868 20.909  22.658  1.00 30.81 ? 49  GLN C C      1 
ATOM   3189 O O      . GLN B 2 49  ? 41.169 21.537  21.874  1.00 39.12 ? 49  GLN C O      1 
ATOM   3190 C CB     . GLN B 2 49  ? 40.708 18.780  22.895  1.00 34.68 ? 49  GLN C CB     1 
ATOM   3191 C CG     . GLN B 2 49  ? 41.759 18.001  22.136  1.00 45.12 ? 49  GLN C CG     1 
ATOM   3192 C CD     . GLN B 2 49  ? 42.553 17.083  23.032  1.00 46.59 ? 49  GLN C CD     1 
ATOM   3193 O OE1    . GLN B 2 49  ? 42.057 16.609  24.051  1.00 38.91 ? 49  GLN C OE1    1 
ATOM   3194 N NE2    . GLN B 2 49  ? 43.792 16.829  22.656  1.00 45.55 ? 49  GLN C NE2    1 
ATOM   3195 N N      . LEU B 2 50  ? 43.176 20.965  22.629  1.00 29.07 ? 50  LEU C N      1 
ATOM   3196 C CA     . LEU B 2 50  ? 43.902 21.959  21.835  1.00 26.55 ? 50  LEU C CA     1 
ATOM   3197 C C      . LEU B 2 50  ? 44.297 21.369  20.491  1.00 32.36 ? 50  LEU C C      1 
ATOM   3198 O O      . LEU B 2 50  ? 45.021 20.369  20.436  1.00 39.76 ? 50  LEU C O      1 
ATOM   3199 C CB     . LEU B 2 50  ? 45.143 22.470  22.571  1.00 25.86 ? 50  LEU C CB     1 
ATOM   3200 C CG     . LEU B 2 50  ? 44.869 23.344  23.798  1.00 20.83 ? 50  LEU C CG     1 
ATOM   3201 C CD1    . LEU B 2 50  ? 46.100 24.068  24.310  1.00 21.27 ? 50  LEU C CD1    1 
ATOM   3202 C CD2    . LEU B 2 50  ? 43.792 24.323  23.459  1.00 24.61 ? 50  LEU C CD2    1 
ATOM   3203 N N      . GLU B 2 51  ? 43.850 22.005  19.411  1.00 42.57 ? 51  GLU C N      1 
ATOM   3204 C CA     . GLU B 2 51  ? 44.134 21.513  18.069  1.00 42.75 ? 51  GLU C CA     1 
ATOM   3205 C C      . GLU B 2 51  ? 45.489 22.004  17.563  1.00 45.94 ? 51  GLU C C      1 
ATOM   3206 O O      . GLU B 2 51  ? 45.967 23.084  17.926  1.00 43.92 ? 51  GLU C O      1 
ATOM   3207 C CB     . GLU B 2 51  ? 43.033 21.932  17.102  1.00 35.04 ? 51  GLU C CB     1 
ATOM   3208 C CG     . GLU B 2 51  ? 41.714 21.301  17.420  1.00 37.25 ? 51  GLU C CG     1 
ATOM   3209 C CD     . GLU B 2 51  ? 40.655 21.697  16.432  1.00 60.07 ? 51  GLU C CD     1 
ATOM   3210 O OE1    . GLU B 2 51  ? 40.770 21.280  15.259  1.00 65.55 ? 51  GLU C OE1    1 
ATOM   3211 O OE2    . GLU B 2 51  ? 39.720 22.437  16.819  1.00 61.03 ? 51  GLU C OE2    1 
ATOM   3212 N N      . ASP B 2 52  ? 46.112 21.188  16.713  1.00 41.34 ? 52  ASP C N      1 
ATOM   3213 C CA     . ASP B 2 52  ? 47.472 21.491  16.291  1.00 46.94 ? 52  ASP C CA     1 
ATOM   3214 C C      . ASP B 2 52  ? 47.517 22.727  15.397  1.00 51.44 ? 52  ASP C C      1 
ATOM   3215 O O      . ASP B 2 52  ? 48.449 23.534  15.497  1.00 45.12 ? 52  ASP C O      1 
ATOM   3216 C CB     . ASP B 2 52  ? 48.080 20.279  15.588  1.00 46.16 ? 52  ASP C CB     1 
ATOM   3217 C CG     . ASP B 2 52  ? 48.138 19.063  16.484  1.00 53.07 ? 52  ASP C CG     1 
ATOM   3218 O OD1    . ASP B 2 52  ? 47.063 18.468  16.737  1.00 62.94 ? 52  ASP C OD1    1 
ATOM   3219 O OD2    . ASP B 2 52  ? 49.248 18.706  16.954  1.00 41.20 ? 52  ASP C OD2    1 
ATOM   3220 N N      . GLY B 2 53  ? 46.508 22.911  14.538  1.00 52.27 ? 53  GLY C N      1 
ATOM   3221 C CA     . GLY B 2 53  ? 46.576 23.991  13.564  1.00 50.23 ? 53  GLY C CA     1 
ATOM   3222 C C      . GLY B 2 53  ? 46.688 25.368  14.199  1.00 47.32 ? 53  GLY C C      1 
ATOM   3223 O O      . GLY B 2 53  ? 47.451 26.223  13.736  1.00 38.64 ? 53  GLY C O      1 
ATOM   3224 N N      . ARG B 2 54  ? 45.936 25.599  15.266  1.00 41.20 ? 54  ARG C N      1 
ATOM   3225 C CA     . ARG B 2 54  ? 45.757 26.955  15.747  1.00 40.98 ? 54  ARG C CA     1 
ATOM   3226 C C      . ARG B 2 54  ? 47.024 27.455  16.427  1.00 40.18 ? 54  ARG C C      1 
ATOM   3227 O O      . ARG B 2 54  ? 48.019 26.743  16.538  1.00 47.66 ? 54  ARG C O      1 
ATOM   3228 C CB     . ARG B 2 54  ? 44.554 27.034  16.679  1.00 43.87 ? 54  ARG C CB     1 
ATOM   3229 C CG     . ARG B 2 54  ? 43.298 27.476  15.967  1.00 42.79 ? 54  ARG C CG     1 
ATOM   3230 C CD     . ARG B 2 54  ? 42.657 26.329  15.246  1.00 45.38 ? 54  ARG C CD     1 
ATOM   3231 N NE     . ARG B 2 54  ? 41.283 26.642  14.882  1.00 53.22 ? 54  ARG C NE     1 
ATOM   3232 C CZ     . ARG B 2 54  ? 40.385 25.727  14.556  1.00 57.72 ? 54  ARG C CZ     1 
ATOM   3233 N NH1    . ARG B 2 54  ? 40.694 24.440  14.542  1.00 64.79 ? 54  ARG C NH1    1 
ATOM   3234 N NH2    . ARG B 2 54  ? 39.147 26.109  14.245  1.00 57.19 ? 54  ARG C NH2    1 
ATOM   3235 N N      . THR B 2 55  ? 46.995 28.712  16.860  1.00 41.43 ? 55  THR C N      1 
ATOM   3236 C CA     . THR B 2 55  ? 48.123 29.339  17.532  1.00 51.09 ? 55  THR C CA     1 
ATOM   3237 C C      . THR B 2 55  ? 47.784 29.567  19.000  1.00 48.82 ? 55  THR C C      1 
ATOM   3238 O O      . THR B 2 55  ? 46.612 29.703  19.368  1.00 48.94 ? 55  THR C O      1 
ATOM   3239 C CB     . THR B 2 55  ? 48.494 30.682  16.868  1.00 57.42 ? 55  THR C CB     1 
ATOM   3240 O OG1    . THR B 2 55  ? 49.723 31.189  17.416  1.00 46.30 ? 55  THR C OG1    1 
ATOM   3241 C CG2    . THR B 2 55  ? 47.373 31.718  17.071  1.00 50.33 ? 55  THR C CG2    1 
ATOM   3242 N N      . LEU B 2 56  ? 48.826 29.609  19.839  1.00 41.25 ? 56  LEU C N      1 
ATOM   3243 C CA     . LEU B 2 56  ? 48.655 30.025  21.227  1.00 40.93 ? 56  LEU C CA     1 
ATOM   3244 C C      . LEU B 2 56  ? 47.896 31.340  21.334  1.00 52.71 ? 56  LEU C C      1 
ATOM   3245 O O      . LEU B 2 56  ? 47.181 31.569  22.318  1.00 57.50 ? 56  LEU C O      1 
ATOM   3246 C CB     . LEU B 2 56  ? 50.011 30.160  21.912  1.00 39.62 ? 56  LEU C CB     1 
ATOM   3247 C CG     . LEU B 2 56  ? 50.493 28.883  22.588  1.00 39.89 ? 56  LEU C CG     1 
ATOM   3248 C CD1    . LEU B 2 56  ? 50.307 27.681  21.657  1.00 36.51 ? 56  LEU C CD1    1 
ATOM   3249 C CD2    . LEU B 2 56  ? 51.950 29.027  23.074  1.00 41.88 ? 56  LEU C CD2    1 
ATOM   3250 N N      . SER B 2 57  ? 48.031 32.218  20.338  1.00 54.41 ? 57  SER C N      1 
ATOM   3251 C CA     . SER B 2 57  ? 47.237 33.441  20.356  1.00 50.12 ? 57  SER C CA     1 
ATOM   3252 C C      . SER B 2 57  ? 45.757 33.152  20.131  1.00 47.94 ? 57  SER C C      1 
ATOM   3253 O O      . SER B 2 57  ? 44.896 33.761  20.777  1.00 60.17 ? 57  SER C O      1 
ATOM   3254 C CB     . SER B 2 57  ? 47.763 34.431  19.325  1.00 56.73 ? 57  SER C CB     1 
ATOM   3255 O OG     . SER B 2 57  ? 48.808 35.206  19.901  1.00 58.35 ? 57  SER C OG     1 
ATOM   3256 N N      . ASP B 2 58  ? 45.435 32.217  19.239  1.00 45.81 ? 58  ASP C N      1 
ATOM   3257 C CA     . ASP B 2 58  ? 44.035 31.879  19.007  1.00 51.75 ? 58  ASP C CA     1 
ATOM   3258 C C      . ASP B 2 58  ? 43.405 31.259  20.251  1.00 51.11 ? 58  ASP C C      1 
ATOM   3259 O O      . ASP B 2 58  ? 42.202 30.988  20.269  1.00 54.11 ? 58  ASP C O      1 
ATOM   3260 C CB     . ASP B 2 58  ? 43.896 30.924  17.814  1.00 55.22 ? 58  ASP C CB     1 
ATOM   3261 C CG     . ASP B 2 58  ? 42.435 30.619  17.477  1.00 70.35 ? 58  ASP C CG     1 
ATOM   3262 O OD1    . ASP B 2 58  ? 41.830 31.400  16.704  1.00 76.74 ? 58  ASP C OD1    1 
ATOM   3263 O OD2    . ASP B 2 58  ? 41.896 29.605  17.986  1.00 60.56 ? 58  ASP C OD2    1 
ATOM   3264 N N      . TYR B 2 59  ? 44.184 31.034  21.290  1.00 43.84 ? 59  TYR C N      1 
ATOM   3265 C CA     . TYR B 2 59  ? 43.649 30.359  22.452  1.00 46.00 ? 59  TYR C CA     1 
ATOM   3266 C C      . TYR B 2 59  ? 43.792 31.150  23.739  1.00 54.01 ? 59  TYR C C      1 
ATOM   3267 O O      . TYR B 2 59  ? 43.705 30.582  24.808  1.00 56.07 ? 59  TYR C O      1 
ATOM   3268 C CB     . TYR B 2 59  ? 44.351 29.009  22.589  1.00 48.12 ? 59  TYR C CB     1 
ATOM   3269 C CG     . TYR B 2 59  ? 43.852 27.907  21.698  1.00 43.07 ? 59  TYR C CG     1 
ATOM   3270 C CD1    . TYR B 2 59  ? 42.505 27.627  21.590  1.00 38.98 ? 59  TYR C CD1    1 
ATOM   3271 C CD2    . TYR B 2 59  ? 44.734 27.131  20.979  1.00 40.10 ? 59  TYR C CD2    1 
ATOM   3272 C CE1    . TYR B 2 59  ? 42.052 26.612  20.775  1.00 38.51 ? 59  TYR C CE1    1 
ATOM   3273 C CE2    . TYR B 2 59  ? 44.288 26.113  20.167  1.00 42.64 ? 59  TYR C CE2    1 
ATOM   3274 C CZ     . TYR B 2 59  ? 42.950 25.859  20.067  1.00 39.22 ? 59  TYR C CZ     1 
ATOM   3275 O OH     . TYR B 2 59  ? 42.510 24.849  19.254  1.00 39.76 ? 59  TYR C OH     1 
ATOM   3276 N N      . ASN B 2 60  ? 43.992 32.449  23.652  1.00 47.43 ? 60  ASN C N      1 
ATOM   3277 C CA     . ASN B 2 60  ? 44.213 33.289  24.827  1.00 52.25 ? 60  ASN C CA     1 
ATOM   3278 C C      . ASN B 2 60  ? 45.225 32.758  25.788  1.00 49.98 ? 60  ASN C C      1 
ATOM   3279 O O      . ASN B 2 60  ? 45.074 32.903  26.982  1.00 54.20 ? 60  ASN C O      1 
ATOM   3280 C CB     . ASN B 2 60  ? 42.931 33.623  25.570  1.00 57.52 ? 60  ASN C CB     1 
ATOM   3281 C CG     . ASN B 2 60  ? 41.851 34.176  24.663  1.00 65.98 ? 60  ASN C CG     1 
ATOM   3282 O OD1    . ASN B 2 60  ? 42.115 34.604  23.541  1.00 73.30 ? 60  ASN C OD1    1 
ATOM   3283 N ND2    . ASN B 2 60  ? 40.619 34.172  25.154  1.00 55.04 ? 60  ASN C ND2    1 
ATOM   3284 N N      . ILE B 2 61  ? 46.275 32.161  25.267  1.00 43.94 ? 61  ILE C N      1 
ATOM   3285 C CA     . ILE B 2 61  ? 47.291 31.618  26.101  1.00 42.53 ? 61  ILE C CA     1 
ATOM   3286 C C      . ILE B 2 61  ? 48.315 32.680  26.140  1.00 43.80 ? 61  ILE C C      1 
ATOM   3287 O O      . ILE B 2 61  ? 48.922 32.999  25.142  1.00 41.22 ? 61  ILE C O      1 
ATOM   3288 C CB     . ILE B 2 61  ? 47.846 30.297  25.555  1.00 44.00 ? 61  ILE C CB     1 
ATOM   3289 C CG1    . ILE B 2 61  ? 46.772 29.222  25.534  1.00 36.56 ? 61  ILE C CG1    1 
ATOM   3290 C CG2    . ILE B 2 61  ? 49.038 29.827  26.368  1.00 43.46 ? 61  ILE C CG2    1 
ATOM   3291 C CD1    . ILE B 2 61  ? 47.175 27.974  24.796  1.00 30.83 ? 61  ILE C CD1    1 
ATOM   3292 N N      . GLN B 2 62  ? 48.488 33.252  27.311  1.00 51.29 ? 62  GLN C N      1 
ATOM   3293 C CA     . GLN B 2 62  ? 49.408 34.315  27.462  1.00 44.36 ? 62  GLN C CA     1 
ATOM   3294 C C      . GLN B 2 62  ? 50.456 33.975  28.415  1.00 40.76 ? 62  GLN C C      1 
ATOM   3295 O O      . GLN B 2 62  ? 50.579 32.860  28.852  1.00 37.69 ? 62  GLN C O      1 
ATOM   3296 C CB     . GLN B 2 62  ? 48.695 35.526  28.010  1.00 53.24 ? 62  GLN C CB     1 
ATOM   3297 C CG     . GLN B 2 62  ? 48.002 36.379  26.959  1.00 53.31 ? 62  GLN C CG     1 
ATOM   3298 C CD     . GLN B 2 62  ? 46.497 36.228  26.983  1.00 62.27 ? 62  GLN C CD     1 
ATOM   3299 O OE1    . GLN B 2 62  ? 45.815 36.563  26.019  1.00 63.10 ? 62  GLN C OE1    1 
ATOM   3300 N NE2    . GLN B 2 62  ? 45.974 35.711  28.086  1.00 63.66 ? 62  GLN C NE2    1 
ATOM   3301 N N      . LYS B 2 63  ? 51.234 34.972  28.751  1.00 50.93 ? 63  LYS C N      1 
ATOM   3302 C CA     . LYS B 2 63  ? 52.337 34.786  29.649  1.00 52.66 ? 63  LYS C CA     1 
ATOM   3303 C C      . LYS B 2 63  ? 51.928 34.090  30.905  1.00 47.51 ? 63  LYS C C      1 
ATOM   3304 O O      . LYS B 2 63  ? 50.881 34.388  31.452  1.00 51.13 ? 63  LYS C O      1 
ATOM   3305 C CB     . LYS B 2 63  ? 52.936 36.163  29.948  1.00 44.16 ? 63  LYS C CB     1 
ATOM   3306 C CG     . LYS B 2 63  ? 54.185 36.171  30.801  1.00 59.31 ? 63  LYS C CG     1 
ATOM   3307 C CD     . LYS B 2 63  ? 54.560 37.591  31.191  1.00 56.32 ? 63  LYS C CD     1 
ATOM   3308 C CE     . LYS B 2 63  ? 53.404 38.308  31.874  1.00 49.15 ? 63  LYS C CE     1 
ATOM   3309 N NZ     . LYS B 2 63  ? 53.071 37.743  33.211  1.00 51.32 ? 63  LYS C NZ     1 
ATOM   3310 N N      . GLU B 2 64  ? 52.745 33.157  31.355  1.00 45.56 ? 64  GLU C N      1 
ATOM   3311 C CA     . GLU B 2 64  ? 52.495 32.444  32.592  1.00 43.49 ? 64  GLU C CA     1 
ATOM   3312 C C      . GLU B 2 64  ? 51.277 31.521  32.600  1.00 39.68 ? 64  GLU C C      1 
ATOM   3313 O O      . GLU B 2 64  ? 50.862 31.049  33.637  1.00 46.25 ? 64  GLU C O      1 
ATOM   3314 C CB     . GLU B 2 64  ? 52.563 33.401  33.775  1.00 44.39 ? 64  GLU C CB     1 
ATOM   3315 C CG     . GLU B 2 64  ? 53.771 34.327  33.778  1.00 51.17 ? 64  GLU C CG     1 
ATOM   3316 C CD     . GLU B 2 64  ? 54.875 33.898  34.718  1.00 60.13 ? 64  GLU C CD     1 
ATOM   3317 O OE1    . GLU B 2 64  ? 55.764 33.143  34.283  1.00 62.47 ? 64  GLU C OE1    1 
ATOM   3318 O OE2    . GLU B 2 64  ? 54.869 34.332  35.885  1.00 48.93 ? 64  GLU C OE2    1 
ATOM   3319 N N      . SER B 2 65  ? 50.747 31.211  31.434  1.00 35.61 ? 65  SER C N      1 
ATOM   3320 C CA     . SER B 2 65  ? 49.577 30.396  31.358  1.00 31.68 ? 65  SER C CA     1 
ATOM   3321 C C      . SER B 2 65  ? 49.918 28.959  31.584  1.00 39.31 ? 65  SER C C      1 
ATOM   3322 O O      . SER B 2 65  ? 50.980 28.515  31.205  1.00 43.73 ? 65  SER C O      1 
ATOM   3323 C CB     . SER B 2 65  ? 48.938 30.588  30.017  1.00 37.07 ? 65  SER C CB     1 
ATOM   3324 O OG     . SER B 2 65  ? 48.267 31.822  29.946  1.00 46.93 ? 65  SER C OG     1 
ATOM   3325 N N      . THR B 2 66  ? 49.024 28.216  32.208  1.00 39.50 ? 66  THR C N      1 
ATOM   3326 C CA     . THR B 2 66  ? 49.327 26.850  32.574  1.00 35.01 ? 66  THR C CA     1 
ATOM   3327 C C      . THR B 2 66  ? 48.503 25.851  31.824  1.00 32.46 ? 66  THR C C      1 
ATOM   3328 O O      . THR B 2 66  ? 47.295 25.900  31.852  1.00 32.53 ? 66  THR C O      1 
ATOM   3329 C CB     . THR B 2 66  ? 49.225 26.637  34.092  1.00 33.34 ? 66  THR C CB     1 
ATOM   3330 O OG1    . THR B 2 66  ? 49.738 27.782  34.775  1.00 36.32 ? 66  THR C OG1    1 
ATOM   3331 C CG2    . THR B 2 66  ? 49.999 25.408  34.525  1.00 34.02 ? 66  THR C CG2    1 
ATOM   3332 N N      . LEU B 2 67  ? 49.171 24.931  31.157  1.00 32.39 ? 67  LEU C N      1 
ATOM   3333 C CA     . LEU B 2 67  ? 48.495 23.947  30.317  1.00 24.99 ? 67  LEU C CA     1 
ATOM   3334 C C      . LEU B 2 67  ? 48.534 22.566  30.960  1.00 22.38 ? 67  LEU C C      1 
ATOM   3335 O O      . LEU B 2 67  ? 49.379 22.279  31.811  1.00 22.25 ? 67  LEU C O      1 
ATOM   3336 C CB     . LEU B 2 67  ? 49.121 23.878  28.922  1.00 24.95 ? 67  LEU C CB     1 
ATOM   3337 C CG     . LEU B 2 67  ? 48.528 24.837  27.889  1.00 29.77 ? 67  LEU C CG     1 
ATOM   3338 C CD1    . LEU B 2 67  ? 49.179 26.205  28.017  1.00 32.19 ? 67  LEU C CD1    1 
ATOM   3339 C CD2    . LEU B 2 67  ? 48.652 24.288  26.458  1.00 25.18 ? 67  LEU C CD2    1 
ATOM   3340 N N      . HIS B 2 68  ? 47.608 21.704  30.546  1.00 19.44 ? 68  HIS C N      1 
ATOM   3341 C CA     . HIS B 2 68  ? 47.528 20.347  31.074  1.00 21.55 ? 68  HIS C CA     1 
ATOM   3342 C C      . HIS B 2 68  ? 47.761 19.341  29.961  1.00 20.92 ? 68  HIS C C      1 
ATOM   3343 O O      . HIS B 2 68  ? 47.073 19.363  28.934  1.00 17.77 ? 68  HIS C O      1 
ATOM   3344 C CB     . HIS B 2 68  ? 46.191 20.084  31.775  1.00 22.00 ? 68  HIS C CB     1 
ATOM   3345 C CG     . HIS B 2 68  ? 46.114 20.696  33.132  1.00 21.87 ? 68  HIS C CG     1 
ATOM   3346 N ND1    . HIS B 2 68  ? 45.742 22.008  33.334  1.00 24.46 ? 68  HIS C ND1    1 
ATOM   3347 C CD2    . HIS B 2 68  ? 46.447 20.205  34.350  1.00 26.80 ? 68  HIS C CD2    1 
ATOM   3348 C CE1    . HIS B 2 68  ? 45.810 22.288  34.624  1.00 28.72 ? 68  HIS C CE1    1 
ATOM   3349 N NE2    . HIS B 2 68  ? 46.234 21.211  35.265  1.00 28.59 ? 68  HIS C NE2    1 
ATOM   3350 N N      . LEU B 2 69  ? 48.729 18.458  30.181  1.00 15.34 ? 69  LEU C N      1 
ATOM   3351 C CA     . LEU B 2 69  ? 49.139 17.466  29.207  1.00 17.86 ? 69  LEU C CA     1 
ATOM   3352 C C      . LEU B 2 69  ? 48.643 16.102  29.650  1.00 14.98 ? 69  LEU C C      1 
ATOM   3353 O O      . LEU B 2 69  ? 48.857 15.717  30.800  1.00 21.66 ? 69  LEU C O      1 
ATOM   3354 C CB     . LEU B 2 69  ? 50.665 17.475  29.071  1.00 14.91 ? 69  LEU C CB     1 
ATOM   3355 C CG     . LEU B 2 69  ? 51.328 16.393  28.218  1.00 9.25  ? 69  LEU C CG     1 
ATOM   3356 C CD1    . LEU B 2 69  ? 50.981 16.522  26.732  1.00 8.67  ? 69  LEU C CD1    1 
ATOM   3357 C CD2    . LEU B 2 69  ? 52.827 16.412  28.468  1.00 9.74  ? 69  LEU C CD2    1 
ATOM   3358 N N      . VAL B 2 70  ? 47.984 15.374  28.753  1.00 12.06 ? 70  VAL C N      1 
ATOM   3359 C CA     . VAL B 2 70  ? 47.649 13.972  28.990  1.00 17.62 ? 70  VAL C CA     1 
ATOM   3360 C C      . VAL B 2 70  ? 48.217 13.133  27.851  1.00 18.62 ? 70  VAL C C      1 
ATOM   3361 O O      . VAL B 2 70  ? 48.148 13.528  26.681  1.00 23.14 ? 70  VAL C O      1 
ATOM   3362 C CB     . VAL B 2 70  ? 46.124 13.741  29.137  1.00 19.91 ? 70  VAL C CB     1 
ATOM   3363 C CG1    . VAL B 2 70  ? 45.452 14.935  29.794  1.00 19.38 ? 70  VAL C CG1    1 
ATOM   3364 C CG2    . VAL B 2 70  ? 45.480 13.435  27.798  1.00 25.09 ? 70  VAL C CG2    1 
ATOM   3365 N N      . LEU B 2 71  ? 48.790 12.001  28.225  1.00 17.65 ? 71  LEU C N      1 
ATOM   3366 C CA     . LEU B 2 71  ? 49.394 11.108  27.251  1.00 19.05 ? 71  LEU C CA     1 
ATOM   3367 C C      . LEU B 2 71  ? 48.526 9.939   26.979  1.00 17.30 ? 71  LEU C C      1 
ATOM   3368 O O      . LEU B 2 71  ? 47.969 9.352   27.866  1.00 22.92 ? 71  LEU C O      1 
ATOM   3369 C CB     . LEU B 2 71  ? 50.776 10.647  27.701  1.00 17.54 ? 71  LEU C CB     1 
ATOM   3370 C CG     . LEU B 2 71  ? 52.022 11.463  27.387  1.00 18.44 ? 71  LEU C CG     1 
ATOM   3371 C CD1    . LEU B 2 71  ? 51.792 12.942  27.612  1.00 13.85 ? 71  LEU C CD1    1 
ATOM   3372 C CD2    . LEU B 2 71  ? 53.171 10.975  28.242  1.00 15.50 ? 71  LEU C CD2    1 
ATOM   3373 N N      . ARG B 2 72  ? 48.433 9.580   25.741  1.00 19.13 ? 72  ARG C N      1 
ATOM   3374 C CA     . ARG B 2 72  ? 47.557 8.528   25.339  1.00 17.62 ? 72  ARG C CA     1 
ATOM   3375 C C      . ARG B 2 72  ? 48.054 7.129   25.404  1.00 19.51 ? 72  ARG C C      1 
ATOM   3376 O O      . ARG B 2 72  ? 49.179 6.843   25.052  1.00 27.09 ? 72  ARG C O      1 
ATOM   3377 C CB     . ARG B 2 72  ? 47.097 8.831   23.929  1.00 19.14 ? 72  ARG C CB     1 
ATOM   3378 C CG     . ARG B 2 72  ? 46.507 10.218  23.765  1.00 25.04 ? 72  ARG C CG     1 
ATOM   3379 C CD     . ARG B 2 72  ? 46.447 10.634  22.308  1.00 20.84 ? 72  ARG C CD     1 
ATOM   3380 N NE     . ARG B 2 72  ? 45.738 9.659   21.491  1.00 25.50 ? 72  ARG C NE     1 
ATOM   3381 C CZ     . ARG B 2 72  ? 45.700 9.689   20.166  1.00 29.73 ? 72  ARG C CZ     1 
ATOM   3382 N NH1    . ARG B 2 72  ? 46.327 10.643  19.508  1.00 35.89 ? 72  ARG C NH1    1 
ATOM   3383 N NH2    . ARG B 2 72  ? 45.043 8.766   19.498  1.00 26.19 ? 72  ARG C NH2    1 
ATOM   3384 N N      . LEU B 2 73  ? 47.200 6.235   25.867  1.00 22.30 ? 73  LEU C N      1 
ATOM   3385 C CA     . LEU B 2 73  ? 47.549 4.839   25.941  1.00 22.96 ? 73  LEU C CA     1 
ATOM   3386 C C      . LEU B 2 73  ? 46.800 4.063   24.894  1.00 24.20 ? 73  LEU C C      1 
ATOM   3387 O O      . LEU B 2 73  ? 45.593 4.117   24.853  1.00 29.94 ? 73  LEU C O      1 
ATOM   3388 C CB     . LEU B 2 73  ? 47.283 4.317   27.329  1.00 22.60 ? 73  LEU C CB     1 
ATOM   3389 C CG     . LEU B 2 73  ? 47.832 5.150   28.473  1.00 25.28 ? 73  LEU C CG     1 
ATOM   3390 C CD1    . LEU B 2 73  ? 46.724 5.945   29.141  1.00 25.22 ? 73  LEU C CD1    1 
ATOM   3391 C CD2    . LEU B 2 73  ? 48.490 4.216   29.465  1.00 33.34 ? 73  LEU C CD2    1 
ATOM   3392 N N      . ARG B 2 74  ? 47.505 3.350   24.041  1.00 19.37 ? 74  ARG C N      1 
ATOM   3393 C CA     . ARG B 2 74  ? 46.902 2.618   22.933  1.00 18.42 ? 74  ARG C CA     1 
ATOM   3394 C C      . ARG B 2 74  ? 47.863 1.499   22.536  1.00 24.18 ? 74  ARG C C      1 
ATOM   3395 O O      . ARG B 2 74  ? 48.974 1.401   23.062  1.00 33.54 ? 74  ARG C O      1 
ATOM   3396 C CB     . ARG B 2 74  ? 46.608 3.572   21.771  1.00 15.50 ? 74  ARG C CB     1 
ATOM   3397 C CG     . ARG B 2 74  ? 47.754 4.548   21.532  1.00 19.21 ? 74  ARG C CG     1 
ATOM   3398 C CD     . ARG B 2 74  ? 47.446 5.666   20.566  1.00 19.38 ? 74  ARG C CD     1 
ATOM   3399 N NE     . ARG B 2 74  ? 48.677 6.356   20.219  1.00 18.44 ? 74  ARG C NE     1 
ATOM   3400 C CZ     . ARG B 2 74  ? 48.927 6.893   19.035  1.00 20.12 ? 74  ARG C CZ     1 
ATOM   3401 N NH1    . ARG B 2 74  ? 48.014 6.899   18.073  1.00 17.55 ? 74  ARG C NH1    1 
ATOM   3402 N NH2    . ARG B 2 74  ? 50.130 7.419   18.803  1.00 17.98 ? 74  ARG C NH2    1 
ATOM   3403 N N      . GLY B 2 75  ? 47.440 0.668   21.581  1.00 31.40 ? 75  GLY C N      1 
ATOM   3404 C CA     . GLY B 2 75  ? 48.259 -0.442  21.098  1.00 20.56 ? 75  GLY C CA     1 
ATOM   3405 C C      . GLY B 2 75  ? 48.793 -0.311  19.682  1.00 16.52 ? 75  GLY C C      1 
ATOM   3406 O O      . GLY B 2 75  ? 48.696 0.759   19.079  1.00 17.75 ? 75  GLY C O      1 
ATOM   3407 N N      . ILE C 3 5   ? 10.762 -0.525  -28.705 1.00 65.11 ? 5   ILE B N      1 
ATOM   3408 C CA     . ILE C 3 5   ? 10.496 0.781   -28.039 1.00 51.04 ? 5   ILE B CA     1 
ATOM   3409 C C      . ILE C 3 5   ? 11.806 1.560   -27.898 1.00 40.80 ? 5   ILE B C      1 
ATOM   3410 O O      . ILE C 3 5   ? 12.801 0.980   -27.455 1.00 48.60 ? 5   ILE B O      1 
ATOM   3411 C CB     . ILE C 3 5   ? 9.767  0.583   -26.697 1.00 61.67 ? 5   ILE B CB     1 
ATOM   3412 C CG1    . ILE C 3 5   ? 8.491  -0.245  -26.872 1.00 68.00 ? 5   ILE B CG1    1 
ATOM   3413 C CG2    . ILE C 3 5   ? 9.474  1.916   -26.025 1.00 58.75 ? 5   ILE B CG2    1 
ATOM   3414 C CD1    . ILE C 3 5   ? 7.214  0.545   -26.693 1.00 60.36 ? 5   ILE B CD1    1 
ATOM   3415 N N      . ALA C 3 6   ? 11.779 2.833   -28.269 1.00 27.54 ? 6   ALA B N      1 
ATOM   3416 C CA     . ALA C 3 6   ? 12.992 3.662   -28.213 1.00 32.71 ? 6   ALA B CA     1 
ATOM   3417 C C      . ALA C 3 6   ? 12.960 4.592   -27.005 1.00 22.73 ? 6   ALA B C      1 
ATOM   3418 O O      . ALA C 3 6   ? 11.926 5.164   -26.713 1.00 21.88 ? 6   ALA B O      1 
ATOM   3419 C CB     . ALA C 3 6   ? 13.159 4.425   -29.500 1.00 17.01 ? 6   ALA B CB     1 
ATOM   3420 N N      . ALA C 3 7   ? 14.093 4.705   -26.341 1.00 10.25 ? 7   ALA B N      1 
ATOM   3421 C CA     . ALA C 3 7   ? 14.210 5.627   -25.217 1.00 12.19 ? 7   ALA B CA     1 
ATOM   3422 C C      . ALA C 3 7   ? 14.721 6.968   -25.736 1.00 12.85 ? 7   ALA B C      1 
ATOM   3423 O O      . ALA C 3 7   ? 15.476 6.995   -26.704 1.00 9.88  ? 7   ALA B O      1 
ATOM   3424 C CB     . ALA C 3 7   ? 15.137 5.022   -24.216 1.00 13.69 ? 7   ALA B CB     1 
ATOM   3425 N N      . LEU C 3 8   ? 14.272 8.037   -25.095 1.00 11.41 ? 8   LEU B N      1 
ATOM   3426 C CA     . LEU C 3 8   ? 14.678 9.393   -25.488 1.00 9.81  ? 8   LEU B CA     1 
ATOM   3427 C C      . LEU C 3 8   ? 15.822 9.813   -24.585 1.00 11.84 ? 8   LEU B C      1 
ATOM   3428 O O      . LEU C 3 8   ? 15.878 9.326   -23.466 1.00 15.46 ? 8   LEU B O      1 
ATOM   3429 C CB     . LEU C 3 8   ? 13.481 10.319  -25.296 1.00 12.33 ? 8   LEU B CB     1 
ATOM   3430 C CG     . LEU C 3 8   ? 12.300 10.075  -26.224 1.00 14.72 ? 8   LEU B CG     1 
ATOM   3431 C CD1    . LEU C 3 8   ? 11.306 11.208  -26.133 1.00 11.25 ? 8   LEU B CD1    1 
ATOM   3432 C CD2    . LEU C 3 8   ? 12.762 9.901   -27.651 1.00 15.02 ? 8   LEU B CD2    1 
ATOM   3433 N N      . VAL C 3 9   ? 16.731 10.620  -25.108 1.00 8.84  ? 9   VAL B N      1 
ATOM   3434 C CA     . VAL C 3 9   ? 17.840 11.157  -24.286 1.00 9.42  ? 9   VAL B CA     1 
ATOM   3435 C C      . VAL C 3 9   ? 17.861 12.667  -24.493 1.00 10.28 ? 9   VAL B C      1 
ATOM   3436 O O      . VAL C 3 9   ? 17.966 13.095  -25.610 1.00 9.89  ? 9   VAL B O      1 
ATOM   3437 C CB     . VAL C 3 9   ? 19.196 10.474  -24.554 1.00 8.96  ? 9   VAL B CB     1 
ATOM   3438 C CG1    . VAL C 3 9   ? 20.306 11.097  -23.725 1.00 8.91  ? 9   VAL B CG1    1 
ATOM   3439 C CG2    . VAL C 3 9   ? 19.147 8.978   -24.319 1.00 8.55  ? 9   VAL B CG2    1 
ATOM   3440 N N      . ILE C 3 10  ? 17.672 13.423  -23.425 1.00 8.20  ? 10  ILE B N      1 
ATOM   3441 C CA     . ILE C 3 10  ? 17.731 14.903  -23.512 1.00 10.06 ? 10  ILE B CA     1 
ATOM   3442 C C      . ILE C 3 10  ? 18.771 15.475  -22.553 1.00 11.06 ? 10  ILE B C      1 
ATOM   3443 O O      . ILE C 3 10  ? 18.645 15.265  -21.353 1.00 15.83 ? 10  ILE B O      1 
ATOM   3444 C CB     . ILE C 3 10  ? 16.347 15.585  -23.435 1.00 30.00 ? 10  ILE B CB     1 
ATOM   3445 C CG1    . ILE C 3 10  ? 16.420 17.032  -22.955 1.00 30.00 ? 10  ILE B CG1    1 
ATOM   3446 C CG2    . ILE C 3 10  ? 15.349 14.749  -22.657 1.00 30.00 ? 10  ILE B CG2    1 
ATOM   3447 C CD1    . ILE C 3 10  ? 15.307 17.869  -23.474 1.00 30.00 ? 10  ILE B CD1    1 
ATOM   3448 N N      . ASP C 3 11  ? 19.775 16.148  -23.108 1.00 13.82 ? 11  ASP B N      1 
ATOM   3449 C CA     . ASP C 3 11  ? 20.807 16.846  -22.314 1.00 11.51 ? 11  ASP B CA     1 
ATOM   3450 C C      . ASP C 3 11  ? 20.418 18.317  -22.300 1.00 16.05 ? 11  ASP B C      1 
ATOM   3451 O O      . ASP C 3 11  ? 20.655 18.997  -23.276 1.00 17.66 ? 11  ASP B O      1 
ATOM   3452 C CB     . ASP C 3 11  ? 22.199 16.564  -22.874 1.00 10.03 ? 11  ASP B CB     1 
ATOM   3453 C CG     . ASP C 3 11  ? 23.349 17.284  -22.214 1.00 16.92 ? 11  ASP B CG     1 
ATOM   3454 O OD1    . ASP C 3 11  ? 23.188 17.800  -21.122 1.00 18.20 ? 11  ASP B OD1    1 
ATOM   3455 O OD2    . ASP C 3 11  ? 24.401 17.311  -22.813 1.00 18.84 ? 11  ASP B OD2    1 
ATOM   3456 N N      . ASN C 3 12  ? 19.816 18.760  -21.214 1.00 17.21 ? 12  ASN B N      1 
ATOM   3457 C CA     . ASN C 3 12  ? 19.426 20.172  -21.044 1.00 16.81 ? 12  ASN B CA     1 
ATOM   3458 C C      . ASN C 3 12  ? 20.631 20.932  -20.546 1.00 23.27 ? 12  ASN B C      1 
ATOM   3459 O O      . ASN C 3 12  ? 20.500 21.616  -19.552 1.00 40.49 ? 12  ASN B O      1 
ATOM   3460 C CB     . ASN C 3 12  ? 18.459 20.257  -19.872 1.00 19.38 ? 12  ASN B CB     1 
ATOM   3461 C CG     . ASN C 3 12  ? 17.483 19.107  -19.813 1.00 28.86 ? 12  ASN B CG     1 
ATOM   3462 O OD1    . ASN C 3 12  ? 16.468 19.142  -20.487 1.00 35.68 ? 12  ASN B OD1    1 
ATOM   3463 N ND2    . ASN C 3 12  ? 17.767 18.100  -19.006 1.00 18.57 ? 12  ASN B ND2    1 
ATOM   3464 N N      . GLY C 3 13  ? 21.768 20.799  -21.194 1.00 19.49 ? 13  GLY B N      1 
ATOM   3465 C CA     . GLY C 3 13  ? 22.964 21.395  -20.655 1.00 26.82 ? 13  GLY B CA     1 
ATOM   3466 C C      . GLY C 3 13  ? 23.385 22.803  -20.935 1.00 35.74 ? 13  GLY B C      1 
ATOM   3467 O O      . GLY C 3 13  ? 23.936 23.098  -22.000 1.00 40.42 ? 13  GLY B O      1 
ATOM   3468 N N      . SER C 3 14  ? 23.197 23.668  -19.959 1.00 26.67 ? 14  SER B N      1 
ATOM   3469 C CA     . SER C 3 14  ? 23.523 25.061  -20.122 1.00 24.20 ? 14  SER B CA     1 
ATOM   3470 C C      . SER C 3 14  ? 22.754 25.568  -21.309 1.00 32.00 ? 14  SER B C      1 
ATOM   3471 O O      . SER C 3 14  ? 21.635 25.137  -21.540 1.00 39.17 ? 14  SER B O      1 
ATOM   3472 C CB     . SER C 3 14  ? 25.027 25.328  -20.188 1.00 24.30 ? 14  SER B CB     1 
ATOM   3473 O OG     . SER C 3 14  ? 25.759 24.656  -19.186 1.00 22.88 ? 14  SER B OG     1 
ATOM   3474 N N      . GLY C 3 15  ? 23.343 26.426  -22.107 1.00 27.95 ? 15  GLY B N      1 
ATOM   3475 C CA     . GLY C 3 15  ? 22.636 27.047  -23.204 1.00 26.87 ? 15  GLY B CA     1 
ATOM   3476 C C      . GLY C 3 15  ? 22.120 26.264  -24.356 1.00 25.43 ? 15  GLY B C      1 
ATOM   3477 O O      . GLY C 3 15  ? 21.258 26.703  -25.082 1.00 24.73 ? 15  GLY B O      1 
ATOM   3478 N N      . MET C 3 16  ? 22.692 25.115  -24.567 1.00 28.08 ? 16  MET B N      1 
ATOM   3479 C CA     . MET C 3 16  ? 22.301 24.315  -25.681 1.00 22.99 ? 16  MET B CA     1 
ATOM   3480 C C      . MET C 3 16  ? 21.732 22.991  -25.239 1.00 19.54 ? 16  MET B C      1 
ATOM   3481 O O      . MET C 3 16  ? 22.271 22.333  -24.403 1.00 22.51 ? 16  MET B O      1 
ATOM   3482 C CB     . MET C 3 16  ? 23.473 24.184  -26.625 1.00 24.52 ? 16  MET B CB     1 
ATOM   3483 C CG     . MET C 3 16  ? 23.424 25.110  -27.811 1.00 28.56 ? 16  MET B CG     1 
ATOM   3484 S SD     . MET C 3 16  ? 25.072 25.134  -28.504 1.00 79.10 ? 16  MET B SD     1 
ATOM   3485 C CE     . MET C 3 16  ? 24.726 25.440  -30.232 1.00 66.97 ? 16  MET B CE     1 
ATOM   3486 N N      . CYS C 3 17  ? 20.600 22.632  -25.782 1.00 19.92 ? 17  CYS B N      1 
ATOM   3487 C CA     . CYS C 3 17  ? 19.947 21.409  -25.432 1.00 17.08 ? 17  CYS B CA     1 
ATOM   3488 C C      . CYS C 3 17  ? 20.164 20.355  -26.503 1.00 14.74 ? 17  CYS B C      1 
ATOM   3489 O O      . CYS C 3 17  ? 19.955 20.603  -27.663 1.00 15.49 ? 17  CYS B O      1 
ATOM   3490 C CB     . CYS C 3 17  ? 18.451 21.682  -25.193 1.00 13.89 ? 17  CYS B CB     1 
ATOM   3491 S SG     . CYS C 3 17  ? 17.389 20.243  -25.304 1.00 37.10 ? 17  CYS B SG     1 
ATOM   3492 N N      . LYS C 3 18  ? 20.579 19.173  -26.094 1.00 15.89 ? 18  LYS B N      1 
ATOM   3493 C CA     . LYS C 3 18  ? 20.799 18.088  -27.053 1.00 13.46 ? 18  LYS B CA     1 
ATOM   3494 C C      . LYS C 3 18  ? 19.804 16.962  -26.783 1.00 10.57 ? 18  LYS B C      1 
ATOM   3495 O O      . LYS C 3 18  ? 19.798 16.380  -25.700 1.00 9.22  ? 18  LYS B O      1 
ATOM   3496 C CB     . LYS C 3 18  ? 22.242 17.566  -27.001 1.00 11.39 ? 18  LYS B CB     1 
ATOM   3497 C CG     . LYS C 3 18  ? 23.329 18.638  -27.096 1.00 10.68 ? 18  LYS B CG     1 
ATOM   3498 C CD     . LYS C 3 18  ? 23.750 19.026  -25.693 1.00 14.49 ? 18  LYS B CD     1 
ATOM   3499 C CE     . LYS C 3 18  ? 24.566 20.279  -25.625 1.00 16.01 ? 18  LYS B CE     1 
ATOM   3500 N NZ     . LYS C 3 18  ? 24.819 20.642  -24.197 1.00 20.42 ? 18  LYS B NZ     1 
ATOM   3501 N N      . ALA C 3 19  ? 18.982 16.638  -27.776 1.00 11.73 ? 19  ALA B N      1 
ATOM   3502 C CA     . ALA C 3 19  ? 17.977 15.595  -27.625 1.00 10.67 ? 19  ALA B CA     1 
ATOM   3503 C C      . ALA C 3 19  ? 18.078 14.602  -28.775 1.00 11.46 ? 19  ALA B C      1 
ATOM   3504 O O      . ALA C 3 19  ? 18.630 14.905  -29.832 1.00 16.21 ? 19  ALA B O      1 
ATOM   3505 C CB     . ALA C 3 19  ? 16.560 16.182  -27.565 1.00 10.92 ? 19  ALA B CB     1 
ATOM   3506 N N      . GLY C 3 20  ? 17.500 13.425  -28.581 1.00 8.77  ? 20  GLY B N      1 
ATOM   3507 C CA     . GLY C 3 20  ? 17.548 12.402  -29.607 1.00 12.64 ? 20  GLY B CA     1 
ATOM   3508 C C      . GLY C 3 20  ? 17.193 11.044  -29.023 1.00 13.04 ? 20  GLY B C      1 
ATOM   3509 O O      . GLY C 3 20  ? 16.662 10.949  -27.927 1.00 11.69 ? 20  GLY B O      1 
ATOM   3510 N N      . PHE C 3 21  ? 17.515 10.007  -29.747 1.00 13.10 ? 21  PHE B N      1 
ATOM   3511 C CA     . PHE C 3 21  ? 17.133 8.687   -29.369 1.00 12.72 ? 21  PHE B CA     1 
ATOM   3512 C C      . PHE C 3 21  ? 18.293 7.819   -29.001 1.00 17.23 ? 21  PHE B C      1 
ATOM   3513 O O      . PHE C 3 21  ? 19.333 7.896   -29.604 1.00 21.17 ? 21  PHE B O      1 
ATOM   3514 C CB     . PHE C 3 21  ? 16.366 8.083   -30.534 1.00 11.87 ? 21  PHE B CB     1 
ATOM   3515 C CG     . PHE C 3 21  ? 15.321 8.985   -31.123 1.00 18.97 ? 21  PHE B CG     1 
ATOM   3516 C CD1    . PHE C 3 21  ? 15.628 9.892   -32.125 1.00 23.58 ? 21  PHE B CD1    1 
ATOM   3517 C CD2    . PHE C 3 21  ? 14.021 8.899   -30.699 1.00 15.36 ? 21  PHE B CD2    1 
ATOM   3518 C CE1    . PHE C 3 21  ? 14.665 10.723  -32.646 1.00 21.21 ? 21  PHE B CE1    1 
ATOM   3519 C CE2    . PHE C 3 21  ? 13.052 9.718   -31.229 1.00 17.99 ? 21  PHE B CE2    1 
ATOM   3520 C CZ     . PHE C 3 21  ? 13.373 10.627  -32.204 1.00 18.13 ? 21  PHE B CZ     1 
ATOM   3521 N N      . ALA C 3 22  ? 18.108 6.985   -27.993 1.00 14.27 ? 22  ALA B N      1 
ATOM   3522 C CA     . ALA C 3 22  ? 19.156 6.097   -27.549 1.00 12.38 ? 22  ALA B CA     1 
ATOM   3523 C C      . ALA C 3 22  ? 19.491 4.987   -28.512 1.00 16.22 ? 22  ALA B C      1 
ATOM   3524 O O      . ALA C 3 22  ? 18.624 4.293   -29.005 1.00 15.07 ? 22  ALA B O      1 
ATOM   3525 C CB     . ALA C 3 22  ? 18.846 5.565   -26.186 1.00 11.10 ? 22  ALA B CB     1 
ATOM   3526 N N      . GLY C 3 23  ? 20.764 4.825   -28.784 1.00 15.05 ? 23  GLY B N      1 
ATOM   3527 C CA     . GLY C 3 23  ? 21.198 3.856   -29.746 1.00 16.22 ? 23  GLY B CA     1 
ATOM   3528 C C      . GLY C 3 23  ? 21.931 4.604   -30.810 1.00 18.69 ? 23  GLY B C      1 
ATOM   3529 O O      . GLY C 3 23  ? 22.870 4.101   -31.386 1.00 21.92 ? 23  GLY B O      1 
ATOM   3530 N N      . ASP C 3 24  ? 21.505 5.822   -31.053 1.00 16.79 ? 24  ASP B N      1 
ATOM   3531 C CA     . ASP C 3 24  ? 22.149 6.662   -32.007 1.00 19.47 ? 24  ASP B CA     1 
ATOM   3532 C C      . ASP C 3 24  ? 23.366 7.245   -31.358 1.00 19.96 ? 24  ASP B C      1 
ATOM   3533 O O      . ASP C 3 24  ? 23.414 7.368   -30.161 1.00 20.57 ? 24  ASP B O      1 
ATOM   3534 C CB     . ASP C 3 24  ? 21.191 7.739   -32.474 1.00 23.55 ? 24  ASP B CB     1 
ATOM   3535 C CG     . ASP C 3 24  ? 19.932 7.196   -33.111 1.00 25.70 ? 24  ASP B CG     1 
ATOM   3536 O OD1    . ASP C 3 24  ? 19.856 5.994   -33.393 1.00 23.84 ? 24  ASP B OD1    1 
ATOM   3537 O OD2    . ASP C 3 24  ? 19.009 7.991   -33.344 1.00 23.50 ? 24  ASP B OD2    1 
ATOM   3538 N N      . ASP C 3 25  ? 24.363 7.606   -32.139 1.00 23.01 ? 25  ASP B N      1 
ATOM   3539 C CA     . ASP C 3 25  ? 25.628 8.071   -31.597 1.00 20.72 ? 25  ASP B CA     1 
ATOM   3540 C C      . ASP C 3 25  ? 25.722 9.549   -31.689 1.00 18.22 ? 25  ASP B C      1 
ATOM   3541 O O      . ASP C 3 25  ? 26.757 10.124  -31.452 1.00 20.73 ? 25  ASP B O      1 
ATOM   3542 C CB     . ASP C 3 25  ? 26.789 7.428   -32.354 1.00 25.30 ? 25  ASP B CB     1 
ATOM   3543 C CG     . ASP C 3 25  ? 27.000 5.987   -31.992 1.00 37.93 ? 25  ASP B CG     1 
ATOM   3544 O OD1    . ASP C 3 25  ? 26.584 5.575   -30.893 1.00 39.17 ? 25  ASP B OD1    1 
ATOM   3545 O OD2    . ASP C 3 25  ? 27.593 5.264   -32.813 1.00 34.90 ? 25  ASP B OD2    1 
ATOM   3546 N N      . ALA C 3 26  ? 24.619 10.165  -32.026 1.00 16.75 ? 26  ALA B N      1 
ATOM   3547 C CA     . ALA C 3 26  ? 24.575 11.564  -32.090 1.00 11.92 ? 26  ALA B CA     1 
ATOM   3548 C C      . ALA C 3 26  ? 23.156 12.064  -31.791 1.00 11.92 ? 26  ALA B C      1 
ATOM   3549 O O      . ALA C 3 26  ? 22.234 11.360  -32.113 1.00 12.04 ? 26  ALA B O      1 
ATOM   3550 C CB     . ALA C 3 26  ? 25.036 12.033  -33.444 1.00 11.83 ? 26  ALA B CB     1 
ATOM   3551 N N      . PRO C 3 27  ? 22.968 13.274  -31.160 1.00 10.77 ? 27  PRO B N      1 
ATOM   3552 C CA     . PRO C 3 27  ? 21.605 13.792  -31.010 1.00 11.08 ? 27  PRO B CA     1 
ATOM   3553 C C      . PRO C 3 27  ? 21.065 14.277  -32.338 1.00 13.51 ? 27  PRO B C      1 
ATOM   3554 O O      . PRO C 3 27  ? 21.804 14.838  -33.145 1.00 15.21 ? 27  PRO B O      1 
ATOM   3555 C CB     . PRO C 3 27  ? 21.782 14.961  -30.038 1.00 11.34 ? 27  PRO B CB     1 
ATOM   3556 C CG     . PRO C 3 27  ? 23.224 15.390  -30.232 1.00 10.57 ? 27  PRO B CG     1 
ATOM   3557 C CD     . PRO C 3 27  ? 23.976 14.140  -30.526 1.00 10.05 ? 27  PRO B CD     1 
ATOM   3558 N N      . ARG C 3 28  ? 19.764 14.158  -32.533 1.00 14.21 ? 28  ARG B N      1 
ATOM   3559 C CA     . ARG C 3 28  ? 19.131 14.614  -33.747 1.00 15.85 ? 28  ARG B CA     1 
ATOM   3560 C C      . ARG C 3 28  ? 18.795 16.072  -33.674 1.00 18.46 ? 28  ARG B C      1 
ATOM   3561 O O      . ARG C 3 28  ? 18.743 16.734  -34.690 1.00 20.97 ? 28  ARG B O      1 
ATOM   3562 C CB     . ARG C 3 28  ? 17.874 13.810  -34.013 1.00 12.85 ? 28  ARG B CB     1 
ATOM   3563 C CG     . ARG C 3 28  ? 18.112 12.341  -34.147 1.00 14.87 ? 28  ARG B CG     1 
ATOM   3564 C CD     . ARG C 3 28  ? 18.113 11.913  -35.592 1.00 14.89 ? 28  ARG B CD     1 
ATOM   3565 N NE     . ARG C 3 28  ? 18.216 10.471  -35.663 1.00 19.35 ? 28  ARG B NE     1 
ATOM   3566 C CZ     . ARG C 3 28  ? 17.174 9.660   -35.727 1.00 26.07 ? 28  ARG B CZ     1 
ATOM   3567 N NH1    . ARG C 3 28  ? 15.949 10.152  -35.752 1.00 30.52 ? 28  ARG B NH1    1 
ATOM   3568 N NH2    . ARG C 3 28  ? 17.359 8.355   -35.774 1.00 29.40 ? 28  ARG B NH2    1 
ATOM   3569 N N      . ALA C 3 29  ? 18.601 16.586  -32.479 1.00 12.70 ? 29  ALA B N      1 
ATOM   3570 C CA     . ALA C 3 29  ? 18.187 17.966  -32.299 1.00 18.30 ? 29  ALA B CA     1 
ATOM   3571 C C      . ALA C 3 29  ? 19.154 18.647  -31.350 1.00 16.76 ? 29  ALA B C      1 
ATOM   3572 O O      . ALA C 3 29  ? 19.407 18.149  -30.251 1.00 17.53 ? 29  ALA B O      1 
ATOM   3573 C CB     . ALA C 3 29  ? 16.757 18.043  -31.768 1.00 14.05 ? 29  ALA B CB     1 
ATOM   3574 N N      . VAL C 3 30  ? 19.708 19.762  -31.787 1.00 9.65  ? 30  VAL B N      1 
ATOM   3575 C CA     . VAL C 3 30  ? 20.460 20.647  -30.924 1.00 9.64  ? 30  VAL B CA     1 
ATOM   3576 C C      . VAL C 3 30  ? 19.922 22.029  -31.206 1.00 15.05 ? 30  VAL B C      1 
ATOM   3577 O O      . VAL C 3 30  ? 19.666 22.365  -32.366 1.00 18.59 ? 30  VAL B O      1 
ATOM   3578 C CB     . VAL C 3 30  ? 21.978 20.567  -31.179 1.00 7.62  ? 30  VAL B CB     1 
ATOM   3579 C CG1    . VAL C 3 30  ? 22.736 21.543  -30.287 1.00 8.32  ? 30  VAL B CG1    1 
ATOM   3580 C CG2    . VAL C 3 30  ? 22.478 19.122  -30.976 1.00 9.49  ? 30  VAL B CG2    1 
ATOM   3581 N N      . PHE C 3 31  ? 19.688 22.805  -30.161 1.00 14.18 ? 31  PHE B N      1 
ATOM   3582 C CA     . PHE C 3 31  ? 19.102 24.120  -30.344 1.00 21.93 ? 31  PHE B CA     1 
ATOM   3583 C C      . PHE C 3 31  ? 19.243 24.896  -29.046 1.00 20.74 ? 31  PHE B C      1 
ATOM   3584 O O      . PHE C 3 31  ? 19.429 24.298  -27.982 1.00 19.38 ? 31  PHE B O      1 
ATOM   3585 C CB     . PHE C 3 31  ? 17.634 24.011  -30.754 1.00 22.80 ? 31  PHE B CB     1 
ATOM   3586 C CG     . PHE C 3 31  ? 16.792 23.323  -29.736 1.00 23.59 ? 31  PHE B CG     1 
ATOM   3587 C CD1    . PHE C 3 31  ? 16.175 24.040  -28.717 1.00 23.37 ? 31  PHE B CD1    1 
ATOM   3588 C CD2    . PHE C 3 31  ? 16.626 21.959  -29.787 1.00 19.25 ? 31  PHE B CD2    1 
ATOM   3589 C CE1    . PHE C 3 31  ? 15.405 23.382  -27.775 1.00 25.05 ? 31  PHE B CE1    1 
ATOM   3590 C CE2    . PHE C 3 31  ? 15.858 21.310  -28.858 1.00 20.22 ? 31  PHE B CE2    1 
ATOM   3591 C CZ     . PHE C 3 31  ? 15.252 22.009  -27.856 1.00 20.53 ? 31  PHE B CZ     1 
ATOM   3592 N N      . PRO C 3 32  ? 19.168 26.221  -29.103 1.00 20.89 ? 32  PRO B N      1 
ATOM   3593 C CA     . PRO C 3 32  ? 19.375 27.021  -27.897 1.00 22.72 ? 32  PRO B CA     1 
ATOM   3594 C C      . PRO C 3 32  ? 18.263 26.830  -26.880 1.00 19.81 ? 32  PRO B C      1 
ATOM   3595 O O      . PRO C 3 32  ? 17.099 26.601  -27.211 1.00 20.36 ? 32  PRO B O      1 
ATOM   3596 C CB     . PRO C 3 32  ? 19.413 28.462  -28.426 1.00 18.82 ? 32  PRO B CB     1 
ATOM   3597 C CG     . PRO C 3 32  ? 18.766 28.405  -29.719 1.00 22.81 ? 32  PRO B CG     1 
ATOM   3598 C CD     . PRO C 3 32  ? 19.126 27.072  -30.297 1.00 21.33 ? 32  PRO B CD     1 
ATOM   3599 N N      . SER C 3 33  ? 18.646 26.966  -25.620 1.00 18.81 ? 33  SER B N      1 
ATOM   3600 C CA     . SER C 3 33  ? 17.739 26.812  -24.488 1.00 21.52 ? 33  SER B CA     1 
ATOM   3601 C C      . SER C 3 33  ? 17.073 28.165  -24.185 1.00 24.29 ? 33  SER B C      1 
ATOM   3602 O O      . SER C 3 33  ? 17.312 28.813  -23.160 1.00 28.85 ? 33  SER B O      1 
ATOM   3603 C CB     . SER C 3 33  ? 18.530 26.250  -23.312 1.00 18.12 ? 33  SER B CB     1 
ATOM   3604 O OG     . SER C 3 33  ? 17.945 26.617  -22.102 1.00 32.48 ? 33  SER B OG     1 
ATOM   3605 N N      . ILE C 3 34  ? 16.246 28.605  -25.143 1.00 21.74 ? 34  ILE B N      1 
ATOM   3606 C CA     . ILE C 3 34  ? 15.764 29.984  -25.232 1.00 20.57 ? 34  ILE B CA     1 
ATOM   3607 C C      . ILE C 3 34  ? 14.256 29.996  -25.453 1.00 22.83 ? 34  ILE B C      1 
ATOM   3608 O O      . ILE C 3 34  ? 13.743 29.319  -26.355 1.00 25.42 ? 34  ILE B O      1 
ATOM   3609 C CB     . ILE C 3 34  ? 16.450 30.771  -26.367 1.00 24.88 ? 34  ILE B CB     1 
ATOM   3610 C CG1    . ILE C 3 34  ? 17.973 30.733  -26.236 1.00 27.56 ? 34  ILE B CG1    1 
ATOM   3611 C CG2    . ILE C 3 34  ? 15.999 32.214  -26.348 1.00 24.55 ? 34  ILE B CG2    1 
ATOM   3612 C CD1    . ILE C 3 34  ? 18.693 31.510  -27.341 1.00 27.05 ? 34  ILE B CD1    1 
ATOM   3613 N N      . VAL C 3 35  ? 13.559 30.790  -24.646 1.00 20.73 ? 35  VAL B N      1 
ATOM   3614 C CA     . VAL C 3 35  ? 12.127 31.038  -24.763 1.00 25.09 ? 35  VAL B CA     1 
ATOM   3615 C C      . VAL C 3 35  ? 11.924 32.546  -24.828 1.00 25.86 ? 35  VAL B C      1 
ATOM   3616 O O      . VAL C 3 35  ? 12.476 33.282  -24.000 1.00 22.46 ? 35  VAL B O      1 
ATOM   3617 C CB     . VAL C 3 35  ? 11.331 30.460  -23.574 1.00 31.43 ? 35  VAL B CB     1 
ATOM   3618 C CG1    . VAL C 3 35  ? 9.858  30.804  -23.724 1.00 32.85 ? 35  VAL B CG1    1 
ATOM   3619 C CG2    . VAL C 3 35  ? 11.555 28.939  -23.392 1.00 22.57 ? 35  VAL B CG2    1 
ATOM   3620 N N      . GLY C 3 36  ? 11.120 32.988  -25.798 1.00 30.26 ? 36  GLY B N      1 
ATOM   3621 C CA     . GLY C 3 36  ? 10.715 34.379  -25.926 1.00 27.85 ? 36  GLY B CA     1 
ATOM   3622 C C      . GLY C 3 36  ? 9.219  34.517  -26.117 1.00 32.79 ? 36  GLY B C      1 
ATOM   3623 O O      . GLY C 3 36  ? 8.590  33.714  -26.819 1.00 32.97 ? 36  GLY B O      1 
ATOM   3624 N N      . ARG C 3 37  ? 8.642  35.531  -25.487 1.00 40.00 ? 37  ARG B N      1 
ATOM   3625 C CA     . ARG C 3 37  ? 7.254  35.923  -25.673 1.00 33.97 ? 37  ARG B CA     1 
ATOM   3626 C C      . ARG C 3 37  ? 7.174  37.324  -26.265 1.00 31.21 ? 37  ARG B C      1 
ATOM   3627 O O      . ARG C 3 37  ? 8.136  38.099  -26.193 1.00 35.12 ? 37  ARG B O      1 
ATOM   3628 C CB     . ARG C 3 37  ? 6.486  35.878  -24.344 1.00 39.00 ? 37  ARG B CB     1 
ATOM   3629 C CG     . ARG C 3 37  ? 6.393  34.499  -23.724 1.00 42.09 ? 37  ARG B CG     1 
ATOM   3630 C CD     . ARG C 3 37  ? 6.115  34.587  -22.231 1.00 39.91 ? 37  ARG B CD     1 
ATOM   3631 N NE     . ARG C 3 37  ? 5.896  33.265  -21.658 1.00 57.53 ? 37  ARG B NE     1 
ATOM   3632 C CZ     . ARG C 3 37  ? 6.851  32.494  -21.155 1.00 49.66 ? 37  ARG B CZ     1 
ATOM   3633 N NH1    . ARG C 3 37  ? 8.101  32.920  -21.056 1.00 44.69 ? 37  ARG B NH1    1 
ATOM   3634 N NH2    . ARG C 3 37  ? 6.547  31.259  -20.760 1.00 43.83 ? 37  ARG B NH2    1 
ATOM   3635 N N      . PRO C 3 38  ? 6.036  37.681  -26.859 1.00 31.67 ? 38  PRO B N      1 
ATOM   3636 C CA     . PRO C 3 38  ? 5.916  38.993  -27.509 1.00 32.29 ? 38  PRO B CA     1 
ATOM   3637 C C      . PRO C 3 38  ? 6.276  40.139  -26.572 1.00 32.04 ? 38  PRO B C      1 
ATOM   3638 O O      . PRO C 3 38  ? 5.987  40.106  -25.374 1.00 27.96 ? 38  PRO B O      1 
ATOM   3639 C CB     . PRO C 3 38  ? 4.438  39.049  -27.919 1.00 38.68 ? 38  PRO B CB     1 
ATOM   3640 C CG     . PRO C 3 38  ? 4.003  37.608  -27.996 1.00 33.15 ? 38  PRO B CG     1 
ATOM   3641 C CD     . PRO C 3 38  ? 4.791  36.895  -26.939 1.00 37.10 ? 38  PRO B CD     1 
ATOM   3642 N N      . ARG C 3 39  ? 6.928  41.159  -27.136 1.00 35.12 ? 39  ARG B N      1 
ATOM   3643 C CA     . ARG C 3 39  ? 7.220  42.377  -26.388 1.00 38.96 ? 39  ARG B CA     1 
ATOM   3644 C C      . ARG C 3 39  ? 5.975  43.244  -26.256 1.00 32.37 ? 39  ARG B C      1 
ATOM   3645 O O      . ARG C 3 39  ? 5.650  43.713  -25.163 1.00 29.56 ? 39  ARG B O      1 
ATOM   3646 C CB     . ARG C 3 39  ? 8.349  43.159  -27.065 1.00 45.66 ? 39  ARG B CB     1 
ATOM   3647 C CG     . ARG C 3 39  ? 9.738  42.614  -26.783 1.00 47.12 ? 39  ARG B CG     1 
ATOM   3648 C CD     . ARG C 3 39  ? 10.814 43.319  -27.599 1.00 50.41 ? 39  ARG B CD     1 
ATOM   3649 N NE     . ARG C 3 39  ? 11.117 44.653  -27.091 1.00 64.58 ? 39  ARG B NE     1 
ATOM   3650 C CZ     . ARG C 3 39  ? 12.149 45.390  -27.485 1.00 78.02 ? 39  ARG B CZ     1 
ATOM   3651 N NH1    . ARG C 3 39  ? 13.010 44.950  -28.393 1.00 73.47 ? 39  ARG B NH1    1 
ATOM   3652 N NH2    . ARG C 3 39  ? 12.325 46.597  -26.953 1.00 80.73 ? 39  ARG B NH2    1 
ATOM   3653 N N      . HIS C 3 40  ? 5.266  43.450  -27.359 1.00 33.03 ? 40  HIS B N      1 
ATOM   3654 C CA     . HIS C 3 40  ? 3.982  44.133  -27.380 1.00 33.52 ? 40  HIS B CA     1 
ATOM   3655 C C      . HIS C 3 40  ? 2.886  43.146  -27.767 1.00 33.81 ? 40  HIS B C      1 
ATOM   3656 O O      . HIS C 3 40  ? 3.145  42.102  -28.378 1.00 27.78 ? 40  HIS B O      1 
ATOM   3657 C CB     . HIS C 3 40  ? 4.007  45.310  -28.362 1.00 34.81 ? 40  HIS B CB     1 
ATOM   3658 C CG     . HIS C 3 40  ? 5.263  46.118  -28.290 1.00 54.36 ? 40  HIS B CG     1 
ATOM   3659 N ND1    . HIS C 3 40  ? 5.562  46.939  -27.222 1.00 57.56 ? 40  HIS B ND1    1 
ATOM   3660 C CD2    . HIS C 3 40  ? 6.310  46.213  -29.143 1.00 54.17 ? 40  HIS B CD2    1 
ATOM   3661 C CE1    . HIS C 3 40  ? 6.736  47.510  -27.426 1.00 58.14 ? 40  HIS B CE1    1 
ATOM   3662 N NE2    . HIS C 3 40  ? 7.212  47.085  -28.584 1.00 60.70 ? 40  HIS B NE2    1 
ATOM   3663 N N      . GLN C 3 41  ? 1.648  43.481  -27.395 1.00 27.43 ? 41  GLN B N      1 
ATOM   3664 C CA     . GLN C 3 41  ? 0.534  42.570  -27.624 1.00 20.87 ? 41  GLN B CA     1 
ATOM   3665 C C      . GLN C 3 41  ? 0.053  42.584  -29.070 1.00 28.13 ? 41  GLN B C      1 
ATOM   3666 O O      . GLN C 3 41  ? -0.519 41.586  -29.531 1.00 26.35 ? 41  GLN B O      1 
ATOM   3667 C CB     . GLN C 3 41  ? -0.621 42.902  -26.673 1.00 25.43 ? 41  GLN B CB     1 
ATOM   3668 C CG     . GLN C 3 41  ? -0.344 42.578  -25.210 1.00 27.36 ? 41  GLN B CG     1 
ATOM   3669 C CD     . GLN C 3 41  ? -1.528 42.850  -24.265 1.00 28.98 ? 41  GLN B CD     1 
ATOM   3670 O OE1    . GLN C 3 41  ? -2.507 43.530  -24.624 1.00 28.39 ? 41  GLN B OE1    1 
ATOM   3671 N NE2    . GLN C 3 41  ? -1.432 42.312  -23.045 1.00 28.03 ? 41  GLN B NE2    1 
ATOM   3672 N N      . GLY C 3 42  ? 0.287  43.681  -29.793 1.00 29.80 ? 42  GLY B N      1 
ATOM   3673 C CA     . GLY C 3 42  ? -0.151 43.812  -31.175 1.00 29.49 ? 42  GLY B CA     1 
ATOM   3674 C C      . GLY C 3 42  ? 0.306  42.697  -32.098 1.00 31.17 ? 42  GLY B C      1 
ATOM   3675 O O      . GLY C 3 42  ? -0.229 42.575  -33.206 1.00 37.45 ? 42  GLY B O      1 
ATOM   3676 N N      . VAL C 3 43  ? 1.282  41.889  -31.676 1.00 31.62 ? 43  VAL B N      1 
ATOM   3677 C CA     . VAL C 3 43  ? 1.805  40.815  -32.511 1.00 31.04 ? 43  VAL B CA     1 
ATOM   3678 C C      . VAL C 3 43  ? 1.152  39.473  -32.233 1.00 36.16 ? 43  VAL B C      1 
ATOM   3679 O O      . VAL C 3 43  ? 1.406  38.512  -32.977 1.00 45.52 ? 43  VAL B O      1 
ATOM   3680 C CB     . VAL C 3 43  ? 3.327  40.677  -32.343 1.00 28.86 ? 43  VAL B CB     1 
ATOM   3681 C CG1    . VAL C 3 43  ? 3.904  39.996  -33.567 1.00 35.26 ? 43  VAL B CG1    1 
ATOM   3682 C CG2    . VAL C 3 43  ? 3.937  42.035  -32.114 1.00 32.21 ? 43  VAL B CG2    1 
ATOM   3683 N N      . MET C 3 44  ? 0.356  39.361  -31.175 1.00 32.19 ? 44  MET B N      1 
ATOM   3684 C CA     . MET C 3 44  ? -0.389 38.137  -30.920 1.00 38.03 ? 44  MET B CA     1 
ATOM   3685 C C      . MET C 3 44  ? -1.694 38.081  -31.696 1.00 38.77 ? 44  MET B C      1 
ATOM   3686 O O      . MET C 3 44  ? -2.326 37.018  -31.758 1.00 39.30 ? 44  MET B O      1 
ATOM   3687 C CB     . MET C 3 44  ? -0.676 37.997  -29.427 1.00 29.76 ? 44  MET B CB     1 
ATOM   3688 C CG     . MET C 3 44  ? 0.406  37.254  -28.663 1.00 38.63 ? 44  MET B CG     1 
ATOM   3689 S SD     . MET C 3 44  ? 0.099  37.119  -26.888 1.00 50.08 ? 44  MET B SD     1 
ATOM   3690 C CE     . MET C 3 44  ? 0.375  38.814  -26.367 1.00 27.60 ? 44  MET B CE     1 
ATOM   3691 N N      . VAL C 3 45  ? -2.093 39.197  -32.297 1.00 34.83 ? 45  VAL B N      1 
ATOM   3692 C CA     . VAL C 3 45  ? -3.406 39.300  -32.906 1.00 34.33 ? 45  VAL B CA     1 
ATOM   3693 C C      . VAL C 3 45  ? -3.489 38.358  -34.097 1.00 33.89 ? 45  VAL B C      1 
ATOM   3694 O O      . VAL C 3 45  ? -2.582 38.307  -34.939 1.00 48.87 ? 45  VAL B O      1 
ATOM   3695 C CB     . VAL C 3 45  ? -3.685 40.759  -33.300 1.00 37.72 ? 45  VAL B CB     1 
ATOM   3696 C CG1    . VAL C 3 45  ? -2.594 41.265  -34.239 1.00 40.36 ? 45  VAL B CG1    1 
ATOM   3697 C CG2    . VAL C 3 45  ? -5.040 40.881  -33.949 1.00 40.22 ? 45  VAL B CG2    1 
ATOM   3698 N N      . GLY C 3 46  ? -4.581 37.600  -34.170 1.00 40.32 ? 46  GLY B N      1 
ATOM   3699 C CA     . GLY C 3 46  ? -4.799 36.672  -35.269 1.00 46.60 ? 46  GLY B CA     1 
ATOM   3700 C C      . GLY C 3 46  ? -3.825 35.515  -35.340 1.00 52.39 ? 46  GLY B C      1 
ATOM   3701 O O      . GLY C 3 46  ? -3.678 34.906  -36.407 1.00 55.39 ? 46  GLY B O      1 
ATOM   3702 N N      . MET C 3 47  ? -3.163 35.185  -34.227 1.00 44.44 ? 47  MET B N      1 
ATOM   3703 C CA     . MET C 3 47  ? -2.095 34.191  -34.196 1.00 50.31 ? 47  MET B CA     1 
ATOM   3704 C C      . MET C 3 47  ? -2.488 32.963  -33.387 1.00 50.90 ? 47  MET B C      1 
ATOM   3705 O O      . MET C 3 47  ? -1.631 32.285  -32.818 1.00 50.90 ? 47  MET B O      1 
ATOM   3706 C CB     . MET C 3 47  ? -0.801 34.799  -33.649 1.00 52.43 ? 47  MET B CB     1 
ATOM   3707 C CG     . MET C 3 47  ? -0.076 35.735  -34.628 1.00 58.84 ? 47  MET B CG     1 
ATOM   3708 S SD     . MET C 3 47  ? 0.286  34.994  -36.244 1.00 83.07 ? 47  MET B SD     1 
ATOM   3709 C CE     . MET C 3 47  ? 1.203  36.329  -37.027 1.00 53.67 ? 47  MET B CE     1 
ATOM   3710 N N      . GLY C 3 48  ? -3.787 32.686  -33.320 1.00 52.76 ? 48  GLY B N      1 
ATOM   3711 C CA     . GLY C 3 48  ? -4.296 31.433  -32.797 1.00 60.54 ? 48  GLY B CA     1 
ATOM   3712 C C      . GLY C 3 48  ? -3.782 31.057  -31.420 1.00 66.52 ? 48  GLY B C      1 
ATOM   3713 O O      . GLY C 3 48  ? -3.166 29.998  -31.244 1.00 70.91 ? 48  GLY B O      1 
ATOM   3714 N N      . GLN C 3 49  ? -4.023 31.919  -30.432 1.00 58.17 ? 49  GLN B N      1 
ATOM   3715 C CA     . GLN C 3 49  ? -3.758 31.578  -29.039 1.00 62.14 ? 49  GLN B CA     1 
ATOM   3716 C C      . GLN C 3 49  ? -2.317 31.134  -28.803 1.00 69.76 ? 49  GLN B C      1 
ATOM   3717 O O      . GLN C 3 49  ? -1.984 30.681  -27.702 1.00 67.53 ? 49  GLN B O      1 
ATOM   3718 C CB     . GLN C 3 49  ? -4.729 30.495  -28.573 1.00 63.20 ? 49  GLN B CB     1 
ATOM   3719 C CG     . GLN C 3 49  ? -6.182 30.878  -28.779 1.00 62.11 ? 49  GLN B CG     1 
ATOM   3720 C CD     . GLN C 3 49  ? -7.108 29.685  -28.794 1.00 66.01 ? 49  GLN B CD     1 
ATOM   3721 O OE1    . GLN C 3 49  ? -7.963 29.560  -29.686 1.00 54.56 ? 49  GLN B OE1    1 
ATOM   3722 N NE2    . GLN C 3 49  ? -6.947 28.791  -27.808 1.00 59.25 ? 49  GLN B NE2    1 
ATOM   3723 N N      . LYS C 3 50  ? -1.454 31.265  -29.812 1.00 64.70 ? 50  LYS B N      1 
ATOM   3724 C CA     . LYS C 3 50  ? -0.027 31.104  -29.583 1.00 64.83 ? 50  LYS B CA     1 
ATOM   3725 C C      . LYS C 3 50  ? 0.501  32.299  -28.790 1.00 65.78 ? 50  LYS B C      1 
ATOM   3726 O O      . LYS C 3 50  ? 0.029  33.431  -28.943 1.00 68.22 ? 50  LYS B O      1 
ATOM   3727 C CB     . LYS C 3 50  ? 0.722  30.954  -30.910 1.00 60.69 ? 50  LYS B CB     1 
ATOM   3728 C CG     . LYS C 3 50  ? 1.028  32.264  -31.633 1.00 64.39 ? 50  LYS B CG     1 
ATOM   3729 C CD     . LYS C 3 50  ? 2.329  32.872  -31.126 1.00 58.92 ? 50  LYS B CD     1 
ATOM   3730 C CE     . LYS C 3 50  ? 2.660  34.186  -31.828 1.00 57.33 ? 50  LYS B CE     1 
ATOM   3731 N NZ     . LYS C 3 50  ? 1.681  35.271  -31.556 1.00 47.33 ? 50  LYS B NZ     1 
ATOM   3732 N N      . ASP C 3 51  ? 1.478  32.031  -27.925 1.00 55.06 ? 51  ASP B N      1 
ATOM   3733 C CA     . ASP C 3 51  ? 2.014  33.049  -27.033 1.00 53.30 ? 51  ASP B CA     1 
ATOM   3734 C C      . ASP C 3 51  ? 3.525  33.017  -26.940 1.00 49.83 ? 51  ASP B C      1 
ATOM   3735 O O      . ASP C 3 51  ? 4.102  33.942  -26.360 1.00 40.30 ? 51  ASP B O      1 
ATOM   3736 C CB     . ASP C 3 51  ? 1.405  32.881  -25.628 1.00 57.86 ? 51  ASP B CB     1 
ATOM   3737 C CG     . ASP C 3 51  ? 2.152  33.667  -24.547 1.00 72.48 ? 51  ASP B CG     1 
ATOM   3738 O OD1    . ASP C 3 51  ? 2.216  34.918  -24.648 1.00 75.33 ? 51  ASP B OD1    1 
ATOM   3739 O OD2    . ASP C 3 51  ? 2.650  33.029  -23.582 1.00 72.54 ? 51  ASP B OD2    1 
ATOM   3740 N N      . SER C 3 52  ? 4.185  32.029  -27.537 1.00 48.58 ? 52  SER B N      1 
ATOM   3741 C CA     . SER C 3 52  ? 5.556  31.711  -27.193 1.00 42.51 ? 52  SER B CA     1 
ATOM   3742 C C      . SER C 3 52  ? 6.303  31.226  -28.424 1.00 38.95 ? 52  SER B C      1 
ATOM   3743 O O      . SER C 3 52  ? 5.716  30.676  -29.360 1.00 38.93 ? 52  SER B O      1 
ATOM   3744 C CB     . SER C 3 52  ? 5.596  30.656  -26.076 1.00 44.54 ? 52  SER B CB     1 
ATOM   3745 O OG     . SER C 3 52  ? 4.841  29.503  -26.424 1.00 51.00 ? 52  SER B OG     1 
ATOM   3746 N N      . TYR C 3 53  ? 7.609  31.467  -28.406 1.00 34.39 ? 53  TYR B N      1 
ATOM   3747 C CA     . TYR C 3 53  ? 8.561  30.933  -29.361 1.00 37.32 ? 53  TYR B CA     1 
ATOM   3748 C C      . TYR C 3 53  ? 9.722  30.348  -28.578 1.00 37.11 ? 53  TYR B C      1 
ATOM   3749 O O      . TYR C 3 53  ? 10.163 30.940  -27.588 1.00 35.98 ? 53  TYR B O      1 
ATOM   3750 C CB     . TYR C 3 53  ? 9.066  32.017  -30.310 1.00 40.58 ? 53  TYR B CB     1 
ATOM   3751 C CG     . TYR C 3 53  ? 8.071  32.414  -31.367 1.00 40.47 ? 53  TYR B CG     1 
ATOM   3752 C CD1    . TYR C 3 53  ? 7.732  31.530  -32.383 1.00 41.30 ? 53  TYR B CD1    1 
ATOM   3753 C CD2    . TYR C 3 53  ? 7.484  33.671  -31.365 1.00 35.29 ? 53  TYR B CD2    1 
ATOM   3754 C CE1    . TYR C 3 53  ? 6.833  31.870  -33.365 1.00 42.30 ? 53  TYR B CE1    1 
ATOM   3755 C CE2    . TYR C 3 53  ? 6.575  34.024  -32.351 1.00 50.73 ? 53  TYR B CE2    1 
ATOM   3756 C CZ     . TYR C 3 53  ? 6.255  33.115  -33.356 1.00 52.16 ? 53  TYR B CZ     1 
ATOM   3757 O OH     . TYR C 3 53  ? 5.354  33.442  -34.355 1.00 54.54 ? 53  TYR B OH     1 
ATOM   3758 N N      . VAL C 3 54  ? 10.221 29.200  -29.022 1.00 34.84 ? 54  VAL B N      1 
ATOM   3759 C CA     . VAL C 3 54  ? 11.189 28.422  -28.258 1.00 36.47 ? 54  VAL B CA     1 
ATOM   3760 C C      . VAL C 3 54  ? 12.319 27.977  -29.175 1.00 34.14 ? 54  VAL B C      1 
ATOM   3761 O O      . VAL C 3 54  ? 12.074 27.378  -30.224 1.00 31.95 ? 54  VAL B O      1 
ATOM   3762 C CB     . VAL C 3 54  ? 10.514 27.206  -27.593 1.00 34.42 ? 54  VAL B CB     1 
ATOM   3763 C CG1    . VAL C 3 54  ? 11.533 26.181  -27.169 1.00 28.38 ? 54  VAL B CG1    1 
ATOM   3764 C CG2    . VAL C 3 54  ? 9.685  27.652  -26.396 1.00 33.73 ? 54  VAL B CG2    1 
ATOM   3765 N N      . GLY C 3 55  ? 13.548 28.268  -28.780 1.00 32.40 ? 55  GLY B N      1 
ATOM   3766 C CA     . GLY C 3 55  ? 14.712 27.706  -29.447 1.00 28.31 ? 55  GLY B CA     1 
ATOM   3767 C C      . GLY C 3 55  ? 15.207 28.595  -30.561 1.00 33.35 ? 55  GLY B C      1 
ATOM   3768 O O      . GLY C 3 55  ? 15.391 29.789  -30.369 1.00 34.43 ? 55  GLY B O      1 
ATOM   3769 N N      . ASP C 3 56  ? 15.404 28.006  -31.741 1.00 41.48 ? 56  ASP B N      1 
ATOM   3770 C CA     . ASP C 3 56  ? 15.970 28.762  -32.855 1.00 38.02 ? 56  ASP B CA     1 
ATOM   3771 C C      . ASP C 3 56  ? 15.035 29.879  -33.304 1.00 43.59 ? 56  ASP B C      1 
ATOM   3772 O O      . ASP C 3 56  ? 15.462 31.030  -33.482 1.00 35.59 ? 56  ASP B O      1 
ATOM   3773 C CB     . ASP C 3 56  ? 16.291 27.818  -34.011 1.00 35.51 ? 56  ASP B CB     1 
ATOM   3774 C CG     . ASP C 3 56  ? 17.741 27.404  -34.016 1.00 41.58 ? 56  ASP B CG     1 
ATOM   3775 O OD1    . ASP C 3 56  ? 18.599 28.292  -33.807 1.00 52.41 ? 56  ASP B OD1    1 
ATOM   3776 O OD2    . ASP C 3 56  ? 18.031 26.202  -34.215 1.00 33.98 ? 56  ASP B OD2    1 
ATOM   3777 N N      . GLU C 3 57  ? 13.744 29.549  -33.480 1.00 44.95 ? 57  GLU B N      1 
ATOM   3778 C CA     . GLU C 3 57  ? 12.762 30.520  -33.953 1.00 36.32 ? 57  GLU B CA     1 
ATOM   3779 C C      . GLU C 3 57  ? 12.640 31.708  -33.005 1.00 35.34 ? 57  GLU B C      1 
ATOM   3780 O O      . GLU C 3 57  ? 12.250 32.803  -33.424 1.00 34.20 ? 57  GLU B O      1 
ATOM   3781 C CB     . GLU C 3 57  ? 11.404 29.841  -34.142 1.00 34.21 ? 57  GLU B CB     1 
ATOM   3782 C CG     . GLU C 3 57  ? 10.454 30.647  -35.030 1.00 43.14 ? 57  GLU B CG     1 
ATOM   3783 C CD     . GLU C 3 57  ? 9.331  29.812  -35.647 1.00 57.86 ? 57  GLU B CD     1 
ATOM   3784 O OE1    . GLU C 3 57  ? 8.809  28.897  -34.969 1.00 70.68 ? 57  GLU B OE1    1 
ATOM   3785 O OE2    . GLU C 3 57  ? 8.964  30.078  -36.814 1.00 49.30 ? 57  GLU B OE2    1 
ATOM   3786 N N      . ALA C 3 58  ? 12.980 31.516  -31.732 1.00 36.96 ? 58  ALA B N      1 
ATOM   3787 C CA     . ALA C 3 58  ? 13.004 32.636  -30.799 1.00 34.74 ? 58  ALA B CA     1 
ATOM   3788 C C      . ALA C 3 58  ? 14.216 33.530  -31.021 1.00 37.54 ? 58  ALA B C      1 
ATOM   3789 O O      . ALA C 3 58  ? 14.154 34.733  -30.735 1.00 36.29 ? 58  ALA B O      1 
ATOM   3790 C CB     . ALA C 3 58  ? 12.991 32.128  -29.358 1.00 34.63 ? 58  ALA B CB     1 
ATOM   3791 N N      . GLN C 3 59  ? 15.326 32.969  -31.515 1.00 38.68 ? 59  GLN B N      1 
ATOM   3792 C CA     . GLN C 3 59  ? 16.489 33.801  -31.809 1.00 37.48 ? 59  GLN B CA     1 
ATOM   3793 C C      . GLN C 3 59  ? 16.286 34.642  -33.061 1.00 38.42 ? 59  GLN B C      1 
ATOM   3794 O O      . GLN C 3 59  ? 16.786 35.775  -33.130 1.00 39.48 ? 59  GLN B O      1 
ATOM   3795 C CB     . GLN C 3 59  ? 17.750 32.951  -31.958 1.00 40.20 ? 59  GLN B CB     1 
ATOM   3796 C CG     . GLN C 3 59  ? 18.708 33.028  -30.755 1.00 46.80 ? 59  GLN B CG     1 
ATOM   3797 C CD     . GLN C 3 59  ? 19.324 34.414  -30.540 1.00 45.69 ? 59  GLN B CD     1 
ATOM   3798 O OE1    . GLN C 3 59  ? 19.338 34.933  -29.420 1.00 42.58 ? 59  GLN B OE1    1 
ATOM   3799 N NE2    . GLN C 3 59  ? 19.853 35.003  -31.606 1.00 42.98 ? 59  GLN B NE2    1 
ATOM   3800 N N      . SER C 3 60  ? 15.559 34.120  -34.052 1.00 39.43 ? 60  SER B N      1 
ATOM   3801 C CA     . SER C 3 60  ? 15.308 34.897  -35.265 1.00 43.50 ? 60  SER B CA     1 
ATOM   3802 C C      . SER C 3 60  ? 14.427 36.112  -34.988 1.00 46.26 ? 60  SER B C      1 
ATOM   3803 O O      . SER C 3 60  ? 14.501 37.118  -35.702 1.00 43.42 ? 60  SER B O      1 
ATOM   3804 C CB     . SER C 3 60  ? 14.654 34.016  -36.334 1.00 40.05 ? 60  SER B CB     1 
ATOM   3805 O OG     . SER C 3 60  ? 15.301 32.758  -36.447 1.00 39.81 ? 60  SER B OG     1 
ATOM   3806 N N      . LYS C 3 61  ? 13.598 36.048  -33.954 1.00 41.97 ? 61  LYS B N      1 
ATOM   3807 C CA     . LYS C 3 61  ? 12.589 37.069  -33.729 1.00 31.11 ? 61  LYS B CA     1 
ATOM   3808 C C      . LYS C 3 61  ? 12.835 37.838  -32.444 1.00 38.04 ? 61  LYS B C      1 
ATOM   3809 O O      . LYS C 3 61  ? 11.907 38.444  -31.904 1.00 39.56 ? 61  LYS B O      1 
ATOM   3810 C CB     . LYS C 3 61  ? 11.209 36.427  -33.727 1.00 27.38 ? 61  LYS B CB     1 
ATOM   3811 C CG     . LYS C 3 61  ? 11.031 35.453  -34.883 1.00 35.48 ? 61  LYS B CG     1 
ATOM   3812 C CD     . LYS C 3 61  ? 9.585  34.959  -34.993 1.00 38.49 ? 61  LYS B CD     1 
ATOM   3813 C CE     . LYS C 3 61  ? 9.361  34.304  -36.332 1.00 31.47 ? 61  LYS B CE     1 
ATOM   3814 N NZ     . LYS C 3 61  ? 8.192  33.414  -36.336 1.00 42.60 ? 61  LYS B NZ     1 
ATOM   3815 N N      . ARG C 3 62  ? 14.073 37.841  -31.951 1.00 35.55 ? 62  ARG B N      1 
ATOM   3816 C CA     . ARG C 3 62  ? 14.380 38.579  -30.731 1.00 35.74 ? 62  ARG B CA     1 
ATOM   3817 C C      . ARG C 3 62  ? 13.988 40.044  -30.818 1.00 36.17 ? 62  ARG B C      1 
ATOM   3818 O O      . ARG C 3 62  ? 13.864 40.697  -29.780 1.00 39.72 ? 62  ARG B O      1 
ATOM   3819 C CB     . ARG C 3 62  ? 15.867 38.458  -30.387 1.00 48.51 ? 62  ARG B CB     1 
ATOM   3820 C CG     . ARG C 3 62  ? 16.811 38.571  -31.578 1.00 44.10 ? 62  ARG B CG     1 
ATOM   3821 C CD     . ARG C 3 62  ? 18.218 38.126  -31.204 1.00 42.40 ? 62  ARG B CD     1 
ATOM   3822 N NE     . ARG C 3 62  ? 19.064 37.986  -32.383 1.00 49.69 ? 62  ARG B NE     1 
ATOM   3823 C CZ     . ARG C 3 62  ? 19.746 38.980  -32.939 1.00 48.86 ? 62  ARG B CZ     1 
ATOM   3824 N NH1    . ARG C 3 62  ? 19.698 40.209  -32.447 1.00 47.55 ? 62  ARG B NH1    1 
ATOM   3825 N NH2    . ARG C 3 62  ? 20.491 38.737  -34.020 1.00 40.69 ? 62  ARG B NH2    1 
ATOM   3826 N N      . GLY C 3 63  ? 13.787 40.580  -32.023 1.00 44.86 ? 63  GLY B N      1 
ATOM   3827 C CA     . GLY C 3 63  ? 13.325 41.955  -32.142 1.00 42.75 ? 63  GLY B CA     1 
ATOM   3828 C C      . GLY C 3 63  ? 11.883 42.133  -31.716 1.00 42.76 ? 63  GLY B C      1 
ATOM   3829 O O      . GLY C 3 63  ? 11.534 43.155  -31.112 1.00 46.53 ? 63  GLY B O      1 
ATOM   3830 N N      . ILE C 3 64  ? 11.035 41.134  -31.990 1.00 44.46 ? 64  ILE B N      1 
ATOM   3831 C CA     . ILE C 3 64  ? 9.633  41.172  -31.571 1.00 48.69 ? 64  ILE B CA     1 
ATOM   3832 C C      . ILE C 3 64  ? 9.370  40.385  -30.285 1.00 37.26 ? 64  ILE B C      1 
ATOM   3833 O O      . ILE C 3 64  ? 8.219  40.325  -29.822 1.00 36.20 ? 64  ILE B O      1 
ATOM   3834 C CB     . ILE C 3 64  ? 8.702  40.679  -32.697 1.00 31.21 ? 64  ILE B CB     1 
ATOM   3835 C CG1    . ILE C 3 64  ? 8.647  39.154  -32.745 1.00 33.64 ? 64  ILE B CG1    1 
ATOM   3836 C CG2    . ILE C 3 64  ? 9.193  41.187  -34.004 1.00 30.50 ? 64  ILE B CG2    1 
ATOM   3837 C CD1    . ILE C 3 64  ? 7.801  38.620  -33.887 1.00 25.23 ? 64  ILE B CD1    1 
ATOM   3838 N N      . LEU C 3 65  ? 10.408 39.862  -29.656 1.00 37.12 ? 65  LEU B N      1 
ATOM   3839 C CA     . LEU C 3 65  ? 10.251 39.039  -28.467 1.00 37.31 ? 65  LEU B CA     1 
ATOM   3840 C C      . LEU C 3 65  ? 11.099 39.393  -27.275 1.00 33.17 ? 65  LEU B C      1 
ATOM   3841 O O      . LEU C 3 65  ? 12.149 39.975  -27.428 1.00 32.33 ? 65  LEU B O      1 
ATOM   3842 C CB     . LEU C 3 65  ? 10.529 37.574  -28.812 1.00 31.83 ? 65  LEU B CB     1 
ATOM   3843 C CG     . LEU C 3 65  ? 9.825  36.826  -29.924 1.00 32.24 ? 65  LEU B CG     1 
ATOM   3844 C CD1    . LEU C 3 65  ? 10.434 35.449  -29.989 1.00 35.92 ? 65  LEU B CD1    1 
ATOM   3845 C CD2    . LEU C 3 65  ? 8.329  36.756  -29.711 1.00 35.93 ? 65  LEU B CD2    1 
ATOM   3846 N N      . THR C 3 66  ? 10.623 39.064  -26.074 1.00 36.08 ? 66  THR B N      1 
ATOM   3847 C CA     . THR C 3 66  ? 11.429 39.245  -24.861 1.00 39.61 ? 66  THR B CA     1 
ATOM   3848 C C      . THR C 3 66  ? 11.952 37.877  -24.483 1.00 33.94 ? 66  THR B C      1 
ATOM   3849 O O      . THR C 3 66  ? 11.202 36.992  -24.177 1.00 34.68 ? 66  THR B O      1 
ATOM   3850 C CB     . THR C 3 66  ? 10.727 39.992  -23.702 1.00 34.28 ? 66  THR B CB     1 
ATOM   3851 O OG1    . THR C 3 66  ? 11.356 39.662  -22.463 1.00 32.40 ? 66  THR B OG1    1 
ATOM   3852 C CG2    . THR C 3 66  ? 9.265  39.662  -23.619 1.00 39.09 ? 66  THR B CG2    1 
ATOM   3853 N N      . LEU C 3 67  ? 13.255 37.712  -24.510 1.00 39.36 ? 67  LEU B N      1 
ATOM   3854 C CA     . LEU C 3 67  ? 13.843 36.402  -24.285 1.00 33.66 ? 67  LEU B CA     1 
ATOM   3855 C C      . LEU C 3 67  ? 14.259 36.056  -22.887 1.00 33.14 ? 67  LEU B C      1 
ATOM   3856 O O      . LEU C 3 67  ? 14.808 36.876  -22.174 1.00 27.45 ? 67  LEU B O      1 
ATOM   3857 C CB     . LEU C 3 67  ? 15.008 36.166  -25.252 1.00 26.25 ? 67  LEU B CB     1 
ATOM   3858 C CG     . LEU C 3 67  ? 14.882 36.471  -26.739 1.00 28.83 ? 67  LEU B CG     1 
ATOM   3859 C CD1    . LEU C 3 67  ? 16.227 36.278  -27.405 1.00 28.44 ? 67  LEU B CD1    1 
ATOM   3860 C CD2    . LEU C 3 67  ? 13.849 35.588  -27.398 1.00 28.91 ? 67  LEU B CD2    1 
ATOM   3861 N N      . LYS C 3 68  ? 13.982 34.819  -22.500 1.00 33.92 ? 68  LYS B N      1 
ATOM   3862 C CA     . LYS C 3 68  ? 14.333 34.349  -21.180 1.00 34.33 ? 68  LYS B CA     1 
ATOM   3863 C C      . LYS C 3 68  ? 15.159 33.062  -21.291 1.00 21.48 ? 68  LYS B C      1 
ATOM   3864 O O      . LYS C 3 68  ? 14.928 32.242  -22.154 1.00 19.09 ? 68  LYS B O      1 
ATOM   3865 C CB     . LYS C 3 68  ? 13.080 34.217  -20.312 1.00 28.23 ? 68  LYS B CB     1 
ATOM   3866 C CG     . LYS C 3 68  ? 12.423 35.540  -19.968 1.00 24.85 ? 68  LYS B CG     1 
ATOM   3867 C CD     . LYS C 3 68  ? 11.928 35.573  -18.538 1.00 28.28 ? 68  LYS B CD     1 
ATOM   3868 C CE     . LYS C 3 68  ? 10.613 34.835  -18.384 1.00 37.85 ? 68  LYS B CE     1 
ATOM   3869 N NZ     . LYS C 3 68  ? 10.149 34.831  -16.972 1.00 44.54 ? 68  LYS B NZ     1 
ATOM   3870 N N      . TYR C 3 69  ? 16.170 32.934  -20.455 1.00 24.27 ? 69  TYR B N      1 
ATOM   3871 C CA     . TYR C 3 69  ? 17.042 31.762  -20.460 1.00 29.33 ? 69  TYR B CA     1 
ATOM   3872 C C      . TYR C 3 69  ? 16.929 30.949  -19.173 1.00 28.06 ? 69  TYR B C      1 
ATOM   3873 O O      . TYR C 3 69  ? 17.521 31.288  -18.169 1.00 21.76 ? 69  TYR B O      1 
ATOM   3874 C CB     . TYR C 3 69  ? 18.455 32.246  -20.677 1.00 28.22 ? 69  TYR B CB     1 
ATOM   3875 C CG     . TYR C 3 69  ? 18.594 33.177  -21.856 1.00 37.32 ? 69  TYR B CG     1 
ATOM   3876 C CD1    . TYR C 3 69  ? 18.815 32.682  -23.126 1.00 27.79 ? 69  TYR B CD1    1 
ATOM   3877 C CD2    . TYR C 3 69  ? 18.497 34.556  -21.702 1.00 34.38 ? 69  TYR B CD2    1 
ATOM   3878 C CE1    . TYR C 3 69  ? 18.932 33.525  -24.206 1.00 24.16 ? 69  TYR B CE1    1 
ATOM   3879 C CE2    . TYR C 3 69  ? 18.607 35.403  -22.781 1.00 24.19 ? 69  TYR B CE2    1 
ATOM   3880 C CZ     . TYR C 3 69  ? 18.827 34.879  -24.032 1.00 31.11 ? 69  TYR B CZ     1 
ATOM   3881 O OH     . TYR C 3 69  ? 18.949 35.710  -25.116 1.00 27.15 ? 69  TYR B OH     1 
ATOM   3882 N N      . PRO C 3 70  ? 16.183 29.852  -19.216 1.00 26.24 ? 70  PRO B N      1 
ATOM   3883 C CA     . PRO C 3 70  ? 15.933 29.052  -18.016 1.00 24.91 ? 70  PRO B CA     1 
ATOM   3884 C C      . PRO C 3 70  ? 17.066 28.224  -17.398 1.00 28.98 ? 70  PRO B C      1 
ATOM   3885 O O      . PRO C 3 70  ? 16.958 27.907  -16.232 1.00 27.18 ? 70  PRO B O      1 
ATOM   3886 C CB     . PRO C 3 70  ? 14.759 28.183  -18.418 1.00 22.91 ? 70  PRO B CB     1 
ATOM   3887 C CG     . PRO C 3 70  ? 14.303 28.666  -19.747 1.00 26.78 ? 70  PRO B CG     1 
ATOM   3888 C CD     . PRO C 3 70  ? 15.471 29.322  -20.380 1.00 18.97 ? 70  PRO B CD     1 
ATOM   3889 N N      . ILE C 3 71  ? 18.067 27.830  -18.167 1.00 28.78 ? 71  ILE B N      1 
ATOM   3890 C CA     . ILE C 3 71  ? 19.143 27.013  -17.657 1.00 31.42 ? 71  ILE B CA     1 
ATOM   3891 C C      . ILE C 3 71  ? 20.470 27.612  -18.110 1.00 34.44 ? 71  ILE B C      1 
ATOM   3892 O O      . ILE C 3 71  ? 21.198 27.029  -18.878 1.00 36.36 ? 71  ILE B O      1 
ATOM   3893 C CB     . ILE C 3 71  ? 18.876 25.520  -18.024 1.00 23.67 ? 71  ILE B CB     1 
ATOM   3894 C CG1    . ILE C 3 71  ? 19.789 24.565  -17.299 1.00 30.50 ? 71  ILE B CG1    1 
ATOM   3895 C CG2    . ILE C 3 71  ? 18.851 25.266  -19.516 1.00 25.35 ? 71  ILE B CG2    1 
ATOM   3896 C CD1    . ILE C 3 71  ? 19.181 23.194  -17.181 1.00 28.89 ? 71  ILE B CD1    1 
ATOM   3897 N N      . GLU C 3 72  ? 20.808 28.784  -17.606 1.00 30.87 ? 72  GLU B N      1 
ATOM   3898 C CA     . GLU C 3 72  ? 22.009 29.475  -18.064 1.00 28.59 ? 72  GLU B CA     1 
ATOM   3899 C C      . GLU C 3 72  ? 23.198 29.036  -17.314 1.00 30.56 ? 72  GLU B C      1 
ATOM   3900 O O      . GLU C 3 72  ? 24.308 29.129  -17.788 1.00 27.06 ? 72  GLU B O      1 
ATOM   3901 C CB     . GLU C 3 72  ? 21.844 30.965  -17.882 1.00 30.72 ? 72  GLU B CB     1 
ATOM   3902 C CG     . GLU C 3 72  ? 21.719 31.740  -19.172 1.00 44.88 ? 72  GLU B CG     1 
ATOM   3903 C CD     . GLU C 3 72  ? 21.615 33.227  -18.929 1.00 56.08 ? 72  GLU B CD     1 
ATOM   3904 O OE1    . GLU C 3 72  ? 21.192 33.615  -17.824 1.00 46.82 ? 72  GLU B OE1    1 
ATOM   3905 O OE2    . GLU C 3 72  ? 21.953 34.002  -19.845 1.00 57.78 ? 72  GLU B OE2    1 
ATOM   3906 N N      . HIS C 3 73  ? 22.987 28.515  -16.126 1.00 36.97 ? 73  HIS B N      1 
ATOM   3907 C CA     . HIS C 3 73  ? 24.067 27.987  -15.338 1.00 28.81 ? 73  HIS B CA     1 
ATOM   3908 C C      . HIS C 3 73  ? 23.836 26.528  -15.052 1.00 27.03 ? 73  HIS B C      1 
ATOM   3909 O O      . HIS C 3 73  ? 24.287 26.030  -14.041 1.00 32.28 ? 73  HIS B O      1 
ATOM   3910 C CB     . HIS C 3 73  ? 24.163 28.767  -14.077 1.00 26.63 ? 73  HIS B CB     1 
ATOM   3911 C CG     . HIS C 3 73  ? 24.450 30.215  -14.302 1.00 35.94 ? 73  HIS B CG     1 
ATOM   3912 N ND1    . HIS C 3 73  ? 25.637 30.657  -14.839 1.00 39.04 ? 73  HIS B ND1    1 
ATOM   3913 C CD2    . HIS C 3 73  ? 23.695 31.317  -14.096 1.00 37.53 ? 73  HIS B CD2    1 
ATOM   3914 C CE1    . HIS C 3 73  ? 25.609 31.973  -14.938 1.00 41.02 ? 73  HIS B CE1    1 
ATOM   3915 N NE2    . HIS C 3 73  ? 24.440 32.398  -14.495 1.00 45.07 ? 73  HIS B NE2    1 
ATOM   3916 N N      . GLY C 3 74  ? 23.140 25.842  -15.942 1.00 16.96 ? 74  GLY B N      1 
ATOM   3917 C CA     . GLY C 3 74  ? 22.896 24.436  -15.776 1.00 20.11 ? 74  GLY B CA     1 
ATOM   3918 C C      . GLY C 3 74  ? 21.869 24.065  -14.736 1.00 17.82 ? 74  GLY B C      1 
ATOM   3919 O O      . GLY C 3 74  ? 21.460 22.905  -14.688 1.00 18.66 ? 74  GLY B O      1 
ATOM   3920 N N      . ILE C 3 75  ? 21.395 25.009  -13.977 1.00 18.60 ? 75  ILE B N      1 
ATOM   3921 C CA     . ILE C 3 75  ? 20.345 24.745  -13.047 1.00 23.71 ? 75  ILE B CA     1 
ATOM   3922 C C      . ILE C 3 75  ? 19.075 25.399  -13.559 1.00 23.88 ? 75  ILE B C      1 
ATOM   3923 O O      . ILE C 3 75  ? 19.073 26.589  -13.807 1.00 22.10 ? 75  ILE B O      1 
ATOM   3924 C CB     . ILE C 3 75  ? 20.733 25.194  -11.629 1.00 20.78 ? 75  ILE B CB     1 
ATOM   3925 C CG1    . ILE C 3 75  ? 21.818 24.283  -11.064 1.00 20.09 ? 75  ILE B CG1    1 
ATOM   3926 C CG2    . ILE C 3 75  ? 19.546 25.173  -10.693 1.00 21.21 ? 75  ILE B CG2    1 
ATOM   3927 C CD1    . ILE C 3 75  ? 23.005 25.028  -10.504 1.00 31.54 ? 75  ILE B CD1    1 
ATOM   3928 N N      . VAL C 3 76  ? 18.037 24.609  -13.817 1.00 21.62 ? 76  VAL B N      1 
ATOM   3929 C CA     . VAL C 3 76  ? 16.729 25.134  -14.199 1.00 18.70 ? 76  VAL B CA     1 
ATOM   3930 C C      . VAL C 3 76  ? 16.295 26.188  -13.199 1.00 19.07 ? 76  VAL B C      1 
ATOM   3931 O O      . VAL C 3 76  ? 16.314 25.942  -11.989 1.00 16.58 ? 76  VAL B O      1 
ATOM   3932 C CB     . VAL C 3 76  ? 15.694 23.996  -14.236 1.00 19.05 ? 76  VAL B CB     1 
ATOM   3933 C CG1    . VAL C 3 76  ? 14.294 24.579  -14.409 1.00 20.69 ? 76  VAL B CG1    1 
ATOM   3934 C CG2    . VAL C 3 76  ? 16.036 22.910  -15.294 1.00 13.48 ? 76  VAL B CG2    1 
ATOM   3935 N N      . THR C 3 77  ? 15.870 27.362  -13.690 1.00 20.59 ? 77  THR B N      1 
ATOM   3936 C CA     . THR C 3 77  ? 15.352 28.401  -12.790 1.00 18.00 ? 77  THR B CA     1 
ATOM   3937 C C      . THR C 3 77  ? 13.900 28.808  -13.030 1.00 18.82 ? 77  THR B C      1 
ATOM   3938 O O      . THR C 3 77  ? 13.243 29.237  -12.088 1.00 26.87 ? 77  THR B O      1 
ATOM   3939 C CB     . THR C 3 77  ? 16.234 29.657  -12.827 1.00 18.18 ? 77  THR B CB     1 
ATOM   3940 O OG1    . THR C 3 77  ? 16.612 29.951  -14.174 1.00 26.66 ? 77  THR B OG1    1 
ATOM   3941 C CG2    . THR C 3 77  ? 17.470 29.411  -12.036 1.00 16.78 ? 77  THR B CG2    1 
ATOM   3942 N N      . ASN C 3 78  ? 13.364 28.668  -14.234 1.00 21.32 ? 78  ASN B N      1 
ATOM   3943 C CA     . ASN C 3 78  ? 11.943 28.918  -14.464 1.00 27.66 ? 78  ASN B CA     1 
ATOM   3944 C C      . ASN C 3 78  ? 11.302 27.658  -15.015 1.00 23.45 ? 78  ASN B C      1 
ATOM   3945 O O      . ASN C 3 78  ? 11.562 27.276  -16.158 1.00 26.47 ? 78  ASN B O      1 
ATOM   3946 C CB     . ASN C 3 78  ? 11.709 30.084  -15.421 1.00 32.91 ? 78  ASN B CB     1 
ATOM   3947 C CG     . ASN C 3 78  ? 10.268 30.561  -15.403 1.00 39.17 ? 78  ASN B CG     1 
ATOM   3948 O OD1    . ASN C 3 78  ? 9.488  30.210  -14.511 1.00 44.55 ? 78  ASN B OD1    1 
ATOM   3949 N ND2    . ASN C 3 78  ? 9.913  31.387  -16.369 1.00 45.82 ? 78  ASN B ND2    1 
ATOM   3950 N N      . TRP C 3 79  ? 10.430 27.044  -14.233 1.00 26.17 ? 79  TRP B N      1 
ATOM   3951 C CA     . TRP C 3 79  ? 9.814  25.796  -14.656 1.00 23.27 ? 79  TRP B CA     1 
ATOM   3952 C C      . TRP C 3 79  ? 8.662  25.997  -15.624 1.00 32.39 ? 79  TRP B C      1 
ATOM   3953 O O      . TRP C 3 79  ? 8.329  25.061  -16.359 1.00 34.62 ? 79  TRP B O      1 
ATOM   3954 C CB     . TRP C 3 79  ? 9.338  25.024  -13.439 1.00 23.80 ? 79  TRP B CB     1 
ATOM   3955 C CG     . TRP C 3 79  ? 10.458 24.608  -12.573 1.00 24.95 ? 79  TRP B CG     1 
ATOM   3956 C CD1    . TRP C 3 79  ? 10.847 25.179  -11.398 1.00 21.41 ? 79  TRP B CD1    1 
ATOM   3957 C CD2    . TRP C 3 79  ? 11.352 23.525  -12.817 1.00 18.83 ? 79  TRP B CD2    1 
ATOM   3958 N NE1    . TRP C 3 79  ? 11.934 24.516  -10.893 1.00 19.20 ? 79  TRP B NE1    1 
ATOM   3959 C CE2    . TRP C 3 79  ? 12.263 23.487  -11.741 1.00 27.19 ? 79  TRP B CE2    1 
ATOM   3960 C CE3    . TRP C 3 79  ? 11.469 22.579  -13.835 1.00 17.56 ? 79  TRP B CE3    1 
ATOM   3961 C CZ2    . TRP C 3 79  ? 13.288 22.527  -11.657 1.00 25.87 ? 79  TRP B CZ2    1 
ATOM   3962 C CZ3    . TRP C 3 79  ? 12.472 21.635  -13.755 1.00 21.61 ? 79  TRP B CZ3    1 
ATOM   3963 C CH2    . TRP C 3 79  ? 13.372 21.613  -12.673 1.00 23.00 ? 79  TRP B CH2    1 
ATOM   3964 N N      . ASP C 3 80  ? 8.037  27.180  -15.645 1.00 33.90 ? 80  ASP B N      1 
ATOM   3965 C CA     . ASP C 3 80  ? 7.075  27.458  -16.707 1.00 32.40 ? 80  ASP B CA     1 
ATOM   3966 C C      . ASP C 3 80  ? 7.775  27.519  -18.057 1.00 29.43 ? 80  ASP B C      1 
ATOM   3967 O O      . ASP C 3 80  ? 7.296  26.943  -19.043 1.00 26.05 ? 80  ASP B O      1 
ATOM   3968 C CB     . ASP C 3 80  ? 6.321  28.762  -16.423 1.00 37.21 ? 80  ASP B CB     1 
ATOM   3969 C CG     . ASP C 3 80  ? 5.249  28.605  -15.347 1.00 41.35 ? 80  ASP B CG     1 
ATOM   3970 O OD1    . ASP C 3 80  ? 4.629  27.512  -15.246 1.00 34.62 ? 80  ASP B OD1    1 
ATOM   3971 O OD2    . ASP C 3 80  ? 5.018  29.586  -14.608 1.00 43.48 ? 80  ASP B OD2    1 
ATOM   3972 N N      . ASP C 3 81  ? 8.921  28.201  -18.116 1.00 31.72 ? 81  ASP B N      1 
ATOM   3973 C CA     . ASP C 3 81  ? 9.699  28.215  -19.347 1.00 30.22 ? 81  ASP B CA     1 
ATOM   3974 C C      . ASP C 3 81  ? 10.279 26.837  -19.659 1.00 29.65 ? 81  ASP B C      1 
ATOM   3975 O O      . ASP C 3 81  ? 10.316 26.424  -20.827 1.00 25.42 ? 81  ASP B O      1 
ATOM   3976 C CB     . ASP C 3 81  ? 10.804 29.266  -19.248 1.00 32.16 ? 81  ASP B CB     1 
ATOM   3977 C CG     . ASP C 3 81  ? 10.259 30.672  -19.084 1.00 44.93 ? 81  ASP B CG     1 
ATOM   3978 O OD1    . ASP C 3 81  ? 9.033  30.868  -19.271 1.00 49.13 ? 81  ASP B OD1    1 
ATOM   3979 O OD2    . ASP C 3 81  ? 11.052 31.581  -18.748 1.00 42.41 ? 81  ASP B OD2    1 
ATOM   3980 N N      . MET C 3 82  ? 10.733 26.100  -18.646 1.00 28.52 ? 82  MET B N      1 
ATOM   3981 C CA     . MET C 3 82  ? 11.376 24.834  -18.967 1.00 21.82 ? 82  MET B CA     1 
ATOM   3982 C C      . MET C 3 82  ? 10.386 23.834  -19.547 1.00 20.19 ? 82  MET B C      1 
ATOM   3983 O O      . MET C 3 82  ? 10.785 22.995  -20.361 1.00 22.19 ? 82  MET B O      1 
ATOM   3984 C CB     . MET C 3 82  ? 12.080 24.269  -17.740 1.00 23.51 ? 82  MET B CB     1 
ATOM   3985 C CG     . MET C 3 82  ? 12.879 22.989  -17.990 1.00 22.85 ? 82  MET B CG     1 
ATOM   3986 S SD     . MET C 3 82  ? 14.294 23.051  -19.123 1.00 22.33 ? 82  MET B SD     1 
ATOM   3987 C CE     . MET C 3 82  ? 15.068 24.579  -18.614 1.00 25.05 ? 82  MET B CE     1 
ATOM   3988 N N      . GLU C 3 83  ? 9.103  23.915  -19.163 1.00 22.68 ? 83  GLU B N      1 
ATOM   3989 C CA     . GLU C 3 83  ? 8.085  23.055  -19.770 1.00 22.02 ? 83  GLU B CA     1 
ATOM   3990 C C      . GLU C 3 83  ? 7.935  23.350  -21.250 1.00 23.43 ? 83  GLU B C      1 
ATOM   3991 O O      . GLU C 3 83  ? 7.683  22.442  -22.054 1.00 26.69 ? 83  GLU B O      1 
ATOM   3992 C CB     . GLU C 3 83  ? 6.720  23.239  -19.103 1.00 29.05 ? 83  GLU B CB     1 
ATOM   3993 C CG     . GLU C 3 83  ? 6.515  22.576  -17.770 1.00 29.23 ? 83  GLU B CG     1 
ATOM   3994 C CD     . GLU C 3 83  ? 5.134  22.859  -17.210 1.00 32.55 ? 83  GLU B CD     1 
ATOM   3995 O OE1    . GLU C 3 83  ? 4.201  22.925  -18.043 1.00 36.01 ? 83  GLU B OE1    1 
ATOM   3996 O OE2    . GLU C 3 83  ? 4.986  23.029  -15.964 1.00 33.79 ? 83  GLU B OE2    1 
ATOM   3997 N N      . LYS C 3 84  ? 8.035  24.619  -21.631 1.00 21.51 ? 84  LYS B N      1 
ATOM   3998 C CA     . LYS C 3 84  ? 7.903  24.942  -23.042 1.00 24.15 ? 84  LYS B CA     1 
ATOM   3999 C C      . LYS C 3 84  ? 9.104  24.445  -23.818 1.00 21.16 ? 84  LYS B C      1 
ATOM   4000 O O      . LYS C 3 84  ? 8.957  23.908  -24.922 1.00 26.81 ? 84  LYS B O      1 
ATOM   4001 C CB     . LYS C 3 84  ? 7.679  26.439  -23.207 1.00 25.07 ? 84  LYS B CB     1 
ATOM   4002 C CG     . LYS C 3 84  ? 6.407  26.831  -22.475 1.00 34.46 ? 84  LYS B CG     1 
ATOM   4003 C CD     . LYS C 3 84  ? 6.069  28.304  -22.519 1.00 44.15 ? 84  LYS B CD     1 
ATOM   4004 C CE     . LYS C 3 84  ? 4.898  28.577  -21.562 1.00 60.67 ? 84  LYS B CE     1 
ATOM   4005 N NZ     . LYS C 3 84  ? 3.741  27.620  -21.782 1.00 45.19 ? 84  LYS B NZ     1 
ATOM   4006 N N      . ILE C 3 85  ? 10.294 24.556  -23.230 1.00 18.66 ? 85  ILE B N      1 
ATOM   4007 C CA     . ILE C 3 85  ? 11.471 23.974  -23.863 1.00 15.94 ? 85  ILE B CA     1 
ATOM   4008 C C      . ILE C 3 85  ? 11.303 22.478  -24.027 1.00 17.48 ? 85  ILE B C      1 
ATOM   4009 O O      . ILE C 3 85  ? 11.771 21.898  -25.010 1.00 18.89 ? 85  ILE B O      1 
ATOM   4010 C CB     . ILE C 3 85  ? 12.742 24.295  -23.069 1.00 16.05 ? 85  ILE B CB     1 
ATOM   4011 C CG1    . ILE C 3 85  ? 13.211 25.706  -23.390 1.00 14.12 ? 85  ILE B CG1    1 
ATOM   4012 C CG2    . ILE C 3 85  ? 13.795 23.316  -23.430 1.00 12.99 ? 85  ILE B CG2    1 
ATOM   4013 C CD1    . ILE C 3 85  ? 14.305 26.203  -22.462 1.00 20.58 ? 85  ILE B CD1    1 
ATOM   4014 N N      . TRP C 3 86  ? 10.614 21.826  -23.090 1.00 17.81 ? 86  TRP B N      1 
ATOM   4015 C CA     . TRP C 3 86  ? 10.477 20.381  -23.171 1.00 15.80 ? 86  TRP B CA     1 
ATOM   4016 C C      . TRP C 3 86  ? 9.368  19.976  -24.125 1.00 17.50 ? 86  TRP B C      1 
ATOM   4017 O O      . TRP C 3 86  ? 9.489  18.971  -24.835 1.00 17.43 ? 86  TRP B O      1 
ATOM   4018 C CB     . TRP C 3 86  ? 10.230 19.811  -21.788 1.00 18.09 ? 86  TRP B CB     1 
ATOM   4019 C CG     . TRP C 3 86  ? 11.489 19.560  -21.050 1.00 19.40 ? 86  TRP B CG     1 
ATOM   4020 C CD1    . TRP C 3 86  ? 12.701 19.220  -21.577 1.00 17.60 ? 86  TRP B CD1    1 
ATOM   4021 C CD2    . TRP C 3 86  ? 11.670 19.624  -19.636 1.00 22.66 ? 86  TRP B CD2    1 
ATOM   4022 N NE1    . TRP C 3 86  ? 13.627 19.068  -20.573 1.00 18.96 ? 86  TRP B NE1    1 
ATOM   4023 C CE2    . TRP C 3 86  ? 13.015 19.312  -19.371 1.00 23.77 ? 86  TRP B CE2    1 
ATOM   4024 C CE3    . TRP C 3 86  ? 10.820 19.911  -18.566 1.00 18.81 ? 86  TRP B CE3    1 
ATOM   4025 C CZ2    . TRP C 3 86  ? 13.527 19.290  -18.086 1.00 24.31 ? 86  TRP B CZ2    1 
ATOM   4026 C CZ3    . TRP C 3 86  ? 11.328 19.888  -17.306 1.00 18.38 ? 86  TRP B CZ3    1 
ATOM   4027 C CH2    . TRP C 3 86  ? 12.667 19.573  -17.068 1.00 25.74 ? 86  TRP B CH2    1 
ATOM   4028 N N      . HIS C 3 87  ? 8.278  20.735  -24.142 1.00 18.12 ? 87  HIS B N      1 
ATOM   4029 C CA     . HIS C 3 87  ? 7.270  20.524  -25.169 1.00 20.24 ? 87  HIS B CA     1 
ATOM   4030 C C      . HIS C 3 87  ? 7.903  20.607  -26.551 1.00 23.99 ? 87  HIS B C      1 
ATOM   4031 O O      . HIS C 3 87  ? 7.763  19.696  -27.382 1.00 21.32 ? 87  HIS B O      1 
ATOM   4032 C CB     . HIS C 3 87  ? 6.156  21.559  -25.021 1.00 20.75 ? 87  HIS B CB     1 
ATOM   4033 C CG     . HIS C 3 87  ? 4.898  21.173  -25.717 1.00 20.73 ? 87  HIS B CG     1 
ATOM   4034 N ND1    . HIS C 3 87  ? 4.679  21.444  -27.048 1.00 22.09 ? 87  HIS B ND1    1 
ATOM   4035 C CD2    . HIS C 3 87  ? 3.803  20.509  -25.278 1.00 24.36 ? 87  HIS B CD2    1 
ATOM   4036 C CE1    . HIS C 3 87  ? 3.494  20.979  -27.399 1.00 31.38 ? 87  HIS B CE1    1 
ATOM   4037 N NE2    . HIS C 3 87  ? 2.945  20.403  -26.344 1.00 31.64 ? 87  HIS B NE2    1 
ATOM   4038 N N      . HIS C 3 88  ? 8.642  21.692  -26.793 1.00 21.91 ? 88  HIS B N      1 
ATOM   4039 C CA     . HIS C 3 88  ? 9.316  21.898  -28.062 1.00 21.35 ? 88  HIS B CA     1 
ATOM   4040 C C      . HIS C 3 88  ? 10.230 20.729  -28.429 1.00 22.96 ? 88  HIS B C      1 
ATOM   4041 O O      . HIS C 3 88  ? 10.270 20.309  -29.591 1.00 23.32 ? 88  HIS B O      1 
ATOM   4042 C CB     . HIS C 3 88  ? 10.095 23.207  -28.001 1.00 25.05 ? 88  HIS B CB     1 
ATOM   4043 C CG     . HIS C 3 88  ? 10.836 23.531  -29.258 1.00 29.14 ? 88  HIS B CG     1 
ATOM   4044 N ND1    . HIS C 3 88  ? 10.198 23.837  -30.441 1.00 30.18 ? 88  HIS B ND1    1 
ATOM   4045 C CD2    . HIS C 3 88  ? 12.163 23.602  -29.514 1.00 28.44 ? 88  HIS B CD2    1 
ATOM   4046 C CE1    . HIS C 3 88  ? 11.102 24.079  -31.372 1.00 35.66 ? 88  HIS B CE1    1 
ATOM   4047 N NE2    . HIS C 3 88  ? 12.302 23.943  -30.836 1.00 33.89 ? 88  HIS B NE2    1 
ATOM   4048 N N      . THR C 3 89  ? 10.968 20.178  -27.462 1.00 20.26 ? 89  THR B N      1 
ATOM   4049 C CA     . THR C 3 89  ? 11.904 19.127  -27.842 1.00 22.69 ? 89  THR B CA     1 
ATOM   4050 C C      . THR C 3 89  ? 11.172 17.829  -28.139 1.00 21.50 ? 89  THR B C      1 
ATOM   4051 O O      . THR C 3 89  ? 11.531 17.119  -29.080 1.00 25.43 ? 89  THR B O      1 
ATOM   4052 C CB     . THR C 3 89  ? 12.982 18.900  -26.772 1.00 23.47 ? 89  THR B CB     1 
ATOM   4053 O OG1    . THR C 3 89  ? 12.464 18.068  -25.738 1.00 35.48 ? 89  THR B OG1    1 
ATOM   4054 C CG2    . THR C 3 89  ? 13.465 20.207  -26.166 1.00 19.21 ? 89  THR B CG2    1 
ATOM   4055 N N      . PHE C 3 90  ? 10.130 17.514  -27.374 1.00 21.07 ? 90  PHE B N      1 
ATOM   4056 C CA     . PHE C 3 90  ? 9.398  16.271  -27.606 1.00 22.71 ? 90  PHE B CA     1 
ATOM   4057 C C      . PHE C 3 90  ? 8.580  16.347  -28.889 1.00 23.68 ? 90  PHE B C      1 
ATOM   4058 O O      . PHE C 3 90  ? 8.755  15.535  -29.808 1.00 22.94 ? 90  PHE B O      1 
ATOM   4059 C CB     . PHE C 3 90  ? 8.486  15.977  -26.421 1.00 22.88 ? 90  PHE B CB     1 
ATOM   4060 C CG     . PHE C 3 90  ? 9.194  15.532  -25.188 1.00 16.58 ? 90  PHE B CG     1 
ATOM   4061 C CD1    . PHE C 3 90  ? 10.069 14.456  -25.216 1.00 16.03 ? 90  PHE B CD1    1 
ATOM   4062 C CD2    . PHE C 3 90  ? 8.951  16.176  -23.984 1.00 16.30 ? 90  PHE B CD2    1 
ATOM   4063 C CE1    . PHE C 3 90  ? 10.696 14.036  -24.068 1.00 16.98 ? 90  PHE B CE1    1 
ATOM   4064 C CE2    . PHE C 3 90  ? 9.568  15.764  -22.827 1.00 15.70 ? 90  PHE B CE2    1 
ATOM   4065 C CZ     . PHE C 3 90  ? 10.449 14.693  -22.863 1.00 14.78 ? 90  PHE B CZ     1 
ATOM   4066 N N      . TYR C 3 91  ? 7.696  17.343  -28.979 1.00 24.71 ? 91  TYR B N      1 
ATOM   4067 C CA     . TYR C 3 91  ? 6.698  17.364  -30.040 1.00 28.06 ? 91  TYR B CA     1 
ATOM   4068 C C      . TYR C 3 91  ? 7.234  17.933  -31.349 1.00 32.99 ? 91  TYR B C      1 
ATOM   4069 O O      . TYR C 3 91  ? 6.746  17.558  -32.422 1.00 35.65 ? 91  TYR B O      1 
ATOM   4070 C CB     . TYR C 3 91  ? 5.467  18.149  -29.582 1.00 26.88 ? 91  TYR B CB     1 
ATOM   4071 C CG     . TYR C 3 91  ? 4.729  17.448  -28.464 1.00 24.91 ? 91  TYR B CG     1 
ATOM   4072 C CD1    . TYR C 3 91  ? 4.036  16.273  -28.703 1.00 23.37 ? 91  TYR B CD1    1 
ATOM   4073 C CD2    . TYR C 3 91  ? 4.736  17.948  -27.176 1.00 19.86 ? 91  TYR B CD2    1 
ATOM   4074 C CE1    . TYR C 3 91  ? 3.373  15.612  -27.696 1.00 23.13 ? 91  TYR B CE1    1 
ATOM   4075 C CE2    . TYR C 3 91  ? 4.064  17.302  -26.167 1.00 22.79 ? 91  TYR B CE2    1 
ATOM   4076 C CZ     . TYR C 3 91  ? 3.386  16.124  -26.435 1.00 24.24 ? 91  TYR B CZ     1 
ATOM   4077 O OH     . TYR C 3 91  ? 2.716  15.446  -25.439 1.00 22.31 ? 91  TYR B OH     1 
ATOM   4078 N N      . ASN C 3 92  ? 8.236  18.809  -31.296 1.00 27.93 ? 92  ASN B N      1 
ATOM   4079 C CA     . ASN C 3 92  ? 8.641  19.570  -32.476 1.00 26.63 ? 92  ASN B CA     1 
ATOM   4080 C C      . ASN C 3 92  ? 10.022 19.217  -33.000 1.00 26.47 ? 92  ASN B C      1 
ATOM   4081 O O      . ASN C 3 92  ? 10.217 19.153  -34.210 1.00 29.46 ? 92  ASN B O      1 
ATOM   4082 C CB     . ASN C 3 92  ? 8.596  21.070  -32.173 1.00 27.56 ? 92  ASN B CB     1 
ATOM   4083 C CG     . ASN C 3 92  ? 7.221  21.533  -31.746 1.00 31.86 ? 92  ASN B CG     1 
ATOM   4084 O OD1    . ASN C 3 92  ? 6.234  20.796  -31.871 1.00 32.02 ? 92  ASN B OD1    1 
ATOM   4085 N ND2    . ASN C 3 92  ? 7.148  22.750  -31.227 1.00 31.64 ? 92  ASN B ND2    1 
ATOM   4086 N N      . GLU C 3 93  ? 11.001 19.034  -32.120 1.00 28.00 ? 93  GLU B N      1 
ATOM   4087 C CA     . GLU C 3 93  ? 12.332 18.621  -32.539 1.00 19.85 ? 93  GLU B CA     1 
ATOM   4088 C C      . GLU C 3 93  ? 12.387 17.122  -32.798 1.00 20.75 ? 93  GLU B C      1 
ATOM   4089 O O      . GLU C 3 93  ? 13.000 16.676  -33.769 1.00 26.93 ? 93  GLU B O      1 
ATOM   4090 C CB     . GLU C 3 93  ? 13.359 19.004  -31.475 1.00 18.10 ? 93  GLU B CB     1 
ATOM   4091 C CG     . GLU C 3 93  ? 13.550 20.493  -31.310 1.00 21.86 ? 93  GLU B CG     1 
ATOM   4092 C CD     . GLU C 3 93  ? 14.148 21.142  -32.550 1.00 34.92 ? 93  GLU B CD     1 
ATOM   4093 O OE1    . GLU C 3 93  ? 14.660 20.398  -33.429 1.00 28.94 ? 93  GLU B OE1    1 
ATOM   4094 O OE2    . GLU C 3 93  ? 14.100 22.395  -32.637 1.00 32.77 ? 93  GLU B OE2    1 
ATOM   4095 N N      . LEU C 3 94  ? 11.766 16.334  -31.929 1.00 24.16 ? 94  LEU B N      1 
ATOM   4096 C CA     . LEU C 3 94  ? 11.774 14.885  -32.020 1.00 22.00 ? 94  LEU B CA     1 
ATOM   4097 C C      . LEU C 3 94  ? 10.546 14.323  -32.724 1.00 30.24 ? 94  LEU B C      1 
ATOM   4098 O O      . LEU C 3 94  ? 10.603 13.198  -33.245 1.00 20.90 ? 94  LEU B O      1 
ATOM   4099 C CB     . LEU C 3 94  ? 11.885 14.295  -30.609 1.00 21.21 ? 94  LEU B CB     1 
ATOM   4100 C CG     . LEU C 3 94  ? 13.307 13.844  -30.244 1.00 24.58 ? 94  LEU B CG     1 
ATOM   4101 C CD1    . LEU C 3 94  ? 14.330 14.863  -30.729 1.00 14.27 ? 94  LEU B CD1    1 
ATOM   4102 C CD2    . LEU C 3 94  ? 13.460 13.571  -28.758 1.00 18.23 ? 94  LEU B CD2    1 
ATOM   4103 N N      . ARG C 3 95  ? 9.457  15.095  -32.760 1.00 34.22 ? 95  ARG B N      1 
ATOM   4104 C CA     . ARG C 3 95  ? 8.179  14.679  -33.338 1.00 29.15 ? 95  ARG B CA     1 
ATOM   4105 C C      . ARG C 3 95  ? 7.739  13.335  -32.764 1.00 26.10 ? 95  ARG B C      1 
ATOM   4106 O O      . ARG C 3 95  ? 7.494  12.370  -33.493 1.00 24.92 ? 95  ARG B O      1 
ATOM   4107 C CB     . ARG C 3 95  ? 8.255  14.628  -34.864 1.00 23.44 ? 95  ARG B CB     1 
ATOM   4108 C CG     . ARG C 3 95  ? 8.726  15.929  -35.507 1.00 32.37 ? 95  ARG B CG     1 
ATOM   4109 C CD     . ARG C 3 95  ? 8.746  15.816  -37.036 1.00 37.42 ? 95  ARG B CD     1 
ATOM   4110 N NE     . ARG C 3 95  ? 7.399  15.625  -37.559 1.00 34.86 ? 95  ARG B NE     1 
ATOM   4111 C CZ     . ARG C 3 95  ? 6.528  16.608  -37.718 1.00 37.38 ? 95  ARG B CZ     1 
ATOM   4112 N NH1    . ARG C 3 95  ? 6.862  17.867  -37.480 1.00 41.16 ? 95  ARG B NH1    1 
ATOM   4113 N NH2    . ARG C 3 95  ? 5.293  16.323  -38.115 1.00 35.22 ? 95  ARG B NH2    1 
ATOM   4114 N N      . VAL C 3 96  ? 7.632  13.294  -31.430 1.00 21.35 ? 96  VAL B N      1 
ATOM   4115 C CA     . VAL C 3 96  ? 7.319  12.064  -30.710 1.00 20.05 ? 96  VAL B CA     1 
ATOM   4116 C C      . VAL C 3 96  ? 6.289  12.323  -29.616 1.00 19.52 ? 96  VAL B C      1 
ATOM   4117 O O      . VAL C 3 96  ? 6.197  13.419  -29.056 1.00 16.83 ? 96  VAL B O      1 
ATOM   4118 C CB     . VAL C 3 96  ? 8.568  11.435  -30.077 1.00 18.79 ? 96  VAL B CB     1 
ATOM   4119 C CG1    . VAL C 3 96  ? 9.603  11.160  -31.146 1.00 20.04 ? 96  VAL B CG1    1 
ATOM   4120 C CG2    . VAL C 3 96  ? 9.102  12.366  -28.994 1.00 16.50 ? 96  VAL B CG2    1 
ATOM   4121 N N      . ALA C 3 97  ? 5.534  11.282  -29.301 1.00 19.66 ? 97  ALA B N      1 
ATOM   4122 C CA     . ALA C 3 97  ? 4.601  11.259  -28.186 1.00 25.28 ? 97  ALA B CA     1 
ATOM   4123 C C      . ALA C 3 97  ? 5.330  10.796  -26.925 1.00 22.75 ? 97  ALA B C      1 
ATOM   4124 O O      . ALA C 3 97  ? 5.549  9.588   -26.739 1.00 20.26 ? 97  ALA B O      1 
ATOM   4125 C CB     . ALA C 3 97  ? 3.420  10.334  -28.499 1.00 24.28 ? 97  ALA B CB     1 
ATOM   4126 N N      . PRO C 3 98  ? 5.719  11.716  -26.041 1.00 20.64 ? 98  PRO B N      1 
ATOM   4127 C CA     . PRO C 3 98  ? 6.540  11.308  -24.894 1.00 18.91 ? 98  PRO B CA     1 
ATOM   4128 C C      . PRO C 3 98  ? 5.888  10.213  -24.075 1.00 17.08 ? 98  PRO B C      1 
ATOM   4129 O O      . PRO C 3 98  ? 6.606  9.396   -23.478 1.00 14.86 ? 98  PRO B O      1 
ATOM   4130 C CB     . PRO C 3 98  ? 6.738  12.616  -24.107 1.00 15.19 ? 98  PRO B CB     1 
ATOM   4131 C CG     . PRO C 3 98  ? 5.669  13.542  -24.600 1.00 18.02 ? 98  PRO B CG     1 
ATOM   4132 C CD     . PRO C 3 98  ? 5.436  13.162  -26.037 1.00 20.87 ? 98  PRO B CD     1 
ATOM   4133 N N      . GLU C 3 99  ? 4.555  10.115  -24.071 1.00 18.62 ? 99  GLU B N      1 
ATOM   4134 C CA     . GLU C 3 99  ? 3.947  8.998   -23.357 1.00 18.47 ? 99  GLU B CA     1 
ATOM   4135 C C      . GLU C 3 99  ? 4.350  7.642   -23.925 1.00 19.87 ? 99  GLU B C      1 
ATOM   4136 O O      . GLU C 3 99  ? 4.057  6.617   -23.303 1.00 17.74 ? 99  GLU B O      1 
ATOM   4137 C CB     . GLU C 3 99  ? 2.428  9.123   -23.346 1.00 24.32 ? 99  GLU B CB     1 
ATOM   4138 C CG     . GLU C 3 99  ? 1.866  9.626   -24.641 1.00 31.51 ? 99  GLU B CG     1 
ATOM   4139 C CD     . GLU C 3 99  ? 0.383  9.926   -24.561 1.00 40.67 ? 99  GLU B CD     1 
ATOM   4140 O OE1    . GLU C 3 99  ? -0.244 9.605   -23.522 1.00 45.54 ? 99  GLU B OE1    1 
ATOM   4141 O OE2    . GLU C 3 99  ? -0.151 10.489  -25.548 1.00 34.50 ? 99  GLU B OE2    1 
ATOM   4142 N N      . GLU C 3 100 ? 4.997  7.591   -25.087 1.00 20.68 ? 100 GLU B N      1 
ATOM   4143 C CA     . GLU C 3 100 ? 5.397  6.314   -25.657 1.00 18.15 ? 100 GLU B CA     1 
ATOM   4144 C C      . GLU C 3 100 ? 6.872  5.996   -25.451 1.00 19.10 ? 100 GLU B C      1 
ATOM   4145 O O      . GLU C 3 100 ? 7.326  4.941   -25.897 1.00 22.89 ? 100 GLU B O      1 
ATOM   4146 C CB     . GLU C 3 100 ? 5.067  6.290   -27.154 1.00 21.62 ? 100 GLU B CB     1 
ATOM   4147 C CG     . GLU C 3 100 ? 3.556  6.358   -27.475 1.00 22.98 ? 100 GLU B CG     1 
ATOM   4148 C CD     . GLU C 3 100 ? 3.228  6.868   -28.889 1.00 35.34 ? 100 GLU B CD     1 
ATOM   4149 O OE1    . GLU C 3 100 ? 4.167  7.101   -29.704 1.00 31.35 ? 100 GLU B OE1    1 
ATOM   4150 O OE2    . GLU C 3 100 ? 2.013  7.041   -29.178 1.00 41.22 ? 100 GLU B OE2    1 
ATOM   4151 N N      . HIS C 3 101 ? 7.626  6.862   -24.777 1.00 17.23 ? 101 HIS B N      1 
ATOM   4152 C CA     . HIS C 3 101 ? 9.082  6.772   -24.765 1.00 17.19 ? 101 HIS B CA     1 
ATOM   4153 C C      . HIS C 3 101 ? 9.676  7.004   -23.381 1.00 16.54 ? 101 HIS B C      1 
ATOM   4154 O O      . HIS C 3 101 ? 9.600  8.119   -22.850 1.00 15.65 ? 101 HIS B O      1 
ATOM   4155 C CB     . HIS C 3 101 ? 9.683  7.808   -25.719 1.00 19.05 ? 101 HIS B CB     1 
ATOM   4156 C CG     . HIS C 3 101 ? 9.275  7.640   -27.151 1.00 20.35 ? 101 HIS B CG     1 
ATOM   4157 N ND1    . HIS C 3 101 ? 9.658  6.559   -27.916 1.00 17.95 ? 101 HIS B ND1    1 
ATOM   4158 C CD2    . HIS C 3 101 ? 8.565  8.452   -27.973 1.00 19.58 ? 101 HIS B CD2    1 
ATOM   4159 C CE1    . HIS C 3 101 ? 9.171  6.695   -29.138 1.00 22.73 ? 101 HIS B CE1    1 
ATOM   4160 N NE2    . HIS C 3 101 ? 8.502  7.833   -29.199 1.00 24.37 ? 101 HIS B NE2    1 
ATOM   4161 N N      . PRO C 3 102 ? 10.319 6.010   -22.782 1.00 16.45 ? 102 PRO B N      1 
ATOM   4162 C CA     . PRO C 3 102 ? 11.061 6.287   -21.549 1.00 15.45 ? 102 PRO B CA     1 
ATOM   4163 C C      . PRO C 3 102 ? 12.145 7.321   -21.815 1.00 12.12 ? 102 PRO B C      1 
ATOM   4164 O O      . PRO C 3 102 ? 12.790 7.312   -22.863 1.00 12.72 ? 102 PRO B O      1 
ATOM   4165 C CB     . PRO C 3 102 ? 11.635 4.918   -21.161 1.00 13.24 ? 102 PRO B CB     1 
ATOM   4166 C CG     . PRO C 3 102 ? 11.471 4.042   -22.334 1.00 9.69  ? 102 PRO B CG     1 
ATOM   4167 C CD     . PRO C 3 102 ? 10.340 4.585   -23.149 1.00 11.84 ? 102 PRO B CD     1 
ATOM   4168 N N      . VAL C 3 103 ? 12.330 8.230   -20.864 1.00 11.52 ? 103 VAL B N      1 
ATOM   4169 C CA     . VAL C 3 103 ? 13.065 9.469   -21.086 1.00 8.89  ? 103 VAL B CA     1 
ATOM   4170 C C      . VAL C 3 103 ? 14.187 9.552   -20.065 1.00 8.64  ? 103 VAL B C      1 
ATOM   4171 O O      . VAL C 3 103 ? 13.936 9.715   -18.869 1.00 11.45 ? 103 VAL B O      1 
ATOM   4172 C CB     . VAL C 3 103 ? 12.148 10.694  -20.998 1.00 9.18  ? 103 VAL B CB     1 
ATOM   4173 C CG1    . VAL C 3 103 ? 12.954 11.948  -21.202 1.00 10.24 ? 103 VAL B CG1    1 
ATOM   4174 C CG2    . VAL C 3 103 ? 11.025 10.599  -22.020 1.00 9.59  ? 103 VAL B CG2    1 
ATOM   4175 N N      . LEU C 3 104 ? 15.420 9.425   -20.532 1.00 9.52  ? 104 LEU B N      1 
ATOM   4176 C CA     . LEU C 3 104 ? 16.605 9.717   -19.739 1.00 9.05  ? 104 LEU B CA     1 
ATOM   4177 C C      . LEU C 3 104 ? 16.868 11.210  -19.807 1.00 9.64  ? 104 LEU B C      1 
ATOM   4178 O O      . LEU C 3 104 ? 17.019 11.753  -20.902 1.00 11.60 ? 104 LEU B O      1 
ATOM   4179 C CB     . LEU C 3 104 ? 17.808 8.949   -20.279 1.00 10.13 ? 104 LEU B CB     1 
ATOM   4180 C CG     . LEU C 3 104 ? 19.142 9.132   -19.566 1.00 8.42  ? 104 LEU B CG     1 
ATOM   4181 C CD1    . LEU C 3 104 ? 18.878 9.609   -18.175 1.00 10.86 ? 104 LEU B CD1    1 
ATOM   4182 C CD2    . LEU C 3 104 ? 19.851 7.808   -19.498 1.00 8.99  ? 104 LEU B CD2    1 
ATOM   4183 N N      . LEU C 3 105 ? 16.931 11.865  -18.653 1.00 9.16  ? 105 LEU B N      1 
ATOM   4184 C CA     . LEU C 3 105 ? 17.211 13.293  -18.548 1.00 9.50  ? 105 LEU B CA     1 
ATOM   4185 C C      . LEU C 3 105 ? 18.496 13.548  -17.769 1.00 13.28 ? 105 LEU B C      1 
ATOM   4186 O O      . LEU C 3 105 ? 18.979 12.710  -17.002 1.00 14.72 ? 105 LEU B O      1 
ATOM   4187 C CB     . LEU C 3 105 ? 16.062 14.042  -17.863 1.00 14.31 ? 105 LEU B CB     1 
ATOM   4188 C CG     . LEU C 3 105 ? 14.829 14.424  -18.666 1.00 15.96 ? 105 LEU B CG     1 
ATOM   4189 C CD1    . LEU C 3 105 ? 13.644 14.351  -17.746 1.00 21.44 ? 105 LEU B CD1    1 
ATOM   4190 C CD2    . LEU C 3 105 ? 14.960 15.831  -19.275 1.00 13.18 ? 105 LEU B CD2    1 
ATOM   4191 N N      . THR C 3 106 ? 18.985 14.771  -17.899 1.00 12.20 ? 106 THR B N      1 
ATOM   4192 C CA     . THR C 3 106 ? 20.333 15.147  -17.512 1.00 11.56 ? 106 THR B CA     1 
ATOM   4193 C C      . THR C 3 106 ? 20.303 16.348  -16.584 1.00 10.82 ? 106 THR B C      1 
ATOM   4194 O O      . THR C 3 106 ? 19.539 17.289  -16.809 1.00 13.73 ? 106 THR B O      1 
ATOM   4195 C CB     . THR C 3 106 ? 21.116 15.508  -18.746 1.00 13.16 ? 106 THR B CB     1 
ATOM   4196 O OG1    . THR C 3 106 ? 22.117 14.517  -18.980 1.00 18.31 ? 106 THR B OG1    1 
ATOM   4197 C CG2    . THR C 3 106 ? 21.718 16.899  -18.608 1.00 12.42 ? 106 THR B CG2    1 
ATOM   4198 N N      . GLU C 3 107 ? 21.173 16.342  -15.577 1.00 11.24 ? 107 GLU B N      1 
ATOM   4199 C CA     . GLU C 3 107 ? 21.158 17.365  -14.542 1.00 12.87 ? 107 GLU B CA     1 
ATOM   4200 C C      . GLU C 3 107 ? 22.584 17.775  -14.196 1.00 16.93 ? 107 GLU B C      1 
ATOM   4201 O O      . GLU C 3 107 ? 23.530 16.999  -14.353 1.00 12.98 ? 107 GLU B O      1 
ATOM   4202 C CB     . GLU C 3 107 ? 20.434 16.874  -13.286 1.00 11.53 ? 107 GLU B CB     1 
ATOM   4203 C CG     . GLU C 3 107 ? 21.167 15.722  -12.605 1.00 14.24 ? 107 GLU B CG     1 
ATOM   4204 C CD     . GLU C 3 107 ? 20.663 15.454  -11.200 1.00 20.59 ? 107 GLU B CD     1 
ATOM   4205 O OE1    . GLU C 3 107 ? 19.983 16.342  -10.643 1.00 27.11 ? 107 GLU B OE1    1 
ATOM   4206 O OE2    . GLU C 3 107 ? 20.932 14.357  -10.655 1.00 25.55 ? 107 GLU B OE2    1 
ATOM   4207 N N      . ALA C 3 108 ? 22.727 19.016  -13.718 1.00 22.39 ? 108 ALA B N      1 
ATOM   4208 C CA     . ALA C 3 108 ? 24.036 19.539  -13.354 1.00 13.81 ? 108 ALA B CA     1 
ATOM   4209 C C      . ALA C 3 108 ? 24.538 18.903  -12.061 1.00 13.39 ? 108 ALA B C      1 
ATOM   4210 O O      . ALA C 3 108 ? 23.792 18.232  -11.339 1.00 11.71 ? 108 ALA B O      1 
ATOM   4211 C CB     . ALA C 3 108 ? 23.975 21.054  -13.190 1.00 13.89 ? 108 ALA B CB     1 
ATOM   4212 N N      . PRO C 3 109 ? 25.810 19.108  -11.735 1.00 14.71 ? 109 PRO B N      1 
ATOM   4213 C CA     . PRO C 3 109 ? 26.300 18.699  -10.419 1.00 13.01 ? 109 PRO B CA     1 
ATOM   4214 C C      . PRO C 3 109 ? 25.759 19.618  -9.344  1.00 16.50 ? 109 PRO B C      1 
ATOM   4215 O O      . PRO C 3 109 ? 25.603 20.826  -9.546  1.00 20.93 ? 109 PRO B O      1 
ATOM   4216 C CB     . PRO C 3 109 ? 27.820 18.849  -10.536 1.00 11.84 ? 109 PRO B CB     1 
ATOM   4217 C CG     . PRO C 3 109 ? 28.089 19.150  -11.991 1.00 11.10 ? 109 PRO B CG     1 
ATOM   4218 C CD     . PRO C 3 109 ? 26.860 19.764  -12.528 1.00 9.97  ? 109 PRO B CD     1 
ATOM   4219 N N      . LEU C 3 110 ? 25.512 19.040  -8.173  1.00 15.21 ? 110 LEU B N      1 
ATOM   4220 C CA     . LEU C 3 110 ? 25.041 19.820  -7.040  1.00 14.71 ? 110 LEU B CA     1 
ATOM   4221 C C      . LEU C 3 110 ? 23.652 20.398  -7.310  1.00 21.79 ? 110 LEU B C      1 
ATOM   4222 O O      . LEU C 3 110 ? 23.291 21.466  -6.804  1.00 25.57 ? 110 LEU B O      1 
ATOM   4223 C CB     . LEU C 3 110 ? 26.038 20.932  -6.705  1.00 15.76 ? 110 LEU B CB     1 
ATOM   4224 C CG     . LEU C 3 110 ? 27.501 20.493  -6.523  1.00 14.36 ? 110 LEU B CG     1 
ATOM   4225 C CD1    . LEU C 3 110 ? 28.420 21.723  -6.530  1.00 6.67  ? 110 LEU B CD1    1 
ATOM   4226 C CD2    . LEU C 3 110 ? 27.724 19.614  -5.275  1.00 6.67  ? 110 LEU B CD2    1 
ATOM   4227 N N      . ASN C 3 111 ? 22.875 19.715  -8.133  1.00 16.52 ? 111 ASN B N      1 
ATOM   4228 C CA     . ASN C 3 111 ? 21.509 20.138  -8.372  1.00 15.88 ? 111 ASN B CA     1 
ATOM   4229 C C      . ASN C 3 111 ? 20.713 20.024  -7.078  1.00 22.38 ? 111 ASN B C      1 
ATOM   4230 O O      . ASN C 3 111 ? 20.697 18.947  -6.459  1.00 24.10 ? 111 ASN B O      1 
ATOM   4231 C CB     . ASN C 3 111 ? 20.876 19.283  -9.453  1.00 14.21 ? 111 ASN B CB     1 
ATOM   4232 C CG     . ASN C 3 111 ? 19.705 19.952  -10.096 1.00 18.52 ? 111 ASN B CG     1 
ATOM   4233 O OD1    . ASN C 3 111 ? 19.606 21.180  -10.117 1.00 17.54 ? 111 ASN B OD1    1 
ATOM   4234 N ND2    . ASN C 3 111 ? 18.797 19.147  -10.638 1.00 20.58 ? 111 ASN B ND2    1 
ATOM   4235 N N      . PRO C 3 112 ? 20.063 21.096  -6.626  1.00 19.00 ? 112 PRO B N      1 
ATOM   4236 C CA     . PRO C 3 112 ? 19.324 21.020  -5.364  1.00 15.27 ? 112 PRO B CA     1 
ATOM   4237 C C      . PRO C 3 112 ? 18.227 19.968  -5.406  1.00 18.96 ? 112 PRO B C      1 
ATOM   4238 O O      . PRO C 3 112 ? 17.645 19.668  -6.451  1.00 19.41 ? 112 PRO B O      1 
ATOM   4239 C CB     . PRO C 3 112 ? 18.759 22.441  -5.183  1.00 14.52 ? 112 PRO B CB     1 
ATOM   4240 C CG     . PRO C 3 112 ? 19.077 23.192  -6.405  1.00 15.21 ? 112 PRO B CG     1 
ATOM   4241 C CD     . PRO C 3 112 ? 20.232 22.486  -7.075  1.00 19.15 ? 112 PRO B CD     1 
ATOM   4242 N N      . LYS C 3 113 ? 17.976 19.383  -4.234  1.00 19.98 ? 113 LYS B N      1 
ATOM   4243 C CA     . LYS C 3 113 ? 17.001 18.314  -4.128  1.00 15.11 ? 113 LYS B CA     1 
ATOM   4244 C C      . LYS C 3 113 ? 15.689 18.742  -4.744  1.00 18.58 ? 113 LYS B C      1 
ATOM   4245 O O      . LYS C 3 113 ? 15.080 17.995  -5.519  1.00 23.73 ? 113 LYS B O      1 
ATOM   4246 C CB     . LYS C 3 113 ? 16.808 17.935  -2.664  1.00 18.42 ? 113 LYS B CB     1 
ATOM   4247 C CG     . LYS C 3 113 ? 18.117 17.857  -1.920  1.00 20.78 ? 113 LYS B CG     1 
ATOM   4248 C CD     . LYS C 3 113 ? 17.937 18.105  -0.426  1.00 27.73 ? 113 LYS B CD     1 
ATOM   4249 C CE     . LYS C 3 113 ? 16.644 17.504  0.085   1.00 25.50 ? 113 LYS B CE     1 
ATOM   4250 N NZ     . LYS C 3 113 ? 16.352 18.005  1.465   1.00 27.27 ? 113 LYS B NZ     1 
ATOM   4251 N N      . ALA C 3 114 ? 15.218 19.943  -4.401  1.00 20.33 ? 114 ALA B N      1 
ATOM   4252 C CA     . ALA C 3 114 ? 13.888 20.317  -4.869  1.00 19.61 ? 114 ALA B CA     1 
ATOM   4253 C C      . ALA C 3 114 ? 13.802 20.186  -6.380  1.00 18.23 ? 114 ALA B C      1 
ATOM   4254 O O      . ALA C 3 114 ? 12.769 19.769  -6.920  1.00 13.62 ? 114 ALA B O      1 
ATOM   4255 C CB     . ALA C 3 114 ? 13.524 21.738  -4.432  1.00 23.87 ? 114 ALA B CB     1 
ATOM   4256 N N      . ASN C 3 115 ? 14.906 20.481  -7.075  1.00 21.69 ? 115 ASN B N      1 
ATOM   4257 C CA     . ASN C 3 115 ? 14.882 20.512  -8.535  1.00 20.22 ? 115 ASN B CA     1 
ATOM   4258 C C      . ASN C 3 115 ? 14.743 19.117  -9.129  1.00 17.58 ? 115 ASN B C      1 
ATOM   4259 O O      . ASN C 3 115 ? 13.992 18.928  -10.094 1.00 17.30 ? 115 ASN B O      1 
ATOM   4260 C CB     . ASN C 3 115 ? 16.126 21.229  -9.054  1.00 19.29 ? 115 ASN B CB     1 
ATOM   4261 C CG     . ASN C 3 115 ? 16.025 22.713  -8.867  1.00 24.14 ? 115 ASN B CG     1 
ATOM   4262 O OD1    . ASN C 3 115 ? 15.086 23.201  -8.233  1.00 36.37 ? 115 ASN B OD1    1 
ATOM   4263 N ND2    . ASN C 3 115 ? 16.973 23.453  -9.422  1.00 31.91 ? 115 ASN B ND2    1 
ATOM   4264 N N      . ARG C 3 116 ? 15.410 18.117  -8.545  1.00 13.61 ? 116 ARG B N      1 
ATOM   4265 C CA     . ARG C 3 116 ? 15.242 16.764  -9.063  1.00 16.52 ? 116 ARG B CA     1 
ATOM   4266 C C      . ARG C 3 116 ? 13.794 16.315  -8.947  1.00 15.17 ? 116 ARG B C      1 
ATOM   4267 O O      . ARG C 3 116 ? 13.266 15.688  -9.869  1.00 16.99 ? 116 ARG B O      1 
ATOM   4268 C CB     . ARG C 3 116 ? 16.177 15.780  -8.356  1.00 16.73 ? 116 ARG B CB     1 
ATOM   4269 C CG     . ARG C 3 116 ? 17.522 16.384  -8.018  1.00 21.48 ? 116 ARG B CG     1 
ATOM   4270 C CD     . ARG C 3 116 ? 18.519 15.398  -7.433  1.00 16.25 ? 116 ARG B CD     1 
ATOM   4271 N NE     . ARG C 3 116 ? 18.977 14.451  -8.433  1.00 14.36 ? 116 ARG B NE     1 
ATOM   4272 C CZ     . ARG C 3 116 ? 18.846 13.136  -8.341  1.00 13.73 ? 116 ARG B CZ     1 
ATOM   4273 N NH1    . ARG C 3 116 ? 18.386 12.557  -7.247  1.00 14.99 ? 116 ARG B NH1    1 
ATOM   4274 N NH2    . ARG C 3 116 ? 19.181 12.379  -9.377  1.00 13.82 ? 116 ARG B NH2    1 
ATOM   4275 N N      . GLU C 3 117 ? 13.126 16.641  -7.841  1.00 14.25 ? 117 GLU B N      1 
ATOM   4276 C CA     . GLU C 3 117 ? 11.723 16.251  -7.703  1.00 18.07 ? 117 GLU B CA     1 
ATOM   4277 C C      . GLU C 3 117 ? 10.844 16.962  -8.722  1.00 15.33 ? 117 GLU B C      1 
ATOM   4278 O O      . GLU C 3 117 ? 10.001 16.335  -9.376  1.00 14.46 ? 117 GLU B O      1 
ATOM   4279 C CB     . GLU C 3 117 ? 11.213 16.543  -6.295  1.00 18.99 ? 117 GLU B CB     1 
ATOM   4280 C CG     . GLU C 3 117 ? 11.895 15.772  -5.226  1.00 24.94 ? 117 GLU B CG     1 
ATOM   4281 C CD     . GLU C 3 117 ? 11.564 16.304  -3.859  1.00 31.46 ? 117 GLU B CD     1 
ATOM   4282 O OE1    . GLU C 3 117 ? 10.569 17.062  -3.751  1.00 37.01 ? 117 GLU B OE1    1 
ATOM   4283 O OE2    . GLU C 3 117 ? 12.299 15.972  -2.902  1.00 36.24 ? 117 GLU B OE2    1 
ATOM   4284 N N      . LYS C 3 118 ? 10.987 18.288  -8.820  1.00 10.73 ? 118 LYS B N      1 
ATOM   4285 C CA     . LYS C 3 118 ? 10.157 19.059  -9.744  1.00 17.99 ? 118 LYS B CA     1 
ATOM   4286 C C      . LYS C 3 118 ? 10.287 18.512  -11.165 1.00 17.32 ? 118 LYS B C      1 
ATOM   4287 O O      . LYS C 3 118 ? 9.285  18.242  -11.842 1.00 15.32 ? 118 LYS B O      1 
ATOM   4288 C CB     . LYS C 3 118 ? 10.539 20.544  -9.673  1.00 18.04 ? 118 LYS B CB     1 
ATOM   4289 C CG     . LYS C 3 118 ? 9.543  21.515  -10.332 1.00 22.91 ? 118 LYS B CG     1 
ATOM   4290 C CD     . LYS C 3 118 ? 8.073  21.332  -9.879  1.00 22.72 ? 118 LYS B CD     1 
ATOM   4291 C CE     . LYS C 3 118 ? 7.170  22.469  -10.411 1.00 28.80 ? 118 LYS B CE     1 
ATOM   4292 N NZ     . LYS C 3 118 ? 5.709  22.177  -10.260 1.00 36.82 ? 118 LYS B NZ     1 
ATOM   4293 N N      . MET C 3 119 ? 11.524 18.303  -11.611 1.00 15.55 ? 119 MET B N      1 
ATOM   4294 C CA     . MET C 3 119 ? 11.767 17.677  -12.903 1.00 16.10 ? 119 MET B CA     1 
ATOM   4295 C C      . MET C 3 119 ? 10.975 16.384  -13.026 1.00 14.89 ? 119 MET B C      1 
ATOM   4296 O O      . MET C 3 119 ? 10.298 16.147  -14.033 1.00 15.57 ? 119 MET B O      1 
ATOM   4297 C CB     . MET C 3 119 ? 13.280 17.459  -13.056 1.00 23.71 ? 119 MET B CB     1 
ATOM   4298 C CG     . MET C 3 119 ? 13.783 16.443  -14.076 1.00 30.07 ? 119 MET B CG     1 
ATOM   4299 S SD     . MET C 3 119 ? 15.601 16.592  -14.183 1.00 42.39 ? 119 MET B SD     1 
ATOM   4300 C CE     . MET C 3 119 ? 15.733 17.890  -15.413 1.00 26.87 ? 119 MET B CE     1 
ATOM   4301 N N      . THR C 3 120 ? 11.012 15.553  -11.982 1.00 14.94 ? 120 THR B N      1 
ATOM   4302 C CA     . THR C 3 120 ? 10.325 14.270  -12.042 1.00 16.06 ? 120 THR B CA     1 
ATOM   4303 C C      . THR C 3 120 ? 8.813  14.442  -12.034 1.00 15.89 ? 120 THR B C      1 
ATOM   4304 O O      . THR C 3 120 ? 8.093  13.638  -12.634 1.00 14.02 ? 120 THR B O      1 
ATOM   4305 C CB     . THR C 3 120 ? 10.733 13.376  -10.866 1.00 18.70 ? 120 THR B CB     1 
ATOM   4306 O OG1    . THR C 3 120 ? 12.157 13.344  -10.738 1.00 14.82 ? 120 THR B OG1    1 
ATOM   4307 C CG2    . THR C 3 120 ? 10.225 11.957  -11.091 1.00 17.29 ? 120 THR B CG2    1 
ATOM   4308 N N      . GLN C 3 121 ? 8.303  15.443  -11.326 1.00 13.38 ? 121 GLN B N      1 
ATOM   4309 C CA     . GLN C 3 121 ? 6.863  15.634  -11.339 1.00 14.26 ? 121 GLN B CA     1 
ATOM   4310 C C      . GLN C 3 121 ? 6.391  16.015  -12.734 1.00 17.97 ? 121 GLN B C      1 
ATOM   4311 O O      . GLN C 3 121 ? 5.418  15.449  -13.251 1.00 17.57 ? 121 GLN B O      1 
ATOM   4312 C CB     . GLN C 3 121 ? 6.476  16.698  -10.321 1.00 18.21 ? 121 GLN B CB     1 
ATOM   4313 C CG     . GLN C 3 121 ? 4.995  16.885  -10.163 1.00 16.82 ? 121 GLN B CG     1 
ATOM   4314 C CD     . GLN C 3 121 ? 4.688  17.994  -9.202  1.00 19.11 ? 121 GLN B CD     1 
ATOM   4315 O OE1    . GLN C 3 121 ? 5.435  18.963  -9.112  1.00 27.79 ? 121 GLN B OE1    1 
ATOM   4316 N NE2    . GLN C 3 121 ? 3.595  17.866  -8.471  1.00 28.06 ? 121 GLN B NE2    1 
ATOM   4317 N N      . ILE C 3 122 ? 7.104  16.953  -13.368 1.00 18.91 ? 122 ILE B N      1 
ATOM   4318 C CA     . ILE C 3 122 ? 6.715  17.457  -14.680 1.00 13.19 ? 122 ILE B CA     1 
ATOM   4319 C C      . ILE C 3 122 ? 6.845  16.371  -15.731 1.00 16.16 ? 122 ILE B C      1 
ATOM   4320 O O      . ILE C 3 122 ? 5.947  16.164  -16.556 1.00 17.66 ? 122 ILE B O      1 
ATOM   4321 C CB     . ILE C 3 122 ? 7.554  18.686  -15.054 1.00 13.25 ? 122 ILE B CB     1 
ATOM   4322 C CG1    . ILE C 3 122 ? 7.210  19.849  -14.136 1.00 14.22 ? 122 ILE B CG1    1 
ATOM   4323 C CG2    . ILE C 3 122 ? 7.268  19.069  -16.480 1.00 13.23 ? 122 ILE B CG2    1 
ATOM   4324 C CD1    . ILE C 3 122 ? 8.101  21.065  -14.335 1.00 16.29 ? 122 ILE B CD1    1 
ATOM   4325 N N      . MET C 3 123 ? 7.978  15.679  -15.729 1.00 15.79 ? 123 MET B N      1 
ATOM   4326 C CA     . MET C 3 123 ? 8.187  14.595  -16.683 1.00 17.12 ? 123 MET B CA     1 
ATOM   4327 C C      . MET C 3 123 ? 7.064  13.565  -16.603 1.00 15.77 ? 123 MET B C      1 
ATOM   4328 O O      . MET C 3 123 ? 6.625  13.033  -17.629 1.00 17.39 ? 123 MET B O      1 
ATOM   4329 C CB     . MET C 3 123 ? 9.542  13.947  -16.418 1.00 19.62 ? 123 MET B CB     1 
ATOM   4330 C CG     . MET C 3 123 ? 10.217 13.415  -17.635 1.00 16.05 ? 123 MET B CG     1 
ATOM   4331 S SD     . MET C 3 123 ? 10.310 14.646  -18.940 1.00 11.56 ? 123 MET B SD     1 
ATOM   4332 C CE     . MET C 3 123 ? 10.857 16.096  -18.048 1.00 19.62 ? 123 MET B CE     1 
ATOM   4333 N N      . PHE C 3 124 ? 6.568  13.289  -15.396 1.00 15.02 ? 124 PHE B N      1 
ATOM   4334 C CA     . PHE C 3 124 ? 5.506  12.298  -15.247 1.00 16.30 ? 124 PHE B CA     1 
ATOM   4335 C C      . PHE C 3 124 ? 4.106  12.904  -15.349 1.00 17.79 ? 124 PHE B C      1 
ATOM   4336 O O      . PHE C 3 124 ? 3.216  12.317  -15.986 1.00 18.05 ? 124 PHE B O      1 
ATOM   4337 C CB     . PHE C 3 124 ? 5.631  11.563  -13.910 1.00 13.35 ? 124 PHE B CB     1 
ATOM   4338 C CG     . PHE C 3 124 ? 6.553  10.385  -13.933 1.00 13.32 ? 124 PHE B CG     1 
ATOM   4339 C CD1    . PHE C 3 124 ? 6.312  9.312   -14.773 1.00 16.91 ? 124 PHE B CD1    1 
ATOM   4340 C CD2    . PHE C 3 124 ? 7.641  10.328  -13.076 1.00 14.20 ? 124 PHE B CD2    1 
ATOM   4341 C CE1    . PHE C 3 124 ? 7.169  8.210   -14.781 1.00 16.51 ? 124 PHE B CE1    1 
ATOM   4342 C CE2    . PHE C 3 124 ? 8.503  9.238   -13.076 1.00 12.32 ? 124 PHE B CE2    1 
ATOM   4343 C CZ     . PHE C 3 124 ? 8.269  8.182   -13.921 1.00 14.71 ? 124 PHE B CZ     1 
ATOM   4344 N N      . GLU C 3 125 ? 3.870  14.055  -14.718 1.00 15.29 ? 125 GLU B N      1 
ATOM   4345 C CA     . GLU C 3 125 ? 2.502  14.558  -14.691 1.00 14.64 ? 125 GLU B CA     1 
ATOM   4346 C C      . GLU C 3 125 ? 2.175  15.344  -15.955 1.00 17.59 ? 125 GLU B C      1 
ATOM   4347 O O      . GLU C 3 125 ? 1.076  15.218  -16.490 1.00 18.04 ? 125 GLU B O      1 
ATOM   4348 C CB     . GLU C 3 125 ? 2.262  15.409  -13.434 1.00 14.74 ? 125 GLU B CB     1 
ATOM   4349 C CG     . GLU C 3 125 ? 2.229  14.598  -12.130 1.00 15.04 ? 125 GLU B CG     1 
ATOM   4350 C CD     . GLU C 3 125 ? 1.955  15.449  -10.870 1.00 24.96 ? 125 GLU B CD     1 
ATOM   4351 O OE1    . GLU C 3 125 ? 1.705  16.673  -11.009 1.00 28.38 ? 125 GLU B OE1    1 
ATOM   4352 O OE2    . GLU C 3 125 ? 1.992  14.887  -9.741  1.00 23.28 ? 125 GLU B OE2    1 
ATOM   4353 N N      . THR C 3 126 ? 3.110  16.143  -16.461 1.00 19.54 ? 126 THR B N      1 
ATOM   4354 C CA     . THR C 3 126 ? 2.783  16.954  -17.622 1.00 15.99 ? 126 THR B CA     1 
ATOM   4355 C C      . THR C 3 126 ? 2.954  16.214  -18.942 1.00 16.52 ? 126 THR B C      1 
ATOM   4356 O O      . THR C 3 126 ? 2.180  16.439  -19.872 1.00 21.47 ? 126 THR B O      1 
ATOM   4357 C CB     . THR C 3 126 ? 3.622  18.221  -17.651 1.00 17.04 ? 126 THR B CB     1 
ATOM   4358 O OG1    . THR C 3 126 ? 3.215  19.087  -16.583 1.00 21.22 ? 126 THR B OG1    1 
ATOM   4359 C CG2    . THR C 3 126 ? 3.421  18.916  -18.981 1.00 15.70 ? 126 THR B CG2    1 
ATOM   4360 N N      . PHE C 3 127 ? 3.951  15.351  -19.069 1.00 16.01 ? 127 PHE B N      1 
ATOM   4361 C CA     . PHE C 3 127 ? 4.178  14.679  -20.340 1.00 16.90 ? 127 PHE B CA     1 
ATOM   4362 C C      . PHE C 3 127 ? 3.829  13.205  -20.300 1.00 16.64 ? 127 PHE B C      1 
ATOM   4363 O O      . PHE C 3 127 ? 3.690  12.590  -21.361 1.00 16.41 ? 127 PHE B O      1 
ATOM   4364 C CB     . PHE C 3 127 ? 5.640  14.834  -20.791 1.00 17.70 ? 127 PHE B CB     1 
ATOM   4365 C CG     . PHE C 3 127 ? 6.096  16.259  -20.901 1.00 15.86 ? 127 PHE B CG     1 
ATOM   4366 C CD1    . PHE C 3 127 ? 5.718  17.035  -21.973 1.00 16.76 ? 127 PHE B CD1    1 
ATOM   4367 C CD2    . PHE C 3 127 ? 6.918  16.821  -19.937 1.00 17.47 ? 127 PHE B CD2    1 
ATOM   4368 C CE1    . PHE C 3 127 ? 6.141  18.351  -22.085 1.00 16.87 ? 127 PHE B CE1    1 
ATOM   4369 C CE2    . PHE C 3 127 ? 7.344  18.141  -20.055 1.00 17.98 ? 127 PHE B CE2    1 
ATOM   4370 C CZ     . PHE C 3 127 ? 6.946  18.903  -21.136 1.00 12.55 ? 127 PHE B CZ     1 
ATOM   4371 N N      . ASN C 3 128 ? 3.689  12.630  -19.109 1.00 18.56 ? 128 ASN B N      1 
ATOM   4372 C CA     . ASN C 3 128 ? 3.098  11.303  -18.968 1.00 22.27 ? 128 ASN B CA     1 
ATOM   4373 C C      . ASN C 3 128 ? 3.981  10.223  -19.595 1.00 19.16 ? 128 ASN B C      1 
ATOM   4374 O O      . ASN C 3 128 ? 3.506  9.272   -20.226 1.00 20.45 ? 128 ASN B O      1 
ATOM   4375 C CB     . ASN C 3 128 ? 1.685  11.278  -19.557 1.00 20.69 ? 128 ASN B CB     1 
ATOM   4376 C CG     . ASN C 3 128 ? 0.953  9.992   -19.248 1.00 29.97 ? 128 ASN B CG     1 
ATOM   4377 O OD1    . ASN C 3 128 ? 1.188  9.358   -18.209 1.00 28.40 ? 128 ASN B OD1    1 
ATOM   4378 N ND2    . ASN C 3 128 ? 0.059  9.590   -20.153 1.00 25.70 ? 128 ASN B ND2    1 
ATOM   4379 N N      . THR C 3 129 ? 5.276  10.363  -19.411 1.00 14.53 ? 129 THR B N      1 
ATOM   4380 C CA     . THR C 3 129 ? 6.188  9.336   -19.853 1.00 14.85 ? 129 THR B CA     1 
ATOM   4381 C C      . THR C 3 129 ? 5.934  8.030   -19.092 1.00 15.33 ? 129 THR B C      1 
ATOM   4382 O O      . THR C 3 129 ? 5.432  8.034   -17.969 1.00 17.53 ? 129 THR B O      1 
ATOM   4383 C CB     . THR C 3 129 ? 7.608  9.812   -19.624 1.00 17.55 ? 129 THR B CB     1 
ATOM   4384 O OG1    . THR C 3 129 ? 7.775  10.072  -18.220 1.00 18.11 ? 129 THR B OG1    1 
ATOM   4385 C CG2    . THR C 3 129 ? 7.846  11.106  -20.399 1.00 15.02 ? 129 THR B CG2    1 
ATOM   4386 N N      . PRO C 3 130 ? 6.272  6.912   -19.677 1.00 11.67 ? 130 PRO B N      1 
ATOM   4387 C CA     . PRO C 3 130 ? 6.167  5.639   -18.951 1.00 12.07 ? 130 PRO B CA     1 
ATOM   4388 C C      . PRO C 3 130 ? 7.265  5.434   -17.919 1.00 13.24 ? 130 PRO B C      1 
ATOM   4389 O O      . PRO C 3 130 ? 6.992  4.948   -16.823 1.00 17.90 ? 130 PRO B O      1 
ATOM   4390 C CB     . PRO C 3 130 ? 6.258  4.595   -20.065 1.00 12.58 ? 130 PRO B CB     1 
ATOM   4391 C CG     . PRO C 3 130 ? 7.001  5.283   -21.162 1.00 14.57 ? 130 PRO B CG     1 
ATOM   4392 C CD     . PRO C 3 130 ? 6.623  6.731   -21.093 1.00 14.19 ? 130 PRO B CD     1 
ATOM   4393 N N      . ALA C 3 131 ? 8.508  5.767   -18.258 1.00 13.09 ? 131 ALA B N      1 
ATOM   4394 C CA     . ALA C 3 131 ? 9.612  5.716   -17.315 1.00 12.48 ? 131 ALA B CA     1 
ATOM   4395 C C      . ALA C 3 131 ? 10.428 6.997   -17.443 1.00 10.41 ? 131 ALA B C      1 
ATOM   4396 O O      . ALA C 3 131 ? 10.214 7.804   -18.344 1.00 14.18 ? 131 ALA B O      1 
ATOM   4397 C CB     . ALA C 3 131 ? 10.480 4.473   -17.542 1.00 12.11 ? 131 ALA B CB     1 
ATOM   4398 N N      . MET C 3 132 ? 11.361 7.189   -16.521 1.00 9.48  ? 132 MET B N      1 
ATOM   4399 C CA     . MET C 3 132 ? 12.325 8.275   -16.619 1.00 10.67 ? 132 MET B CA     1 
ATOM   4400 C C      . MET C 3 132 ? 13.481 7.965   -15.682 1.00 10.00 ? 132 MET B C      1 
ATOM   4401 O O      . MET C 3 132 ? 13.376 7.103   -14.811 1.00 13.15 ? 132 MET B O      1 
ATOM   4402 C CB     . MET C 3 132 ? 11.702 9.614   -16.259 1.00 12.07 ? 132 MET B CB     1 
ATOM   4403 C CG     . MET C 3 132 ? 11.499 9.733   -14.792 1.00 14.77 ? 132 MET B CG     1 
ATOM   4404 S SD     . MET C 3 132 ? 11.836 11.404  -14.290 1.00 31.11 ? 132 MET B SD     1 
ATOM   4405 C CE     . MET C 3 132 ? 13.565 11.584  -14.738 1.00 16.01 ? 132 MET B CE     1 
ATOM   4406 N N      . TYR C 3 133 ? 14.585 8.676   -15.879 1.00 5.75  ? 133 TYR B N      1 
ATOM   4407 C CA     . TYR C 3 133 ? 15.765 8.564   -15.036 1.00 7.30  ? 133 TYR B CA     1 
ATOM   4408 C C      . TYR C 3 133 ? 16.488 9.897   -15.090 1.00 11.90 ? 133 TYR B C      1 
ATOM   4409 O O      . TYR C 3 133 ? 16.325 10.662  -16.042 1.00 11.55 ? 133 TYR B O      1 
ATOM   4410 C CB     . TYR C 3 133 ? 16.683 7.434   -15.501 1.00 7.99  ? 133 TYR B CB     1 
ATOM   4411 C CG     . TYR C 3 133 ? 17.769 7.018   -14.537 1.00 10.70 ? 133 TYR B CG     1 
ATOM   4412 C CD1    . TYR C 3 133 ? 17.516 6.096   -13.529 1.00 16.47 ? 133 TYR B CD1    1 
ATOM   4413 C CD2    . TYR C 3 133 ? 19.051 7.509   -14.658 1.00 10.32 ? 133 TYR B CD2    1 
ATOM   4414 C CE1    . TYR C 3 133 ? 18.507 5.707   -12.651 1.00 17.53 ? 133 TYR B CE1    1 
ATOM   4415 C CE2    . TYR C 3 133 ? 20.049 7.128   -13.789 1.00 9.89  ? 133 TYR B CE2    1 
ATOM   4416 C CZ     . TYR C 3 133 ? 19.778 6.230   -12.786 1.00 21.11 ? 133 TYR B CZ     1 
ATOM   4417 O OH     . TYR C 3 133 ? 20.786 5.858   -11.914 1.00 26.82 ? 133 TYR B OH     1 
ATOM   4418 N N      . VAL C 3 134 ? 17.293 10.184  -14.066 1.00 15.65 ? 134 VAL B N      1 
ATOM   4419 C CA     . VAL C 3 134 ? 18.107 11.397  -14.049 1.00 11.57 ? 134 VAL B CA     1 
ATOM   4420 C C      . VAL C 3 134 ? 19.548 11.004  -13.774 1.00 8.70  ? 134 VAL B C      1 
ATOM   4421 O O      . VAL C 3 134 ? 19.827 10.353  -12.767 1.00 7.41  ? 134 VAL B O      1 
ATOM   4422 C CB     . VAL C 3 134 ? 17.617 12.424  -13.006 1.00 9.86  ? 134 VAL B CB     1 
ATOM   4423 C CG1    . VAL C 3 134 ? 18.207 13.777  -13.306 1.00 9.50  ? 134 VAL B CG1    1 
ATOM   4424 C CG2    . VAL C 3 134 ? 16.123 12.508  -13.023 1.00 15.66 ? 134 VAL B CG2    1 
ATOM   4425 N N      . ALA C 3 135 ? 20.460 11.409  -14.658 1.00 9.97  ? 135 ALA B N      1 
ATOM   4426 C CA     . ALA C 3 135 ? 21.895 11.242  -14.467 1.00 6.71  ? 135 ALA B CA     1 
ATOM   4427 C C      . ALA C 3 135 ? 22.593 12.598  -14.358 1.00 8.64  ? 135 ALA B C      1 
ATOM   4428 O O      . ALA C 3 135 ? 22.080 13.621  -14.813 1.00 10.13 ? 135 ALA B O      1 
ATOM   4429 C CB     . ALA C 3 135 ? 22.499 10.441  -15.613 1.00 6.28  ? 135 ALA B CB     1 
ATOM   4430 N N      . ILE C 3 136 ? 23.775 12.599  -13.747 1.00 8.73  ? 136 ILE B N      1 
ATOM   4431 C CA     . ILE C 3 136 ? 24.604 13.803  -13.673 1.00 8.60  ? 136 ILE B CA     1 
ATOM   4432 C C      . ILE C 3 136 ? 25.415 13.944  -14.955 1.00 12.24 ? 136 ILE B C      1 
ATOM   4433 O O      . ILE C 3 136 ? 26.065 12.991  -15.406 1.00 11.32 ? 136 ILE B O      1 
ATOM   4434 C CB     . ILE C 3 136 ? 25.538 13.751  -12.457 1.00 9.78  ? 136 ILE B CB     1 
ATOM   4435 C CG1    . ILE C 3 136 ? 24.747 13.726  -11.153 1.00 7.21  ? 136 ILE B CG1    1 
ATOM   4436 C CG2    . ILE C 3 136 ? 26.498 14.904  -12.510 1.00 11.17 ? 136 ILE B CG2    1 
ATOM   4437 C CD1    . ILE C 3 136 ? 25.532 14.148  -9.952  1.00 10.18 ? 136 ILE B CD1    1 
ATOM   4438 N N      . GLN C 3 137 ? 25.403 15.143  -15.542 1.00 13.19 ? 137 GLN B N      1 
ATOM   4439 C CA     . GLN C 3 137 ? 25.975 15.302  -16.873 1.00 9.59  ? 137 GLN B CA     1 
ATOM   4440 C C      . GLN C 3 137 ? 27.376 14.716  -16.947 1.00 7.95  ? 137 GLN B C      1 
ATOM   4441 O O      . GLN C 3 137 ? 27.665 13.862  -17.791 1.00 6.04  ? 137 GLN B O      1 
ATOM   4442 C CB     . GLN C 3 137 ? 25.972 16.767  -17.275 1.00 9.19  ? 137 GLN B CB     1 
ATOM   4443 C CG     . GLN C 3 137 ? 24.679 17.166  -17.871 1.00 10.81 ? 137 GLN B CG     1 
ATOM   4444 C CD     . GLN C 3 137 ? 24.282 18.559  -17.471 1.00 13.49 ? 137 GLN B CD     1 
ATOM   4445 O OE1    . GLN C 3 137 ? 23.096 18.862  -17.304 1.00 12.63 ? 137 GLN B OE1    1 
ATOM   4446 N NE2    . GLN C 3 137 ? 25.277 19.426  -17.299 1.00 17.49 ? 137 GLN B NE2    1 
ATOM   4447 N N      . ALA C 3 138 ? 28.259 15.167  -16.056 1.00 11.43 ? 138 ALA B N      1 
ATOM   4448 C CA     . ALA C 3 138 ? 29.651 14.741  -16.100 1.00 7.59  ? 138 ALA B CA     1 
ATOM   4449 C C      . ALA C 3 138 ? 29.793 13.228  -15.976 1.00 7.94  ? 138 ALA B C      1 
ATOM   4450 O O      . ALA C 3 138 ? 30.706 12.647  -16.560 1.00 7.77  ? 138 ALA B O      1 
ATOM   4451 C CB     . ALA C 3 138 ? 30.456 15.446  -15.009 1.00 5.50  ? 138 ALA B CB     1 
ATOM   4452 N N      . VAL C 3 139 ? 28.911 12.564  -15.232 1.00 8.89  ? 139 VAL B N      1 
ATOM   4453 C CA     . VAL C 3 139 ? 29.073 11.117  -15.078 1.00 7.26  ? 139 VAL B CA     1 
ATOM   4454 C C      . VAL C 3 139 ? 28.842 10.414  -16.412 1.00 4.96  ? 139 VAL B C      1 
ATOM   4455 O O      . VAL C 3 139 ? 29.587 9.501   -16.780 1.00 5.12  ? 139 VAL B O      1 
ATOM   4456 C CB     . VAL C 3 139 ? 28.154 10.553  -13.968 1.00 7.22  ? 139 VAL B CB     1 
ATOM   4457 C CG1    . VAL C 3 139 ? 28.192 9.024   -13.963 1.00 7.58  ? 139 VAL B CG1    1 
ATOM   4458 C CG2    . VAL C 3 139 ? 28.591 11.046  -12.638 1.00 4.29  ? 139 VAL B CG2    1 
ATOM   4459 N N      . LEU C 3 140 ? 27.821 10.828  -17.164 1.00 8.55  ? 140 LEU B N      1 
ATOM   4460 C CA     . LEU C 3 140 ? 27.570 10.197  -18.462 1.00 7.76  ? 140 LEU B CA     1 
ATOM   4461 C C      . LEU C 3 140 ? 28.753 10.399  -19.392 1.00 8.91  ? 140 LEU B C      1 
ATOM   4462 O O      . LEU C 3 140 ? 29.107 9.515   -20.185 1.00 11.51 ? 140 LEU B O      1 
ATOM   4463 C CB     . LEU C 3 140 ? 26.302 10.760  -19.112 1.00 6.75  ? 140 LEU B CB     1 
ATOM   4464 C CG     . LEU C 3 140 ? 24.985 10.646  -18.356 1.00 8.46  ? 140 LEU B CG     1 
ATOM   4465 C CD1    . LEU C 3 140 ? 23.929 11.496  -19.023 1.00 8.58  ? 140 LEU B CD1    1 
ATOM   4466 C CD2    . LEU C 3 140 ? 24.524 9.196   -18.264 1.00 7.35  ? 140 LEU B CD2    1 
ATOM   4467 N N      . SER C 3 141 ? 29.368 11.566  -19.310 1.00 4.98  ? 141 SER B N      1 
ATOM   4468 C CA     . SER C 3 141 ? 30.527 11.858  -20.132 1.00 8.68  ? 141 SER B CA     1 
ATOM   4469 C C      . SER C 3 141 ? 31.673 10.885  -19.833 1.00 12.61 ? 141 SER B C      1 
ATOM   4470 O O      . SER C 3 141 ? 32.344 10.371  -20.740 1.00 10.22 ? 141 SER B O      1 
ATOM   4471 C CB     . SER C 3 141 ? 30.920 13.299  -19.866 1.00 8.75  ? 141 SER B CB     1 
ATOM   4472 O OG     . SER C 3 141 ? 31.906 13.691  -20.758 1.00 17.12 ? 141 SER B OG     1 
ATOM   4473 N N      . LEU C 3 142 ? 31.889 10.601  -18.557 1.00 9.55  ? 142 LEU B N      1 
ATOM   4474 C CA     . LEU C 3 142 ? 32.829 9.562   -18.185 1.00 8.12  ? 142 LEU B CA     1 
ATOM   4475 C C      . LEU C 3 142 ? 32.434 8.224   -18.796 1.00 12.12 ? 142 LEU B C      1 
ATOM   4476 O O      . LEU C 3 142 ? 33.299 7.475   -19.279 1.00 11.97 ? 142 LEU B O      1 
ATOM   4477 C CB     . LEU C 3 142 ? 32.894 9.467   -16.667 1.00 6.91  ? 142 LEU B CB     1 
ATOM   4478 C CG     . LEU C 3 142 ? 34.067 8.710   -16.074 1.00 7.73  ? 142 LEU B CG     1 
ATOM   4479 C CD1    . LEU C 3 142 ? 35.323 9.458   -16.362 1.00 4.77  ? 142 LEU B CD1    1 
ATOM   4480 C CD2    . LEU C 3 142 ? 33.819 8.553   -14.590 1.00 6.94  ? 142 LEU B CD2    1 
ATOM   4481 N N      . TYR C 3 143 ? 31.132 7.892   -18.763 1.00 8.82  ? 143 TYR B N      1 
ATOM   4482 C CA     . TYR C 3 143 ? 30.683 6.596   -19.271 1.00 9.76  ? 143 TYR B CA     1 
ATOM   4483 C C      . TYR C 3 143 ? 30.918 6.494   -20.768 1.00 12.93 ? 143 TYR B C      1 
ATOM   4484 O O      . TYR C 3 143 ? 31.156 5.399   -21.296 1.00 9.31  ? 143 TYR B O      1 
ATOM   4485 C CB     . TYR C 3 143 ? 29.193 6.361   -18.992 1.00 8.73  ? 143 TYR B CB     1 
ATOM   4486 C CG     . TYR C 3 143 ? 28.787 6.060   -17.565 1.00 7.56  ? 143 TYR B CG     1 
ATOM   4487 C CD1    . TYR C 3 143 ? 29.708 5.781   -16.592 1.00 8.53  ? 143 TYR B CD1    1 
ATOM   4488 C CD2    . TYR C 3 143 ? 27.457 6.041   -17.203 1.00 10.27 ? 143 TYR B CD2    1 
ATOM   4489 C CE1    . TYR C 3 143 ? 29.304 5.516   -15.278 1.00 12.44 ? 143 TYR B CE1    1 
ATOM   4490 C CE2    . TYR C 3 143 ? 27.050 5.765   -15.915 1.00 7.57  ? 143 TYR B CE2    1 
ATOM   4491 C CZ     . TYR C 3 143 ? 27.975 5.513   -14.953 1.00 11.01 ? 143 TYR B CZ     1 
ATOM   4492 O OH     . TYR C 3 143 ? 27.560 5.244   -13.664 1.00 11.37 ? 143 TYR B OH     1 
ATOM   4493 N N      . ALA C 3 144 ? 30.831 7.618   -21.476 1.00 17.23 ? 144 ALA B N      1 
ATOM   4494 C CA     . ALA C 3 144 ? 31.025 7.570   -22.919 1.00 15.66 ? 144 ALA B CA     1 
ATOM   4495 C C      . ALA C 3 144 ? 32.466 7.277   -23.291 1.00 13.13 ? 144 ALA B C      1 
ATOM   4496 O O      . ALA C 3 144 ? 32.735 6.936   -24.443 1.00 12.24 ? 144 ALA B O      1 
ATOM   4497 C CB     . ALA C 3 144 ? 30.563 8.880   -23.554 1.00 13.58 ? 144 ALA B CB     1 
ATOM   4498 N N      . SER C 3 145 ? 33.392 7.413   -22.351 1.00 14.69 ? 145 SER B N      1 
ATOM   4499 C CA     . SER C 3 145 ? 34.772 7.022   -22.572 1.00 15.47 ? 145 SER B CA     1 
ATOM   4500 C C      . SER C 3 145 ? 35.091 5.673   -21.950 1.00 14.44 ? 145 SER B C      1 
ATOM   4501 O O      . SER C 3 145 ? 36.269 5.323   -21.848 1.00 12.05 ? 145 SER B O      1 
ATOM   4502 C CB     . SER C 3 145 ? 35.724 8.093   -22.026 1.00 14.34 ? 145 SER B CB     1 
ATOM   4503 O OG     . SER C 3 145 ? 35.912 7.944   -20.631 1.00 12.18 ? 145 SER B OG     1 
ATOM   4504 N N      . GLY C 3 146 ? 34.070 4.924   -21.515 1.00 14.17 ? 146 GLY B N      1 
ATOM   4505 C CA     . GLY C 3 146 ? 34.242 3.594   -20.957 1.00 15.27 ? 146 GLY B CA     1 
ATOM   4506 C C      . GLY C 3 146 ? 34.806 3.545   -19.559 1.00 13.02 ? 146 GLY B C      1 
ATOM   4507 O O      . GLY C 3 146 ? 35.337 2.509   -19.154 1.00 16.68 ? 146 GLY B O      1 
ATOM   4508 N N      . ARG C 3 147 ? 34.729 4.638   -18.809 1.00 11.57 ? 147 ARG B N      1 
ATOM   4509 C CA     . ARG C 3 147 ? 35.232 4.682   -17.450 1.00 10.74 ? 147 ARG B CA     1 
ATOM   4510 C C      . ARG C 3 147 ? 34.070 4.849   -16.490 1.00 14.83 ? 147 ARG B C      1 
ATOM   4511 O O      . ARG C 3 147 ? 33.000 5.354   -16.869 1.00 11.45 ? 147 ARG B O      1 
ATOM   4512 C CB     . ARG C 3 147 ? 36.216 5.827   -17.251 1.00 10.21 ? 147 ARG B CB     1 
ATOM   4513 C CG     . ARG C 3 147 ? 37.513 5.647   -17.996 1.00 8.49  ? 147 ARG B CG     1 
ATOM   4514 C CD     . ARG C 3 147 ? 38.135 6.977   -18.312 1.00 9.62  ? 147 ARG B CD     1 
ATOM   4515 N NE     . ARG C 3 147 ? 39.411 6.833   -18.995 1.00 12.51 ? 147 ARG B NE     1 
ATOM   4516 C CZ     . ARG C 3 147 ? 39.546 6.645   -20.296 1.00 11.50 ? 147 ARG B CZ     1 
ATOM   4517 N NH1    . ARG C 3 147 ? 38.499 6.608   -21.100 1.00 9.79  ? 147 ARG B NH1    1 
ATOM   4518 N NH2    . ARG C 3 147 ? 40.761 6.463   -20.795 1.00 18.18 ? 147 ARG B NH2    1 
ATOM   4519 N N      . THR C 3 148 ? 34.297 4.404   -15.239 1.00 13.23 ? 148 THR B N      1 
ATOM   4520 C CA     . THR C 3 148 ? 33.418 4.706   -14.113 1.00 9.57  ? 148 THR B CA     1 
ATOM   4521 C C      . THR C 3 148 ? 34.128 5.382   -12.951 1.00 12.36 ? 148 THR B C      1 
ATOM   4522 O O      . THR C 3 148 ? 33.463 5.697   -11.952 1.00 14.30 ? 148 THR B O      1 
ATOM   4523 C CB     . THR C 3 148 ? 32.726 3.436   -13.578 1.00 11.17 ? 148 THR B CB     1 
ATOM   4524 O OG1    . THR C 3 148 ? 33.684 2.573   -12.949 1.00 9.27  ? 148 THR B OG1    1 
ATOM   4525 C CG2    . THR C 3 148 ? 32.026 2.704   -14.692 1.00 11.63 ? 148 THR B CG2    1 
ATOM   4526 N N      . THR C 3 149 ? 35.450 5.562   -13.029 1.00 10.94 ? 149 THR B N      1 
ATOM   4527 C CA     . THR C 3 149 ? 36.217 6.352   -12.077 1.00 8.54  ? 149 THR B CA     1 
ATOM   4528 C C      . THR C 3 149 ? 37.117 7.306   -12.845 1.00 9.53  ? 149 THR B C      1 
ATOM   4529 O O      . THR C 3 149 ? 37.944 6.861   -13.643 1.00 13.86 ? 149 THR B O      1 
ATOM   4530 C CB     . THR C 3 149 ? 37.066 5.464   -11.170 1.00 7.39  ? 149 THR B CB     1 
ATOM   4531 O OG1    . THR C 3 149 ? 36.240 4.864   -10.172 1.00 14.68 ? 149 THR B OG1    1 
ATOM   4532 C CG2    . THR C 3 149 ? 38.141 6.286   -10.487 1.00 7.08  ? 149 THR B CG2    1 
ATOM   4533 N N      . GLY C 3 150 ? 36.968 8.602   -12.591 1.00 2.33  ? 150 GLY B N      1 
ATOM   4534 C CA     . GLY C 3 150 ? 37.835 9.619   -13.161 1.00 6.61  ? 150 GLY B CA     1 
ATOM   4535 C C      . GLY C 3 150 ? 37.373 10.985  -12.696 1.00 8.18  ? 150 GLY B C      1 
ATOM   4536 O O      . GLY C 3 150 ? 36.489 11.101  -11.841 1.00 7.28  ? 150 GLY B O      1 
ATOM   4537 N N      . ILE C 3 151 ? 37.983 12.039  -13.252 1.00 6.61  ? 151 ILE B N      1 
ATOM   4538 C CA     . ILE C 3 151 ? 37.511 13.398  -12.988 1.00 6.93  ? 151 ILE B CA     1 
ATOM   4539 C C      . ILE C 3 151 ? 37.230 14.084  -14.308 1.00 5.73  ? 151 ILE B C      1 
ATOM   4540 O O      . ILE C 3 151 ? 38.142 14.317  -15.107 1.00 7.46  ? 151 ILE B O      1 
ATOM   4541 C CB     . ILE C 3 151 ? 38.480 14.234  -12.145 1.00 7.63  ? 151 ILE B CB     1 
ATOM   4542 C CG1    . ILE C 3 151 ? 37.877 15.628  -11.945 1.00 6.36  ? 151 ILE B CG1    1 
ATOM   4543 C CG2    . ILE C 3 151 ? 39.845 14.328  -12.805 1.00 7.81  ? 151 ILE B CG2    1 
ATOM   4544 C CD1    . ILE C 3 151 ? 38.752 16.556  -11.167 1.00 7.36  ? 151 ILE B CD1    1 
ATOM   4545 N N      . VAL C 3 152 ? 36.003 14.402  -14.520 1.00 5.90  ? 152 VAL B N      1 
ATOM   4546 C CA     . VAL C 3 152 ? 35.527 15.006  -15.751 1.00 8.36  ? 152 VAL B CA     1 
ATOM   4547 C C      . VAL C 3 152 ? 35.630 16.515  -15.629 1.00 7.73  ? 152 VAL B C      1 
ATOM   4548 O O      . VAL C 3 152 ? 35.323 17.082  -14.582 1.00 8.35  ? 152 VAL B O      1 
ATOM   4549 C CB     . VAL C 3 152 ? 34.074 14.573  -15.997 1.00 5.83  ? 152 VAL B CB     1 
ATOM   4550 C CG1    . VAL C 3 152 ? 33.466 15.374  -17.113 1.00 5.01  ? 152 VAL B CG1    1 
ATOM   4551 C CG2    . VAL C 3 152 ? 34.019 13.079  -16.248 1.00 5.39  ? 152 VAL B CG2    1 
ATOM   4552 N N      . MET C 3 153 ? 36.040 17.183  -16.687 1.00 7.55  ? 153 MET B N      1 
ATOM   4553 C CA     . MET C 3 153 ? 35.848 18.619  -16.767 1.00 7.90  ? 153 MET B CA     1 
ATOM   4554 C C      . MET C 3 153 ? 34.775 18.893  -17.809 1.00 11.83 ? 153 MET B C      1 
ATOM   4555 O O      . MET C 3 153 ? 35.004 18.719  -19.008 1.00 14.30 ? 153 MET B O      1 
ATOM   4556 C CB     . MET C 3 153 ? 37.132 19.352  -17.103 1.00 9.44  ? 153 MET B CB     1 
ATOM   4557 C CG     . MET C 3 153 ? 36.990 20.823  -16.746 1.00 18.63 ? 153 MET B CG     1 
ATOM   4558 S SD     . MET C 3 153 ? 38.059 21.880  -17.700 1.00 38.99 ? 153 MET B SD     1 
ATOM   4559 C CE     . MET C 3 153 ? 37.713 21.223  -19.330 1.00 19.54 ? 153 MET B CE     1 
ATOM   4560 N N      . ASP C 3 154 ? 33.605 19.305  -17.350 1.00 10.35 ? 154 ASP B N      1 
ATOM   4561 C CA     . ASP C 3 154 ? 32.461 19.567  -18.206 1.00 13.27 ? 154 ASP B CA     1 
ATOM   4562 C C      . ASP C 3 154 ? 32.341 21.070  -18.385 1.00 12.31 ? 154 ASP B C      1 
ATOM   4563 O O      . ASP C 3 154 ? 32.259 21.805  -17.397 1.00 15.14 ? 154 ASP B O      1 
ATOM   4564 C CB     . ASP C 3 154 ? 31.189 18.995  -17.581 1.00 14.43 ? 154 ASP B CB     1 
ATOM   4565 C CG     . ASP C 3 154 ? 30.078 18.741  -18.609 1.00 23.63 ? 154 ASP B CG     1 
ATOM   4566 O OD1    . ASP C 3 154 ? 30.403 18.606  -19.823 1.00 17.54 ? 154 ASP B OD1    1 
ATOM   4567 O OD2    . ASP C 3 154 ? 28.882 18.666  -18.187 1.00 28.87 ? 154 ASP B OD2    1 
ATOM   4568 N N      . SER C 3 155 ? 32.323 21.532  -19.624 1.00 10.78 ? 155 SER B N      1 
ATOM   4569 C CA     . SER C 3 155 ? 32.234 22.966  -19.871 1.00 12.88 ? 155 SER B CA     1 
ATOM   4570 C C      . SER C 3 155 ? 31.416 23.195  -21.123 1.00 14.64 ? 155 SER B C      1 
ATOM   4571 O O      . SER C 3 155 ? 31.835 22.827  -22.233 1.00 9.85  ? 155 SER B O      1 
ATOM   4572 C CB     . SER C 3 155 ? 33.615 23.610  -19.999 1.00 13.09 ? 155 SER B CB     1 
ATOM   4573 O OG     . SER C 3 155 ? 33.489 25.022  -20.054 1.00 15.88 ? 155 SER B OG     1 
ATOM   4574 N N      . GLY C 3 156 ? 30.261 23.817  -20.937 1.00 15.46 ? 156 GLY B N      1 
ATOM   4575 C CA     . GLY C 3 156 ? 29.454 24.182  -22.068 1.00 17.70 ? 156 GLY B CA     1 
ATOM   4576 C C      . GLY C 3 156 ? 29.294 25.678  -22.138 1.00 17.20 ? 156 GLY B C      1 
ATOM   4577 O O      . GLY C 3 156 ? 30.260 26.441  -22.039 1.00 14.81 ? 156 GLY B O      1 
ATOM   4578 N N      . ASP C 3 157 ? 28.051 26.108  -22.238 1.00 21.80 ? 157 ASP B N      1 
ATOM   4579 C CA     . ASP C 3 157 ? 27.763 27.450  -22.707 1.00 19.85 ? 157 ASP B CA     1 
ATOM   4580 C C      . ASP C 3 157 ? 27.859 28.472  -21.592 1.00 22.95 ? 157 ASP B C      1 
ATOM   4581 O O      . ASP C 3 157 ? 28.359 29.577  -21.812 1.00 20.78 ? 157 ASP B O      1 
ATOM   4582 C CB     . ASP C 3 157 ? 26.390 27.413  -23.347 1.00 27.70 ? 157 ASP B CB     1 
ATOM   4583 C CG     . ASP C 3 157 ? 26.180 26.112  -24.127 1.00 48.48 ? 157 ASP B CG     1 
ATOM   4584 O OD1    . ASP C 3 157 ? 25.755 25.061  -23.523 1.00 34.10 ? 157 ASP B OD1    1 
ATOM   4585 O OD2    . ASP C 3 157 ? 26.505 26.150  -25.351 1.00 54.57 ? 157 ASP B OD2    1 
ATOM   4586 N N      . GLY C 3 158 ? 27.429 28.106  -20.384 1.00 25.46 ? 158 GLY B N      1 
ATOM   4587 C CA     . GLY C 3 158 ? 27.306 29.066  -19.302 1.00 20.41 ? 158 GLY B CA     1 
ATOM   4588 C C      . GLY C 3 158 ? 27.906 28.633  -17.980 1.00 21.63 ? 158 GLY B C      1 
ATOM   4589 O O      . GLY C 3 158 ? 27.860 29.396  -17.008 1.00 26.80 ? 158 GLY B O      1 
ATOM   4590 N N      . VAL C 3 159 ? 28.373 27.391  -17.932 1.00 15.48 ? 159 VAL B N      1 
ATOM   4591 C CA     . VAL C 3 159 ? 28.983 26.850  -16.724 1.00 16.33 ? 159 VAL B CA     1 
ATOM   4592 C C      . VAL C 3 159 ? 30.033 25.777  -16.933 1.00 12.68 ? 159 VAL B C      1 
ATOM   4593 O O      . VAL C 3 159 ? 29.909 24.936  -17.788 1.00 16.63 ? 159 VAL B O      1 
ATOM   4594 C CB     . VAL C 3 159 ? 27.917 26.432  -15.672 1.00 19.61 ? 159 VAL B CB     1 
ATOM   4595 C CG1    . VAL C 3 159 ? 27.302 25.074  -15.943 1.00 14.80 ? 159 VAL B CG1    1 
ATOM   4596 C CG2    . VAL C 3 159 ? 28.447 26.564  -14.264 1.00 21.14 ? 159 VAL B CG2    1 
ATOM   4597 N N      . THR C 3 160 ? 31.106 25.866  -16.184 1.00 12.62 ? 160 THR B N      1 
ATOM   4598 C CA     . THR C 3 160 ? 32.141 24.869  -16.216 1.00 13.62 ? 160 THR B CA     1 
ATOM   4599 C C      . THR C 3 160 ? 32.161 24.103  -14.890 1.00 14.34 ? 160 THR B C      1 
ATOM   4600 O O      . THR C 3 160 ? 31.930 24.662  -13.844 1.00 12.74 ? 160 THR B O      1 
ATOM   4601 C CB     . THR C 3 160 ? 33.505 25.503  -16.510 1.00 16.91 ? 160 THR B CB     1 
ATOM   4602 O OG1    . THR C 3 160 ? 33.455 26.162  -17.765 1.00 13.68 ? 160 THR B OG1    1 
ATOM   4603 C CG2    . THR C 3 160 ? 34.641 24.489  -16.519 1.00 13.17 ? 160 THR B CG2    1 
ATOM   4604 N N      . HIS C 3 161 ? 32.388 22.803  -14.948 1.00 14.95 ? 161 HIS B N      1 
ATOM   4605 C CA     . HIS C 3 161 ? 32.461 21.971  -13.747 1.00 12.68 ? 161 HIS B CA     1 
ATOM   4606 C C      . HIS C 3 161 ? 33.596 20.985  -13.691 1.00 9.60  ? 161 HIS B C      1 
ATOM   4607 O O      . HIS C 3 161 ? 33.896 20.379  -14.676 1.00 7.84  ? 161 HIS B O      1 
ATOM   4608 C CB     . HIS C 3 161 ? 31.177 21.177  -13.583 1.00 10.02 ? 161 HIS B CB     1 
ATOM   4609 C CG     . HIS C 3 161 ? 29.989 21.981  -13.177 1.00 11.91 ? 161 HIS B CG     1 
ATOM   4610 N ND1    . HIS C 3 161 ? 29.731 22.318  -11.870 1.00 13.78 ? 161 HIS B ND1    1 
ATOM   4611 C CD2    . HIS C 3 161 ? 28.957 22.464  -13.901 1.00 12.04 ? 161 HIS B CD2    1 
ATOM   4612 C CE1    . HIS C 3 161 ? 28.604 22.998  -11.809 1.00 13.14 ? 161 HIS B CE1    1 
ATOM   4613 N NE2    . HIS C 3 161 ? 28.117 23.105  -13.028 1.00 12.99 ? 161 HIS B NE2    1 
ATOM   4614 N N      . THR C 3 162 ? 34.295 20.893  -12.566 1.00 9.49  ? 162 THR B N      1 
ATOM   4615 C CA     . THR C 3 162 ? 35.243 19.800  -12.389 1.00 11.84 ? 162 THR B CA     1 
ATOM   4616 C C      . THR C 3 162 ? 34.545 18.841  -11.443 1.00 8.32  ? 162 THR B C      1 
ATOM   4617 O O      . THR C 3 162 ? 34.032 19.259  -10.407 1.00 7.99  ? 162 THR B O      1 
ATOM   4618 C CB     . THR C 3 162 ? 36.614 20.262  -11.862 1.00 12.75 ? 162 THR B CB     1 
ATOM   4619 O OG1    . THR C 3 162 ? 36.441 21.415  -11.051 1.00 22.28 ? 162 THR B OG1    1 
ATOM   4620 C CG2    . THR C 3 162 ? 37.609 20.630  -13.009 1.00 7.27  ? 162 THR B CG2    1 
ATOM   4621 N N      . VAL C 3 163 ? 34.443 17.585  -11.851 1.00 8.71  ? 163 VAL B N      1 
ATOM   4622 C CA     . VAL C 3 163 ? 33.616 16.609  -11.160 1.00 7.47  ? 163 VAL B CA     1 
ATOM   4623 C C      . VAL C 3 163 ? 34.430 15.344  -10.947 1.00 5.44  ? 163 VAL B C      1 
ATOM   4624 O O      . VAL C 3 163 ? 34.568 14.555  -11.881 1.00 7.76  ? 163 VAL B O      1 
ATOM   4625 C CB     . VAL C 3 163 ? 32.340 16.324  -11.963 1.00 5.59  ? 163 VAL B CB     1 
ATOM   4626 C CG1    . VAL C 3 163 ? 31.527 15.303  -11.262 1.00 5.25  ? 163 VAL B CG1    1 
ATOM   4627 C CG2    . VAL C 3 163 ? 31.528 17.613  -12.145 1.00 7.54  ? 163 VAL B CG2    1 
ATOM   4628 N N      . PRO C 3 164 ? 34.903 15.139  -9.731  1.00 7.25  ? 164 PRO B N      1 
ATOM   4629 C CA     . PRO C 3 164 ? 35.522 13.861  -9.435  1.00 6.62  ? 164 PRO B CA     1 
ATOM   4630 C C      . PRO C 3 164 ? 34.473 12.752  -9.240  1.00 6.29  ? 164 PRO B C      1 
ATOM   4631 O O      . PRO C 3 164 ? 33.533 12.924  -8.519  1.00 5.03  ? 164 PRO B O      1 
ATOM   4632 C CB     . PRO C 3 164 ? 36.314 14.170  -8.182  1.00 5.63  ? 164 PRO B CB     1 
ATOM   4633 C CG     . PRO C 3 164 ? 35.620 15.296  -7.536  1.00 5.63  ? 164 PRO B CG     1 
ATOM   4634 C CD     . PRO C 3 164 ? 35.211 16.134  -8.686  1.00 7.71  ? 164 PRO B CD     1 
ATOM   4635 N N      . ILE C 3 165 ? 34.618 11.651  -9.944  1.00 8.30  ? 165 ILE B N      1 
ATOM   4636 C CA     . ILE C 3 165 ? 33.714 10.513  -9.865  1.00 7.62  ? 165 ILE B CA     1 
ATOM   4637 C C      . ILE C 3 165 ? 34.426 9.224   -9.476  1.00 8.71  ? 165 ILE B C      1 
ATOM   4638 O O      . ILE C 3 165 ? 35.412 8.870   -10.055 1.00 8.08  ? 165 ILE B O      1 
ATOM   4639 C CB     . ILE C 3 165 ? 32.940 10.296  -11.195 1.00 4.84  ? 165 ILE B CB     1 
ATOM   4640 C CG1    . ILE C 3 165 ? 32.162 11.545  -11.591 1.00 6.28  ? 165 ILE B CG1    1 
ATOM   4641 C CG2    . ILE C 3 165 ? 32.048 9.075   -11.129 1.00 6.32  ? 165 ILE B CG2    1 
ATOM   4642 C CD1    . ILE C 3 165 ? 32.280 11.889  -13.054 1.00 5.18  ? 165 ILE B CD1    1 
ATOM   4643 N N      . TYR C 3 166 ? 33.940 8.557   -8.453  1.00 9.47  ? 166 TYR B N      1 
ATOM   4644 C CA     . TYR C 3 166 ? 34.473 7.280   -8.033  1.00 10.19 ? 166 TYR B CA     1 
ATOM   4645 C C      . TYR C 3 166 ? 33.394 6.274   -8.141  1.00 11.70 ? 166 TYR B C      1 
ATOM   4646 O O      . TYR C 3 166 ? 32.428 6.357   -7.428  1.00 10.73 ? 166 TYR B O      1 
ATOM   4647 C CB     . TYR C 3 166 ? 34.970 7.315   -6.594  1.00 11.63 ? 166 TYR B CB     1 
ATOM   4648 C CG     . TYR C 3 166 ? 35.628 6.049   -6.143  1.00 14.96 ? 166 TYR B CG     1 
ATOM   4649 C CD1    . TYR C 3 166 ? 36.840 5.655   -6.671  1.00 13.05 ? 166 TYR B CD1    1 
ATOM   4650 C CD2    . TYR C 3 166 ? 35.032 5.244   -5.193  1.00 15.55 ? 166 TYR B CD2    1 
ATOM   4651 C CE1    . TYR C 3 166 ? 37.443 4.489   -6.263  1.00 14.83 ? 166 TYR B CE1    1 
ATOM   4652 C CE2    . TYR C 3 166 ? 35.628 4.081   -4.778  1.00 17.38 ? 166 TYR B CE2    1 
ATOM   4653 C CZ     . TYR C 3 166 ? 36.834 3.711   -5.316  1.00 20.94 ? 166 TYR B CZ     1 
ATOM   4654 O OH     . TYR C 3 166 ? 37.426 2.548   -4.901  1.00 27.82 ? 166 TYR B OH     1 
ATOM   4655 N N      . GLU C 3 167 ? 33.563 5.315   -9.028  1.00 11.98 ? 167 GLU B N      1 
ATOM   4656 C CA     . GLU C 3 167 ? 32.600 4.256   -9.248  1.00 10.89 ? 167 GLU B CA     1 
ATOM   4657 C C      . GLU C 3 167 ? 31.200 4.706   -9.563  1.00 10.74 ? 167 GLU B C      1 
ATOM   4658 O O      . GLU C 3 167 ? 30.263 4.231   -8.969  1.00 7.88  ? 167 GLU B O      1 
ATOM   4659 C CB     . GLU C 3 167 ? 32.687 3.195   -8.159  1.00 12.00 ? 167 GLU B CB     1 
ATOM   4660 C CG     . GLU C 3 167 ? 34.094 2.735   -7.861  1.00 13.50 ? 167 GLU B CG     1 
ATOM   4661 C CD     . GLU C 3 167 ? 34.122 1.658   -6.806  1.00 23.57 ? 167 GLU B CD     1 
ATOM   4662 O OE1    . GLU C 3 167 ? 33.260 1.685   -5.913  1.00 33.68 ? 167 GLU B OE1    1 
ATOM   4663 O OE2    . GLU C 3 167 ? 35.002 0.785   -6.866  1.00 32.86 ? 167 GLU B OE2    1 
ATOM   4664 N N      . GLY C 3 168 ? 31.071 5.607   -10.515 1.00 8.19  ? 168 GLY B N      1 
ATOM   4665 C CA     . GLY C 3 168 ? 29.788 6.119   -10.920 1.00 9.82  ? 168 GLY B CA     1 
ATOM   4666 C C      . GLY C 3 168 ? 29.216 7.198   -10.085 1.00 6.09  ? 168 GLY B C      1 
ATOM   4667 O O      . GLY C 3 168 ? 28.176 7.717   -10.394 1.00 7.90  ? 168 GLY B O      1 
ATOM   4668 N N      . TYR C 3 169 ? 29.898 7.527   -9.015  1.00 6.69  ? 169 TYR B N      1 
ATOM   4669 C CA     . TYR C 3 169 ? 29.406 8.495   -8.090  1.00 10.90 ? 169 TYR B CA     1 
ATOM   4670 C C      . TYR C 3 169 ? 30.186 9.773   -8.030  1.00 11.22 ? 169 TYR B C      1 
ATOM   4671 O O      . TYR C 3 169 ? 31.338 9.779   -7.690  1.00 10.09 ? 169 TYR B O      1 
ATOM   4672 C CB     . TYR C 3 169 ? 29.278 7.856   -6.715  1.00 8.34  ? 169 TYR B CB     1 
ATOM   4673 C CG     . TYR C 3 169 ? 28.685 8.708   -5.637  1.00 9.19  ? 169 TYR B CG     1 
ATOM   4674 C CD1    . TYR C 3 169 ? 27.349 9.052   -5.663  1.00 11.60 ? 169 TYR B CD1    1 
ATOM   4675 C CD2    . TYR C 3 169 ? 29.454 9.145   -4.576  1.00 11.34 ? 169 TYR B CD2    1 
ATOM   4676 C CE1    . TYR C 3 169 ? 26.795 9.823   -4.671  1.00 10.31 ? 169 TYR B CE1    1 
ATOM   4677 C CE2    . TYR C 3 169 ? 28.908 9.922   -3.582  1.00 12.30 ? 169 TYR B CE2    1 
ATOM   4678 C CZ     . TYR C 3 169 ? 27.578 10.252  -3.638  1.00 10.60 ? 169 TYR B CZ     1 
ATOM   4679 O OH     . TYR C 3 169 ? 27.020 11.012  -2.659  1.00 9.86  ? 169 TYR B OH     1 
ATOM   4680 N N      . ALA C 3 170 ? 29.522 10.863  -8.340  1.00 5.57  ? 170 ALA B N      1 
ATOM   4681 C CA     . ALA C 3 170 ? 30.144 12.136  -8.209  1.00 8.81  ? 170 ALA B CA     1 
ATOM   4682 C C      . ALA C 3 170 ? 30.297 12.496  -6.773  1.00 10.46 ? 170 ALA B C      1 
ATOM   4683 O O      . ALA C 3 170 ? 29.346 12.505  -6.035  1.00 10.06 ? 170 ALA B O      1 
ATOM   4684 C CB     . ALA C 3 170 ? 29.372 13.183  -8.956  1.00 7.58  ? 170 ALA B CB     1 
ATOM   4685 N N      . LEU C 3 171 ? 31.508 12.805  -6.388  1.00 8.43  ? 171 LEU B N      1 
ATOM   4686 C CA     . LEU C 3 171 ? 31.838 13.098  -5.036  1.00 7.44  ? 171 LEU B CA     1 
ATOM   4687 C C      . LEU C 3 171 ? 31.475 14.513  -4.704  1.00 11.17 ? 171 LEU B C      1 
ATOM   4688 O O      . LEU C 3 171 ? 32.167 15.423  -5.091  1.00 10.85 ? 171 LEU B O      1 
ATOM   4689 C CB     . LEU C 3 171 ? 33.309 12.766  -4.848  1.00 5.72  ? 171 LEU B CB     1 
ATOM   4690 C CG     . LEU C 3 171 ? 33.746 11.393  -5.312  1.00 7.63  ? 171 LEU B CG     1 
ATOM   4691 C CD1    . LEU C 3 171 ? 35.257 11.312  -5.278  1.00 9.97  ? 171 LEU B CD1    1 
ATOM   4692 C CD2    . LEU C 3 171 ? 33.114 10.320  -4.450  1.00 7.86  ? 171 LEU B CD2    1 
ATOM   4693 N N      . PRO C 3 172 ? 30.400 14.689  -3.934  1.00 12.97 ? 172 PRO B N      1 
ATOM   4694 C CA     . PRO C 3 172 ? 29.843 16.001  -3.661  1.00 9.62  ? 172 PRO B CA     1 
ATOM   4695 C C      . PRO C 3 172 ? 30.706 16.948  -2.902  1.00 11.47 ? 172 PRO B C      1 
ATOM   4696 O O      . PRO C 3 172 ? 30.496 18.135  -3.013  1.00 12.90 ? 172 PRO B O      1 
ATOM   4697 C CB     . PRO C 3 172 ? 28.615 15.644  -2.848  1.00 10.58 ? 172 PRO B CB     1 
ATOM   4698 C CG     . PRO C 3 172 ? 28.343 14.211  -3.100  1.00 13.19 ? 172 PRO B CG     1 
ATOM   4699 C CD     . PRO C 3 172 ? 29.711 13.648  -3.168  1.00 12.07 ? 172 PRO B CD     1 
ATOM   4700 N N      . HIS C 3 173 ? 31.662 16.436  -2.162  1.00 11.11 ? 173 HIS B N      1 
ATOM   4701 C CA     . HIS C 3 173 ? 32.597 17.248  -1.392  1.00 11.33 ? 173 HIS B CA     1 
ATOM   4702 C C      . HIS C 3 173 ? 33.763 17.780  -2.205  1.00 9.97  ? 173 HIS B C      1 
ATOM   4703 O O      . HIS C 3 173 ? 34.557 18.543  -1.653  1.00 11.21 ? 173 HIS B O      1 
ATOM   4704 C CB     . HIS C 3 173 ? 33.142 16.445  -0.241  1.00 8.75  ? 173 HIS B CB     1 
ATOM   4705 C CG     . HIS C 3 173 ? 33.497 15.053  -0.623  1.00 8.11  ? 173 HIS B CG     1 
ATOM   4706 N ND1    . HIS C 3 173 ? 34.763 14.696  -1.033  1.00 7.59  ? 173 HIS B ND1    1 
ATOM   4707 C CD2    . HIS C 3 173 ? 32.749 13.925  -0.663  1.00 6.74  ? 173 HIS B CD2    1 
ATOM   4708 C CE1    . HIS C 3 173 ? 34.782 13.403  -1.299  1.00 9.02  ? 173 HIS B CE1    1 
ATOM   4709 N NE2    . HIS C 3 173 ? 33.573 12.913  -1.082  1.00 8.90  ? 173 HIS B NE2    1 
ATOM   4710 N N      . ALA C 3 174 ? 33.905 17.401  -3.475  1.00 7.14  ? 174 ALA B N      1 
ATOM   4711 C CA     . ALA C 3 174 ? 35.019 17.904  -4.273  1.00 11.83 ? 174 ALA B CA     1 
ATOM   4712 C C      . ALA C 3 174 ? 34.611 18.532  -5.602  1.00 10.82 ? 174 ALA B C      1 
ATOM   4713 O O      . ALA C 3 174 ? 35.454 19.155  -6.254  1.00 4.50  ? 174 ALA B O      1 
ATOM   4714 C CB     . ALA C 3 174 ? 36.044 16.786  -4.522  1.00 8.11  ? 174 ALA B CB     1 
ATOM   4715 N N      . ILE C 3 175 ? 33.332 18.515  -5.909  1.00 9.94  ? 175 ILE B N      1 
ATOM   4716 C CA     . ILE C 3 175 ? 32.829 19.183  -7.089  1.00 11.29 ? 175 ILE B CA     1 
ATOM   4717 C C      . ILE C 3 175 ? 33.060 20.693  -7.087  1.00 11.75 ? 175 ILE B C      1 
ATOM   4718 O O      . ILE C 3 175 ? 32.711 21.377  -6.158  1.00 17.08 ? 175 ILE B O      1 
ATOM   4719 C CB     . ILE C 3 175 ? 31.355 18.825  -7.371  1.00 9.23  ? 175 ILE B CB     1 
ATOM   4720 C CG1    . ILE C 3 175 ? 31.225 17.342  -7.669  1.00 8.28  ? 175 ILE B CG1    1 
ATOM   4721 C CG2    . ILE C 3 175 ? 30.828 19.596  -8.561  1.00 7.67  ? 175 ILE B CG2    1 
ATOM   4722 C CD1    . ILE C 3 175 ? 29.797 16.867  -7.733  1.00 9.06  ? 175 ILE B CD1    1 
ATOM   4723 N N      . LEU C 3 176 ? 33.669 21.197  -8.136  1.00 10.21 ? 176 LEU B N      1 
ATOM   4724 C CA     . LEU C 3 176 ? 33.923 22.599  -8.252  1.00 14.29 ? 176 LEU B CA     1 
ATOM   4725 C C      . LEU C 3 176 ? 33.217 23.252  -9.450  1.00 16.82 ? 176 LEU B C      1 
ATOM   4726 O O      . LEU C 3 176 ? 33.325 22.796  -10.556 1.00 15.01 ? 176 LEU B O      1 
ATOM   4727 C CB     . LEU C 3 176 ? 35.425 22.802  -8.294  1.00 14.22 ? 176 LEU B CB     1 
ATOM   4728 C CG     . LEU C 3 176 ? 36.107 23.100  -6.974  1.00 23.55 ? 176 LEU B CG     1 
ATOM   4729 C CD1    . LEU C 3 176 ? 37.611 23.089  -7.123  1.00 12.11 ? 176 LEU B CD1    1 
ATOM   4730 C CD2    . LEU C 3 176 ? 35.616 24.433  -6.430  1.00 26.50 ? 176 LEU B CD2    1 
ATOM   4731 N N      . ARG C 3 177 ? 32.474 24.315  -9.207  1.00 17.73 ? 177 ARG B N      1 
ATOM   4732 C CA     . ARG C 3 177 ? 31.773 25.039  -10.272 1.00 16.95 ? 177 ARG B CA     1 
ATOM   4733 C C      . ARG C 3 177 ? 32.480 26.313  -10.635 1.00 19.03 ? 177 ARG B C      1 
ATOM   4734 O O      . ARG C 3 177 ? 32.794 27.119  -9.783  1.00 16.60 ? 177 ARG B O      1 
ATOM   4735 C CB     . ARG C 3 177 ? 30.327 25.326  -9.887  1.00 18.80 ? 177 ARG B CB     1 
ATOM   4736 C CG     . ARG C 3 177 ? 29.616 26.364  -10.717 1.00 20.06 ? 177 ARG B CG     1 
ATOM   4737 C CD     . ARG C 3 177 ? 28.150 26.437  -10.360 1.00 25.97 ? 177 ARG B CD     1 
ATOM   4738 N NE     . ARG C 3 177 ? 27.526 27.602  -10.965 1.00 30.37 ? 177 ARG B NE     1 
ATOM   4739 C CZ     . ARG C 3 177 ? 26.362 28.106  -10.588 1.00 36.55 ? 177 ARG B CZ     1 
ATOM   4740 N NH1    . ARG C 3 177 ? 25.688 27.548  -9.602  1.00 44.98 ? 177 ARG B NH1    1 
ATOM   4741 N NH2    . ARG C 3 177 ? 25.877 29.173  -11.191 1.00 28.78 ? 177 ARG B NH2    1 
ATOM   4742 N N      . LEU C 3 178 ? 32.749 26.471  -11.914 1.00 21.29 ? 178 LEU B N      1 
ATOM   4743 C CA     . LEU C 3 178 ? 33.428 27.641  -12.405 1.00 21.15 ? 178 LEU B CA     1 
ATOM   4744 C C      . LEU C 3 178 ? 32.457 28.410  -13.236 1.00 25.66 ? 178 LEU B C      1 
ATOM   4745 O O      . LEU C 3 178 ? 31.826 27.878  -14.117 1.00 24.75 ? 178 LEU B O      1 
ATOM   4746 C CB     . LEU C 3 178 ? 34.638 27.221  -13.231 1.00 20.27 ? 178 LEU B CB     1 
ATOM   4747 C CG     . LEU C 3 178 ? 35.666 28.277  -13.623 1.00 29.54 ? 178 LEU B CG     1 
ATOM   4748 C CD1    . LEU C 3 178 ? 36.007 29.163  -12.441 1.00 22.38 ? 178 LEU B CD1    1 
ATOM   4749 C CD2    . LEU C 3 178 ? 36.910 27.597  -14.158 1.00 19.43 ? 178 LEU B CD2    1 
ATOM   4750 N N      . ASP C 3 179 ? 32.310 29.682  -12.930 1.00 27.91 ? 179 ASP B N      1 
ATOM   4751 C CA     . ASP C 3 179 ? 31.329 30.486  -13.646 1.00 31.11 ? 179 ASP B CA     1 
ATOM   4752 C C      . ASP C 3 179 ? 31.972 31.235  -14.775 1.00 28.83 ? 179 ASP B C      1 
ATOM   4753 O O      . ASP C 3 179 ? 31.850 32.441  -14.881 1.00 29.73 ? 179 ASP B O      1 
ATOM   4754 C CB     . ASP C 3 179 ? 30.432 31.274  -12.704 1.00 36.06 ? 179 ASP B CB     1 
ATOM   4755 C CG     . ASP C 3 179 ? 29.302 30.445  -12.181 1.00 36.85 ? 179 ASP B CG     1 
ATOM   4756 O OD1    . ASP C 3 179 ? 28.348 30.199  -12.938 1.00 30.05 ? 179 ASP B OD1    1 
ATOM   4757 O OD2    . ASP C 3 179 ? 29.381 30.016  -11.016 1.00 47.82 ? 179 ASP B OD2    1 
ATOM   4758 N N      . LEU C 3 180 ? 32.648 30.495  -15.612 1.00 21.56 ? 180 LEU B N      1 
ATOM   4759 C CA     . LEU C 3 180 ? 33.331 30.986  -16.792 1.00 21.26 ? 180 LEU B CA     1 
ATOM   4760 C C      . LEU C 3 180 ? 33.220 29.888  -17.842 1.00 20.67 ? 180 LEU B C      1 
ATOM   4761 O O      . LEU C 3 180 ? 33.768 28.794  -17.664 1.00 16.11 ? 180 LEU B O      1 
ATOM   4762 C CB     . LEU C 3 180 ? 34.788 31.319  -16.454 1.00 26.18 ? 180 LEU B CB     1 
ATOM   4763 C CG     . LEU C 3 180 ? 35.677 31.977  -17.511 1.00 24.76 ? 180 LEU B CG     1 
ATOM   4764 C CD1    . LEU C 3 180 ? 36.862 32.627  -16.845 1.00 25.18 ? 180 LEU B CD1    1 
ATOM   4765 C CD2    . LEU C 3 180 ? 36.155 30.965  -18.523 1.00 20.73 ? 180 LEU B CD2    1 
ATOM   4766 N N      . ALA C 3 181 ? 32.491 30.157  -18.917 1.00 21.54 ? 181 ALA B N      1 
ATOM   4767 C CA     . ALA C 3 181 ? 32.290 29.111  -19.905 1.00 19.09 ? 181 ALA B CA     1 
ATOM   4768 C C      . ALA C 3 181 ? 32.244 29.742  -21.301 1.00 18.89 ? 181 ALA B C      1 
ATOM   4769 O O      . ALA C 3 181 ? 32.730 30.858  -21.508 1.00 19.84 ? 181 ALA B O      1 
ATOM   4770 C CB     . ALA C 3 181 ? 31.037 28.301  -19.539 1.00 18.97 ? 181 ALA B CB     1 
ATOM   4771 N N      . GLY C 3 182 ? 31.640 29.027  -22.256 1.00 15.45 ? 182 GLY B N      1 
ATOM   4772 C CA     . GLY C 3 182 ? 31.718 29.425  -23.661 1.00 17.35 ? 182 GLY B CA     1 
ATOM   4773 C C      . GLY C 3 182 ? 31.291 30.856  -23.947 1.00 18.55 ? 182 GLY B C      1 
ATOM   4774 O O      . GLY C 3 182 ? 31.920 31.552  -24.747 1.00 22.50 ? 182 GLY B O      1 
ATOM   4775 N N      . ARG C 3 183 ? 30.209 31.313  -23.321 1.00 18.45 ? 183 ARG B N      1 
ATOM   4776 C CA     . ARG C 3 183 ? 29.691 32.650  -23.585 1.00 19.94 ? 183 ARG B CA     1 
ATOM   4777 C C      . ARG C 3 183 ? 30.528 33.763  -22.955 1.00 18.76 ? 183 ARG B C      1 
ATOM   4778 O O      . ARG C 3 183 ? 30.485 34.892  -23.445 1.00 22.19 ? 183 ARG B O      1 
ATOM   4779 C CB     . ARG C 3 183 ? 28.237 32.738  -23.114 1.00 22.89 ? 183 ARG B CB     1 
ATOM   4780 C CG     . ARG C 3 183 ? 27.270 31.885  -23.967 1.00 29.67 ? 183 ARG B CG     1 
ATOM   4781 C CD     . ARG C 3 183 ? 25.978 31.490  -23.232 1.00 28.88 ? 183 ARG B CD     1 
ATOM   4782 N NE     . ARG C 3 183 ? 25.841 32.215  -21.974 1.00 41.60 ? 183 ARG B NE     1 
ATOM   4783 C CZ     . ARG C 3 183 ? 25.273 31.730  -20.875 1.00 42.16 ? 183 ARG B CZ     1 
ATOM   4784 N NH1    . ARG C 3 183 ? 24.763 30.500  -20.838 1.00 25.79 ? 183 ARG B NH1    1 
ATOM   4785 N NH2    . ARG C 3 183 ? 25.226 32.494  -19.782 1.00 39.65 ? 183 ARG B NH2    1 
ATOM   4786 N N      . ASP C 3 184 ? 31.363 33.467  -22.009 1.00 21.23 ? 184 ASP B N      1 
ATOM   4787 C CA     . ASP C 3 184 ? 32.247 34.469  -21.471 1.00 23.23 ? 184 ASP B CA     1 
ATOM   4788 C C      . ASP C 3 184 ? 33.419 34.615  -22.412 1.00 22.62 ? 184 ASP B C      1 
ATOM   4789 O O      . ASP C 3 184 ? 34.061 35.652  -22.453 1.00 22.94 ? 184 ASP B O      1 
ATOM   4790 C CB     . ASP C 3 184 ? 32.700 34.054  -20.080 1.00 24.58 ? 184 ASP B CB     1 
ATOM   4791 C CG     . ASP C 3 184 ? 31.558 33.725  -19.157 1.00 31.03 ? 184 ASP B CG     1 
ATOM   4792 O OD1    . ASP C 3 184 ? 31.145 34.610  -18.393 1.00 35.03 ? 184 ASP B OD1    1 
ATOM   4793 O OD2    . ASP C 3 184 ? 31.082 32.578  -19.168 1.00 26.32 ? 184 ASP B OD2    1 
ATOM   4794 N N      . LEU C 3 185 ? 33.671 33.594  -23.211 1.00 19.71 ? 185 LEU B N      1 
ATOM   4795 C CA     . LEU C 3 185 ? 34.784 33.591  -24.137 1.00 20.69 ? 185 LEU B CA     1 
ATOM   4796 C C      . LEU C 3 185 ? 34.441 34.263  -25.440 1.00 21.66 ? 185 LEU B C      1 
ATOM   4797 O O      . LEU C 3 185 ? 35.253 34.927  -26.036 1.00 22.36 ? 185 LEU B O      1 
ATOM   4798 C CB     . LEU C 3 185 ? 35.177 32.142  -24.359 1.00 18.01 ? 185 LEU B CB     1 
ATOM   4799 C CG     . LEU C 3 185 ? 36.483 31.580  -23.812 1.00 19.47 ? 185 LEU B CG     1 
ATOM   4800 C CD1    . LEU C 3 185 ? 36.685 31.911  -22.348 1.00 20.14 ? 185 LEU B CD1    1 
ATOM   4801 C CD2    . LEU C 3 185 ? 36.509 30.086  -24.024 1.00 13.04 ? 185 LEU B CD2    1 
ATOM   4802 N N      . THR C 3 186 ? 33.209 34.136  -25.865 1.00 24.70 ? 186 THR B N      1 
ATOM   4803 C CA     . THR C 3 186 ? 32.750 34.769  -27.069 1.00 24.14 ? 186 THR B CA     1 
ATOM   4804 C C      . THR C 3 186 ? 32.672 36.285  -26.860 1.00 28.77 ? 186 THR B C      1 
ATOM   4805 O O      . THR C 3 186 ? 32.885 37.056  -27.774 1.00 29.93 ? 186 THR B O      1 
ATOM   4806 C CB     . THR C 3 186 ? 31.429 34.104  -27.502 1.00 20.70 ? 186 THR B CB     1 
ATOM   4807 O OG1    . THR C 3 186 ? 31.672 33.235  -28.601 1.00 23.41 ? 186 THR B OG1    1 
ATOM   4808 C CG2    . THR C 3 186 ? 30.377 35.110  -27.898 1.00 26.81 ? 186 THR B CG2    1 
ATOM   4809 N N      . ASP C 3 187 ? 32.471 36.724  -25.638 1.00 21.14 ? 187 ASP B N      1 
ATOM   4810 C CA     . ASP C 3 187 ? 32.440 38.120  -25.369 1.00 23.48 ? 187 ASP B CA     1 
ATOM   4811 C C      . ASP C 3 187 ? 33.826 38.741  -25.311 1.00 27.83 ? 187 ASP B C      1 
ATOM   4812 O O      . ASP C 3 187 ? 34.002 39.880  -25.683 1.00 31.20 ? 187 ASP B O      1 
ATOM   4813 C CB     . ASP C 3 187 ? 31.672 38.366  -24.085 1.00 21.06 ? 187 ASP B CB     1 
ATOM   4814 C CG     . ASP C 3 187 ? 30.190 38.250  -24.264 1.00 43.20 ? 187 ASP B CG     1 
ATOM   4815 O OD1    . ASP C 3 187 ? 29.718 38.380  -25.404 1.00 52.02 ? 187 ASP B OD1    1 
ATOM   4816 O OD2    . ASP C 3 187 ? 29.491 38.030  -23.259 1.00 48.68 ? 187 ASP B OD2    1 
ATOM   4817 N N      . TYR C 3 188 ? 34.812 38.016  -24.827 1.00 26.85 ? 188 TYR B N      1 
ATOM   4818 C CA     . TYR C 3 188 ? 36.169 38.509  -24.819 1.00 21.25 ? 188 TYR B CA     1 
ATOM   4819 C C      . TYR C 3 188 ? 36.694 38.617  -26.236 1.00 24.56 ? 188 TYR B C      1 
ATOM   4820 O O      . TYR C 3 188 ? 37.368 39.564  -26.561 1.00 16.80 ? 188 TYR B O      1 
ATOM   4821 C CB     . TYR C 3 188 ? 37.037 37.580  -23.987 1.00 16.77 ? 188 TYR B CB     1 
ATOM   4822 C CG     . TYR C 3 188 ? 38.481 37.966  -23.840 1.00 14.68 ? 188 TYR B CG     1 
ATOM   4823 C CD1    . TYR C 3 188 ? 38.846 39.124  -23.188 1.00 13.42 ? 188 TYR B CD1    1 
ATOM   4824 C CD2    . TYR C 3 188 ? 39.481 37.147  -24.326 1.00 19.73 ? 188 TYR B CD2    1 
ATOM   4825 C CE1    . TYR C 3 188 ? 40.167 39.465  -23.042 1.00 18.20 ? 188 TYR B CE1    1 
ATOM   4826 C CE2    . TYR C 3 188 ? 40.802 37.484  -24.188 1.00 17.24 ? 188 TYR B CE2    1 
ATOM   4827 C CZ     . TYR C 3 188 ? 41.140 38.641  -23.546 1.00 17.97 ? 188 TYR B CZ     1 
ATOM   4828 O OH     . TYR C 3 188 ? 42.459 38.977  -23.416 1.00 18.60 ? 188 TYR B OH     1 
ATOM   4829 N N      . LEU C 3 189 ? 36.359 37.655  -27.084 1.00 24.34 ? 189 LEU B N      1 
ATOM   4830 C CA     . LEU C 3 189 ? 36.808 37.689  -28.439 1.00 21.17 ? 189 LEU B CA     1 
ATOM   4831 C C      . LEU C 3 189 ? 36.312 38.936  -29.086 1.00 24.45 ? 189 LEU B C      1 
ATOM   4832 O O      . LEU C 3 189 ? 37.027 39.565  -29.824 1.00 29.79 ? 189 LEU B O      1 
ATOM   4833 C CB     . LEU C 3 189 ? 36.396 36.438  -29.186 1.00 17.73 ? 189 LEU B CB     1 
ATOM   4834 C CG     . LEU C 3 189 ? 37.084 36.249  -30.537 1.00 28.78 ? 189 LEU B CG     1 
ATOM   4835 C CD1    . LEU C 3 189 ? 38.592 36.393  -30.455 1.00 16.26 ? 189 LEU B CD1    1 
ATOM   4836 C CD2    . LEU C 3 189 ? 36.693 34.949  -31.207 1.00 21.75 ? 189 LEU B CD2    1 
ATOM   4837 N N      . MET C 3 190 ? 35.099 39.321  -28.798 1.00 26.71 ? 190 MET B N      1 
ATOM   4838 C CA     . MET C 3 190 ? 34.552 40.552  -29.304 1.00 26.11 ? 190 MET B CA     1 
ATOM   4839 C C      . MET C 3 190 ? 35.361 41.744  -28.850 1.00 22.53 ? 190 MET B C      1 
ATOM   4840 O O      . MET C 3 190 ? 35.742 42.545  -29.651 1.00 24.56 ? 190 MET B O      1 
ATOM   4841 C CB     . MET C 3 190 ? 33.141 40.658  -28.763 1.00 28.27 ? 190 MET B CB     1 
ATOM   4842 C CG     . MET C 3 190 ? 32.055 40.058  -29.624 1.00 35.10 ? 190 MET B CG     1 
ATOM   4843 S SD     . MET C 3 190 ? 30.554 39.833  -28.671 1.00 38.44 ? 190 MET B SD     1 
ATOM   4844 C CE     . MET C 3 190 ? 30.229 41.502  -28.154 1.00 38.39 ? 190 MET B CE     1 
ATOM   4845 N N      . LYS C 3 191 ? 35.617 41.862  -27.566 1.00 21.94 ? 191 LYS B N      1 
ATOM   4846 C CA     . LYS C 3 191 ? 36.423 42.934  -27.018 1.00 21.44 ? 191 LYS B CA     1 
ATOM   4847 C C      . LYS C 3 191 ? 37.790 43.132  -27.625 1.00 22.43 ? 191 LYS B C      1 
ATOM   4848 O O      . LYS C 3 191 ? 38.192 44.233  -27.890 1.00 22.10 ? 191 LYS B O      1 
ATOM   4849 C CB     . LYS C 3 191 ? 36.563 42.671  -25.515 1.00 15.69 ? 191 LYS B CB     1 
ATOM   4850 C CG     . LYS C 3 191 ? 37.189 43.777  -24.699 1.00 22.16 ? 191 LYS B CG     1 
ATOM   4851 C CD     . LYS C 3 191 ? 38.283 43.216  -23.816 1.00 25.82 ? 191 LYS B CD     1 
ATOM   4852 C CE     . LYS C 3 191 ? 38.520 44.094  -22.604 1.00 26.03 ? 191 LYS B CE     1 
ATOM   4853 N NZ     . LYS C 3 191 ? 39.550 43.511  -21.706 1.00 31.52 ? 191 LYS B NZ     1 
ATOM   4854 N N      . ILE C 3 192 ? 38.492 42.056  -27.860 1.00 25.42 ? 192 ILE B N      1 
ATOM   4855 C CA     . ILE C 3 192 ? 39.834 42.116  -28.367 1.00 22.26 ? 192 ILE B CA     1 
ATOM   4856 C C      . ILE C 3 192 ? 39.893 42.297  -29.856 1.00 23.94 ? 192 ILE B C      1 
ATOM   4857 O O      . ILE C 3 192 ? 40.877 42.797  -30.364 1.00 26.72 ? 192 ILE B O      1 
ATOM   4858 C CB     . ILE C 3 192 ? 40.663 40.910  -27.846 1.00 20.83 ? 192 ILE B CB     1 
ATOM   4859 C CG1    . ILE C 3 192 ? 40.134 39.580  -28.363 1.00 17.74 ? 192 ILE B CG1    1 
ATOM   4860 C CG2    . ILE C 3 192 ? 40.738 40.947  -26.338 1.00 18.52 ? 192 ILE B CG2    1 
ATOM   4861 C CD1    . ILE C 3 192 ? 40.914 38.394  -27.860 1.00 22.30 ? 192 ILE B CD1    1 
ATOM   4862 N N      . LEU C 3 193 ? 38.853 41.903  -30.561 1.00 20.63 ? 193 LEU B N      1 
ATOM   4863 C CA     . LEU C 3 193 ? 38.799 42.167  -31.975 1.00 21.77 ? 193 LEU B CA     1 
ATOM   4864 C C      . LEU C 3 193 ? 38.364 43.604  -32.173 1.00 26.34 ? 193 LEU B C      1 
ATOM   4865 O O      . LEU C 3 193 ? 38.783 44.239  -33.115 1.00 33.22 ? 193 LEU B O      1 
ATOM   4866 C CB     . LEU C 3 193 ? 37.885 41.185  -32.688 1.00 20.49 ? 193 LEU B CB     1 
ATOM   4867 C CG     . LEU C 3 193 ? 38.423 39.802  -33.018 1.00 18.37 ? 193 LEU B CG     1 
ATOM   4868 C CD1    . LEU C 3 193 ? 37.323 38.970  -33.642 1.00 21.42 ? 193 LEU B CD1    1 
ATOM   4869 C CD2    . LEU C 3 193 ? 39.600 39.896  -33.962 1.00 21.34 ? 193 LEU B CD2    1 
ATOM   4870 N N      . THR C 3 194 ? 37.559 44.144  -31.278 1.00 26.68 ? 194 THR B N      1 
ATOM   4871 C CA     . THR C 3 194 ? 37.162 45.540  -31.345 1.00 26.44 ? 194 THR B CA     1 
ATOM   4872 C C      . THR C 3 194 ? 38.346 46.420  -30.998 1.00 29.40 ? 194 THR B C      1 
ATOM   4873 O O      . THR C 3 194 ? 38.460 47.525  -31.482 1.00 33.57 ? 194 THR B O      1 
ATOM   4874 C CB     . THR C 3 194 ? 35.893 45.806  -30.501 1.00 23.94 ? 194 THR B CB     1 
ATOM   4875 O OG1    . THR C 3 194 ? 34.916 44.808  -30.783 1.00 31.69 ? 194 THR B OG1    1 
ATOM   4876 C CG2    . THR C 3 194 ? 35.294 47.141  -30.826 1.00 29.10 ? 194 THR B CG2    1 
ATOM   4877 N N      . GLU C 3 195 ? 39.275 45.909  -30.214 1.00 27.33 ? 195 GLU B N      1 
ATOM   4878 C CA     . GLU C 3 195 ? 40.469 46.643  -29.876 1.00 26.61 ? 195 GLU B CA     1 
ATOM   4879 C C      . GLU C 3 195 ? 41.452 46.678  -31.010 1.00 30.24 ? 195 GLU B C      1 
ATOM   4880 O O      . GLU C 3 195 ? 42.282 47.569  -31.076 1.00 37.04 ? 195 GLU B O      1 
ATOM   4881 C CB     . GLU C 3 195 ? 41.116 46.037  -28.663 1.00 26.73 ? 195 GLU B CB     1 
ATOM   4882 C CG     . GLU C 3 195 ? 40.699 46.675  -27.358 1.00 37.94 ? 195 GLU B CG     1 
ATOM   4883 C CD     . GLU C 3 195 ? 40.808 45.730  -26.184 1.00 44.02 ? 195 GLU B CD     1 
ATOM   4884 O OE1    . GLU C 3 195 ? 41.461 44.683  -26.314 1.00 52.91 ? 195 GLU B OE1    1 
ATOM   4885 O OE2    . GLU C 3 195 ? 40.249 46.041  -25.121 1.00 42.86 ? 195 GLU B OE2    1 
ATOM   4886 N N      . ARG C 3 196 ? 41.381 45.722  -31.909 1.00 24.24 ? 196 ARG B N      1 
ATOM   4887 C CA     . ARG C 3 196 ? 42.222 45.760  -33.060 1.00 26.20 ? 196 ARG B CA     1 
ATOM   4888 C C      . ARG C 3 196 ? 41.651 46.787  -33.987 1.00 36.17 ? 196 ARG B C      1 
ATOM   4889 O O      . ARG C 3 196 ? 42.379 47.582  -34.564 1.00 37.98 ? 196 ARG B O      1 
ATOM   4890 C CB     . ARG C 3 196 ? 42.269 44.401  -33.728 1.00 29.62 ? 196 ARG B CB     1 
ATOM   4891 C CG     . ARG C 3 196 ? 43.109 44.335  -34.986 1.00 34.07 ? 196 ARG B CG     1 
ATOM   4892 C CD     . ARG C 3 196 ? 44.175 43.267  -34.887 1.00 40.56 ? 196 ARG B CD     1 
ATOM   4893 N NE     . ARG C 3 196 ? 44.685 43.130  -33.529 1.00 40.14 ? 196 ARG B NE     1 
ATOM   4894 C CZ     . ARG C 3 196 ? 45.966 42.962  -33.228 1.00 42.35 ? 196 ARG B CZ     1 
ATOM   4895 N NH1    . ARG C 3 196 ? 46.872 42.919  -34.188 1.00 53.77 ? 196 ARG B NH1    1 
ATOM   4896 N NH2    . ARG C 3 196 ? 46.339 42.836  -31.966 1.00 38.04 ? 196 ARG B NH2    1 
ATOM   4897 N N      . GLY C 3 197 ? 40.340 46.788  -34.137 1.00 37.74 ? 197 GLY B N      1 
ATOM   4898 C CA     . GLY C 3 197 ? 39.697 47.756  -34.989 1.00 29.17 ? 197 GLY B CA     1 
ATOM   4899 C C      . GLY C 3 197 ? 38.494 47.270  -35.739 1.00 33.57 ? 197 GLY B C      1 
ATOM   4900 O O      . GLY C 3 197 ? 37.860 48.036  -36.447 1.00 35.14 ? 197 GLY B O      1 
ATOM   4901 N N      . TYR C 3 198 ? 38.175 46.000  -35.612 1.00 30.85 ? 198 TYR B N      1 
ATOM   4902 C CA     . TYR C 3 198 ? 36.971 45.504  -36.236 1.00 32.51 ? 198 TYR B CA     1 
ATOM   4903 C C      . TYR C 3 198 ? 35.861 45.529  -35.210 1.00 27.70 ? 198 TYR B C      1 
ATOM   4904 O O      . TYR C 3 198 ? 35.998 44.962  -34.163 1.00 41.27 ? 198 TYR B O      1 
ATOM   4905 C CB     . TYR C 3 198 ? 37.164 44.098  -36.787 1.00 33.68 ? 198 TYR B CB     1 
ATOM   4906 C CG     . TYR C 3 198 ? 38.498 43.758  -37.382 1.00 32.62 ? 198 TYR B CG     1 
ATOM   4907 C CD1    . TYR C 3 198 ? 38.832 44.166  -38.654 1.00 31.05 ? 198 TYR B CD1    1 
ATOM   4908 C CD2    . TYR C 3 198 ? 39.395 42.968  -36.694 1.00 38.18 ? 198 TYR B CD2    1 
ATOM   4909 C CE1    . TYR C 3 198 ? 40.046 43.830  -39.213 1.00 39.99 ? 198 TYR B CE1    1 
ATOM   4910 C CE2    . TYR C 3 198 ? 40.608 42.625  -37.242 1.00 41.41 ? 198 TYR B CE2    1 
ATOM   4911 C CZ     . TYR C 3 198 ? 40.929 43.061  -38.502 1.00 43.02 ? 198 TYR B CZ     1 
ATOM   4912 O OH     . TYR C 3 198 ? 42.139 42.727  -39.054 1.00 38.60 ? 198 TYR B OH     1 
ATOM   4913 N N      . SER C 3 199 ? 34.742 46.154  -35.512 1.00 26.17 ? 199 SER B N      1 
ATOM   4914 C CA     . SER C 3 199 ? 33.696 46.314  -34.511 1.00 36.84 ? 199 SER B CA     1 
ATOM   4915 C C      . SER C 3 199 ? 32.619 45.250  -34.370 1.00 37.53 ? 199 SER B C      1 
ATOM   4916 O O      . SER C 3 199 ? 31.855 45.015  -35.293 1.00 32.09 ? 199 SER B O      1 
ATOM   4917 C CB     . SER C 3 199 ? 33.104 47.727  -34.553 1.00 40.33 ? 199 SER B CB     1 
ATOM   4918 O OG     . SER C 3 199 ? 32.568 48.119  -33.304 1.00 40.19 ? 199 SER B OG     1 
ATOM   4919 N N      . PHE C 3 200 ? 32.582 44.601  -33.215 1.00 32.50 ? 200 PHE B N      1 
ATOM   4920 C CA     . PHE C 3 200 ? 31.597 43.564  -32.900 1.00 33.48 ? 200 PHE B CA     1 
ATOM   4921 C C      . PHE C 3 200 ? 30.957 43.935  -31.565 1.00 37.70 ? 200 PHE B C      1 
ATOM   4922 O O      . PHE C 3 200 ? 31.565 43.780  -30.501 1.00 27.03 ? 200 PHE B O      1 
ATOM   4923 C CB     . PHE C 3 200 ? 32.233 42.182  -32.839 1.00 31.46 ? 200 PHE B CB     1 
ATOM   4924 C CG     . PHE C 3 200 ? 32.832 41.742  -34.126 1.00 27.11 ? 200 PHE B CG     1 
ATOM   4925 C CD1    . PHE C 3 200 ? 32.059 41.112  -35.079 1.00 26.95 ? 200 PHE B CD1    1 
ATOM   4926 C CD2    . PHE C 3 200 ? 34.171 41.968  -34.388 1.00 28.56 ? 200 PHE B CD2    1 
ATOM   4927 C CE1    . PHE C 3 200 ? 32.613 40.700  -36.277 1.00 36.50 ? 200 PHE B CE1    1 
ATOM   4928 C CE2    . PHE C 3 200 ? 34.741 41.563  -35.581 1.00 29.72 ? 200 PHE B CE2    1 
ATOM   4929 C CZ     . PHE C 3 200 ? 33.960 40.923  -36.529 1.00 34.47 ? 200 PHE B CZ     1 
ATOM   4930 N N      . THR C 3 201 ? 29.730 44.435  -31.622 1.00 41.87 ? 201 THR B N      1 
ATOM   4931 C CA     . THR C 3 201 ? 29.091 44.972  -30.426 1.00 37.99 ? 201 THR B CA     1 
ATOM   4932 C C      . THR C 3 201 ? 27.586 44.726  -30.357 1.00 39.42 ? 201 THR B C      1 
ATOM   4933 O O      . THR C 3 201 ? 27.040 44.717  -29.248 1.00 41.25 ? 201 THR B O      1 
ATOM   4934 C CB     . THR C 3 201 ? 29.386 46.481  -30.315 1.00 45.73 ? 201 THR B CB     1 
ATOM   4935 O OG1    . THR C 3 201 ? 28.782 47.035  -29.135 1.00 49.34 ? 201 THR B OG1    1 
ATOM   4936 C CG2    . THR C 3 201 ? 28.920 47.226  -31.571 1.00 41.89 ? 201 THR B CG2    1 
ATOM   4937 N N      . THR C 3 202 ? 26.907 44.484  -31.480 1.00 38.36 ? 202 THR B N      1 
ATOM   4938 C CA     . THR C 3 202 ? 25.483 44.182  -31.546 1.00 36.85 ? 202 THR B CA     1 
ATOM   4939 C C      . THR C 3 202 ? 25.251 42.682  -31.416 1.00 39.55 ? 202 THR B C      1 
ATOM   4940 O O      . THR C 3 202 ? 26.115 41.867  -31.744 1.00 43.12 ? 202 THR B O      1 
ATOM   4941 C CB     . THR C 3 202 ? 24.882 44.677  -32.870 1.00 41.98 ? 202 THR B CB     1 
ATOM   4942 O OG1    . THR C 3 202 ? 25.118 43.717  -33.917 1.00 40.79 ? 202 THR B OG1    1 
ATOM   4943 C CG2    . THR C 3 202 ? 25.502 46.002  -33.261 1.00 42.52 ? 202 THR B CG2    1 
ATOM   4944 N N      . THR C 3 203 ? 24.043 42.325  -30.971 1.00 40.52 ? 203 THR B N      1 
ATOM   4945 C CA     . THR C 3 203 ? 23.690 40.921  -30.771 1.00 38.18 ? 203 THR B CA     1 
ATOM   4946 C C      . THR C 3 203 ? 23.931 40.084  -32.025 1.00 38.70 ? 203 THR B C      1 
ATOM   4947 O O      . THR C 3 203 ? 24.411 38.945  -31.942 1.00 31.91 ? 203 THR B O      1 
ATOM   4948 C CB     . THR C 3 203 ? 22.234 40.831  -30.318 1.00 33.39 ? 203 THR B CB     1 
ATOM   4949 O OG1    . THR C 3 203 ? 22.146 41.354  -28.989 1.00 32.61 ? 203 THR B OG1    1 
ATOM   4950 C CG2    . THR C 3 203 ? 21.721 39.383  -30.366 1.00 35.32 ? 203 THR B CG2    1 
ATOM   4951 N N      . ALA C 3 204 ? 23.596 40.627  -33.199 1.00 38.54 ? 204 ALA B N      1 
ATOM   4952 C CA     . ALA C 3 204 ? 23.938 39.943  -34.439 1.00 40.29 ? 204 ALA B CA     1 
ATOM   4953 C C      . ALA C 3 204 ? 25.449 39.874  -34.656 1.00 43.33 ? 204 ALA B C      1 
ATOM   4954 O O      . ALA C 3 204 ? 25.931 38.986  -35.385 1.00 31.74 ? 204 ALA B O      1 
ATOM   4955 C CB     . ALA C 3 204 ? 23.270 40.642  -35.619 1.00 32.10 ? 204 ALA B CB     1 
ATOM   4956 N N      . GLU C 3 205 ? 26.253 40.699  -34.007 1.00 35.88 ? 205 GLU B N      1 
ATOM   4957 C CA     . GLU C 3 205 ? 27.695 40.626  -34.154 1.00 31.63 ? 205 GLU B CA     1 
ATOM   4958 C C      . GLU C 3 205 ? 28.319 39.642  -33.218 1.00 30.28 ? 205 GLU B C      1 
ATOM   4959 O O      . GLU C 3 205 ? 29.410 39.169  -33.460 1.00 37.19 ? 205 GLU B O      1 
ATOM   4960 C CB     . GLU C 3 205 ? 28.315 42.001  -34.001 1.00 35.46 ? 205 GLU B CB     1 
ATOM   4961 C CG     . GLU C 3 205 ? 28.555 42.707  -35.320 1.00 44.13 ? 205 GLU B CG     1 
ATOM   4962 C CD     . GLU C 3 205 ? 28.600 44.214  -35.190 1.00 45.18 ? 205 GLU B CD     1 
ATOM   4963 O OE1    . GLU C 3 205 ? 28.518 44.714  -34.065 1.00 36.72 ? 205 GLU B OE1    1 
ATOM   4964 O OE2    . GLU C 3 205 ? 28.721 44.903  -36.217 1.00 49.62 ? 205 GLU B OE2    1 
ATOM   4965 N N      . ARG C 3 206 ? 27.617 39.286  -32.167 1.00 33.06 ? 206 ARG B N      1 
ATOM   4966 C CA     . ARG C 3 206 ? 28.093 38.297  -31.226 1.00 34.51 ? 206 ARG B CA     1 
ATOM   4967 C C      . ARG C 3 206 ? 28.051 36.982  -31.903 1.00 33.04 ? 206 ARG B C      1 
ATOM   4968 O O      . ARG C 3 206 ? 28.983 36.213  -31.818 1.00 43.23 ? 206 ARG B O      1 
ATOM   4969 C CB     . ARG C 3 206 ? 27.203 38.284  -29.997 1.00 28.21 ? 206 ARG B CB     1 
ATOM   4970 C CG     . ARG C 3 206 ? 27.534 37.274  -28.929 1.00 30.69 ? 206 ARG B CG     1 
ATOM   4971 C CD     . ARG C 3 206 ? 26.724 37.558  -27.683 1.00 26.32 ? 206 ARG B CD     1 
ATOM   4972 N NE     . ARG C 3 206 ? 27.324 38.623  -26.896 1.00 37.65 ? 206 ARG B NE     1 
ATOM   4973 C CZ     . ARG C 3 206 ? 26.832 39.852  -26.780 1.00 48.07 ? 206 ARG B CZ     1 
ATOM   4974 N NH1    . ARG C 3 206 ? 25.713 40.194  -27.400 1.00 38.56 ? 206 ARG B NH1    1 
ATOM   4975 N NH2    . ARG C 3 206 ? 27.470 40.741  -26.040 1.00 48.06 ? 206 ARG B NH2    1 
ATOM   4976 N N      . GLU C 3 207 ? 26.989 36.715  -32.612 1.00 28.43 ? 207 GLU B N      1 
ATOM   4977 C CA     . GLU C 3 207 ? 26.863 35.491  -33.320 1.00 29.38 ? 207 GLU B CA     1 
ATOM   4978 C C      . GLU C 3 207 ? 27.894 35.255  -34.386 1.00 26.83 ? 207 GLU B C      1 
ATOM   4979 O O      . GLU C 3 207 ? 28.124 34.125  -34.781 1.00 27.68 ? 207 GLU B O      1 
ATOM   4980 C CB     . GLU C 3 207 ? 25.475 35.462  -33.915 1.00 36.76 ? 207 GLU B CB     1 
ATOM   4981 C CG     . GLU C 3 207 ? 24.391 34.949  -32.969 1.00 52.00 ? 207 GLU B CG     1 
ATOM   4982 C CD     . GLU C 3 207 ? 24.727 33.616  -32.305 1.00 59.14 ? 207 GLU B CD     1 
ATOM   4983 O OE1    . GLU C 3 207 ? 24.895 32.597  -33.009 1.00 57.58 ? 207 GLU B OE1    1 
ATOM   4984 O OE2    . GLU C 3 207 ? 24.803 33.578  -31.062 1.00 44.25 ? 207 GLU B OE2    1 
ATOM   4985 N N      . ILE C 3 208 ? 28.523 36.310  -34.863 1.00 29.69 ? 208 ILE B N      1 
ATOM   4986 C CA     . ILE C 3 208 ? 29.549 36.193  -35.866 1.00 32.42 ? 208 ILE B CA     1 
ATOM   4987 C C      . ILE C 3 208 ? 30.815 35.769  -35.174 1.00 30.52 ? 208 ILE B C      1 
ATOM   4988 O O      . ILE C 3 208 ? 31.506 34.895  -35.636 1.00 21.06 ? 208 ILE B O      1 
ATOM   4989 C CB     . ILE C 3 208 ? 29.735 37.544  -36.589 1.00 27.60 ? 208 ILE B CB     1 
ATOM   4990 C CG1    . ILE C 3 208 ? 28.455 37.967  -37.288 1.00 31.60 ? 208 ILE B CG1    1 
ATOM   4991 C CG2    . ILE C 3 208 ? 30.859 37.493  -37.608 1.00 27.82 ? 208 ILE B CG2    1 
ATOM   4992 C CD1    . ILE C 3 208 ? 28.536 39.341  -37.909 1.00 29.50 ? 208 ILE B CD1    1 
ATOM   4993 N N      . VAL C 3 209 ? 31.064 36.348  -34.022 1.00 23.11 ? 209 VAL B N      1 
ATOM   4994 C CA     . VAL C 3 209 ? 32.266 36.063  -33.300 1.00 26.64 ? 209 VAL B CA     1 
ATOM   4995 C C      . VAL C 3 209 ? 32.230 34.665  -32.749 1.00 27.09 ? 209 VAL B C      1 
ATOM   4996 O O      . VAL C 3 209 ? 33.254 34.024  -32.632 1.00 23.56 ? 209 VAL B O      1 
ATOM   4997 C CB     . VAL C 3 209 ? 32.507 37.188  -32.267 1.00 37.02 ? 209 VAL B CB     1 
ATOM   4998 C CG1    . VAL C 3 209 ? 33.154 36.690  -30.998 1.00 29.34 ? 209 VAL B CG1    1 
ATOM   4999 C CG2    . VAL C 3 209 ? 33.353 38.274  -32.879 1.00 41.95 ? 209 VAL B CG2    1 
ATOM   5000 N N      . ARG C 3 210 ? 31.042 34.166  -32.476 1.00 28.63 ? 210 ARG B N      1 
ATOM   5001 C CA     . ARG C 3 210 ? 30.884 32.797  -32.020 1.00 29.73 ? 210 ARG B CA     1 
ATOM   5002 C C      . ARG C 3 210 ? 31.278 31.811  -33.091 1.00 26.16 ? 210 ARG B C      1 
ATOM   5003 O O      . ARG C 3 210 ? 31.720 30.725  -32.774 1.00 28.93 ? 210 ARG B O      1 
ATOM   5004 C CB     . ARG C 3 210 ? 29.452 32.560  -31.587 1.00 31.65 ? 210 ARG B CB     1 
ATOM   5005 C CG     . ARG C 3 210 ? 29.305 31.591  -30.434 1.00 33.75 ? 210 ARG B CG     1 
ATOM   5006 C CD     . ARG C 3 210 ? 28.006 30.823  -30.519 1.00 37.30 ? 210 ARG B CD     1 
ATOM   5007 N NE     . ARG C 3 210 ? 28.025 29.877  -31.624 1.00 44.58 ? 210 ARG B NE     1 
ATOM   5008 C CZ     . ARG C 3 210 ? 27.090 28.960  -31.832 1.00 58.58 ? 210 ARG B CZ     1 
ATOM   5009 N NH1    . ARG C 3 210 ? 26.064 28.863  -31.004 1.00 66.79 ? 210 ARG B NH1    1 
ATOM   5010 N NH2    . ARG C 3 210 ? 27.182 28.132  -32.861 1.00 58.71 ? 210 ARG B NH2    1 
ATOM   5011 N N      . ASP C 3 211 ? 31.133 32.174  -34.352 1.00 22.58 ? 211 ASP B N      1 
ATOM   5012 C CA     . ASP C 3 211 ? 31.593 31.328  -35.445 1.00 28.77 ? 211 ASP B CA     1 
ATOM   5013 C C      . ASP C 3 211 ? 33.092 31.378  -35.667 1.00 30.22 ? 211 ASP B C      1 
ATOM   5014 O O      . ASP C 3 211 ? 33.700 30.361  -35.884 1.00 27.04 ? 211 ASP B O      1 
ATOM   5015 C CB     . ASP C 3 211 ? 30.855 31.694  -36.721 1.00 21.50 ? 211 ASP B CB     1 
ATOM   5016 C CG     . ASP C 3 211 ? 30.633 30.547  -37.606 1.00 32.84 ? 211 ASP B CG     1 
ATOM   5017 O OD1    . ASP C 3 211 ? 30.206 29.496  -37.114 1.00 38.73 ? 211 ASP B OD1    1 
ATOM   5018 O OD2    . ASP C 3 211 ? 30.875 30.705  -38.808 1.00 42.17 ? 211 ASP B OD2    1 
ATOM   5019 N N      . ILE C 3 212 ? 33.688 32.553  -35.607 1.00 26.40 ? 212 ILE B N      1 
ATOM   5020 C CA     . ILE C 3 212 ? 35.108 32.691  -35.745 1.00 22.65 ? 212 ILE B CA     1 
ATOM   5021 C C      . ILE C 3 212 ? 35.810 31.940  -34.610 1.00 28.84 ? 212 ILE B C      1 
ATOM   5022 O O      . ILE C 3 212 ? 36.861 31.391  -34.812 1.00 31.75 ? 212 ILE B O      1 
ATOM   5023 C CB     . ILE C 3 212 ? 35.495 34.180  -35.714 1.00 29.08 ? 212 ILE B CB     1 
ATOM   5024 C CG1    . ILE C 3 212 ? 34.514 35.041  -36.466 1.00 21.65 ? 212 ILE B CG1    1 
ATOM   5025 C CG2    . ILE C 3 212 ? 36.872 34.417  -36.285 1.00 29.34 ? 212 ILE B CG2    1 
ATOM   5026 C CD1    . ILE C 3 212 ? 34.822 36.516  -36.387 1.00 23.43 ? 212 ILE B CD1    1 
ATOM   5027 N N      . LYS C 3 213 ? 35.227 31.904  -33.424 1.00 27.55 ? 213 LYS B N      1 
ATOM   5028 C CA     . LYS C 3 213 ? 35.781 31.171  -32.297 1.00 20.61 ? 213 LYS B CA     1 
ATOM   5029 C C      . LYS C 3 213 ? 35.761 29.704  -32.513 1.00 20.70 ? 213 LYS B C      1 
ATOM   5030 O O      . LYS C 3 213 ? 36.730 29.018  -32.323 1.00 24.38 ? 213 LYS B O      1 
ATOM   5031 C CB     . LYS C 3 213 ? 34.981 31.494  -31.046 1.00 21.09 ? 213 LYS B CB     1 
ATOM   5032 C CG     . LYS C 3 213 ? 35.691 31.328  -29.726 1.00 23.91 ? 213 LYS B CG     1 
ATOM   5033 C CD     . LYS C 3 213 ? 34.687 31.380  -28.597 1.00 21.44 ? 213 LYS B CD     1 
ATOM   5034 C CE     . LYS C 3 213 ? 33.508 30.472  -28.894 1.00 28.07 ? 213 LYS B CE     1 
ATOM   5035 N NZ     . LYS C 3 213 ? 32.505 30.474  -27.799 1.00 16.28 ? 213 LYS B NZ     1 
ATOM   5036 N N      . GLU C 3 214 ? 34.638 29.208  -32.931 1.00 22.60 ? 214 GLU B N      1 
ATOM   5037 C CA     . GLU C 3 214 ? 34.505 27.813  -33.135 1.00 24.75 ? 214 GLU B CA     1 
ATOM   5038 C C      . GLU C 3 214 ? 35.270 27.292  -34.310 1.00 25.97 ? 214 GLU B C      1 
ATOM   5039 O O      . GLU C 3 214 ? 35.565 26.117  -34.376 1.00 28.83 ? 214 GLU B O      1 
ATOM   5040 C CB     . GLU C 3 214 ? 33.034 27.500  -33.281 1.00 30.18 ? 214 GLU B CB     1 
ATOM   5041 C CG     . GLU C 3 214 ? 32.313 27.327  -31.960 1.00 40.05 ? 214 GLU B CG     1 
ATOM   5042 C CD     . GLU C 3 214 ? 30.817 27.508  -32.080 1.00 43.07 ? 214 GLU B CD     1 
ATOM   5043 O OE1    . GLU C 3 214 ? 30.260 27.162  -33.135 1.00 42.74 ? 214 GLU B OE1    1 
ATOM   5044 O OE2    . GLU C 3 214 ? 30.200 27.995  -31.118 1.00 39.63 ? 214 GLU B OE2    1 
ATOM   5045 N N      . LYS C 3 215 ? 35.609 28.159  -35.232 1.00 26.91 ? 215 LYS B N      1 
ATOM   5046 C CA     . LYS C 3 215 ? 36.315 27.751  -36.409 1.00 28.29 ? 215 LYS B CA     1 
ATOM   5047 C C      . LYS C 3 215 ? 37.779 28.072  -36.439 1.00 25.12 ? 215 LYS B C      1 
ATOM   5048 O O      . LYS C 3 215 ? 38.522 27.404  -37.140 1.00 25.21 ? 215 LYS B O      1 
ATOM   5049 C CB     . LYS C 3 215 ? 35.671 28.404  -37.622 1.00 28.45 ? 215 LYS B CB     1 
ATOM   5050 C CG     . LYS C 3 215 ? 34.447 27.702  -38.161 1.00 32.52 ? 215 LYS B CG     1 
ATOM   5051 C CD     . LYS C 3 215 ? 33.704 28.618  -39.110 1.00 32.34 ? 215 LYS B CD     1 
ATOM   5052 C CE     . LYS C 3 215 ? 32.502 27.916  -39.707 1.00 33.71 ? 215 LYS B CE     1 
ATOM   5053 N NZ     . LYS C 3 215 ? 31.885 28.723  -40.792 1.00 26.97 ? 215 LYS B NZ     1 
ATOM   5054 N N      . LEU C 3 216 ? 38.218 29.096  -35.723 1.00 22.32 ? 216 LEU B N      1 
ATOM   5055 C CA     . LEU C 3 216 ? 39.615 29.530  -35.797 1.00 18.01 ? 216 LEU B CA     1 
ATOM   5056 C C      . LEU C 3 216 ? 40.394 29.642  -34.482 1.00 16.72 ? 216 LEU B C      1 
ATOM   5057 O O      . LEU C 3 216 ? 41.588 29.771  -34.515 1.00 16.07 ? 216 LEU B O      1 
ATOM   5058 C CB     . LEU C 3 216 ? 39.749 30.830  -36.615 1.00 20.51 ? 216 LEU B CB     1 
ATOM   5059 C CG     . LEU C 3 216 ? 39.218 30.942  -38.039 1.00 19.11 ? 216 LEU B CG     1 
ATOM   5060 C CD1    . LEU C 3 216 ? 39.216 32.383  -38.496 1.00 22.35 ? 216 LEU B CD1    1 
ATOM   5061 C CD2    . LEU C 3 216 ? 40.055 30.100  -38.975 1.00 16.84 ? 216 LEU B CD2    1 
ATOM   5062 N N      . CYS C 3 217 ? 39.748 29.531  -33.332 1.00 14.82 ? 217 CYS B N      1 
ATOM   5063 C CA     . CYS C 3 217 ? 40.503 29.575  -32.088 1.00 13.69 ? 217 CYS B CA     1 
ATOM   5064 C C      . CYS C 3 217 ? 41.096 28.216  -31.715 1.00 15.51 ? 217 CYS B C      1 
ATOM   5065 O O      . CYS C 3 217 ? 40.564 27.155  -32.062 1.00 17.10 ? 217 CYS B O      1 
ATOM   5066 C CB     . CYS C 3 217 ? 39.626 30.072  -30.950 1.00 18.03 ? 217 CYS B CB     1 
ATOM   5067 S SG     . CYS C 3 217 ? 39.016 31.703  -31.255 1.00 17.69 ? 217 CYS B SG     1 
ATOM   5068 N N      . TYR C 3 218 ? 42.230 28.267  -31.017 1.00 11.99 ? 218 TYR B N      1 
ATOM   5069 C CA     . TYR C 3 218 ? 42.898 27.078  -30.505 1.00 11.81 ? 218 TYR B CA     1 
ATOM   5070 C C      . TYR C 3 218 ? 43.577 27.447  -29.187 1.00 14.60 ? 218 TYR B C      1 
ATOM   5071 O O      . TYR C 3 218 ? 43.621 28.619  -28.801 1.00 15.36 ? 218 TYR B O      1 
ATOM   5072 C CB     . TYR C 3 218 ? 43.902 26.525  -31.517 1.00 10.02 ? 218 TYR B CB     1 
ATOM   5073 C CG     . TYR C 3 218 ? 45.083 27.440  -31.777 1.00 10.93 ? 218 TYR B CG     1 
ATOM   5074 C CD1    . TYR C 3 218 ? 44.948 28.552  -32.602 1.00 13.15 ? 218 TYR B CD1    1 
ATOM   5075 C CD2    . TYR C 3 218 ? 46.328 27.186  -31.225 1.00 10.58 ? 218 TYR B CD2    1 
ATOM   5076 C CE1    . TYR C 3 218 ? 46.018 29.401  -32.870 1.00 13.59 ? 218 TYR B CE1    1 
ATOM   5077 C CE2    . TYR C 3 218 ? 47.403 28.019  -31.490 1.00 13.87 ? 218 TYR B CE2    1 
ATOM   5078 C CZ     . TYR C 3 218 ? 47.238 29.130  -32.311 1.00 12.26 ? 218 TYR B CZ     1 
ATOM   5079 O OH     . TYR C 3 218 ? 48.284 29.976  -32.579 1.00 8.80  ? 218 TYR B OH     1 
ATOM   5080 N N      . VAL C 3 219 ? 44.101 26.439  -28.488 1.00 11.07 ? 219 VAL B N      1 
ATOM   5081 C CA     . VAL C 3 219 ? 44.807 26.648  -27.227 1.00 12.28 ? 219 VAL B CA     1 
ATOM   5082 C C      . VAL C 3 219 ? 46.305 26.524  -27.468 1.00 10.35 ? 219 VAL B C      1 
ATOM   5083 O O      . VAL C 3 219 ? 46.793 25.447  -27.823 1.00 13.68 ? 219 VAL B O      1 
ATOM   5084 C CB     . VAL C 3 219 ? 44.354 25.638  -26.159 1.00 12.20 ? 219 VAL B CB     1 
ATOM   5085 C CG1    . VAL C 3 219 ? 45.240 25.755  -24.952 1.00 8.89  ? 219 VAL B CG1    1 
ATOM   5086 C CG2    . VAL C 3 219 ? 42.880 25.818  -25.779 1.00 9.63  ? 219 VAL B CG2    1 
ATOM   5087 N N      . ALA C 3 220 ? 47.051 27.600  -27.239 1.00 11.55 ? 220 ALA B N      1 
ATOM   5088 C CA     . ALA C 3 220 ? 48.506 27.528  -27.356 1.00 11.69 ? 220 ALA B CA     1 
ATOM   5089 C C      . ALA C 3 220 ? 49.073 26.560  -26.328 1.00 13.12 ? 220 ALA B C      1 
ATOM   5090 O O      . ALA C 3 220 ? 48.565 26.444  -25.210 1.00 12.77 ? 220 ALA B O      1 
ATOM   5091 C CB     . ALA C 3 220 ? 49.144 28.907  -27.160 1.00 9.59  ? 220 ALA B CB     1 
ATOM   5092 N N      . LEU C 3 221 ? 50.140 25.850  -26.724 1.00 10.74 ? 221 LEU B N      1 
ATOM   5093 C CA     . LEU C 3 221 ? 50.835 24.959  -25.799 1.00 11.58 ? 221 LEU B CA     1 
ATOM   5094 C C      . LEU C 3 221 ? 51.607 25.753  -24.759 1.00 13.64 ? 221 LEU B C      1 
ATOM   5095 O O      . LEU C 3 221 ? 51.653 25.370  -23.580 1.00 11.24 ? 221 LEU B O      1 
ATOM   5096 C CB     . LEU C 3 221 ? 51.775 24.015  -26.553 1.00 5.48  ? 221 LEU B CB     1 
ATOM   5097 C CG     . LEU C 3 221 ? 52.534 22.961  -25.733 1.00 5.02  ? 221 LEU B CG     1 
ATOM   5098 C CD1    . LEU C 3 221 ? 51.627 22.110  -24.821 1.00 8.57  ? 221 LEU B CD1    1 
ATOM   5099 C CD2    . LEU C 3 221 ? 53.296 22.049  -26.646 1.00 5.75  ? 221 LEU B CD2    1 
ATOM   5100 N N      . ASP C 3 222 ? 52.213 26.857  -25.187 1.00 13.42 ? 222 ASP B N      1 
ATOM   5101 C CA     . ASP C 3 222 ? 52.875 27.821  -24.313 1.00 16.04 ? 222 ASP B CA     1 
ATOM   5102 C C      . ASP C 3 222 ? 52.422 29.210  -24.752 1.00 19.96 ? 222 ASP B C      1 
ATOM   5103 O O      . ASP C 3 222 ? 52.782 29.665  -25.846 1.00 13.63 ? 222 ASP B O      1 
ATOM   5104 C CB     . ASP C 3 222 ? 54.403 27.684  -24.382 1.00 13.18 ? 222 ASP B CB     1 
ATOM   5105 C CG     . ASP C 3 222 ? 55.121 28.572  -23.364 1.00 25.21 ? 222 ASP B CG     1 
ATOM   5106 O OD1    . ASP C 3 222 ? 54.840 28.419  -22.151 1.00 26.07 ? 222 ASP B OD1    1 
ATOM   5107 O OD2    . ASP C 3 222 ? 55.976 29.407  -23.769 1.00 31.15 ? 222 ASP B OD2    1 
ATOM   5108 N N      . PHE C 3 223 ? 51.607 29.867  -23.952 1.00 14.22 ? 223 PHE B N      1 
ATOM   5109 C CA     . PHE C 3 223 ? 51.143 31.183  -24.309 1.00 13.87 ? 223 PHE B CA     1 
ATOM   5110 C C      . PHE C 3 223 ? 52.252 32.108  -24.706 1.00 13.86 ? 223 PHE B C      1 
ATOM   5111 O O      . PHE C 3 223 ? 52.189 32.747  -25.728 1.00 12.34 ? 223 PHE B O      1 
ATOM   5112 C CB     . PHE C 3 223 ? 50.317 31.807  -23.196 1.00 11.18 ? 223 PHE B CB     1 
ATOM   5113 C CG     . PHE C 3 223 ? 49.610 33.059  -23.594 1.00 12.81 ? 223 PHE B CG     1 
ATOM   5114 C CD1    . PHE C 3 223 ? 48.661 33.045  -24.586 1.00 12.86 ? 223 PHE B CD1    1 
ATOM   5115 C CD2    . PHE C 3 223 ? 49.897 34.248  -22.969 1.00 13.73 ? 223 PHE B CD2    1 
ATOM   5116 C CE1    . PHE C 3 223 ? 48.001 34.193  -24.939 1.00 17.66 ? 223 PHE B CE1    1 
ATOM   5117 C CE2    . PHE C 3 223 ? 49.248 35.403  -23.325 1.00 17.74 ? 223 PHE B CE2    1 
ATOM   5118 C CZ     . PHE C 3 223 ? 48.296 35.374  -24.312 1.00 16.17 ? 223 PHE B CZ     1 
ATOM   5119 N N      . GLU C 3 224 ? 53.245 32.211  -23.860 1.00 17.40 ? 224 GLU B N      1 
ATOM   5120 C CA     . GLU C 3 224 ? 54.321 33.145  -24.141 1.00 18.16 ? 224 GLU B CA     1 
ATOM   5121 C C      . GLU C 3 224 ? 54.990 32.795  -25.470 1.00 13.95 ? 224 GLU B C      1 
ATOM   5122 O O      . GLU C 3 224 ? 55.197 33.661  -26.320 1.00 13.68 ? 224 GLU B O      1 
ATOM   5123 C CB     . GLU C 3 224 ? 55.284 33.147  -22.943 1.00 15.30 ? 224 GLU B CB     1 
ATOM   5124 C CG     . GLU C 3 224 ? 56.097 34.397  -22.763 1.00 18.40 ? 224 GLU B CG     1 
ATOM   5125 C CD     . GLU C 3 224 ? 56.623 34.606  -21.349 1.00 23.26 ? 224 GLU B CD     1 
ATOM   5126 O OE1    . GLU C 3 224 ? 55.807 34.709  -20.397 1.00 22.95 ? 224 GLU B OE1    1 
ATOM   5127 O OE2    . GLU C 3 224 ? 57.863 34.707  -21.199 1.00 26.03 ? 224 GLU B OE2    1 
ATOM   5128 N N      . GLN C 3 225 ? 55.280 31.561  -25.765 1.00 17.69 ? 225 GLN B N      1 
ATOM   5129 C CA     . GLN C 3 225 ? 55.887 31.222  -27.038 1.00 21.13 ? 225 GLN B CA     1 
ATOM   5130 C C      . GLN C 3 225 ? 55.076 31.556  -28.280 1.00 17.87 ? 225 GLN B C      1 
ATOM   5131 O O      . GLN C 3 225 ? 55.627 32.018  -29.249 1.00 22.65 ? 225 GLN B O      1 
ATOM   5132 C CB     . GLN C 3 225 ? 56.275 29.729  -27.021 1.00 24.60 ? 225 GLN B CB     1 
ATOM   5133 C CG     . GLN C 3 225 ? 56.909 29.191  -28.292 1.00 31.85 ? 225 GLN B CG     1 
ATOM   5134 C CD     . GLN C 3 225 ? 58.367 29.578  -28.436 1.00 53.01 ? 225 GLN B CD     1 
ATOM   5135 O OE1    . GLN C 3 225 ? 58.950 30.199  -27.553 1.00 50.25 ? 225 GLN B OE1    1 
ATOM   5136 N NE2    . GLN C 3 225 ? 58.966 29.199  -29.556 1.00 59.36 ? 225 GLN B NE2    1 
ATOM   5137 N N      . GLU C 3 226 ? 53.786 31.299  -28.274 1.00 15.14 ? 226 GLU B N      1 
ATOM   5138 C CA     . GLU C 3 226 ? 52.921 31.579  -29.391 1.00 14.03 ? 226 GLU B CA     1 
ATOM   5139 C C      . GLU C 3 226 ? 52.797 33.042  -29.672 1.00 17.49 ? 226 GLU B C      1 
ATOM   5140 O O      . GLU C 3 226 ? 52.659 33.438  -30.810 1.00 20.72 ? 226 GLU B O      1 
ATOM   5141 C CB     . GLU C 3 226 ? 51.565 30.928  -29.169 1.00 16.80 ? 226 GLU B CB     1 
ATOM   5142 C CG     . GLU C 3 226 ? 50.823 30.503  -30.420 1.00 14.39 ? 226 GLU B CG     1 
ATOM   5143 C CD     . GLU C 3 226 ? 51.171 29.107  -30.865 1.00 19.50 ? 226 GLU B CD     1 
ATOM   5144 O OE1    . GLU C 3 226 ? 51.968 28.443  -30.187 1.00 27.63 ? 226 GLU B OE1    1 
ATOM   5145 O OE2    . GLU C 3 226 ? 50.642 28.665  -31.895 1.00 17.77 ? 226 GLU B OE2    1 
ATOM   5146 N N      . MET C 3 227 ? 52.799 33.861  -28.640 1.00 17.42 ? 227 MET B N      1 
ATOM   5147 C CA     . MET C 3 227 ? 52.757 35.294  -28.795 1.00 17.38 ? 227 MET B CA     1 
ATOM   5148 C C      . MET C 3 227 ? 53.962 35.757  -29.517 1.00 23.61 ? 227 MET B C      1 
ATOM   5149 O O      . MET C 3 227 ? 53.903 36.695  -30.283 1.00 25.47 ? 227 MET B O      1 
ATOM   5150 C CB     . MET C 3 227 ? 52.703 35.952  -27.444 1.00 12.44 ? 227 MET B CB     1 
ATOM   5151 C CG     . MET C 3 227 ? 51.373 35.824  -26.719 1.00 18.78 ? 227 MET B CG     1 
ATOM   5152 S SD     . MET C 3 227 ? 50.007 36.734  -27.453 1.00 22.42 ? 227 MET B SD     1 
ATOM   5153 C CE     . MET C 3 227 ? 50.724 38.361  -27.577 1.00 28.53 ? 227 MET B CE     1 
ATOM   5154 N N      . ALA C 3 228 ? 55.080 35.146  -29.236 1.00 17.36 ? 228 ALA B N      1 
ATOM   5155 C CA     . ALA C 3 228 ? 56.266 35.458  -29.935 1.00 16.28 ? 228 ALA B CA     1 
ATOM   5156 C C      . ALA C 3 228 ? 56.204 35.111  -31.398 1.00 21.97 ? 228 ALA B C      1 
ATOM   5157 O O      . ALA C 3 228 ? 56.687 35.846  -32.221 1.00 24.87 ? 228 ALA B O      1 
ATOM   5158 C CB     . ALA C 3 228 ? 57.411 34.767  -29.274 1.00 13.76 ? 228 ALA B CB     1 
ATOM   5159 N N      . THR C 3 229 ? 55.641 33.986  -31.735 1.00 22.00 ? 229 THR B N      1 
ATOM   5160 C CA     . THR C 3 229 ? 55.533 33.570  -33.115 1.00 24.79 ? 229 THR B CA     1 
ATOM   5161 C C      . THR C 3 229 ? 54.632 34.510  -33.873 1.00 25.12 ? 229 THR B C      1 
ATOM   5162 O O      . THR C 3 229 ? 54.873 34.833  -35.008 1.00 31.85 ? 229 THR B O      1 
ATOM   5163 C CB     . THR C 3 229 ? 55.057 32.106  -33.178 1.00 23.63 ? 229 THR B CB     1 
ATOM   5164 O OG1    . THR C 3 229 ? 56.051 31.264  -32.590 1.00 27.68 ? 229 THR B OG1    1 
ATOM   5165 C CG2    . THR C 3 229 ? 54.795 31.657  -34.600 1.00 20.78 ? 229 THR B CG2    1 
ATOM   5166 N N      . ALA C 3 230 ? 53.570 34.942  -33.239 1.00 23.36 ? 230 ALA B N      1 
ATOM   5167 C CA     . ALA C 3 230 ? 52.646 35.844  -33.847 1.00 27.59 ? 230 ALA B CA     1 
ATOM   5168 C C      . ALA C 3 230 ? 53.239 37.192  -34.162 1.00 30.12 ? 230 ALA B C      1 
ATOM   5169 O O      . ALA C 3 230 ? 52.859 37.824  -35.129 1.00 28.17 ? 230 ALA B O      1 
ATOM   5170 C CB     . ALA C 3 230 ? 51.452 35.976  -32.954 1.00 19.25 ? 230 ALA B CB     1 
ATOM   5171 N N      . ALA C 3 231 ? 54.131 37.666  -33.321 1.00 27.50 ? 231 ALA B N      1 
ATOM   5172 C CA     . ALA C 3 231 ? 54.684 38.985  -33.486 1.00 29.68 ? 231 ALA B CA     1 
ATOM   5173 C C      . ALA C 3 231 ? 55.915 38.940  -34.311 1.00 30.28 ? 231 ALA B C      1 
ATOM   5174 O O      . ALA C 3 231 ? 56.455 39.964  -34.683 1.00 27.95 ? 231 ALA B O      1 
ATOM   5175 C CB     . ALA C 3 231 ? 55.006 39.560  -32.134 1.00 23.27 ? 231 ALA B CB     1 
ATOM   5176 N N      . SER C 3 232 ? 56.372 37.744  -34.588 1.00 28.09 ? 232 SER B N      1 
ATOM   5177 C CA     . SER C 3 232 ? 57.567 37.570  -35.391 1.00 25.02 ? 232 SER B CA     1 
ATOM   5178 C C      . SER C 3 232 ? 57.310 36.806  -36.665 1.00 30.42 ? 232 SER B C      1 
ATOM   5179 O O      . SER C 3 232 ? 58.239 36.461  -37.363 1.00 35.91 ? 232 SER B O      1 
ATOM   5180 C CB     . SER C 3 232 ? 58.600 36.818  -34.599 1.00 22.72 ? 232 SER B CB     1 
ATOM   5181 O OG     . SER C 3 232 ? 58.727 37.361  -33.300 1.00 39.19 ? 232 SER B OG     1 
ATOM   5182 N N      . SER C 3 233 ? 56.055 36.561  -36.986 1.00 30.20 ? 233 SER B N      1 
ATOM   5183 C CA     . SER C 3 233 ? 55.704 35.786  -38.166 1.00 30.28 ? 233 SER B CA     1 
ATOM   5184 C C      . SER C 3 233 ? 54.240 36.030  -38.500 1.00 33.74 ? 233 SER B C      1 
ATOM   5185 O O      . SER C 3 233 ? 53.467 36.547  -37.688 1.00 29.83 ? 233 SER B O      1 
ATOM   5186 C CB     . SER C 3 233 ? 55.964 34.296  -37.951 1.00 21.27 ? 233 SER B CB     1 
ATOM   5187 O OG     . SER C 3 233 ? 55.179 33.539  -38.849 1.00 21.75 ? 233 SER B OG     1 
ATOM   5188 N N      . SER C 3 234 ? 53.779 35.542  -39.638 1.00 30.59 ? 234 SER B N      1 
ATOM   5189 C CA     . SER C 3 234 ? 52.378 35.679  -40.006 1.00 30.46 ? 234 SER B CA     1 
ATOM   5190 C C      . SER C 3 234 ? 51.808 34.313  -40.192 1.00 29.23 ? 234 SER B C      1 
ATOM   5191 O O      . SER C 3 234 ? 50.665 34.175  -40.572 1.00 32.91 ? 234 SER B O      1 
ATOM   5192 C CB     . SER C 3 234 ? 52.291 36.444  -41.307 1.00 34.19 ? 234 SER B CB     1 
ATOM   5193 O OG     . SER C 3 234 ? 50.992 36.934  -41.549 1.00 59.34 ? 234 SER B OG     1 
ATOM   5194 N N      . SER C 3 235 ? 52.596 33.298  -39.894 1.00 24.26 ? 235 SER B N      1 
ATOM   5195 C CA     . SER C 3 235 ? 52.179 31.927  -40.140 1.00 23.49 ? 235 SER B CA     1 
ATOM   5196 C C      . SER C 3 235 ? 50.803 31.603  -39.564 1.00 32.30 ? 235 SER B C      1 
ATOM   5197 O O      . SER C 3 235 ? 50.061 30.791  -40.135 1.00 37.68 ? 235 SER B O      1 
ATOM   5198 C CB     . SER C 3 235 ? 53.230 30.990  -39.558 1.00 27.89 ? 235 SER B CB     1 
ATOM   5199 O OG     . SER C 3 235 ? 53.413 31.248  -38.168 1.00 34.56 ? 235 SER B OG     1 
ATOM   5200 N N      . LEU C 3 236 ? 50.438 32.215  -38.454 1.00 29.74 ? 236 LEU B N      1 
ATOM   5201 C CA     . LEU C 3 236 ? 49.207 31.863  -37.793 1.00 27.40 ? 236 LEU B CA     1 
ATOM   5202 C C      . LEU C 3 236 ? 48.009 32.738  -38.035 1.00 28.68 ? 236 LEU B C      1 
ATOM   5203 O O      . LEU C 3 236 ? 46.915 32.400  -37.661 1.00 28.13 ? 236 LEU B O      1 
ATOM   5204 C CB     . LEU C 3 236 ? 49.494 31.741  -36.300 1.00 26.99 ? 236 LEU B CB     1 
ATOM   5205 C CG     . LEU C 3 236 ? 49.996 32.852  -35.385 1.00 31.57 ? 236 LEU B CG     1 
ATOM   5206 C CD1    . LEU C 3 236 ? 48.830 33.608  -34.768 1.00 29.06 ? 236 LEU B CD1    1 
ATOM   5207 C CD2    . LEU C 3 236 ? 50.838 32.220  -34.292 1.00 24.76 ? 236 LEU B CD2    1 
ATOM   5208 N N      . GLU C 3 237 ? 48.204 33.863  -38.678 1.00 28.95 ? 237 GLU B N      1 
ATOM   5209 C CA     . GLU C 3 237 ? 47.062 34.721  -38.993 1.00 25.70 ? 237 GLU B CA     1 
ATOM   5210 C C      . GLU C 3 237 ? 46.137 34.025  -39.979 1.00 27.15 ? 237 GLU B C      1 
ATOM   5211 O O      . GLU C 3 237 ? 46.597 33.440  -40.964 1.00 39.68 ? 237 GLU B O      1 
ATOM   5212 C CB     . GLU C 3 237 ? 47.547 36.053  -39.570 1.00 24.22 ? 237 GLU B CB     1 
ATOM   5213 C CG     . GLU C 3 237 ? 48.448 36.812  -38.591 1.00 42.13 ? 237 GLU B CG     1 
ATOM   5214 C CD     . GLU C 3 237 ? 49.212 37.990  -39.201 1.00 51.14 ? 237 GLU B CD     1 
ATOM   5215 O OE1    . GLU C 3 237 ? 48.778 38.539  -40.238 1.00 54.28 ? 237 GLU B OE1    1 
ATOM   5216 O OE2    . GLU C 3 237 ? 50.260 38.370  -38.628 1.00 55.70 ? 237 GLU B OE2    1 
ATOM   5217 N N      . LYS C 3 238 ? 44.839 34.093  -39.724 1.00 25.54 ? 238 LYS B N      1 
ATOM   5218 C CA     . LYS C 3 238 ? 43.866 33.443  -40.586 1.00 34.37 ? 238 LYS B CA     1 
ATOM   5219 C C      . LYS C 3 238 ? 42.806 34.434  -41.031 1.00 38.17 ? 238 LYS B C      1 
ATOM   5220 O O      . LYS C 3 238 ? 42.584 35.423  -40.383 1.00 33.46 ? 238 LYS B O      1 
ATOM   5221 C CB     . LYS C 3 238 ? 43.229 32.238  -39.898 1.00 24.72 ? 238 LYS B CB     1 
ATOM   5222 C CG     . LYS C 3 238 ? 44.137 31.043  -39.765 1.00 21.37 ? 238 LYS B CG     1 
ATOM   5223 C CD     . LYS C 3 238 ? 43.746 29.932  -40.707 1.00 23.48 ? 238 LYS B CD     1 
ATOM   5224 C CE     . LYS C 3 238 ? 44.797 28.846  -40.700 1.00 24.37 ? 238 LYS B CE     1 
ATOM   5225 N NZ     . LYS C 3 238 ? 46.126 29.413  -40.351 1.00 34.15 ? 238 LYS B NZ     1 
ATOM   5226 N N      . SER C 3 239 ? 42.147 34.161  -42.145 1.00 37.43 ? 239 SER B N      1 
ATOM   5227 C CA     . SER C 3 239 ? 41.184 35.098  -42.665 1.00 34.42 ? 239 SER B CA     1 
ATOM   5228 C C      . SER C 3 239 ? 39.742 34.639  -42.535 1.00 41.66 ? 239 SER B C      1 
ATOM   5229 O O      . SER C 3 239 ? 39.463 33.454  -42.588 1.00 33.17 ? 239 SER B O      1 
ATOM   5230 C CB     . SER C 3 239 ? 41.526 35.410  -44.097 1.00 37.90 ? 239 SER B CB     1 
ATOM   5231 O OG     . SER C 3 239 ? 42.673 36.224  -44.185 1.00 42.95 ? 239 SER B OG     1 
ATOM   5232 N N      . TYR C 3 240 ? 38.832 35.582  -42.343 1.00 34.08 ? 240 TYR B N      1 
ATOM   5233 C CA     . TYR C 3 240 ? 37.436 35.242  -42.187 1.00 37.32 ? 240 TYR B CA     1 
ATOM   5234 C C      . TYR C 3 240 ? 36.562 36.130  -43.018 1.00 40.22 ? 240 TYR B C      1 
ATOM   5235 O O      . TYR C 3 240 ? 36.615 37.338  -42.920 1.00 34.93 ? 240 TYR B O      1 
ATOM   5236 C CB     . TYR C 3 240 ? 37.013 35.280  -40.710 1.00 33.92 ? 240 TYR B CB     1 
ATOM   5237 C CG     . TYR C 3 240 ? 35.628 34.780  -40.389 1.00 27.70 ? 240 TYR B CG     1 
ATOM   5238 C CD1    . TYR C 3 240 ? 35.381 33.431  -40.217 1.00 31.49 ? 240 TYR B CD1    1 
ATOM   5239 C CD2    . TYR C 3 240 ? 34.578 35.660  -40.219 1.00 29.42 ? 240 TYR B CD2    1 
ATOM   5240 C CE1    . TYR C 3 240 ? 34.118 32.972  -39.908 1.00 32.05 ? 240 TYR B CE1    1 
ATOM   5241 C CE2    . TYR C 3 240 ? 33.313 35.213  -39.916 1.00 30.76 ? 240 TYR B CE2    1 
ATOM   5242 C CZ     . TYR C 3 240 ? 33.092 33.868  -39.758 1.00 35.78 ? 240 TYR B CZ     1 
ATOM   5243 O OH     . TYR C 3 240 ? 31.837 33.423  -39.457 1.00 31.05 ? 240 TYR B OH     1 
ATOM   5244 N N      . GLU C 3 241 ? 35.715 35.507  -43.815 1.00 44.62 ? 241 GLU B N      1 
ATOM   5245 C CA     . GLU C 3 241 ? 34.834 36.255  -44.676 1.00 45.83 ? 241 GLU B CA     1 
ATOM   5246 C C      . GLU C 3 241 ? 33.591 36.608  -43.916 1.00 41.42 ? 241 GLU B C      1 
ATOM   5247 O O      . GLU C 3 241 ? 32.853 35.749  -43.471 1.00 40.70 ? 241 GLU B O      1 
ATOM   5248 C CB     . GLU C 3 241 ? 34.538 35.459  -45.935 1.00 43.21 ? 241 GLU B CB     1 
ATOM   5249 C CG     . GLU C 3 241 ? 35.704 35.323  -46.908 1.00 49.45 ? 241 GLU B CG     1 
ATOM   5250 C CD     . GLU C 3 241 ? 36.842 34.464  -46.380 1.00 63.03 ? 241 GLU B CD     1 
ATOM   5251 O OE1    . GLU C 3 241 ? 36.558 33.423  -45.751 1.00 55.87 ? 241 GLU B OE1    1 
ATOM   5252 O OE2    . GLU C 3 241 ? 38.017 34.844  -46.564 1.00 57.74 ? 241 GLU B OE2    1 
ATOM   5253 N N      . LEU C 3 242 ? 33.371 37.892  -43.748 1.00 39.14 ? 242 LEU B N      1 
ATOM   5254 C CA     . LEU C 3 242 ? 32.257 38.332  -42.979 1.00 38.18 ? 242 LEU B CA     1 
ATOM   5255 C C      . LEU C 3 242 ? 30.914 38.284  -43.762 1.00 49.67 ? 242 LEU B C      1 
ATOM   5256 O O      . LEU C 3 242 ? 30.932 38.078  -44.972 1.00 48.93 ? 242 LEU B O      1 
ATOM   5257 C CB     . LEU C 3 242 ? 32.513 39.723  -42.431 1.00 31.44 ? 242 LEU B CB     1 
ATOM   5258 C CG     . LEU C 3 242 ? 32.493 39.997  -40.934 1.00 47.59 ? 242 LEU B CG     1 
ATOM   5259 C CD1    . LEU C 3 242 ? 33.607 39.239  -40.255 1.00 44.53 ? 242 LEU B CD1    1 
ATOM   5260 C CD2    . LEU C 3 242 ? 32.589 41.482  -40.637 1.00 42.69 ? 242 LEU B CD2    1 
ATOM   5261 N N      . PRO C 3 243 ? 29.737 38.431  -43.083 1.00 51.11 ? 243 PRO B N      1 
ATOM   5262 C CA     . PRO C 3 243 ? 28.519 38.397  -43.881 1.00 51.59 ? 243 PRO B CA     1 
ATOM   5263 C C      . PRO C 3 243 ? 28.397 39.495  -44.965 1.00 50.48 ? 243 PRO B C      1 
ATOM   5264 O O      . PRO C 3 243 ? 27.854 39.189  -46.015 1.00 57.33 ? 243 PRO B O      1 
ATOM   5265 C CB     . PRO C 3 243 ? 27.443 38.509  -42.811 1.00 42.40 ? 243 PRO B CB     1 
ATOM   5266 C CG     . PRO C 3 243 ? 28.010 37.788  -41.651 1.00 35.42 ? 243 PRO B CG     1 
ATOM   5267 C CD     . PRO C 3 243 ? 29.460 38.151  -41.662 1.00 44.15 ? 243 PRO B CD     1 
ATOM   5268 N N      . ASP C 3 244 ? 28.911 40.705  -44.761 1.00 52.22 ? 244 ASP B N      1 
ATOM   5269 C CA     . ASP C 3 244 ? 28.890 41.777  -45.779 1.00 44.95 ? 244 ASP B CA     1 
ATOM   5270 C C      . ASP C 3 244 ? 29.828 41.578  -46.923 1.00 37.34 ? 244 ASP B C      1 
ATOM   5271 O O      . ASP C 3 244 ? 29.716 42.229  -47.937 1.00 41.55 ? 244 ASP B O      1 
ATOM   5272 C CB     . ASP C 3 244 ? 29.205 43.140  -45.164 1.00 46.06 ? 244 ASP B CB     1 
ATOM   5273 C CG     . ASP C 3 244 ? 30.108 43.058  -43.952 1.00 59.30 ? 244 ASP B CG     1 
ATOM   5274 O OD1    . ASP C 3 244 ? 31.000 42.194  -43.913 1.00 56.35 ? 244 ASP B OD1    1 
ATOM   5275 O OD2    . ASP C 3 244 ? 29.943 43.890  -43.038 1.00 55.23 ? 244 ASP B OD2    1 
ATOM   5276 N N      . GLY C 3 245 ? 30.782 40.696  -46.751 1.00 41.91 ? 245 GLY B N      1 
ATOM   5277 C CA     . GLY C 3 245 ? 31.724 40.415  -47.799 1.00 42.28 ? 245 GLY B CA     1 
ATOM   5278 C C      . GLY C 3 245 ? 33.098 40.794  -47.362 1.00 41.38 ? 245 GLY B C      1 
ATOM   5279 O O      . GLY C 3 245 ? 34.069 40.496  -48.033 1.00 42.42 ? 245 GLY B O      1 
ATOM   5280 N N      . GLN C 3 246 ? 33.182 41.433  -46.218 1.00 37.79 ? 246 GLN B N      1 
ATOM   5281 C CA     . GLN C 3 246 ? 34.452 41.888  -45.727 1.00 34.88 ? 246 GLN B CA     1 
ATOM   5282 C C      . GLN C 3 246 ? 35.327 40.798  -45.184 1.00 34.46 ? 246 GLN B C      1 
ATOM   5283 O O      . GLN C 3 246 ? 34.886 39.964  -44.464 1.00 38.36 ? 246 GLN B O      1 
ATOM   5284 C CB     . GLN C 3 246 ? 34.205 42.952  -44.690 1.00 34.38 ? 246 GLN B CB     1 
ATOM   5285 C CG     . GLN C 3 246 ? 33.392 44.107  -45.240 1.00 36.22 ? 246 GLN B CG     1 
ATOM   5286 C CD     . GLN C 3 246 ? 33.483 45.338  -44.381 1.00 39.38 ? 246 GLN B CD     1 
ATOM   5287 O OE1    . GLN C 3 246 ? 32.526 45.718  -43.712 1.00 44.19 ? 246 GLN B OE1    1 
ATOM   5288 N NE2    . GLN C 3 246 ? 34.644 45.971  -44.389 1.00 33.15 ? 246 GLN B NE2    1 
ATOM   5289 N N      . VAL C 3 247 ? 36.583 40.783  -45.574 1.00 40.12 ? 247 VAL B N      1 
ATOM   5290 C CA     . VAL C 3 247 ? 37.506 39.809  -45.064 1.00 37.98 ? 247 VAL B CA     1 
ATOM   5291 C C      . VAL C 3 247 ? 38.304 40.401  -43.938 1.00 49.27 ? 247 VAL B C      1 
ATOM   5292 O O      . VAL C 3 247 ? 39.043 41.357  -44.130 1.00 52.79 ? 247 VAL B O      1 
ATOM   5293 C CB     . VAL C 3 247 ? 38.435 39.290  -46.134 1.00 35.29 ? 247 VAL B CB     1 
ATOM   5294 C CG1    . VAL C 3 247 ? 39.403 38.274  -45.556 1.00 32.24 ? 247 VAL B CG1    1 
ATOM   5295 C CG2    . VAL C 3 247 ? 37.616 38.651  -47.239 1.00 40.87 ? 247 VAL B CG2    1 
ATOM   5296 N N      . ILE C 3 248 ? 38.125 39.865  -42.739 1.00 47.75 ? 248 ILE B N      1 
ATOM   5297 C CA     . ILE C 3 248 ? 38.905 40.319  -41.627 1.00 40.24 ? 248 ILE B CA     1 
ATOM   5298 C C      . ILE C 3 248 ? 39.987 39.303  -41.398 1.00 30.43 ? 248 ILE B C      1 
ATOM   5299 O O      . ILE C 3 248 ? 39.861 38.174  -41.806 1.00 35.65 ? 248 ILE B O      1 
ATOM   5300 C CB     . ILE C 3 248 ? 38.023 40.552  -40.394 1.00 42.67 ? 248 ILE B CB     1 
ATOM   5301 C CG1    . ILE C 3 248 ? 37.402 39.260  -39.892 1.00 40.84 ? 248 ILE B CG1    1 
ATOM   5302 C CG2    . ILE C 3 248 ? 36.927 41.550  -40.715 1.00 34.46 ? 248 ILE B CG2    1 
ATOM   5303 C CD1    . ILE C 3 248 ? 36.865 39.396  -38.492 1.00 38.05 ? 248 ILE B CD1    1 
ATOM   5304 N N      . THR C 3 249 ? 41.077 39.720  -40.796 1.00 31.32 ? 249 THR B N      1 
ATOM   5305 C CA     . THR C 3 249 ? 42.149 38.794  -40.475 1.00 38.40 ? 249 THR B CA     1 
ATOM   5306 C C      . THR C 3 249 ? 42.245 38.536  -38.964 1.00 35.86 ? 249 THR B C      1 
ATOM   5307 O O      . THR C 3 249 ? 42.027 39.430  -38.173 1.00 36.69 ? 249 THR B O      1 
ATOM   5308 C CB     . THR C 3 249 ? 43.485 39.285  -41.005 1.00 35.96 ? 249 THR B CB     1 
ATOM   5309 O OG1    . THR C 3 249 ? 43.269 40.422  -41.845 1.00 44.25 ? 249 THR B OG1    1 
ATOM   5310 C CG2    . THR C 3 249 ? 44.169 38.206  -41.803 1.00 39.90 ? 249 THR B CG2    1 
ATOM   5311 N N      . ILE C 3 250 ? 42.539 37.301  -38.569 1.00 33.14 ? 250 ILE B N      1 
ATOM   5312 C CA     . ILE C 3 250 ? 42.596 36.975  -37.144 1.00 28.02 ? 250 ILE B CA     1 
ATOM   5313 C C      . ILE C 3 250 ? 44.021 36.575  -36.804 1.00 24.07 ? 250 ILE B C      1 
ATOM   5314 O O      . ILE C 3 250 ? 44.540 35.589  -37.350 1.00 25.32 ? 250 ILE B O      1 
ATOM   5315 C CB     . ILE C 3 250 ? 41.618 35.851  -36.758 1.00 26.56 ? 250 ILE B CB     1 
ATOM   5316 C CG1    . ILE C 3 250 ? 40.272 35.980  -37.501 1.00 32.32 ? 250 ILE B CG1    1 
ATOM   5317 C CG2    . ILE C 3 250 ? 41.454 35.802  -35.234 1.00 22.83 ? 250 ILE B CG2    1 
ATOM   5318 C CD1    . ILE C 3 250 ? 39.474 37.286  -37.243 1.00 35.61 ? 250 ILE B CD1    1 
ATOM   5319 N N      . GLY C 3 251 ? 44.645 37.320  -35.891 1.00 22.04 ? 251 GLY B N      1 
ATOM   5320 C CA     . GLY C 3 251 ? 46.012 37.040  -35.492 1.00 22.57 ? 251 GLY B CA     1 
ATOM   5321 C C      . GLY C 3 251 ? 46.126 36.305  -34.169 1.00 17.69 ? 251 GLY B C      1 
ATOM   5322 O O      . GLY C 3 251 ? 45.587 35.210  -34.009 1.00 13.25 ? 251 GLY B O      1 
ATOM   5323 N N      . ASN C 3 252 ? 46.847 36.895  -33.214 1.00 22.02 ? 252 ASN B N      1 
ATOM   5324 C CA     . ASN C 3 252 ? 46.988 36.270  -31.911 1.00 17.70 ? 252 ASN B CA     1 
ATOM   5325 C C      . ASN C 3 252 ? 45.653 36.141  -31.185 1.00 19.03 ? 252 ASN B C      1 
ATOM   5326 O O      . ASN C 3 252 ? 45.589 35.455  -30.156 1.00 19.42 ? 252 ASN B O      1 
ATOM   5327 C CB     . ASN C 3 252 ? 47.983 37.063  -31.065 1.00 15.65 ? 252 ASN B CB     1 
ATOM   5328 C CG     . ASN C 3 252 ? 47.553 38.491  -30.847 1.00 19.01 ? 252 ASN B CG     1 
ATOM   5329 O OD1    . ASN C 3 252 ? 46.400 38.844  -31.088 1.00 18.86 ? 252 ASN B OD1    1 
ATOM   5330 N ND2    . ASN C 3 252 ? 48.474 39.324  -30.376 1.00 18.04 ? 252 ASN B ND2    1 
ATOM   5331 N N      . GLU C 3 253 ? 44.593 36.786  -31.687 1.00 17.69 ? 253 GLU B N      1 
ATOM   5332 C CA     . GLU C 3 253 ? 43.293 36.673  -31.043 1.00 18.21 ? 253 GLU B CA     1 
ATOM   5333 C C      . GLU C 3 253 ? 42.796 35.242  -31.035 1.00 15.85 ? 253 GLU B C      1 
ATOM   5334 O O      . GLU C 3 253 ? 41.972 34.888  -30.181 1.00 17.97 ? 253 GLU B O      1 
ATOM   5335 C CB     . GLU C 3 253 ? 42.269 37.561  -31.748 1.00 18.98 ? 253 GLU B CB     1 
ATOM   5336 C CG     . GLU C 3 253 ? 42.448 39.044  -31.521 1.00 22.19 ? 253 GLU B CG     1 
ATOM   5337 C CD     . GLU C 3 253 ? 43.539 39.644  -32.394 1.00 27.31 ? 253 GLU B CD     1 
ATOM   5338 O OE1    . GLU C 3 253 ? 43.890 39.018  -33.422 1.00 18.10 ? 253 GLU B OE1    1 
ATOM   5339 O OE2    . GLU C 3 253 ? 44.043 40.744  -32.049 1.00 31.90 ? 253 GLU B OE2    1 
ATOM   5340 N N      . ARG C 3 254 ? 43.276 34.423  -31.975 1.00 14.00 ? 254 ARG B N      1 
ATOM   5341 C CA     . ARG C 3 254 ? 42.753 33.072  -32.132 1.00 15.96 ? 254 ARG B CA     1 
ATOM   5342 C C      . ARG C 3 254 ? 43.011 32.239  -30.891 1.00 18.24 ? 254 ARG B C      1 
ATOM   5343 O O      . ARG C 3 254 ? 42.155 31.448  -30.480 1.00 20.46 ? 254 ARG B O      1 
ATOM   5344 C CB     . ARG C 3 254 ? 43.384 32.382  -33.346 1.00 17.61 ? 254 ARG B CB     1 
ATOM   5345 C CG     . ARG C 3 254 ? 43.321 33.143  -34.637 1.00 13.94 ? 254 ARG B CG     1 
ATOM   5346 C CD     . ARG C 3 254 ? 44.058 32.393  -35.712 1.00 17.15 ? 254 ARG B CD     1 
ATOM   5347 N NE     . ARG C 3 254 ? 43.698 30.982  -35.767 1.00 18.81 ? 254 ARG B NE     1 
ATOM   5348 C CZ     . ARG C 3 254 ? 44.506 30.033  -36.222 1.00 19.55 ? 254 ARG B CZ     1 
ATOM   5349 N NH1    . ARG C 3 254 ? 45.710 30.322  -36.691 1.00 22.61 ? 254 ARG B NH1    1 
ATOM   5350 N NH2    . ARG C 3 254 ? 44.109 28.764  -36.184 1.00 13.27 ? 254 ARG B NH2    1 
ATOM   5351 N N      . PHE C 3 255 ? 44.176 32.423  -30.280 1.00 20.23 ? 255 PHE B N      1 
ATOM   5352 C CA     . PHE C 3 255 ? 44.571 31.692  -29.061 1.00 17.98 ? 255 PHE B CA     1 
ATOM   5353 C C      . PHE C 3 255 ? 44.465 32.478  -27.752 1.00 15.78 ? 255 PHE B C      1 
ATOM   5354 O O      . PHE C 3 255 ? 44.551 31.904  -26.698 1.00 16.31 ? 255 PHE B O      1 
ATOM   5355 C CB     . PHE C 3 255 ? 45.976 31.071  -29.232 1.00 11.53 ? 255 PHE B CB     1 
ATOM   5356 C CG     . PHE C 3 255 ? 47.079 32.058  -29.415 1.00 16.69 ? 255 PHE B CG     1 
ATOM   5357 C CD1    . PHE C 3 255 ? 47.734 32.591  -28.330 1.00 14.58 ? 255 PHE B CD1    1 
ATOM   5358 C CD2    . PHE C 3 255 ? 47.491 32.418  -30.676 1.00 16.36 ? 255 PHE B CD2    1 
ATOM   5359 C CE1    . PHE C 3 255 ? 48.751 33.486  -28.498 1.00 16.32 ? 255 PHE B CE1    1 
ATOM   5360 C CE2    . PHE C 3 255 ? 48.522 33.300  -30.853 1.00 13.23 ? 255 PHE B CE2    1 
ATOM   5361 C CZ     . PHE C 3 255 ? 49.148 33.841  -29.761 1.00 13.70 ? 255 PHE B CZ     1 
ATOM   5362 N N      . ARG C 3 256 ? 44.274 33.782  -27.826 1.00 15.74 ? 256 ARG B N      1 
ATOM   5363 C CA     . ARG C 3 256 ? 44.184 34.619  -26.652 1.00 14.61 ? 256 ARG B CA     1 
ATOM   5364 C C      . ARG C 3 256 ? 42.826 34.533  -26.061 1.00 19.05 ? 256 ARG B C      1 
ATOM   5365 O O      . ARG C 3 256 ? 42.645 34.809  -24.894 1.00 22.38 ? 256 ARG B O      1 
ATOM   5366 C CB     . ARG C 3 256 ? 44.487 36.054  -26.978 1.00 14.92 ? 256 ARG B CB     1 
ATOM   5367 C CG     . ARG C 3 256 ? 45.937 36.456  -26.946 1.00 17.48 ? 256 ARG B CG     1 
ATOM   5368 C CD     . ARG C 3 256 ? 46.116 37.813  -27.597 1.00 16.15 ? 256 ARG B CD     1 
ATOM   5369 N NE     . ARG C 3 256 ? 45.514 38.889  -26.824 1.00 21.28 ? 256 ARG B NE     1 
ATOM   5370 C CZ     . ARG C 3 256 ? 44.850 39.911  -27.348 1.00 18.28 ? 256 ARG B CZ     1 
ATOM   5371 N NH1    . ARG C 3 256 ? 44.694 40.010  -28.657 1.00 20.91 ? 256 ARG B NH1    1 
ATOM   5372 N NH2    . ARG C 3 256 ? 44.345 40.838  -26.557 1.00 16.65 ? 256 ARG B NH2    1 
ATOM   5373 N N      . CYS C 3 257 ? 41.859 34.128  -26.856 1.00 21.58 ? 257 CYS B N      1 
ATOM   5374 C CA     . CYS C 3 257 ? 40.525 33.914  -26.331 1.00 18.20 ? 257 CYS B CA     1 
ATOM   5375 C C      . CYS C 3 257 ? 40.433 32.633  -25.480 1.00 15.59 ? 257 CYS B C      1 
ATOM   5376 O O      . CYS C 3 257 ? 39.980 32.701  -24.357 1.00 22.24 ? 257 CYS B O      1 
ATOM   5377 C CB     . CYS C 3 257 ? 39.472 33.963  -27.448 1.00 19.90 ? 257 CYS B CB     1 
ATOM   5378 S SG     . CYS C 3 257 ? 37.880 33.213  -27.129 1.00 25.21 ? 257 CYS B SG     1 
ATOM   5379 N N      . PRO C 3 258 ? 40.853 31.456  -26.009 1.00 13.09 ? 258 PRO B N      1 
ATOM   5380 C CA     . PRO C 3 258 ? 40.745 30.338  -25.093 1.00 16.89 ? 258 PRO B CA     1 
ATOM   5381 C C      . PRO C 3 258 ? 41.766 30.338  -23.938 1.00 19.74 ? 258 PRO B C      1 
ATOM   5382 O O      . PRO C 3 258 ? 41.655 29.494  -23.075 1.00 12.39 ? 258 PRO B O      1 
ATOM   5383 C CB     . PRO C 3 258 ? 40.916 29.138  -26.025 1.00 16.05 ? 258 PRO B CB     1 
ATOM   5384 C CG     . PRO C 3 258 ? 40.554 29.621  -27.362 1.00 17.21 ? 258 PRO B CG     1 
ATOM   5385 C CD     . PRO C 3 258 ? 41.149 30.974  -27.367 1.00 15.99 ? 258 PRO B CD     1 
ATOM   5386 N N      . GLU C 3 259 ? 42.705 31.276  -23.902 1.00 15.31 ? 259 GLU B N      1 
ATOM   5387 C CA     . GLU C 3 259 ? 43.656 31.382  -22.827 1.00 12.19 ? 259 GLU B CA     1 
ATOM   5388 C C      . GLU C 3 259 ? 42.971 31.792  -21.574 1.00 12.20 ? 259 GLU B C      1 
ATOM   5389 O O      . GLU C 3 259 ? 43.412 31.448  -20.518 1.00 11.79 ? 259 GLU B O      1 
ATOM   5390 C CB     . GLU C 3 259 ? 44.771 32.347  -23.218 1.00 10.86 ? 259 GLU B CB     1 
ATOM   5391 C CG     . GLU C 3 259 ? 45.943 32.439  -22.258 1.00 13.11 ? 259 GLU B CG     1 
ATOM   5392 C CD     . GLU C 3 259 ? 46.700 31.147  -22.091 1.00 15.10 ? 259 GLU B CD     1 
ATOM   5393 O OE1    . GLU C 3 259 ? 46.855 30.402  -23.067 1.00 14.40 ? 259 GLU B OE1    1 
ATOM   5394 O OE2    . GLU C 3 259 ? 47.162 30.887  -20.973 1.00 12.31 ? 259 GLU B OE2    1 
ATOM   5395 N N      . ALA C 3 260 ? 41.852 32.474  -21.683 1.00 16.88 ? 260 ALA B N      1 
ATOM   5396 C CA     . ALA C 3 260 ? 41.039 32.868  -20.546 1.00 16.91 ? 260 ALA B CA     1 
ATOM   5397 C C      . ALA C 3 260 ? 40.530 31.736  -19.678 1.00 13.05 ? 260 ALA B C      1 
ATOM   5398 O O      . ALA C 3 260 ? 40.035 31.960  -18.615 1.00 10.55 ? 260 ALA B O      1 
ATOM   5399 C CB     . ALA C 3 260 ? 39.894 33.724  -21.031 1.00 8.96  ? 260 ALA B CB     1 
ATOM   5400 N N      . LEU C 3 261 ? 40.673 30.514  -20.127 1.00 10.99 ? 261 LEU B N      1 
ATOM   5401 C CA     . LEU C 3 261 ? 40.294 29.378  -19.332 1.00 10.61 ? 261 LEU B CA     1 
ATOM   5402 C C      . LEU C 3 261 ? 41.360 29.049  -18.344 1.00 10.92 ? 261 LEU B C      1 
ATOM   5403 O O      . LEU C 3 261 ? 41.068 28.690  -17.239 1.00 9.06  ? 261 LEU B O      1 
ATOM   5404 C CB     . LEU C 3 261 ? 40.034 28.212  -20.237 1.00 10.60 ? 261 LEU B CB     1 
ATOM   5405 C CG     . LEU C 3 261 ? 38.860 28.279  -21.208 1.00 13.98 ? 261 LEU B CG     1 
ATOM   5406 C CD1    . LEU C 3 261 ? 38.923 27.165  -22.240 1.00 5.95  ? 261 LEU B CD1    1 
ATOM   5407 C CD2    . LEU C 3 261 ? 37.563 28.197  -20.441 1.00 8.55  ? 261 LEU B CD2    1 
ATOM   5408 N N      . PHE C 3 262 ? 42.597 29.231  -18.724 1.00 12.10 ? 262 PHE B N      1 
ATOM   5409 C CA     . PHE C 3 262 ? 43.713 28.965  -17.869 1.00 11.35 ? 262 PHE B CA     1 
ATOM   5410 C C      . PHE C 3 262 ? 44.108 30.241  -17.178 1.00 15.26 ? 262 PHE B C      1 
ATOM   5411 O O      . PHE C 3 262 ? 44.670 30.194  -16.109 1.00 14.57 ? 262 PHE B O      1 
ATOM   5412 C CB     . PHE C 3 262 ? 44.861 28.439  -18.727 1.00 10.88 ? 262 PHE B CB     1 
ATOM   5413 C CG     . PHE C 3 262 ? 44.558 27.168  -19.453 1.00 8.85  ? 262 PHE B CG     1 
ATOM   5414 C CD1    . PHE C 3 262 ? 44.767 25.951  -18.845 1.00 8.52  ? 262 PHE B CD1    1 
ATOM   5415 C CD2    . PHE C 3 262 ? 44.088 27.189  -20.750 1.00 8.78  ? 262 PHE B CD2    1 
ATOM   5416 C CE1    . PHE C 3 262 ? 44.498 24.778  -19.505 1.00 9.01  ? 262 PHE B CE1    1 
ATOM   5417 C CE2    . PHE C 3 262 ? 43.803 26.021  -21.412 1.00 8.43  ? 262 PHE B CE2    1 
ATOM   5418 C CZ     . PHE C 3 262 ? 44.010 24.812  -20.790 1.00 9.26  ? 262 PHE B CZ     1 
ATOM   5419 N N      . GLN C 3 263 ? 43.857 31.381  -17.802 1.00 15.96 ? 263 GLN B N      1 
ATOM   5420 C CA     . GLN C 3 263 ? 44.131 32.695  -17.221 1.00 14.78 ? 263 GLN B CA     1 
ATOM   5421 C C      . GLN C 3 263 ? 42.796 33.492  -17.131 1.00 18.63 ? 263 GLN B C      1 
ATOM   5422 O O      . GLN C 3 263 ? 42.574 34.330  -17.974 1.00 18.47 ? 263 GLN B O      1 
ATOM   5423 C CB     . GLN C 3 263 ? 45.168 33.470  -17.989 1.00 14.07 ? 263 GLN B CB     1 
ATOM   5424 C CG     . GLN C 3 263 ? 46.519 32.809  -18.088 1.00 13.91 ? 263 GLN B CG     1 
ATOM   5425 C CD     . GLN C 3 263 ? 47.588 33.781  -18.500 1.00 13.16 ? 263 GLN B CD     1 
ATOM   5426 O OE1    . GLN C 3 263 ? 48.188 33.643  -19.556 1.00 17.75 ? 263 GLN B OE1    1 
ATOM   5427 N NE2    . GLN C 3 263 ? 47.828 34.776  -17.669 1.00 11.12 ? 263 GLN B NE2    1 
ATOM   5428 N N      . PRO C 3 264 ? 41.904 33.238  -16.110 1.00 20.96 ? 264 PRO B N      1 
ATOM   5429 C CA     . PRO C 3 264 ? 40.606 33.906  -16.022 1.00 18.55 ? 264 PRO B CA     1 
ATOM   5430 C C      . PRO C 3 264 ? 40.705 35.405  -15.778 1.00 17.91 ? 264 PRO B C      1 
ATOM   5431 O O      . PRO C 3 264 ? 39.727 36.073  -15.979 1.00 20.62 ? 264 PRO B O      1 
ATOM   5432 C CB     . PRO C 3 264 ? 39.915 33.129  -14.903 1.00 18.84 ? 264 PRO B CB     1 
ATOM   5433 C CG     . PRO C 3 264 ? 40.613 31.834  -14.854 1.00 16.94 ? 264 PRO B CG     1 
ATOM   5434 C CD     . PRO C 3 264 ? 42.033 32.214  -15.069 1.00 16.76 ? 264 PRO B CD     1 
ATOM   5435 N N      . SER C 3 265 ? 41.867 35.909  -15.416 1.00 20.96 ? 265 SER B N      1 
ATOM   5436 C CA     . SER C 3 265 ? 42.115 37.332  -15.168 1.00 27.77 ? 265 SER B CA     1 
ATOM   5437 C C      . SER C 3 265 ? 41.925 38.213  -16.358 1.00 24.52 ? 265 SER B C      1 
ATOM   5438 O O      . SER C 3 265 ? 41.705 39.398  -16.215 1.00 25.77 ? 265 SER B O      1 
ATOM   5439 C CB     . SER C 3 265 ? 43.542 37.508  -14.672 1.00 26.76 ? 265 SER B CB     1 
ATOM   5440 O OG     . SER C 3 265 ? 44.479 37.197  -15.682 1.00 27.13 ? 265 SER B OG     1 
ATOM   5441 N N      . PHE C 3 266 ? 42.006 37.632  -17.536 1.00 15.24 ? 266 PHE B N      1 
ATOM   5442 C CA     . PHE C 3 266 ? 41.855 38.355  -18.764 1.00 18.69 ? 266 PHE B CA     1 
ATOM   5443 C C      . PHE C 3 266 ? 40.495 38.959  -18.810 1.00 23.55 ? 266 PHE B C      1 
ATOM   5444 O O      . PHE C 3 266 ? 40.259 39.874  -19.570 1.00 33.22 ? 266 PHE B O      1 
ATOM   5445 C CB     . PHE C 3 266 ? 41.967 37.385  -19.926 1.00 18.03 ? 266 PHE B CB     1 
ATOM   5446 C CG     . PHE C 3 266 ? 43.363 36.986  -20.297 1.00 13.63 ? 266 PHE B CG     1 
ATOM   5447 C CD1    . PHE C 3 266 ? 44.451 37.313  -19.520 1.00 18.14 ? 266 PHE B CD1    1 
ATOM   5448 C CD2    . PHE C 3 266 ? 43.572 36.252  -21.445 1.00 14.60 ? 266 PHE B CD2    1 
ATOM   5449 C CE1    . PHE C 3 266 ? 45.718 36.923  -19.882 1.00 15.94 ? 266 PHE B CE1    1 
ATOM   5450 C CE2    . PHE C 3 266 ? 44.833 35.863  -21.818 1.00 15.10 ? 266 PHE B CE2    1 
ATOM   5451 C CZ     . PHE C 3 266 ? 45.909 36.198  -21.034 1.00 17.36 ? 266 PHE B CZ     1 
ATOM   5452 N N      . LEU C 3 267 ? 39.595 38.464  -17.992 1.00 24.02 ? 267 LEU B N      1 
ATOM   5453 C CA     . LEU C 3 267 ? 38.234 38.922  -17.987 1.00 21.01 ? 267 LEU B CA     1 
ATOM   5454 C C      . LEU C 3 267 ? 37.861 39.691  -16.711 1.00 31.24 ? 267 LEU B C      1 
ATOM   5455 O O      . LEU C 3 267 ? 36.712 40.059  -16.548 1.00 33.36 ? 267 LEU B O      1 
ATOM   5456 C CB     . LEU C 3 267 ? 37.375 37.688  -18.084 1.00 18.90 ? 267 LEU B CB     1 
ATOM   5457 C CG     . LEU C 3 267 ? 36.434 37.333  -19.211 1.00 28.93 ? 267 LEU B CG     1 
ATOM   5458 C CD1    . LEU C 3 267 ? 37.256 36.894  -20.397 1.00 23.98 ? 267 LEU B CD1    1 
ATOM   5459 C CD2    . LEU C 3 267 ? 35.602 36.177  -18.692 1.00 21.95 ? 267 LEU B CD2    1 
ATOM   5460 N N      . GLY C 3 268 ? 38.799 39.908  -15.793 1.00 27.32 ? 268 GLY B N      1 
ATOM   5461 C CA     . GLY C 3 268 ? 38.550 40.651  -14.562 1.00 29.79 ? 268 GLY B CA     1 
ATOM   5462 C C      . GLY C 3 268 ? 38.065 39.720  -13.509 1.00 24.21 ? 268 GLY B C      1 
ATOM   5463 O O      . GLY C 3 268 ? 37.430 40.124  -12.558 1.00 29.98 ? 268 GLY B O      1 
ATOM   5464 N N      . MET C 3 269 ? 38.412 38.478  -13.648 1.00 26.04 ? 269 MET B N      1 
ATOM   5465 C CA     . MET C 3 269 ? 37.947 37.421  -12.764 1.00 25.44 ? 269 MET B CA     1 
ATOM   5466 C C      . MET C 3 269 ? 39.128 36.911  -11.933 1.00 30.92 ? 269 MET B C      1 
ATOM   5467 O O      . MET C 3 269 ? 40.155 36.501  -12.485 1.00 27.57 ? 269 MET B O      1 
ATOM   5468 C CB     . MET C 3 269 ? 37.295 36.318  -13.599 1.00 18.35 ? 269 MET B CB     1 
ATOM   5469 C CG     . MET C 3 269 ? 36.612 35.233  -12.830 1.00 17.75 ? 269 MET B CG     1 
ATOM   5470 S SD     . MET C 3 269 ? 35.594 34.208  -13.912 1.00 27.49 ? 269 MET B SD     1 
ATOM   5471 C CE     . MET C 3 269 ? 34.871 33.080  -12.685 1.00 29.34 ? 269 MET B CE     1 
ATOM   5472 N N      . GLU C 3 270 ? 38.995 36.953  -10.606 1.00 36.42 ? 270 GLU B N      1 
ATOM   5473 C CA     . GLU C 3 270 ? 40.105 36.577  -9.739  1.00 32.61 ? 270 GLU B CA     1 
ATOM   5474 C C      . GLU C 3 270 ? 40.198 35.078  -9.469  1.00 32.81 ? 270 GLU B C      1 
ATOM   5475 O O      . GLU C 3 270 ? 41.182 34.634  -8.856  1.00 30.95 ? 270 GLU B O      1 
ATOM   5476 C CB     . GLU C 3 270 ? 40.009 37.318  -8.407  1.00 38.25 ? 270 GLU B CB     1 
ATOM   5477 C CG     . GLU C 3 270 ? 41.372 37.523  -7.763  1.00 50.68 ? 270 GLU B CG     1 
ATOM   5478 C CD     . GLU C 3 270 ? 41.268 37.985  -6.332  1.00 56.21 ? 270 GLU B CD     1 
ATOM   5479 O OE1    . GLU C 3 270 ? 40.201 38.548  -5.973  1.00 56.80 ? 270 GLU B OE1    1 
ATOM   5480 O OE2    . GLU C 3 270 ? 42.249 37.776  -5.578  1.00 51.72 ? 270 GLU B OE2    1 
ATOM   5481 N N      . SER C 3 271 ? 39.208 34.297  -9.901  1.00 23.54 ? 271 SER B N      1 
ATOM   5482 C CA     . SER C 3 271 ? 39.242 32.855  -9.731  1.00 25.60 ? 271 SER B CA     1 
ATOM   5483 C C      . SER C 3 271 ? 40.441 32.231  -10.460 1.00 26.55 ? 271 SER B C      1 
ATOM   5484 O O      . SER C 3 271 ? 41.196 32.886  -11.187 1.00 22.84 ? 271 SER B O      1 
ATOM   5485 C CB     . SER C 3 271 ? 37.929 32.232  -10.224 1.00 40.12 ? 271 SER B CB     1 
ATOM   5486 O OG     . SER C 3 271 ? 37.928 31.962  -11.623 1.00 36.54 ? 271 SER B OG     1 
ATOM   5487 N N      . CYS C 3 272 ? 40.608 30.931  -10.248 1.00 27.04 ? 272 CYS B N      1 
ATOM   5488 C CA     . CYS C 3 272 ? 41.709 30.195  -10.835 1.00 21.87 ? 272 CYS B CA     1 
ATOM   5489 C C      . CYS C 3 272 ? 41.302 29.596  -12.175 1.00 17.64 ? 272 CYS B C      1 
ATOM   5490 O O      . CYS C 3 272 ? 40.128 29.578  -12.541 1.00 17.28 ? 272 CYS B O      1 
ATOM   5491 C CB     . CYS C 3 272 ? 42.155 29.094  -9.896  1.00 24.01 ? 272 CYS B CB     1 
ATOM   5492 S SG     . CYS C 3 272 ? 41.022 27.710  -9.947  1.00 58.65 ? 272 CYS B SG     1 
ATOM   5493 N N      . GLY C 3 273 ? 42.306 29.059  -12.900 1.00 15.97 ? 273 GLY B N      1 
ATOM   5494 C CA     . GLY C 3 273 ? 42.087 28.523  -14.229 1.00 15.15 ? 273 GLY B CA     1 
ATOM   5495 C C      . GLY C 3 273 ? 41.693 27.069  -14.194 1.00 15.45 ? 273 GLY B C      1 
ATOM   5496 O O      . GLY C 3 273 ? 41.847 26.406  -13.158 1.00 17.24 ? 273 GLY B O      1 
ATOM   5497 N N      . ILE C 3 274 ? 41.201 26.572  -15.340 1.00 12.71 ? 274 ILE B N      1 
ATOM   5498 C CA     . ILE C 3 274 ? 40.632 25.226  -15.365 1.00 10.94 ? 274 ILE B CA     1 
ATOM   5499 C C      . ILE C 3 274 ? 41.648 24.154  -15.020 1.00 10.17 ? 274 ILE B C      1 
ATOM   5500 O O      . ILE C 3 274 ? 41.261 23.040  -14.660 1.00 8.80  ? 274 ILE B O      1 
ATOM   5501 C CB     . ILE C 3 274 ? 39.992 24.909  -16.717 1.00 7.43  ? 274 ILE B CB     1 
ATOM   5502 C CG1    . ILE C 3 274 ? 41.022 24.999  -17.831 1.00 7.16  ? 274 ILE B CG1    1 
ATOM   5503 C CG2    . ILE C 3 274 ? 38.874 25.846  -16.994 1.00 9.42  ? 274 ILE B CG2    1 
ATOM   5504 C CD1    . ILE C 3 274 ? 40.423 24.637  -19.193 1.00 7.82  ? 274 ILE B CD1    1 
ATOM   5505 N N      . HIS C 3 275 ? 42.946 24.447  -15.120 1.00 8.99  ? 275 HIS B N      1 
ATOM   5506 C CA     . HIS C 3 275 ? 43.928 23.470  -14.663 1.00 11.03 ? 275 HIS B CA     1 
ATOM   5507 C C      . HIS C 3 275 ? 44.065 23.455  -13.135 1.00 13.89 ? 275 HIS B C      1 
ATOM   5508 O O      . HIS C 3 275 ? 44.166 22.379  -12.522 1.00 8.71  ? 275 HIS B O      1 
ATOM   5509 C CB     . HIS C 3 275 ? 45.271 23.762  -15.304 1.00 9.55  ? 275 HIS B CB     1 
ATOM   5510 C CG     . HIS C 3 275 ? 45.741 25.146  -15.048 1.00 10.39 ? 275 HIS B CG     1 
ATOM   5511 N ND1    . HIS C 3 275 ? 44.942 26.248  -15.264 1.00 11.04 ? 275 HIS B ND1    1 
ATOM   5512 C CD2    . HIS C 3 275 ? 46.917 25.615  -14.574 1.00 14.79 ? 275 HIS B CD2    1 
ATOM   5513 C CE1    . HIS C 3 275 ? 45.614 27.338  -14.951 1.00 15.54 ? 275 HIS B CE1    1 
ATOM   5514 N NE2    . HIS C 3 275 ? 46.814 26.983  -14.527 1.00 14.74 ? 275 HIS B NE2    1 
ATOM   5515 N N      . GLU C 3 276 ? 44.107 24.634  -12.500 1.00 15.52 ? 276 GLU B N      1 
ATOM   5516 C CA     . GLU C 3 276 ? 44.224 24.678  -11.046 1.00 11.83 ? 276 GLU B CA     1 
ATOM   5517 C C      . GLU C 3 276 ? 42.923 24.234  -10.381 1.00 11.38 ? 276 GLU B C      1 
ATOM   5518 O O      . GLU C 3 276 ? 42.941 23.609  -9.322  1.00 8.71  ? 276 GLU B O      1 
ATOM   5519 C CB     . GLU C 3 276 ? 44.638 26.089  -10.622 1.00 13.67 ? 276 GLU B CB     1 
ATOM   5520 C CG     . GLU C 3 276 ? 45.682 26.706  -11.577 1.00 21.71 ? 276 GLU B CG     1 
ATOM   5521 C CD     . GLU C 3 276 ? 45.942 28.230  -11.371 1.00 32.68 ? 276 GLU B CD     1 
ATOM   5522 O OE1    . GLU C 3 276 ? 45.094 29.080  -11.795 1.00 17.85 ? 276 GLU B OE1    1 
ATOM   5523 O OE2    . GLU C 3 276 ? 47.031 28.556  -10.813 1.00 35.57 ? 276 GLU B OE2    1 
ATOM   5524 N N      . THR C 3 277 ? 41.787 24.539  -10.997 1.00 13.14 ? 277 THR B N      1 
ATOM   5525 C CA     . THR C 3 277 ? 40.527 23.969  -10.543 1.00 11.00 ? 277 THR B CA     1 
ATOM   5526 C C      . THR C 3 277 ? 40.588 22.446  -10.519 1.00 11.34 ? 277 THR B C      1 
ATOM   5527 O O      . THR C 3 277 ? 40.101 21.806  -9.582  1.00 12.65 ? 277 THR B O      1 
ATOM   5528 C CB     . THR C 3 277 ? 39.411 24.443  -11.463 1.00 11.96 ? 277 THR B CB     1 
ATOM   5529 O OG1    . THR C 3 277 ? 39.069 25.798  -11.142 1.00 12.63 ? 277 THR B OG1    1 
ATOM   5530 C CG2    . THR C 3 277 ? 38.212 23.532  -11.351 1.00 12.58 ? 277 THR B CG2    1 
ATOM   5531 N N      . THR C 3 278 ? 41.167 21.843  -11.550 1.00 11.56 ? 278 THR B N      1 
ATOM   5532 C CA     . THR C 3 278 ? 41.270 20.392  -11.582 1.00 11.09 ? 278 THR B CA     1 
ATOM   5533 C C      . THR C 3 278 ? 42.118 19.889  -10.421 1.00 8.69  ? 278 THR B C      1 
ATOM   5534 O O      . THR C 3 278 ? 41.683 19.027  -9.651  1.00 8.00  ? 278 THR B O      1 
ATOM   5535 C CB     . THR C 3 278 ? 41.846 19.958  -12.931 1.00 10.54 ? 278 THR B CB     1 
ATOM   5536 O OG1    . THR C 3 278 ? 40.878 20.211  -13.959 1.00 8.58  ? 278 THR B OG1    1 
ATOM   5537 C CG2    . THR C 3 278 ? 42.258 18.470  -12.935 1.00 7.46  ? 278 THR B CG2    1 
ATOM   5538 N N      . PHE C 3 279 ? 43.339 20.423  -10.286 1.00 9.09  ? 279 PHE B N      1 
ATOM   5539 C CA     . PHE C 3 279 ? 44.161 20.141  -9.114  1.00 8.00  ? 279 PHE B CA     1 
ATOM   5540 C C      . PHE C 3 279 ? 43.337 20.314  -7.841  1.00 7.69  ? 279 PHE B C      1 
ATOM   5541 O O      . PHE C 3 279 ? 43.134 19.358  -7.090  1.00 8.51  ? 279 PHE B O      1 
ATOM   5542 C CB     . PHE C 3 279 ? 45.423 21.035  -9.106  1.00 7.22  ? 279 PHE B CB     1 
ATOM   5543 C CG     . PHE C 3 279 ? 46.398 20.741  -7.969  1.00 5.84  ? 279 PHE B CG     1 
ATOM   5544 C CD1    . PHE C 3 279 ? 47.169 19.566  -7.954  1.00 4.09  ? 279 PHE B CD1    1 
ATOM   5545 C CD2    . PHE C 3 279 ? 46.555 21.645  -6.923  1.00 4.62  ? 279 PHE B CD2    1 
ATOM   5546 C CE1    . PHE C 3 279 ? 48.074 19.290  -6.895  1.00 7.25  ? 279 PHE B CE1    1 
ATOM   5547 C CE2    . PHE C 3 279 ? 47.485 21.385  -5.849  1.00 7.08  ? 279 PHE B CE2    1 
ATOM   5548 C CZ     . PHE C 3 279 ? 48.239 20.196  -5.835  1.00 6.63  ? 279 PHE B CZ     1 
ATOM   5549 N N      . ASN C 3 280 ? 42.802 21.515  -7.610  1.00 8.79  ? 280 ASN B N      1 
ATOM   5550 C CA     . ASN C 3 280 ? 42.123 21.783  -6.339  1.00 9.27  ? 280 ASN B CA     1 
ATOM   5551 C C      . ASN C 3 280 ? 41.022 20.775  -6.071  1.00 10.99 ? 280 ASN B C      1 
ATOM   5552 O O      . ASN C 3 280 ? 40.872 20.291  -4.941  1.00 9.27  ? 280 ASN B O      1 
ATOM   5553 C CB     . ASN C 3 280 ? 41.561 23.192  -6.322  1.00 7.22  ? 280 ASN B CB     1 
ATOM   5554 C CG     . ASN C 3 280 ? 42.639 24.222  -6.435  1.00 9.74  ? 280 ASN B CG     1 
ATOM   5555 O OD1    . ASN C 3 280 ? 43.823 23.927  -6.222  1.00 8.11  ? 280 ASN B OD1    1 
ATOM   5556 N ND2    . ASN C 3 280 ? 42.249 25.447  -6.782  1.00 10.83 ? 280 ASN B ND2    1 
ATOM   5557 N N      . SER C 3 281 ? 40.245 20.446  -7.102  1.00 8.71  ? 281 SER B N      1 
ATOM   5558 C CA     . SER C 3 281 ? 39.231 19.418  -6.967  1.00 4.37  ? 281 SER B CA     1 
ATOM   5559 C C      . SER C 3 281 ? 39.852 18.101  -6.523  1.00 8.56  ? 281 SER B C      1 
ATOM   5560 O O      . SER C 3 281 ? 39.418 17.488  -5.543  1.00 12.24 ? 281 SER B O      1 
ATOM   5561 C CB     . SER C 3 281 ? 38.516 19.270  -8.295  1.00 10.49 ? 281 SER B CB     1 
ATOM   5562 O OG     . SER C 3 281 ? 37.376 18.452  -8.166  1.00 14.80 ? 281 SER B OG     1 
ATOM   5563 N N      . ILE C 3 282 ? 40.885 17.650  -7.228  1.00 7.44  ? 282 ILE B N      1 
ATOM   5564 C CA     . ILE C 3 282 ? 41.538 16.415  -6.839  1.00 5.13  ? 282 ILE B CA     1 
ATOM   5565 C C      . ILE C 3 282 ? 42.105 16.461  -5.420  1.00 9.30  ? 282 ILE B C      1 
ATOM   5566 O O      . ILE C 3 282 ? 42.287 15.415  -4.794  1.00 11.61 ? 282 ILE B O      1 
ATOM   5567 C CB     . ILE C 3 282 ? 42.648 16.091  -7.838  1.00 6.56  ? 282 ILE B CB     1 
ATOM   5568 C CG1    . ILE C 3 282 ? 42.048 15.906  -9.232  1.00 9.31  ? 282 ILE B CG1    1 
ATOM   5569 C CG2    . ILE C 3 282 ? 43.377 14.886  -7.373  1.00 6.18  ? 282 ILE B CG2    1 
ATOM   5570 C CD1    . ILE C 3 282 ? 43.068 15.845  -10.383 1.00 6.03  ? 282 ILE B CD1    1 
ATOM   5571 N N      . MET C 3 283 ? 42.417 17.642  -4.891  1.00 11.37 ? 283 MET B N      1 
ATOM   5572 C CA     . MET C 3 283 ? 42.976 17.670  -3.545  1.00 10.40 ? 283 MET B CA     1 
ATOM   5573 C C      . MET C 3 283 ? 41.910 17.653  -2.451  1.00 11.21 ? 283 MET B C      1 
ATOM   5574 O O      . MET C 3 283 ? 42.264 17.453  -1.290  1.00 9.00  ? 283 MET B O      1 
ATOM   5575 C CB     . MET C 3 283 ? 43.891 18.883  -3.369  1.00 8.34  ? 283 MET B CB     1 
ATOM   5576 C CG     . MET C 3 283 ? 45.191 18.806  -4.130  1.00 5.76  ? 283 MET B CG     1 
ATOM   5577 S SD     . MET C 3 283 ? 46.237 17.360  -3.734  1.00 16.59 ? 283 MET B SD     1 
ATOM   5578 C CE     . MET C 3 283 ? 46.892 17.774  -2.127  1.00 6.68  ? 283 MET B CE     1 
ATOM   5579 N N      . LYS C 3 284 ? 40.626 17.862  -2.776  1.00 12.72 ? 284 LYS B N      1 
ATOM   5580 C CA     . LYS C 3 284 ? 39.533 17.611  -1.840  1.00 9.97  ? 284 LYS B CA     1 
ATOM   5581 C C      . LYS C 3 284 ? 39.064 16.146  -1.864  1.00 11.34 ? 284 LYS B C      1 
ATOM   5582 O O      . LYS C 3 284 ? 38.009 15.829  -1.304  1.00 8.78  ? 284 LYS B O      1 
ATOM   5583 C CB     . LYS C 3 284 ? 38.360 18.572  -2.113  1.00 10.55 ? 284 LYS B CB     1 
ATOM   5584 C CG     . LYS C 3 284 ? 38.772 20.024  -1.884  1.00 15.29 ? 284 LYS B CG     1 
ATOM   5585 C CD     . LYS C 3 284 ? 37.695 21.072  -2.095  1.00 14.53 ? 284 LYS B CD     1 
ATOM   5586 C CE     . LYS C 3 284 ? 37.508 21.363  -3.566  1.00 21.96 ? 284 LYS B CE     1 
ATOM   5587 N NZ     . LYS C 3 284 ? 36.213 22.064  -3.818  1.00 19.03 ? 284 LYS B NZ     1 
ATOM   5588 N N      . CYS C 3 285 ? 39.829 15.249  -2.479  1.00 10.38 ? 285 CYS B N      1 
ATOM   5589 C CA     . CYS C 3 285 ? 39.563 13.825  -2.401  1.00 10.75 ? 285 CYS B CA     1 
ATOM   5590 C C      . CYS C 3 285 ? 40.643 13.115  -1.595  1.00 15.95 ? 285 CYS B C      1 
ATOM   5591 O O      . CYS C 3 285 ? 41.797 13.555  -1.535  1.00 15.10 ? 285 CYS B O      1 
ATOM   5592 C CB     . CYS C 3 285 ? 39.496 13.181  -3.771  1.00 8.66  ? 285 CYS B CB     1 
ATOM   5593 S SG     . CYS C 3 285 ? 38.329 13.870  -4.911  1.00 8.67  ? 285 CYS B SG     1 
ATOM   5594 N N      . ASP C 3 286 ? 40.242 11.993  -1.004  1.00 13.39 ? 286 ASP B N      1 
ATOM   5595 C CA     . ASP C 3 286 ? 41.163 11.047  -0.392  1.00 19.20 ? 286 ASP B CA     1 
ATOM   5596 C C      . ASP C 3 286 ? 42.374 10.791  -1.288  1.00 18.09 ? 286 ASP B C      1 
ATOM   5597 O O      . ASP C 3 286 ? 42.221 10.388  -2.442  1.00 19.48 ? 286 ASP B O      1 
ATOM   5598 C CB     . ASP C 3 286 ? 40.411 9.739   -0.147  1.00 17.64 ? 286 ASP B CB     1 
ATOM   5599 C CG     . ASP C 3 286 ? 41.222 8.732   0.607   1.00 24.54 ? 286 ASP B CG     1 
ATOM   5600 O OD1    . ASP C 3 286 ? 42.315 9.079   1.084   1.00 28.50 ? 286 ASP B OD1    1 
ATOM   5601 O OD2    . ASP C 3 286 ? 40.767 7.577   0.740   1.00 41.68 ? 286 ASP B OD2    1 
ATOM   5602 N N      . VAL C 3 287 ? 43.581 11.003  -0.747  1.00 15.41 ? 287 VAL B N      1 
ATOM   5603 C CA     . VAL C 3 287 ? 44.804 10.662  -1.474  1.00 15.07 ? 287 VAL B CA     1 
ATOM   5604 C C      . VAL C 3 287 ? 44.728 9.261   -2.076  1.00 15.88 ? 287 VAL B C      1 
ATOM   5605 O O      . VAL C 3 287 ? 45.387 8.977   -3.080  1.00 17.02 ? 287 VAL B O      1 
ATOM   5606 C CB     . VAL C 3 287 ? 46.034 10.782  -0.541  1.00 23.56 ? 287 VAL B CB     1 
ATOM   5607 C CG1    . VAL C 3 287 ? 46.077 9.592   0.425   1.00 23.76 ? 287 VAL B CG1    1 
ATOM   5608 C CG2    . VAL C 3 287 ? 47.332 10.868  -1.336  1.00 16.97 ? 287 VAL B CG2    1 
ATOM   5609 N N      . ASP C 3 288 ? 43.941 8.360   -1.482  1.00 19.01 ? 288 ASP B N      1 
ATOM   5610 C CA     . ASP C 3 288 ? 43.866 6.970   -1.942  1.00 18.02 ? 288 ASP B CA     1 
ATOM   5611 C C      . ASP C 3 288 ? 43.174 6.794   -3.289  1.00 17.34 ? 288 ASP B C      1 
ATOM   5612 O O      . ASP C 3 288 ? 43.285 5.711   -3.876  1.00 16.97 ? 288 ASP B O      1 
ATOM   5613 C CB     . ASP C 3 288 ? 43.163 6.121   -0.890  1.00 17.84 ? 288 ASP B CB     1 
ATOM   5614 C CG     . ASP C 3 288 ? 43.999 5.980   0.358   1.00 32.19 ? 288 ASP B CG     1 
ATOM   5615 O OD1    . ASP C 3 288 ? 45.238 5.927   0.179   1.00 33.94 ? 288 ASP B OD1    1 
ATOM   5616 O OD2    . ASP C 3 288 ? 43.455 5.947   1.495   1.00 34.74 ? 288 ASP B OD2    1 
ATOM   5617 N N      . ILE C 3 289 ? 42.472 7.809   -3.790  1.00 14.80 ? 289 ILE B N      1 
ATOM   5618 C CA     . ILE C 3 289 ? 41.880 7.758   -5.124  1.00 14.75 ? 289 ILE B CA     1 
ATOM   5619 C C      . ILE C 3 289 ? 42.487 8.763   -6.096  1.00 7.48  ? 289 ILE B C      1 
ATOM   5620 O O      . ILE C 3 289 ? 42.160 8.716   -7.287  1.00 7.50  ? 289 ILE B O      1 
ATOM   5621 C CB     . ILE C 3 289 ? 40.344 7.935   -5.072  1.00 11.79 ? 289 ILE B CB     1 
ATOM   5622 C CG1    . ILE C 3 289 ? 39.970 9.365   -4.648  1.00 10.18 ? 289 ILE B CG1    1 
ATOM   5623 C CG2    . ILE C 3 289 ? 39.749 6.943   -4.120  1.00 6.70  ? 289 ILE B CG2    1 
ATOM   5624 C CD1    . ILE C 3 289 ? 38.571 9.795   -5.000  1.00 6.67  ? 289 ILE B CD1    1 
ATOM   5625 N N      . ARG C 3 290 ? 43.378 9.645   -5.652  1.00 6.29  ? 290 ARG B N      1 
ATOM   5626 C CA     . ARG C 3 290 ? 43.894 10.678  -6.543  1.00 7.87  ? 290 ARG B CA     1 
ATOM   5627 C C      . ARG C 3 290 ? 44.660 10.078  -7.703  1.00 10.10 ? 290 ARG B C      1 
ATOM   5628 O O      . ARG C 3 290 ? 44.659 10.621  -8.816  1.00 8.39  ? 290 ARG B O      1 
ATOM   5629 C CB     . ARG C 3 290 ? 44.800 11.642  -5.788  1.00 7.40  ? 290 ARG B CB     1 
ATOM   5630 C CG     . ARG C 3 290 ? 44.065 12.542  -4.898  1.00 8.52  ? 290 ARG B CG     1 
ATOM   5631 C CD     . ARG C 3 290 ? 45.002 13.429  -4.164  1.00 12.77 ? 290 ARG B CD     1 
ATOM   5632 N NE     . ARG C 3 290 ? 44.424 13.823  -2.887  1.00 15.17 ? 290 ARG B NE     1 
ATOM   5633 C CZ     . ARG C 3 290 ? 45.122 14.334  -1.889  1.00 12.83 ? 290 ARG B CZ     1 
ATOM   5634 N NH1    . ARG C 3 290 ? 46.413 14.583  -2.008  1.00 11.88 ? 290 ARG B NH1    1 
ATOM   5635 N NH2    . ARG C 3 290 ? 44.510 14.601  -0.748  1.00 11.09 ? 290 ARG B NH2    1 
ATOM   5636 N N      . LYS C 3 291 ? 45.398 9.004   -7.446  1.00 10.46 ? 291 LYS B N      1 
ATOM   5637 C CA     . LYS C 3 291 ? 46.125 8.390   -8.539  1.00 8.43  ? 291 LYS B CA     1 
ATOM   5638 C C      . LYS C 3 291 ? 45.171 8.037   -9.674  1.00 10.66 ? 291 LYS B C      1 
ATOM   5639 O O      . LYS C 3 291 ? 45.455 8.314   -10.844 1.00 6.52  ? 291 LYS B O      1 
ATOM   5640 C CB     . LYS C 3 291 ? 46.883 7.174   -8.032  1.00 7.89  ? 291 LYS B CB     1 
ATOM   5641 C CG     . LYS C 3 291 ? 48.294 7.125   -8.559  1.00 16.83 ? 291 LYS B CG     1 
ATOM   5642 C CD     . LYS C 3 291 ? 49.219 6.265   -7.699  1.00 28.01 ? 291 LYS B CD     1 
ATOM   5643 C CE     . LYS C 3 291 ? 49.804 7.063   -6.540  1.00 22.97 ? 291 LYS B CE     1 
ATOM   5644 N NZ     . LYS C 3 291 ? 50.994 6.370   -5.980  1.00 31.40 ? 291 LYS B NZ     1 
ATOM   5645 N N      . ASP C 3 292 ? 43.992 7.499   -9.339  1.00 12.74 ? 292 ASP B N      1 
ATOM   5646 C CA     . ASP C 3 292 ? 43.031 7.158   -10.383 1.00 10.57 ? 292 ASP B CA     1 
ATOM   5647 C C      . ASP C 3 292 ? 42.442 8.395   -11.051 1.00 10.39 ? 292 ASP B C      1 
ATOM   5648 O O      . ASP C 3 292 ? 42.146 8.342   -12.249 1.00 12.67 ? 292 ASP B O      1 
ATOM   5649 C CB     . ASP C 3 292 ? 41.902 6.276   -9.833  1.00 14.25 ? 292 ASP B CB     1 
ATOM   5650 C CG     . ASP C 3 292 ? 42.386 4.884   -9.355  1.00 28.47 ? 292 ASP B CG     1 
ATOM   5651 O OD1    . ASP C 3 292 ? 43.288 4.254   -9.978  1.00 32.55 ? 292 ASP B OD1    1 
ATOM   5652 O OD2    . ASP C 3 292 ? 41.834 4.407   -8.338  1.00 30.89 ? 292 ASP B OD2    1 
ATOM   5653 N N      . LEU C 3 293 ? 42.261 9.508   -10.316 1.00 8.69  ? 293 LEU B N      1 
ATOM   5654 C CA     . LEU C 3 293 ? 41.723 10.729  -10.933 1.00 8.41  ? 293 LEU B CA     1 
ATOM   5655 C C      . LEU C 3 293 ? 42.728 11.372  -11.886 1.00 9.26  ? 293 LEU B C      1 
ATOM   5656 O O      . LEU C 3 293 ? 42.361 11.814  -12.987 1.00 6.87  ? 293 LEU B O      1 
ATOM   5657 C CB     . LEU C 3 293 ? 41.298 11.739  -9.862  1.00 7.10  ? 293 LEU B CB     1 
ATOM   5658 C CG     . LEU C 3 293 ? 40.299 11.219  -8.816  1.00 6.46  ? 293 LEU B CG     1 
ATOM   5659 C CD1    . LEU C 3 293 ? 39.941 12.284  -7.786  1.00 5.52  ? 293 LEU B CD1    1 
ATOM   5660 C CD2    . LEU C 3 293 ? 39.048 10.541  -9.430  1.00 4.47  ? 293 LEU B CD2    1 
ATOM   5661 N N      . TYR C 3 294 ? 44.002 11.431  -11.483 1.00 8.40  ? 294 TYR B N      1 
ATOM   5662 C CA     . TYR C 3 294 ? 45.018 11.968  -12.377 1.00 7.37  ? 294 TYR B CA     1 
ATOM   5663 C C      . TYR C 3 294 ? 45.065 11.200  -13.701 1.00 9.07  ? 294 TYR B C      1 
ATOM   5664 O O      . TYR C 3 294 ? 45.148 11.802  -14.779 1.00 8.42  ? 294 TYR B O      1 
ATOM   5665 C CB     . TYR C 3 294 ? 46.378 11.941  -11.683 1.00 6.63  ? 294 TYR B CB     1 
ATOM   5666 C CG     . TYR C 3 294 ? 46.629 13.090  -10.726 1.00 8.42  ? 294 TYR B CG     1 
ATOM   5667 C CD1    . TYR C 3 294 ? 46.554 14.404  -11.154 1.00 6.31  ? 294 TYR B CD1    1 
ATOM   5668 C CD2    . TYR C 3 294 ? 46.978 12.855  -9.408  1.00 8.97  ? 294 TYR B CD2    1 
ATOM   5669 C CE1    . TYR C 3 294 ? 46.794 15.442  -10.303 1.00 5.58  ? 294 TYR B CE1    1 
ATOM   5670 C CE2    . TYR C 3 294 ? 47.231 13.891  -8.555  1.00 7.90  ? 294 TYR B CE2    1 
ATOM   5671 C CZ     . TYR C 3 294 ? 47.144 15.187  -9.010  1.00 8.83  ? 294 TYR B CZ     1 
ATOM   5672 O OH     . TYR C 3 294 ? 47.405 16.245  -8.158  1.00 8.72  ? 294 TYR B OH     1 
ATOM   5673 N N      . ALA C 3 295 ? 45.004 9.873   -13.645 1.00 11.28 ? 295 ALA B N      1 
ATOM   5674 C CA     . ALA C 3 295 ? 45.134 9.082   -14.855 1.00 7.86  ? 295 ALA B CA     1 
ATOM   5675 C C      . ALA C 3 295 ? 43.875 9.068   -15.699 1.00 8.88  ? 295 ALA B C      1 
ATOM   5676 O O      . ALA C 3 295 ? 43.842 8.337   -16.694 1.00 13.90 ? 295 ALA B O      1 
ATOM   5677 C CB     . ALA C 3 295 ? 45.527 7.655   -14.503 1.00 9.22  ? 295 ALA B CB     1 
ATOM   5678 N N      . ASN C 3 296 ? 42.851 9.857   -15.356 1.00 9.39  ? 296 ASN B N      1 
ATOM   5679 C CA     . ASN C 3 296 ? 41.562 9.810   -16.049 1.00 8.01  ? 296 ASN B CA     1 
ATOM   5680 C C      . ASN C 3 296 ? 40.859 11.166  -15.998 1.00 9.31  ? 296 ASN B C      1 
ATOM   5681 O O      . ASN C 3 296 ? 39.735 11.295  -15.508 1.00 12.64 ? 296 ASN B O      1 
ATOM   5682 C CB     . ASN C 3 296 ? 40.663 8.731   -15.456 1.00 8.37  ? 296 ASN B CB     1 
ATOM   5683 C CG     . ASN C 3 296 ? 41.227 7.321   -15.629 1.00 9.05  ? 296 ASN B CG     1 
ATOM   5684 O OD1    . ASN C 3 296 ? 41.049 6.692   -16.664 1.00 8.60  ? 296 ASN B OD1    1 
ATOM   5685 N ND2    . ASN C 3 296 ? 41.894 6.819   -14.597 1.00 6.82  ? 296 ASN B ND2    1 
ATOM   5686 N N      . THR C 3 297 ? 41.520 12.202  -16.529 1.00 7.35  ? 297 THR B N      1 
ATOM   5687 C CA     . THR C 3 297 ? 40.882 13.500  -16.737 1.00 7.43  ? 297 THR B CA     1 
ATOM   5688 C C      . THR C 3 297 ? 40.161 13.473  -18.079 1.00 9.40  ? 297 THR B C      1 
ATOM   5689 O O      . THR C 3 297 ? 40.802 13.382  -19.131 1.00 9.49  ? 297 THR B O      1 
ATOM   5690 C CB     . THR C 3 297 ? 41.881 14.660  -16.718 1.00 7.35  ? 297 THR B CB     1 
ATOM   5691 O OG1    . THR C 3 297 ? 42.770 14.547  -15.596 1.00 13.41 ? 297 THR B OG1    1 
ATOM   5692 C CG2    . THR C 3 297 ? 41.130 15.992  -16.628 1.00 5.83  ? 297 THR B CG2    1 
ATOM   5693 N N      . VAL C 3 298 ? 38.837 13.578  -18.049 1.00 9.58  ? 298 VAL B N      1 
ATOM   5694 C CA     . VAL C 3 298 ? 38.020 13.503  -19.254 1.00 10.66 ? 298 VAL B CA     1 
ATOM   5695 C C      . VAL C 3 298 ? 37.452 14.882  -19.566 1.00 7.68  ? 298 VAL B C      1 
ATOM   5696 O O      . VAL C 3 298 ? 36.733 15.458  -18.745 1.00 9.99  ? 298 VAL B O      1 
ATOM   5697 C CB     . VAL C 3 298 ? 36.909 12.451  -19.089 1.00 11.81 ? 298 VAL B CB     1 
ATOM   5698 C CG1    . VAL C 3 298 ? 36.071 12.364  -20.334 1.00 9.77  ? 298 VAL B CG1    1 
ATOM   5699 C CG2    . VAL C 3 298 ? 37.536 11.099  -18.793 1.00 10.38 ? 298 VAL B CG2    1 
ATOM   5700 N N      . LEU C 3 299 ? 37.762 15.405  -20.753 1.00 9.55  ? 299 LEU B N      1 
ATOM   5701 C CA     . LEU C 3 299 ? 37.325 16.739  -21.173 1.00 12.18 ? 299 LEU B CA     1 
ATOM   5702 C C      . LEU C 3 299 ? 36.002 16.612  -21.925 1.00 10.44 ? 299 LEU B C      1 
ATOM   5703 O O      . LEU C 3 299 ? 35.794 15.657  -22.679 1.00 11.93 ? 299 LEU B O      1 
ATOM   5704 C CB     . LEU C 3 299 ? 38.392 17.444  -22.041 1.00 10.04 ? 299 LEU B CB     1 
ATOM   5705 C CG     . LEU C 3 299 ? 39.724 17.953  -21.433 1.00 10.52 ? 299 LEU B CG     1 
ATOM   5706 C CD1    . LEU C 3 299 ? 40.569 18.748  -22.381 1.00 9.87  ? 299 LEU B CD1    1 
ATOM   5707 C CD2    . LEU C 3 299 ? 39.501 18.844  -20.272 1.00 13.78 ? 299 LEU B CD2    1 
ATOM   5708 N N      . SER C 3 300 ? 35.105 17.569  -21.719 1.00 10.48 ? 300 SER B N      1 
ATOM   5709 C CA     . SER C 3 300 ? 33.719 17.349  -22.109 1.00 10.44 ? 300 SER B CA     1 
ATOM   5710 C C      . SER C 3 300 ? 33.027 18.662  -22.438 1.00 12.25 ? 300 SER B C      1 
ATOM   5711 O O      . SER C 3 300 ? 33.180 19.635  -21.697 1.00 11.16 ? 300 SER B O      1 
ATOM   5712 C CB     . SER C 3 300 ? 32.999 16.636  -20.972 1.00 10.03 ? 300 SER B CB     1 
ATOM   5713 O OG     . SER C 3 300 ? 31.664 16.431  -21.313 1.00 13.34 ? 300 SER B OG     1 
ATOM   5714 N N      . GLY C 3 301 ? 32.309 18.730  -23.531 1.00 13.67 ? 301 GLY B N      1 
ATOM   5715 C CA     . GLY C 3 301 ? 31.562 19.907  -23.863 1.00 13.58 ? 301 GLY B CA     1 
ATOM   5716 C C      . GLY C 3 301 ? 31.991 20.746  -25.012 1.00 15.82 ? 301 GLY B C      1 
ATOM   5717 O O      . GLY C 3 301 ? 32.997 20.481  -25.643 1.00 17.50 ? 301 GLY B O      1 
ATOM   5718 N N      . GLY C 3 302 ? 31.237 21.791  -25.264 1.00 15.54 ? 302 GLY B N      1 
ATOM   5719 C CA     . GLY C 3 302 ? 31.553 22.691  -26.337 1.00 14.07 ? 302 GLY B CA     1 
ATOM   5720 C C      . GLY C 3 302 ? 32.685 23.616  -26.076 1.00 14.21 ? 302 GLY B C      1 
ATOM   5721 O O      . GLY C 3 302 ? 33.361 24.014  -26.996 1.00 12.91 ? 302 GLY B O      1 
ATOM   5722 N N      . THR C 3 303 ? 32.924 23.942  -24.826 1.00 14.01 ? 303 THR B N      1 
ATOM   5723 C CA     . THR C 3 303 ? 34.092 24.763  -24.567 1.00 13.06 ? 303 THR B CA     1 
ATOM   5724 C C      . THR C 3 303 ? 35.383 23.964  -24.505 1.00 18.05 ? 303 THR B C      1 
ATOM   5725 O O      . THR C 3 303 ? 36.459 24.557  -24.596 1.00 23.56 ? 303 THR B O      1 
ATOM   5726 C CB     . THR C 3 303 ? 33.938 25.527  -23.262 1.00 14.25 ? 303 THR B CB     1 
ATOM   5727 O OG1    . THR C 3 303 ? 32.649 26.142  -23.233 1.00 14.39 ? 303 THR B OG1    1 
ATOM   5728 C CG2    . THR C 3 303 ? 35.015 26.583  -23.164 1.00 14.45 ? 303 THR B CG2    1 
ATOM   5729 N N      . THR C 3 304 ? 35.328 22.653  -24.331 1.00 15.22 ? 304 THR B N      1 
ATOM   5730 C CA     . THR C 3 304 ? 36.565 21.883  -24.395 1.00 17.52 ? 304 THR B CA     1 
ATOM   5731 C C      . THR C 3 304 ? 37.025 21.653  -25.830 1.00 18.37 ? 304 THR B C      1 
ATOM   5732 O O      . THR C 3 304 ? 37.975 20.896  -26.064 1.00 19.90 ? 304 THR B O      1 
ATOM   5733 C CB     . THR C 3 304 ? 36.383 20.529  -23.700 1.00 14.45 ? 304 THR B CB     1 
ATOM   5734 O OG1    . THR C 3 304 ? 35.317 19.816  -24.341 1.00 16.65 ? 304 THR B OG1    1 
ATOM   5735 C CG2    . THR C 3 304 ? 36.039 20.718  -22.230 1.00 13.25 ? 304 THR B CG2    1 
ATOM   5736 N N      . MET C 3 305 ? 36.273 22.166  -26.778 1.00 18.04 ? 305 MET B N      1 
ATOM   5737 C CA     . MET C 3 305 ? 36.491 21.874  -28.185 1.00 18.91 ? 305 MET B CA     1 
ATOM   5738 C C      . MET C 3 305 ? 37.417 22.796  -28.927 1.00 22.16 ? 305 MET B C      1 
ATOM   5739 O O      . MET C 3 305 ? 37.093 23.328  -29.961 1.00 27.70 ? 305 MET B O      1 
ATOM   5740 C CB     . MET C 3 305 ? 35.127 21.771  -28.869 1.00 12.42 ? 305 MET B CB     1 
ATOM   5741 C CG     . MET C 3 305 ? 35.075 20.876  -30.079 1.00 23.91 ? 305 MET B CG     1 
ATOM   5742 S SD     . MET C 3 305 ? 35.261 19.153  -29.672 1.00 32.37 ? 305 MET B SD     1 
ATOM   5743 C CE     . MET C 3 305 ? 33.830 18.536  -30.529 1.00 24.15 ? 305 MET B CE     1 
ATOM   5744 N N      . TYR C 3 306 ? 38.587 22.982  -28.376 1.00 20.19 ? 306 TYR B N      1 
ATOM   5745 C CA     . TYR C 3 306 ? 39.580 23.778  -29.062 1.00 13.33 ? 306 TYR B CA     1 
ATOM   5746 C C      . TYR C 3 306 ? 40.817 22.944  -29.332 1.00 15.26 ? 306 TYR B C      1 
ATOM   5747 O O      . TYR C 3 306 ? 41.358 22.328  -28.406 1.00 11.56 ? 306 TYR B O      1 
ATOM   5748 C CB     . TYR C 3 306 ? 39.955 24.988  -28.232 1.00 14.76 ? 306 TYR B CB     1 
ATOM   5749 C CG     . TYR C 3 306 ? 38.828 25.913  -27.941 1.00 17.36 ? 306 TYR B CG     1 
ATOM   5750 C CD1    . TYR C 3 306 ? 38.229 26.657  -28.948 1.00 22.57 ? 306 TYR B CD1    1 
ATOM   5751 C CD2    . TYR C 3 306 ? 38.376 26.070  -26.653 1.00 16.69 ? 306 TYR B CD2    1 
ATOM   5752 C CE1    . TYR C 3 306 ? 37.180 27.529  -28.677 1.00 24.61 ? 306 TYR B CE1    1 
ATOM   5753 C CE2    . TYR C 3 306 ? 37.327 26.932  -26.367 1.00 22.13 ? 306 TYR B CE2    1 
ATOM   5754 C CZ     . TYR C 3 306 ? 36.737 27.659  -27.382 1.00 23.12 ? 306 TYR B CZ     1 
ATOM   5755 O OH     . TYR C 3 306 ? 35.703 28.515  -27.100 1.00 28.42 ? 306 TYR B OH     1 
ATOM   5756 N N      . PRO C 3 307 ? 41.312 22.934  -30.565 1.00 14.60 ? 307 PRO B N      1 
ATOM   5757 C CA     . PRO C 3 307 ? 42.592 22.276  -30.832 1.00 10.23 ? 307 PRO B CA     1 
ATOM   5758 C C      . PRO C 3 307 ? 43.629 22.659  -29.789 1.00 11.31 ? 307 PRO B C      1 
ATOM   5759 O O      . PRO C 3 307 ? 43.785 23.834  -29.439 1.00 12.70 ? 307 PRO B O      1 
ATOM   5760 C CB     . PRO C 3 307 ? 42.968 22.791  -32.223 1.00 7.06  ? 307 PRO B CB     1 
ATOM   5761 C CG     . PRO C 3 307 ? 41.827 23.622  -32.684 1.00 5.70  ? 307 PRO B CG     1 
ATOM   5762 C CD     . PRO C 3 307 ? 40.720 23.555  -31.761 1.00 7.24  ? 307 PRO B CD     1 
ATOM   5763 N N      . GLY C 3 308 ? 44.333 21.655  -29.281 1.00 10.39 ? 308 GLY B N      1 
ATOM   5764 C CA     . GLY C 3 308 ? 45.455 21.876  -28.404 1.00 9.23  ? 308 GLY B CA     1 
ATOM   5765 C C      . GLY C 3 308 ? 45.121 21.978  -26.937 1.00 13.52 ? 308 GLY B C      1 
ATOM   5766 O O      . GLY C 3 308 ? 46.038 22.227  -26.135 1.00 14.44 ? 308 GLY B O      1 
ATOM   5767 N N      . ILE C 3 309 ? 43.848 21.777  -26.549 1.00 9.52  ? 309 ILE B N      1 
ATOM   5768 C CA     . ILE C 3 309 ? 43.490 21.900  -25.138 1.00 9.82  ? 309 ILE B CA     1 
ATOM   5769 C C      . ILE C 3 309 ? 44.102 20.760  -24.333 1.00 7.67  ? 309 ILE B C      1 
ATOM   5770 O O      . ILE C 3 309 ? 44.794 20.998  -23.341 1.00 10.31 ? 309 ILE B O      1 
ATOM   5771 C CB     . ILE C 3 309 ? 41.960 22.005  -24.949 1.00 12.05 ? 309 ILE B CB     1 
ATOM   5772 C CG1    . ILE C 3 309 ? 41.639 22.587  -23.568 1.00 7.55  ? 309 ILE B CG1    1 
ATOM   5773 C CG2    . ILE C 3 309 ? 41.254 20.672  -25.151 1.00 8.40  ? 309 ILE B CG2    1 
ATOM   5774 C CD1    . ILE C 3 309 ? 40.169 22.884  -23.337 1.00 10.41 ? 309 ILE B CD1    1 
ATOM   5775 N N      . ALA C 3 310 ? 43.930 19.519  -24.790 1.00 6.54  ? 310 ALA B N      1 
ATOM   5776 C CA     . ALA C 3 310 ? 44.415 18.358  -24.037 1.00 7.56  ? 310 ALA B CA     1 
ATOM   5777 C C      . ALA C 3 310 ? 45.931 18.387  -23.830 1.00 10.73 ? 310 ALA B C      1 
ATOM   5778 O O      . ALA C 3 310 ? 46.417 18.107  -22.730 1.00 12.23 ? 310 ALA B O      1 
ATOM   5779 C CB     . ALA C 3 310 ? 44.010 17.061  -24.745 1.00 13.30 ? 310 ALA B CB     1 
ATOM   5780 N N      . ASP C 3 311 ? 46.704 18.671  -24.884 1.00 11.28 ? 311 ASP B N      1 
ATOM   5781 C CA     . ASP C 3 311 ? 48.148 18.792  -24.708 1.00 8.97  ? 311 ASP B CA     1 
ATOM   5782 C C      . ASP C 3 311 ? 48.472 19.829  -23.653 1.00 9.66  ? 311 ASP B C      1 
ATOM   5783 O O      . ASP C 3 311 ? 49.394 19.648  -22.848 1.00 11.11 ? 311 ASP B O      1 
ATOM   5784 C CB     . ASP C 3 311 ? 48.835 19.166  -26.021 1.00 10.12 ? 311 ASP B CB     1 
ATOM   5785 C CG     . ASP C 3 311 ? 48.850 18.038  -27.009 1.00 15.37 ? 311 ASP B CG     1 
ATOM   5786 O OD1    . ASP C 3 311 ? 48.740 16.884  -26.558 1.00 21.05 ? 311 ASP B OD1    1 
ATOM   5787 O OD2    . ASP C 3 311 ? 48.998 18.288  -28.231 1.00 18.64 ? 311 ASP B OD2    1 
ATOM   5788 N N      . ARG C 3 312 ? 47.768 20.929  -23.655 1.00 9.87  ? 312 ARG B N      1 
ATOM   5789 C CA     . ARG C 3 312 ? 48.011 21.978  -22.687 1.00 9.31  ? 312 ARG B CA     1 
ATOM   5790 C C      . ARG C 3 312 ? 47.692 21.573  -21.278 1.00 10.52 ? 312 ARG B C      1 
ATOM   5791 O O      . ARG C 3 312 ? 48.479 21.780  -20.386 1.00 12.36 ? 312 ARG B O      1 
ATOM   5792 C CB     . ARG C 3 312 ? 47.231 23.232  -23.033 1.00 10.38 ? 312 ARG B CB     1 
ATOM   5793 C CG     . ARG C 3 312 ? 47.312 24.330  -22.009 1.00 9.05  ? 312 ARG B CG     1 
ATOM   5794 C CD     . ARG C 3 312 ? 48.635 25.039  -22.058 1.00 8.85  ? 312 ARG B CD     1 
ATOM   5795 N NE     . ARG C 3 312 ? 48.625 26.137  -21.118 1.00 14.87 ? 312 ARG B NE     1 
ATOM   5796 C CZ     . ARG C 3 312 ? 48.341 27.387  -21.432 1.00 10.87 ? 312 ARG B CZ     1 
ATOM   5797 N NH1    . ARG C 3 312 ? 48.050 27.719  -22.675 1.00 5.77  ? 312 ARG B NH1    1 
ATOM   5798 N NH2    . ARG C 3 312 ? 48.358 28.305  -20.492 1.00 11.96 ? 312 ARG B NH2    1 
ATOM   5799 N N      . MET C 3 313 ? 46.528 20.981  -21.095 1.00 8.96  ? 313 MET B N      1 
ATOM   5800 C CA     . MET C 3 313 ? 46.159 20.569  -19.750 1.00 9.55  ? 313 MET B CA     1 
ATOM   5801 C C      . MET C 3 313 ? 47.162 19.564  -19.201 1.00 10.05 ? 313 MET B C      1 
ATOM   5802 O O      . MET C 3 313 ? 47.591 19.671  -18.047 1.00 8.86  ? 313 MET B O      1 
ATOM   5803 C CB     . MET C 3 313 ? 44.745 20.000  -19.749 1.00 11.26 ? 313 MET B CB     1 
ATOM   5804 C CG     . MET C 3 313 ? 44.173 19.816  -18.353 1.00 16.47 ? 313 MET B CG     1 
ATOM   5805 S SD     . MET C 3 313 ? 43.553 21.360  -17.626 1.00 21.13 ? 313 MET B SD     1 
ATOM   5806 C CE     . MET C 3 313 ? 42.012 21.627  -18.487 1.00 14.67 ? 313 MET B CE     1 
ATOM   5807 N N      . GLN C 3 314 ? 47.567 18.599  -20.031 1.00 11.18 ? 314 GLN B N      1 
ATOM   5808 C CA     . GLN C 3 314 ? 48.592 17.641  -19.633 1.00 7.89  ? 314 GLN B CA     1 
ATOM   5809 C C      . GLN C 3 314 ? 49.836 18.353  -19.114 1.00 8.64  ? 314 GLN B C      1 
ATOM   5810 O O      . GLN C 3 314 ? 50.432 17.941  -18.113 1.00 10.64 ? 314 GLN B O      1 
ATOM   5811 C CB     . GLN C 3 314 ? 48.915 16.740  -20.821 1.00 9.47  ? 314 GLN B CB     1 
ATOM   5812 C CG     . GLN C 3 314 ? 50.232 16.013  -20.748 1.00 11.28 ? 314 GLN B CG     1 
ATOM   5813 C CD     . GLN C 3 314 ? 50.114 14.678  -20.052 1.00 20.51 ? 314 GLN B CD     1 
ATOM   5814 O OE1    . GLN C 3 314 ? 49.064 14.019  -20.091 1.00 17.92 ? 314 GLN B OE1    1 
ATOM   5815 N NE2    . GLN C 3 314 ? 51.194 14.267  -19.396 1.00 23.40 ? 314 GLN B NE2    1 
ATOM   5816 N N      . LYS C 3 315 ? 50.231 19.443  -19.763 1.00 7.56  ? 315 LYS B N      1 
ATOM   5817 C CA     . LYS C 3 315 ? 51.425 20.156  -19.339 1.00 8.93  ? 315 LYS B CA     1 
ATOM   5818 C C      . LYS C 3 315 ? 51.180 20.952  -18.056 1.00 9.97  ? 315 LYS B C      1 
ATOM   5819 O O      . LYS C 3 315 ? 52.098 21.080  -17.233 1.00 11.27 ? 315 LYS B O      1 
ATOM   5820 C CB     . LYS C 3 315 ? 51.922 21.052  -20.490 1.00 7.99  ? 315 LYS B CB     1 
ATOM   5821 C CG     . LYS C 3 315 ? 52.592 22.335  -20.066 1.00 6.00  ? 315 LYS B CG     1 
ATOM   5822 C CD     . LYS C 3 315 ? 53.209 23.016  -21.241 1.00 10.08 ? 315 LYS B CD     1 
ATOM   5823 C CE     . LYS C 3 315 ? 53.796 24.407  -20.885 1.00 20.83 ? 315 LYS B CE     1 
ATOM   5824 N NZ     . LYS C 3 315 ? 52.886 25.635  -21.072 1.00 14.26 ? 315 LYS B NZ     1 
ATOM   5825 N N      . GLU C 3 316 ? 49.969 21.488  -17.864 1.00 6.21  ? 316 GLU B N      1 
ATOM   5826 C CA     . GLU C 3 316 ? 49.688 22.285  -16.668 1.00 10.28 ? 316 GLU B CA     1 
ATOM   5827 C C      . GLU C 3 316 ? 49.473 21.415  -15.440 1.00 9.01  ? 316 GLU B C      1 
ATOM   5828 O O      . GLU C 3 316 ? 50.007 21.693  -14.360 1.00 9.13  ? 316 GLU B O      1 
ATOM   5829 C CB     . GLU C 3 316 ? 48.459 23.172  -16.880 1.00 12.23 ? 316 GLU B CB     1 
ATOM   5830 C CG     . GLU C 3 316 ? 48.620 24.222  -17.941 1.00 10.78 ? 316 GLU B CG     1 
ATOM   5831 C CD     . GLU C 3 316 ? 49.606 25.266  -17.539 1.00 15.14 ? 316 GLU B CD     1 
ATOM   5832 O OE1    . GLU C 3 316 ? 50.135 25.133  -16.405 1.00 18.18 ? 316 GLU B OE1    1 
ATOM   5833 O OE2    . GLU C 3 316 ? 49.860 26.194  -18.352 1.00 12.33 ? 316 GLU B OE2    1 
ATOM   5834 N N      . ILE C 3 317 ? 48.677 20.367  -15.572 1.00 6.82  ? 317 ILE B N      1 
ATOM   5835 C CA     . ILE C 3 317 ? 48.528 19.477  -14.436 1.00 10.13 ? 317 ILE B CA     1 
ATOM   5836 C C      . ILE C 3 317 ? 49.848 18.798  -14.096 1.00 11.33 ? 317 ILE B C      1 
ATOM   5837 O O      . ILE C 3 317 ? 50.152 18.587  -12.912 1.00 11.04 ? 317 ILE B O      1 
ATOM   5838 C CB     . ILE C 3 317 ? 47.404 18.475  -14.716 1.00 13.06 ? 317 ILE B CB     1 
ATOM   5839 C CG1    . ILE C 3 317 ? 46.091 19.227  -14.738 1.00 13.25 ? 317 ILE B CG1    1 
ATOM   5840 C CG2    . ILE C 3 317 ? 47.342 17.411  -13.639 1.00 9.69  ? 317 ILE B CG2    1 
ATOM   5841 C CD1    . ILE C 3 317 ? 45.027 18.356  -15.139 1.00 21.12 ? 317 ILE B CD1    1 
ATOM   5842 N N      . THR C 3 318 ? 50.669 18.479  -15.104 1.00 8.11  ? 318 THR B N      1 
ATOM   5843 C CA     . THR C 3 318 ? 51.984 17.919  -14.810 1.00 11.04 ? 318 THR B CA     1 
ATOM   5844 C C      . THR C 3 318 ? 52.820 18.880  -13.979 1.00 10.95 ? 318 THR B C      1 
ATOM   5845 O O      . THR C 3 318 ? 53.675 18.446  -13.197 1.00 9.37  ? 318 THR B O      1 
ATOM   5846 C CB     . THR C 3 318 ? 52.702 17.547  -16.101 1.00 9.82  ? 318 THR B CB     1 
ATOM   5847 O OG1    . THR C 3 318 ? 52.093 16.374  -16.643 1.00 15.05 ? 318 THR B OG1    1 
ATOM   5848 C CG2    . THR C 3 318 ? 54.169 17.262  -15.855 1.00 6.95  ? 318 THR B CG2    1 
ATOM   5849 N N      . ALA C 3 319 ? 52.562 20.178  -14.095 1.00 10.76 ? 319 ALA B N      1 
ATOM   5850 C CA     . ALA C 3 319 ? 53.364 21.119  -13.346 1.00 9.87  ? 319 ALA B CA     1 
ATOM   5851 C C      . ALA C 3 319 ? 52.828 21.346  -11.946 1.00 9.79  ? 319 ALA B C      1 
ATOM   5852 O O      . ALA C 3 319 ? 53.570 21.855  -11.106 1.00 12.95 ? 319 ALA B O      1 
ATOM   5853 C CB     . ALA C 3 319 ? 53.461 22.443  -14.097 1.00 10.15 ? 319 ALA B CB     1 
ATOM   5854 N N      . LEU C 3 320 ? 51.571 20.976  -11.672 1.00 8.68  ? 320 LEU B N      1 
ATOM   5855 C CA     . LEU C 3 320 ? 50.995 21.067  -10.329 1.00 9.65  ? 320 LEU B CA     1 
ATOM   5856 C C      . LEU C 3 320 ? 51.020 19.746  -9.577  1.00 9.35  ? 320 LEU B C      1 
ATOM   5857 O O      . LEU C 3 320 ? 50.977 19.750  -8.337  1.00 7.20  ? 320 LEU B O      1 
ATOM   5858 C CB     . LEU C 3 320 ? 49.538 21.553  -10.387 1.00 7.84  ? 320 LEU B CB     1 
ATOM   5859 C CG     . LEU C 3 320 ? 49.250 22.848  -11.151 1.00 6.54  ? 320 LEU B CG     1 
ATOM   5860 C CD1    . LEU C 3 320 ? 47.799 22.942  -11.614 1.00 5.32  ? 320 LEU B CD1    1 
ATOM   5861 C CD2    . LEU C 3 320 ? 49.614 24.023  -10.293 1.00 6.60  ? 320 LEU B CD2    1 
ATOM   5862 N N      . ALA C 3 321 ? 51.084 18.623  -10.288 1.00 9.80  ? 321 ALA B N      1 
ATOM   5863 C CA     . ALA C 3 321 ? 50.990 17.358  -9.594  1.00 8.65  ? 321 ALA B CA     1 
ATOM   5864 C C      . ALA C 3 321 ? 52.352 16.931  -9.081  1.00 14.64 ? 321 ALA B C      1 
ATOM   5865 O O      . ALA C 3 321 ? 53.379 17.468  -9.500  1.00 18.60 ? 321 ALA B O      1 
ATOM   5866 C CB     . ALA C 3 321 ? 50.426 16.300  -10.526 1.00 8.95  ? 321 ALA B CB     1 
ATOM   5867 N N      . PRO C 3 322 ? 52.396 15.961  -8.164  1.00 14.87 ? 322 PRO B N      1 
ATOM   5868 C CA     . PRO C 3 322 ? 53.682 15.373  -7.776  1.00 12.17 ? 322 PRO B CA     1 
ATOM   5869 C C      . PRO C 3 322 ? 54.458 14.900  -8.997  1.00 17.04 ? 322 PRO B C      1 
ATOM   5870 O O      . PRO C 3 322 ? 53.888 14.531  -10.027 1.00 16.18 ? 322 PRO B O      1 
ATOM   5871 C CB     . PRO C 3 322 ? 53.283 14.201  -6.872  1.00 10.31 ? 322 PRO B CB     1 
ATOM   5872 C CG     . PRO C 3 322 ? 51.959 14.557  -6.356  1.00 8.61  ? 322 PRO B CG     1 
ATOM   5873 C CD     . PRO C 3 322 ? 51.274 15.362  -7.425  1.00 10.66 ? 322 PRO B CD     1 
ATOM   5874 N N      . SER C 3 323 ? 55.773 14.831  -8.885  1.00 22.18 ? 323 SER B N      1 
ATOM   5875 C CA     . SER C 3 323 ? 56.637 14.446  -9.999  1.00 22.49 ? 323 SER B CA     1 
ATOM   5876 C C      . SER C 3 323 ? 56.366 13.070  -10.447 1.00 21.40 ? 323 SER B C      1 
ATOM   5877 O O      . SER C 3 323 ? 56.360 12.758  -11.620 1.00 28.42 ? 323 SER B O      1 
ATOM   5878 C CB     . SER C 3 323 ? 58.087 14.503  -9.563  1.00 19.58 ? 323 SER B CB     1 
ATOM   5879 O OG     . SER C 3 323 ? 58.287 15.521  -8.610  1.00 30.93 ? 323 SER B OG     1 
ATOM   5880 N N      . THR C 3 324 ? 56.153 12.203  -9.506  1.00 23.03 ? 324 THR B N      1 
ATOM   5881 C CA     . THR C 3 324 ? 55.889 10.831  -9.821  1.00 34.31 ? 324 THR B CA     1 
ATOM   5882 C C      . THR C 3 324 ? 54.402 10.646  -9.949  1.00 41.62 ? 324 THR B C      1 
ATOM   5883 O O      . THR C 3 324 ? 53.752 10.239  -8.987  1.00 43.64 ? 324 THR B O      1 
ATOM   5884 C CB     . THR C 3 324 ? 56.367 9.972   -8.665  1.00 40.85 ? 324 THR B CB     1 
ATOM   5885 O OG1    . THR C 3 324 ? 56.135 10.667  -7.435  1.00 34.40 ? 324 THR B OG1    1 
ATOM   5886 C CG2    . THR C 3 324 ? 57.845 9.698   -8.808  1.00 44.20 ? 324 THR B CG2    1 
ATOM   5887 N N      . MET C 3 325 ? 53.848 10.933  -11.107 1.00 30.08 ? 325 MET B N      1 
ATOM   5888 C CA     . MET C 3 325 ? 52.383 10.887  -11.240 1.00 22.40 ? 325 MET B CA     1 
ATOM   5889 C C      . MET C 3 325 ? 51.948 10.706  -12.691 1.00 19.08 ? 325 MET B C      1 
ATOM   5890 O O      . MET C 3 325 ? 52.112 11.616  -13.504 1.00 19.70 ? 325 MET B O      1 
ATOM   5891 C CB     . MET C 3 325 ? 51.753 12.142  -10.633 1.00 18.51 ? 325 MET B CB     1 
ATOM   5892 C CG     . MET C 3 325 ? 50.222 12.079  -10.561 1.00 18.95 ? 325 MET B CG     1 
ATOM   5893 S SD     . MET C 3 325 ? 49.473 10.811  -9.475  1.00 12.53 ? 325 MET B SD     1 
ATOM   5894 C CE     . MET C 3 325 ? 49.622 11.532  -7.840  1.00 13.03 ? 325 MET B CE     1 
ATOM   5895 N N      . LYS C 3 326 ? 51.340 9.562   -12.996 1.00 13.81 ? 326 LYS B N      1 
ATOM   5896 C CA     . LYS C 3 326 ? 50.861 9.302   -14.348 1.00 14.17 ? 326 LYS B CA     1 
ATOM   5897 C C      . LYS C 3 326 ? 49.644 10.175  -14.635 1.00 13.49 ? 326 LYS B C      1 
ATOM   5898 O O      . LYS C 3 326 ? 48.565 9.942   -14.087 1.00 15.97 ? 326 LYS B O      1 
ATOM   5899 C CB     . LYS C 3 326 ? 50.511 7.826   -14.521 1.00 23.00 ? 326 LYS B CB     1 
ATOM   5900 C CG     . LYS C 3 326 ? 51.626 6.849   -14.187 1.00 33.41 ? 326 LYS B CG     1 
ATOM   5901 C CD     . LYS C 3 326 ? 51.620 6.372   -12.742 1.00 25.47 ? 326 LYS B CD     1 
ATOM   5902 C CE     . LYS C 3 326 ? 52.916 5.605   -12.442 1.00 35.34 ? 326 LYS B CE     1 
ATOM   5903 N NZ     . LYS C 3 326 ? 54.179 6.418   -12.648 1.00 19.36 ? 326 LYS B NZ     1 
ATOM   5904 N N      . ILE C 3 327 ? 49.803 11.171  -15.498 1.00 13.63 ? 327 ILE B N      1 
ATOM   5905 C CA     . ILE C 3 327 ? 48.729 12.088  -15.876 1.00 14.52 ? 327 ILE B CA     1 
ATOM   5906 C C      . ILE C 3 327 ? 48.291 11.771  -17.303 1.00 13.37 ? 327 ILE B C      1 
ATOM   5907 O O      . ILE C 3 327 ? 49.121 11.708  -18.214 1.00 16.72 ? 327 ILE B O      1 
ATOM   5908 C CB     . ILE C 3 327 ? 49.183 13.559  -15.769 1.00 15.89 ? 327 ILE B CB     1 
ATOM   5909 C CG1    . ILE C 3 327 ? 49.567 13.912  -14.334 1.00 10.64 ? 327 ILE B CG1    1 
ATOM   5910 C CG2    . ILE C 3 327 ? 48.138 14.530  -16.368 1.00 11.29 ? 327 ILE B CG2    1 
ATOM   5911 C CD1    . ILE C 3 327 ? 50.421 15.131  -14.253 1.00 12.88 ? 327 ILE B CD1    1 
ATOM   5912 N N      . LYS C 3 328 ? 46.987 11.611  -17.503 1.00 12.59 ? 328 LYS B N      1 
ATOM   5913 C CA     . LYS C 3 328 ? 46.415 11.330  -18.816 1.00 14.09 ? 328 LYS B CA     1 
ATOM   5914 C C      . LYS C 3 328 ? 45.142 12.150  -18.990 1.00 9.03  ? 328 LYS B C      1 
ATOM   5915 O O      . LYS C 3 328 ? 44.193 12.009  -18.217 1.00 8.94  ? 328 LYS B O      1 
ATOM   5916 C CB     . LYS C 3 328 ? 46.132 9.828   -18.987 1.00 12.69 ? 328 LYS B CB     1 
ATOM   5917 C CG     . LYS C 3 328 ? 45.616 9.412   -20.363 1.00 12.39 ? 328 LYS B CG     1 
ATOM   5918 C CD     . LYS C 3 328 ? 45.820 7.904   -20.528 1.00 24.27 ? 328 LYS B CD     1 
ATOM   5919 C CE     . LYS C 3 328 ? 45.373 7.363   -21.883 1.00 32.81 ? 328 LYS B CE     1 
ATOM   5920 N NZ     . LYS C 3 328 ? 45.400 5.863   -21.896 1.00 26.29 ? 328 LYS B NZ     1 
ATOM   5921 N N      . ILE C 3 329 ? 45.132 13.016  -19.989 1.00 10.40 ? 329 ILE B N      1 
ATOM   5922 C CA     . ILE C 3 329 ? 43.939 13.747  -20.379 1.00 10.90 ? 329 ILE B CA     1 
ATOM   5923 C C      . ILE C 3 329 ? 43.280 13.007  -21.535 1.00 10.65 ? 329 ILE B C      1 
ATOM   5924 O O      . ILE C 3 329 ? 43.918 12.729  -22.555 1.00 13.21 ? 329 ILE B O      1 
ATOM   5925 C CB     . ILE C 3 329 ? 44.276 15.188  -20.771 1.00 10.15 ? 329 ILE B CB     1 
ATOM   5926 C CG1    . ILE C 3 329 ? 44.576 16.010  -19.527 1.00 8.66  ? 329 ILE B CG1    1 
ATOM   5927 C CG2    . ILE C 3 329 ? 43.127 15.793  -21.512 1.00 13.88 ? 329 ILE B CG2    1 
ATOM   5928 C CD1    . ILE C 3 329 ? 45.901 15.760  -18.950 1.00 12.28 ? 329 ILE B CD1    1 
ATOM   5929 N N      . ILE C 3 330 ? 42.006 12.673  -21.387 1.00 10.04 ? 330 ILE B N      1 
ATOM   5930 C CA     . ILE C 3 330 ? 41.225 12.044  -22.448 1.00 12.70 ? 330 ILE B CA     1 
ATOM   5931 C C      . ILE C 3 330 ? 40.265 13.110  -22.971 1.00 11.27 ? 330 ILE B C      1 
ATOM   5932 O O      . ILE C 3 330 ? 39.530 13.728  -22.193 1.00 10.63 ? 330 ILE B O      1 
ATOM   5933 C CB     . ILE C 3 330 ? 40.485 10.791  -21.941 1.00 10.11 ? 330 ILE B CB     1 
ATOM   5934 C CG1    . ILE C 3 330 ? 41.466 9.754   -21.410 1.00 15.11 ? 330 ILE B CG1    1 
ATOM   5935 C CG2    . ILE C 3 330 ? 39.713 10.135  -23.030 1.00 10.21 ? 330 ILE B CG2    1 
ATOM   5936 C CD1    . ILE C 3 330 ? 41.772 9.851   -19.892 1.00 13.77 ? 330 ILE B CD1    1 
ATOM   5937 N N      . ALA C 3 331 ? 40.306 13.375  -24.268 1.00 13.50 ? 331 ALA B N      1 
ATOM   5938 C CA     . ALA C 3 331 ? 39.438 14.382  -24.882 1.00 17.05 ? 331 ALA B CA     1 
ATOM   5939 C C      . ALA C 3 331 ? 39.052 13.909  -26.279 1.00 19.99 ? 331 ALA B C      1 
ATOM   5940 O O      . ALA C 3 331 ? 39.617 14.349  -27.291 1.00 18.51 ? 331 ALA B O      1 
ATOM   5941 C CB     . ALA C 3 331 ? 40.109 15.756  -24.904 1.00 11.63 ? 331 ALA B CB     1 
ATOM   5942 N N      . PRO C 3 332 ? 38.067 13.018  -26.365 1.00 18.45 ? 332 PRO B N      1 
ATOM   5943 C CA     . PRO C 3 332 ? 37.646 12.482  -27.656 1.00 16.10 ? 332 PRO B CA     1 
ATOM   5944 C C      . PRO C 3 332 ? 37.345 13.597  -28.650 1.00 22.22 ? 332 PRO B C      1 
ATOM   5945 O O      . PRO C 3 332 ? 37.137 14.756  -28.265 1.00 22.27 ? 332 PRO B O      1 
ATOM   5946 C CB     . PRO C 3 332 ? 36.377 11.692  -27.307 1.00 18.49 ? 332 PRO B CB     1 
ATOM   5947 C CG     . PRO C 3 332 ? 36.396 11.503  -25.851 1.00 17.30 ? 332 PRO B CG     1 
ATOM   5948 C CD     . PRO C 3 332 ? 37.224 12.555  -25.248 1.00 16.36 ? 332 PRO B CD     1 
ATOM   5949 N N      . PRO C 3 333 ? 37.308 13.283  -29.952 1.00 25.27 ? 333 PRO B N      1 
ATOM   5950 C CA     . PRO C 3 333 ? 36.925 14.306  -30.941 1.00 21.98 ? 333 PRO B CA     1 
ATOM   5951 C C      . PRO C 3 333 ? 35.442 14.632  -30.951 1.00 21.70 ? 333 PRO B C      1 
ATOM   5952 O O      . PRO C 3 333 ? 35.068 15.744  -31.366 1.00 19.67 ? 333 PRO B O      1 
ATOM   5953 C CB     . PRO C 3 333 ? 37.367 13.684  -32.273 1.00 16.23 ? 333 PRO B CB     1 
ATOM   5954 C CG     . PRO C 3 333 ? 37.463 12.273  -32.030 1.00 18.87 ? 333 PRO B CG     1 
ATOM   5955 C CD     . PRO C 3 333 ? 37.789 12.052  -30.594 1.00 22.01 ? 333 PRO B CD     1 
ATOM   5956 N N      . GLU C 3 334 ? 34.630 13.778  -30.363 1.00 23.93 ? 334 GLU B N      1 
ATOM   5957 C CA     . GLU C 3 334 ? 33.199 13.953  -30.268 1.00 25.32 ? 334 GLU B CA     1 
ATOM   5958 C C      . GLU C 3 334 ? 32.841 14.584  -28.970 1.00 22.39 ? 334 GLU B C      1 
ATOM   5959 O O      . GLU C 3 334 ? 31.679 14.646  -28.637 1.00 21.96 ? 334 GLU B O      1 
ATOM   5960 C CB     . GLU C 3 334 ? 32.604 12.560  -30.275 1.00 23.13 ? 334 GLU B CB     1 
ATOM   5961 C CG     . GLU C 3 334 ? 33.183 11.613  -29.246 1.00 18.53 ? 334 GLU B CG     1 
ATOM   5962 C CD     . GLU C 3 334 ? 34.132 10.607  -29.850 1.00 34.72 ? 334 GLU B CD     1 
ATOM   5963 O OE1    . GLU C 3 334 ? 34.555 10.804  -31.001 1.00 33.18 ? 334 GLU B OE1    1 
ATOM   5964 O OE2    . GLU C 3 334 ? 34.464 9.619   -29.168 1.00 44.74 ? 334 GLU B OE2    1 
ATOM   5965 N N      . ARG C 3 335 ? 33.821 15.115  -28.268 1.00 19.30 ? 335 ARG B N      1 
ATOM   5966 C CA     . ARG C 3 335 ? 33.632 15.652  -26.933 1.00 14.95 ? 335 ARG B CA     1 
ATOM   5967 C C      . ARG C 3 335 ? 32.589 16.696  -26.621 1.00 13.13 ? 335 ARG B C      1 
ATOM   5968 O O      . ARG C 3 335 ? 32.291 16.896  -25.477 1.00 14.32 ? 335 ARG B O      1 
ATOM   5969 C CB     . ARG C 3 335 ? 34.992 15.982  -26.335 1.00 16.41 ? 335 ARG B CB     1 
ATOM   5970 C CG     . ARG C 3 335 ? 35.554 17.343  -26.589 1.00 16.57 ? 335 ARG B CG     1 
ATOM   5971 C CD     . ARG C 3 335 ? 36.989 17.327  -26.137 1.00 17.72 ? 335 ARG B CD     1 
ATOM   5972 N NE     . ARG C 3 335 ? 37.763 18.384  -26.749 1.00 20.99 ? 335 ARG B NE     1 
ATOM   5973 C CZ     . ARG C 3 335 ? 38.508 18.252  -27.831 1.00 17.39 ? 335 ARG B CZ     1 
ATOM   5974 N NH1    . ARG C 3 335 ? 38.589 17.093  -28.446 1.00 18.16 ? 335 ARG B NH1    1 
ATOM   5975 N NH2    . ARG C 3 335 ? 39.168 19.292  -28.301 1.00 16.53 ? 335 ARG B NH2    1 
ATOM   5976 N N      . LYS C 3 336 ? 32.003 17.303  -27.626 1.00 15.32 ? 336 LYS B N      1 
ATOM   5977 C CA     . LYS C 3 336 ? 30.964 18.286  -27.446 1.00 14.65 ? 336 LYS B CA     1 
ATOM   5978 C C      . LYS C 3 336 ? 29.680 17.676  -27.013 1.00 17.03 ? 336 LYS B C      1 
ATOM   5979 O O      . LYS C 3 336 ? 28.936 18.266  -26.259 1.00 14.58 ? 336 LYS B O      1 
ATOM   5980 C CB     . LYS C 3 336 ? 30.747 18.963  -28.764 1.00 18.58 ? 336 LYS B CB     1 
ATOM   5981 C CG     . LYS C 3 336 ? 29.991 20.267  -28.739 1.00 24.35 ? 336 LYS B CG     1 
ATOM   5982 C CD     . LYS C 3 336 ? 29.668 20.714  -30.149 1.00 29.39 ? 336 LYS B CD     1 
ATOM   5983 C CE     . LYS C 3 336 ? 28.824 21.968  -30.118 1.00 31.53 ? 336 LYS B CE     1 
ATOM   5984 N NZ     . LYS C 3 336 ? 28.540 22.329  -28.708 1.00 32.91 ? 336 LYS B NZ     1 
ATOM   5985 N N      . TYR C 3 337 ? 29.409 16.484  -27.494 1.00 10.37 ? 337 TYR B N      1 
ATOM   5986 C CA     . TYR C 3 337 ? 28.166 15.855  -27.189 1.00 10.89 ? 337 TYR B CA     1 
ATOM   5987 C C      . TYR C 3 337 ? 28.385 14.649  -26.381 1.00 11.83 ? 337 TYR B C      1 
ATOM   5988 O O      . TYR C 3 337 ? 27.574 13.778  -26.409 1.00 10.58 ? 337 TYR B O      1 
ATOM   5989 C CB     . TYR C 3 337 ? 27.428 15.533  -28.461 1.00 12.30 ? 337 TYR B CB     1 
ATOM   5990 C CG     . TYR C 3 337 ? 27.056 16.730  -29.296 1.00 16.20 ? 337 TYR B CG     1 
ATOM   5991 C CD1    . TYR C 3 337 ? 26.543 17.875  -28.716 1.00 16.52 ? 337 TYR B CD1    1 
ATOM   5992 C CD2    . TYR C 3 337 ? 27.214 16.711  -30.664 1.00 11.47 ? 337 TYR B CD2    1 
ATOM   5993 C CE1    . TYR C 3 337 ? 26.214 18.971  -29.477 1.00 15.99 ? 337 TYR B CE1    1 
ATOM   5994 C CE2    . TYR C 3 337 ? 26.878 17.800  -31.432 1.00 10.28 ? 337 TYR B CE2    1 
ATOM   5995 C CZ     . TYR C 3 337 ? 26.377 18.925  -30.833 1.00 14.93 ? 337 TYR B CZ     1 
ATOM   5996 O OH     . TYR C 3 337 ? 26.042 20.009  -31.598 1.00 16.12 ? 337 TYR B OH     1 
ATOM   5997 N N      . SER C 3 338 ? 29.429 14.638  -25.585 1.00 10.30 ? 338 SER B N      1 
ATOM   5998 C CA     . SER C 3 338 ? 29.810 13.482  -24.818 1.00 11.39 ? 338 SER B CA     1 
ATOM   5999 C C      . SER C 3 338 ? 28.825 13.123  -23.707 1.00 14.11 ? 338 SER B C      1 
ATOM   6000 O O      . SER C 3 338 ? 28.655 11.957  -23.419 1.00 11.34 ? 338 SER B O      1 
ATOM   6001 C CB     . SER C 3 338 ? 31.269 13.667  -24.421 1.00 14.05 ? 338 SER B CB     1 
ATOM   6002 O OG     . SER C 3 338 ? 32.120 13.125  -25.395 1.00 13.70 ? 338 SER B OG     1 
ATOM   6003 N N      . VAL C 3 339 ? 28.235 14.096  -23.043 1.00 10.92 ? 339 VAL B N      1 
ATOM   6004 C CA     . VAL C 3 339 ? 27.131 13.871  -22.123 1.00 10.19 ? 339 VAL B CA     1 
ATOM   6005 C C      . VAL C 3 339 ? 26.013 13.136  -22.849 1.00 8.93  ? 339 VAL B C      1 
ATOM   6006 O O      . VAL C 3 339 ? 25.677 12.000  -22.512 1.00 7.24  ? 339 VAL B O      1 
ATOM   6007 C CB     . VAL C 3 339 ? 26.658 15.207  -21.527 1.00 12.06 ? 339 VAL B CB     1 
ATOM   6008 C CG1    . VAL C 3 339 ? 25.546 15.017  -20.530 1.00 8.69  ? 339 VAL B CG1    1 
ATOM   6009 C CG2    . VAL C 3 339 ? 27.813 15.881  -20.885 1.00 12.94 ? 339 VAL B CG2    1 
ATOM   6010 N N      . TRP C 3 340 ? 25.418 13.719  -23.882 1.00 11.19 ? 340 TRP B N      1 
ATOM   6011 C CA     . TRP C 3 340 ? 24.391 13.048  -24.628 1.00 8.99  ? 340 TRP B CA     1 
ATOM   6012 C C      . TRP C 3 340 ? 24.817 11.649  -25.003 1.00 8.52  ? 340 TRP B C      1 
ATOM   6013 O O      . TRP C 3 340 ? 24.031 10.728  -24.908 1.00 8.56  ? 340 TRP B O      1 
ATOM   6014 C CB     . TRP C 3 340 ? 23.914 13.850  -25.853 1.00 9.73  ? 340 TRP B CB     1 
ATOM   6015 C CG     . TRP C 3 340 ? 22.671 13.286  -26.456 1.00 8.83  ? 340 TRP B CG     1 
ATOM   6016 C CD1    . TRP C 3 340 ? 21.415 13.689  -26.208 1.00 10.39 ? 340 TRP B CD1    1 
ATOM   6017 C CD2    . TRP C 3 340 ? 22.564 12.185  -27.370 1.00 7.43  ? 340 TRP B CD2    1 
ATOM   6018 N NE1    . TRP C 3 340 ? 20.526 12.932  -26.907 1.00 11.73 ? 340 TRP B NE1    1 
ATOM   6019 C CE2    . TRP C 3 340 ? 21.208 11.990  -27.620 1.00 9.02  ? 340 TRP B CE2    1 
ATOM   6020 C CE3    . TRP C 3 340 ? 23.487 11.347  -27.995 1.00 10.61 ? 340 TRP B CE3    1 
ATOM   6021 C CZ2    . TRP C 3 340 ? 20.750 11.006  -28.458 1.00 9.60  ? 340 TRP B CZ2    1 
ATOM   6022 C CZ3    . TRP C 3 340 ? 23.032 10.372  -28.807 1.00 12.02 ? 340 TRP B CZ3    1 
ATOM   6023 C CH2    . TRP C 3 340 ? 21.676 10.210  -29.047 1.00 12.58 ? 340 TRP B CH2    1 
ATOM   6024 N N      . ILE C 3 341 ? 26.040 11.485  -25.462 1.00 7.82  ? 341 ILE B N      1 
ATOM   6025 C CA     . ILE C 3 341 ? 26.442 10.148  -25.887 1.00 14.39 ? 341 ILE B CA     1 
ATOM   6026 C C      . ILE C 3 341 ? 26.398 9.162   -24.719 1.00 14.57 ? 341 ILE B C      1 
ATOM   6027 O O      . ILE C 3 341 ? 25.878 8.044   -24.856 1.00 11.73 ? 341 ILE B O      1 
ATOM   6028 C CB     . ILE C 3 341 ? 27.824 10.195  -26.553 1.00 14.79 ? 341 ILE B CB     1 
ATOM   6029 C CG1    . ILE C 3 341 ? 27.712 10.998  -27.842 1.00 14.76 ? 341 ILE B CG1    1 
ATOM   6030 C CG2    . ILE C 3 341 ? 28.309 8.785   -26.818 1.00 8.41  ? 341 ILE B CG2    1 
ATOM   6031 C CD1    . ILE C 3 341 ? 29.005 11.133  -28.574 1.00 19.48 ? 341 ILE B CD1    1 
ATOM   6032 N N      . GLY C 3 342 ? 26.947 9.556   -23.558 1.00 13.23 ? 342 GLY B N      1 
ATOM   6033 C CA     . GLY C 3 342 ? 26.812 8.740   -22.362 1.00 8.56  ? 342 GLY B CA     1 
ATOM   6034 C C      . GLY C 3 342 ? 25.369 8.361   -22.080 1.00 9.06  ? 342 GLY B C      1 
ATOM   6035 O O      . GLY C 3 342 ? 25.076 7.221   -21.699 1.00 7.75  ? 342 GLY B O      1 
ATOM   6036 N N      . GLY C 3 343 ? 24.449 9.312   -22.259 1.00 7.63  ? 343 GLY B N      1 
ATOM   6037 C CA     . GLY C 3 343 ? 23.033 9.004   -22.109 1.00 8.87  ? 343 GLY B CA     1 
ATOM   6038 C C      . GLY C 3 343 ? 22.572 7.883   -23.023 1.00 8.79  ? 343 GLY B C      1 
ATOM   6039 O O      . GLY C 3 343 ? 21.910 6.939   -22.585 1.00 10.92 ? 343 GLY B O      1 
ATOM   6040 N N      . SER C 3 344 ? 22.837 7.986   -24.307 1.00 9.96  ? 344 SER B N      1 
ATOM   6041 C CA     . SER C 3 344 ? 22.427 6.975   -25.256 1.00 12.12 ? 344 SER B CA     1 
ATOM   6042 C C      . SER C 3 344 ? 22.992 5.600   -24.966 1.00 13.29 ? 344 SER B C      1 
ATOM   6043 O O      . SER C 3 344 ? 22.268 4.637   -25.049 1.00 14.03 ? 344 SER B O      1 
ATOM   6044 C CB     . SER C 3 344 ? 22.701 7.416   -26.686 1.00 11.83 ? 344 SER B CB     1 
ATOM   6045 O OG     . SER C 3 344 ? 22.806 6.322   -27.559 1.00 12.95 ? 344 SER B OG     1 
ATOM   6046 N N      . ILE C 3 345 ? 24.244 5.483   -24.565 1.00 8.84  ? 345 ILE B N      1 
ATOM   6047 C CA     . ILE C 3 345 ? 24.792 4.197   -24.208 1.00 10.79 ? 345 ILE B CA     1 
ATOM   6048 C C      . ILE C 3 345 ? 24.083 3.644   -23.016 1.00 13.43 ? 345 ILE B C      1 
ATOM   6049 O O      . ILE C 3 345 ? 23.539 2.570   -23.082 1.00 17.92 ? 345 ILE B O      1 
ATOM   6050 C CB     . ILE C 3 345 ? 26.308 4.250   -23.953 1.00 15.99 ? 345 ILE B CB     1 
ATOM   6051 C CG1    . ILE C 3 345 ? 27.054 4.644   -25.217 1.00 17.53 ? 345 ILE B CG1    1 
ATOM   6052 C CG2    . ILE C 3 345 ? 26.834 2.918   -23.460 1.00 13.90 ? 345 ILE B CG2    1 
ATOM   6053 C CD1    . ILE C 3 345 ? 28.364 5.326   -24.928 1.00 20.47 ? 345 ILE B CD1    1 
ATOM   6054 N N      . LEU C 3 346 ? 24.056 4.396   -21.941 1.00 14.39 ? 346 LEU B N      1 
ATOM   6055 C CA     . LEU C 3 346 ? 23.366 3.979   -20.722 1.00 10.23 ? 346 LEU B CA     1 
ATOM   6056 C C      . LEU C 3 346 ? 21.928 3.551   -21.006 1.00 13.76 ? 346 LEU B C      1 
ATOM   6057 O O      . LEU C 3 346 ? 21.506 2.450   -20.629 1.00 11.93 ? 346 LEU B O      1 
ATOM   6058 C CB     . LEU C 3 346 ? 23.397 5.110   -19.698 1.00 9.97  ? 346 LEU B CB     1 
ATOM   6059 C CG     . LEU C 3 346 ? 22.693 4.849   -18.367 1.00 12.19 ? 346 LEU B CG     1 
ATOM   6060 C CD1    . LEU C 3 346 ? 23.565 3.992   -17.473 1.00 10.70 ? 346 LEU B CD1    1 
ATOM   6061 C CD2    . LEU C 3 346 ? 22.315 6.143   -17.669 1.00 10.18 ? 346 LEU B CD2    1 
ATOM   6062 N N      . ALA C 3 347 ? 21.159 4.406   -21.689 1.00 12.44 ? 347 ALA B N      1 
ATOM   6063 C CA     . ALA C 3 347 ? 19.742 4.103   -21.898 1.00 13.65 ? 347 ALA B CA     1 
ATOM   6064 C C      . ALA C 3 347 ? 19.526 2.884   -22.793 1.00 17.13 ? 347 ALA B C      1 
ATOM   6065 O O      . ALA C 3 347 ? 18.435 2.300   -22.790 1.00 14.70 ? 347 ALA B O      1 
ATOM   6066 C CB     . ALA C 3 347 ? 19.016 5.324   -22.476 1.00 7.50  ? 347 ALA B CB     1 
ATOM   6067 N N      . SER C 3 348 ? 20.533 2.475   -23.556 1.00 17.34 ? 348 SER B N      1 
ATOM   6068 C CA     . SER C 3 348 ? 20.385 1.315   -24.420 1.00 16.62 ? 348 SER B CA     1 
ATOM   6069 C C      . SER C 3 348 ? 21.078 0.085   -23.860 1.00 18.10 ? 348 SER B C      1 
ATOM   6070 O O      . SER C 3 348 ? 21.116 -0.953  -24.534 1.00 21.23 ? 348 SER B O      1 
ATOM   6071 C CB     . SER C 3 348 ? 20.916 1.629   -25.817 1.00 13.68 ? 348 SER B CB     1 
ATOM   6072 O OG     . SER C 3 348 ? 22.302 1.800   -25.734 1.00 14.81 ? 348 SER B OG     1 
ATOM   6073 N N      . LEU C 3 349 ? 21.542 0.139   -22.621 1.00 18.35 ? 349 LEU B N      1 
ATOM   6074 C CA     . LEU C 3 349 ? 22.134 -1.023  -21.987 1.00 16.37 ? 349 LEU B CA     1 
ATOM   6075 C C      . LEU C 3 349 ? 21.017 -1.878  -21.473 1.00 16.52 ? 349 LEU B C      1 
ATOM   6076 O O      . LEU C 3 349 ? 20.017 -1.365  -21.018 1.00 16.66 ? 349 LEU B O      1 
ATOM   6077 C CB     . LEU C 3 349 ? 23.070 -0.616  -20.869 1.00 14.97 ? 349 LEU B CB     1 
ATOM   6078 C CG     . LEU C 3 349 ? 24.421 0.024   -21.155 1.00 19.08 ? 349 LEU B CG     1 
ATOM   6079 C CD1    . LEU C 3 349 ? 25.054 0.498   -19.867 1.00 13.60 ? 349 LEU B CD1    1 
ATOM   6080 C CD2    . LEU C 3 349 ? 25.362 -0.892  -21.906 1.00 21.75 ? 349 LEU B CD2    1 
ATOM   6081 N N      . SER C 3 350 ? 21.172 -3.190  -21.563 1.00 18.48 ? 350 SER B N      1 
ATOM   6082 C CA     . SER C 3 350 ? 20.131 -4.098  -21.087 1.00 22.60 ? 350 SER B CA     1 
ATOM   6083 C C      . SER C 3 350 ? 19.847 -3.887  -19.599 1.00 19.67 ? 350 SER B C      1 
ATOM   6084 O O      . SER C 3 350 ? 18.690 -3.731  -19.199 1.00 16.47 ? 350 SER B O      1 
ATOM   6085 C CB     . SER C 3 350 ? 20.535 -5.550  -21.373 1.00 20.21 ? 350 SER B CB     1 
ATOM   6086 O OG     . SER C 3 350 ? 19.713 -6.488  -20.693 1.00 35.83 ? 350 SER B OG     1 
ATOM   6087 N N      . THR C 3 351 ? 20.857 -3.899  -18.760 1.00 16.52 ? 351 THR B N      1 
ATOM   6088 C CA     . THR C 3 351 ? 20.640 -3.754  -17.341 1.00 15.46 ? 351 THR B CA     1 
ATOM   6089 C C      . THR C 3 351 ? 19.924 -2.466  -16.942 1.00 18.17 ? 351 THR B C      1 
ATOM   6090 O O      . THR C 3 351 ? 19.252 -2.437  -15.936 1.00 15.98 ? 351 THR B O      1 
ATOM   6091 C CB     . THR C 3 351 ? 21.943 -3.961  -16.554 1.00 14.85 ? 351 THR B CB     1 
ATOM   6092 O OG1    . THR C 3 351 ? 21.751 -3.578  -15.192 1.00 22.78 ? 351 THR B OG1    1 
ATOM   6093 C CG2    . THR C 3 351 ? 22.989 -3.149  -17.138 1.00 15.13 ? 351 THR B CG2    1 
ATOM   6094 N N      . PHE C 3 352 ? 20.055 -1.420  -17.744 1.00 14.97 ? 352 PHE B N      1 
ATOM   6095 C CA     . PHE C 3 352 ? 19.389 -0.174  -17.401 1.00 12.41 ? 352 PHE B CA     1 
ATOM   6096 C C      . PHE C 3 352 ? 17.893 -0.300  -17.532 1.00 12.49 ? 352 PHE B C      1 
ATOM   6097 O O      . PHE C 3 352 ? 17.161 0.547   -17.019 1.00 17.28 ? 352 PHE B O      1 
ATOM   6098 C CB     . PHE C 3 352 ? 19.889 0.962   -18.286 1.00 15.65 ? 352 PHE B CB     1 
ATOM   6099 C CG     . PHE C 3 352 ? 19.397 2.338   -17.883 1.00 12.50 ? 352 PHE B CG     1 
ATOM   6100 C CD1    . PHE C 3 352 ? 20.033 3.051   -16.878 1.00 14.07 ? 352 PHE B CD1    1 
ATOM   6101 C CD2    . PHE C 3 352 ? 18.357 2.955   -18.573 1.00 9.98  ? 352 PHE B CD2    1 
ATOM   6102 C CE1    . PHE C 3 352 ? 19.617 4.340   -16.541 1.00 11.34 ? 352 PHE B CE1    1 
ATOM   6103 C CE2    . PHE C 3 352 ? 17.930 4.231   -18.229 1.00 9.60  ? 352 PHE B CE2    1 
ATOM   6104 C CZ     . PHE C 3 352 ? 18.566 4.926   -17.212 1.00 9.61  ? 352 PHE B CZ     1 
ATOM   6105 N N      . GLN C 3 353 ? 17.414 -1.332  -18.210 1.00 14.17 ? 353 GLN B N      1 
ATOM   6106 C CA     . GLN C 3 353 ? 15.972 -1.484  -18.310 1.00 17.10 ? 353 GLN B CA     1 
ATOM   6107 C C      . GLN C 3 353 ? 15.364 -1.711  -16.936 1.00 19.02 ? 353 GLN B C      1 
ATOM   6108 O O      . GLN C 3 353 ? 14.291 -1.177  -16.639 1.00 16.96 ? 353 GLN B O      1 
ATOM   6109 C CB     . GLN C 3 353 ? 15.633 -2.608  -19.288 1.00 15.03 ? 353 GLN B CB     1 
ATOM   6110 C CG     . GLN C 3 353 ? 16.050 -2.292  -20.738 1.00 18.95 ? 353 GLN B CG     1 
ATOM   6111 C CD     . GLN C 3 353 ? 15.995 -0.793  -21.085 1.00 21.59 ? 353 GLN B CD     1 
ATOM   6112 O OE1    . GLN C 3 353 ? 14.961 -0.146  -20.919 1.00 18.33 ? 353 GLN B OE1    1 
ATOM   6113 N NE2    . GLN C 3 353 ? 17.123 -0.240  -21.551 1.00 19.81 ? 353 GLN B NE2    1 
ATOM   6114 N N      . GLN C 3 354 ? 16.079 -2.433  -16.061 1.00 19.55 ? 354 GLN B N      1 
ATOM   6115 C CA     . GLN C 3 354 ? 15.695 -2.610  -14.665 1.00 16.57 ? 354 GLN B CA     1 
ATOM   6116 C C      . GLN C 3 354 ? 15.873 -1.365  -13.812 1.00 15.49 ? 354 GLN B C      1 
ATOM   6117 O O      . GLN C 3 354 ? 15.426 -1.376  -12.665 1.00 15.79 ? 354 GLN B O      1 
ATOM   6118 C CB     . GLN C 3 354 ? 16.505 -3.732  -14.036 1.00 17.94 ? 354 GLN B CB     1 
ATOM   6119 C CG     . GLN C 3 354 ? 16.158 -5.084  -14.593 1.00 28.91 ? 354 GLN B CG     1 
ATOM   6120 C CD     . GLN C 3 354 ? 14.663 -5.244  -14.866 1.00 36.88 ? 354 GLN B CD     1 
ATOM   6121 O OE1    . GLN C 3 354 ? 13.828 -5.021  -13.982 1.00 35.51 ? 354 GLN B OE1    1 
ATOM   6122 N NE2    . GLN C 3 354 ? 14.321 -5.627  -16.101 1.00 33.90 ? 354 GLN B NE2    1 
ATOM   6123 N N      . MET C 3 355 ? 16.517 -0.313  -14.321 1.00 16.18 ? 355 MET B N      1 
ATOM   6124 C CA     . MET C 3 355 ? 16.918 0.833   -13.510 1.00 13.53 ? 355 MET B CA     1 
ATOM   6125 C C      . MET C 3 355 ? 16.040 2.062   -13.712 1.00 18.09 ? 355 MET B C      1 
ATOM   6126 O O      . MET C 3 355 ? 16.293 3.087   -13.066 1.00 18.01 ? 355 MET B O      1 
ATOM   6127 C CB     . MET C 3 355 ? 18.381 1.201   -13.801 1.00 13.97 ? 355 MET B CB     1 
ATOM   6128 C CG     . MET C 3 355 ? 19.422 0.195   -13.301 1.00 17.12 ? 355 MET B CG     1 
ATOM   6129 S SD     . MET C 3 355 ? 21.077 0.456   -14.029 1.00 21.49 ? 355 MET B SD     1 
ATOM   6130 C CE     . MET C 3 355 ? 21.763 1.784   -13.057 1.00 22.44 ? 355 MET B CE     1 
ATOM   6131 N N      . TRP C 3 356 ? 15.038 1.993   -14.598 1.00 17.22 ? 356 TRP B N      1 
ATOM   6132 C CA     . TRP C 3 356 ? 14.105 3.096   -14.816 1.00 16.32 ? 356 TRP B CA     1 
ATOM   6133 C C      . TRP C 3 356 ? 13.246 3.354   -13.579 1.00 15.35 ? 356 TRP B C      1 
ATOM   6134 O O      . TRP C 3 356 ? 13.006 2.462   -12.764 1.00 20.33 ? 356 TRP B O      1 
ATOM   6135 C CB     . TRP C 3 356 ? 13.168 2.806   -15.997 1.00 15.76 ? 356 TRP B CB     1 
ATOM   6136 C CG     . TRP C 3 356 ? 13.794 2.818   -17.375 1.00 15.71 ? 356 TRP B CG     1 
ATOM   6137 C CD1    . TRP C 3 356 ? 14.068 1.737   -18.161 1.00 14.06 ? 356 TRP B CD1    1 
ATOM   6138 C CD2    . TRP C 3 356 ? 14.194 3.972   -18.131 1.00 12.90 ? 356 TRP B CD2    1 
ATOM   6139 N NE1    . TRP C 3 356 ? 14.621 2.144   -19.346 1.00 11.76 ? 356 TRP B NE1    1 
ATOM   6140 C CE2    . TRP C 3 356 ? 14.711 3.511   -19.355 1.00 9.95  ? 356 TRP B CE2    1 
ATOM   6141 C CE3    . TRP C 3 356 ? 14.187 5.347   -17.877 1.00 10.31 ? 356 TRP B CE3    1 
ATOM   6142 C CZ2    . TRP C 3 356 ? 15.208 4.372   -20.324 1.00 9.21  ? 356 TRP B CZ2    1 
ATOM   6143 C CZ3    . TRP C 3 356 ? 14.683 6.202   -18.839 1.00 8.09  ? 356 TRP B CZ3    1 
ATOM   6144 C CH2    . TRP C 3 356 ? 15.190 5.713   -20.042 1.00 11.03 ? 356 TRP B CH2    1 
ATOM   6145 N N      . ILE C 3 357 ? 12.784 4.593   -13.445 1.00 15.63 ? 357 ILE B N      1 
ATOM   6146 C CA     . ILE C 3 357 ? 11.723 4.946   -12.508 1.00 17.93 ? 357 ILE B CA     1 
ATOM   6147 C C      . ILE C 3 357 ? 10.416 4.796   -13.278 1.00 17.72 ? 357 ILE B C      1 
ATOM   6148 O O      . ILE C 3 357 ? 10.190 5.518   -14.249 1.00 18.34 ? 357 ILE B O      1 
ATOM   6149 C CB     . ILE C 3 357 ? 11.895 6.375   -11.975 1.00 15.77 ? 357 ILE B CB     1 
ATOM   6150 C CG1    . ILE C 3 357 ? 12.989 6.439   -10.916 1.00 18.82 ? 357 ILE B CG1    1 
ATOM   6151 C CG2    . ILE C 3 357 ? 10.597 6.905   -11.451 1.00 14.82 ? 357 ILE B CG2    1 
ATOM   6152 C CD1    . ILE C 3 357 ? 13.277 7.855   -10.435 1.00 20.84 ? 357 ILE B CD1    1 
ATOM   6153 N N      . SER C 3 358 ? 9.562  3.859   -12.864 1.00 21.35 ? 358 SER B N      1 
ATOM   6154 C CA     . SER C 3 358 ? 8.317  3.564   -13.573 1.00 18.04 ? 358 SER B CA     1 
ATOM   6155 C C      . SER C 3 358 ? 7.184  4.480   -13.140 1.00 15.68 ? 358 SER B C      1 
ATOM   6156 O O      . SER C 3 358 ? 7.130  4.947   -12.002 1.00 17.38 ? 358 SER B O      1 
ATOM   6157 C CB     . SER C 3 358 ? 7.882  2.126   -13.328 1.00 17.81 ? 358 SER B CB     1 
ATOM   6158 O OG     . SER C 3 358 ? 8.979  1.249   -13.472 1.00 25.06 ? 358 SER B OG     1 
ATOM   6159 N N      . LYS C 3 359 ? 6.243  4.696   -14.054 1.00 21.19 ? 359 LYS B N      1 
ATOM   6160 C CA     . LYS C 3 359 ? 5.027  5.418   -13.705 1.00 18.07 ? 359 LYS B CA     1 
ATOM   6161 C C      . LYS C 3 359 ? 4.369  4.827   -12.455 1.00 19.36 ? 359 LYS B C      1 
ATOM   6162 O O      . LYS C 3 359 ? 3.941  5.574   -11.562 1.00 17.20 ? 359 LYS B O      1 
ATOM   6163 C CB     . LYS C 3 359 ? 4.080  5.411   -14.894 1.00 14.17 ? 359 LYS B CB     1 
ATOM   6164 C CG     . LYS C 3 359 ? 2.868  6.265   -14.706 1.00 25.50 ? 359 LYS B CG     1 
ATOM   6165 C CD     . LYS C 3 359 ? 2.159  6.472   -16.036 1.00 39.10 ? 359 LYS B CD     1 
ATOM   6166 C CE     . LYS C 3 359 ? 0.754  7.021   -15.831 1.00 51.62 ? 359 LYS B CE     1 
ATOM   6167 N NZ     . LYS C 3 359 ? -0.112 6.127   -15.016 1.00 51.25 ? 359 LYS B NZ     1 
ATOM   6168 N N      . GLN C 3 360 ? 4.333  3.486   -12.342 1.00 17.37 ? 360 GLN B N      1 
ATOM   6169 C CA     . GLN C 3 360 ? 3.830  2.852   -11.115 1.00 22.09 ? 360 GLN B CA     1 
ATOM   6170 C C      . GLN C 3 360 ? 4.559  3.368   -9.886  1.00 22.39 ? 360 GLN B C      1 
ATOM   6171 O O      . GLN C 3 360 ? 3.932  3.756   -8.893  1.00 24.73 ? 360 GLN B O      1 
ATOM   6172 C CB     . GLN C 3 360 ? 3.960  1.325   -11.169 1.00 21.69 ? 360 GLN B CB     1 
ATOM   6173 C CG     . GLN C 3 360 ? 2.974  0.647   -12.082 1.00 39.05 ? 360 GLN B CG     1 
ATOM   6174 C CD     . GLN C 3 360 ? 2.506  -0.685  -11.536 1.00 50.16 ? 360 GLN B CD     1 
ATOM   6175 O OE1    . GLN C 3 360 ? 3.211  -1.332  -10.755 1.00 50.38 ? 360 GLN B OE1    1 
ATOM   6176 N NE2    . GLN C 3 360 ? 1.303  -1.101  -11.940 1.00 45.37 ? 360 GLN B NE2    1 
ATOM   6177 N N      . GLU C 3 361 ? 5.888  3.331   -9.911  1.00 18.89 ? 361 GLU B N      1 
ATOM   6178 C CA     . GLU C 3 361 ? 6.633  3.834   -8.771  1.00 16.48 ? 361 GLU B CA     1 
ATOM   6179 C C      . GLU C 3 361 ? 6.296  5.297   -8.503  1.00 19.73 ? 361 GLU B C      1 
ATOM   6180 O O      . GLU C 3 361 ? 6.177  5.714   -7.348  1.00 18.75 ? 361 GLU B O      1 
ATOM   6181 C CB     . GLU C 3 361 ? 8.133  3.628   -8.998  1.00 16.07 ? 361 GLU B CB     1 
ATOM   6182 C CG     . GLU C 3 361 ? 8.565  2.163   -8.883  1.00 25.73 ? 361 GLU B CG     1 
ATOM   6183 C CD     . GLU C 3 361 ? 10.012 1.915   -9.316  1.00 33.06 ? 361 GLU B CD     1 
ATOM   6184 O OE1    . GLU C 3 361 ? 10.489 2.621   -10.227 1.00 30.57 ? 361 GLU B OE1    1 
ATOM   6185 O OE2    . GLU C 3 361 ? 10.672 1.008   -8.760  1.00 34.80 ? 361 GLU B OE2    1 
ATOM   6186 N N      . TYR C 3 362 ? 6.118  6.095   -9.550  1.00 16.12 ? 362 TYR B N      1 
ATOM   6187 C CA     . TYR C 3 362 ? 5.870  7.505   -9.286  1.00 20.80 ? 362 TYR B CA     1 
ATOM   6188 C C      . TYR C 3 362 ? 4.535  7.709   -8.587  1.00 24.03 ? 362 TYR B C      1 
ATOM   6189 O O      . TYR C 3 362 ? 4.437  8.507   -7.643  1.00 20.17 ? 362 TYR B O      1 
ATOM   6190 C CB     . TYR C 3 362 ? 5.916  8.322   -10.572 1.00 20.53 ? 362 TYR B CB     1 
ATOM   6191 C CG     . TYR C 3 362 ? 5.593  9.777   -10.326 1.00 18.13 ? 362 TYR B CG     1 
ATOM   6192 C CD1    . TYR C 3 362 ? 6.538  10.645  -9.813  1.00 14.64 ? 362 TYR B CD1    1 
ATOM   6193 C CD2    . TYR C 3 362 ? 4.330  10.270  -10.585 1.00 18.54 ? 362 TYR B CD2    1 
ATOM   6194 C CE1    . TYR C 3 362 ? 6.228  11.966  -9.587  1.00 18.91 ? 362 TYR B CE1    1 
ATOM   6195 C CE2    . TYR C 3 362 ? 4.015  11.583  -10.368 1.00 15.35 ? 362 TYR B CE2    1 
ATOM   6196 C CZ     . TYR C 3 362 ? 4.957  12.427  -9.868  1.00 19.18 ? 362 TYR B CZ     1 
ATOM   6197 O OH     . TYR C 3 362 ? 4.612  13.740  -9.659  1.00 19.73 ? 362 TYR B OH     1 
ATOM   6198 N N      . ASP C 3 363 ? 3.490  7.017   -9.052  1.00 23.31 ? 363 ASP B N      1 
ATOM   6199 C CA     . ASP C 3 363 ? 2.178  7.158   -8.430  1.00 24.36 ? 363 ASP B CA     1 
ATOM   6200 C C      . ASP C 3 363 ? 2.209  6.706   -6.967  1.00 24.15 ? 363 ASP B C      1 
ATOM   6201 O O      . ASP C 3 363 ? 1.650  7.371   -6.083  1.00 23.20 ? 363 ASP B O      1 
ATOM   6202 C CB     . ASP C 3 363 ? 1.140  6.379   -9.249  1.00 21.86 ? 363 ASP B CB     1 
ATOM   6203 C CG     . ASP C 3 363 ? 0.807  7.065   -10.595 1.00 32.40 ? 363 ASP B CG     1 
ATOM   6204 O OD1    . ASP C 3 363 ? 0.637  8.304   -10.628 1.00 32.55 ? 363 ASP B OD1    1 
ATOM   6205 O OD2    . ASP C 3 363 ? 0.719  6.376   -11.638 1.00 36.76 ? 363 ASP B OD2    1 
ATOM   6206 N N      . GLU C 3 364 ? 2.905  5.604   -6.694  1.00 25.21 ? 364 GLU B N      1 
ATOM   6207 C CA     . GLU C 3 364 ? 2.998  5.066   -5.340  1.00 24.35 ? 364 GLU B CA     1 
ATOM   6208 C C      . GLU C 3 364 ? 3.716  6.028   -4.400  1.00 19.94 ? 364 GLU B C      1 
ATOM   6209 O O      . GLU C 3 364 ? 3.249  6.304   -3.293  1.00 28.39 ? 364 GLU B O      1 
ATOM   6210 C CB     . GLU C 3 364 ? 3.727  3.725   -5.399  1.00 24.99 ? 364 GLU B CB     1 
ATOM   6211 C CG     . GLU C 3 364 ? 3.701  2.863   -4.172  1.00 25.51 ? 364 GLU B CG     1 
ATOM   6212 C CD     . GLU C 3 364 ? 4.032  1.436   -4.566  1.00 46.03 ? 364 GLU B CD     1 
ATOM   6213 O OE1    . GLU C 3 364 ? 3.782  1.118   -5.759  1.00 43.43 ? 364 GLU B OE1    1 
ATOM   6214 O OE2    . GLU C 3 364 ? 4.547  0.651   -3.721  1.00 51.02 ? 364 GLU B OE2    1 
ATOM   6215 N N      . SER C 3 365 ? 4.853  6.557   -4.829  1.00 20.99 ? 365 SER B N      1 
ATOM   6216 C CA     . SER C 3 365 ? 5.753  7.253   -3.928  1.00 19.95 ? 365 SER B CA     1 
ATOM   6217 C C      . SER C 3 365 ? 5.860  8.764   -4.140  1.00 20.47 ? 365 SER B C      1 
ATOM   6218 O O      . SER C 3 365 ? 6.378  9.453   -3.252  1.00 15.70 ? 365 SER B O      1 
ATOM   6219 C CB     . SER C 3 365 ? 7.154  6.644   -4.041  1.00 20.25 ? 365 SER B CB     1 
ATOM   6220 O OG     . SER C 3 365 ? 8.135  7.645   -3.838  1.00 36.75 ? 365 SER B OG     1 
ATOM   6221 N N      . GLY C 3 366 ? 5.433  9.296   -5.288  1.00 16.86 ? 366 GLY B N      1 
ATOM   6222 C CA     . GLY C 3 366 ? 5.510  10.718  -5.527  1.00 15.76 ? 366 GLY B CA     1 
ATOM   6223 C C      . GLY C 3 366 ? 6.866  11.159  -6.032  1.00 21.44 ? 366 GLY B C      1 
ATOM   6224 O O      . GLY C 3 366 ? 7.795  10.361  -6.187  1.00 16.77 ? 366 GLY B O      1 
ATOM   6225 N N      . PRO C 3 367 ? 7.020  12.465  -6.263  1.00 23.51 ? 367 PRO B N      1 
ATOM   6226 C CA     . PRO C 3 367 ? 8.251  12.956  -6.901  1.00 17.95 ? 367 PRO B CA     1 
ATOM   6227 C C      . PRO C 3 367 ? 9.522  12.636  -6.133  1.00 16.25 ? 367 PRO B C      1 
ATOM   6228 O O      . PRO C 3 367 ? 10.604 12.667  -6.730  1.00 25.62 ? 367 PRO B O      1 
ATOM   6229 C CB     . PRO C 3 367 ? 8.016  14.468  -6.991  1.00 14.35 ? 367 PRO B CB     1 
ATOM   6230 C CG     . PRO C 3 367 ? 6.528  14.601  -7.005  1.00 14.75 ? 367 PRO B CG     1 
ATOM   6231 C CD     . PRO C 3 367 ? 6.051  13.549  -6.044  1.00 19.55 ? 367 PRO B CD     1 
ATOM   6232 N N      . SER C 3 368 ? 9.448  12.317  -4.850  1.00 19.83 ? 368 SER B N      1 
ATOM   6233 C CA     . SER C 3 368 ? 10.672 12.060  -4.106  1.00 24.25 ? 368 SER B CA     1 
ATOM   6234 C C      . SER C 3 368 ? 11.318 10.734  -4.472  1.00 19.35 ? 368 SER B C      1 
ATOM   6235 O O      . SER C 3 368 ? 12.435 10.468  -4.014  1.00 21.29 ? 368 SER B O      1 
ATOM   6236 C CB     . SER C 3 368 ? 10.404 12.087  -2.599  1.00 26.31 ? 368 SER B CB     1 
ATOM   6237 O OG     . SER C 3 368 ? 9.485  11.068  -2.202  1.00 22.12 ? 368 SER B OG     1 
ATOM   6238 N N      . ILE C 3 369 ? 10.645 9.895   -5.265  1.00 16.71 ? 369 ILE B N      1 
ATOM   6239 C CA     . ILE C 3 369 ? 11.152 8.566   -5.596  1.00 17.43 ? 369 ILE B CA     1 
ATOM   6240 C C      . ILE C 3 369 ? 12.467 8.751   -6.322  1.00 18.17 ? 369 ILE B C      1 
ATOM   6241 O O      . ILE C 3 369 ? 13.298 7.839   -6.406  1.00 20.29 ? 369 ILE B O      1 
ATOM   6242 C CB     . ILE C 3 369 ? 10.147 7.774   -6.454  1.00 19.71 ? 369 ILE B CB     1 
ATOM   6243 C CG1    . ILE C 3 369 ? 10.666 6.372   -6.745  1.00 15.18 ? 369 ILE B CG1    1 
ATOM   6244 C CG2    . ILE C 3 369 ? 9.845  8.515   -7.751  1.00 20.67 ? 369 ILE B CG2    1 
ATOM   6245 C CD1    . ILE C 3 369 ? 10.955 5.611   -5.501  1.00 21.22 ? 369 ILE B CD1    1 
ATOM   6246 N N      . VAL C 3 370 ? 12.655 9.949   -6.854  1.00 18.16 ? 370 VAL B N      1 
ATOM   6247 C CA     . VAL C 3 370 ? 13.867 10.213  -7.600  1.00 19.80 ? 370 VAL B CA     1 
ATOM   6248 C C      . VAL C 3 370 ? 15.092 10.097  -6.700  1.00 19.84 ? 370 VAL B C      1 
ATOM   6249 O O      . VAL C 3 370 ? 16.188 9.750   -7.166  1.00 20.19 ? 370 VAL B O      1 
ATOM   6250 C CB     . VAL C 3 370 ? 13.783 11.596  -8.279  1.00 19.58 ? 370 VAL B CB     1 
ATOM   6251 C CG1    . VAL C 3 370 ? 13.631 12.694  -7.232  1.00 13.85 ? 370 VAL B CG1    1 
ATOM   6252 C CG2    . VAL C 3 370 ? 14.995 11.811  -9.188  1.00 15.07 ? 370 VAL B CG2    1 
ATOM   6253 N N      . HIS C 3 371 ? 14.953 10.387  -5.412  1.00 16.62 ? 371 HIS B N      1 
ATOM   6254 C CA     . HIS C 3 371 ? 16.144 10.327  -4.571  1.00 16.36 ? 371 HIS B CA     1 
ATOM   6255 C C      . HIS C 3 371 ? 16.577 8.894   -4.301  1.00 16.72 ? 371 HIS B C      1 
ATOM   6256 O O      . HIS C 3 371 ? 17.762 8.642   -4.095  1.00 20.00 ? 371 HIS B O      1 
ATOM   6257 C CB     . HIS C 3 371 ? 15.914 11.059  -3.256  1.00 15.92 ? 371 HIS B CB     1 
ATOM   6258 C CG     . HIS C 3 371 ? 15.571 12.499  -3.431  1.00 13.83 ? 371 HIS B CG     1 
ATOM   6259 N ND1    . HIS C 3 371 ? 16.475 13.422  -3.905  1.00 20.62 ? 371 HIS B ND1    1 
ATOM   6260 C CD2    . HIS C 3 371 ? 14.423 13.176  -3.205  1.00 15.16 ? 371 HIS B CD2    1 
ATOM   6261 C CE1    . HIS C 3 371 ? 15.893 14.606  -3.974  1.00 23.54 ? 371 HIS B CE1    1 
ATOM   6262 N NE2    . HIS C 3 371 ? 14.647 14.484  -3.558  1.00 19.87 ? 371 HIS B NE2    1 
ATOM   6263 N N      . ARG C 3 372 ? 15.692 7.932   -4.330  1.00 18.29 ? 372 ARG B N      1 
ATOM   6264 C CA     . ARG C 3 372 ? 16.062 6.590   -3.998  1.00 17.57 ? 372 ARG B CA     1 
ATOM   6265 C C      . ARG C 3 372 ? 16.526 5.755   -5.165  1.00 18.25 ? 372 ARG B C      1 
ATOM   6266 O O      . ARG C 3 372 ? 17.182 4.749   -4.982  1.00 17.91 ? 372 ARG B O      1 
ATOM   6267 C CB     . ARG C 3 372 ? 14.887 5.915   -3.327  1.00 22.61 ? 372 ARG B CB     1 
ATOM   6268 C CG     . ARG C 3 372 ? 14.688 6.305   -1.882  1.00 36.07 ? 372 ARG B CG     1 
ATOM   6269 C CD     . ARG C 3 372 ? 13.219 6.204   -1.531  1.00 43.04 ? 372 ARG B CD     1 
ATOM   6270 N NE     . ARG C 3 372 ? 12.652 4.934   -1.962  1.00 40.82 ? 372 ARG B NE     1 
ATOM   6271 C CZ     . ARG C 3 372 ? 11.352 4.706   -2.091  1.00 37.98 ? 372 ARG B CZ     1 
ATOM   6272 N NH1    . ARG C 3 372 ? 10.483 5.673   -1.844  1.00 26.93 ? 372 ARG B NH1    1 
ATOM   6273 N NH2    . ARG C 3 372 ? 10.924 3.517   -2.479  1.00 37.07 ? 372 ARG B NH2    1 
ATOM   6274 N N      . LYS C 3 373 ? 16.147 6.156   -6.367  1.00 18.66 ? 373 LYS B N      1 
ATOM   6275 C CA     . LYS C 3 373 ? 16.570 5.411   -7.543  1.00 20.17 ? 373 LYS B CA     1 
ATOM   6276 C C      . LYS C 3 373 ? 17.569 6.145   -8.440  1.00 18.67 ? 373 LYS B C      1 
ATOM   6277 O O      . LYS C 3 373 ? 18.029 5.552   -9.417  1.00 27.96 ? 373 LYS B O      1 
ATOM   6278 C CB     . LYS C 3 373 ? 15.350 4.991   -8.385  1.00 23.28 ? 373 LYS B CB     1 
ATOM   6279 C CG     . LYS C 3 373 ? 14.354 4.061   -7.666  1.00 18.84 ? 373 LYS B CG     1 
ATOM   6280 C CD     . LYS C 3 373 ? 13.402 3.345   -8.638  1.00 21.47 ? 373 LYS B CD     1 
ATOM   6281 C CE     . LYS C 3 373 ? 14.135 2.271   -9.489  1.00 34.47 ? 373 LYS B CE     1 
ATOM   6282 N NZ     . LYS C 3 373 ? 13.291 1.115   -9.993  1.00 18.92 ? 373 LYS B NZ     1 
ATOM   6283 N N      . CYS C 3 374 ? 17.957 7.386   -8.136  1.00 14.79 ? 374 CYS B N      1 
ATOM   6284 C CA     . CYS C 3 374 ? 18.857 8.130   -9.026  1.00 18.93 ? 374 CYS B CA     1 
ATOM   6285 C C      . CYS C 3 374 ? 19.896 8.877   -8.194  1.00 21.39 ? 374 CYS B C      1 
ATOM   6286 O O      . CYS C 3 374 ? 19.702 10.050  -7.865  1.00 18.66 ? 374 CYS B O      1 
ATOM   6287 C CB     . CYS C 3 374 ? 18.087 9.091   -9.917  1.00 15.29 ? 374 CYS B CB     1 
ATOM   6288 S SG     . CYS C 3 374 ? 16.934 8.369   -11.072 1.00 17.54 ? 374 CYS B SG     1 
ATOM   6289 N N      . PHE C 3 375 ? 21.029 8.247   -7.934  1.00 25.75 ? 375 PHE B N      1 
ATOM   6290 C CA     . PHE C 3 375 ? 22.095 8.840   -7.116  1.00 27.14 ? 375 PHE B CA     1 
ATOM   6291 C C      . PHE C 3 375 ? 23.011 9.886   -7.840  1.00 52.58 ? 375 PHE B C      1 
ATOM   6292 O O      . PHE C 3 375 ? 22.681 10.427  -8.902  1.00 43.15 ? 375 PHE B O      1 
ATOM   6293 C CB     . PHE C 3 375 ? 22.967 7.751   -6.548  1.00 19.50 ? 375 PHE B CB     1 
ATOM   6294 C CG     . PHE C 3 375 ? 22.295 6.842   -5.547  1.00 22.51 ? 375 PHE B CG     1 
ATOM   6295 C CD1    . PHE C 3 375 ? 20.921 6.767   -5.423  1.00 21.07 ? 375 PHE B CD1    1 
ATOM   6296 C CD2    . PHE C 3 375 ? 23.071 6.029   -4.742  1.00 13.14 ? 375 PHE B CD2    1 
ATOM   6297 C CE1    . PHE C 3 375 ? 20.342 5.906   -4.530  1.00 14.20 ? 375 PHE B CE1    1 
ATOM   6298 C CE2    . PHE C 3 375 ? 22.499 5.171   -3.839  1.00 13.95 ? 375 PHE B CE2    1 
ATOM   6299 C CZ     . PHE C 3 375 ? 21.133 5.107   -3.736  1.00 18.06 ? 375 PHE B CZ     1 
ATOM   6300 O OXT    . PHE C 3 375 ? 24.103 10.266  -7.416  1.00 37.90 ? 375 PHE B OXT    1 
HETATM 6301 P PG     . ANP D 4 .   ? 38.360 1.701   6.752   1.00 60.98 ? 401 ANP A PG     1 
HETATM 6302 O O1G    . ANP D 4 .   ? 37.500 0.862   7.647   1.00 53.66 ? 401 ANP A O1G    1 
HETATM 6303 O O2G    . ANP D 4 .   ? 37.999 1.579   5.299   1.00 65.15 ? 401 ANP A O2G    1 
HETATM 6304 O O3G    . ANP D 4 .   ? 39.829 1.570   7.051   1.00 36.77 ? 401 ANP A O3G    1 
HETATM 6305 P PB     . ANP D 4 .   ? 36.669 4.140   6.391   1.00 80.49 ? 401 ANP A PB     1 
HETATM 6306 O O1B    . ANP D 4 .   ? 37.063 4.758   5.069   1.00 71.96 ? 401 ANP A O1B    1 
HETATM 6307 O O2B    . ANP D 4 .   ? 35.623 3.075   6.382   1.00 51.66 ? 401 ANP A O2B    1 
HETATM 6308 N N3B    . ANP D 4 .   ? 38.026 3.358   7.148   1.00 48.69 ? 401 ANP A N3B    1 
HETATM 6309 P PA     . ANP D 4 .   ? 34.837 5.712   7.896   1.00 92.55 ? 401 ANP A PA     1 
HETATM 6310 O O1A    . ANP D 4 .   ? 34.601 5.236   9.305   1.00 39.50 ? 401 ANP A O1A    1 
HETATM 6311 O O2A    . ANP D 4 .   ? 33.956 5.250   6.819   1.00 66.84 ? 401 ANP A O2A    1 
HETATM 6312 O O3A    . ANP D 4 .   ? 36.313 5.368   7.373   1.00 63.76 ? 401 ANP A O3A    1 
HETATM 6313 O "O5'"  . ANP D 4 .   ? 34.720 7.306   7.816   1.00 49.80 ? 401 ANP A "O5'"  1 
HETATM 6314 C "C5'"  . ANP D 4 .   ? 33.408 7.834   7.739   1.00 50.58 ? 401 ANP A "C5'"  1 
HETATM 6315 C "C4'"  . ANP D 4 .   ? 33.048 8.646   8.950   1.00 49.78 ? 401 ANP A "C4'"  1 
HETATM 6316 O "O4'"  . ANP D 4 .   ? 33.795 8.218   10.067  1.00 39.66 ? 401 ANP A "O4'"  1 
HETATM 6317 C "C3'"  . ANP D 4 .   ? 33.272 10.133  8.811   1.00 52.54 ? 401 ANP A "C3'"  1 
HETATM 6318 O "O3'"  . ANP D 4 .   ? 32.001 10.765  8.625   1.00 45.64 ? 401 ANP A "O3'"  1 
HETATM 6319 C "C2'"  . ANP D 4 .   ? 33.975 10.536  10.094  1.00 46.62 ? 401 ANP A "C2'"  1 
HETATM 6320 O "O2'"  . ANP D 4 .   ? 33.340 11.646  10.739  1.00 43.48 ? 401 ANP A "O2'"  1 
HETATM 6321 C "C1'"  . ANP D 4 .   ? 33.826 9.321   10.949  1.00 40.35 ? 401 ANP A "C1'"  1 
HETATM 6322 N N9     . ANP D 4 .   ? 34.844 9.131   12.025  1.00 48.95 ? 401 ANP A N9     1 
HETATM 6323 C C8     . ANP D 4 .   ? 35.646 8.062   12.180  1.00 44.14 ? 401 ANP A C8     1 
HETATM 6324 N N7     . ANP D 4 .   ? 36.396 8.189   13.289  1.00 39.35 ? 401 ANP A N7     1 
HETATM 6325 C C5     . ANP D 4 .   ? 36.092 9.340   13.878  1.00 34.60 ? 401 ANP A C5     1 
HETATM 6326 C C6     . ANP D 4 .   ? 36.537 10.065  15.079  1.00 40.45 ? 401 ANP A C6     1 
HETATM 6327 N N6     . ANP D 4 .   ? 37.498 9.561   15.884  1.00 30.47 ? 401 ANP A N6     1 
HETATM 6328 N N1     . ANP D 4 .   ? 35.951 11.252  15.334  1.00 53.56 ? 401 ANP A N1     1 
HETATM 6329 C C2     . ANP D 4 .   ? 35.001 11.769  14.536  1.00 49.18 ? 401 ANP A C2     1 
HETATM 6330 N N3     . ANP D 4 .   ? 34.553 11.149  13.439  1.00 52.87 ? 401 ANP A N3     1 
HETATM 6331 C C4     . ANP D 4 .   ? 35.056 9.957   13.055  1.00 47.56 ? 401 ANP A C4     1 
HETATM 6332 H HNB1   . ANP D 4 .   ? 38.607 3.856   7.809   1.00 58.43 ? 401 ANP A HNB1   1 
HETATM 6333 H "H5'1" . ANP D 4 .   ? 32.671 7.042   7.803   1.00 60.70 ? 401 ANP A "H5'1" 1 
HETATM 6334 H "H5'2" . ANP D 4 .   ? 33.260 8.383   6.806   1.00 60.70 ? 401 ANP A "H5'2" 1 
HETATM 6335 H "H4'"  . ANP D 4 .   ? 31.992 8.469   9.131   1.00 59.74 ? 401 ANP A "H4'"  1 
HETATM 6336 H "H3'"  . ANP D 4 .   ? 33.931 10.320  7.960   1.00 63.04 ? 401 ANP A "H3'"  1 
HETATM 6337 H "HO3'" . ANP D 4 .   ? 31.985 11.203  7.764   1.00 54.76 ? 401 ANP A "HO3'" 1 
HETATM 6338 H "H2'"  . ANP D 4 .   ? 35.044 10.697  9.915   1.00 55.94 ? 401 ANP A "H2'"  1 
HETATM 6339 H "HO2'" . ANP D 4 .   ? 32.505 11.854  10.301  1.00 52.18 ? 401 ANP A "HO2'" 1 
HETATM 6340 H "H1'"  . ANP D 4 .   ? 32.830 9.444   11.364  1.00 48.42 ? 401 ANP A "H1'"  1 
HETATM 6341 H H8     . ANP D 4 .   ? 35.697 7.208   11.522  1.00 52.96 ? 401 ANP A H8     1 
HETATM 6342 H HN61   . ANP D 4 .   ? 37.920 8.670   15.665  1.00 36.57 ? 401 ANP A HN61   1 
HETATM 6343 H HN62   . ANP D 4 .   ? 37.792 10.071  16.704  1.00 36.57 ? 401 ANP A HN62   1 
HETATM 6344 H H2     . ANP D 4 .   ? 34.564 12.723  14.798  1.00 59.02 ? 401 ANP A H2     1 
HETATM 6345 P PB     . AR6 E 5 .   ? 37.849 6.146   21.605  1.00 9.15  ? 402 AR6 A PB     1 
HETATM 6346 O O1B    . AR6 E 5 .   ? 38.437 4.823   21.919  1.00 22.29 ? 402 AR6 A O1B    1 
HETATM 6347 C C1D    . AR6 E 5 .   ? 40.920 8.896   19.562  1.00 37.20 ? 402 AR6 A C1D    1 
HETATM 6348 O O1D    . AR6 E 5 .   ? 41.903 9.846   19.520  1.00 29.49 ? 402 AR6 A O1D    1 
HETATM 6349 O O2B    . AR6 E 5 .   ? 37.949 6.365   20.033  1.00 23.27 ? 402 AR6 A O2B    1 
HETATM 6350 C C2D    . AR6 E 5 .   ? 39.730 9.488   18.811  1.00 33.55 ? 402 AR6 A C2D    1 
HETATM 6351 O O2D    . AR6 E 5 .   ? 40.052 10.713  18.189  1.00 30.47 ? 402 AR6 A O2D    1 
HETATM 6352 O O3A    . AR6 E 5 .   ? 36.452 6.407   22.024  1.00 14.34 ? 402 AR6 A O3A    1 
HETATM 6353 C C3D    . AR6 E 5 .   ? 38.607 9.671   19.825  1.00 33.12 ? 402 AR6 A C3D    1 
HETATM 6354 O O3D    . AR6 E 5 .   ? 38.051 10.978  19.772  1.00 33.26 ? 402 AR6 A O3D    1 
HETATM 6355 C C4D    . AR6 E 5 .   ? 39.301 9.434   21.173  1.00 25.52 ? 402 AR6 A C4D    1 
HETATM 6356 O O4D    . AR6 E 5 .   ? 40.485 8.661   20.890  1.00 34.92 ? 402 AR6 A O4D    1 
HETATM 6357 C C5D    . AR6 E 5 .   ? 38.486 8.698   22.204  1.00 29.49 ? 402 AR6 A C5D    1 
HETATM 6358 O O5D    . AR6 E 5 .   ? 38.825 7.285   22.165  1.00 28.72 ? 402 AR6 A O5D    1 
HETATM 6359 H H1D    . AR6 E 5 .   ? 41.246 8.052   19.164  1.00 44.64 ? 402 AR6 A H1D    1 
HETATM 6360 H H2D    . AR6 E 5 .   ? 39.438 8.853   18.111  1.00 40.26 ? 402 AR6 A H2D    1 
HETATM 6361 H HO2D   . AR6 E 5 .   ? 40.220 11.293  18.772  1.00 36.57 ? 402 AR6 A HO2D   1 
HETATM 6362 H H3D    . AR6 E 5 .   ? 37.900 8.999   19.663  1.00 39.75 ? 402 AR6 A H3D    1 
HETATM 6363 H HO3D   . AR6 E 5 .   ? 37.566 11.032  19.090  1.00 39.91 ? 402 AR6 A HO3D   1 
HETATM 6364 H H4D    . AR6 E 5 .   ? 39.570 10.306  21.556  1.00 30.62 ? 402 AR6 A H4D    1 
HETATM 6365 H H5D    . AR6 E 5 .   ? 37.522 8.826   22.020  1.00 35.39 ? 402 AR6 A H5D    1 
HETATM 6366 H H5DA   . AR6 E 5 .   ? 38.682 9.065   23.101  1.00 35.39 ? 402 AR6 A H5DA   1 
HETATM 6367 O O      . HOH F 6 .   ? 16.204 21.299  35.468  1.00 27.80 ? 501 HOH A O      1 
HETATM 6368 O O      . HOH F 6 .   ? 48.746 1.337   8.690   1.00 23.62 ? 502 HOH A O      1 
HETATM 6369 O O      . HOH F 6 .   ? 25.254 21.017  27.956  1.00 29.89 ? 503 HOH A O      1 
HETATM 6370 O O      . HOH F 6 .   ? 38.639 6.288   7.958   1.00 30.00 ? 504 HOH A O      1 
HETATM 6371 O O      . HOH F 6 .   ? 37.421 18.518  39.324  1.00 17.45 ? 505 HOH A O      1 
HETATM 6372 O O      . HOH F 6 .   ? 33.344 14.542  22.165  1.00 30.86 ? 506 HOH A O      1 
HETATM 6373 O O      . HOH F 6 .   ? 29.958 -11.956 -10.468 1.00 26.51 ? 507 HOH A O      1 
HETATM 6374 O O      . HOH F 6 .   ? 34.729 -3.635  28.206  1.00 18.63 ? 508 HOH A O      1 
HETATM 6375 O O      . HOH F 6 .   ? 46.165 2.549   18.154  1.00 13.38 ? 509 HOH A O      1 
HETATM 6376 O O      . HOH F 6 .   ? 13.001 14.961  25.201  1.00 37.18 ? 510 HOH A O      1 
HETATM 6377 O O      . HOH F 6 .   ? 27.221 3.436   3.430   1.00 9.96  ? 511 HOH A O      1 
HETATM 6378 O O      . HOH F 6 .   ? 22.909 -22.637 0.406   1.00 23.22 ? 512 HOH A O      1 
HETATM 6379 O O      . HOH F 6 .   ? 27.028 -5.822  20.038  1.00 22.79 ? 513 HOH A O      1 
HETATM 6380 O O      . HOH F 6 .   ? 36.930 11.584  -1.151  1.00 17.30 ? 514 HOH A O      1 
HETATM 6381 O O      . HOH F 6 .   ? 37.122 12.372  1.210   1.00 22.10 ? 515 HOH A O      1 
HETATM 6382 O O      . HOH F 6 .   ? 34.593 -4.930  12.856  1.00 18.97 ? 516 HOH A O      1 
HETATM 6383 O O      . HOH F 6 .   ? 12.111 9.835   30.802  1.00 29.39 ? 517 HOH A O      1 
HETATM 6384 O O      . HOH F 6 .   ? 41.851 13.838  29.558  1.00 22.10 ? 518 HOH A O      1 
HETATM 6385 O O      . HOH F 6 .   ? 36.958 8.448   6.687   1.00 30.00 ? 519 HOH A O      1 
HETATM 6386 O O      . HOH F 6 .   ? 43.846 -1.758  23.045  1.00 20.79 ? 520 HOH A O      1 
HETATM 6387 O O      . HOH F 6 .   ? 40.289 5.090   18.747  1.00 15.10 ? 521 HOH A O      1 
HETATM 6388 O O      . HOH F 6 .   ? 27.349 -12.673 -5.374  1.00 25.51 ? 522 HOH A O      1 
HETATM 6389 O O      . HOH F 6 .   ? 26.540 17.657  19.393  1.00 34.24 ? 523 HOH A O      1 
HETATM 6390 O O      . HOH F 6 .   ? 44.491 16.184  7.816   1.00 19.31 ? 524 HOH A O      1 
HETATM 6391 O O      . HOH F 6 .   ? 28.099 -2.331  14.777  1.00 13.27 ? 525 HOH A O      1 
HETATM 6392 O O      . HOH F 6 .   ? 33.231 6.388   39.617  1.00 18.76 ? 526 HOH A O      1 
HETATM 6393 O O      . HOH F 6 .   ? 25.435 0.800   -25.862 1.00 34.22 ? 527 HOH A O      1 
HETATM 6394 O O      . HOH F 6 .   ? 7.830  -20.757 5.778   1.00 34.88 ? 528 HOH A O      1 
HETATM 6395 O O      . HOH F 6 .   ? 21.061 1.065   26.711  1.00 15.64 ? 529 HOH A O      1 
HETATM 6396 O O      . HOH F 6 .   ? 30.564 12.505  0.678   1.00 14.33 ? 530 HOH A O      1 
HETATM 6397 O O      . HOH F 6 .   ? 12.289 -1.419  -0.128  1.00 24.80 ? 531 HOH A O      1 
HETATM 6398 O O      . HOH F 6 .   ? 16.673 1.895   -5.263  1.00 21.06 ? 532 HOH A O      1 
HETATM 6399 O O      . HOH F 6 .   ? 45.135 1.099   26.251  1.00 21.11 ? 533 HOH A O      1 
HETATM 6400 O O      . HOH F 6 .   ? 9.618  -27.630 -11.340 1.00 35.09 ? 534 HOH A O      1 
HETATM 6401 O O      . HOH F 6 .   ? 14.985 3.727   26.149  1.00 48.47 ? 535 HOH A O      1 
HETATM 6402 O O      . HOH F 6 .   ? 16.474 -1.823  17.114  1.00 14.66 ? 536 HOH A O      1 
HETATM 6403 O O      . HOH F 6 .   ? 48.521 -8.558  18.739  1.00 14.52 ? 537 HOH A O      1 
HETATM 6404 O O      . HOH F 6 .   ? 41.752 23.196  31.425  1.00 19.88 ? 538 HOH A O      1 
HETATM 6405 O O      . HOH F 6 .   ? 38.764 -3.503  1.330   1.00 24.81 ? 539 HOH A O      1 
HETATM 6406 O O      . HOH F 6 .   ? 35.728 6.575   1.431   1.00 9.63  ? 540 HOH A O      1 
HETATM 6407 O O      . HOH F 6 .   ? 32.642 -12.867 7.604   1.00 18.81 ? 541 HOH A O      1 
HETATM 6408 O O      . HOH F 6 .   ? 29.465 20.224  27.929  1.00 24.31 ? 542 HOH A O      1 
HETATM 6409 O O      . HOH F 6 .   ? 12.477 -19.798 8.721   1.00 34.95 ? 543 HOH A O      1 
HETATM 6410 O O      . HOH F 6 .   ? 48.128 -11.171 12.563  1.00 16.21 ? 544 HOH A O      1 
HETATM 6411 O O      . HOH F 6 .   ? 28.408 -10.153 25.932  1.00 20.18 ? 545 HOH A O      1 
HETATM 6412 O O      . HOH F 6 .   ? 4.365  -6.299  -0.907  1.00 35.93 ? 546 HOH A O      1 
HETATM 6413 O O      . HOH F 6 .   ? 36.627 23.727  37.396  1.00 27.57 ? 547 HOH A O      1 
HETATM 6414 O O      . HOH F 6 .   ? 27.347 20.957  1.625   1.00 26.96 ? 548 HOH A O      1 
HETATM 6415 O O      . HOH F 6 .   ? 18.357 9.747   9.387   1.00 30.28 ? 549 HOH A O      1 
HETATM 6416 O O      . HOH F 6 .   ? 2.758  -14.483 12.167  1.00 32.16 ? 550 HOH A O      1 
HETATM 6417 O O      . HOH F 6 .   ? 12.986 6.948   46.126  1.00 21.89 ? 551 HOH A O      1 
HETATM 6418 O O      . HOH F 6 .   ? 24.861 -6.908  18.834  1.00 21.88 ? 552 HOH A O      1 
HETATM 6419 O O      . HOH F 6 .   ? 14.987 6.259   26.517  1.00 44.92 ? 553 HOH A O      1 
HETATM 6420 O O      . HOH F 6 .   ? 22.994 4.184   -7.766  1.00 10.66 ? 554 HOH A O      1 
HETATM 6421 O O      . HOH F 6 .   ? 5.022  -15.979 13.179  1.00 42.19 ? 555 HOH A O      1 
HETATM 6422 O O      . HOH G 6 .   ? 49.260 17.488  37.328  1.00 27.78 ? 101 HOH C O      1 
HETATM 6423 O O      . HOH G 6 .   ? 50.179 4.989   23.813  1.00 24.20 ? 102 HOH C O      1 
HETATM 6424 O O      . HOH G 6 .   ? 46.305 18.308  21.259  1.00 27.73 ? 103 HOH C O      1 
HETATM 6425 O O      . HOH G 6 .   ? 45.124 21.146  13.005  1.00 35.23 ? 104 HOH C O      1 
HETATM 6426 O O      . HOH G 6 .   ? 60.823 17.357  18.622  1.00 26.61 ? 105 HOH C O      1 
HETATM 6427 O O      . HOH G 6 .   ? 59.927 10.868  21.366  1.00 26.41 ? 106 HOH C O      1 
HETATM 6428 O O      . HOH G 6 .   ? 50.371 13.504  32.086  1.00 26.34 ? 107 HOH C O      1 
HETATM 6429 O O      . HOH G 6 .   ? 62.869 11.889  22.013  1.00 23.02 ? 108 HOH C O      1 
HETATM 6430 O O      . HOH H 6 .   ? 50.872 18.187  -23.570 1.00 23.25 ? 401 HOH B O      1 
HETATM 6431 O O      . HOH H 6 .   ? 25.332 21.548  -16.603 1.00 15.17 ? 402 HOH B O      1 
HETATM 6432 O O      . HOH H 6 .   ? 59.165 38.597  -31.475 1.00 24.93 ? 403 HOH B O      1 
HETATM 6433 O O      . HOH H 6 .   ? 6.130  14.286  -38.888 1.00 36.24 ? 404 HOH B O      1 
HETATM 6434 O O      . HOH H 6 .   ? 24.526 11.054  -12.236 1.00 21.83 ? 405 HOH B O      1 
HETATM 6435 O O      . HOH H 6 .   ? 35.420 19.877  0.000   1.00 33.82 ? 406 HOH B O      1 
HETATM 6436 O O      . HOH H 6 .   ? 52.880 5.501   -7.018  1.00 24.75 ? 407 HOH B O      1 
HETATM 6437 O O      . HOH H 6 .   ? 33.571 27.917  -26.119 1.00 17.11 ? 408 HOH B O      1 
HETATM 6438 O O      . HOH H 6 .   ? 19.955 24.736  -34.775 1.00 32.37 ? 409 HOH B O      1 
HETATM 6439 O O      . HOH H 6 .   ? 26.119 16.721  -24.525 1.00 25.96 ? 410 HOH B O      1 
HETATM 6440 O O      . HOH H 6 .   ? 42.232 21.740  -3.352  1.00 35.12 ? 411 HOH B O      1 
HETATM 6441 O O      . HOH H 6 .   ? 53.943 15.030  -12.544 1.00 17.90 ? 412 HOH B O      1 
HETATM 6442 O O      . HOH H 6 .   ? 54.590 20.498  -17.508 1.00 13.49 ? 413 HOH B O      1 
HETATM 6443 O O      . HOH H 6 .   ? 48.073 15.585  -5.719  1.00 17.38 ? 414 HOH B O      1 
HETATM 6444 O O      . HOH H 6 .   ? 25.296 19.589  -21.853 1.00 18.71 ? 415 HOH B O      1 
HETATM 6445 O O      . HOH H 6 .   ? 45.991 29.666  -25.478 1.00 26.52 ? 416 HOH B O      1 
HETATM 6446 O O      . HOH H 6 .   ? 51.212 35.301  -36.969 1.00 30.50 ? 417 HOH B O      1 
HETATM 6447 O O      . HOH H 6 .   ? 16.123 21.608  -2.472  1.00 18.09 ? 418 HOH B O      1 
HETATM 6448 O O      . HOH H 6 .   ? 28.785 17.560  -23.606 1.00 17.10 ? 419 HOH B O      1 
HETATM 6449 O O      . HOH H 6 .   ? 33.904 10.624  -23.015 1.00 26.92 ? 420 HOH B O      1 
HETATM 6450 O O      . HOH H 6 .   ? 2.482  6.693   -20.062 1.00 28.92 ? 421 HOH B O      1 
HETATM 6451 O O      . HOH H 6 .   ? 41.886 44.659  -23.348 1.00 41.51 ? 422 HOH B O      1 
HETATM 6452 O O      . HOH H 6 .   ? 6.043  28.665  -35.228 1.00 33.87 ? 423 HOH B O      1 
HETATM 6453 O O      . HOH H 6 .   ? 28.049 12.350  -0.434  1.00 8.57  ? 424 HOH B O      1 
HETATM 6454 O O      . HOH H 6 .   ? 43.002 41.692  -23.008 1.00 25.98 ? 425 HOH B O      1 
HETATM 6455 O O      . HOH H 6 .   ? 28.690 25.123  -28.435 1.00 39.09 ? 426 HOH B O      1 
HETATM 6456 O O      . HOH H 6 .   ? 31.260 44.820  -38.053 1.00 27.57 ? 427 HOH B O      1 
HETATM 6457 O O      . HOH H 6 .   ? 30.323 28.442  -28.317 1.00 21.20 ? 428 HOH B O      1 
HETATM 6458 O O      . HOH H 6 .   ? 34.102 47.276  -41.922 1.00 34.84 ? 429 HOH B O      1 
HETATM 6459 O O      . HOH H 6 .   ? 19.525 10.428  -31.973 1.00 52.02 ? 430 HOH B O      1 
HETATM 6460 O O      . HOH H 6 .   ? 27.762 4.641   -7.663  1.00 17.56 ? 431 HOH B O      1 
HETATM 6461 O O      . HOH H 6 .   ? 31.204 5.163   -5.138  1.00 12.53 ? 432 HOH B O      1 
HETATM 6462 O O      . HOH H 6 .   ? 7.422  32.793  -16.602 1.00 35.19 ? 433 HOH B O      1 
HETATM 6463 O O      . HOH H 6 .   ? 28.459 24.037  -25.391 1.00 26.72 ? 434 HOH B O      1 
HETATM 6464 O O      . HOH H 6 .   ? 41.560 26.914  -34.874 1.00 24.05 ? 435 HOH B O      1 
HETATM 6465 O O      . HOH H 6 .   ? 31.453 20.841  -3.269  1.00 17.77 ? 436 HOH B O      1 
HETATM 6466 O O      . HOH H 6 .   ? 42.057 11.767  -25.909 1.00 18.31 ? 437 HOH B O      1 
HETATM 6467 O O      . HOH H 6 .   ? 32.068 37.156  -19.414 1.00 26.55 ? 438 HOH B O      1 
HETATM 6468 O O      . HOH H 6 .   ? 49.121 28.600  -13.842 1.00 24.86 ? 439 HOH B O      1 
HETATM 6469 O O      . HOH H 6 .   ? 40.005 16.309  -30.858 1.00 23.68 ? 440 HOH B O      1 
HETATM 6470 O O      . HOH H 6 .   ? 12.032 -4.729  -17.669 1.00 21.58 ? 441 HOH B O      1 
HETATM 6471 O O      . HOH H 6 .   ? 11.083 -2.836  -30.559 1.00 37.68 ? 442 HOH B O      1 
HETATM 6472 O O      . HOH H 6 .   ? 38.504 50.971  -36.402 1.00 23.45 ? 443 HOH B O      1 
HETATM 6473 O O      . HOH H 6 .   ? 54.014 13.739  -14.485 1.00 32.56 ? 444 HOH B O      1 
HETATM 6474 O O      . HOH H 6 .   ? 44.286 5.819   -6.814  1.00 16.32 ? 445 HOH B O      1 
HETATM 6475 O O      . HOH H 6 .   ? 54.670 28.649  -31.603 1.00 20.81 ? 446 HOH B O      1 
HETATM 6476 O O      . HOH H 6 .   ? 38.539 42.896  -11.846 1.00 29.71 ? 447 HOH B O      1 
HETATM 6477 O O      . HOH H 6 .   ? 51.604 26.229  -33.516 1.00 25.16 ? 448 HOH B O      1 
HETATM 6478 O O      . HOH H 6 .   ? 52.689 13.349  -16.659 1.00 26.69 ? 449 HOH B O      1 
HETATM 6479 O O      . HOH H 6 .   ? 48.519 13.159  -3.767  1.00 21.56 ? 450 HOH B O      1 
HETATM 6480 O O      . HOH H 6 .   ? 26.411 13.326  -6.571  1.00 26.46 ? 451 HOH B O      1 
HETATM 6481 O O      . HOH H 6 .   ? 26.566 10.477  -9.303  1.00 28.35 ? 452 HOH B O      1 
HETATM 6482 O O      . HOH H 6 .   ? 46.300 39.404  -16.983 1.00 22.00 ? 453 HOH B O      1 
HETATM 6483 O O      . HOH H 6 .   ? 33.987 44.795  -38.277 1.00 29.31 ? 454 HOH B O      1 
HETATM 6484 O O      . HOH H 6 .   ? 15.108 39.889  -25.893 1.00 37.33 ? 455 HOH B O      1 
HETATM 6485 O O      . HOH H 6 .   ? 11.470 48.548  -24.596 1.00 28.62 ? 456 HOH B O      1 
HETATM 6486 O O      . HOH H 6 .   ? 48.363 12.032  -22.487 1.00 17.01 ? 457 HOH B O      1 
HETATM 6487 O O      . HOH H 6 .   ? 27.921 21.175  -25.303 1.00 25.41 ? 458 HOH B O      1 
HETATM 6488 O O      . HOH H 6 .   ? 24.208 -1.562  -25.235 1.00 33.83 ? 459 HOH B O      1 
HETATM 6489 O O      . HOH H 6 .   ? 14.822 40.320  -23.235 1.00 33.20 ? 460 HOH B O      1 
HETATM 6490 O O      . HOH H 6 .   ? 56.041 11.627  -14.723 1.00 23.48 ? 461 HOH B O      1 
HETATM 6491 O O      . HOH H 6 .   ? 20.996 3.302   -9.785  1.00 14.02 ? 462 HOH B O      1 
HETATM 6492 O O      . HOH H 6 .   ? 11.231 -3.295  -15.222 1.00 21.85 ? 463 HOH B O      1 
HETATM 6493 O O      . HOH H 6 .   ? 31.237 24.954  -6.115  1.00 36.90 ? 464 HOH B O      1 
HETATM 6494 O O      . HOH H 6 .   ? 44.301 32.233  -43.941 1.00 59.89 ? 465 HOH B O      1 
HETATM 6495 O O      . HOH H 6 .   ? 37.830 8.863   2.147   1.00 20.23 ? 466 HOH B O      1 
HETATM 6496 O O      . HOH H 6 .   ? 28.267 32.309  -28.070 1.00 34.07 ? 467 HOH B O      1 
HETATM 6497 O O      . HOH H 6 .   ? 27.941 20.343  -21.782 1.00 14.33 ? 468 HOH B O      1 
HETATM 6498 O O      . HOH H 6 .   ? 46.855 14.358  -23.842 1.00 24.32 ? 469 HOH B O      1 
HETATM 6499 O O      . HOH H 6 .   ? 61.661 28.152  -26.333 1.00 25.42 ? 470 HOH B O      1 
HETATM 6500 O O      . HOH H 6 .   ? 14.336 21.048  -0.265  1.00 18.05 ? 471 HOH B O      1 
# 
